data_5800 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5800 _Entry.Title ; Sequence-specific 1H, 13C, 15N resonance assignments of the carboxyterminal domain of the transcription factor NusA from E.coli ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2003-05-19 _Entry.Accession_date 2003-05-19 _Entry.Last_release_date 2004-02-11 _Entry.Original_release_date 2004-02-11 _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 Anke Eisenmann . . . 5800 2 Sabine Schwarz . . . 5800 3 Kristian Schweimer . . . 5800 4 Paul Roesch . . . 5800 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5800 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 625 5800 '15N chemical shifts' 154 5800 '1H chemical shifts' 1051 5800 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 . . 2004-02-11 2003-05-19 original author . 5800 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5800 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 14755165 _Citation.Full_citation . _Citation.Title ; Letter to the Editor: Sequence-specific 1H, 13C, 15N resonance assignments and secondary structure of the carboxyterminal domain of the E.coli Transcription factor NusA ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 28 _Citation.Journal_issue 2 _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 193 _Citation.Page_last 194 _Citation.Year 2004 _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 Anke Eisenmann . . . 5800 1 2 Sabine Schwarz . . . 5800 1 3 Paul Roesch . . . 5800 1 4 Kristian Schweimer . . . 5800 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5800 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11430821 _Citation.Full_citation ; Worbs et. al. An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA. Mol Cell. 2001 Jun;7(6):1177-89. ; _Citation.Title 'An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Mol. Cell' _Citation.Journal_name_full 'Molecular cell' _Citation.Journal_volume 7 _Citation.Journal_issue 6 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1097-2765 _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 1177 _Citation.Page_last 1189 _Citation.Year 2001 _Citation.Details ; The crystal structure of Thermotoga maritima NusA, a transcription factor involved in pausing, termination, and antitermination processes, reveals a four-domain, rod-shaped molecule. An N-terminal alpha/beta portion, a five-stranded beta-barrel (S1 domain), and two K-homology (KH) modules create a continuous spine of positive electrostatic potential, suitable for nonspecific mRNA attraction. Homology models suggest how, in addition, specific mRNA regulatory sequences can be recognized by the S1 and KH motifs. An arrangement of multiple S1 and KH domains mediated by highly conserved residues is seen, creating an extended RNA binding surface, a paradigm for other proteins with similar domain arrays. Structural and mutational analyses indicate that the motifs cooperate, modulating strength and specificity of RNA binding. ; 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 M Worbs M. . . 5800 2 2 'G P' Bourenkov G. P. . 5800 2 3 'H D' Bartunik H. D. . 5800 2 4 R Huber R. . . 5800 2 5 'M C' Wahl M. C. . 5800 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 5800 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11743725 _Citation.Full_citation ; Gopal et. al. Crystal structure of the transcription elongation/anti-termination factor NusA from Mycobacterium tuberculosis at 1.7 A resolution. J Mol Biol. 2001 Dec 14;314(5):1087-95. ; _Citation.Title 'Crystal structure of the transcription elongation/anti-termination factor NusA from Mycobacterium tuberculosis at 1.7 A resolution.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 314 _Citation.Journal_issue 5 _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 1087 _Citation.Page_last 1095 _Citation.Year 2001 _Citation.Details ; Mycobacterium tuberculosis is the cause of tuberculosis in humans, a disease that affects over a one-third of the world's population. This slow-growing pathogen has only one ribosomal RNA operon, thus making its transcriptional apparatus a fundamentally interesting target for drug discovery. NusA binds to RNA polymerase and modulates several of the ribosomal RNA transcriptional processes. Here, we report the crystal structure of NusA, and reveal that the molecule consists of four domains. They are organised as two distinct entities. The N-terminal domain (residues 1 to 99) that resembles the B chain of the Rad50cd ATP binding cassette-ATPase (ABC-ATPase) and a C-terminal module (residues 108 to 329) consisting of a ribosomal S1 protein domain followed by two K homology domains. The S1 and KH domains are tightly integrated together to form an extensive RNA-binding structure, but are flexibly tethered to the N-terminal domain. The molecule's surfaces and architecture provide insights into RNA and polymerase interactions and the mechanism of pause site discrimination. They also allow us to rationalize certain termination-defective and cold shock-sensitive mutations in the nusA gene that have been studied in Escherichia coli. ; 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 B Gopal B. . . 5800 3 2 'L F' Haire L. F. . 5800 3 3 'S J' Gamblin S. J. . 5800 3 4 'E J' Dodson E. J. . 5800 3 5 'A N' Lane A. N. . 5800 3 6 'K G' Papavinasasundaram K. G. . 5800 3 7 'M J' Colston M. J. . 5800 3 8 G Dodson G. . . 5800 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 5800 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11040219 _Citation.Full_citation ; Mah et. al. The alpha subunit of E. coli RNA polymerase activates RNA binding by NusA. Genes Dev. 2000 Oct 15;14(20):2664-75. ; _Citation.Title 'The alpha subunit of E. coli RNA polymerase activates RNA binding by NusA.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Genes Dev.' _Citation.Journal_name_full 'Genes & development' _Citation.Journal_volume 14 _Citation.Journal_issue 20 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0890-9369 _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 2664 _Citation.Page_last 2675 _Citation.Year 2000 _Citation.Details ; The Escherichia coli NusA protein modulates pausing, termination, and antitermination by associating with the transcribing RNA polymerase core enzyme. NusA can be covalently cross-linked to nascent RNA within a transcription complex, but does not bind RNA on its own. We have found that deletion of the 79 carboxy-terminal amino acids of the 495-amino-acid NusA protein allows NusA to bind RNA in gel mobility shift assays. The carboxy-terminal domain (CTD) of the alpha subunit of RNA polymerase, as well as the bacteriophage lambda N gene antiterminator protein, bind to carboxy-terminal regions of NusA and enable full-length NusA to bind RNA. Binding of NusA to RNA in the presence of alpha or N involves an amino-terminal S1 homology region that is otherwise inactive in full-length NusA. The interaction of the alpha-CTD with full-length NusA stimulates termination. N may prevent termination by inducing NusA to interact with N utilization (nut) site RNA rather than RNA near the 3' end of the nascent transcript. Sequence analysis showed that the alpha-CTD contains a modified helix-hairpin-helix motif (HhH), which is also conserved in the carboxy-terminal regions of some eubacterial NusA proteins. These HhH motifs may mediate protein-protein interactions in NusA and the alpha-CTD. ; 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 'T F' Mah T. F. . 5800 4 2 K Kuznedelov K. . . 5800 4 3 A Mushegian A. . . 5800 4 4 K Severinov K. . . 5800 4 5 J Greenblatt J. . . 5800 4 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_EcoNusA_(339-495) _Assembly.Sf_category assembly _Assembly.Sf_framecode system_EcoNusA_(339-495) _Assembly.Entry_ID 5800 _Assembly.ID 1 _Assembly.Name 'Escherichia coli N utilization substance (339-495)' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _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 . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5800 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 'EcoNusA (339-495)' 1 $EcoNusA_(339-495) . . . native . . . . . 5800 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'EcoNusA (339-495)' abbreviation 5800 1 'Escherichia coli N utilization substance (339-495)' system 5800 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_EcoNusA_(339-495) _Entity.Sf_category entity _Entity.Sf_framecode EcoNusA_(339-495) _Entity.Entry_ID 5800 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Escherichia coli N utilization substance A (339-495)' _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 ; GPMTVDDLQAKHQAEAHAAI DTFTKYLDIDEDFATVLVEE GFSTLEELAYVPMKELLEIE GLDEPTVEALRERAKNALAT IAQAQEESLGDNKPADDLLN LEGVDRDLAFKLAARGVCTL EDLAEQGIDDLADIEGLTDE KAGALIMAARNICWFGDEA ; _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 159 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all free' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 17294 _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 DBJ BAB37473 . "transcription termination-antitermination factor NusA [Escherichia coli O157:H7 str. Sakai]" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 2 no DBJ BAE77215 . "transcription termination/antitermination L factor [Escherichia coli str. K-12 substr. W3110]" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 3 no DBJ BAG78979 . "N utilization substance protein A [Escherichia coli SE11]" . . . . . 98.74 495 99.36 100.00 1.15e-101 . . . . 5800 1 4 no DBJ BAI27449 . "transcription termination/antitermination L factor NusA [Escherichia coli O26:H11 str. 11368]" . . . . . 98.74 495 99.36 100.00 1.15e-101 . . . . 5800 1 5 no DBJ BAI32628 . "transcription termination/antitermination L factor NusA [Escherichia coli O103:H2 str. 12009]" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 6 no EMBL CAA25200 . "unnamed protein product [Escherichia coli]" . . . . . 98.74 494 100.00 100.00 6.44e-102 . . . . 5800 1 7 no EMBL CAP77631 . "Transcription elongation protein nusA [Escherichia coli LF82]" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 8 no EMBL CAQ33504 . "transcription termination/antitermination L factor [Escherichia coli BL21(DE3)]" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 9 no EMBL CAQ90641 . "transcription termination/antitermination L factor [Escherichia fergusonii ATCC 35469]" . . . . . 98.74 495 99.36 100.00 1.12e-101 . . . . 5800 1 10 no EMBL CAR00133 . "transcription termination/antitermination L factor [Escherichia coli IAI1]" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 11 no GB AAA57972 . "L factor [Escherichia coli str. K-12 substr. MG1655]" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 12 no GB AAC76203 . "transcription termination/antitermination L factor [Escherichia coli str. K-12 substr. MG1655]" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 13 no GB AAG58305 . "transcription pausing; L factor [Escherichia coli O157:H7 str. EDL933]" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 14 no GB AAN44677 . "transcription pausing; L factor [Shigella flexneri 2a str. 301]" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 15 no GB AAN82367 . "N utilization substance protein A [Escherichia coli CFT073]" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 16 no REF NP_289745 . "transcription elongation factor NusA [Escherichia coli O157:H7 str. EDL933]" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 17 no REF NP_312077 . "transcription elongation factor NusA [Escherichia coli O157:H7 str. Sakai]" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 18 no REF NP_417638 . "transcription termination/antitermination L factor [Escherichia coli str. K-12 substr. MG1655]" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 19 no REF NP_708970 . "transcription elongation factor NusA [Shigella flexneri 2a str. 301]" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 20 no REF NP_755793 . "transcription elongation factor NusA [Escherichia coli CFT073]" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 21 no SP P0AFF6 . "RecName: Full=Transcription termination/antitermination protein NusA; AltName: Full=N utilization substance protein A; AltName:" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 22 no SP P0AFF7 . "RecName: Full=Transcription termination/antitermination protein NusA [Escherichia coli CFT073]" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 23 no SP P0AFF8 . "RecName: Full=Transcription termination/antitermination protein NusA [Escherichia coli O157:H7]" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 24 no SP P0AFF9 . "RecName: Full=Transcription termination/antitermination protein NusA [Shigella flexneri]" . . . . . 98.74 495 100.00 100.00 5.63e-102 . . . . 5800 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'EcoNusA (339-495)' abbreviation 5800 1 'EcoNusA (339-495)' variant 5800 1 'Escherichia coli N utilization substance A (339-495)' common 5800 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 . GLY . 5800 1 2 . PRO . 5800 1 3 . MET . 5800 1 4 . THR . 5800 1 5 . VAL . 5800 1 6 . ASP . 5800 1 7 . ASP . 5800 1 8 . LEU . 5800 1 9 . GLN . 5800 1 10 . ALA . 5800 1 11 . LYS . 5800 1 12 . HIS . 5800 1 13 . GLN . 5800 1 14 . ALA . 5800 1 15 . GLU . 5800 1 16 . ALA . 5800 1 17 . HIS . 5800 1 18 . ALA . 5800 1 19 . ALA . 5800 1 20 . ILE . 5800 1 21 . ASP . 5800 1 22 . THR . 5800 1 23 . PHE . 5800 1 24 . THR . 5800 1 25 . LYS . 5800 1 26 . TYR . 5800 1 27 . LEU . 5800 1 28 . ASP . 5800 1 29 . ILE . 5800 1 30 . ASP . 5800 1 31 . GLU . 5800 1 32 . ASP . 5800 1 33 . PHE . 5800 1 34 . ALA . 5800 1 35 . THR . 5800 1 36 . VAL . 5800 1 37 . LEU . 5800 1 38 . VAL . 5800 1 39 . GLU . 5800 1 40 . GLU . 5800 1 41 . GLY . 5800 1 42 . PHE . 5800 1 43 . SER . 5800 1 44 . THR . 5800 1 45 . LEU . 5800 1 46 . GLU . 5800 1 47 . GLU . 5800 1 48 . LEU . 5800 1 49 . ALA . 5800 1 50 . TYR . 5800 1 51 . VAL . 5800 1 52 . PRO . 5800 1 53 . MET . 5800 1 54 . LYS . 5800 1 55 . GLU . 5800 1 56 . LEU . 5800 1 57 . LEU . 5800 1 58 . GLU . 5800 1 59 . ILE . 5800 1 60 . GLU . 5800 1 61 . GLY . 5800 1 62 . LEU . 5800 1 63 . ASP . 5800 1 64 . GLU . 5800 1 65 . PRO . 5800 1 66 . THR . 5800 1 67 . VAL . 5800 1 68 . GLU . 5800 1 69 . ALA . 5800 1 70 . LEU . 5800 1 71 . ARG . 5800 1 72 . GLU . 5800 1 73 . ARG . 5800 1 74 . ALA . 5800 1 75 . LYS . 5800 1 76 . ASN . 5800 1 77 . ALA . 5800 1 78 . LEU . 5800 1 79 . ALA . 5800 1 80 . THR . 5800 1 81 . ILE . 5800 1 82 . ALA . 5800 1 83 . GLN . 5800 1 84 . ALA . 5800 1 85 . GLN . 5800 1 86 . GLU . 5800 1 87 . GLU . 5800 1 88 . SER . 5800 1 89 . LEU . 5800 1 90 . GLY . 5800 1 91 . ASP . 5800 1 92 . ASN . 5800 1 93 . LYS . 5800 1 94 . PRO . 5800 1 95 . ALA . 5800 1 96 . ASP . 5800 1 97 . ASP . 5800 1 98 . LEU . 5800 1 99 . LEU . 5800 1 100 . ASN . 5800 1 101 . LEU . 5800 1 102 . GLU . 5800 1 103 . GLY . 5800 1 104 . VAL . 5800 1 105 . ASP . 5800 1 106 . ARG . 5800 1 107 . ASP . 5800 1 108 . LEU . 5800 1 109 . ALA . 5800 1 110 . PHE . 5800 1 111 . LYS . 5800 1 112 . LEU . 5800 1 113 . ALA . 5800 1 114 . ALA . 5800 1 115 . ARG . 5800 1 116 . GLY . 5800 1 117 . VAL . 5800 1 118 . CYS . 5800 1 119 . THR . 5800 1 120 . LEU . 5800 1 121 . GLU . 5800 1 122 . ASP . 5800 1 123 . LEU . 5800 1 124 . ALA . 5800 1 125 . GLU . 5800 1 126 . GLN . 5800 1 127 . GLY . 5800 1 128 . ILE . 5800 1 129 . ASP . 5800 1 130 . ASP . 5800 1 131 . LEU . 5800 1 132 . ALA . 5800 1 133 . ASP . 5800 1 134 . ILE . 5800 1 135 . GLU . 5800 1 136 . GLY . 5800 1 137 . LEU . 5800 1 138 . THR . 5800 1 139 . ASP . 5800 1 140 . GLU . 5800 1 141 . LYS . 5800 1 142 . ALA . 5800 1 143 . GLY . 5800 1 144 . ALA . 5800 1 145 . LEU . 5800 1 146 . ILE . 5800 1 147 . MET . 5800 1 148 . ALA . 5800 1 149 . ALA . 5800 1 150 . ARG . 5800 1 151 . ASN . 5800 1 152 . ILE . 5800 1 153 . CYS . 5800 1 154 . TRP . 5800 1 155 . PHE . 5800 1 156 . GLY . 5800 1 157 . ASP . 5800 1 158 . GLU . 5800 1 159 . ALA . 5800 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 . GLY 1 1 5800 1 . PRO 2 2 5800 1 . MET 3 3 5800 1 . THR 4 4 5800 1 . VAL 5 5 5800 1 . ASP 6 6 5800 1 . ASP 7 7 5800 1 . LEU 8 8 5800 1 . GLN 9 9 5800 1 . ALA 10 10 5800 1 . LYS 11 11 5800 1 . HIS 12 12 5800 1 . GLN 13 13 5800 1 . ALA 14 14 5800 1 . GLU 15 15 5800 1 . ALA 16 16 5800 1 . HIS 17 17 5800 1 . ALA 18 18 5800 1 . ALA 19 19 5800 1 . ILE 20 20 5800 1 . ASP 21 21 5800 1 . THR 22 22 5800 1 . PHE 23 23 5800 1 . THR 24 24 5800 1 . LYS 25 25 5800 1 . TYR 26 26 5800 1 . LEU 27 27 5800 1 . ASP 28 28 5800 1 . ILE 29 29 5800 1 . ASP 30 30 5800 1 . GLU 31 31 5800 1 . ASP 32 32 5800 1 . PHE 33 33 5800 1 . ALA 34 34 5800 1 . THR 35 35 5800 1 . VAL 36 36 5800 1 . LEU 37 37 5800 1 . VAL 38 38 5800 1 . GLU 39 39 5800 1 . GLU 40 40 5800 1 . GLY 41 41 5800 1 . PHE 42 42 5800 1 . SER 43 43 5800 1 . THR 44 44 5800 1 . LEU 45 45 5800 1 . GLU 46 46 5800 1 . GLU 47 47 5800 1 . LEU 48 48 5800 1 . ALA 49 49 5800 1 . TYR 50 50 5800 1 . VAL 51 51 5800 1 . PRO 52 52 5800 1 . MET 53 53 5800 1 . LYS 54 54 5800 1 . GLU 55 55 5800 1 . LEU 56 56 5800 1 . LEU 57 57 5800 1 . GLU 58 58 5800 1 . ILE 59 59 5800 1 . GLU 60 60 5800 1 . GLY 61 61 5800 1 . LEU 62 62 5800 1 . ASP 63 63 5800 1 . GLU 64 64 5800 1 . PRO 65 65 5800 1 . THR 66 66 5800 1 . VAL 67 67 5800 1 . GLU 68 68 5800 1 . ALA 69 69 5800 1 . LEU 70 70 5800 1 . ARG 71 71 5800 1 . GLU 72 72 5800 1 . ARG 73 73 5800 1 . ALA 74 74 5800 1 . LYS 75 75 5800 1 . ASN 76 76 5800 1 . ALA 77 77 5800 1 . LEU 78 78 5800 1 . ALA 79 79 5800 1 . THR 80 80 5800 1 . ILE 81 81 5800 1 . ALA 82 82 5800 1 . GLN 83 83 5800 1 . ALA 84 84 5800 1 . GLN 85 85 5800 1 . GLU 86 86 5800 1 . GLU 87 87 5800 1 . SER 88 88 5800 1 . LEU 89 89 5800 1 . GLY 90 90 5800 1 . ASP 91 91 5800 1 . ASN 92 92 5800 1 . LYS 93 93 5800 1 . PRO 94 94 5800 1 . ALA 95 95 5800 1 . ASP 96 96 5800 1 . ASP 97 97 5800 1 . LEU 98 98 5800 1 . LEU 99 99 5800 1 . ASN 100 100 5800 1 . LEU 101 101 5800 1 . GLU 102 102 5800 1 . GLY 103 103 5800 1 . VAL 104 104 5800 1 . ASP 105 105 5800 1 . ARG 106 106 5800 1 . ASP 107 107 5800 1 . LEU 108 108 5800 1 . ALA 109 109 5800 1 . PHE 110 110 5800 1 . LYS 111 111 5800 1 . LEU 112 112 5800 1 . ALA 113 113 5800 1 . ALA 114 114 5800 1 . ARG 115 115 5800 1 . GLY 116 116 5800 1 . VAL 117 117 5800 1 . CYS 118 118 5800 1 . THR 119 119 5800 1 . LEU 120 120 5800 1 . GLU 121 121 5800 1 . ASP 122 122 5800 1 . LEU 123 123 5800 1 . ALA 124 124 5800 1 . GLU 125 125 5800 1 . GLN 126 126 5800 1 . GLY 127 127 5800 1 . ILE 128 128 5800 1 . ASP 129 129 5800 1 . ASP 130 130 5800 1 . LEU 131 131 5800 1 . ALA 132 132 5800 1 . ASP 133 133 5800 1 . ILE 134 134 5800 1 . GLU 135 135 5800 1 . GLY 136 136 5800 1 . LEU 137 137 5800 1 . THR 138 138 5800 1 . ASP 139 139 5800 1 . GLU 140 140 5800 1 . LYS 141 141 5800 1 . ALA 142 142 5800 1 . GLY 143 143 5800 1 . ALA 144 144 5800 1 . LEU 145 145 5800 1 . ILE 146 146 5800 1 . MET 147 147 5800 1 . ALA 148 148 5800 1 . ALA 149 149 5800 1 . ARG 150 150 5800 1 . ASN 151 151 5800 1 . ILE 152 152 5800 1 . CYS 153 153 5800 1 . TRP 154 154 5800 1 . PHE 155 155 5800 1 . GLY 156 156 5800 1 . ASP 157 157 5800 1 . GLU 158 158 5800 1 . ALA 159 159 5800 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 5800 _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 $EcoNusA_(339-495) . 562 . . 'Escherichia coli' 'E. Coli' . . Eubacteria . Escherichia coli . . . . . . . . . . . . . . . . . . . . . 5800 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 5800 _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 $EcoNusA_(339-495) . 'recombinant technology' 'Escherichia coli' E.coli . . Escherichia coli BL21(DE3) . . . . . . . . . . . . plasmid . . pET43a . . . . . . 5800 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5800 _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 'Escherichia coli N utilization substance A (339-495)' '[U-13C; U-15N]' . . 1 $EcoNusA_(339-495) . . 1.5 . . mM . . . . 5800 1 2 'potassium phosphate' . . . . . . . 50 . . mM . . . . 5800 1 3 NaCl . . . . . . . 50 . . mM . . . . 5800 1 4 D2O . . . . . . . 10 . . '% v/v' . . . . 5800 1 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_1 _Sample_condition_list.Entry_ID 5800 _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 6.4 0.1 na 5800 1 temperature 298 1 K 5800 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRVIEW _Software.Sf_category software _Software.Sf_framecode NMRVIEW _Software.Entry_ID 5800 _Software.ID 1 _Software.Name NMRView _Software.Version 5.0.4 _Software.Details 'B.A. Johnson, Merck, Whitehouse Station, NJ, USA' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 5800 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 5800 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AVANCE _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5800 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer_1 Bruker DRX . 600 . . . 5800 1 2 NMR_spectrometer_2 Bruker AVANCE . 700 . . . 5800 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 5800 _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 HNCO . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5800 1 2 HNCACB . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5800 1 3 CBCA(CO)NH . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5800 1 4 CCONH . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5800 1 5 HBHA(CO)NH . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5800 1 6 H(C)CH-COSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5800 1 7 H(C)CH-TOCSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5800 1 8 HNHA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5800 1 9 NNH-NOESY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5800 1 10 '1H-15N NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5800 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 5800 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name HNCO _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 5800 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name HNCACB _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 5800 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name CBCA(CO)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 5800 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name CCONH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 5800 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name HBHA(CO)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 5800 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name H(C)CH-COSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 5800 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name H(C)CH-TOCSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_8 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_8 _NMR_spec_expt.Entry_ID 5800 _NMR_spec_expt.ID 8 _NMR_spec_expt.Name HNHA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_9 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_9 _NMR_spec_expt.Entry_ID 5800 _NMR_spec_expt.ID 9 _NMR_spec_expt.Name NNH-NOESY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_10 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_10 _NMR_spec_expt.Entry_ID 5800 _NMR_spec_expt.ID 10 _NMR_spec_expt.Name '1H-15N NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . 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 5800 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5800 1 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.000000000 . . . . . . . . . 5800 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5800 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5800 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_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 HNCO 1 $sample_1 . 5800 1 2 HNCACB 1 $sample_1 . 5800 1 3 CBCA(CO)NH 1 $sample_1 . 5800 1 4 CCONH 1 $sample_1 . 5800 1 5 HBHA(CO)NH 1 $sample_1 . 5800 1 6 H(C)CH-COSY 1 $sample_1 . 5800 1 7 H(C)CH-TOCSY 1 $sample_1 . 5800 1 8 HNHA 1 $sample_1 . 5800 1 9 NNH-NOESY 1 $sample_1 . 5800 1 10 '1H-15N NOESY' 1 $sample_1 . 5800 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 PRO HA H 1 4.47 0.02 . 1 . . . . . . . . 5800 1 2 . 1 1 2 2 PRO HB2 H 1 1.94 0.02 . 2 . . . . . . . . 5800 1 3 . 1 1 2 2 PRO HB3 H 1 2.31 0.02 . 2 . . . . . . . . 5800 1 4 . 1 1 2 2 PRO HG2 H 1 2.01 0.02 . 1 . . . . . . . . 5800 1 5 . 1 1 2 2 PRO HG3 H 1 2.01 0.02 . 1 . . . . . . . . 5800 1 6 . 1 1 2 2 PRO HD2 H 1 3.61 0.02 . 2 . . . . . . . . 5800 1 7 . 1 1 2 2 PRO HD3 H 1 3.56 0.02 . 2 . . . . . . . . 5800 1 8 . 1 1 2 2 PRO C C 13 176.84 0.2 . 1 . . . . . . . . 5800 1 9 . 1 1 2 2 PRO CA C 13 63.02 0.2 . 1 . . . . . . . . 5800 1 10 . 1 1 2 2 PRO CB C 13 32.26 0.2 . 1 . . . . . . . . 5800 1 11 . 1 1 2 2 PRO CG C 13 27.06 0.2 . 1 . . . . . . . . 5800 1 12 . 1 1 2 2 PRO CD C 13 50.26 0.2 . 1 . . . . . . . . 5800 1 13 . 1 1 3 3 MET H H 1 8.58 0.02 . 1 . . . . . . . . 5800 1 14 . 1 1 3 3 MET HA H 1 4.57 0.02 . 1 . . . . . . . . 5800 1 15 . 1 1 3 3 MET HB2 H 1 2.03 0.02 . 2 . . . . . . . . 5800 1 16 . 1 1 3 3 MET HB3 H 1 2.10 0.02 . 2 . . . . . . . . 5800 1 17 . 1 1 3 3 MET HG2 H 1 2.57 0.02 . 2 . . . . . . . . 5800 1 18 . 1 1 3 3 MET HG3 H 1 2.64 0.02 . 2 . . . . . . . . 5800 1 19 . 1 1 3 3 MET C C 13 176.46 0.2 . 1 . . . . . . . . 5800 1 20 . 1 1 3 3 MET CA C 13 55.56 0.2 . 1 . . . . . . . . 5800 1 21 . 1 1 3 3 MET CB C 13 33.27 0.2 . 1 . . . . . . . . 5800 1 22 . 1 1 3 3 MET CG C 13 32.00 0.2 . 1 . . . . . . . . 5800 1 23 . 1 1 3 3 MET N N 15 120.73 0.2 . 1 . . . . . . . . 5800 1 24 . 1 1 4 4 THR H H 1 8.36 0.02 . 1 . . . . . . . . 5800 1 25 . 1 1 4 4 THR HA H 1 4.41 0.02 . 1 . . . . . . . . 5800 1 26 . 1 1 4 4 THR HB H 1 4.30 0.02 . 1 . . . . . . . . 5800 1 27 . 1 1 4 4 THR HG21 H 1 1.22 0.02 . 1 . . . . . . . . 5800 1 28 . 1 1 4 4 THR HG22 H 1 1.22 0.02 . 1 . . . . . . . . 5800 1 29 . 1 1 4 4 THR HG23 H 1 1.22 0.02 . 1 . . . . . . . . 5800 1 30 . 1 1 4 4 THR C C 13 174.73 0.2 . 1 . . . . . . . . 5800 1 31 . 1 1 4 4 THR CA C 13 61.50 0.2 . 1 . . . . . . . . 5800 1 32 . 1 1 4 4 THR CB C 13 70.34 0.2 . 1 . . . . . . . . 5800 1 33 . 1 1 4 4 THR N N 15 116.03 0.2 . 1 . . . . . . . . 5800 1 34 . 1 1 5 5 VAL H H 1 8.33 0.02 . 1 . . . . . . . . 5800 1 35 . 1 1 5 5 VAL HA H 1 4.06 0.02 . 1 . . . . . . . . 5800 1 36 . 1 1 5 5 VAL HB H 1 2.10 0.02 . 1 . . . . . . . . 5800 1 37 . 1 1 5 5 VAL HG11 H 1 0.94 0.02 . 1 . . . . . . . . 5800 1 38 . 1 1 5 5 VAL HG12 H 1 0.94 0.02 . 1 . . . . . . . . 5800 1 39 . 1 1 5 5 VAL HG13 H 1 0.94 0.02 . 1 . . . . . . . . 5800 1 40 . 1 1 5 5 VAL HG21 H 1 0.94 0.02 . 1 . . . . . . . . 5800 1 41 . 1 1 5 5 VAL HG22 H 1 0.94 0.02 . 1 . . . . . . . . 5800 1 42 . 1 1 5 5 VAL HG23 H 1 0.94 0.02 . 1 . . . . . . . . 5800 1 43 . 1 1 5 5 VAL C C 13 176.34 0.2 . 1 . . . . . . . . 5800 1 44 . 1 1 5 5 VAL CA C 13 63.21 0.2 . 1 . . . . . . . . 5800 1 45 . 1 1 5 5 VAL CB C 13 32.49 0.2 . 1 . . . . . . . . 5800 1 46 . 1 1 5 5 VAL CG1 C 13 20.95 0.2 . 1 . . . . . . . . 5800 1 47 . 1 1 5 5 VAL CG2 C 13 20.95 0.2 . 1 . . . . . . . . 5800 1 48 . 1 1 5 5 VAL N N 15 121.43 0.2 . 1 . . . . . . . . 5800 1 49 . 1 1 6 6 ASP H H 1 8.24 0.02 . 1 . . . . . . . . 5800 1 50 . 1 1 6 6 ASP HA H 1 4.54 0.02 . 1 . . . . . . . . 5800 1 51 . 1 1 6 6 ASP HB2 H 1 2.61 0.02 . 2 . . . . . . . . 5800 1 52 . 1 1 6 6 ASP HB3 H 1 2.70 0.02 . 2 . . . . . . . . 5800 1 53 . 1 1 6 6 ASP C C 13 176.69 0.2 . 1 . . . . . . . . 5800 1 54 . 1 1 6 6 ASP CA C 13 54.70 0.2 . 1 . . . . . . . . 5800 1 55 . 1 1 6 6 ASP CB C 13 40.91 0.2 . 1 . . . . . . . . 5800 1 56 . 1 1 6 6 ASP N N 15 122.77 0.2 . 1 . . . . . . . . 5800 1 57 . 1 1 7 7 ASP H H 1 8.15 0.02 . 1 . . . . . . . . 5800 1 58 . 1 1 7 7 ASP HA H 1 4.55 0.02 . 1 . . . . . . . . 5800 1 59 . 1 1 7 7 ASP HB2 H 1 2.70 0.02 . 1 . . . . . . . . 5800 1 60 . 1 1 7 7 ASP HB3 H 1 2.70 0.02 . 1 . . . . . . . . 5800 1 61 . 1 1 7 7 ASP C C 13 177.59 0.2 . 1 . . . . . . . . 5800 1 62 . 1 1 7 7 ASP CA C 13 55.68 0.2 . 1 . . . . . . . . 5800 1 63 . 1 1 7 7 ASP CB C 13 41.94 0.2 . 1 . . . . . . . . 5800 1 64 . 1 1 7 7 ASP N N 15 121.29 0.2 . 1 . . . . . . . . 5800 1 65 . 1 1 8 8 LEU H H 1 8.22 0.02 . 1 . . . . . . . . 5800 1 66 . 1 1 8 8 LEU HA H 1 4.15 0.02 . 1 . . . . . . . . 5800 1 67 . 1 1 8 8 LEU HB2 H 1 1.55 0.02 . 2 . . . . . . . . 5800 1 68 . 1 1 8 8 LEU HB3 H 1 1.74 0.02 . 2 . . . . . . . . 5800 1 69 . 1 1 8 8 LEU HG H 1 1.62 0.02 . 1 . . . . . . . . 5800 1 70 . 1 1 8 8 LEU HD11 H 1 0.91 0.02 . 2 . . . . . . . . 5800 1 71 . 1 1 8 8 LEU HD12 H 1 0.91 0.02 . 2 . . . . . . . . 5800 1 72 . 1 1 8 8 LEU HD13 H 1 0.91 0.02 . 2 . . . . . . . . 5800 1 73 . 1 1 8 8 LEU HD21 H 1 0.87 0.02 . 2 . . . . . . . . 5800 1 74 . 1 1 8 8 LEU HD22 H 1 0.87 0.02 . 2 . . . . . . . . 5800 1 75 . 1 1 8 8 LEU HD23 H 1 0.87 0.02 . 2 . . . . . . . . 5800 1 76 . 1 1 8 8 LEU C C 13 178.83 0.2 . 1 . . . . . . . . 5800 1 77 . 1 1 8 8 LEU CA C 13 56.90 0.2 . 1 . . . . . . . . 5800 1 78 . 1 1 8 8 LEU CB C 13 41.64 0.2 . 1 . . . . . . . . 5800 1 79 . 1 1 8 8 LEU CG C 13 27.16 0.2 . 1 . . . . . . . . 5800 1 80 . 1 1 8 8 LEU CD1 C 13 25.10 0.2 . 2 . . . . . . . . 5800 1 81 . 1 1 8 8 LEU CD2 C 13 24.10 0.2 . 2 . . . . . . . . 5800 1 82 . 1 1 8 8 LEU N N 15 122.26 0.2 . 1 . . . . . . . . 5800 1 83 . 1 1 9 9 GLN H H 1 8.21 0.02 . 1 . . . . . . . . 5800 1 84 . 1 1 9 9 GLN HA H 1 4.16 0.02 . 1 . . . . . . . . 5800 1 85 . 1 1 9 9 GLN HB2 H 1 2.11 0.02 . 1 . . . . . . . . 5800 1 86 . 1 1 9 9 GLN HB3 H 1 2.11 0.02 . 1 . . . . . . . . 5800 1 87 . 1 1 9 9 GLN HG2 H 1 2.39 0.02 . 2 . . . . . . . . 5800 1 88 . 1 1 9 9 GLN HG3 H 1 2.45 0.02 . 2 . . . . . . . . 5800 1 89 . 1 1 9 9 GLN C C 13 177.71 0.2 . 1 . . . . . . . . 5800 1 90 . 1 1 9 9 GLN CA C 13 57.97 0.2 . 1 . . . . . . . . 5800 1 91 . 1 1 9 9 GLN CB C 13 28.49 0.2 . 1 . . . . . . . . 5800 1 92 . 1 1 9 9 GLN CG C 13 33.90 0.2 . 1 . . . . . . . . 5800 1 93 . 1 1 9 9 GLN N N 15 119.68 0.2 . 1 . . . . . . . . 5800 1 94 . 1 1 10 10 ALA H H 1 8.08 0.02 . 1 . . . . . . . . 5800 1 95 . 1 1 10 10 ALA HA H 1 4.16 0.02 . 1 . . . . . . . . 5800 1 96 . 1 1 10 10 ALA HB1 H 1 1.41 0.02 . 1 . . . . . . . . 5800 1 97 . 1 1 10 10 ALA HB2 H 1 1.41 0.02 . 1 . . . . . . . . 5800 1 98 . 1 1 10 10 ALA HB3 H 1 1.41 0.02 . 1 . . . . . . . . 5800 1 99 . 1 1 10 10 ALA C C 13 179.89 0.2 . 1 . . . . . . . . 5800 1 100 . 1 1 10 10 ALA CA C 13 54.27 0.2 . 1 . . . . . . . . 5800 1 101 . 1 1 10 10 ALA CB C 13 18.43 0.2 . 1 . . . . . . . . 5800 1 102 . 1 1 10 10 ALA N N 15 123.04 0.2 . 1 . . . . . . . . 5800 1 103 . 1 1 11 11 LYS H H 1 8.05 0.02 . 1 . . . . . . . . 5800 1 104 . 1 1 11 11 LYS HA H 1 4.16 0.02 . 1 . . . . . . . . 5800 1 105 . 1 1 11 11 LYS HB2 H 1 1.81 0.02 . 1 . . . . . . . . 5800 1 106 . 1 1 11 11 LYS HB3 H 1 1.81 0.02 . 1 . . . . . . . . 5800 1 107 . 1 1 11 11 LYS HG2 H 1 1.45 0.02 . 2 . . . . . . . . 5800 1 108 . 1 1 11 11 LYS HG3 H 1 1.35 0.02 . 2 . . . . . . . . 5800 1 109 . 1 1 11 11 LYS HD2 H 1 1.63 0.02 . 1 . . . . . . . . 5800 1 110 . 1 1 11 11 LYS HD3 H 1 1.63 0.02 . 1 . . . . . . . . 5800 1 111 . 1 1 11 11 LYS C C 13 177.96 0.2 . 1 . . . . . . . . 5800 1 112 . 1 1 11 11 LYS CA C 13 58.35 0.2 . 1 . . . . . . . . 5800 1 113 . 1 1 11 11 LYS CB C 13 32.56 0.2 . 1 . . . . . . . . 5800 1 114 . 1 1 11 11 LYS CG C 13 24.77 0.2 . 1 . . . . . . . . 5800 1 115 . 1 1 11 11 LYS CD C 13 29.22 0.2 . 1 . . . . . . . . 5800 1 116 . 1 1 11 11 LYS N N 15 120.12 0.2 . 1 . . . . . . . . 5800 1 117 . 1 1 12 12 HIS H H 1 8.26 0.02 . 1 . . . . . . . . 5800 1 118 . 1 1 12 12 HIS HA H 1 4.57 0.02 . 1 . . . . . . . . 5800 1 119 . 1 1 12 12 HIS HB2 H 1 3.27 0.02 . 1 . . . . . . . . 5800 1 120 . 1 1 12 12 HIS HB3 H 1 3.27 0.02 . 1 . . . . . . . . 5800 1 121 . 1 1 12 12 HIS HD2 H 1 8.37 0.02 . 1 . . . . . . . . 5800 1 122 . 1 1 12 12 HIS HE1 H 1 7.20 0.02 . 1 . . . . . . . . 5800 1 123 . 1 1 12 12 HIS C C 13 176.72 0.2 . 1 . . . . . . . . 5800 1 124 . 1 1 12 12 HIS CA C 13 57.24 0.2 . 1 . . . . . . . . 5800 1 125 . 1 1 12 12 HIS CB C 13 28.99 0.2 . 1 . . . . . . . . 5800 1 126 . 1 1 12 12 HIS CE1 C 13 137.129 0.2 . 1 . . . . . . . . 5800 1 127 . 1 1 12 12 HIS CD2 C 13 119.948 0.2 . 1 . . . . . . . . 5800 1 128 . 1 1 12 12 HIS N N 15 118.25 0.2 . 1 . . . . . . . . 5800 1 129 . 1 1 13 13 GLN H H 1 8.39 0.02 . 1 . . . . . . . . 5800 1 130 . 1 1 13 13 GLN HA H 1 4.17 0.02 . 1 . . . . . . . . 5800 1 131 . 1 1 13 13 GLN HB2 H 1 2.12 0.02 . 1 . . . . . . . . 5800 1 132 . 1 1 13 13 GLN HB3 H 1 2.12 0.02 . 1 . . . . . . . . 5800 1 133 . 1 1 13 13 GLN HG2 H 1 2.41 0.02 . 1 . . . . . . . . 5800 1 134 . 1 1 13 13 GLN HG3 H 1 2.41 0.02 . 1 . . . . . . . . 5800 1 135 . 1 1 13 13 GLN C C 13 177.59 0.2 . 1 . . . . . . . . 5800 1 136 . 1 1 13 13 GLN CA C 13 58.05 0.2 . 1 . . . . . . . . 5800 1 137 . 1 1 13 13 GLN CB C 13 28.66 0.2 . 1 . . . . . . . . 5800 1 138 . 1 1 13 13 GLN CG C 13 34.10 0.2 . 1 . . . . . . . . 5800 1 139 . 1 1 13 13 GLN N N 15 120.16 0.2 . 1 . . . . . . . . 5800 1 140 . 1 1 14 14 ALA H H 1 8.18 0.02 . 1 . . . . . . . . 5800 1 141 . 1 1 14 14 ALA HA H 1 4.25 0.02 . 1 . . . . . . . . 5800 1 142 . 1 1 14 14 ALA HB1 H 1 1.50 0.02 . 1 . . . . . . . . 5800 1 143 . 1 1 14 14 ALA HB2 H 1 1.50 0.02 . 1 . . . . . . . . 5800 1 144 . 1 1 14 14 ALA HB3 H 1 1.50 0.02 . 1 . . . . . . . . 5800 1 145 . 1 1 14 14 ALA C C 13 180.34 0.2 . 1 . . . . . . . . 5800 1 146 . 1 1 14 14 ALA CA C 13 54.89 0.2 . 1 . . . . . . . . 5800 1 147 . 1 1 14 14 ALA CB C 13 18.28 0.2 . 1 . . . . . . . . 5800 1 148 . 1 1 14 14 ALA N N 15 123.49 0.2 . 1 . . . . . . . . 5800 1 149 . 1 1 15 15 GLU H H 1 8.34 0.02 . 1 . . . . . . . . 5800 1 150 . 1 1 15 15 GLU HA H 1 4.12 0.02 . 1 . . . . . . . . 5800 1 151 . 1 1 15 15 GLU HB2 H 1 2.11 0.02 . 1 . . . . . . . . 5800 1 152 . 1 1 15 15 GLU HB3 H 1 2.11 0.02 . 1 . . . . . . . . 5800 1 153 . 1 1 15 15 GLU HG2 H 1 2.46 0.02 . 2 . . . . . . . . 5800 1 154 . 1 1 15 15 GLU HG3 H 1 2.31 0.02 . 2 . . . . . . . . 5800 1 155 . 1 1 15 15 GLU C C 13 178.84 0.2 . 1 . . . . . . . . 5800 1 156 . 1 1 15 15 GLU CA C 13 58.56 0.2 . 1 . . . . . . . . 5800 1 157 . 1 1 15 15 GLU CB C 13 29.34 0.2 . 1 . . . . . . . . 5800 1 158 . 1 1 15 15 GLU CG C 13 36.47 0.2 . 1 . . . . . . . . 5800 1 159 . 1 1 15 15 GLU N N 15 119.82 0.2 . 1 . . . . . . . . 5800 1 160 . 1 1 16 16 ALA H H 1 8.19 0.02 . 1 . . . . . . . . 5800 1 161 . 1 1 16 16 ALA HA H 1 4.13 0.02 . 1 . . . . . . . . 5800 1 162 . 1 1 16 16 ALA HB1 H 1 1.37 0.02 . 1 . . . . . . . . 5800 1 163 . 1 1 16 16 ALA HB2 H 1 1.37 0.02 . 1 . . . . . . . . 5800 1 164 . 1 1 16 16 ALA HB3 H 1 1.37 0.02 . 1 . . . . . . . . 5800 1 165 . 1 1 16 16 ALA C C 13 178.97 0.2 . 1 . . . . . . . . 5800 1 166 . 1 1 16 16 ALA CA C 13 54.75 0.2 . 1 . . . . . . . . 5800 1 167 . 1 1 16 16 ALA CB C 13 18.05 0.2 . 1 . . . . . . . . 5800 1 168 . 1 1 16 16 ALA N N 15 123.91 0.2 . 1 . . . . . . . . 5800 1 169 . 1 1 17 17 HIS H H 1 8.23 0.02 . 1 . . . . . . . . 5800 1 170 . 1 1 17 17 HIS HA H 1 4.27 0.02 . 1 . . . . . . . . 5800 1 171 . 1 1 17 17 HIS HB2 H 1 3.28 0.02 . 1 . . . . . . . . 5800 1 172 . 1 1 17 17 HIS HB3 H 1 3.28 0.02 . 1 . . . . . . . . 5800 1 173 . 1 1 17 17 HIS HD2 H 1 8.43 0.02 . 1 . . . . . . . . 5800 1 174 . 1 1 17 17 HIS HE1 H 1 7.26 0.02 . 1 . . . . . . . . 5800 1 175 . 1 1 17 17 HIS C C 13 176.53 0.2 . 1 . . . . . . . . 5800 1 176 . 1 1 17 17 HIS CA C 13 58.70 0.2 . 1 . . . . . . . . 5800 1 177 . 1 1 17 17 HIS CB C 13 28.61 0.2 . 1 . . . . . . . . 5800 1 178 . 1 1 17 17 HIS CD2 C 13 119.962 0.2 . 1 . . . . . . . . 5800 1 179 . 1 1 17 17 HIS CE1 C 13 136.885 0.2 . 1 . . . . . . . . 5800 1 180 . 1 1 17 17 HIS N N 15 115.45 0.2 . 1 . . . . . . . . 5800 1 181 . 1 1 18 18 ALA H H 1 7.95 0.02 . 1 . . . . . . . . 5800 1 182 . 1 1 18 18 ALA HA H 1 4.21 0.02 . 1 . . . . . . . . 5800 1 183 . 1 1 18 18 ALA HB1 H 1 1.49 0.02 . 1 . . . . . . . . 5800 1 184 . 1 1 18 18 ALA HB2 H 1 1.49 0.02 . 1 . . . . . . . . 5800 1 185 . 1 1 18 18 ALA HB3 H 1 1.49 0.02 . 1 . . . . . . . . 5800 1 186 . 1 1 18 18 ALA C C 13 179.84 0.2 . 1 . . . . . . . . 5800 1 187 . 1 1 18 18 ALA CA C 13 54.83 0.2 . 1 . . . . . . . . 5800 1 188 . 1 1 18 18 ALA CB C 13 17.97 0.2 . 1 . . . . . . . . 5800 1 189 . 1 1 18 18 ALA N N 15 121.98 0.2 . 1 . . . . . . . . 5800 1 190 . 1 1 19 19 ALA H H 1 7.81 0.02 . 1 . . . . . . . . 5800 1 191 . 1 1 19 19 ALA HA H 1 3.82 0.02 . 1 . . . . . . . . 5800 1 192 . 1 1 19 19 ALA HB1 H 1 1.21 0.02 . 1 . . . . . . . . 5800 1 193 . 1 1 19 19 ALA HB2 H 1 1.21 0.02 . 1 . . . . . . . . 5800 1 194 . 1 1 19 19 ALA HB3 H 1 1.21 0.02 . 1 . . . . . . . . 5800 1 195 . 1 1 19 19 ALA C C 13 178.46 0.2 . 1 . . . . . . . . 5800 1 196 . 1 1 19 19 ALA CA C 13 54.94 0.2 . 1 . . . . . . . . 5800 1 197 . 1 1 19 19 ALA CB C 13 18.74 0.2 . 1 . . . . . . . . 5800 1 198 . 1 1 19 19 ALA N N 15 122.43 0.2 . 1 . . . . . . . . 5800 1 199 . 1 1 20 20 ILE H H 1 7.95 0.02 . 1 . . . . . . . . 5800 1 200 . 1 1 20 20 ILE HA H 1 3.33 0.02 . 1 . . . . . . . . 5800 1 201 . 1 1 20 20 ILE HB H 1 1.82 0.02 . 1 . . . . . . . . 5800 1 202 . 1 1 20 20 ILE HG12 H 1 0.87 0.02 . 1 . . . . . . . . 5800 1 203 . 1 1 20 20 ILE HG13 H 1 0.87 0.02 . 1 . . . . . . . . 5800 1 204 . 1 1 20 20 ILE HG21 H 1 0.92 0.02 . 1 . . . . . . . . 5800 1 205 . 1 1 20 20 ILE HG22 H 1 0.92 0.02 . 1 . . . . . . . . 5800 1 206 . 1 1 20 20 ILE HG23 H 1 0.92 0.02 . 1 . . . . . . . . 5800 1 207 . 1 1 20 20 ILE HD11 H 1 0.81 0.02 . 1 . . . . . . . . 5800 1 208 . 1 1 20 20 ILE HD12 H 1 0.81 0.02 . 1 . . . . . . . . 5800 1 209 . 1 1 20 20 ILE HD13 H 1 0.81 0.02 . 1 . . . . . . . . 5800 1 210 . 1 1 20 20 ILE C C 13 178.22 0.2 . 1 . . . . . . . . 5800 1 211 . 1 1 20 20 ILE CA C 13 65.92 0.2 . 1 . . . . . . . . 5800 1 212 . 1 1 20 20 ILE CB C 13 38.05 0.2 . 1 . . . . . . . . 5800 1 213 . 1 1 20 20 ILE CG1 C 13 29.73 0.2 . 1 . . . . . . . . 5800 1 214 . 1 1 20 20 ILE CG2 C 13 17.27 0.2 . 1 . . . . . . . . 5800 1 215 . 1 1 20 20 ILE CD1 C 13 13.85 0.2 . 1 . . . . . . . . 5800 1 216 . 1 1 20 20 ILE N N 15 117.99 0.2 . 1 . . . . . . . . 5800 1 217 . 1 1 21 21 ASP H H 1 7.89 0.02 . 1 . . . . . . . . 5800 1 218 . 1 1 21 21 ASP HA H 1 4.37 0.02 . 1 . . . . . . . . 5800 1 219 . 1 1 21 21 ASP HB2 H 1 2.69 0.02 . 1 . . . . . . . . 5800 1 220 . 1 1 21 21 ASP HB3 H 1 2.69 0.02 . 1 . . . . . . . . 5800 1 221 . 1 1 21 21 ASP C C 13 178.29 0.2 . 1 . . . . . . . . 5800 1 222 . 1 1 21 21 ASP CA C 13 57.13 0.2 . 1 . . . . . . . . 5800 1 223 . 1 1 21 21 ASP CB C 13 40.49 0.2 . 1 . . . . . . . . 5800 1 224 . 1 1 21 21 ASP N N 15 119.35 0.2 . 1 . . . . . . . . 5800 1 225 . 1 1 22 22 THR H H 1 7.97 0.02 . 1 . . . . . . . . 5800 1 226 . 1 1 22 22 THR HA H 1 4.02 0.02 . 1 . . . . . . . . 5800 1 227 . 1 1 22 22 THR HB H 1 4.26 0.02 . 1 . . . . . . . . 5800 1 228 . 1 1 22 22 THR HG21 H 1 1.36 0.02 . 1 . . . . . . . . 5800 1 229 . 1 1 22 22 THR HG22 H 1 1.36 0.02 . 1 . . . . . . . . 5800 1 230 . 1 1 22 22 THR HG23 H 1 1.36 0.02 . 1 . . . . . . . . 5800 1 231 . 1 1 22 22 THR C C 13 176.09 0.2 . 1 . . . . . . . . 5800 1 232 . 1 1 22 22 THR CA C 13 67.07 0.2 . 1 . . . . . . . . 5800 1 233 . 1 1 22 22 THR CB C 13 68.64 0.2 . 1 . . . . . . . . 5800 1 234 . 1 1 22 22 THR N N 15 117.54 0.2 . 1 . . . . . . . . 5800 1 235 . 1 1 23 23 PHE H H 1 8.64 0.02 . 1 . . . . . . . . 5800 1 236 . 1 1 23 23 PHE HA H 1 4.51 0.02 . 1 . . . . . . . . 5800 1 237 . 1 1 23 23 PHE HB2 H 1 2.96 0.02 . 2 . . . . . . . . 5800 1 238 . 1 1 23 23 PHE HB3 H 1 3.37 0.02 . 2 . . . . . . . . 5800 1 239 . 1 1 23 23 PHE HD1 H 1 6.86 0.02 . 1 . . . . . . . . 5800 1 240 . 1 1 23 23 PHE HD2 H 1 6.86 0.02 . 1 . . . . . . . . 5800 1 241 . 1 1 23 23 PHE HE1 H 1 6.99 0.02 . 1 . . . . . . . . 5800 1 242 . 1 1 23 23 PHE HE2 H 1 6.99 0.02 . 1 . . . . . . . . 5800 1 243 . 1 1 23 23 PHE HZ H 1 6.73 0.02 . 1 . . . . . . . . 5800 1 244 . 1 1 23 23 PHE C C 13 178.76 0.2 . 1 . . . . . . . . 5800 1 245 . 1 1 23 23 PHE CA C 13 57.92 0.2 . 1 . . . . . . . . 5800 1 246 . 1 1 23 23 PHE CB C 13 37.54 0.2 . 1 . . . . . . . . 5800 1 247 . 1 1 23 23 PHE N N 15 120.69 0.2 . 1 . . . . . . . . 5800 1 248 . 1 1 24 24 THR H H 1 8.80 0.02 . 1 . . . . . . . . 5800 1 249 . 1 1 24 24 THR HA H 1 4.13 0.02 . 1 . . . . . . . . 5800 1 250 . 1 1 24 24 THR HB H 1 4.30 0.02 . 1 . . . . . . . . 5800 1 251 . 1 1 24 24 THR HG21 H 1 1.30 0.02 . 1 . . . . . . . . 5800 1 252 . 1 1 24 24 THR HG22 H 1 1.30 0.02 . 1 . . . . . . . . 5800 1 253 . 1 1 24 24 THR HG23 H 1 1.30 0.02 . 1 . . . . . . . . 5800 1 254 . 1 1 24 24 THR C C 13 179.34 0.2 . 1 . . . . . . . . 5800 1 255 . 1 1 24 24 THR CA C 13 65.76 0.2 . 1 . . . . . . . . 5800 1 256 . 1 1 24 24 THR CB C 13 68.75 0.2 . 1 . . . . . . . . 5800 1 257 . 1 1 24 24 THR N N 15 111.91 0.2 . 1 . . . . . . . . 5800 1 258 . 1 1 25 25 LYS H H 1 7.74 0.02 . 1 . . . . . . . . 5800 1 259 . 1 1 25 25 LYS HA H 1 4.00 0.02 . 1 . . . . . . . . 5800 1 260 . 1 1 25 25 LYS HB2 H 1 1.59 0.02 . 2 . . . . . . . . 5800 1 261 . 1 1 25 25 LYS HB3 H 1 1.86 0.02 . 2 . . . . . . . . 5800 1 262 . 1 1 25 25 LYS HG2 H 1 1.06 0.02 . 2 . . . . . . . . 5800 1 263 . 1 1 25 25 LYS HG3 H 1 0.51 0.02 . 2 . . . . . . . . 5800 1 264 . 1 1 25 25 LYS HD2 H 1 1.38 0.02 . 2 . . . . . . . . 5800 1 265 . 1 1 25 25 LYS HD3 H 1 1.45 0.02 . 2 . . . . . . . . 5800 1 266 . 1 1 25 25 LYS HE2 H 1 2.75 0.02 . 1 . . . . . . . . 5800 1 267 . 1 1 25 25 LYS HE3 H 1 2.75 0.02 . 1 . . . . . . . . 5800 1 268 . 1 1 25 25 LYS C C 13 178.97 0.2 . 1 . . . . . . . . 5800 1 269 . 1 1 25 25 LYS CA C 13 59.27 0.2 . 1 . . . . . . . . 5800 1 270 . 1 1 25 25 LYS CB C 13 32.84 0.2 . 1 . . . . . . . . 5800 1 271 . 1 1 25 25 LYS CG C 13 24.58 0.2 . 1 . . . . . . . . 5800 1 272 . 1 1 25 25 LYS CD C 13 29.22 0.2 . 1 . . . . . . . . 5800 1 273 . 1 1 25 25 LYS CE C 13 42.00 0.2 . 1 . . . . . . . . 5800 1 274 . 1 1 25 25 LYS N N 15 120.94 0.2 . 1 . . . . . . . . 5800 1 275 . 1 1 26 26 TYR H H 1 8.07 0.02 . 1 . . . . . . . . 5800 1 276 . 1 1 26 26 TYR HA H 1 4.60 0.02 . 1 . . . . . . . . 5800 1 277 . 1 1 26 26 TYR HB2 H 1 2.83 0.02 . 2 . . . . . . . . 5800 1 278 . 1 1 26 26 TYR HB3 H 1 3.05 0.02 . 2 . . . . . . . . 5800 1 279 . 1 1 26 26 TYR HD1 H 1 7.54 0.02 . 1 . . . . . . . . 5800 1 280 . 1 1 26 26 TYR HD2 H 1 7.54 0.02 . 1 . . . . . . . . 5800 1 281 . 1 1 26 26 TYR HE1 H 1 6.88 0.02 . 1 . . . . . . . . 5800 1 282 . 1 1 26 26 TYR HE2 H 1 6.88 0.02 . 1 . . . . . . . . 5800 1 283 . 1 1 26 26 TYR C C 13 177.34 0.2 . 1 . . . . . . . . 5800 1 284 . 1 1 26 26 TYR CA C 13 60.95 0.2 . 1 . . . . . . . . 5800 1 285 . 1 1 26 26 TYR CB C 13 39.70 0.2 . 1 . . . . . . . . 5800 1 286 . 1 1 26 26 TYR N N 15 112.43 0.2 . 1 . . . . . . . . 5800 1 287 . 1 1 27 27 LEU H H 1 8.18 0.02 . 1 . . . . . . . . 5800 1 288 . 1 1 27 27 LEU HA H 1 4.51 0.02 . 1 . . . . . . . . 5800 1 289 . 1 1 27 27 LEU HB2 H 1 1.37 0.02 . 2 . . . . . . . . 5800 1 290 . 1 1 27 27 LEU HB3 H 1 1.97 0.02 . 2 . . . . . . . . 5800 1 291 . 1 1 27 27 LEU HG H 1 2.00 0.02 . 1 . . . . . . . . 5800 1 292 . 1 1 27 27 LEU HD11 H 1 0.62 0.02 . 2 . . . . . . . . 5800 1 293 . 1 1 27 27 LEU HD12 H 1 0.62 0.02 . 2 . . . . . . . . 5800 1 294 . 1 1 27 27 LEU HD13 H 1 0.62 0.02 . 2 . . . . . . . . 5800 1 295 . 1 1 27 27 LEU HD21 H 1 0.36 0.02 . 2 . . . . . . . . 5800 1 296 . 1 1 27 27 LEU HD22 H 1 0.36 0.02 . 2 . . . . . . . . 5800 1 297 . 1 1 27 27 LEU HD23 H 1 0.36 0.02 . 2 . . . . . . . . 5800 1 298 . 1 1 27 27 LEU C C 13 175.46 0.2 . 1 . . . . . . . . 5800 1 299 . 1 1 27 27 LEU CA C 13 53.97 0.2 . 1 . . . . . . . . 5800 1 300 . 1 1 27 27 LEU CB C 13 41.71 0.2 . 1 . . . . . . . . 5800 1 301 . 1 1 27 27 LEU CG C 13 27.60 0.2 . 1 . . . . . . . . 5800 1 302 . 1 1 27 27 LEU CD1 C 13 22.22 0.2 . 2 . . . . . . . . 5800 1 303 . 1 1 27 27 LEU CD2 C 13 25.85 0.2 . 2 . . . . . . . . 5800 1 304 . 1 1 27 27 LEU N N 15 114.45 0.2 . 1 . . . . . . . . 5800 1 305 . 1 1 28 28 ASP H H 1 7.72 0.02 . 1 . . . . . . . . 5800 1 306 . 1 1 28 28 ASP HA H 1 4.42 0.02 . 1 . . . . . . . . 5800 1 307 . 1 1 28 28 ASP HB2 H 1 2.42 0.02 . 2 . . . . . . . . 5800 1 308 . 1 1 28 28 ASP HB3 H 1 3.03 0.02 . 2 . . . . . . . . 5800 1 309 . 1 1 28 28 ASP C C 13 174.59 0.2 . 1 . . . . . . . . 5800 1 310 . 1 1 28 28 ASP CA C 13 55.38 0.2 . 1 . . . . . . . . 5800 1 311 . 1 1 28 28 ASP CB C 13 39.41 0.2 . 1 . . . . . . . . 5800 1 312 . 1 1 28 28 ASP N N 15 116.62 0.2 . 1 . . . . . . . . 5800 1 313 . 1 1 29 29 ILE H H 1 6.59 0.02 . 1 . . . . . . . . 5800 1 314 . 1 1 29 29 ILE HA H 1 4.78 0.02 . 1 . . . . . . . . 5800 1 315 . 1 1 29 29 ILE HB H 1 2.10 0.02 . 1 . . . . . . . . 5800 1 316 . 1 1 29 29 ILE HG12 H 1 1.28 0.02 . 2 . . . . . . . . 5800 1 317 . 1 1 29 29 ILE HG13 H 1 0.82 0.02 . 2 . . . . . . . . 5800 1 318 . 1 1 29 29 ILE HG21 H 1 0.69 0.02 . 1 . . . . . . . . 5800 1 319 . 1 1 29 29 ILE HG22 H 1 0.69 0.02 . 1 . . . . . . . . 5800 1 320 . 1 1 29 29 ILE HG23 H 1 0.69 0.02 . 1 . . . . . . . . 5800 1 321 . 1 1 29 29 ILE HD11 H 1 0.41 0.02 . 1 . . . . . . . . 5800 1 322 . 1 1 29 29 ILE HD12 H 1 0.41 0.02 . 1 . . . . . . . . 5800 1 323 . 1 1 29 29 ILE HD13 H 1 0.41 0.02 . 1 . . . . . . . . 5800 1 324 . 1 1 29 29 ILE C C 13 174.83 0.2 . 1 . . . . . . . . 5800 1 325 . 1 1 29 29 ILE CA C 13 58.67 0.2 . 1 . . . . . . . . 5800 1 326 . 1 1 29 29 ILE CB C 13 41.23 0.2 . 1 . . . . . . . . 5800 1 327 . 1 1 29 29 ILE CG1 C 13 24.30 0.2 . 1 . . . . . . . . 5800 1 328 . 1 1 29 29 ILE CG2 C 13 17.06 0.2 . 1 . . . . . . . . 5800 1 329 . 1 1 29 29 ILE CD1 C 13 14.09 0.2 . 1 . . . . . . . . 5800 1 330 . 1 1 29 29 ILE N N 15 107.14 0.2 . 1 . . . . . . . . 5800 1 331 . 1 1 30 30 ASP H H 1 8.35 0.02 . 1 . . . . . . . . 5800 1 332 . 1 1 30 30 ASP HA H 1 4.72 0.02 . 1 . . . . . . . . 5800 1 333 . 1 1 30 30 ASP HB2 H 1 2.79 0.02 . 2 . . . . . . . . 5800 1 334 . 1 1 30 30 ASP HB3 H 1 3.09 0.02 . 2 . . . . . . . . 5800 1 335 . 1 1 30 30 ASP C C 13 176.41 0.2 . 1 . . . . . . . . 5800 1 336 . 1 1 30 30 ASP CA C 13 52.81 0.2 . 1 . . . . . . . . 5800 1 337 . 1 1 30 30 ASP CB C 13 42.05 0.2 . 1 . . . . . . . . 5800 1 338 . 1 1 30 30 ASP N N 15 119.21 0.2 . 1 . . . . . . . . 5800 1 339 . 1 1 31 31 GLU H H 1 8.89 0.02 . 1 . . . . . . . . 5800 1 340 . 1 1 31 31 GLU HA H 1 3.77 0.02 . 1 . . . . . . . . 5800 1 341 . 1 1 31 31 GLU HB2 H 1 2.06 0.02 . 2 . . . . . . . . 5800 1 342 . 1 1 31 31 GLU HB3 H 1 2.13 0.02 . 2 . . . . . . . . 5800 1 343 . 1 1 31 31 GLU HG2 H 1 2.28 0.02 . 1 . . . . . . . . 5800 1 344 . 1 1 31 31 GLU HG3 H 1 2.28 0.02 . 1 . . . . . . . . 5800 1 345 . 1 1 31 31 GLU C C 13 179.04 0.2 . 1 . . . . . . . . 5800 1 346 . 1 1 31 31 GLU CA C 13 60.08 0.2 . 1 . . . . . . . . 5800 1 347 . 1 1 31 31 GLU CB C 13 29.68 0.2 . 1 . . . . . . . . 5800 1 348 . 1 1 31 31 GLU CG C 13 36.95 0.2 . 1 . . . . . . . . 5800 1 349 . 1 1 31 31 GLU N N 15 119.48 0.2 . 1 . . . . . . . . 5800 1 350 . 1 1 32 32 ASP H H 1 8.60 0.02 . 1 . . . . . . . . 5800 1 351 . 1 1 32 32 ASP HA H 1 4.42 0.02 . 1 . . . . . . . . 5800 1 352 . 1 1 32 32 ASP HB2 H 1 2.71 0.02 . 2 . . . . . . . . 5800 1 353 . 1 1 32 32 ASP HB3 H 1 2.83 0.02 . 2 . . . . . . . . 5800 1 354 . 1 1 32 32 ASP C C 13 178.34 0.2 . 1 . . . . . . . . 5800 1 355 . 1 1 32 32 ASP CA C 13 57.79 0.2 . 1 . . . . . . . . 5800 1 356 . 1 1 32 32 ASP CB C 13 39.58 0.2 . 1 . . . . . . . . 5800 1 357 . 1 1 32 32 ASP N N 15 121.89 0.2 . 1 . . . . . . . . 5800 1 358 . 1 1 33 33 PHE H H 1 8.33 0.02 . 1 . . . . . . . . 5800 1 359 . 1 1 33 33 PHE HA H 1 4.68 0.02 . 1 . . . . . . . . 5800 1 360 . 1 1 33 33 PHE HB2 H 1 3.13 0.02 . 2 . . . . . . . . 5800 1 361 . 1 1 33 33 PHE HB3 H 1 3.45 0.02 . 2 . . . . . . . . 5800 1 362 . 1 1 33 33 PHE HD1 H 1 7.17 0.02 . 1 . . . . . . . . 5800 1 363 . 1 1 33 33 PHE HD2 H 1 7.17 0.02 . 1 . . . . . . . . 5800 1 364 . 1 1 33 33 PHE HE1 H 1 7.38 0.02 . 1 . . . . . . . . 5800 1 365 . 1 1 33 33 PHE HE2 H 1 7.38 0.02 . 1 . . . . . . . . 5800 1 366 . 1 1 33 33 PHE HZ H 1 6.95 0.02 . 1 . . . . . . . . 5800 1 367 . 1 1 33 33 PHE C C 13 177.84 0.2 . 1 . . . . . . . . 5800 1 368 . 1 1 33 33 PHE CA C 13 58.45 0.2 . 1 . . . . . . . . 5800 1 369 . 1 1 33 33 PHE CB C 13 38.60 0.2 . 1 . . . . . . . . 5800 1 370 . 1 1 33 33 PHE N N 15 123.51 0.2 . 1 . . . . . . . . 5800 1 371 . 1 1 34 34 ALA H H 1 8.56 0.02 . 1 . . . . . . . . 5800 1 372 . 1 1 34 34 ALA HA H 1 3.86 0.02 . 1 . . . . . . . . 5800 1 373 . 1 1 34 34 ALA HB1 H 1 1.63 0.02 . 1 . . . . . . . . 5800 1 374 . 1 1 34 34 ALA HB2 H 1 1.63 0.02 . 1 . . . . . . . . 5800 1 375 . 1 1 34 34 ALA HB3 H 1 1.63 0.02 . 1 . . . . . . . . 5800 1 376 . 1 1 34 34 ALA C C 13 178.34 0.2 . 1 . . . . . . . . 5800 1 377 . 1 1 34 34 ALA CA C 13 55.89 0.2 . 1 . . . . . . . . 5800 1 378 . 1 1 34 34 ALA CB C 13 20.45 0.2 . 1 . . . . . . . . 5800 1 379 . 1 1 34 34 ALA N N 15 120.30 0.2 . 1 . . . . . . . . 5800 1 380 . 1 1 35 35 THR H H 1 8.17 0.02 . 1 . . . . . . . . 5800 1 381 . 1 1 35 35 THR HA H 1 3.78 0.02 . 1 . . . . . . . . 5800 1 382 . 1 1 35 35 THR HB H 1 4.49 0.02 . 1 . . . . . . . . 5800 1 383 . 1 1 35 35 THR HG21 H 1 1.25 0.02 . 1 . . . . . . . . 5800 1 384 . 1 1 35 35 THR HG22 H 1 1.25 0.02 . 1 . . . . . . . . 5800 1 385 . 1 1 35 35 THR HG23 H 1 1.25 0.02 . 1 . . . . . . . . 5800 1 386 . 1 1 35 35 THR C C 13 175.71 0.2 . 1 . . . . . . . . 5800 1 387 . 1 1 35 35 THR CA C 13 67.71 0.2 . 1 . . . . . . . . 5800 1 388 . 1 1 35 35 THR CB C 13 68.84 0.2 . 1 . . . . . . . . 5800 1 389 . 1 1 35 35 THR N N 15 112.85 0.2 . 1 . . . . . . . . 5800 1 390 . 1 1 36 36 VAL H H 1 7.49 0.02 . 1 . . . . . . . . 5800 1 391 . 1 1 36 36 VAL HA H 1 3.76 0.02 . 1 . . . . . . . . 5800 1 392 . 1 1 36 36 VAL HB H 1 2.40 0.02 . 1 . . . . . . . . 5800 1 393 . 1 1 36 36 VAL HG11 H 1 1.17 0.02 . 2 . . . . . . . . 5800 1 394 . 1 1 36 36 VAL HG12 H 1 1.17 0.02 . 2 . . . . . . . . 5800 1 395 . 1 1 36 36 VAL HG13 H 1 1.17 0.02 . 2 . . . . . . . . 5800 1 396 . 1 1 36 36 VAL HG21 H 1 1.01 0.02 . 2 . . . . . . . . 5800 1 397 . 1 1 36 36 VAL HG22 H 1 1.01 0.02 . 2 . . . . . . . . 5800 1 398 . 1 1 36 36 VAL HG23 H 1 1.01 0.02 . 2 . . . . . . . . 5800 1 399 . 1 1 36 36 VAL C C 13 178.10 0.2 . 1 . . . . . . . . 5800 1 400 . 1 1 36 36 VAL CA C 13 66.75 0.2 . 1 . . . . . . . . 5800 1 401 . 1 1 36 36 VAL CB C 13 31.52 0.2 . 1 . . . . . . . . 5800 1 402 . 1 1 36 36 VAL CG1 C 13 22.76 0.2 . 2 . . . . . . . . 5800 1 403 . 1 1 36 36 VAL CG2 C 13 20.96 0.2 . 2 . . . . . . . . 5800 1 404 . 1 1 36 36 VAL N N 15 122.79 0.2 . 1 . . . . . . . . 5800 1 405 . 1 1 37 37 LEU H H 1 7.58 0.02 . 1 . . . . . . . . 5800 1 406 . 1 1 37 37 LEU HA H 1 3.95 0.02 . 1 . . . . . . . . 5800 1 407 . 1 1 37 37 LEU HB2 H 1 2.16 0.02 . 2 . . . . . . . . 5800 1 408 . 1 1 37 37 LEU HB3 H 1 1.24 0.02 . 2 . . . . . . . . 5800 1 409 . 1 1 37 37 LEU HG H 1 1.47 0.02 . 1 . . . . . . . . 5800 1 410 . 1 1 37 37 LEU HD11 H 1 0.44 0.02 . 2 . . . . . . . . 5800 1 411 . 1 1 37 37 LEU HD12 H 1 0.44 0.02 . 2 . . . . . . . . 5800 1 412 . 1 1 37 37 LEU HD13 H 1 0.44 0.02 . 2 . . . . . . . . 5800 1 413 . 1 1 37 37 LEU HD21 H 1 0.14 0.02 . 2 . . . . . . . . 5800 1 414 . 1 1 37 37 LEU HD22 H 1 0.14 0.02 . 2 . . . . . . . . 5800 1 415 . 1 1 37 37 LEU HD23 H 1 0.14 0.02 . 2 . . . . . . . . 5800 1 416 . 1 1 37 37 LEU C C 13 178.90 0.2 . 1 . . . . . . . . 5800 1 417 . 1 1 37 37 LEU CA C 13 58.60 0.2 . 1 . . . . . . . . 5800 1 418 . 1 1 37 37 LEU CB C 13 41.65 0.2 . 1 . . . . . . . . 5800 1 419 . 1 1 37 37 LEU CG C 13 26.05 0.2 . 1 . . . . . . . . 5800 1 420 . 1 1 37 37 LEU CD1 C 13 22.10 0.2 . 2 . . . . . . . . 5800 1 421 . 1 1 37 37 LEU CD2 C 13 25.60 0.2 . 2 . . . . . . . . 5800 1 422 . 1 1 37 37 LEU N N 15 117.03 0.2 . 1 . . . . . . . . 5800 1 423 . 1 1 38 38 VAL H H 1 8.01 0.02 . 1 . . . . . . . . 5800 1 424 . 1 1 38 38 VAL HA H 1 4.28 0.02 . 1 . . . . . . . . 5800 1 425 . 1 1 38 38 VAL HB H 1 2.10 0.02 . 1 . . . . . . . . 5800 1 426 . 1 1 38 38 VAL HG11 H 1 1.09 0.02 . 2 . . . . . . . . 5800 1 427 . 1 1 38 38 VAL HG12 H 1 1.09 0.02 . 2 . . . . . . . . 5800 1 428 . 1 1 38 38 VAL HG13 H 1 1.09 0.02 . 2 . . . . . . . . 5800 1 429 . 1 1 38 38 VAL HG21 H 1 0.97 0.02 . 2 . . . . . . . . 5800 1 430 . 1 1 38 38 VAL HG22 H 1 0.97 0.02 . 2 . . . . . . . . 5800 1 431 . 1 1 38 38 VAL HG23 H 1 0.97 0.02 . 2 . . . . . . . . 5800 1 432 . 1 1 38 38 VAL C C 13 181.72 0.2 . 1 . . . . . . . . 5800 1 433 . 1 1 38 38 VAL CA C 13 65.84 0.2 . 1 . . . . . . . . 5800 1 434 . 1 1 38 38 VAL CB C 13 32.06 0.2 . 1 . . . . . . . . 5800 1 435 . 1 1 38 38 VAL CG1 C 13 24.16 0.2 . 2 . . . . . . . . 5800 1 436 . 1 1 38 38 VAL CG2 C 13 21.27 0.2 . 2 . . . . . . . . 5800 1 437 . 1 1 38 38 VAL N N 15 119.15 0.2 . 1 . . . . . . . . 5800 1 438 . 1 1 39 39 GLU H H 1 8.92 0.02 . 1 . . . . . . . . 5800 1 439 . 1 1 39 39 GLU HA H 1 4.06 0.02 . 1 . . . . . . . . 5800 1 440 . 1 1 39 39 GLU HB2 H 1 2.14 0.02 . 2 . . . . . . . . 5800 1 441 . 1 1 39 39 GLU HB3 H 1 2.29 0.02 . 2 . . . . . . . . 5800 1 442 . 1 1 39 39 GLU HG2 H 1 2.56 0.02 . 2 . . . . . . . . 5800 1 443 . 1 1 39 39 GLU HG3 H 1 2.37 0.02 . 2 . . . . . . . . 5800 1 444 . 1 1 39 39 GLU C C 13 178.91 0.2 . 1 . . . . . . . . 5800 1 445 . 1 1 39 39 GLU CA C 13 59.19 0.2 . 1 . . . . . . . . 5800 1 446 . 1 1 39 39 GLU CB C 13 28.84 0.2 . 1 . . . . . . . . 5800 1 447 . 1 1 39 39 GLU CG C 13 36.95 0.2 . 1 . . . . . . . . 5800 1 448 . 1 1 39 39 GLU N N 15 123.10 0.2 . 1 . . . . . . . . 5800 1 449 . 1 1 40 40 GLU H H 1 8.00 0.02 . 1 . . . . . . . . 5800 1 450 . 1 1 40 40 GLU HA H 1 4.34 0.02 . 1 . . . . . . . . 5800 1 451 . 1 1 40 40 GLU HB2 H 1 2.19 0.02 . 2 . . . . . . . . 5800 1 452 . 1 1 40 40 GLU HB3 H 1 2.49 0.02 . 2 . . . . . . . . 5800 1 453 . 1 1 40 40 GLU HG2 H 1 2.66 0.02 . 2 . . . . . . . . 5800 1 454 . 1 1 40 40 GLU HG3 H 1 2.42 0.02 . 2 . . . . . . . . 5800 1 455 . 1 1 40 40 GLU C C 13 175.86 0.2 . 1 . . . . . . . . 5800 1 456 . 1 1 40 40 GLU CA C 13 56.15 0.2 . 1 . . . . . . . . 5800 1 457 . 1 1 40 40 GLU CB C 13 28.62 0.2 . 1 . . . . . . . . 5800 1 458 . 1 1 40 40 GLU CG C 13 35.66 0.2 . 1 . . . . . . . . 5800 1 459 . 1 1 40 40 GLU N N 15 117.61 0.2 . 1 . . . . . . . . 5800 1 460 . 1 1 41 41 GLY H H 1 7.74 0.02 . 1 . . . . . . . . 5800 1 461 . 1 1 41 41 GLY HA2 H 1 3.53 0.02 . 2 . . . . . . . . 5800 1 462 . 1 1 41 41 GLY HA3 H 1 4.09 0.02 . 2 . . . . . . . . 5800 1 463 . 1 1 41 41 GLY C C 13 174.04 0.2 . 1 . . . . . . . . 5800 1 464 . 1 1 41 41 GLY CA C 13 44.95 0.2 . 1 . . . . . . . . 5800 1 465 . 1 1 41 41 GLY N N 15 105.00 0.2 . 1 . . . . . . . . 5800 1 466 . 1 1 42 42 PHE H H 1 8.15 0.02 . 1 . . . . . . . . 5800 1 467 . 1 1 42 42 PHE HA H 1 4.72 0.02 . 1 . . . . . . . . 5800 1 468 . 1 1 42 42 PHE HB2 H 1 2.79 0.02 . 1 . . . . . . . . 5800 1 469 . 1 1 42 42 PHE HB3 H 1 2.79 0.02 . 1 . . . . . . . . 5800 1 470 . 1 1 42 42 PHE C C 13 174.47 0.2 . 1 . . . . . . . . 5800 1 471 . 1 1 42 42 PHE CA C 13 57.85 0.2 . 1 . . . . . . . . 5800 1 472 . 1 1 42 42 PHE CB C 13 39.22 0.2 . 1 . . . . . . . . 5800 1 473 . 1 1 42 42 PHE N N 15 121.53 0.2 . 1 . . . . . . . . 5800 1 474 . 1 1 43 43 SER H H 1 9.26 0.02 . 1 . . . . . . . . 5800 1 475 . 1 1 43 43 SER HA H 1 4.68 0.02 . 1 . . . . . . . . 5800 1 476 . 1 1 43 43 SER HB2 H 1 3.76 0.02 . 2 . . . . . . . . 5800 1 477 . 1 1 43 43 SER HB3 H 1 3.95 0.02 . 2 . . . . . . . . 5800 1 478 . 1 1 43 43 SER C C 13 173.59 0.2 . 1 . . . . . . . . 5800 1 479 . 1 1 43 43 SER CA C 13 58.73 0.2 . 1 . . . . . . . . 5800 1 480 . 1 1 43 43 SER CB C 13 65.46 0.2 . 1 . . . . . . . . 5800 1 481 . 1 1 43 43 SER N N 15 113.54 0.2 . 1 . . . . . . . . 5800 1 482 . 1 1 44 44 THR H H 1 7.90 0.02 . 1 . . . . . . . . 5800 1 483 . 1 1 44 44 THR HA H 1 4.94 0.02 . 1 . . . . . . . . 5800 1 484 . 1 1 44 44 THR HB H 1 4.79 0.02 . 1 . . . . . . . . 5800 1 485 . 1 1 44 44 THR HG21 H 1 1.20 0.02 . 1 . . . . . . . . 5800 1 486 . 1 1 44 44 THR HG22 H 1 1.20 0.02 . 1 . . . . . . . . 5800 1 487 . 1 1 44 44 THR HG23 H 1 1.20 0.02 . 1 . . . . . . . . 5800 1 488 . 1 1 44 44 THR C C 13 174.74 0.2 . 1 . . . . . . . . 5800 1 489 . 1 1 44 44 THR CA C 13 58.91 0.2 . 1 . . . . . . . . 5800 1 490 . 1 1 44 44 THR CB C 13 72.34 0.2 . 1 . . . . . . . . 5800 1 491 . 1 1 44 44 THR N N 15 110.09 0.2 . 1 . . . . . . . . 5800 1 492 . 1 1 45 45 LEU H H 1 9.20 0.02 . 1 . . . . . . . . 5800 1 493 . 1 1 45 45 LEU HA H 1 3.95 0.02 . 1 . . . . . . . . 5800 1 494 . 1 1 45 45 LEU HB2 H 1 1.20 0.02 . 2 . . . . . . . . 5800 1 495 . 1 1 45 45 LEU HB3 H 1 1.84 0.02 . 2 . . . . . . . . 5800 1 496 . 1 1 45 45 LEU HG H 1 1.83 0.02 . 1 . . . . . . . . 5800 1 497 . 1 1 45 45 LEU HD11 H 1 0.88 0.02 . 2 . . . . . . . . 5800 1 498 . 1 1 45 45 LEU HD12 H 1 0.88 0.02 . 2 . . . . . . . . 5800 1 499 . 1 1 45 45 LEU HD13 H 1 0.88 0.02 . 2 . . . . . . . . 5800 1 500 . 1 1 45 45 LEU HD21 H 1 0.62 0.02 . 2 . . . . . . . . 5800 1 501 . 1 1 45 45 LEU HD22 H 1 0.62 0.02 . 2 . . . . . . . . 5800 1 502 . 1 1 45 45 LEU HD23 H 1 0.62 0.02 . 2 . . . . . . . . 5800 1 503 . 1 1 45 45 LEU C C 13 178.59 0.2 . 1 . . . . . . . . 5800 1 504 . 1 1 45 45 LEU CA C 13 57.89 0.2 . 1 . . . . . . . . 5800 1 505 . 1 1 45 45 LEU CB C 13 42.22 0.2 . 1 . . . . . . . . 5800 1 506 . 1 1 45 45 LEU CG C 13 27.03 0.2 . 1 . . . . . . . . 5800 1 507 . 1 1 45 45 LEU CD1 C 13 23.48 0.2 . 2 . . . . . . . . 5800 1 508 . 1 1 45 45 LEU CD2 C 13 25.93 0.2 . 2 . . . . . . . . 5800 1 509 . 1 1 45 45 LEU N N 15 121.16 0.2 . 1 . . . . . . . . 5800 1 510 . 1 1 46 46 GLU H H 1 9.44 0.02 . 1 . . . . . . . . 5800 1 511 . 1 1 46 46 GLU HA H 1 3.72 0.02 . 1 . . . . . . . . 5800 1 512 . 1 1 46 46 GLU HB2 H 1 2.02 0.02 . 2 . . . . . . . . 5800 1 513 . 1 1 46 46 GLU HB3 H 1 2.15 0.02 . 2 . . . . . . . . 5800 1 514 . 1 1 46 46 GLU HG2 H 1 2.33 0.02 . 2 . . . . . . . . 5800 1 515 . 1 1 46 46 GLU HG3 H 1 2.59 0.02 . 2 . . . . . . . . 5800 1 516 . 1 1 46 46 GLU C C 13 178.64 0.2 . 1 . . . . . . . . 5800 1 517 . 1 1 46 46 GLU CA C 13 60.96 0.2 . 1 . . . . . . . . 5800 1 518 . 1 1 46 46 GLU CB C 13 29.00 0.2 . 1 . . . . . . . . 5800 1 519 . 1 1 46 46 GLU CG C 13 37.57 0.2 . 1 . . . . . . . . 5800 1 520 . 1 1 46 46 GLU N N 15 118.38 0.2 . 1 . . . . . . . . 5800 1 521 . 1 1 47 47 GLU H H 1 7.81 0.02 . 1 . . . . . . . . 5800 1 522 . 1 1 47 47 GLU HA H 1 4.08 0.02 . 1 . . . . . . . . 5800 1 523 . 1 1 47 47 GLU HB2 H 1 2.19 0.02 . 2 . . . . . . . . 5800 1 524 . 1 1 47 47 GLU HB3 H 1 2.57 0.02 . 2 . . . . . . . . 5800 1 525 . 1 1 47 47 GLU HG2 H 1 2.42 0.02 . 1 . . . . . . . . 5800 1 526 . 1 1 47 47 GLU HG3 H 1 2.42 0.02 . 1 . . . . . . . . 5800 1 527 . 1 1 47 47 GLU C C 13 178.41 0.2 . 1 . . . . . . . . 5800 1 528 . 1 1 47 47 GLU CA C 13 58.98 0.2 . 1 . . . . . . . . 5800 1 529 . 1 1 47 47 GLU CB C 13 30.36 0.2 . 1 . . . . . . . . 5800 1 530 . 1 1 47 47 GLU CG C 13 37.31 0.2 . 1 . . . . . . . . 5800 1 531 . 1 1 47 47 GLU N N 15 117.45 0.2 . 1 . . . . . . . . 5800 1 532 . 1 1 48 48 LEU H H 1 7.07 0.02 . 1 . . . . . . . . 5800 1 533 . 1 1 48 48 LEU HA H 1 3.77 0.02 . 1 . . . . . . . . 5800 1 534 . 1 1 48 48 LEU HB2 H 1 1.03 0.02 . 2 . . . . . . . . 5800 1 535 . 1 1 48 48 LEU HB3 H 1 1.54 0.02 . 2 . . . . . . . . 5800 1 536 . 1 1 48 48 LEU HG H 1 1.45 0.02 . 1 . . . . . . . . 5800 1 537 . 1 1 48 48 LEU HD11 H 1 0.08 0.02 . 2 . . . . . . . . 5800 1 538 . 1 1 48 48 LEU HD12 H 1 0.08 0.02 . 2 . . . . . . . . 5800 1 539 . 1 1 48 48 LEU HD13 H 1 0.08 0.02 . 2 . . . . . . . . 5800 1 540 . 1 1 48 48 LEU HD21 H 1 0.20 0.02 . 2 . . . . . . . . 5800 1 541 . 1 1 48 48 LEU HD22 H 1 0.20 0.02 . 2 . . . . . . . . 5800 1 542 . 1 1 48 48 LEU HD23 H 1 0.20 0.02 . 2 . . . . . . . . 5800 1 543 . 1 1 48 48 LEU C C 13 176.96 0.2 . 1 . . . . . . . . 5800 1 544 . 1 1 48 48 LEU CA C 13 56.90 0.2 . 1 . . . . . . . . 5800 1 545 . 1 1 48 48 LEU CB C 13 42.65 0.2 . 1 . . . . . . . . 5800 1 546 . 1 1 48 48 LEU CG C 13 26.63 0.2 . 1 . . . . . . . . 5800 1 547 . 1 1 48 48 LEU CD1 C 13 26.53 0.2 . 2 . . . . . . . . 5800 1 548 . 1 1 48 48 LEU CD2 C 13 24.07 0.2 . 2 . . . . . . . . 5800 1 549 . 1 1 48 48 LEU N N 15 116.02 0.2 . 1 . . . . . . . . 5800 1 550 . 1 1 49 49 ALA H H 1 7.84 0.02 . 1 . . . . . . . . 5800 1 551 . 1 1 49 49 ALA HA H 1 3.82 0.02 . 1 . . . . . . . . 5800 1 552 . 1 1 49 49 ALA HB1 H 1 0.73 0.02 . 1 . . . . . . . . 5800 1 553 . 1 1 49 49 ALA HB2 H 1 0.73 0.02 . 1 . . . . . . . . 5800 1 554 . 1 1 49 49 ALA HB3 H 1 0.73 0.02 . 1 . . . . . . . . 5800 1 555 . 1 1 49 49 ALA C C 13 178.24 0.2 . 1 . . . . . . . . 5800 1 556 . 1 1 49 49 ALA CA C 13 54.34 0.2 . 1 . . . . . . . . 5800 1 557 . 1 1 49 49 ALA CB C 13 19.04 0.2 . 1 . . . . . . . . 5800 1 558 . 1 1 49 49 ALA N N 15 115.92 0.2 . 1 . . . . . . . . 5800 1 559 . 1 1 50 50 TYR H H 1 7.29 0.02 . 1 . . . . . . . . 5800 1 560 . 1 1 50 50 TYR HA H 1 4.77 0.02 . 1 . . . . . . . . 5800 1 561 . 1 1 50 50 TYR HB2 H 1 2.79 0.02 . 2 . . . . . . . . 5800 1 562 . 1 1 50 50 TYR HB3 H 1 3.29 0.02 . 2 . . . . . . . . 5800 1 563 . 1 1 50 50 TYR HD1 H 1 7.20 0.02 . 1 . . . . . . . . 5800 1 564 . 1 1 50 50 TYR HD2 H 1 7.20 0.02 . 1 . . . . . . . . 5800 1 565 . 1 1 50 50 TYR HE1 H 1 6.72 0.02 . 1 . . . . . . . . 5800 1 566 . 1 1 50 50 TYR HE2 H 1 6.72 0.02 . 1 . . . . . . . . 5800 1 567 . 1 1 50 50 TYR C C 13 177.21 0.2 . 1 . . . . . . . . 5800 1 568 . 1 1 50 50 TYR CA C 13 57.11 0.2 . 1 . . . . . . . . 5800 1 569 . 1 1 50 50 TYR CB C 13 39.47 0.2 . 1 . . . . . . . . 5800 1 570 . 1 1 50 50 TYR N N 15 110.41 0.2 . 1 . . . . . . . . 5800 1 571 . 1 1 51 51 VAL H H 1 7.81 0.02 . 1 . . . . . . . . 5800 1 572 . 1 1 51 51 VAL HA H 1 4.49 0.02 . 1 . . . . . . . . 5800 1 573 . 1 1 51 51 VAL HB H 1 2.53 0.02 . 1 . . . . . . . . 5800 1 574 . 1 1 51 51 VAL HG11 H 1 1.16 0.02 . 2 . . . . . . . . 5800 1 575 . 1 1 51 51 VAL HG12 H 1 1.16 0.02 . 2 . . . . . . . . 5800 1 576 . 1 1 51 51 VAL HG13 H 1 1.16 0.02 . 2 . . . . . . . . 5800 1 577 . 1 1 51 51 VAL HG21 H 1 1.00 0.02 . 2 . . . . . . . . 5800 1 578 . 1 1 51 51 VAL HG22 H 1 1.00 0.02 . 2 . . . . . . . . 5800 1 579 . 1 1 51 51 VAL HG23 H 1 1.00 0.02 . 2 . . . . . . . . 5800 1 580 . 1 1 51 51 VAL CA C 13 60.68 0.2 . 1 . . . . . . . . 5800 1 581 . 1 1 51 51 VAL CB C 13 31.73 0.2 . 1 . . . . . . . . 5800 1 582 . 1 1 51 51 VAL CG1 C 13 21.28 0.2 . 2 . . . . . . . . 5800 1 583 . 1 1 51 51 VAL CG2 C 13 20.99 0.2 . 2 . . . . . . . . 5800 1 584 . 1 1 51 51 VAL N N 15 122.63 0.2 . 1 . . . . . . . . 5800 1 585 . 1 1 52 52 PRO HA H 1 4.38 0.02 . 1 . . . . . . . . 5800 1 586 . 1 1 52 52 PRO HB2 H 1 1.89 0.02 . 2 . . . . . . . . 5800 1 587 . 1 1 52 52 PRO HB3 H 1 2.45 0.02 . 2 . . . . . . . . 5800 1 588 . 1 1 52 52 PRO HG2 H 1 2.04 0.02 . 2 . . . . . . . . 5800 1 589 . 1 1 52 52 PRO HG3 H 1 2.22 0.02 . 2 . . . . . . . . 5800 1 590 . 1 1 52 52 PRO HD2 H 1 3.72 0.02 . 2 . . . . . . . . 5800 1 591 . 1 1 52 52 PRO HD3 H 1 3.99 0.02 . 2 . . . . . . . . 5800 1 592 . 1 1 52 52 PRO C C 13 177.84 0.2 . 1 . . . . . . . . 5800 1 593 . 1 1 52 52 PRO CA C 13 63.67 0.2 . 1 . . . . . . . . 5800 1 594 . 1 1 52 52 PRO CB C 13 32.21 0.2 . 1 . . . . . . . . 5800 1 595 . 1 1 52 52 PRO CG C 13 28.37 0.2 . 1 . . . . . . . . 5800 1 596 . 1 1 52 52 PRO CD C 13 51.40 0.2 . 1 . . . . . . . . 5800 1 597 . 1 1 53 53 MET H H 1 8.66 0.02 . 1 . . . . . . . . 5800 1 598 . 1 1 53 53 MET HA H 1 3.86 0.02 . 1 . . . . . . . . 5800 1 599 . 1 1 53 53 MET HB2 H 1 1.93 0.02 . 1 . . . . . . . . 5800 1 600 . 1 1 53 53 MET HB3 H 1 1.93 0.02 . 1 . . . . . . . . 5800 1 601 . 1 1 53 53 MET HG2 H 1 2.52 0.02 . 1 . . . . . . . . 5800 1 602 . 1 1 53 53 MET HG3 H 1 2.52 0.02 . 1 . . . . . . . . 5800 1 603 . 1 1 53 53 MET C C 13 177.59 0.2 . 1 . . . . . . . . 5800 1 604 . 1 1 53 53 MET CA C 13 59.20 0.2 . 1 . . . . . . . . 5800 1 605 . 1 1 53 53 MET CB C 13 32.29 0.2 . 1 . . . . . . . . 5800 1 606 . 1 1 53 53 MET CG C 13 32.30 0.2 . 1 . . . . . . . . 5800 1 607 . 1 1 53 53 MET N N 15 124.39 0.2 . 1 . . . . . . . . 5800 1 608 . 1 1 54 54 LYS H H 1 8.52 0.02 . 1 . . . . . . . . 5800 1 609 . 1 1 54 54 LYS HA H 1 3.95 0.02 . 1 . . . . . . . . 5800 1 610 . 1 1 54 54 LYS HB2 H 1 1.76 0.02 . 2 . . . . . . . . 5800 1 611 . 1 1 54 54 LYS HB3 H 1 1.93 0.02 . 2 . . . . . . . . 5800 1 612 . 1 1 54 54 LYS HG2 H 1 1.44 0.02 . 1 . . . . . . . . 5800 1 613 . 1 1 54 54 LYS HG3 H 1 1.44 0.02 . 1 . . . . . . . . 5800 1 614 . 1 1 54 54 LYS HD2 H 1 1.67 0.02 . 1 . . . . . . . . 5800 1 615 . 1 1 54 54 LYS HD3 H 1 1.67 0.02 . 1 . . . . . . . . 5800 1 616 . 1 1 54 54 LYS HE2 H 1 2.98 0.02 . 1 . . . . . . . . 5800 1 617 . 1 1 54 54 LYS HE3 H 1 2.98 0.02 . 1 . . . . . . . . 5800 1 618 . 1 1 54 54 LYS C C 13 177.84 0.2 . 1 . . . . . . . . 5800 1 619 . 1 1 54 54 LYS CA C 13 59.13 0.2 . 1 . . . . . . . . 5800 1 620 . 1 1 54 54 LYS CB C 13 32.32 0.2 . 1 . . . . . . . . 5800 1 621 . 1 1 54 54 LYS CG C 13 24.59 0.2 . 1 . . . . . . . . 5800 1 622 . 1 1 54 54 LYS CD C 13 29.38 0.2 . 1 . . . . . . . . 5800 1 623 . 1 1 54 54 LYS CE C 13 41.90 0.2 . 1 . . . . . . . . 5800 1 624 . 1 1 54 54 LYS N N 15 115.62 0.2 . 1 . . . . . . . . 5800 1 625 . 1 1 55 55 GLU H H 1 7.64 0.02 . 1 . . . . . . . . 5800 1 626 . 1 1 55 55 GLU HA H 1 4.16 0.02 . 1 . . . . . . . . 5800 1 627 . 1 1 55 55 GLU HB2 H 1 2.10 0.02 . 2 . . . . . . . . 5800 1 628 . 1 1 55 55 GLU HB3 H 1 2.26 0.02 . 2 . . . . . . . . 5800 1 629 . 1 1 55 55 GLU HG2 H 1 2.37 0.02 . 1 . . . . . . . . 5800 1 630 . 1 1 55 55 GLU HG3 H 1 2.37 0.02 . 1 . . . . . . . . 5800 1 631 . 1 1 55 55 GLU C C 13 179.22 0.2 . 1 . . . . . . . . 5800 1 632 . 1 1 55 55 GLU CA C 13 58.84 0.2 . 1 . . . . . . . . 5800 1 633 . 1 1 55 55 GLU CB C 13 29.30 0.2 . 1 . . . . . . . . 5800 1 634 . 1 1 55 55 GLU CG C 13 36.97 0.2 . 1 . . . . . . . . 5800 1 635 . 1 1 55 55 GLU N N 15 116.23 0.2 . 1 . . . . . . . . 5800 1 636 . 1 1 56 56 LEU H H 1 7.17 0.02 . 1 . . . . . . . . 5800 1 637 . 1 1 56 56 LEU HA H 1 4.16 0.02 . 1 . . . . . . . . 5800 1 638 . 1 1 56 56 LEU HB2 H 1 1.33 0.02 . 2 . . . . . . . . 5800 1 639 . 1 1 56 56 LEU HB3 H 1 1.72 0.02 . 2 . . . . . . . . 5800 1 640 . 1 1 56 56 LEU HG H 1 1.37 0.02 . 1 . . . . . . . . 5800 1 641 . 1 1 56 56 LEU HD11 H 1 0.64 0.02 . 2 . . . . . . . . 5800 1 642 . 1 1 56 56 LEU HD12 H 1 0.64 0.02 . 2 . . . . . . . . 5800 1 643 . 1 1 56 56 LEU HD13 H 1 0.64 0.02 . 2 . . . . . . . . 5800 1 644 . 1 1 56 56 LEU HD21 H 1 0.28 0.02 . 2 . . . . . . . . 5800 1 645 . 1 1 56 56 LEU HD22 H 1 0.28 0.02 . 2 . . . . . . . . 5800 1 646 . 1 1 56 56 LEU HD23 H 1 0.28 0.02 . 2 . . . . . . . . 5800 1 647 . 1 1 56 56 LEU C C 13 177.64 0.2 . 1 . . . . . . . . 5800 1 648 . 1 1 56 56 LEU CA C 13 56.85 0.2 . 1 . . . . . . . . 5800 1 649 . 1 1 56 56 LEU CB C 13 42.73 0.2 . 1 . . . . . . . . 5800 1 650 . 1 1 56 56 LEU CG C 13 27.54 0.2 . 1 . . . . . . . . 5800 1 651 . 1 1 56 56 LEU CD1 C 13 26.18 0.2 . 2 . . . . . . . . 5800 1 652 . 1 1 56 56 LEU CD2 C 13 23.68 0.2 . 2 . . . . . . . . 5800 1 653 . 1 1 56 56 LEU N N 15 118.56 0.2 . 1 . . . . . . . . 5800 1 654 . 1 1 57 57 LEU H H 1 7.62 0.02 . 1 . . . . . . . . 5800 1 655 . 1 1 57 57 LEU HA H 1 4.01 0.02 . 1 . . . . . . . . 5800 1 656 . 1 1 57 57 LEU HB2 H 1 1.71 0.02 . 2 . . . . . . . . 5800 1 657 . 1 1 57 57 LEU HB3 H 1 1.63 0.02 . 2 . . . . . . . . 5800 1 658 . 1 1 57 57 LEU HG H 1 1.69 0.02 . 1 . . . . . . . . 5800 1 659 . 1 1 57 57 LEU HD11 H 1 0.87 0.02 . 2 . . . . . . . . 5800 1 660 . 1 1 57 57 LEU HD12 H 1 0.87 0.02 . 2 . . . . . . . . 5800 1 661 . 1 1 57 57 LEU HD13 H 1 0.87 0.02 . 2 . . . . . . . . 5800 1 662 . 1 1 57 57 LEU HD21 H 1 0.73 0.02 . 2 . . . . . . . . 5800 1 663 . 1 1 57 57 LEU HD22 H 1 0.73 0.02 . 2 . . . . . . . . 5800 1 664 . 1 1 57 57 LEU HD23 H 1 0.73 0.02 . 2 . . . . . . . . 5800 1 665 . 1 1 57 57 LEU C C 13 177.34 0.2 . 1 . . . . . . . . 5800 1 666 . 1 1 57 57 LEU CA C 13 56.06 0.2 . 1 . . . . . . . . 5800 1 667 . 1 1 57 57 LEU CB C 13 41.47 0.2 . 1 . . . . . . . . 5800 1 668 . 1 1 57 57 LEU CG C 13 27.00 0.2 . 1 . . . . . . . . 5800 1 669 . 1 1 57 57 LEU CD1 C 13 22.61 0.2 . 2 . . . . . . . . 5800 1 670 . 1 1 57 57 LEU CD2 C 13 25.30 0.2 . 2 . . . . . . . . 5800 1 671 . 1 1 57 57 LEU N N 15 115.31 0.2 . 1 . . . . . . . . 5800 1 672 . 1 1 58 58 GLU H H 1 7.10 0.02 . 1 . . . . . . . . 5800 1 673 . 1 1 58 58 GLU HA H 1 4.16 0.02 . 1 . . . . . . . . 5800 1 674 . 1 1 58 58 GLU HB2 H 1 2.00 0.02 . 2 . . . . . . . . 5800 1 675 . 1 1 58 58 GLU HB3 H 1 2.23 0.02 . 2 . . . . . . . . 5800 1 676 . 1 1 58 58 GLU HG2 H 1 2.56 0.02 . 2 . . . . . . . . 5800 1 677 . 1 1 58 58 GLU HG3 H 1 2.33 0.02 . 2 . . . . . . . . 5800 1 678 . 1 1 58 58 GLU C C 13 176.95 0.2 . 1 . . . . . . . . 5800 1 679 . 1 1 58 58 GLU CA C 13 56.93 0.2 . 1 . . . . . . . . 5800 1 680 . 1 1 58 58 GLU CB C 13 29.65 0.2 . 1 . . . . . . . . 5800 1 681 . 1 1 58 58 GLU CG C 13 36.44 0.2 . 1 . . . . . . . . 5800 1 682 . 1 1 58 58 GLU N N 15 115.72 0.2 . 1 . . . . . . . . 5800 1 683 . 1 1 59 59 ILE H H 1 7.52 0.02 . 1 . . . . . . . . 5800 1 684 . 1 1 59 59 ILE HA H 1 3.86 0.02 . 1 . . . . . . . . 5800 1 685 . 1 1 59 59 ILE HB H 1 2.03 0.02 . 1 . . . . . . . . 5800 1 686 . 1 1 59 59 ILE HG12 H 1 1.05 0.02 . 2 . . . . . . . . 5800 1 687 . 1 1 59 59 ILE HG13 H 1 1.81 0.02 . 2 . . . . . . . . 5800 1 688 . 1 1 59 59 ILE HG21 H 1 0.87 0.02 . 1 . . . . . . . . 5800 1 689 . 1 1 59 59 ILE HG22 H 1 0.87 0.02 . 1 . . . . . . . . 5800 1 690 . 1 1 59 59 ILE HG23 H 1 0.87 0.02 . 1 . . . . . . . . 5800 1 691 . 1 1 59 59 ILE HD11 H 1 0.93 0.02 . 1 . . . . . . . . 5800 1 692 . 1 1 59 59 ILE HD12 H 1 0.93 0.02 . 1 . . . . . . . . 5800 1 693 . 1 1 59 59 ILE HD13 H 1 0.93 0.02 . 1 . . . . . . . . 5800 1 694 . 1 1 59 59 ILE C C 13 175.84 0.2 . 1 . . . . . . . . 5800 1 695 . 1 1 59 59 ILE CA C 13 62.18 0.2 . 1 . . . . . . . . 5800 1 696 . 1 1 59 59 ILE CB C 13 36.93 0.2 . 1 . . . . . . . . 5800 1 697 . 1 1 59 59 ILE CG1 C 13 27.97 0.2 . 1 . . . . . . . . 5800 1 698 . 1 1 59 59 ILE CG2 C 13 16.84 0.2 . 1 . . . . . . . . 5800 1 699 . 1 1 59 59 ILE CD1 C 13 13.86 0.2 . 1 . . . . . . . . 5800 1 700 . 1 1 59 59 ILE N N 15 122.23 0.2 . 1 . . . . . . . . 5800 1 701 . 1 1 60 60 GLU H H 1 8.50 0.02 . 1 . . . . . . . . 5800 1 702 . 1 1 60 60 GLU HA H 1 3.99 0.02 . 1 . . . . . . . . 5800 1 703 . 1 1 60 60 GLU HB2 H 1 2.01 0.02 . 1 . . . . . . . . 5800 1 704 . 1 1 60 60 GLU HB3 H 1 2.01 0.02 . 1 . . . . . . . . 5800 1 705 . 1 1 60 60 GLU HG2 H 1 2.37 0.02 . 2 . . . . . . . . 5800 1 706 . 1 1 60 60 GLU HG3 H 1 2.28 0.02 . 2 . . . . . . . . 5800 1 707 . 1 1 60 60 GLU C C 13 177.09 0.2 . 1 . . . . . . . . 5800 1 708 . 1 1 60 60 GLU CA C 13 58.21 0.2 . 1 . . . . . . . . 5800 1 709 . 1 1 60 60 GLU CB C 13 29.39 0.2 . 1 . . . . . . . . 5800 1 710 . 1 1 60 60 GLU CG C 13 35.59 0.2 . 1 . . . . . . . . 5800 1 711 . 1 1 60 60 GLU N N 15 104.83 0.2 . 1 . . . . . . . . 5800 1 712 . 1 1 61 61 GLY H H 1 8.67 0.02 . 1 . . . . . . . . 5800 1 713 . 1 1 61 61 GLY HA2 H 1 3.65 0.02 . 2 . . . . . . . . 5800 1 714 . 1 1 61 61 GLY HA3 H 1 4.21 0.02 . 2 . . . . . . . . 5800 1 715 . 1 1 61 61 GLY C C 13 174.53 0.2 . 1 . . . . . . . . 5800 1 716 . 1 1 61 61 GLY CA C 13 45.04 0.2 . 1 . . . . . . . . 5800 1 717 . 1 1 61 61 GLY N N 15 111.93 0.2 . 1 . . . . . . . . 5800 1 718 . 1 1 62 62 LEU H H 1 7.56 0.02 . 1 . . . . . . . . 5800 1 719 . 1 1 62 62 LEU HA H 1 4.51 0.02 . 1 . . . . . . . . 5800 1 720 . 1 1 62 62 LEU HB2 H 1 1.28 0.02 . 2 . . . . . . . . 5800 1 721 . 1 1 62 62 LEU HB3 H 1 1.84 0.02 . 2 . . . . . . . . 5800 1 722 . 1 1 62 62 LEU HG H 1 1.53 0.02 . 1 . . . . . . . . 5800 1 723 . 1 1 62 62 LEU HD11 H 1 0.87 0.02 . 2 . . . . . . . . 5800 1 724 . 1 1 62 62 LEU HD12 H 1 0.87 0.02 . 2 . . . . . . . . 5800 1 725 . 1 1 62 62 LEU HD13 H 1 0.87 0.02 . 2 . . . . . . . . 5800 1 726 . 1 1 62 62 LEU HD21 H 1 0.69 0.02 . 2 . . . . . . . . 5800 1 727 . 1 1 62 62 LEU HD22 H 1 0.69 0.02 . 2 . . . . . . . . 5800 1 728 . 1 1 62 62 LEU HD23 H 1 0.69 0.02 . 2 . . . . . . . . 5800 1 729 . 1 1 62 62 LEU C C 13 175.22 0.2 . 1 . . . . . . . . 5800 1 730 . 1 1 62 62 LEU CA C 13 54.27 0.2 . 1 . . . . . . . . 5800 1 731 . 1 1 62 62 LEU CB C 13 42.09 0.2 . 1 . . . . . . . . 5800 1 732 . 1 1 62 62 LEU CG C 13 27.17 0.2 . 1 . . . . . . . . 5800 1 733 . 1 1 62 62 LEU CD1 C 13 25.14 0.2 . 2 . . . . . . . . 5800 1 734 . 1 1 62 62 LEU CD2 C 13 23.83 0.2 . 2 . . . . . . . . 5800 1 735 . 1 1 62 62 LEU N N 15 120.59 0.2 . 1 . . . . . . . . 5800 1 736 . 1 1 63 63 ASP H H 1 7.44 0.02 . 1 . . . . . . . . 5800 1 737 . 1 1 63 63 ASP HA H 1 4.73 0.02 . 1 . . . . . . . . 5800 1 738 . 1 1 63 63 ASP HB2 H 1 2.77 0.02 . 2 . . . . . . . . 5800 1 739 . 1 1 63 63 ASP HB3 H 1 3.01 0.02 . 2 . . . . . . . . 5800 1 740 . 1 1 63 63 ASP C C 13 175.34 0.2 . 1 . . . . . . . . 5800 1 741 . 1 1 63 63 ASP CA C 13 51.66 0.2 . 1 . . . . . . . . 5800 1 742 . 1 1 63 63 ASP CB C 13 42.77 0.2 . 1 . . . . . . . . 5800 1 743 . 1 1 63 63 ASP N N 15 118.81 0.2 . 1 . . . . . . . . 5800 1 744 . 1 1 64 64 GLU H H 1 9.00 0.02 . 1 . . . . . . . . 5800 1 745 . 1 1 64 64 GLU HA H 1 4.06 0.02 . 1 . . . . . . . . 5800 1 746 . 1 1 64 64 GLU HB2 H 1 2.13 0.02 . 1 . . . . . . . . 5800 1 747 . 1 1 64 64 GLU HB3 H 1 2.13 0.02 . 1 . . . . . . . . 5800 1 748 . 1 1 64 64 GLU HG2 H 1 2.36 0.02 . 2 . . . . . . . . 5800 1 749 . 1 1 64 64 GLU HG3 H 1 2.33 0.02 . 2 . . . . . . . . 5800 1 750 . 1 1 64 64 GLU CA C 13 62.07 0.2 . 1 . . . . . . . . 5800 1 751 . 1 1 64 64 GLU CB C 13 27.12 0.2 . 1 . . . . . . . . 5800 1 752 . 1 1 64 64 GLU N N 15 119.33 0.2 . 1 . . . . . . . . 5800 1 753 . 1 1 65 65 PRO HA H 1 4.36 0.02 . 1 . . . . . . . . 5800 1 754 . 1 1 65 65 PRO HB2 H 1 1.84 0.02 . 2 . . . . . . . . 5800 1 755 . 1 1 65 65 PRO HB3 H 1 2.30 0.02 . 2 . . . . . . . . 5800 1 756 . 1 1 65 65 PRO HG2 H 1 2.13 0.02 . 2 . . . . . . . . 5800 1 757 . 1 1 65 65 PRO HG3 H 1 1.98 0.02 . 2 . . . . . . . . 5800 1 758 . 1 1 65 65 PRO HD2 H 1 3.73 0.02 . 2 . . . . . . . . 5800 1 759 . 1 1 65 65 PRO HD3 H 1 3.83 0.02 . 2 . . . . . . . . 5800 1 760 . 1 1 65 65 PRO C C 13 180.37 0.2 . 1 . . . . . . . . 5800 1 761 . 1 1 65 65 PRO CA C 13 66.00 0.2 . 1 . . . . . . . . 5800 1 762 . 1 1 65 65 PRO CB C 13 30.64 0.2 . 1 . . . . . . . . 5800 1 763 . 1 1 65 65 PRO CG C 13 28.19 0.2 . 1 . . . . . . . . 5800 1 764 . 1 1 65 65 PRO CD C 13 49.65 0.2 . 1 . . . . . . . . 5800 1 765 . 1 1 66 66 THR H H 1 7.83 0.02 . 1 . . . . . . . . 5800 1 766 . 1 1 66 66 THR HA H 1 3.97 0.02 . 1 . . . . . . . . 5800 1 767 . 1 1 66 66 THR HB H 1 4.25 0.02 . 1 . . . . . . . . 5800 1 768 . 1 1 66 66 THR HG21 H 1 1.25 0.02 . 1 . . . . . . . . 5800 1 769 . 1 1 66 66 THR HG22 H 1 1.25 0.02 . 1 . . . . . . . . 5800 1 770 . 1 1 66 66 THR HG23 H 1 1.25 0.02 . 1 . . . . . . . . 5800 1 771 . 1 1 66 66 THR C C 13 177.20 0.2 . 1 . . . . . . . . 5800 1 772 . 1 1 66 66 THR CA C 13 67.18 0.2 . 1 . . . . . . . . 5800 1 773 . 1 1 66 66 THR CB C 13 67.93 0.2 . 1 . . . . . . . . 5800 1 774 . 1 1 66 66 THR N N 15 115.65 0.2 . 1 . . . . . . . . 5800 1 775 . 1 1 67 67 VAL H H 1 8.30 0.02 . 1 . . . . . . . . 5800 1 776 . 1 1 67 67 VAL HA H 1 3.52 0.02 . 1 . . . . . . . . 5800 1 777 . 1 1 67 67 VAL HB H 1 2.21 0.02 . 1 . . . . . . . . 5800 1 778 . 1 1 67 67 VAL HG11 H 1 0.97 0.02 . 2 . . . . . . . . 5800 1 779 . 1 1 67 67 VAL HG12 H 1 0.97 0.02 . 2 . . . . . . . . 5800 1 780 . 1 1 67 67 VAL HG13 H 1 0.97 0.02 . 2 . . . . . . . . 5800 1 781 . 1 1 67 67 VAL HG21 H 1 0.93 0.02 . 2 . . . . . . . . 5800 1 782 . 1 1 67 67 VAL HG22 H 1 0.93 0.02 . 2 . . . . . . . . 5800 1 783 . 1 1 67 67 VAL HG23 H 1 0.93 0.02 . 2 . . . . . . . . 5800 1 784 . 1 1 67 67 VAL C C 13 177.47 0.2 . 1 . . . . . . . . 5800 1 785 . 1 1 67 67 VAL CA C 13 67.43 0.2 . 1 . . . . . . . . 5800 1 786 . 1 1 67 67 VAL CB C 13 31.44 0.2 . 1 . . . . . . . . 5800 1 787 . 1 1 67 67 VAL CG1 C 13 24.60 0.2 . 2 . . . . . . . . 5800 1 788 . 1 1 67 67 VAL CG2 C 13 23.06 0.2 . 2 . . . . . . . . 5800 1 789 . 1 1 67 67 VAL N N 15 122.19 0.2 . 1 . . . . . . . . 5800 1 790 . 1 1 68 68 GLU H H 1 8.66 0.02 . 1 . . . . . . . . 5800 1 791 . 1 1 68 68 GLU HA H 1 4.03 0.02 . 1 . . . . . . . . 5800 1 792 . 1 1 68 68 GLU HB2 H 1 2.06 0.02 . 1 . . . . . . . . 5800 1 793 . 1 1 68 68 GLU HB3 H 1 2.06 0.02 . 1 . . . . . . . . 5800 1 794 . 1 1 68 68 GLU HG2 H 1 2.25 0.02 . 2 . . . . . . . . 5800 1 795 . 1 1 68 68 GLU HG3 H 1 2.42 0.02 . 2 . . . . . . . . 5800 1 796 . 1 1 68 68 GLU C C 13 177.59 0.2 . 1 . . . . . . . . 5800 1 797 . 1 1 68 68 GLU CA C 13 59.70 0.2 . 1 . . . . . . . . 5800 1 798 . 1 1 68 68 GLU CB C 13 29.09 0.2 . 1 . . . . . . . . 5800 1 799 . 1 1 68 68 GLU CG C 13 36.42 0.2 . 1 . . . . . . . . 5800 1 800 . 1 1 68 68 GLU N N 15 119.36 0.2 . 1 . . . . . . . . 5800 1 801 . 1 1 69 69 ALA H H 1 7.71 0.02 . 1 . . . . . . . . 5800 1 802 . 1 1 69 69 ALA HA H 1 4.21 0.02 . 1 . . . . . . . . 5800 1 803 . 1 1 69 69 ALA HB1 H 1 1.54 0.02 . 1 . . . . . . . . 5800 1 804 . 1 1 69 69 ALA HB2 H 1 1.54 0.02 . 1 . . . . . . . . 5800 1 805 . 1 1 69 69 ALA HB3 H 1 1.54 0.02 . 1 . . . . . . . . 5800 1 806 . 1 1 69 69 ALA C C 13 180.23 0.2 . 1 . . . . . . . . 5800 1 807 . 1 1 69 69 ALA CA C 13 54.97 0.2 . 1 . . . . . . . . 5800 1 808 . 1 1 69 69 ALA CB C 13 18.04 0.2 . 1 . . . . . . . . 5800 1 809 . 1 1 69 69 ALA N N 15 121.04 0.2 . 1 . . . . . . . . 5800 1 810 . 1 1 70 70 LEU H H 1 8.14 0.02 . 1 . . . . . . . . 5800 1 811 . 1 1 70 70 LEU HA H 1 3.91 0.02 . 1 . . . . . . . . 5800 1 812 . 1 1 70 70 LEU HB2 H 1 1.54 0.02 . 2 . . . . . . . . 5800 1 813 . 1 1 70 70 LEU HB3 H 1 1.84 0.02 . 2 . . . . . . . . 5800 1 814 . 1 1 70 70 LEU HG H 1 1.71 0.02 . 1 . . . . . . . . 5800 1 815 . 1 1 70 70 LEU HD11 H 1 0.86 0.02 . 2 . . . . . . . . 5800 1 816 . 1 1 70 70 LEU HD12 H 1 0.86 0.02 . 2 . . . . . . . . 5800 1 817 . 1 1 70 70 LEU HD13 H 1 0.86 0.02 . 2 . . . . . . . . 5800 1 818 . 1 1 70 70 LEU HD21 H 1 0.72 0.02 . 2 . . . . . . . . 5800 1 819 . 1 1 70 70 LEU HD22 H 1 0.72 0.02 . 2 . . . . . . . . 5800 1 820 . 1 1 70 70 LEU HD23 H 1 0.72 0.02 . 2 . . . . . . . . 5800 1 821 . 1 1 70 70 LEU C C 13 178.41 0.2 . 1 . . . . . . . . 5800 1 822 . 1 1 70 70 LEU CA C 13 58.11 0.2 . 1 . . . . . . . . 5800 1 823 . 1 1 70 70 LEU CB C 13 42.52 0.2 . 1 . . . . . . . . 5800 1 824 . 1 1 70 70 LEU CG C 13 26.52 0.2 . 1 . . . . . . . . 5800 1 825 . 1 1 70 70 LEU CD1 C 13 25.07 0.2 . 2 . . . . . . . . 5800 1 826 . 1 1 70 70 LEU CD2 C 13 26.64 0.2 . 2 . . . . . . . . 5800 1 827 . 1 1 70 70 LEU N N 15 120.08 0.2 . 1 . . . . . . . . 5800 1 828 . 1 1 71 71 ARG H H 1 8.26 0.02 . 1 . . . . . . . . 5800 1 829 . 1 1 71 71 ARG HA H 1 3.68 0.02 . 1 . . . . . . . . 5800 1 830 . 1 1 71 71 ARG HB2 H 1 1.86 0.02 . 1 . . . . . . . . 5800 1 831 . 1 1 71 71 ARG HB3 H 1 1.86 0.02 . 1 . . . . . . . . 5800 1 832 . 1 1 71 71 ARG HG2 H 1 1.76 0.02 . 1 . . . . . . . . 5800 1 833 . 1 1 71 71 ARG HG3 H 1 1.76 0.02 . 1 . . . . . . . . 5800 1 834 . 1 1 71 71 ARG HD2 H 1 3.12 0.02 . 1 . . . . . . . . 5800 1 835 . 1 1 71 71 ARG HD3 H 1 3.12 0.02 . 1 . . . . . . . . 5800 1 836 . 1 1 71 71 ARG C C 13 178.67 0.2 . 1 . . . . . . . . 5800 1 837 . 1 1 71 71 ARG CA C 13 59.98 0.2 . 1 . . . . . . . . 5800 1 838 . 1 1 71 71 ARG CB C 13 30.55 0.2 . 1 . . . . . . . . 5800 1 839 . 1 1 71 71 ARG CG C 13 27.17 0.2 . 1 . . . . . . . . 5800 1 840 . 1 1 71 71 ARG CD C 13 45.40 0.2 . 1 . . . . . . . . 5800 1 841 . 1 1 71 71 ARG N N 15 117.97 0.2 . 1 . . . . . . . . 5800 1 842 . 1 1 72 72 GLU H H 1 7.80 0.02 . 1 . . . . . . . . 5800 1 843 . 1 1 72 72 GLU HA H 1 4.29 0.02 . 1 . . . . . . . . 5800 1 844 . 1 1 72 72 GLU HB2 H 1 2.14 0.02 . 1 . . . . . . . . 5800 1 845 . 1 1 72 72 GLU HB3 H 1 2.14 0.02 . 1 . . . . . . . . 5800 1 846 . 1 1 72 72 GLU HG2 H 1 2.36 0.02 . 1 . . . . . . . . 5800 1 847 . 1 1 72 72 GLU HG3 H 1 2.36 0.02 . 1 . . . . . . . . 5800 1 848 . 1 1 72 72 GLU C C 13 179.16 0.2 . 1 . . . . . . . . 5800 1 849 . 1 1 72 72 GLU CA C 13 59.18 0.2 . 1 . . . . . . . . 5800 1 850 . 1 1 72 72 GLU CB C 13 29.28 0.2 . 1 . . . . . . . . 5800 1 851 . 1 1 72 72 GLU CG C 13 35.92 0.2 . 1 . . . . . . . . 5800 1 852 . 1 1 72 72 GLU N N 15 118.67 0.2 . 1 . . . . . . . . 5800 1 853 . 1 1 73 73 ARG H H 1 8.26 0.02 . 1 . . . . . . . . 5800 1 854 . 1 1 73 73 ARG HA H 1 4.12 0.02 . 1 . . . . . . . . 5800 1 855 . 1 1 73 73 ARG HB2 H 1 1.97 0.02 . 1 . . . . . . . . 5800 1 856 . 1 1 73 73 ARG HB3 H 1 1.97 0.02 . 1 . . . . . . . . 5800 1 857 . 1 1 73 73 ARG HG2 H 1 1.76 0.02 . 2 . . . . . . . . 5800 1 858 . 1 1 73 73 ARG HG3 H 1 2.05 0.02 . 2 . . . . . . . . 5800 1 859 . 1 1 73 73 ARG HD2 H 1 3.08 0.02 . 2 . . . . . . . . 5800 1 860 . 1 1 73 73 ARG HD3 H 1 3.33 0.02 . 2 . . . . . . . . 5800 1 861 . 1 1 73 73 ARG C C 13 179.72 0.2 . 1 . . . . . . . . 5800 1 862 . 1 1 73 73 ARG CA C 13 59.44 0.2 . 1 . . . . . . . . 5800 1 863 . 1 1 73 73 ARG CB C 13 30.18 0.2 . 1 . . . . . . . . 5800 1 864 . 1 1 73 73 ARG CG C 13 27.88 0.2 . 1 . . . . . . . . 5800 1 865 . 1 1 73 73 ARG CD C 13 43.97 0.2 . 1 . . . . . . . . 5800 1 866 . 1 1 73 73 ARG N N 15 119.07 0.2 . 1 . . . . . . . . 5800 1 867 . 1 1 74 74 ALA H H 1 8.51 0.02 . 1 . . . . . . . . 5800 1 868 . 1 1 74 74 ALA HA H 1 3.86 0.02 . 1 . . . . . . . . 5800 1 869 . 1 1 74 74 ALA HB1 H 1 1.33 0.02 . 1 . . . . . . . . 5800 1 870 . 1 1 74 74 ALA HB2 H 1 1.33 0.02 . 1 . . . . . . . . 5800 1 871 . 1 1 74 74 ALA HB3 H 1 1.33 0.02 . 1 . . . . . . . . 5800 1 872 . 1 1 74 74 ALA C C 13 178.47 0.2 . 1 . . . . . . . . 5800 1 873 . 1 1 74 74 ALA CA C 13 55.65 0.2 . 1 . . . . . . . . 5800 1 874 . 1 1 74 74 ALA CB C 13 17.57 0.2 . 1 . . . . . . . . 5800 1 875 . 1 1 74 74 ALA N N 15 123.51 0.2 . 1 . . . . . . . . 5800 1 876 . 1 1 75 75 LYS H H 1 8.19 0.02 . 1 . . . . . . . . 5800 1 877 . 1 1 75 75 LYS HA H 1 3.73 0.02 . 1 . . . . . . . . 5800 1 878 . 1 1 75 75 LYS HB2 H 1 1.88 0.02 . 1 . . . . . . . . 5800 1 879 . 1 1 75 75 LYS HB3 H 1 1.88 0.02 . 1 . . . . . . . . 5800 1 880 . 1 1 75 75 LYS HG2 H 1 1.27 0.02 . 2 . . . . . . . . 5800 1 881 . 1 1 75 75 LYS HG3 H 1 1.59 0.02 . 2 . . . . . . . . 5800 1 882 . 1 1 75 75 LYS HD2 H 1 1.67 0.02 . 1 . . . . . . . . 5800 1 883 . 1 1 75 75 LYS HD3 H 1 1.67 0.02 . 1 . . . . . . . . 5800 1 884 . 1 1 75 75 LYS HE2 H 1 2.88 0.02 . 1 . . . . . . . . 5800 1 885 . 1 1 75 75 LYS HE3 H 1 2.88 0.02 . 1 . . . . . . . . 5800 1 886 . 1 1 75 75 LYS C C 13 179.96 0.2 . 1 . . . . . . . . 5800 1 887 . 1 1 75 75 LYS CA C 13 60.43 0.2 . 1 . . . . . . . . 5800 1 888 . 1 1 75 75 LYS CB C 13 32.28 0.2 . 1 . . . . . . . . 5800 1 889 . 1 1 75 75 LYS CG C 13 26.19 0.2 . 1 . . . . . . . . 5800 1 890 . 1 1 75 75 LYS CD C 13 29.30 0.2 . 1 . . . . . . . . 5800 1 891 . 1 1 75 75 LYS CE C 13 42.07 0.2 . 1 . . . . . . . . 5800 1 892 . 1 1 75 75 LYS N N 15 117.79 0.2 . 1 . . . . . . . . 5800 1 893 . 1 1 76 76 ASN H H 1 8.35 0.02 . 1 . . . . . . . . 5800 1 894 . 1 1 76 76 ASN HA H 1 4.50 0.02 . 1 . . . . . . . . 5800 1 895 . 1 1 76 76 ASN HB2 H 1 2.87 0.02 . 1 . . . . . . . . 5800 1 896 . 1 1 76 76 ASN HB3 H 1 2.87 0.02 . 1 . . . . . . . . 5800 1 897 . 1 1 76 76 ASN C C 13 177.90 0.2 . 1 . . . . . . . . 5800 1 898 . 1 1 76 76 ASN CA C 13 56.03 0.2 . 1 . . . . . . . . 5800 1 899 . 1 1 76 76 ASN CB C 13 38.21 0.2 . 1 . . . . . . . . 5800 1 900 . 1 1 76 76 ASN N N 15 118.87 0.2 . 1 . . . . . . . . 5800 1 901 . 1 1 77 77 ALA H H 1 8.40 0.02 . 1 . . . . . . . . 5800 1 902 . 1 1 77 77 ALA HA H 1 4.21 0.02 . 1 . . . . . . . . 5800 1 903 . 1 1 77 77 ALA HB1 H 1 1.43 0.02 . 1 . . . . . . . . 5800 1 904 . 1 1 77 77 ALA HB2 H 1 1.43 0.02 . 1 . . . . . . . . 5800 1 905 . 1 1 77 77 ALA HB3 H 1 1.43 0.02 . 1 . . . . . . . . 5800 1 906 . 1 1 77 77 ALA C C 13 179.47 0.2 . 1 . . . . . . . . 5800 1 907 . 1 1 77 77 ALA CA C 13 55.08 0.2 . 1 . . . . . . . . 5800 1 908 . 1 1 77 77 ALA CB C 13 18.88 0.2 . 1 . . . . . . . . 5800 1 909 . 1 1 77 77 ALA N N 15 124.34 0.2 . 1 . . . . . . . . 5800 1 910 . 1 1 78 78 LEU H H 1 8.06 0.02 . 1 . . . . . . . . 5800 1 911 . 1 1 78 78 LEU HA H 1 3.86 0.02 . 1 . . . . . . . . 5800 1 912 . 1 1 78 78 LEU HB2 H 1 1.46 0.02 . 2 . . . . . . . . 5800 1 913 . 1 1 78 78 LEU HB3 H 1 1.93 0.02 . 2 . . . . . . . . 5800 1 914 . 1 1 78 78 LEU HD11 H 1 0.73 0.02 . 2 . . . . . . . . 5800 1 915 . 1 1 78 78 LEU HD12 H 1 0.73 0.02 . 2 . . . . . . . . 5800 1 916 . 1 1 78 78 LEU HD13 H 1 0.73 0.02 . 2 . . . . . . . . 5800 1 917 . 1 1 78 78 LEU C C 13 179.73 0.2 . 1 . . . . . . . . 5800 1 918 . 1 1 78 78 LEU CA C 13 57.91 0.2 . 1 . . . . . . . . 5800 1 919 . 1 1 78 78 LEU CB C 13 41.64 0.2 . 1 . . . . . . . . 5800 1 920 . 1 1 78 78 LEU CG C 13 29.21 0.2 . 1 . . . . . . . . 5800 1 921 . 1 1 78 78 LEU CD1 C 13 26.11 0.2 . 2 . . . . . . . . 5800 1 922 . 1 1 78 78 LEU CD2 C 13 23.58 0.2 . 2 . . . . . . . . 5800 1 923 . 1 1 78 78 LEU N N 15 117.46 0.2 . 1 . . . . . . . . 5800 1 924 . 1 1 79 79 ALA H H 1 7.59 0.02 . 1 . . . . . . . . 5800 1 925 . 1 1 79 79 ALA HA H 1 4.25 0.02 . 1 . . . . . . . . 5800 1 926 . 1 1 79 79 ALA HB1 H 1 1.54 0.02 . 1 . . . . . . . . 5800 1 927 . 1 1 79 79 ALA HB2 H 1 1.54 0.02 . 1 . . . . . . . . 5800 1 928 . 1 1 79 79 ALA HB3 H 1 1.54 0.02 . 1 . . . . . . . . 5800 1 929 . 1 1 79 79 ALA C C 13 180.04 0.2 . 1 . . . . . . . . 5800 1 930 . 1 1 79 79 ALA CA C 13 54.89 0.2 . 1 . . . . . . . . 5800 1 931 . 1 1 79 79 ALA CB C 13 18.02 0.2 . 1 . . . . . . . . 5800 1 932 . 1 1 79 79 ALA N N 15 121.53 0.2 . 1 . . . . . . . . 5800 1 933 . 1 1 80 80 THR H H 1 8.08 0.02 . 1 . . . . . . . . 5800 1 934 . 1 1 80 80 THR HA H 1 4.05 0.02 . 1 . . . . . . . . 5800 1 935 . 1 1 80 80 THR HB H 1 4.43 0.02 . 1 . . . . . . . . 5800 1 936 . 1 1 80 80 THR HG21 H 1 1.35 0.02 . 1 . . . . . . . . 5800 1 937 . 1 1 80 80 THR HG22 H 1 1.35 0.02 . 1 . . . . . . . . 5800 1 938 . 1 1 80 80 THR HG23 H 1 1.35 0.02 . 1 . . . . . . . . 5800 1 939 . 1 1 80 80 THR C C 13 176.97 0.2 . 1 . . . . . . . . 5800 1 940 . 1 1 80 80 THR CA C 13 66.03 0.2 . 1 . . . . . . . . 5800 1 941 . 1 1 80 80 THR CB C 13 69.06 0.2 . 1 . . . . . . . . 5800 1 942 . 1 1 80 80 THR N N 15 116.30 0.2 . 1 . . . . . . . . 5800 1 943 . 1 1 81 81 ILE H H 1 8.32 0.02 . 1 . . . . . . . . 5800 1 944 . 1 1 81 81 ILE HA H 1 3.75 0.02 . 1 . . . . . . . . 5800 1 945 . 1 1 81 81 ILE HB H 1 1.67 0.02 . 1 . . . . . . . . 5800 1 946 . 1 1 81 81 ILE HG12 H 1 1.50 0.02 . 2 . . . . . . . . 5800 1 947 . 1 1 81 81 ILE HG13 H 1 0.89 0.02 . 2 . . . . . . . . 5800 1 948 . 1 1 81 81 ILE HG21 H 1 0.84 0.02 . 1 . . . . . . . . 5800 1 949 . 1 1 81 81 ILE HG22 H 1 0.84 0.02 . 1 . . . . . . . . 5800 1 950 . 1 1 81 81 ILE HG23 H 1 0.84 0.02 . 1 . . . . . . . . 5800 1 951 . 1 1 81 81 ILE HD11 H 1 0.31 0.02 . 1 . . . . . . . . 5800 1 952 . 1 1 81 81 ILE HD12 H 1 0.31 0.02 . 1 . . . . . . . . 5800 1 953 . 1 1 81 81 ILE HD13 H 1 0.31 0.02 . 1 . . . . . . . . 5800 1 954 . 1 1 81 81 ILE C C 13 178.09 0.2 . 1 . . . . . . . . 5800 1 955 . 1 1 81 81 ILE CA C 13 64.83 0.2 . 1 . . . . . . . . 5800 1 956 . 1 1 81 81 ILE CB C 13 38.92 0.2 . 1 . . . . . . . . 5800 1 957 . 1 1 81 81 ILE CG1 C 13 29.46 0.2 . 1 . . . . . . . . 5800 1 958 . 1 1 81 81 ILE CG2 C 13 16.91 0.2 . 1 . . . . . . . . 5800 1 959 . 1 1 81 81 ILE CD1 C 13 13.43 0.2 . 1 . . . . . . . . 5800 1 960 . 1 1 81 81 ILE N N 15 123.88 0.2 . 1 . . . . . . . . 5800 1 961 . 1 1 82 82 ALA H H 1 7.87 0.02 . 1 . . . . . . . . 5800 1 962 . 1 1 82 82 ALA HA H 1 4.21 0.02 . 1 . . . . . . . . 5800 1 963 . 1 1 82 82 ALA HB1 H 1 1.50 0.02 . 1 . . . . . . . . 5800 1 964 . 1 1 82 82 ALA HB2 H 1 1.50 0.02 . 1 . . . . . . . . 5800 1 965 . 1 1 82 82 ALA HB3 H 1 1.50 0.02 . 1 . . . . . . . . 5800 1 966 . 1 1 82 82 ALA C C 13 179.73 0.2 . 1 . . . . . . . . 5800 1 967 . 1 1 82 82 ALA CA C 13 54.38 0.2 . 1 . . . . . . . . 5800 1 968 . 1 1 82 82 ALA CB C 13 18.28 0.2 . 1 . . . . . . . . 5800 1 969 . 1 1 82 82 ALA N N 15 122.30 0.2 . 1 . . . . . . . . 5800 1 970 . 1 1 83 83 GLN H H 1 7.91 0.02 . 1 . . . . . . . . 5800 1 971 . 1 1 83 83 GLN HA H 1 4.16 0.02 . 1 . . . . . . . . 5800 1 972 . 1 1 83 83 GLN HB2 H 1 2.17 0.02 . 1 . . . . . . . . 5800 1 973 . 1 1 83 83 GLN HB3 H 1 2.17 0.02 . 1 . . . . . . . . 5800 1 974 . 1 1 83 83 GLN HG2 H 1 2.47 0.02 . 1 . . . . . . . . 5800 1 975 . 1 1 83 83 GLN HG3 H 1 2.47 0.02 . 1 . . . . . . . . 5800 1 976 . 1 1 83 83 GLN C C 13 177.17 0.2 . 1 . . . . . . . . 5800 1 977 . 1 1 83 83 GLN CA C 13 57.45 0.2 . 1 . . . . . . . . 5800 1 978 . 1 1 83 83 GLN CB C 13 28.69 0.2 . 1 . . . . . . . . 5800 1 979 . 1 1 83 83 GLN CG C 13 33.87 0.2 . 1 . . . . . . . . 5800 1 980 . 1 1 83 83 GLN N N 15 117.69 0.2 . 1 . . . . . . . . 5800 1 981 . 1 1 84 84 ALA H H 1 7.89 0.02 . 1 . . . . . . . . 5800 1 982 . 1 1 84 84 ALA HA H 1 4.29 0.02 . 1 . . . . . . . . 5800 1 983 . 1 1 84 84 ALA HB1 H 1 1.50 0.02 . 1 . . . . . . . . 5800 1 984 . 1 1 84 84 ALA HB2 H 1 1.50 0.02 . 1 . . . . . . . . 5800 1 985 . 1 1 84 84 ALA HB3 H 1 1.50 0.02 . 1 . . . . . . . . 5800 1 986 . 1 1 84 84 ALA C C 13 178.98 0.2 . 1 . . . . . . . . 5800 1 987 . 1 1 84 84 ALA CA C 13 53.56 0.2 . 1 . . . . . . . . 5800 1 988 . 1 1 84 84 ALA CB C 13 18.50 0.2 . 1 . . . . . . . . 5800 1 989 . 1 1 84 84 ALA N N 15 122.51 0.2 . 1 . . . . . . . . 5800 1 990 . 1 1 85 85 GLN H H 1 8.03 0.02 . 1 . . . . . . . . 5800 1 991 . 1 1 85 85 GLN HA H 1 4.25 0.02 . 1 . . . . . . . . 5800 1 992 . 1 1 85 85 GLN HB2 H 1 2.14 0.02 . 1 . . . . . . . . 5800 1 993 . 1 1 85 85 GLN HB3 H 1 2.14 0.02 . 1 . . . . . . . . 5800 1 994 . 1 1 85 85 GLN HG2 H 1 2.47 0.02 . 1 . . . . . . . . 5800 1 995 . 1 1 85 85 GLN HG3 H 1 2.47 0.02 . 1 . . . . . . . . 5800 1 996 . 1 1 85 85 GLN C C 13 176.97 0.2 . 1 . . . . . . . . 5800 1 997 . 1 1 85 85 GLN CA C 13 56.75 0.2 . 1 . . . . . . . . 5800 1 998 . 1 1 85 85 GLN CB C 13 28.99 0.2 . 1 . . . . . . . . 5800 1 999 . 1 1 85 85 GLN CG C 13 33.88 0.2 . 1 . . . . . . . . 5800 1 1000 . 1 1 85 85 GLN N N 15 118.18 0.2 . 1 . . . . . . . . 5800 1 1001 . 1 1 86 86 GLU H H 1 8.14 0.02 . 1 . . . . . . . . 5800 1 1002 . 1 1 86 86 GLU HA H 1 4.21 0.02 . 1 . . . . . . . . 5800 1 1003 . 1 1 86 86 GLU HB2 H 1 2.06 0.02 . 1 . . . . . . . . 5800 1 1004 . 1 1 86 86 GLU HB3 H 1 2.06 0.02 . 1 . . . . . . . . 5800 1 1005 . 1 1 86 86 GLU HG2 H 1 2.33 0.02 . 1 . . . . . . . . 5800 1 1006 . 1 1 86 86 GLU HG3 H 1 2.33 0.02 . 1 . . . . . . . . 5800 1 1007 . 1 1 86 86 GLU CA C 13 57.57 0.2 . 1 . . . . . . . . 5800 1 1008 . 1 1 86 86 GLU CB C 13 30.18 0.2 . 1 . . . . . . . . 5800 1 1009 . 1 1 86 86 GLU CG C 13 36.45 0.2 . 1 . . . . . . . . 5800 1 1010 . 1 1 86 86 GLU N N 15 121.13 0.2 . 1 . . . . . . . . 5800 1 1011 . 1 1 87 87 GLU H H 1 8.31 0.02 . 1 . . . . . . . . 5800 1 1012 . 1 1 87 87 GLU HA H 1 4.25 0.02 . 1 . . . . . . . . 5800 1 1013 . 1 1 87 87 GLU HB2 H 1 2.04 0.02 . 1 . . . . . . . . 5800 1 1014 . 1 1 87 87 GLU HB3 H 1 2.04 0.02 . 1 . . . . . . . . 5800 1 1015 . 1 1 87 87 GLU HG2 H 1 2.33 0.02 . 1 . . . . . . . . 5800 1 1016 . 1 1 87 87 GLU HG3 H 1 2.33 0.02 . 1 . . . . . . . . 5800 1 1017 . 1 1 87 87 GLU C C 13 176.97 0.2 . 1 . . . . . . . . 5800 1 1018 . 1 1 87 87 GLU CA C 13 57.08 0.2 . 1 . . . . . . . . 5800 1 1019 . 1 1 87 87 GLU CB C 13 30.10 0.2 . 1 . . . . . . . . 5800 1 1020 . 1 1 87 87 GLU CG C 13 36.45 0.2 . 1 . . . . . . . . 5800 1 1021 . 1 1 87 87 GLU N N 15 120.93 0.2 . 1 . . . . . . . . 5800 1 1022 . 1 1 88 88 SER H H 1 8.21 0.02 . 1 . . . . . . . . 5800 1 1023 . 1 1 88 88 SER HA H 1 4.46 0.02 . 1 . . . . . . . . 5800 1 1024 . 1 1 88 88 SER HB2 H 1 3.91 0.02 . 1 . . . . . . . . 5800 1 1025 . 1 1 88 88 SER HB3 H 1 3.91 0.02 . 1 . . . . . . . . 5800 1 1026 . 1 1 88 88 SER C C 13 174.88 0.2 . 1 . . . . . . . . 5800 1 1027 . 1 1 88 88 SER CA C 13 58.67 0.2 . 1 . . . . . . . . 5800 1 1028 . 1 1 88 88 SER CB C 13 63.75 0.2 . 1 . . . . . . . . 5800 1 1029 . 1 1 88 88 SER N N 15 116.15 0.2 . 1 . . . . . . . . 5800 1 1030 . 1 1 89 89 LEU H H 1 8.14 0.02 . 1 . . . . . . . . 5800 1 1031 . 1 1 89 89 LEU HA H 1 4.34 0.02 . 1 . . . . . . . . 5800 1 1032 . 1 1 89 89 LEU HB2 H 1 1.62 0.02 . 2 . . . . . . . . 5800 1 1033 . 1 1 89 89 LEU HB3 H 1 1.71 0.02 . 2 . . . . . . . . 5800 1 1034 . 1 1 89 89 LEU HG H 1 1.68 0.02 . 1 . . . . . . . . 5800 1 1035 . 1 1 89 89 LEU HD11 H 1 0.93 0.02 . 2 . . . . . . . . 5800 1 1036 . 1 1 89 89 LEU HD12 H 1 0.93 0.02 . 2 . . . . . . . . 5800 1 1037 . 1 1 89 89 LEU HD13 H 1 0.93 0.02 . 2 . . . . . . . . 5800 1 1038 . 1 1 89 89 LEU HD21 H 1 0.87 0.02 . 2 . . . . . . . . 5800 1 1039 . 1 1 89 89 LEU HD22 H 1 0.87 0.02 . 2 . . . . . . . . 5800 1 1040 . 1 1 89 89 LEU HD23 H 1 0.87 0.02 . 2 . . . . . . . . 5800 1 1041 . 1 1 89 89 LEU C C 13 178.08 0.2 . 1 . . . . . . . . 5800 1 1042 . 1 1 89 89 LEU CA C 13 55.51 0.2 . 1 . . . . . . . . 5800 1 1043 . 1 1 89 89 LEU CB C 13 42.30 0.2 . 1 . . . . . . . . 5800 1 1044 . 1 1 89 89 LEU CG C 13 27.08 0.2 . 1 . . . . . . . . 5800 1 1045 . 1 1 89 89 LEU CD1 C 13 25.11 0.2 . 2 . . . . . . . . 5800 1 1046 . 1 1 89 89 LEU CD2 C 13 23.43 0.2 . 2 . . . . . . . . 5800 1 1047 . 1 1 89 89 LEU N N 15 123.83 0.2 . 1 . . . . . . . . 5800 1 1048 . 1 1 90 90 GLY H H 1 8.22 0.02 . 1 . . . . . . . . 5800 1 1049 . 1 1 90 90 GLY HA2 H 1 3.95 0.02 . 1 . . . . . . . . 5800 1 1050 . 1 1 90 90 GLY HA3 H 1 3.95 0.02 . 1 . . . . . . . . 5800 1 1051 . 1 1 90 90 GLY C C 13 173.96 0.2 . 1 . . . . . . . . 5800 1 1052 . 1 1 90 90 GLY CA C 13 45.44 0.2 . 1 . . . . . . . . 5800 1 1053 . 1 1 90 90 GLY N N 15 108.62 0.2 . 1 . . . . . . . . 5800 1 1054 . 1 1 91 91 ASP H H 1 8.26 0.02 . 1 . . . . . . . . 5800 1 1055 . 1 1 91 91 ASP HA H 1 4.62 0.02 . 1 . . . . . . . . 5800 1 1056 . 1 1 91 91 ASP HB2 H 1 2.58 0.02 . 2 . . . . . . . . 5800 1 1057 . 1 1 91 91 ASP HB3 H 1 2.70 0.02 . 2 . . . . . . . . 5800 1 1058 . 1 1 91 91 ASP C C 13 176.09 0.2 . 1 . . . . . . . . 5800 1 1059 . 1 1 91 91 ASP CA C 13 54.38 0.2 . 1 . . . . . . . . 5800 1 1060 . 1 1 91 91 ASP CB C 13 41.19 0.2 . 1 . . . . . . . . 5800 1 1061 . 1 1 91 91 ASP N N 15 120.61 0.2 . 1 . . . . . . . . 5800 1 1062 . 1 1 92 92 ASN H H 1 8.35 0.02 . 1 . . . . . . . . 5800 1 1063 . 1 1 92 92 ASN HA H 1 4.64 0.02 . 1 . . . . . . . . 5800 1 1064 . 1 1 92 92 ASN HB2 H 1 2.66 0.02 . 1 . . . . . . . . 5800 1 1065 . 1 1 92 92 ASN HB3 H 1 2.66 0.02 . 1 . . . . . . . . 5800 1 1066 . 1 1 92 92 ASN C C 13 177.59 0.2 . 1 . . . . . . . . 5800 1 1067 . 1 1 92 92 ASN CA C 13 53.14 0.2 . 1 . . . . . . . . 5800 1 1068 . 1 1 92 92 ASN CB C 13 38.87 0.2 . 1 . . . . . . . . 5800 1 1069 . 1 1 92 92 ASN N N 15 118.87 0.2 . 1 . . . . . . . . 5800 1 1070 . 1 1 93 93 LYS H H 1 8.02 0.02 . 1 . . . . . . . . 5800 1 1071 . 1 1 93 93 LYS HA H 1 4.53 0.02 . 1 . . . . . . . . 5800 1 1072 . 1 1 93 93 LYS HB2 H 1 1.64 0.02 . 2 . . . . . . . . 5800 1 1073 . 1 1 93 93 LYS HB3 H 1 1.75 0.02 . 2 . . . . . . . . 5800 1 1074 . 1 1 93 93 LYS HG2 H 1 1.42 0.02 . 1 . . . . . . . . 5800 1 1075 . 1 1 93 93 LYS HG3 H 1 1.42 0.02 . 1 . . . . . . . . 5800 1 1076 . 1 1 93 93 LYS HD2 H 1 1.71 0.02 . 1 . . . . . . . . 5800 1 1077 . 1 1 93 93 LYS HD3 H 1 1.71 0.02 . 1 . . . . . . . . 5800 1 1078 . 1 1 93 93 LYS HE2 H 1 3.05 0.02 . 1 . . . . . . . . 5800 1 1079 . 1 1 93 93 LYS HE3 H 1 3.05 0.02 . 1 . . . . . . . . 5800 1 1080 . 1 1 93 93 LYS CA C 13 53.18 0.2 . 1 . . . . . . . . 5800 1 1081 . 1 1 93 93 LYS CB C 13 33.20 0.2 . 1 . . . . . . . . 5800 1 1082 . 1 1 93 93 LYS CG C 13 24.50 0.2 . 1 . . . . . . . . 5800 1 1083 . 1 1 93 93 LYS CD C 13 29.17 0.2 . 1 . . . . . . . . 5800 1 1084 . 1 1 93 93 LYS CE C 13 42.22 0.2 . 1 . . . . . . . . 5800 1 1085 . 1 1 93 93 LYS N N 15 120.49 0.2 . 1 . . . . . . . . 5800 1 1086 . 1 1 94 94 PRO HA H 1 4.40 0.02 . 1 . . . . . . . . 5800 1 1087 . 1 1 94 94 PRO HB2 H 1 2.29 0.02 . 2 . . . . . . . . 5800 1 1088 . 1 1 94 94 PRO HB3 H 1 1.92 0.02 . 2 . . . . . . . . 5800 1 1089 . 1 1 94 94 PRO HG2 H 1 2.01 0.02 . 1 . . . . . . . . 5800 1 1090 . 1 1 94 94 PRO HG3 H 1 2.01 0.02 . 1 . . . . . . . . 5800 1 1091 . 1 1 94 94 PRO HD2 H 1 3.62 0.02 . 2 . . . . . . . . 5800 1 1092 . 1 1 94 94 PRO HD3 H 1 3.81 0.02 . 2 . . . . . . . . 5800 1 1093 . 1 1 94 94 PRO C C 13 176.72 0.2 . 1 . . . . . . . . 5800 1 1094 . 1 1 94 94 PRO CA C 13 63.04 0.2 . 1 . . . . . . . . 5800 1 1095 . 1 1 94 94 PRO CB C 13 32.14 0.2 . 1 . . . . . . . . 5800 1 1096 . 1 1 94 94 PRO CG C 13 27.66 0.2 . 1 . . . . . . . . 5800 1 1097 . 1 1 94 94 PRO CD C 13 50.65 0.2 . 1 . . . . . . . . 5800 1 1098 . 1 1 95 95 ALA H H 1 8.40 0.02 . 1 . . . . . . . . 5800 1 1099 . 1 1 95 95 ALA HA H 1 4.37 0.02 . 1 . . . . . . . . 5800 1 1100 . 1 1 95 95 ALA HB1 H 1 1.61 0.02 . 1 . . . . . . . . 5800 1 1101 . 1 1 95 95 ALA HB2 H 1 1.61 0.02 . 1 . . . . . . . . 5800 1 1102 . 1 1 95 95 ALA HB3 H 1 1.61 0.02 . 1 . . . . . . . . 5800 1 1103 . 1 1 95 95 ALA C C 13 178.07 0.2 . 1 . . . . . . . . 5800 1 1104 . 1 1 95 95 ALA CA C 13 51.22 0.2 . 1 . . . . . . . . 5800 1 1105 . 1 1 95 95 ALA CB C 13 20.69 0.2 . 1 . . . . . . . . 5800 1 1106 . 1 1 95 95 ALA N N 15 124.34 0.2 . 1 . . . . . . . . 5800 1 1107 . 1 1 96 96 ASP H H 1 8.56 0.02 . 1 . . . . . . . . 5800 1 1108 . 1 1 96 96 ASP HA H 1 4.29 0.02 . 1 . . . . . . . . 5800 1 1109 . 1 1 96 96 ASP HB2 H 1 2.57 0.02 . 1 . . . . . . . . 5800 1 1110 . 1 1 96 96 ASP HB3 H 1 2.57 0.02 . 1 . . . . . . . . 5800 1 1111 . 1 1 96 96 ASP C C 13 177.40 0.2 . 1 . . . . . . . . 5800 1 1112 . 1 1 96 96 ASP CA C 13 57.47 0.2 . 1 . . . . . . . . 5800 1 1113 . 1 1 96 96 ASP CB C 13 40.52 0.2 . 1 . . . . . . . . 5800 1 1114 . 1 1 96 96 ASP N N 15 119.82 0.2 . 1 . . . . . . . . 5800 1 1115 . 1 1 97 97 ASP H H 1 8.43 0.02 . 1 . . . . . . . . 5800 1 1116 . 1 1 97 97 ASP HA H 1 4.21 0.02 . 1 . . . . . . . . 5800 1 1117 . 1 1 97 97 ASP HB2 H 1 2.62 0.02 . 2 . . . . . . . . 5800 1 1118 . 1 1 97 97 ASP HB3 H 1 2.71 0.02 . 2 . . . . . . . . 5800 1 1119 . 1 1 97 97 ASP C C 13 177.48 0.2 . 1 . . . . . . . . 5800 1 1120 . 1 1 97 97 ASP CA C 13 56.09 0.2 . 1 . . . . . . . . 5800 1 1121 . 1 1 97 97 ASP CB C 13 39.06 0.2 . 1 . . . . . . . . 5800 1 1122 . 1 1 97 97 ASP N N 15 116.26 0.2 . 1 . . . . . . . . 5800 1 1123 . 1 1 98 98 LEU H H 1 7.37 0.02 . 1 . . . . . . . . 5800 1 1124 . 1 1 98 98 LEU HA H 1 4.01 0.02 . 1 . . . . . . . . 5800 1 1125 . 1 1 98 98 LEU HB2 H 1 1.07 0.02 . 2 . . . . . . . . 5800 1 1126 . 1 1 98 98 LEU HB3 H 1 1.84 0.02 . 2 . . . . . . . . 5800 1 1127 . 1 1 98 98 LEU HG H 1 1.37 0.02 . 1 . . . . . . . . 5800 1 1128 . 1 1 98 98 LEU HD11 H 1 0.73 0.02 . 1 . . . . . . . . 5800 1 1129 . 1 1 98 98 LEU HD12 H 1 0.73 0.02 . 1 . . . . . . . . 5800 1 1130 . 1 1 98 98 LEU HD13 H 1 0.73 0.02 . 1 . . . . . . . . 5800 1 1131 . 1 1 98 98 LEU HD21 H 1 0.73 0.02 . 1 . . . . . . . . 5800 1 1132 . 1 1 98 98 LEU HD22 H 1 0.73 0.02 . 1 . . . . . . . . 5800 1 1133 . 1 1 98 98 LEU HD23 H 1 0.73 0.02 . 1 . . . . . . . . 5800 1 1134 . 1 1 98 98 LEU C C 13 177.34 0.2 . 1 . . . . . . . . 5800 1 1135 . 1 1 98 98 LEU CA C 13 57.24 0.2 . 1 . . . . . . . . 5800 1 1136 . 1 1 98 98 LEU CB C 13 42.93 0.2 . 1 . . . . . . . . 5800 1 1137 . 1 1 98 98 LEU CG C 13 27.90 0.2 . 1 . . . . . . . . 5800 1 1138 . 1 1 98 98 LEU CD1 C 13 25.10 0.2 . 1 . . . . . . . . 5800 1 1139 . 1 1 98 98 LEU CD2 C 13 25.10 0.2 . 1 . . . . . . . . 5800 1 1140 . 1 1 98 98 LEU N N 15 122.75 0.2 . 1 . . . . . . . . 5800 1 1141 . 1 1 99 99 LEU H H 1 7.65 0.02 . 1 . . . . . . . . 5800 1 1142 . 1 1 99 99 LEU HA H 1 3.76 0.02 . 1 . . . . . . . . 5800 1 1143 . 1 1 99 99 LEU HB2 H 1 1.46 0.02 . 2 . . . . . . . . 5800 1 1144 . 1 1 99 99 LEU HB3 H 1 1.72 0.02 . 2 . . . . . . . . 5800 1 1145 . 1 1 99 99 LEU HG H 1 1.42 0.02 . 1 . . . . . . . . 5800 1 1146 . 1 1 99 99 LEU HD11 H 1 0.79 0.02 . 2 . . . . . . . . 5800 1 1147 . 1 1 99 99 LEU HD12 H 1 0.79 0.02 . 2 . . . . . . . . 5800 1 1148 . 1 1 99 99 LEU HD13 H 1 0.79 0.02 . 2 . . . . . . . . 5800 1 1149 . 1 1 99 99 LEU HD21 H 1 0.81 0.02 . 2 . . . . . . . . 5800 1 1150 . 1 1 99 99 LEU HD22 H 1 0.81 0.02 . 2 . . . . . . . . 5800 1 1151 . 1 1 99 99 LEU HD23 H 1 0.81 0.02 . 2 . . . . . . . . 5800 1 1152 . 1 1 99 99 LEU C C 13 177.87 0.2 . 1 . . . . . . . . 5800 1 1153 . 1 1 99 99 LEU CA C 13 57.08 0.2 . 1 . . . . . . . . 5800 1 1154 . 1 1 99 99 LEU CB C 13 42.60 0.2 . 1 . . . . . . . . 5800 1 1155 . 1 1 99 99 LEU CG C 13 27.33 0.2 . 1 . . . . . . . . 5800 1 1156 . 1 1 99 99 LEU CD1 C 13 24.22 0.2 . 2 . . . . . . . . 5800 1 1157 . 1 1 99 99 LEU CD2 C 13 25.40 0.2 . 2 . . . . . . . . 5800 1 1158 . 1 1 99 99 LEU N N 15 115.21 0.2 . 1 . . . . . . . . 5800 1 1159 . 1 1 100 100 ASN H H 1 7.48 0.02 . 1 . . . . . . . . 5800 1 1160 . 1 1 100 100 ASN HA H 1 4.68 0.02 . 1 . . . . . . . . 5800 1 1161 . 1 1 100 100 ASN HB2 H 1 2.66 0.02 . 2 . . . . . . . . 5800 1 1162 . 1 1 100 100 ASN HB3 H 1 2.92 0.02 . 2 . . . . . . . . 5800 1 1163 . 1 1 100 100 ASN C C 13 174.84 0.2 . 1 . . . . . . . . 5800 1 1164 . 1 1 100 100 ASN CA C 13 53.01 0.2 . 1 . . . . . . . . 5800 1 1165 . 1 1 100 100 ASN CB C 13 39.34 0.2 . 1 . . . . . . . . 5800 1 1166 . 1 1 100 100 ASN N N 15 112.32 0.2 . 1 . . . . . . . . 5800 1 1167 . 1 1 101 101 LEU H H 1 7.32 0.02 . 1 . . . . . . . . 5800 1 1168 . 1 1 101 101 LEU HA H 1 4.12 0.02 . 1 . . . . . . . . 5800 1 1169 . 1 1 101 101 LEU HB2 H 1 1.46 0.02 . 2 . . . . . . . . 5800 1 1170 . 1 1 101 101 LEU HB3 H 1 1.88 0.02 . 2 . . . . . . . . 5800 1 1171 . 1 1 101 101 LEU HG H 1 1.74 0.02 . 1 . . . . . . . . 5800 1 1172 . 1 1 101 101 LEU HD11 H 1 0.86 0.02 . 2 . . . . . . . . 5800 1 1173 . 1 1 101 101 LEU HD12 H 1 0.86 0.02 . 2 . . . . . . . . 5800 1 1174 . 1 1 101 101 LEU HD13 H 1 0.86 0.02 . 2 . . . . . . . . 5800 1 1175 . 1 1 101 101 LEU HD21 H 1 0.72 0.02 . 2 . . . . . . . . 5800 1 1176 . 1 1 101 101 LEU HD22 H 1 0.72 0.02 . 2 . . . . . . . . 5800 1 1177 . 1 1 101 101 LEU HD23 H 1 0.72 0.02 . 2 . . . . . . . . 5800 1 1178 . 1 1 101 101 LEU C C 13 176.69 0.2 . 1 . . . . . . . . 5800 1 1179 . 1 1 101 101 LEU CA C 13 55.25 0.2 . 1 . . . . . . . . 5800 1 1180 . 1 1 101 101 LEU CB C 13 41.85 0.2 . 1 . . . . . . . . 5800 1 1181 . 1 1 101 101 LEU CG C 13 25.53 0.2 . 1 . . . . . . . . 5800 1 1182 . 1 1 101 101 LEU CD1 C 13 23.56 0.2 . 2 . . . . . . . . 5800 1 1183 . 1 1 101 101 LEU CD2 C 13 25.65 0.2 . 2 . . . . . . . . 5800 1 1184 . 1 1 101 101 LEU N N 15 125.04 0.2 . 1 . . . . . . . . 5800 1 1185 . 1 1 102 102 GLU H H 1 8.57 0.02 . 1 . . . . . . . . 5800 1 1186 . 1 1 102 102 GLU HA H 1 3.95 0.02 . 1 . . . . . . . . 5800 1 1187 . 1 1 102 102 GLU HB2 H 1 1.89 0.02 . 2 . . . . . . . . 5800 1 1188 . 1 1 102 102 GLU HB3 H 1 2.02 0.02 . 2 . . . . . . . . 5800 1 1189 . 1 1 102 102 GLU HG2 H 1 2.23 0.02 . 1 . . . . . . . . 5800 1 1190 . 1 1 102 102 GLU HG3 H 1 2.23 0.02 . 1 . . . . . . . . 5800 1 1191 . 1 1 102 102 GLU C C 13 176.34 0.2 . 1 . . . . . . . . 5800 1 1192 . 1 1 102 102 GLU CA C 13 58.49 0.2 . 1 . . . . . . . . 5800 1 1193 . 1 1 102 102 GLU CB C 13 29.13 0.2 . 1 . . . . . . . . 5800 1 1194 . 1 1 102 102 GLU CG C 13 35.91 0.2 . 1 . . . . . . . . 5800 1 1195 . 1 1 102 102 GLU N N 15 105.02 0.2 . 1 . . . . . . . . 5800 1 1196 . 1 1 103 103 GLY H H 1 8.58 0.02 . 1 . . . . . . . . 5800 1 1197 . 1 1 103 103 GLY HA2 H 1 3.61 0.02 . 2 . . . . . . . . 5800 1 1198 . 1 1 103 103 GLY HA3 H 1 4.23 0.02 . 2 . . . . . . . . 5800 1 1199 . 1 1 103 103 GLY C C 13 174.36 0.2 . 1 . . . . . . . . 5800 1 1200 . 1 1 103 103 GLY CA C 13 44.68 0.2 . 1 . . . . . . . . 5800 1 1201 . 1 1 103 103 GLY N N 15 112.15 0.2 . 1 . . . . . . . . 5800 1 1202 . 1 1 104 104 VAL H H 1 7.89 0.02 . 1 . . . . . . . . 5800 1 1203 . 1 1 104 104 VAL HA H 1 3.99 0.02 . 1 . . . . . . . . 5800 1 1204 . 1 1 104 104 VAL HB H 1 2.43 0.02 . 1 . . . . . . . . 5800 1 1205 . 1 1 104 104 VAL HG11 H 1 0.81 0.02 . 2 . . . . . . . . 5800 1 1206 . 1 1 104 104 VAL HG12 H 1 0.81 0.02 . 2 . . . . . . . . 5800 1 1207 . 1 1 104 104 VAL HG13 H 1 0.81 0.02 . 2 . . . . . . . . 5800 1 1208 . 1 1 104 104 VAL HG21 H 1 0.74 0.02 . 2 . . . . . . . . 5800 1 1209 . 1 1 104 104 VAL HG22 H 1 0.74 0.02 . 2 . . . . . . . . 5800 1 1210 . 1 1 104 104 VAL HG23 H 1 0.74 0.02 . 2 . . . . . . . . 5800 1 1211 . 1 1 104 104 VAL C C 13 174.59 0.2 . 1 . . . . . . . . 5800 1 1212 . 1 1 104 104 VAL CA C 13 62.78 0.2 . 1 . . . . . . . . 5800 1 1213 . 1 1 104 104 VAL CB C 13 32.10 0.2 . 1 . . . . . . . . 5800 1 1214 . 1 1 104 104 VAL CG1 C 13 22.50 0.2 . 2 . . . . . . . . 5800 1 1215 . 1 1 104 104 VAL CG2 C 13 24.10 0.2 . 2 . . . . . . . . 5800 1 1216 . 1 1 104 104 VAL N N 15 121.81 0.2 . 1 . . . . . . . . 5800 1 1217 . 1 1 105 105 ASP H H 1 7.37 0.02 . 1 . . . . . . . . 5800 1 1218 . 1 1 105 105 ASP HA H 1 4.85 0.02 . 1 . . . . . . . . 5800 1 1219 . 1 1 105 105 ASP HB2 H 1 2.70 0.02 . 2 . . . . . . . . 5800 1 1220 . 1 1 105 105 ASP HB3 H 1 3.03 0.02 . 2 . . . . . . . . 5800 1 1221 . 1 1 105 105 ASP C C 13 175.53 0.2 . 1 . . . . . . . . 5800 1 1222 . 1 1 105 105 ASP CA C 13 51.73 0.2 . 1 . . . . . . . . 5800 1 1223 . 1 1 105 105 ASP CB C 13 42.08 0.2 . 1 . . . . . . . . 5800 1 1224 . 1 1 105 105 ASP N N 15 124.80 0.2 . 1 . . . . . . . . 5800 1 1225 . 1 1 106 106 ARG H H 1 8.64 0.02 . 1 . . . . . . . . 5800 1 1226 . 1 1 106 106 ARG HA H 1 3.84 0.02 . 1 . . . . . . . . 5800 1 1227 . 1 1 106 106 ARG HB2 H 1 1.91 0.02 . 2 . . . . . . . . 5800 1 1228 . 1 1 106 106 ARG HB3 H 1 1.82 0.02 . 2 . . . . . . . . 5800 1 1229 . 1 1 106 106 ARG HG2 H 1 1.76 0.02 . 2 . . . . . . . . 5800 1 1230 . 1 1 106 106 ARG HG3 H 1 1.67 0.02 . 2 . . . . . . . . 5800 1 1231 . 1 1 106 106 ARG HD2 H 1 3.21 0.02 . 1 . . . . . . . . 5800 1 1232 . 1 1 106 106 ARG HD3 H 1 3.21 0.02 . 1 . . . . . . . . 5800 1 1233 . 1 1 106 106 ARG C C 13 177.85 0.2 . 1 . . . . . . . . 5800 1 1234 . 1 1 106 106 ARG CA C 13 60.65 0.2 . 1 . . . . . . . . 5800 1 1235 . 1 1 106 106 ARG CB C 13 29.98 0.2 . 1 . . . . . . . . 5800 1 1236 . 1 1 106 106 ARG CG C 13 28.00 0.2 . 1 . . . . . . . . 5800 1 1237 . 1 1 106 106 ARG CD C 13 43.15 0.2 . 1 . . . . . . . . 5800 1 1238 . 1 1 106 106 ARG N N 15 120.86 0.2 . 1 . . . . . . . . 5800 1 1239 . 1 1 107 107 ASP H H 1 8.11 0.02 . 1 . . . . . . . . 5800 1 1240 . 1 1 107 107 ASP HA H 1 4.55 0.02 . 1 . . . . . . . . 5800 1 1241 . 1 1 107 107 ASP HB2 H 1 2.73 0.02 . 2 . . . . . . . . 5800 1 1242 . 1 1 107 107 ASP HB3 H 1 2.64 0.02 . 2 . . . . . . . . 5800 1 1243 . 1 1 107 107 ASP C C 13 178.97 0.2 . 1 . . . . . . . . 5800 1 1244 . 1 1 107 107 ASP CA C 13 57.58 0.2 . 1 . . . . . . . . 5800 1 1245 . 1 1 107 107 ASP CB C 13 40.88 0.2 . 1 . . . . . . . . 5800 1 1246 . 1 1 107 107 ASP N N 15 116.73 0.2 . 1 . . . . . . . . 5800 1 1247 . 1 1 108 108 LEU H H 1 8.18 0.02 . 1 . . . . . . . . 5800 1 1248 . 1 1 108 108 LEU HA H 1 4.14 0.02 . 1 . . . . . . . . 5800 1 1249 . 1 1 108 108 LEU HB2 H 1 1.83 0.02 . 2 . . . . . . . . 5800 1 1250 . 1 1 108 108 LEU HB3 H 1 1.87 0.02 . 2 . . . . . . . . 5800 1 1251 . 1 1 108 108 LEU HG H 1 1.60 0.02 . 1 . . . . . . . . 5800 1 1252 . 1 1 108 108 LEU HD11 H 1 1.05 0.02 . 2 . . . . . . . . 5800 1 1253 . 1 1 108 108 LEU HD12 H 1 1.05 0.02 . 2 . . . . . . . . 5800 1 1254 . 1 1 108 108 LEU HD13 H 1 1.05 0.02 . 2 . . . . . . . . 5800 1 1255 . 1 1 108 108 LEU HD21 H 1 1.02 0.02 . 2 . . . . . . . . 5800 1 1256 . 1 1 108 108 LEU HD22 H 1 1.02 0.02 . 2 . . . . . . . . 5800 1 1257 . 1 1 108 108 LEU HD23 H 1 1.02 0.02 . 2 . . . . . . . . 5800 1 1258 . 1 1 108 108 LEU C C 13 178.48 0.2 . 1 . . . . . . . . 5800 1 1259 . 1 1 108 108 LEU CA C 13 57.69 0.2 . 1 . . . . . . . . 5800 1 1260 . 1 1 108 108 LEU CB C 13 41.24 0.2 . 1 . . . . . . . . 5800 1 1261 . 1 1 108 108 LEU CG C 13 27.43 0.2 . 1 . . . . . . . . 5800 1 1262 . 1 1 108 108 LEU CD1 C 13 26.51 0.2 . 2 . . . . . . . . 5800 1 1263 . 1 1 108 108 LEU CD2 C 13 23.39 0.2 . 2 . . . . . . . . 5800 1 1264 . 1 1 108 108 LEU N N 15 121.86 0.2 . 1 . . . . . . . . 5800 1 1265 . 1 1 109 109 ALA H H 1 8.64 0.02 . 1 . . . . . . . . 5800 1 1266 . 1 1 109 109 ALA HA H 1 3.80 0.02 . 1 . . . . . . . . 5800 1 1267 . 1 1 109 109 ALA HB1 H 1 1.33 0.02 . 1 . . . . . . . . 5800 1 1268 . 1 1 109 109 ALA HB2 H 1 1.33 0.02 . 1 . . . . . . . . 5800 1 1269 . 1 1 109 109 ALA HB3 H 1 1.33 0.02 . 1 . . . . . . . . 5800 1 1270 . 1 1 109 109 ALA C C 13 179.72 0.2 . 1 . . . . . . . . 5800 1 1271 . 1 1 109 109 ALA CA C 13 55.76 0.2 . 1 . . . . . . . . 5800 1 1272 . 1 1 109 109 ALA CB C 13 18.05 0.2 . 1 . . . . . . . . 5800 1 1273 . 1 1 109 109 ALA N N 15 120.86 0.2 . 1 . . . . . . . . 5800 1 1274 . 1 1 110 110 PHE H H 1 8.18 0.02 . 1 . . . . . . . . 5800 1 1275 . 1 1 110 110 PHE HA H 1 4.12 0.02 . 1 . . . . . . . . 5800 1 1276 . 1 1 110 110 PHE HB2 H 1 3.22 0.02 . 1 . . . . . . . . 5800 1 1277 . 1 1 110 110 PHE HB3 H 1 3.22 0.02 . 1 . . . . . . . . 5800 1 1278 . 1 1 110 110 PHE HD1 H 1 7.58 0.02 . 1 . . . . . . . . 5800 1 1279 . 1 1 110 110 PHE HD2 H 1 7.58 0.02 . 1 . . . . . . . . 5800 1 1280 . 1 1 110 110 PHE HE1 H 1 7.32 0.02 . 1 . . . . . . . . 5800 1 1281 . 1 1 110 110 PHE HE2 H 1 7.32 0.02 . 1 . . . . . . . . 5800 1 1282 . 1 1 110 110 PHE C C 13 179.16 0.2 . 1 . . . . . . . . 5800 1 1283 . 1 1 110 110 PHE CA C 13 62.48 0.2 . 1 . . . . . . . . 5800 1 1284 . 1 1 110 110 PHE CB C 13 38.56 0.2 . 1 . . . . . . . . 5800 1 1285 . 1 1 110 110 PHE N N 15 115.53 0.2 . 1 . . . . . . . . 5800 1 1286 . 1 1 111 111 LYS H H 1 8.04 0.02 . 1 . . . . . . . . 5800 1 1287 . 1 1 111 111 LYS HA H 1 4.14 0.02 . 1 . . . . . . . . 5800 1 1288 . 1 1 111 111 LYS HB2 H 1 1.88 0.02 . 1 . . . . . . . . 5800 1 1289 . 1 1 111 111 LYS HB3 H 1 1.88 0.02 . 1 . . . . . . . . 5800 1 1290 . 1 1 111 111 LYS HG2 H 1 1.56 0.02 . 1 . . . . . . . . 5800 1 1291 . 1 1 111 111 LYS HG3 H 1 1.56 0.02 . 1 . . . . . . . . 5800 1 1292 . 1 1 111 111 LYS HD2 H 1 1.63 0.02 . 2 . . . . . . . . 5800 1 1293 . 1 1 111 111 LYS HD3 H 1 1.79 0.02 . 2 . . . . . . . . 5800 1 1294 . 1 1 111 111 LYS HE2 H 1 2.98 0.02 . 1 . . . . . . . . 5800 1 1295 . 1 1 111 111 LYS HE3 H 1 2.98 0.02 . 1 . . . . . . . . 5800 1 1296 . 1 1 111 111 LYS C C 13 179.99 0.2 . 1 . . . . . . . . 5800 1 1297 . 1 1 111 111 LYS CA C 13 60.06 0.2 . 1 . . . . . . . . 5800 1 1298 . 1 1 111 111 LYS CB C 13 32.91 0.2 . 1 . . . . . . . . 5800 1 1299 . 1 1 111 111 LYS CG C 13 26.50 0.2 . 1 . . . . . . . . 5800 1 1300 . 1 1 111 111 LYS CD C 13 29.50 0.2 . 1 . . . . . . . . 5800 1 1301 . 1 1 111 111 LYS CE C 13 42.00 0.2 . 1 . . . . . . . . 5800 1 1302 . 1 1 111 111 LYS N N 15 122.92 0.2 . 1 . . . . . . . . 5800 1 1303 . 1 1 112 112 LEU H H 1 8.64 0.02 . 1 . . . . . . . . 5800 1 1304 . 1 1 112 112 LEU HA H 1 4.16 0.02 . 1 . . . . . . . . 5800 1 1305 . 1 1 112 112 LEU C C 13 179.53 0.2 . 1 . . . . . . . . 5800 1 1306 . 1 1 112 112 LEU CA C 13 58.18 0.2 . 1 . . . . . . . . 5800 1 1307 . 1 1 112 112 LEU CB C 13 38.19 0.2 . 1 . . . . . . . . 5800 1 1308 . 1 1 112 112 LEU N N 15 120.86 0.2 . 1 . . . . . . . . 5800 1 1309 . 1 1 113 113 ALA H H 1 8.20 0.02 . 1 . . . . . . . . 5800 1 1310 . 1 1 113 113 ALA HA H 1 3.80 0.02 . 1 . . . . . . . . 5800 1 1311 . 1 1 113 113 ALA HB1 H 1 1.15 0.02 . 1 . . . . . . . . 5800 1 1312 . 1 1 113 113 ALA HB2 H 1 1.15 0.02 . 1 . . . . . . . . 5800 1 1313 . 1 1 113 113 ALA HB3 H 1 1.15 0.02 . 1 . . . . . . . . 5800 1 1314 . 1 1 113 113 ALA C C 13 180.90 0.2 . 1 . . . . . . . . 5800 1 1315 . 1 1 113 113 ALA CA C 13 54.85 0.2 . 1 . . . . . . . . 5800 1 1316 . 1 1 113 113 ALA CB C 13 18.01 0.2 . 1 . . . . . . . . 5800 1 1317 . 1 1 113 113 ALA N N 15 123.66 0.2 . 1 . . . . . . . . 5800 1 1318 . 1 1 114 114 ALA H H 1 7.82 0.02 . 1 . . . . . . . . 5800 1 1319 . 1 1 114 114 ALA HA H 1 4.16 0.02 . 1 . . . . . . . . 5800 1 1320 . 1 1 114 114 ALA HB1 H 1 1.54 0.02 . 1 . . . . . . . . 5800 1 1321 . 1 1 114 114 ALA HB2 H 1 1.54 0.02 . 1 . . . . . . . . 5800 1 1322 . 1 1 114 114 ALA HB3 H 1 1.54 0.02 . 1 . . . . . . . . 5800 1 1323 . 1 1 114 114 ALA C C 13 179.09 0.2 . 1 . . . . . . . . 5800 1 1324 . 1 1 114 114 ALA CA C 13 54.48 0.2 . 1 . . . . . . . . 5800 1 1325 . 1 1 114 114 ALA CB C 13 18.00 0.2 . 1 . . . . . . . . 5800 1 1326 . 1 1 114 114 ALA N N 15 120.96 0.2 . 1 . . . . . . . . 5800 1 1327 . 1 1 115 115 ARG H H 1 7.39 0.02 . 1 . . . . . . . . 5800 1 1328 . 1 1 115 115 ARG HA H 1 4.55 0.02 . 1 . . . . . . . . 5800 1 1329 . 1 1 115 115 ARG HB2 H 1 1.88 0.02 . 2 . . . . . . . . 5800 1 1330 . 1 1 115 115 ARG HB3 H 1 2.14 0.02 . 2 . . . . . . . . 5800 1 1331 . 1 1 115 115 ARG HG2 H 1 1.75 0.02 . 2 . . . . . . . . 5800 1 1332 . 1 1 115 115 ARG HG3 H 1 1.81 0.02 . 2 . . . . . . . . 5800 1 1333 . 1 1 115 115 ARG HD2 H 1 3.13 0.02 . 2 . . . . . . . . 5800 1 1334 . 1 1 115 115 ARG HD3 H 1 3.24 0.02 . 2 . . . . . . . . 5800 1 1335 . 1 1 115 115 ARG C C 13 175.94 0.2 . 1 . . . . . . . . 5800 1 1336 . 1 1 115 115 ARG CA C 13 54.52 0.2 . 1 . . . . . . . . 5800 1 1337 . 1 1 115 115 ARG CB C 13 29.95 0.2 . 1 . . . . . . . . 5800 1 1338 . 1 1 115 115 ARG CG C 13 27.30 0.2 . 1 . . . . . . . . 5800 1 1339 . 1 1 115 115 ARG CD C 13 43.15 0.2 . 1 . . . . . . . . 5800 1 1340 . 1 1 115 115 ARG N N 15 115.50 0.2 . 1 . . . . . . . . 5800 1 1341 . 1 1 116 116 GLY H H 1 7.95 0.02 . 1 . . . . . . . . 5800 1 1342 . 1 1 116 116 GLY HA2 H 1 3.60 0.02 . 2 . . . . . . . . 5800 1 1343 . 1 1 116 116 GLY HA3 H 1 4.20 0.02 . 2 . . . . . . . . 5800 1 1344 . 1 1 116 116 GLY C C 13 173.84 0.2 . 1 . . . . . . . . 5800 1 1345 . 1 1 116 116 GLY CA C 13 45.38 0.2 . 1 . . . . . . . . 5800 1 1346 . 1 1 116 116 GLY N N 15 107.71 0.2 . 1 . . . . . . . . 5800 1 1347 . 1 1 117 117 VAL H H 1 8.01 0.02 . 1 . . . . . . . . 5800 1 1348 . 1 1 117 117 VAL HA H 1 3.97 0.02 . 1 . . . . . . . . 5800 1 1349 . 1 1 117 117 VAL HB H 1 1.99 0.02 . 1 . . . . . . . . 5800 1 1350 . 1 1 117 117 VAL HG11 H 1 0.70 0.02 . 2 . . . . . . . . 5800 1 1351 . 1 1 117 117 VAL HG12 H 1 0.70 0.02 . 2 . . . . . . . . 5800 1 1352 . 1 1 117 117 VAL HG13 H 1 0.70 0.02 . 2 . . . . . . . . 5800 1 1353 . 1 1 117 117 VAL HG21 H 1 0.63 0.02 . 2 . . . . . . . . 5800 1 1354 . 1 1 117 117 VAL HG22 H 1 0.63 0.02 . 2 . . . . . . . . 5800 1 1355 . 1 1 117 117 VAL HG23 H 1 0.63 0.02 . 2 . . . . . . . . 5800 1 1356 . 1 1 117 117 VAL C C 13 172.36 0.2 . 1 . . . . . . . . 5800 1 1357 . 1 1 117 117 VAL CA C 13 61.34 0.2 . 1 . . . . . . . . 5800 1 1358 . 1 1 117 117 VAL CB C 13 29.88 0.2 . 1 . . . . . . . . 5800 1 1359 . 1 1 117 117 VAL CG1 C 13 21.51 0.2 . 2 . . . . . . . . 5800 1 1360 . 1 1 117 117 VAL CG2 C 13 19.94 0.2 . 2 . . . . . . . . 5800 1 1361 . 1 1 117 117 VAL N N 15 125.27 0.2 . 1 . . . . . . . . 5800 1 1362 . 1 1 118 118 CYS H H 1 8.46 0.02 . 1 . . . . . . . . 5800 1 1363 . 1 1 118 118 CYS HA H 1 4.36 0.02 . 1 . . . . . . . . 5800 1 1364 . 1 1 118 118 CYS HB2 H 1 2.90 0.02 . 2 . . . . . . . . 5800 1 1365 . 1 1 118 118 CYS HB3 H 1 3.16 0.02 . 2 . . . . . . . . 5800 1 1366 . 1 1 118 118 CYS C C 13 173.85 0.2 . 1 . . . . . . . . 5800 1 1367 . 1 1 118 118 CYS CA C 13 60.19 0.2 . 1 . . . . . . . . 5800 1 1368 . 1 1 118 118 CYS CB C 13 30.28 0.2 . 1 . . . . . . . . 5800 1 1369 . 1 1 118 118 CYS N N 15 119.22 0.2 . 1 . . . . . . . . 5800 1 1370 . 1 1 119 119 THR H H 1 7.97 0.02 . 1 . . . . . . . . 5800 1 1371 . 1 1 119 119 THR HA H 1 4.89 0.02 . 1 . . . . . . . . 5800 1 1372 . 1 1 119 119 THR HB H 1 4.76 0.02 . 1 . . . . . . . . 5800 1 1373 . 1 1 119 119 THR HG21 H 1 1.18 0.02 . 1 . . . . . . . . 5800 1 1374 . 1 1 119 119 THR HG22 H 1 1.18 0.02 . 1 . . . . . . . . 5800 1 1375 . 1 1 119 119 THR HG23 H 1 1.18 0.02 . 1 . . . . . . . . 5800 1 1376 . 1 1 119 119 THR C C 13 175.19 0.2 . 1 . . . . . . . . 5800 1 1377 . 1 1 119 119 THR CA C 13 58.71 0.2 . 1 . . . . . . . . 5800 1 1378 . 1 1 119 119 THR CB C 13 72.34 0.2 . 1 . . . . . . . . 5800 1 1379 . 1 1 119 119 THR N N 15 107.89 0.2 . 1 . . . . . . . . 5800 1 1380 . 1 1 120 120 LEU H H 1 8.78 0.02 . 1 . . . . . . . . 5800 1 1381 . 1 1 120 120 LEU HA H 1 3.87 0.02 . 1 . . . . . . . . 5800 1 1382 . 1 1 120 120 LEU HB2 H 1 1.27 0.02 . 2 . . . . . . . . 5800 1 1383 . 1 1 120 120 LEU HB3 H 1 1.60 0.02 . 2 . . . . . . . . 5800 1 1384 . 1 1 120 120 LEU HG H 1 1.47 0.02 . 1 . . . . . . . . 5800 1 1385 . 1 1 120 120 LEU HD11 H 1 0.96 0.02 . 2 . . . . . . . . 5800 1 1386 . 1 1 120 120 LEU HD12 H 1 0.96 0.02 . 2 . . . . . . . . 5800 1 1387 . 1 1 120 120 LEU HD13 H 1 0.96 0.02 . 2 . . . . . . . . 5800 1 1388 . 1 1 120 120 LEU HD21 H 1 0.86 0.02 . 2 . . . . . . . . 5800 1 1389 . 1 1 120 120 LEU HD22 H 1 0.86 0.02 . 2 . . . . . . . . 5800 1 1390 . 1 1 120 120 LEU HD23 H 1 0.86 0.02 . 2 . . . . . . . . 5800 1 1391 . 1 1 120 120 LEU C C 13 178.09 0.2 . 1 . . . . . . . . 5800 1 1392 . 1 1 120 120 LEU CA C 13 58.09 0.2 . 1 . . . . . . . . 5800 1 1393 . 1 1 120 120 LEU CB C 13 41.81 0.2 . 1 . . . . . . . . 5800 1 1394 . 1 1 120 120 LEU CG C 13 26.96 0.2 . 1 . . . . . . . . 5800 1 1395 . 1 1 120 120 LEU CD1 C 13 26.79 0.2 . 2 . . . . . . . . 5800 1 1396 . 1 1 120 120 LEU CD2 C 13 25.42 0.2 . 2 . . . . . . . . 5800 1 1397 . 1 1 120 120 LEU N N 15 120.45 0.2 . 1 . . . . . . . . 5800 1 1398 . 1 1 121 121 GLU H H 1 8.48 0.02 . 1 . . . . . . . . 5800 1 1399 . 1 1 121 121 GLU HA H 1 3.99 0.02 . 1 . . . . . . . . 5800 1 1400 . 1 1 121 121 GLU HB2 H 1 2.06 0.02 . 2 . . . . . . . . 5800 1 1401 . 1 1 121 121 GLU HB3 H 1 1.93 0.02 . 2 . . . . . . . . 5800 1 1402 . 1 1 121 121 GLU HG2 H 1 2.45 0.02 . 1 . . . . . . . . 5800 1 1403 . 1 1 121 121 GLU HG3 H 1 2.45 0.02 . 1 . . . . . . . . 5800 1 1404 . 1 1 121 121 GLU C C 13 178.68 0.2 . 1 . . . . . . . . 5800 1 1405 . 1 1 121 121 GLU CA C 13 59.56 0.2 . 1 . . . . . . . . 5800 1 1406 . 1 1 121 121 GLU CB C 13 28.51 0.2 . 1 . . . . . . . . 5800 1 1407 . 1 1 121 121 GLU CG C 13 36.63 0.2 . 1 . . . . . . . . 5800 1 1408 . 1 1 121 121 GLU N N 15 118.96 0.2 . 1 . . . . . . . . 5800 1 1409 . 1 1 122 122 ASP H H 1 7.75 0.02 . 1 . . . . . . . . 5800 1 1410 . 1 1 122 122 ASP HA H 1 4.29 0.02 . 1 . . . . . . . . 5800 1 1411 . 1 1 122 122 ASP HB3 H 1 2.80 0.02 . 2 . . . . . . . . 5800 1 1412 . 1 1 122 122 ASP C C 13 179.21 0.2 . 1 . . . . . . . . 5800 1 1413 . 1 1 122 122 ASP CA C 13 57.09 0.2 . 1 . . . . . . . . 5800 1 1414 . 1 1 122 122 ASP CB C 13 41.96 0.2 . 1 . . . . . . . . 5800 1 1415 . 1 1 122 122 ASP N N 15 117.74 0.2 . 1 . . . . . . . . 5800 1 1416 . 1 1 123 123 LEU H H 1 7.81 0.02 . 1 . . . . . . . . 5800 1 1417 . 1 1 123 123 LEU HA H 1 3.82 0.02 . 1 . . . . . . . . 5800 1 1418 . 1 1 123 123 LEU HB2 H 1 1.09 0.02 . 2 . . . . . . . . 5800 1 1419 . 1 1 123 123 LEU HB3 H 1 1.89 0.02 . 2 . . . . . . . . 5800 1 1420 . 1 1 123 123 LEU HG H 1 1.30 0.02 . 1 . . . . . . . . 5800 1 1421 . 1 1 123 123 LEU HD11 H 1 0.73 0.02 . 2 . . . . . . . . 5800 1 1422 . 1 1 123 123 LEU HD12 H 1 0.73 0.02 . 2 . . . . . . . . 5800 1 1423 . 1 1 123 123 LEU HD13 H 1 0.73 0.02 . 2 . . . . . . . . 5800 1 1424 . 1 1 123 123 LEU HD21 H 1 0.61 0.02 . 2 . . . . . . . . 5800 1 1425 . 1 1 123 123 LEU HD22 H 1 0.61 0.02 . 2 . . . . . . . . 5800 1 1426 . 1 1 123 123 LEU HD23 H 1 0.61 0.02 . 2 . . . . . . . . 5800 1 1427 . 1 1 123 123 LEU C C 13 177.09 0.2 . 1 . . . . . . . . 5800 1 1428 . 1 1 123 123 LEU CA C 13 57.90 0.2 . 1 . . . . . . . . 5800 1 1429 . 1 1 123 123 LEU CB C 13 41.20 0.2 . 1 . . . . . . . . 5800 1 1430 . 1 1 123 123 LEU CG C 13 26.63 0.2 . 1 . . . . . . . . 5800 1 1431 . 1 1 123 123 LEU CD1 C 13 23.08 0.2 . 2 . . . . . . . . 5800 1 1432 . 1 1 123 123 LEU CD2 C 13 26.95 0.2 . 2 . . . . . . . . 5800 1 1433 . 1 1 123 123 LEU N N 15 122.18 0.2 . 1 . . . . . . . . 5800 1 1434 . 1 1 124 124 ALA H H 1 8.26 0.02 . 1 . . . . . . . . 5800 1 1435 . 1 1 124 124 ALA HA H 1 3.73 0.02 . 1 . . . . . . . . 5800 1 1436 . 1 1 124 124 ALA HB1 H 1 0.85 0.02 . 1 . . . . . . . . 5800 1 1437 . 1 1 124 124 ALA HB2 H 1 0.85 0.02 . 1 . . . . . . . . 5800 1 1438 . 1 1 124 124 ALA HB3 H 1 0.85 0.02 . 1 . . . . . . . . 5800 1 1439 . 1 1 124 124 ALA C C 13 177.44 0.2 . 1 . . . . . . . . 5800 1 1440 . 1 1 124 124 ALA CA C 13 54.26 0.2 . 1 . . . . . . . . 5800 1 1441 . 1 1 124 124 ALA CB C 13 18.02 0.2 . 1 . . . . . . . . 5800 1 1442 . 1 1 124 124 ALA N N 15 118.25 0.2 . 1 . . . . . . . . 5800 1 1443 . 1 1 125 125 GLU H H 1 7.07 0.02 . 1 . . . . . . . . 5800 1 1444 . 1 1 125 125 GLU HA H 1 4.42 0.02 . 1 . . . . . . . . 5800 1 1445 . 1 1 125 125 GLU HB2 H 1 2.14 0.02 . 2 . . . . . . . . 5800 1 1446 . 1 1 125 125 GLU HB3 H 1 2.36 0.02 . 2 . . . . . . . . 5800 1 1447 . 1 1 125 125 GLU HG2 H 1 2.66 0.02 . 1 . . . . . . . . 5800 1 1448 . 1 1 125 125 GLU HG3 H 1 2.66 0.02 . 1 . . . . . . . . 5800 1 1449 . 1 1 125 125 GLU C C 13 178.19 0.2 . 1 . . . . . . . . 5800 1 1450 . 1 1 125 125 GLU CA C 13 56.13 0.2 . 1 . . . . . . . . 5800 1 1451 . 1 1 125 125 GLU CB C 13 29.82 0.2 . 1 . . . . . . . . 5800 1 1452 . 1 1 125 125 GLU CG C 13 35.91 0.2 . 1 . . . . . . . . 5800 1 1453 . 1 1 125 125 GLU N N 15 111.80 0.2 . 1 . . . . . . . . 5800 1 1454 . 1 1 126 126 GLN H H 1 7.55 0.02 . 1 . . . . . . . . 5800 1 1455 . 1 1 126 126 GLN HA H 1 4.12 0.02 . 1 . . . . . . . . 5800 1 1456 . 1 1 126 126 GLN HB2 H 1 1.97 0.02 . 2 . . . . . . . . 5800 1 1457 . 1 1 126 126 GLN HB3 H 1 2.36 0.02 . 2 . . . . . . . . 5800 1 1458 . 1 1 126 126 GLN HG2 H 1 1.91 0.02 . 2 . . . . . . . . 5800 1 1459 . 1 1 126 126 GLN HG3 H 1 3.16 0.02 . 2 . . . . . . . . 5800 1 1460 . 1 1 126 126 GLN C C 13 174.84 0.2 . 1 . . . . . . . . 5800 1 1461 . 1 1 126 126 GLN CA C 13 55.06 0.2 . 1 . . . . . . . . 5800 1 1462 . 1 1 126 126 GLN CB C 13 29.32 0.2 . 1 . . . . . . . . 5800 1 1463 . 1 1 126 126 GLN CG C 13 34.15 0.2 . 1 . . . . . . . . 5800 1 1464 . 1 1 126 126 GLN N N 15 118.63 0.2 . 1 . . . . . . . . 5800 1 1465 . 1 1 127 127 GLY H H 1 8.83 0.02 . 1 . . . . . . . . 5800 1 1466 . 1 1 127 127 GLY HA2 H 1 3.65 0.02 . 2 . . . . . . . . 5800 1 1467 . 1 1 127 127 GLY HA3 H 1 4.64 0.02 . 2 . . . . . . . . 5800 1 1468 . 1 1 127 127 GLY C C 13 175.89 0.2 . 1 . . . . . . . . 5800 1 1469 . 1 1 127 127 GLY CA C 13 43.33 0.2 . 1 . . . . . . . . 5800 1 1470 . 1 1 127 127 GLY N N 15 105.37 0.2 . 1 . . . . . . . . 5800 1 1471 . 1 1 128 128 ILE H H 1 8.46 0.02 . 1 . . . . . . . . 5800 1 1472 . 1 1 128 128 ILE HA H 1 3.39 0.02 . 1 . . . . . . . . 5800 1 1473 . 1 1 128 128 ILE HB H 1 1.76 0.02 . 1 . . . . . . . . 5800 1 1474 . 1 1 128 128 ILE HG12 H 1 1.03 0.02 . 2 . . . . . . . . 5800 1 1475 . 1 1 128 128 ILE HG13 H 1 1.62 0.02 . 2 . . . . . . . . 5800 1 1476 . 1 1 128 128 ILE HG21 H 1 0.92 0.02 . 1 . . . . . . . . 5800 1 1477 . 1 1 128 128 ILE HG22 H 1 0.92 0.02 . 1 . . . . . . . . 5800 1 1478 . 1 1 128 128 ILE HG23 H 1 0.92 0.02 . 1 . . . . . . . . 5800 1 1479 . 1 1 128 128 ILE HD11 H 1 0.91 0.02 . 1 . . . . . . . . 5800 1 1480 . 1 1 128 128 ILE HD12 H 1 0.91 0.02 . 1 . . . . . . . . 5800 1 1481 . 1 1 128 128 ILE HD13 H 1 0.91 0.02 . 1 . . . . . . . . 5800 1 1482 . 1 1 128 128 ILE C C 13 178.72 0.2 . 1 . . . . . . . . 5800 1 1483 . 1 1 128 128 ILE CA C 13 65.90 0.2 . 1 . . . . . . . . 5800 1 1484 . 1 1 128 128 ILE CB C 13 38.12 0.2 . 1 . . . . . . . . 5800 1 1485 . 1 1 128 128 ILE CG1 C 13 29.00 0.2 . 1 . . . . . . . . 5800 1 1486 . 1 1 128 128 ILE CG2 C 13 17.77 0.2 . 1 . . . . . . . . 5800 1 1487 . 1 1 128 128 ILE CD1 C 13 13.53 0.2 . 1 . . . . . . . . 5800 1 1488 . 1 1 128 128 ILE N N 15 120.55 0.2 . 1 . . . . . . . . 5800 1 1489 . 1 1 129 129 ASP H H 1 8.58 0.02 . 1 . . . . . . . . 5800 1 1490 . 1 1 129 129 ASP HA H 1 4.34 0.02 . 1 . . . . . . . . 5800 1 1491 . 1 1 129 129 ASP HB2 H 1 2.55 0.02 . 2 . . . . . . . . 5800 1 1492 . 1 1 129 129 ASP HB3 H 1 2.66 0.02 . 2 . . . . . . . . 5800 1 1493 . 1 1 129 129 ASP C C 13 178.20 0.2 . 1 . . . . . . . . 5800 1 1494 . 1 1 129 129 ASP CA C 13 56.30 0.2 . 1 . . . . . . . . 5800 1 1495 . 1 1 129 129 ASP CB C 13 39.81 0.2 . 1 . . . . . . . . 5800 1 1496 . 1 1 129 129 ASP N N 15 116.47 0.2 . 1 . . . . . . . . 5800 1 1497 . 1 1 130 130 ASP H H 1 7.47 0.02 . 1 . . . . . . . . 5800 1 1498 . 1 1 130 130 ASP HA H 1 4.51 0.02 . 1 . . . . . . . . 5800 1 1499 . 1 1 130 130 ASP HB2 H 1 2.96 0.02 . 1 . . . . . . . . 5800 1 1500 . 1 1 130 130 ASP HB3 H 1 2.96 0.02 . 1 . . . . . . . . 5800 1 1501 . 1 1 130 130 ASP C C 13 176.80 0.2 . 1 . . . . . . . . 5800 1 1502 . 1 1 130 130 ASP CA C 13 56.71 0.2 . 1 . . . . . . . . 5800 1 1503 . 1 1 130 130 ASP CB C 13 41.83 0.2 . 1 . . . . . . . . 5800 1 1504 . 1 1 130 130 ASP N N 15 117.51 0.2 . 1 . . . . . . . . 5800 1 1505 . 1 1 131 131 LEU H H 1 7.27 0.02 . 1 . . . . . . . . 5800 1 1506 . 1 1 131 131 LEU HA H 1 4.42 0.02 . 1 . . . . . . . . 5800 1 1507 . 1 1 131 131 LEU HB2 H 1 1.63 0.02 . 2 . . . . . . . . 5800 1 1508 . 1 1 131 131 LEU HB3 H 1 1.54 0.02 . 2 . . . . . . . . 5800 1 1509 . 1 1 131 131 LEU HG H 1 1.63 0.02 . 1 . . . . . . . . 5800 1 1510 . 1 1 131 131 LEU HD11 H 1 0.72 0.02 . 2 . . . . . . . . 5800 1 1511 . 1 1 131 131 LEU HD12 H 1 0.72 0.02 . 2 . . . . . . . . 5800 1 1512 . 1 1 131 131 LEU HD13 H 1 0.72 0.02 . 2 . . . . . . . . 5800 1 1513 . 1 1 131 131 LEU HD21 H 1 0.67 0.02 . 2 . . . . . . . . 5800 1 1514 . 1 1 131 131 LEU HD22 H 1 0.67 0.02 . 2 . . . . . . . . 5800 1 1515 . 1 1 131 131 LEU HD23 H 1 0.67 0.02 . 2 . . . . . . . . 5800 1 1516 . 1 1 131 131 LEU C C 13 176.40 0.2 . 1 . . . . . . . . 5800 1 1517 . 1 1 131 131 LEU CA C 13 53.97 0.2 . 1 . . . . . . . . 5800 1 1518 . 1 1 131 131 LEU CB C 13 42.39 0.2 . 1 . . . . . . . . 5800 1 1519 . 1 1 131 131 LEU CG C 13 27.60 0.2 . 1 . . . . . . . . 5800 1 1520 . 1 1 131 131 LEU CD1 C 13 26.21 0.2 . 2 . . . . . . . . 5800 1 1521 . 1 1 131 131 LEU CD2 C 13 23.05 0.2 . 2 . . . . . . . . 5800 1 1522 . 1 1 131 131 LEU N N 15 116.57 0.2 . 1 . . . . . . . . 5800 1 1523 . 1 1 132 132 ALA H H 1 7.27 0.02 . 1 . . . . . . . . 5800 1 1524 . 1 1 132 132 ALA HA H 1 4.08 0.02 . 1 . . . . . . . . 5800 1 1525 . 1 1 132 132 ALA HB1 H 1 1.41 0.02 . 1 . . . . . . . . 5800 1 1526 . 1 1 132 132 ALA HB2 H 1 1.41 0.02 . 1 . . . . . . . . 5800 1 1527 . 1 1 132 132 ALA HB3 H 1 1.41 0.02 . 1 . . . . . . . . 5800 1 1528 . 1 1 132 132 ALA C C 13 177.16 0.2 . 1 . . . . . . . . 5800 1 1529 . 1 1 132 132 ALA CA C 13 54.20 0.2 . 1 . . . . . . . . 5800 1 1530 . 1 1 132 132 ALA CB C 13 19.15 0.2 . 1 . . . . . . . . 5800 1 1531 . 1 1 132 132 ALA N N 15 119.82 0.2 . 1 . . . . . . . . 5800 1 1532 . 1 1 133 133 ASP H H 1 8.35 0.02 . 1 . . . . . . . . 5800 1 1533 . 1 1 133 133 ASP HA H 1 4.47 0.02 . 1 . . . . . . . . 5800 1 1534 . 1 1 133 133 ASP HB2 H 1 2.71 0.02 . 1 . . . . . . . . 5800 1 1535 . 1 1 133 133 ASP HB3 H 1 2.71 0.02 . 1 . . . . . . . . 5800 1 1536 . 1 1 133 133 ASP C C 13 176.23 0.2 . 1 . . . . . . . . 5800 1 1537 . 1 1 133 133 ASP CA C 13 54.13 0.2 . 1 . . . . . . . . 5800 1 1538 . 1 1 133 133 ASP CB C 13 39.93 0.2 . 1 . . . . . . . . 5800 1 1539 . 1 1 133 133 ASP N N 15 114.30 0.2 . 1 . . . . . . . . 5800 1 1540 . 1 1 134 134 ILE H H 1 7.79 0.02 . 1 . . . . . . . . 5800 1 1541 . 1 1 134 134 ILE HA H 1 3.84 0.02 . 1 . . . . . . . . 5800 1 1542 . 1 1 134 134 ILE HB H 1 1.90 0.02 . 1 . . . . . . . . 5800 1 1543 . 1 1 134 134 ILE HG12 H 1 0.92 0.02 . 2 . . . . . . . . 5800 1 1544 . 1 1 134 134 ILE HG13 H 1 1.60 0.02 . 2 . . . . . . . . 5800 1 1545 . 1 1 134 134 ILE HG21 H 1 0.79 0.02 . 1 . . . . . . . . 5800 1 1546 . 1 1 134 134 ILE HG22 H 1 0.79 0.02 . 1 . . . . . . . . 5800 1 1547 . 1 1 134 134 ILE HG23 H 1 0.79 0.02 . 1 . . . . . . . . 5800 1 1548 . 1 1 134 134 ILE HD11 H 1 0.75 0.02 . 1 . . . . . . . . 5800 1 1549 . 1 1 134 134 ILE HD12 H 1 0.75 0.02 . 1 . . . . . . . . 5800 1 1550 . 1 1 134 134 ILE HD13 H 1 0.75 0.02 . 1 . . . . . . . . 5800 1 1551 . 1 1 134 134 ILE C C 13 176.10 0.2 . 1 . . . . . . . . 5800 1 1552 . 1 1 134 134 ILE CA C 13 61.92 0.2 . 1 . . . . . . . . 5800 1 1553 . 1 1 134 134 ILE CB C 13 37.08 0.2 . 1 . . . . . . . . 5800 1 1554 . 1 1 134 134 ILE CG1 C 13 28.35 0.2 . 1 . . . . . . . . 5800 1 1555 . 1 1 134 134 ILE CG2 C 13 17.41 0.2 . 1 . . . . . . . . 5800 1 1556 . 1 1 134 134 ILE CD1 C 13 13.46 0.2 . 1 . . . . . . . . 5800 1 1557 . 1 1 134 134 ILE N N 15 121.88 0.2 . 1 . . . . . . . . 5800 1 1558 . 1 1 135 135 GLU H H 1 8.65 0.02 . 1 . . . . . . . . 5800 1 1559 . 1 1 135 135 GLU HA H 1 3.99 0.02 . 1 . . . . . . . . 5800 1 1560 . 1 1 135 135 GLU HB2 H 1 1.89 0.02 . 2 . . . . . . . . 5800 1 1561 . 1 1 135 135 GLU HB3 H 1 1.97 0.02 . 2 . . . . . . . . 5800 1 1562 . 1 1 135 135 GLU HG2 H 1 2.28 0.02 . 1 . . . . . . . . 5800 1 1563 . 1 1 135 135 GLU HG3 H 1 2.28 0.02 . 1 . . . . . . . . 5800 1 1564 . 1 1 135 135 GLU C C 13 177.02 0.2 . 1 . . . . . . . . 5800 1 1565 . 1 1 135 135 GLU CA C 13 58.38 0.2 . 1 . . . . . . . . 5800 1 1566 . 1 1 135 135 GLU CB C 13 29.36 0.2 . 1 . . . . . . . . 5800 1 1567 . 1 1 135 135 GLU CG C 13 35.93 0.2 . 1 . . . . . . . . 5800 1 1568 . 1 1 135 135 GLU N N 15 106.36 0.2 . 1 . . . . . . . . 5800 1 1569 . 1 1 136 136 GLY H H 1 8.82 0.02 . 1 . . . . . . . . 5800 1 1570 . 1 1 136 136 GLY HA2 H 1 3.67 0.02 . 2 . . . . . . . . 5800 1 1571 . 1 1 136 136 GLY HA3 H 1 4.27 0.02 . 2 . . . . . . . . 5800 1 1572 . 1 1 136 136 GLY C C 13 173.97 0.2 . 1 . . . . . . . . 5800 1 1573 . 1 1 136 136 GLY CA C 13 45.14 0.2 . 1 . . . . . . . . 5800 1 1574 . 1 1 136 136 GLY N N 15 113.49 0.2 . 1 . . . . . . . . 5800 1 1575 . 1 1 137 137 LEU H H 1 7.88 0.02 . 1 . . . . . . . . 5800 1 1576 . 1 1 137 137 LEU HA H 1 4.71 0.02 . 1 . . . . . . . . 5800 1 1577 . 1 1 137 137 LEU HB2 H 1 1.33 0.02 . 2 . . . . . . . . 5800 1 1578 . 1 1 137 137 LEU HB3 H 1 1.89 0.02 . 2 . . . . . . . . 5800 1 1579 . 1 1 137 137 LEU HG H 1 1.63 0.02 . 1 . . . . . . . . 5800 1 1580 . 1 1 137 137 LEU HD11 H 1 0.89 0.02 . 2 . . . . . . . . 5800 1 1581 . 1 1 137 137 LEU HD12 H 1 0.89 0.02 . 2 . . . . . . . . 5800 1 1582 . 1 1 137 137 LEU HD13 H 1 0.89 0.02 . 2 . . . . . . . . 5800 1 1583 . 1 1 137 137 LEU HD21 H 1 0.90 0.02 . 2 . . . . . . . . 5800 1 1584 . 1 1 137 137 LEU HD22 H 1 0.90 0.02 . 2 . . . . . . . . 5800 1 1585 . 1 1 137 137 LEU HD23 H 1 0.90 0.02 . 2 . . . . . . . . 5800 1 1586 . 1 1 137 137 LEU C C 13 175.59 0.2 . 1 . . . . . . . . 5800 1 1587 . 1 1 137 137 LEU CA C 13 53.57 0.2 . 1 . . . . . . . . 5800 1 1588 . 1 1 137 137 LEU CB C 13 43.04 0.2 . 1 . . . . . . . . 5800 1 1589 . 1 1 137 137 LEU CG C 13 29.50 0.2 . 1 . . . . . . . . 5800 1 1590 . 1 1 137 137 LEU CD1 C 13 26.10 0.2 . 2 . . . . . . . . 5800 1 1591 . 1 1 137 137 LEU CD2 C 13 24.80 0.2 . 2 . . . . . . . . 5800 1 1592 . 1 1 137 137 LEU N N 15 122.70 0.2 . 1 . . . . . . . . 5800 1 1593 . 1 1 138 138 THR H H 1 7.42 0.02 . 1 . . . . . . . . 5800 1 1594 . 1 1 138 138 THR HA H 1 4.62 0.02 . 1 . . . . . . . . 5800 1 1595 . 1 1 138 138 THR HB H 1 4.72 0.02 . 1 . . . . . . . . 5800 1 1596 . 1 1 138 138 THR HG21 H 1 1.33 0.02 . 1 . . . . . . . . 5800 1 1597 . 1 1 138 138 THR HG22 H 1 1.33 0.02 . 1 . . . . . . . . 5800 1 1598 . 1 1 138 138 THR HG23 H 1 1.33 0.02 . 1 . . . . . . . . 5800 1 1599 . 1 1 138 138 THR C C 13 174.80 0.2 . 1 . . . . . . . . 5800 1 1600 . 1 1 138 138 THR CA C 13 59.97 0.2 . 1 . . . . . . . . 5800 1 1601 . 1 1 138 138 THR CB C 13 71.67 0.2 . 1 . . . . . . . . 5800 1 1602 . 1 1 138 138 THR N N 15 113.82 0.2 . 1 . . . . . . . . 5800 1 1603 . 1 1 139 139 ASP H H 1 8.94 0.02 . 1 . . . . . . . . 5800 1 1604 . 1 1 139 139 ASP HA H 1 4.25 0.02 . 1 . . . . . . . . 5800 1 1605 . 1 1 139 139 ASP HB2 H 1 2.66 0.02 . 1 . . . . . . . . 5800 1 1606 . 1 1 139 139 ASP HB3 H 1 2.66 0.02 . 1 . . . . . . . . 5800 1 1607 . 1 1 139 139 ASP C C 13 179.09 0.2 . 1 . . . . . . . . 5800 1 1608 . 1 1 139 139 ASP CA C 13 57.44 0.2 . 1 . . . . . . . . 5800 1 1609 . 1 1 139 139 ASP CB C 13 39.44 0.2 . 1 . . . . . . . . 5800 1 1610 . 1 1 139 139 ASP N N 15 121.68 0.2 . 1 . . . . . . . . 5800 1 1611 . 1 1 140 140 GLU H H 1 8.49 0.02 . 1 . . . . . . . . 5800 1 1612 . 1 1 140 140 GLU HA H 1 4.00 0.02 . 1 . . . . . . . . 5800 1 1613 . 1 1 140 140 GLU HB2 H 1 1.93 0.02 . 2 . . . . . . . . 5800 1 1614 . 1 1 140 140 GLU HB3 H 1 2.06 0.02 . 2 . . . . . . . . 5800 1 1615 . 1 1 140 140 GLU HG2 H 1 2.28 0.02 . 1 . . . . . . . . 5800 1 1616 . 1 1 140 140 GLU HG3 H 1 2.28 0.02 . 1 . . . . . . . . 5800 1 1617 . 1 1 140 140 GLU C C 13 179.21 0.2 . 1 . . . . . . . . 5800 1 1618 . 1 1 140 140 GLU CA C 13 59.39 0.2 . 1 . . . . . . . . 5800 1 1619 . 1 1 140 140 GLU CB C 13 29.55 0.2 . 1 . . . . . . . . 5800 1 1620 . 1 1 140 140 GLU CG C 13 36.43 0.2 . 1 . . . . . . . . 5800 1 1621 . 1 1 140 140 GLU N N 15 119.93 0.2 . 1 . . . . . . . . 5800 1 1622 . 1 1 141 141 LYS H H 1 7.83 0.02 . 1 . . . . . . . . 5800 1 1623 . 1 1 141 141 LYS HA H 1 4.14 0.02 . 1 . . . . . . . . 5800 1 1624 . 1 1 141 141 LYS HB2 H 1 1.84 0.02 . 1 . . . . . . . . 5800 1 1625 . 1 1 141 141 LYS HB3 H 1 1.84 0.02 . 1 . . . . . . . . 5800 1 1626 . 1 1 141 141 LYS HG2 H 1 1.36 0.02 . 2 . . . . . . . . 5800 1 1627 . 1 1 141 141 LYS HG3 H 1 1.51 0.02 . 2 . . . . . . . . 5800 1 1628 . 1 1 141 141 LYS HD2 H 1 1.79 0.02 . 1 . . . . . . . . 5800 1 1629 . 1 1 141 141 LYS HD3 H 1 1.79 0.02 . 1 . . . . . . . . 5800 1 1630 . 1 1 141 141 LYS HE2 H 1 2.88 0.02 . 2 . . . . . . . . 5800 1 1631 . 1 1 141 141 LYS HE3 H 1 2.95 0.02 . 2 . . . . . . . . 5800 1 1632 . 1 1 141 141 LYS C C 13 178.34 0.2 . 1 . . . . . . . . 5800 1 1633 . 1 1 141 141 LYS CA C 13 58.94 0.2 . 1 . . . . . . . . 5800 1 1634 . 1 1 141 141 LYS CB C 13 32.63 0.2 . 1 . . . . . . . . 5800 1 1635 . 1 1 141 141 LYS CG C 13 25.78 0.2 . 1 . . . . . . . . 5800 1 1636 . 1 1 141 141 LYS CD C 13 29.24 0.2 . 1 . . . . . . . . 5800 1 1637 . 1 1 141 141 LYS CE C 13 42.46 0.2 . 1 . . . . . . . . 5800 1 1638 . 1 1 141 141 LYS N N 15 121.74 0.2 . 1 . . . . . . . . 5800 1 1639 . 1 1 142 142 ALA H H 1 8.88 0.02 . 1 . . . . . . . . 5800 1 1640 . 1 1 142 142 ALA HA H 1 3.82 0.02 . 1 . . . . . . . . 5800 1 1641 . 1 1 142 142 ALA HB1 H 1 1.48 0.02 . 1 . . . . . . . . 5800 1 1642 . 1 1 142 142 ALA HB2 H 1 1.48 0.02 . 1 . . . . . . . . 5800 1 1643 . 1 1 142 142 ALA HB3 H 1 1.48 0.02 . 1 . . . . . . . . 5800 1 1644 . 1 1 142 142 ALA C C 13 179.10 0.2 . 1 . . . . . . . . 5800 1 1645 . 1 1 142 142 ALA CA C 13 55.74 0.2 . 1 . . . . . . . . 5800 1 1646 . 1 1 142 142 ALA CB C 13 18.65 0.2 . 1 . . . . . . . . 5800 1 1647 . 1 1 142 142 ALA N N 15 121.41 0.2 . 1 . . . . . . . . 5800 1 1648 . 1 1 143 143 GLY H H 1 8.25 0.02 . 1 . . . . . . . . 5800 1 1649 . 1 1 143 143 GLY HA2 H 1 3.63 0.02 . 2 . . . . . . . . 5800 1 1650 . 1 1 143 143 GLY HA3 H 1 3.90 0.02 . 2 . . . . . . . . 5800 1 1651 . 1 1 143 143 GLY C C 13 175.83 0.2 . 1 . . . . . . . . 5800 1 1652 . 1 1 143 143 GLY CA C 13 47.35 0.2 . 1 . . . . . . . . 5800 1 1653 . 1 1 143 143 GLY N N 15 126.41 0.2 . 1 . . . . . . . . 5800 1 1654 . 1 1 144 144 ALA H H 1 7.68 0.02 . 1 . . . . . . . . 5800 1 1655 . 1 1 144 144 ALA HA H 1 4.13 0.02 . 1 . . . . . . . . 5800 1 1656 . 1 1 144 144 ALA HB1 H 1 1.50 0.02 . 1 . . . . . . . . 5800 1 1657 . 1 1 144 144 ALA HB2 H 1 1.50 0.02 . 1 . . . . . . . . 5800 1 1658 . 1 1 144 144 ALA HB3 H 1 1.50 0.02 . 1 . . . . . . . . 5800 1 1659 . 1 1 144 144 ALA C C 13 181.15 0.2 . 1 . . . . . . . . 5800 1 1660 . 1 1 144 144 ALA CA C 13 55.06 0.2 . 1 . . . . . . . . 5800 1 1661 . 1 1 144 144 ALA CB C 13 18.16 0.2 . 1 . . . . . . . . 5800 1 1662 . 1 1 144 144 ALA N N 15 123.90 0.2 . 1 . . . . . . . . 5800 1 1663 . 1 1 145 145 LEU H H 1 8.26 0.02 . 1 . . . . . . . . 5800 1 1664 . 1 1 145 145 LEU HA H 1 4.04 0.02 . 1 . . . . . . . . 5800 1 1665 . 1 1 145 145 LEU HB2 H 1 1.27 0.02 . 2 . . . . . . . . 5800 1 1666 . 1 1 145 145 LEU HB3 H 1 1.96 0.02 . 2 . . . . . . . . 5800 1 1667 . 1 1 145 145 LEU HG H 1 1.91 0.02 . 1 . . . . . . . . 5800 1 1668 . 1 1 145 145 LEU HD11 H 1 0.72 0.02 . 1 . . . . . . . . 5800 1 1669 . 1 1 145 145 LEU HD12 H 1 0.72 0.02 . 1 . . . . . . . . 5800 1 1670 . 1 1 145 145 LEU HD13 H 1 0.72 0.02 . 1 . . . . . . . . 5800 1 1671 . 1 1 145 145 LEU HD21 H 1 0.72 0.02 . 1 . . . . . . . . 5800 1 1672 . 1 1 145 145 LEU HD22 H 1 0.72 0.02 . 1 . . . . . . . . 5800 1 1673 . 1 1 145 145 LEU HD23 H 1 0.72 0.02 . 1 . . . . . . . . 5800 1 1674 . 1 1 145 145 LEU C C 13 178.22 0.2 . 1 . . . . . . . . 5800 1 1675 . 1 1 145 145 LEU CA C 13 57.85 0.2 . 1 . . . . . . . . 5800 1 1676 . 1 1 145 145 LEU CB C 13 42.34 0.2 . 1 . . . . . . . . 5800 1 1677 . 1 1 145 145 LEU CG C 13 26.14 0.2 . 1 . . . . . . . . 5800 1 1678 . 1 1 145 145 LEU CD1 C 13 26.34 0.2 . 2 . . . . . . . . 5800 1 1679 . 1 1 145 145 LEU CD2 C 13 23.05 0.2 . 2 . . . . . . . . 5800 1 1680 . 1 1 145 145 LEU N N 15 120.76 0.2 . 1 . . . . . . . . 5800 1 1681 . 1 1 146 146 ILE H H 1 7.95 0.02 . 1 . . . . . . . . 5800 1 1682 . 1 1 146 146 ILE HA H 1 3.22 0.02 . 1 . . . . . . . . 5800 1 1683 . 1 1 146 146 ILE HB H 1 1.57 0.02 . 1 . . . . . . . . 5800 1 1684 . 1 1 146 146 ILE HG12 H 1 1.00 0.02 . 2 . . . . . . . . 5800 1 1685 . 1 1 146 146 ILE HG13 H 1 1.54 0.02 . 2 . . . . . . . . 5800 1 1686 . 1 1 146 146 ILE HG21 H 1 0.83 0.02 . 1 . . . . . . . . 5800 1 1687 . 1 1 146 146 ILE HG22 H 1 0.83 0.02 . 1 . . . . . . . . 5800 1 1688 . 1 1 146 146 ILE HG23 H 1 0.83 0.02 . 1 . . . . . . . . 5800 1 1689 . 1 1 146 146 ILE HD11 H 1 0.53 0.02 . 1 . . . . . . . . 5800 1 1690 . 1 1 146 146 ILE HD12 H 1 0.53 0.02 . 1 . . . . . . . . 5800 1 1691 . 1 1 146 146 ILE HD13 H 1 0.53 0.02 . 1 . . . . . . . . 5800 1 1692 . 1 1 146 146 ILE C C 13 178.60 0.2 . 1 . . . . . . . . 5800 1 1693 . 1 1 146 146 ILE CA C 13 66.17 0.2 . 1 . . . . . . . . 5800 1 1694 . 1 1 146 146 ILE CB C 13 39.28 0.2 . 1 . . . . . . . . 5800 1 1695 . 1 1 146 146 ILE CG1 C 13 28.70 0.2 . 1 . . . . . . . . 5800 1 1696 . 1 1 146 146 ILE CG2 C 13 16.55 0.2 . 1 . . . . . . . . 5800 1 1697 . 1 1 146 146 ILE CD1 C 13 14.03 0.2 . 1 . . . . . . . . 5800 1 1698 . 1 1 146 146 ILE N N 15 119.31 0.2 . 1 . . . . . . . . 5800 1 1699 . 1 1 147 147 MET H H 1 7.99 0.02 . 1 . . . . . . . . 5800 1 1700 . 1 1 147 147 MET HA H 1 4.08 0.02 . 1 . . . . . . . . 5800 1 1701 . 1 1 147 147 MET HB2 H 1 2.14 0.02 . 2 . . . . . . . . 5800 1 1702 . 1 1 147 147 MET HB3 H 1 2.06 0.02 . 2 . . . . . . . . 5800 1 1703 . 1 1 147 147 MET HG2 H 1 2.67 0.02 . 1 . . . . . . . . 5800 1 1704 . 1 1 147 147 MET HG3 H 1 2.67 0.02 . 1 . . . . . . . . 5800 1 1705 . 1 1 147 147 MET C C 13 178.61 0.2 . 1 . . . . . . . . 5800 1 1706 . 1 1 147 147 MET CA C 13 58.38 0.2 . 1 . . . . . . . . 5800 1 1707 . 1 1 147 147 MET CB C 13 31.42 0.2 . 1 . . . . . . . . 5800 1 1708 . 1 1 147 147 MET CG C 13 32.07 0.2 . 1 . . . . . . . . 5800 1 1709 . 1 1 147 147 MET N N 15 116.36 0.2 . 1 . . . . . . . . 5800 1 1710 . 1 1 148 148 ALA H H 1 8.12 0.02 . 1 . . . . . . . . 5800 1 1711 . 1 1 148 148 ALA HA H 1 4.23 0.02 . 1 . . . . . . . . 5800 1 1712 . 1 1 148 148 ALA HB1 H 1 1.54 0.02 . 1 . . . . . . . . 5800 1 1713 . 1 1 148 148 ALA HB2 H 1 1.54 0.02 . 1 . . . . . . . . 5800 1 1714 . 1 1 148 148 ALA HB3 H 1 1.54 0.02 . 1 . . . . . . . . 5800 1 1715 . 1 1 148 148 ALA C C 13 180.59 0.2 . 1 . . . . . . . . 5800 1 1716 . 1 1 148 148 ALA CA C 13 55.18 0.2 . 1 . . . . . . . . 5800 1 1717 . 1 1 148 148 ALA CB C 13 21.58 0.2 . 1 . . . . . . . . 5800 1 1718 . 1 1 148 148 ALA N N 15 122.63 0.2 . 1 . . . . . . . . 5800 1 1719 . 1 1 149 149 ALA H H 1 8.15 0.02 . 1 . . . . . . . . 5800 1 1720 . 1 1 149 149 ALA HA H 1 3.94 0.02 . 1 . . . . . . . . 5800 1 1721 . 1 1 149 149 ALA HB1 H 1 1.42 0.02 . 1 . . . . . . . . 5800 1 1722 . 1 1 149 149 ALA HB2 H 1 1.42 0.02 . 1 . . . . . . . . 5800 1 1723 . 1 1 149 149 ALA HB3 H 1 1.42 0.02 . 1 . . . . . . . . 5800 1 1724 . 1 1 149 149 ALA C C 13 179.84 0.2 . 1 . . . . . . . . 5800 1 1725 . 1 1 149 149 ALA CA C 13 55.26 0.2 . 1 . . . . . . . . 5800 1 1726 . 1 1 149 149 ALA CB C 13 17.76 0.2 . 1 . . . . . . . . 5800 1 1727 . 1 1 149 149 ALA N N 15 120.24 0.2 . 1 . . . . . . . . 5800 1 1728 . 1 1 150 150 ARG H H 1 8.42 0.02 . 1 . . . . . . . . 5800 1 1729 . 1 1 150 150 ARG HA H 1 3.00 0.02 . 1 . . . . . . . . 5800 1 1730 . 1 1 150 150 ARG HB2 H 1 1.41 0.02 . 2 . . . . . . . . 5800 1 1731 . 1 1 150 150 ARG HB3 H 1 1.74 0.02 . 2 . . . . . . . . 5800 1 1732 . 1 1 150 150 ARG HG2 H 1 0.03 0.02 . 2 . . . . . . . . 5800 1 1733 . 1 1 150 150 ARG HG3 H 1 1.54 0.02 . 2 . . . . . . . . 5800 1 1734 . 1 1 150 150 ARG HD2 H 1 2.83 0.02 . 1 . . . . . . . . 5800 1 1735 . 1 1 150 150 ARG HD3 H 1 2.83 0.02 . 1 . . . . . . . . 5800 1 1736 . 1 1 150 150 ARG C C 13 178.29 0.2 . 1 . . . . . . . . 5800 1 1737 . 1 1 150 150 ARG CA C 13 60.26 0.2 . 1 . . . . . . . . 5800 1 1738 . 1 1 150 150 ARG CB C 13 29.83 0.2 . 1 . . . . . . . . 5800 1 1739 . 1 1 150 150 ARG CG C 13 28.19 0.2 . 1 . . . . . . . . 5800 1 1740 . 1 1 150 150 ARG CD C 13 43.69 0.2 . 1 . . . . . . . . 5800 1 1741 . 1 1 150 150 ARG N N 15 118.79 0.2 . 1 . . . . . . . . 5800 1 1742 . 1 1 151 151 ASN H H 1 8.33 0.02 . 1 . . . . . . . . 5800 1 1743 . 1 1 151 151 ASN HA H 1 4.59 0.02 . 1 . . . . . . . . 5800 1 1744 . 1 1 151 151 ASN HB2 H 1 2.92 0.02 . 1 . . . . . . . . 5800 1 1745 . 1 1 151 151 ASN HB3 H 1 2.92 0.02 . 1 . . . . . . . . 5800 1 1746 . 1 1 151 151 ASN C C 13 176.84 0.2 . 1 . . . . . . . . 5800 1 1747 . 1 1 151 151 ASN CA C 13 56.12 0.2 . 1 . . . . . . . . 5800 1 1748 . 1 1 151 151 ASN CB C 13 38.01 0.2 . 1 . . . . . . . . 5800 1 1749 . 1 1 151 151 ASN N N 15 117.91 0.2 . 1 . . . . . . . . 5800 1 1750 . 1 1 152 152 ILE H H 1 7.32 0.02 . 1 . . . . . . . . 5800 1 1751 . 1 1 152 152 ILE HA H 1 3.91 0.02 . 1 . . . . . . . . 5800 1 1752 . 1 1 152 152 ILE HB H 1 1.77 0.02 . 1 . . . . . . . . 5800 1 1753 . 1 1 152 152 ILE HG12 H 1 1.10 0.02 . 2 . . . . . . . . 5800 1 1754 . 1 1 152 152 ILE HG13 H 1 1.71 0.02 . 2 . . . . . . . . 5800 1 1755 . 1 1 152 152 ILE HG21 H 1 0.91 0.02 . 1 . . . . . . . . 5800 1 1756 . 1 1 152 152 ILE HG22 H 1 0.91 0.02 . 1 . . . . . . . . 5800 1 1757 . 1 1 152 152 ILE HG23 H 1 0.91 0.02 . 1 . . . . . . . . 5800 1 1758 . 1 1 152 152 ILE HD11 H 1 0.83 0.02 . 1 . . . . . . . . 5800 1 1759 . 1 1 152 152 ILE HD12 H 1 0.83 0.02 . 1 . . . . . . . . 5800 1 1760 . 1 1 152 152 ILE HD13 H 1 0.83 0.02 . 1 . . . . . . . . 5800 1 1761 . 1 1 152 152 ILE C C 13 178.09 0.2 . 1 . . . . . . . . 5800 1 1762 . 1 1 152 152 ILE CA C 13 64.08 0.2 . 1 . . . . . . . . 5800 1 1763 . 1 1 152 152 ILE CB C 13 39.41 0.2 . 1 . . . . . . . . 5800 1 1764 . 1 1 152 152 ILE CG1 C 13 29.24 0.2 . 1 . . . . . . . . 5800 1 1765 . 1 1 152 152 ILE CG2 C 13 17.56 0.2 . 1 . . . . . . . . 5800 1 1766 . 1 1 152 152 ILE CD1 C 13 13.75 0.2 . 1 . . . . . . . . 5800 1 1767 . 1 1 152 152 ILE N N 15 117.62 0.2 . 1 . . . . . . . . 5800 1 1768 . 1 1 153 153 CYS H H 1 8.34 0.02 . 1 . . . . . . . . 5800 1 1769 . 1 1 153 153 CYS HA H 1 4.32 0.02 . 1 . . . . . . . . 5800 1 1770 . 1 1 153 153 CYS HB2 H 1 2.49 0.02 . 2 . . . . . . . . 5800 1 1771 . 1 1 153 153 CYS HB3 H 1 2.94 0.02 . 2 . . . . . . . . 5800 1 1772 . 1 1 153 153 CYS C C 13 175.85 0.2 . 1 . . . . . . . . 5800 1 1773 . 1 1 153 153 CYS CA C 13 62.06 0.2 . 1 . . . . . . . . 5800 1 1774 . 1 1 153 153 CYS CB C 13 28.61 0.2 . 1 . . . . . . . . 5800 1 1775 . 1 1 153 153 CYS N N 15 115.43 0.2 . 1 . . . . . . . . 5800 1 1776 . 1 1 154 154 TRP H H 1 8.60 0.02 . 1 . . . . . . . . 5800 1 1777 . 1 1 154 154 TRP HA H 1 4.98 0.02 . 1 . . . . . . . . 5800 1 1778 . 1 1 154 154 TRP HB2 H 1 2.79 0.02 . 2 . . . . . . . . 5800 1 1779 . 1 1 154 154 TRP HB3 H 1 2.96 0.02 . 2 . . . . . . . . 5800 1 1780 . 1 1 154 154 TRP HD1 H 1 6.82 0.02 . 1 . . . . . . . . 5800 1 1781 . 1 1 154 154 TRP HE1 H 1 10.35 0.02 . 1 . . . . . . . . 5800 1 1782 . 1 1 154 154 TRP HE3 H 1 7.42 0.02 . 1 . . . . . . . . 5800 1 1783 . 1 1 154 154 TRP HZ2 H 1 7.30 0.02 . 1 . . . . . . . . 5800 1 1784 . 1 1 154 154 TRP HZ3 H 1 7.05 0.02 . 1 . . . . . . . . 5800 1 1785 . 1 1 154 154 TRP HH2 H 1 7.14 0.02 . 1 . . . . . . . . 5800 1 1786 . 1 1 154 154 TRP C C 13 176.97 0.2 . 1 . . . . . . . . 5800 1 1787 . 1 1 154 154 TRP CA C 13 55.84 0.2 . 1 . . . . . . . . 5800 1 1788 . 1 1 154 154 TRP CB C 13 29.43 0.2 . 1 . . . . . . . . 5800 1 1789 . 1 1 154 154 TRP N N 15 119.21 0.2 . 1 . . . . . . . . 5800 1 1790 . 1 1 154 154 TRP NE1 N 15 127.82 0.2 . 1 . . . . . . . . 5800 1 1791 . 1 1 155 155 PHE H H 1 7.59 0.02 . 1 . . . . . . . . 5800 1 1792 . 1 1 155 155 PHE HA H 1 4.94 0.02 . 1 . . . . . . . . 5800 1 1793 . 1 1 155 155 PHE HB2 H 1 3.13 0.02 . 2 . . . . . . . . 5800 1 1794 . 1 1 155 155 PHE HB3 H 1 3.43 0.02 . 2 . . . . . . . . 5800 1 1795 . 1 1 155 155 PHE HD1 H 1 7.36 0.02 . 1 . . . . . . . . 5800 1 1796 . 1 1 155 155 PHE HD2 H 1 7.36 0.02 . 1 . . . . . . . . 5800 1 1797 . 1 1 155 155 PHE HE1 H 1 7.43 0.02 . 1 . . . . . . . . 5800 1 1798 . 1 1 155 155 PHE HE2 H 1 7.43 0.02 . 1 . . . . . . . . 5800 1 1799 . 1 1 155 155 PHE C C 13 176.47 0.2 . 1 . . . . . . . . 5800 1 1800 . 1 1 155 155 PHE CA C 13 57.02 0.2 . 1 . . . . . . . . 5800 1 1801 . 1 1 155 155 PHE CB C 13 39.39 0.2 . 1 . . . . . . . . 5800 1 1802 . 1 1 155 155 PHE N N 15 118.32 0.2 . 1 . . . . . . . . 5800 1 1803 . 1 1 156 156 GLY H H 1 8.07 0.02 . 1 . . . . . . . . 5800 1 1804 . 1 1 156 156 GLY HA2 H 1 3.66 0.02 . 2 . . . . . . . . 5800 1 1805 . 1 1 156 156 GLY HA3 H 1 4.03 0.02 . 2 . . . . . . . . 5800 1 1806 . 1 1 156 156 GLY C C 13 174.10 0.2 . 1 . . . . . . . . 5800 1 1807 . 1 1 156 156 GLY CA C 13 45.82 0.2 . 1 . . . . . . . . 5800 1 1808 . 1 1 156 156 GLY N N 15 109.74 0.2 . 1 . . . . . . . . 5800 1 1809 . 1 1 157 157 ASP H H 1 8.30 0.02 . 1 . . . . . . . . 5800 1 1810 . 1 1 157 157 ASP HA H 1 4.64 0.02 . 1 . . . . . . . . 5800 1 1811 . 1 1 157 157 ASP HB2 H 1 2.57 0.02 . 2 . . . . . . . . 5800 1 1812 . 1 1 157 157 ASP HB3 H 1 2.74 0.02 . 2 . . . . . . . . 5800 1 1813 . 1 1 157 157 ASP CA C 13 54.39 0.2 . 1 . . . . . . . . 5800 1 1814 . 1 1 157 157 ASP CB C 13 41.29 0.2 . 1 . . . . . . . . 5800 1 1815 . 1 1 157 157 ASP N N 15 120.38 0.2 . 1 . . . . . . . . 5800 1 1816 . 1 1 158 158 GLU H H 1 8.31 0.02 . 1 . . . . . . . . 5800 1 1817 . 1 1 158 158 GLU HA H 1 4.29 0.02 . 1 . . . . . . . . 5800 1 1818 . 1 1 158 158 GLU HB2 H 1 1.93 0.02 . 2 . . . . . . . . 5800 1 1819 . 1 1 158 158 GLU HB3 H 1 2.10 0.02 . 2 . . . . . . . . 5800 1 1820 . 1 1 158 158 GLU HG2 H 1 2.28 0.02 . 1 . . . . . . . . 5800 1 1821 . 1 1 158 158 GLU HG3 H 1 2.28 0.02 . 1 . . . . . . . . 5800 1 1822 . 1 1 158 158 GLU C C 13 175.34 0.2 . 1 . . . . . . . . 5800 1 1823 . 1 1 158 158 GLU CA C 13 56.51 0.2 . 1 . . . . . . . . 5800 1 1824 . 1 1 158 158 GLU CB C 13 30.68 0.2 . 1 . . . . . . . . 5800 1 1825 . 1 1 158 158 GLU CG C 13 36.44 0.2 . 1 . . . . . . . . 5800 1 1826 . 1 1 158 158 GLU N N 15 120.93 0.2 . 1 . . . . . . . . 5800 1 stop_ save_