data_4154 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4154 _Entry.Title ; 13C and Stereospecific 13C and 1H Resonance Assignments for Oxidized Putidaredoxin ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1998-06-28 _Entry.Accession_date 1998-06-28 _Entry.Last_release_date . _Entry.Original_release_date . _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 Nitin Jain . . . 4154 2 Teresa Lyons . . . 4154 3 Thomas Pochapsky . C. . 4154 4 Miklos Kuti . . . 4154 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4154 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 376 4154 '15N chemical shifts' 96 4154 '1H chemical shifts' 625 4154 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 . . 1999-09-28 . update author 'chemical shift values updated' 4154 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4154 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 99218076 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Pochapsky, T. C., Jain, N. U., Kuti, M., Lyons, T. A., and Heymont, J., "A Refined Model for the Solution Structure of Oxidized Putidaredoxin", Biochemistry, 38, 4681-4690 (1999). ; _Citation.Title 'A Refined Model for the Solution Structure of Oxidized Putidaredoxin' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 38 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 4681 _Citation.Page_last 4690 _Citation.Year 1999 _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 Thomas Pochapsky . C. . 4154 1 2 Nitin Jain . U. . 4154 1 3 Teresa Lyons . . . 4154 1 4 Miklos Kuti . . . 4154 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID adrenodoxin 4154 1 'cytochrome P450' 4154 1 ferredoxin 4154 1 stop_ save_ save_citation_one _Citation.Sf_category citations _Citation.Sf_framecode citation_one _Citation.Entry_ID 4154 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 1536837 _Citation.Full_citation ; Ye, X. M., Pochapsky, T. C. and Pochapsky, S. S., "1H NMR Sequential Assignments and Identification of Secondary Structural Elements in Oxidized Putidaredoxin, an Electron-transfer Protein from Pseudomonas," Biochemistry 31, 1961-1968 (1992) ; _Citation.Title '1H NMR sequential assignments and identification of secondary structural elements in oxidized putidaredoxin, an electron-transfer protein from Pseudomonas.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 31 _Citation.Journal_issue 7 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-2960 _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 1961 _Citation.Page_last 1968 _Citation.Year 1992 _Citation.Details ; Sequential 1H resonance assignments and secondary structural features of putidaredoxin (Pdx), a 106-residue globular protein consisting of a single polypeptide chain and a [2Fe-2S] cluster, are reported. No crystal structure has been obtained for Pdx or for any closely homologous protein. The sequentially assigned resonances represent ca. 83% of all the protons in Pdx and a large majority of those protons which are unaffected by the paramagnetism of the iron-sulfur cluster. A total of three alpha-helices, two beta-sheets, and two type I beta-turns have been identified from NOE (nuclear Overhauser effect) patterns. Besides the extensive beta-sheet described previously, a second sheet is identified, consisting of two short antiparallel strands (Ile 89-Thr 91 and Val 21-Leu 23), one of which ends in a tight type I turn (Thr 91-Pro 92-Glu 93-Leu 94). One short helix (Ala 26-Gly 31) and a second longer helical region (Glu 54-Cys 73) are present. This second helical region is discontinuous, breaking at Pro 61, resuming at Glu 65, and ending at Cys 73. The functionally important C-terminal tryptophan residue has been identified, and some structural constraints on this residue are described. Previously reported functional data concerning Pdx are discussed in light of present structural information. Finally, approaches to the determination of a high-resolution solution structure of the protein are discussed. ; 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 'X M' Ye X. M. . 4154 2 2 'T C' Pochapsky T. C. . 4154 2 3 'S S' Pochapsky S. S. . 4154 2 stop_ save_ save_citation_two _Citation.Sf_category citations _Citation.Sf_framecode citation_two _Citation.Entry_ID 4154 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8845752 _Citation.Full_citation ; Lyons, T. A., Ratnaswamy, G. and Pochapsky, T. C., "Redox-dependent Dynamics of Putidaredoxin Characterized by Amide Proton Exchange," Protein Sci. 5, 627-639 (1996). ; _Citation.Title 'Redox-dependent dynamics of putidaredoxin characterized by amide proton exchange.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Sci.' _Citation.Journal_name_full 'Protein science : a publication of the Protein Society' _Citation.Journal_volume 5 _Citation.Journal_issue 4 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0961-8368 _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 627 _Citation.Page_last 639 _Citation.Year 1996 _Citation.Details ; Multidimensional NMR methods were used to obtain 1H-15N correlations and 15N resonance assignments for amide and side-chain nitrogens of oxidized and reduced putidaredoxin (Pdx), the Fe2S2 ferredoxin, which acts as the physiological reductant of cytochrome P-450cam (CYP101). A model for the solution structure of oxidized Pdx has been determined recently using NMR methods (Pochapsky TC, Ye XM, Ratnaswamy G, Lyons TA, 1994, Biochemistry 33:6424-6432) and redox-dependent 1H NMR spectral features have been described (Pochapsky TC, Ratnaswamy G, Patera A, 1994, Biochemistry 33:6433-6441). 15N assignments were made with NOESY-(1H/15N) HMQC and TOCSY-(1H/15N) HSQC spectra obtained using samples of Pdx uniformly labeled with 15N. Local dynamics in both oxidation states of Pdx were then characterized by comparison of residue-specific amide proton exchange rates, which were measured by a combination of saturation transfer and H2O/D2O exchange methods at pH 6.4 and 7.4 (uncorrected for isotope effects). In general, where exchange rates for a given site exhibit significant oxidation-state dependence, the oxidized protein exchanges more rapidly than the reduced protein. The largest dependence of exchange rate upon oxidation state is found for residues near the metal center and in a region of compact structure that includes the loop-turn Val 74-Ser 82 and the C-terminal residues (Pro 102-Trp 106). The significance of these findings is discussed in light of the considerable dependence of the binding interaction between Pdx and CYP101 upon the oxidation state of Pdx. ; 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 A' Lyons T. A. . 4154 3 2 G Ratnaswamy G. . . 4154 3 3 'T C' Pochapsky T. C. . 4154 3 stop_ save_ save_citation_three _Citation.Sf_category citations _Citation.Sf_framecode citation_three _Citation.Entry_ID 4154 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8589602 _Citation.Full_citation ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995). ; _Citation.Title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 6 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0925-2738 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 135 _Citation.Page_last 140 _Citation.Year 1995 _Citation.Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; 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 'D S' Wishart D. S. . 4154 4 2 'C G' Bigam C. G. . 4154 4 3 J Yao J. . . 4154 4 4 F Abildgaard F. . . 4154 4 5 'H J' Dyson H. J. . 4154 4 6 E Oldfield E. . . 4154 4 7 'J L' Markley J. L. . 4154 4 8 'B D' Sykes B. D. . 4154 4 stop_ save_ save_citation_four _Citation.Sf_category citations _Citation.Sf_framecode citation_four _Citation.Entry_ID 4154 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; "Recommendations for Presentations of NMR Structures of Proteins and Nucleic Acids," IUPAC/IUB Draft version. ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_Pdxo _Assembly.Sf_category assembly _Assembly.Sf_framecode system_Pdxo _Assembly.Entry_ID 4154 _Assembly.ID 1 _Assembly.Name 'oxidized putidaredoxin' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic yes _Assembly.Thiol_state . _Assembly.Molecular_mass 12600 _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 4154 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 Pdxo 1 $Pdxo . . . native . . . . . 4154 1 2 2Fe2S 2 $FES . . . native . . . . . 4154 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'oxidized putidaredoxin' system 4154 1 Pdxo abbreviation 4154 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'Electron transfer to cytochrome P450cam' 4154 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Pdxo _Entity.Sf_category entity _Entity.Sf_framecode Pdxo _Entity.Entry_ID 4154 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name putidaredoxin _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 ; SKVVYVSHDGTRRELDVADG VSLMQAAVSNGIYDIVGDCG GSASCATCHVYVNEAFTDKV PAANEREIGMLECVTAELKP NSRLCCQIIMTPELDGIVVD VPDRQW ; _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 106 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 1551 . "P450 reductase" . . . . . 100.00 106 99.06 100.00 2.24e-70 . . . . 4154 1 2 no BMRB 2278 . putidaredoxin . . . . . 100.00 106 99.06 100.00 2.24e-70 . . . . 4154 1 3 no BMRB 4149 . putidaredoxin . . . . . 100.00 106 99.06 99.06 7.86e-70 . . . . 4154 1 4 no PDB 1GPX . "C85s Gapdx, Nmr, 20 Structures" . . . . . 100.00 106 99.06 99.06 7.86e-70 . . . . 4154 1 5 no PDB 1OQQ . "Crystal Structure Of C73sC85S MUTANT OF PUTIDAREDOXIN, A [2FE-2s] Ferredoxin From Pseudomonas Putida, At 1.47a Resolution" . . . . . 100.00 106 98.11 98.11 8.21e-69 . . . . 4154 1 6 no PDB 1OQR . "Crystal Structure Of C73s Mutant Of Putidaredoxin, A [2fe- 2s] Ferredoxin From Pseudomonas Putida, At 1.65a Resolution" . . . . . 100.00 106 99.06 99.06 7.86e-70 . . . . 4154 1 7 no PDB 1PDX . Putidaredoxin . . . . . 100.00 106 100.00 100.00 8.49e-71 . . . . 4154 1 8 no PDB 1PUT . "An Nmr-Derived Model For The Solution Structure Of Oxidized Putidaredoxin, A 2fe, 2-S Ferredoxin From Pseudomonas" . . . . . 100.00 106 99.06 100.00 2.24e-70 . . . . 4154 1 9 no PDB 1R7S . "Putidaredoxin (Fe2s2 Ferredoxin), C73g Mutant" . . . . . 100.00 106 99.06 99.06 2.29e-69 . . . . 4154 1 10 no PDB 1XLN . "Crystal Structure Of Oxidized C73sC85S PUTIDAREDOXIN, A [2fe-2s] Ferredoxin From Pseudomonas Putida" . . . . . 100.00 106 98.11 98.11 8.21e-69 . . . . 4154 1 11 no PDB 1XLO . "Structure Of Reduced C73s/c85s Putidaredoxin, A [2fe-2s] Ferredoxin From Pseudomonas Putida" . . . . . 100.00 106 98.11 98.11 8.21e-69 . . . . 4154 1 12 no PDB 1XLP . "Structure Of Oxidized C73s Putidaredoxin From Pseudomonas Putida" . . . . . 100.00 106 99.06 99.06 7.86e-70 . . . . 4154 1 13 no PDB 1XLQ . "Crystal Structure Of Reduced C73s Putidaredoxin From Pseudomonas Putida" . . . . . 100.00 106 99.06 99.06 7.86e-70 . . . . 4154 1 14 no PDB 1YJI . "Rdc-Refined Solution Nmr Structure Of Reduced Putidaredoxin" . . . . . 100.00 106 100.00 100.00 8.49e-71 . . . . 4154 1 15 no PDB 1YJJ . "Rdc-Refined Solution Nmr Structure Of Oxidized Putidaredoxin" . . . . . 100.00 106 100.00 100.00 8.49e-71 . . . . 4154 1 16 no PDB 2M56 . "The Structure Of The Complex Of Cytochrome P450cam And Its Electron Donor Putidaredoxin Determined By Paramagnetic Nmr Spectros" . . . . . 100.00 106 99.06 99.06 7.86e-70 . . . . 4154 1 17 no PDB 3LB8 . "Crystal Structure Of The Covalent Putidaredoxin Reductase- Putidaredoxin Complex" . . . . . 100.00 106 98.11 98.11 8.21e-69 . . . . 4154 1 18 no PDB 3W9C . "Crystal Structure Of The Electron Transfer Complex Of Cytochrome P450cam With Putidaredoxin" . . . . . 100.00 108 99.06 99.06 1.05e-69 . . . . 4154 1 19 no PDB 4JWS . "Crystal Structure Of Cytochrome P450cam-putidaredoxin Complex" . . . . . 100.00 112 100.00 100.00 8.32e-71 . . . . 4154 1 20 no PDB 4JWU . "Crystal Structure Of Cytochrome P450cam-putidaredoxin Complex" . . . . . 100.00 113 98.11 98.11 3.39e-68 . . . . 4154 1 21 no PDB 4JX1 . "Crystal Structure Of Reduced Cytochrome P450cam-putidaredoxin Complex Bound To Camphor And 5-exo-hydroxycamphor" . . . . . 100.00 113 98.11 98.11 3.39e-68 . . . . 4154 1 22 no DBJ BAA00414 . "putidaredoxin [Pseudomonas putida]" . . . . . 100.00 107 100.00 100.00 8.48e-71 . . . . 4154 1 23 no DBJ BAN13288 . "putidaredoxin [Pseudomonas putida]" . . . . . 100.00 107 100.00 100.00 8.48e-71 . . . . 4154 1 24 no GB AAA25759 . "putidaredoxin [Pseudomonas putida]" . . . . . 100.00 107 100.00 100.00 8.48e-71 . . . . 4154 1 25 no REF WP_032492635 . "putidaredoxin [Pseudomonas putida]" . . . . . 100.00 107 100.00 100.00 8.48e-71 . . . . 4154 1 26 no REF YP_009083114 . "putidaredoxin [Pseudomonas putida]" . . . . . 100.00 107 100.00 100.00 8.48e-71 . . . . 4154 1 27 no SP P00259 . "RecName: Full=Putidaredoxin; Short=PDX" . . . . . 100.00 107 100.00 100.00 8.48e-71 . . . . 4154 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID Pdxo abbreviation 4154 1 putidaredoxin common 4154 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 . SER . 4154 1 2 . LYS . 4154 1 3 . VAL . 4154 1 4 . VAL . 4154 1 5 . TYR . 4154 1 6 . VAL . 4154 1 7 . SER . 4154 1 8 . HIS . 4154 1 9 . ASP . 4154 1 10 . GLY . 4154 1 11 . THR . 4154 1 12 . ARG . 4154 1 13 . ARG . 4154 1 14 . GLU . 4154 1 15 . LEU . 4154 1 16 . ASP . 4154 1 17 . VAL . 4154 1 18 . ALA . 4154 1 19 . ASP . 4154 1 20 . GLY . 4154 1 21 . VAL . 4154 1 22 . SER . 4154 1 23 . LEU . 4154 1 24 . MET . 4154 1 25 . GLN . 4154 1 26 . ALA . 4154 1 27 . ALA . 4154 1 28 . VAL . 4154 1 29 . SER . 4154 1 30 . ASN . 4154 1 31 . GLY . 4154 1 32 . ILE . 4154 1 33 . TYR . 4154 1 34 . ASP . 4154 1 35 . ILE . 4154 1 36 . VAL . 4154 1 37 . GLY . 4154 1 38 . ASP . 4154 1 39 . CYS . 4154 1 40 . GLY . 4154 1 41 . GLY . 4154 1 42 . SER . 4154 1 43 . ALA . 4154 1 44 . SER . 4154 1 45 . CYS . 4154 1 46 . ALA . 4154 1 47 . THR . 4154 1 48 . CYS . 4154 1 49 . HIS . 4154 1 50 . VAL . 4154 1 51 . TYR . 4154 1 52 . VAL . 4154 1 53 . ASN . 4154 1 54 . GLU . 4154 1 55 . ALA . 4154 1 56 . PHE . 4154 1 57 . THR . 4154 1 58 . ASP . 4154 1 59 . LYS . 4154 1 60 . VAL . 4154 1 61 . PRO . 4154 1 62 . ALA . 4154 1 63 . ALA . 4154 1 64 . ASN . 4154 1 65 . GLU . 4154 1 66 . ARG . 4154 1 67 . GLU . 4154 1 68 . ILE . 4154 1 69 . GLY . 4154 1 70 . MET . 4154 1 71 . LEU . 4154 1 72 . GLU . 4154 1 73 . CYS . 4154 1 74 . VAL . 4154 1 75 . THR . 4154 1 76 . ALA . 4154 1 77 . GLU . 4154 1 78 . LEU . 4154 1 79 . LYS . 4154 1 80 . PRO . 4154 1 81 . ASN . 4154 1 82 . SER . 4154 1 83 . ARG . 4154 1 84 . LEU . 4154 1 85 . CYS . 4154 1 86 . CYS . 4154 1 87 . GLN . 4154 1 88 . ILE . 4154 1 89 . ILE . 4154 1 90 . MET . 4154 1 91 . THR . 4154 1 92 . PRO . 4154 1 93 . GLU . 4154 1 94 . LEU . 4154 1 95 . ASP . 4154 1 96 . GLY . 4154 1 97 . ILE . 4154 1 98 . VAL . 4154 1 99 . VAL . 4154 1 100 . ASP . 4154 1 101 . VAL . 4154 1 102 . PRO . 4154 1 103 . ASP . 4154 1 104 . ARG . 4154 1 105 . GLN . 4154 1 106 . TRP . 4154 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 . SER 1 1 4154 1 . LYS 2 2 4154 1 . VAL 3 3 4154 1 . VAL 4 4 4154 1 . TYR 5 5 4154 1 . VAL 6 6 4154 1 . SER 7 7 4154 1 . HIS 8 8 4154 1 . ASP 9 9 4154 1 . GLY 10 10 4154 1 . THR 11 11 4154 1 . ARG 12 12 4154 1 . ARG 13 13 4154 1 . GLU 14 14 4154 1 . LEU 15 15 4154 1 . ASP 16 16 4154 1 . VAL 17 17 4154 1 . ALA 18 18 4154 1 . ASP 19 19 4154 1 . GLY 20 20 4154 1 . VAL 21 21 4154 1 . SER 22 22 4154 1 . LEU 23 23 4154 1 . MET 24 24 4154 1 . GLN 25 25 4154 1 . ALA 26 26 4154 1 . ALA 27 27 4154 1 . VAL 28 28 4154 1 . SER 29 29 4154 1 . ASN 30 30 4154 1 . GLY 31 31 4154 1 . ILE 32 32 4154 1 . TYR 33 33 4154 1 . ASP 34 34 4154 1 . ILE 35 35 4154 1 . VAL 36 36 4154 1 . GLY 37 37 4154 1 . ASP 38 38 4154 1 . CYS 39 39 4154 1 . GLY 40 40 4154 1 . GLY 41 41 4154 1 . SER 42 42 4154 1 . ALA 43 43 4154 1 . SER 44 44 4154 1 . CYS 45 45 4154 1 . ALA 46 46 4154 1 . THR 47 47 4154 1 . CYS 48 48 4154 1 . HIS 49 49 4154 1 . VAL 50 50 4154 1 . TYR 51 51 4154 1 . VAL 52 52 4154 1 . ASN 53 53 4154 1 . GLU 54 54 4154 1 . ALA 55 55 4154 1 . PHE 56 56 4154 1 . THR 57 57 4154 1 . ASP 58 58 4154 1 . LYS 59 59 4154 1 . VAL 60 60 4154 1 . PRO 61 61 4154 1 . ALA 62 62 4154 1 . ALA 63 63 4154 1 . ASN 64 64 4154 1 . GLU 65 65 4154 1 . ARG 66 66 4154 1 . GLU 67 67 4154 1 . ILE 68 68 4154 1 . GLY 69 69 4154 1 . MET 70 70 4154 1 . LEU 71 71 4154 1 . GLU 72 72 4154 1 . CYS 73 73 4154 1 . VAL 74 74 4154 1 . THR 75 75 4154 1 . ALA 76 76 4154 1 . GLU 77 77 4154 1 . LEU 78 78 4154 1 . LYS 79 79 4154 1 . PRO 80 80 4154 1 . ASN 81 81 4154 1 . SER 82 82 4154 1 . ARG 83 83 4154 1 . LEU 84 84 4154 1 . CYS 85 85 4154 1 . CYS 86 86 4154 1 . GLN 87 87 4154 1 . ILE 88 88 4154 1 . ILE 89 89 4154 1 . MET 90 90 4154 1 . THR 91 91 4154 1 . PRO 92 92 4154 1 . GLU 93 93 4154 1 . LEU 94 94 4154 1 . ASP 95 95 4154 1 . GLY 96 96 4154 1 . ILE 97 97 4154 1 . VAL 98 98 4154 1 . VAL 99 99 4154 1 . ASP 100 100 4154 1 . VAL 101 101 4154 1 . PRO 102 102 4154 1 . ASP 103 103 4154 1 . ARG 104 104 4154 1 . GLN 105 105 4154 1 . TRP 106 106 4154 1 stop_ save_ save_FES _Entity.Sf_category entity _Entity.Sf_framecode FES _Entity.Entry_ID 4154 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name FES _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer . _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID FES _Entity.Nonpolymer_comp_label $chem_comp_FES _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 2 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . 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 . FES . 4154 2 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 4154 _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 $Pdxo . 303 organism . 'Pseudomonas putida' 'Pseudomonas putida' . . Eubacteria . Pseudomonas putida . . . . . . . . . . . . . . . . . . . . . 4154 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 4154 _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 $Pdxo . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4154 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_FES _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_FES _Chem_comp.Entry_ID 4154 _Chem_comp.ID FES _Chem_comp.Provenance . _Chem_comp.Name 'FE2/S2 (INORGANIC) CLUSTER' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code FES _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code FES _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula 'Fe2 S2' _Chem_comp.Formula_weight 175.820 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code 1CZP _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Jun 14 11:26:54 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID [Fe]1S[Fe]S1 SMILES ACDLabs 10.04 4154 FES InChI=1S/2Fe.2S InChI InChI 1.03 4154 FES NIXDOXVAJZFRNF-UHFFFAOYSA-N InChIKey InChI 1.03 4154 FES S1[Fe]S[Fe]1 SMILES CACTVS 3.341 4154 FES S1[Fe]S[Fe]1 SMILES 'OpenEye OEToolkits' 1.5.0 4154 FES S1[Fe]S[Fe]1 SMILES_CANONICAL CACTVS 3.341 4154 FES S1[Fe]S[Fe]1 SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 4154 FES stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID 1,3-dithia-2$l^{2},4$l^{2}-diferracyclobutane 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 4154 FES di-mu-sulfidediiron 'SYSTEMATIC NAME' ACDLabs 10.04 4154 FES stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID FE1 . FE1 . . FE . . N 0 . . . . no no . . . . 16.237 . 5.409 . 27.398 . 0.000 -0.213 -1.531 1 . 4154 FES FE2 . FE2 . . FE . . N 0 . . . . no no . . . . 16.361 . 2.666 . 27.488 . 0.000 -0.213 1.531 2 . 4154 FES S1 . S1 . . S . . N 0 . . . . no no . . . . 17.422 . 4.079 . 28.829 . 1.461 0.372 0.000 3 . 4154 FES S2 . S2 . . S . . N 0 . . . . no no . . . . 15.380 . 3.919 . 25.972 . -1.461 0.372 0.000 4 . 4154 FES stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING FE1 S1 no N 1 . 4154 FES 2 . SING FE1 S2 no N 2 . 4154 FES 3 . SING FE2 S1 no N 3 . 4154 FES 4 . SING FE2 S2 no N 4 . 4154 FES stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 4154 _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 putidaredoxin '[U-13C, U-15N]' . . 1 $Pdxo . . 1 . . mM . . . . 4154 1 2 deutero-trisbuffer . . . . . . . . . . . . . . . 4154 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_one _Sample_condition_list.Entry_ID 4154 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 7.4 0.2 na 4154 1 temperature 290 0.2 K 4154 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 4154 _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 HNCA . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . 1 $NMR_spectrometer_one . . . . . . . . . . . . . . . . 4154 1 2 HNCO . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . 1 $NMR_spectrometer_one . . . . . . . . . . . . . . . . 4154 1 3 HCCH-TOCSY . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . 1 $NMR_spectrometer_one . . . . . . . . . . . . . . . . 4154 1 4 '1H-13C HSQC' . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions_one . . . 1 $NMR_spectrometer_one . . . . . . . . . . . . . . . . 4154 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 4154 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name HNCA _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 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer_one _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 4154 _NMR_spec_expt.ID 2 _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 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer_one _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 4154 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name HCCH-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 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer_one _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 4154 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name '1H-13C HSQC' _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 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer_one _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_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_one _Chem_shift_reference.Entry_ID 4154 _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 0.00 . indirect 0.251449530 . . . 4 $citation_three . . . . 4154 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 . direct 1.0 . . . 4 $citation_three . . . . 4154 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 . indirect 0.101329118 . . . 5 $citation_four . . . . 4154 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_assigned_chemical_shifts_one _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chemical_shifts_one _Assigned_chem_shift_list.Entry_ID 4154 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_one _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_one . 4154 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 1 1 SER HA H 1 3.88 0.02 . 1 . . . . . . . . 4154 1 2 . 1 1 1 1 SER HB2 H 1 3.57 0.02 . 1 . . . . . . . . 4154 1 3 . 1 1 1 1 SER HB3 H 1 3.40 0.02 . 1 . . . . . . . . 4154 1 4 . 1 1 1 1 SER C C 13 169.3 0.1 . 1 . . . . . . . . 4154 1 5 . 1 1 1 1 SER CA C 13 58.3 0.1 . 1 . . . . . . . . 4154 1 6 . 1 1 1 1 SER CB C 13 63.7 0.1 . 1 . . . . . . . . 4154 1 7 . 1 1 2 2 LYS H H 1 9.15 0.02 . 1 . . . . . . . . 4154 1 8 . 1 1 2 2 LYS HA H 1 4.58 0.02 . 1 . . . . . . . . 4154 1 9 . 1 1 2 2 LYS HB2 H 1 1.56 0.02 . 1 . . . . . . . . 4154 1 10 . 1 1 2 2 LYS HB3 H 1 1.25 0.02 . 1 . . . . . . . . 4154 1 11 . 1 1 2 2 LYS HG2 H 1 1.12 0.02 . 2 . . . . . . . . 4154 1 12 . 1 1 2 2 LYS HG3 H 1 1.00 0.02 . 2 . . . . . . . . 4154 1 13 . 1 1 2 2 LYS HD2 H 1 1.25 0.02 . 2 . . . . . . . . 4154 1 14 . 1 1 2 2 LYS HD3 H 1 1.35 0.02 . 2 . . . . . . . . 4154 1 15 . 1 1 2 2 LYS HE2 H 1 2.65 0.02 . 2 . . . . . . . . 4154 1 16 . 1 1 2 2 LYS HE3 H 1 2.63 0.02 . 2 . . . . . . . . 4154 1 17 . 1 1 2 2 LYS C C 13 175.0 0.1 . 1 . . . . . . . . 4154 1 18 . 1 1 2 2 LYS CA C 13 56.8 0.1 . 1 . . . . . . . . 4154 1 19 . 1 1 2 2 LYS CB C 13 33.0 0.1 . 1 . . . . . . . . 4154 1 20 . 1 1 2 2 LYS CG C 13 24.3 0.1 . 1 . . . . . . . . 4154 1 21 . 1 1 2 2 LYS CD C 13 28.3 0.1 . 1 . . . . . . . . 4154 1 22 . 1 1 2 2 LYS CE C 13 41.2 0.1 . 1 . . . . . . . . 4154 1 23 . 1 1 2 2 LYS N N 15 128.4 0.1 . 1 . . . . . . . . 4154 1 24 . 1 1 3 3 VAL H H 1 8.48 0.02 . 1 . . . . . . . . 4154 1 25 . 1 1 3 3 VAL HA H 1 4.18 0.02 . 1 . . . . . . . . 4154 1 26 . 1 1 3 3 VAL HB H 1 1.38 0.02 . 1 . . . . . . . . 4154 1 27 . 1 1 3 3 VAL HG11 H 1 0.05 0.02 . 1 . . . . . . . . 4154 1 28 . 1 1 3 3 VAL HG12 H 1 0.05 0.02 . 1 . . . . . . . . 4154 1 29 . 1 1 3 3 VAL HG13 H 1 0.05 0.02 . 1 . . . . . . . . 4154 1 30 . 1 1 3 3 VAL HG21 H 1 0.45 0.02 . 1 . . . . . . . . 4154 1 31 . 1 1 3 3 VAL HG22 H 1 0.45 0.02 . 1 . . . . . . . . 4154 1 32 . 1 1 3 3 VAL HG23 H 1 0.45 0.02 . 1 . . . . . . . . 4154 1 33 . 1 1 3 3 VAL C C 13 173.5 0.1 . 1 . . . . . . . . 4154 1 34 . 1 1 3 3 VAL CA C 13 60.0 0.1 . 1 . . . . . . . . 4154 1 35 . 1 1 3 3 VAL CB C 13 34.9 0.1 . 1 . . . . . . . . 4154 1 36 . 1 1 3 3 VAL CG1 C 13 20.4 0.1 . 1 . . . . . . . . 4154 1 37 . 1 1 3 3 VAL CG2 C 13 22.5 0.1 . 1 . . . . . . . . 4154 1 38 . 1 1 3 3 VAL N N 15 124.3 0.1 . 1 . . . . . . . . 4154 1 39 . 1 1 4 4 VAL H H 1 8.50 0.02 . 1 . . . . . . . . 4154 1 40 . 1 1 4 4 VAL HA H 1 4.40 0.02 . 1 . . . . . . . . 4154 1 41 . 1 1 4 4 VAL HB H 1 1.78 0.02 . 1 . . . . . . . . 4154 1 42 . 1 1 4 4 VAL HG11 H 1 0.53 0.02 . 1 . . . . . . . . 4154 1 43 . 1 1 4 4 VAL HG12 H 1 0.53 0.02 . 1 . . . . . . . . 4154 1 44 . 1 1 4 4 VAL HG13 H 1 0.53 0.02 . 1 . . . . . . . . 4154 1 45 . 1 1 4 4 VAL HG21 H 1 0.50 0.02 . 1 . . . . . . . . 4154 1 46 . 1 1 4 4 VAL HG22 H 1 0.50 0.02 . 1 . . . . . . . . 4154 1 47 . 1 1 4 4 VAL HG23 H 1 0.50 0.02 . 1 . . . . . . . . 4154 1 48 . 1 1 4 4 VAL C C 13 173.6 0.1 . 1 . . . . . . . . 4154 1 49 . 1 1 4 4 VAL CA C 13 60.5 0.1 . 1 . . . . . . . . 4154 1 50 . 1 1 4 4 VAL CB C 13 32.8 0.1 . 1 . . . . . . . . 4154 1 51 . 1 1 4 4 VAL CG1 C 13 21.0 0.1 . 1 . . . . . . . . 4154 1 52 . 1 1 4 4 VAL CG2 C 13 20.0 0.1 . 1 . . . . . . . . 4154 1 53 . 1 1 4 4 VAL N N 15 126.8 0.1 . 1 . . . . . . . . 4154 1 54 . 1 1 5 5 TYR H H 1 8.84 0.02 . 1 . . . . . . . . 4154 1 55 . 1 1 5 5 TYR HA H 1 4.72 0.02 . 1 . . . . . . . . 4154 1 56 . 1 1 5 5 TYR HB2 H 1 2.23 0.02 . 1 . . . . . . . . 4154 1 57 . 1 1 5 5 TYR HB3 H 1 2.72 0.02 . 1 . . . . . . . . 4154 1 58 . 1 1 5 5 TYR HD1 H 1 6.48 0.02 . 1 . . . . . . . . 4154 1 59 . 1 1 5 5 TYR HD2 H 1 6.48 0.02 . 1 . . . . . . . . 4154 1 60 . 1 1 5 5 TYR HE1 H 1 6.05 0.02 . 1 . . . . . . . . 4154 1 61 . 1 1 5 5 TYR HE2 H 1 6.05 0.02 . 1 . . . . . . . . 4154 1 62 . 1 1 5 5 TYR HH H 1 8.02 0.02 . 1 . . . . . . . . 4154 1 63 . 1 1 5 5 TYR C C 13 176.4 0.1 . 1 . . . . . . . . 4154 1 64 . 1 1 5 5 TYR CA C 13 55.2 0.1 . 1 . . . . . . . . 4154 1 65 . 1 1 5 5 TYR CB C 13 39.2 0.1 . 1 . . . . . . . . 4154 1 66 . 1 1 5 5 TYR CD1 C 13 133.1 0.1 . 1 . . . . . . . . 4154 1 67 . 1 1 5 5 TYR CD2 C 13 133.1 0.1 . 1 . . . . . . . . 4154 1 68 . 1 1 5 5 TYR CE1 C 13 117.7 0.1 . 1 . . . . . . . . 4154 1 69 . 1 1 5 5 TYR CE2 C 13 117.7 0.1 . 1 . . . . . . . . 4154 1 70 . 1 1 5 5 TYR N N 15 125.3 0.1 . 1 . . . . . . . . 4154 1 71 . 1 1 6 6 VAL H H 1 9.50 0.02 . 1 . . . . . . . . 4154 1 72 . 1 1 6 6 VAL HA H 1 4.68 0.02 . 1 . . . . . . . . 4154 1 73 . 1 1 6 6 VAL HB H 1 2.18 0.02 . 1 . . . . . . . . 4154 1 74 . 1 1 6 6 VAL HG11 H 1 0.72 0.02 . 1 . . . . . . . . 4154 1 75 . 1 1 6 6 VAL HG12 H 1 0.72 0.02 . 1 . . . . . . . . 4154 1 76 . 1 1 6 6 VAL HG13 H 1 0.72 0.02 . 1 . . . . . . . . 4154 1 77 . 1 1 6 6 VAL HG21 H 1 0.56 0.02 . 1 . . . . . . . . 4154 1 78 . 1 1 6 6 VAL HG22 H 1 0.56 0.02 . 1 . . . . . . . . 4154 1 79 . 1 1 6 6 VAL HG23 H 1 0.56 0.02 . 1 . . . . . . . . 4154 1 80 . 1 1 6 6 VAL C C 13 176.6 0.1 . 1 . . . . . . . . 4154 1 81 . 1 1 6 6 VAL CA C 13 61.7 0.1 . 1 . . . . . . . . 4154 1 82 . 1 1 6 6 VAL CB C 13 31.2 0.1 . 1 . . . . . . . . 4154 1 83 . 1 1 6 6 VAL CG1 C 13 20.8 0.1 . 1 . . . . . . . . 4154 1 84 . 1 1 6 6 VAL CG2 C 13 21.5 0.1 . 1 . . . . . . . . 4154 1 85 . 1 1 6 6 VAL N N 15 130.2 0.1 . 1 . . . . . . . . 4154 1 86 . 1 1 7 7 SER H H 1 8.95 0.02 . 1 . . . . . . . . 4154 1 87 . 1 1 7 7 SER HA H 1 4.31 0.02 . 1 . . . . . . . . 4154 1 88 . 1 1 7 7 SER HB2 H 1 3.78 0.02 . 2 . . . . . . . . 4154 1 89 . 1 1 7 7 SER HB3 H 1 3.68 0.02 . 2 . . . . . . . . 4154 1 90 . 1 1 7 7 SER C C 13 175.3 0.1 . 1 . . . . . . . . 4154 1 91 . 1 1 7 7 SER CA C 13 59.2 0.1 . 1 . . . . . . . . 4154 1 92 . 1 1 7 7 SER CB C 13 64.2 0.1 . 1 . . . . . . . . 4154 1 93 . 1 1 7 7 SER N N 15 124.2 0.1 . 1 . . . . . . . . 4154 1 94 . 1 1 8 8 HIS HA H 1 4.23 0.02 . 1 . . . . . . . . 4154 1 95 . 1 1 8 8 HIS HB2 H 1 3.10 0.02 . 2 . . . . . . . . 4154 1 96 . 1 1 8 8 HIS HB3 H 1 2.90 0.02 . 2 . . . . . . . . 4154 1 97 . 1 1 8 8 HIS HD1 H 1 9.45 0.02 . 1 . . . . . . . . 4154 1 98 . 1 1 8 8 HIS HD2 H 1 7.15 0.02 . 1 . . . . . . . . 4154 1 99 . 1 1 8 8 HIS HE1 H 1 7.92 0.02 . 1 . . . . . . . . 4154 1 100 . 1 1 8 8 HIS C C 13 175.1 0.1 . 1 . . . . . . . . 4154 1 101 . 1 1 8 8 HIS CA C 13 58.8 0.1 . 1 . . . . . . . . 4154 1 102 . 1 1 8 8 HIS CB C 13 29.6 0.1 . 1 . . . . . . . . 4154 1 103 . 1 1 8 8 HIS CD2 C 13 125.9 0.1 . 1 . . . . . . . . 4154 1 104 . 1 1 8 8 HIS CE1 C 13 138.0 0.1 . 1 . . . . . . . . 4154 1 105 . 1 1 8 8 HIS ND1 N 15 126.0 0.1 . 1 . . . . . . . . 4154 1 106 . 1 1 8 8 HIS NE2 N 15 187.0 0.1 . 1 . . . . . . . . 4154 1 107 . 1 1 9 9 ASP H H 1 7.41 0.02 . 1 . . . . . . . . 4154 1 108 . 1 1 9 9 ASP HA H 1 4.18 0.02 . 1 . . . . . . . . 4154 1 109 . 1 1 9 9 ASP HB2 H 1 2.09 0.02 . 1 . . . . . . . . 4154 1 110 . 1 1 9 9 ASP HB3 H 1 2.75 0.02 . 1 . . . . . . . . 4154 1 111 . 1 1 9 9 ASP C C 13 176.6 0.1 . 1 . . . . . . . . 4154 1 112 . 1 1 9 9 ASP CA C 13 52.5 0.1 . 1 . . . . . . . . 4154 1 113 . 1 1 9 9 ASP CB C 13 39.4 0.1 . 1 . . . . . . . . 4154 1 114 . 1 1 9 9 ASP N N 15 116.7 0.1 . 1 . . . . . . . . 4154 1 115 . 1 1 10 10 GLY H H 1 7.99 0.02 . 1 . . . . . . . . 4154 1 116 . 1 1 10 10 GLY HA2 H 1 4.05 0.02 . 2 . . . . . . . . 4154 1 117 . 1 1 10 10 GLY HA3 H 1 3.27 0.02 . 2 . . . . . . . . 4154 1 118 . 1 1 10 10 GLY C C 13 173.7 0.1 . 1 . . . . . . . . 4154 1 119 . 1 1 10 10 GLY CA C 13 44.6 0.1 . 1 . . . . . . . . 4154 1 120 . 1 1 10 10 GLY N N 15 109.7 0.1 . 1 . . . . . . . . 4154 1 121 . 1 1 11 11 THR H H 1 7.81 0.02 . 1 . . . . . . . . 4154 1 122 . 1 1 11 11 THR HA H 1 3.78 0.02 . 1 . . . . . . . . 4154 1 123 . 1 1 11 11 THR HB H 1 3.94 0.02 . 1 . . . . . . . . 4154 1 124 . 1 1 11 11 THR HG21 H 1 0.95 0.02 . 1 . . . . . . . . 4154 1 125 . 1 1 11 11 THR HG22 H 1 0.95 0.02 . 1 . . . . . . . . 4154 1 126 . 1 1 11 11 THR HG23 H 1 0.95 0.02 . 1 . . . . . . . . 4154 1 127 . 1 1 11 11 THR C C 13 173.1 0.1 . 1 . . . . . . . . 4154 1 128 . 1 1 11 11 THR CA C 13 64.2 0.1 . 1 . . . . . . . . 4154 1 129 . 1 1 11 11 THR CB C 13 68.2 0.1 . 1 . . . . . . . . 4154 1 130 . 1 1 11 11 THR CG2 C 13 21.3 0.1 . 1 . . . . . . . . 4154 1 131 . 1 1 11 11 THR N N 15 119.6 0.1 . 1 . . . . . . . . 4154 1 132 . 1 1 12 12 ARG H H 1 8.72 0.02 . 1 . . . . . . . . 4154 1 133 . 1 1 12 12 ARG HA H 1 4.58 0.02 . 1 . . . . . . . . 4154 1 134 . 1 1 12 12 ARG HB2 H 1 1.46 0.02 . 1 . . . . . . . . 4154 1 135 . 1 1 12 12 ARG HB3 H 1 1.53 0.02 . 1 . . . . . . . . 4154 1 136 . 1 1 12 12 ARG HG2 H 1 1.17 0.02 . 2 . . . . . . . . 4154 1 137 . 1 1 12 12 ARG HG3 H 1 1.50 0.02 . 2 . . . . . . . . 4154 1 138 . 1 1 12 12 ARG HD2 H 1 2.89 0.02 . 2 . . . . . . . . 4154 1 139 . 1 1 12 12 ARG HD3 H 1 3.12 0.02 . 2 . . . . . . . . 4154 1 140 . 1 1 12 12 ARG HE H 1 7.29 0.02 . 1 . . . . . . . . 4154 1 141 . 1 1 12 12 ARG C C 13 175.4 0.1 . 1 . . . . . . . . 4154 1 142 . 1 1 12 12 ARG CA C 13 55.5 0.1 . 1 . . . . . . . . 4154 1 143 . 1 1 12 12 ARG CB C 13 32.1 0.1 . 1 . . . . . . . . 4154 1 144 . 1 1 12 12 ARG CG C 13 28.2 0.1 . 1 . . . . . . . . 4154 1 145 . 1 1 12 12 ARG CD C 13 43.2 0.1 . 1 . . . . . . . . 4154 1 146 . 1 1 12 12 ARG N N 15 128.0 0.1 . 1 . . . . . . . . 4154 1 147 . 1 1 12 12 ARG NE N 15 86.1 0.1 . 1 . . . . . . . . 4154 1 148 . 1 1 13 13 ARG H H 1 8.49 0.02 . 1 . . . . . . . . 4154 1 149 . 1 1 13 13 ARG HA H 1 4.45 0.02 . 1 . . . . . . . . 4154 1 150 . 1 1 13 13 ARG HB2 H 1 1.66 0.02 . 1 . . . . . . . . 4154 1 151 . 1 1 13 13 ARG HB3 H 1 1.66 0.02 . 1 . . . . . . . . 4154 1 152 . 1 1 13 13 ARG HG2 H 1 1.30 0.02 . 2 . . . . . . . . 4154 1 153 . 1 1 13 13 ARG HG3 H 1 1.51 0.02 . 2 . . . . . . . . 4154 1 154 . 1 1 13 13 ARG HD2 H 1 2.97 0.02 . 2 . . . . . . . . 4154 1 155 . 1 1 13 13 ARG HD3 H 1 3.02 0.02 . 2 . . . . . . . . 4154 1 156 . 1 1 13 13 ARG HE H 1 6.74 0.02 . 1 . . . . . . . . 4154 1 157 . 1 1 13 13 ARG HH11 H 1 6.23 0.02 . 1 . . . . . . . . 4154 1 158 . 1 1 13 13 ARG HH12 H 1 6.23 0.02 . 1 . . . . . . . . 4154 1 159 . 1 1 13 13 ARG HH21 H 1 7.20 0.02 . 1 . . . . . . . . 4154 1 160 . 1 1 13 13 ARG HH22 H 1 7.20 0.02 . 1 . . . . . . . . 4154 1 161 . 1 1 13 13 ARG C C 13 173.4 0.1 . 1 . . . . . . . . 4154 1 162 . 1 1 13 13 ARG CA C 13 54.6 0.1 . 1 . . . . . . . . 4154 1 163 . 1 1 13 13 ARG CB C 13 32.4 0.1 . 1 . . . . . . . . 4154 1 164 . 1 1 13 13 ARG CG C 13 26.6 0.1 . 1 . . . . . . . . 4154 1 165 . 1 1 13 13 ARG CD C 13 43.2 0.1 . 1 . . . . . . . . 4154 1 166 . 1 1 13 13 ARG N N 15 123.2 0.1 . 1 . . . . . . . . 4154 1 167 . 1 1 13 13 ARG NE N 15 86.4 0.1 . 1 . . . . . . . . 4154 1 168 . 1 1 14 14 GLU H H 1 8.55 0.02 . 1 . . . . . . . . 4154 1 169 . 1 1 14 14 GLU HA H 1 5.10 0.02 . 1 . . . . . . . . 4154 1 170 . 1 1 14 14 GLU HB2 H 1 1.65 0.02 . 1 . . . . . . . . 4154 1 171 . 1 1 14 14 GLU HB3 H 1 1.68 0.02 . 1 . . . . . . . . 4154 1 172 . 1 1 14 14 GLU HG2 H 1 1.82 0.02 . 2 . . . . . . . . 4154 1 173 . 1 1 14 14 GLU HG3 H 1 1.97 0.02 . 2 . . . . . . . . 4154 1 174 . 1 1 14 14 GLU C C 13 175.3 0.1 . 1 . . . . . . . . 4154 1 175 . 1 1 14 14 GLU CA C 13 54.5 0.1 . 1 . . . . . . . . 4154 1 176 . 1 1 14 14 GLU CB C 13 31.8 0.1 . 1 . . . . . . . . 4154 1 177 . 1 1 14 14 GLU CG C 13 36.6 0.1 . 1 . . . . . . . . 4154 1 178 . 1 1 14 14 GLU N N 15 125.0 0.1 . 1 . . . . . . . . 4154 1 179 . 1 1 15 15 LEU H H 1 9.19 0.02 . 1 . . . . . . . . 4154 1 180 . 1 1 15 15 LEU HA H 1 4.54 0.02 . 1 . . . . . . . . 4154 1 181 . 1 1 15 15 LEU HB2 H 1 1.31 0.02 . 1 . . . . . . . . 4154 1 182 . 1 1 15 15 LEU HB3 H 1 1.23 0.02 . 1 . . . . . . . . 4154 1 183 . 1 1 15 15 LEU HG H 1 1.31 0.02 . 1 . . . . . . . . 4154 1 184 . 1 1 15 15 LEU HD11 H 1 0.52 0.02 . 1 . . . . . . . . 4154 1 185 . 1 1 15 15 LEU HD12 H 1 0.52 0.02 . 1 . . . . . . . . 4154 1 186 . 1 1 15 15 LEU HD13 H 1 0.52 0.02 . 1 . . . . . . . . 4154 1 187 . 1 1 15 15 LEU HD21 H 1 0.61 0.02 . 1 . . . . . . . . 4154 1 188 . 1 1 15 15 LEU HD22 H 1 0.61 0.02 . 1 . . . . . . . . 4154 1 189 . 1 1 15 15 LEU HD23 H 1 0.61 0.02 . 1 . . . . . . . . 4154 1 190 . 1 1 15 15 LEU C C 13 174.4 0.1 . 1 . . . . . . . . 4154 1 191 . 1 1 15 15 LEU CA C 13 53.0 0.1 . 1 . . . . . . . . 4154 1 192 . 1 1 15 15 LEU CB C 13 46.1 0.1 . 1 . . . . . . . . 4154 1 193 . 1 1 15 15 LEU CG C 13 26.5 0.1 . 1 . . . . . . . . 4154 1 194 . 1 1 15 15 LEU CD1 C 13 26.0 0.1 . 1 . . . . . . . . 4154 1 195 . 1 1 15 15 LEU CD2 C 13 23.5 0.1 . 1 . . . . . . . . 4154 1 196 . 1 1 15 15 LEU N N 15 126.8 0.1 . 1 . . . . . . . . 4154 1 197 . 1 1 16 16 ASP H H 1 8.19 0.02 . 1 . . . . . . . . 4154 1 198 . 1 1 16 16 ASP HA H 1 4.71 0.02 . 1 . . . . . . . . 4154 1 199 . 1 1 16 16 ASP HB2 H 1 2.42 0.02 . 2 . . . . . . . . 4154 1 200 . 1 1 16 16 ASP HB3 H 1 2.14 0.02 . 2 . . . . . . . . 4154 1 201 . 1 1 16 16 ASP C C 13 174.9 0.1 . 1 . . . . . . . . 4154 1 202 . 1 1 16 16 ASP CA C 13 53.3 0.1 . 1 . . . . . . . . 4154 1 203 . 1 1 16 16 ASP CB C 13 41.6 0.1 . 1 . . . . . . . . 4154 1 204 . 1 1 16 16 ASP N N 15 121.8 0.1 . 1 . . . . . . . . 4154 1 205 . 1 1 17 17 VAL H H 1 8.99 0.02 . 1 . . . . . . . . 4154 1 206 . 1 1 17 17 VAL HA H 1 3.81 0.02 . 1 . . . . . . . . 4154 1 207 . 1 1 17 17 VAL HB H 1 1.58 0.02 . 1 . . . . . . . . 4154 1 208 . 1 1 17 17 VAL HG11 H 1 0.66 0.02 . 1 . . . . . . . . 4154 1 209 . 1 1 17 17 VAL HG12 H 1 0.66 0.02 . 1 . . . . . . . . 4154 1 210 . 1 1 17 17 VAL HG13 H 1 0.66 0.02 . 1 . . . . . . . . 4154 1 211 . 1 1 17 17 VAL HG21 H 1 0.58 0.02 . 1 . . . . . . . . 4154 1 212 . 1 1 17 17 VAL HG22 H 1 0.58 0.02 . 1 . . . . . . . . 4154 1 213 . 1 1 17 17 VAL HG23 H 1 0.58 0.02 . 1 . . . . . . . . 4154 1 214 . 1 1 17 17 VAL C C 13 174.5 0.1 . 1 . . . . . . . . 4154 1 215 . 1 1 17 17 VAL CA C 13 61.5 0.1 . 1 . . . . . . . . 4154 1 216 . 1 1 17 17 VAL CB C 13 34.2 0.1 . 1 . . . . . . . . 4154 1 217 . 1 1 17 17 VAL CG1 C 13 21.4 0.1 . 1 . . . . . . . . 4154 1 218 . 1 1 17 17 VAL CG2 C 13 22.5 0.1 . 1 . . . . . . . . 4154 1 219 . 1 1 17 17 VAL N N 15 127.8 0.1 . 1 . . . . . . . . 4154 1 220 . 1 1 18 18 ALA H H 1 8.40 0.02 . 1 . . . . . . . . 4154 1 221 . 1 1 18 18 ALA HA H 1 3.92 0.02 . 1 . . . . . . . . 4154 1 222 . 1 1 18 18 ALA HB1 H 1 1.10 0.02 . 1 . . . . . . . . 4154 1 223 . 1 1 18 18 ALA HB2 H 1 1.10 0.02 . 1 . . . . . . . . 4154 1 224 . 1 1 18 18 ALA HB3 H 1 1.10 0.02 . 1 . . . . . . . . 4154 1 225 . 1 1 18 18 ALA C C 13 175.5 0.1 . 1 . . . . . . . . 4154 1 226 . 1 1 18 18 ALA CA C 13 51.7 0.1 . 1 . . . . . . . . 4154 1 227 . 1 1 18 18 ALA CB C 13 18.7 0.1 . 1 . . . . . . . . 4154 1 228 . 1 1 18 18 ALA N N 15 132.7 0.1 . 1 . . . . . . . . 4154 1 229 . 1 1 19 19 ASP H H 1 7.77 0.02 . 1 . . . . . . . . 4154 1 230 . 1 1 19 19 ASP HA H 1 3.88 0.02 . 1 . . . . . . . . 4154 1 231 . 1 1 19 19 ASP HB2 H 1 2.19 0.02 . 1 . . . . . . . . 4154 1 232 . 1 1 19 19 ASP HB3 H 1 2.42 0.02 . 1 . . . . . . . . 4154 1 233 . 1 1 19 19 ASP C C 13 178.1 0.1 . 1 . . . . . . . . 4154 1 234 . 1 1 19 19 ASP CA C 13 55.0 0.1 . 1 . . . . . . . . 4154 1 235 . 1 1 19 19 ASP CB C 13 39.8 0.1 . 1 . . . . . . . . 4154 1 236 . 1 1 19 19 ASP N N 15 119.4 0.1 . 1 . . . . . . . . 4154 1 237 . 1 1 20 20 GLY H H 1 8.80 0.02 . 1 . . . . . . . . 4154 1 238 . 1 1 20 20 GLY HA2 H 1 3.23 0.02 . 1 . . . . . . . . 4154 1 239 . 1 1 20 20 GLY HA3 H 1 4.08 0.02 . 1 . . . . . . . . 4154 1 240 . 1 1 20 20 GLY C C 13 173.2 0.1 . 1 . . . . . . . . 4154 1 241 . 1 1 20 20 GLY CA C 13 44.9 0.1 . 1 . . . . . . . . 4154 1 242 . 1 1 20 20 GLY N N 15 110.9 0.1 . 1 . . . . . . . . 4154 1 243 . 1 1 21 21 VAL H H 1 7.34 0.02 . 1 . . . . . . . . 4154 1 244 . 1 1 21 21 VAL HA H 1 3.87 0.02 . 1 . . . . . . . . 4154 1 245 . 1 1 21 21 VAL HB H 1 1.93 0.02 . 1 . . . . . . . . 4154 1 246 . 1 1 21 21 VAL HG11 H 1 0.89 0.02 . 1 . . . . . . . . 4154 1 247 . 1 1 21 21 VAL HG12 H 1 0.89 0.02 . 1 . . . . . . . . 4154 1 248 . 1 1 21 21 VAL HG13 H 1 0.89 0.02 . 1 . . . . . . . . 4154 1 249 . 1 1 21 21 VAL HG21 H 1 0.62 0.02 . 1 . . . . . . . . 4154 1 250 . 1 1 21 21 VAL HG22 H 1 0.62 0.02 . 1 . . . . . . . . 4154 1 251 . 1 1 21 21 VAL HG23 H 1 0.62 0.02 . 1 . . . . . . . . 4154 1 252 . 1 1 21 21 VAL C C 13 175.2 0.1 . 1 . . . . . . . . 4154 1 253 . 1 1 21 21 VAL CA C 13 61.4 0.1 . 1 . . . . . . . . 4154 1 254 . 1 1 21 21 VAL CB C 13 32.3 0.1 . 1 . . . . . . . . 4154 1 255 . 1 1 21 21 VAL CG1 C 13 20.8 0.1 . 1 . . . . . . . . 4154 1 256 . 1 1 21 21 VAL CG2 C 13 22.1 0.1 . 1 . . . . . . . . 4154 1 257 . 1 1 21 21 VAL N N 15 124.3 0.1 . 1 . . . . . . . . 4154 1 258 . 1 1 22 22 SER H H 1 8.75 0.02 . 1 . . . . . . . . 4154 1 259 . 1 1 22 22 SER HA H 1 5.18 0.02 . 1 . . . . . . . . 4154 1 260 . 1 1 22 22 SER HB2 H 1 3.69 0.02 . 1 . . . . . . . . 4154 1 261 . 1 1 22 22 SER HB3 H 1 4.08 0.02 . 1 . . . . . . . . 4154 1 262 . 1 1 22 22 SER C C 13 174.8 0.1 . 1 . . . . . . . . 4154 1 263 . 1 1 22 22 SER CA C 13 57.0 0.1 . 1 . . . . . . . . 4154 1 264 . 1 1 22 22 SER CB C 13 65.8 0.1 . 1 . . . . . . . . 4154 1 265 . 1 1 22 22 SER N N 15 122.8 0.1 . 1 . . . . . . . . 4154 1 266 . 1 1 23 23 LEU H H 1 8.38 0.02 . 1 . . . . . . . . 4154 1 267 . 1 1 23 23 LEU HA H 1 3.90 0.02 . 1 . . . . . . . . 4154 1 268 . 1 1 23 23 LEU HB2 H 1 1.65 0.02 . 1 . . . . . . . . 4154 1 269 . 1 1 23 23 LEU HB3 H 1 1.36 0.02 . 1 . . . . . . . . 4154 1 270 . 1 1 23 23 LEU HG H 1 1.65 0.02 . 1 . . . . . . . . 4154 1 271 . 1 1 23 23 LEU HD11 H 1 0.57 0.02 . 1 . . . . . . . . 4154 1 272 . 1 1 23 23 LEU HD12 H 1 0.57 0.02 . 1 . . . . . . . . 4154 1 273 . 1 1 23 23 LEU HD13 H 1 0.57 0.02 . 1 . . . . . . . . 4154 1 274 . 1 1 23 23 LEU HD21 H 1 0.52 0.02 . 1 . . . . . . . . 4154 1 275 . 1 1 23 23 LEU HD22 H 1 0.52 0.02 . 1 . . . . . . . . 4154 1 276 . 1 1 23 23 LEU HD23 H 1 0.52 0.02 . 1 . . . . . . . . 4154 1 277 . 1 1 23 23 LEU C C 13 180.5 0.1 . 1 . . . . . . . . 4154 1 278 . 1 1 23 23 LEU CA C 13 57.8 0.1 . 1 . . . . . . . . 4154 1 279 . 1 1 23 23 LEU CB C 13 41.4 0.1 . 1 . . . . . . . . 4154 1 280 . 1 1 23 23 LEU CG C 13 29.5 0.1 . 1 . . . . . . . . 4154 1 281 . 1 1 23 23 LEU CD1 C 13 23.5 0.1 . 1 . . . . . . . . 4154 1 282 . 1 1 23 23 LEU CD2 C 13 24.2 0.1 . 1 . . . . . . . . 4154 1 283 . 1 1 23 23 LEU N N 15 120.1 0.1 . 1 . . . . . . . . 4154 1 284 . 1 1 24 24 MET H H 1 7.98 0.02 . 1 . . . . . . . . 4154 1 285 . 1 1 24 24 MET HA H 1 4.18 0.02 . 1 . . . . . . . . 4154 1 286 . 1 1 24 24 MET HB2 H 1 1.83 0.02 . 1 . . . . . . . . 4154 1 287 . 1 1 24 24 MET HB3 H 1 2.05 0.02 . 1 . . . . . . . . 4154 1 288 . 1 1 24 24 MET HG2 H 1 0.69 0.02 . 1 . . . . . . . . 4154 1 289 . 1 1 24 24 MET HG3 H 1 0.69 0.02 . 1 . . . . . . . . 4154 1 290 . 1 1 24 24 MET C C 13 175.6 0.1 . 1 . . . . . . . . 4154 1 291 . 1 1 25 25 GLN HA H 1 3.63 0.02 . 1 . . . . . . . . 4154 1 292 . 1 1 25 25 GLN HB2 H 1 2.16 0.02 . 1 . . . . . . . . 4154 1 293 . 1 1 25 25 GLN HB3 H 1 1.80 0.02 . 1 . . . . . . . . 4154 1 294 . 1 1 25 25 GLN HG2 H 1 2.32 0.02 . 1 . . . . . . . . 4154 1 295 . 1 1 25 25 GLN HG3 H 1 2.32 0.02 . 1 . . . . . . . . 4154 1 296 . 1 1 25 25 GLN HE21 H 1 7.60 0.02 . 2 . . . . . . . . 4154 1 297 . 1 1 25 25 GLN HE22 H 1 6.34 0.02 . 2 . . . . . . . . 4154 1 298 . 1 1 25 25 GLN C C 13 179.2 0.1 . 1 . . . . . . . . 4154 1 299 . 1 1 25 25 GLN CA C 13 57.9 0.1 . 1 . . . . . . . . 4154 1 300 . 1 1 25 25 GLN CB C 13 32.3 0.1 . 1 . . . . . . . . 4154 1 301 . 1 1 25 25 GLN CG C 13 31.7 0.1 . 1 . . . . . . . . 4154 1 302 . 1 1 25 25 GLN CD C 13 175.5 0.1 . 1 . . . . . . . . 4154 1 303 . 1 1 25 25 GLN N N 15 115.3 0.1 . 1 . . . . . . . . 4154 1 304 . 1 1 25 25 GLN NE2 N 15 103.5 0.1 . 1 . . . . . . . . 4154 1 305 . 1 1 26 26 ALA H H 1 7.87 0.02 . 1 . . . . . . . . 4154 1 306 . 1 1 26 26 ALA HA H 1 3.82 0.02 . 1 . . . . . . . . 4154 1 307 . 1 1 26 26 ALA HB1 H 1 1.23 0.02 . 1 . . . . . . . . 4154 1 308 . 1 1 26 26 ALA HB2 H 1 1.23 0.02 . 1 . . . . . . . . 4154 1 309 . 1 1 26 26 ALA HB3 H 1 1.23 0.02 . 1 . . . . . . . . 4154 1 310 . 1 1 26 26 ALA C C 13 178.7 0.1 . 1 . . . . . . . . 4154 1 311 . 1 1 26 26 ALA CA C 13 54.3 0.1 . 1 . . . . . . . . 4154 1 312 . 1 1 26 26 ALA CB C 13 18.6 0.1 . 1 . . . . . . . . 4154 1 313 . 1 1 26 26 ALA N N 15 121.4 0.1 . 1 . . . . . . . . 4154 1 314 . 1 1 27 27 ALA H H 1 6.81 0.02 . 1 . . . . . . . . 4154 1 315 . 1 1 27 27 ALA HA H 1 3.23 0.02 . 1 . . . . . . . . 4154 1 316 . 1 1 27 27 ALA HB1 H 1 1.04 0.02 . 1 . . . . . . . . 4154 1 317 . 1 1 27 27 ALA HB2 H 1 1.04 0.02 . 1 . . . . . . . . 4154 1 318 . 1 1 27 27 ALA HB3 H 1 1.04 0.02 . 1 . . . . . . . . 4154 1 319 . 1 1 27 27 ALA C C 13 179.5 0.1 . 1 . . . . . . . . 4154 1 320 . 1 1 27 27 ALA CA C 13 54.6 0.1 . 1 . . . . . . . . 4154 1 321 . 1 1 27 27 ALA CB C 13 18.4 0.1 . 1 . . . . . . . . 4154 1 322 . 1 1 27 27 ALA N N 15 120.5 0.1 . 1 . . . . . . . . 4154 1 323 . 1 1 28 28 VAL H H 1 8.18 0.02 . 1 . . . . . . . . 4154 1 324 . 1 1 28 28 VAL HA H 1 3.71 0.02 . 1 . . . . . . . . 4154 1 325 . 1 1 28 28 VAL HB H 1 1.90 0.02 . 1 . . . . . . . . 4154 1 326 . 1 1 28 28 VAL HG11 H 1 0.68 0.02 . 1 . . . . . . . . 4154 1 327 . 1 1 28 28 VAL HG12 H 1 0.68 0.02 . 1 . . . . . . . . 4154 1 328 . 1 1 28 28 VAL HG13 H 1 0.68 0.02 . 1 . . . . . . . . 4154 1 329 . 1 1 28 28 VAL HG21 H 1 0.75 0.02 . 1 . . . . . . . . 4154 1 330 . 1 1 28 28 VAL HG22 H 1 0.75 0.02 . 1 . . . . . . . . 4154 1 331 . 1 1 28 28 VAL HG23 H 1 0.75 0.02 . 1 . . . . . . . . 4154 1 332 . 1 1 28 28 VAL C C 13 180.0 0.1 . 1 . . . . . . . . 4154 1 333 . 1 1 28 28 VAL CA C 13 64.7 0.1 . 1 . . . . . . . . 4154 1 334 . 1 1 28 28 VAL CB C 13 32.1 0.1 . 1 . . . . . . . . 4154 1 335 . 1 1 28 28 VAL CG1 C 13 20.1 0.1 . 1 . . . . . . . . 4154 1 336 . 1 1 28 28 VAL CG2 C 13 23.6 0.1 . 1 . . . . . . . . 4154 1 337 . 1 1 28 28 VAL N N 15 116.3 0.1 . 1 . . . . . . . . 4154 1 338 . 1 1 29 29 SER H H 1 7.71 0.02 . 1 . . . . . . . . 4154 1 339 . 1 1 29 29 SER HA H 1 4.18 0.02 . 1 . . . . . . . . 4154 1 340 . 1 1 29 29 SER HB2 H 1 3.71 0.02 . 2 . . . . . . . . 4154 1 341 . 1 1 29 29 SER HB3 H 1 3.65 0.02 . 2 . . . . . . . . 4154 1 342 . 1 1 29 29 SER C C 13 174.1 0.1 . 1 . . . . . . . . 4154 1 343 . 1 1 29 29 SER CA C 13 60.0 0.1 . 1 . . . . . . . . 4154 1 344 . 1 1 29 29 SER CB C 13 63.4 0.1 . 1 . . . . . . . . 4154 1 345 . 1 1 29 29 SER N N 15 115.3 0.1 . 1 . . . . . . . . 4154 1 346 . 1 1 30 30 ASN H H 1 7.04 0.02 . 1 . . . . . . . . 4154 1 347 . 1 1 30 30 ASN HA H 1 4.69 0.02 . 1 . . . . . . . . 4154 1 348 . 1 1 30 30 ASN HB2 H 1 2.60 0.02 . 1 . . . . . . . . 4154 1 349 . 1 1 30 30 ASN HB3 H 1 2.28 0.02 . 1 . . . . . . . . 4154 1 350 . 1 1 30 30 ASN HD21 H 1 7.05 0.02 . 2 . . . . . . . . 4154 1 351 . 1 1 30 30 ASN HD22 H 1 8.41 0.02 . 2 . . . . . . . . 4154 1 352 . 1 1 30 30 ASN C C 13 174.0 0.1 . 1 . . . . . . . . 4154 1 353 . 1 1 30 30 ASN CA C 13 53.1 0.1 . 1 . . . . . . . . 4154 1 354 . 1 1 30 30 ASN CB C 13 40.8 0.1 . 1 . . . . . . . . 4154 1 355 . 1 1 30 30 ASN CG C 13 178.2 0.1 . 1 . . . . . . . . 4154 1 356 . 1 1 30 30 ASN N N 15 118.2 0.1 . 1 . . . . . . . . 4154 1 357 . 1 1 30 30 ASN ND2 N 15 119.1 0.1 . 1 . . . . . . . . 4154 1 358 . 1 1 31 31 GLY H H 1 7.39 0.02 . 1 . . . . . . . . 4154 1 359 . 1 1 31 31 GLY HA2 H 1 3.55 0.02 . 1 . . . . . . . . 4154 1 360 . 1 1 31 31 GLY HA3 H 1 3.33 0.02 . 1 . . . . . . . . 4154 1 361 . 1 1 31 31 GLY C C 13 174.1 0.1 . 1 . . . . . . . . 4154 1 362 . 1 1 31 31 GLY CA C 13 46.7 0.1 . 1 . . . . . . . . 4154 1 363 . 1 1 31 31 GLY N N 15 107.2 0.1 . 1 . . . . . . . . 4154 1 364 . 1 1 32 32 ILE H H 1 7.52 0.02 . 1 . . . . . . . . 4154 1 365 . 1 1 32 32 ILE HA H 1 3.68 0.02 . 1 . . . . . . . . 4154 1 366 . 1 1 32 32 ILE HB H 1 1.37 0.02 . 1 . . . . . . . . 4154 1 367 . 1 1 32 32 ILE HG12 H 1 0.39 0.02 . 2 . . . . . . . . 4154 1 368 . 1 1 32 32 ILE HG13 H 1 0.65 0.02 . 2 . . . . . . . . 4154 1 369 . 1 1 32 32 ILE HG21 H 1 0.23 0.02 . 1 . . . . . . . . 4154 1 370 . 1 1 32 32 ILE HG22 H 1 0.23 0.02 . 1 . . . . . . . . 4154 1 371 . 1 1 32 32 ILE HG23 H 1 0.23 0.02 . 1 . . . . . . . . 4154 1 372 . 1 1 32 32 ILE HD11 H 1 -0.02 0.02 . 1 . . . . . . . . 4154 1 373 . 1 1 32 32 ILE HD12 H 1 -0.02 0.02 . 1 . . . . . . . . 4154 1 374 . 1 1 32 32 ILE HD13 H 1 -0.02 0.02 . 1 . . . . . . . . 4154 1 375 . 1 1 32 32 ILE C C 13 175.1 0.1 . 1 . . . . . . . . 4154 1 376 . 1 1 32 32 ILE CA C 13 58.5 0.1 . 1 . . . . . . . . 4154 1 377 . 1 1 32 32 ILE CB C 13 32.8 0.1 . 1 . . . . . . . . 4154 1 378 . 1 1 32 32 ILE CG1 C 13 27.5 0.1 . 1 . . . . . . . . 4154 1 379 . 1 1 32 32 ILE CG2 C 13 15.8 0.1 . 1 . . . . . . . . 4154 1 380 . 1 1 32 32 ILE CD1 C 13 10.7 0.1 . 1 . . . . . . . . 4154 1 381 . 1 1 32 32 ILE N N 15 122.7 0.1 . 1 . . . . . . . . 4154 1 382 . 1 1 33 33 TYR H H 1 6.96 0.02 . 1 . . . . . . . . 4154 1 383 . 1 1 33 33 TYR HA H 1 4.25 0.02 . 1 . . . . . . . . 4154 1 384 . 1 1 33 33 TYR HB2 H 1 2.71 0.02 . 1 . . . . . . . . 4154 1 385 . 1 1 33 33 TYR HB3 H 1 2.88 0.02 . 1 . . . . . . . . 4154 1 386 . 1 1 33 33 TYR HD1 H 1 6.93 0.02 . 1 . . . . . . . . 4154 1 387 . 1 1 33 33 TYR HD2 H 1 6.93 0.02 . 1 . . . . . . . . 4154 1 388 . 1 1 33 33 TYR HE1 H 1 6.67 0.02 . 1 . . . . . . . . 4154 1 389 . 1 1 33 33 TYR HE2 H 1 6.67 0.02 . 1 . . . . . . . . 4154 1 390 . 1 1 33 33 TYR C C 13 175.3 0.1 . 1 . . . . . . . . 4154 1 391 . 1 1 33 33 TYR CA C 13 58.6 0.1 . 1 . . . . . . . . 4154 1 392 . 1 1 33 33 TYR CB C 13 38.0 0.1 . 1 . . . . . . . . 4154 1 393 . 1 1 33 33 TYR CD1 C 13 132.7 0.1 . 1 . . . . . . . . 4154 1 394 . 1 1 33 33 TYR CD2 C 13 132.7 0.1 . 1 . . . . . . . . 4154 1 395 . 1 1 33 33 TYR CE1 C 13 118.2 0.1 . 1 . . . . . . . . 4154 1 396 . 1 1 33 33 TYR CE2 C 13 118.2 0.1 . 1 . . . . . . . . 4154 1 397 . 1 1 33 33 TYR N N 15 122.2 0.1 . 1 . . . . . . . . 4154 1 398 . 1 1 34 34 ASP H H 1 9.47 0.02 . 1 . . . . . . . . 4154 1 399 . 1 1 34 34 ASP HA H 1 4.09 0.02 . 1 . . . . . . . . 4154 1 400 . 1 1 34 34 ASP HB2 H 1 2.50 0.02 . 1 . . . . . . . . 4154 1 401 . 1 1 34 34 ASP HB3 H 1 2.43 0.02 . 1 . . . . . . . . 4154 1 402 . 1 1 34 34 ASP C C 13 175.1 0.1 . 1 . . . . . . . . 4154 1 403 . 1 1 34 34 ASP CA C 13 52.2 0.1 . 1 . . . . . . . . 4154 1 404 . 1 1 34 34 ASP CB C 13 38.6 0.1 . 1 . . . . . . . . 4154 1 405 . 1 1 34 34 ASP N N 15 116.1 0.1 . 1 . . . . . . . . 4154 1 406 . 1 1 35 35 ILE H H 1 7.41 0.02 . 1 . . . . . . . . 4154 1 407 . 1 1 35 35 ILE HA H 1 3.50 0.02 . 1 . . . . . . . . 4154 1 408 . 1 1 35 35 ILE HB H 1 1.39 0.02 . 1 . . . . . . . . 4154 1 409 . 1 1 35 35 ILE HG12 H 1 0.40 0.02 . 2 . . . . . . . . 4154 1 410 . 1 1 35 35 ILE HG13 H 1 1.12 0.02 . 2 . . . . . . . . 4154 1 411 . 1 1 35 35 ILE CA C 13 61.4 0.1 . 1 . . . . . . . . 4154 1 412 . 1 1 35 35 ILE CB C 13 38.6 0.1 . 1 . . . . . . . . 4154 1 413 . 1 1 35 35 ILE CG1 C 13 27.9 0.1 . 1 . . . . . . . . 4154 1 414 . 1 1 35 35 ILE N N 15 121.5 0.1 . 1 . . . . . . . . 4154 1 415 . 1 1 49 49 HIS HB2 H 1 3.07 0.02 . 1 . . . . . . . . 4154 1 416 . 1 1 49 49 HIS HB3 H 1 3.18 0.02 . 1 . . . . . . . . 4154 1 417 . 1 1 49 49 HIS HD1 H 1 12.01 0.02 . 1 . . . . . . . . 4154 1 418 . 1 1 49 49 HIS HD2 H 1 6.68 0.02 . 1 . . . . . . . . 4154 1 419 . 1 1 49 49 HIS HE1 H 1 7.23 0.02 . 1 . . . . . . . . 4154 1 420 . 1 1 49 49 HIS C C 13 174.0 0.1 . 1 . . . . . . . . 4154 1 421 . 1 1 49 49 HIS CB C 13 37.1 0.1 . 1 . . . . . . . . 4154 1 422 . 1 1 49 49 HIS CD2 C 13 122.8 0.1 . 1 . . . . . . . . 4154 1 423 . 1 1 49 49 HIS CE1 C 13 136.3 0.1 . 1 . . . . . . . . 4154 1 424 . 1 1 49 49 HIS ND1 N 15 167.8 0.1 . 1 . . . . . . . . 4154 1 425 . 1 1 49 49 HIS NE2 N 15 246.8 0.1 . 1 . . . . . . . . 4154 1 426 . 1 1 50 50 VAL H H 1 8.92 0.02 . 1 . . . . . . . . 4154 1 427 . 1 1 50 50 VAL HA H 1 4.12 0.02 . 1 . . . . . . . . 4154 1 428 . 1 1 50 50 VAL HB H 1 1.78 0.02 . 1 . . . . . . . . 4154 1 429 . 1 1 50 50 VAL HG11 H 1 0.38 0.02 . 1 . . . . . . . . 4154 1 430 . 1 1 50 50 VAL HG12 H 1 0.38 0.02 . 1 . . . . . . . . 4154 1 431 . 1 1 50 50 VAL HG13 H 1 0.38 0.02 . 1 . . . . . . . . 4154 1 432 . 1 1 50 50 VAL HG21 H 1 0.71 0.02 . 1 . . . . . . . . 4154 1 433 . 1 1 50 50 VAL HG22 H 1 0.71 0.02 . 1 . . . . . . . . 4154 1 434 . 1 1 50 50 VAL HG23 H 1 0.71 0.02 . 1 . . . . . . . . 4154 1 435 . 1 1 50 50 VAL C C 13 171.7 0.1 . 1 . . . . . . . . 4154 1 436 . 1 1 50 50 VAL CA C 13 58.4 0.1 . 1 . . . . . . . . 4154 1 437 . 1 1 50 50 VAL CB C 13 36.8 0.1 . 1 . . . . . . . . 4154 1 438 . 1 1 50 50 VAL CG1 C 13 18.7 0.1 . 1 . . . . . . . . 4154 1 439 . 1 1 50 50 VAL CG2 C 13 23.8 0.1 . 1 . . . . . . . . 4154 1 440 . 1 1 50 50 VAL N N 15 118.0 0.1 . 1 . . . . . . . . 4154 1 441 . 1 1 51 51 TYR H H 1 8.95 0.02 . 1 . . . . . . . . 4154 1 442 . 1 1 51 51 TYR HA H 1 4.96 0.02 . 1 . . . . . . . . 4154 1 443 . 1 1 51 51 TYR HB2 H 1 2.69 0.02 . 1 . . . . . . . . 4154 1 444 . 1 1 51 51 TYR HB3 H 1 2.62 0.02 . 1 . . . . . . . . 4154 1 445 . 1 1 51 51 TYR HD1 H 1 6.63 0.02 . 1 . . . . . . . . 4154 1 446 . 1 1 51 51 TYR HD2 H 1 6.63 0.02 . 1 . . . . . . . . 4154 1 447 . 1 1 51 51 TYR HE1 H 1 6.65 0.02 . 1 . . . . . . . . 4154 1 448 . 1 1 51 51 TYR HE2 H 1 6.65 0.02 . 1 . . . . . . . . 4154 1 449 . 1 1 51 51 TYR C C 13 177.2 0.1 . 1 . . . . . . . . 4154 1 450 . 1 1 51 51 TYR CA C 13 53.9 0.1 . 1 . . . . . . . . 4154 1 451 . 1 1 51 51 TYR CB C 13 38.5 0.1 . 1 . . . . . . . . 4154 1 452 . 1 1 51 51 TYR CD1 C 13 132.5 0.1 . 1 . . . . . . . . 4154 1 453 . 1 1 51 51 TYR CD2 C 13 132.5 0.1 . 1 . . . . . . . . 4154 1 454 . 1 1 51 51 TYR CE1 C 13 117.8 0.1 . 1 . . . . . . . . 4154 1 455 . 1 1 51 51 TYR CE2 C 13 117.8 0.1 . 1 . . . . . . . . 4154 1 456 . 1 1 51 51 TYR N N 15 118.3 0.1 . 1 . . . . . . . . 4154 1 457 . 1 1 52 52 VAL H H 1 8.61 0.02 . 1 . . . . . . . . 4154 1 458 . 1 1 52 52 VAL HA H 1 3.63 0.02 . 1 . . . . . . . . 4154 1 459 . 1 1 52 52 VAL HB H 1 1.89 0.02 . 1 . . . . . . . . 4154 1 460 . 1 1 52 52 VAL HG11 H 1 0.82 0.02 . 1 . . . . . . . . 4154 1 461 . 1 1 52 52 VAL HG12 H 1 0.82 0.02 . 1 . . . . . . . . 4154 1 462 . 1 1 52 52 VAL HG13 H 1 0.82 0.02 . 1 . . . . . . . . 4154 1 463 . 1 1 52 52 VAL HG21 H 1 0.65 0.02 . 1 . . . . . . . . 4154 1 464 . 1 1 52 52 VAL HG22 H 1 0.65 0.02 . 1 . . . . . . . . 4154 1 465 . 1 1 52 52 VAL HG23 H 1 0.65 0.02 . 1 . . . . . . . . 4154 1 466 . 1 1 52 52 VAL C C 13 174.9 0.1 . 1 . . . . . . . . 4154 1 467 . 1 1 52 52 VAL CA C 13 64.5 0.1 . 1 . . . . . . . . 4154 1 468 . 1 1 52 52 VAL CB C 13 31.9 0.1 . 1 . . . . . . . . 4154 1 469 . 1 1 52 52 VAL CG1 C 13 21.1 0.1 . 1 . . . . . . . . 4154 1 470 . 1 1 52 52 VAL CG2 C 13 22.5 0.1 . 1 . . . . . . . . 4154 1 471 . 1 1 52 52 VAL N N 15 128.2 0.1 . 1 . . . . . . . . 4154 1 472 . 1 1 53 53 ASN H H 1 8.26 0.02 . 1 . . . . . . . . 4154 1 473 . 1 1 53 53 ASN HA H 1 4.28 0.02 . 1 . . . . . . . . 4154 1 474 . 1 1 53 53 ASN HB2 H 1 2.57 0.02 . 1 . . . . . . . . 4154 1 475 . 1 1 53 53 ASN HB3 H 1 2.79 0.02 . 1 . . . . . . . . 4154 1 476 . 1 1 53 53 ASN HD21 H 1 7.08 0.02 . 1 . . . . . . . . 4154 1 477 . 1 1 53 53 ASN HD22 H 1 8.04 0.02 . 1 . . . . . . . . 4154 1 478 . 1 1 53 53 ASN C C 13 176.5 0.1 . 1 . . . . . . . . 4154 1 479 . 1 1 53 53 ASN CA C 13 56.0 0.1 . 1 . . . . . . . . 4154 1 480 . 1 1 53 53 ASN CB C 13 38.6 0.1 . 1 . . . . . . . . 4154 1 481 . 1 1 53 53 ASN CG C 13 176.4 0.1 . 1 . . . . . . . . 4154 1 482 . 1 1 53 53 ASN N N 15 128.8 0.1 . 1 . . . . . . . . 4154 1 483 . 1 1 53 53 ASN ND2 N 15 116.9 0.1 . 1 . . . . . . . . 4154 1 484 . 1 1 54 54 GLU H H 1 9.09 0.02 . 1 . . . . . . . . 4154 1 485 . 1 1 54 54 GLU HA H 1 4.04 0.02 . 1 . . . . . . . . 4154 1 486 . 1 1 54 54 GLU HB2 H 1 1.80 0.02 . 1 . . . . . . . . 4154 1 487 . 1 1 54 54 GLU HB3 H 1 1.90 0.02 . 1 . . . . . . . . 4154 1 488 . 1 1 54 54 GLU HG2 H 1 2.14 0.02 . 1 . . . . . . . . 4154 1 489 . 1 1 54 54 GLU HG3 H 1 2.14 0.02 . 1 . . . . . . . . 4154 1 490 . 1 1 54 54 GLU C C 13 176.3 0.1 . 1 . . . . . . . . 4154 1 491 . 1 1 54 54 GLU CA C 13 59.3 0.1 . 1 . . . . . . . . 4154 1 492 . 1 1 54 54 GLU CB C 13 28.4 0.1 . 1 . . . . . . . . 4154 1 493 . 1 1 54 54 GLU CG C 13 35.9 0.1 . 1 . . . . . . . . 4154 1 494 . 1 1 54 54 GLU N N 15 125.5 0.1 . 1 . . . . . . . . 4154 1 495 . 1 1 55 55 ALA H H 1 8.30 0.02 . 1 . . . . . . . . 4154 1 496 . 1 1 55 55 ALA HA H 1 4.00 0.02 . 1 . . . . . . . . 4154 1 497 . 1 1 55 55 ALA HB1 H 1 1.00 0.02 . 1 . . . . . . . . 4154 1 498 . 1 1 55 55 ALA HB2 H 1 1.00 0.02 . 1 . . . . . . . . 4154 1 499 . 1 1 55 55 ALA HB3 H 1 1.00 0.02 . 1 . . . . . . . . 4154 1 500 . 1 1 55 55 ALA C C 13 177.7 0.1 . 1 . . . . . . . . 4154 1 501 . 1 1 55 55 ALA CA C 13 53.4 0.1 . 1 . . . . . . . . 4154 1 502 . 1 1 55 55 ALA CB C 13 17.6 0.1 . 1 . . . . . . . . 4154 1 503 . 1 1 55 55 ALA N N 15 122.2 0.1 . 1 . . . . . . . . 4154 1 504 . 1 1 56 56 PHE H H 1 8.66 0.02 . 1 . . . . . . . . 4154 1 505 . 1 1 56 56 PHE HA H 1 4.26 0.02 . 1 . . . . . . . . 4154 1 506 . 1 1 56 56 PHE HB2 H 1 2.98 0.02 . 1 . . . . . . . . 4154 1 507 . 1 1 56 56 PHE HB3 H 1 2.57 0.02 . 1 . . . . . . . . 4154 1 508 . 1 1 56 56 PHE HD1 H 1 6.96 0.02 . 1 . . . . . . . . 4154 1 509 . 1 1 56 56 PHE HD2 H 1 6.96 0.02 . 1 . . . . . . . . 4154 1 510 . 1 1 56 56 PHE HE1 H 1 7.10 0.02 . 1 . . . . . . . . 4154 1 511 . 1 1 56 56 PHE HE2 H 1 7.10 0.02 . 1 . . . . . . . . 4154 1 512 . 1 1 56 56 PHE HZ H 1 7.00 0.02 . 1 . . . . . . . . 4154 1 513 . 1 1 56 56 PHE C C 13 176.4 0.1 . 1 . . . . . . . . 4154 1 514 . 1 1 56 56 PHE CA C 13 58.1 0.1 . 1 . . . . . . . . 4154 1 515 . 1 1 56 56 PHE CB C 13 42.3 0.1 . 1 . . . . . . . . 4154 1 516 . 1 1 56 56 PHE CD1 C 13 133.1 0.1 . 1 . . . . . . . . 4154 1 517 . 1 1 56 56 PHE CD2 C 13 133.1 0.1 . 1 . . . . . . . . 4154 1 518 . 1 1 56 56 PHE CE1 C 13 132.1 0.1 . 1 . . . . . . . . 4154 1 519 . 1 1 56 56 PHE CE2 C 13 131.7 0.1 . 1 . . . . . . . . 4154 1 520 . 1 1 56 56 PHE CZ C 13 126.8 0.1 . 1 . . . . . . . . 4154 1 521 . 1 1 56 56 PHE N N 15 114.6 0.1 . 1 . . . . . . . . 4154 1 522 . 1 1 57 57 THR H H 1 7.33 0.02 . 1 . . . . . . . . 4154 1 523 . 1 1 57 57 THR HA H 1 3.58 0.02 . 1 . . . . . . . . 4154 1 524 . 1 1 57 57 THR HB H 1 4.03 0.02 . 1 . . . . . . . . 4154 1 525 . 1 1 57 57 THR HG21 H 1 1.11 0.02 . 1 . . . . . . . . 4154 1 526 . 1 1 57 57 THR HG22 H 1 1.11 0.02 . 1 . . . . . . . . 4154 1 527 . 1 1 57 57 THR HG23 H 1 1.11 0.02 . 1 . . . . . . . . 4154 1 528 . 1 1 57 57 THR C C 13 175.5 0.1 . 1 . . . . . . . . 4154 1 529 . 1 1 57 57 THR CA C 13 65.6 0.1 . 1 . . . . . . . . 4154 1 530 . 1 1 57 57 THR CB C 13 68.1 0.1 . 1 . . . . . . . . 4154 1 531 . 1 1 57 57 THR CG2 C 13 23.0 0.1 . 1 . . . . . . . . 4154 1 532 . 1 1 57 57 THR N N 15 114.6 0.1 . 1 . . . . . . . . 4154 1 533 . 1 1 58 58 ASP H H 1 8.52 0.02 . 1 . . . . . . . . 4154 1 534 . 1 1 58 58 ASP HA H 1 4.45 0.02 . 1 . . . . . . . . 4154 1 535 . 1 1 58 58 ASP HB2 H 1 2.45 0.02 . 2 . . . . . . . . 4154 1 536 . 1 1 58 58 ASP HB3 H 1 2.46 0.02 . 2 . . . . . . . . 4154 1 537 . 1 1 58 58 ASP C C 13 176.2 0.1 . 1 . . . . . . . . 4154 1 538 . 1 1 58 58 ASP CA C 13 54.4 0.1 . 1 . . . . . . . . 4154 1 539 . 1 1 58 58 ASP CB C 13 39.8 0.1 . 1 . . . . . . . . 4154 1 540 . 1 1 58 58 ASP CG C 13 178.9 0.1 . 1 . . . . . . . . 4154 1 541 . 1 1 58 58 ASP N N 15 118.4 0.1 . 1 . . . . . . . . 4154 1 542 . 1 1 59 59 LYS H H 1 7.32 0.02 . 1 . . . . . . . . 4154 1 543 . 1 1 59 59 LYS HA H 1 4.12 0.02 . 1 . . . . . . . . 4154 1 544 . 1 1 59 59 LYS HB2 H 1 1.73 0.02 . 1 . . . . . . . . 4154 1 545 . 1 1 59 59 LYS HB3 H 1 1.56 0.02 . 1 . . . . . . . . 4154 1 546 . 1 1 59 59 LYS HG2 H 1 1.25 0.02 . 2 . . . . . . . . 4154 1 547 . 1 1 59 59 LYS HG3 H 1 1.20 0.02 . 2 . . . . . . . . 4154 1 548 . 1 1 59 59 LYS HD2 H 1 1.49 0.02 . 2 . . . . . . . . 4154 1 549 . 1 1 59 59 LYS HD3 H 1 1.32 0.02 . 2 . . . . . . . . 4154 1 550 . 1 1 59 59 LYS HE2 H 1 2.74 0.02 . 2 . . . . . . . . 4154 1 551 . 1 1 59 59 LYS HE3 H 1 2.72 0.02 . 2 . . . . . . . . 4154 1 552 . 1 1 59 59 LYS C C 13 175.9 0.1 . 1 . . . . . . . . 4154 1 553 . 1 1 59 59 LYS CA C 13 56.1 0.1 . 1 . . . . . . . . 4154 1 554 . 1 1 59 59 LYS CB C 13 34.1 0.1 . 1 . . . . . . . . 4154 1 555 . 1 1 59 59 LYS CG C 13 24.9 0.1 . 1 . . . . . . . . 4154 1 556 . 1 1 59 59 LYS CD C 13 29.1 0.1 . 1 . . . . . . . . 4154 1 557 . 1 1 59 59 LYS CE C 13 41.7 0.1 . 1 . . . . . . . . 4154 1 558 . 1 1 59 59 LYS N N 15 118.3 0.1 . 1 . . . . . . . . 4154 1 559 . 1 1 60 60 VAL H H 1 6.88 0.02 . 1 . . . . . . . . 4154 1 560 . 1 1 60 60 VAL HA H 1 4.11 0.02 . 1 . . . . . . . . 4154 1 561 . 1 1 60 60 VAL HB H 1 1.86 0.02 . 1 . . . . . . . . 4154 1 562 . 1 1 60 60 VAL HG11 H 1 0.87 0.02 . 1 . . . . . . . . 4154 1 563 . 1 1 60 60 VAL HG12 H 1 0.87 0.02 . 1 . . . . . . . . 4154 1 564 . 1 1 60 60 VAL HG13 H 1 0.87 0.02 . 1 . . . . . . . . 4154 1 565 . 1 1 60 60 VAL HG21 H 1 0.79 0.02 . 1 . . . . . . . . 4154 1 566 . 1 1 60 60 VAL HG22 H 1 0.79 0.02 . 1 . . . . . . . . 4154 1 567 . 1 1 60 60 VAL HG23 H 1 0.79 0.02 . 1 . . . . . . . . 4154 1 568 . 1 1 60 60 VAL CA C 13 59.1 0.1 . 1 . . . . . . . . 4154 1 569 . 1 1 60 60 VAL CB C 13 32.5 0.1 . 1 . . . . . . . . 4154 1 570 . 1 1 60 60 VAL CG1 C 13 23.2 0.1 . 1 . . . . . . . . 4154 1 571 . 1 1 60 60 VAL CG2 C 13 21.4 0.1 . 1 . . . . . . . . 4154 1 572 . 1 1 60 60 VAL N N 15 118.4 0.1 . 1 . . . . . . . . 4154 1 573 . 1 1 61 61 PRO HA H 1 4.13 0.02 . 1 . . . . . . . . 4154 1 574 . 1 1 61 61 PRO HB2 H 1 2.18 0.02 . 2 . . . . . . . . 4154 1 575 . 1 1 61 61 PRO HB3 H 1 1.71 0.02 . 2 . . . . . . . . 4154 1 576 . 1 1 61 61 PRO HG2 H 1 1.84 0.02 . 2 . . . . . . . . 4154 1 577 . 1 1 61 61 PRO HG3 H 1 1.97 0.02 . 2 . . . . . . . . 4154 1 578 . 1 1 61 61 PRO HD2 H 1 3.84 0.02 . 1 . . . . . . . . 4154 1 579 . 1 1 61 61 PRO HD3 H 1 3.44 0.02 . 1 . . . . . . . . 4154 1 580 . 1 1 61 61 PRO C C 13 176.0 0.1 . 1 . . . . . . . . 4154 1 581 . 1 1 61 61 PRO CA C 13 63.2 0.1 . 1 . . . . . . . . 4154 1 582 . 1 1 61 61 PRO CB C 13 31.4 0.1 . 1 . . . . . . . . 4154 1 583 . 1 1 61 61 PRO CG C 13 27.8 0.1 . 1 . . . . . . . . 4154 1 584 . 1 1 61 61 PRO CD C 13 50.7 0.1 . 1 . . . . . . . . 4154 1 585 . 1 1 62 62 ALA H H 1 8.36 0.02 . 1 . . . . . . . . 4154 1 586 . 1 1 62 62 ALA HA H 1 3.88 0.02 . 1 . . . . . . . . 4154 1 587 . 1 1 62 62 ALA HB1 H 1 1.21 0.02 . 1 . . . . . . . . 4154 1 588 . 1 1 62 62 ALA HB2 H 1 1.21 0.02 . 1 . . . . . . . . 4154 1 589 . 1 1 62 62 ALA HB3 H 1 1.21 0.02 . 1 . . . . . . . . 4154 1 590 . 1 1 62 62 ALA C C 13 177.6 0.1 . 1 . . . . . . . . 4154 1 591 . 1 1 62 62 ALA CA C 13 52.1 0.1 . 1 . . . . . . . . 4154 1 592 . 1 1 62 62 ALA CB C 13 18.9 0.1 . 1 . . . . . . . . 4154 1 593 . 1 1 62 62 ALA N N 15 127.2 0.1 . 1 . . . . . . . . 4154 1 594 . 1 1 63 63 ALA H H 1 8.53 0.02 . 1 . . . . . . . . 4154 1 595 . 1 1 63 63 ALA HA H 1 3.89 0.02 . 1 . . . . . . . . 4154 1 596 . 1 1 63 63 ALA HB1 H 1 1.01 0.02 . 1 . . . . . . . . 4154 1 597 . 1 1 63 63 ALA HB2 H 1 1.01 0.02 . 1 . . . . . . . . 4154 1 598 . 1 1 63 63 ALA HB3 H 1 1.01 0.02 . 1 . . . . . . . . 4154 1 599 . 1 1 63 63 ALA C C 13 177.2 0.1 . 1 . . . . . . . . 4154 1 600 . 1 1 63 63 ALA CA C 13 53.0 0.1 . 1 . . . . . . . . 4154 1 601 . 1 1 63 63 ALA CB C 13 19.2 0.1 . 1 . . . . . . . . 4154 1 602 . 1 1 63 63 ALA N N 15 126.0 0.1 . 1 . . . . . . . . 4154 1 603 . 1 1 64 64 ASN H H 1 8.45 0.02 . 1 . . . . . . . . 4154 1 604 . 1 1 64 64 ASN HA H 1 4.57 0.02 . 1 . . . . . . . . 4154 1 605 . 1 1 64 64 ASN HB2 H 1 2.75 0.02 . 1 . . . . . . . . 4154 1 606 . 1 1 64 64 ASN HB3 H 1 3.15 0.02 . 1 . . . . . . . . 4154 1 607 . 1 1 64 64 ASN HD21 H 1 6.47 0.02 . 2 . . . . . . . . 4154 1 608 . 1 1 64 64 ASN HD22 H 1 7.48 0.02 . 2 . . . . . . . . 4154 1 609 . 1 1 64 64 ASN C C 13 174.3 0.1 . 1 . . . . . . . . 4154 1 610 . 1 1 64 64 ASN CA C 13 50.6 0.1 . 1 . . . . . . . . 4154 1 611 . 1 1 64 64 ASN CB C 13 38.6 0.1 . 1 . . . . . . . . 4154 1 612 . 1 1 64 64 ASN CG C 13 175.8 0.1 . 1 . . . . . . . . 4154 1 613 . 1 1 64 64 ASN N N 15 121.4 0.1 . 1 . . . . . . . . 4154 1 614 . 1 1 64 64 ASN ND2 N 15 111.9 0.1 . 1 . . . . . . . . 4154 1 615 . 1 1 65 65 GLU H H 1 8.48 0.02 . 1 . . . . . . . . 4154 1 616 . 1 1 65 65 GLU HA H 1 3.71 0.02 . 1 . . . . . . . . 4154 1 617 . 1 1 65 65 GLU HB2 H 1 1.88 0.02 . 1 . . . . . . . . 4154 1 618 . 1 1 65 65 GLU HB3 H 1 1.83 0.02 . 1 . . . . . . . . 4154 1 619 . 1 1 65 65 GLU HG2 H 1 2.09 0.02 . 2 . . . . . . . . 4154 1 620 . 1 1 65 65 GLU HG3 H 1 1.83 0.02 . 2 . . . . . . . . 4154 1 621 . 1 1 65 65 GLU C C 13 178.7 0.1 . 1 . . . . . . . . 4154 1 622 . 1 1 65 65 GLU CA C 13 59.7 0.1 . 1 . . . . . . . . 4154 1 623 . 1 1 65 65 GLU CB C 13 29.4 0.1 . 1 . . . . . . . . 4154 1 624 . 1 1 65 65 GLU CG C 13 35.5 0.1 . 1 . . . . . . . . 4154 1 625 . 1 1 65 65 GLU N N 15 117.3 0.1 . 1 . . . . . . . . 4154 1 626 . 1 1 66 66 ARG H H 1 7.88 0.02 . 1 . . . . . . . . 4154 1 627 . 1 1 66 66 ARG HA H 1 3.90 0.02 . 1 . . . . . . . . 4154 1 628 . 1 1 66 66 ARG HB2 H 1 1.70 0.02 . 1 . . . . . . . . 4154 1 629 . 1 1 66 66 ARG HB3 H 1 1.63 0.02 . 1 . . . . . . . . 4154 1 630 . 1 1 66 66 ARG HG2 H 1 1.52 0.02 . 1 . . . . . . . . 4154 1 631 . 1 1 66 66 ARG HG3 H 1 1.52 0.02 . 1 . . . . . . . . 4154 1 632 . 1 1 66 66 ARG HD2 H 1 2.99 0.02 . 2 . . . . . . . . 4154 1 633 . 1 1 66 66 ARG HD3 H 1 3.01 0.02 . 2 . . . . . . . . 4154 1 634 . 1 1 66 66 ARG HE H 1 6.74 0.02 . 1 . . . . . . . . 4154 1 635 . 1 1 66 66 ARG C C 13 178.7 0.1 . 1 . . . . . . . . 4154 1 636 . 1 1 66 66 ARG CA C 13 58.7 0.1 . 1 . . . . . . . . 4154 1 637 . 1 1 66 66 ARG CB C 13 28.9 0.1 . 1 . . . . . . . . 4154 1 638 . 1 1 66 66 ARG CG C 13 27.2 0.1 . 1 . . . . . . . . 4154 1 639 . 1 1 66 66 ARG CD C 13 43.0 0.1 . 1 . . . . . . . . 4154 1 640 . 1 1 66 66 ARG N N 15 122.3 0.1 . 1 . . . . . . . . 4154 1 641 . 1 1 67 67 GLU H H 1 8.09 0.02 . 1 . . . . . . . . 4154 1 642 . 1 1 67 67 GLU HA H 1 4.04 0.02 . 1 . . . . . . . . 4154 1 643 . 1 1 67 67 GLU HB2 H 1 1.61 0.02 . 1 . . . . . . . . 4154 1 644 . 1 1 67 67 GLU HB3 H 1 1.61 0.02 . 1 . . . . . . . . 4154 1 645 . 1 1 67 67 GLU HG2 H 1 2.00 0.02 . 1 . . . . . . . . 4154 1 646 . 1 1 67 67 GLU HG3 H 1 2.00 0.02 . 1 . . . . . . . . 4154 1 647 . 1 1 67 67 GLU C C 13 177.3 0.1 . 1 . . . . . . . . 4154 1 648 . 1 1 67 67 GLU CA C 13 59.0 0.1 . 1 . . . . . . . . 4154 1 649 . 1 1 67 67 GLU CB C 13 29.1 0.1 . 1 . . . . . . . . 4154 1 650 . 1 1 67 67 GLU CG C 13 33.5 0.1 . 1 . . . . . . . . 4154 1 651 . 1 1 67 67 GLU N N 15 122.2 0.1 . 1 . . . . . . . . 4154 1 652 . 1 1 68 68 ILE H H 1 8.29 0.02 . 1 . . . . . . . . 4154 1 653 . 1 1 68 68 ILE HA H 1 3.40 0.02 . 1 . . . . . . . . 4154 1 654 . 1 1 68 68 ILE HB H 1 1.61 0.02 . 1 . . . . . . . . 4154 1 655 . 1 1 68 68 ILE HG12 H 1 0.92 0.02 . 2 . . . . . . . . 4154 1 656 . 1 1 68 68 ILE HG13 H 1 1.36 0.02 . 2 . . . . . . . . 4154 1 657 . 1 1 68 68 ILE HG21 H 1 0.72 0.02 . 1 . . . . . . . . 4154 1 658 . 1 1 68 68 ILE HG22 H 1 0.72 0.02 . 1 . . . . . . . . 4154 1 659 . 1 1 68 68 ILE HG23 H 1 0.72 0.02 . 1 . . . . . . . . 4154 1 660 . 1 1 68 68 ILE HD11 H 1 0.52 0.02 . 1 . . . . . . . . 4154 1 661 . 1 1 68 68 ILE HD12 H 1 0.52 0.02 . 1 . . . . . . . . 4154 1 662 . 1 1 68 68 ILE HD13 H 1 0.52 0.02 . 1 . . . . . . . . 4154 1 663 . 1 1 68 68 ILE C C 13 178.3 0.1 . 1 . . . . . . . . 4154 1 664 . 1 1 68 68 ILE CA C 13 64.9 0.1 . 1 . . . . . . . . 4154 1 665 . 1 1 68 68 ILE CB C 13 37.4 0.1 . 1 . . . . . . . . 4154 1 666 . 1 1 68 68 ILE CG1 C 13 28.7 0.1 . 1 . . . . . . . . 4154 1 667 . 1 1 68 68 ILE CG2 C 13 16.8 0.1 . 1 . . . . . . . . 4154 1 668 . 1 1 68 68 ILE CD1 C 13 12.1 0.1 . 1 . . . . . . . . 4154 1 669 . 1 1 68 68 ILE N N 15 119.2 0.1 . 1 . . . . . . . . 4154 1 670 . 1 1 69 69 GLY H H 1 7.62 0.02 . 1 . . . . . . . . 4154 1 671 . 1 1 69 69 GLY HA2 H 1 3.62 0.02 . 1 . . . . . . . . 4154 1 672 . 1 1 69 69 GLY HA3 H 1 3.71 0.02 . 1 . . . . . . . . 4154 1 673 . 1 1 69 69 GLY C C 13 176.3 0.1 . 1 . . . . . . . . 4154 1 674 . 1 1 69 69 GLY CA C 13 46.7 0.1 . 1 . . . . . . . . 4154 1 675 . 1 1 69 69 GLY N N 15 105.3 0.1 . 1 . . . . . . . . 4154 1 676 . 1 1 70 70 MET H H 1 7.42 0.02 . 1 . . . . . . . . 4154 1 677 . 1 1 70 70 MET HA H 1 4.37 0.02 . 1 . . . . . . . . 4154 1 678 . 1 1 70 70 MET HE1 H 1 1.86 0.02 . 1 . . . . . . . . 4154 1 679 . 1 1 70 70 MET HE2 H 1 1.86 0.02 . 1 . . . . . . . . 4154 1 680 . 1 1 70 70 MET HE3 H 1 1.86 0.02 . 1 . . . . . . . . 4154 1 681 . 1 1 70 70 MET C C 13 179.3 0.1 . 1 . . . . . . . . 4154 1 682 . 1 1 70 70 MET CE C 13 16.6 0.1 . 1 . . . . . . . . 4154 1 683 . 1 1 70 70 MET N N 15 121.7 0.1 . 1 . . . . . . . . 4154 1 684 . 1 1 71 71 LEU H H 1 8.38 0.02 . 1 . . . . . . . . 4154 1 685 . 1 1 71 71 LEU HD11 H 1 0.71 0.02 . 1 . . . . . . . . 4154 1 686 . 1 1 71 71 LEU HD12 H 1 0.71 0.02 . 1 . . . . . . . . 4154 1 687 . 1 1 71 71 LEU HD13 H 1 0.71 0.02 . 1 . . . . . . . . 4154 1 688 . 1 1 71 71 LEU HD21 H 1 0.41 0.02 . 1 . . . . . . . . 4154 1 689 . 1 1 71 71 LEU HD22 H 1 0.41 0.02 . 1 . . . . . . . . 4154 1 690 . 1 1 71 71 LEU HD23 H 1 0.41 0.02 . 1 . . . . . . . . 4154 1 691 . 1 1 71 71 LEU C C 13 177.3 0.1 . 1 . . . . . . . . 4154 1 692 . 1 1 71 71 LEU CD1 C 13 25.6 0.1 . 1 . . . . . . . . 4154 1 693 . 1 1 71 71 LEU CD2 C 13 23.0 0.1 . 1 . . . . . . . . 4154 1 694 . 1 1 71 71 LEU N N 15 122.7 0.1 . 1 . . . . . . . . 4154 1 695 . 1 1 72 72 GLU H H 1 6.77 0.02 . 1 . . . . . . . . 4154 1 696 . 1 1 72 72 GLU HA H 1 3.83 0.02 . 1 . . . . . . . . 4154 1 697 . 1 1 72 72 GLU HB2 H 1 1.90 0.02 . 1 . . . . . . . . 4154 1 698 . 1 1 72 72 GLU HB3 H 1 1.90 0.02 . 1 . . . . . . . . 4154 1 699 . 1 1 72 72 GLU HG2 H 1 2.13 0.02 . 2 . . . . . . . . 4154 1 700 . 1 1 72 72 GLU HG3 H 1 2.36 0.02 . 2 . . . . . . . . 4154 1 701 . 1 1 72 72 GLU C C 13 177.8 0.1 . 1 . . . . . . . . 4154 1 702 . 1 1 72 72 GLU CA C 13 57.8 0.1 . 1 . . . . . . . . 4154 1 703 . 1 1 72 72 GLU CB C 13 28.9 0.1 . 1 . . . . . . . . 4154 1 704 . 1 1 72 72 GLU CG C 13 36.3 0.1 . 1 . . . . . . . . 4154 1 705 . 1 1 72 72 GLU N N 15 113.8 0.1 . 1 . . . . . . . . 4154 1 706 . 1 1 73 73 CYS H H 1 7.80 0.02 . 1 . . . . . . . . 4154 1 707 . 1 1 73 73 CYS HA H 1 4.49 0.02 . 1 . . . . . . . . 4154 1 708 . 1 1 73 73 CYS HB2 H 1 3.15 0.02 . 1 . . . . . . . . 4154 1 709 . 1 1 73 73 CYS HB3 H 1 2.89 0.02 . 1 . . . . . . . . 4154 1 710 . 1 1 73 73 CYS C C 13 175.3 0.1 . 1 . . . . . . . . 4154 1 711 . 1 1 73 73 CYS CA C 13 54.0 0.1 . 1 . . . . . . . . 4154 1 712 . 1 1 73 73 CYS CB C 13 29.9 0.1 . 1 . . . . . . . . 4154 1 713 . 1 1 73 73 CYS N N 15 115.9 0.1 . 1 . . . . . . . . 4154 1 714 . 1 1 74 74 VAL H H 1 7.11 0.02 . 1 . . . . . . . . 4154 1 715 . 1 1 74 74 VAL HA H 1 4.09 0.02 . 1 . . . . . . . . 4154 1 716 . 1 1 74 74 VAL HB H 1 1.68 0.02 . 1 . . . . . . . . 4154 1 717 . 1 1 74 74 VAL HG11 H 1 0.39 0.02 . 1 . . . . . . . . 4154 1 718 . 1 1 74 74 VAL HG12 H 1 0.39 0.02 . 1 . . . . . . . . 4154 1 719 . 1 1 74 74 VAL HG13 H 1 0.39 0.02 . 1 . . . . . . . . 4154 1 720 . 1 1 74 74 VAL HG21 H 1 0.68 0.02 . 1 . . . . . . . . 4154 1 721 . 1 1 74 74 VAL HG22 H 1 0.68 0.02 . 1 . . . . . . . . 4154 1 722 . 1 1 74 74 VAL HG23 H 1 0.68 0.02 . 1 . . . . . . . . 4154 1 723 . 1 1 74 74 VAL C C 13 176.6 0.1 . 1 . . . . . . . . 4154 1 724 . 1 1 74 74 VAL CA C 13 61.5 0.1 . 1 . . . . . . . . 4154 1 725 . 1 1 74 74 VAL CB C 13 32.9 0.1 . 1 . . . . . . . . 4154 1 726 . 1 1 74 74 VAL CG1 C 13 21.1 0.1 . 1 . . . . . . . . 4154 1 727 . 1 1 74 74 VAL CG2 C 13 17.7 0.1 . 1 . . . . . . . . 4154 1 728 . 1 1 74 74 VAL N N 15 115.8 0.1 . 1 . . . . . . . . 4154 1 729 . 1 1 75 75 THR H H 1 8.16 0.02 . 1 . . . . . . . . 4154 1 730 . 1 1 75 75 THR HA H 1 4.02 0.02 . 1 . . . . . . . . 4154 1 731 . 1 1 75 75 THR HB H 1 3.80 0.02 . 1 . . . . . . . . 4154 1 732 . 1 1 75 75 THR HG21 H 1 0.97 0.02 . 1 . . . . . . . . 4154 1 733 . 1 1 75 75 THR HG22 H 1 0.97 0.02 . 1 . . . . . . . . 4154 1 734 . 1 1 75 75 THR HG23 H 1 0.97 0.02 . 1 . . . . . . . . 4154 1 735 . 1 1 75 75 THR C C 13 176.6 0.1 . 1 . . . . . . . . 4154 1 736 . 1 1 75 75 THR CA C 13 61.9 0.1 . 1 . . . . . . . . 4154 1 737 . 1 1 75 75 THR CB C 13 68.5 0.1 . 1 . . . . . . . . 4154 1 738 . 1 1 75 75 THR CG2 C 13 22.7 0.1 . 1 . . . . . . . . 4154 1 739 . 1 1 75 75 THR N N 15 112.6 0.1 . 1 . . . . . . . . 4154 1 740 . 1 1 76 76 ALA H H 1 7.62 0.02 . 1 . . . . . . . . 4154 1 741 . 1 1 76 76 ALA HA H 1 4.38 0.02 . 1 . . . . . . . . 4154 1 742 . 1 1 76 76 ALA HB1 H 1 1.41 0.02 . 1 . . . . . . . . 4154 1 743 . 1 1 76 76 ALA HB2 H 1 1.41 0.02 . 1 . . . . . . . . 4154 1 744 . 1 1 76 76 ALA HB3 H 1 1.41 0.02 . 1 . . . . . . . . 4154 1 745 . 1 1 76 76 ALA C C 13 175.0 0.1 . 1 . . . . . . . . 4154 1 746 . 1 1 76 76 ALA CA C 13 50.6 0.1 . 1 . . . . . . . . 4154 1 747 . 1 1 76 76 ALA CB C 13 21.0 0.1 . 1 . . . . . . . . 4154 1 748 . 1 1 76 76 ALA N N 15 125.7 0.1 . 1 . . . . . . . . 4154 1 749 . 1 1 77 77 GLU H H 1 7.91 0.02 . 1 . . . . . . . . 4154 1 750 . 1 1 77 77 GLU HA H 1 3.71 0.02 . 1 . . . . . . . . 4154 1 751 . 1 1 77 77 GLU HB2 H 1 1.81 0.02 . 1 . . . . . . . . 4154 1 752 . 1 1 77 77 GLU HB3 H 1 1.58 0.02 . 1 . . . . . . . . 4154 1 753 . 1 1 77 77 GLU HG2 H 1 2.09 0.02 . 1 . . . . . . . . 4154 1 754 . 1 1 77 77 GLU HG3 H 1 2.09 0.02 . 1 . . . . . . . . 4154 1 755 . 1 1 77 77 GLU C C 13 176.5 0.1 . 1 . . . . . . . . 4154 1 756 . 1 1 77 77 GLU CA C 13 57.3 0.1 . 1 . . . . . . . . 4154 1 757 . 1 1 77 77 GLU CB C 13 30.2 0.1 . 1 . . . . . . . . 4154 1 758 . 1 1 77 77 GLU CG C 13 36.1 0.1 . 1 . . . . . . . . 4154 1 759 . 1 1 77 77 GLU N N 15 117.7 0.1 . 1 . . . . . . . . 4154 1 760 . 1 1 78 78 LEU H H 1 8.49 0.02 . 1 . . . . . . . . 4154 1 761 . 1 1 78 78 LEU HA H 1 4.41 0.02 . 1 . . . . . . . . 4154 1 762 . 1 1 78 78 LEU HB2 H 1 1.58 0.02 . 2 . . . . . . . . 4154 1 763 . 1 1 78 78 LEU HB3 H 1 1.18 0.02 . 2 . . . . . . . . 4154 1 764 . 1 1 78 78 LEU HG H 1 1.17 0.02 . 1 . . . . . . . . 4154 1 765 . 1 1 78 78 LEU HD11 H 1 0.82 0.02 . 1 . . . . . . . . 4154 1 766 . 1 1 78 78 LEU HD12 H 1 0.82 0.02 . 1 . . . . . . . . 4154 1 767 . 1 1 78 78 LEU HD13 H 1 0.82 0.02 . 1 . . . . . . . . 4154 1 768 . 1 1 78 78 LEU HD21 H 1 0.67 0.02 . 1 . . . . . . . . 4154 1 769 . 1 1 78 78 LEU HD22 H 1 0.67 0.02 . 1 . . . . . . . . 4154 1 770 . 1 1 78 78 LEU HD23 H 1 0.67 0.02 . 1 . . . . . . . . 4154 1 771 . 1 1 78 78 LEU C C 13 176.0 0.1 . 1 . . . . . . . . 4154 1 772 . 1 1 78 78 LEU CA C 13 54.8 0.1 . 1 . . . . . . . . 4154 1 773 . 1 1 78 78 LEU CB C 13 41.4 0.1 . 1 . . . . . . . . 4154 1 774 . 1 1 78 78 LEU CG C 13 26.1 0.1 . 1 . . . . . . . . 4154 1 775 . 1 1 78 78 LEU CD1 C 13 22.8 0.1 . 1 . . . . . . . . 4154 1 776 . 1 1 78 78 LEU CD2 C 13 25.4 0.1 . 1 . . . . . . . . 4154 1 777 . 1 1 78 78 LEU N N 15 131.1 0.1 . 1 . . . . . . . . 4154 1 778 . 1 1 79 79 LYS H H 1 9.71 0.02 . 1 . . . . . . . . 4154 1 779 . 1 1 79 79 LYS HA H 1 4.80 0.02 . 1 . . . . . . . . 4154 1 780 . 1 1 79 79 LYS HB2 H 1 1.73 0.02 . 1 . . . . . . . . 4154 1 781 . 1 1 79 79 LYS HB3 H 1 1.58 0.02 . 1 . . . . . . . . 4154 1 782 . 1 1 79 79 LYS HG2 H 1 0.93 0.02 . 2 . . . . . . . . 4154 1 783 . 1 1 79 79 LYS HG3 H 1 2.14 0.02 . 2 . . . . . . . . 4154 1 784 . 1 1 79 79 LYS HD2 H 1 1.07 0.02 . 2 . . . . . . . . 4154 1 785 . 1 1 79 79 LYS HD3 H 1 0.43 0.02 . 2 . . . . . . . . 4154 1 786 . 1 1 79 79 LYS HE2 H 1 2.57 0.02 . 2 . . . . . . . . 4154 1 787 . 1 1 79 79 LYS HE3 H 1 2.51 0.02 . 2 . . . . . . . . 4154 1 788 . 1 1 79 79 LYS CA C 13 54.3 0.1 . 1 . . . . . . . . 4154 1 789 . 1 1 79 79 LYS CB C 13 34.1 0.1 . 1 . . . . . . . . 4154 1 790 . 1 1 79 79 LYS CD C 13 28.4 0.1 . 1 . . . . . . . . 4154 1 791 . 1 1 79 79 LYS CE C 13 41.5 0.1 . 1 . . . . . . . . 4154 1 792 . 1 1 79 79 LYS N N 15 130.5 0.1 . 1 . . . . . . . . 4154 1 793 . 1 1 80 80 PRO HA H 1 4.24 0.02 . 1 . . . . . . . . 4154 1 794 . 1 1 80 80 PRO HB2 H 1 2.28 0.02 . 2 . . . . . . . . 4154 1 795 . 1 1 80 80 PRO HB3 H 1 1.76 0.02 . 2 . . . . . . . . 4154 1 796 . 1 1 80 80 PRO HG2 H 1 1.93 0.02 . 2 . . . . . . . . 4154 1 797 . 1 1 80 80 PRO HG3 H 1 2.14 0.02 . 2 . . . . . . . . 4154 1 798 . 1 1 80 80 PRO HD2 H 1 3.70 0.02 . 1 . . . . . . . . 4154 1 799 . 1 1 80 80 PRO HD3 H 1 3.52 0.02 . 1 . . . . . . . . 4154 1 800 . 1 1 80 80 PRO C C 13 176.7 0.1 . 1 . . . . . . . . 4154 1 801 . 1 1 80 80 PRO CA C 13 64.8 0.1 . 1 . . . . . . . . 4154 1 802 . 1 1 80 80 PRO CB C 13 31.5 0.1 . 1 . . . . . . . . 4154 1 803 . 1 1 80 80 PRO CG C 13 28.0 0.1 . 1 . . . . . . . . 4154 1 804 . 1 1 80 80 PRO CD C 13 50.4 0.1 . 1 . . . . . . . . 4154 1 805 . 1 1 81 81 ASN H H 1 8.62 0.02 . 1 . . . . . . . . 4154 1 806 . 1 1 81 81 ASN HA H 1 4.68 0.02 . 1 . . . . . . . . 4154 1 807 . 1 1 81 81 ASN HB2 H 1 2.58 0.02 . 1 . . . . . . . . 4154 1 808 . 1 1 81 81 ASN HB3 H 1 3.51 0.02 . 1 . . . . . . . . 4154 1 809 . 1 1 81 81 ASN HD21 H 1 7.45 0.02 . 1 . . . . . . . . 4154 1 810 . 1 1 81 81 ASN HD22 H 1 6.54 0.02 . 1 . . . . . . . . 4154 1 811 . 1 1 81 81 ASN C C 13 175.0 0.1 . 1 . . . . . . . . 4154 1 812 . 1 1 81 81 ASN CA C 13 51.3 0.1 . 1 . . . . . . . . 4154 1 813 . 1 1 81 81 ASN CB C 13 34.9 0.1 . 1 . . . . . . . . 4154 1 814 . 1 1 81 81 ASN CG C 13 178.6 0.1 . 1 . . . . . . . . 4154 1 815 . 1 1 81 81 ASN N N 15 110.9 0.1 . 1 . . . . . . . . 4154 1 816 . 1 1 81 81 ASN ND2 N 15 112.9 0.1 . 1 . . . . . . . . 4154 1 817 . 1 1 82 82 SER H H 1 7.98 0.02 . 1 . . . . . . . . 4154 1 818 . 1 1 82 82 SER HA H 1 5.03 0.02 . 1 . . . . . . . . 4154 1 819 . 1 1 82 82 SER HB2 H 1 3.98 0.02 . 1 . . . . . . . . 4154 1 820 . 1 1 82 82 SER HB3 H 1 3.90 0.02 . 1 . . . . . . . . 4154 1 821 . 1 1 82 82 SER HG H 1 10.10 0.02 . 1 . . . . . . . . 4154 1 822 . 1 1 82 82 SER C C 13 174.2 0.1 . 1 . . . . . . . . 4154 1 823 . 1 1 82 82 SER CA C 13 61.9 0.1 . 1 . . . . . . . . 4154 1 824 . 1 1 82 82 SER CB C 13 64.0 0.1 . 1 . . . . . . . . 4154 1 825 . 1 1 82 82 SER N N 15 122.0 0.1 . 1 . . . . . . . . 4154 1 826 . 1 1 83 83 ARG H H 1 9.37 0.02 . 1 . . . . . . . . 4154 1 827 . 1 1 83 83 ARG HA H 1 4.65 0.02 . 1 . . . . . . . . 4154 1 828 . 1 1 83 83 ARG HB2 H 1 1.57 0.02 . 1 . . . . . . . . 4154 1 829 . 1 1 83 83 ARG HB3 H 1 1.05 0.02 . 1 . . . . . . . . 4154 1 830 . 1 1 83 83 ARG HG2 H 1 1.56 0.02 . 2 . . . . . . . . 4154 1 831 . 1 1 83 83 ARG HG3 H 1 1.22 0.02 . 2 . . . . . . . . 4154 1 832 . 1 1 83 83 ARG HD2 H 1 3.39 0.02 . 2 . . . . . . . . 4154 1 833 . 1 1 83 83 ARG HD3 H 1 3.08 0.02 . 2 . . . . . . . . 4154 1 834 . 1 1 83 83 ARG HE H 1 10.29 0.02 . 1 . . . . . . . . 4154 1 835 . 1 1 83 83 ARG HH11 H 1 8.37 0.02 . 1 . . . . . . . . 4154 1 836 . 1 1 83 83 ARG HH12 H 1 8.37 0.02 . 1 . . . . . . . . 4154 1 837 . 1 1 83 83 ARG HH21 H 1 5.50 0.02 . 1 . . . . . . . . 4154 1 838 . 1 1 83 83 ARG HH22 H 1 5.50 0.02 . 1 . . . . . . . . 4154 1 839 . 1 1 83 83 ARG CA C 13 51.5 0.1 . 1 . . . . . . . . 4154 1 840 . 1 1 83 83 ARG CB C 13 34.2 0.1 . 1 . . . . . . . . 4154 1 841 . 1 1 83 83 ARG CD C 13 38.8 0.1 . 1 . . . . . . . . 4154 1 842 . 1 1 83 83 ARG N N 15 121.4 0.1 . 1 . . . . . . . . 4154 1 843 . 1 1 83 83 ARG NE N 15 85.6 0.1 . 1 . . . . . . . . 4154 1 844 . 1 1 87 87 GLN C C 13 180.6 0.1 . 1 . . . . . . . . 4154 1 845 . 1 1 88 88 ILE H H 1 6.84 0.02 . 1 . . . . . . . . 4154 1 846 . 1 1 88 88 ILE HA H 1 3.88 0.02 . 1 . . . . . . . . 4154 1 847 . 1 1 88 88 ILE HB H 1 1.56 0.02 . 1 . . . . . . . . 4154 1 848 . 1 1 88 88 ILE HG12 H 1 0.64 0.02 . 2 . . . . . . . . 4154 1 849 . 1 1 88 88 ILE HG13 H 1 1.34 0.02 . 2 . . . . . . . . 4154 1 850 . 1 1 88 88 ILE HG21 H 1 0.47 0.02 . 1 . . . . . . . . 4154 1 851 . 1 1 88 88 ILE HG22 H 1 0.47 0.02 . 1 . . . . . . . . 4154 1 852 . 1 1 88 88 ILE HG23 H 1 0.47 0.02 . 1 . . . . . . . . 4154 1 853 . 1 1 88 88 ILE HD11 H 1 0.35 0.02 . 1 . . . . . . . . 4154 1 854 . 1 1 88 88 ILE HD12 H 1 0.35 0.02 . 1 . . . . . . . . 4154 1 855 . 1 1 88 88 ILE HD13 H 1 0.35 0.02 . 1 . . . . . . . . 4154 1 856 . 1 1 88 88 ILE C C 13 172.4 0.1 . 1 . . . . . . . . 4154 1 857 . 1 1 88 88 ILE CA C 13 60.6 0.1 . 1 . . . . . . . . 4154 1 858 . 1 1 88 88 ILE CB C 13 38.1 0.1 . 1 . . . . . . . . 4154 1 859 . 1 1 88 88 ILE CG2 C 13 17.1 0.1 . 1 . . . . . . . . 4154 1 860 . 1 1 88 88 ILE CD1 C 13 13.8 0.1 . 1 . . . . . . . . 4154 1 861 . 1 1 88 88 ILE N N 15 120.2 0.1 . 1 . . . . . . . . 4154 1 862 . 1 1 89 89 ILE H H 1 8.37 0.02 . 1 . . . . . . . . 4154 1 863 . 1 1 89 89 ILE HA H 1 3.63 0.02 . 1 . . . . . . . . 4154 1 864 . 1 1 89 89 ILE HB H 1 1.60 0.02 . 1 . . . . . . . . 4154 1 865 . 1 1 89 89 ILE HG12 H 1 1.08 0.02 . 2 . . . . . . . . 4154 1 866 . 1 1 89 89 ILE HG13 H 1 1.12 0.02 . 2 . . . . . . . . 4154 1 867 . 1 1 89 89 ILE HG21 H 1 0.49 0.02 . 1 . . . . . . . . 4154 1 868 . 1 1 89 89 ILE HG22 H 1 0.49 0.02 . 1 . . . . . . . . 4154 1 869 . 1 1 89 89 ILE HG23 H 1 0.49 0.02 . 1 . . . . . . . . 4154 1 870 . 1 1 89 89 ILE HD11 H 1 0.33 0.02 . 1 . . . . . . . . 4154 1 871 . 1 1 89 89 ILE HD12 H 1 0.33 0.02 . 1 . . . . . . . . 4154 1 872 . 1 1 89 89 ILE HD13 H 1 0.33 0.02 . 1 . . . . . . . . 4154 1 873 . 1 1 89 89 ILE C C 13 175.1 0.1 . 1 . . . . . . . . 4154 1 874 . 1 1 89 89 ILE CA C 13 58.0 0.1 . 1 . . . . . . . . 4154 1 875 . 1 1 89 89 ILE CB C 13 36.2 0.1 . 1 . . . . . . . . 4154 1 876 . 1 1 89 89 ILE CG2 C 13 17.4 0.1 . 1 . . . . . . . . 4154 1 877 . 1 1 89 89 ILE CD1 C 13 9.3 0.1 . 1 . . . . . . . . 4154 1 878 . 1 1 89 89 ILE N N 15 129.1 0.1 . 1 . . . . . . . . 4154 1 879 . 1 1 90 90 MET H H 1 8.12 0.02 . 1 . . . . . . . . 4154 1 880 . 1 1 90 90 MET HA H 1 4.26 0.02 . 1 . . . . . . . . 4154 1 881 . 1 1 90 90 MET HB2 H 1 2.12 0.02 . 1 . . . . . . . . 4154 1 882 . 1 1 90 90 MET HB3 H 1 1.58 0.02 . 1 . . . . . . . . 4154 1 883 . 1 1 90 90 MET HG2 H 1 2.20 0.02 . 1 . . . . . . . . 4154 1 884 . 1 1 90 90 MET HG3 H 1 2.20 0.02 . 1 . . . . . . . . 4154 1 885 . 1 1 90 90 MET HE1 H 1 1.54 0.02 . 1 . . . . . . . . 4154 1 886 . 1 1 90 90 MET HE2 H 1 1.54 0.02 . 1 . . . . . . . . 4154 1 887 . 1 1 90 90 MET HE3 H 1 1.54 0.02 . 1 . . . . . . . . 4154 1 888 . 1 1 90 90 MET C C 13 175.3 0.1 . 1 . . . . . . . . 4154 1 889 . 1 1 90 90 MET CA C 13 56.2 0.1 . 1 . . . . . . . . 4154 1 890 . 1 1 90 90 MET CB C 13 30.8 0.1 . 1 . . . . . . . . 4154 1 891 . 1 1 90 90 MET CG C 13 32.4 0.1 . 1 . . . . . . . . 4154 1 892 . 1 1 90 90 MET CE C 13 18.1 0.1 . 1 . . . . . . . . 4154 1 893 . 1 1 90 90 MET N N 15 126.6 0.1 . 1 . . . . . . . . 4154 1 894 . 1 1 91 91 THR H H 1 7.10 0.02 . 1 . . . . . . . . 4154 1 895 . 1 1 91 91 THR HA H 1 4.53 0.02 . 1 . . . . . . . . 4154 1 896 . 1 1 91 91 THR HB H 1 4.40 0.02 . 1 . . . . . . . . 4154 1 897 . 1 1 91 91 THR HG21 H 1 1.04 0.02 . 1 . . . . . . . . 4154 1 898 . 1 1 91 91 THR HG22 H 1 1.04 0.02 . 1 . . . . . . . . 4154 1 899 . 1 1 91 91 THR HG23 H 1 1.04 0.02 . 1 . . . . . . . . 4154 1 900 . 1 1 91 91 THR CA C 13 58.3 0.1 . 1 . . . . . . . . 4154 1 901 . 1 1 91 91 THR CB C 13 69.7 0.1 . 1 . . . . . . . . 4154 1 902 . 1 1 91 91 THR CG2 C 13 21.2 0.1 . 1 . . . . . . . . 4154 1 903 . 1 1 91 91 THR N N 15 116.7 0.1 . 1 . . . . . . . . 4154 1 904 . 1 1 92 92 PRO HA H 1 4.28 0.02 . 1 . . . . . . . . 4154 1 905 . 1 1 92 92 PRO HB2 H 1 1.67 0.02 . 2 . . . . . . . . 4154 1 906 . 1 1 92 92 PRO HB3 H 1 2.24 0.02 . 2 . . . . . . . . 4154 1 907 . 1 1 92 92 PRO HG2 H 1 1.90 0.02 . 1 . . . . . . . . 4154 1 908 . 1 1 92 92 PRO HG3 H 1 1.90 0.02 . 1 . . . . . . . . 4154 1 909 . 1 1 92 92 PRO HD2 H 1 3.64 0.02 . 2 . . . . . . . . 4154 1 910 . 1 1 92 92 PRO HD3 H 1 3.61 0.02 . 2 . . . . . . . . 4154 1 911 . 1 1 92 92 PRO C C 13 179.4 0.1 . 1 . . . . . . . . 4154 1 912 . 1 1 92 92 PRO CA C 13 64.8 0.1 . 1 . . . . . . . . 4154 1 913 . 1 1 92 92 PRO CB C 13 31.4 0.1 . 1 . . . . . . . . 4154 1 914 . 1 1 92 92 PRO CG C 13 27.8 0.1 . 1 . . . . . . . . 4154 1 915 . 1 1 92 92 PRO CD C 13 50.4 0.1 . 1 . . . . . . . . 4154 1 916 . 1 1 93 93 GLU H H 1 8.13 0.02 . 1 . . . . . . . . 4154 1 917 . 1 1 93 93 GLU HA H 1 3.92 0.02 . 1 . . . . . . . . 4154 1 918 . 1 1 93 93 GLU HB2 H 1 1.81 0.02 . 2 . . . . . . . . 4154 1 919 . 1 1 93 93 GLU HB3 H 1 1.82 0.02 . 2 . . . . . . . . 4154 1 920 . 1 1 93 93 GLU HG2 H 1 2.14 0.02 . 2 . . . . . . . . 4154 1 921 . 1 1 93 93 GLU HG3 H 1 2.26 0.02 . 2 . . . . . . . . 4154 1 922 . 1 1 93 93 GLU C C 13 177.5 0.1 . 1 . . . . . . . . 4154 1 923 . 1 1 93 93 GLU CA C 13 58.8 0.1 . 1 . . . . . . . . 4154 1 924 . 1 1 93 93 GLU CB C 13 28.9 0.1 . 1 . . . . . . . . 4154 1 925 . 1 1 93 93 GLU CG C 13 37.1 0.1 . 1 . . . . . . . . 4154 1 926 . 1 1 93 93 GLU N N 15 117.0 0.1 . 1 . . . . . . . . 4154 1 927 . 1 1 94 94 LEU H H 1 7.56 0.02 . 1 . . . . . . . . 4154 1 928 . 1 1 94 94 LEU HA H 1 4.23 0.02 . 1 . . . . . . . . 4154 1 929 . 1 1 94 94 LEU HB2 H 1 1.39 0.02 . 1 . . . . . . . . 4154 1 930 . 1 1 94 94 LEU HB3 H 1 1.88 0.02 . 1 . . . . . . . . 4154 1 931 . 1 1 94 94 LEU HG H 1 1.57 0.02 . 1 . . . . . . . . 4154 1 932 . 1 1 94 94 LEU HD11 H 1 0.78 0.02 . 1 . . . . . . . . 4154 1 933 . 1 1 94 94 LEU HD12 H 1 0.78 0.02 . 1 . . . . . . . . 4154 1 934 . 1 1 94 94 LEU HD13 H 1 0.78 0.02 . 1 . . . . . . . . 4154 1 935 . 1 1 94 94 LEU HD21 H 1 0.61 0.02 . 1 . . . . . . . . 4154 1 936 . 1 1 94 94 LEU HD22 H 1 0.61 0.02 . 1 . . . . . . . . 4154 1 937 . 1 1 94 94 LEU HD23 H 1 0.61 0.02 . 1 . . . . . . . . 4154 1 938 . 1 1 94 94 LEU C C 13 174.3 0.1 . 1 . . . . . . . . 4154 1 939 . 1 1 94 94 LEU CA C 13 53.2 0.1 . 1 . . . . . . . . 4154 1 940 . 1 1 94 94 LEU CB C 13 41.9 0.1 . 1 . . . . . . . . 4154 1 941 . 1 1 94 94 LEU CG C 13 26.4 0.1 . 1 . . . . . . . . 4154 1 942 . 1 1 94 94 LEU CD1 C 13 25.8 0.1 . 1 . . . . . . . . 4154 1 943 . 1 1 94 94 LEU CD2 C 13 23.5 0.1 . 1 . . . . . . . . 4154 1 944 . 1 1 94 94 LEU N N 15 118.6 0.1 . 1 . . . . . . . . 4154 1 945 . 1 1 95 95 ASP H H 1 6.96 0.02 . 1 . . . . . . . . 4154 1 946 . 1 1 95 95 ASP HA H 1 3.89 0.02 . 1 . . . . . . . . 4154 1 947 . 1 1 95 95 ASP HB2 H 1 2.48 0.02 . 1 . . . . . . . . 4154 1 948 . 1 1 95 95 ASP HB3 H 1 2.74 0.02 . 1 . . . . . . . . 4154 1 949 . 1 1 95 95 ASP C C 13 176.3 0.1 . 1 . . . . . . . . 4154 1 950 . 1 1 95 95 ASP CA C 13 61.1 0.1 . 1 . . . . . . . . 4154 1 951 . 1 1 95 95 ASP CB C 13 42.3 0.1 . 1 . . . . . . . . 4154 1 952 . 1 1 95 95 ASP N N 15 118.1 0.1 . 1 . . . . . . . . 4154 1 953 . 1 1 96 96 GLY H H 1 9.64 0.02 . 1 . . . . . . . . 4154 1 954 . 1 1 96 96 GLY HA2 H 1 4.02 0.02 . 1 . . . . . . . . 4154 1 955 . 1 1 96 96 GLY HA3 H 1 2.82 0.02 . 1 . . . . . . . . 4154 1 956 . 1 1 96 96 GLY C C 13 171.8 0.1 . 1 . . . . . . . . 4154 1 957 . 1 1 96 96 GLY CA C 13 44.2 0.1 . 1 . . . . . . . . 4154 1 958 . 1 1 96 96 GLY N N 15 118.6 0.1 . 1 . . . . . . . . 4154 1 959 . 1 1 97 97 ILE H H 1 7.77 0.02 . 1 . . . . . . . . 4154 1 960 . 1 1 97 97 ILE HA H 1 1.03 0.02 . 1 . . . . . . . . 4154 1 961 . 1 1 97 97 ILE HB H 1 1.33 0.02 . 1 . . . . . . . . 4154 1 962 . 1 1 97 97 ILE HG12 H 1 0.53 0.02 . 2 . . . . . . . . 4154 1 963 . 1 1 97 97 ILE HG13 H 1 0.31 0.02 . 2 . . . . . . . . 4154 1 964 . 1 1 97 97 ILE HG21 H 1 0.64 0.02 . 1 . . . . . . . . 4154 1 965 . 1 1 97 97 ILE HG22 H 1 0.64 0.02 . 1 . . . . . . . . 4154 1 966 . 1 1 97 97 ILE HG23 H 1 0.64 0.02 . 1 . . . . . . . . 4154 1 967 . 1 1 97 97 ILE HD11 H 1 0.47 0.02 . 1 . . . . . . . . 4154 1 968 . 1 1 97 97 ILE HD12 H 1 0.47 0.02 . 1 . . . . . . . . 4154 1 969 . 1 1 97 97 ILE HD13 H 1 0.47 0.02 . 1 . . . . . . . . 4154 1 970 . 1 1 97 97 ILE C C 13 169.5 0.1 . 1 . . . . . . . . 4154 1 971 . 1 1 97 97 ILE CA C 13 61.1 0.1 . 1 . . . . . . . . 4154 1 972 . 1 1 97 97 ILE CB C 13 37.0 0.1 . 1 . . . . . . . . 4154 1 973 . 1 1 97 97 ILE CG1 C 13 28.9 0.1 . 1 . . . . . . . . 4154 1 974 . 1 1 97 97 ILE CG2 C 13 16.2 0.1 . 1 . . . . . . . . 4154 1 975 . 1 1 97 97 ILE CD1 C 13 14.1 0.1 . 1 . . . . . . . . 4154 1 976 . 1 1 97 97 ILE N N 15 121.6 0.1 . 1 . . . . . . . . 4154 1 977 . 1 1 98 98 VAL H H 1 4.88 0.02 . 1 . . . . . . . . 4154 1 978 . 1 1 98 98 VAL HA H 1 4.48 0.02 . 1 . . . . . . . . 4154 1 979 . 1 1 98 98 VAL HB H 1 1.39 0.02 . 1 . . . . . . . . 4154 1 980 . 1 1 98 98 VAL HG11 H 1 0.60 0.02 . 1 . . . . . . . . 4154 1 981 . 1 1 98 98 VAL HG12 H 1 0.60 0.02 . 1 . . . . . . . . 4154 1 982 . 1 1 98 98 VAL HG13 H 1 0.60 0.02 . 1 . . . . . . . . 4154 1 983 . 1 1 98 98 VAL HG21 H 1 0.74 0.02 . 1 . . . . . . . . 4154 1 984 . 1 1 98 98 VAL HG22 H 1 0.74 0.02 . 1 . . . . . . . . 4154 1 985 . 1 1 98 98 VAL HG23 H 1 0.74 0.02 . 1 . . . . . . . . 4154 1 986 . 1 1 98 98 VAL C C 13 175.1 0.1 . 1 . . . . . . . . 4154 1 987 . 1 1 98 98 VAL CA C 13 59.0 0.1 . 1 . . . . . . . . 4154 1 988 . 1 1 98 98 VAL CB C 13 34.5 0.1 . 1 . . . . . . . . 4154 1 989 . 1 1 98 98 VAL CG1 C 13 21.3 0.1 . 1 . . . . . . . . 4154 1 990 . 1 1 98 98 VAL CG2 C 13 20.2 0.1 . 1 . . . . . . . . 4154 1 991 . 1 1 98 98 VAL N N 15 126.2 0.1 . 1 . . . . . . . . 4154 1 992 . 1 1 99 99 VAL H H 1 8.59 0.02 . 1 . . . . . . . . 4154 1 993 . 1 1 99 99 VAL HA H 1 4.75 0.02 . 1 . . . . . . . . 4154 1 994 . 1 1 99 99 VAL HB H 1 1.48 0.02 . 1 . . . . . . . . 4154 1 995 . 1 1 99 99 VAL HG11 H 1 0.36 0.02 . 1 . . . . . . . . 4154 1 996 . 1 1 99 99 VAL HG12 H 1 0.36 0.02 . 1 . . . . . . . . 4154 1 997 . 1 1 99 99 VAL HG13 H 1 0.36 0.02 . 1 . . . . . . . . 4154 1 998 . 1 1 99 99 VAL HG21 H 1 0.30 0.02 . 1 . . . . . . . . 4154 1 999 . 1 1 99 99 VAL HG22 H 1 0.30 0.02 . 1 . . . . . . . . 4154 1 1000 . 1 1 99 99 VAL HG23 H 1 0.30 0.02 . 1 . . . . . . . . 4154 1 1001 . 1 1 99 99 VAL C C 13 172.5 0.1 . 1 . . . . . . . . 4154 1 1002 . 1 1 99 99 VAL CA C 13 57.3 0.1 . 1 . . . . . . . . 4154 1 1003 . 1 1 99 99 VAL CB C 13 33.7 0.1 . 1 . . . . . . . . 4154 1 1004 . 1 1 99 99 VAL CG1 C 13 22.2 0.1 . 1 . . . . . . . . 4154 1 1005 . 1 1 99 99 VAL CG2 C 13 19.5 0.1 . 1 . . . . . . . . 4154 1 1006 . 1 1 99 99 VAL N N 15 118.5 0.1 . 1 . . . . . . . . 4154 1 1007 . 1 1 100 100 ASP H H 1 8.82 0.02 . 1 . . . . . . . . 4154 1 1008 . 1 1 100 100 ASP HA H 1 5.28 0.02 . 1 . . . . . . . . 4154 1 1009 . 1 1 100 100 ASP HB2 H 1 2.50 0.02 . 1 . . . . . . . . 4154 1 1010 . 1 1 100 100 ASP HB3 H 1 2.50 0.02 . 1 . . . . . . . . 4154 1 1011 . 1 1 100 100 ASP C C 13 174.6 0.1 . 1 . . . . . . . . 4154 1 1012 . 1 1 100 100 ASP CA C 13 52.4 0.1 . 1 . . . . . . . . 4154 1 1013 . 1 1 100 100 ASP CB C 13 42.8 0.1 . 1 . . . . . . . . 4154 1 1014 . 1 1 100 100 ASP N N 15 125.0 0.1 . 1 . . . . . . . . 4154 1 1015 . 1 1 101 101 VAL H H 1 8.96 0.02 . 1 . . . . . . . . 4154 1 1016 . 1 1 101 101 VAL HA H 1 4.23 0.02 . 1 . . . . . . . . 4154 1 1017 . 1 1 101 101 VAL HB H 1 1.88 0.02 . 1 . . . . . . . . 4154 1 1018 . 1 1 101 101 VAL HG11 H 1 0.73 0.02 . 1 . . . . . . . . 4154 1 1019 . 1 1 101 101 VAL HG12 H 1 0.73 0.02 . 1 . . . . . . . . 4154 1 1020 . 1 1 101 101 VAL HG13 H 1 0.73 0.02 . 1 . . . . . . . . 4154 1 1021 . 1 1 101 101 VAL HG21 H 1 0.58 0.02 . 1 . . . . . . . . 4154 1 1022 . 1 1 101 101 VAL HG22 H 1 0.58 0.02 . 1 . . . . . . . . 4154 1 1023 . 1 1 101 101 VAL HG23 H 1 0.58 0.02 . 1 . . . . . . . . 4154 1 1024 . 1 1 101 101 VAL CA C 13 59.0 0.1 . 1 . . . . . . . . 4154 1 1025 . 1 1 101 101 VAL CB C 13 32.9 0.1 . 1 . . . . . . . . 4154 1 1026 . 1 1 101 101 VAL CG1 C 13 22.9 0.1 . 1 . . . . . . . . 4154 1 1027 . 1 1 101 101 VAL CG2 C 13 20.8 0.1 . 1 . . . . . . . . 4154 1 1028 . 1 1 101 101 VAL N N 15 125.0 0.1 . 1 . . . . . . . . 4154 1 1029 . 1 1 102 102 PRO HA H 1 4.50 0.02 . 1 . . . . . . . . 4154 1 1030 . 1 1 102 102 PRO HB2 H 1 2.02 0.02 . 1 . . . . . . . . 4154 1 1031 . 1 1 102 102 PRO HB3 H 1 1.72 0.02 . 1 . . . . . . . . 4154 1 1032 . 1 1 102 102 PRO HG2 H 1 0.70 0.02 . 2 . . . . . . . . 4154 1 1033 . 1 1 102 102 PRO HG3 H 1 1.20 0.02 . 2 . . . . . . . . 4154 1 1034 . 1 1 102 102 PRO HD2 H 1 3.54 0.02 . 2 . . . . . . . . 4154 1 1035 . 1 1 102 102 PRO HD3 H 1 2.73 0.02 . 2 . . . . . . . . 4154 1 1036 . 1 1 102 102 PRO C C 13 176.1 0.1 . 1 . . . . . . . . 4154 1 1037 . 1 1 102 102 PRO CA C 13 61.7 0.1 . 1 . . . . . . . . 4154 1 1038 . 1 1 102 102 PRO CB C 13 31.5 0.1 . 1 . . . . . . . . 4154 1 1039 . 1 1 102 102 PRO CG C 13 25.7 0.1 . 1 . . . . . . . . 4154 1 1040 . 1 1 102 102 PRO CD C 13 51.7 0.1 . 1 . . . . . . . . 4154 1 1041 . 1 1 103 103 ASP H H 1 8.64 0.02 . 1 . . . . . . . . 4154 1 1042 . 1 1 103 103 ASP HA H 1 3.76 0.02 . 1 . . . . . . . . 4154 1 1043 . 1 1 103 103 ASP HB2 H 1 2.60 0.02 . 1 . . . . . . . . 4154 1 1044 . 1 1 103 103 ASP HB3 H 1 2.18 0.02 . 1 . . . . . . . . 4154 1 1045 . 1 1 103 103 ASP C C 13 175.9 0.1 . 1 . . . . . . . . 4154 1 1046 . 1 1 103 103 ASP CA C 13 54.4 0.1 . 1 . . . . . . . . 4154 1 1047 . 1 1 103 103 ASP CB C 13 41.4 0.1 . 1 . . . . . . . . 4154 1 1048 . 1 1 103 103 ASP N N 15 119.4 0.1 . 1 . . . . . . . . 4154 1 1049 . 1 1 104 104 ARG H H 1 6.82 0.02 . 1 . . . . . . . . 4154 1 1050 . 1 1 104 104 ARG HA H 1 4.37 0.02 . 1 . . . . . . . . 4154 1 1051 . 1 1 104 104 ARG HB2 H 1 1.59 0.02 . 2 . . . . . . . . 4154 1 1052 . 1 1 104 104 ARG HB3 H 1 1.66 0.02 . 2 . . . . . . . . 4154 1 1053 . 1 1 104 104 ARG HG2 H 1 1.31 0.02 . 1 . . . . . . . . 4154 1 1054 . 1 1 104 104 ARG HG3 H 1 1.31 0.02 . 1 . . . . . . . . 4154 1 1055 . 1 1 104 104 ARG HD2 H 1 2.78 0.02 . 2 . . . . . . . . 4154 1 1056 . 1 1 104 104 ARG HD3 H 1 2.83 0.02 . 2 . . . . . . . . 4154 1 1057 . 1 1 104 104 ARG HE H 1 7.13 0.02 . 1 . . . . . . . . 4154 1 1058 . 1 1 104 104 ARG C C 13 173.5 0.1 . 1 . . . . . . . . 4154 1 1059 . 1 1 104 104 ARG CA C 13 55.0 0.1 . 1 . . . . . . . . 4154 1 1060 . 1 1 104 104 ARG CB C 13 30.5 0.1 . 1 . . . . . . . . 4154 1 1061 . 1 1 104 104 ARG CG C 13 24.0 0.1 . 1 . . . . . . . . 4154 1 1062 . 1 1 104 104 ARG CD C 13 43.5 0.1 . 1 . . . . . . . . 4154 1 1063 . 1 1 104 104 ARG N N 15 115.1 0.1 . 1 . . . . . . . . 4154 1 1064 . 1 1 104 104 ARG NE N 15 70.0 0.1 . 1 . . . . . . . . 4154 1 1065 . 1 1 105 105 GLN H H 1 8.43 0.02 . 1 . . . . . . . . 4154 1 1066 . 1 1 105 105 GLN HA H 1 4.34 0.02 . 1 . . . . . . . . 4154 1 1067 . 1 1 105 105 GLN HB2 H 1 0.97 0.02 . 1 . . . . . . . . 4154 1 1068 . 1 1 105 105 GLN HB3 H 1 0.97 0.02 . 1 . . . . . . . . 4154 1 1069 . 1 1 105 105 GLN HG2 H 1 2.33 0.02 . 2 . . . . . . . . 4154 1 1070 . 1 1 105 105 GLN HG3 H 1 1.44 0.02 . 2 . . . . . . . . 4154 1 1071 . 1 1 105 105 GLN HE21 H 1 7.31 0.02 . 2 . . . . . . . . 4154 1 1072 . 1 1 105 105 GLN HE22 H 1 6.77 0.02 . 2 . . . . . . . . 4154 1 1073 . 1 1 105 105 GLN C C 13 176.8 0.1 . 1 . . . . . . . . 4154 1 1074 . 1 1 105 105 GLN CA C 13 55.0 0.1 . 1 . . . . . . . . 4154 1 1075 . 1 1 105 105 GLN CB C 13 27.0 0.1 . 1 . . . . . . . . 4154 1 1076 . 1 1 105 105 GLN CD C 13 179.6 0.1 . 1 . . . . . . . . 4154 1 1077 . 1 1 105 105 GLN N N 15 118.5 0.1 . 1 . . . . . . . . 4154 1 1078 . 1 1 105 105 GLN NE2 N 15 113.6 0.1 . 1 . . . . . . . . 4154 1 1079 . 1 1 106 106 TRP H H 1 7.84 0.02 . 1 . . . . . . . . 4154 1 1080 . 1 1 106 106 TRP HA H 1 4.46 0.02 . 1 . . . . . . . . 4154 1 1081 . 1 1 106 106 TRP HB2 H 1 3.32 0.02 . 1 . . . . . . . . 4154 1 1082 . 1 1 106 106 TRP HB3 H 1 2.82 0.02 . 1 . . . . . . . . 4154 1 1083 . 1 1 106 106 TRP HD1 H 1 7.06 0.02 . 1 . . . . . . . . 4154 1 1084 . 1 1 106 106 TRP HE1 H 1 10.04 0.02 . 1 . . . . . . . . 4154 1 1085 . 1 1 106 106 TRP HE3 H 1 7.56 0.02 . 1 . . . . . . . . 4154 1 1086 . 1 1 106 106 TRP HZ2 H 1 7.20 0.02 . 1 . . . . . . . . 4154 1 1087 . 1 1 106 106 TRP HZ3 H 1 6.90 0.02 . 1 . . . . . . . . 4154 1 1088 . 1 1 106 106 TRP HH2 H 1 6.92 0.02 . 1 . . . . . . . . 4154 1 1089 . 1 1 106 106 TRP CA C 13 57.8 0.1 . 1 . . . . . . . . 4154 1 1090 . 1 1 106 106 TRP CB C 13 30.2 0.1 . 1 . . . . . . . . 4154 1 1091 . 1 1 106 106 TRP CD1 C 13 126.5 0.1 . 1 . . . . . . . . 4154 1 1092 . 1 1 106 106 TRP CE3 C 13 138.5 0.1 . 1 . . . . . . . . 4154 1 1093 . 1 1 106 106 TRP CZ2 C 13 114.1 0.1 . 1 . . . . . . . . 4154 1 1094 . 1 1 106 106 TRP CZ3 C 13 132.7 0.1 . 1 . . . . . . . . 4154 1 1095 . 1 1 106 106 TRP CH2 C 13 133.1 0.1 . 1 . . . . . . . . 4154 1 1096 . 1 1 106 106 TRP N N 15 127.0 0.1 . 1 . . . . . . . . 4154 1 1097 . 1 1 106 106 TRP NE1 N 15 126.9 0.1 . 1 . . . . . . . . 4154 1 stop_ save_