data_4107 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4107 _Entry.Title ; Acid Denatured Cold Shock Protein A (CspA) ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 1998-02-16 _Entry.Accession_date 1998-02-17 _Entry.Last_release_date 1998-03-04 _Entry.Original_release_date 1998-03-04 _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 ; NMR assignments for acid denatured (pH 2, temperature = 20 C) cold shock protein A. Residual structure in the acid denatured protein induces aggregation, and eventually fibril formation. NMR experiments aimed at understanding the mechanisms of aggregation & polymerization are in progress. NMR assignments for acid denatured CspA made use of additional data for the acid/urea denatured protein (pH 2.7/ 6M urea), to overcome problems with broad lines in the acid denatured state. The acid & acid/urea denatured forms of the protein are in fast exchange. NMR assignments for the acid/urea denatured protein have been deposited in a separate entry. Denatured (e.g. non-native) protein. ; _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 Andrei Alexandrescu . T. . 4107 2 K. Rathgeb-Szabo . . . 4107 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4107 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 124 4107 '15N chemical shifts' 66 4107 '1H chemical shifts' 270 4107 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 . . 1998-03-04 1998-02-17 original author . 4107 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 4108 'chemical shifts for CspA in the acid/urea denatured state' 4107 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4107 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 98356294 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Alexandrescu, A. T., and Rathgeb-Szabo, K., "NMR Assignments for Acid-Denatured Cold Shock Protein A," J. Biomol. NMR 11, 461-462 (1998). ; _Citation.Title 'NMR Assignments for Acid-Denatured Cold Shock Protein A' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 11 _Citation.Journal_issue 4 _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 461 _Citation.Page_last 462 _Citation.Year 1998 _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 Andrei Alexandrescu . T. . 4107 1 2 K. Rathgeb-Szabo . . . 4107 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID aggregation 4107 1 CspA 4107 1 'fibril formation' 4107 1 'protein folding' 4107 1 stop_ save_ save_citation_one _Citation.Sf_category citations _Citation.Sf_framecode citation_one _Citation.Entry_ID 4107 _Citation.ID 2 _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., Sykes, B. D., "1H, 13C and 15N Chemical Shift Referencing in Biomolecular NMR," 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. . 4107 2 2 'C G' Bigam C. G. . 4107 2 3 J Yao J. . . 4107 2 4 F Abildgaard F. . . 4107 2 5 'H J' Dyson H. J. . 4107 2 6 E Oldfield E. . . 4107 2 7 'J L' Markley J. L. . 4107 2 8 'B D' Sykes B. D. . 4107 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_CspA _Assembly.Sf_category assembly _Assembly.Sf_framecode system_CspA _Assembly.Entry_ID 4107 _Assembly.ID 1 _Assembly.Name CspA _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4107 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 CspA 1 $CspA . . . denatured . . . . . 4107 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1MJC . 'Major Cold Shock Protein 7.4 (Cspa (Cs 7.4)) Of (Escherichia Coli)' . . . . 4107 1 yes PDB 3MEF . 'A Chain A, Major Cold-Shock Protein From Escherichia Coli Solution Nmr Structure' . . . . 4107 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID CspA abbreviation 4107 1 CspA system 4107 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'transcription regulator' 4107 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_CspA _Entity.Sf_category entity _Entity.Sf_framecode CspA _Entity.Entry_ID 4107 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Cold shock protein A' _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 ; MSGKMTGIVKWFNADKGFGF ITPDDGSKDVFVHFSAIQND GYKSLDEGQKVSFTIESGAK GPAAGNVTSL ; _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 70 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 7400 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 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 4108 . "Cold shock protein A" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 2 no BMRB 4296 . "Cold shock protein A" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 3 no PDB 1MJC . "Crystal Structure Of Cspa, The Major Cold Shock Protein Of Escherichia Coli" . . . . . 98.57 69 100.00 100.00 1.89e-40 . . . . 4107 1 4 no PDB 2BH8 . "Combinatorial Protein 1b11" . . . . . 50.00 101 100.00 100.00 5.60e-15 . . . . 4107 1 5 no PDB 2L15 . "Solution Structure Of Cold Shock Protein Cspa Using Combined Nmr And Cs-Rosetta Method" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 6 no PDB 3MEF . "Major Cold-Shock Protein From Escherichia Coli Solution Nmr Structure" . . . . . 97.14 69 100.00 100.00 7.03e-40 . . . . 4107 1 7 no DBJ BAB37864 . "cold shock protein 7.4 [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 8 no DBJ BAE77739 . "major cold shock protein [Escherichia coli str. K12 substr. W3110]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 9 no DBJ BAG79354 . "cold shock protein [Escherichia coli SE11]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 10 no DBJ BAH65698 . "cold shock protein [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 11 no DBJ BAI28199 . "major cold shock protein CspA [Escherichia coli O26:H11 str. 11368]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 12 no EMBL CAD07979 . "cold shock protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 13 no EMBL CAP78016 . "Cold shock protein cspA [Escherichia coli LF82]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 14 no EMBL CAQ33874 . "CspA transcriptional activator [Escherichia coli BL21(DE3)]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 15 no EMBL CAQ91030 . "major cold shock protein [Escherichia fergusonii ATCC 35469]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 16 no EMBL CAR00519 . "major cold shock protein [Escherichia coli IAI1]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 17 no GB AAA23617 . "cold shock protein (cspA) [Escherichia coli]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 18 no GB AAB18533 . "cold regulated [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 19 no GB AAB66357 . "cold shock protein [Salmonella enterica subsp. enterica serovar Typhimurium]" . . . . . 100.00 70 98.57 98.57 7.04e-41 . . . . 4107 1 20 no GB AAB69447 . "cold shock protein [Salmonella enterica subsp. enterica serovar Enteritidis]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 21 no GB AAC06036 . "cold shock protein A [Salmonella enterica subsp. enterica serovar Typhimurium]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 22 no PIR AG0981 . "cold shock protein [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 23 no REF NP_312468 . "major cold shock protein [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 24 no REF NP_418012 . "RNA chaperone and antiterminator, cold-inducible [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 25 no REF NP_458276 . "cold shock protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 26 no REF NP_462550 . "cold shock protein CspA [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 27 no REF NP_709333 . "RNA chaperone/anti-terminator [Shigella flexneri 2a str. 301]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 28 no SP P0A9X9 . "RecName: Full=Cold shock protein CspA; Short=CSP-A; AltName: Full=7.4 kDa cold shock protein; AltName: Full=CS7.4" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 29 no SP P0A9Y0 . "RecName: Full=Cold shock protein CspA; Short=CSP-A; AltName: Full=7.4 kDa cold shock protein; AltName: Full=CS7.4" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 30 no SP P0A9Y1 . "RecName: Full=Cold shock protein CspA; Short=CSP-A; AltName: Full=7.4 kDa cold shock protein; AltName: Full=CS7.4" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 31 no SP P0A9Y2 . "RecName: Full=Cold shock protein CspA; Short=CSP-A; AltName: Full=7.4 kDa cold shock protein; AltName: Full=CS7.4" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 32 no SP P0A9Y3 . "RecName: Full=Cold shock protein CspA; Short=CSP-A; AltName: Full=7.4 kDa cold shock protein; AltName: Full=CS7.4" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4107 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Cold shock protein A' common 4107 1 CspA abbreviation 4107 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 . MET . 4107 1 2 . SER . 4107 1 3 . GLY . 4107 1 4 . LYS . 4107 1 5 . MET . 4107 1 6 . THR . 4107 1 7 . GLY . 4107 1 8 . ILE . 4107 1 9 . VAL . 4107 1 10 . LYS . 4107 1 11 . TRP . 4107 1 12 . PHE . 4107 1 13 . ASN . 4107 1 14 . ALA . 4107 1 15 . ASP . 4107 1 16 . LYS . 4107 1 17 . GLY . 4107 1 18 . PHE . 4107 1 19 . GLY . 4107 1 20 . PHE . 4107 1 21 . ILE . 4107 1 22 . THR . 4107 1 23 . PRO . 4107 1 24 . ASP . 4107 1 25 . ASP . 4107 1 26 . GLY . 4107 1 27 . SER . 4107 1 28 . LYS . 4107 1 29 . ASP . 4107 1 30 . VAL . 4107 1 31 . PHE . 4107 1 32 . VAL . 4107 1 33 . HIS . 4107 1 34 . PHE . 4107 1 35 . SER . 4107 1 36 . ALA . 4107 1 37 . ILE . 4107 1 38 . GLN . 4107 1 39 . ASN . 4107 1 40 . ASP . 4107 1 41 . GLY . 4107 1 42 . TYR . 4107 1 43 . LYS . 4107 1 44 . SER . 4107 1 45 . LEU . 4107 1 46 . ASP . 4107 1 47 . GLU . 4107 1 48 . GLY . 4107 1 49 . GLN . 4107 1 50 . LYS . 4107 1 51 . VAL . 4107 1 52 . SER . 4107 1 53 . PHE . 4107 1 54 . THR . 4107 1 55 . ILE . 4107 1 56 . GLU . 4107 1 57 . SER . 4107 1 58 . GLY . 4107 1 59 . ALA . 4107 1 60 . LYS . 4107 1 61 . GLY . 4107 1 62 . PRO . 4107 1 63 . ALA . 4107 1 64 . ALA . 4107 1 65 . GLY . 4107 1 66 . ASN . 4107 1 67 . VAL . 4107 1 68 . THR . 4107 1 69 . SER . 4107 1 70 . LEU . 4107 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 . MET 1 1 4107 1 . SER 2 2 4107 1 . GLY 3 3 4107 1 . LYS 4 4 4107 1 . MET 5 5 4107 1 . THR 6 6 4107 1 . GLY 7 7 4107 1 . ILE 8 8 4107 1 . VAL 9 9 4107 1 . LYS 10 10 4107 1 . TRP 11 11 4107 1 . PHE 12 12 4107 1 . ASN 13 13 4107 1 . ALA 14 14 4107 1 . ASP 15 15 4107 1 . LYS 16 16 4107 1 . GLY 17 17 4107 1 . PHE 18 18 4107 1 . GLY 19 19 4107 1 . PHE 20 20 4107 1 . ILE 21 21 4107 1 . THR 22 22 4107 1 . PRO 23 23 4107 1 . ASP 24 24 4107 1 . ASP 25 25 4107 1 . GLY 26 26 4107 1 . SER 27 27 4107 1 . LYS 28 28 4107 1 . ASP 29 29 4107 1 . VAL 30 30 4107 1 . PHE 31 31 4107 1 . VAL 32 32 4107 1 . HIS 33 33 4107 1 . PHE 34 34 4107 1 . SER 35 35 4107 1 . ALA 36 36 4107 1 . ILE 37 37 4107 1 . GLN 38 38 4107 1 . ASN 39 39 4107 1 . ASP 40 40 4107 1 . GLY 41 41 4107 1 . TYR 42 42 4107 1 . LYS 43 43 4107 1 . SER 44 44 4107 1 . LEU 45 45 4107 1 . ASP 46 46 4107 1 . GLU 47 47 4107 1 . GLY 48 48 4107 1 . GLN 49 49 4107 1 . LYS 50 50 4107 1 . VAL 51 51 4107 1 . SER 52 52 4107 1 . PHE 53 53 4107 1 . THR 54 54 4107 1 . ILE 55 55 4107 1 . GLU 56 56 4107 1 . SER 57 57 4107 1 . GLY 58 58 4107 1 . ALA 59 59 4107 1 . LYS 60 60 4107 1 . GLY 61 61 4107 1 . PRO 62 62 4107 1 . ALA 63 63 4107 1 . ALA 64 64 4107 1 . GLY 65 65 4107 1 . ASN 66 66 4107 1 . VAL 67 67 4107 1 . THR 68 68 4107 1 . SER 69 69 4107 1 . LEU 70 70 4107 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 4107 _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 $CspA . 562 . . 'Escherichia coli' 'E. coli' . . Eubacteria . Escherichia coli . . . . . . . . . . . . . . . . . . . . . 4107 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 4107 _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 $CspA . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21(DE3) . . . . . . . . . . . . plasmid . . pET11-cspA . . . ; synthetic (Clone is a gift from M. Inouye, Rutgers University: Reference - S. Chatterjee, W. Jiang, S.D. Emerson, M. Inouye, "The Backbone Structure of the Major Cold-Shock Protein CS7.4 of Escherichia coli in Solution Includes Extensive B-sheet Structure", J. Biochem., 114, pp 663-669, (1993).) ; . . 4107 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 4107 _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 'Cold shock protein A' [U-15N] . . 1 $CspA . . 1 . . mM . . . . 4107 1 stop_ save_ save_sample_two _Sample.Sf_category sample _Sample.Sf_framecode sample_two _Sample.Entry_ID 4107 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'Cold shock protein A' [U-15N;U-13C] . . 1 $CspA . . 2 . . mM . . . . 4107 2 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 4107 _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 2.0 0.2 n/a 4107 1 temperature 293 1 K 4107 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_one _NMR_spectrometer.Entry_ID 4107 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model Unity+600 _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4107 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer_one Varian Unity+600 . 600 . . . 4107 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 4107 _Experiment_list.ID 1 _Experiment_list.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 4107 _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 . . . . ppm 0.00 external indirect 0.251449530 . . . 2 $citation_one . . . . 4107 1 H 1 DSS methyl . . . . ppm 0.00 internal direct . . . . . . . . . . 4107 1 N 15 DSS methyl . . . . ppm 0.00 external indirect 0.101329118 . . . 2 $citation_one . . . . 4107 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_one _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_assignment_one _Assigned_chem_shift_list.Entry_ID 4107 _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 . 4107 1 . . 2 $sample_two . 4107 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 2 2 SER CA C 13 57.6 0.4 . 1 . . . . . . . . 4107 1 2 . 1 1 2 2 SER CB C 13 63.2 0.4 . 1 . . . . . . . . 4107 1 3 . 1 1 3 3 GLY H H 1 8.65 0.01 . 1 . . . . . . . . 4107 1 4 . 1 1 3 3 GLY HA2 H 1 3.93 0.01 . 2 . . . . . . . . 4107 1 5 . 1 1 3 3 GLY CA C 13 45.2 0.4 . 1 . . . . . . . . 4107 1 6 . 1 1 3 3 GLY N N 15 109.6 0.1 . 1 . . . . . . . . 4107 1 7 . 1 1 4 4 LYS H H 1 8.31 0.01 . 1 . . . . . . . . 4107 1 8 . 1 1 4 4 LYS HA H 1 4.29 0.01 . 1 . . . . . . . . 4107 1 9 . 1 1 4 4 LYS HB2 H 1 1.71 0.01 . 4 . . . . . . . . 4107 1 10 . 1 1 4 4 LYS HG2 H 1 1.35 0.01 . 4 . . . . . . . . 4107 1 11 . 1 1 4 4 LYS CA C 13 56.3 0.4 . 1 . . . . . . . . 4107 1 12 . 1 1 4 4 LYS CB C 13 33.1 0.4 . 1 . . . . . . . . 4107 1 13 . 1 1 4 4 LYS N N 15 121.3 0.1 . 1 . . . . . . . . 4107 1 14 . 1 1 5 5 MET H H 1 8.47 0.01 . 1 . . . . . . . . 4107 1 15 . 1 1 5 5 MET HA H 1 4.5 0.01 . 1 . . . . . . . . 4107 1 16 . 1 1 5 5 MET HB2 H 1 1.99 0.01 . 2 . . . . . . . . 4107 1 17 . 1 1 5 5 MET HG2 H 1 2.49 0.01 . 2 . . . . . . . . 4107 1 18 . 1 1 5 5 MET CA C 13 55.5 0.4 . 1 . . . . . . . . 4107 1 19 . 1 1 5 5 MET CB C 13 33.1 0.4 . 1 . . . . . . . . 4107 1 20 . 1 1 5 5 MET N N 15 122.2 0.1 . 1 . . . . . . . . 4107 1 21 . 1 1 6 6 THR H H 1 8.1 0.01 . 1 . . . . . . . . 4107 1 22 . 1 1 6 6 THR HA H 1 4.29 0.01 . 4 . . . . . . . . 4107 1 23 . 1 1 6 6 THR HG21 H 1 1.13 0.01 . 1 . . . . . . . . 4107 1 24 . 1 1 6 6 THR HG22 H 1 1.13 0.01 . 1 . . . . . . . . 4107 1 25 . 1 1 6 6 THR HG23 H 1 1.13 0.01 . 1 . . . . . . . . 4107 1 26 . 1 1 6 6 THR CA C 13 61.9 0.4 . 1 . . . . . . . . 4107 1 27 . 1 1 6 6 THR CB C 13 70.1 0.4 . 1 . . . . . . . . 4107 1 28 . 1 1 6 6 THR N N 15 115.6 0.1 . 1 . . . . . . . . 4107 1 29 . 1 1 7 7 GLY H H 1 8.34 0.01 . 1 . . . . . . . . 4107 1 30 . 1 1 7 7 GLY HA2 H 1 3.86 0.01 . 2 . . . . . . . . 4107 1 31 . 1 1 7 7 GLY CA C 13 45.2 0.4 . 1 . . . . . . . . 4107 1 32 . 1 1 7 7 GLY N N 15 111.1 0.1 . 1 . . . . . . . . 4107 1 33 . 1 1 8 8 ILE H H 1 7.94 0.01 . 1 . . . . . . . . 4107 1 34 . 1 1 8 8 ILE HA H 1 4.07 0.01 . 1 . . . . . . . . 4107 1 35 . 1 1 8 8 ILE HB H 1 1.78 0.01 . 1 . . . . . . . . 4107 1 36 . 1 1 8 8 ILE HG21 H 1 0.78 0.01 . 1 . . . . . . . . 4107 1 37 . 1 1 8 8 ILE HG22 H 1 0.78 0.01 . 1 . . . . . . . . 4107 1 38 . 1 1 8 8 ILE HG23 H 1 0.78 0.01 . 1 . . . . . . . . 4107 1 39 . 1 1 8 8 ILE HD11 H 1 1.06 0.01 . 1 . . . . . . . . 4107 1 40 . 1 1 8 8 ILE HD12 H 1 1.06 0.01 . 1 . . . . . . . . 4107 1 41 . 1 1 8 8 ILE HD13 H 1 1.06 0.01 . 1 . . . . . . . . 4107 1 42 . 1 1 8 8 ILE CA C 13 61.1 0.4 . 1 . . . . . . . . 4107 1 43 . 1 1 8 8 ILE CB C 13 38.7 0.4 . 1 . . . . . . . . 4107 1 44 . 1 1 8 8 ILE N N 15 120.4 0.1 . 1 . . . . . . . . 4107 1 45 . 1 1 9 9 VAL H H 1 8.13 0.01 . 1 . . . . . . . . 4107 1 46 . 1 1 9 9 VAL HA H 1 3.93 0.01 . 1 . . . . . . . . 4107 1 47 . 1 1 9 9 VAL HB H 1 1.85 0.01 . 1 . . . . . . . . 4107 1 48 . 1 1 9 9 VAL HG11 H 1 0.78 0.01 . 2 . . . . . . . . 4107 1 49 . 1 1 9 9 VAL HG12 H 1 0.78 0.01 . 2 . . . . . . . . 4107 1 50 . 1 1 9 9 VAL HG13 H 1 0.78 0.01 . 2 . . . . . . . . 4107 1 51 . 1 1 9 9 VAL CA C 13 62.4 0.4 . 1 . . . . . . . . 4107 1 52 . 1 1 9 9 VAL CB C 13 32.7 0.4 . 1 . . . . . . . . 4107 1 53 . 1 1 9 9 VAL N N 15 125.2 0.1 . 1 . . . . . . . . 4107 1 54 . 1 1 10 10 LYS H H 1 8.19 0.01 . 1 . . . . . . . . 4107 1 55 . 1 1 10 10 LYS HA H 1 4.14 0.01 . 1 . . . . . . . . 4107 1 56 . 1 1 10 10 LYS HB2 H 1 1.49 0.01 . 4 . . . . . . . . 4107 1 57 . 1 1 10 10 LYS HG2 H 1 1.21 0.01 . 4 . . . . . . . . 4107 1 58 . 1 1 10 10 LYS CA C 13 61.9 0.4 . 1 . . . . . . . . 4107 1 59 . 1 1 10 10 LYS CB C 13 33.1 0.4 . 1 . . . . . . . . 4107 1 60 . 1 1 10 10 LYS N N 15 125.3 0.1 . 1 . . . . . . . . 4107 1 61 . 1 1 11 11 TRP H H 1 7.96 0.01 . 1 . . . . . . . . 4107 1 62 . 1 1 11 11 TRP HA H 1 4.57 0.01 . 1 . . . . . . . . 4107 1 63 . 1 1 11 11 TRP HB2 H 1 3.14 0.01 . 2 . . . . . . . . 4107 1 64 . 1 1 11 11 TRP CA C 13 57.2 0.4 . 1 . . . . . . . . 4107 1 65 . 1 1 11 11 TRP CB C 13 30.1 0.4 . 1 . . . . . . . . 4107 1 66 . 1 1 11 11 TRP N N 15 122.00 0.1 . 1 . . . . . . . . 4107 1 67 . 1 1 12 12 PHE H H 1 7.82 0.01 . 1 . . . . . . . . 4107 1 68 . 1 1 12 12 PHE HA H 1 4.36 0.01 . 1 . . . . . . . . 4107 1 69 . 1 1 12 12 PHE HB2 H 1 2.78 0.01 . 2 . . . . . . . . 4107 1 70 . 1 1 12 12 PHE CA C 13 57.2 0.4 . 1 . . . . . . . . 4107 1 71 . 1 1 12 12 PHE CB C 13 39.6 0.4 . 1 . . . . . . . . 4107 1 72 . 1 1 12 12 PHE N N 15 121.8 0.1 . 1 . . . . . . . . 4107 1 73 . 1 1 13 13 ASN H H 1 8.05 0.01 . 1 . . . . . . . . 4107 1 74 . 1 1 13 13 ASN HA H 1 4.43 0.01 . 1 . . . . . . . . 4107 1 75 . 1 1 13 13 ASN HB2 H 1 2.64 0.01 . 2 . . . . . . . . 4107 1 76 . 1 1 13 13 ASN HB3 H 1 2.49 0.01 . 2 . . . . . . . . 4107 1 77 . 1 1 13 13 ASN CA C 13 52.9 0.4 . 1 . . . . . . . . 4107 1 78 . 1 1 13 13 ASN CB C 13 38.7 0.4 . 1 . . . . . . . . 4107 1 79 . 1 1 13 13 ASN N N 15 120.7 0.1 . 1 . . . . . . . . 4107 1 80 . 1 1 14 14 ALA H H 1 8.08 0.01 . 1 . . . . . . . . 4107 1 81 . 1 1 14 14 ALA HA H 1 4.07 0.01 . 1 . . . . . . . . 4107 1 82 . 1 1 14 14 ALA HB1 H 1 1.28 0.01 . 1 . . . . . . . . 4107 1 83 . 1 1 14 14 ALA HB2 H 1 1.28 0.01 . 1 . . . . . . . . 4107 1 84 . 1 1 14 14 ALA HB3 H 1 1.28 0.01 . 1 . . . . . . . . 4107 1 85 . 1 1 14 14 ALA CB C 13 18.9 0.4 . 1 . . . . . . . . 4107 1 86 . 1 1 14 14 ALA N N 15 124.5 0.1 . 1 . . . . . . . . 4107 1 87 . 1 1 15 15 ASP H H 1 8.21 0.01 . 1 . . . . . . . . 4107 1 88 . 1 1 15 15 ASP HA H 1 4.5 0.01 . 1 . . . . . . . . 4107 1 89 . 1 1 15 15 ASP HB2 H 1 2.78 0.01 . 2 . . . . . . . . 4107 1 90 . 1 1 15 15 ASP CA C 13 52.9 0.4 . 1 . . . . . . . . 4107 1 91 . 1 1 15 15 ASP CB C 13 37.9 0.4 . 1 . . . . . . . . 4107 1 92 . 1 1 15 15 ASP N N 15 117.1 0.1 . 1 . . . . . . . . 4107 1 93 . 1 1 16 16 LYS H H 1 7.99 0.01 . 1 . . . . . . . . 4107 1 94 . 1 1 16 16 LYS HA H 1 4.14 0.01 . 1 . . . . . . . . 4107 1 95 . 1 1 16 16 LYS HB2 H 1 1.64 0.01 . 4 . . . . . . . . 4107 1 96 . 1 1 16 16 LYS HG2 H 1 1.28 0.01 . 4 . . . . . . . . 4107 1 97 . 1 1 16 16 LYS CA C 13 56.3 0.4 . 1 . . . . . . . . 4107 1 98 . 1 1 16 16 LYS N N 15 120.8 0.1 . 1 . . . . . . . . 4107 1 99 . 1 1 17 17 GLY H H 1 8.11 0.01 . 1 . . . . . . . . 4107 1 100 . 1 1 17 17 GLY HA2 H 1 3.78 0.01 . 2 . . . . . . . . 4107 1 101 . 1 1 17 17 GLY CA C 13 45.2 0.4 . 1 . . . . . . . . 4107 1 102 . 1 1 17 17 GLY N N 15 109.00 0.1 . 1 . . . . . . . . 4107 1 103 . 1 1 18 18 PHE H H 1 8.01 0.01 . 1 . . . . . . . . 4107 1 104 . 1 1 18 18 PHE HA H 1 4.5 0.01 . 1 . . . . . . . . 4107 1 105 . 1 1 18 18 PHE HB2 H 1 2.93 0.01 . 2 . . . . . . . . 4107 1 106 . 1 1 18 18 PHE CA C 13 58.1 0.4 . 1 . . . . . . . . 4107 1 107 . 1 1 18 18 PHE CB C 13 39.6 0.4 . 1 . . . . . . . . 4107 1 108 . 1 1 18 18 PHE N N 15 119.8 0.1 . 1 . . . . . . . . 4107 1 109 . 1 1 19 19 GLY H H 1 8.23 0.01 . 1 . . . . . . . . 4107 1 110 . 1 1 19 19 GLY HA2 H 1 3.71 0.01 . 2 . . . . . . . . 4107 1 111 . 1 1 19 19 GLY CA C 13 45.2 0.4 . 1 . . . . . . . . 4107 1 112 . 1 1 19 19 GLY N N 15 110.2 0.1 . 1 . . . . . . . . 4107 1 113 . 1 1 20 20 PHE H H 1 7.88 0.01 . 1 . . . . . . . . 4107 1 114 . 1 1 20 20 PHE HA H 1 4.57 0.01 . 1 . . . . . . . . 4107 1 115 . 1 1 20 20 PHE HB2 H 1 2.93 0.01 . 2 . . . . . . . . 4107 1 116 . 1 1 20 20 PHE CA C 13 58.1 0.4 . 1 . . . . . . . . 4107 1 117 . 1 1 20 20 PHE CB C 13 39.6 0.4 . 1 . . . . . . . . 4107 1 118 . 1 1 20 20 PHE N N 15 119.8 0.1 . 1 . . . . . . . . 4107 1 119 . 1 1 21 21 ILE H H 1 8.03 0.01 . 1 . . . . . . . . 4107 1 120 . 1 1 21 21 ILE HA H 1 4.14 0.01 . 1 . . . . . . . . 4107 1 121 . 1 1 21 21 ILE HB H 1 1.71 0.01 . 1 . . . . . . . . 4107 1 122 . 1 1 21 21 ILE HG21 H 1 0.78 0.01 . 1 . . . . . . . . 4107 1 123 . 1 1 21 21 ILE HG22 H 1 0.78 0.01 . 1 . . . . . . . . 4107 1 124 . 1 1 21 21 ILE HG23 H 1 0.78 0.01 . 1 . . . . . . . . 4107 1 125 . 1 1 21 21 ILE CA C 13 60.6 0.4 . 1 . . . . . . . . 4107 1 126 . 1 1 21 21 ILE CB C 13 39.1 0.4 . 1 . . . . . . . . 4107 1 127 . 1 1 21 21 ILE N N 15 123.1 0.1 . 1 . . . . . . . . 4107 1 128 . 1 1 22 22 THR H H 1 8.16 0.01 . 1 . . . . . . . . 4107 1 129 . 1 1 22 22 THR HA H 1 4.5 0.01 . 4 . . . . . . . . 4107 1 130 . 1 1 22 22 THR HB H 1 4.07 0.01 . 4 . . . . . . . . 4107 1 131 . 1 1 22 22 THR HG21 H 1 1.21 0.01 . 1 . . . . . . . . 4107 1 132 . 1 1 22 22 THR HG22 H 1 1.21 0.01 . 1 . . . . . . . . 4107 1 133 . 1 1 22 22 THR HG23 H 1 1.21 0.01 . 1 . . . . . . . . 4107 1 134 . 1 1 22 22 THR CA C 13 59.8 0.4 . 1 . . . . . . . . 4107 1 135 . 1 1 22 22 THR CB C 13 63.6 0.4 . 1 . . . . . . . . 4107 1 136 . 1 1 22 22 THR N N 15 121.2 0.1 . 1 . . . . . . . . 4107 1 137 . 1 1 24 24 ASP H H 1 8.46 0.01 . 1 . . . . . . . . 4107 1 138 . 1 1 24 24 ASP HA H 1 4.64 0.01 . 1 . . . . . . . . 4107 1 139 . 1 1 24 24 ASP HB2 H 1 2.85 0.01 . 2 . . . . . . . . 4107 1 140 . 1 1 24 24 ASP CA C 13 53.3 0.4 . 1 . . . . . . . . 4107 1 141 . 1 1 24 24 ASP CB C 13 38.3 0.4 . 1 . . . . . . . . 4107 1 142 . 1 1 24 24 ASP N N 15 118.8 0.1 . 1 . . . . . . . . 4107 1 143 . 1 1 25 25 ASP H H 1 8.4 0.01 . 1 . . . . . . . . 4107 1 144 . 1 1 25 25 ASP HA H 1 4.64 0.01 . 1 . . . . . . . . 4107 1 145 . 1 1 25 25 ASP HB2 H 1 2.85 0.01 . 2 . . . . . . . . 4107 1 146 . 1 1 25 25 ASP CA C 13 52.9 0.4 . 1 . . . . . . . . 4107 1 147 . 1 1 25 25 ASP CB C 13 38.3 0.4 . 1 . . . . . . . . 4107 1 148 . 1 1 25 25 ASP N N 15 119.3 0.1 . 1 . . . . . . . . 4107 1 149 . 1 1 26 26 GLY H H 1 8.26 0.01 . 1 . . . . . . . . 4107 1 150 . 1 1 26 26 GLY HA2 H 1 3.86 0.01 . 2 . . . . . . . . 4107 1 151 . 1 1 26 26 GLY CA C 13 45.6 0.4 . 1 . . . . . . . . 4107 1 152 . 1 1 26 26 GLY N N 15 109.1 0.1 . 1 . . . . . . . . 4107 1 153 . 1 1 27 27 SER H H 1 8.05 0.01 . 1 . . . . . . . . 4107 1 154 . 1 1 27 27 SER HA H 1 4.36 0.01 . 1 . . . . . . . . 4107 1 155 . 1 1 27 27 SER HB2 H 1 3.78 0.01 . 2 . . . . . . . . 4107 1 156 . 1 1 27 27 SER CA C 13 58.5 0.4 . 1 . . . . . . . . 4107 1 157 . 1 1 27 27 SER CB C 13 64.1 0.4 . 1 . . . . . . . . 4107 1 158 . 1 1 27 27 SER N N 15 115.5 0.1 . 1 . . . . . . . . 4107 1 159 . 1 1 28 28 LYS H H 1 8.24 0.01 . 1 . . . . . . . . 4107 1 160 . 1 1 28 28 LYS HA H 1 4.21 0.01 . 1 . . . . . . . . 4107 1 161 . 1 1 28 28 LYS HB2 H 1 1.71 0.01 . 4 . . . . . . . . 4107 1 162 . 1 1 28 28 LYS HG2 H 1 1.35 0.01 . 4 . . . . . . . . 4107 1 163 . 1 1 28 28 LYS CA C 13 56.3 0.4 . 1 . . . . . . . . 4107 1 164 . 1 1 28 28 LYS CB C 13 33.1 0.4 . 1 . . . . . . . . 4107 1 165 . 1 1 28 28 LYS N N 15 122.5 0.1 . 1 . . . . . . . . 4107 1 166 . 1 1 29 29 ASP H H 1 8.33 0.01 . 1 . . . . . . . . 4107 1 167 . 1 1 29 29 ASP HA H 1 4.64 0.01 . 1 . . . . . . . . 4107 1 168 . 1 1 29 29 ASP HB2 H 1 2.85 0.01 . 2 . . . . . . . . 4107 1 169 . 1 1 29 29 ASP CA C 13 52.9 0.4 . 1 . . . . . . . . 4107 1 170 . 1 1 29 29 ASP CB C 13 37.9 0.4 . 1 . . . . . . . . 4107 1 171 . 1 1 29 29 ASP N N 15 119.5 0.1 . 1 . . . . . . . . 4107 1 172 . 1 1 30 30 VAL H H 1 7.84 0.01 . 1 . . . . . . . . 4107 1 173 . 1 1 30 30 VAL HA H 1 4.00 0.01 . 1 . . . . . . . . 4107 1 174 . 1 1 30 30 VAL HB H 1 1.92 0.01 . 1 . . . . . . . . 4107 1 175 . 1 1 30 30 VAL HG11 H 1 0.7 0.01 . 2 . . . . . . . . 4107 1 176 . 1 1 30 30 VAL HG12 H 1 0.7 0.01 . 2 . . . . . . . . 4107 1 177 . 1 1 30 30 VAL HG13 H 1 0.7 0.01 . 2 . . . . . . . . 4107 1 178 . 1 1 30 30 VAL CA C 13 62.4 0.4 . 1 . . . . . . . . 4107 1 179 . 1 1 30 30 VAL CB C 13 32.7 0.4 . 1 . . . . . . . . 4107 1 180 . 1 1 30 30 VAL N N 15 120.00 0.1 . 1 . . . . . . . . 4107 1 181 . 1 1 31 31 PHE H H 1 8.15 0.01 . 1 . . . . . . . . 4107 1 182 . 1 1 31 31 PHE HA H 1 4.57 0.01 . 1 . . . . . . . . 4107 1 183 . 1 1 31 31 PHE HB2 H 1 2.93 0.01 . 2 . . . . . . . . 4107 1 184 . 1 1 31 31 PHE CA C 13 57.6 0.4 . 1 . . . . . . . . 4107 1 185 . 1 1 31 31 PHE CB C 13 39.6 0.4 . 1 . . . . . . . . 4107 1 186 . 1 1 31 31 PHE N N 15 123.7 0.1 . 1 . . . . . . . . 4107 1 187 . 1 1 32 32 VAL H H 1 7.89 0.01 . 1 . . . . . . . . 4107 1 188 . 1 1 32 32 VAL HA H 1 3.93 0.01 . 1 . . . . . . . . 4107 1 189 . 1 1 32 32 VAL HB H 1 1.78 0.01 . 1 . . . . . . . . 4107 1 190 . 1 1 32 32 VAL HG11 H 1 0.7 0.01 . 2 . . . . . . . . 4107 1 191 . 1 1 32 32 VAL HG12 H 1 0.7 0.01 . 2 . . . . . . . . 4107 1 192 . 1 1 32 32 VAL HG13 H 1 0.7 0.01 . 2 . . . . . . . . 4107 1 193 . 1 1 32 32 VAL CA C 13 62.4 0.4 . 1 . . . . . . . . 4107 1 194 . 1 1 32 32 VAL CB C 13 33.1 0.4 . 1 . . . . . . . . 4107 1 195 . 1 1 32 32 VAL N N 15 121.8 0.1 . 1 . . . . . . . . 4107 1 196 . 1 1 33 33 HIS H H 1 8.37 0.01 . 1 . . . . . . . . 4107 1 197 . 1 1 33 33 HIS HA H 1 4.57 0.01 . 1 . . . . . . . . 4107 1 198 . 1 1 33 33 HIS HB2 H 1 3.07 0.01 . 2 . . . . . . . . 4107 1 199 . 1 1 33 33 HIS CA C 13 55.00 0.4 . 1 . . . . . . . . 4107 1 200 . 1 1 33 33 HIS CB C 13 29.3 0.4 . 1 . . . . . . . . 4107 1 201 . 1 1 33 33 HIS N N 15 122.00 0.1 . 1 . . . . . . . . 4107 1 202 . 1 1 34 34 PHE H H 1 8.27 0.01 . 1 . . . . . . . . 4107 1 203 . 1 1 34 34 PHE HA H 1 4.57 0.01 . 1 . . . . . . . . 4107 1 204 . 1 1 34 34 PHE HB2 H 1 3.00 0.01 . 2 . . . . . . . . 4107 1 205 . 1 1 34 34 PHE CA C 13 58.1 0.4 . 1 . . . . . . . . 4107 1 206 . 1 1 34 34 PHE CB C 13 40.00 0.4 . 1 . . . . . . . . 4107 1 207 . 1 1 34 34 PHE N N 15 122.7 0.1 . 1 . . . . . . . . 4107 1 208 . 1 1 35 35 SER H H 1 8.2 0.01 . 1 . . . . . . . . 4107 1 209 . 1 1 35 35 SER HA H 1 4.29 0.01 . 1 . . . . . . . . 4107 1 210 . 1 1 35 35 SER HB2 H 1 3.71 0.01 . 2 . . . . . . . . 4107 1 211 . 1 1 35 35 SER CA C 13 58.1 0.4 . 1 . . . . . . . . 4107 1 212 . 1 1 35 35 SER CB C 13 64.1 0.4 . 1 . . . . . . . . 4107 1 213 . 1 1 35 35 SER N N 15 118.00 0.1 . 1 . . . . . . . . 4107 1 214 . 1 1 36 36 ALA H H 1 8.25 0.01 . 1 . . . . . . . . 4107 1 215 . 1 1 36 36 ALA HA H 1 4.21 0.01 . 1 . . . . . . . . 4107 1 216 . 1 1 36 36 ALA HB1 H 1 1.35 0.01 . 1 . . . . . . . . 4107 1 217 . 1 1 36 36 ALA HB2 H 1 1.35 0.01 . 1 . . . . . . . . 4107 1 218 . 1 1 36 36 ALA HB3 H 1 1.35 0.01 . 1 . . . . . . . . 4107 1 219 . 1 1 36 36 ALA CA C 13 52.9 0.4 . 1 . . . . . . . . 4107 1 220 . 1 1 36 36 ALA CB C 13 19.4 0.4 . 1 . . . . . . . . 4107 1 221 . 1 1 36 36 ALA N N 15 126.3 0.1 . 1 . . . . . . . . 4107 1 222 . 1 1 37 37 ILE H H 1 7.93 0.01 . 1 . . . . . . . . 4107 1 223 . 1 1 37 37 ILE HA H 1 4.00 0.01 . 1 . . . . . . . . 4107 1 224 . 1 1 37 37 ILE HB H 1 1.78 0.01 . 1 . . . . . . . . 4107 1 225 . 1 1 37 37 ILE HG21 H 1 0.78 0.01 . 1 . . . . . . . . 4107 1 226 . 1 1 37 37 ILE HG22 H 1 0.78 0.01 . 1 . . . . . . . . 4107 1 227 . 1 1 37 37 ILE HG23 H 1 0.78 0.01 . 1 . . . . . . . . 4107 1 228 . 1 1 37 37 ILE HD11 H 1 1.13 0.01 . 1 . . . . . . . . 4107 1 229 . 1 1 37 37 ILE HD12 H 1 1.13 0.01 . 1 . . . . . . . . 4107 1 230 . 1 1 37 37 ILE HD13 H 1 1.13 0.01 . 1 . . . . . . . . 4107 1 231 . 1 1 37 37 ILE CA C 13 61.5 0.4 . 1 . . . . . . . . 4107 1 232 . 1 1 37 37 ILE CB C 13 38.7 0.4 . 1 . . . . . . . . 4107 1 233 . 1 1 37 37 ILE N N 15 119.3 0.1 . 1 . . . . . . . . 4107 1 234 . 1 1 38 38 GLN H H 1 8.27 0.01 . 1 . . . . . . . . 4107 1 235 . 1 1 38 38 GLN HA H 1 4.21 0.01 . 1 . . . . . . . . 4107 1 236 . 1 1 38 38 GLN HB2 H 1 1.92 0.01 . 2 . . . . . . . . 4107 1 237 . 1 1 38 38 GLN HG2 H 1 2.28 0.01 . 2 . . . . . . . . 4107 1 238 . 1 1 38 38 GLN CA C 13 55.9 0.4 . 1 . . . . . . . . 4107 1 239 . 1 1 38 38 GLN CB C 13 29.3 0.4 . 1 . . . . . . . . 4107 1 240 . 1 1 38 38 GLN N N 15 124.1 0.1 . 1 . . . . . . . . 4107 1 241 . 1 1 39 39 ASN H H 1 8.39 0.01 . 1 . . . . . . . . 4107 1 242 . 1 1 39 39 ASN HA H 1 4.64 0.01 . 1 . . . . . . . . 4107 1 243 . 1 1 39 39 ASN HB2 H 1 2.71 0.01 . 2 . . . . . . . . 4107 1 244 . 1 1 39 39 ASN CA C 13 53.3 0.4 . 1 . . . . . . . . 4107 1 245 . 1 1 39 39 ASN CB C 13 38.7 0.4 . 1 . . . . . . . . 4107 1 246 . 1 1 39 39 ASN N N 15 120.00 0.1 . 1 . . . . . . . . 4107 1 247 . 1 1 40 40 ASP H H 1 8.3 0.01 . 1 . . . . . . . . 4107 1 248 . 1 1 40 40 ASP HA H 1 4.64 0.01 . 1 . . . . . . . . 4107 1 249 . 1 1 40 40 ASP HB2 H 1 2.71 0.01 . 2 . . . . . . . . 4107 1 250 . 1 1 40 40 ASP CA C 13 52.9 0.4 . 1 . . . . . . . . 4107 1 251 . 1 1 40 40 ASP CB C 13 37.9 0.4 . 1 . . . . . . . . 4107 1 252 . 1 1 40 40 ASP N N 15 119.6 0.1 . 1 . . . . . . . . 4107 1 253 . 1 1 41 41 GLY H H 1 8.29 0.01 . 1 . . . . . . . . 4107 1 254 . 1 1 41 41 GLY HA2 H 1 3.78 0.01 . 2 . . . . . . . . 4107 1 255 . 1 1 41 41 GLY CA C 13 45.6 0.4 . 1 . . . . . . . . 4107 1 256 . 1 1 41 41 GLY N N 15 109.00 0.1 . 1 . . . . . . . . 4107 1 257 . 1 1 42 42 TYR H H 1 7.89 0.01 . 1 . . . . . . . . 4107 1 258 . 1 1 42 42 TYR HA H 1 4.43 0.01 . 1 . . . . . . . . 4107 1 259 . 1 1 42 42 TYR HB2 H 1 2.92 0.01 . 2 . . . . . . . . 4107 1 260 . 1 1 42 42 TYR CA C 13 58.1 0.4 . 1 . . . . . . . . 4107 1 261 . 1 1 42 42 TYR CB C 13 38.7 0.4 . 1 . . . . . . . . 4107 1 262 . 1 1 42 42 TYR N N 15 120.1 0.1 . 1 . . . . . . . . 4107 1 263 . 1 1 43 43 LYS H H 1 8.03 0.01 . 1 . . . . . . . . 4107 1 264 . 1 1 43 43 LYS HA H 1 4.21 0.01 . 1 . . . . . . . . 4107 1 265 . 1 1 43 43 LYS HB2 H 1 1.64 0.01 . 4 . . . . . . . . 4107 1 266 . 1 1 43 43 LYS HG2 H 1 1.28 0.01 . 4 . . . . . . . . 4107 1 267 . 1 1 43 43 LYS CA C 13 56.3 0.4 . 1 . . . . . . . . 4107 1 268 . 1 1 43 43 LYS CB C 13 33.1 0.4 . 1 . . . . . . . . 4107 1 269 . 1 1 43 43 LYS N N 15 123.1 0.1 . 1 . . . . . . . . 4107 1 270 . 1 1 44 44 SER H H 1 8.07 0.01 . 1 . . . . . . . . 4107 1 271 . 1 1 44 44 SER HA H 1 4.29 0.01 . 1 . . . . . . . . 4107 1 272 . 1 1 44 44 SER HB2 H 1 3.78 0.01 . 2 . . . . . . . . 4107 1 273 . 1 1 44 44 SER CA C 13 58.5 0.4 . 1 . . . . . . . . 4107 1 274 . 1 1 44 44 SER CB C 13 63.6 0.4 . 1 . . . . . . . . 4107 1 275 . 1 1 44 44 SER N N 15 116.3 0.1 . 1 . . . . . . . . 4107 1 276 . 1 1 45 45 LEU H H 1 8.15 0.01 . 1 . . . . . . . . 4107 1 277 . 1 1 45 45 LEU HA H 1 4.29 0.01 . 1 . . . . . . . . 4107 1 278 . 1 1 45 45 LEU HB2 H 1 1.56 0.01 . 2 . . . . . . . . 4107 1 279 . 1 1 45 45 LEU HD11 H 1 0.78 0.01 . 2 . . . . . . . . 4107 1 280 . 1 1 45 45 LEU HD12 H 1 0.78 0.01 . 2 . . . . . . . . 4107 1 281 . 1 1 45 45 LEU HD13 H 1 0.78 0.01 . 2 . . . . . . . . 4107 1 282 . 1 1 45 45 LEU CA C 13 55.5 0.4 . 1 . . . . . . . . 4107 1 283 . 1 1 45 45 LEU CB C 13 42.2 0.4 . 1 . . . . . . . . 4107 1 284 . 1 1 45 45 LEU N N 15 123.7 0.1 . 1 . . . . . . . . 4107 1 285 . 1 1 46 46 ASP H H 1 8.38 0.01 . 1 . . . . . . . . 4107 1 286 . 1 1 46 46 ASP HA H 1 4.64 0.01 . 1 . . . . . . . . 4107 1 287 . 1 1 46 46 ASP HB2 H 1 2.78 0.01 . 2 . . . . . . . . 4107 1 288 . 1 1 46 46 ASP CA C 13 53.3 0.4 . 1 . . . . . . . . 4107 1 289 . 1 1 46 46 ASP CB C 13 37.9 0.4 . 1 . . . . . . . . 4107 1 290 . 1 1 46 46 ASP N N 15 119.00 0.1 . 1 . . . . . . . . 4107 1 291 . 1 1 47 47 GLU H H 1 8.22 0.01 . 1 . . . . . . . . 4107 1 292 . 1 1 47 47 GLU HA H 1 4.29 0.01 . 1 . . . . . . . . 4107 1 293 . 1 1 47 47 GLU HB2 H 1 2.07 0.01 . 2 . . . . . . . . 4107 1 294 . 1 1 47 47 GLU HB3 H 1 1.92 0.01 . 2 . . . . . . . . 4107 1 295 . 1 1 47 47 GLU HG2 H 1 2.42 0.01 . 2 . . . . . . . . 4107 1 296 . 1 1 47 47 GLU CA C 13 56.3 0.4 . 1 . . . . . . . . 4107 1 297 . 1 1 47 47 GLU CB C 13 28.8 0.4 . 1 . . . . . . . . 4107 1 298 . 1 1 47 47 GLU N N 15 120.6 0.1 . 1 . . . . . . . . 4107 1 299 . 1 1 48 48 GLY H H 1 8.33 0.01 . 1 . . . . . . . . 4107 1 300 . 1 1 48 48 GLY HA2 H 1 3.86 0.01 . 1 . . . . . . . . 4107 1 301 . 1 1 48 48 GLY CA C 13 45.6 0.4 . 1 . . . . . . . . 4107 1 302 . 1 1 48 48 GLY N N 15 109.4 0.1 . 1 . . . . . . . . 4107 1 303 . 1 1 49 49 GLN H H 1 8.08 0.01 . 1 . . . . . . . . 4107 1 304 . 1 1 49 49 GLN HA H 1 4.21 0.01 . 1 . . . . . . . . 4107 1 305 . 1 1 49 49 GLN HB2 H 1 1.92 0.01 . 2 . . . . . . . . 4107 1 306 . 1 1 49 49 GLN HG2 H 1 2.28 0.01 . 2 . . . . . . . . 4107 1 307 . 1 1 49 49 GLN CA C 13 55.9 0.4 . 1 . . . . . . . . 4107 1 308 . 1 1 49 49 GLN CB C 13 29.7 0.4 . 1 . . . . . . . . 4107 1 309 . 1 1 49 49 GLN N N 15 119.8 0.1 . 1 . . . . . . . . 4107 1 310 . 1 1 50 50 LYS H H 1 8.31 0.01 . 1 . . . . . . . . 4107 1 311 . 1 1 50 50 LYS HA H 1 4.29 0.01 . 1 . . . . . . . . 4107 1 312 . 1 1 50 50 LYS HB2 H 1 1.71 0.01 . 4 . . . . . . . . 4107 1 313 . 1 1 50 50 LYS HG2 H 1 1.35 0.01 . 4 . . . . . . . . 4107 1 314 . 1 1 50 50 LYS CA C 13 56.3 0.4 . 1 . . . . . . . . 4107 1 315 . 1 1 50 50 LYS CB C 13 33.1 0.4 . 1 . . . . . . . . 4107 1 316 . 1 1 50 50 LYS N N 15 122.9 0.1 . 1 . . . . . . . . 4107 1 317 . 1 1 51 51 VAL H H 1 8.09 0.01 . 1 . . . . . . . . 4107 1 318 . 1 1 51 51 VAL HA H 1 4.07 0.01 . 1 . . . . . . . . 4107 1 319 . 1 1 51 51 VAL HB H 1 1.92 0.01 . 1 . . . . . . . . 4107 1 320 . 1 1 51 51 VAL HG11 H 1 0.78 0.01 . 2 . . . . . . . . 4107 1 321 . 1 1 51 51 VAL HG12 H 1 0.78 0.01 . 2 . . . . . . . . 4107 1 322 . 1 1 51 51 VAL HG13 H 1 0.78 0.01 . 2 . . . . . . . . 4107 1 323 . 1 1 51 51 VAL CA C 13 62.4 0.4 . 1 . . . . . . . . 4107 1 324 . 1 1 51 51 VAL CB C 13 33.1 0.4 . 1 . . . . . . . . 4107 1 325 . 1 1 51 51 VAL N N 15 121.5 0.1 . 1 . . . . . . . . 4107 1 326 . 1 1 52 52 SER H H 1 8.23 0.01 . 1 . . . . . . . . 4107 1 327 . 1 1 52 52 SER HA H 1 4.36 0.01 . 1 . . . . . . . . 4107 1 328 . 1 1 52 52 SER HB2 H 1 3.71 0.01 . 2 . . . . . . . . 4107 1 329 . 1 1 52 52 SER CA C 13 58.1 0.4 . 1 . . . . . . . . 4107 1 330 . 1 1 52 52 SER CB C 13 64.1 0.4 . 1 . . . . . . . . 4107 1 331 . 1 1 52 52 SER N N 15 119.3 0.1 . 1 . . . . . . . . 4107 1 332 . 1 1 53 53 PHE H H 1 8.19 0.01 . 1 . . . . . . . . 4107 1 333 . 1 1 53 53 PHE HA H 1 4.64 0.01 . 1 . . . . . . . . 4107 1 334 . 1 1 53 53 PHE HB2 H 1 3.00 0.01 . 2 . . . . . . . . 4107 1 335 . 1 1 53 53 PHE CA C 13 57.6 0.4 . 1 . . . . . . . . 4107 1 336 . 1 1 53 53 PHE CB C 13 40.00 0.4 . 1 . . . . . . . . 4107 1 337 . 1 1 53 53 PHE N N 15 122.5 0.1 . 1 . . . . . . . . 4107 1 338 . 1 1 54 54 THR H H 1 8.09 0.01 . 1 . . . . . . . . 4107 1 339 . 1 1 54 54 THR HA H 1 4.29 0.01 . 4 . . . . . . . . 4107 1 340 . 1 1 54 54 THR HB H 1 4.00 0.01 . 4 . . . . . . . . 4107 1 341 . 1 1 54 54 THR HG21 H 1 1.06 0.01 . 1 . . . . . . . . 4107 1 342 . 1 1 54 54 THR HG22 H 1 1.06 0.01 . 1 . . . . . . . . 4107 1 343 . 1 1 54 54 THR HG23 H 1 1.06 0.01 . 1 . . . . . . . . 4107 1 344 . 1 1 54 54 THR CA C 13 61.9 0.4 . 1 . . . . . . . . 4107 1 345 . 1 1 54 54 THR CB C 13 70.1 0.4 . 1 . . . . . . . . 4107 1 346 . 1 1 54 54 THR N N 15 116.6 0.1 . 1 . . . . . . . . 4107 1 347 . 1 1 55 55 ILE H H 1 8.14 0.01 . 1 . . . . . . . . 4107 1 348 . 1 1 55 55 ILE HA H 1 4.07 0.01 . 1 . . . . . . . . 4107 1 349 . 1 1 55 55 ILE HB H 1 1.78 0.01 . 1 . . . . . . . . 4107 1 350 . 1 1 55 55 ILE HG21 H 1 0.85 0.01 . 1 . . . . . . . . 4107 1 351 . 1 1 55 55 ILE HG22 H 1 0.85 0.01 . 1 . . . . . . . . 4107 1 352 . 1 1 55 55 ILE HG23 H 1 0.85 0.01 . 1 . . . . . . . . 4107 1 353 . 1 1 55 55 ILE HD11 H 1 1.12 0.01 . 1 . . . . . . . . 4107 1 354 . 1 1 55 55 ILE HD12 H 1 1.12 0.01 . 1 . . . . . . . . 4107 1 355 . 1 1 55 55 ILE HD13 H 1 1.12 0.01 . 1 . . . . . . . . 4107 1 356 . 1 1 55 55 ILE CA C 13 61.5 0.4 . 1 . . . . . . . . 4107 1 357 . 1 1 55 55 ILE CB C 13 38.7 0.4 . 1 . . . . . . . . 4107 1 358 . 1 1 55 55 ILE N N 15 123.7 0.1 . 1 . . . . . . . . 4107 1 359 . 1 1 56 56 GLU H H 1 8.38 0.01 . 1 . . . . . . . . 4107 1 360 . 1 1 56 56 GLU HA H 1 4.36 0.01 . 1 . . . . . . . . 4107 1 361 . 1 1 56 56 GLU HB2 H 1 2.06 0.01 . 2 . . . . . . . . 4107 1 362 . 1 1 56 56 GLU HB3 H 1 1.92 0.01 . 2 . . . . . . . . 4107 1 363 . 1 1 56 56 GLU HG2 H 1 2.42 0.01 . 2 . . . . . . . . 4107 1 364 . 1 1 56 56 GLU CA C 13 55.9 0.4 . 1 . . . . . . . . 4107 1 365 . 1 1 56 56 GLU CB C 13 28.8 0.4 . 1 . . . . . . . . 4107 1 366 . 1 1 56 56 GLU N N 15 124.6 0.1 . 1 . . . . . . . . 4107 1 367 . 1 1 57 57 SER H H 1 8.3 0.01 . 1 . . . . . . . . 4107 1 368 . 1 1 57 57 SER HA H 1 4.36 0.01 . 1 . . . . . . . . 4107 1 369 . 1 1 57 57 SER HB2 H 1 3.78 0.01 . 2 . . . . . . . . 4107 1 370 . 1 1 57 57 SER CA C 13 58.5 0.4 . 1 . . . . . . . . 4107 1 371 . 1 1 57 57 SER CB C 13 64.1 0.4 . 1 . . . . . . . . 4107 1 372 . 1 1 57 57 SER N N 15 117.3 0.1 . 1 . . . . . . . . 4107 1 373 . 1 1 58 58 GLY H H 1 8.34 0.01 . 1 . . . . . . . . 4107 1 374 . 1 1 58 58 GLY HA2 H 1 3.86 0.01 . 2 . . . . . . . . 4107 1 375 . 1 1 58 58 GLY CA C 13 45.2 0.4 . 1 . . . . . . . . 4107 1 376 . 1 1 58 58 GLY N N 15 111.1 0.1 . 1 . . . . . . . . 4107 1 377 . 1 1 59 59 ALA H H 1 8.05 0.01 . 1 . . . . . . . . 4107 1 378 . 1 1 59 59 ALA HA H 1 4.21 0.01 . 1 . . . . . . . . 4107 1 379 . 1 1 59 59 ALA HB1 H 1 1.35 0.01 . 1 . . . . . . . . 4107 1 380 . 1 1 59 59 ALA HB2 H 1 1.35 0.01 . 1 . . . . . . . . 4107 1 381 . 1 1 59 59 ALA HB3 H 1 1.35 0.01 . 1 . . . . . . . . 4107 1 382 . 1 1 59 59 ALA CA C 13 52.5 0.4 . 1 . . . . . . . . 4107 1 383 . 1 1 59 59 ALA CB C 13 19.4 0.4 . 1 . . . . . . . . 4107 1 384 . 1 1 59 59 ALA N N 15 123.8 0.1 . 1 . . . . . . . . 4107 1 385 . 1 1 60 60 LYS H H 1 8.28 0.01 . 1 . . . . . . . . 4107 1 386 . 1 1 60 60 LYS HA H 1 4.29 0.01 . 1 . . . . . . . . 4107 1 387 . 1 1 60 60 LYS HB2 H 1 1.71 0.01 . 4 . . . . . . . . 4107 1 388 . 1 1 60 60 LYS HG2 H 1 1.42 0.01 . 4 . . . . . . . . 4107 1 389 . 1 1 60 60 LYS CA C 13 56.3 0.4 . 1 . . . . . . . . 4107 1 390 . 1 1 60 60 LYS CB C 13 33.6 0.4 . 1 . . . . . . . . 4107 1 391 . 1 1 60 60 LYS N N 15 120.4 0.1 . 1 . . . . . . . . 4107 1 392 . 1 1 61 61 GLY H H 1 8.13 0.01 . 1 . . . . . . . . 4107 1 393 . 1 1 61 61 GLY HA2 H 1 4.00 0.01 . 2 . . . . . . . . 4107 1 394 . 1 1 61 61 GLY CA C 13 44.7 0.4 . 1 . . . . . . . . 4107 1 395 . 1 1 61 61 GLY N N 15 110.00 0.1 . 1 . . . . . . . . 4107 1 396 . 1 1 62 62 PRO HA H 1 4.36 0.01 . 1 . . . . . . . . 4107 1 397 . 1 1 62 62 PRO CA C 13 63.2 0.4 . 1 . . . . . . . . 4107 1 398 . 1 1 62 62 PRO CB C 13 32.3 0.4 . 1 . . . . . . . . 4107 1 399 . 1 1 63 63 ALA H H 1 8.35 0.01 . 1 . . . . . . . . 4107 1 400 . 1 1 63 63 ALA HA H 1 4.21 0.01 . 1 . . . . . . . . 4107 1 401 . 1 1 63 63 ALA HB1 H 1 1.35 0.01 . 1 . . . . . . . . 4107 1 402 . 1 1 63 63 ALA HB2 H 1 1.35 0.01 . 1 . . . . . . . . 4107 1 403 . 1 1 63 63 ALA HB3 H 1 1.35 0.01 . 1 . . . . . . . . 4107 1 404 . 1 1 63 63 ALA CA C 13 52.5 0.4 . 1 . . . . . . . . 4107 1 405 . 1 1 63 63 ALA CB C 13 19.4 0.4 . 1 . . . . . . . . 4107 1 406 . 1 1 63 63 ALA N N 15 124.3 0.1 . 1 . . . . . . . . 4107 1 407 . 1 1 64 64 ALA H H 1 8.16 0.01 . 1 . . . . . . . . 4107 1 408 . 1 1 64 64 ALA HA H 1 4.21 0.01 . 1 . . . . . . . . 4107 1 409 . 1 1 64 64 ALA HB1 H 1 1.35 0.01 . 1 . . . . . . . . 4107 1 410 . 1 1 64 64 ALA HB2 H 1 1.35 0.01 . 1 . . . . . . . . 4107 1 411 . 1 1 64 64 ALA HB3 H 1 1.35 0.01 . 1 . . . . . . . . 4107 1 412 . 1 1 64 64 ALA CA C 13 52.5 0.4 . 1 . . . . . . . . 4107 1 413 . 1 1 64 64 ALA CB C 13 19.4 0.4 . 1 . . . . . . . . 4107 1 414 . 1 1 64 64 ALA N N 15 123.2 0.1 . 1 . . . . . . . . 4107 1 415 . 1 1 65 65 GLY H H 1 8.22 0.01 . 1 . . . . . . . . 4107 1 416 . 1 1 65 65 GLY HA2 H 1 3.86 0.01 . 2 . . . . . . . . 4107 1 417 . 1 1 65 65 GLY CA C 13 45.2 0.4 . 1 . . . . . . . . 4107 1 418 . 1 1 65 65 GLY N N 15 107.6 0.1 . 1 . . . . . . . . 4107 1 419 . 1 1 66 66 ASN H H 1 8.22 0.01 . 1 . . . . . . . . 4107 1 420 . 1 1 66 66 ASN HA H 1 4.71 0.01 . 1 . . . . . . . . 4107 1 421 . 1 1 66 66 ASN HB2 H 1 2.71 0.01 . 2 . . . . . . . . 4107 1 422 . 1 1 66 66 ASN CA C 13 53.3 0.4 . 1 . . . . . . . . 4107 1 423 . 1 1 66 66 ASN CB C 13 39.1 0.4 . 1 . . . . . . . . 4107 1 424 . 1 1 66 66 ASN N N 15 118.7 0.1 . 1 . . . . . . . . 4107 1 425 . 1 1 67 67 VAL H H 1 8.11 0.01 . 1 . . . . . . . . 4107 1 426 . 1 1 67 67 VAL HA H 1 4.14 0.01 . 1 . . . . . . . . 4107 1 427 . 1 1 67 67 VAL HB H 1 2.07 0.01 . 1 . . . . . . . . 4107 1 428 . 1 1 67 67 VAL HG11 H 1 0.85 0.01 . 2 . . . . . . . . 4107 1 429 . 1 1 67 67 VAL HG12 H 1 0.85 0.01 . 2 . . . . . . . . 4107 1 430 . 1 1 67 67 VAL HG13 H 1 0.85 0.01 . 2 . . . . . . . . 4107 1 431 . 1 1 67 67 VAL CA C 13 62.4 0.4 . 1 . . . . . . . . 4107 1 432 . 1 1 67 67 VAL CB C 13 32.7 0.4 . 1 . . . . . . . . 4107 1 433 . 1 1 67 67 VAL N N 15 120.3 0.1 . 1 . . . . . . . . 4107 1 434 . 1 1 68 68 THR H H 1 8.21 0.01 . 1 . . . . . . . . 4107 1 435 . 1 1 68 68 THR HA H 1 4.14 0.01 . 4 . . . . . . . . 4107 1 436 . 1 1 68 68 THR HB H 1 4.29 0.01 . 4 . . . . . . . . 4107 1 437 . 1 1 68 68 THR HG21 H 1 1.13 0.01 . 1 . . . . . . . . 4107 1 438 . 1 1 68 68 THR HG22 H 1 1.13 0.01 . 1 . . . . . . . . 4107 1 439 . 1 1 68 68 THR HG23 H 1 1.13 0.01 . 1 . . . . . . . . 4107 1 440 . 1 1 68 68 THR CA C 13 61.9 0.4 . 1 . . . . . . . . 4107 1 441 . 1 1 68 68 THR CB C 13 69.7 0.4 . 1 . . . . . . . . 4107 1 442 . 1 1 68 68 THR N N 15 117.9 0.1 . 1 . . . . . . . . 4107 1 443 . 1 1 69 69 SER H H 1 8.2 0.01 . 1 . . . . . . . . 4107 1 444 . 1 1 69 69 SER HA H 1 4.43 0.01 . 1 . . . . . . . . 4107 1 445 . 1 1 69 69 SER HB2 H 1 3.78 0.01 . 2 . . . . . . . . 4107 1 446 . 1 1 69 69 SER CA C 13 58.1 0.4 . 1 . . . . . . . . 4107 1 447 . 1 1 69 69 SER CB C 13 64.1 0.4 . 1 . . . . . . . . 4107 1 448 . 1 1 69 69 SER N N 15 118.5 0.1 . 1 . . . . . . . . 4107 1 449 . 1 1 70 70 LEU H H 1 8.25 0.01 . 1 . . . . . . . . 4107 1 450 . 1 1 70 70 LEU HA H 1 4.36 0.01 . 1 . . . . . . . . 4107 1 451 . 1 1 70 70 LEU HB2 H 1 1.56 0.01 . 2 . . . . . . . . 4107 1 452 . 1 1 70 70 LEU HD11 H 1 0.85 0.01 . 2 . . . . . . . . 4107 1 453 . 1 1 70 70 LEU HD12 H 1 0.85 0.01 . 2 . . . . . . . . 4107 1 454 . 1 1 70 70 LEU HD13 H 1 0.85 0.01 . 2 . . . . . . . . 4107 1 455 . 1 1 70 70 LEU HD21 H 1 0.78 0.01 . 2 . . . . . . . . 4107 1 456 . 1 1 70 70 LEU HD22 H 1 0.78 0.01 . 2 . . . . . . . . 4107 1 457 . 1 1 70 70 LEU HD23 H 1 0.78 0.01 . 2 . . . . . . . . 4107 1 458 . 1 1 70 70 LEU CA C 13 54.2 0.4 . 1 . . . . . . . . 4107 1 459 . 1 1 70 70 LEU CB C 13 42.4 0.4 . 1 . . . . . . . . 4107 1 460 . 1 1 70 70 LEU N N 15 124.6 0.1 . 1 . . . . . . . . 4107 1 stop_ save_