data_4296 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4296 _Entry.Title ; 1H, 13C, and 15N Chemical Shift Assignments for E. coli Cold-shock Protein A (CspA) ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 1999-01-18 _Entry.Accession_date 1999-01-19 _Entry.Last_release_date 1999-02-10 _Entry.Original_release_date 1999-02-10 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Wenqing Feng . . . 4296 2 Roberto Tejero . . . 4296 3 Diane Zimmerman . E. . 4296 4 Masayori Inouye . . . 4296 5 Gaetano Montelione . T. . 4296 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4296 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 449 4296 '13C chemical shifts' 244 4296 '15N chemical shifts' 72 4296 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 . . 1999-02-10 1999-01-18 original author . 4296 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4296 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 98359762 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Feng, W., Tejero, R., Zimmerman, D. E., Inouye, M., and Montelione, G. T., "Solution NMR Structure and Backbone Dynamics of the Major Cold-shock Protein (CspA) from Escherichia coli: Evidence for Conformational Dyanamics in the Single-stranded RNA-binding Site," Biochemistry 37, 10881-10896 (1998). ; _Citation.Title ; Solution NMR Structure and Backbone Dynamics of the Major Cold-shock Protein (CspA) from Escherichia coli: Evidence for Conformational Dyanamics in the Single-stranded RNA-binding Site ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 37 _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 10881 _Citation.Page_last 10896 _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 Wenqing Feng . . . 4296 1 2 Roberto Tejero . . . 4296 1 3 Diane Zimmerman . E. . 4296 1 4 Masayori Inouye . . . 4296 1 5 Gaetano Montelione . T. . 4296 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'RNA-binding protein' 4296 1 'DNA-binding protein' 4296 1 '15N relaxation' 4296 1 'OB fold' 4296 1 'transcriptional regulation' 4296 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4296 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 7515185 _Citation.Full_citation ; Newkirk K., Feng W., Jiang W., Tejero R., Emerson S. D., Inouye M., Montelione G. T., "Solution NMR Structure of the Major Cold Shock Protein (CspA) from Escherichia coli: Identification of a Binding Epitope for DNA," Proc. Natl. Acad. Sci. USA 91, 5114-5118 (1994). ; _Citation.Title 'Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Proc. Natl. Acad. Sci. U.S.A.' _Citation.Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Citation.Journal_volume 91 _Citation.Journal_issue 11 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0027-8424 _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 5114 _Citation.Page_last 5118 _Citation.Year 1994 _Citation.Details ; Sequence-specific 1H and 15N resonance assignments have been determined for the major cold shock protein (CspA) from Escherichia coli with recently developed three-dimensional triple-resonance NMR experiments. By use of these assignments, five antiparallel beta-strands were identified from analysis of NMR data. Strands 1-4 have a classical 3-2-1-4 Greek key beta-sheet topology and there are two beta-bulges, at positions Lys10-Trp11 and Gly65-Asn66. Three-dimensional structures of CspA were generated from NMR data by using simulated annealing with molecular dynamics. The overall chain fold of CspA is a beta-barrel structure, with a tightly packed hydrophobic core. Two-dimensional isotope-edited pulsed-field gradient 15N-1H heteronuclear single-quantum coherence spectroscopy was used to characterize the 15N-1H fingerprint spectrum with and without a 24-base oligodeoxyribonucleotide, 5'-AACGGTTTGACGTACAGACCATTA-3'. Protein-DNA complex formation perturbs a subset of the amide resonances that are located mostly on one face of the CspA molecule. This portion of the CspA molecular surface includes two putative RNA-binding sequence motifs which contribute to an unusual cluster of eight surface aromatic side chains: Trp11, Phe12, Phe18, Phe20, Phe31, His33, Phe34, and Tyr42. These surface aromatic groups, and also residues Lys16, Ser44, and Lys60 located on this same face of CspA, are highly conserved in the family of CspA homologues. These isotope-edited pulsed-field gradient NMR data provide a low-resolution mapping of a DNA-binding epitope on CspA. ; 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 K Newkirk K. . . 4296 2 2 W Feng W. . . 4296 2 3 W Jiang W. . . 4296 2 4 R Tejero R. . . 4296 2 5 'S D' Emerson S. D. . 4296 2 6 M Inouye M. . . 4296 2 7 'G T' Montelione G. T. . 4296 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 4296 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9217263 _Citation.Full_citation 'Zimmerman et al. (1997) J. Mol. Biol. 269, 592 - 610' _Citation.Title 'Automated analysis of protein NMR assignments using methods from artificial intelligence.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 269 _Citation.Journal_issue 4 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0022-2836 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 592 _Citation.Page_last 610 _Citation.Year 1997 _Citation.Details ; An expert system for determining resonance assignments from NMR spectra of proteins is described. Given the amino acid sequence, a two-dimensional 15N-1H heteronuclear correlation spectrum and seven to eight three-dimensional triple-resonance NMR spectra for seven proteins, AUTOASSIGN obtained an average of 98% of sequence-specific spin-system assignments with an error rate of less than 0.5%. Execution times on a Sparc 10 workstation varied from 16 seconds for smaller proteins with simple spectra to one to nine minutes for medium size proteins exhibiting numerous extra spin systems attributed to conformational isomerization. AUTOASSIGN combines symbolic constraint satisfaction methods with a domain-specific knowledge base to exploit the logical structure of the sequential assignment problem, the specific features of the various NMR experiments, and the expected chemical shift frequencies of different amino acids. The current implementation specializes in the analysis of data derived from the most sensitive of the currently available triple-resonance experiments. Potential extensions of the system for analysis of additional types of protein NMR data are also 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 'D E' Zimmerman D. E. . 4296 3 2 'C A' Kulikowski C. A. . 4296 3 3 Y Huang Y. . . 4296 3 4 W Feng W. . . 4296 3 5 M Tashiro M. . . 4296 3 6 S Shimotakahara S. . . 4296 3 7 C Chien C. . . 4296 3 8 R Powers R. . . 4296 3 9 'G T' Montelione G. T. . 4296 3 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_CspA _Assembly.Sf_category assembly _Assembly.Sf_framecode system_CspA _Assembly.Entry_ID 4296 _Assembly.ID 1 _Assembly.Name 'Major cold shock protein from E. coli' _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 momomer 4296 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 monomer' 1 $CspA . . . native . . . . . 4296 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID . PDB 1MJC . 'Major Cold Shock Protein 7.4 (Cspa (Cs 7.4)) Of (Escherichia Coli)' . . . . 4296 1 . PDB 3MEF . 'A Chain A, Major Cold-Shock Protein From Escherichia Coli Solution Nmr Structure' . . . . 4296 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Major cold shock protein from E. coli' system 4296 1 CspA abbreviation 4296 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'single-strand RNA binding protein' 4296 1 'single-strand DNA binding protein' 4296 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_CspA _Entity.Sf_category entity _Entity.Sf_framecode CspA _Entity.Entry_ID 4296 _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 2015-11-24 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 4107 . "Cold shock protein A" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4296 1 2 no BMRB 4108 . "Cold shock protein A" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4296 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 . . . . 4296 1 4 no PDB 2BH8 . "Combinatorial Protein 1b11" . . . . . 50.00 101 100.00 100.00 5.60e-15 . . . . 4296 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 . . . . 4296 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 . . . . 4296 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 . . . . 4296 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 . . . . 4296 1 9 no DBJ BAG79354 . "cold shock protein [Escherichia coli SE11]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4296 1 10 no DBJ BAH65698 . "cold shock protein [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4296 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 . . . . 4296 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 . . . . 4296 1 13 no EMBL CAP78016 . "Cold shock protein cspA [Escherichia coli LF82]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4296 1 14 no EMBL CAQ33874 . "CspA transcriptional activator [Escherichia coli BL21(DE3)]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4296 1 15 no EMBL CAQ91030 . "major cold shock protein [Escherichia fergusonii ATCC 35469]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4296 1 16 no EMBL CAR00519 . "major cold shock protein [Escherichia coli IAI1]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4296 1 17 no GB AAA23617 . "cold shock protein (cspA) [Escherichia coli]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4296 1 18 no GB AAB18533 . "cold regulated [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4296 1 19 no GB AAB66357 . "cold shock protein [Salmonella enterica subsp. enterica serovar Typhimurium]" . . . . . 100.00 70 98.57 98.57 7.04e-41 . . . . 4296 1 20 no GB AAB69447 . "cold shock protein [Salmonella enterica subsp. enterica serovar Enteritidis]" . . . . . 100.00 70 100.00 100.00 1.71e-41 . . . . 4296 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 . . . . 4296 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 . . . . 4296 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 . . . . 4296 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 . . . . 4296 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 . . . . 4296 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 . . . . 4296 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 . . . . 4296 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 . . . . 4296 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 . . . . 4296 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 . . . . 4296 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 . . . . 4296 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 . . . . 4296 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 4296 1 CspA abbreviation 4296 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 . 4296 1 2 . SER . 4296 1 3 . GLY . 4296 1 4 . LYS . 4296 1 5 . MET . 4296 1 6 . THR . 4296 1 7 . GLY . 4296 1 8 . ILE . 4296 1 9 . VAL . 4296 1 10 . LYS . 4296 1 11 . TRP . 4296 1 12 . PHE . 4296 1 13 . ASN . 4296 1 14 . ALA . 4296 1 15 . ASP . 4296 1 16 . LYS . 4296 1 17 . GLY . 4296 1 18 . PHE . 4296 1 19 . GLY . 4296 1 20 . PHE . 4296 1 21 . ILE . 4296 1 22 . THR . 4296 1 23 . PRO . 4296 1 24 . ASP . 4296 1 25 . ASP . 4296 1 26 . GLY . 4296 1 27 . SER . 4296 1 28 . LYS . 4296 1 29 . ASP . 4296 1 30 . VAL . 4296 1 31 . PHE . 4296 1 32 . VAL . 4296 1 33 . HIS . 4296 1 34 . PHE . 4296 1 35 . SER . 4296 1 36 . ALA . 4296 1 37 . ILE . 4296 1 38 . GLN . 4296 1 39 . ASN . 4296 1 40 . ASP . 4296 1 41 . GLY . 4296 1 42 . TYR . 4296 1 43 . LYS . 4296 1 44 . SER . 4296 1 45 . LEU . 4296 1 46 . ASP . 4296 1 47 . GLU . 4296 1 48 . GLY . 4296 1 49 . GLN . 4296 1 50 . LYS . 4296 1 51 . VAL . 4296 1 52 . SER . 4296 1 53 . PHE . 4296 1 54 . THR . 4296 1 55 . ILE . 4296 1 56 . GLU . 4296 1 57 . SER . 4296 1 58 . GLY . 4296 1 59 . ALA . 4296 1 60 . LYS . 4296 1 61 . GLY . 4296 1 62 . PRO . 4296 1 63 . ALA . 4296 1 64 . ALA . 4296 1 65 . GLY . 4296 1 66 . ASN . 4296 1 67 . VAL . 4296 1 68 . THR . 4296 1 69 . SER . 4296 1 70 . LEU . 4296 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 4296 1 . SER 2 2 4296 1 . GLY 3 3 4296 1 . LYS 4 4 4296 1 . MET 5 5 4296 1 . THR 6 6 4296 1 . GLY 7 7 4296 1 . ILE 8 8 4296 1 . VAL 9 9 4296 1 . LYS 10 10 4296 1 . TRP 11 11 4296 1 . PHE 12 12 4296 1 . ASN 13 13 4296 1 . ALA 14 14 4296 1 . ASP 15 15 4296 1 . LYS 16 16 4296 1 . GLY 17 17 4296 1 . PHE 18 18 4296 1 . GLY 19 19 4296 1 . PHE 20 20 4296 1 . ILE 21 21 4296 1 . THR 22 22 4296 1 . PRO 23 23 4296 1 . ASP 24 24 4296 1 . ASP 25 25 4296 1 . GLY 26 26 4296 1 . SER 27 27 4296 1 . LYS 28 28 4296 1 . ASP 29 29 4296 1 . VAL 30 30 4296 1 . PHE 31 31 4296 1 . VAL 32 32 4296 1 . HIS 33 33 4296 1 . PHE 34 34 4296 1 . SER 35 35 4296 1 . ALA 36 36 4296 1 . ILE 37 37 4296 1 . GLN 38 38 4296 1 . ASN 39 39 4296 1 . ASP 40 40 4296 1 . GLY 41 41 4296 1 . TYR 42 42 4296 1 . LYS 43 43 4296 1 . SER 44 44 4296 1 . LEU 45 45 4296 1 . ASP 46 46 4296 1 . GLU 47 47 4296 1 . GLY 48 48 4296 1 . GLN 49 49 4296 1 . LYS 50 50 4296 1 . VAL 51 51 4296 1 . SER 52 52 4296 1 . PHE 53 53 4296 1 . THR 54 54 4296 1 . ILE 55 55 4296 1 . GLU 56 56 4296 1 . SER 57 57 4296 1 . GLY 58 58 4296 1 . ALA 59 59 4296 1 . LYS 60 60 4296 1 . GLY 61 61 4296 1 . PRO 62 62 4296 1 . ALA 63 63 4296 1 . ALA 64 64 4296 1 . GLY 65 65 4296 1 . ASN 66 66 4296 1 . VAL 67 67 4296 1 . THR 68 68 4296 1 . SER 69 69 4296 1 . LEU 70 70 4296 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 4296 _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 . . . . . . . . . . . . cytoplasmic . . . cspA . . . . 4296 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 4296 _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' . . . . . . . . . . . . . . . . . . . . . . . . . . 'Produced using plasmid pET11-CspA in E. coli strain BL21(DE3)' . . 4296 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4296 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details ; Samples were prepared in H2O containing 5% deuterium oxide for locking purposes. Solutions were buffered at pH* 6.0 +/- 0.1. ; _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-98% 13C; U-90% 15N]' . . 1 $CspA . . . 1.0 3.0 mM . . . . 4296 1 2 KH2PO4 . . . . . . . 50 . . mM . . . . 4296 1 3 NaEDTA . . . . . . . 0.1 . . mM . . . . 4296 1 4 NaN3 . . . . . . . 1 . . mM . . . . 4296 1 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_1 _Sample_condition_list.Entry_ID 4296 _Sample_condition_list.ID 1 _Sample_condition_list.Details 'Samples were prepared in 95% H2O, 5% 2H2O' loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH* 6.0 0.1 na 4296 1 temperature 303 0.5 K 4296 1 stop_ save_ ############################ # Computer software used # ############################ save_AutoAssign _Software.Sf_category software _Software.Sf_framecode AutoAssign _Software.Entry_ID 4296 _Software.ID 1 _Software.Name AutoAssign _Software.Version 1.0 _Software.Details ; In-house developed software for automatic analysis of resonance assignments from triple-resonance spectra. ; loop_ _Task.Task _Task.Entry_ID _Task.Software_ID ; automated analysis of backbone N, C, H, and sidechain Cb resonance assignments ; 4296 1 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 3 $ref_2 4296 1 stop_ save_ save_Varian_VNMR _Software.Sf_category software _Software.Sf_framecode Varian_VNMR _Software.Entry_ID 4296 _Software.ID 2 _Software.Name Varian_VNMR _Software.Version 5.3 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Varian Associates' 'Palo Alto, CA' . 4296 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Data collection and processing of 3D Fourier transforms' 4296 2 stop_ save_ save_NMRCompass _Software.Sf_category software _Software.Sf_framecode NMRCompass _Software.Entry_ID 4296 _Software.ID 3 _Software.Name NMRCompass _Software.Version . _Software.Details ; Frequency-domain data generated with VNMR is inport into NMRCompass for automated peak-picking. Peak picking is valadidated by interactive graphics analysis. Peak lists are then input to the AutoAssign software for automated analysis of resonance assignments. ; loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID MSI . . 4296 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Automatic peak pick of frequency-domain 2D and 3D data sets.' 4296 3 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 4296 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model Unity _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4296 _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 Varian Unity . 500 . . . 4296 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 4296 _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 'Most of the triple resonance experiments were exectuted' . . . . . . . . . . . 1 $sample_1 . . . . . . . . . . . . . . . . . . . . . . . . . . 4296 1 2 'with C-H or C-C phase labeling to aid assignments' . . . . . . . . . . . 1 $sample_1 . . . . . . . . . . . . . . . . . . . . . . . . . . 4296 1 3 '[Tashiro et al. J. Biomol. NMR (1995) 6: 211 - 216;' . . . . . . . . . . . 1 $sample_1 . . . . . . . . . . . . . . . . . . . . . . . . . . 4296 1 4 'Feng et al., J. Biomol. NMR (1996) 8, 98 - 104; Rios et al.,' . . . . . . . . . . . 1 $sample_1 . . . . . . . . . . . . . . . . . . . . . . . . . . 4296 1 5 'J. Biomol. NMR (1996) 8, 345 - 350].' . . . . . . . . . . . 1 $sample_1 . . . . . . . . . . . . . . . . . . . . . . . . . . 4296 1 6 HSQC . . . . . . . . . . . 1 $sample_1 . . . . . . . . . . . . . . . . . . . . . . . . . . 4296 1 7 HNCO . . . . . . . . . . . 1 $sample_1 . . . . . . . . . . . . . . . . . . . . . . . . . . 4296 1 8 HNCA . . . . . . . . . . . 1 $sample_1 . . . . . . . . . . . . . . . . . . . . . . . . . . 4296 1 9 CANH . . . . . . . . . . . 1 $sample_1 . . . . . . . . . . . . . . . . . . . . . . . . . . 4296 1 10 CA(CO)NH . . . . . . . . . . . 1 $sample_1 . . . . . . . . . . . . . . . . . . . . . . . . . . 4296 1 11 HA(CA)NH . . . . . . . . . . . 1 $sample_1 . . . . . . . . . . . . . . . . . . . . . . . . . . 4296 1 12 HA(CA)(CO)NH . . . . . . . . . . . 1 $sample_1 . . . . . . . . . . . . . . . . . . . . . . . . . . 4296 1 13 CBCANH . . . . . . . . . . . 1 $sample_1 . . . . . . . . . . . . . . . . . . . . . . . . . . 4296 1 14 CBCA(CO)NH . . . . . . . . . . . 1 $sample_1 . . . . . . . . . . . . . . . . . . . . . . . . . . 4296 1 15 HCCNH-TOCSY . . . . . . . . . . . 1 $sample_1 . . . . . . . . . . . . . . . . . . . . . . . . . . 4296 1 16 HCC(CO)NH-TOCSY . . . . . . . . . . . 1 $sample_1 . . . . . . . . . . . . . . . . . . . . . . . . . . 4296 1 17 'homonuclear 2D H-TOCSY' . . . . . . . . . . . 1 $sample_1 . . . . . . . . . . . . . . . . . . . . . . . . . . 4296 1 18 '15N-edited 3D NOESY"' . . . . . . . . . . . 1 $sample_1 . . . . . . . . . . . . . . . . . . . . . . . . . . 4296 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 4296 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name 'Most of the triple resonance experiments were exectuted' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 4296 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name 'with C-H or C-C phase labeling to aid assignments' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 4296 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name '[Tashiro et al. J. Biomol. NMR (1995) 6: 211 - 216;' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 4296 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name 'Feng et al., J. Biomol. NMR (1996) 8, 98 - 104; Rios et al.,' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 4296 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name 'J. Biomol. NMR (1996) 8, 345 - 350].' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 4296 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name 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 . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 4296 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name HNCO _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_8 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_8 _NMR_spec_expt.Entry_ID 4296 _NMR_spec_expt.ID 8 _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 . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_9 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_9 _NMR_spec_expt.Entry_ID 4296 _NMR_spec_expt.ID 9 _NMR_spec_expt.Name CANH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_10 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_10 _NMR_spec_expt.Entry_ID 4296 _NMR_spec_expt.ID 10 _NMR_spec_expt.Name CA(CO)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_11 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_11 _NMR_spec_expt.Entry_ID 4296 _NMR_spec_expt.ID 11 _NMR_spec_expt.Name HA(CA)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_12 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_12 _NMR_spec_expt.Entry_ID 4296 _NMR_spec_expt.ID 12 _NMR_spec_expt.Name HA(CA)(CO)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_13 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_13 _NMR_spec_expt.Entry_ID 4296 _NMR_spec_expt.ID 13 _NMR_spec_expt.Name CBCANH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_14 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_14 _NMR_spec_expt.Entry_ID 4296 _NMR_spec_expt.ID 14 _NMR_spec_expt.Name CBCA(CO)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_15 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_15 _NMR_spec_expt.Entry_ID 4296 _NMR_spec_expt.ID 15 _NMR_spec_expt.Name HCCNH-TOCSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_16 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_16 _NMR_spec_expt.Entry_ID 4296 _NMR_spec_expt.ID 16 _NMR_spec_expt.Name HCC(CO)NH-TOCSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_17 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_17 _NMR_spec_expt.Entry_ID 4296 _NMR_spec_expt.ID 17 _NMR_spec_expt.Name 'homonuclear 2D H-TOCSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_18 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_18 _NMR_spec_expt.Entry_ID 4296 _NMR_spec_expt.ID 18 _NMR_spec_expt.Name '15N-edited 3D NOESY"' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 4296 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 internal spherical . . . . . . . 4296 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 4296 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 4296 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_CsCspA_Ecoli_pH6.0_30degC _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode CsCspA_Ecoli_pH6.0_30degC _Assigned_chem_shift_list.Entry_ID 4296 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_1 . 4296 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 HA H 1 4.39 0.02 . 1 . . . . . . . . 4296 1 2 . 1 1 2 2 SER C C 13 177.2 0.10 . 1 . . . . . . . . 4296 1 3 . 1 1 2 2 SER CA C 13 58.0 0.10 . 1 . . . . . . . . 4296 1 4 . 1 1 2 2 SER CB C 13 63.6 0.10 . 1 . . . . . . . . 4296 1 5 . 1 1 3 3 GLY H H 1 8.43 0.02 . 1 . . . . . . . . 4296 1 6 . 1 1 3 3 GLY HA2 H 1 3.95 0.02 . 1 . . . . . . . . 4296 1 7 . 1 1 3 3 GLY HA3 H 1 3.95 0.02 . 1 . . . . . . . . 4296 1 8 . 1 1 3 3 GLY C C 13 173.4 0.10 . 1 . . . . . . . . 4296 1 9 . 1 1 3 3 GLY CA C 13 45.2 0.10 . 1 . . . . . . . . 4296 1 10 . 1 1 3 3 GLY N N 15 111.0 0.10 . 1 . . . . . . . . 4296 1 11 . 1 1 4 4 LYS H H 1 8.21 0.02 . 1 . . . . . . . . 4296 1 12 . 1 1 4 4 LYS HA H 1 4.28 0.02 . 1 . . . . . . . . 4296 1 13 . 1 1 4 4 LYS HB2 H 1 1.76 0.02 . 1 . . . . . . . . 4296 1 14 . 1 1 4 4 LYS HB3 H 1 1.58 0.02 . 1 . . . . . . . . 4296 1 15 . 1 1 4 4 LYS HG2 H 1 1.52 0.02 . 2 . . . . . . . . 4296 1 16 . 1 1 4 4 LYS HG3 H 1 1.15 0.02 . 2 . . . . . . . . 4296 1 17 . 1 1 4 4 LYS HD2 H 1 1.69 0.02 . 1 . . . . . . . . 4296 1 18 . 1 1 4 4 LYS HD3 H 1 1.69 0.02 . 1 . . . . . . . . 4296 1 19 . 1 1 4 4 LYS HE2 H 1 2.89 0.02 . 1 . . . . . . . . 4296 1 20 . 1 1 4 4 LYS HE3 H 1 2.89 0.02 . 1 . . . . . . . . 4296 1 21 . 1 1 4 4 LYS C C 13 176.0 0.10 . 1 . . . . . . . . 4296 1 22 . 1 1 4 4 LYS CA C 13 56.6 0.10 . 1 . . . . . . . . 4296 1 23 . 1 1 4 4 LYS CB C 13 33.4 0.10 . 1 . . . . . . . . 4296 1 24 . 1 1 4 4 LYS CG C 13 24.6 0.10 . 1 . . . . . . . . 4296 1 25 . 1 1 4 4 LYS CD C 13 28.4 0.10 . 1 . . . . . . . . 4296 1 26 . 1 1 4 4 LYS CE C 13 41.7 0.10 . 1 . . . . . . . . 4296 1 27 . 1 1 4 4 LYS N N 15 120.1 0.10 . 1 . . . . . . . . 4296 1 28 . 1 1 5 5 MET H H 1 8.63 0.02 . 1 . . . . . . . . 4296 1 29 . 1 1 5 5 MET HA H 1 4.57 0.02 . 1 . . . . . . . . 4296 1 30 . 1 1 5 5 MET HB3 H 1 1.40 0.02 . 1 . . . . . . . . 4296 1 31 . 1 1 5 5 MET HB2 H 1 1.06 0.02 . 1 . . . . . . . . 4296 1 32 . 1 1 5 5 MET HG2 H 1 2.38 0.02 . 2 . . . . . . . . 4296 1 33 . 1 1 5 5 MET HG3 H 1 2.24 0.02 . 2 . . . . . . . . 4296 1 34 . 1 1 5 5 MET C C 13 174.1 0.10 . 1 . . . . . . . . 4296 1 35 . 1 1 5 5 MET CA C 13 53.6 0.10 . 1 . . . . . . . . 4296 1 36 . 1 1 5 5 MET CB C 13 34.0 0.10 . 1 . . . . . . . . 4296 1 37 . 1 1 5 5 MET CG C 13 31.5 0.10 . 1 . . . . . . . . 4296 1 38 . 1 1 5 5 MET N N 15 122.7 0.10 . 1 . . . . . . . . 4296 1 39 . 1 1 6 6 THR H H 1 7.69 0.02 . 1 . . . . . . . . 4296 1 40 . 1 1 6 6 THR HA H 1 5.50 0.02 . 1 . . . . . . . . 4296 1 41 . 1 1 6 6 THR HB H 1 4.43 0.02 . 1 . . . . . . . . 4296 1 42 . 1 1 6 6 THR HG21 H 1 1.12 0.02 . 1 . . . . . . . . 4296 1 43 . 1 1 6 6 THR HG22 H 1 1.12 0.02 . 1 . . . . . . . . 4296 1 44 . 1 1 6 6 THR HG23 H 1 1.12 0.02 . 1 . . . . . . . . 4296 1 45 . 1 1 6 6 THR C C 13 175.7 0.10 . 1 . . . . . . . . 4296 1 46 . 1 1 6 6 THR CA C 13 59.4 0.10 . 1 . . . . . . . . 4296 1 47 . 1 1 6 6 THR CB C 13 71.4 0.10 . 1 . . . . . . . . 4296 1 48 . 1 1 6 6 THR CG2 C 13 21.6 0.10 . 1 . . . . . . . . 4296 1 49 . 1 1 6 6 THR N N 15 107.5 0.10 . 1 . . . . . . . . 4296 1 50 . 1 1 7 7 GLY H H 1 8.96 0.02 . 1 . . . . . . . . 4296 1 51 . 1 1 7 7 GLY HA2 H 1 4.58 0.02 . 2 . . . . . . . . 4296 1 52 . 1 1 7 7 GLY HA3 H 1 3.96 0.02 . 2 . . . . . . . . 4296 1 53 . 1 1 7 7 GLY C C 13 171.1 0.10 . 1 . . . . . . . . 4296 1 54 . 1 1 7 7 GLY CA C 13 46.2 0.10 . 1 . . . . . . . . 4296 1 55 . 1 1 7 7 GLY N N 15 108.7 0.10 . 1 . . . . . . . . 4296 1 56 . 1 1 8 8 ILE H H 1 8.20 0.02 . 1 . . . . . . . . 4296 1 57 . 1 1 8 8 ILE HA H 1 5.13 0.02 . 1 . . . . . . . . 4296 1 58 . 1 1 8 8 ILE HB H 1 1.65 0.02 . 1 . . . . . . . . 4296 1 59 . 1 1 8 8 ILE HG21 H 1 0.85 0.02 . 1 . . . . . . . . 4296 1 60 . 1 1 8 8 ILE HG22 H 1 0.85 0.02 . 1 . . . . . . . . 4296 1 61 . 1 1 8 8 ILE HG23 H 1 0.85 0.02 . 1 . . . . . . . . 4296 1 62 . 1 1 8 8 ILE HG12 H 1 1.54 0.02 . 2 . . . . . . . . 4296 1 63 . 1 1 8 8 ILE HG13 H 1 1.13 0.02 . 2 . . . . . . . . 4296 1 64 . 1 1 8 8 ILE HD11 H 1 0.90 0.02 . 1 . . . . . . . . 4296 1 65 . 1 1 8 8 ILE HD12 H 1 0.90 0.02 . 1 . . . . . . . . 4296 1 66 . 1 1 8 8 ILE HD13 H 1 0.90 0.02 . 1 . . . . . . . . 4296 1 67 . 1 1 8 8 ILE C C 13 175.6 0.10 . 1 . . . . . . . . 4296 1 68 . 1 1 8 8 ILE CA C 13 58.3 0.10 . 1 . . . . . . . . 4296 1 69 . 1 1 8 8 ILE CB C 13 41.9 0.10 . 1 . . . . . . . . 4296 1 70 . 1 1 8 8 ILE CG1 C 13 27.1 0.10 . 1 . . . . . . . . 4296 1 71 . 1 1 8 8 ILE CG2 C 13 16.7 0.10 . 1 . . . . . . . . 4296 1 72 . 1 1 8 8 ILE CD1 C 13 12.5 0.10 . 1 . . . . . . . . 4296 1 73 . 1 1 8 8 ILE N N 15 118.1 0.10 . 1 . . . . . . . . 4296 1 74 . 1 1 9 9 VAL H H 1 8.83 0.02 . 1 . . . . . . . . 4296 1 75 . 1 1 9 9 VAL HA H 1 3.61 0.02 . 1 . . . . . . . . 4296 1 76 . 1 1 9 9 VAL HB H 1 2.42 0.02 . 1 . . . . . . . . 4296 1 77 . 1 1 9 9 VAL HG11 H 1 0.86 0.02 . 2 . . . . . . . . 4296 1 78 . 1 1 9 9 VAL HG12 H 1 0.86 0.02 . 2 . . . . . . . . 4296 1 79 . 1 1 9 9 VAL HG13 H 1 0.86 0.02 . 2 . . . . . . . . 4296 1 80 . 1 1 9 9 VAL HG21 H 1 0.56 0.02 . 2 . . . . . . . . 4296 1 81 . 1 1 9 9 VAL HG22 H 1 0.56 0.02 . 2 . . . . . . . . 4296 1 82 . 1 1 9 9 VAL HG23 H 1 0.56 0.02 . 2 . . . . . . . . 4296 1 83 . 1 1 9 9 VAL C C 13 175.0 0.10 . 1 . . . . . . . . 4296 1 84 . 1 1 9 9 VAL CA C 13 64.4 0.10 . 1 . . . . . . . . 4296 1 85 . 1 1 9 9 VAL CB C 13 31.0 0.10 . 1 . . . . . . . . 4296 1 86 . 1 1 9 9 VAL CG1 C 13 20.7 0.10 . 1 . . . . . . . . 4296 1 87 . 1 1 9 9 VAL CG2 C 13 20.7 0.10 . 1 . . . . . . . . 4296 1 88 . 1 1 9 9 VAL N N 15 126.3 0.10 . 1 . . . . . . . . 4296 1 89 . 1 1 10 10 LYS H H 1 9.11 0.02 . 1 . . . . . . . . 4296 1 90 . 1 1 10 10 LYS HA H 1 4.21 0.02 . 1 . . . . . . . . 4296 1 91 . 1 1 10 10 LYS HB2 H 1 1.55 0.02 . 1 . . . . . . . . 4296 1 92 . 1 1 10 10 LYS HB3 H 1 1.55 0.02 . 1 . . . . . . . . 4296 1 93 . 1 1 10 10 LYS HG2 H 1 2.06 0.02 . 2 . . . . . . . . 4296 1 94 . 1 1 10 10 LYS HG3 H 1 2.04 0.02 . 2 . . . . . . . . 4296 1 95 . 1 1 10 10 LYS C C 13 176.3 0.10 . 1 . . . . . . . . 4296 1 96 . 1 1 10 10 LYS CA C 13 58.5 0.10 . 1 . . . . . . . . 4296 1 97 . 1 1 10 10 LYS CB C 13 33.8 0.10 . 1 . . . . . . . . 4296 1 98 . 1 1 10 10 LYS CE C 13 41.8 0.10 . 1 . . . . . . . . 4296 1 99 . 1 1 10 10 LYS N N 15 135.9 0.10 . 1 . . . . . . . . 4296 1 100 . 1 1 11 11 TRP H H 1 7.45 0.02 . 1 . . . . . . . . 4296 1 101 . 1 1 11 11 TRP HA H 1 4.66 0.02 . 1 . . . . . . . . 4296 1 102 . 1 1 11 11 TRP HB3 H 1 3.54 0.02 . 1 . . . . . . . . 4296 1 103 . 1 1 11 11 TRP HB2 H 1 3.44 0.02 . 1 . . . . . . . . 4296 1 104 . 1 1 11 11 TRP HD1 H 1 7.14 0.02 . 1 . . . . . . . . 4296 1 105 . 1 1 11 11 TRP HE1 H 1 10.47 0.02 . 1 . . . . . . . . 4296 1 106 . 1 1 11 11 TRP HE3 H 1 7.37 0.02 . 1 . . . . . . . . 4296 1 107 . 1 1 11 11 TRP HZ2 H 1 7.50 0.02 . 1 . . . . . . . . 4296 1 108 . 1 1 11 11 TRP HZ3 H 1 7.37 0.02 . 1 . . . . . . . . 4296 1 109 . 1 1 11 11 TRP HH2 H 1 6.74 0.02 . 1 . . . . . . . . 4296 1 110 . 1 1 11 11 TRP C C 13 173.7 0.10 . 1 . . . . . . . . 4296 1 111 . 1 1 11 11 TRP CA C 13 56.2 0.10 . 1 . . . . . . . . 4296 1 112 . 1 1 11 11 TRP CB C 13 31.2 0.10 . 1 . . . . . . . . 4296 1 113 . 1 1 11 11 TRP N N 15 111.2 0.10 . 1 . . . . . . . . 4296 1 114 . 1 1 11 11 TRP NE1 N 15 130.0 0.10 . 1 . . . . . . . . 4296 1 115 . 1 1 12 12 PHE H H 1 9.25 0.02 . 1 . . . . . . . . 4296 1 116 . 1 1 12 12 PHE HA H 1 4.27 0.02 . 1 . . . . . . . . 4296 1 117 . 1 1 12 12 PHE HB3 H 1 2.93 0.02 . 1 . . . . . . . . 4296 1 118 . 1 1 12 12 PHE HB2 H 1 2.47 0.02 . 1 . . . . . . . . 4296 1 119 . 1 1 12 12 PHE HD1 H 1 6.76 0.02 . 1 . . . . . . . . 4296 1 120 . 1 1 12 12 PHE HD2 H 1 6.76 0.02 . 1 . . . . . . . . 4296 1 121 . 1 1 12 12 PHE HE1 H 1 7.01 0.02 . 1 . . . . . . . . 4296 1 122 . 1 1 12 12 PHE HE2 H 1 7.01 0.02 . 1 . . . . . . . . 4296 1 123 . 1 1 12 12 PHE HZ H 1 7.56 0.02 . 1 . . . . . . . . 4296 1 124 . 1 1 12 12 PHE C C 13 172.4 0.10 . 1 . . . . . . . . 4296 1 125 . 1 1 12 12 PHE CA C 13 59.3 0.10 . 1 . . . . . . . . 4296 1 126 . 1 1 12 12 PHE CB C 13 42.2 0.10 . 1 . . . . . . . . 4296 1 127 . 1 1 12 12 PHE N N 15 121.5 0.10 . 1 . . . . . . . . 4296 1 128 . 1 1 13 13 ASN H H 1 8.13 0.02 . 1 . . . . . . . . 4296 1 129 . 1 1 13 13 ASN HA H 1 4.82 0.02 . 1 . . . . . . . . 4296 1 130 . 1 1 13 13 ASN HB2 H 1 2.55 0.02 . 2 . . . . . . . . 4296 1 131 . 1 1 13 13 ASN HB3 H 1 2.45 0.02 . 2 . . . . . . . . 4296 1 132 . 1 1 13 13 ASN HD21 H 1 7.54 0.02 . 1 . . . . . . . . 4296 1 133 . 1 1 13 13 ASN HD22 H 1 7.32 0.02 . 1 . . . . . . . . 4296 1 134 . 1 1 13 13 ASN C C 13 174.1 0.10 . 1 . . . . . . . . 4296 1 135 . 1 1 13 13 ASN CA C 13 51.2 0.10 . 1 . . . . . . . . 4296 1 136 . 1 1 13 13 ASN CB C 13 39.1 0.10 . 1 . . . . . . . . 4296 1 137 . 1 1 13 13 ASN N N 15 126.6 0.10 . 1 . . . . . . . . 4296 1 138 . 1 1 13 13 ASN ND2 N 15 112.7 0.10 . 1 . . . . . . . . 4296 1 139 . 1 1 14 14 ALA H H 1 9.07 0.02 . 1 . . . . . . . . 4296 1 140 . 1 1 14 14 ALA HA H 1 4.09 0.02 . 1 . . . . . . . . 4296 1 141 . 1 1 14 14 ALA HB1 H 1 1.59 0.02 . 1 . . . . . . . . 4296 1 142 . 1 1 14 14 ALA HB2 H 1 1.59 0.02 . 1 . . . . . . . . 4296 1 143 . 1 1 14 14 ALA HB3 H 1 1.59 0.02 . 1 . . . . . . . . 4296 1 144 . 1 1 14 14 ALA C C 13 178.6 0.10 . 1 . . . . . . . . 4296 1 145 . 1 1 14 14 ALA CA C 13 54.5 0.10 . 1 . . . . . . . . 4296 1 146 . 1 1 14 14 ALA CB C 13 18.5 0.10 . 1 . . . . . . . . 4296 1 147 . 1 1 14 14 ALA N N 15 128.6 0.10 . 1 . . . . . . . . 4296 1 148 . 1 1 15 15 ASP H H 1 7.98 0.02 . 1 . . . . . . . . 4296 1 149 . 1 1 15 15 ASP HA H 1 4.35 0.02 . 1 . . . . . . . . 4296 1 150 . 1 1 15 15 ASP HB2 H 1 2.77 0.02 . 2 . . . . . . . . 4296 1 151 . 1 1 15 15 ASP HB3 H 1 2.70 0.02 . 2 . . . . . . . . 4296 1 152 . 1 1 15 15 ASP C C 13 177.7 0.10 . 1 . . . . . . . . 4296 1 153 . 1 1 15 15 ASP CA C 13 56.6 0.10 . 1 . . . . . . . . 4296 1 154 . 1 1 15 15 ASP CB C 13 40.5 0.10 . 1 . . . . . . . . 4296 1 155 . 1 1 15 15 ASP N N 15 117.0 0.10 . 1 . . . . . . . . 4296 1 156 . 1 1 16 16 LYS H H 1 7.45 0.02 . 1 . . . . . . . . 4296 1 157 . 1 1 16 16 LYS HA H 1 4.21 0.02 . 1 . . . . . . . . 4296 1 158 . 1 1 16 16 LYS HB3 H 1 1.60 0.02 . 1 . . . . . . . . 4296 1 159 . 1 1 16 16 LYS HB2 H 1 1.09 0.02 . 1 . . . . . . . . 4296 1 160 . 1 1 16 16 LYS HG2 H 1 1.42 0.02 . 2 . . . . . . . . 4296 1 161 . 1 1 16 16 LYS HG3 H 1 1.35 0.02 . 2 . . . . . . . . 4296 1 162 . 1 1 16 16 LYS HD2 H 1 1.67 0.02 . 2 . . . . . . . . 4296 1 163 . 1 1 16 16 LYS HD3 H 1 1.65 0.02 . 2 . . . . . . . . 4296 1 164 . 1 1 16 16 LYS HE2 H 1 3.01 0.02 . 2 . . . . . . . . 4296 1 165 . 1 1 16 16 LYS HE3 H 1 2.97 0.02 . 2 . . . . . . . . 4296 1 166 . 1 1 16 16 LYS C C 13 177.3 0.10 . 1 . . . . . . . . 4296 1 167 . 1 1 16 16 LYS CA C 13 56.1 0.10 . 1 . . . . . . . . 4296 1 168 . 1 1 16 16 LYS CB C 13 33.6 0.10 . 1 . . . . . . . . 4296 1 169 . 1 1 16 16 LYS CG C 13 25.0 0.10 . 1 . . . . . . . . 4296 1 170 . 1 1 16 16 LYS CE C 13 41.2 0.10 . 1 . . . . . . . . 4296 1 171 . 1 1 16 16 LYS N N 15 115.8 0.10 . 1 . . . . . . . . 4296 1 172 . 1 1 17 17 GLY H H 1 8.16 0.02 . 1 . . . . . . . . 4296 1 173 . 1 1 17 17 GLY HA2 H 1 4.10 0.02 . 2 . . . . . . . . 4296 1 174 . 1 1 17 17 GLY HA3 H 1 3.79 0.02 . 2 . . . . . . . . 4296 1 175 . 1 1 17 17 GLY C C 13 172.4 0.10 . 1 . . . . . . . . 4296 1 176 . 1 1 17 17 GLY CA C 13 46.2 0.10 . 1 . . . . . . . . 4296 1 177 . 1 1 17 17 GLY N N 15 107.5 0.10 . 1 . . . . . . . . 4296 1 178 . 1 1 18 18 PHE H H 1 6.66 0.02 . 1 . . . . . . . . 4296 1 179 . 1 1 18 18 PHE HA H 1 5.11 0.02 . 1 . . . . . . . . 4296 1 180 . 1 1 18 18 PHE HB2 H 1 3.01 0.02 . 2 . . . . . . . . 4296 1 181 . 1 1 18 18 PHE HB3 H 1 2.88 0.02 . 2 . . . . . . . . 4296 1 182 . 1 1 18 18 PHE HD1 H 1 7.00 0.02 . 1 . . . . . . . . 4296 1 183 . 1 1 18 18 PHE HD2 H 1 7.00 0.02 . 1 . . . . . . . . 4296 1 184 . 1 1 18 18 PHE HE1 H 1 7.53 0.02 . 1 . . . . . . . . 4296 1 185 . 1 1 18 18 PHE HE2 H 1 7.53 0.02 . 1 . . . . . . . . 4296 1 186 . 1 1 18 18 PHE HZ H 1 7.47 0.02 . 1 . . . . . . . . 4296 1 187 . 1 1 18 18 PHE C C 13 171.9 0.10 . 1 . . . . . . . . 4296 1 188 . 1 1 18 18 PHE CA C 13 54.6 0.10 . 1 . . . . . . . . 4296 1 189 . 1 1 18 18 PHE CB C 13 41.9 0.10 . 1 . . . . . . . . 4296 1 190 . 1 1 18 18 PHE N N 15 112.3 0.10 . 1 . . . . . . . . 4296 1 191 . 1 1 19 19 GLY H H 1 8.04 0.02 . 1 . . . . . . . . 4296 1 192 . 1 1 19 19 GLY HA2 H 1 3.93 0.02 . 1 . . . . . . . . 4296 1 193 . 1 1 19 19 GLY HA3 H 1 3.93 0.02 . 1 . . . . . . . . 4296 1 194 . 1 1 19 19 GLY C C 13 170.4 0.10 . 1 . . . . . . . . 4296 1 195 . 1 1 19 19 GLY CA C 13 45.3 0.10 . 1 . . . . . . . . 4296 1 196 . 1 1 19 19 GLY N N 15 105.3 0.10 . 1 . . . . . . . . 4296 1 197 . 1 1 20 20 PHE H H 1 7.96 0.02 . 1 . . . . . . . . 4296 1 198 . 1 1 20 20 PHE HA H 1 5.29 0.02 . 1 . . . . . . . . 4296 1 199 . 1 1 20 20 PHE HB3 H 1 2.59 0.02 . 1 . . . . . . . . 4296 1 200 . 1 1 20 20 PHE HB2 H 1 2.23 0.02 . 1 . . . . . . . . 4296 1 201 . 1 1 20 20 PHE HD1 H 1 6.79 0.02 . 1 . . . . . . . . 4296 1 202 . 1 1 20 20 PHE HD2 H 1 6.79 0.02 . 1 . . . . . . . . 4296 1 203 . 1 1 20 20 PHE HE1 H 1 7.35 0.02 . 1 . . . . . . . . 4296 1 204 . 1 1 20 20 PHE HE2 H 1 7.35 0.02 . 1 . . . . . . . . 4296 1 205 . 1 1 20 20 PHE HZ H 1 7.24 0.02 . 1 . . . . . . . . 4296 1 206 . 1 1 20 20 PHE C C 13 174.6 0.10 . 1 . . . . . . . . 4296 1 207 . 1 1 20 20 PHE CA C 13 56.6 0.10 . 1 . . . . . . . . 4296 1 208 . 1 1 20 20 PHE CB C 13 45.2 0.10 . 1 . . . . . . . . 4296 1 209 . 1 1 20 20 PHE N N 15 114.9 0.10 . 1 . . . . . . . . 4296 1 210 . 1 1 21 21 ILE H H 1 9.43 0.02 . 1 . . . . . . . . 4296 1 211 . 1 1 21 21 ILE HA H 1 4.24 0.02 . 1 . . . . . . . . 4296 1 212 . 1 1 21 21 ILE HB H 1 0.94 0.02 . 1 . . . . . . . . 4296 1 213 . 1 1 21 21 ILE HG21 H 1 0.12 0.02 . 1 . . . . . . . . 4296 1 214 . 1 1 21 21 ILE HG22 H 1 0.12 0.02 . 1 . . . . . . . . 4296 1 215 . 1 1 21 21 ILE HG23 H 1 0.12 0.02 . 1 . . . . . . . . 4296 1 216 . 1 1 21 21 ILE HG12 H 1 1.21 0.02 . 2 . . . . . . . . 4296 1 217 . 1 1 21 21 ILE HG13 H 1 0.35 0.02 . 2 . . . . . . . . 4296 1 218 . 1 1 21 21 ILE HD11 H 1 -0.09 0.02 . 1 . . . . . . . . 4296 1 219 . 1 1 21 21 ILE HD12 H 1 -0.09 0.02 . 1 . . . . . . . . 4296 1 220 . 1 1 21 21 ILE HD13 H 1 -0.09 0.02 . 1 . . . . . . . . 4296 1 221 . 1 1 21 21 ILE C C 13 174.7 0.10 . 1 . . . . . . . . 4296 1 222 . 1 1 21 21 ILE CA C 13 59.3 0.10 . 1 . . . . . . . . 4296 1 223 . 1 1 21 21 ILE CB C 13 42.0 0.10 . 1 . . . . . . . . 4296 1 224 . 1 1 21 21 ILE CG1 C 13 27.3 0.10 . 1 . . . . . . . . 4296 1 225 . 1 1 21 21 ILE CG2 C 13 17.9 0.10 . 1 . . . . . . . . 4296 1 226 . 1 1 21 21 ILE CD1 C 13 13.2 0.10 . 1 . . . . . . . . 4296 1 227 . 1 1 21 21 ILE N N 15 121.7 0.10 . 1 . . . . . . . . 4296 1 228 . 1 1 22 22 THR H H 1 9.37 0.02 . 1 . . . . . . . . 4296 1 229 . 1 1 22 22 THR HA H 1 5.17 0.02 . 1 . . . . . . . . 4296 1 230 . 1 1 22 22 THR HB H 1 3.95 0.02 . 1 . . . . . . . . 4296 1 231 . 1 1 22 22 THR HG21 H 1 1.39 0.02 . 1 . . . . . . . . 4296 1 232 . 1 1 22 22 THR HG22 H 1 1.39 0.02 . 1 . . . . . . . . 4296 1 233 . 1 1 22 22 THR HG23 H 1 1.39 0.02 . 1 . . . . . . . . 4296 1 234 . 1 1 22 22 THR CA C 13 59.3 0.10 . 1 . . . . . . . . 4296 1 235 . 1 1 22 22 THR CB C 13 70.3 0.10 . 1 . . . . . . . . 4296 1 236 . 1 1 22 22 THR N N 15 126.6 0.10 . 1 . . . . . . . . 4296 1 237 . 1 1 23 23 PRO HA H 1 4.77 0.02 . 1 . . . . . . . . 4296 1 238 . 1 1 23 23 PRO HB2 H 1 2.45 0.02 . 2 . . . . . . . . 4296 1 239 . 1 1 23 23 PRO HB3 H 1 2.36 0.02 . 2 . . . . . . . . 4296 1 240 . 1 1 23 23 PRO HG2 H 1 2.30 0.02 . 2 . . . . . . . . 4296 1 241 . 1 1 23 23 PRO HG3 H 1 1.86 0.02 . 2 . . . . . . . . 4296 1 242 . 1 1 23 23 PRO HD2 H 1 4.51 0.02 . 2 . . . . . . . . 4296 1 243 . 1 1 23 23 PRO HD3 H 1 3.85 0.02 . 2 . . . . . . . . 4296 1 244 . 1 1 23 23 PRO C C 13 177.5 0.10 . 1 . . . . . . . . 4296 1 245 . 1 1 23 23 PRO CA C 13 63.0 0.10 . 1 . . . . . . . . 4296 1 246 . 1 1 23 23 PRO CB C 13 33.6 0.10 . 1 . . . . . . . . 4296 1 247 . 1 1 23 23 PRO CD C 13 52.6 0.10 . 1 . . . . . . . . 4296 1 248 . 1 1 24 24 ASP H H 1 9.21 0.02 . 1 . . . . . . . . 4296 1 249 . 1 1 24 24 ASP HA H 1 4.66 0.02 . 1 . . . . . . . . 4296 1 250 . 1 1 24 24 ASP HB2 H 1 2.77 0.02 . 2 . . . . . . . . 4296 1 251 . 1 1 24 24 ASP HB3 H 1 2.50 0.02 . 2 . . . . . . . . 4296 1 252 . 1 1 24 24 ASP C C 13 176.5 0.10 . 1 . . . . . . . . 4296 1 253 . 1 1 24 24 ASP CA C 13 56.6 0.10 . 1 . . . . . . . . 4296 1 254 . 1 1 24 24 ASP CB C 13 40.3 0.10 . 1 . . . . . . . . 4296 1 255 . 1 1 24 24 ASP N N 15 123.1 0.10 . 1 . . . . . . . . 4296 1 256 . 1 1 25 25 ASP H H 1 7.98 0.02 . 1 . . . . . . . . 4296 1 257 . 1 1 25 25 ASP HA H 1 4.55 0.02 . 1 . . . . . . . . 4296 1 258 . 1 1 25 25 ASP HB2 H 1 3.09 0.02 . 2 . . . . . . . . 4296 1 259 . 1 1 25 25 ASP HB3 H 1 2.60 0.02 . 2 . . . . . . . . 4296 1 260 . 1 1 25 25 ASP C C 13 177.6 0.10 . 1 . . . . . . . . 4296 1 261 . 1 1 25 25 ASP CA C 13 53.6 0.10 . 1 . . . . . . . . 4296 1 262 . 1 1 25 25 ASP CB C 13 40.5 0.10 . 1 . . . . . . . . 4296 1 263 . 1 1 25 25 ASP N N 15 117.0 0.10 . 1 . . . . . . . . 4296 1 264 . 1 1 26 26 GLY H H 1 7.69 0.02 . 1 . . . . . . . . 4296 1 265 . 1 1 26 26 GLY HA2 H 1 4.18 0.02 . 2 . . . . . . . . 4296 1 266 . 1 1 26 26 GLY HA3 H 1 3.90 0.02 . 2 . . . . . . . . 4296 1 267 . 1 1 26 26 GLY C C 13 174.7 0.10 . 1 . . . . . . . . 4296 1 268 . 1 1 26 26 GLY CA C 13 45.8 0.10 . 1 . . . . . . . . 4296 1 269 . 1 1 26 26 GLY N N 15 107.5 0.10 . 1 . . . . . . . . 4296 1 270 . 1 1 27 27 SER H H 1 8.00 0.02 . 1 . . . . . . . . 4296 1 271 . 1 1 27 27 SER HA H 1 4.37 0.02 . 1 . . . . . . . . 4296 1 272 . 1 1 27 27 SER HB2 H 1 4.19 0.02 . 2 . . . . . . . . 4296 1 273 . 1 1 27 27 SER HB3 H 1 3.95 0.02 . 2 . . . . . . . . 4296 1 274 . 1 1 27 27 SER C C 13 172.5 0.10 . 1 . . . . . . . . 4296 1 275 . 1 1 27 27 SER CA C 13 58.6 0.10 . 1 . . . . . . . . 4296 1 276 . 1 1 27 27 SER CB C 13 62.9 0.10 . 1 . . . . . . . . 4296 1 277 . 1 1 27 27 SER N N 15 116.0 0.10 . 1 . . . . . . . . 4296 1 278 . 1 1 28 28 LYS H H 1 7.72 0.02 . 1 . . . . . . . . 4296 1 279 . 1 1 28 28 LYS HA H 1 4.09 0.02 . 1 . . . . . . . . 4296 1 280 . 1 1 28 28 LYS HB2 H 1 1.86 0.02 . 2 . . . . . . . . 4296 1 281 . 1 1 28 28 LYS HB3 H 1 1.86 0.02 . 2 . . . . . . . . 4296 1 282 . 1 1 28 28 LYS HG2 H 1 1.60 0.02 . 1 . . . . . . . . 4296 1 283 . 1 1 28 28 LYS HG3 H 1 1.60 0.02 . 1 . . . . . . . . 4296 1 284 . 1 1 28 28 LYS HD2 H 1 1.76 0.02 . 1 . . . . . . . . 4296 1 285 . 1 1 28 28 LYS HD3 H 1 1.76 0.02 . 1 . . . . . . . . 4296 1 286 . 1 1 28 28 LYS HE2 H 1 3.07 0.02 . 1 . . . . . . . . 4296 1 287 . 1 1 28 28 LYS HE3 H 1 3.07 0.02 . 1 . . . . . . . . 4296 1 288 . 1 1 28 28 LYS C C 13 175.1 0.10 . 1 . . . . . . . . 4296 1 289 . 1 1 28 28 LYS CA C 13 56.9 0.10 . 1 . . . . . . . . 4296 1 290 . 1 1 28 28 LYS CB C 13 33.0 0.10 . 1 . . . . . . . . 4296 1 291 . 1 1 28 28 LYS CG C 13 24.1 0.10 . 1 . . . . . . . . 4296 1 292 . 1 1 28 28 LYS CD C 13 29.1 0.10 . 1 . . . . . . . . 4296 1 293 . 1 1 28 28 LYS CE C 13 42.2 0.10 . 1 . . . . . . . . 4296 1 294 . 1 1 28 28 LYS N N 15 117.1 0.10 . 1 . . . . . . . . 4296 1 295 . 1 1 29 29 ASP H H 1 7.93 0.02 . 1 . . . . . . . . 4296 1 296 . 1 1 29 29 ASP HA H 1 4.90 0.02 . 1 . . . . . . . . 4296 1 297 . 1 1 29 29 ASP HB3 H 1 2.45 0.02 . 1 . . . . . . . . 4296 1 298 . 1 1 29 29 ASP HB2 H 1 2.36 0.02 . 1 . . . . . . . . 4296 1 299 . 1 1 29 29 ASP C C 13 176.3 0.10 . 1 . . . . . . . . 4296 1 300 . 1 1 29 29 ASP CA C 13 55.3 0.10 . 1 . . . . . . . . 4296 1 301 . 1 1 29 29 ASP CB C 13 41.1 0.10 . 1 . . . . . . . . 4296 1 302 . 1 1 29 29 ASP N N 15 118.0 0.10 . 1 . . . . . . . . 4296 1 303 . 1 1 30 30 VAL H H 1 9.30 0.02 . 1 . . . . . . . . 4296 1 304 . 1 1 30 30 VAL HA H 1 4.34 0.02 . 1 . . . . . . . . 4296 1 305 . 1 1 30 30 VAL HB H 1 1.66 0.02 . 1 . . . . . . . . 4296 1 306 . 1 1 30 30 VAL HG11 H 1 1.03 0.02 . 2 . . . . . . . . 4296 1 307 . 1 1 30 30 VAL HG12 H 1 1.03 0.02 . 2 . . . . . . . . 4296 1 308 . 1 1 30 30 VAL HG13 H 1 1.03 0.02 . 2 . . . . . . . . 4296 1 309 . 1 1 30 30 VAL HG21 H 1 0.84 0.02 . 2 . . . . . . . . 4296 1 310 . 1 1 30 30 VAL HG22 H 1 0.84 0.02 . 2 . . . . . . . . 4296 1 311 . 1 1 30 30 VAL HG23 H 1 0.84 0.02 . 2 . . . . . . . . 4296 1 312 . 1 1 30 30 VAL C C 13 174.7 0.10 . 1 . . . . . . . . 4296 1 313 . 1 1 30 30 VAL CA C 13 60.6 0.10 . 1 . . . . . . . . 4296 1 314 . 1 1 30 30 VAL CG1 C 13 21.9 0.10 . 1 . . . . . . . . 4296 1 315 . 1 1 30 30 VAL CG2 C 13 21.9 0.10 . 1 . . . . . . . . 4296 1 316 . 1 1 30 30 VAL N N 15 120.4 0.10 . 1 . . . . . . . . 4296 1 317 . 1 1 31 31 PHE H H 1 8.55 0.02 . 1 . . . . . . . . 4296 1 318 . 1 1 31 31 PHE HA H 1 3.71 0.02 . 1 . . . . . . . . 4296 1 319 . 1 1 31 31 PHE HB2 H 1 2.86 0.02 . 2 . . . . . . . . 4296 1 320 . 1 1 31 31 PHE HB3 H 1 2.74 0.02 . 2 . . . . . . . . 4296 1 321 . 1 1 31 31 PHE HD1 H 1 6.77 0.02 . 1 . . . . . . . . 4296 1 322 . 1 1 31 31 PHE HD2 H 1 6.77 0.02 . 1 . . . . . . . . 4296 1 323 . 1 1 31 31 PHE HE1 H 1 7.01 0.02 . 1 . . . . . . . . 4296 1 324 . 1 1 31 31 PHE HE2 H 1 7.01 0.02 . 1 . . . . . . . . 4296 1 325 . 1 1 31 31 PHE HZ H 1 6.96 0.02 . 1 . . . . . . . . 4296 1 326 . 1 1 31 31 PHE C C 13 172.6 0.10 . 1 . . . . . . . . 4296 1 327 . 1 1 31 31 PHE CA C 13 58.2 0.10 . 1 . . . . . . . . 4296 1 328 . 1 1 31 31 PHE CB C 13 40.2 0.10 . 1 . . . . . . . . 4296 1 329 . 1 1 31 31 PHE N N 15 129.7 0.10 . 1 . . . . . . . . 4296 1 330 . 1 1 32 32 VAL H H 1 7.77 0.02 . 1 . . . . . . . . 4296 1 331 . 1 1 32 32 VAL HA H 1 4.48 0.02 . 1 . . . . . . . . 4296 1 332 . 1 1 32 32 VAL HB H 1 1.45 0.02 . 1 . . . . . . . . 4296 1 333 . 1 1 32 32 VAL HG11 H 1 0.60 0.02 . 2 . . . . . . . . 4296 1 334 . 1 1 32 32 VAL HG12 H 1 0.60 0.02 . 2 . . . . . . . . 4296 1 335 . 1 1 32 32 VAL HG13 H 1 0.60 0.02 . 2 . . . . . . . . 4296 1 336 . 1 1 32 32 VAL HG21 H 1 0.47 0.02 . 2 . . . . . . . . 4296 1 337 . 1 1 32 32 VAL HG22 H 1 0.47 0.02 . 2 . . . . . . . . 4296 1 338 . 1 1 32 32 VAL HG23 H 1 0.47 0.02 . 2 . . . . . . . . 4296 1 339 . 1 1 32 32 VAL C C 13 170.4 0.10 . 1 . . . . . . . . 4296 1 340 . 1 1 32 32 VAL CA C 13 57.9 0.10 . 1 . . . . . . . . 4296 1 341 . 1 1 32 32 VAL CB C 13 34.1 0.10 . 1 . . . . . . . . 4296 1 342 . 1 1 32 32 VAL N N 15 124.3 0.10 . 1 . . . . . . . . 4296 1 343 . 1 1 33 33 HIS H H 1 8.72 0.02 . 1 . . . . . . . . 4296 1 344 . 1 1 33 33 HIS HA H 1 4.78 0.02 . 1 . . . . . . . . 4296 1 345 . 1 1 33 33 HIS HB2 H 1 3.15 0.02 . 2 . . . . . . . . 4296 1 346 . 1 1 33 33 HIS HB3 H 1 2.84 0.02 . 2 . . . . . . . . 4296 1 347 . 1 1 33 33 HIS HD2 H 1 7.33 0.02 . 1 . . . . . . . . 4296 1 348 . 1 1 33 33 HIS HE1 H 1 8.45 0.02 . 1 . . . . . . . . 4296 1 349 . 1 1 33 33 HIS C C 13 177.2 0.10 . 1 . . . . . . . . 4296 1 350 . 1 1 33 33 HIS CA C 13 55.5 0.10 . 1 . . . . . . . . 4296 1 351 . 1 1 33 33 HIS CB C 13 34.1 0.10 . 1 . . . . . . . . 4296 1 352 . 1 1 33 33 HIS N N 15 127.1 0.10 . 1 . . . . . . . . 4296 1 353 . 1 1 34 34 PHE H H 1 8.32 0.02 . 1 . . . . . . . . 4296 1 354 . 1 1 34 34 PHE HA H 1 4.14 0.02 . 1 . . . . . . . . 4296 1 355 . 1 1 34 34 PHE HB2 H 1 3.31 0.02 . 2 . . . . . . . . 4296 1 356 . 1 1 34 34 PHE HB3 H 1 2.99 0.02 . 2 . . . . . . . . 4296 1 357 . 1 1 34 34 PHE HD1 H 1 7.16 0.02 . 1 . . . . . . . . 4296 1 358 . 1 1 34 34 PHE HD2 H 1 7.16 0.02 . 1 . . . . . . . . 4296 1 359 . 1 1 34 34 PHE HE1 H 1 7.36 0.02 . 1 . . . . . . . . 4296 1 360 . 1 1 34 34 PHE HE2 H 1 7.36 0.02 . 1 . . . . . . . . 4296 1 361 . 1 1 34 34 PHE HZ H 1 7.45 0.02 . 1 . . . . . . . . 4296 1 362 . 1 1 34 34 PHE C C 13 176.0 0.10 . 1 . . . . . . . . 4296 1 363 . 1 1 34 34 PHE CA C 13 59.9 0.10 . 1 . . . . . . . . 4296 1 364 . 1 1 34 34 PHE CB C 13 37.2 0.10 . 1 . . . . . . . . 4296 1 365 . 1 1 34 34 PHE N N 15 123.1 0.10 . 1 . . . . . . . . 4296 1 366 . 1 1 35 35 SER H H 1 7.59 0.02 . 1 . . . . . . . . 4296 1 367 . 1 1 35 35 SER HA H 1 3.87 0.02 . 1 . . . . . . . . 4296 1 368 . 1 1 35 35 SER HB2 H 1 3.57 0.02 . 1 . . . . . . . . 4296 1 369 . 1 1 35 35 SER HB3 H 1 3.57 0.02 . 1 . . . . . . . . 4296 1 370 . 1 1 35 35 SER C C 13 175.0 0.10 . 1 . . . . . . . . 4296 1 371 . 1 1 35 35 SER CA C 13 59.9 0.10 . 1 . . . . . . . . 4296 1 372 . 1 1 35 35 SER CB C 13 62.3 0.10 . 1 . . . . . . . . 4296 1 373 . 1 1 35 35 SER N N 15 117.0 0.10 . 1 . . . . . . . . 4296 1 374 . 1 1 36 36 ALA H H 1 8.06 0.02 . 1 . . . . . . . . 4296 1 375 . 1 1 36 36 ALA HA H 1 4.46 0.02 . 1 . . . . . . . . 4296 1 376 . 1 1 36 36 ALA HB1 H 1 1.61 0.02 . 1 . . . . . . . . 4296 1 377 . 1 1 36 36 ALA HB2 H 1 1.61 0.02 . 1 . . . . . . . . 4296 1 378 . 1 1 36 36 ALA HB3 H 1 1.61 0.02 . 1 . . . . . . . . 4296 1 379 . 1 1 36 36 ALA C C 13 177.5 0.10 . 1 . . . . . . . . 4296 1 380 . 1 1 36 36 ALA CA C 13 52.3 0.10 . 1 . . . . . . . . 4296 1 381 . 1 1 36 36 ALA CB C 13 22.6 0.10 . 1 . . . . . . . . 4296 1 382 . 1 1 36 36 ALA N N 15 124.1 0.10 . 1 . . . . . . . . 4296 1 383 . 1 1 37 37 ILE H H 1 7.50 0.02 . 1 . . . . . . . . 4296 1 384 . 1 1 37 37 ILE HA H 1 3.89 0.02 . 1 . . . . . . . . 4296 1 385 . 1 1 37 37 ILE HB H 1 1.86 0.02 . 1 . . . . . . . . 4296 1 386 . 1 1 37 37 ILE HG21 H 1 0.81 0.02 . 1 . . . . . . . . 4296 1 387 . 1 1 37 37 ILE HG22 H 1 0.81 0.02 . 1 . . . . . . . . 4296 1 388 . 1 1 37 37 ILE HG23 H 1 0.81 0.02 . 1 . . . . . . . . 4296 1 389 . 1 1 37 37 ILE HG12 H 1 1.86 0.02 . 2 . . . . . . . . 4296 1 390 . 1 1 37 37 ILE HG13 H 1 1.56 0.02 . 2 . . . . . . . . 4296 1 391 . 1 1 37 37 ILE HD11 H 1 0.41 0.02 . 1 . . . . . . . . 4296 1 392 . 1 1 37 37 ILE HD12 H 1 0.41 0.02 . 1 . . . . . . . . 4296 1 393 . 1 1 37 37 ILE HD13 H 1 0.41 0.02 . 1 . . . . . . . . 4296 1 394 . 1 1 37 37 ILE C C 13 176.1 0.10 . 1 . . . . . . . . 4296 1 395 . 1 1 37 37 ILE CA C 13 62.6 0.10 . 1 . . . . . . . . 4296 1 396 . 1 1 37 37 ILE CB C 13 37.8 0.10 . 1 . . . . . . . . 4296 1 397 . 1 1 37 37 ILE N N 15 119.2 0.10 . 1 . . . . . . . . 4296 1 398 . 1 1 38 38 GLN H H 1 9.02 0.02 . 1 . . . . . . . . 4296 1 399 . 1 1 38 38 GLN HA H 1 4.36 0.02 . 1 . . . . . . . . 4296 1 400 . 1 1 38 38 GLN HB2 H 1 2.13 0.02 . 2 . . . . . . . . 4296 1 401 . 1 1 38 38 GLN HB3 H 1 1.79 0.02 . 2 . . . . . . . . 4296 1 402 . 1 1 38 38 GLN HG2 H 1 2.33 0.02 . 2 . . . . . . . . 4296 1 403 . 1 1 38 38 GLN HG3 H 1 2.30 0.02 . 2 . . . . . . . . 4296 1 404 . 1 1 38 38 GLN HE21 H 1 7.19 0.02 . 1 . . . . . . . . 4296 1 405 . 1 1 38 38 GLN HE22 H 1 6.85 0.02 . 1 . . . . . . . . 4296 1 406 . 1 1 38 38 GLN C C 13 175.6 0.10 . 1 . . . . . . . . 4296 1 407 . 1 1 38 38 GLN CA C 13 55.2 0.10 . 1 . . . . . . . . 4296 1 408 . 1 1 38 38 GLN CB C 13 28.7 0.10 . 1 . . . . . . . . 4296 1 409 . 1 1 38 38 GLN CG C 13 33.7 0.10 . 1 . . . . . . . . 4296 1 410 . 1 1 38 38 GLN N N 15 127.1 0.10 . 1 . . . . . . . . 4296 1 411 . 1 1 38 38 GLN NE2 N 15 112.1 0.10 . 1 . . . . . . . . 4296 1 412 . 1 1 39 39 ASN H H 1 7.53 0.02 . 1 . . . . . . . . 4296 1 413 . 1 1 39 39 ASN HA H 1 4.61 0.02 . 1 . . . . . . . . 4296 1 414 . 1 1 39 39 ASN HB2 H 1 2.87 0.02 . 2 . . . . . . . . 4296 1 415 . 1 1 39 39 ASN HB3 H 1 2.61 0.02 . 2 . . . . . . . . 4296 1 416 . 1 1 39 39 ASN HD21 H 1 7.76 0.02 . 1 . . . . . . . . 4296 1 417 . 1 1 39 39 ASN HD22 H 1 6.85 0.02 . 1 . . . . . . . . 4296 1 418 . 1 1 39 39 ASN C C 13 174.6 0.10 . 1 . . . . . . . . 4296 1 419 . 1 1 39 39 ASN CA C 13 53.3 0.10 . 1 . . . . . . . . 4296 1 420 . 1 1 39 39 ASN CB C 13 38.9 0.10 . 1 . . . . . . . . 4296 1 421 . 1 1 39 39 ASN N N 15 118.7 0.10 . 1 . . . . . . . . 4296 1 422 . 1 1 39 39 ASN ND2 N 15 112.3 0.10 . 1 . . . . . . . . 4296 1 423 . 1 1 40 40 ASP H H 1 8.59 0.02 . 1 . . . . . . . . 4296 1 424 . 1 1 40 40 ASP HA H 1 4.51 0.02 . 1 . . . . . . . . 4296 1 425 . 1 1 40 40 ASP HB2 H 1 2.70 0.02 . 2 . . . . . . . . 4296 1 426 . 1 1 40 40 ASP HB3 H 1 2.63 0.02 . 2 . . . . . . . . 4296 1 427 . 1 1 40 40 ASP C C 13 176.5 0.10 . 1 . . . . . . . . 4296 1 428 . 1 1 40 40 ASP CA C 13 54.9 0.10 . 1 . . . . . . . . 4296 1 429 . 1 1 40 40 ASP CB C 13 40.8 0.10 . 1 . . . . . . . . 4296 1 430 . 1 1 40 40 ASP N N 15 121.5 0.10 . 1 . . . . . . . . 4296 1 431 . 1 1 41 41 GLY H H 1 8.29 0.02 . 1 . . . . . . . . 4296 1 432 . 1 1 41 41 GLY HA2 H 1 3.97 0.02 . 2 . . . . . . . . 4296 1 433 . 1 1 41 41 GLY HA3 H 1 3.77 0.02 . 2 . . . . . . . . 4296 1 434 . 1 1 41 41 GLY C C 13 173.7 0.10 . 1 . . . . . . . . 4296 1 435 . 1 1 41 41 GLY CA C 13 45.2 0.10 . 1 . . . . . . . . 4296 1 436 . 1 1 41 41 GLY N N 15 108.9 0.10 . 1 . . . . . . . . 4296 1 437 . 1 1 42 42 TYR H H 1 8.08 0.02 . 1 . . . . . . . . 4296 1 438 . 1 1 42 42 TYR HA H 1 4.41 0.02 . 1 . . . . . . . . 4296 1 439 . 1 1 42 42 TYR HB2 H 1 2.95 0.02 . 1 . . . . . . . . 4296 1 440 . 1 1 42 42 TYR HB3 H 1 2.95 0.02 . 1 . . . . . . . . 4296 1 441 . 1 1 42 42 TYR HD1 H 1 7.06 0.02 . 1 . . . . . . . . 4296 1 442 . 1 1 42 42 TYR HD2 H 1 7.06 0.02 . 1 . . . . . . . . 4296 1 443 . 1 1 42 42 TYR HE1 H 1 6.72 0.02 . 1 . . . . . . . . 4296 1 444 . 1 1 42 42 TYR HE2 H 1 6.72 0.02 . 1 . . . . . . . . 4296 1 445 . 1 1 42 42 TYR C C 13 176.0 0.10 . 1 . . . . . . . . 4296 1 446 . 1 1 42 42 TYR CA C 13 58.2 0.10 . 1 . . . . . . . . 4296 1 447 . 1 1 42 42 TYR CB C 13 38.3 0.10 . 1 . . . . . . . . 4296 1 448 . 1 1 42 42 TYR N N 15 121.2 0.10 . 1 . . . . . . . . 4296 1 449 . 1 1 43 43 LYS H H 1 8.27 0.02 . 1 . . . . . . . . 4296 1 450 . 1 1 43 43 LYS HA H 1 4.19 0.02 . 1 . . . . . . . . 4296 1 451 . 1 1 43 43 LYS HB2 H 1 1.46 0.02 . 2 . . . . . . . . 4296 1 452 . 1 1 43 43 LYS HB3 H 1 1.40 0.02 . 2 . . . . . . . . 4296 1 453 . 1 1 43 43 LYS HG2 H 1 1.86 0.02 . 1 . . . . . . . . 4296 1 454 . 1 1 43 43 LYS HG3 H 1 1.86 0.02 . 1 . . . . . . . . 4296 1 455 . 1 1 43 43 LYS HD2 H 1 1.71 0.02 . 1 . . . . . . . . 4296 1 456 . 1 1 43 43 LYS HD3 H 1 1.71 0.02 . 1 . . . . . . . . 4296 1 457 . 1 1 43 43 LYS HE2 H 1 3.11 0.02 . 2 . . . . . . . . 4296 1 458 . 1 1 43 43 LYS HE3 H 1 3.01 0.02 . 2 . . . . . . . . 4296 1 459 . 1 1 43 43 LYS C C 13 174.0 0.10 . 1 . . . . . . . . 4296 1 460 . 1 1 43 43 LYS CA C 13 55.0 0.10 . 1 . . . . . . . . 4296 1 461 . 1 1 43 43 LYS CB C 13 31.8 0.10 . 1 . . . . . . . . 4296 1 462 . 1 1 43 43 LYS CG C 13 24.4 0.10 . 1 . . . . . . . . 4296 1 463 . 1 1 43 43 LYS CD C 13 28.4 0.10 . 1 . . . . . . . . 4296 1 464 . 1 1 43 43 LYS CE C 13 42.8 0.10 . 1 . . . . . . . . 4296 1 465 . 1 1 43 43 LYS N N 15 125.1 0.10 . 1 . . . . . . . . 4296 1 466 . 1 1 44 44 SER H H 1 7.41 0.02 . 1 . . . . . . . . 4296 1 467 . 1 1 44 44 SER HA H 1 3.98 0.02 . 1 . . . . . . . . 4296 1 468 . 1 1 44 44 SER HB2 H 1 3.50 0.02 . 1 . . . . . . . . 4296 1 469 . 1 1 44 44 SER HB3 H 1 3.43 0.02 . 1 . . . . . . . . 4296 1 470 . 1 1 44 44 SER C C 13 171.7 0.10 . 1 . . . . . . . . 4296 1 471 . 1 1 44 44 SER CA C 13 56.2 0.10 . 1 . . . . . . . . 4296 1 472 . 1 1 44 44 SER CB C 13 63.8 0.10 . 1 . . . . . . . . 4296 1 473 . 1 1 44 44 SER N N 15 113.8 0.10 . 1 . . . . . . . . 4296 1 474 . 1 1 45 45 LEU H H 1 5.85 0.02 . 1 . . . . . . . . 4296 1 475 . 1 1 45 45 LEU HA H 1 4.44 0.02 . 1 . . . . . . . . 4296 1 476 . 1 1 45 45 LEU HB2 H 1 1.01 0.02 . 2 . . . . . . . . 4296 1 477 . 1 1 45 45 LEU HB3 H 1 0.43 0.02 . 2 . . . . . . . . 4296 1 478 . 1 1 45 45 LEU HG H 1 0.78 0.02 . 1 . . . . . . . . 4296 1 479 . 1 1 45 45 LEU HD11 H 1 0.48 0.02 . 2 . . . . . . . . 4296 1 480 . 1 1 45 45 LEU HD12 H 1 0.48 0.02 . 2 . . . . . . . . 4296 1 481 . 1 1 45 45 LEU HD13 H 1 0.48 0.02 . 2 . . . . . . . . 4296 1 482 . 1 1 45 45 LEU HD21 H 1 0.29 0.02 . 2 . . . . . . . . 4296 1 483 . 1 1 45 45 LEU HD22 H 1 0.29 0.02 . 2 . . . . . . . . 4296 1 484 . 1 1 45 45 LEU HD23 H 1 0.29 0.02 . 2 . . . . . . . . 4296 1 485 . 1 1 45 45 LEU C C 13 174.1 0.10 . 1 . . . . . . . . 4296 1 486 . 1 1 45 45 LEU CA C 13 52.7 0.10 . 1 . . . . . . . . 4296 1 487 . 1 1 45 45 LEU CB C 13 44.9 0.10 . 1 . . . . . . . . 4296 1 488 . 1 1 45 45 LEU CG C 13 32.7 0.10 . 1 . . . . . . . . 4296 1 489 . 1 1 45 45 LEU CD1 C 13 24.2 0.10 . 1 . . . . . . . . 4296 1 490 . 1 1 45 45 LEU CD2 C 13 24.2 0.10 . 1 . . . . . . . . 4296 1 491 . 1 1 45 45 LEU N N 15 119.1 0.10 . 1 . . . . . . . . 4296 1 492 . 1 1 46 46 ASP H H 1 8.21 0.02 . 1 . . . . . . . . 4296 1 493 . 1 1 46 46 ASP HA H 1 4.89 0.02 . 1 . . . . . . . . 4296 1 494 . 1 1 46 46 ASP HB2 H 1 2.62 0.02 . 2 . . . . . . . . 4296 1 495 . 1 1 46 46 ASP HB3 H 1 2.37 0.02 . 2 . . . . . . . . 4296 1 496 . 1 1 46 46 ASP C C 13 175.5 0.10 . 1 . . . . . . . . 4296 1 497 . 1 1 46 46 ASP CA C 13 52.6 0.10 . 1 . . . . . . . . 4296 1 498 . 1 1 46 46 ASP CB C 13 43.8 0.10 . 1 . . . . . . . . 4296 1 499 . 1 1 46 46 ASP N N 15 120.1 0.10 . 1 . . . . . . . . 4296 1 500 . 1 1 47 47 GLU H H 1 8.66 0.02 . 1 . . . . . . . . 4296 1 501 . 1 1 47 47 GLU HA H 1 3.58 0.02 . 1 . . . . . . . . 4296 1 502 . 1 1 47 47 GLU HB2 H 1 2.16 0.02 . 2 . . . . . . . . 4296 1 503 . 1 1 47 47 GLU HB3 H 1 2.01 0.02 . 2 . . . . . . . . 4296 1 504 . 1 1 47 47 GLU HG2 H 1 2.55 0.02 . 2 . . . . . . . . 4296 1 505 . 1 1 47 47 GLU HG3 H 1 2.24 0.02 . 2 . . . . . . . . 4296 1 506 . 1 1 47 47 GLU C C 13 177.3 0.10 . 1 . . . . . . . . 4296 1 507 . 1 1 47 47 GLU CA C 13 58.0 0.10 . 1 . . . . . . . . 4296 1 508 . 1 1 47 47 GLU CB C 13 29.4 0.10 . 1 . . . . . . . . 4296 1 509 . 1 1 47 47 GLU CG C 13 35.5 0.10 . 1 . . . . . . . . 4296 1 510 . 1 1 47 47 GLU N N 15 120.9 0.10 . 1 . . . . . . . . 4296 1 511 . 1 1 48 48 GLY H H 1 9.12 0.02 . 1 . . . . . . . . 4296 1 512 . 1 1 48 48 GLY HA2 H 1 4.35 0.02 . 2 . . . . . . . . 4296 1 513 . 1 1 48 48 GLY HA3 H 1 3.58 0.02 . 2 . . . . . . . . 4296 1 514 . 1 1 48 48 GLY C C 13 173.6 0.10 . 1 . . . . . . . . 4296 1 515 . 1 1 48 48 GLY CA C 13 45.2 0.10 . 1 . . . . . . . . 4296 1 516 . 1 1 48 48 GLY N N 15 113.6 0.10 . 1 . . . . . . . . 4296 1 517 . 1 1 49 49 GLN H H 1 7.77 0.02 . 1 . . . . . . . . 4296 1 518 . 1 1 49 49 GLN HA H 1 4.18 0.02 . 1 . . . . . . . . 4296 1 519 . 1 1 49 49 GLN HB2 H 1 2.21 0.02 . 2 . . . . . . . . 4296 1 520 . 1 1 49 49 GLN HB3 H 1 1.96 0.02 . 2 . . . . . . . . 4296 1 521 . 1 1 49 49 GLN HG2 H 1 2.37 0.02 . 1 . . . . . . . . 4296 1 522 . 1 1 49 49 GLN HG3 H 1 2.37 0.02 . 1 . . . . . . . . 4296 1 523 . 1 1 49 49 GLN HE21 H 1 7.55 0.02 . 1 . . . . . . . . 4296 1 524 . 1 1 49 49 GLN HE22 H 1 6.81 0.02 . 1 . . . . . . . . 4296 1 525 . 1 1 49 49 GLN C C 13 175.6 0.10 . 1 . . . . . . . . 4296 1 526 . 1 1 49 49 GLN CA C 13 56.3 0.10 . 1 . . . . . . . . 4296 1 527 . 1 1 49 49 GLN CB C 13 30.3 0.10 . 1 . . . . . . . . 4296 1 528 . 1 1 49 49 GLN CG C 13 33.7 0.10 . 1 . . . . . . . . 4296 1 529 . 1 1 49 49 GLN N N 15 120.6 0.10 . 1 . . . . . . . . 4296 1 530 . 1 1 49 49 GLN NE2 N 15 111.0 0.10 . 1 . . . . . . . . 4296 1 531 . 1 1 50 50 LYS H H 1 8.79 0.02 . 1 . . . . . . . . 4296 1 532 . 1 1 50 50 LYS HA H 1 5.05 0.02 . 1 . . . . . . . . 4296 1 533 . 1 1 50 50 LYS HB2 H 1 1.91 0.02 . 1 . . . . . . . . 4296 1 534 . 1 1 50 50 LYS HB3 H 1 1.91 0.02 . 1 . . . . . . . . 4296 1 535 . 1 1 50 50 LYS HG2 H 1 1.71 0.02 . 2 . . . . . . . . 4296 1 536 . 1 1 50 50 LYS HG3 H 1 1.50 0.02 . 2 . . . . . . . . 4296 1 537 . 1 1 50 50 LYS HD2 H 1 1.79 0.02 . 1 . . . . . . . . 4296 1 538 . 1 1 50 50 LYS HD3 H 1 1.79 0.02 . 1 . . . . . . . . 4296 1 539 . 1 1 50 50 LYS HE2 H 1 3.02 0.02 . 1 . . . . . . . . 4296 1 540 . 1 1 50 50 LYS HE3 H 1 3.02 0.02 . 1 . . . . . . . . 4296 1 541 . 1 1 50 50 LYS C C 13 177.1 0.10 . 1 . . . . . . . . 4296 1 542 . 1 1 50 50 LYS CA C 13 56.3 0.10 . 1 . . . . . . . . 4296 1 543 . 1 1 50 50 LYS CB C 13 32.9 0.10 . 1 . . . . . . . . 4296 1 544 . 1 1 50 50 LYS CG C 13 25.0 0.10 . 1 . . . . . . . . 4296 1 545 . 1 1 50 50 LYS CD C 13 28.6 0.10 . 1 . . . . . . . . 4296 1 546 . 1 1 50 50 LYS CE C 13 42.1 0.10 . 1 . . . . . . . . 4296 1 547 . 1 1 50 50 LYS N N 15 126.6 0.10 . 1 . . . . . . . . 4296 1 548 . 1 1 51 51 VAL H H 1 8.63 0.02 . 1 . . . . . . . . 4296 1 549 . 1 1 51 51 VAL HA H 1 5.35 0.02 . 1 . . . . . . . . 4296 1 550 . 1 1 51 51 VAL HB H 1 2.17 0.02 . 1 . . . . . . . . 4296 1 551 . 1 1 51 51 VAL HG11 H 1 0.62 0.02 . 2 . . . . . . . . 4296 1 552 . 1 1 51 51 VAL HG12 H 1 0.62 0.02 . 2 . . . . . . . . 4296 1 553 . 1 1 51 51 VAL HG13 H 1 0.62 0.02 . 2 . . . . . . . . 4296 1 554 . 1 1 51 51 VAL HG21 H 1 0.52 0.02 . 2 . . . . . . . . 4296 1 555 . 1 1 51 51 VAL HG22 H 1 0.52 0.02 . 2 . . . . . . . . 4296 1 556 . 1 1 51 51 VAL HG23 H 1 0.52 0.02 . 2 . . . . . . . . 4296 1 557 . 1 1 51 51 VAL C C 13 174.3 0.10 . 1 . . . . . . . . 4296 1 558 . 1 1 51 51 VAL CA C 13 58.4 0.10 . 1 . . . . . . . . 4296 1 559 . 1 1 51 51 VAL CB C 13 36.8 0.10 . 1 . . . . . . . . 4296 1 560 . 1 1 51 51 VAL CG1 C 13 22.2 0.10 . 2 . . . . . . . . 4296 1 561 . 1 1 51 51 VAL CG2 C 13 17.6 0.10 . 2 . . . . . . . . 4296 1 562 . 1 1 51 51 VAL N N 15 115.5 0.10 . 1 . . . . . . . . 4296 1 563 . 1 1 52 52 SER H H 1 9.14 0.02 . 1 . . . . . . . . 4296 1 564 . 1 1 52 52 SER HA H 1 5.70 0.02 . 1 . . . . . . . . 4296 1 565 . 1 1 52 52 SER HB2 H 1 3.83 0.02 . 2 . . . . . . . . 4296 1 566 . 1 1 52 52 SER HB3 H 1 3.75 0.02 . 2 . . . . . . . . 4296 1 567 . 1 1 52 52 SER C C 13 173.9 0.10 . 1 . . . . . . . . 4296 1 568 . 1 1 52 52 SER CA C 13 55.8 0.10 . 1 . . . . . . . . 4296 1 569 . 1 1 52 52 SER CB C 13 65.7 0.10 . 1 . . . . . . . . 4296 1 570 . 1 1 52 52 SER N N 15 114.7 0.10 . 1 . . . . . . . . 4296 1 571 . 1 1 53 53 PHE H H 1 8.70 0.02 . 1 . . . . . . . . 4296 1 572 . 1 1 53 53 PHE HA H 1 5.28 0.02 . 1 . . . . . . . . 4296 1 573 . 1 1 53 53 PHE HB2 H 1 3.27 0.02 . 2 . . . . . . . . 4296 1 574 . 1 1 53 53 PHE HB3 H 1 3.20 0.02 . 2 . . . . . . . . 4296 1 575 . 1 1 53 53 PHE HD1 H 1 6.84 0.02 . 1 . . . . . . . . 4296 1 576 . 1 1 53 53 PHE HD2 H 1 6.84 0.02 . 1 . . . . . . . . 4296 1 577 . 1 1 53 53 PHE HE1 H 1 6.77 0.02 . 1 . . . . . . . . 4296 1 578 . 1 1 53 53 PHE HE2 H 1 6.77 0.02 . 1 . . . . . . . . 4296 1 579 . 1 1 53 53 PHE HZ H 1 6.96 0.02 . 1 . . . . . . . . 4296 1 580 . 1 1 53 53 PHE C C 13 172.8 0.10 . 1 . . . . . . . . 4296 1 581 . 1 1 53 53 PHE CA C 13 56.2 0.10 . 1 . . . . . . . . 4296 1 582 . 1 1 53 53 PHE CB C 13 40.2 0.10 . 1 . . . . . . . . 4296 1 583 . 1 1 53 53 PHE N N 15 117.3 0.10 . 1 . . . . . . . . 4296 1 584 . 1 1 54 54 THR H H 1 8.99 0.02 . 1 . . . . . . . . 4296 1 585 . 1 1 54 54 THR HA H 1 4.71 0.02 . 1 . . . . . . . . 4296 1 586 . 1 1 54 54 THR HB H 1 4.20 0.02 . 1 . . . . . . . . 4296 1 587 . 1 1 54 54 THR HG21 H 1 1.15 0.02 . 1 . . . . . . . . 4296 1 588 . 1 1 54 54 THR HG22 H 1 1.15 0.02 . 1 . . . . . . . . 4296 1 589 . 1 1 54 54 THR HG23 H 1 1.15 0.02 . 1 . . . . . . . . 4296 1 590 . 1 1 54 54 THR C C 13 174.5 0.10 . 1 . . . . . . . . 4296 1 591 . 1 1 54 54 THR CA C 13 59.9 0.10 . 1 . . . . . . . . 4296 1 592 . 1 1 54 54 THR CB C 13 70.4 0.10 . 1 . . . . . . . . 4296 1 593 . 1 1 54 54 THR CG2 C 13 22.5 0.10 . 1 . . . . . . . . 4296 1 594 . 1 1 54 54 THR N N 15 110.4 0.10 . 1 . . . . . . . . 4296 1 595 . 1 1 55 55 ILE H H 1 8.66 0.02 . 1 . . . . . . . . 4296 1 596 . 1 1 55 55 ILE HA H 1 4.69 0.02 . 1 . . . . . . . . 4296 1 597 . 1 1 55 55 ILE HB H 1 1.82 0.02 . 1 . . . . . . . . 4296 1 598 . 1 1 55 55 ILE HG21 H 1 0.95 0.02 . 1 . . . . . . . . 4296 1 599 . 1 1 55 55 ILE HG22 H 1 0.95 0.02 . 1 . . . . . . . . 4296 1 600 . 1 1 55 55 ILE HG23 H 1 0.95 0.02 . 1 . . . . . . . . 4296 1 601 . 1 1 55 55 ILE HG12 H 1 1.72 0.02 . 2 . . . . . . . . 4296 1 602 . 1 1 55 55 ILE HG13 H 1 1.16 0.02 . 2 . . . . . . . . 4296 1 603 . 1 1 55 55 ILE HD11 H 1 1.01 0.02 . 1 . . . . . . . . 4296 1 604 . 1 1 55 55 ILE HD12 H 1 1.01 0.02 . 1 . . . . . . . . 4296 1 605 . 1 1 55 55 ILE HD13 H 1 1.01 0.02 . 1 . . . . . . . . 4296 1 606 . 1 1 55 55 ILE C C 13 175.6 0.10 . 1 . . . . . . . . 4296 1 607 . 1 1 55 55 ILE CA C 13 61.0 0.10 . 1 . . . . . . . . 4296 1 608 . 1 1 55 55 ILE CB C 13 39.0 0.10 . 1 . . . . . . . . 4296 1 609 . 1 1 55 55 ILE CG1 C 13 28.0 0.10 . 1 . . . . . . . . 4296 1 610 . 1 1 55 55 ILE CG2 C 13 17.9 0.10 . 1 . . . . . . . . 4296 1 611 . 1 1 55 55 ILE CD1 C 13 13.6 0.10 . 1 . . . . . . . . 4296 1 612 . 1 1 55 55 ILE N N 15 120.9 0.10 . 1 . . . . . . . . 4296 1 613 . 1 1 56 56 GLU H H 1 9.18 0.02 . 1 . . . . . . . . 4296 1 614 . 1 1 56 56 GLU HA H 1 4.67 0.02 . 1 . . . . . . . . 4296 1 615 . 1 1 56 56 GLU HB2 H 1 2.06 0.02 . 1 . . . . . . . . 4296 1 616 . 1 1 56 56 GLU HB3 H 1 1.84 0.02 . 1 . . . . . . . . 4296 1 617 . 1 1 56 56 GLU HG2 H 1 2.22 0.02 . 2 . . . . . . . . 4296 1 618 . 1 1 56 56 GLU HG3 H 1 2.13 0.02 . 2 . . . . . . . . 4296 1 619 . 1 1 56 56 GLU C C 13 176.0 0.10 . 1 . . . . . . . . 4296 1 620 . 1 1 56 56 GLU CA C 13 54.2 0.10 . 1 . . . . . . . . 4296 1 621 . 1 1 56 56 GLU CB C 13 31.5 0.10 . 1 . . . . . . . . 4296 1 622 . 1 1 56 56 GLU CG C 13 35.2 0.10 . 1 . . . . . . . . 4296 1 623 . 1 1 56 56 GLU N N 15 127.9 0.10 . 1 . . . . . . . . 4296 1 624 . 1 1 57 57 SER H H 1 8.77 0.02 . 1 . . . . . . . . 4296 1 625 . 1 1 57 57 SER HA H 1 4.50 0.02 . 1 . . . . . . . . 4296 1 626 . 1 1 57 57 SER HB2 H 1 3.88 0.02 . 2 . . . . . . . . 4296 1 627 . 1 1 57 57 SER HB3 H 1 3.79 0.02 . 2 . . . . . . . . 4296 1 628 . 1 1 57 57 SER C C 13 174.4 0.10 . 1 . . . . . . . . 4296 1 629 . 1 1 57 57 SER CA C 13 58.0 0.10 . 1 . . . . . . . . 4296 1 630 . 1 1 57 57 SER CB C 13 62.9 0.10 . 1 . . . . . . . . 4296 1 631 . 1 1 57 57 SER N N 15 118.4 0.10 . 1 . . . . . . . . 4296 1 632 . 1 1 58 58 GLY H H 1 7.82 0.02 . 1 . . . . . . . . 4296 1 633 . 1 1 58 58 GLY HA2 H 1 4.30 0.02 . 2 . . . . . . . . 4296 1 634 . 1 1 58 58 GLY HA3 H 1 3.93 0.02 . 2 . . . . . . . . 4296 1 635 . 1 1 58 58 GLY C C 13 174.6 0.10 . 1 . . . . . . . . 4296 1 636 . 1 1 58 58 GLY CA C 13 44.5 0.10 . 1 . . . . . . . . 4296 1 637 . 1 1 58 58 GLY N N 15 111.9 0.10 . 1 . . . . . . . . 4296 1 638 . 1 1 59 59 ALA H H 1 8.59 0.02 . 1 . . . . . . . . 4296 1 639 . 1 1 59 59 ALA HA H 1 4.13 0.02 . 1 . . . . . . . . 4296 1 640 . 1 1 59 59 ALA HB1 H 1 1.40 0.02 . 1 . . . . . . . . 4296 1 641 . 1 1 59 59 ALA HB2 H 1 1.40 0.02 . 1 . . . . . . . . 4296 1 642 . 1 1 59 59 ALA HB3 H 1 1.40 0.02 . 1 . . . . . . . . 4296 1 643 . 1 1 59 59 ALA C C 13 179.1 0.10 . 1 . . . . . . . . 4296 1 644 . 1 1 59 59 ALA CA C 13 54.3 0.10 . 1 . . . . . . . . 4296 1 645 . 1 1 59 59 ALA CB C 13 18.7 0.10 . 1 . . . . . . . . 4296 1 646 . 1 1 59 59 ALA N N 15 123.5 0.10 . 1 . . . . . . . . 4296 1 647 . 1 1 60 60 LYS H H 1 8.37 0.02 . 1 . . . . . . . . 4296 1 648 . 1 1 60 60 LYS HA H 1 4.37 0.02 . 1 . . . . . . . . 4296 1 649 . 1 1 60 60 LYS HB2 H 1 1.80 0.02 . 2 . . . . . . . . 4296 1 650 . 1 1 60 60 LYS HB3 H 1 1.53 0.02 . 2 . . . . . . . . 4296 1 651 . 1 1 60 60 LYS HG2 H 1 1.27 0.02 . 2 . . . . . . . . 4296 1 652 . 1 1 60 60 LYS HG3 H 1 1.15 0.02 . 2 . . . . . . . . 4296 1 653 . 1 1 60 60 LYS HD2 H 1 1.50 0.02 . 1 . . . . . . . . 4296 1 654 . 1 1 60 60 LYS HD3 H 1 1.50 0.02 . 1 . . . . . . . . 4296 1 655 . 1 1 60 60 LYS HE2 H 1 2.82 0.02 . 1 . . . . . . . . 4296 1 656 . 1 1 60 60 LYS HE3 H 1 2.82 0.02 . 1 . . . . . . . . 4296 1 657 . 1 1 60 60 LYS C C 13 175.9 0.10 . 1 . . . . . . . . 4296 1 658 . 1 1 60 60 LYS CA C 13 55.2 0.10 . 1 . . . . . . . . 4296 1 659 . 1 1 60 60 LYS CB C 13 31.8 0.10 . 1 . . . . . . . . 4296 1 660 . 1 1 60 60 LYS CG C 13 24.7 0.10 . 1 . . . . . . . . 4296 1 661 . 1 1 60 60 LYS CD C 13 28.4 0.10 . 1 . . . . . . . . 4296 1 662 . 1 1 60 60 LYS CE C 13 42.1 0.10 . 1 . . . . . . . . 4296 1 663 . 1 1 60 60 LYS N N 15 115.2 0.10 . 1 . . . . . . . . 4296 1 664 . 1 1 61 61 GLY H H 1 7.51 0.02 . 1 . . . . . . . . 4296 1 665 . 1 1 61 61 GLY HA2 H 1 4.36 0.02 . 2 . . . . . . . . 4296 1 666 . 1 1 61 61 GLY HA3 H 1 3.83 0.02 . 2 . . . . . . . . 4296 1 667 . 1 1 61 61 GLY CA C 13 44.2 0.10 . 1 . . . . . . . . 4296 1 668 . 1 1 61 61 GLY N N 15 108.2 0.10 . 1 . . . . . . . . 4296 1 669 . 1 1 62 62 PRO HA H 1 4.89 0.02 . 1 . . . . . . . . 4296 1 670 . 1 1 62 62 PRO HB2 H 1 2.32 0.02 . 2 . . . . . . . . 4296 1 671 . 1 1 62 62 PRO HB3 H 1 1.94 0.02 . 2 . . . . . . . . 4296 1 672 . 1 1 62 62 PRO HG2 H 1 2.24 0.02 . 2 . . . . . . . . 4296 1 673 . 1 1 62 62 PRO HG3 H 1 2.09 0.02 . 2 . . . . . . . . 4296 1 674 . 1 1 62 62 PRO HD2 H 1 3.74 0.02 . 2 . . . . . . . . 4296 1 675 . 1 1 62 62 PRO HD3 H 1 3.68 0.02 . 2 . . . . . . . . 4296 1 676 . 1 1 62 62 PRO C C 13 175.6 0.10 . 1 . . . . . . . . 4296 1 677 . 1 1 62 62 PRO CA C 13 63.0 0.10 . 1 . . . . . . . . 4296 1 678 . 1 1 62 62 PRO CB C 13 32.7 0.10 . 1 . . . . . . . . 4296 1 679 . 1 1 62 62 PRO CG C 13 29.9 0.10 . 1 . . . . . . . . 4296 1 680 . 1 1 62 62 PRO CD C 13 56.0 0.10 . 1 . . . . . . . . 4296 1 681 . 1 1 63 63 ALA H H 1 8.79 0.02 . 1 . . . . . . . . 4296 1 682 . 1 1 63 63 ALA HA H 1 5.18 0.02 . 1 . . . . . . . . 4296 1 683 . 1 1 63 63 ALA HB1 H 1 1.51 0.02 . 1 . . . . . . . . 4296 1 684 . 1 1 63 63 ALA HB2 H 1 1.51 0.02 . 1 . . . . . . . . 4296 1 685 . 1 1 63 63 ALA HB3 H 1 1.51 0.02 . 1 . . . . . . . . 4296 1 686 . 1 1 63 63 ALA C C 13 175.2 0.10 . 1 . . . . . . . . 4296 1 687 . 1 1 63 63 ALA CA C 13 50.7 0.10 . 1 . . . . . . . . 4296 1 688 . 1 1 63 63 ALA CB C 13 22.0 0.10 . 1 . . . . . . . . 4296 1 689 . 1 1 63 63 ALA N N 15 126.0 0.10 . 1 . . . . . . . . 4296 1 690 . 1 1 64 64 ALA H H 1 8.90 0.02 . 1 . . . . . . . . 4296 1 691 . 1 1 64 64 ALA HA H 1 5.09 0.02 . 1 . . . . . . . . 4296 1 692 . 1 1 64 64 ALA HB1 H 1 0.95 0.02 . 1 . . . . . . . . 4296 1 693 . 1 1 64 64 ALA HB2 H 1 0.95 0.02 . 1 . . . . . . . . 4296 1 694 . 1 1 64 64 ALA HB3 H 1 0.95 0.02 . 1 . . . . . . . . 4296 1 695 . 1 1 64 64 ALA C C 13 177.4 0.10 . 1 . . . . . . . . 4296 1 696 . 1 1 64 64 ALA CA C 13 50.9 0.10 . 1 . . . . . . . . 4296 1 697 . 1 1 64 64 ALA CB C 13 20.1 0.10 . 1 . . . . . . . . 4296 1 698 . 1 1 64 64 ALA N N 15 122.1 0.10 . 1 . . . . . . . . 4296 1 699 . 1 1 65 65 GLY H H 1 9.29 0.02 . 1 . . . . . . . . 4296 1 700 . 1 1 65 65 GLY HA2 H 1 4.67 0.02 . 2 . . . . . . . . 4296 1 701 . 1 1 65 65 GLY HA3 H 1 3.59 0.02 . 2 . . . . . . . . 4296 1 702 . 1 1 65 65 GLY C C 13 172.9 0.10 . 1 . . . . . . . . 4296 1 703 . 1 1 65 65 GLY CA C 13 43.5 0.10 . 1 . . . . . . . . 4296 1 704 . 1 1 65 65 GLY N N 15 108.7 0.10 . 1 . . . . . . . . 4296 1 705 . 1 1 66 66 ASN H H 1 9.22 0.02 . 1 . . . . . . . . 4296 1 706 . 1 1 66 66 ASN HA H 1 4.18 0.02 . 1 . . . . . . . . 4296 1 707 . 1 1 66 66 ASN HB2 H 1 2.81 0.02 . 1 . . . . . . . . 4296 1 708 . 1 1 66 66 ASN HB3 H 1 2.81 0.02 . 1 . . . . . . . . 4296 1 709 . 1 1 66 66 ASN HD21 H 1 7.57 0.02 . 1 . . . . . . . . 4296 1 710 . 1 1 66 66 ASN HD22 H 1 6.87 0.02 . 1 . . . . . . . . 4296 1 711 . 1 1 66 66 ASN C C 13 174.1 0.10 . 1 . . . . . . . . 4296 1 712 . 1 1 66 66 ASN CA C 13 54.3 0.10 . 1 . . . . . . . . 4296 1 713 . 1 1 66 66 ASN CB C 13 38.0 0.10 . 1 . . . . . . . . 4296 1 714 . 1 1 66 66 ASN N N 15 116.4 0.10 . 1 . . . . . . . . 4296 1 715 . 1 1 66 66 ASN ND2 N 15 114.4 0.10 . 1 . . . . . . . . 4296 1 716 . 1 1 67 67 VAL H H 1 8.19 0.02 . 1 . . . . . . . . 4296 1 717 . 1 1 67 67 VAL HA H 1 4.68 0.02 . 1 . . . . . . . . 4296 1 718 . 1 1 67 67 VAL HB H 1 1.82 0.02 . 1 . . . . . . . . 4296 1 719 . 1 1 67 67 VAL HG11 H 1 0.68 0.02 . 1 . . . . . . . . 4296 1 720 . 1 1 67 67 VAL HG12 H 1 0.68 0.02 . 1 . . . . . . . . 4296 1 721 . 1 1 67 67 VAL HG13 H 1 0.68 0.02 . 1 . . . . . . . . 4296 1 722 . 1 1 67 67 VAL HG21 H 1 0.68 0.02 . 1 . . . . . . . . 4296 1 723 . 1 1 67 67 VAL HG22 H 1 0.68 0.02 . 1 . . . . . . . . 4296 1 724 . 1 1 67 67 VAL HG23 H 1 0.68 0.02 . 1 . . . . . . . . 4296 1 725 . 1 1 67 67 VAL C C 13 176.0 0.10 . 1 . . . . . . . . 4296 1 726 . 1 1 67 67 VAL CA C 13 63.3 0.10 . 1 . . . . . . . . 4296 1 727 . 1 1 67 67 VAL CB C 13 31.0 0.10 . 1 . . . . . . . . 4296 1 728 . 1 1 67 67 VAL CG1 C 13 21.4 0.10 . 1 . . . . . . . . 4296 1 729 . 1 1 67 67 VAL CG2 C 13 21.4 0.10 . 1 . . . . . . . . 4296 1 730 . 1 1 67 67 VAL N N 15 118.1 0.10 . 1 . . . . . . . . 4296 1 731 . 1 1 68 68 THR H H 1 9.05 0.02 . 1 . . . . . . . . 4296 1 732 . 1 1 68 68 THR HA H 1 4.76 0.02 . 1 . . . . . . . . 4296 1 733 . 1 1 68 68 THR HB H 1 4.16 0.02 . 1 . . . . . . . . 4296 1 734 . 1 1 68 68 THR HG21 H 1 1.13 0.02 . 1 . . . . . . . . 4296 1 735 . 1 1 68 68 THR HG22 H 1 1.13 0.02 . 1 . . . . . . . . 4296 1 736 . 1 1 68 68 THR HG23 H 1 1.13 0.02 . 1 . . . . . . . . 4296 1 737 . 1 1 68 68 THR C C 13 173.9 0.10 . 1 . . . . . . . . 4296 1 738 . 1 1 68 68 THR CA C 13 59.6 0.10 . 1 . . . . . . . . 4296 1 739 . 1 1 68 68 THR CB C 13 71.7 0.10 . 1 . . . . . . . . 4296 1 740 . 1 1 68 68 THR N N 15 120.6 0.10 . 1 . . . . . . . . 4296 1 741 . 1 1 69 69 SER H H 1 8.81 0.02 . 1 . . . . . . . . 4296 1 742 . 1 1 69 69 SER HA H 1 4.66 0.02 . 1 . . . . . . . . 4296 1 743 . 1 1 69 69 SER HB3 H 1 3.93 0.02 . 1 . . . . . . . . 4296 1 744 . 1 1 69 69 SER HB2 H 1 3.83 0.02 . 1 . . . . . . . . 4296 1 745 . 1 1 69 69 SER C C 13 173.8 0.10 . 1 . . . . . . . . 4296 1 746 . 1 1 69 69 SER CA C 13 59.3 0.10 . 1 . . . . . . . . 4296 1 747 . 1 1 69 69 SER CB C 13 63.2 0.10 . 1 . . . . . . . . 4296 1 748 . 1 1 69 69 SER N N 15 119.5 0.10 . 1 . . . . . . . . 4296 1 749 . 1 1 70 70 LEU H H 1 8.00 0.02 . 1 . . . . . . . . 4296 1 750 . 1 1 70 70 LEU HA H 1 4.26 0.02 . 1 . . . . . . . . 4296 1 751 . 1 1 70 70 LEU HB2 H 1 1.39 0.02 . 1 . . . . . . . . 4296 1 752 . 1 1 70 70 LEU HB3 H 1 1.39 0.02 . 1 . . . . . . . . 4296 1 753 . 1 1 70 70 LEU HG H 1 1.61 0.02 . 1 . . . . . . . . 4296 1 754 . 1 1 70 70 LEU HD11 H 1 0.89 0.02 . 1 . . . . . . . . 4296 1 755 . 1 1 70 70 LEU HD12 H 1 0.89 0.02 . 1 . . . . . . . . 4296 1 756 . 1 1 70 70 LEU HD13 H 1 0.89 0.02 . 1 . . . . . . . . 4296 1 757 . 1 1 70 70 LEU HD21 H 1 0.89 0.02 . 1 . . . . . . . . 4296 1 758 . 1 1 70 70 LEU HD22 H 1 0.89 0.02 . 1 . . . . . . . . 4296 1 759 . 1 1 70 70 LEU HD23 H 1 0.89 0.02 . 1 . . . . . . . . 4296 1 760 . 1 1 70 70 LEU CA C 13 56.3 0.10 . 1 . . . . . . . . 4296 1 761 . 1 1 70 70 LEU CB C 13 43.3 0.10 . 1 . . . . . . . . 4296 1 762 . 1 1 70 70 LEU CG C 13 27.8 0.10 . 1 . . . . . . . . 4296 1 763 . 1 1 70 70 LEU CD1 C 13 26.4 0.10 . 2 . . . . . . . . 4296 1 764 . 1 1 70 70 LEU CD2 C 13 24.3 0.10 . 2 . . . . . . . . 4296 1 765 . 1 1 70 70 LEU N N 15 131.1 0.10 . 1 . . . . . . . . 4296 1 stop_ save_