data_4352 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Inhibitor-Bound DNase Domain of Colicin E9. ; _BMRB_accession_number 4352 _BMRB_flat_file_name bmr4352.str _Entry_type original _Submission_date 1999-06-14 _Accession_date 1999-07-02 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Whittaker Sara B.-M. . 2 Czisch Michael . . 3 Wechselberger Rainer . . 4 Kaptein Robert . . 5 Hemmings Andrew M. . 6 James Richard . . 7 Kleanthous Colin . . 8 Moore Geoffrey R. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 460 "13C chemical shifts" 420 "15N chemical shifts" 156 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-10-07 original author 'original release' 2006-10-27 update BMRB 'update the relationship loop' stop_ loop_ _Related_BMRB_accession_number _Relationship 4115 'homologous Immunity protein Im9 bound to DNase domain of colicin E9' 4116 'homologous Immunity protein Im9' 4293 'DNase domain of non cognate binding partner E9' 7323 'Colicin immunity protein IM2' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Whittaker, S. B.-M., Czisch, M., Wechselberger, R., Kaptein, R., Hemmings, A. M., James, R., Kleanthous, C., and Moore, G. R., "Slow Conformational Dynamics of an Endonuclease Persist in its Complex with its Natural Protein Inhibitor," Protein Sci. 9, 713-720 (2000). ; _Citation_title ; Slow Conformational Dynamics of an Endonuclease Persist in its Complex with its Natural Protein Inhibitor ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20252387 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Whittaker Sara B.-M. . 2 Czisch Michael . . 3 Wechselberger Rainer . . 4 Kaptein Robert . . 5 Hemmings Andrew M. . 6 James Richard . . 7 Kleanthous Colin . . 8 Moore Geoffrey R. . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein Science' _Journal_volume 9 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 713 _Page_last 720 _Year 2000 _Details . loop_ _Keyword 'chemical exchange' colicin EXSY 'immunity protein' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J. & Bax, A. (1995) J. Biomol. NMR 6, 277-293 ; _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F . . 2 Grzesiek S . . 3 Vuister 'G W' W. . 4 Zhu G . . 5 Pfeifer J . . 6 Bax A . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ save_citation_two _Saveframe_category citation _Citation_full ; Bartels, C., Xia, T.-H., Billeter, M., Guentert, P. & Wuethrich, K. (1995) J. Biomol. NMR 6, 1-10 ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_citation_three _Saveframe_category citation _Citation_full 'Eaton, T. & James, R. (1989) Nucleic Acids Res. 17, 1761-1761' _Citation_title 'Complete nucleotide sequence of the colicin E9 (cei) gene.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 2646600 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Eaton T . . 2 James R . . stop_ _Journal_abbreviation 'Nucleic Acids Res.' _Journal_name_full 'Nucleic acids research' _Journal_volume 17 _Journal_issue 4 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1761 _Page_last 1761 _Year 1989 _Details . save_ save_citation_four _Saveframe_category citation _Citation_full 'James, R., Jarvis, M. & Barker, D.F. (1987) J. Gen. Microbiol. 133, 1553-1562.' _Citation_title 'Nucleotide sequence of the immunity and lysis region of the ColE9-J plasmid.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 3312476 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 James R . . 2 Jarvis M . . 3 Barker 'D F' F. . stop_ _Journal_abbreviation 'J. Gen. Microbiol.' _Journal_name_full 'Journal of general microbiology' _Journal_volume 133 _Journal_issue 6 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1553 _Page_last 1562 _Year 1987 _Details ; We have determined the nucleotide sequence of a 1500 bp fragment of the ColE9-J plasmid which encodes colicin E9 immunity and colicin E5 immunity and contains two lys genes. Open reading frames corresponding to the four genes have been located and their position confirmed by transposon mutagenesis of sub-clones of the ColE9-J plasmid. The E9imm gene shows 69% homology at both the nucleotide and the amino acid level to the previously sequenced E2imm gene. The E5imm gene shows little homology to any other E colicin immunity gene which has been sequenced. The lys gene distal to the 3' end of the E5imm gene shows considerable sequence homology to all other previously sequenced E colicin lys genes. The lys gene distal to the 3' end of the E9imm gene is identical to the pColE2 and pColE3 lys genes for the first 59 nucleotides but encodes a much smaller gene product than any other lys gene which has been sequenced. The two lys genes sequenced here are exceptions to Shepherd's rule concerning the number of RNY codons in the three possible reading frames. ; save_ ################################## # Molecular system description # ################################## save_E9_DNase-Im9 _Saveframe_category molecular_system _Mol_system_name 'Inhibitor (Im9)-bound DNase domain of colicin E9' _Abbreviation_common 'E9 DNase-Im9' _Enzyme_commission_number 3.1.21.1 loop_ _Mol_system_component_name _Mol_label 'E9 DNase' $E9_DNase Im9 $Im9 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function ; The E9 DNase forms the cytotoxic domain of colicin E9 and is located at its C-terminus (the last 134 residues). It acts as an endonuclease and is active on both single- and double-stranded DNA but with undefined specificity. Colicins are plasmid-encoded protein antibiotics produced by, and active against, Eschericia coli and closely related bacteria. The cytotoxic activity of colicin E9 is neutralised by the binding of its 9.5 kDa cognate immunity protein, Im9, to the E9 DNase. ; stop_ _Database_query_date . _Details ; The DNase domain of colicin E9 (E9 DNase) represents the 134 C-terminal-most residues of intact colicin E9, with a methionine residue substituted for a lysine at the N-terminus. In this study, isotopically labelled E9 DNase is in complex with its unlabelled inhibitor protein, Im9. Thus, only the E9 DNase component is observed. The crystal structure of the E9 DNase-Im9 complex contains a Ni2+ ion in the putative active site of E9 DNase. In this study, E9 DNase in complex with Im9 is metal-free in solution. ; save_ ######################## # Monomeric polymers # ######################## save_E9_DNase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'DNase domain of colicin E9' _Abbreviation_common 'E9 DNase' _Molecular_mass 15090 _Mol_thiol_state . _Details ; E9 DNase exists as two conformers in solution (60:40) that undergo slow chemical exchange. This conformational heterogeneity remains upon inhibitor-binding. ; ############################## # Polymer residue sequence # ############################## _Residue_count 134 _Mol_residue_sequence ; MESKRNKPGKATGKGKPVGD KWLDDAGKDSGAPIPDRIAD KLRDKEFKSFDDFRKAVWEE VSKDPELSKNLNPSNKSSVS KGYSPFTPKNQQVGGRKVYE LHHDKPISQGGEVYDMDNIR VTTPKRHIDIHRGK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLU 3 SER 4 LYS 5 ARG 6 ASN 7 LYS 8 PRO 9 GLY 10 LYS 11 ALA 12 THR 13 GLY 14 LYS 15 GLY 16 LYS 17 PRO 18 VAL 19 GLY 20 ASP 21 LYS 22 TRP 23 LEU 24 ASP 25 ASP 26 ALA 27 GLY 28 LYS 29 ASP 30 SER 31 GLY 32 ALA 33 PRO 34 ILE 35 PRO 36 ASP 37 ARG 38 ILE 39 ALA 40 ASP 41 LYS 42 LEU 43 ARG 44 ASP 45 LYS 46 GLU 47 PHE 48 LYS 49 SER 50 PHE 51 ASP 52 ASP 53 PHE 54 ARG 55 LYS 56 ALA 57 VAL 58 TRP 59 GLU 60 GLU 61 VAL 62 SER 63 LYS 64 ASP 65 PRO 66 GLU 67 LEU 68 SER 69 LYS 70 ASN 71 LEU 72 ASN 73 PRO 74 SER 75 ASN 76 LYS 77 SER 78 SER 79 VAL 80 SER 81 LYS 82 GLY 83 TYR 84 SER 85 PRO 86 PHE 87 THR 88 PRO 89 LYS 90 ASN 91 GLN 92 GLN 93 VAL 94 GLY 95 GLY 96 ARG 97 LYS 98 VAL 99 TYR 100 GLU 101 LEU 102 HIS 103 HIS 104 ASP 105 LYS 106 PRO 107 ILE 108 SER 109 GLN 110 GLY 111 GLY 112 GLU 113 VAL 114 TYR 115 ASP 116 MET 117 ASP 118 ASN 119 ILE 120 ARG 121 VAL 122 THR 123 THR 124 PRO 125 LYS 126 ARG 127 HIS 128 ILE 129 ASP 130 ILE 131 HIS 132 ARG 133 GLY 134 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 4293 "DNase domain of colicin E9" 100.00 134 100.00 100.00 7.35e-91 PDB 1BXI "Crystal Structure Of The Escherichia Coli Colicin E9 Dnase Domain With Its Cognate Immunity Protein Im9" 99.25 134 99.25 99.25 1.36e-88 PDB 1EMV "Crystal Structure Of Colicin E9 Dnase Domain With Its Cognate Immunity Protein Im9 (1.7 Angstroms)" 100.00 134 100.00 100.00 7.35e-91 PDB 1FR2 "Crystal Structure Of The E9 Dnase Domain With A Mutant Immunity Protein Im9(E41a)" 100.00 134 100.00 100.00 7.35e-91 PDB 1FSJ "Crystal Structure Of The E9 Dnase Domain" 100.00 134 100.00 100.00 7.35e-91 PDB 1V13 "Crystal Structure Of The Mutant His103ala Of The Colicin E9 Dnase Domain In Complex With Zn+2 (2.0 Angstroms)" 100.00 134 99.25 99.25 1.15e-89 PDB 1V14 "Crystal Structure Of The Colicin E9, Mutant His103ala, In Complex With Mg+2 And Dsdna (Resolution 2.9a)" 100.00 134 99.25 99.25 1.15e-89 PDB 1V15 "Crystal Structure Of The Colicin E9, Mutant His103ala, In Complex With Zn+2 And Dsdna (Resolution 2.4a)" 100.00 134 99.25 99.25 1.15e-89 PDB 2GYK "Crystal Structure Of The Complex Of The Colicin E9 Dnase Domain With A Mutant Immunity Protein, Imme9 (D51a)" 100.00 134 100.00 100.00 7.35e-91 PDB 2GZE "Crystal Structure Of The E9 Dnase Domain With A Mutant Immunity Protein Im9 (Y55a)" 100.00 134 100.00 100.00 7.35e-91 PDB 2GZF "Crystal Structure Of The E9 Dnase Domain With A Mutant Immunity Protein Im9 (Y54f)" 100.00 134 100.00 100.00 7.35e-91 PDB 2GZG "Crystal Structure Of The E9 Dnase Domain With A Mutant Immunity Protein Im9 (Y55f)" 100.00 134 100.00 100.00 7.35e-91 PDB 2GZI "Crystal Structure Of The E9 Dnase Domain With A Mutant Immunity Protein Im9 (V34a)" 100.00 134 100.00 100.00 7.35e-91 PDB 2GZJ "Crystal Structure Of The E9 Dnase Domain With A Mutant Immunity Protein Im9 (D51a)" 100.00 134 100.00 100.00 7.35e-91 PDB 2K5X "Chemical Shift Structure Of Colicin E9 Dnase Domain With Its Cognate Immunity Protein Im9" 100.00 134 100.00 100.00 7.35e-91 PDB 2VLN "N75a Mutant Of E9 Dnase Domain In Complex With Im9" 100.00 134 99.25 99.25 7.20e-90 PDB 2VLO "K97a Mutant Of E9 Dnase Domain In Complex With Im9" 100.00 134 99.25 99.25 3.11e-90 PDB 2VLP "R54a Mutant Of E9 Dnase Domain In Complex With Im9" 100.00 134 99.25 99.25 6.60e-90 PDB 2VLQ "F86a Mutant Of E9 Dnase Domain In Complex With Im9" 100.00 134 99.25 99.25 1.07e-89 PDB 2WPT "The Crystal Structure Of Im2 In Complex With Colicin E9 Dnase" 100.00 134 99.25 99.25 4.91e-90 EMBL CAA31104 "colicin E9 [Escherichia coli str. K-12 substr. W3110]" 99.25 582 100.00 100.00 8.97e-87 EMBL CAA33862 "colcinin E9 C-terminal fragment [Plasmid ColE9-J]" 99.25 205 100.00 100.00 7.35e-91 GB ACM07430 "colicin E9 [Escherichia coli]" 99.25 582 100.00 100.00 8.97e-87 PRF 1615299E "colicin E9" 99.25 205 99.25 99.25 6.88e-90 REF WP_012644886 "colicin E9 [Escherichia coli]" 99.25 582 100.00 100.00 8.97e-87 REF WP_044860894 "colicin [Escherichia coli]" 99.25 581 100.00 100.00 1.43e-86 REF YP_002533537 "colicin E9 [Escherichia coli]" 99.25 582 100.00 100.00 8.97e-87 SP P09883 "RecName: Full=Colicin-E9" 99.25 582 100.00 100.00 8.97e-87 stop_ save_ save_Im9 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Immunity protein of colicin E9' _Abbreviation_common Im9 _Molecular_mass 9582 _Mol_thiol_state . _Details . _Residue_count 86 _Mol_residue_sequence ; MELKHSISDYTEAEFLQLVT TICNADTSSEEELVKLVTHF EEMTEHPSGSDLIYYPKEGD DDSPSGIVNTVKQWRAANGK SGFKQG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLU 3 LEU 4 LYS 5 HIS 6 SER 7 ILE 8 SER 9 ASP 10 TYR 11 THR 12 GLU 13 ALA 14 GLU 15 PHE 16 LEU 17 GLN 18 LEU 19 VAL 20 THR 21 THR 22 ILE 23 CYS 24 ASN 25 ALA 26 ASP 27 THR 28 SER 29 SER 30 GLU 31 GLU 32 GLU 33 LEU 34 VAL 35 LYS 36 LEU 37 VAL 38 THR 39 HIS 40 PHE 41 GLU 42 GLU 43 MET 44 THR 45 GLU 46 HIS 47 PRO 48 SER 49 GLY 50 SER 51 ASP 52 LEU 53 ILE 54 TYR 55 TYR 56 PRO 57 LYS 58 GLU 59 GLY 60 ASP 61 ASP 62 ASP 63 SER 64 PRO 65 SER 66 GLY 67 ILE 68 VAL 69 ASN 70 THR 71 VAL 72 LYS 73 GLN 74 TRP 75 ARG 76 ALA 77 ALA 78 ASN 79 GLY 80 LYS 81 SER 82 GLY 83 PHE 84 LYS 85 GLN 86 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $E9_DNase 'E. coli' 562 Eubacteria . Escherichia coli cea9_ecoli $Im9 'E. coli' 562 Eubacteria . Escherichia coli ceie9 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $E9_DNase 'recombinant technology' 'E. coli' Eschericia coli 'BL21 (DE3)' plasmid pRJ353 ; To produce Im9-bound E9 DNase, purified unlabelled Im9 was added to uniformly 13C/15N-labelled E9 DNase. ; $Im9 'recombinant technology' 'E. coli' Eschericia coli JM83 plasmid pRJ345 . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $E9_DNase 2.0 mM '[U-99% 13C; U-99% 15N]' $Im9 2.5 mM . Potassium_phosphate 50.0 mM . H20 90 % . D20 10 % . Sodium_azide 0.01 % . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 95.0 loop_ _Task ; Simultaneous analysis of triple resonance spectra. Very useful for analysing multiple data sets simultaneously. ; stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task 'Data processing.' stop_ _Details . _Citation_label $citation_one save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.2 loop_ _Task ; Defining strips for 3D NOESY to aid sequential assignment. ; stop_ _Details . _Citation_label $citation_two save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_one save_ save_1H-1H-15N_NOESY-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H-15N NOESY-HSQC' _Sample_label $sample_one save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_one save_ save_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_one save_ save_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_one save_ save_HBHA(CBCACO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CBCACO)NH _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.2 0.2 n/a temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_set_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio TSP C 13 methyl ppm 0.00 External_in_the_sample indirect cylindrical External_in_the_sample parallel_to_Bo .25144954 Dioxane H 1 methylene ppm 3.77 internal direct cylindrical internal parallel_to_Bo 1.00000000 TSP N 15 methyl ppm 0.00 External_in_the_sample indirect cylindrical External_in_the_sample parallel_to_Bo .10132900 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_for_major_conformer_of_E9_DNase _Saveframe_category assigned_chemical_shifts _Details ; Assignments refer to the major conformational species of E9 DNase when bound to its inhibitor, Im9. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_set_one _Mol_system_component_name 'E9 DNase' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 GLU HA H 4.37 . 1 2 . 2 GLU HB2 H 1.97 . 1 3 . 2 GLU C C 175.96 . 1 4 . 2 GLU CA C 55.06 . 1 5 . 2 GLU CB C 29.36 . 1 6 . 3 SER H H 8.65 . 1 7 . 3 SER HA H 4.41 . 1 8 . 3 SER HB2 H 3.86 . 1 9 . 3 SER C C 175.50 . 1 10 . 3 SER CA C 56.95 . 1 11 . 3 SER CB C 62.24 . 1 12 . 3 SER N N 118.5 . 1 13 . 4 LYS H H 8.66 . 1 14 . 4 LYS HA H 4.13 . 1 15 . 4 LYS HB2 H 1.81 . 1 16 . 4 LYS HB3 H 1.68 . 1 17 . 4 LYS C C 177.17 . 1 18 . 4 LYS CA C 56.70 . 1 19 . 4 LYS CB C 31.73 . 1 20 . 4 LYS N N 124.1 . 1 21 . 5 ARG H H 8.20 . 1 22 . 5 ARG HA H 4.06 . 1 23 . 5 ARG HB2 H 1.72 . 1 24 . 5 ARG C C 175.31 . 1 25 . 5 ARG CA C 56.05 . 1 26 . 5 ARG CB C 29.74 . 1 27 . 5 ARG N N 118.8 . 1 28 . 6 ASN H H 8.03 . 1 29 . 6 ASN HA H 4.93 . 1 30 . 6 ASN HB2 H 3.06 . 1 31 . 6 ASN HB3 H 2.77 . 1 32 . 6 ASN HD21 H 7.01 . 1 33 . 6 ASN HD22 H 7.69 . 1 34 . 6 ASN C C 173.65 . 1 35 . 6 ASN CA C 51.24 . 1 36 . 6 ASN CB C 37.90 . 1 37 . 6 ASN CG C 176.98 . 1 38 . 6 ASN N N 117.8 . 1 39 . 6 ASN ND2 N 113.4 . 1 40 . 7 LYS H H 7.71 . 1 41 . 7 LYS CA C 52.16 . 1 42 . 7 LYS N N 121.4 . 1 43 . 8 PRO HA H 4.93 . 1 44 . 8 PRO HB2 H 2.35 . 1 45 . 8 PRO HB3 H 1.87 . 1 46 . 8 PRO C C 176.77 . 1 47 . 8 PRO CA C 61.48 . 1 48 . 8 PRO CB C 32.46 . 1 49 . 9 GLY H H 8.30 . 1 50 . 9 GLY HA2 H 4.13 . 1 51 . 9 GLY HA3 H 3.79 . 1 52 . 9 GLY C C 170.52 . 1 53 . 9 GLY CA C 44.28 . 1 54 . 9 GLY N N 109.0 . 1 55 . 10 LYS H H 8.11 . 1 56 . 10 LYS HA H 5.07 . 1 57 . 10 LYS HB2 H 1.49 . 1 58 . 10 LYS C C 175.62 . 1 59 . 10 LYS CA C 52.75 . 1 60 . 10 LYS CB C 34.07 . 1 61 . 10 LYS N N 119.4 . 1 62 . 11 ALA H H 8.31 . 1 63 . 11 ALA HA H 5.09 . 1 64 . 11 ALA HB H 1.75 . 1 65 . 11 ALA C C 177.73 . 1 66 . 11 ALA CA C 50.92 . 1 67 . 11 ALA CB C 17.81 . 1 68 . 11 ALA N N 125.6 . 1 69 . 12 THR H H 8.41 . 1 70 . 12 THR HA H 4.69 . 1 71 . 12 THR HB H 4.30 . 1 72 . 12 THR C C 172.54 . 1 73 . 12 THR CA C 58.61 . 1 74 . 12 THR CB C 70.86 . 1 75 . 12 THR N N 114.9 . 1 76 . 13 GLY H H 8.62 . 1 77 . 13 GLY HA2 H 4.47 . 1 78 . 13 GLY HA3 H 3.84 . 1 79 . 13 GLY C C 173.30 . 1 80 . 13 GLY CA C 43.11 . 1 81 . 13 GLY N N 108.6 . 1 82 . 14 LYS H H 9.32 . 1 83 . 14 LYS HA H 4.10 . 1 84 . 14 LYS HB2 H 1.89 . 1 85 . 14 LYS C C 178.63 . 1 86 . 14 LYS CA C 56.40 . 1 87 . 14 LYS CB C 33.95 . 1 88 . 14 LYS N N 119.6 . 1 89 . 15 GLY H H 9.05 . 1 90 . 15 GLY HA2 H 3.84 . 1 91 . 15 GLY HA3 H 3.61 . 1 92 . 15 GLY C C 173.54 . 1 93 . 15 GLY CA C 43.54 . 1 94 . 15 GLY N N 106.7 . 1 95 . 16 LYS H H 8.14 . 1 96 . 16 LYS CA C 51.37 . 1 97 . 16 LYS N N 117.3 . 1 98 . 17 PRO HA H 4.66 . 1 99 . 17 PRO HB2 H 2.25 . 2 100 . 17 PRO C C 176.92 . 1 101 . 17 PRO CA C 61.47 . 1 102 . 17 PRO CB C 30.06 . 1 103 . 18 VAL H H 8.59 . 1 104 . 18 VAL HA H 4.70 . 1 105 . 18 VAL HB H 2.46 . 1 106 . 18 VAL C C 175.71 . 1 107 . 18 VAL CA C 57.94 . 1 108 . 18 VAL N N 118.2 . 1 109 . 19 GLY H H 8.40 . 1 110 . 19 GLY HA2 H 4.52 . 1 111 . 19 GLY HA3 H 3.85 . 1 112 . 19 GLY C C 174.21 . 1 113 . 19 GLY CA C 42.32 . 1 114 . 19 GLY N N 108.9 . 1 115 . 20 ASP H H 8.32 . 1 116 . 20 ASP HA H 4.46 . 1 117 . 20 ASP HB2 H 2.89 . 1 118 . 20 ASP HB3 H 2.77 . 1 119 . 20 ASP C C 178.03 . 1 120 . 20 ASP CA C 54.98 . 1 121 . 20 ASP CB C 40.19 . 1 122 . 20 ASP N N 116.0 . 1 123 . 21 LYS H H 8.43 . 1 124 . 21 LYS HA H 4.64 . 1 125 . 21 LYS HB2 H 1.66 . 1 126 . 21 LYS HB3 H 1.66 . 1 127 . 21 LYS C C 178.38 . 1 128 . 21 LYS CA C 54.61 . 1 129 . 21 LYS CB C 29.69 . 1 130 . 21 LYS N N 121.6 . 1 131 . 22 TRP H H 7.71 . 1 132 . 22 TRP HA H 4.35 . 1 133 . 22 TRP C C 176.87 . 1 134 . 22 TRP CA C 59.14 . 1 135 . 22 TRP N N 121.8 . 1 136 . 23 LEU H H 7.55 . 1 137 . 23 LEU HA H 3.34 . 1 138 . 23 LEU C C 180.50 . 1 139 . 23 LEU CA C 55.25 . 1 140 . 23 LEU CB C 37.88 . 1 141 . 23 LEU N N 119.1 . 1 142 . 24 ASP H H 8.29 . 1 143 . 24 ASP HA H 4.29 . 1 144 . 24 ASP HB2 H 2.91 . 1 145 . 24 ASP HB3 H 2.63 . 1 146 . 24 ASP CA C 56.16 . 1 147 . 24 ASP CB C 38.75 . 1 148 . 24 ASP N N 123.4 . 1 149 . 25 ASP H H 7.56 . 1 150 . 25 ASP HA H 4.37 . 1 151 . 25 ASP C C 177.22 . 1 152 . 25 ASP CA C 55.01 . 1 153 . 25 ASP CB C 38.64 . 1 154 . 25 ASP N N 119.8 . 1 155 . 26 ALA H H 7.53 . 1 156 . 26 ALA HA H 4.60 . 1 157 . 26 ALA HB H 1.48 . 1 158 . 26 ALA C C 176.97 . 1 159 . 26 ALA CA C 52.73 . 1 160 . 26 ALA N N 120.0 . 1 161 . 27 GLY H H 7.38 . 1 162 . 27 GLY HA2 H 4.51 . 1 163 . 27 GLY HA3 H 3.62 . 1 164 . 27 GLY C C 173.14 . 1 165 . 27 GLY CA C 43.14 . 1 166 . 27 GLY N N 101.9 . 1 167 . 28 LYS H H 7.60 . 1 168 . 28 LYS HA H 4.62 . 1 169 . 28 LYS HB2 H 1.76 . 1 170 . 28 LYS HB3 H 1.76 . 1 171 . 28 LYS C C 173.66 . 1 172 . 28 LYS CA C 53.15 . 1 173 . 28 LYS CB C 35.24 . 1 174 . 28 LYS N N 119.8 . 1 175 . 29 ASP H H 8.91 . 1 176 . 29 ASP HA H 4.16 . 1 177 . 29 ASP HB2 H 2.85 . 1 178 . 29 ASP HB3 H 2.85 . 1 179 . 29 ASP C C 176.12 . 1 180 . 29 ASP CA C 55.13 . 1 181 . 29 ASP CB C 38.98 . 1 182 . 29 ASP N N 119.3 . 1 183 . 30 SER H H 8.30 . 1 184 . 30 SER HA H 4.53 . 1 185 . 30 SER HB2 H 3.91 . 1 186 . 30 SER C C 174.06 . 1 187 . 30 SER CA C 56.80 . 1 188 . 30 SER CB C 62.33 . 1 189 . 30 SER N N 117.6 . 1 190 . 31 GLY H H 8.39 . 1 191 . 31 GLY HA2 H 4.33 . 1 192 . 31 GLY HA3 H 4.33 . 1 193 . 31 GLY C C 173.85 . 1 194 . 31 GLY CA C 43.00 . 1 195 . 31 GLY N N 108.3 . 1 196 . 32 ALA H H 9.36 . 1 197 . 32 ALA CA C 47.63 . 1 198 . 32 ALA N N 123.9 . 1 199 . 33 PRO HA H 4.63 . 1 200 . 33 PRO HB2 H 2.26 . 1 201 . 33 PRO HB3 H 1.90 . 1 202 . 34 ILE H H 8.61 . 1 203 . 34 ILE N N 118.6 . 1 204 . 35 PRO HA H 4.64 . 1 205 . 35 PRO C C 177.47 . 1 206 . 35 PRO CA C 60.48 . 1 207 . 35 PRO CB C 31.8 . 1 208 . 36 ASP H H 8.58 . 1 209 . 36 ASP HA H 4.39 . 1 210 . 36 ASP HB2 H 2.73 . 1 211 . 36 ASP HB3 H 2.11 . 1 212 . 36 ASP C C 178.14 . 1 213 . 36 ASP CA C 55.06 . 1 214 . 36 ASP CB C 37.07 . 1 215 . 36 ASP N N 130.0 . 1 216 . 37 ARG H H 8.24 . 1 217 . 37 ARG HA H 4.01 . 1 218 . 37 ARG C C 178.63 . 1 219 . 37 ARG CA C 57.62 . 1 220 . 37 ARG CB C 30.43 . 1 221 . 37 ARG N N 118.6 . 1 222 . 38 ILE H H 6.94 . 1 223 . 38 ILE HA H 3.64 . 1 224 . 38 ILE HB H 1.93 . 1 225 . 38 ILE C C 177.32 . 1 226 . 38 ILE CA C 60.60 . 1 227 . 38 ILE CB C 34.17 . 1 228 . 38 ILE N N 116.3 . 1 229 . 39 ALA H H 8.08 . 1 230 . 39 ALA HA H 3.92 . 1 231 . 39 ALA HB H 1.09 . 1 232 . 39 ALA C C 179.24 . 1 233 . 39 ALA CA C 53.82 . 1 234 . 39 ALA CB C 15.12 . 1 235 . 39 ALA N N 124.8 . 1 236 . 40 ASP H H 8.30 . 1 237 . 40 ASP HA H 4.25 . 1 238 . 40 ASP HB2 H 2.59 . 1 239 . 40 ASP HB3 H 2.59 . 1 240 . 40 ASP C C 178.23 . 1 241 . 40 ASP CA C 55.63 . 1 242 . 40 ASP CB C 39.35 . 1 243 . 40 ASP N N 115.0 . 1 244 . 41 LYS H H 7.11 . 1 245 . 41 LYS HA H 4.14 . 1 246 . 41 LYS HB2 H 1.91 . 9 247 . 41 LYS C C 177.72 . 1 248 . 41 LYS CA C 55.67 . 1 249 . 41 LYS CB C 31.95 . 1 250 . 41 LYS N N 117.2 . 1 251 . 42 LEU H H 7.50 . 1 252 . 42 LEU HA H 4.40 . 1 253 . 42 LEU HB2 H 1.61 . 1 254 . 42 LEU HB3 H 1.61 . 1 255 . 42 LEU C C 176.02 . 1 256 . 42 LEU CA C 53.70 . 1 257 . 42 LEU CB C 41.72 . 1 258 . 42 LEU N N 117.2 . 1 259 . 43 ARG H H 7.93 . 1 260 . 43 ARG HA H 3.48 . 1 261 . 43 ARG C C 176.37 . 1 262 . 43 ARG CA C 57.95 . 1 263 . 43 ARG CB C 27.91 . 1 264 . 43 ARG N N 119.7 . 1 265 . 44 ASP H H 9.08 . 1 266 . 44 ASP HA H 4.18 . 1 267 . 44 ASP HB2 H 3.12 . 1 268 . 44 ASP HB3 H 2.83 . 1 269 . 44 ASP C C 174.75 . 1 270 . 44 ASP CA C 55.90 . 1 271 . 44 ASP CB C 38.36 . 1 272 . 44 ASP N N 118.7 . 1 273 . 45 LYS H H 8.08 . 1 274 . 45 LYS HA H 4.17 . 1 275 . 45 LYS HB2 H 1.99 . 1 276 . 45 LYS HB3 H 1.36 . 1 277 . 45 LYS C C 174.41 . 1 278 . 45 LYS CA C 55.13 . 1 279 . 45 LYS CB C 31.73 . 1 280 . 45 LYS N N 121.0 . 1 281 . 46 GLU H H 7.95 . 1 282 . 46 GLU HA H 4.51 . 1 283 . 46 GLU HB2 H 1.75 . 1 284 . 46 GLU HB3 H 1.61 . 1 285 . 46 GLU C C 175.21 . 1 286 . 46 GLU CA C 53.66 . 1 287 . 46 GLU CB C 30.43 . 1 288 . 46 GLU N N 120.2 . 1 289 . 47 PHE H H 8.59 . 1 290 . 47 PHE HA H 4.68 . 1 291 . 47 PHE HB2 H 3.22 . 1 292 . 47 PHE HB3 H 2.26 . 1 293 . 47 PHE C C 175.17 . 1 294 . 47 PHE CA C 56.08 . 1 295 . 47 PHE CB C 42.41 . 1 296 . 47 PHE N N 122.5 . 1 297 . 48 LYS H H 9.52 . 1 298 . 48 LYS HA H 4.06 . 1 299 . 48 LYS HB2 H 1.91 . 1 300 . 48 LYS HB3 H 1.91 . 1 301 . 48 LYS C C 174.96 . 1 302 . 48 LYS CA C 56.44 . 1 303 . 48 LYS CB C 32.02 . 1 304 . 48 LYS N N 120.1 . 1 305 . 49 SER H H 7.69 . 1 306 . 49 SER HA H 4.55 . 1 307 . 49 SER HB2 H 4.05 . 1 308 . 49 SER C C 175.56 . 1 309 . 49 SER CA C 56.41 . 1 310 . 49 SER CB C 64.45 . 1 311 . 49 SER N N 108.9 . 1 312 . 50 PHE H H 9.30 . 1 313 . 50 PHE HA H 4.43 . 1 314 . 50 PHE HB2 H 3.06 . 1 315 . 50 PHE C C 176.93 . 1 316 . 50 PHE CA C 60.97 . 1 317 . 50 PHE CB C 37.98 . 1 318 . 50 PHE N N 122.5 . 1 319 . 51 ASP H H 8.36 . 1 320 . 51 ASP HA H 4.43 . 1 321 . 51 ASP HB2 H 2.69 . 1 322 . 51 ASP C C 178.18 . 1 323 . 51 ASP CA C 56.43 . 1 324 . 51 ASP CB C 39.58 . 1 325 . 51 ASP N N 118.3 . 1 326 . 52 ASP H H 7.85 . 1 327 . 52 ASP HA H 4.53 . 1 328 . 52 ASP HB2 H 3.11 . 1 329 . 52 ASP C C 178.28 . 1 330 . 52 ASP CA C 56.16 . 1 331 . 52 ASP CB C 40.88 . 1 332 . 52 ASP N N 121.0 . 1 333 . 53 PHE H H 7.52 . 1 334 . 53 PHE HA H 3.28 . 1 335 . 53 PHE C C 174.36 . 1 336 . 53 PHE CA C 59.58 . 1 337 . 53 PHE CB C 37.52 . 1 338 . 53 PHE N N 122.9 . 1 339 . 54 ARG H H 8.27 . 1 340 . 54 ARG HA H 3.03 . 1 341 . 54 ARG HB2 H 1.97 . 1 342 . 54 ARG HB3 H 1.53 . 1 343 . 54 ARG C C 175.97 . 1 344 . 54 ARG CA C 58.15 . 1 345 . 54 ARG CB C 29.07 . 1 346 . 54 ARG N N 120.2 . 1 347 . 55 LYS H H 7.35 . 1 348 . 55 LYS HA H 4.61 . 1 349 . 55 LYS HB2 H 1.99 . 1 350 . 55 LYS C C 177.83 . 1 351 . 55 LYS CA C 57.34 . 1 352 . 55 LYS CB C 32.57 . 1 353 . 55 LYS N N 116.4 . 1 354 . 56 ALA H H 7.16 . 1 355 . 56 ALA HA H 4.14 . 1 356 . 56 ALA HB H 1.48 . 1 357 . 56 ALA C C 179.79 . 1 358 . 56 ALA CA C 53.39 . 1 359 . 56 ALA CB C 17.62 . 1 360 . 56 ALA N N 120.5 . 1 361 . 57 VAL H H 7.64 . 1 362 . 57 VAL HA H 2.80 . 1 363 . 57 VAL HB H 1.37 . 1 364 . 57 VAL C C 177.48 . 1 365 . 57 VAL CA C 65.32 . 1 366 . 57 VAL CB C 29.44 . 1 367 . 57 VAL N N 118.5 . 1 368 . 58 TRP H H 7.40 . 1 369 . 58 TRP HA H 4.73 . 1 370 . 58 TRP C C 178.44 . 1 371 . 58 TRP CA C 58.30 . 1 372 . 58 TRP CB C 27.84 . 1 373 . 58 TRP N N 118.3 . 1 374 . 59 GLU H H 8.70 . 1 375 . 59 GLU HA H 4.13 . 1 376 . 59 GLU C C 181.10 . 1 377 . 59 GLU CA C 58.38 . 1 378 . 59 GLU CB C 28.46 . 1 379 . 59 GLU N N 119.4 . 1 380 . 60 GLU H H 8.32 . 1 381 . 60 GLU HA H 4.05 . 1 382 . 60 GLU HB2 H 2.03 . 1 383 . 60 GLU C C 180.49 . 1 384 . 60 GLU CA C 57.48 . 1 385 . 60 GLU N N 119.2 . 1 386 . 61 VAL H H 8.63 . 1 387 . 61 VAL HA H 3.42 . 1 388 . 61 VAL C C 177.98 . 1 389 . 61 VAL CA C 66.15 . 1 390 . 61 VAL CB C 30.70 . 1 391 . 61 VAL N N 124.1 . 1 392 . 62 SER H H 8.18 . 1 393 . 62 SER HB2 H 3.94 . 1 394 . 62 SER HB3 H 3.94 . 1 395 . 62 SER C C 174.56 . 1 396 . 62 SER CA C 60.01 . 1 397 . 62 SER CB C 62.46 . 1 398 . 62 SER N N 113.8 . 1 399 . 63 LYS H H 6.99 . 1 400 . 63 LYS HA H 4.20 . 1 401 . 63 LYS HB2 H 2.06 . 1 402 . 63 LYS HB3 H 1.66 . 1 403 . 63 LYS C C 175.01 . 1 404 . 63 LYS CA C 55.09 . 1 405 . 63 LYS CB C 32.91 . 1 406 . 63 LYS N N 119.4 . 1 407 . 64 ASP H H 7.68 . 1 408 . 64 ASP CA C 49.57 . 1 409 . 64 ASP N N 123.6 . 1 410 . 65 PRO HA H 4.22 . 1 411 . 65 PRO HB2 H 2.33 . 1 412 . 65 PRO HB3 H 2.01 . 1 413 . 65 PRO C C 178.18 . 1 414 . 65 PRO CA C 63.59 . 1 415 . 65 PRO CB C 31.31 . 1 416 . 66 GLU H H 7.82 . 1 417 . 66 GLU HA H 4.29 . 1 418 . 66 GLU HB2 H 1.94 . 1 419 . 66 GLU HB3 H 1.94 . 1 420 . 66 GLU C C 178.39 . 1 421 . 66 GLU CA C 57.17 . 1 422 . 66 GLU CB C 28.86 . 1 423 . 66 GLU N N 115.9 . 1 424 . 67 LEU H H 8.38 . 1 425 . 67 LEU HA H 4.35 . 1 426 . 67 LEU HB2 H 1.44 . 1 427 . 67 LEU HB3 H 1.44 . 1 428 . 67 LEU C C 179.29 . 1 429 . 67 LEU CA C 55.12 . 1 430 . 67 LEU CB C 41.31 . 1 431 . 67 LEU N N 116.8 . 1 432 . 68 SER H H 8.00 . 1 433 . 68 SER HA H 4.50 . 1 434 . 68 SER HB2 H 4.05 . 1 435 . 68 SER HB3 H 4.05 . 1 436 . 68 SER C C 175.20 . 1 437 . 68 SER CA C 56.87 . 1 438 . 68 SER CB C 63.13 . 1 439 . 68 SER N N 110.4 . 1 440 . 69 LYS H H 7.20 . 1 441 . 69 LYS HA H 4.03 . 1 442 . 69 LYS HB2 H 2.33 . 1 443 . 69 LYS HB3 H 1.93 . 1 444 . 69 LYS C C 176.93 . 1 445 . 69 LYS CA C 58.50 . 1 446 . 69 LYS CB C 32.23 . 1 447 . 69 LYS N N 123.7 . 1 448 . 70 ASN H H 8.75 . 1 449 . 70 ASN HA H 4.90 . 1 450 . 70 ASN HB2 H 3.04 . 1 451 . 70 ASN HB3 H 2.59 . 1 452 . 70 ASN C C 175.32 . 1 453 . 70 ASN CA C 52.19 . 1 454 . 70 ASN CB C 38.03 . 1 455 . 70 ASN N N 113.8 . 1 456 . 71 LEU H H 7.49 . 1 457 . 71 LEU HA H 4.44 . 1 458 . 71 LEU C C 175.06 . 1 459 . 71 LEU CA C 52.31 . 1 460 . 71 LEU CB C 41.83 . 1 461 . 71 LEU N N 120.8 . 1 462 . 72 ASN H H 9.02 . 1 463 . 72 ASN CA C 50.17 . 1 464 . 72 ASN N N 125.9 . 1 465 . 73 PRO HA H 4.07 . 1 466 . 73 PRO HB2 H 2.32 . 9 467 . 73 PRO C C 178.78 . 1 468 . 73 PRO CA C 65.35 . 1 469 . 73 PRO CB C 30.14 . 1 470 . 74 SER H H 6.97 . 1 471 . 74 SER HA H 4.90 . 1 472 . 74 SER HB2 H 3.49 . 1 473 . 74 SER C C 177.33 . 1 474 . 74 SER CA C 59.85 . 1 475 . 74 SER CB C 61.90 . 1 476 . 74 SER N N 113.0 . 1 477 . 75 ASN H H 8.33 . 1 478 . 75 ASN HA H 5.35 . 1 479 . 75 ASN HB2 H 3.31 . 1 480 . 75 ASN HB3 H 2.63 . 1 481 . 75 ASN C C 178.94 . 1 482 . 75 ASN CA C 51.99 . 1 483 . 75 ASN CB C 37.78 . 1 484 . 75 ASN N N 126.7 . 1 485 . 76 LYS H H 9.14 . 1 486 . 76 LYS HA H 4.00 . 1 487 . 76 LYS HB2 H 1.91 . 1 488 . 76 LYS HB3 H 1.91 . 1 489 . 76 LYS C C 179.74 . 1 490 . 76 LYS CA C 58.90 . 1 491 . 76 LYS CB C 31.05 . 1 492 . 76 LYS N N 120.8 . 1 493 . 77 SER H H 8.39 . 1 494 . 77 SER C C 175.92 . 1 495 . 77 SER CA C 61.14 . 1 496 . 77 SER N N 118.1 . 1 497 . 78 SER H H 7.21 . 1 498 . 78 SER HA H 4.23 . 1 499 . 78 SER HB2 H 3.92 . 1 500 . 78 SER C C 177.38 . 1 501 . 78 SER CA C 61.31 . 1 502 . 78 SER N N 115.9 . 1 503 . 79 VAL H H 7.86 . 1 504 . 79 VAL HA H 4.87 . 1 505 . 79 VAL C C 179.74 . 1 506 . 79 VAL CA C 62.94 . 1 507 . 79 VAL CB C 28.98 . 1 508 . 79 VAL N N 112.6 . 1 509 . 80 SER H H 8.08 . 1 510 . 80 SER HA H 4.43 . 1 511 . 80 SER HB2 H 3.97 . 1 512 . 80 SER HB3 H 3.97 . 1 513 . 80 SER C C 175.72 . 1 514 . 80 SER CA C 60.09 . 1 515 . 80 SER CB C 61.85 . 1 516 . 80 SER N N 117.3 . 1 517 . 81 LYS H H 7.15 . 1 518 . 81 LYS HA H 4.26 . 1 519 . 81 LYS HB2 H 1.91 . 1 520 . 81 LYS HB3 H 1.66 . 1 521 . 81 LYS C C 176.11 . 1 522 . 81 LYS CA C 53.98 . 1 523 . 81 LYS CB C 29.99 . 1 524 . 81 LYS N N 119.7 . 1 525 . 82 GLY H H 8.25 . 1 526 . 82 GLY HA2 H 4.24 . 1 527 . 82 GLY HA3 H 3.74 . 1 528 . 82 GLY C C 173.09 . 1 529 . 82 GLY CA C 44.54 . 1 530 . 82 GLY N N 107.8 . 1 531 . 83 TYR H H 7.35 . 1 532 . 83 TYR HA H 4.86 . 1 533 . 83 TYR C C 172.85 . 1 534 . 83 TYR CA C 50.84 . 1 535 . 83 TYR CB C 34.44 . 1 536 . 83 TYR N N 120.5 . 1 537 . 84 SER H H 7.81 . 1 538 . 84 SER CA C 54.14 . 1 539 . 84 SER N N 114.4 . 1 540 . 85 PRO HA H 4.34 . 1 541 . 85 PRO C C 176.37 . 1 542 . 85 PRO CA C 60.05 . 1 543 . 86 PHE H H 9.18 . 1 544 . 86 PHE HA H 4.15 . 1 545 . 86 PHE C C 178.28 . 1 546 . 86 PHE CA C 57.35 . 1 547 . 86 PHE CB C 39.20 . 1 548 . 86 PHE N N 120.0 . 1 549 . 87 THR H H 8.48 . 1 550 . 87 THR CA C 58.61 . 1 551 . 87 THR N N 114.7 . 1 552 . 88 PRO HA H 4.00 . 1 553 . 88 PRO C C 178.28 . 1 554 . 88 PRO CA C 61.71 . 1 555 . 89 LYS H H 10.99 . 1 556 . 89 LYS HA H 3.62 . 1 557 . 89 LYS HB2 H 1.80 . 1 558 . 89 LYS C C 178.18 . 1 559 . 89 LYS CA C 58.58 . 1 560 . 89 LYS CB C 30.44 . 1 561 . 89 LYS N N 133.1 . 1 562 . 90 ASN H H 8.83 . 1 563 . 90 ASN HA H 4.35 . 1 564 . 90 ASN HB2 H 3.05 . 1 565 . 90 ASN HB3 H 2.74 . 1 566 . 90 ASN C C 175.97 . 1 567 . 90 ASN CA C 53.07 . 1 568 . 90 ASN CB C 35.71 . 1 569 . 90 ASN N N 115.3 . 1 570 . 91 GLN H H 7.84 . 1 571 . 91 GLN HA H 4.24 . 1 572 . 91 GLN C C 173.96 . 1 573 . 91 GLN CA C 53.05 . 1 574 . 91 GLN CB C 28.06 . 1 575 . 91 GLN N N 117.5 . 1 576 . 92 GLN H H 7.32 . 1 577 . 92 GLN HA H 4.12 . 1 578 . 92 GLN HB2 H 1.97 . 1 579 . 92 GLN C C 176.32 . 1 580 . 92 GLN CA C 53.87 . 1 581 . 92 GLN N N 119.1 . 1 582 . 93 VAL H H 8.17 . 1 583 . 93 VAL HA H 4.18 . 1 584 . 93 VAL HB H 1.74 . 1 585 . 93 VAL C C 176.07 . 1 586 . 93 VAL CA C 60.49 . 1 587 . 93 VAL CB C 33.71 . 1 588 . 93 VAL N N 119.3 . 1 589 . 94 GLY H H 9.10 . 1 590 . 94 GLY HA2 H 3.79 . 1 591 . 94 GLY HA3 H 3.67 . 1 592 . 94 GLY C C 174.66 . 1 593 . 94 GLY CA C 45.89 . 1 594 . 94 GLY N N 119.3 . 1 595 . 95 GLY H H 8.65 . 1 596 . 95 GLY HA2 H 4.05 . 1 597 . 95 GLY HA3 H 3.68 . 1 598 . 95 GLY C C 174.26 . 1 599 . 95 GLY CA C 44.55 . 1 600 . 95 GLY N N 114.1 . 1 601 . 96 ARG H H 8.16 . 1 602 . 96 ARG HA H 4.43 . 1 603 . 96 ARG HB2 H 2.08 . 1 604 . 96 ARG C C 174.70 . 1 605 . 96 ARG CA C 54.50 . 1 606 . 96 ARG CB C 31.36 . 9 607 . 96 ARG N N 123.3 . 1 608 . 97 LYS H H 8.57 . 1 609 . 97 LYS HA H 4.28 . 1 610 . 97 LYS HB2 H 1.37 . 1 611 . 97 LYS C C 173.60 . 1 612 . 97 LYS CA C 54.54 . 1 613 . 97 LYS CB C 34.94 . 1 614 . 97 LYS N N 121.2 . 1 615 . 98 VAL H H 6.78 . 1 616 . 98 VAL HA H 4.63 . 1 617 . 98 VAL HB H 1.55 . 1 618 . 98 VAL C C 176.20 . 1 619 . 98 VAL CA C 56.56 . 1 620 . 98 VAL N N 107.3 . 1 621 . 99 TYR H H 7.64 . 1 622 . 99 TYR C C 175.00 . 1 623 . 99 TYR CA C 60.17 . 1 624 . 99 TYR N N 117.8 . 1 625 . 100 GLU H H 8.85 . 1 626 . 100 GLU HA H 4.49 . 1 627 . 100 GLU C C 174.51 . 1 628 . 100 GLU CA C 52.99 . 1 629 . 100 GLU CB C 32.20 . 1 630 . 100 GLU N N 119.9 . 1 631 . 101 LEU H H 8.40 . 1 632 . 101 LEU HA H 5.22 . 1 633 . 101 LEU HB2 H 1.70 . 1 634 . 101 LEU C C 175.46 . 1 635 . 101 LEU CA C 52.49 . 1 636 . 101 LEU CB C 42.02 . 1 637 . 101 LEU N N 120.7 . 1 638 . 102 HIS H H 9.02 . 1 639 . 102 HIS HA H 5.01 . 1 640 . 102 HIS C C 173.05 . 1 641 . 102 HIS CA C 52.51 . 1 642 . 102 HIS N N 119.3 . 1 643 . 103 HIS H H 10.00 . 1 644 . 103 HIS HA H 5.16 . 1 645 . 103 HIS HB2 H 2.93 . 1 646 . 103 HIS HB3 H 2.93 . 1 647 . 103 HIS C C 175.06 . 1 648 . 103 HIS CA C 55.53 . 1 649 . 103 HIS CB C 28.22 . 1 650 . 103 HIS N N 120.3 . 1 651 . 104 ASP H H 8.21 . 1 652 . 104 ASP HA H 4.37 . 1 653 . 104 ASP HB2 H 2.81 . 1 654 . 104 ASP HB3 H 2.39 . 1 655 . 104 ASP C C 175.67 . 1 656 . 104 ASP CA C 55.45 . 1 657 . 104 ASP CB C 40.74 . 1 658 . 104 ASP N N 125.5 . 1 659 . 105 LYS H H 9.49 . 1 660 . 105 LYS CA C 51.64 . 1 661 . 105 LYS N N 122.1 . 1 662 . 106 PRO HA H 4.31 . 1 663 . 106 PRO HB2 H 2.38 . 1 664 . 106 PRO HB3 H 1.72 . 1 665 . 106 PRO C C 178.54 . 1 666 . 106 PRO CA C 61.40 . 1 667 . 106 PRO CB C 31.42 . 1 668 . 107 ILE H H 8.72 . 1 669 . 107 ILE HA H 3.97 . 1 670 . 107 ILE HB H 1.62 . 1 671 . 107 ILE C C 179.29 . 1 672 . 107 ILE CA C 61.32 . 1 673 . 107 ILE CB C 36.15 . 1 674 . 107 ILE N N 125.6 . 1 675 . 108 SER H H 8.53 . 1 676 . 108 SER HA H 4.19 . 1 677 . 108 SER HB2 H 3.91 . 1 678 . 108 SER HB3 H 3.91 . 1 679 . 108 SER C C 174.97 . 1 680 . 108 SER CA C 58.61 . 1 681 . 108 SER CB C 61.63 . 1 682 . 108 SER N N 115.7 . 1 683 . 109 GLN H H 7.47 . 1 684 . 109 GLN HA H 4.53 . 1 685 . 109 GLN HB2 H 2.41 . 1 686 . 109 GLN HB3 H 1.62 . 1 687 . 109 GLN C C 175.32 . 1 688 . 109 GLN CA C 53.35 . 1 689 . 109 GLN CB C 28.22 . 1 690 . 109 GLN N N 119.8 . 1 691 . 110 GLY H H 7.84 . 1 692 . 110 GLY HA2 H 4.26 . 1 693 . 110 GLY HA3 H 3.65 . 1 694 . 110 GLY C C 175.22 . 1 695 . 110 GLY CA C 43.69 . 1 696 . 110 GLY N N 107.3 . 1 697 . 111 GLY H H 8.09 . 1 698 . 111 GLY HA2 H 3.75 . 1 699 . 111 GLY HA3 H 3.41 . 1 700 . 111 GLY C C 172.50 . 1 701 . 111 GLY CA C 43.21 . 1 702 . 111 GLY N N 109.7 . 1 703 . 112 GLU H H 8.70 . 1 704 . 112 GLU HA H 4.38 . 1 705 . 112 GLU HB2 H 2.03 . 1 706 . 112 GLU C C 178.03 . 1 707 . 112 GLU CA C 54.46 . 1 708 . 112 GLU CB C 29.97 . 1 709 . 112 GLU N N 122.2 . 1 710 . 113 VAL H H 8.40 . 1 711 . 113 VAL HA H 2.89 . 1 712 . 113 VAL HB H 1.46 . 1 713 . 113 VAL C C 177.27 . 1 714 . 113 VAL CA C 63.68 . 1 715 . 113 VAL CB C 31.42 . 1 716 . 113 VAL N N 121.6 . 1 717 . 114 TYR H H 8.55 . 1 718 . 114 TYR HA H 4.11 . 1 719 . 114 TYR HB2 H 2.86 . 1 720 . 114 TYR C C 173.34 . 1 721 . 114 TYR CA C 54.98 . 1 722 . 114 TYR CB C 36.30 . 1 723 . 114 TYR N N 116.1 . 1 724 . 115 ASP H H 6.12 . 1 725 . 115 ASP HA H 4.77 . 1 726 . 115 ASP HB2 H 2.59 . 1 727 . 115 ASP C C 177.57 . 1 728 . 115 ASP CA C 50.72 . 1 729 . 115 ASP N N 116.4 . 1 730 . 116 MET H H 9.92 . 1 731 . 116 MET HA H 3.83 . 1 732 . 116 MET C C 176.78 . 1 733 . 116 MET CA C 57.75 . 1 734 . 116 MET CB C 32.38 . 1 735 . 116 MET N N 126.4 . 1 736 . 117 ASP H H 8.70 . 1 737 . 117 ASP HA H 4.92 . 1 738 . 117 ASP HB2 H 2.89 . 1 739 . 117 ASP C C 175.51 . 1 740 . 117 ASP CA C 55.13 . 1 741 . 117 ASP CB C 38.75 . 1 742 . 117 ASP N N 118.0 . 1 743 . 118 ASN H H 8.29 . 1 744 . 118 ASN HA H 5.19 . 1 745 . 118 ASN HB2 H 3.07 . 1 746 . 118 ASN HB3 H 2.65 . 1 747 . 118 ASN C C 173.75 . 1 748 . 118 ASN CA C 50.53 . 1 749 . 118 ASN CB C 40.41 . 1 750 . 118 ASN N N 119.1 . 1 751 . 119 ILE H H 6.70 . 1 752 . 119 ILE HA H 4.76 . 1 753 . 119 ILE HB H 1.50 . 1 754 . 119 ILE C C 173.85 . 1 755 . 119 ILE CA C 58.11 . 1 756 . 119 ILE CB C 39.48 . 1 757 . 119 ILE N N 119.6 . 1 758 . 120 ARG H H 8.92 . 1 759 . 120 ARG HA H 5.09 . 1 760 . 120 ARG C C 174.80 . 1 761 . 120 ARG CA C 50.97 . 1 762 . 120 ARG N N 125.3 . 1 763 . 121 VAL H H 9.97 . 1 764 . 121 VAL HA H 5.16 . 1 765 . 121 VAL HB H 2.07 . 1 766 . 121 VAL C C 176.82 . 1 767 . 121 VAL CA C 59.41 . 1 768 . 121 VAL CB C 31.36 . 1 769 . 121 VAL N N 123.7 . 1 770 . 122 THR H H 9.68 . 1 771 . 122 THR HA H 6.05 . 1 772 . 122 THR HB H 4.46 . 1 773 . 122 THR C C 175.67 . 1 774 . 122 THR CA C 58.38 . 1 775 . 122 THR CB C 66.04 . 1 776 . 122 THR N N 116.5 . 1 777 . 123 THR H H 7.52 . 1 778 . 123 THR CA C 58.39 . 1 779 . 123 THR N N 111.2 . 1 780 . 124 PRO HA H 4.17 . 1 781 . 124 PRO C C 177.13 . 1 782 . 124 PRO CA C 64.55 . 1 783 . 124 PRO CB C 31.76 . 1 784 . 125 LYS H H 7.59 . 1 785 . 125 LYS HA H 3.61 . 1 786 . 125 LYS C C 177.13 . 1 787 . 125 LYS CA C 57.73 . 1 788 . 125 LYS CB C 31.91 . 1 789 . 125 LYS N N 114.0 . 1 790 . 126 ARG H H 7.69 . 1 791 . 126 ARG HA H 4.23 . 1 792 . 126 ARG C C 177.18 . 1 793 . 126 ARG CA C 55.49 . 1 794 . 126 ARG CB C 28.93 . 1 795 . 126 ARG N N 116.7 . 1 796 . 127 HIS H H 8.02 . 1 797 . 127 HIS HA H 3.91 . 1 798 . 127 HIS HB2 H 3.03 . 9 799 . 127 HIS C C 177.62 . 1 800 . 127 HIS CA C 60.64 . 1 801 . 127 HIS CB C 29.29 . 1 802 . 127 HIS N N 118.5 . 1 803 . 128 ILE H H 8.03 . 1 804 . 128 ILE HA H 3.72 . 1 805 . 128 ILE HB H 1.94 . 1 806 . 128 ILE C C 178.38 . 1 807 . 128 ILE CA C 62.81 . 1 808 . 128 ILE CB C 36.88 . 1 809 . 128 ILE N N 118.8 . 1 810 . 129 ASP H H 8.15 . 1 811 . 129 ASP HA H 4.44 . 1 812 . 129 ASP HB2 H 2.75 . 1 813 . 129 ASP C C 179.08 . 1 814 . 129 ASP CA C 55.87 . 1 815 . 129 ASP CB C 39.44 . 1 816 . 129 ASP N N 121.8 . 1 817 . 130 ILE H H 8.35 . 1 818 . 130 ILE HA H 3.67 . 1 819 . 130 ILE HB H 1.57 . 1 820 . 130 ILE C C 177.64 . 1 821 . 130 ILE CA C 63.07 . 1 822 . 130 ILE CB C 37.34 . 1 823 . 130 ILE N N 119.9 . 1 824 . 131 HIS H H 7.45 . 1 825 . 131 HIS HA H 4.33 . 1 826 . 131 HIS HB2 H 3.23 . 1 827 . 131 HIS HB3 H 2.70 . 1 828 . 131 HIS C C 174.50 . 1 829 . 131 HIS CA C 55.83 . 1 830 . 131 HIS CB C 27.85 . 1 831 . 131 HIS N N 117.2 . 1 832 . 132 ARG H H 7.74 . 1 833 . 132 ARG HA H 4.27 . 1 834 . 132 ARG HB2 H 1.84 . 1 835 . 132 ARG C C 176.57 . 1 836 . 132 ARG CA C 55.65 . 1 837 . 132 ARG CB C 29.41 . 1 838 . 132 ARG N N 120.9 . 1 839 . 133 GLY H H 8.24 . 1 840 . 133 GLY HA2 H 3.91 . 1 841 . 133 GLY C C 173.15 . 1 842 . 133 GLY CA C 44.17 . 1 843 . 133 GLY N N 110.2 . 1 844 . 134 LYS H H 7.76 . 1 845 . 134 LYS CA C 55.73 . 1 846 . 134 LYS N N 126.0 . 1 stop_ save_ save_assigned_chemical_shifts_for_minor_conformer_of_E9_DNase _Saveframe_category assigned_chemical_shifts _Details ; Assignments refer to the minor conformational species of E9 DNase when bound to its inhibitor, Im9. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_set_one _Mol_system_component_name 'E9 DNase' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 14 LYS C C 178.68 . 1 2 . 14 LYS CA C 56.40 . 1 3 . 14 LYS CB C 34.06 . 1 4 . 15 GLY H H 9.17 . 1 5 . 15 GLY HA2 H 3.84 . 1 6 . 15 GLY HA3 H 3.61 . 1 7 . 15 GLY CA C 43.42 . 1 8 . 15 GLY N N 106.7 . 1 9 . 17 PRO HA H 4.67 . 1 10 . 17 PRO HB2 H 2.31 . 1 11 . 17 PRO C C 177.27 . 1 12 . 17 PRO CA C 61.47 . 1 13 . 17 PRO CB C 29.83 . 1 14 . 18 VAL H H 8.68 . 1 15 . 18 VAL HA H 4.68 . 1 16 . 18 VAL HB H 2.26 . 1 17 . 18 VAL C C 175.56 . 1 18 . 18 VAL CA C 58.06 . 1 19 . 18 VAL CB C 34.09 . 1 20 . 18 VAL N N 118.2 . 1 21 . 19 GLY H H 8.39 . 1 22 . 19 GLY HA2 H 4.48 . 1 23 . 19 GLY HA3 H 3.81 . 1 24 . 19 GLY C C 174.30 . 1 25 . 19 GLY CA C 42.90 . 1 26 . 19 GLY N N 110.5 . 1 27 . 20 ASP H H 8.38 . 1 28 . 20 ASP HA H 4.41 . 1 29 . 20 ASP HB2 H 2.73 . 1 30 . 20 ASP C C 177.03 . 1 31 . 20 ASP CA C 54.33 . 1 32 . 20 ASP CB C 39.84 . 1 33 . 20 ASP N N 119.1 . 1 34 . 21 LYS H H 8.33 . 1 35 . 21 LYS HA H 4.62 . 1 36 . 21 LYS HB2 H 1.70 . 1 37 . 21 LYS C C 175.67 . 1 38 . 21 LYS CA C 53.78 . 1 39 . 21 LYS CB C 30.12 . 1 40 . 21 LYS N N 119.9 . 1 41 . 22 TRP H H 7.55 . 1 42 . 22 TRP HA H 4.41 . 1 43 . 22 TRP C C 176.32 . 1 44 . 22 TRP CA C 59.34 . 1 45 . 22 TRP N N 122.1 . 1 46 . 23 LEU H H 8.41 . 1 47 . 23 LEU HA H 3.23 . 1 48 . 23 LEU C C 180.34 . 1 49 . 23 LEU CA C 55.26 . 1 50 . 23 LEU CB C 38.34 . 1 51 . 23 LEU N N 113.2 . 1 52 . 24 ASP H H 8.05 . 1 53 . 24 ASP HA H 4.35 . 1 54 . 24 ASP HB2 H 2.90 . 1 55 . 24 ASP HB3 H 2.63 . 1 56 . 24 ASP CA C 56.32 . 1 57 . 24 ASP CB C 39.18 . 1 58 . 24 ASP N N 123.6 . 1 59 . 25 ASP H H 7.92 . 1 60 . 25 ASP HA H 4.37 . 1 61 . 25 ASP C C 177.37 . 1 62 . 25 ASP CA C 55.17 . 1 63 . 25 ASP CB C 38.34 . 1 64 . 25 ASP N N 120.1 . 1 65 . 26 ALA H H 7.43 . 1 66 . 26 ALA HA H 4.47 . 1 67 . 26 ALA HB H 1.37 . 1 68 . 26 ALA C C 176.93 . 1 69 . 26 ALA CA C 52.55 . 1 70 . 26 ALA N N 120.2 . 1 71 . 27 GLY H H 7.44 . 1 72 . 27 GLY HA2 H 4.47 . 1 73 . 27 GLY HA3 H 3.62 . 1 74 . 27 GLY C C 173.17 . 1 75 . 27 GLY CA C 43.14 . 1 76 . 27 GLY N N 102.1 . 1 77 . 28 LYS H H 7.54 . 1 78 . 28 LYS HA H 4.62 . 1 79 . 28 LYS HB2 H 1.76 . 1 80 . 28 LYS C C 173.66 . 1 81 . 28 LYS CA C 53.15 . 1 82 . 28 LYS CB C 35.24 . 1 83 . 28 LYS N N 119.8 . 1 84 . 29 ASP H H 8.91 . 1 85 . 29 ASP HA H 4.08 . 1 86 . 29 ASP HB2 H 2.82 . 1 87 . 29 ASP HB3 H 2.82 . 1 88 . 29 ASP C C 176.06 . 1 89 . 29 ASP CA C 55.13 . 1 90 . 29 ASP CB C 38.98 . 1 91 . 29 ASP N N 119.3 . 1 92 . 30 SER H H 8.22 . 1 93 . 30 SER CA C 56.80 . 1 94 . 30 SER N N 117.4 . 1 95 . 31 GLY H H 8.39 . 1 96 . 31 GLY HA2 H 4.33 . 1 97 . 31 GLY HA3 H 4.33 . 1 98 . 31 GLY C C 173.29 . 1 99 . 31 GLY CA C 43.00 . 1 100 . 31 GLY N N 108.3 . 1 101 . 32 ALA H H 9.37 . 1 102 . 32 ALA CA C 47.59 . 1 103 . 32 ALA N N 124.1 . 1 104 . 36 ASP H H 8.74 . 1 105 . 36 ASP HA H 4.39 . 1 106 . 36 ASP HB2 H 2.73 . 1 107 . 36 ASP HB3 H 2.11 . 1 108 . 36 ASP C C 178.28 . 1 109 . 36 ASP CA C 55.06 . 1 110 . 36 ASP CB C 36.91 . 1 111 . 36 ASP N N 131.3 . 1 112 . 37 ARG H H 8.57 . 1 113 . 37 ARG HA H 4.04 . 1 114 . 37 ARG C C 178.44 . 1 115 . 37 ARG CA C 57.18 . 1 116 . 37 ARG CB C 30.35 . 1 117 . 37 ARG N N 118.6 . 1 118 . 38 ILE H H 6.91 . 1 119 . 38 ILE HA H 3.68 . 1 120 . 38 ILE C C 177.23 . 1 121 . 38 ILE CA C 60.75 . 1 122 . 38 ILE N N 116.9 . 1 123 . 39 ALA H H 8.24 . 1 124 . 39 ALA HA H 3.92 . 1 125 . 39 ALA HB H 1.09 . 1 126 . 39 ALA C C 179.30 . 1 127 . 39 ALA CA C 53.82 . 1 128 . 39 ALA N N 124.8 . 1 129 . 40 ASP H H 8.33 . 1 130 . 40 ASP CA C 55.71 . 1 131 . 40 ASP N N 115.4 . 1 132 . 42 LEU H H 7.41 . 1 133 . 42 LEU CA C 53.82 . 1 134 . 42 LEU N N 117.2 . 1 135 . 59 GLU H H 8.70 . 1 136 . 59 GLU HA H 4.13 . 1 137 . 59 GLU HB2 H 2.15 . 1 138 . 59 GLU HB3 H 1.92 . 1 139 . 59 GLU C C 181.10 . 1 140 . 59 GLU CA C 58.71 . 1 141 . 59 GLU CB C 28.46 . 1 142 . 59 GLU N N 119.4 . 1 143 . 60 GLU H H 8.24 . 1 144 . 60 GLU C C 180.49 . 1 145 . 60 GLU CA C 57.53 . 1 146 . 60 GLU N N 119.4 . 1 147 . 61 VAL H H 8.61 . 1 148 . 61 VAL N N 124.1 . 1 149 . 64 ASP H H 7.70 . 1 150 . 64 ASP CA C 49.57 . 1 151 . 64 ASP N N 123.6 . 1 152 . 68 SER HA H 4.23 . 1 153 . 68 SER C C 175.80 . 1 154 . 68 SER CB C 63.13 . 1 155 . 69 LYS H H 7.12 . 1 156 . 69 LYS HA H 4.09 . 1 157 . 69 LYS HB2 H 2.12 . 1 158 . 69 LYS HB3 H 1.92 . 1 159 . 69 LYS C C 176.78 . 1 160 . 69 LYS CA C 58.03 . 1 161 . 69 LYS CB C 31.07 . 1 162 . 69 LYS N N 122.1 . 1 163 . 70 ASN H H 8.27 . 1 164 . 70 ASN HA H 4.86 . 1 165 . 70 ASN HB2 H 3.13 . 1 166 . 70 ASN HB3 H 2.75 . 1 167 . 70 ASN C C 175.06 . 1 168 . 70 ASN CA C 52.28 . 1 169 . 70 ASN CB C 38.01 . 1 170 . 70 ASN N N 114.6 . 1 171 . 71 LEU H H 7.65 . 1 172 . 71 LEU CA C 52.27 . 1 173 . 71 LEU N N 120.9 . 1 174 . 121 VAL H H 9.86 . 1 175 . 121 VAL HA H 5.16 . 1 176 . 121 VAL HB H 2.07 . 1 177 . 121 VAL CA C 59.06 . 1 178 . 121 VAL N N 123.4 . 1 179 . 122 THR H H 9.63 . 1 180 . 122 THR HA H 6.05 . 1 181 . 122 THR HB H 4.46 . 1 182 . 122 THR N N 116.5 . 1 183 . 133 GLY H H 7.99 . 1 184 . 133 GLY HA2 H 4.00 . 1 185 . 133 GLY C C 173.15 . 1 186 . 133 GLY CA C 44.43 . 1 187 . 133 GLY N N 109.1 . 1 188 . 134 LYS H H 7.85 . 1 189 . 134 LYS CA C 55.17 . 1 190 . 134 LYS N N 126.0 . 1 stop_ save_