data_5860 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of Subtilosin A, an Antimicrobial Peptide from Bacillus subtilis with Unusual Post-translational Modifications Linking Cysteine Sulfurs to alpha-Carbons of Phenylalanine and Threonine ; _BMRB_accession_number 5860 _BMRB_flat_file_name bmr5860.str _Entry_type original _Submission_date 2003-07-04 _Accession_date 2003-07-04 _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 Kawulka Karen . . 2 Sprules Tara . . 3 McKay Ryan T. . 4 Mercier Pascal . . 5 Diaper Christopher M. . 6 Zuber Peter . . 7 Vederas John C. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 165 "13C chemical shifts" 93 "15N chemical shifts" 35 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-12-19 original author . stop_ _Original_release_date 2003-12-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure of Subtilosin A, an Antimicrobial Peptide from Bacillus subtilis with Unusual Posttranslational Modifications Linking Cysteine Sulfurs to alpha-Carbons of Phenylalanine and Threonine ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22583854 _PubMed_ID 12696888 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kawulka Karen . . 2 Sprules Tara . . 3 McKay Ryan T. . 4 Mercier Pascal . . 5 Diaper Christopher M. . 6 Zuber Peter . . 7 Vederas John C. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_volume 125 _Journal_issue 16 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4726 _Page_last 4727 _Year 2003 _Details . loop_ _Keyword bacteriocin thioether subtilosin stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Kawulka K, Sprules T, McKay RT, Mercier P, Diaper CM, Zuber P, Vederas JC. J Am Chem Soc. 2003 Apr 23;125(16):4726-7. ; _Citation_title 'Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to alpha-carbons of phenylalanine and threonine.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12696888 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kawulka Karen . . 2 Sprules Tara . . 3 McKay 'Ryan T' T. . 4 Mercier Pascal . . 5 Diaper 'Christopher M' M. . 6 Zuber Peter . . 7 Vederas 'John C' C. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full 'Journal of the American Chemical Society' _Journal_volume 125 _Journal_issue 16 _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 4726 _Page_last 4727 _Year 2003 _Details ; The complete primary and three-dimensional solution structures of subtilosin A (1), a bacteriocin from Bacillus subtilis, were determined by multidimensional NMR studies on peptide produced using isotopically labeled [(13)C,(15)N]medium derived from Anabaena sp. grown on sodium [(13)C]bicarbonate and [(15)N]nitrate. Additional samples of 1 were also generated by separate incorporations of [U-(13)C,(15)N]phenylalanine and [U-(13)C,(15)N]threonine using otherwise unlabeled media. The results demonstrate that in addition to having a cyclized peptide backbone (N and C termini), three cross-links are formed between the sulfurs of Cys13, Cys7, and Cys4 and the alpha-positions of Phe22, Thr28, and Phe31, respectively. Such posttranslational linkage of a thiol to the alpha-carbon of an amino acid residue is very unusual in natural peptides or proteins. Subtilosin A (1) belongs to a new class of bacteriocins. ; save_ ################################## # Molecular system description # ################################## save_system_SubA _Saveframe_category molecular_system _Mol_system_name 'Subtilosin A' _Abbreviation_common SubA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Subtilosin A' $SubA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'other bound, and free' loop_ _Biological_function bacteriocin stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SubA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Subtilosin A' _Abbreviation_common SubA _Molecular_mass 3401 _Mol_thiol_state 'other bound, and free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 35 _Mol_residue_sequence ; NKGCATCSIGAACLVDGPIP DFEIAGATGLFGLWG ; loop_ _Residue_seq_code _Residue_label 1 ASN 2 LYS 3 GLY 4 CYS 5 ALA 6 THR 7 CYS 8 SER 9 ILE 10 GLY 11 ALA 12 ALA 13 CYS 14 LEU 15 VAL 16 ASP 17 GLY 18 PRO 19 ILE 20 PRO 21 ASP 22 PHE 23 GLU 24 ILE 25 ALA 26 GLY 27 ALA 28 THR 29 GLY 30 LEU 31 PHE 32 GLY 33 LEU 34 TRP 35 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-12-21 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 DBJ BAI87397 "subtilosin A [Bacillus subtilis subsp. natto BEST195]" 100.00 43 100.00 100.00 2.09e-15 DBJ BAM55818 "subtilosin A [Bacillus subtilis BEST7613]" 100.00 43 100.00 100.00 2.09e-15 DBJ BAM59830 "subtilosin A [Bacillus subtilis BEST7003]" 100.00 43 100.00 100.00 2.09e-15 DBJ GAK81054 "subtilosin A [Bacillus subtilis Miyagi-4]" 100.00 43 100.00 100.00 2.09e-15 EMBL CAB09701 "subtilosin A [Bacillus subtilis subsp. subtilis str. 168]" 100.00 43 100.00 100.00 2.09e-15 EMBL CAB15763 "subtilosin A [Bacillus subtilis subsp. subtilis str. 168]" 100.00 43 100.00 100.00 2.09e-15 EMBL CAD23198 "subtilosin A [Bacillus subtilis]" 100.00 43 100.00 100.00 2.09e-15 EMBL CCU60834 "subtilosin A [Bacillus subtilis E1]" 100.00 43 100.00 100.00 2.09e-15 EMBL CEI59543 "subtilosin-A [Bacillus subtilis]" 100.00 43 100.00 100.00 2.09e-15 GB ABD92636 "subtilosin A [Bacillus subtilis]" 100.00 43 100.00 100.00 2.09e-15 GB ABD92637 "subtilosin A [Bacillus subtilis]" 100.00 43 100.00 100.00 2.09e-15 GB ABD92638 "subtilosin A [Bacillus subtilis]" 100.00 43 100.00 100.00 2.09e-15 GB ABW83032 "SboA [Bacillus amyloliquefaciens]" 100.00 43 100.00 100.00 2.09e-15 GB ACO72595 "subtilosin A [Bacillus subtilis]" 100.00 43 100.00 100.00 2.09e-15 REF NP_391616 "subtilosin-A [Bacillus subtilis subsp. subtilis str. 168]" 100.00 43 100.00 100.00 2.09e-15 REF WP_003222002 "MULTISPECIES: serine protease [Bacillales]" 100.00 43 100.00 100.00 2.09e-15 REF YP_003868035 "subtilosin A [Bacillus subtilis subsp. spizizenii str. W23]" 100.00 43 100.00 100.00 2.09e-15 REF YP_003975177 "subtilosin A [Bacillus atrophaeus 1942]" 100.00 43 100.00 100.00 2.09e-15 REF YP_004205572 "subtilosin A [Bacillus subtilis BSn5]" 100.00 43 100.00 100.00 2.09e-15 SP O07623 "RecName: Full=Subtilosin-A; AltName: Full=Antilisterial bacteriocin subtilosin; Flags: Precursor [Bacillus subtilis subsp. subt" 100.00 43 100.00 100.00 2.09e-15 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Fraction _Gene_mnemonic $SubA 'Bacillus subtilis' 1423 Eubacteria . Bacillus subtilis JH642 secreted sboA stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $SubA 'purified from the natural source' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SubA 1.0 mM '[U-100% 13C; U-80% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 2.2 loop_ _Task 'data processing' stop_ _Details ; Delaglio, F.; Grzesiek, S.; Vuister, G. W.; Zhu, G.; Pfeifer, J.; Bax, A. J. Biomolecular NMR \t1995, 6, 277-293 ; save_ save_NMRVIEW _Saveframe_category software _Name NMRVIEW _Version 5.0 loop_ _Task 'data analysis' stop_ _Details ; Johnson, B. A.; Blevins, R. A. J. Biomolecular NMR 1994, 4, 603-614." with in-house (NANUC) modifications ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-13C_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _Sample_label $sample_1 save_ save_1H-15N-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-15N-HSQC _Sample_label $sample_1 save_ save_HNHA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label $sample_1 save_ save_CBCA(CO)NNH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NNH _Sample_label $sample_1 save_ save_HCCH-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_1 save_ save_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HNCA_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HNCACB_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_13C-NOESYHSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-NOESYHSQC _Sample_label $sample_1 save_ save_15N-NOESYHSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-NOESYHSQC _Sample_label $sample_1 save_ save_15N-TOCSYHSQC_11 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-TOCSYHSQC _Sample_label $sample_1 save_ save_13C,15N-NOESY_12 _Saveframe_category NMR_applied_experiment _Experiment_name 13C,15N-NOESY _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-15N-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NNH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-NOESYHSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-NOESYHSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-TOCSYHSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name 13C,15N-NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.5 . n/a temperature 288 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_SubA_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Subtilosin A' _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 . 1 ASN N N 116.219 0.2 1 2 . 1 ASN H H 7.450 0.01 1 3 . 1 ASN CA C 52.377 0.2 1 4 . 1 ASN HA H 4.708 0.01 1 5 . 1 ASN CB C 39.328 0.2 1 6 . 1 ASN HB3 H 2.491 0.01 2 7 . 1 ASN HB2 H 3.880 0.01 2 8 . 1 ASN ND2 N 107.758 0.2 1 9 . 1 ASN HD21 H 7.968 0.01 2 10 . 1 ASN HD22 H 7.092 0.01 2 11 . 2 LYS N N 127.218 0.2 1 12 . 2 LYS H H 9.257 0.01 1 13 . 2 LYS CA C 59.068 0.2 1 14 . 2 LYS HA H 3.933 0.01 1 15 . 2 LYS CB C 32.258 0.2 1 16 . 2 LYS HB3 H 1.836 0.01 2 17 . 2 LYS HB2 H 1.730 0.01 2 18 . 2 LYS CG C 25.692 0.2 1 19 . 2 LYS HG3 H 1.473 0.01 2 20 . 2 LYS HG2 H 1.581 0.01 2 21 . 2 LYS CD C 29.435 0.2 1 22 . 2 LYS HD2 H 1.618 0.01 2 23 . 2 LYS CE C 41.909 0.2 1 24 . 2 LYS HE2 H 2.887 0.01 2 25 . 3 GLY N N 105.736 0.2 1 26 . 3 GLY H H 9.133 0.01 1 27 . 3 GLY CA C 46.573 0.2 1 28 . 3 GLY HA3 H 3.749 0.01 2 29 . 3 GLY HA2 H 3.827 0.01 2 30 . 4 CYS N N 118.627 0.2 1 31 . 4 CYS H H 7.769 0.01 1 32 . 4 CYS CA C 57.701 0.2 1 33 . 4 CYS HA H 3.974 0.01 1 34 . 4 CYS CB C 33.339 0.2 1 35 . 4 CYS HB3 H 3.145 0.01 2 36 . 4 CYS HB2 H 3.453 0.01 2 37 . 5 ALA N N 120.179 0.2 1 38 . 5 ALA H H 7.827 0.01 1 39 . 5 ALA CA C 54.716 0.2 1 40 . 5 ALA HA H 4.104 0.01 1 41 . 5 ALA CB C 17.879 0.2 1 42 . 5 ALA HB H 1.474 0.01 1 43 . 6 THR N N 111.274 0.2 1 44 . 6 THR H H 7.783 0.01 1 45 . 6 THR CA C 65.206 0.2 1 46 . 6 THR HA H 3.895 0.01 1 47 . 6 THR CB C 68.745 0.2 1 48 . 6 THR HB H 4.128 0.01 1 49 . 6 THR CG2 C 21.609 0.2 1 50 . 6 THR HG2 H 1.237 0.01 1 51 . 7 CYS N N 117.128 0.2 1 52 . 7 CYS H H 7.147 0.01 1 53 . 7 CYS CA C 56.913 0.2 1 54 . 7 CYS HA H 4.025 0.01 1 55 . 7 CYS CB C 31.841 0.2 1 56 . 7 CYS HB3 H 3.610 0.01 2 57 . 7 CYS HB2 H 2.840 0.01 2 58 . 8 SER N N 116.232 0.2 1 59 . 8 SER H H 8.000 0.01 1 60 . 8 SER CA C 61.886 0.2 1 61 . 8 SER HA H 4.045 0.01 1 62 . 8 SER CB C 62.614 0.2 1 63 . 8 SER HB3 H 3.936 0.01 2 64 . 9 ILE N N 119.568 0.2 1 65 . 9 ILE H H 7.468 0.01 1 66 . 9 ILE CA C 62.826 0.2 1 67 . 9 ILE HA H 4.053 0.01 1 68 . 9 ILE CB C 38.438 0.2 1 69 . 9 ILE HB H 1.912 0.01 1 70 . 9 ILE CG1 C 27.658 0.2 1 71 . 9 ILE HG13 H 1.446 0.01 2 72 . 9 ILE HG12 H 1.450 0.01 2 73 . 9 ILE CD1 C 13.412 0.2 1 74 . 9 ILE HD1 H 0.875 0.01 1 75 . 9 ILE CG2 C 17.439 0.2 1 76 . 9 ILE HG2 H 0.935 0.01 1 77 . 10 GLY N N 106.889 0.2 1 78 . 10 GLY H H 7.948 0.01 1 79 . 10 GLY CA C 47.134 0.2 1 80 . 10 GLY HA3 H 3.455 0.01 2 81 . 10 GLY HA2 H 4.008 0.01 2 82 . 11 ALA N N 121.647 0.2 1 83 . 11 ALA H H 7.988 0.01 1 84 . 11 ALA CA C 54.686 0.2 1 85 . 11 ALA HA H 3.981 0.01 1 86 . 11 ALA CB C 17.697 0.2 1 87 . 11 ALA HB H 1.427 0.01 1 88 . 12 ALA N N 118.722 0.2 1 89 . 12 ALA H H 8.023 0.01 1 90 . 12 ALA CA C 54.664 0.2 1 91 . 12 ALA HA H 3.998 0.01 1 92 . 12 ALA CB C 17.434 0.2 1 93 . 12 ALA HB H 1.471 0.01 1 94 . 13 CYS N N 110.215 0.2 1 95 . 13 CYS H H 7.515 0.01 1 96 . 13 CYS CA C 56.141 0.2 1 97 . 13 CYS HA H 4.175 0.01 1 98 . 13 CYS CB C 32.111 0.2 1 99 . 13 CYS HB3 H 3.281 0.01 2 100 . 13 CYS HB2 H 3.492 0.01 2 101 . 14 LEU N N 125.160 0.2 1 102 . 14 LEU H H 8.073 0.01 1 103 . 14 LEU CA C 56.668 0.2 1 104 . 14 LEU HA H 4.222 0.01 1 105 . 14 LEU CB C 40.939 0.2 1 106 . 14 LEU HB3 H 1.904 0.01 2 107 . 14 LEU HB2 H 1.506 0.01 2 108 . 14 LEU CG C 27.597 0.2 1 109 . 14 LEU HG H 1.691 0.01 1 110 . 14 LEU CD1 C 24.815 0.2 4 111 . 14 LEU HD1 H 0.900 0.01 2 112 . 14 LEU CD2 C 22.353 0.2 4 113 . 14 LEU HD2 H 0.857 0.01 2 114 . 15 VAL N N 118.019 0.2 1 115 . 15 VAL H H 7.516 0.01 1 116 . 15 VAL CA C 65.064 0.2 1 117 . 15 VAL HA H 3.817 0.01 1 118 . 15 VAL CB C 31.525 0.2 1 119 . 15 VAL HB H 2.225 0.01 1 120 . 15 VAL CG2 C 20.872 0.2 4 121 . 15 VAL HG2 H 1.020 0.01 2 122 . 15 VAL CG1 C 20.123 0.2 4 123 . 15 VAL HG1 H 0.951 0.01 2 124 . 16 ASP N N 114.415 0.2 1 125 . 16 ASP H H 6.758 0.01 1 126 . 16 ASP CA C 50.473 0.2 1 127 . 16 ASP HA H 4.804 0.01 1 128 . 16 ASP CB C 38.405 0.2 1 129 . 16 ASP HB3 H 2.420 0.01 2 130 . 16 ASP HB2 H 3.197 0.01 2 131 . 17 GLY N N 104.272 0.2 1 132 . 17 GLY H H 7.897 0.01 1 133 . 17 GLY CA C 44.130 0.2 1 134 . 17 GLY HA3 H 3.727 0.01 2 135 . 17 GLY HA2 H 4.402 0.01 2 136 . 18 PRO CA C 63.577 0.2 1 137 . 18 PRO HA H 4.497 0.01 1 138 . 18 PRO CB C 30.965 0.2 1 139 . 18 PRO HB3 H 1.940 0.01 2 140 . 18 PRO HB2 H 2.093 0.01 2 141 . 18 PRO CG C 26.391 0.2 1 142 . 18 PRO HG3 H 1.753 0.01 2 143 . 18 PRO HG2 H 1.920 0.01 2 144 . 18 PRO CD C 49.738 0.2 1 145 . 18 PRO HD3 H 3.500 0.01 2 146 . 18 PRO HD2 H 3.765 0.01 2 147 . 19 ILE N N 121.987 0.2 1 148 . 19 ILE H H 7.067 0.01 1 149 . 19 ILE CA C 60.079 0.2 1 150 . 19 ILE HA H 4.036 0.01 1 151 . 19 ILE CB C 38.228 0.2 1 152 . 19 ILE HB H 1.563 0.01 1 153 . 19 ILE CG1 C 28.186 0.2 1 154 . 19 ILE HG13 H 1.543 0.01 2 155 . 19 ILE HG12 H 1.050 0.01 2 156 . 19 ILE CD1 C 12.892 0.2 1 157 . 19 ILE HD1 H 0.858 0.01 1 158 . 19 ILE CG2 C 16.157 0.2 1 159 . 19 ILE HG2 H 0.726 0.01 1 160 . 20 PRO CA C 63.046 0.2 1 161 . 20 PRO HA H 4.115 0.01 1 162 . 20 PRO CB C 30.602 0.2 1 163 . 20 PRO HB3 H 1.887 0.01 2 164 . 20 PRO HB2 H 1.952 0.01 2 165 . 20 PRO CG C 27.704 0.2 1 166 . 20 PRO HG3 H 2.281 0.01 2 167 . 20 PRO HG2 H 1.948 0.01 2 168 . 20 PRO CD C 51.552 0.2 1 169 . 20 PRO HD3 H 3.545 0.01 2 170 . 20 PRO HD2 H 3.873 0.01 2 171 . 21 ASP N N 122.249 0.2 1 172 . 21 ASP H H 8.917 0.01 1 173 . 21 ASP CA C 54.223 0.2 1 174 . 21 ASP HA H 4.447 0.01 1 175 . 21 ASP CB C 38.190 0.2 1 176 . 21 ASP HB3 H 2.244 0.01 2 177 . 21 ASP HB2 H 2.759 0.01 2 178 . 22 PHE N N 124.887 0.2 1 179 . 22 PHE H H 7.979 0.01 1 180 . 22 PHE CA C 69.380 0.2 1 181 . 22 PHE CB C 40.743 0.2 1 182 . 22 PHE HB3 H 3.752 0.01 2 183 . 22 PHE HB2 H 3.213 0.01 2 184 . 22 PHE HD1 H 7.120 0.01 3 185 . 23 GLU N N 120.458 0.2 1 186 . 23 GLU H H 10.482 0.01 1 187 . 23 GLU CA C 61.498 0.2 1 188 . 23 GLU HA H 3.853 0.01 1 189 . 23 GLU CB C 28.737 0.2 1 190 . 23 GLU HB3 H 1.729 0.01 2 191 . 23 GLU HB2 H 1.883 0.01 2 192 . 23 GLU CG C 36.879 0.2 1 193 . 23 GLU HG3 H 2.119 0.01 2 194 . 23 GLU HG2 H 2.514 0.01 2 195 . 24 ILE N N 117.787 0.2 1 196 . 24 ILE H H 7.771 0.01 1 197 . 24 ILE CA C 63.861 0.2 1 198 . 24 ILE HA H 3.791 0.01 1 199 . 24 ILE CB C 38.086 0.2 1 200 . 24 ILE HB H 1.908 0.01 1 201 . 24 ILE CG1 C 28.629 0.2 1 202 . 24 ILE HG13 H 1.323 0.01 2 203 . 24 ILE HG12 H 1.495 0.01 2 204 . 24 ILE CD1 C 17.093 0.2 1 205 . 24 ILE HD1 H 0.947 0.01 1 206 . 24 ILE CG2 C 20.030 0.2 1 207 . 24 ILE HG2 H 0.905 0.01 1 208 . 25 ALA N N 120.818 0.2 1 209 . 25 ALA H H 8.017 0.01 1 210 . 25 ALA CA C 53.946 0.2 1 211 . 25 ALA HA H 4.116 0.01 1 212 . 25 ALA CB C 17.953 0.2 1 213 . 25 ALA HB H 1.440 0.01 1 214 . 26 GLY N N 102.808 0.2 1 215 . 26 GLY H H 8.137 0.01 1 216 . 26 GLY CA C 45.993 0.2 1 217 . 26 GLY HA3 H 3.783 0.01 2 218 . 26 GLY HA2 H 4.228 0.01 2 219 . 27 ALA N N 123.622 0.2 1 220 . 27 ALA H H 7.748 0.01 1 221 . 27 ALA CA C 54.881 0.2 1 222 . 27 ALA HA H 3.946 0.01 1 223 . 27 ALA CB C 17.850 0.2 1 224 . 27 ALA HB H 1.429 0.01 1 225 . 28 THR N N 120.253 0.2 1 226 . 28 THR H H 8.105 0.01 1 227 . 28 THR CA C 72.797 0.2 1 228 . 28 THR CB C 70.885 0.2 1 229 . 28 THR HB H 4.228 0.01 1 230 . 28 THR CG2 C 18.425 0.2 1 231 . 28 THR HG2 H 0.995 0.01 1 232 . 29 GLY N N 108.686 0.2 1 233 . 29 GLY H H 8.115 0.01 1 234 . 29 GLY CA C 46.828 0.2 1 235 . 29 GLY HA3 H 3.889 0.01 2 236 . 29 GLY HA2 H 3.808 0.01 2 237 . 30 LEU N N 120.842 0.2 1 238 . 30 LEU H H 7.616 0.01 1 239 . 30 LEU CA C 57.845 0.2 1 240 . 30 LEU HA H 3.943 0.01 1 241 . 30 LEU CB C 42.402 0.2 1 242 . 30 LEU HB2 H 1.491 0.01 2 243 . 30 LEU CG C 27.057 0.2 1 244 . 30 LEU HG H 1.840 0.01 1 245 . 30 LEU CD1 C 25.476 0.2 4 246 . 30 LEU HD1 H 0.865 0.01 2 247 . 30 LEU CD2 C 24.985 0.2 4 248 . 30 LEU HD2 H 0.945 0.01 2 249 . 31 PHE N N 122.357 0.2 1 250 . 31 PHE H H 8.430 0.01 1 251 . 31 PHE CA C 69.821 0.2 1 252 . 31 PHE CB C 42.503 0.2 1 253 . 31 PHE HB3 H 3.896 0.01 2 254 . 31 PHE HB2 H 3.323 0.01 2 255 . 31 PHE HD1 H 6.997 0.01 3 256 . 31 PHE HE1 H 7.100 0.01 3 257 . 32 GLY N N 107.682 0.2 1 258 . 32 GLY H H 8.147 0.01 1 259 . 32 GLY CA C 47.161 0.2 1 260 . 32 GLY HA3 H 3.809 0.01 2 261 . 32 GLY HA2 H 4.014 0.01 2 262 . 33 LEU N N 120.187 0.2 1 263 . 33 LEU H H 7.893 0.01 1 264 . 33 LEU CA C 57.029 0.2 1 265 . 33 LEU HA H 3.977 0.01 1 266 . 33 LEU CB C 40.867 0.2 1 267 . 33 LEU HB3 H 1.188 0.01 2 268 . 33 LEU HB2 H 1.773 0.01 2 269 . 33 LEU CG C 27.187 0.2 1 270 . 33 LEU HG H 1.634 0.01 1 271 . 33 LEU CD1 C 22.219 0.2 4 272 . 33 LEU HD1 H 0.747 0.01 2 273 . 33 LEU CD2 C 25.199 0.2 4 274 . 33 LEU HD2 H 0.875 0.01 2 275 . 34 TRP N N 114.289 0.2 1 276 . 34 TRP H H 7.124 0.01 1 277 . 34 TRP CA C 56.045 0.2 1 278 . 34 TRP HA H 4.722 0.01 1 279 . 34 TRP CB C 29.924 0.2 1 280 . 34 TRP HB3 H 3.700 0.01 2 281 . 34 TRP HB2 H 2.985 0.01 2 282 . 34 TRP HD1 H 7.243 0.01 1 283 . 34 TRP NE1 N 127.108 0.2 1 284 . 34 TRP HE1 H 10.406 0.01 1 285 . 34 TRP HZ2 H 7.050 0.01 1 286 . 34 TRP HH2 H 7.457 0.01 1 287 . 34 TRP HZ3 H 6.895 0.01 1 288 . 34 TRP HE3 H 7.050 0.01 1 289 . 35 GLY N N 105.341 0.2 1 290 . 35 GLY H H 7.813 0.01 1 291 . 35 GLY CA C 45.836 0.2 1 292 . 35 GLY HA3 H 3.664 0.01 2 293 . 35 GLY HA2 H 4.038 0.01 2 stop_ loop_ _Atom_shift_assign_ID_ambiguity 112 110 '122,120' '247,245' '256,255' '273,271' stop_ save_