data_5494 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Structure of PW2 Bound to SDS Micelles: A Tryptophan-rich Anticocidial Peptide Selected from Phage Display Libraries ; _BMRB_accession_number 5494 _BMRB_flat_file_name bmr5494.str _Entry_type original _Submission_date 2002-08-07 _Accession_date 2002-08-07 _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 Tinoco L. W. . 2 'da Silva' A. . Jr. 3 Leite A. . . 4 Valente A. P. . 5 Almeida F. C. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 3 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 252 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-08-22 original author . stop_ _Original_release_date 2002-08-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Structure of PW2 bound to SDS Micelles. A Tryptophan-rich Anticocidial Peptide selected from Phage Display Libraries ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22229374 _PubMed_ID 12130641 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tinoco L. W. . 2 'da Silva' A. . Jr. 3 Leite A. . . 4 Valente A. P. . 5 Almeida F. C. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 277 _Journal_issue 39 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 36351 _Page_last 36356 _Year 2002 _Details . loop_ _Keyword PW2 'Anticoccidial peptide' Eimeria SDS micelle antimicrobial stop_ save_ ################################## # Molecular system description # ################################## save_system_cationic_peptide _Saveframe_category molecular_system _Mol_system_name 'PW2 Bound to SDS Micelles' _Abbreviation_common 'cationic peptide' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'cationic peptide' $PW2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PW2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'anticocidial peptide' _Abbreviation_common PW2 _Molecular_mass 1611 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 12 _Mol_residue_sequence HPLKQYWWRPSI loop_ _Residue_seq_code _Residue_label 1 HIS 2 PRO 3 LEU 4 LYS 5 GLN 6 TYR 7 TRP 8 TRP 9 ARG 10 PRO 11 SER 12 ILE stop_ _Sequence_homology_query_date 2005-11-24 _Sequence_homology_query_revised_last_date 2005-11-22 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 5494 'anticocidial peptide' 100.00 12 100 100 0.92 PDB 1M02 'A Chain A, Nmr Structure Of Pw2 Bound To SdsMicelles: A Tryptophan- Rich Anticocidial PeptideSelected From Phage Display Libraries' 100.00 12 100 100 0.92 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PW2 . . . . . . 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 _Details $PW2 'chemical synthesis' . . . . . 'Selected from phage display library' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_PW2_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PW2 4.0 mM . sodium_phosphate_buffer 20.0 mM . sodium_chloride 100.0 mM . D2O 10 % . stop_ save_ save_PW2-40SDS _Saveframe_category sample _Sample_type bi-cell _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PW2 4.0 mM . sodium_phosphate_buffer 20.0 mM . SDS 40.0 mM . sodium_chloride 100.0 mM . stop_ save_ save_PW2-160SDS _Saveframe_category sample _Sample_type bi-cell _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PW2 4.0 mM . sodium_phosphate_buffer 20.0 mM . sodium_chloride 100.0 mM . SDS 160.0 mM . D2O 10.0 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task processing stop_ _Details 'Delaglio, F. Grzesiek, S., Zhu, G., Vuister, G. W., Pfeifer, J. and Bax, A.' save_ save_NMRVIEW _Saveframe_category software _Name NMRVIEW _Version 4.1.2 loop_ _Task 'data analysis' stop_ _Details 'Johnson, B. A. and Blevins, R. A.' save_ save_CNS _Saveframe_category software _Name CNS _Version 1.1 loop_ _Task refinement stop_ _Details ; Brunger, A. T., Adams, P.D., Clore, G.M., Delano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N.S., Read, R.J., Rice, L.M., Simonson, T., Warren, G.L. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 400 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_2D_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conds _Saveframe_category sample_conditions _Details 'PW2 in 20 mM sodium phosphate buffer' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 0.1 n/a temperature 298 1 K 'ionic strength' 100 . mM pressure 1 . atm 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_PW2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $PW2_1 stop_ _Sample_conditions_label $sample_conds _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'cationic peptide' _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 HIS H H 7.97 . 1 2 . 1 HIS HA H 4.22 . 1 3 . 1 HIS HB3 H 3.24 . 2 4 . 1 HIS HB2 H 3.12 . 2 5 . 2 PRO HA H 4.54 . 1 6 . 2 PRO HB3 H 2.38 . 1 7 . 2 PRO HB2 H 2.38 . 1 8 . 2 PRO HG3 H 2.02 . 2 9 . 2 PRO HG2 H 1.92 . 2 10 . 2 PRO HD3 H 3.79 . 2 11 . 2 PRO HD2 H 3.48 . 2 12 . 3 LEU H H 8.61 . 1 13 . 3 LEU HA H 4.38 . 1 14 . 3 LEU HB3 H 1.64 . 1 15 . 3 LEU HB2 H 1.64 . 1 16 . 3 LEU HD1 H 0.92 . 2 17 . 4 LYS H H 8.27 . 1 18 . 4 LYS HA H 4.21 . 1 19 . 4 LYS HB3 H 1.70 . 1 20 . 4 LYS HB2 H 1.70 . 1 21 . 4 LYS HG3 H 1.29 . 1 22 . 4 LYS HG2 H 1.29 . 1 23 . 4 LYS HD3 H 1.61 . 1 24 . 4 LYS HD2 H 1.61 . 1 25 . 4 LYS HE3 H 2.89 . 1 26 . 4 LYS HE2 H 2.89 . 1 27 . 5 GLN H H 8.21 . 1 28 . 5 GLN HA H 4.17 . 1 29 . 5 GLN HB3 H 1.72 . 1 30 . 5 GLN HB2 H 1.72 . 1 31 . 5 GLN HG3 H 2.09 . 1 32 . 5 GLN HG2 H 2.09 . 1 33 . 6 TYR H H 8.12 . 1 34 . 6 TYR HA H 4.23 . 1 35 . 6 TYR HB3 H 2.71 . 1 36 . 6 TYR HB2 H 2.71 . 1 37 . 6 TYR HD1 H 6.98 . 1 38 . 6 TYR HE1 H 6.80 . 1 39 . 6 TYR HE2 H 6.80 . 1 40 . 6 TYR HD2 H 6.98 . 1 41 . 7 TRP H H 7.62 . 1 42 . 7 TRP HA H 4.53 . 1 43 . 7 TRP HB3 H 3.22 . 2 44 . 7 TRP HB2 H 3.12 . 2 45 . 7 TRP HD1 H 7.24 . 1 46 . 7 TRP HE1 H 10.21 . 1 47 . 8 TRP H H 7.45 . 1 48 . 8 TRP HA H 4.41 . 1 49 . 8 TRP HB3 H 3.04 . 2 50 . 8 TRP HB2 H 2.79 . 2 51 . 8 TRP HD1 H 7.02 . 1 52 . 8 TRP HE1 H 10.10 . 1 53 . 9 ARG H H 7.52 . 1 54 . 9 ARG HA H 4.35 . 1 55 . 9 ARG HB3 H 1.63 . 1 56 . 9 ARG HB2 H 1.63 . 1 57 . 9 ARG HG3 H 1.40 . 1 58 . 9 ARG HG2 H 1.40 . 1 59 . 9 ARG HD3 H 3.04 . 1 60 . 9 ARG HD2 H 3.04 . 1 61 . 9 ARG HE H 7.53 . 1 62 . 10 PRO HA H 4.26 . 1 63 . 10 PRO HB3 H 2.27 . 1 64 . 10 PRO HB2 H 2.27 . 1 65 . 10 PRO HG3 H 1.96 . 1 66 . 10 PRO HG2 H 1.96 . 1 67 . 10 PRO HD3 H 3.49 . 1 68 . 10 PRO HD2 H 3.49 . 1 69 . 11 SER H H 8.36 . 1 70 . 11 SER HA H 4.36 . 1 71 . 11 SER HB3 H 3.85 . 1 72 . 11 SER HB2 H 3.85 . 1 73 . 12 ILE H H 8.33 . 1 74 . 12 ILE HA H 4.19 . 1 75 . 12 ILE HB H 1.70 . 1 76 . 12 ILE HG13 H 1.30 . 1 77 . 12 ILE HG12 H 1.30 . 1 stop_ save_ save_chemical_shift_PW2-40SDS _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $PW2-40SDS stop_ _Sample_conditions_label $sample_conds _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'cationic peptide' _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 HIS H H 7.96 . 1 2 . 1 HIS HA H 4.43 . 1 3 . 1 HIS HB3 H 3.19 . 2 4 . 1 HIS HB2 H 3.05 . 2 5 . 1 HIS HD2 H 7.18 . 3 6 . 1 HIS HE1 H 8.51 . 3 7 . 2 PRO HA H 4.54 . 1 8 . 2 PRO HB3 H 2.42 . 2 9 . 2 PRO HB2 H 1.89 . 2 10 . 2 PRO HG3 H 2.03 . 2 11 . 2 PRO HG2 H 1.97 . 2 12 . 2 PRO HD3 H 3.31 . 2 13 . 2 PRO HD2 H 3.54 . 2 14 . 3 LEU H H 8.41 . 1 15 . 3 LEU HA H 4.43 . 1 16 . 3 LEU HB3 H 1.88 . 2 17 . 3 LEU HB2 H 1.68 . 2 18 . 3 LEU HG H 1.61 . 1 19 . 3 LEU HD1 H 0.85 . 2 20 . 4 LYS H H 7.86 . 1 21 . 4 LYS HA H 3.99 . 1 22 . 4 LYS HB3 H 1.69 . 2 23 . 4 LYS HB2 H 1.68 . 2 24 . 4 LYS HG3 H 1.29 . 1 25 . 4 LYS HG2 H 1.29 . 1 26 . 4 LYS HD3 H 1.57 . 1 27 . 4 LYS HD2 H 1.57 . 1 28 . 4 LYS HE3 H 2.87 . 1 29 . 4 LYS HE2 H 2.87 . 1 30 . 4 LYS HZ H 6.95 . 1 31 . 5 GLN H H 7.96 . 1 32 . 5 GLN HA H 4.09 . 1 33 . 5 GLN HB3 H 1.71 . 1 34 . 5 GLN HB2 H 1.71 . 1 35 . 5 GLN HG3 H 2.00 . 2 36 . 5 GLN HG2 H 1.92 . 2 37 . 5 GLN HE21 H 6.73 . 2 38 . 5 GLN HE22 H 7.27 . 2 39 . 6 TYR H H 7.89 . 1 40 . 6 TYR HA H 4.10 . 1 41 . 6 TYR HB3 H 2.81 . 2 42 . 6 TYR HB2 H 2.73 . 2 43 . 6 TYR HD1 H 6.97 . 3 44 . 6 TYR HE1 H 6.75 . 1 45 . 6 TYR HE2 H 6.75 . 1 46 . 6 TYR HD2 H 6.96 . 3 47 . 7 TRP H H 7.66 . 1 48 . 7 TRP HA H 4.43 . 1 49 . 7 TRP HB3 H 3.05 . 2 50 . 7 TRP HB2 H 2.60 . 2 51 . 7 TRP HD1 H 6.82 . 1 52 . 7 TRP HE1 H 9.84 . 3 53 . 7 TRP HZ2 H 7.35 . 3 54 . 7 TRP HH2 H 7.03 . 1 55 . 7 TRP HZ3 H 6.91 . 3 56 . 7 TRP HE3 H 7.22 . 3 57 . 8 TRP H H 7.45 . 1 58 . 8 TRP HA H 4.33 . 1 59 . 8 TRP HB3 H 3.24 . 2 60 . 8 TRP HB2 H 3.30 . 2 61 . 8 TRP HD1 H 7.24 . 1 62 . 8 TRP HE1 H 9.91 . 3 63 . 8 TRP HZ2 H 7.37 . 3 64 . 8 TRP HH2 H 7.04 . 1 65 . 8 TRP HZ3 H 6.98 . 3 66 . 8 TRP HE3 H 6.83 . 3 67 . 9 ARG H H 7.67 . 1 68 . 9 ARG HA H 4.21 . 1 69 . 9 ARG HB3 H 1.57 . 1 70 . 9 ARG HB2 H 1.57 . 1 71 . 9 ARG HG3 H 1.26 . 2 72 . 9 ARG HG2 H 1.19 . 2 73 . 9 ARG HD3 H 3.00 . 2 74 . 9 ARG HD2 H 2.92 . 2 75 . 9 ARG HE H 6.91 . 1 76 . 9 ARG HH21 H 7.22 . 1 77 . 9 ARG HH22 H 7.22 . 1 78 . 10 PRO HA H 4.24 . 1 79 . 10 PRO HB3 H 2.20 . 2 80 . 10 PRO HB2 H 1.91 . 2 81 . 10 PRO HG3 H 1.84 . 2 82 . 10 PRO HG2 H 1.78 . 2 83 . 10 PRO HD3 H 3.45 . 2 84 . 10 PRO HD2 H 3.40 . 2 85 . 11 SER H H 8.14 . 1 86 . 11 SER HA H 4.33 . 1 87 . 11 SER HB3 H 3.80 . 1 88 . 11 SER HB2 H 3.80 . 1 89 . 12 ILE H H 7.96 . 1 90 . 12 ILE HA H 4.42 . 1 91 . 12 ILE HB H 1.91 . 1 92 . 12 ILE HG13 H 1.26 . 1 93 . 12 ILE HG12 H 1.26 . 1 94 . 12 ILE HD1 H 0.74 . 1 95 . 12 ILE HG2 H 0.85 . 1 stop_ save_ save_chemical_shift_PW2-160SDS _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $PW2-160SDS stop_ _Sample_conditions_label $sample_conds _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'cationic peptide' _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 HIS H H 7.99 . 1 2 . 1 HIS HA H 4.47 . 1 3 . 1 HIS HB3 H 3.09 . 2 4 . 1 HIS HB2 H 3.24 . 2 5 . 1 HIS HD2 H 7.23 . 3 6 . 1 HIS HE2 H 7.74 . 3 7 . 2 PRO HA H 4.59 . 1 8 . 2 PRO HB3 H 2.46 . 2 9 . 2 PRO HB2 H 1.94 . 2 10 . 2 PRO HG3 H 2.08 . 2 11 . 2 PRO HG2 H 2.02 . 2 12 . 2 PRO HD3 H 3.57 . 2 13 . 2 PRO HD2 H 3.34 . 2 14 . 3 LEU H H 8.44 . 1 15 . 3 LEU HA H 4.48 . 1 16 . 3 LEU HB3 H 1.92 . 2 17 . 3 LEU HB2 H 1.72 . 2 18 . 3 LEU HG H 1.67 . 1 19 . 3 LEU HD1 H 0.91 . 2 20 . 4 LYS H H 7.87 . 1 21 . 4 LYS HA H 4.01 . 1 22 . 4 LYS HB3 H 1.72 . 2 23 . 4 LYS HB2 H 1.71 . 2 24 . 4 LYS HG3 H 1.32 . 2 25 . 4 LYS HG2 H 1.31 . 2 26 . 4 LYS HD2 H 1.59 . 2 27 . 4 LYS HE2 H 2.90 . 2 28 . 4 LYS HZ H 7.37 . 1 29 . 5 GLN H H 7.97 . 1 30 . 5 GLN HA H 4.13 . 1 31 . 5 GLN HB3 H 1.75 . 2 32 . 5 GLN HG2 H 2.00 . 2 33 . 5 GLN HE21 H 6.75 . 2 34 . 5 GLN HE22 H 7.29 . 2 35 . 6 TYR H H 7.88 . 1 36 . 6 TYR HA H 4.22 . 1 37 . 6 TYR HB3 H 2.78 . 2 38 . 6 TYR HB2 H 2.89 . 2 39 . 6 TYR HD1 H 7.02 . 3 40 . 6 TYR HE1 H 6.79 . 3 41 . 7 TRP H H 7.68 . 1 42 . 7 TRP HA H 4.49 . 1 43 . 7 TRP HB3 H 3.26 . 2 44 . 7 TRP HD1 H 7.25 . 1 45 . 7 TRP HE1 H 9.92 . 3 46 . 7 TRP HZ2 H 7.41 . 3 47 . 7 TRP HH2 H 7.08 . 1 48 . 7 TRP HZ3 H 7.03 . 3 49 . 7 TRP HE3 H 7.49 . 3 50 . 8 TRP H H 7.07 . 1 51 . 8 TRP HA H 4.38 . 1 52 . 8 TRP HB3 H 2.72 . 2 53 . 8 TRP HB2 H 3.09 . 2 54 . 8 TRP HD1 H 6.92 . 1 55 . 8 TRP HE1 H 9.85 . 3 56 . 8 TRP HZ2 H 7.40 . 3 57 . 8 TRP HH2 H 6.95 . 1 58 . 8 TRP HZ3 H 7.07 . 3 59 . 8 TRP HE3 H 7.30 . 3 60 . 9 ARG H H 6.92 . 1 61 . 9 ARG HA H 4.21 . 1 62 . 9 ARG HB3 H 1.61 . 2 63 . 9 ARG HG3 H 1.32 . 2 64 . 9 ARG HG2 H 1.30 . 2 65 . 9 ARG HD3 H 3.08 . 2 66 . 9 ARG HD2 H 2.98 . 2 67 . 9 ARG HE H 6.97 . 1 68 . 9 ARG HH21 H 6.94 . 1 69 . 10 PRO HA H 4.26 . 1 70 . 10 PRO HB3 H 2.25 . 2 71 . 10 PRO HB2 H 1.95 . 2 72 . 10 PRO HG3 H 1.88 . 2 73 . 10 PRO HG2 H 1.82 . 2 74 . 10 PRO HD3 H 3.48 . 2 75 . 10 PRO HD2 H 3.40 . 2 76 . 11 SER H H 8.15 . 1 77 . 11 SER HA H 4.37 . 1 78 . 11 SER HB3 H 3.84 . 2 79 . 12 ILE H H 7.99 . 1 80 . 12 ILE HA H 4.47 . 1 stop_ save_