data_5815 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5815 _Entry.Title ; Structure of the coat protein in fd filamentous bacteriophage particles ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2003-06-03 _Entry.Accession_date 2003-06-04 _Entry.Last_release_date 2003-10-17 _Entry.Original_release_date 2003-10-17 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 A. Zeri . C. . 5815 2 M. Mesleh . F. . 5815 3 A. Nevzorov . A. . 5815 4 S. Opella . J. . 5815 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5815 RDCs 1 5815 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 43 5815 'residual dipolar couplings' 43 5815 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2003-10-17 2003-06-03 original author . 5815 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5815 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 22656956 _Citation.DOI . _Citation.PubMed_ID 12750469 _Citation.Full_citation . _Citation.Title ; Structure of the Coat Protein in fd Filamentous Bacteriophage Particles Determined by Solid-state NMR Spectroscopy ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Proc. Natl. Acad. Sci. U. S. A.' _Citation.Journal_name_full . _Citation.Journal_volume 100 _Citation.Journal_issue 11 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 6458 _Citation.Page_last 6463 _Citation.Year 2003 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 A. Zeri . C. . 5815 1 2 M. Mesleh . F. . 5815 1 3 A. Nevzorov . A. . 5815 1 4 S. Opella . J. . 5815 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'ALPHA HELIX' 5815 1 bacteriophage 5815 1 'solid-state NMR' 5815 1 PISEMA 5815 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5815 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 12750469 _Citation.Full_citation ; Zeri AC, Mesleh MF, Nevzorov AA, Opella SJ. Proc Natl Acad Sci U S A. 2003 May 27;100(11) ; _Citation.Title 'Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Proc. Natl. Acad. Sci. U.S.A.' _Citation.Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Citation.Journal_volume 100 _Citation.Journal_issue 11 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0027-8424 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 6458 _Citation.Page_last 6463 _Citation.Year 2003 _Citation.Details ; The atomic resolution structure of fd coat protein determined by solid-state NMR spectroscopy of magnetically aligned filamentous bacteriophage particles differs from that previously determined by x-ray fiber diffraction. Most notably, the 50-residue protein is not a single curved helix, but rather is a nearly ideal straight helix between residues 7 and 38, where there is a distinct kink, and then a straight helix with a different orientation between residues 39 and 49. Residues 1-5 have been shown to be mobile and unstructured, and proline 6 terminates the helix. The structure of the coat protein in virus particles, in combination with the structure of the membrane-bound form of the same protein in bilayers, also recently determined by solid-state NMR spectroscopy, provides insight into the viral assembly process. In addition to their roles in molecular biology and biotechnology, the filamentous bacteriophages continue to serve as model systems for the development of experimental methods for determining the structures of proteins in biological supramolecular assemblies. New NMR results include the complete sequential assignment of the two-dimensional polarization inversion spin-exchange at the magic angle spectrum of a uniformly 15N-labeled 50-residue protein in a 1.6 x 107 Da particle in solution, and the calculation of the three-dimensional structure of the protein from orientational restraints with an accuracy equivalent to an rms deviation of approximately 1A. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'Ana Carolina' Zeri A. C. . 5815 2 2 'Michael F' Mesleh M. F. . 5815 2 3 'Alexander A' Nevzorov A. A. . 5815 2 4 'Stanley J' Opella S. J. . 5815 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_p8 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_p8 _Assembly.Entry_ID 5815 _Assembly.ID 1 _Assembly.Name 'Major coat protein' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'not present' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID 'virus particle' 5815 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'p8 monomer' 1 $p8 . . . native . . . . . 5815 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1NH4 . . . . . . 5815 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Major coat protein' system 5815 1 p8 abbreviation 5815 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'bacteriophage coat protein' 5815 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_p8 _Entity.Sf_category entity _Entity.Sf_framecode p8 _Entity.Entry_ID 5815 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'bacteriophage fd major coat protein' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; AEGDDPAKAAFDSLQASATE MIGYAWAMVVVIVGATIGIK LFKKFTSKAS ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 50 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID . . SWISS-PROT P69539 . 'Coat protein B precursor (Major coat protein)' . . . . . 100.00 73 98.00 98.00 3.96e-19 . . . . 5815 1 . . SWISS-PROT P69540 . 'Coat protein B precursor (Major coat protein)' . . . . . 100.00 73 98.00 98.00 3.96e-19 . . . . 5815 1 . . GenBank AAF75598 . 'major coat protein pVIII precursor [Filamentous phage cloning vector fd-tet]' . . . . . 100.00 73 98.00 98.00 3.96e-19 . . . . 5815 1 . . PRF 0812197K . DNA,phage . . . . . 100.00 73 98.00 98.00 3.96e-19 . . . . 5815 1 . . GenBank AAA32308 . 'VIII [Enterobacteria phage fd]' . . . . . 100.00 73 98.00 98.00 3.96e-19 . . . . 5815 1 . . GenBank AAB24445 . 'gene-8 protein, g8p=major coat protein [bacteriophage fd, Peptide, 50 aa]' . . . . . 100.00 50 98.00 98.00 7.86e-19 . . . . 5815 1 . . GenBank AAA32214 . 'protein VIII' . . . . . 100.00 73 98.00 98.00 3.96e-19 . . . . 5815 1 . . GenBank AAA32220 . 'major coat protein B' . . . . . 100.00 73 98.00 98.00 3.96e-19 . . . . 5815 1 . . PDB 2HI5 . 'Model For Bacteriophage Fd From Cryo-Em' . . . . . 100.00 50 98.00 98.00 7.86e-19 . . . . 5815 1 . . EMBL CAA23871 . 'unnamed protein product [Enterobacteria phage f1]' . . . . . 100.00 73 98.00 98.00 3.96e-19 . . . . 5815 1 . . PDB 2C0W . 'Molecular Structure Of Fd Filamentous Bacteriophage Refined With Respect To X-Ray Fibre Diffraction' . . . . . 100.00 50 100.00 100.00 1.34e-19 . . . . 5815 1 . . PDB 2C0X . 'Molecular Structure Of Fd Filamentous Bacteriophage Refined With Respect To X-Ray Fibre Diffraction And Solid-State Nmr Data' . . . . . 100.00 50 100.00 100.00 1.34e-19 . . . . 5815 1 . . PDB 1MZT . 'Nmr Structure Of The Fd Bacteriophage Pviii Coat Protein In Lipid Bilayer Membranes' . . . . . 100.00 50 98.00 98.00 7.86e-19 . . . . 5815 1 . . PDB 1NH4 . 'Structure Of The Coat Protein In Fd Filamentous Bacteriophage Particles' . . . . . 100.00 50 100.00 100.00 1.34e-19 . . . . 5815 1 . . PDB 1IFI . 'Molecular Models And Structural Comparisons Of Native And Mutant Class I Filamentous Bacteriophages Ff (Fd, F1, M13), If1 And Ike' . . . . . 100.00 50 98.00 98.00 7.86e-19 . . . . 5815 1 . . PDB 1IFJ . 'Molecular Models And Structural Comparisons Of Native And Mutant Class I Filamentous Bacteriophages Ff (Fd, F1, M13), If1 And Ike' . . . . . 100.00 50 98.00 98.00 7.86e-19 . . . . 5815 1 . . PDB 1FDM . 'Fd Major Coat Protein In Sds Micelles, Nmr, 20 Structures' . . . . . 100.00 50 98.00 98.00 7.86e-19 . . . . 5815 1 . . PDB 1IFD . 'Model-Building Studies Of Inovirus: Genetic Variations On A Geometric Theme' . . . . . 100.00 50 98.00 98.00 7.86e-19 . . . . 5815 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'bacteriophage fd major coat protein' common 5815 1 p8 abbreviation 5815 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . ALA . 5815 1 2 . GLU . 5815 1 3 . GLY . 5815 1 4 . ASP . 5815 1 5 . ASP . 5815 1 6 . PRO . 5815 1 7 . ALA . 5815 1 8 . LYS . 5815 1 9 . ALA . 5815 1 10 . ALA . 5815 1 11 . PHE . 5815 1 12 . ASP . 5815 1 13 . SER . 5815 1 14 . LEU . 5815 1 15 . GLN . 5815 1 16 . ALA . 5815 1 17 . SER . 5815 1 18 . ALA . 5815 1 19 . THR . 5815 1 20 . GLU . 5815 1 21 . MET . 5815 1 22 . ILE . 5815 1 23 . GLY . 5815 1 24 . TYR . 5815 1 25 . ALA . 5815 1 26 . TRP . 5815 1 27 . ALA . 5815 1 28 . MET . 5815 1 29 . VAL . 5815 1 30 . VAL . 5815 1 31 . VAL . 5815 1 32 . ILE . 5815 1 33 . VAL . 5815 1 34 . GLY . 5815 1 35 . ALA . 5815 1 36 . THR . 5815 1 37 . ILE . 5815 1 38 . GLY . 5815 1 39 . ILE . 5815 1 40 . LYS . 5815 1 41 . LEU . 5815 1 42 . PHE . 5815 1 43 . LYS . 5815 1 44 . LYS . 5815 1 45 . PHE . 5815 1 46 . THR . 5815 1 47 . SER . 5815 1 48 . LYS . 5815 1 49 . ALA . 5815 1 50 . SER . 5815 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . ALA 1 1 5815 1 . GLU 2 2 5815 1 . GLY 3 3 5815 1 . ASP 4 4 5815 1 . ASP 5 5 5815 1 . PRO 6 6 5815 1 . ALA 7 7 5815 1 . LYS 8 8 5815 1 . ALA 9 9 5815 1 . ALA 10 10 5815 1 . PHE 11 11 5815 1 . ASP 12 12 5815 1 . SER 13 13 5815 1 . LEU 14 14 5815 1 . GLN 15 15 5815 1 . ALA 16 16 5815 1 . SER 17 17 5815 1 . ALA 18 18 5815 1 . THR 19 19 5815 1 . GLU 20 20 5815 1 . MET 21 21 5815 1 . ILE 22 22 5815 1 . GLY 23 23 5815 1 . TYR 24 24 5815 1 . ALA 25 25 5815 1 . TRP 26 26 5815 1 . ALA 27 27 5815 1 . MET 28 28 5815 1 . VAL 29 29 5815 1 . VAL 30 30 5815 1 . VAL 31 31 5815 1 . ILE 32 32 5815 1 . VAL 33 33 5815 1 . GLY 34 34 5815 1 . ALA 35 35 5815 1 . THR 36 36 5815 1 . ILE 37 37 5815 1 . GLY 38 38 5815 1 . ILE 39 39 5815 1 . LYS 40 40 5815 1 . LEU 41 41 5815 1 . PHE 42 42 5815 1 . LYS 43 43 5815 1 . LYS 44 44 5815 1 . PHE 45 45 5815 1 . THR 46 46 5815 1 . SER 47 47 5815 1 . LYS 48 48 5815 1 . ALA 49 49 5815 1 . SER 50 50 5815 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 5815 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $p8 . 12420 virus . 'Filamentous bacteriophage' bacteriophage . . virus . Filamentous bacteriophage . . . . . . . . . . . . . . . . . . . . . 5815 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 5815 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $p8 . 'purified from the natural source' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5815 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5815 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details 'bacteriophage particles were suspended in aqueous buffer' _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'bacteriophage fd major coat protein' [U-15N] . . 1 $p8 . . 50 . . mg/ml . . . . 5815 1 2 'sodium borate buffer' . . . . . . . 5 . . mM . . . . 5815 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_cond_1 _Sample_condition_list.Entry_ID 5815 _Sample_condition_list.ID 1 _Sample_condition_list.Details ; at the concentration used for the experiment, 50 mg/ml, the virus particles orient spontaneously in the magnetic field ; loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 8.0 0.2 na 5815 1 temperature 338 1 K 5815 1 pressure 1 . atm 5815 1 stop_ save_ ############################ # Computer software used # ############################ save_tecmag _Software.Sf_category software _Software.Sf_framecode tecmag _Software.Entry_ID 5815 _Software.ID 1 _Software.Name tecmag _Software.Version libra _Software.Details tecmag loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 5815 1 stop_ save_ save_FELIX _Software.Sf_category software _Software.Sf_framecode FELIX _Software.Entry_ID 5815 _Software.ID 2 _Software.Name FELIX _Software.Version 97 _Software.Details MSI loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 5815 2 stop_ save_ save_SCWRL _Software.Sf_category software _Software.Sf_framecode SCWRL _Software.Entry_ID 5815 _Software.ID 3 _Software.Name SCWRL _Software.Version 2.1 _Software.Details 'Dunbrack, R.' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 5815 3 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 5815 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer homebuilt _NMR_spectrometer.Model . _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 550 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5815 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer homebuilt . . 550 . . . 5815 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 5815 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 PISEMA-Polarization . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5815 1 2 'Inversion and Spin Exchange at the Magic Angle' . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5815 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 5815 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name PISEMA-Polarization _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 5815 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name 'Inversion and Spin Exchange at the Magic Angle' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5815 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID N 15 AMS ammonium . . . . ppm 26.8 external direct . external_to_the_sample cylindrical perpendicular_to_Bo . . . . . . 5815 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_set_1 _Assigned_chem_shift_list.Entry_ID 5815 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 PISEMA-Polarization 1 $sample_1 . 5815 1 2 'Inversion and Spin Exchange at the Magic Angle' 1 $sample_1 . 5815 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 7 7 ALA N N 15 179.4 . . 1 . . . . . . . . 5815 1 2 . 1 1 8 8 LYS N N 15 217 . . 1 . . . . . . . . 5815 1 3 . 1 1 9 9 ALA N N 15 219.6 . . 1 . . . . . . . . 5815 1 4 . 1 1 10 10 ALA N N 15 159.5 . . 1 . . . . . . . . 5815 1 5 . 1 1 11 11 PHE N N 15 197.2 . . 1 . . . . . . . . 5815 1 6 . 1 1 12 12 ASP N N 15 216.7 . . 1 . . . . . . . . 5815 1 7 . 1 1 13 13 SER N N 15 172.3 . . 1 . . . . . . . . 5815 1 8 . 1 1 14 14 LEU N N 15 183.5 . . 1 . . . . . . . . 5815 1 9 . 1 1 15 15 GLN N N 15 216.5 . . 1 . . . . . . . . 5815 1 10 . 1 1 16 16 ALA N N 15 217.9 . . 1 . . . . . . . . 5815 1 11 . 1 1 17 17 SER N N 15 169.8 . . 1 . . . . . . . . 5815 1 12 . 1 1 18 18 ALA N N 15 200 . . 1 . . . . . . . . 5815 1 13 . 1 1 19 19 THR N N 15 211.5 . . 1 . . . . . . . . 5815 1 14 . 1 1 20 20 GLU N N 15 203.8 . . 1 . . . . . . . . 5815 1 15 . 1 1 21 21 MET N N 15 179 . . 1 . . . . . . . . 5815 1 16 . 1 1 22 22 ILE N N 15 199 . . 1 . . . . . . . . 5815 1 17 . 1 1 23 23 GLY N N 15 211.8 . . 1 . . . . . . . . 5815 1 18 . 1 1 24 24 TYR N N 15 190.4 . . 1 . . . . . . . . 5815 1 19 . 1 1 25 25 ALA N N 15 175 . . 1 . . . . . . . . 5815 1 20 . 1 1 26 26 TRP N N 15 207.7 . . 1 . . . . . . . . 5815 1 21 . 1 1 27 27 ALA N N 15 214.6 . . 1 . . . . . . . . 5815 1 22 . 1 1 28 28 MET N N 15 166.2 . . 1 . . . . . . . . 5815 1 23 . 1 1 29 29 VAL N N 15 185.3 . . 1 . . . . . . . . 5815 1 24 . 1 1 30 30 VAL N N 15 217 . . 1 . . . . . . . . 5815 1 25 . 1 1 31 31 VAL N N 15 210 . . 1 . . . . . . . . 5815 1 26 . 1 1 32 32 ILE N N 15 164 . . 1 . . . . . . . . 5815 1 27 . 1 1 33 33 VAL N N 15 193.2 . . 1 . . . . . . . . 5815 1 28 . 1 1 34 34 GLY N N 15 216 . . 1 . . . . . . . . 5815 1 29 . 1 1 35 35 ALA N N 15 192 . . 1 . . . . . . . . 5815 1 30 . 1 1 36 36 THR N N 15 159.6 . . 1 . . . . . . . . 5815 1 31 . 1 1 37 37 ILE N N 15 202 . . 1 . . . . . . . . 5815 1 32 . 1 1 38 38 GLY N N 15 210.8 . . 1 . . . . . . . . 5815 1 33 . 1 1 39 39 ILE N N 15 209.2 . . 1 . . . . . . . . 5815 1 34 . 1 1 40 40 LYS N N 15 201.5 . . 1 . . . . . . . . 5815 1 35 . 1 1 41 41 LEU N N 15 216.6 . . 1 . . . . . . . . 5815 1 36 . 1 1 42 42 PHE N N 15 229 . . 1 . . . . . . . . 5815 1 37 . 1 1 43 43 LYS N N 15 206.3 . . 1 . . . . . . . . 5815 1 38 . 1 1 44 44 LYS N N 15 192.5 . . 1 . . . . . . . . 5815 1 39 . 1 1 45 45 PHE N N 15 215.7 . . 1 . . . . . . . . 5815 1 40 . 1 1 46 46 THR N N 15 210.5 . . 1 . . . . . . . . 5815 1 41 . 1 1 47 47 SER N N 15 196.2 . . 1 . . . . . . . . 5815 1 42 . 1 1 48 48 LYS N N 15 190.2 . . 1 . . . . . . . . 5815 1 43 . 1 1 49 49 ALA N N 15 205.4 . . 1 . . . . . . . . 5815 1 stop_ save_ ################################ # Residual dipolar couplings # ################################ save_Dipolar_couplings _RDC_list.Sf_category RDCs _RDC_list.Sf_framecode Dipolar_couplings _RDC_list.Entry_ID 5815 _RDC_list.ID 1 _RDC_list.Sample_condition_list_ID 1 _RDC_list.Sample_condition_list_label $sample_cond_1 _RDC_list.Spectrometer_frequency_1H 550 _RDC_list.Bond_length_usage_flag . _RDC_list.Dipolar_constraint_calib_method . _RDC_list.Mol_align_tensor_axial_sym_mol . _RDC_list.Mol_align_tensor_rhombic_mol . _RDC_list.General_order_param_int_motions . _RDC_list.Assumed_H_N_bond_length . _RDC_list.Assumed_H_C_bond_length . _RDC_list.Assumed_C_N_bond_length . _RDC_list.Details . _RDC_list.Text_data_format . _RDC_list.Text_data . loop_ _RDC_experiment.Experiment_ID _RDC_experiment.Experiment_name _RDC_experiment.Sample_ID _RDC_experiment.Sample_label _RDC_experiment.Sample_state _RDC_experiment.Entry_ID _RDC_experiment.RDC_list_ID . . 1 $sample_1 . 5815 1 stop_ loop_ _RDC.ID _RDC.RDC_code _RDC.Assembly_atom_ID_1 _RDC.Entity_assembly_ID_1 _RDC.Entity_ID_1 _RDC.Comp_index_ID_1 _RDC.Seq_ID_1 _RDC.Comp_ID_1 _RDC.Atom_ID_1 _RDC.Atom_type_1 _RDC.Atom_isotope_number_1 _RDC.Ambiguity_code_1 _RDC.Assembly_atom_ID_2 _RDC.Entity_assembly_ID_2 _RDC.Entity_ID_2 _RDC.Comp_index_ID_2 _RDC.Seq_ID_2 _RDC.Comp_ID_2 _RDC.Atom_ID_2 _RDC.Atom_type_2 _RDC.Atom_isotope_number_2 _RDC.Ambiguity_code_2 _RDC.Val _RDC.Val_min _RDC.Val_max _RDC.Val_err _RDC.Val_bond_length _RDC.Resonance_ID_1 _RDC.Resonance_ID_2 _RDC.Auth_entity_assembly_ID_1 _RDC.Auth_seq_ID_1 _RDC.Auth_comp_ID_1 _RDC.Auth_atom_ID_1 _RDC.Auth_entity_assembly_ID_2 _RDC.Auth_seq_ID_2 _RDC.Auth_comp_ID_2 _RDC.Auth_atom_ID_2 _RDC.Entry_ID _RDC.RDC_list_ID 1 1DHN . 1 1 7 7 ALA H . . . . 1 1 7 7 ALA N . . . 2.7 . . . . . . . . . . . . . . 5815 1 2 1DHN . 1 1 8 8 LYS H . . . . 1 1 8 8 LYS N . . . 7.1 . . . . . . . . . . . . . . 5815 1 3 1DHN . 1 1 9 9 ALA H . . . . 1 1 9 9 ALA N . . . 10.1 . . . . . . . . . . . . . . 5815 1 4 1DHN . 1 1 10 10 ALA H . . . . 1 1 10 10 ALA N . . . 5.6 . . . . . . . . . . . . . . 5815 1 5 1DHN . 1 1 11 11 PHE H . . . . 1 1 11 11 PHE N . . . 4 . . . . . . . . . . . . . . 5815 1 6 1DHN . 1 1 12 12 ASP H . . . . 1 1 12 12 ASP N . . . 8.6 . . . . . . . . . . . . . . 5815 1 7 1DHN . 1 1 13 13 SER H . . . . 1 1 13 13 SER N . . . 9.1 . . . . . . . . . . . . . . 5815 1 8 1DHN . 1 1 14 14 LEU H . . . . 1 1 14 14 LEU N . . . 5.1 . . . . . . . . . . . . . . 5815 1 9 1DHN . 1 1 15 15 GLN H . . . . 1 1 15 15 GLN N . . . 6.3 . . . . . . . . . . . . . . 5815 1 10 1DHN . 1 1 16 16 ALA H . . . . 1 1 16 16 ALA N . . . 9.7 . . . . . . . . . . . . . . 5815 1 11 1DHN . 1 1 17 17 SER H . . . . 1 1 17 17 SER N . . . 8.3 . . . . . . . . . . . . . . 5815 1 12 1DHN . 1 1 18 18 ALA H . . . . 1 1 18 18 ALA N . . . 5.3 . . . . . . . . . . . . . . 5815 1 13 1DHN . 1 1 19 19 THR H . . . . 1 1 19 19 THR N . . . 7.5 . . . . . . . . . . . . . . 5815 1 14 1DHN . 1 1 20 20 GLU H . . . . 1 1 20 20 GLU N . . . 9.9 . . . . . . . . . . . . . . 5815 1 15 1DHN . 1 1 21 21 MET H . . . . 1 1 21 21 MET N . . . 7.6 . . . . . . . . . . . . . . 5815 1 16 1DHN . 1 1 22 22 ILE H . . . . 1 1 22 22 ILE N . . . 4.3 . . . . . . . . . . . . . . 5815 1 17 1DHN . 1 1 23 23 GLY H . . . . 1 1 23 23 GLY N . . . 7.1 . . . . . . . . . . . . . . 5815 1 18 1DHN . 1 1 24 24 TYR H . . . . 1 1 24 24 TYR N . . . 9.3 . . . . . . . . . . . . . . 5815 1 19 1DHN . 1 1 25 25 ALA H . . . . 1 1 25 25 ALA N . . . 6 . . . . . . . . . . . . . . 5815 1 20 1DHN . 1 1 26 26 TRP H . . . . 1 1 26 26 TRP N . . . 5.4 . . . . . . . . . . . . . . 5815 1 21 1DHN . 1 1 27 27 ALA H . . . . 1 1 27 27 ALA N . . . 9.5 . . . . . . . . . . . . . . 5815 1 22 1DHN . 1 1 28 28 MET H . . . . 1 1 28 28 MET N . . . 7.9 . . . . . . . . . . . . . . 5815 1 23 1DHN . 1 1 29 29 VAL H . . . . 1 1 29 29 VAL N . . . 5.4 . . . . . . . . . . . . . . 5815 1 24 1DHN . 1 1 30 30 VAL H . . . . 1 1 30 30 VAL N . . . 6 . . . . . . . . . . . . . . 5815 1 25 1DHN . 1 1 31 31 VAL H . . . . 1 1 31 31 VAL N . . . 9.9 . . . . . . . . . . . . . . 5815 1 26 1DHN . 1 1 32 32 ILE H . . . . 1 1 32 32 ILE N . . . 7.7 . . . . . . . . . . . . . . 5815 1 27 1DHN . 1 1 33 33 VAL H . . . . 1 1 33 33 VAL N . . . 4.9 . . . . . . . . . . . . . . 5815 1 28 1DHN . 1 1 34 34 GLY H . . . . 1 1 34 34 GLY N . . . 8.4 . . . . . . . . . . . . . . 5815 1 29 1DHN . 1 1 35 35 ALA H . . . . 1 1 35 35 ALA N . . . 9.6 . . . . . . . . . . . . . . 5815 1 30 1DHN . 1 1 36 36 THR H . . . . 1 1 36 36 THR N . . . 7.5 . . . . . . . . . . . . . . 5815 1 31 1DHN . 1 1 37 37 ILE H . . . . 1 1 37 37 ILE N . . . 5.6 . . . . . . . . . . . . . . 5815 1 32 1DHN . 1 1 38 38 GLY H . . . . 1 1 38 38 GLY N . . . 8.5 . . . . . . . . . . . . . . 5815 1 33 1DHN . 1 1 39 39 ILE H . . . . 1 1 39 39 ILE N . . . 10.3 . . . . . . . . . . . . . . 5815 1 34 1DHN . 1 1 40 40 LYS H . . . . 1 1 40 40 LYS N . . . 8.5 . . . . . . . . . . . . . . 5815 1 35 1DHN . 1 1 41 41 LEU H . . . . 1 1 41 41 LEU N . . . 6.9 . . . . . . . . . . . . . . 5815 1 36 1DHN . 1 1 42 42 PHE H . . . . 1 1 42 42 PHE N . . . 9.5 . . . . . . . . . . . . . . 5815 1 37 1DHN . 1 1 43 43 LYS H . . . . 1 1 43 43 LYS N . . . 10 . . . . . . . . . . . . . . 5815 1 38 1DHN . 1 1 44 44 LYS H . . . . 1 1 44 44 LYS N . . . 8 . . . . . . . . . . . . . . 5815 1 39 1DHN . 1 1 45 45 PHE H . . . . 1 1 45 45 PHE N . . . 8 . . . . . . . . . . . . . . 5815 1 40 1DHN . 1 1 46 46 THR H . . . . 1 1 46 46 THR N . . . 9.6 . . . . . . . . . . . . . . 5815 1 41 1DHN . 1 1 47 47 SER H . . . . 1 1 47 47 SER N . . . 9.6 . . . . . . . . . . . . . . 5815 1 42 1DHN . 1 1 48 48 LYS H . . . . 1 1 48 48 LYS N . . . 7.9 . . . . . . . . . . . . . . 5815 1 43 1DHN . 1 1 49 49 ALA H . . . . 1 1 49 49 ALA N . . . 7.7 . . . . . . . . . . . . . . 5815 1 stop_ save_