data_4209 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4209 _Entry.Title ; Solution NMR structures of the major coat protein of filamentous bacteriophage M13 solubilized in Dodecyl Phosphocholine micelles, 25 lowest energy structures ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 1998-04-17 _Entry.Accession_date 1998-04-17 _Entry.Last_release_date 2000-02-03 _Entry.Original_release_date 2000-02-03 _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 C. Papavoine . H.M. . 4209 2 B. Christiaans . E.C. . 4209 3 R. Folmer . H.A. . 4209 4 R. Konings . N.H. . 4209 5 C. Hilbers . W. . 4209 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4209 coupling_constants 1 4209 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 157 4209 '15N chemical shifts' 50 4209 '1H chemical shifts' 317 4209 'coupling constants' 29 4209 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 . . 2000-02-03 1998-04-17 original author . 4209 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4209 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 98407983 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Solution structure of the M13 major coat protein in detergent micelles: A basis for a model of phage assembly involving specific residues ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of Molecular Biology' _Citation.Journal_volume 282 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 401 _Citation.Page_last 419 _Citation.Year 1998 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 C. Papavoine . H.M. . 4209 1 2 B. Christiaans . E.C. . 4209 1 3 R. Folmer . H.A. . 4209 1 4 R. Konings . N.H. . 4209 1 5 C. Hilbers . W. . 4209 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID assembly 4209 1 'bacteriophage M13' 4209 1 'major coat protein' 4209 1 membrane 4209 1 micelle 4209 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4209 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 7947703 _Citation.Full_citation ; Biochemistry 1994 Nov 8;33(44):12990-7 Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR. Papavoine CH, Konings RN, Hilbers CW, van de Ven FJ ; _Citation.Title 'Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 33 _Citation.Journal_issue 44 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-2960 _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 12990 _Citation.Page_last 12997 _Citation.Year 1994 _Citation.Details ; The major coat protein (gVIIIp) of bacteriophage M13 solubilized in sodium dodecyl sulfate (SDS) detergent micelles was used as a model system to study this protein in the lipid-bound form. In order to probe the position of gVIIIp relative to the SDS micelles, stearate was added, spin-labeled at the 5- or 16-position with a doxyl group containing a stable nitroxide radical. The average position of the spin-labels in the micelles was derived from the line broadening of the resonances in the 13C spectrum of SDS. Subsequently, we derived a model of the relative position of gVIIIp in the SDS micelle from the effect of the spin-labels on the gVIIIp resonances, monitored via 1H-15N HSQC and TOCSY experiments. The results are consistent with the structure of gVIIIp having two helical strands. One strand is a long hydrophobic helix that spans the micelle, and the other is a shorter amphipathic helix on the surface of the micelle. These results are in good agreement with the structure of gVIIIp in membranes proposed by McDonnell et al. on the basis of solid state NMR data [McDonnell, P. A., Shon, K., Kim, Y., & Opella, S. J. (1993) J. Mol. Biol. 233, 447-463]. This study indicates that high-resolution NMR on this membrane protein, solubilized in detergent micelles, is a very suitable technique for mimicking these proteins in their natural environment. Furthermore, the data indicate that the structure of the micelle near the C-terminus of the major coat protein is distorted.(ABSTRACT TRUNCATED AT 250 WORDS) ; 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 'C H' Papavoine C. H. . 4209 2 2 'R N' Konings R. N. . 4209 2 3 'C W' Hilbers C. W. . 4209 2 4 'F J' 'van de Ven' F. J. . 4209 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 4209 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 7556198 _Citation.Full_citation ; Eur J Biochem 1995 Sep 1;232(2):490-500 NMR studies of the major coat protein of bacteriophage M13. Structural information of gVIIIp in dodecylphosphocholine micelles. Papavoine CH, Aelen JM, Konings RN, Hilbers CW, Van de Ven FJ ; _Citation.Title 'NMR studies of the major coat protein of bacteriophage M13. Structural information of gVIIIp in dodecylphosphocholine micelles.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Eur. J. Biochem.' _Citation.Journal_name_full 'European journal of biochemistry / FEBS' _Citation.Journal_volume 232 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0014-2956 _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 490 _Citation.Page_last 500 _Citation.Year 1995 _Citation.Details ; The membrane-bound form of the major coat protein (gVIIIp) of bacteriophage M13 has been studied using nuclear magnetic resonance spectroscopy. As membrane mimetics, we used dodecylphosphocholine (DodPCho) detergent micelles to solubilize the protein. We were able to nearly completely assign all resonances of the protein solubilized in DodPCho micelles by using both homonuclear and heteronuclear multidimensional experiments. Based on the patterns of the nuclear Overhauser enhancements and the chemical shifts of the resonances, we deduced the secondary structure of the protein. Additional structural information was obtained from amide proton exchange data and J-coupling constants. The protein consists of two alpha-helices which are connected by a hinge region around residue 21. From spin-label experiments, the location of the protein relative to the DodPCho micelles was determined. One, hydrophobic, helix spans the micelle, and another, amphipathic, helix, is located beneath the surface of the micelle. Comparison of the data of gVIIIp in DodPCho micelles with those of gVIIIp in sodium dodecyl sulfate (SDS) micelles [Van de Ven, F. J. M., van Os, J. W. M., Aelen, J. M. A., Wymenga, S. S., Remerowski, M. L., Konings, R. N. H. & Hilbers, C. W. (1993) Biochemistry 32, 8322-8328; Papavoine, C. H. M., Konings, R. N. H., Hilbers, C. W. & Van de Ven, F. J. M. (1994) Biochemistry 33, 12,990-12,997] reveals that the structures of the protein in the two detergent micelles are very similar. They differ only in the arrangement of the detergent molecules around the protein. For gVIIIp in SDS micelles, we found a micellar structure which is distorted near the C-terminus of the protein; whereas for DodPCho micelles, both distorted and regular elliptical micelles occur. This distortion is probably due to the interaction of the positively charged lysine side chains with the negatively charged head group of the detergent molecules. ; 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 'C H' Papavoine C. H. . 4209 3 2 'J M' Aelen J. M. . 4209 3 3 'R N' Konings R. N. . 4209 3 4 'C W' Hilbers C. W. . 4209 3 5 'F J' 'Van de Ven' F. J. . 4209 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 4209 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9092832 _Citation.Full_citation ; Biochemistry 1997 Apr 1;36(13):4015-26 Backbone dynamics of the major coat protein of bacteriophage M13 in detergent micelles by 15N nuclear magnetic resonance relaxation measurements using the model-free approach and reduced spectral density mapping. Papavoine CH, Remerowski ML, Horstink LM, Konings RN, Hilbers CW, van de Ven FJ ; _Citation.Title 'Backbone dynamics of the major coat protein of bacteriophage M13 in detergent micelles by 15N nuclear magnetic resonance relaxation measurements using the model-free approach and reduced spectral density mapping.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 36 _Citation.Journal_issue 13 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-2960 _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 4015 _Citation.Page_last 4026 _Citation.Year 1997 _Citation.Details ; The backbone dynamics of the major coat protein (gVIIIp) of the filamentous bacteriophage M13, solubilized in detergent micelles, have been studied using 15N nuclear magnetic resonance spectroscopy at three frequencies. Motional parameters and overall and internal correlation times were derived with the model-free approach. It was also checked whether these parameters had to be modified due to anisotropic motion of the protein/micelle complex. Reduced spectral density mapping was used to calculate the spectral densities at J(O), J(omegaN), and [J(omegaH)]. The spectral densities were interpreted by mapping a linear or scaled linear combination of two Lorentzians onto a J(O)-J(omega) plot. The major coat protein of bacteriophage M13 consists of two alpha-helices, one of which is hydrophobic and located within the micelle, while the other is amphipathic and located on the surface of the micelle. Our results indicate that the motion of the hydrophobic helix is restricted such that it corresponds to the overall tumbling of the protein/micelle complex. The interpretation of the relaxation data of the amphipathic helix by means of the model-free approach and the reduced spectral density mapping indicate that in addition to the overall motion all residues in this helix are subject to motion on the fast nanosecond and picosecond time scales. The motions of the vectors in the low nanosecond range are characterized by similar values of the spectral densities and correlation times and represent the motion of the amphipathic helix on and away from the surface of the micelle. The relaxation data of the residues in the hinge region connecting the helices show that there is an abrupt change from highly restricted to less restricted motion. Both the C-terminal and N-terminal residues are very mobile. ; 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 'C H' Papavoine C. H. . 4209 4 2 'M L' Remerowski M. L. . 4209 4 3 'L M' Horstink L. M. . 4209 4 4 'R N' Konings R. N. . 4209 4 5 'C W' Hilbers C. W. . 4209 4 6 'F J' 'van de Ven' F. J. . 4209 4 stop_ save_ save_ref_4 _Citation.Sf_category citations _Citation.Sf_framecode ref_4 _Citation.Entry_ID 4209 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8347628 _Citation.Full_citation ; Biochemistry 1993 Aug 17;32(32):8322-8 Assignment of 1H, 15N, and backbone 13C resonances in detergent-solubilized M13 coat protein via multinuclear multidimensional NMR: a model for the coat protein monomer. van de Ven FJ, van Os JW, Aelen JM, Wymenga SS, Remerowski ML, Konings RN, Hilbers CW ; _Citation.Title 'Assignment of 1H, 15N, and backbone 13C resonances in detergent-solubilized M13 coat protein via multinuclear multidimensional NMR: a model for the coat protein monomer.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 32 _Citation.Journal_issue 32 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-2960 _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 8322 _Citation.Page_last 8328 _Citation.Year 1993 _Citation.Details ; The major coat protein (gVIIIp) of bacteriophage M13 complexed with SDS detergent micelles was used as a model system to study the lipid-bound conformation of the protein. Conditions were found that allowed the recording of good quality of NMR spectra. By making extensive use of three-dimensional heteronuclear (13C, 15N) NMR, we obtained a complete set of resonance assignments for 1HN, 1H alpha, 1H beta, 13C alpha, CO, and 15N and partially assigned the rest of the 1H spectrum. Analysis of NOE and chemical shift data reveals that gVIIIp is composed of two alpha-helical domains, one ranging from Pro-6 to Glu20 and the other ranging from Tyr-24 all the way to the C-terminus Ser-50. In contrast to the results reported by Henry and Sykes [Henry, G.D., & Sykes, B.D. (1992) Biochemistry 31, 5285-5297], at a high SDS to protein ratio the protein appears to be monomeric. ; 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 'F J' 'van de Ven' F. J. . 4209 5 2 'J W' 'van Os' J. W. . 4209 5 3 'J M' Aelen J. M. . 4209 5 4 'S S' Wymenga S. S. . 4209 5 5 'M L' Remerowski M. L. . 4209 5 6 'R N' Konings R. N. . 4209 5 7 'C W' Hilbers C. W. . 4209 5 stop_ save_ save_ref_5 _Citation.Sf_category citations _Citation.Sf_framecode ref_5 _Citation.Entry_ID 4209 _Citation.ID 6 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8411155 _Citation.Full_citation ; J Mol Biol 1993 Oct 5;233(3):447-63 fd coat protein structure in membrane environments. McDonnell PA, Shon K, Kim Y, Opella SJ ; _Citation.Title 'fd coat protein structure in membrane environments.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 233 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0022-2836 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 447 _Citation.Page_last 463 _Citation.Year 1993 _Citation.Details ; The membrane bound form of bacteriophage fd coat protein has a long hydrophobic membrane spanning helix and a shorter amphipathic helix in the plane of the bilayer. Residues near the N and C termini and in the turn connecting the two helices are mobile. The locations and orientations of the helical secondary structure elements and the protein backbone dynamics were characterized by combining results from multidimensional solution NMR experiments on protein samples in micelles and high resolution solid-state NMR experiments on protein samples in oriented and unoriented lipid bilayers. The coat protein is a monomer in micelles. The secondary structure of the membrane bound form of fd coat protein is very similar to that of the structural form found in the virus particles, since it is nearly all alpha helix. However, the membrane bound form of the protein differs from the structural form of the protein in virus particles in the arrangement of the secondary structure, since the membrane bound form of the protein has two distinct helical domains oriented perpendicular to each other and the structural form of the protein in the virus particles has a nearly continuous helix aligned approximately along the filament axis. In addition, there are substantial differences in the dynamics of residues in the bend between the two helices and near the C terminus, since they are mobile in the membrane bound form of the protein and not in the virus particles. Residues 1 to 5 at the N terminus are highly mobile and unstructured in both the membrane bound and structural forms of the coat protein. ; 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 'P A' McDonnell P. A. . 4209 6 2 K Shon K. . . 4209 6 3 Y Kim Y. . . 4209 6 4 'S J' Opella S. J. . 4209 6 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_gVIIIp_g8p_gene_VIII_protein _Assembly.Sf_category assembly _Assembly.Sf_framecode gVIIIp_g8p_gene_VIII_protein _Assembly.Entry_ID 4209 _Assembly.ID 1 _Assembly.Name 'M13 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 monomer 4209 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 gVIIIp 1 $gVIIIp . . . native . . . . . 4209 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'gVIIIp, g8p, gene VIII protein' abbreviation 4209 1 'M13 major coat protein' system 4209 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_gVIIIp _Entity.Sf_category entity _Entity.Sf_framecode gVIIIp _Entity.Entry_ID 4209 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'M13 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 ; AEGDDPAKAAFNSLQASATE YIGYAWAMVVVIVGATIGIK 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 . _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 . _Entity.DB_query_revised_last_date 2015-11-24 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 17728 . fd . . . . . 100.00 50 98.00 100.00 8.09e-25 . . . . 4209 1 2 no BMRB 19734 . fd_bacteriophage . . . . . 100.00 50 98.00 100.00 8.09e-25 . . . . 4209 1 3 no BMRB 19747 . M13_bacteriophage . . . . . 100.00 50 100.00 100.00 1.38e-25 . . . . 4209 1 4 no BMRB 2590 . "viral coat protein" . . . . . 100.00 50 100.00 100.00 1.38e-25 . . . . 4209 1 5 no BMRB 2591 . "viral coat protein" . . . . . 100.00 50 98.00 98.00 4.91e-25 . . . . 4209 1 6 no BMRB 2592 . "viral coat protein" . . . . . 100.00 50 98.00 100.00 2.28e-25 . . . . 4209 1 7 no BMRB 4197 . "M13 major coat protein" . . . . . 100.00 50 100.00 100.00 1.38e-25 . . . . 4209 1 8 no PDB 1FDM . "Fd Major Coat Protein In Sds Micelles, Nmr, 20 Structures" . . . . . 100.00 50 98.00 100.00 8.09e-25 . . . . 4209 1 9 no PDB 1IFD . "Model-Building Studies Of Inovirus: Genetic Variations On A Geometric Theme" . . . . . 100.00 50 98.00 100.00 8.09e-25 . . . . 4209 1 10 no PDB 1IFI . "Molecular Models And Structural Comparisons Of Native And Mutant Class I Filamentous Bacteriophages Ff (Fd, F1, M13), If1 And I" . . . . . 100.00 50 98.00 100.00 8.09e-25 . . . . 4209 1 11 no PDB 1IFJ . "Molecular Models And Structural Comparisons Of Native And Mutant Class I Filamentous Bacteriophages Ff (Fd, F1, M13), If1 And I" . . . . . 100.00 50 98.00 100.00 8.09e-25 . . . . 4209 1 12 no PDB 1MZT . "Nmr Structure Of The Fd Bacteriophage Pviii Coat Protein In Lipid Bilayer Membranes" . . . . . 100.00 50 98.00 100.00 8.09e-25 . . . . 4209 1 13 no PDB 2CPB . "Solution Nmr Structures Of The Major Coat Protein Of Filamentous Bacteriophage M13 Solubilized In Dodecylphosphocholine Micelle" . . . . . 100.00 50 100.00 100.00 1.38e-25 . . . . 4209 1 14 no PDB 2CPS . "Solution Nmr Structures Of The Major Coat Protein Of Filamentous Bacteriophage M13 Solubilized In Sodium Dodecyl Sulphate Micel" . . . . . 100.00 50 100.00 100.00 1.38e-25 . . . . 4209 1 15 no PDB 2HI5 . "Model For Bacteriophage Fd From Cryo-Em" . . . . . 100.00 50 98.00 100.00 8.09e-25 . . . . 4209 1 16 no PDB 2MJZ . "Capsid Model Of M13 Bacteriophage Virus From Magic-angle Spinning Nmr And Rosetta Modeling" . . . . . 100.00 50 100.00 100.00 1.38e-25 . . . . 4209 1 17 no EMBL CAA23861 . "structural protein [Enterobacteria phage M13]" . . . . . 100.00 73 100.00 100.00 6.72e-26 . . . . 4209 1 18 no EMBL CAA23871 . "unnamed protein product [Enterobacteria phage f1]" . . . . . 100.00 73 98.00 100.00 4.01e-25 . . . . 4209 1 19 no GB AAA32207 . "gene VIII protein, partial [Enterobacteria phage f1]" . . . . . 84.00 65 97.62 100.00 1.42e-19 . . . . 4209 1 20 no GB AAA32214 . "protein VIII [Enterobacteria phage f1]" . . . . . 100.00 73 98.00 100.00 4.01e-25 . . . . 4209 1 21 no GB AAA32220 . "major coat protein B [Enterobacteria phage f1]" . . . . . 100.00 73 98.00 100.00 4.01e-25 . . . . 4209 1 22 no GB AAA32308 . "VIII [Enterobacteria phage fd]" . . . . . 100.00 73 98.00 100.00 4.01e-25 . . . . 4209 1 23 no GB AAB24445 . "gene-8 protein, g8p=major coat protein [bacteriophage fd, Peptide, 50 aa]" . . . . . 100.00 50 98.00 100.00 8.09e-25 . . . . 4209 1 24 no PRF 0812197K . DNA,phage . . . . . 100.00 73 98.00 100.00 4.01e-25 . . . . 4209 1 25 no REF NP_510890 . "structural protein [Enterobacteria phage M13]" . . . . . 100.00 73 100.00 100.00 6.72e-26 . . . . 4209 1 26 no REF YP_009111292 . "protein VIII [Enterobacteria phage f1]" . . . . . 100.00 73 98.00 100.00 4.01e-25 . . . . 4209 1 27 no REF YP_009111302 . "VIII [Enterobacteria phage fd]" . . . . . 100.00 73 98.00 100.00 4.01e-25 . . . . 4209 1 28 no SP P69539 . "RecName: Full=Capsid protein G8P; AltName: Full=Coat protein B; AltName: Full=Gene 8 protein; Short=G8P; AltName: Full=Major co" . . . . . 100.00 73 98.00 100.00 4.01e-25 . . . . 4209 1 29 no SP P69540 . "RecName: Full=Capsid protein G8P; AltName: Full=Coat protein B; AltName: Full=Gene 8 protein; Short=G8P; AltName: Full=Major co" . . . . . 100.00 73 98.00 100.00 4.01e-25 . . . . 4209 1 30 no SP P69541 . "RecName: Full=Capsid protein G8P; AltName: Full=Coat protein B; AltName: Full=Gene 8 protein; Short=G8P; AltName: Full=M13 proc" . . . . . 100.00 73 100.00 100.00 6.72e-26 . . . . 4209 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'gVIIIp, g8p' abbreviation 4209 1 'M13 major coat protein' common 4209 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 . 4209 1 2 . GLU . 4209 1 3 . GLY . 4209 1 4 . ASP . 4209 1 5 . ASP . 4209 1 6 . PRO . 4209 1 7 . ALA . 4209 1 8 . LYS . 4209 1 9 . ALA . 4209 1 10 . ALA . 4209 1 11 . PHE . 4209 1 12 . ASN . 4209 1 13 . SER . 4209 1 14 . LEU . 4209 1 15 . GLN . 4209 1 16 . ALA . 4209 1 17 . SER . 4209 1 18 . ALA . 4209 1 19 . THR . 4209 1 20 . GLU . 4209 1 21 . TYR . 4209 1 22 . ILE . 4209 1 23 . GLY . 4209 1 24 . TYR . 4209 1 25 . ALA . 4209 1 26 . TRP . 4209 1 27 . ALA . 4209 1 28 . MET . 4209 1 29 . VAL . 4209 1 30 . VAL . 4209 1 31 . VAL . 4209 1 32 . ILE . 4209 1 33 . VAL . 4209 1 34 . GLY . 4209 1 35 . ALA . 4209 1 36 . THR . 4209 1 37 . ILE . 4209 1 38 . GLY . 4209 1 39 . ILE . 4209 1 40 . LYS . 4209 1 41 . LEU . 4209 1 42 . PHE . 4209 1 43 . LYS . 4209 1 44 . LYS . 4209 1 45 . PHE . 4209 1 46 . THR . 4209 1 47 . SER . 4209 1 48 . LYS . 4209 1 49 . ALA . 4209 1 50 . SER . 4209 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 4209 1 . GLU 2 2 4209 1 . GLY 3 3 4209 1 . ASP 4 4 4209 1 . ASP 5 5 4209 1 . PRO 6 6 4209 1 . ALA 7 7 4209 1 . LYS 8 8 4209 1 . ALA 9 9 4209 1 . ALA 10 10 4209 1 . PHE 11 11 4209 1 . ASN 12 12 4209 1 . SER 13 13 4209 1 . LEU 14 14 4209 1 . GLN 15 15 4209 1 . ALA 16 16 4209 1 . SER 17 17 4209 1 . ALA 18 18 4209 1 . THR 19 19 4209 1 . GLU 20 20 4209 1 . TYR 21 21 4209 1 . ILE 22 22 4209 1 . GLY 23 23 4209 1 . TYR 24 24 4209 1 . ALA 25 25 4209 1 . TRP 26 26 4209 1 . ALA 27 27 4209 1 . MET 28 28 4209 1 . VAL 29 29 4209 1 . VAL 30 30 4209 1 . VAL 31 31 4209 1 . ILE 32 32 4209 1 . VAL 33 33 4209 1 . GLY 34 34 4209 1 . ALA 35 35 4209 1 . THR 36 36 4209 1 . ILE 37 37 4209 1 . GLY 38 38 4209 1 . ILE 39 39 4209 1 . LYS 40 40 4209 1 . LEU 41 41 4209 1 . PHE 42 42 4209 1 . LYS 43 43 4209 1 . LYS 44 44 4209 1 . PHE 45 45 4209 1 . THR 46 46 4209 1 . SER 47 47 4209 1 . LYS 48 48 4209 1 . ALA 49 49 4209 1 . SER 50 50 4209 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 4209 _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 $gVIIIp . 10870 . . 'Inoviridae Coliphage M13' 'bacteriophage M13' . . viruses . Inoviridae 'Coliphage M13' . . . . . . . . . . . . . . . . . . . . . 4209 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 4209 _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 $gVIIIp . 'purified from the natural source' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4209 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4209 _Sample.ID 1 _Sample.Type micelles _Sample.Sub_type . _Sample.Details . _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 'M13 major coat protein' '[U-100% 13C; U-100% 15N]' . . 1 $gVIIIp . . . 1.5 2 mM . . . . 4209 1 2 'dodecyl phosphocholine' . . . . . . . . . . . . . . . 4209 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 4209 _Sample_condition_list.ID 1 _Sample_condition_list.Details ; The sample was in dry form added to dry dodecyl phosphocholine. To this H2O or D2O was added. This sample was then vortexed and pH adjusted. The end volume was 500 uL. ; 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 4.9 0.2 n/a 4209 1 temperature 311 1 K 4209 1 stop_ save_ ############################ # Computer software used # ############################ save_MNMR _Software.Sf_category software _Software.Sf_framecode MNMR _Software.Entry_ID 4209 _Software.ID 1 _Software.Name MNMR _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'FT of the recorded spectra' 4209 1 stop_ save_ save_XEASY _Software.Sf_category software _Software.Sf_framecode XEASY _Software.Entry_ID 4209 _Software.ID 2 _Software.Name XEASY _Software.Version 3.9.1 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID ; Analysis of the spectra to obtain assignments and structural information ; 4209 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 4209 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AM _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 400 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 4209 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AM _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_3 _NMR_spectrometer.Entry_ID 4209 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model Unity+ _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_4 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_4 _NMR_spectrometer.Entry_ID 4209 _NMR_spectrometer.ID 4 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4209 _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_1 Bruker AM . 400 . . . 4209 1 2 NMR_spectrometer_2 Bruker AM . 500 . . . 4209 1 3 NMR_spectrometer_3 Varian Unity+ . 500 . . . 4209 1 4 NMR_spectrometer_4 Bruker AMX . 600 . . . 4209 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 4209 _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 DQF-COSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4209 1 2 TOCSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4209 1 3 NOESY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4209 1 4 'NOESY-HMQC (15N and 13C)' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4209 1 5 'TOCSY-HMQC (15N)' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4209 1 6 HCCH-TOCSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4209 1 7 ROESY-GHSQC . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4209 1 8 HMQC-NOESY-GHSQC . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4209 1 9 HMQC-J . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4209 1 10 HNHA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4209 1 11 HACACB-COSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4209 1 12 HNHB . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4209 1 13 'HSQC(3J CGN)' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4209 1 14 HSQC(3JCGC') . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4209 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 4209 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name DQF-COSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 4209 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name TOCSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 4209 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name NOESY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 4209 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name 'NOESY-HMQC (15N and 13C)' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 4209 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name 'TOCSY-HMQC (15N)' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 4209 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name HCCH-TOCSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 4209 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name ROESY-GHSQC _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_8 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_8 _NMR_spec_expt.Entry_ID 4209 _NMR_spec_expt.ID 8 _NMR_spec_expt.Name HMQC-NOESY-GHSQC _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_9 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_9 _NMR_spec_expt.Entry_ID 4209 _NMR_spec_expt.ID 9 _NMR_spec_expt.Name HMQC-J _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_10 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_10 _NMR_spec_expt.Entry_ID 4209 _NMR_spec_expt.ID 10 _NMR_spec_expt.Name HNHA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_11 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_11 _NMR_spec_expt.Entry_ID 4209 _NMR_spec_expt.ID 11 _NMR_spec_expt.Name HACACB-COSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_12 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_12 _NMR_spec_expt.Entry_ID 4209 _NMR_spec_expt.ID 12 _NMR_spec_expt.Name HNHB _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_13 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_13 _NMR_spec_expt.Entry_ID 4209 _NMR_spec_expt.ID 13 _NMR_spec_expt.Name 'HSQC(3J CGN)' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_14 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_14 _NMR_spec_expt.Entry_ID 4209 _NMR_spec_expt.ID 14 _NMR_spec_expt.Name HSQC(3JCGC') _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 4209 _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 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 4209 1 H 1 TSP 'methyl protons' . . . . ppm 0.0 external direct . external spherical parallel . . . . . . 4209 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 4209 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_chem_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chem_shift_set_1 _Assigned_chem_shift_list.Entry_ID 4209 _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 $sample_1 . 4209 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 1 1 ALA CA C 13 51.5 . . 1 . . . . . . . . 4209 1 2 . 1 1 1 1 ALA HA H 1 4.04 . . 1 . . . . . . . . 4209 1 3 . 1 1 1 1 ALA CB C 13 19.1 . . 1 . . . . . . . . 4209 1 4 . 1 1 1 1 ALA HB1 H 1 1.47 . . 1 . . . . . . . . 4209 1 5 . 1 1 1 1 ALA HB2 H 1 1.47 . . 1 . . . . . . . . 4209 1 6 . 1 1 1 1 ALA HB3 H 1 1.47 . . 1 . . . . . . . . 4209 1 7 . 1 1 2 2 GLU H H 1 8.68 . . 1 . . . . . . . . 4209 1 8 . 1 1 2 2 GLU CA C 13 57.1 . . 1 . . . . . . . . 4209 1 9 . 1 1 2 2 GLU HA H 1 4.19 . . 1 . . . . . . . . 4209 1 10 . 1 1 2 2 GLU CB C 13 29.3 . . 1 . . . . . . . . 4209 1 11 . 1 1 2 2 GLU HB2 H 1 1.90 . . 1 . . . . . . . . 4209 1 12 . 1 1 2 2 GLU HB3 H 1 1.98 . . 1 . . . . . . . . 4209 1 13 . 1 1 2 2 GLU HG2 H 1 2.24 . . 2 . . . . . . . . 4209 1 14 . 1 1 2 2 GLU CG C 13 35.3 . . 1 . . . . . . . . 4209 1 15 . 1 1 3 3 GLY N N 15 112.6 . . 1 . . . . . . . . 4209 1 16 . 1 1 3 3 GLY H H 1 8.47 . . 1 . . . . . . . . 4209 1 17 . 1 1 3 3 GLY CA C 13 44.6 . . 1 . . . . . . . . 4209 1 18 . 1 1 3 3 GLY HA2 H 1 3.81 . . 1 . . . . . . . . 4209 1 19 . 1 1 3 3 GLY HA3 H 1 3.94 . . 1 . . . . . . . . 4209 1 20 . 1 1 4 4 ASP N N 15 122.0 . . 1 . . . . . . . . 4209 1 21 . 1 1 4 4 ASP H H 1 7.92 . . 1 . . . . . . . . 4209 1 22 . 1 1 4 4 ASP CA C 13 54.1 . . 1 . . . . . . . . 4209 1 23 . 1 1 4 4 ASP HA H 1 4.52 . . 1 . . . . . . . . 4209 1 24 . 1 1 4 4 ASP CB C 13 40.8 . . 1 . . . . . . . . 4209 1 25 . 1 1 4 4 ASP HB2 H 1 2.57 . . 1 . . . . . . . . 4209 1 26 . 1 1 4 4 ASP HB3 H 1 2.57 . . 1 . . . . . . . . 4209 1 27 . 1 1 5 5 ASP N N 15 123.0 . . 1 . . . . . . . . 4209 1 28 . 1 1 5 5 ASP H H 1 8.18 . . 1 . . . . . . . . 4209 1 29 . 1 1 5 5 ASP CA C 13 52.0 . . 1 . . . . . . . . 4209 1 30 . 1 1 5 5 ASP HA H 1 4.81 . . 1 . . . . . . . . 4209 1 31 . 1 1 5 5 ASP CB C 13 40.8 . . 1 . . . . . . . . 4209 1 32 . 1 1 5 5 ASP HB2 H 1 2.60 . . 1 . . . . . . . . 4209 1 33 . 1 1 5 5 ASP HB3 H 1 2.74 . . 1 . . . . . . . . 4209 1 34 . 1 1 6 6 PRO CA C 13 64.5 . . 1 . . . . . . . . 4209 1 35 . 1 1 6 6 PRO HA H 1 4.30 . . 1 . . . . . . . . 4209 1 36 . 1 1 6 6 PRO CB C 13 31.7 . . 1 . . . . . . . . 4209 1 37 . 1 1 6 6 PRO HB2 H 1 1.86 . . 1 . . . . . . . . 4209 1 38 . 1 1 6 6 PRO HB3 H 1 2.29 . . 1 . . . . . . . . 4209 1 39 . 1 1 6 6 PRO HG2 H 1 1.99 . . 1 . . . . . . . . 4209 1 40 . 1 1 6 6 PRO HD2 H 1 3.81 . . 1 . . . . . . . . 4209 1 41 . 1 1 6 6 PRO HD3 H 1 3.81 . . 1 . . . . . . . . 4209 1 42 . 1 1 6 6 PRO CG C 13 27.1 . . 1 . . . . . . . . 4209 1 43 . 1 1 6 6 PRO CD C 13 50.7 . . 1 . . . . . . . . 4209 1 44 . 1 1 7 7 ALA N N 15 123.1 . . 1 . . . . . . . . 4209 1 45 . 1 1 7 7 ALA H H 1 8.26 . . 1 . . . . . . . . 4209 1 46 . 1 1 7 7 ALA CA C 13 54.2 . . 1 . . . . . . . . 4209 1 47 . 1 1 7 7 ALA HA H 1 4.10 . . 1 . . . . . . . . 4209 1 48 . 1 1 7 7 ALA CB C 13 18.4 . . 1 . . . . . . . . 4209 1 49 . 1 1 7 7 ALA HB1 H 1 1.36 . . 1 . . . . . . . . 4209 1 50 . 1 1 7 7 ALA HB2 H 1 1.36 . . 1 . . . . . . . . 4209 1 51 . 1 1 7 7 ALA HB3 H 1 1.36 . . 1 . . . . . . . . 4209 1 52 . 1 1 8 8 LYS N N 15 120.4 . . 1 . . . . . . . . 4209 1 53 . 1 1 8 8 LYS H H 1 7.67 . . 1 . . . . . . . . 4209 1 54 . 1 1 8 8 LYS CA C 13 58.0 . . 1 . . . . . . . . 4209 1 55 . 1 1 8 8 LYS HA H 1 4.01 . . 1 . . . . . . . . 4209 1 56 . 1 1 8 8 LYS CB C 13 32.4 . . 1 . . . . . . . . 4209 1 57 . 1 1 8 8 LYS HB2 H 1 1.83 . . 1 . . . . . . . . 4209 1 58 . 1 1 8 8 LYS HB3 H 1 1.83 . . 1 . . . . . . . . 4209 1 59 . 1 1 8 8 LYS HG2 H 1 1.34 . . 1 . . . . . . . . 4209 1 60 . 1 1 8 8 LYS HG3 H 1 1.44 . . 1 . . . . . . . . 4209 1 61 . 1 1 8 8 LYS HD2 H 1 1.65 . . 1 . . . . . . . . 4209 1 62 . 1 1 8 8 LYS HE2 H 1 2.92 . . 1 . . . . . . . . 4209 1 63 . 1 1 8 8 LYS CG C 13 25.0 . . 1 . . . . . . . . 4209 1 64 . 1 1 8 8 LYS CD C 13 28.9 . . 1 . . . . . . . . 4209 1 65 . 1 1 8 8 LYS CE C 13 41.8 . . 1 . . . . . . . . 4209 1 66 . 1 1 9 9 ALA N N 15 124.2 . . 1 . . . . . . . . 4209 1 67 . 1 1 9 9 ALA H H 1 7.92 . . 1 . . . . . . . . 4209 1 68 . 1 1 9 9 ALA CA C 13 53.6 . . 1 . . . . . . . . 4209 1 69 . 1 1 9 9 ALA HA H 1 4.15 . . 1 . . . . . . . . 4209 1 70 . 1 1 9 9 ALA CB C 13 18.4 . . 1 . . . . . . . . 4209 1 71 . 1 1 9 9 ALA HB1 H 1 1.36 . . 1 . . . . . . . . 4209 1 72 . 1 1 9 9 ALA HB2 H 1 1.36 . . 1 . . . . . . . . 4209 1 73 . 1 1 9 9 ALA HB3 H 1 1.36 . . 1 . . . . . . . . 4209 1 74 . 1 1 10 10 ALA N N 15 123.8 . . 1 . . . . . . . . 4209 1 75 . 1 1 10 10 ALA H H 1 8.05 . . 1 . . . . . . . . 4209 1 76 . 1 1 10 10 ALA CA C 13 54.2 . . 1 . . . . . . . . 4209 1 77 . 1 1 10 10 ALA HA H 1 4.08 . . 1 . . . . . . . . 4209 1 78 . 1 1 10 10 ALA CB C 13 18.4 . . 1 . . . . . . . . 4209 1 79 . 1 1 10 10 ALA HB1 H 1 1.35 . . 1 . . . . . . . . 4209 1 80 . 1 1 10 10 ALA HB2 H 1 1.35 . . 1 . . . . . . . . 4209 1 81 . 1 1 10 10 ALA HB3 H 1 1.35 . . 1 . . . . . . . . 4209 1 82 . 1 1 11 11 PHE N N 15 120.0 . . 1 . . . . . . . . 4209 1 83 . 1 1 11 11 PHE H H 1 8.19 . . 1 . . . . . . . . 4209 1 84 . 1 1 11 11 PHE CA C 13 60.1 . . 1 . . . . . . . . 4209 1 85 . 1 1 11 11 PHE HA H 1 4.21 . . 1 . . . . . . . . 4209 1 86 . 1 1 11 11 PHE CB C 13 38.8 . . 1 . . . . . . . . 4209 1 87 . 1 1 11 11 PHE HB2 H 1 3.07 . . 1 . . . . . . . . 4209 1 88 . 1 1 11 11 PHE HB3 H 1 3.15 . . 1 . . . . . . . . 4209 1 89 . 1 1 11 11 PHE HD1 H 1 7.15 . . 3 . . . . . . . . 4209 1 90 . 1 1 11 11 PHE CD1 C 13 131.6 . . 3 . . . . . . . . 4209 1 91 . 1 1 12 12 ASN N N 15 120.3 . . 1 . . . . . . . . 4209 1 92 . 1 1 12 12 ASN H H 1 8.33 . . 1 . . . . . . . . 4209 1 93 . 1 1 12 12 ASN CA C 13 55.0 . . 1 . . . . . . . . 4209 1 94 . 1 1 12 12 ASN HA H 1 4.43 . . 1 . . . . . . . . 4209 1 95 . 1 1 12 12 ASN CB C 13 38.3 . . 1 . . . . . . . . 4209 1 96 . 1 1 12 12 ASN HB2 H 1 2.77 . . 1 . . . . . . . . 4209 1 97 . 1 1 12 12 ASN HB3 H 1 2.83 . . 1 . . . . . . . . 4209 1 98 . 1 1 12 12 ASN HD21 H 1 6.80 . . 1 . . . . . . . . 4209 1 99 . 1 1 12 12 ASN HD22 H 1 7.51 . . 1 . . . . . . . . 4209 1 100 . 1 1 12 12 ASN ND2 N 15 113.4 . . 1 . . . . . . . . 4209 1 101 . 1 1 13 13 SER N N 15 118.0 . . 1 . . . . . . . . 4209 1 102 . 1 1 13 13 SER H H 1 8.02 . . 1 . . . . . . . . 4209 1 103 . 1 1 13 13 SER CA C 13 60.5 . . 1 . . . . . . . . 4209 1 104 . 1 1 13 13 SER HA H 1 4.28 . . 1 . . . . . . . . 4209 1 105 . 1 1 13 13 SER CB C 13 63.0 . . 1 . . . . . . . . 4209 1 106 . 1 1 13 13 SER HB2 H 1 3.85 . . 1 . . . . . . . . 4209 1 107 . 1 1 13 13 SER HB3 H 1 3.93 . . 1 . . . . . . . . 4209 1 108 . 1 1 14 14 LEU N N 15 125.1 . . 1 . . . . . . . . 4209 1 109 . 1 1 14 14 LEU H H 1 8.03 . . 1 . . . . . . . . 4209 1 110 . 1 1 14 14 LEU CA C 13 57.1 . . 1 . . . . . . . . 4209 1 111 . 1 1 14 14 LEU HA H 1 4.07 . . 1 . . . . . . . . 4209 1 112 . 1 1 14 14 LEU CB C 13 41.8 . . 1 . . . . . . . . 4209 1 113 . 1 1 14 14 LEU HB2 H 1 1.51 . . 1 . . . . . . . . 4209 1 114 . 1 1 14 14 LEU HB3 H 1 1.66 . . 1 . . . . . . . . 4209 1 115 . 1 1 14 14 LEU HG H 1 1.64 . . 1 . . . . . . . . 4209 1 116 . 1 1 14 14 LEU HD11 H 1 0.76 . . 1 . . . . . . . . 4209 1 117 . 1 1 14 14 LEU HD12 H 1 0.76 . . 1 . . . . . . . . 4209 1 118 . 1 1 14 14 LEU HD13 H 1 0.76 . . 1 . . . . . . . . 4209 1 119 . 1 1 14 14 LEU HD21 H 1 0.79 . . 1 . . . . . . . . 4209 1 120 . 1 1 14 14 LEU HD22 H 1 0.79 . . 1 . . . . . . . . 4209 1 121 . 1 1 14 14 LEU HD23 H 1 0.79 . . 1 . . . . . . . . 4209 1 122 . 1 1 14 14 LEU CG C 13 27.1 . . 1 . . . . . . . . 4209 1 123 . 1 1 14 14 LEU CD1 C 13 24.1 . . 1 . . . . . . . . 4209 1 124 . 1 1 14 14 LEU CD2 C 13 25.0 . . 1 . . . . . . . . 4209 1 125 . 1 1 15 15 GLN N N 15 120.0 . . 1 . . . . . . . . 4209 1 126 . 1 1 15 15 GLN H H 1 8.16 . . 1 . . . . . . . . 4209 1 127 . 1 1 15 15 GLN CA C 13 58.4 . . 1 . . . . . . . . 4209 1 128 . 1 1 15 15 GLN HA H 1 3.83 . . 1 . . . . . . . . 4209 1 129 . 1 1 15 15 GLN CB C 13 28.5 . . 1 . . . . . . . . 4209 1 130 . 1 1 15 15 GLN HB2 H 1 1.91 . . 1 . . . . . . . . 4209 1 131 . 1 1 15 15 GLN HB3 H 1 1.96 . . 1 . . . . . . . . 4209 1 132 . 1 1 15 15 GLN HG2 H 1 2.13 . . 1 . . . . . . . . 4209 1 133 . 1 1 15 15 GLN HG3 H 1 2.20 . . 1 . . . . . . . . 4209 1 134 . 1 1 15 15 GLN HE21 H 1 6.64 . . 1 . . . . . . . . 4209 1 135 . 1 1 15 15 GLN HE22 H 1 7.05 . . 1 . . . . . . . . 4209 1 136 . 1 1 15 15 GLN CG C 13 33.9 . . 1 . . . . . . . . 4209 1 137 . 1 1 15 15 GLN NE2 N 15 112.3 . . 1 . . . . . . . . 4209 1 138 . 1 1 16 16 ALA N N 15 123.5 . . 1 . . . . . . . . 4209 1 139 . 1 1 16 16 ALA H H 1 7.86 . . 1 . . . . . . . . 4209 1 140 . 1 1 16 16 ALA CA C 13 54.0 . . 1 . . . . . . . . 4209 1 141 . 1 1 16 16 ALA HA H 1 4.15 . . 1 . . . . . . . . 4209 1 142 . 1 1 16 16 ALA CB C 13 18.5 . . 1 . . . . . . . . 4209 1 143 . 1 1 16 16 ALA HB1 H 1 1.40 . . 1 . . . . . . . . 4209 1 144 . 1 1 16 16 ALA HB2 H 1 1.40 . . 1 . . . . . . . . 4209 1 145 . 1 1 16 16 ALA HB3 H 1 1.40 . . 1 . . . . . . . . 4209 1 146 . 1 1 17 17 SER N N 15 115.8 . . 1 . . . . . . . . 4209 1 147 . 1 1 17 17 SER H H 1 7.90 . . 1 . . . . . . . . 4209 1 148 . 1 1 17 17 SER CA C 13 60.1 . . 1 . . . . . . . . 4209 1 149 . 1 1 17 17 SER HA H 1 4.39 . . 1 . . . . . . . . 4209 1 150 . 1 1 17 17 SER CB C 13 63.4 . . 1 . . . . . . . . 4209 1 151 . 1 1 17 17 SER HB2 H 1 3.86 . . 1 . . . . . . . . 4209 1 152 . 1 1 18 18 ALA N N 15 125.5 . . 1 . . . . . . . . 4209 1 153 . 1 1 18 18 ALA H H 1 8.23 . . 1 . . . . . . . . 4209 1 154 . 1 1 18 18 ALA CA C 13 54.6 . . 1 . . . . . . . . 4209 1 155 . 1 1 18 18 ALA HA H 1 4.10 . . 1 . . . . . . . . 4209 1 156 . 1 1 18 18 ALA CB C 13 18.4 . . 1 . . . . . . . . 4209 1 157 . 1 1 18 18 ALA HB1 H 1 1.37 . . 1 . . . . . . . . 4209 1 158 . 1 1 18 18 ALA HB2 H 1 1.37 . . 1 . . . . . . . . 4209 1 159 . 1 1 18 18 ALA HB3 H 1 1.37 . . 1 . . . . . . . . 4209 1 160 . 1 1 19 19 THR N N 15 111.7 . . 1 . . . . . . . . 4209 1 161 . 1 1 19 19 THR H H 1 7.78 . . 1 . . . . . . . . 4209 1 162 . 1 1 19 19 THR CA C 13 65.0 . . 1 . . . . . . . . 4209 1 163 . 1 1 19 19 THR HA H 1 3.88 . . 1 . . . . . . . . 4209 1 164 . 1 1 19 19 THR CB C 13 68.5 . . 1 . . . . . . . . 4209 1 165 . 1 1 19 19 THR HB H 1 4.17 . . 1 . . . . . . . . 4209 1 166 . 1 1 19 19 THR HG21 H 1 1.19 . . 1 . . . . . . . . 4209 1 167 . 1 1 19 19 THR HG22 H 1 1.19 . . 1 . . . . . . . . 4209 1 168 . 1 1 19 19 THR HG23 H 1 1.19 . . 1 . . . . . . . . 4209 1 169 . 1 1 19 19 THR CG2 C 13 22.0 . . 1 . . . . . . . . 4209 1 170 . 1 1 20 20 GLU N N 15 122.2 . . 1 . . . . . . . . 4209 1 171 . 1 1 20 20 GLU H H 1 7.89 . . 1 . . . . . . . . 4209 1 172 . 1 1 20 20 GLU CA C 13 57.6 . . 1 . . . . . . . . 4209 1 173 . 1 1 20 20 GLU HA H 1 4.03 . . 1 . . . . . . . . 4209 1 174 . 1 1 20 20 GLU CB C 13 28.5 . . 1 . . . . . . . . 4209 1 175 . 1 1 20 20 GLU HB2 H 1 1.75 . . 1 . . . . . . . . 4209 1 176 . 1 1 20 20 GLU HB3 H 1 1.87 . . 1 . . . . . . . . 4209 1 177 . 1 1 20 20 GLU HG2 H 1 2.05 . . 1 . . . . . . . . 4209 1 178 . 1 1 20 20 GLU HG3 H 1 2.16 . . 1 . . . . . . . . 4209 1 179 . 1 1 20 20 GLU CG C 13 33.9 . . 1 . . . . . . . . 4209 1 180 . 1 1 21 21 TYR N N 15 118.3 . . 1 . . . . . . . . 4209 1 181 . 1 1 21 21 TYR H H 1 7.76 . . 1 . . . . . . . . 4209 1 182 . 1 1 21 21 TYR CA C 13 58.6 . . 1 . . . . . . . . 4209 1 183 . 1 1 21 21 TYR HA H 1 4.61 . . 1 . . . . . . . . 4209 1 184 . 1 1 21 21 TYR CB C 13 38.7 . . 1 . . . . . . . . 4209 1 185 . 1 1 21 21 TYR HB2 H 1 2.75 . . 1 . . . . . . . . 4209 1 186 . 1 1 21 21 TYR HB3 H 1 3.25 . . 1 . . . . . . . . 4209 1 187 . 1 1 21 21 TYR HD1 H 1 7.00 . . 3 . . . . . . . . 4209 1 188 . 1 1 21 21 TYR HE1 H 1 6.71 . . 3 . . . . . . . . 4209 1 189 . 1 1 21 21 TYR CD1 C 13 132.6 . . 3 . . . . . . . . 4209 1 190 . 1 1 21 21 TYR CE1 C 13 117.8 . . 3 . . . . . . . . 4209 1 191 . 1 1 22 22 ILE N N 15 121.2 . . 1 . . . . . . . . 4209 1 192 . 1 1 22 22 ILE H H 1 7.53 . . 1 . . . . . . . . 4209 1 193 . 1 1 22 22 ILE CA C 13 63.4 . . 1 . . . . . . . . 4209 1 194 . 1 1 22 22 ILE HA H 1 3.89 . . 1 . . . . . . . . 4209 1 195 . 1 1 22 22 ILE CB C 13 38.3 . . 1 . . . . . . . . 4209 1 196 . 1 1 22 22 ILE HB H 1 1.96 . . 1 . . . . . . . . 4209 1 197 . 1 1 22 22 ILE HG12 H 1 1.24 . . 1 . . . . . . . . 4209 1 198 . 1 1 22 22 ILE HG13 H 1 1.54 . . 1 . . . . . . . . 4209 1 199 . 1 1 22 22 ILE HG21 H 1 0.93 . . 1 . . . . . . . . 4209 1 200 . 1 1 22 22 ILE HG22 H 1 0.93 . . 1 . . . . . . . . 4209 1 201 . 1 1 22 22 ILE HG23 H 1 0.93 . . 1 . . . . . . . . 4209 1 202 . 1 1 22 22 ILE HD11 H 1 0.83 . . 1 . . . . . . . . 4209 1 203 . 1 1 22 22 ILE HD12 H 1 0.83 . . 1 . . . . . . . . 4209 1 204 . 1 1 22 22 ILE HD13 H 1 0.83 . . 1 . . . . . . . . 4209 1 205 . 1 1 22 22 ILE CG1 C 13 28.9 . . 1 . . . . . . . . 4209 1 206 . 1 1 22 22 ILE CG2 C 13 13.5 . . 1 . . . . . . . . 4209 1 207 . 1 1 22 22 ILE CD1 C 13 13.5 . . 1 . . . . . . . . 4209 1 208 . 1 1 23 23 GLY N N 15 111.1 . . 1 . . . . . . . . 4209 1 209 . 1 1 23 23 GLY H H 1 8.49 . . 1 . . . . . . . . 4209 1 210 . 1 1 23 23 GLY CA C 13 46.1 . . 1 . . . . . . . . 4209 1 211 . 1 1 23 23 GLY HA2 H 1 3.75 . . 1 . . . . . . . . 4209 1 212 . 1 1 23 23 GLY HA3 H 1 3.89 . . 1 . . . . . . . . 4209 1 213 . 1 1 24 24 TYR N N 15 119.9 . . 1 . . . . . . . . 4209 1 214 . 1 1 24 24 TYR H H 1 7.81 . . 1 . . . . . . . . 4209 1 215 . 1 1 24 24 TYR CA C 13 59.6 . . 1 . . . . . . . . 4209 1 216 . 1 1 24 24 TYR HA H 1 4.34 . . 1 . . . . . . . . 4209 1 217 . 1 1 24 24 TYR CB C 13 38.2 . . 1 . . . . . . . . 4209 1 218 . 1 1 24 24 TYR HB2 H 1 2.99 . . 1 . . . . . . . . 4209 1 219 . 1 1 24 24 TYR HB3 H 1 3.06 . . 1 . . . . . . . . 4209 1 220 . 1 1 24 24 TYR HD1 H 1 7.04 . . 3 . . . . . . . . 4209 1 221 . 1 1 24 24 TYR HE1 H 1 6.78 . . 3 . . . . . . . . 4209 1 222 . 1 1 24 24 TYR CD1 C 13 132.1 . . 3 . . . . . . . . 4209 1 223 . 1 1 24 24 TYR CE1 C 13 118.4 . . 3 . . . . . . . . 4209 1 224 . 1 1 25 25 ALA N N 15 123.8 . . 1 . . . . . . . . 4209 1 225 . 1 1 25 25 ALA H H 1 8.05 . . 1 . . . . . . . . 4209 1 226 . 1 1 25 25 ALA CA C 13 55.6 . . 1 . . . . . . . . 4209 1 227 . 1 1 25 25 ALA HA H 1 3.93 . . 1 . . . . . . . . 4209 1 228 . 1 1 25 25 ALA CB C 13 18.0 . . 1 . . . . . . . . 4209 1 229 . 1 1 25 25 ALA HB1 H 1 1.35 . . 1 . . . . . . . . 4209 1 230 . 1 1 25 25 ALA HB2 H 1 1.35 . . 1 . . . . . . . . 4209 1 231 . 1 1 25 25 ALA HB3 H 1 1.35 . . 1 . . . . . . . . 4209 1 232 . 1 1 26 26 TRP N N 15 118.0 . . 1 . . . . . . . . 4209 1 233 . 1 1 26 26 TRP H H 1 8.20 . . 1 . . . . . . . . 4209 1 234 . 1 1 26 26 TRP CA C 13 59.6 . . 1 . . . . . . . . 4209 1 235 . 1 1 26 26 TRP HA H 1 4.31 . . 1 . . . . . . . . 4209 1 236 . 1 1 26 26 TRP CB C 13 28.9 . . 1 . . . . . . . . 4209 1 237 . 1 1 26 26 TRP HB2 H 1 3.19 . . 1 . . . . . . . . 4209 1 238 . 1 1 26 26 TRP HB3 H 1 3.25 . . 1 . . . . . . . . 4209 1 239 . 1 1 26 26 TRP HD1 H 1 7.29 . . 1 . . . . . . . . 4209 1 240 . 1 1 26 26 TRP HE1 H 1 10.22 . . 1 . . . . . . . . 4209 1 241 . 1 1 26 26 TRP HE3 H 1 7.35 . . 1 . . . . . . . . 4209 1 242 . 1 1 26 26 TRP HZ2 H 1 6.82 . . 1 . . . . . . . . 4209 1 243 . 1 1 26 26 TRP HZ3 H 1 7.32 . . 1 . . . . . . . . 4209 1 244 . 1 1 26 26 TRP HH2 H 1 6.95 . . 1 . . . . . . . . 4209 1 245 . 1 1 26 26 TRP CD1 C 13 127.1 . . 1 . . . . . . . . 4209 1 246 . 1 1 26 26 TRP CE3 C 13 119.7 . . 1 . . . . . . . . 4209 1 247 . 1 1 26 26 TRP CZ2 C 13 114.3 . . 1 . . . . . . . . 4209 1 248 . 1 1 26 26 TRP CZ3 C 13 120.7 . . 1 . . . . . . . . 4209 1 249 . 1 1 26 26 TRP CH2 C 13 123.2 . . 1 . . . . . . . . 4209 1 250 . 1 1 26 26 TRP NE1 N 15 130.9 . . 1 . . . . . . . . 4209 1 251 . 1 1 27 27 ALA N N 15 122.5 . . 1 . . . . . . . . 4209 1 252 . 1 1 27 27 ALA H H 1 7.57 . . 1 . . . . . . . . 4209 1 253 . 1 1 27 27 ALA CA C 13 55.3 . . 1 . . . . . . . . 4209 1 254 . 1 1 27 27 ALA HA H 1 3.75 . . 1 . . . . . . . . 4209 1 255 . 1 1 27 27 ALA CB C 13 18.1 . . 1 . . . . . . . . 4209 1 256 . 1 1 27 27 ALA HB1 H 1 1.25 . . 1 . . . . . . . . 4209 1 257 . 1 1 27 27 ALA HB2 H 1 1.25 . . 1 . . . . . . . . 4209 1 258 . 1 1 27 27 ALA HB3 H 1 1.25 . . 1 . . . . . . . . 4209 1 259 . 1 1 28 28 MET N N 15 117.1 . . 1 . . . . . . . . 4209 1 260 . 1 1 28 28 MET H H 1 7.83 . . 1 . . . . . . . . 4209 1 261 . 1 1 28 28 MET CA C 13 58.3 . . 1 . . . . . . . . 4209 1 262 . 1 1 28 28 MET HA H 1 3.99 . . 1 . . . . . . . . 4209 1 263 . 1 1 28 28 MET CB C 13 31.7 . . 1 . . . . . . . . 4209 1 264 . 1 1 28 28 MET HB2 H 1 2.05 . . 1 . . . . . . . . 4209 1 265 . 1 1 28 28 MET HB3 H 1 2.13 . . 1 . . . . . . . . 4209 1 266 . 1 1 28 28 MET HG2 H 1 2.37 . . 1 . . . . . . . . 4209 1 267 . 1 1 28 28 MET HG3 H 1 2.48 . . 1 . . . . . . . . 4209 1 268 . 1 1 28 28 MET HE1 H 1 1.83 . . 1 . . . . . . . . 4209 1 269 . 1 1 28 28 MET HE2 H 1 1.83 . . 1 . . . . . . . . 4209 1 270 . 1 1 28 28 MET HE3 H 1 1.83 . . 1 . . . . . . . . 4209 1 271 . 1 1 28 28 MET CG C 13 32.7 . . 1 . . . . . . . . 4209 1 272 . 1 1 28 28 MET CE C 13 17.2 . . 1 . . . . . . . . 4209 1 273 . 1 1 29 29 VAL N N 15 120.3 . . 1 . . . . . . . . 4209 1 274 . 1 1 29 29 VAL H H 1 7.89 . . 1 . . . . . . . . 4209 1 275 . 1 1 29 29 VAL CA C 13 67.5 . . 1 . . . . . . . . 4209 1 276 . 1 1 29 29 VAL HA H 1 3.40 . . 1 . . . . . . . . 4209 1 277 . 1 1 29 29 VAL CB C 13 30.9 . . 1 . . . . . . . . 4209 1 278 . 1 1 29 29 VAL HB H 1 2.33 . . 1 . . . . . . . . 4209 1 279 . 1 1 29 29 VAL HG11 H 1 0.83 . . 1 . . . . . . . . 4209 1 280 . 1 1 29 29 VAL HG12 H 1 0.83 . . 1 . . . . . . . . 4209 1 281 . 1 1 29 29 VAL HG13 H 1 0.83 . . 1 . . . . . . . . 4209 1 282 . 1 1 29 29 VAL HG21 H 1 0.93 . . 1 . . . . . . . . 4209 1 283 . 1 1 29 29 VAL HG22 H 1 0.93 . . 1 . . . . . . . . 4209 1 284 . 1 1 29 29 VAL HG23 H 1 0.93 . . 1 . . . . . . . . 4209 1 285 . 1 1 29 29 VAL CG1 C 13 21.4 . . 1 . . . . . . . . 4209 1 286 . 1 1 29 29 VAL CG2 C 13 23.0 . . 1 . . . . . . . . 4209 1 287 . 1 1 30 30 VAL N N 15 120.3 . . 1 . . . . . . . . 4209 1 288 . 1 1 30 30 VAL H H 1 7.86 . . 1 . . . . . . . . 4209 1 289 . 1 1 30 30 VAL CA C 13 67.5 . . 1 . . . . . . . . 4209 1 290 . 1 1 30 30 VAL HA H 1 3.33 . . 1 . . . . . . . . 4209 1 291 . 1 1 30 30 VAL CB C 13 30.7 . . 1 . . . . . . . . 4209 1 292 . 1 1 30 30 VAL HB H 1 2.17 . . 1 . . . . . . . . 4209 1 293 . 1 1 30 30 VAL HG11 H 1 0.80 . . 1 . . . . . . . . 4209 1 294 . 1 1 30 30 VAL HG12 H 1 0.80 . . 1 . . . . . . . . 4209 1 295 . 1 1 30 30 VAL HG13 H 1 0.80 . . 1 . . . . . . . . 4209 1 296 . 1 1 30 30 VAL HG21 H 1 0.90 . . 1 . . . . . . . . 4209 1 297 . 1 1 30 30 VAL HG22 H 1 0.90 . . 1 . . . . . . . . 4209 1 298 . 1 1 30 30 VAL HG23 H 1 0.90 . . 1 . . . . . . . . 4209 1 299 . 1 1 30 30 VAL CG1 C 13 21.4 . . 1 . . . . . . . . 4209 1 300 . 1 1 30 30 VAL CG2 C 13 23.0 . . 1 . . . . . . . . 4209 1 301 . 1 1 31 31 VAL N N 15 120.3 . . 1 . . . . . . . . 4209 1 302 . 1 1 31 31 VAL H H 1 7.90 . . 1 . . . . . . . . 4209 1 303 . 1 1 31 31 VAL CA C 13 67.0 . . 1 . . . . . . . . 4209 1 304 . 1 1 31 31 VAL HA H 1 3.46 . . 1 . . . . . . . . 4209 1 305 . 1 1 31 31 VAL CB C 13 30.7 . . 1 . . . . . . . . 4209 1 306 . 1 1 31 31 VAL HB H 1 2.15 . . 1 . . . . . . . . 4209 1 307 . 1 1 31 31 VAL HG11 H 1 0.77 . . 1 . . . . . . . . 4209 1 308 . 1 1 31 31 VAL HG12 H 1 0.77 . . 1 . . . . . . . . 4209 1 309 . 1 1 31 31 VAL HG13 H 1 0.77 . . 1 . . . . . . . . 4209 1 310 . 1 1 31 31 VAL HG21 H 1 0.94 . . 1 . . . . . . . . 4209 1 311 . 1 1 31 31 VAL HG22 H 1 0.94 . . 1 . . . . . . . . 4209 1 312 . 1 1 31 31 VAL HG23 H 1 0.94 . . 1 . . . . . . . . 4209 1 313 . 1 1 31 31 VAL CG1 C 13 21.1 . . 1 . . . . . . . . 4209 1 314 . 1 1 31 31 VAL CG2 C 13 23.0 . . 1 . . . . . . . . 4209 1 315 . 1 1 32 32 ILE N N 15 120.8 . . 1 . . . . . . . . 4209 1 316 . 1 1 32 32 ILE H H 1 8.20 . . 1 . . . . . . . . 4209 1 317 . 1 1 32 32 ILE CA C 13 65.5 . . 1 . . . . . . . . 4209 1 318 . 1 1 32 32 ILE HA H 1 3.54 . . 1 . . . . . . . . 4209 1 319 . 1 1 32 32 ILE CB C 13 37.8 . . 1 . . . . . . . . 4209 1 320 . 1 1 32 32 ILE HB H 1 1.86 . . 1 . . . . . . . . 4209 1 321 . 1 1 32 32 ILE HG12 H 1 0.94 . . 1 . . . . . . . . 4209 1 322 . 1 1 32 32 ILE HG13 H 1 1.77 . . 1 . . . . . . . . 4209 1 323 . 1 1 32 32 ILE HG21 H 1 0.76 . . 1 . . . . . . . . 4209 1 324 . 1 1 32 32 ILE HG22 H 1 0.76 . . 1 . . . . . . . . 4209 1 325 . 1 1 32 32 ILE HG23 H 1 0.76 . . 1 . . . . . . . . 4209 1 326 . 1 1 32 32 ILE HD11 H 1 0.68 . . 1 . . . . . . . . 4209 1 327 . 1 1 32 32 ILE HD12 H 1 0.68 . . 1 . . . . . . . . 4209 1 328 . 1 1 32 32 ILE HD13 H 1 0.68 . . 1 . . . . . . . . 4209 1 329 . 1 1 32 32 ILE CG1 C 13 29.4 . . 1 . . . . . . . . 4209 1 330 . 1 1 32 32 ILE CG2 C 13 13.1 . . 1 . . . . . . . . 4209 1 331 . 1 1 32 32 ILE CD1 C 13 13.1 . . 1 . . . . . . . . 4209 1 332 . 1 1 33 33 VAL N N 15 123.7 . . 1 . . . . . . . . 4209 1 333 . 1 1 33 33 VAL H H 1 8.69 . . 1 . . . . . . . . 4209 1 334 . 1 1 33 33 VAL CA C 13 67.5 . . 1 . . . . . . . . 4209 1 335 . 1 1 33 33 VAL HA H 1 3.44 . . 1 . . . . . . . . 4209 1 336 . 1 1 33 33 VAL CB C 13 30.7 . . 1 . . . . . . . . 4209 1 337 . 1 1 33 33 VAL HB H 1 2.11 . . 1 . . . . . . . . 4209 1 338 . 1 1 33 33 VAL HG11 H 1 0.80 . . 1 . . . . . . . . 4209 1 339 . 1 1 33 33 VAL HG12 H 1 0.80 . . 1 . . . . . . . . 4209 1 340 . 1 1 33 33 VAL HG13 H 1 0.80 . . 1 . . . . . . . . 4209 1 341 . 1 1 33 33 VAL HG21 H 1 0.95 . . 1 . . . . . . . . 4209 1 342 . 1 1 33 33 VAL HG22 H 1 0.95 . . 1 . . . . . . . . 4209 1 343 . 1 1 33 33 VAL HG23 H 1 0.95 . . 1 . . . . . . . . 4209 1 344 . 1 1 33 33 VAL CG1 C 13 21.4 . . 1 . . . . . . . . 4209 1 345 . 1 1 33 33 VAL CG2 C 13 23.0 . . 1 . . . . . . . . 4209 1 346 . 1 1 34 34 GLY N N 15 109.7 . . 1 . . . . . . . . 4209 1 347 . 1 1 34 34 GLY H H 1 8.89 . . 1 . . . . . . . . 4209 1 348 . 1 1 34 34 GLY CA C 13 47.7 . . 1 . . . . . . . . 4209 1 349 . 1 1 34 34 GLY HA2 H 1 3.50 . . 1 . . . . . . . . 4209 1 350 . 1 1 35 35 ALA N N 15 123.9 . . 1 . . . . . . . . 4209 1 351 . 1 1 35 35 ALA H H 1 8.83 . . 1 . . . . . . . . 4209 1 352 . 1 1 35 35 ALA CA C 13 54.6 . . 1 . . . . . . . . 4209 1 353 . 1 1 35 35 ALA HA H 1 3.93 . . 1 . . . . . . . . 4209 1 354 . 1 1 35 35 ALA CB C 13 18.0 . . 1 . . . . . . . . 4209 1 355 . 1 1 35 35 ALA HB1 H 1 1.35 . . 1 . . . . . . . . 4209 1 356 . 1 1 35 35 ALA HB2 H 1 1.35 . . 1 . . . . . . . . 4209 1 357 . 1 1 35 35 ALA HB3 H 1 1.35 . . 1 . . . . . . . . 4209 1 358 . 1 1 36 36 THR N N 15 115.3 . . 1 . . . . . . . . 4209 1 359 . 1 1 36 36 THR H H 1 7.85 . . 1 . . . . . . . . 4209 1 360 . 1 1 36 36 THR CA C 13 67.5 . . 1 . . . . . . . . 4209 1 361 . 1 1 36 36 THR HA H 1 3.74 . . 1 . . . . . . . . 4209 1 362 . 1 1 36 36 THR CB C 13 68.0 . . 1 . . . . . . . . 4209 1 363 . 1 1 36 36 THR HB H 1 4.22 . . 1 . . . . . . . . 4209 1 364 . 1 1 36 36 THR HG21 H 1 1.07 . . 1 . . . . . . . . 4209 1 365 . 1 1 36 36 THR HG22 H 1 1.07 . . 1 . . . . . . . . 4209 1 366 . 1 1 36 36 THR HG23 H 1 1.07 . . 1 . . . . . . . . 4209 1 367 . 1 1 36 36 THR CG2 C 13 21.4 . . 1 . . . . . . . . 4209 1 368 . 1 1 37 37 ILE N N 15 122.0 . . 1 . . . . . . . . 4209 1 369 . 1 1 37 37 ILE H H 1 8.23 . . 1 . . . . . . . . 4209 1 370 . 1 1 37 37 ILE CA C 13 65.0 . . 1 . . . . . . . . 4209 1 371 . 1 1 37 37 ILE HA H 1 3.57 . . 1 . . . . . . . . 4209 1 372 . 1 1 37 37 ILE CB C 13 37.8 . . 1 . . . . . . . . 4209 1 373 . 1 1 37 37 ILE HB H 1 1.91 . . 1 . . . . . . . . 4209 1 374 . 1 1 37 37 ILE HG12 H 1 1.01 . . 1 . . . . . . . . 4209 1 375 . 1 1 37 37 ILE HG13 H 1 1.78 . . 1 . . . . . . . . 4209 1 376 . 1 1 37 37 ILE HG21 H 1 0.82 . . 1 . . . . . . . . 4209 1 377 . 1 1 37 37 ILE HG22 H 1 0.82 . . 1 . . . . . . . . 4209 1 378 . 1 1 37 37 ILE HG23 H 1 0.82 . . 1 . . . . . . . . 4209 1 379 . 1 1 37 37 ILE HD11 H 1 0.74 . . 1 . . . . . . . . 4209 1 380 . 1 1 37 37 ILE HD12 H 1 0.74 . . 1 . . . . . . . . 4209 1 381 . 1 1 37 37 ILE HD13 H 1 0.74 . . 1 . . . . . . . . 4209 1 382 . 1 1 37 37 ILE CG1 C 13 28.9 . . 1 . . . . . . . . 4209 1 383 . 1 1 37 37 ILE CG2 C 13 13.5 . . 1 . . . . . . . . 4209 1 384 . 1 1 37 37 ILE CD1 C 13 13.5 . . 1 . . . . . . . . 4209 1 385 . 1 1 38 38 GLY N N 15 109.4 . . 1 . . . . . . . . 4209 1 386 . 1 1 38 38 GLY H H 1 8.67 . . 1 . . . . . . . . 4209 1 387 . 1 1 38 38 GLY CA C 13 47.7 . . 1 . . . . . . . . 4209 1 388 . 1 1 38 38 GLY HA2 H 1 3.61 . . 1 . . . . . . . . 4209 1 389 . 1 1 39 39 ILE N N 15 122.9 . . 1 . . . . . . . . 4209 1 390 . 1 1 39 39 ILE H H 1 8.53 . . 1 . . . . . . . . 4209 1 391 . 1 1 39 39 ILE CA C 13 65.0 . . 1 . . . . . . . . 4209 1 392 . 1 1 39 39 ILE HA H 1 3.75 . . 1 . . . . . . . . 4209 1 393 . 1 1 39 39 ILE CB C 13 37.8 . . 1 . . . . . . . . 4209 1 394 . 1 1 39 39 ILE HB H 1 1.92 . . 1 . . . . . . . . 4209 1 395 . 1 1 39 39 ILE HG12 H 1 1.02 . . 1 . . . . . . . . 4209 1 396 . 1 1 39 39 ILE HG13 H 1 1.83 . . 1 . . . . . . . . 4209 1 397 . 1 1 39 39 ILE HG21 H 1 0.91 . . 1 . . . . . . . . 4209 1 398 . 1 1 39 39 ILE HG22 H 1 0.91 . . 1 . . . . . . . . 4209 1 399 . 1 1 39 39 ILE HG23 H 1 0.91 . . 1 . . . . . . . . 4209 1 400 . 1 1 39 39 ILE HD11 H 1 0.80 . . 1 . . . . . . . . 4209 1 401 . 1 1 39 39 ILE HD12 H 1 0.80 . . 1 . . . . . . . . 4209 1 402 . 1 1 39 39 ILE HD13 H 1 0.80 . . 1 . . . . . . . . 4209 1 403 . 1 1 39 39 ILE CG1 C 13 29.8 . . 1 . . . . . . . . 4209 1 404 . 1 1 39 39 ILE CG2 C 13 13.5 . . 1 . . . . . . . . 4209 1 405 . 1 1 39 39 ILE CD1 C 13 13.5 . . 1 . . . . . . . . 4209 1 406 . 1 1 40 40 LYS N N 15 120.9 . . 1 . . . . . . . . 4209 1 407 . 1 1 40 40 LYS H H 1 7.88 . . 1 . . . . . . . . 4209 1 408 . 1 1 40 40 LYS CA C 13 58.0 . . 1 . . . . . . . . 4209 1 409 . 1 1 40 40 LYS HA H 1 4.01 . . 1 . . . . . . . . 4209 1 410 . 1 1 40 40 LYS CB C 13 31.7 . . 1 . . . . . . . . 4209 1 411 . 1 1 40 40 LYS HB2 H 1 1.82 . . 1 . . . . . . . . 4209 1 412 . 1 1 40 40 LYS HB3 H 1 1.97 . . 1 . . . . . . . . 4209 1 413 . 1 1 40 40 LYS HG2 H 1 1.52 . . 1 . . . . . . . . 4209 1 414 . 1 1 40 40 LYS HD2 H 1 1.43 . . 1 . . . . . . . . 4209 1 415 . 1 1 40 40 LYS HD3 H 1 1.52 . . 1 . . . . . . . . 4209 1 416 . 1 1 40 40 LYS HE2 H 1 2.81 . . 1 . . . . . . . . 4209 1 417 . 1 1 40 40 LYS HE3 H 1 2.86 . . 1 . . . . . . . . 4209 1 418 . 1 1 40 40 LYS CG C 13 25.0 . . 1 . . . . . . . . 4209 1 419 . 1 1 40 40 LYS CD C 13 28.9 . . 1 . . . . . . . . 4209 1 420 . 1 1 40 40 LYS CE C 13 41.3 . . 1 . . . . . . . . 4209 1 421 . 1 1 41 41 LEU N N 15 120.9 . . 1 . . . . . . . . 4209 1 422 . 1 1 41 41 LEU H H 1 8.56 . . 1 . . . . . . . . 4209 1 423 . 1 1 41 41 LEU CA C 13 57.1 . . 1 . . . . . . . . 4209 1 424 . 1 1 41 41 LEU HA H 1 4.06 . . 1 . . . . . . . . 4209 1 425 . 1 1 41 41 LEU CB C 13 41.8 . . 1 . . . . . . . . 4209 1 426 . 1 1 41 41 LEU HB2 H 1 1.37 . . 1 . . . . . . . . 4209 1 427 . 1 1 41 41 LEU HB3 H 1 1.91 . . 1 . . . . . . . . 4209 1 428 . 1 1 41 41 LEU HG H 1 1.80 . . 1 . . . . . . . . 4209 1 429 . 1 1 41 41 LEU HD11 H 1 0.80 . . 1 . . . . . . . . 4209 1 430 . 1 1 41 41 LEU HD12 H 1 0.80 . . 1 . . . . . . . . 4209 1 431 . 1 1 41 41 LEU HD13 H 1 0.80 . . 1 . . . . . . . . 4209 1 432 . 1 1 41 41 LEU HD21 H 1 0.80 . . 1 . . . . . . . . 4209 1 433 . 1 1 41 41 LEU HD22 H 1 0.80 . . 1 . . . . . . . . 4209 1 434 . 1 1 41 41 LEU HD23 H 1 0.80 . . 1 . . . . . . . . 4209 1 435 . 1 1 41 41 LEU CG C 13 27.1 . . 1 . . . . . . . . 4209 1 436 . 1 1 41 41 LEU CD1 C 13 23.5 . . 1 . . . . . . . . 4209 1 437 . 1 1 41 41 LEU CD2 C 13 25.5 . . 1 . . . . . . . . 4209 1 438 . 1 1 42 42 PHE N N 15 121.8 . . 1 . . . . . . . . 4209 1 439 . 1 1 42 42 PHE H H 1 8.57 . . 1 . . . . . . . . 4209 1 440 . 1 1 42 42 PHE CA C 13 61.6 . . 1 . . . . . . . . 4209 1 441 . 1 1 42 42 PHE HA H 1 4.15 . . 1 . . . . . . . . 4209 1 442 . 1 1 42 42 PHE CB C 13 39.3 . . 1 . . . . . . . . 4209 1 443 . 1 1 42 42 PHE HB2 H 1 3.16 . . 1 . . . . . . . . 4209 1 444 . 1 1 42 42 PHE HB3 H 1 3.26 . . 1 . . . . . . . . 4209 1 445 . 1 1 42 42 PHE HD1 H 1 7.07 . . 3 . . . . . . . . 4209 1 446 . 1 1 42 42 PHE HD2 H 1 7.22 . . 3 . . . . . . . . 4209 1 447 . 1 1 42 42 PHE CD1 C 13 131.1 . . 3 . . . . . . . . 4209 1 448 . 1 1 43 43 LYS N N 15 120.6 . . 1 . . . . . . . . 4209 1 449 . 1 1 43 43 LYS H H 1 8.29 . . 1 . . . . . . . . 4209 1 450 . 1 1 43 43 LYS CA C 13 58.6 . . 1 . . . . . . . . 4209 1 451 . 1 1 43 43 LYS HA H 1 3.84 . . 1 . . . . . . . . 4209 1 452 . 1 1 43 43 LYS CB C 13 31.7 . . 1 . . . . . . . . 4209 1 453 . 1 1 43 43 LYS HB2 H 1 1.82 . . 1 . . . . . . . . 4209 1 454 . 1 1 43 43 LYS HB3 H 1 1.90 . . 1 . . . . . . . . 4209 1 455 . 1 1 43 43 LYS HG2 H 1 1.47 . . 1 . . . . . . . . 4209 1 456 . 1 1 43 43 LYS HG3 H 1 1.64 . . 1 . . . . . . . . 4209 1 457 . 1 1 43 43 LYS HD2 H 1 1.64 . . 1 . . . . . . . . 4209 1 458 . 1 1 43 43 LYS HE2 H 1 2.88 . . 1 . . . . . . . . 4209 1 459 . 1 1 43 43 LYS CG C 13 25.5 . . 1 . . . . . . . . 4209 1 460 . 1 1 43 43 LYS CD C 13 28.9 . . 1 . . . . . . . . 4209 1 461 . 1 1 43 43 LYS CE C 13 41.3 . . 1 . . . . . . . . 4209 1 462 . 1 1 44 44 LYS N N 15 121.3 . . 1 . . . . . . . . 4209 1 463 . 1 1 44 44 LYS H H 1 7.80 . . 1 . . . . . . . . 4209 1 464 . 1 1 44 44 LYS CA C 13 58.3 . . 1 . . . . . . . . 4209 1 465 . 1 1 44 44 LYS HA H 1 4.01 . . 1 . . . . . . . . 4209 1 466 . 1 1 44 44 LYS CB C 13 32.4 . . 1 . . . . . . . . 4209 1 467 . 1 1 44 44 LYS HB2 H 1 1.67 . . 1 . . . . . . . . 4209 1 468 . 1 1 44 44 LYS HB3 H 1 1.76 . . 1 . . . . . . . . 4209 1 469 . 1 1 44 44 LYS HG2 H 1 1.08 . . 1 . . . . . . . . 4209 1 470 . 1 1 44 44 LYS HG3 H 1 1.23 . . 1 . . . . . . . . 4209 1 471 . 1 1 44 44 LYS HD2 H 1 1.43 . . 1 . . . . . . . . 4209 1 472 . 1 1 44 44 LYS HD3 H 1 1.52 . . 1 . . . . . . . . 4209 1 473 . 1 1 44 44 LYS HE2 H 1 2.77 . . 1 . . . . . . . . 4209 1 474 . 1 1 44 44 LYS CG C 13 24.5 . . 1 . . . . . . . . 4209 1 475 . 1 1 44 44 LYS CD C 13 28.9 . . 1 . . . . . . . . 4209 1 476 . 1 1 44 44 LYS CE C 13 41.3 . . 1 . . . . . . . . 4209 1 477 . 1 1 45 45 PHE N N 15 118.3 . . 1 . . . . . . . . 4209 1 478 . 1 1 45 45 PHE H H 1 8.10 . . 1 . . . . . . . . 4209 1 479 . 1 1 45 45 PHE CA C 13 59.1 . . 1 . . . . . . . . 4209 1 480 . 1 1 45 45 PHE HA H 1 4.45 . . 1 . . . . . . . . 4209 1 481 . 1 1 45 45 PHE CB C 13 39.3 . . 1 . . . . . . . . 4209 1 482 . 1 1 45 45 PHE HB2 H 1 2.90 . . 1 . . . . . . . . 4209 1 483 . 1 1 45 45 PHE HB3 H 1 3.16 . . 1 . . . . . . . . 4209 1 484 . 1 1 45 45 PHE HD1 H 1 7.24 . . 3 . . . . . . . . 4209 1 485 . 1 1 45 45 PHE CD1 C 13 131.6 . . 3 . . . . . . . . 4209 1 486 . 1 1 46 46 THR N N 15 110.9 . . 1 . . . . . . . . 4209 1 487 . 1 1 46 46 THR H H 1 7.52 . . 1 . . . . . . . . 4209 1 488 . 1 1 46 46 THR CA C 13 62.0 . . 1 . . . . . . . . 4209 1 489 . 1 1 46 46 THR HA H 1 4.25 . . 1 . . . . . . . . 4209 1 490 . 1 1 46 46 THR CB C 13 69.5 . . 1 . . . . . . . . 4209 1 491 . 1 1 46 46 THR HB H 1 4.09 . . 1 . . . . . . . . 4209 1 492 . 1 1 46 46 THR HG21 H 1 0.88 . . 1 . . . . . . . . 4209 1 493 . 1 1 46 46 THR HG22 H 1 0.88 . . 1 . . . . . . . . 4209 1 494 . 1 1 46 46 THR HG23 H 1 0.88 . . 1 . . . . . . . . 4209 1 495 . 1 1 46 46 THR CG2 C 13 21.4 . . 1 . . . . . . . . 4209 1 496 . 1 1 47 47 SER N N 15 119.4 . . 1 . . . . . . . . 4209 1 497 . 1 1 47 47 SER H H 1 7.65 . . 1 . . . . . . . . 4209 1 498 . 1 1 47 47 SER CA C 13 58.6 . . 1 . . . . . . . . 4209 1 499 . 1 1 47 47 SER HA H 1 4.35 . . 1 . . . . . . . . 4209 1 500 . 1 1 47 47 SER CB C 13 63.5 . . 1 . . . . . . . . 4209 1 501 . 1 1 47 47 SER HB2 H 1 3.83 . . 1 . . . . . . . . 4209 1 502 . 1 1 48 48 LYS N N 15 124.9 . . 1 . . . . . . . . 4209 1 503 . 1 1 48 48 LYS H H 1 8.13 . . 1 . . . . . . . . 4209 1 504 . 1 1 48 48 LYS CA C 13 56.2 . . 1 . . . . . . . . 4209 1 505 . 1 1 48 48 LYS HA H 1 4.27 . . 1 . . . . . . . . 4209 1 506 . 1 1 48 48 LYS CB C 13 32.7 . . 1 . . . . . . . . 4209 1 507 . 1 1 48 48 LYS HB2 H 1 1.68 . . 1 . . . . . . . . 4209 1 508 . 1 1 48 48 LYS HB3 H 1 1.80 . . 1 . . . . . . . . 4209 1 509 . 1 1 48 48 LYS HG2 H 1 1.36 . . 1 . . . . . . . . 4209 1 510 . 1 1 48 48 LYS HD2 H 1 1.61 . . 1 . . . . . . . . 4209 1 511 . 1 1 48 48 LYS CG C 13 24.5 . . 1 . . . . . . . . 4209 1 512 . 1 1 48 48 LYS CD C 13 28.9 . . 1 . . . . . . . . 4209 1 513 . 1 1 49 49 ALA N N 15 127.8 . . 1 . . . . . . . . 4209 1 514 . 1 1 49 49 ALA H H 1 8.18 . . 1 . . . . . . . . 4209 1 515 . 1 1 49 49 ALA CA C 13 52.4 . . 1 . . . . . . . . 4209 1 516 . 1 1 49 49 ALA HA H 1 4.28 . . 1 . . . . . . . . 4209 1 517 . 1 1 49 49 ALA CB C 13 19.6 . . 1 . . . . . . . . 4209 1 518 . 1 1 49 49 ALA HB1 H 1 1.31 . . 1 . . . . . . . . 4209 1 519 . 1 1 49 49 ALA HB2 H 1 1.31 . . 1 . . . . . . . . 4209 1 520 . 1 1 49 49 ALA HB3 H 1 1.31 . . 1 . . . . . . . . 4209 1 521 . 1 1 50 50 SER N N 15 122.4 . . 1 . . . . . . . . 4209 1 522 . 1 1 50 50 SER H H 1 7.74 . . 1 . . . . . . . . 4209 1 523 . 1 1 50 50 SER CA C 13 59.5 . . 1 . . . . . . . . 4209 1 524 . 1 1 50 50 SER HA H 1 4.15 . . 1 . . . . . . . . 4209 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants_set_1 _Coupling_constant_list.Sf_category coupling_constants _Coupling_constant_list.Sf_framecode coupling_constants_set_1 _Coupling_constant_list.Entry_ID 4209 _Coupling_constant_list.ID 1 _Coupling_constant_list.Sample_condition_list_ID 1 _Coupling_constant_list.Sample_condition_list_label $sample_cond_1 _Coupling_constant_list.Spectrometer_frequency_1H 500 _Coupling_constant_list.Details ; Couplings not reported are not resolved due to overlap. Residue 06 is a proline residue. Data collected at both 400 and 500 MHz ; _Coupling_constant_list.Text_data_format . _Coupling_constant_list.Text_data . loop_ _Coupling_constant_experiment.Experiment_ID _Coupling_constant_experiment.Experiment_name _Coupling_constant_experiment.Sample_ID _Coupling_constant_experiment.Sample_label _Coupling_constant_experiment.Sample_state _Coupling_constant_experiment.Entry_ID _Coupling_constant_experiment.Coupling_constant_list_ID . . 1 $sample_1 . 4209 1 stop_ loop_ _Coupling_constant.ID _Coupling_constant.Code _Coupling_constant.Assembly_atom_ID_1 _Coupling_constant.Entity_assembly_ID_1 _Coupling_constant.Entity_ID_1 _Coupling_constant.Comp_index_ID_1 _Coupling_constant.Seq_ID_1 _Coupling_constant.Comp_ID_1 _Coupling_constant.Atom_ID_1 _Coupling_constant.Atom_type_1 _Coupling_constant.Atom_isotope_number_1 _Coupling_constant.Ambiguity_code_1 _Coupling_constant.Assembly_atom_ID_2 _Coupling_constant.Entity_assembly_ID_2 _Coupling_constant.Entity_ID_2 _Coupling_constant.Comp_index_ID_2 _Coupling_constant.Seq_ID_2 _Coupling_constant.Comp_ID_2 _Coupling_constant.Atom_ID_2 _Coupling_constant.Atom_type_2 _Coupling_constant.Atom_isotope_number_2 _Coupling_constant.Ambiguity_code_2 _Coupling_constant.Val _Coupling_constant.Val_min _Coupling_constant.Val_max _Coupling_constant.Val_err _Coupling_constant.Resonance_ID_1 _Coupling_constant.Resonance_ID_2 _Coupling_constant.Auth_entity_assembly_ID_1 _Coupling_constant.Auth_seq_ID_1 _Coupling_constant.Auth_comp_ID_1 _Coupling_constant.Auth_atom_ID_1 _Coupling_constant.Auth_entity_assembly_ID_2 _Coupling_constant.Auth_seq_ID_2 _Coupling_constant.Auth_comp_ID_2 _Coupling_constant.Auth_atom_ID_2 _Coupling_constant.Details _Coupling_constant.Entry_ID _Coupling_constant.Coupling_constant_list_ID 1 3JHNHA . 1 1 4 4 ASP H . . . . 1 1 4 4 ASP HA . . . . 6 8 . . . . . . . . . . . . 4209 1 2 3JHNHA . 1 1 5 5 ASP H . . . . 1 1 5 5 ASP HA . . . . 6 8 . . . . . . . . . . . . 4209 1 3 3JHNHA . 1 1 7 7 ALA H . . . . 1 1 7 7 ALA HA . . . . . 6 . . . . . . . . . . . . 4209 1 4 3JHNHA . 1 1 8 8 LYS H . . . . 1 1 8 8 LYS HA . . . . 6 8 . . . . . . . . . . . . 4209 1 5 3JHNHA . 1 1 9 9 ALA H . . . . 1 1 9 9 ALA HA . . . . . 6 . . . . . . . . . . . . 4209 1 6 3JHNHA . 1 1 12 12 ASN H . . . . 1 1 12 12 ASN HA . . . . . 6 . . . . . . . . . . . . 4209 1 7 3JHNHA . 1 1 13 13 SER H . . . . 1 1 13 13 SER HA . . . . . 6 . . . . . . . . . . . . 4209 1 8 3JHNHA . 1 1 14 14 LEU H . . . . 1 1 14 14 LEU HA . . . . . 6 . . . . . . . . . . . . 4209 1 9 3JHNHA . 1 1 16 16 ALA H . . . . 1 1 16 16 ALA HA . . . . . 6 . . . . . . . . . . . . 4209 1 10 3JHNHA . 1 1 18 18 ALA H . . . . 1 1 18 18 ALA HA . . . . . 6 . . . . . . . . . . . . 4209 1 11 3JHNHA . 1 1 19 19 THR H . . . . 1 1 19 19 THR HA . . . . . 6 . . . . . . . . . . . . 4209 1 12 3JHNHA . 1 1 20 20 GLU H . . . . 1 1 20 20 GLU HA . . . . . 6 . . . . . . . . . . . . 4209 1 13 3JHNHA . 1 1 21 21 TYR H . . . . 1 1 21 21 TYR HA . . . . 8 . . . . . . . . . . . . . 4209 1 14 3JHNHA . 1 1 24 24 TYR H . . . . 1 1 24 24 TYR HA . . . . 6 8 . . . . . . . . . . . . 4209 1 15 3JHNHA . 1 1 28 28 MET H . . . . 1 1 28 28 MET HA . . . . . 6 . . . . . . . . . . . . 4209 1 16 3JHNHA . 1 1 31 31 VAL H . . . . 1 1 31 31 VAL HA . . . . . 6 . . . . . . . . . . . . 4209 1 17 3JHNHA . 1 1 32 32 ILE H . . . . 1 1 32 32 ILE HA . . . . . 6 . . . . . . . . . . . . 4209 1 18 3JHNHA . 1 1 35 35 ALA H . . . . 1 1 35 35 ALA HA . . . . . 6 . . . . . . . . . . . . 4209 1 19 3JHNHA . 1 1 39 39 ILE H . . . . 1 1 39 39 ILE HA . . . . . 6 . . . . . . . . . . . . 4209 1 20 3JHNHA . 1 1 40 40 LYS H . . . . 1 1 40 40 LYS HA . . . . . 6 . . . . . . . . . . . . 4209 1 21 3JHNHA . 1 1 41 41 LEU H . . . . 1 1 41 41 LEU HA . . . . . 6 . . . . . . . . . . . . 4209 1 22 3JHNHA . 1 1 42 42 PHE H . . . . 1 1 42 42 PHE HA . . . . . 6 . . . . . . . . . . . . 4209 1 23 3JHNHA . 1 1 44 44 LYS H . . . . 1 1 44 44 LYS HA . . . . . 6 . . . . . . . . . . . . 4209 1 24 3JHNHA . 1 1 45 45 PHE H . . . . 1 1 45 45 PHE HA . . . . 6 8 . . . . . . . . . . . . 4209 1 25 3JHNHA . 1 1 46 46 THR H . . . . 1 1 46 46 THR HA . . . . 8 . . . . . . . . . . . . . 4209 1 26 3JHNHA . 1 1 47 47 SER H . . . . 1 1 47 47 SER HA . . . . 6 8 . . . . . . . . . . . . 4209 1 27 3JHNHA . 1 1 48 48 LYS H . . . . 1 1 48 48 LYS HA . . . . 6 8 . . . . . . . . . . . . 4209 1 28 3JHNHA . 1 1 49 49 ALA H . . . . 1 1 49 49 ALA HA . . . . 6 8 . . . . . . . . . . . . 4209 1 29 3JHNHA . 1 1 50 50 SER H . . . . 1 1 50 50 SER HA . . . . 6 8 . . . . . . . . . . . . 4209 1 stop_ save_