data_4774 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4774 _Entry.Title ; Three-dimensional Structure of the Histidine-containing Phosphocarrier Protein (Hpr) from Enterococcus faecalis in Solution ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2000-07-03 _Entry.Accession_date 2000-07-05 _Entry.Last_release_date 2001-05-03 _Entry.Original_release_date 2001-05-03 _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 Till Maurer . . . 4774 2 Rolf Doker . . . 4774 3 Adrian Gorler . . . 4774 4 Wolfgang Hengstenberg . . . 4774 5 Hans Kalbitzer . R. . 4774 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4774 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 609 4774 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 . . 2001-05-03 2000-07-03 original author . 4774 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4774 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 21099332 _Citation.DOI . _Citation.PubMed_ID 11168402 _Citation.Full_citation . _Citation.Title ; Three-dimensional Structure of the Histidine-containing Phosphocarrier Protein (Hpr) from Enterococcus faecalis in Solution ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Eur. J. Biochem.' _Citation.Journal_name_full 'European Journal of Biochemistry' _Citation.Journal_volume 268 _Citation.Journal_issue 3 _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 635 _Citation.Page_last 644 _Citation.Year 2001 _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 Till Maurer . . . 4774 1 2 Rolf Doker . . . 4774 1 3 Adrian Gorler . . . 4774 1 4 Wolfgang Hengstenberg . . . 4774 1 5 Hans Kalbitzer . R. . 4774 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'HISTIDINE CONTAINING PHOSPHCARRIER PROTEIN' 4774 1 'ENTEROCOCCUS FAECALIS' 4774 1 NMR 4774 1 PROTEIN 4774 1 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 4774 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8421502 _Citation.Full_citation ; Jia Z, Vandonselaar M, Quail JW, Delbaere LT., Active-centre torsion-angle strain revealed in 1.6 A-resolution structure of histidine-containing phosphocarrier protein. Nature. 1993 Jan 7;361(6407):94-7. PMID: 8421502; UI: 93133294 ; _Citation.Title 'Active-centre torsion-angle strain revealed in 1.6 A-resolution structure of histidine-containing phosphocarrier protein.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Nature _Citation.Journal_name_full Nature _Citation.Journal_volume 361 _Citation.Journal_issue 6407 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0028-0836 _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 94 _Citation.Page_last 97 _Citation.Year 1993 _Citation.Details ; The histidine-containing phosphocarrier protein (HPr) is a central component of the phosphoenolpyruvate: sugar phosphotransferase system that transports carbohydrates across the cell membrane of bacteria. A typical phosphotransfer sequence is phosphoenolpyruvate-->enzyme I-->HPr-->enzyme II/IIIsugar-->sugar. This is thermodynamically favourable owing to the participation of the high-energy phosphoenolpyruvate. We report here the structure of HPr from Streptococcus faecalis determined at 1.6 A resolution. Remarkable disallowed Ramachandran torsion angles at the active centre, revealed by the X-ray structure, demonstrate a unique example of torsion-angle strain that is probably directly involved in protein function. During phosphorylation, the active-centre torsion-angle strain should facilitate the phosphotransfer reaction by lowering the activation-energy barrier. A recently reported Bacillus subtilis HPr structure, which represents the phosphorylated state of HPr with no torsion-angle strain, provides direct evidence supporting our hypothesis that torsion-angle strain plays a direct part in the function of HPr. An HPr phosphotransfer cycling mechanism is proposed, based primarily on the structures of HPr and other phosphotransferase system proteins. ; 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 Z. Jia Z. . . 4774 2 2 M. Vandonselaar M. . . 4774 2 3 'J. W.' Quail J. W. . 4774 2 4 'L. T.' Delbaere L. T. . 4774 2 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 4774 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9523711 _Citation.Full_citation ; Hahmann M, Maurer T, Lorenz M, Hengstenberg W, Glaser S, Kalbitzer HR., Structural studies of histidine-containing phosphocarrier protein from Enterococcus faecalis. Eur J Biochem. 1998 Feb 15;252(1):51-8. PMID: 9523711; UI: 98181885 ; _Citation.Title 'Structural studies of histidine-containing phosphocarrier protein from Enterococcus faecalis.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Eur. J. Biochem.' _Citation.Journal_name_full 'European journal of biochemistry / FEBS' _Citation.Journal_volume 252 _Citation.Journal_issue 1 _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 51 _Citation.Page_last 58 _Citation.Year 1998 _Citation.Details ; Based on the complete sequential assignment of the 1H-NMR spectrum by multidimensional NMR techniques the secondary structure and the local geometry of the active site of histidine-containing phosphocarrier protein (HPr) from Enterococcus faecalis were elucidated. We present a comparative analysis of the active site in the seven known structures of HPr from different organisms determined by NMR or X-ray crystallography. In catalysis, HPr is phosphorylated at the ring N61 of His15. No general agreement exists in literature regarding the structure of the active-centre loop. In the crystal structure of HPr from E. faecalis, a torsion strain of the backbone at position 16 was observed, which was assumed to be important to the catalytic mechanism. Coupling constants were determined in order to calculate phi angles to establish whether there are strained torsion angles in HPr from E. faecalis in the solution state. The evaluation of data obtained indicate a stable and well-defined structure of HPr from E. faecalis, with an overall fold similar to that found in HPr from other bacteria. We find that in the active-site region there are relatively large variations in local geometry between the evaluated structures. In HPr from E. faecalis, a particularly detailed view of the phosphate-binding His15 and residues in close spatial proximity was obtained by determination of coupling constants obtained from the double-quantum-filtered COSY spectrum. Our data indicate that in aqueous solution, in the dominant conformational state there is no torsion strain of the backbone at position 16, as observed in the crystal state. The maximum population of a strained conformation in solution can be estimated to be smaller than 23%. The analysis of the data suggests that the active-centre loop is able to adopt different conformations in solution. A similar observation was made for HPr from E. faecalis phosphorylated at its regulatory site (Ser46). 31P-NMR shows that phosphorylated HPr exists in two conformational substates with nearly equal populations. ; 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 M. Hahmann M. . . 4774 3 2 T. Maurer T. . . 4774 3 3 M. Lorenz M. . . 4774 3 4 W. Hengstenberg W. . . 4774 3 5 S. Glaser S. . . 4774 3 6 'H. R.' Kalbitzer H. R. . 4774 3 stop_ save_ save_ref_4 _Citation.Sf_category citations _Citation.Sf_framecode ref_4 _Citation.Entry_ID 4774 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8126724 _Citation.Full_citation ; Jia Z, Vandonselaar M, Hengstenberg W, Quail JW, Delbaere LT., The 1.6 A structure of histidine-containing phosphotransfer protein HPr from Streptococcus faecalis. J Mol Biol. 1994 Mar 11;236(5):1341-55. PMID: 8126724; UI: 94172632 ; _Citation.Title 'The 1.6 A structure of histidine-containing phosphotransfer protein HPr from Streptococcus faecalis.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 236 _Citation.Journal_issue 5 _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 1341 _Citation.Page_last 1355 _Citation.Year 1994 _Citation.Details ; The histidine-containing phosphocarrier protein (HPr) is a central component of the phosphoenolpyruvate: sugar phosphotransferase system (PTS) that transports carbohydrates across the cell membrane of bacteria. The three-dimensional structure of Gram-positive Streptococcus faecalis HPr has been determined using the method of multiple isomorphous replacement. The R factor for all data is 0.156 for S. faecalis HPr at 1.6 A resolution with very good geometry. The overall folding topology of HPr is a classical open-faced beta-sandwich, consisting of four antiparallel beta-strands and three alpha-helices. Remarkable disallowed Ramachandran torsion angles of Ala16 at the active center, revealed by the X-ray structure of S. faecalis HPr, demonstrate a unique example of torsion-angle strain that is likely involved directly in protein function. A brief report concerning the torsion-angle strain has been presented recently. A newly-determined pH 7.0 structure is shown to have the same open conformation of the active center and the same torsion-angle strain at Ala16, suggesting that pH is not responsible for the structural observations. The current structure suggests a role for residues 12 and 51 in HPr's function, since they are involved in the active center through direct and indirect hydrogen-bonding interactions with the imidazole ring of His15. It is found that Ser46, the regulatory site in HPr from Gram-positive bacteria, N-caps the minor alpha-B helix and is also involved in the Asn43-Ser46 beta-turn. This finding, in conjunction with the proposed routes of communication between the regulatory site Ser46 and the active center in S. faecalis HPr, provides new insight into the understanding of how Ser46 might function. The putative involvement of the C-terminal alpha-carboxyl group and the related Gly67-Glu70 reverse beta-turn with respect to the function of HPr are described. ; 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 Z. Jia Z. . . 4774 4 2 M. Vandonselaar M. . . 4774 4 3 W. Hengstenberg W. . . 4774 4 4 'J. W.' Quail J. W. . 4774 4 5 'L. T.' Delbaere L. T. . 4774 4 stop_ save_ save_ref_5 _Citation.Sf_category citations _Citation.Sf_framecode ref_5 _Citation.Entry_ID 4774 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9367762 _Citation.Full_citation ; GUNTERT, P., MUMENTHALER, C. & WUTHRICH, K. (1997). Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273, 283-298. ; _Citation.Title 'Torsion angle dynamics for NMR structure calculation with the new program DYANA.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 273 _Citation.Journal_issue 1 _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 283 _Citation.Page_last 298 _Citation.Year 1997 _Citation.Details ; The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the "bundle" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures. ; 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. Guntert P. . . 4774 5 2 C. Mumenthaler C. . . 4774 5 3 K. Wuthrich K. . . 4774 5 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_HPr _Assembly.Sf_category assembly _Assembly.Sf_framecode system_HPr _Assembly.Entry_ID 4774 _Assembly.ID 1 _Assembly.Name 'PHOSPHOCARRIER PROTEIN HPR' _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 4774 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 HPr 1 $HPr . . . native . . . . . 4774 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1QFR . . . . . 'STRUCTURE HAS BEEN REFINED' 4774 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'PHOSPHOCARRIER PROTEIN HPR' system 4774 1 HPr abbreviation 4774 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'PHOSPHATE GROUP TRANSLOCATION IN CARBOHYDRATE TRANSPORT' 4774 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_HPr _Entity.Sf_category entity _Entity.Sf_framecode HPr _Entity.Entry_ID 4774 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'HISTIDINE CONTAINING PHOSPHCARRIER 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 ; MEKKEFHIVAETGIHARPAT LLVQTASKFNSDINLEYKGK SVNLKSIMGVMSLGVGQGSD VTITVDGADEAEGMAAIVET LQKEGLAEQ ; _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 89 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-29 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 PDB 1FU0 . "Crystal Structure Analysis Of The Phospho-Serine 46 Hpr From Enterococcus Faecalis" . . . . . 97.75 87 98.85 98.85 2.03e-53 . . . . 4774 1 2 no PDB 1PTF . "The 1.6 Angstroms Structure Of Histidine-Containing Phosphotransfer Protein Hpr From Streptococcus Faecalis" . . . . . 98.88 88 100.00 100.00 7.63e-55 . . . . 4774 1 3 no PDB 1QFR . "Nmr Solution Structure Of Phosphocarrier Protein Hpr From Enterococcus Faecalis" . . . . . 98.88 89 100.00 100.00 7.28e-55 . . . . 4774 1 4 no EMBL CAA79533 . "HPr [Enterococcus faecalis]" . . . . . 98.88 88 100.00 100.00 7.63e-55 . . . . 4774 1 5 no EMBL CBL32713 . "Phosphotransferase System HPr (HPr) Family [Enterococcus sp. 7L76]" . . . . . 98.88 88 100.00 100.00 7.63e-55 . . . . 4774 1 6 no EMBL CCO71634 . "phosphocarrier protein HPr [Enterococcus faecalis str. Symbioflor 1]" . . . . . 98.88 88 100.00 100.00 7.63e-55 . . . . 4774 1 7 no GB AAO80530 . "phosphocarrier protein HPr [Enterococcus faecalis V583]" . . . . . 98.88 88 100.00 100.00 7.63e-55 . . . . 4774 1 8 no GB ADX79343 . "phosphocarrier protein HPr [Enterococcus faecalis 62]" . . . . . 98.88 88 100.00 100.00 7.63e-55 . . . . 4774 1 9 no GB AEA93134 . "PTS family porter, phosphocarrier protein HPR [Enterococcus faecalis OG1RF]" . . . . . 98.88 88 100.00 100.00 7.63e-55 . . . . 4774 1 10 no GB AFO43418 . "phosphocarrier protein HPr [Enterococcus faecalis D32]" . . . . . 98.88 88 100.00 100.00 7.63e-55 . . . . 4774 1 11 no GB AHI39812 . "Phosphocarrier protein HPr [Enterococcus faecalis DENG1]" . . . . . 98.88 88 100.00 100.00 7.63e-55 . . . . 4774 1 12 no REF NP_814460 . "phosphocarrier protein HPr [Enterococcus faecalis V583]" . . . . . 98.88 88 100.00 100.00 7.63e-55 . . . . 4774 1 13 no REF WP_002355551 . "MULTISPECIES: phosphocarrier protein HPr [Enterococcus]" . . . . . 98.88 88 100.00 100.00 7.63e-55 . . . . 4774 1 14 no REF WP_002358685 . "phosphocarrier protein HPr [Enterococcus faecalis]" . . . . . 98.88 88 98.86 100.00 2.24e-54 . . . . 4774 1 15 no REF WP_002388527 . "phosphocarrier protein HPr [Enterococcus faecalis]" . . . . . 98.88 88 98.86 98.86 1.51e-53 . . . . 4774 1 16 no REF WP_010776971 . "phosphocarrier protein HPr [Enterococcus faecalis]" . . . . . 98.88 88 98.86 98.86 7.44e-54 . . . . 4774 1 17 no SP P07515 . "RecName: Full=Phosphocarrier protein HPr; AltName: Full=Histidine-containing protein [Enterococcus faecalis V583]" . . . . . 98.88 88 100.00 100.00 7.63e-55 . . . . 4774 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'HISTIDINE CONTAINING PHOSPHCARRIER PROTEIN' common 4774 1 HPr abbreviation 4774 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 . MET . 4774 1 2 . GLU . 4774 1 3 . LYS . 4774 1 4 . LYS . 4774 1 5 . GLU . 4774 1 6 . PHE . 4774 1 7 . HIS . 4774 1 8 . ILE . 4774 1 9 . VAL . 4774 1 10 . ALA . 4774 1 11 . GLU . 4774 1 12 . THR . 4774 1 13 . GLY . 4774 1 14 . ILE . 4774 1 15 . HIS . 4774 1 16 . ALA . 4774 1 17 . ARG . 4774 1 18 . PRO . 4774 1 19 . ALA . 4774 1 20 . THR . 4774 1 21 . LEU . 4774 1 22 . LEU . 4774 1 23 . VAL . 4774 1 24 . GLN . 4774 1 25 . THR . 4774 1 26 . ALA . 4774 1 27 . SER . 4774 1 28 . LYS . 4774 1 29 . PHE . 4774 1 30 . ASN . 4774 1 31 . SER . 4774 1 32 . ASP . 4774 1 33 . ILE . 4774 1 34 . ASN . 4774 1 35 . LEU . 4774 1 36 . GLU . 4774 1 37 . TYR . 4774 1 38 . LYS . 4774 1 39 . GLY . 4774 1 40 . LYS . 4774 1 41 . SER . 4774 1 42 . VAL . 4774 1 43 . ASN . 4774 1 44 . LEU . 4774 1 45 . LYS . 4774 1 46 . SER . 4774 1 47 . ILE . 4774 1 48 . MET . 4774 1 49 . GLY . 4774 1 50 . VAL . 4774 1 51 . MET . 4774 1 52 . SER . 4774 1 53 . LEU . 4774 1 54 . GLY . 4774 1 55 . VAL . 4774 1 56 . GLY . 4774 1 57 . GLN . 4774 1 58 . GLY . 4774 1 59 . SER . 4774 1 60 . ASP . 4774 1 61 . VAL . 4774 1 62 . THR . 4774 1 63 . ILE . 4774 1 64 . THR . 4774 1 65 . VAL . 4774 1 66 . ASP . 4774 1 67 . GLY . 4774 1 68 . ALA . 4774 1 69 . ASP . 4774 1 70 . GLU . 4774 1 71 . ALA . 4774 1 72 . GLU . 4774 1 73 . GLY . 4774 1 74 . MET . 4774 1 75 . ALA . 4774 1 76 . ALA . 4774 1 77 . ILE . 4774 1 78 . VAL . 4774 1 79 . GLU . 4774 1 80 . THR . 4774 1 81 . LEU . 4774 1 82 . GLN . 4774 1 83 . LYS . 4774 1 84 . GLU . 4774 1 85 . GLY . 4774 1 86 . LEU . 4774 1 87 . ALA . 4774 1 88 . GLU . 4774 1 89 . GLN . 4774 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 . MET 1 1 4774 1 . GLU 2 2 4774 1 . LYS 3 3 4774 1 . LYS 4 4 4774 1 . GLU 5 5 4774 1 . PHE 6 6 4774 1 . HIS 7 7 4774 1 . ILE 8 8 4774 1 . VAL 9 9 4774 1 . ALA 10 10 4774 1 . GLU 11 11 4774 1 . THR 12 12 4774 1 . GLY 13 13 4774 1 . ILE 14 14 4774 1 . HIS 15 15 4774 1 . ALA 16 16 4774 1 . ARG 17 17 4774 1 . PRO 18 18 4774 1 . ALA 19 19 4774 1 . THR 20 20 4774 1 . LEU 21 21 4774 1 . LEU 22 22 4774 1 . VAL 23 23 4774 1 . GLN 24 24 4774 1 . THR 25 25 4774 1 . ALA 26 26 4774 1 . SER 27 27 4774 1 . LYS 28 28 4774 1 . PHE 29 29 4774 1 . ASN 30 30 4774 1 . SER 31 31 4774 1 . ASP 32 32 4774 1 . ILE 33 33 4774 1 . ASN 34 34 4774 1 . LEU 35 35 4774 1 . GLU 36 36 4774 1 . TYR 37 37 4774 1 . LYS 38 38 4774 1 . GLY 39 39 4774 1 . LYS 40 40 4774 1 . SER 41 41 4774 1 . VAL 42 42 4774 1 . ASN 43 43 4774 1 . LEU 44 44 4774 1 . LYS 45 45 4774 1 . SER 46 46 4774 1 . ILE 47 47 4774 1 . MET 48 48 4774 1 . GLY 49 49 4774 1 . VAL 50 50 4774 1 . MET 51 51 4774 1 . SER 52 52 4774 1 . LEU 53 53 4774 1 . GLY 54 54 4774 1 . VAL 55 55 4774 1 . GLY 56 56 4774 1 . GLN 57 57 4774 1 . GLY 58 58 4774 1 . SER 59 59 4774 1 . ASP 60 60 4774 1 . VAL 61 61 4774 1 . THR 62 62 4774 1 . ILE 63 63 4774 1 . THR 64 64 4774 1 . VAL 65 65 4774 1 . ASP 66 66 4774 1 . GLY 67 67 4774 1 . ALA 68 68 4774 1 . ASP 69 69 4774 1 . GLU 70 70 4774 1 . ALA 71 71 4774 1 . GLU 72 72 4774 1 . GLY 73 73 4774 1 . MET 74 74 4774 1 . ALA 75 75 4774 1 . ALA 76 76 4774 1 . ILE 77 77 4774 1 . VAL 78 78 4774 1 . GLU 79 79 4774 1 . THR 80 80 4774 1 . LEU 81 81 4774 1 . GLN 82 82 4774 1 . LYS 83 83 4774 1 . GLU 84 84 4774 1 . GLY 85 85 4774 1 . LEU 86 86 4774 1 . ALA 87 87 4774 1 . GLU 88 88 4774 1 . GLN 89 89 4774 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 4774 _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 $HPr . 1351 organism . 'Enterococcus faecalis' . . . Eubacteria Firmicutes Enterococcus faecalis 26487 . . . . . . . . . . . . . . . . . . . . 4774 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 4774 _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 $HPr . 'purified from the natural source' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4774 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4774 _Sample.ID 1 _Sample.Type solution _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 'HISTIDINE CONTAINING PHOSPHCARRIER PROTEIN' . . . 1 $HPr . . 5.0 . . mM . . . . 4774 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 4774 _Sample_condition_list.ID 1 _Sample_condition_list.Details . 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 7.4 0.2 n/a 4774 1 temperature 298 3 K 4774 1 pressure 1 . atm 4774 1 stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Software.Sf_category software _Software.Sf_framecode DYANA _Software.Entry_ID 4774 _Software.ID 1 _Software.Name DYANA _Software.Version 1.5 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'STRUCTURE CALCULATION, REFINEMENT' 4774 1 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 5 $ref_5 4774 1 stop_ save_ save_XWINNMR _Software.Sf_category software _Software.Sf_framecode XWINNMR _Software.Entry_ID 4774 _Software.ID 2 _Software.Name XWINNMR _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Data processing' 4774 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 4774 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 4774 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4774 _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 DRX . 500 . . . 4774 1 2 NMR_spectrometer_2 Bruker DMX . 800 . . . 4774 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 4774 _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 NOESY . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 4774 1 2 COSY . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 4774 1 3 TOCSY . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 4774 1 4 NOESY-TOCSY . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 4774 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 4774 _NMR_spec_expt.ID 1 _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_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 4774 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name 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_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 4774 _NMR_spec_expt.ID 3 _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_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 4774 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name NOESY-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_ #################### # 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 4774 _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 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct . . . . . . . . . . 4774 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_set_1 _Assigned_chem_shift_list.Entry_ID 4774 _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 NOESY 1 $sample_1 . 4774 1 2 COSY 1 $sample_1 . 4774 1 3 TOCSY 1 $sample_1 . 4774 1 4 NOESY-TOCSY 1 $sample_1 . 4774 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 MET HA H 1 4.45 0.05 . 1 . . . . . . . . 4774 1 2 . 1 1 1 1 MET HB3 H 1 2.23 0.05 . 1 . . . . . . . . 4774 1 3 . 1 1 1 1 MET HB2 H 1 2.29 0.05 . 1 . . . . . . . . 4774 1 4 . 1 1 1 1 MET HG3 H 1 2.13 0.05 . 1 . . . . . . . . 4774 1 5 . 1 1 1 1 MET HG2 H 1 2.13 0.05 . 1 . . . . . . . . 4774 1 6 . 1 1 2 2 GLU HA H 1 4.54 0.05 . 1 . . . . . . . . 4774 1 7 . 1 1 2 2 GLU H H 1 9.16 0.05 . 1 . . . . . . . . 4774 1 8 . 1 1 2 2 GLU HB3 H 1 1.63 0.05 . 1 . . . . . . . . 4774 1 9 . 1 1 2 2 GLU HB2 H 1 1.63 0.05 . 1 . . . . . . . . 4774 1 10 . 1 1 2 2 GLU HG3 H 1 1.96 0.05 . 1 . . . . . . . . 4774 1 11 . 1 1 2 2 GLU HG2 H 1 1.96 0.05 . 1 . . . . . . . . 4774 1 12 . 1 1 3 3 LYS HA H 1 5.22 0.05 . 1 . . . . . . . . 4774 1 13 . 1 1 3 3 LYS H H 1 8.63 0.05 . 1 . . . . . . . . 4774 1 14 . 1 1 3 3 LYS HB3 H 1 1.56 0.05 . 1 . . . . . . . . 4774 1 15 . 1 1 3 3 LYS HB2 H 1 1.66 0.05 . 1 . . . . . . . . 4774 1 16 . 1 1 3 3 LYS HG3 H 1 1.31 0.05 . 1 . . . . . . . . 4774 1 17 . 1 1 3 3 LYS HG2 H 1 1.13 0.05 . 1 . . . . . . . . 4774 1 18 . 1 1 3 3 LYS HD3 H 1 1.11 0.05 . 1 . . . . . . . . 4774 1 19 . 1 1 3 3 LYS HD2 H 1 1.11 0.05 . 1 . . . . . . . . 4774 1 20 . 1 1 3 3 LYS HE2 H 1 2.92 0.05 . 1 . . . . . . . . 4774 1 21 . 1 1 3 3 LYS HE3 H 1 2.92 0.05 . 1 . . . . . . . . 4774 1 22 . 1 1 4 4 LYS H H 1 8.69 0.05 . 1 . . . . . . . . 4774 1 23 . 1 1 4 4 LYS HA H 1 4.34 0.05 . 1 . . . . . . . . 4774 1 24 . 1 1 4 4 LYS HB3 H 1 1.28 0.05 . 1 . . . . . . . . 4774 1 25 . 1 1 4 4 LYS HB2 H 1 1.20 0.05 . 1 . . . . . . . . 4774 1 26 . 1 1 4 4 LYS HG3 H 1 1.45 0.05 . 1 . . . . . . . . 4774 1 27 . 1 1 4 4 LYS HG2 H 1 1.45 0.05 . 1 . . . . . . . . 4774 1 28 . 1 1 4 4 LYS HD3 H 1 1.23 0.05 . 1 . . . . . . . . 4774 1 29 . 1 1 4 4 LYS HD2 H 1 1.23 0.05 . 1 . . . . . . . . 4774 1 30 . 1 1 4 4 LYS HE3 H 1 2.87 0.05 . 1 . . . . . . . . 4774 1 31 . 1 1 4 4 LYS HE2 H 1 2.92 0.05 . 1 . . . . . . . . 4774 1 32 . 1 1 5 5 GLU H H 1 7.89 0.05 . 1 . . . . . . . . 4774 1 33 . 1 1 5 5 GLU HA H 1 5.12 0.05 . 1 . . . . . . . . 4774 1 34 . 1 1 5 5 GLU HB3 H 1 1.71 0.05 . 1 . . . . . . . . 4774 1 35 . 1 1 5 5 GLU HB2 H 1 2.19 0.05 . 1 . . . . . . . . 4774 1 36 . 1 1 5 5 GLU HG3 H 1 2.06 0.05 . 1 . . . . . . . . 4774 1 37 . 1 1 5 5 GLU HG2 H 1 1.89 0.05 . 1 . . . . . . . . 4774 1 38 . 1 1 6 6 PHE H H 1 9.14 0.05 . 1 . . . . . . . . 4774 1 39 . 1 1 6 6 PHE HA H 1 4.82 0.05 . 1 . . . . . . . . 4774 1 40 . 1 1 6 6 PHE HB3 H 1 2.34 0.05 . 1 . . . . . . . . 4774 1 41 . 1 1 6 6 PHE HB2 H 1 2.77 0.05 . 1 . . . . . . . . 4774 1 42 . 1 1 6 6 PHE HD1 H 1 6.95 0.05 . 1 . . . . . . . . 4774 1 43 . 1 1 6 6 PHE HD2 H 1 6.94 0.05 . 1 . . . . . . . . 4774 1 44 . 1 1 6 6 PHE HE1 H 1 7.03 0.05 . 1 . . . . . . . . 4774 1 45 . 1 1 6 6 PHE HE2 H 1 7.03 0.05 . 1 . . . . . . . . 4774 1 46 . 1 1 6 6 PHE HZ H 1 7.02 0.05 . 1 . . . . . . . . 4774 1 47 . 1 1 7 7 HIS H H 1 9.10 0.05 . 1 . . . . . . . . 4774 1 48 . 1 1 7 7 HIS HA H 1 5.40 0.05 . 1 . . . . . . . . 4774 1 49 . 1 1 7 7 HIS HB3 H 1 3.24 0.05 . 1 . . . . . . . . 4774 1 50 . 1 1 7 7 HIS HB2 H 1 2.92 0.05 . 1 . . . . . . . . 4774 1 51 . 1 1 7 7 HIS HD2 H 1 6.73 0.05 . 1 . . . . . . . . 4774 1 52 . 1 1 7 7 HIS HE1 H 1 8.00 0.05 . 1 . . . . . . . . 4774 1 53 . 1 1 8 8 ILE H H 1 9.10 0.05 . 1 . . . . . . . . 4774 1 54 . 1 1 8 8 ILE HA H 1 4.57 0.05 . 1 . . . . . . . . 4774 1 55 . 1 1 8 8 ILE HG12 H 1 1.68 0.05 . 1 . . . . . . . . 4774 1 56 . 1 1 8 8 ILE HG13 H 1 1.74 0.05 . 1 . . . . . . . . 4774 1 57 . 1 1 8 8 ILE HB H 1 2.15 0.05 . 1 . . . . . . . . 4774 1 58 . 1 1 8 8 ILE HG21 H 1 0.76 0.05 . 1 . . . . . . . . 4774 1 59 . 1 1 8 8 ILE HG22 H 1 0.76 0.05 . 1 . . . . . . . . 4774 1 60 . 1 1 8 8 ILE HG23 H 1 0.76 0.05 . 1 . . . . . . . . 4774 1 61 . 1 1 8 8 ILE HD11 H 1 0.40 0.05 . 1 . . . . . . . . 4774 1 62 . 1 1 8 8 ILE HD12 H 1 0.40 0.05 . 1 . . . . . . . . 4774 1 63 . 1 1 8 8 ILE HD13 H 1 0.40 0.05 . 1 . . . . . . . . 4774 1 64 . 1 1 9 9 VAL H H 1 8.29 0.05 . 1 . . . . . . . . 4774 1 65 . 1 1 9 9 VAL HA H 1 4.42 0.05 . 1 . . . . . . . . 4774 1 66 . 1 1 9 9 VAL HB H 1 2.30 0.05 . 1 . . . . . . . . 4774 1 67 . 1 1 9 9 VAL HG11 H 1 0.98 0.05 . 1 . . . . . . . . 4774 1 68 . 1 1 9 9 VAL HG12 H 1 0.98 0.05 . 1 . . . . . . . . 4774 1 69 . 1 1 9 9 VAL HG13 H 1 0.98 0.05 . 1 . . . . . . . . 4774 1 70 . 1 1 9 9 VAL HG21 H 1 0.67 0.05 . 1 . . . . . . . . 4774 1 71 . 1 1 9 9 VAL HG22 H 1 0.67 0.05 . 1 . . . . . . . . 4774 1 72 . 1 1 9 9 VAL HG23 H 1 0.67 0.05 . 1 . . . . . . . . 4774 1 73 . 1 1 10 10 ALA H H 1 6.63 0.05 . 1 . . . . . . . . 4774 1 74 . 1 1 10 10 ALA HA H 1 4.27 0.05 . 1 . . . . . . . . 4774 1 75 . 1 1 10 10 ALA HB1 H 1 1.45 0.05 . 1 . . . . . . . . 4774 1 76 . 1 1 10 10 ALA HB2 H 1 1.45 0.05 . 1 . . . . . . . . 4774 1 77 . 1 1 10 10 ALA HB3 H 1 1.45 0.05 . 1 . . . . . . . . 4774 1 78 . 1 1 11 11 GLU H H 1 9.02 0.05 . 1 . . . . . . . . 4774 1 79 . 1 1 11 11 GLU HA H 1 3.82 0.05 . 1 . . . . . . . . 4774 1 80 . 1 1 11 11 GLU HB3 H 1 2.04 0.05 . 1 . . . . . . . . 4774 1 81 . 1 1 11 11 GLU HB2 H 1 2.02 0.05 . 1 . . . . . . . . 4774 1 82 . 1 1 11 11 GLU HG3 H 1 2.31 0.05 . 1 . . . . . . . . 4774 1 83 . 1 1 11 11 GLU HG2 H 1 2.31 0.05 . 1 . . . . . . . . 4774 1 84 . 1 1 12 12 THR H H 1 7.70 0.05 . 1 . . . . . . . . 4774 1 85 . 1 1 12 12 THR HA H 1 3.47 0.05 . 1 . . . . . . . . 4774 1 86 . 1 1 12 12 THR HB H 1 4.25 0.05 . 1 . . . . . . . . 4774 1 87 . 1 1 12 12 THR HG21 H 1 1.41 0.05 . 1 . . . . . . . . 4774 1 88 . 1 1 12 12 THR HG22 H 1 1.41 0.05 . 1 . . . . . . . . 4774 1 89 . 1 1 12 12 THR HG23 H 1 1.41 0.05 . 1 . . . . . . . . 4774 1 90 . 1 1 13 13 GLY H H 1 7.70 0.05 . 1 . . . . . . . . 4774 1 91 . 1 1 13 13 GLY HA3 H 1 3.02 0.05 . 1 . . . . . . . . 4774 1 92 . 1 1 13 13 GLY HA2 H 1 4.20 0.05 . 1 . . . . . . . . 4774 1 93 . 1 1 14 14 ILE H H 1 8.06 0.05 . 1 . . . . . . . . 4774 1 94 . 1 1 14 14 ILE HA H 1 3.87 0.05 . 1 . . . . . . . . 4774 1 95 . 1 1 14 14 ILE HG12 H 1 1.26 0.05 . 1 . . . . . . . . 4774 1 96 . 1 1 14 14 ILE HG13 H 1 1.26 0.05 . 1 . . . . . . . . 4774 1 97 . 1 1 14 14 ILE HB H 1 1.81 0.05 . 1 . . . . . . . . 4774 1 98 . 1 1 14 14 ILE HG21 H 1 0.49 0.05 . 1 . . . . . . . . 4774 1 99 . 1 1 14 14 ILE HG22 H 1 0.49 0.05 . 1 . . . . . . . . 4774 1 100 . 1 1 14 14 ILE HG23 H 1 0.49 0.05 . 1 . . . . . . . . 4774 1 101 . 1 1 14 14 ILE HD11 H 1 0.59 0.05 . 1 . . . . . . . . 4774 1 102 . 1 1 14 14 ILE HD12 H 1 0.59 0.05 . 1 . . . . . . . . 4774 1 103 . 1 1 14 14 ILE HD13 H 1 0.59 0.05 . 1 . . . . . . . . 4774 1 104 . 1 1 15 15 HIS H H 1 6.97 0.05 . 1 . . . . . . . . 4774 1 105 . 1 1 15 15 HIS HA H 1 4.56 0.05 . 1 . . . . . . . . 4774 1 106 . 1 1 15 15 HIS HB2 H 1 3.17 0.05 . 1 . . . . . . . . 4774 1 107 . 1 1 15 15 HIS HB3 H 1 2.98 0.05 . 1 . . . . . . . . 4774 1 108 . 1 1 15 15 HIS HD2 H 1 7.07 0.05 . 1 . . . . . . . . 4774 1 109 . 1 1 15 15 HIS HE1 H 1 7.61 0.05 . 1 . . . . . . . . 4774 1 110 . 1 1 16 16 ALA H H 1 8.23 0.05 . 1 . . . . . . . . 4774 1 111 . 1 1 16 16 ALA HA H 1 3.99 0.05 . 1 . . . . . . . . 4774 1 112 . 1 1 16 16 ALA HB1 H 1 1.47 0.05 . 1 . . . . . . . . 4774 1 113 . 1 1 16 16 ALA HB2 H 1 1.47 0.05 . 1 . . . . . . . . 4774 1 114 . 1 1 16 16 ALA HB3 H 1 1.47 0.05 . 1 . . . . . . . . 4774 1 115 . 1 1 17 17 ARG H H 1 8.32 0.05 . 1 . . . . . . . . 4774 1 116 . 1 1 17 17 ARG HA H 1 4.23 0.05 . 1 . . . . . . . . 4774 1 117 . 1 1 17 17 ARG HB3 H 1 1.89 0.05 . 1 . . . . . . . . 4774 1 118 . 1 1 17 17 ARG HB2 H 1 1.89 0.05 . 1 . . . . . . . . 4774 1 119 . 1 1 17 17 ARG HG3 H 1 1.62 0.05 . 1 . . . . . . . . 4774 1 120 . 1 1 17 17 ARG HG2 H 1 1.62 0.05 . 1 . . . . . . . . 4774 1 121 . 1 1 17 17 ARG HD3 H 1 3.66 0.05 . 1 . . . . . . . . 4774 1 122 . 1 1 17 17 ARG HD2 H 1 3.14 0.05 . 1 . . . . . . . . 4774 1 123 . 1 1 18 18 PRO HA H 1 3.84 0.05 . 1 . . . . . . . . 4774 1 124 . 1 1 18 18 PRO HB3 H 1 1.96 0.05 . 1 . . . . . . . . 4774 1 125 . 1 1 18 18 PRO HB2 H 1 2.01 0.05 . 1 . . . . . . . . 4774 1 126 . 1 1 18 18 PRO HG3 H 1 2.10 0.05 . 1 . . . . . . . . 4774 1 127 . 1 1 18 18 PRO HG2 H 1 1.96 0.05 . 1 . . . . . . . . 4774 1 128 . 1 1 18 18 PRO HD2 H 1 3.39 0.05 . 1 . . . . . . . . 4774 1 129 . 1 1 18 18 PRO HD3 H 1 3.50 0.05 . 1 . . . . . . . . 4774 1 130 . 1 1 19 19 ALA H H 1 7.89 0.05 . 1 . . . . . . . . 4774 1 131 . 1 1 19 19 ALA HA H 1 4.04 0.05 . 1 . . . . . . . . 4774 1 132 . 1 1 19 19 ALA HB1 H 1 1.12 0.05 . 1 . . . . . . . . 4774 1 133 . 1 1 19 19 ALA HB2 H 1 1.12 0.05 . 1 . . . . . . . . 4774 1 134 . 1 1 19 19 ALA HB3 H 1 1.12 0.05 . 1 . . . . . . . . 4774 1 135 . 1 1 20 20 THR H H 1 7.88 0.05 . 1 . . . . . . . . 4774 1 136 . 1 1 20 20 THR HA H 1 3.65 0.05 . 1 . . . . . . . . 4774 1 137 . 1 1 20 20 THR HB H 1 4.33 0.05 . 1 . . . . . . . . 4774 1 138 . 1 1 20 20 THR HG21 H 1 1.12 0.05 . 1 . . . . . . . . 4774 1 139 . 1 1 20 20 THR HG22 H 1 1.12 0.05 . 1 . . . . . . . . 4774 1 140 . 1 1 20 20 THR HG23 H 1 1.12 0.05 . 1 . . . . . . . . 4774 1 141 . 1 1 21 21 LEU H H 1 7.82 0.05 . 1 . . . . . . . . 4774 1 142 . 1 1 21 21 LEU HA H 1 3.99 0.05 . 1 . . . . . . . . 4774 1 143 . 1 1 21 21 LEU HB3 H 1 1.57 0.05 . 1 . . . . . . . . 4774 1 144 . 1 1 21 21 LEU HB2 H 1 1.63 0.05 . 1 . . . . . . . . 4774 1 145 . 1 1 21 21 LEU HG H 1 2.10 0.05 . 1 . . . . . . . . 4774 1 146 . 1 1 21 21 LEU HD11 H 1 0.73 0.05 . 1 . . . . . . . . 4774 1 147 . 1 1 21 21 LEU HD12 H 1 0.73 0.05 . 1 . . . . . . . . 4774 1 148 . 1 1 21 21 LEU HD13 H 1 0.73 0.05 . 1 . . . . . . . . 4774 1 149 . 1 1 21 21 LEU HD21 H 1 0.73 0.05 . 1 . . . . . . . . 4774 1 150 . 1 1 21 21 LEU HD22 H 1 0.73 0.05 . 1 . . . . . . . . 4774 1 151 . 1 1 21 21 LEU HD23 H 1 0.73 0.05 . 1 . . . . . . . . 4774 1 152 . 1 1 22 22 LEU H H 1 8.22 0.05 . 1 . . . . . . . . 4774 1 153 . 1 1 22 22 LEU HA H 1 3.91 0.05 . 1 . . . . . . . . 4774 1 154 . 1 1 22 22 LEU HB3 H 1 1.49 0.05 . 1 . . . . . . . . 4774 1 155 . 1 1 22 22 LEU HB2 H 1 1.49 0.05 . 1 . . . . . . . . 4774 1 156 . 1 1 22 22 LEU HG H 1 1.68 0.05 . 1 . . . . . . . . 4774 1 157 . 1 1 22 22 LEU HD11 H 1 0.61 0.05 . 1 . . . . . . . . 4774 1 158 . 1 1 22 22 LEU HD12 H 1 0.61 0.05 . 1 . . . . . . . . 4774 1 159 . 1 1 22 22 LEU HD13 H 1 0.61 0.05 . 1 . . . . . . . . 4774 1 160 . 1 1 22 22 LEU HD21 H 1 0.66 0.05 . 1 . . . . . . . . 4774 1 161 . 1 1 22 22 LEU HD22 H 1 0.66 0.05 . 1 . . . . . . . . 4774 1 162 . 1 1 22 22 LEU HD23 H 1 0.66 0.05 . 1 . . . . . . . . 4774 1 163 . 1 1 23 23 VAL H H 1 8.14 0.05 . 1 . . . . . . . . 4774 1 164 . 1 1 23 23 VAL HA H 1 4.13 0.05 . 1 . . . . . . . . 4774 1 165 . 1 1 23 23 VAL HB H 1 1.83 0.05 . 1 . . . . . . . . 4774 1 166 . 1 1 23 23 VAL HG11 H 1 0.93 0.05 . 1 . . . . . . . . 4774 1 167 . 1 1 23 23 VAL HG12 H 1 0.93 0.05 . 1 . . . . . . . . 4774 1 168 . 1 1 23 23 VAL HG13 H 1 0.93 0.05 . 1 . . . . . . . . 4774 1 169 . 1 1 23 23 VAL HG21 H 1 0.74 0.05 . 1 . . . . . . . . 4774 1 170 . 1 1 23 23 VAL HG22 H 1 0.74 0.05 . 1 . . . . . . . . 4774 1 171 . 1 1 23 23 VAL HG23 H 1 0.74 0.05 . 1 . . . . . . . . 4774 1 172 . 1 1 24 24 GLN H H 1 8.41 0.05 . 1 . . . . . . . . 4774 1 173 . 1 1 24 24 GLN HA H 1 3.98 0.05 . 1 . . . . . . . . 4774 1 174 . 1 1 24 24 GLN HB3 H 1 2.47 0.05 . 1 . . . . . . . . 4774 1 175 . 1 1 24 24 GLN HB2 H 1 2.24 0.05 . 1 . . . . . . . . 4774 1 176 . 1 1 24 24 GLN HG3 H 1 2.52 0.05 . 1 . . . . . . . . 4774 1 177 . 1 1 24 24 GLN HG2 H 1 2.52 0.05 . 1 . . . . . . . . 4774 1 178 . 1 1 25 25 THR H H 1 8.10 0.05 . 1 . . . . . . . . 4774 1 179 . 1 1 25 25 THR HA H 1 3.84 0.05 . 1 . . . . . . . . 4774 1 180 . 1 1 25 25 THR HB H 1 4.32 0.05 . 1 . . . . . . . . 4774 1 181 . 1 1 25 25 THR HG21 H 1 1.17 0.05 . 1 . . . . . . . . 4774 1 182 . 1 1 25 25 THR HG22 H 1 1.17 0.05 . 1 . . . . . . . . 4774 1 183 . 1 1 25 25 THR HG23 H 1 1.17 0.05 . 1 . . . . . . . . 4774 1 184 . 1 1 26 26 ALA H H 1 8.41 0.05 . 1 . . . . . . . . 4774 1 185 . 1 1 26 26 ALA HA H 1 3.86 0.05 . 1 . . . . . . . . 4774 1 186 . 1 1 26 26 ALA HB1 H 1 1.27 0.05 . 1 . . . . . . . . 4774 1 187 . 1 1 26 26 ALA HB2 H 1 1.27 0.05 . 1 . . . . . . . . 4774 1 188 . 1 1 26 26 ALA HB3 H 1 1.27 0.05 . 1 . . . . . . . . 4774 1 189 . 1 1 27 27 SER H H 1 8.11 0.05 . 1 . . . . . . . . 4774 1 190 . 1 1 27 27 SER HA H 1 3.89 0.05 . 1 . . . . . . . . 4774 1 191 . 1 1 27 27 SER HB3 H 1 4.15 0.05 . 1 . . . . . . . . 4774 1 192 . 1 1 27 27 SER HB2 H 1 4.56 0.05 . 1 . . . . . . . . 4774 1 193 . 1 1 28 28 LYS H H 1 7.33 0.05 . 1 . . . . . . . . 4774 1 194 . 1 1 28 28 LYS HA H 1 3.87 0.05 . 1 . . . . . . . . 4774 1 195 . 1 1 28 28 LYS HB3 H 1 1.36 0.05 . 1 . . . . . . . . 4774 1 196 . 1 1 28 28 LYS HB2 H 1 1.36 0.05 . 1 . . . . . . . . 4774 1 197 . 1 1 28 28 LYS HG3 H 1 1.39 0.05 . 1 . . . . . . . . 4774 1 198 . 1 1 28 28 LYS HG2 H 1 1.39 0.05 . 1 . . . . . . . . 4774 1 199 . 1 1 28 28 LYS HD3 H 1 1.19 0.05 . 1 . . . . . . . . 4774 1 200 . 1 1 28 28 LYS HD2 H 1 1.52 0.05 . 1 . . . . . . . . 4774 1 201 . 1 1 28 28 LYS HE2 H 1 2.62 0.05 . 1 . . . . . . . . 4774 1 202 . 1 1 28 28 LYS HE3 H 1 2.62 0.05 . 1 . . . . . . . . 4774 1 203 . 1 1 29 29 PHE H H 1 7.32 0.05 . 1 . . . . . . . . 4774 1 204 . 1 1 29 29 PHE HA H 1 4.45 0.05 . 1 . . . . . . . . 4774 1 205 . 1 1 29 29 PHE HB2 H 1 3.29 0.05 . 1 . . . . . . . . 4774 1 206 . 1 1 29 29 PHE HB3 H 1 2.61 0.05 . 1 . . . . . . . . 4774 1 207 . 1 1 29 29 PHE HD1 H 1 7.25 0.05 . 1 . . . . . . . . 4774 1 208 . 1 1 29 29 PHE HD2 H 1 7.25 0.05 . 1 . . . . . . . . 4774 1 209 . 1 1 29 29 PHE HE1 H 1 7.11 0.05 . 1 . . . . . . . . 4774 1 210 . 1 1 29 29 PHE HE2 H 1 7.11 0.05 . 1 . . . . . . . . 4774 1 211 . 1 1 29 29 PHE HZ H 1 7.05 0.05 . 1 . . . . . . . . 4774 1 212 . 1 1 30 30 ASN H H 1 11.4 0.05 . 1 . . . . . . . . 4774 1 213 . 1 1 30 30 ASN HA H 1 4.50 0.05 . 1 . . . . . . . . 4774 1 214 . 1 1 30 30 ASN HB3 H 1 2.70 0.05 . 1 . . . . . . . . 4774 1 215 . 1 1 30 30 ASN HB2 H 1 2.70 0.05 . 1 . . . . . . . . 4774 1 216 . 1 1 31 31 SER H H 1 8.95 0.05 . 1 . . . . . . . . 4774 1 217 . 1 1 31 31 SER HA H 1 4.27 0.05 . 1 . . . . . . . . 4774 1 218 . 1 1 31 31 SER HB3 H 1 3.10 0.05 . 1 . . . . . . . . 4774 1 219 . 1 1 31 31 SER HB2 H 1 3.39 0.05 . 1 . . . . . . . . 4774 1 220 . 1 1 32 32 ASP H H 1 8.38 0.05 . 1 . . . . . . . . 4774 1 221 . 1 1 32 32 ASP HA H 1 4.62 0.05 . 1 . . . . . . . . 4774 1 222 . 1 1 32 32 ASP HB3 H 1 2.63 0.05 . 1 . . . . . . . . 4774 1 223 . 1 1 32 32 ASP HB2 H 1 2.63 0.05 . 1 . . . . . . . . 4774 1 224 . 1 1 33 33 ILE H H 1 9.43 0.05 . 1 . . . . . . . . 4774 1 225 . 1 1 33 33 ILE HA H 1 5.19 0.05 . 1 . . . . . . . . 4774 1 226 . 1 1 33 33 ILE HG12 H 1 0.74 0.05 . 1 . . . . . . . . 4774 1 227 . 1 1 33 33 ILE HG13 H 1 0.74 0.05 . 1 . . . . . . . . 4774 1 228 . 1 1 33 33 ILE HB H 1 1.46 0.05 . 1 . . . . . . . . 4774 1 229 . 1 1 33 33 ILE HG21 H 1 0.81 0.05 . 1 . . . . . . . . 4774 1 230 . 1 1 33 33 ILE HG22 H 1 0.81 0.05 . 1 . . . . . . . . 4774 1 231 . 1 1 33 33 ILE HG23 H 1 0.81 0.05 . 1 . . . . . . . . 4774 1 232 . 1 1 33 33 ILE HD11 H 1 0.88 0.05 . 1 . . . . . . . . 4774 1 233 . 1 1 33 33 ILE HD12 H 1 0.88 0.05 . 1 . . . . . . . . 4774 1 234 . 1 1 33 33 ILE HD13 H 1 0.88 0.05 . 1 . . . . . . . . 4774 1 235 . 1 1 34 34 ASN H H 1 8.73 0.05 . 1 . . . . . . . . 4774 1 236 . 1 1 34 34 ASN HA H 1 5.69 0.05 . 1 . . . . . . . . 4774 1 237 . 1 1 34 34 ASN HB3 H 1 2.32 0.05 . 1 . . . . . . . . 4774 1 238 . 1 1 34 34 ASN HB2 H 1 2.44 0.05 . 1 . . . . . . . . 4774 1 239 . 1 1 35 35 LEU H H 1 9.08 0.05 . 1 . . . . . . . . 4774 1 240 . 1 1 35 35 LEU HA H 1 5.05 0.05 . 1 . . . . . . . . 4774 1 241 . 1 1 35 35 LEU HB3 H 1 1.54 0.05 . 1 . . . . . . . . 4774 1 242 . 1 1 35 35 LEU HB2 H 1 1.38 0.05 . 1 . . . . . . . . 4774 1 243 . 1 1 35 35 LEU HG H 1 1.39 0.05 . 1 . . . . . . . . 4774 1 244 . 1 1 35 35 LEU HD11 H 1 0.69 0.05 . 1 . . . . . . . . 4774 1 245 . 1 1 35 35 LEU HD12 H 1 0.69 0.05 . 1 . . . . . . . . 4774 1 246 . 1 1 35 35 LEU HD13 H 1 0.69 0.05 . 1 . . . . . . . . 4774 1 247 . 1 1 35 35 LEU HD21 H 1 0.69 0.05 . 1 . . . . . . . . 4774 1 248 . 1 1 35 35 LEU HD22 H 1 0.69 0.05 . 1 . . . . . . . . 4774 1 249 . 1 1 35 35 LEU HD23 H 1 0.69 0.05 . 1 . . . . . . . . 4774 1 250 . 1 1 36 36 GLU H H 1 9.45 0.05 . 1 . . . . . . . . 4774 1 251 . 1 1 36 36 GLU HA H 1 5.53 0.05 . 1 . . . . . . . . 4774 1 252 . 1 1 36 36 GLU HB3 H 1 2.06 0.05 . 1 . . . . . . . . 4774 1 253 . 1 1 36 36 GLU HB2 H 1 1.95 0.05 . 1 . . . . . . . . 4774 1 254 . 1 1 36 36 GLU HG3 H 1 1.67 0.05 . 1 . . . . . . . . 4774 1 255 . 1 1 36 36 GLU HG2 H 1 1.67 0.05 . 1 . . . . . . . . 4774 1 256 . 1 1 37 37 TYR H H 1 8.79 0.05 . 1 . . . . . . . . 4774 1 257 . 1 1 37 37 TYR HA H 1 5.08 0.05 . 1 . . . . . . . . 4774 1 258 . 1 1 37 37 TYR HB3 H 1 2.67 0.05 . 1 . . . . . . . . 4774 1 259 . 1 1 37 37 TYR HB2 H 1 2.94 0.05 . 1 . . . . . . . . 4774 1 260 . 1 1 37 37 TYR HD1 H 1 7.24 0.05 . 1 . . . . . . . . 4774 1 261 . 1 1 37 37 TYR HD2 H 1 7.24 0.05 . 1 . . . . . . . . 4774 1 262 . 1 1 37 37 TYR HE1 H 1 6.94 0.05 . 1 . . . . . . . . 4774 1 263 . 1 1 37 37 TYR HE2 H 1 6.94 0.05 . 1 . . . . . . . . 4774 1 264 . 1 1 38 38 LYS H H 1 9.35 0.05 . 1 . . . . . . . . 4774 1 265 . 1 1 38 38 LYS HA H 1 3.69 0.05 . 1 . . . . . . . . 4774 1 266 . 1 1 38 38 LYS HB3 H 1 1.68 0.05 . 1 . . . . . . . . 4774 1 267 . 1 1 38 38 LYS HB2 H 1 1.68 0.05 . 1 . . . . . . . . 4774 1 268 . 1 1 38 38 LYS HG3 H 1 1.07 0.05 . 1 . . . . . . . . 4774 1 269 . 1 1 38 38 LYS HG2 H 1 1.07 0.05 . 1 . . . . . . . . 4774 1 270 . 1 1 38 38 LYS HD3 H 1 1.40 0.05 . 1 . . . . . . . . 4774 1 271 . 1 1 38 38 LYS HD2 H 1 1.40 0.05 . 1 . . . . . . . . 4774 1 272 . 1 1 38 38 LYS HE2 H 1 2.93 0.05 . 1 . . . . . . . . 4774 1 273 . 1 1 38 38 LYS HE3 H 1 2.93 0.05 . 1 . . . . . . . . 4774 1 274 . 1 1 38 38 LYS HZ1 H 1 2.93 0.05 . 1 . . . . . . . . 4774 1 275 . 1 1 38 38 LYS HZ2 H 1 2.93 0.05 . 1 . . . . . . . . 4774 1 276 . 1 1 38 38 LYS HZ3 H 1 2.93 0.05 . 1 . . . . . . . . 4774 1 277 . 1 1 39 39 GLY H H 1 8.79 0.05 . 1 . . . . . . . . 4774 1 278 . 1 1 39 39 GLY HA3 H 1 3.99 0.05 . 1 . . . . . . . . 4774 1 279 . 1 1 39 39 GLY HA2 H 1 3.51 0.05 . 1 . . . . . . . . 4774 1 280 . 1 1 40 40 LYS H H 1 7.86 0.05 . 1 . . . . . . . . 4774 1 281 . 1 1 40 40 LYS HA H 1 4.52 0.05 . 1 . . . . . . . . 4774 1 282 . 1 1 40 40 LYS HB3 H 1 1.80 0.05 . 1 . . . . . . . . 4774 1 283 . 1 1 40 40 LYS HB2 H 1 1.80 0.05 . 1 . . . . . . . . 4774 1 284 . 1 1 40 40 LYS HG3 H 1 1.25 0.05 . 1 . . . . . . . . 4774 1 285 . 1 1 40 40 LYS HG2 H 1 1.25 0.05 . 1 . . . . . . . . 4774 1 286 . 1 1 40 40 LYS HD3 H 1 1.31 0.05 . 1 . . . . . . . . 4774 1 287 . 1 1 40 40 LYS HD2 H 1 1.31 0.05 . 1 . . . . . . . . 4774 1 288 . 1 1 40 40 LYS HE2 H 1 1.65 0.05 . 1 . . . . . . . . 4774 1 289 . 1 1 40 40 LYS HE3 H 1 1.65 0.05 . 1 . . . . . . . . 4774 1 290 . 1 1 41 41 SER H H 1 8.35 0.05 . 1 . . . . . . . . 4774 1 291 . 1 1 41 41 SER HA H 1 5.55 0.05 . 1 . . . . . . . . 4774 1 292 . 1 1 41 41 SER HB3 H 1 3.50 0.05 . 1 . . . . . . . . 4774 1 293 . 1 1 41 41 SER HB2 H 1 3.55 0.05 . 1 . . . . . . . . 4774 1 294 . 1 1 42 42 VAL H H 1 9.11 0.05 . 1 . . . . . . . . 4774 1 295 . 1 1 42 42 VAL HA H 1 4.63 0.05 . 1 . . . . . . . . 4774 1 296 . 1 1 42 42 VAL HB H 1 2.00 0.05 . 1 . . . . . . . . 4774 1 297 . 1 1 42 42 VAL HG11 H 1 0.88 0.05 . 1 . . . . . . . . 4774 1 298 . 1 1 42 42 VAL HG12 H 1 0.88 0.05 . 1 . . . . . . . . 4774 1 299 . 1 1 42 42 VAL HG13 H 1 0.88 0.05 . 1 . . . . . . . . 4774 1 300 . 1 1 42 42 VAL HG21 H 1 0.88 0.05 . 1 . . . . . . . . 4774 1 301 . 1 1 42 42 VAL HG22 H 1 0.88 0.05 . 1 . . . . . . . . 4774 1 302 . 1 1 42 42 VAL HG23 H 1 0.88 0.05 . 1 . . . . . . . . 4774 1 303 . 1 1 43 43 ASN H H 1 8.31 0.05 . 1 . . . . . . . . 4774 1 304 . 1 1 43 43 ASN HA H 1 4.79 0.05 . 1 . . . . . . . . 4774 1 305 . 1 1 43 43 ASN HB3 H 1 2.88 0.05 . 1 . . . . . . . . 4774 1 306 . 1 1 43 43 ASN HB2 H 1 2.88 0.05 . 1 . . . . . . . . 4774 1 307 . 1 1 44 44 LEU H H 1 8.89 0.05 . 1 . . . . . . . . 4774 1 308 . 1 1 44 44 LEU HA H 1 3.97 0.05 . 1 . . . . . . . . 4774 1 309 . 1 1 44 44 LEU HB2 H 1 1.36 0.05 . 1 . . . . . . . . 4774 1 310 . 1 1 44 44 LEU HB3 H 1 1.36 0.05 . 1 . . . . . . . . 4774 1 311 . 1 1 44 44 LEU HG H 1 1.82 0.05 . 1 . . . . . . . . 4774 1 312 . 1 1 44 44 LEU HD11 H 1 1.00 0.05 . 1 . . . . . . . . 4774 1 313 . 1 1 44 44 LEU HD12 H 1 1.00 0.05 . 1 . . . . . . . . 4774 1 314 . 1 1 44 44 LEU HD13 H 1 1.00 0.05 . 1 . . . . . . . . 4774 1 315 . 1 1 44 44 LEU HD21 H 1 0.76 0.05 . 1 . . . . . . . . 4774 1 316 . 1 1 44 44 LEU HD22 H 1 0.76 0.05 . 1 . . . . . . . . 4774 1 317 . 1 1 44 44 LEU HD23 H 1 0.76 0.05 . 1 . . . . . . . . 4774 1 318 . 1 1 45 45 LYS H H 1 7.95 0.05 . 1 . . . . . . . . 4774 1 319 . 1 1 45 45 LYS HA H 1 4.32 0.05 . 1 . . . . . . . . 4774 1 320 . 1 1 45 45 LYS HB3 H 1 1.86 0.05 . 1 . . . . . . . . 4774 1 321 . 1 1 45 45 LYS HB2 H 1 1.86 0.05 . 1 . . . . . . . . 4774 1 322 . 1 1 45 45 LYS HG3 H 1 1.59 0.05 . 1 . . . . . . . . 4774 1 323 . 1 1 45 45 LYS HG2 H 1 1.59 0.05 . 1 . . . . . . . . 4774 1 324 . 1 1 45 45 LYS HD3 H 1 1.70 0.05 . 1 . . . . . . . . 4774 1 325 . 1 1 45 45 LYS HD2 H 1 1.70 0.05 . 1 . . . . . . . . 4774 1 326 . 1 1 45 45 LYS HE2 H 1 2.04 0.05 . 1 . . . . . . . . 4774 1 327 . 1 1 45 45 LYS HE3 H 1 2.04 0.05 . 1 . . . . . . . . 4774 1 328 . 1 1 46 46 SER H H 1 7.60 0.05 . 1 . . . . . . . . 4774 1 329 . 1 1 46 46 SER HA H 1 4.73 0.05 . 1 . . . . . . . . 4774 1 330 . 1 1 46 46 SER HB3 H 1 4.23 0.05 . 1 . . . . . . . . 4774 1 331 . 1 1 46 46 SER HB2 H 1 3.78 0.05 . 1 . . . . . . . . 4774 1 332 . 1 1 47 47 ILE H H 1 9.01 0.05 . 1 . . . . . . . . 4774 1 333 . 1 1 47 47 ILE HA H 1 3.94 0.05 . 1 . . . . . . . . 4774 1 334 . 1 1 47 47 ILE HG12 H 1 1.34 0.05 . 1 . . . . . . . . 4774 1 335 . 1 1 47 47 ILE HG13 H 1 1.34 0.05 . 1 . . . . . . . . 4774 1 336 . 1 1 47 47 ILE HB H 1 1.81 0.05 . 1 . . . . . . . . 4774 1 337 . 1 1 47 47 ILE HG21 H 1 0.94 0.05 . 1 . . . . . . . . 4774 1 338 . 1 1 47 47 ILE HG22 H 1 0.94 0.05 . 1 . . . . . . . . 4774 1 339 . 1 1 47 47 ILE HG23 H 1 0.94 0.05 . 1 . . . . . . . . 4774 1 340 . 1 1 47 47 ILE HD11 H 1 0.80 0.05 . 1 . . . . . . . . 4774 1 341 . 1 1 47 47 ILE HD12 H 1 0.80 0.05 . 1 . . . . . . . . 4774 1 342 . 1 1 47 47 ILE HD13 H 1 0.80 0.05 . 1 . . . . . . . . 4774 1 343 . 1 1 48 48 MET H H 1 8.25 0.05 . 1 . . . . . . . . 4774 1 344 . 1 1 48 48 MET HA H 1 4.15 0.05 . 1 . . . . . . . . 4774 1 345 . 1 1 48 48 MET HB3 H 1 2.01 0.05 . 1 . . . . . . . . 4774 1 346 . 1 1 48 48 MET HB2 H 1 2.52 0.05 . 1 . . . . . . . . 4774 1 347 . 1 1 48 48 MET HG3 H 1 2.67 0.05 . 1 . . . . . . . . 4774 1 348 . 1 1 48 48 MET HG2 H 1 2.67 0.05 . 1 . . . . . . . . 4774 1 349 . 1 1 48 48 MET HE1 H 1 1.88 0.05 . 1 . . . . . . . . 4774 1 350 . 1 1 48 48 MET HE2 H 1 1.88 0.05 . 1 . . . . . . . . 4774 1 351 . 1 1 48 48 MET HE3 H 1 1.88 0.05 . 1 . . . . . . . . 4774 1 352 . 1 1 49 49 GLY H H 1 8.36 0.05 . 1 . . . . . . . . 4774 1 353 . 1 1 49 49 GLY HA3 H 1 4.10 0.05 . 1 . . . . . . . . 4774 1 354 . 1 1 49 49 GLY HA2 H 1 3.89 0.05 . 1 . . . . . . . . 4774 1 355 . 1 1 50 50 VAL H H 1 8.30 0.05 . 1 . . . . . . . . 4774 1 356 . 1 1 50 50 VAL HA H 1 3.42 0.05 . 1 . . . . . . . . 4774 1 357 . 1 1 50 50 VAL HB H 1 1.93 0.05 . 1 . . . . . . . . 4774 1 358 . 1 1 50 50 VAL HG11 H 1 1.02 0.05 . 1 . . . . . . . . 4774 1 359 . 1 1 50 50 VAL HG12 H 1 1.02 0.05 . 1 . . . . . . . . 4774 1 360 . 1 1 50 50 VAL HG13 H 1 1.02 0.05 . 1 . . . . . . . . 4774 1 361 . 1 1 50 50 VAL HG21 H 1 0.71 0.05 . 1 . . . . . . . . 4774 1 362 . 1 1 50 50 VAL HG22 H 1 0.71 0.05 . 1 . . . . . . . . 4774 1 363 . 1 1 50 50 VAL HG23 H 1 0.71 0.05 . 1 . . . . . . . . 4774 1 364 . 1 1 51 51 MET H H 1 8.33 0.05 . 1 . . . . . . . . 4774 1 365 . 1 1 51 51 MET HA H 1 4.24 0.05 . 1 . . . . . . . . 4774 1 366 . 1 1 51 51 MET HB3 H 1 2.12 0.05 . 1 . . . . . . . . 4774 1 367 . 1 1 51 51 MET HB2 H 1 1.92 0.05 . 1 . . . . . . . . 4774 1 368 . 1 1 51 51 MET HG3 H 1 2.67 0.05 . 1 . . . . . . . . 4774 1 369 . 1 1 51 51 MET HG2 H 1 2.58 0.05 . 1 . . . . . . . . 4774 1 370 . 1 1 51 51 MET HE1 H 1 1.90 0.05 . 1 . . . . . . . . 4774 1 371 . 1 1 51 51 MET HE2 H 1 1.90 0.05 . 1 . . . . . . . . 4774 1 372 . 1 1 51 51 MET HE3 H 1 1.90 0.05 . 1 . . . . . . . . 4774 1 373 . 1 1 52 52 SER H H 1 7.85 0.05 . 1 . . . . . . . . 4774 1 374 . 1 1 52 52 SER HA H 1 4.27 0.05 . 1 . . . . . . . . 4774 1 375 . 1 1 52 52 SER HB3 H 1 4.03 0.05 . 1 . . . . . . . . 4774 1 376 . 1 1 52 52 SER HB2 H 1 3.96 0.05 . 1 . . . . . . . . 4774 1 377 . 1 1 53 53 LEU H H 1 7.20 0.05 . 1 . . . . . . . . 4774 1 378 . 1 1 53 53 LEU HA H 1 4.17 0.05 . 1 . . . . . . . . 4774 1 379 . 1 1 53 53 LEU HB3 H 1 1.42 0.05 . 1 . . . . . . . . 4774 1 380 . 1 1 53 53 LEU HB2 H 1 1.47 0.05 . 1 . . . . . . . . 4774 1 381 . 1 1 53 53 LEU HG H 1 1.79 0.05 . 1 . . . . . . . . 4774 1 382 . 1 1 53 53 LEU HD11 H 1 0.86 0.05 . 1 . . . . . . . . 4774 1 383 . 1 1 53 53 LEU HD12 H 1 0.86 0.05 . 1 . . . . . . . . 4774 1 384 . 1 1 53 53 LEU HD13 H 1 0.86 0.05 . 1 . . . . . . . . 4774 1 385 . 1 1 53 53 LEU HD21 H 1 0.90 0.05 . 1 . . . . . . . . 4774 1 386 . 1 1 53 53 LEU HD22 H 1 0.90 0.05 . 1 . . . . . . . . 4774 1 387 . 1 1 53 53 LEU HD23 H 1 0.90 0.05 . 1 . . . . . . . . 4774 1 388 . 1 1 54 54 GLY H H 1 7.31 0.05 . 1 . . . . . . . . 4774 1 389 . 1 1 54 54 GLY HA2 H 1 3.85 0.05 . 1 . . . . . . . . 4774 1 390 . 1 1 54 54 GLY HA3 H 1 3.67 0.05 . 1 . . . . . . . . 4774 1 391 . 1 1 55 55 VAL H H 1 8.39 0.05 . 1 . . . . . . . . 4774 1 392 . 1 1 55 55 VAL HA H 1 2.84 0.05 . 1 . . . . . . . . 4774 1 393 . 1 1 55 55 VAL HB H 1 1.61 0.05 . 1 . . . . . . . . 4774 1 394 . 1 1 55 55 VAL HG11 H 1 0.42 0.05 . 1 . . . . . . . . 4774 1 395 . 1 1 55 55 VAL HG12 H 1 0.42 0.05 . 1 . . . . . . . . 4774 1 396 . 1 1 55 55 VAL HG13 H 1 0.42 0.05 . 1 . . . . . . . . 4774 1 397 . 1 1 55 55 VAL HG21 H 1 0.29 0.05 . 1 . . . . . . . . 4774 1 398 . 1 1 55 55 VAL HG22 H 1 0.29 0.05 . 1 . . . . . . . . 4774 1 399 . 1 1 55 55 VAL HG23 H 1 0.29 0.05 . 1 . . . . . . . . 4774 1 400 . 1 1 56 56 GLY H H 1 8.03 0.05 . 1 . . . . . . . . 4774 1 401 . 1 1 56 56 GLY HA3 H 1 4.28 0.05 . 1 . . . . . . . . 4774 1 402 . 1 1 56 56 GLY HA2 H 1 3.67 0.05 . 1 . . . . . . . . 4774 1 403 . 1 1 57 57 GLN H H 1 8.69 0.05 . 1 . . . . . . . . 4774 1 404 . 1 1 57 57 GLN HA H 1 3.52 0.05 . 1 . . . . . . . . 4774 1 405 . 1 1 57 57 GLN HB3 H 1 1.95 0.05 . 1 . . . . . . . . 4774 1 406 . 1 1 57 57 GLN HB2 H 1 1.85 0.05 . 1 . . . . . . . . 4774 1 407 . 1 1 57 57 GLN HG3 H 1 2.14 0.05 . 1 . . . . . . . . 4774 1 408 . 1 1 57 57 GLN HG2 H 1 2.14 0.05 . 1 . . . . . . . . 4774 1 409 . 1 1 58 58 GLY H H 1 8.82 0.05 . 1 . . . . . . . . 4774 1 410 . 1 1 58 58 GLY HA3 H 1 3.46 0.05 . 1 . . . . . . . . 4774 1 411 . 1 1 58 58 GLY HA2 H 1 4.12 0.05 . 1 . . . . . . . . 4774 1 412 . 1 1 59 59 SER H H 1 7.09 0.05 . 1 . . . . . . . . 4774 1 413 . 1 1 59 59 SER HA H 1 4.54 0.05 . 1 . . . . . . . . 4774 1 414 . 1 1 59 59 SER HB3 H 1 3.66 0.05 . 1 . . . . . . . . 4774 1 415 . 1 1 59 59 SER HB2 H 1 3.42 0.05 . 1 . . . . . . . . 4774 1 416 . 1 1 60 60 ASP H H 1 8.72 0.05 . 1 . . . . . . . . 4774 1 417 . 1 1 60 60 ASP HA H 1 5.88 0.05 . 1 . . . . . . . . 4774 1 418 . 1 1 60 60 ASP HB3 H 1 2.55 0.05 . 1 . . . . . . . . 4774 1 419 . 1 1 60 60 ASP HB2 H 1 2.73 0.05 . 1 . . . . . . . . 4774 1 420 . 1 1 61 61 VAL H H 1 9.07 0.05 . 1 . . . . . . . . 4774 1 421 . 1 1 61 61 VAL HA H 1 5.38 0.05 . 1 . . . . . . . . 4774 1 422 . 1 1 61 61 VAL HB H 1 2.25 0.05 . 1 . . . . . . . . 4774 1 423 . 1 1 61 61 VAL HG11 H 1 0.82 0.05 . 1 . . . . . . . . 4774 1 424 . 1 1 61 61 VAL HG12 H 1 0.82 0.05 . 1 . . . . . . . . 4774 1 425 . 1 1 61 61 VAL HG13 H 1 0.82 0.05 . 1 . . . . . . . . 4774 1 426 . 1 1 61 61 VAL HG21 H 1 0.73 0.05 . 1 . . . . . . . . 4774 1 427 . 1 1 61 61 VAL HG22 H 1 0.73 0.05 . 1 . . . . . . . . 4774 1 428 . 1 1 61 61 VAL HG23 H 1 0.73 0.05 . 1 . . . . . . . . 4774 1 429 . 1 1 62 62 THR H H 1 8.76 0.05 . 1 . . . . . . . . 4774 1 430 . 1 1 62 62 THR HA H 1 5.22 0.05 . 1 . . . . . . . . 4774 1 431 . 1 1 62 62 THR HB H 1 3.91 0.05 . 1 . . . . . . . . 4774 1 432 . 1 1 62 62 THR HG21 H 1 1.01 0.05 . 1 . . . . . . . . 4774 1 433 . 1 1 62 62 THR HG22 H 1 1.01 0.05 . 1 . . . . . . . . 4774 1 434 . 1 1 62 62 THR HG23 H 1 1.01 0.05 . 1 . . . . . . . . 4774 1 435 . 1 1 63 63 ILE H H 1 9.20 0.05 . 1 . . . . . . . . 4774 1 436 . 1 1 63 63 ILE HA H 1 5.22 0.05 . 1 . . . . . . . . 4774 1 437 . 1 1 63 63 ILE HG12 H 1 1.12 0.05 . 1 . . . . . . . . 4774 1 438 . 1 1 63 63 ILE HG13 H 1 0.74 0.05 . 1 . . . . . . . . 4774 1 439 . 1 1 63 63 ILE HB H 1 1.68 0.05 . 1 . . . . . . . . 4774 1 440 . 1 1 63 63 ILE HG21 H 1 0.75 0.05 . 1 . . . . . . . . 4774 1 441 . 1 1 63 63 ILE HG22 H 1 0.75 0.05 . 1 . . . . . . . . 4774 1 442 . 1 1 63 63 ILE HG23 H 1 0.75 0.05 . 1 . . . . . . . . 4774 1 443 . 1 1 63 63 ILE HD11 H 1 0.53 0.05 . 1 . . . . . . . . 4774 1 444 . 1 1 63 63 ILE HD12 H 1 0.53 0.05 . 1 . . . . . . . . 4774 1 445 . 1 1 63 63 ILE HD13 H 1 0.53 0.05 . 1 . . . . . . . . 4774 1 446 . 1 1 64 64 THR H H 1 8.68 0.05 . 1 . . . . . . . . 4774 1 447 . 1 1 64 64 THR HA H 1 5.25 0.05 . 1 . . . . . . . . 4774 1 448 . 1 1 64 64 THR HB H 1 4.08 0.05 . 1 . . . . . . . . 4774 1 449 . 1 1 64 64 THR HG21 H 1 1.05 0.05 . 1 . . . . . . . . 4774 1 450 . 1 1 64 64 THR HG22 H 1 1.05 0.05 . 1 . . . . . . . . 4774 1 451 . 1 1 64 64 THR HG23 H 1 1.05 0.05 . 1 . . . . . . . . 4774 1 452 . 1 1 65 65 VAL H H 1 9.07 0.05 . 1 . . . . . . . . 4774 1 453 . 1 1 65 65 VAL HA H 1 4.73 0.05 . 1 . . . . . . . . 4774 1 454 . 1 1 65 65 VAL HB H 1 1.86 0.05 . 1 . . . . . . . . 4774 1 455 . 1 1 65 65 VAL HG11 H 1 0.86 0.05 . 1 . . . . . . . . 4774 1 456 . 1 1 65 65 VAL HG12 H 1 0.86 0.05 . 1 . . . . . . . . 4774 1 457 . 1 1 65 65 VAL HG13 H 1 0.86 0.05 . 1 . . . . . . . . 4774 1 458 . 1 1 65 65 VAL HG21 H 1 1.56 0.05 . 1 . . . . . . . . 4774 1 459 . 1 1 65 65 VAL HG22 H 1 1.56 0.05 . 1 . . . . . . . . 4774 1 460 . 1 1 65 65 VAL HG23 H 1 1.56 0.05 . 1 . . . . . . . . 4774 1 461 . 1 1 66 66 ASP H H 1 8.85 0.05 . 1 . . . . . . . . 4774 1 462 . 1 1 66 66 ASP HA H 1 5.47 0.05 . 1 . . . . . . . . 4774 1 463 . 1 1 66 66 ASP HB3 H 1 2.88 0.05 . 1 . . . . . . . . 4774 1 464 . 1 1 66 66 ASP HB2 H 1 2.32 0.05 . 1 . . . . . . . . 4774 1 465 . 1 1 67 67 GLY H H 1 10.1 0.05 . 1 . . . . . . . . 4774 1 466 . 1 1 67 67 GLY HA3 H 1 3.90 0.05 . 1 . . . . . . . . 4774 1 467 . 1 1 67 67 GLY HA2 H 1 3.90 0.05 . 1 . . . . . . . . 4774 1 468 . 1 1 68 68 ALA H H 1 8.85 0.05 . 1 . . . . . . . . 4774 1 469 . 1 1 68 68 ALA HA H 1 4.05 0.05 . 1 . . . . . . . . 4774 1 470 . 1 1 68 68 ALA HB1 H 1 1.46 0.05 . 1 . . . . . . . . 4774 1 471 . 1 1 68 68 ALA HB2 H 1 1.46 0.05 . 1 . . . . . . . . 4774 1 472 . 1 1 68 68 ALA HB3 H 1 1.46 0.05 . 1 . . . . . . . . 4774 1 473 . 1 1 69 69 ASP H H 1 7.54 0.05 . 1 . . . . . . . . 4774 1 474 . 1 1 69 69 ASP HA H 1 4.93 0.05 . 1 . . . . . . . . 4774 1 475 . 1 1 69 69 ASP HB3 H 1 2.64 0.05 . 1 . . . . . . . . 4774 1 476 . 1 1 69 69 ASP HB2 H 1 3.42 0.05 . 1 . . . . . . . . 4774 1 477 . 1 1 70 70 GLU H H 1 7.13 0.05 . 1 . . . . . . . . 4774 1 478 . 1 1 70 70 GLU HA H 1 3.90 0.05 . 1 . . . . . . . . 4774 1 479 . 1 1 70 70 GLU HB3 H 1 2.12 0.05 . 1 . . . . . . . . 4774 1 480 . 1 1 70 70 GLU HB2 H 1 2.15 0.05 . 1 . . . . . . . . 4774 1 481 . 1 1 70 70 GLU HG3 H 1 2.43 0.05 . 1 . . . . . . . . 4774 1 482 . 1 1 70 70 GLU HG2 H 1 2.59 0.05 . 1 . . . . . . . . 4774 1 483 . 1 1 71 71 ALA H H 1 8.41 0.05 . 1 . . . . . . . . 4774 1 484 . 1 1 71 71 ALA HA H 1 4.06 0.05 . 1 . . . . . . . . 4774 1 485 . 1 1 71 71 ALA HB1 H 1 1.40 0.05 . 1 . . . . . . . . 4774 1 486 . 1 1 71 71 ALA HB2 H 1 1.40 0.05 . 1 . . . . . . . . 4774 1 487 . 1 1 71 71 ALA HB3 H 1 1.40 0.05 . 1 . . . . . . . . 4774 1 488 . 1 1 72 72 GLU H H 1 8.48 0.05 . 1 . . . . . . . . 4774 1 489 . 1 1 72 72 GLU HA H 1 3.90 0.05 . 1 . . . . . . . . 4774 1 490 . 1 1 72 72 GLU HB3 H 1 1.97 0.05 . 1 . . . . . . . . 4774 1 491 . 1 1 72 72 GLU HB2 H 1 2.29 0.05 . 1 . . . . . . . . 4774 1 492 . 1 1 72 72 GLU HG3 H 1 2.11 0.05 . 1 . . . . . . . . 4774 1 493 . 1 1 72 72 GLU HG2 H 1 2.11 0.05 . 1 . . . . . . . . 4774 1 494 . 1 1 73 73 GLY H H 1 8.61 0.05 . 1 . . . . . . . . 4774 1 495 . 1 1 73 73 GLY HA3 H 1 2.22 0.05 . 1 . . . . . . . . 4774 1 496 . 1 1 73 73 GLY HA2 H 1 1.53 0.05 . 1 . . . . . . . . 4774 1 497 . 1 1 74 74 MET H H 1 8.38 0.05 . 1 . . . . . . . . 4774 1 498 . 1 1 74 74 MET HA H 1 3.88 0.05 . 1 . . . . . . . . 4774 1 499 . 1 1 74 74 MET HB3 H 1 2.31 0.05 . 1 . . . . . . . . 4774 1 500 . 1 1 74 74 MET HB2 H 1 2.18 0.05 . 1 . . . . . . . . 4774 1 501 . 1 1 74 74 MET HG3 H 1 2.51 0.05 . 1 . . . . . . . . 4774 1 502 . 1 1 74 74 MET HG2 H 1 2.30 0.05 . 1 . . . . . . . . 4774 1 503 . 1 1 74 74 MET HE1 H 1 1.88 0.05 . 1 . . . . . . . . 4774 1 504 . 1 1 74 74 MET HE2 H 1 1.88 0.05 . 1 . . . . . . . . 4774 1 505 . 1 1 74 74 MET HE3 H 1 1.88 0.05 . 1 . . . . . . . . 4774 1 506 . 1 1 75 75 ALA H H 1 7.36 0.05 . 1 . . . . . . . . 4774 1 507 . 1 1 75 75 ALA HA H 1 3.94 0.05 . 1 . . . . . . . . 4774 1 508 . 1 1 75 75 ALA HB1 H 1 1.35 0.05 . 1 . . . . . . . . 4774 1 509 . 1 1 75 75 ALA HB2 H 1 1.35 0.05 . 1 . . . . . . . . 4774 1 510 . 1 1 75 75 ALA HB3 H 1 1.35 0.05 . 1 . . . . . . . . 4774 1 511 . 1 1 76 76 ALA H H 1 7.78 0.05 . 1 . . . . . . . . 4774 1 512 . 1 1 76 76 ALA HA H 1 4.16 0.05 . 1 . . . . . . . . 4774 1 513 . 1 1 76 76 ALA HB1 H 1 1.54 0.05 . 1 . . . . . . . . 4774 1 514 . 1 1 76 76 ALA HB2 H 1 1.54 0.05 . 1 . . . . . . . . 4774 1 515 . 1 1 76 76 ALA HB3 H 1 1.54 0.05 . 1 . . . . . . . . 4774 1 516 . 1 1 77 77 ILE H H 1 8.00 0.05 . 1 . . . . . . . . 4774 1 517 . 1 1 77 77 ILE HA H 1 3.39 0.05 . 1 . . . . . . . . 4774 1 518 . 1 1 77 77 ILE HG12 H 1 0.98 0.05 . 1 . . . . . . . . 4774 1 519 . 1 1 77 77 ILE HG13 H 1 1.52 0.05 . 1 . . . . . . . . 4774 1 520 . 1 1 77 77 ILE HB H 1 2.10 0.05 . 1 . . . . . . . . 4774 1 521 . 1 1 77 77 ILE HG21 H 1 0.56 0.05 . 1 . . . . . . . . 4774 1 522 . 1 1 77 77 ILE HG22 H 1 0.56 0.05 . 1 . . . . . . . . 4774 1 523 . 1 1 77 77 ILE HG23 H 1 0.56 0.05 . 1 . . . . . . . . 4774 1 524 . 1 1 77 77 ILE HD11 H 1 0.57 0.05 . 1 . . . . . . . . 4774 1 525 . 1 1 77 77 ILE HD12 H 1 0.57 0.05 . 1 . . . . . . . . 4774 1 526 . 1 1 77 77 ILE HD13 H 1 0.57 0.05 . 1 . . . . . . . . 4774 1 527 . 1 1 78 78 VAL H H 1 8.52 0.05 . 1 . . . . . . . . 4774 1 528 . 1 1 78 78 VAL HA H 1 3.22 0.05 . 1 . . . . . . . . 4774 1 529 . 1 1 78 78 VAL HB H 1 2.12 0.05 . 1 . . . . . . . . 4774 1 530 . 1 1 78 78 VAL HG11 H 1 1.16 0.05 . 1 . . . . . . . . 4774 1 531 . 1 1 78 78 VAL HG12 H 1 1.16 0.05 . 1 . . . . . . . . 4774 1 532 . 1 1 78 78 VAL HG13 H 1 1.16 0.05 . 1 . . . . . . . . 4774 1 533 . 1 1 78 78 VAL HG21 H 1 0.91 0.05 . 1 . . . . . . . . 4774 1 534 . 1 1 78 78 VAL HG22 H 1 0.91 0.05 . 1 . . . . . . . . 4774 1 535 . 1 1 78 78 VAL HG23 H 1 0.91 0.05 . 1 . . . . . . . . 4774 1 536 . 1 1 79 79 GLU H H 1 7.73 0.05 . 1 . . . . . . . . 4774 1 537 . 1 1 79 79 GLU HA H 1 4.06 0.05 . 1 . . . . . . . . 4774 1 538 . 1 1 79 79 GLU HB3 H 1 2.18 0.05 . 1 . . . . . . . . 4774 1 539 . 1 1 79 79 GLU HB2 H 1 2.09 0.05 . 1 . . . . . . . . 4774 1 540 . 1 1 79 79 GLU HG3 H 1 3.06 0.05 . 1 . . . . . . . . 4774 1 541 . 1 1 79 79 GLU HG2 H 1 3.06 0.05 . 1 . . . . . . . . 4774 1 542 . 1 1 80 80 THR H H 1 8.19 0.05 . 1 . . . . . . . . 4774 1 543 . 1 1 80 80 THR HA H 1 3.94 0.05 . 1 . . . . . . . . 4774 1 544 . 1 1 80 80 THR HB H 1 4.09 0.05 . 1 . . . . . . . . 4774 1 545 . 1 1 80 80 THR HG21 H 1 0.97 0.05 . 1 . . . . . . . . 4774 1 546 . 1 1 80 80 THR HG22 H 1 0.97 0.05 . 1 . . . . . . . . 4774 1 547 . 1 1 80 80 THR HG23 H 1 0.97 0.05 . 1 . . . . . . . . 4774 1 548 . 1 1 81 81 LEU H H 1 8.46 0.05 . 1 . . . . . . . . 4774 1 549 . 1 1 81 81 LEU HA H 1 3.65 0.05 . 1 . . . . . . . . 4774 1 550 . 1 1 81 81 LEU HB3 H 1 1.77 0.05 . 1 . . . . . . . . 4774 1 551 . 1 1 81 81 LEU HB2 H 1 1.77 0.05 . 1 . . . . . . . . 4774 1 552 . 1 1 81 81 LEU HG H 1 1.38 0.05 . 1 . . . . . . . . 4774 1 553 . 1 1 81 81 LEU HD11 H 1 -0.4 0.05 . 1 . . . . . . . . 4774 1 554 . 1 1 81 81 LEU HD12 H 1 -0.4 0.05 . 1 . . . . . . . . 4774 1 555 . 1 1 81 81 LEU HD13 H 1 -0.4 0.05 . 1 . . . . . . . . 4774 1 556 . 1 1 81 81 LEU HD21 H 1 0.28 0.05 . 1 . . . . . . . . 4774 1 557 . 1 1 81 81 LEU HD22 H 1 0.28 0.05 . 1 . . . . . . . . 4774 1 558 . 1 1 81 81 LEU HD23 H 1 0.28 0.05 . 1 . . . . . . . . 4774 1 559 . 1 1 82 82 GLN H H 1 8.16 0.05 . 1 . . . . . . . . 4774 1 560 . 1 1 82 82 GLN HA H 1 4.39 0.05 . 1 . . . . . . . . 4774 1 561 . 1 1 82 82 GLN HB3 H 1 2.28 0.05 . 1 . . . . . . . . 4774 1 562 . 1 1 82 82 GLN HB2 H 1 2.28 0.05 . 1 . . . . . . . . 4774 1 563 . 1 1 82 82 GLN HG3 H 1 2.51 0.05 . 1 . . . . . . . . 4774 1 564 . 1 1 82 82 GLN HG2 H 1 2.51 0.05 . 1 . . . . . . . . 4774 1 565 . 1 1 83 83 LYS H H 1 9.10 0.05 . 1 . . . . . . . . 4774 1 566 . 1 1 83 83 LYS HA H 1 4.01 0.05 . 1 . . . . . . . . 4774 1 567 . 1 1 83 83 LYS HB3 H 1 2.06 0.05 . 1 . . . . . . . . 4774 1 568 . 1 1 83 83 LYS HB2 H 1 1.85 0.05 . 1 . . . . . . . . 4774 1 569 . 1 1 83 83 LYS HG3 H 1 1.65 0.05 . 1 . . . . . . . . 4774 1 570 . 1 1 83 83 LYS HG2 H 1 1.57 0.05 . 1 . . . . . . . . 4774 1 571 . 1 1 83 83 LYS HD3 H 1 1.71 0.05 . 1 . . . . . . . . 4774 1 572 . 1 1 83 83 LYS HD2 H 1 1.71 0.05 . 1 . . . . . . . . 4774 1 573 . 1 1 83 83 LYS HE3 H 1 2.98 0.05 . 1 . . . . . . . . 4774 1 574 . 1 1 83 83 LYS HE2 H 1 2.98 0.05 . 1 . . . . . . . . 4774 1 575 . 1 1 84 84 GLU H H 1 7.78 0.05 . 1 . . . . . . . . 4774 1 576 . 1 1 84 84 GLU HA H 1 4.37 0.05 . 1 . . . . . . . . 4774 1 577 . 1 1 84 84 GLU HB3 H 1 2.03 0.05 . 1 . . . . . . . . 4774 1 578 . 1 1 84 84 GLU HB2 H 1 1.70 0.05 . 1 . . . . . . . . 4774 1 579 . 1 1 84 84 GLU HG3 H 1 2.39 0.05 . 1 . . . . . . . . 4774 1 580 . 1 1 84 84 GLU HG2 H 1 2.27 0.05 . 1 . . . . . . . . 4774 1 581 . 1 1 85 85 GLY H H 1 7.81 0.05 . 1 . . . . . . . . 4774 1 582 . 1 1 85 85 GLY HA3 H 1 3.82 0.05 . 1 . . . . . . . . 4774 1 583 . 1 1 85 85 GLY HA2 H 1 3.83 0.05 . 1 . . . . . . . . 4774 1 584 . 1 1 86 86 LEU H H 1 8.10 0.05 . 1 . . . . . . . . 4774 1 585 . 1 1 86 86 LEU HA H 1 4.16 0.05 . 1 . . . . . . . . 4774 1 586 . 1 1 86 86 LEU HB3 H 1 1.83 0.05 . 1 . . . . . . . . 4774 1 587 . 1 1 86 86 LEU HB2 H 1 1.83 0.05 . 1 . . . . . . . . 4774 1 588 . 1 1 86 86 LEU HG H 1 1.51 0.05 . 1 . . . . . . . . 4774 1 589 . 1 1 86 86 LEU HD11 H 1 0.80 0.05 . 1 . . . . . . . . 4774 1 590 . 1 1 86 86 LEU HD12 H 1 0.80 0.05 . 1 . . . . . . . . 4774 1 591 . 1 1 86 86 LEU HD13 H 1 0.80 0.05 . 1 . . . . . . . . 4774 1 592 . 1 1 86 86 LEU HD21 H 1 0.66 0.05 . 1 . . . . . . . . 4774 1 593 . 1 1 86 86 LEU HD22 H 1 0.66 0.05 . 1 . . . . . . . . 4774 1 594 . 1 1 86 86 LEU HD23 H 1 0.66 0.05 . 1 . . . . . . . . 4774 1 595 . 1 1 87 87 ALA H H 1 7.32 0.05 . 1 . . . . . . . . 4774 1 596 . 1 1 87 87 ALA HA H 1 5.05 0.05 . 1 . . . . . . . . 4774 1 597 . 1 1 87 87 ALA HB1 H 1 1.38 0.05 . 1 . . . . . . . . 4774 1 598 . 1 1 87 87 ALA HB2 H 1 1.38 0.05 . 1 . . . . . . . . 4774 1 599 . 1 1 87 87 ALA HB3 H 1 1.38 0.05 . 1 . . . . . . . . 4774 1 600 . 1 1 88 88 GLU H H 1 8.59 0.05 . 1 . . . . . . . . 4774 1 601 . 1 1 88 88 GLU HA H 1 4.22 0.05 . 1 . . . . . . . . 4774 1 602 . 1 1 88 88 GLU HG2 H 1 1.95 0.05 . 1 . . . . . . . . 4774 1 603 . 1 1 88 88 GLU HG3 H 1 1.95 0.05 . 1 . . . . . . . . 4774 1 604 . 1 1 89 89 GLN H H 1 8.45 0.05 . 1 . . . . . . . . 4774 1 605 . 1 1 89 89 GLN HA H 1 4.19 0.05 . 1 . . . . . . . . 4774 1 606 . 1 1 89 89 GLN HB2 H 1 2.05 0.05 . 1 . . . . . . . . 4774 1 607 . 1 1 89 89 GLN HB3 H 1 2.02 0.05 . 1 . . . . . . . . 4774 1 608 . 1 1 89 89 GLN HG2 H 1 2.26 0.05 . 1 . . . . . . . . 4774 1 609 . 1 1 89 89 GLN HG3 H 1 2.36 0.05 . 1 . . . . . . . . 4774 1 stop_ save_