data_5757 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5757 _Entry.Title ; 13C, 15N solid state NMR chemical shift assignments for the microcrystallin Crh domain swapped dimer ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2003-03-27 _Entry.Accession_date 2003-03-27 _Entry.Last_release_date 2003-10-16 _Entry.Original_release_date 2003-10-16 _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 SOLID-STATE _Entry.Details ; Chemical shifts for the monomeric (BMRB-4972) and dimeric forms of Crh show important differences due to conformational changes induced by the N-terminal 3D domain swap observed in the dimeric form ; _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 Anja Bockmann . . . 5757 2 Adam Lange . . . 5757 3 Anne Galinier . . . 5757 4 Sorin Luca . . . 5757 5 Nicolas Giraud . . . 5757 6 Michel Juy . . . 5757 7 Henrike Heise . . . 5757 8 Roland Montserret . . . 5757 9 Francois Penin . . . 5757 10 Marc Baldus . . . 5757 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 2 5757 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 90 5757 '13C chemical shifts' 360 5757 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2003-10-16 2003-03-27 original author . 5757 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 4972 'Crh monomer in solution state' 5757 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5757 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Solid state NMR sequential resonance assignments and conformational analysis of the 2x10.4 kDa dimeric form of the Bacillus subtilis protein Crh ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 27 _Citation.Journal_issue 4 _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 323 _Citation.Page_last 339 _Citation.Year 2003 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Anja Bockmann . . . 5757 1 2 Adam Lange . . . 5757 1 3 Anne Galinier . . . 5757 1 4 Sorin Luca . . . 5757 1 5 Nicolas Giraud . . . 5757 1 6 Michel Juy . . . 5757 1 7 Henrike Heise . . . 5757 1 8 Roland Montserret . . . 5757 1 9 Francois Penin . . . 5757 1 10 Marc Baldus . . . 5757 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID Assignments 5757 1 'catabolite repression histidine-containing phosphocarrier protein (Crh)' 5757 1 MAS 5757 1 'protein dynamics' 5757 1 'protein structure' 5757 1 'solid state NMR spectroscopy' 5757 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5757 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11361074 _Citation.Full_citation . _Citation.Title 'Evidence for a dimerisation state of the Bacillus subtilis catabolite repression HPr-like protein, Crh.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Microbiol. Biotechnol.' _Citation.Journal_name_full 'Journal of molecular microbiology and biotechnology' _Citation.Journal_volume 3 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1464-1801 _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 429 _Citation.Page_last 432 _Citation.Year 2001 _Citation.Details ; The Bacillus subtilis catabolite repression HPr (Crh) exhibits 45% sequence identity when compared to histidine-containing protein (HPr), a phosphocarrier protein of the phosphoenolpyruvate:carbohydrate phosphotransferase system. We report here that Crh preparations contain a mixture of monomers and homodimers, whereas HPr is known to be monomeric in solution. The dissociation rate of dimers is very slow (t1/2 of about 10 hours), and the percentage of dimers in Crh preparations increases with rising temperature or protein concentration. However, at temperatures above 25 degrees C and a protein concentration of 10 mg/ml, Crh dimers slowly aggregate. Typically, NMR spectra recorded at 25 degrees C showed the coexistence of both forms of Crh, while in Crh solutions kept at 35 degrees C, almost exclusively Crh monomers could be detected. Circular dichroism analysis revealed that the monomeric and dimeric forms of Crh are well folded and exhibit the same overall structure. The physiological significance of the slow Crh monomer/dimer equilibrium remains enigmatic. ; 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. Penin F. . . 5757 2 2 A. Favier A. . . 5757 2 3 R. Montserret R. . . 5757 2 4 B. Brutscher B. . . 5757 2 5 J. Deutscher J. . . 5757 2 6 D. Marion D. . . 5757 2 7 D. Galinier D. . . 5757 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 5757 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11916384 _Citation.Full_citation . _Citation.Title 'Solution structure and dynamics of Crh, the Bacillus subtilis catabolite repression HPr.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 317 _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 131 _Citation.Page_last 144 _Citation.Year 2002 _Citation.Details ; The solution structure and dynamics of the Bacillus subtilis HPr-like protein, Crh, have been investigated using NMR spectroscopy. Crh exhibits high sequence identity (45 %) to the histidine-containing protein (HPr), a phospho-carrier protein of the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system, but contains no catalytic His15, the site of PEP-dependent phosphorylation in HPr. Crh also forms a mixture of monomers and dimers in solution whereas HPr is known to be monomeric. Complete backbone and side-chain assignments were obtained for the monomeric form, and 60 % of the dimer backbone resonances; allowing the identification of the Crh dimer interface from chemical-shift mapping. The conformation of Crh was determined to a precision of 0.46(+/-0.06) A for the backbone atoms, and 1.01(+/-0.08) A for the heavy atoms. The monomer structure is similar to that of known HPr 2.67(+/-0.22) A (C(alpha) rmsd), but has a few notable differences, including a change in the orientation of one of the helices (B), and a two-residue shift in beta-sheet pairing of the N-terminal strand with the beta4 strand. This shift results in a shortening of the surface loop present in HPr and consequently provides a flatter surface in the region of dimerisation contact, which may be related to the different oligomeric nature of these two proteins. A binding site of phospho-serine(P-Ser)-Crh with catabolite control protein A (CcpA) is proposed on the basis of highly conserved surface side-chains between Crh and HPr. This binding site is consistent with the model of a dimer-dimer interaction between P-Ser-Crh and CcpA. (15)N relaxation measured in the monomeric form also identified differential local mobility in the helix B which is located in the vicinity of this site. ; 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 Adrien Favier A. . . 5757 3 2 Bernhard Brutscher B. . . 5757 3 3 Martin Blackledge M. . . 5757 3 4 Anne Galinier A. . . 5757 3 5 Josef Deutscher J. . . 5757 3 6 Francois Penin F. . . 5757 3 7 Dominique Marion D. . . 5757 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 5757 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 12972249 _Citation.Full_citation ; Dimerization of Crh by reversible 3D domain swapping induces structural adjustments to its monomeric homologue HPr Juy, M., Penin, F., Favier, A., Galinier, A., Montserret, R., Haser, R., Deutscher, J. and Bockmann, A. (2003) submitted ; _Citation.Title 'Dimerization of Crh by reversible 3D domain swapping induces structural adjustments to its monomeric homologue Hpr.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 332 _Citation.Journal_issue 4 _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 767 _Citation.Page_last 776 _Citation.Year 2003 _Citation.Details ; The crystal structure of the regulatory protein Crh from Bacillus subtilis was solved at 1.8A resolution and showed an intertwined dimer formed by N-terminal beta1-strand swapping of two monomers. Comparison with the monomeric NMR structure of Crh revealed a domain swap induced conformational rearrangement of the putative interaction site with the repressor CcpA. The resulting conformation closely resembles that observed for the monomeric Crh homologue HPr, indicating that the Crh dimer is the active form binding to CcpA. An analogous dimer of HPr can be constructed without domain swapping, suggesting that HPr may dimerize upon binding to CcpA. Our data suggest that reversible 3D domain swapping of Crh might be an efficient regulatory mechanism to modulate its activity. ; 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 Michel Juy M. . . 5757 4 2 Francois Penin F. . . 5757 4 3 Adrien Favier A. . . 5757 4 4 Anne Galinier A. . . 5757 4 5 Roland Montserret R. . . 5757 4 6 Richard Haser R. . . 5757 4 7 Josef Deutscher J. . . 5757 4 8 Anja Bockmann A. . . 5757 4 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_Crh _Assembly.Sf_category assembly _Assembly.Sf_framecode system_Crh _Assembly.Entry_ID 5757 _Assembly.ID 1 _Assembly.Name 'Crh dimer' _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 dimer 5757 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 'Crh subunit 1' 1 $Crh . . . native . . 1 . . 5757 1 2 'Crh subunit 2' 1 $Crh . . . native . . 1 . . 5757 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 . PDB 1MU4 . . . . . ; The system reported in the PDB data base corresponds to the Crh domain swapped dimer structure solved by a single crystal X-ray study. The system reported here corresponds to microcrystalline PEG precipitated Crh. TALOS dihedral angle predictions strongly indicate that the microcrystallin protein is equally in the dimeric domain swapped form observed for the diffracting crystals ; 5757 1 . PDB 1K1C . . . . . ; The system reported in the PDB data base corresponds to the Crh monomer structure as determined by liquid state NMR methods.The system reported here corresponds to microcrystalline PEG precipitated Crh. TALOS dihedral angle predictions strongly indicate that the microcrystallin protein is in the dimeric domain swapped form observed for diffracting crystals (PDB 1mu4) ; 5757 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Crh dimer' system 5757 1 Crh abbreviation 5757 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'phospho-carrier protein' 5757 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Crh _Entity.Sf_category entity _Entity.Sf_framecode Crh _Entity.Entry_ID 5757 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'catabolite repression HPr' _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 ; MVQQKVEVRLKTGLQARPAA LFVQEANRFTSDVFLEKDGK KVNAKSIMGLMSLAVSTGTE VTLIAQGEDEQEALEKLAAY VQEEVLQHHHHHH ; _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 93 _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 10391 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details ; Crh has been shown to exist in a slow monomer-dimer equilibrium in solution. The structure of the monomeric form could be solved by liquid state NMR spectroscopy. We recently solved the domain swapped dimer structure by X-ray crystallograpy. The microcrystall in solid Crh dimer serves us as model molecule for the development of solid state NMR methods ; _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 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 4972 . crh_monomer . . . . . 93.55 87 100.00 100.00 1.13e-53 . . . . 5757 1 2 no PDB 1K1C . "Solution Structure Of Crh, The Bacillus Subtilis Catabolite Repression Hpr" . . . . . 90.32 84 100.00 100.00 2.37e-51 . . . . 5757 1 3 no PDB 1MO1 . "Crystal Structure At 1.8 Angstroms Of Seleno Methionyled Crh, The Bacillus Subtilis Catabolite Repression Containing Protein Cr" . . . . . 93.55 87 97.70 97.70 1.47e-51 . . . . 5757 1 4 no PDB 1MU4 . "Crystal Structure At 1.8 Angstroms Of The Bacillus Subtilis Catabolite Repression Histidine Containing Protein (crh)" . . . . . 93.55 87 100.00 100.00 1.13e-53 . . . . 5757 1 5 no PDB 2AK7 . "Structure Of A Dimeric P-Ser-Crh" . . . . . 92.47 86 98.84 98.84 4.25e-52 . . . . 5757 1 6 no PDB 2RLZ . "Solid-State Mas Nmr Structure Of The Dimer Crh" . . . . . 91.40 85 100.00 100.00 2.50e-52 . . . . 5757 1 7 no DBJ BAI87096 . "phosphocarrier protein Chr [Bacillus subtilis subsp. natto BEST195]" . . . . . 91.40 85 100.00 100.00 2.50e-52 . . . . 5757 1 8 no DBJ BAM55550 . "phosphocarrier protein Chr [Bacillus subtilis BEST7613]" . . . . . 91.40 85 100.00 100.00 2.50e-52 . . . . 5757 1 9 no DBJ BAM59563 . "phosphocarrier protein Chr [Bacillus subtilis BEST7003]" . . . . . 91.40 85 100.00 100.00 2.50e-52 . . . . 5757 1 10 no DBJ GAK79281 . "phosphocarrier protein Chr [Bacillus subtilis Miyagi-4]" . . . . . 91.40 85 100.00 100.00 2.50e-52 . . . . 5757 1 11 no EMBL CAB08060 . "hypothetical protein [Bacillus subtilis]" . . . . . 91.40 85 100.00 100.00 2.50e-52 . . . . 5757 1 12 no EMBL CAB15479 . "catabolite repression HPr-like protein [Bacillus subtilis subsp. subtilis str. 168]" . . . . . 91.40 85 100.00 100.00 2.50e-52 . . . . 5757 1 13 no EMBL CCU60557 . "Catabolite repression HPr-like protein Crh [Bacillus subtilis E1]" . . . . . 91.40 85 100.00 100.00 2.50e-52 . . . . 5757 1 14 no EMBL CEI59278 . "HPr-like protein Crh [Bacillus subtilis]" . . . . . 91.40 85 100.00 100.00 2.50e-52 . . . . 5757 1 15 no EMBL CEJ79135 . "HPr-like protein Crh [Bacillus sp.]" . . . . . 91.40 85 100.00 100.00 2.50e-52 . . . . 5757 1 16 no GB ADM39440 . "catabolite repression HPr-like protein [Bacillus subtilis subsp. spizizenii str. W23]" . . . . . 91.40 85 100.00 100.00 2.50e-52 . . . . 5757 1 17 no GB ADV94285 . "phosphocarrier protein Chr [Bacillus subtilis BSn5]" . . . . . 91.40 85 100.00 100.00 2.50e-52 . . . . 5757 1 18 no GB AEP88381 . "HPr like protein, Crh [Bacillus subtilis subsp. spizizenii TU-B-10]" . . . . . 91.40 85 100.00 100.00 2.50e-52 . . . . 5757 1 19 no GB AEP92509 . "HPr like protein, Crh [Bacillus subtilis subsp. subtilis str. RO-NN-1]" . . . . . 91.40 85 100.00 100.00 2.50e-52 . . . . 5757 1 20 no GB AFI30049 . "phosphocarrier protein Chr [Bacillus sp. JS]" . . . . . 91.40 85 100.00 100.00 2.50e-52 . . . . 5757 1 21 no REF NP_391354 . "HPr-like protein Crh [Bacillus subtilis subsp. subtilis str. 168]" . . . . . 91.40 85 100.00 100.00 2.50e-52 . . . . 5757 1 22 no REF WP_003219835 . "MULTISPECIES: phosphate ABC transporter permease [Bacillales]" . . . . . 91.40 85 100.00 100.00 2.50e-52 . . . . 5757 1 23 no REF WP_024122965 . "phosphate ABC transporter permease [Bacillus mojavensis]" . . . . . 91.40 85 97.65 100.00 2.21e-51 . . . . 5757 1 24 no REF WP_024713407 . "phosphocarrier protein Chr [Bacillus tequilensis]" . . . . . 91.40 85 98.82 98.82 1.38e-51 . . . . 5757 1 25 no REF YP_003867749 . "catabolite repression HPr-like protein [Bacillus subtilis subsp. spizizenii str. W23]" . . . . . 91.40 85 100.00 100.00 2.50e-52 . . . . 5757 1 26 no SP O06976 . "RecName: Full=HPr-like protein Crh; AltName: Full=Catabolite repression HPr [Bacillus subtilis subsp. subtilis str. 168]" . . . . . 91.40 85 100.00 100.00 2.50e-52 . . . . 5757 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'catabolite repression HPr' common 5757 1 Crh abbreviation 5757 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 . 5757 1 2 . VAL . 5757 1 3 . GLN . 5757 1 4 . GLN . 5757 1 5 . LYS . 5757 1 6 . VAL . 5757 1 7 . GLU . 5757 1 8 . VAL . 5757 1 9 . ARG . 5757 1 10 . LEU . 5757 1 11 . LYS . 5757 1 12 . THR . 5757 1 13 . GLY . 5757 1 14 . LEU . 5757 1 15 . GLN . 5757 1 16 . ALA . 5757 1 17 . ARG . 5757 1 18 . PRO . 5757 1 19 . ALA . 5757 1 20 . ALA . 5757 1 21 . LEU . 5757 1 22 . PHE . 5757 1 23 . VAL . 5757 1 24 . GLN . 5757 1 25 . GLU . 5757 1 26 . ALA . 5757 1 27 . ASN . 5757 1 28 . ARG . 5757 1 29 . PHE . 5757 1 30 . THR . 5757 1 31 . SER . 5757 1 32 . ASP . 5757 1 33 . VAL . 5757 1 34 . PHE . 5757 1 35 . LEU . 5757 1 36 . GLU . 5757 1 37 . LYS . 5757 1 38 . ASP . 5757 1 39 . GLY . 5757 1 40 . LYS . 5757 1 41 . LYS . 5757 1 42 . VAL . 5757 1 43 . ASN . 5757 1 44 . ALA . 5757 1 45 . LYS . 5757 1 46 . SER . 5757 1 47 . ILE . 5757 1 48 . MET . 5757 1 49 . GLY . 5757 1 50 . LEU . 5757 1 51 . MET . 5757 1 52 . SER . 5757 1 53 . LEU . 5757 1 54 . ALA . 5757 1 55 . VAL . 5757 1 56 . SER . 5757 1 57 . THR . 5757 1 58 . GLY . 5757 1 59 . THR . 5757 1 60 . GLU . 5757 1 61 . VAL . 5757 1 62 . THR . 5757 1 63 . LEU . 5757 1 64 . ILE . 5757 1 65 . ALA . 5757 1 66 . GLN . 5757 1 67 . GLY . 5757 1 68 . GLU . 5757 1 69 . ASP . 5757 1 70 . GLU . 5757 1 71 . GLN . 5757 1 72 . GLU . 5757 1 73 . ALA . 5757 1 74 . LEU . 5757 1 75 . GLU . 5757 1 76 . LYS . 5757 1 77 . LEU . 5757 1 78 . ALA . 5757 1 79 . ALA . 5757 1 80 . TYR . 5757 1 81 . VAL . 5757 1 82 . GLN . 5757 1 83 . GLU . 5757 1 84 . GLU . 5757 1 85 . VAL . 5757 1 86 . LEU . 5757 1 87 . GLN . 5757 1 88 . HIS . 5757 1 89 . HIS . 5757 1 90 . HIS . 5757 1 91 . HIS . 5757 1 92 . HIS . 5757 1 93 . HIS . 5757 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 5757 1 . VAL 2 2 5757 1 . GLN 3 3 5757 1 . GLN 4 4 5757 1 . LYS 5 5 5757 1 . VAL 6 6 5757 1 . GLU 7 7 5757 1 . VAL 8 8 5757 1 . ARG 9 9 5757 1 . LEU 10 10 5757 1 . LYS 11 11 5757 1 . THR 12 12 5757 1 . GLY 13 13 5757 1 . LEU 14 14 5757 1 . GLN 15 15 5757 1 . ALA 16 16 5757 1 . ARG 17 17 5757 1 . PRO 18 18 5757 1 . ALA 19 19 5757 1 . ALA 20 20 5757 1 . LEU 21 21 5757 1 . PHE 22 22 5757 1 . VAL 23 23 5757 1 . GLN 24 24 5757 1 . GLU 25 25 5757 1 . ALA 26 26 5757 1 . ASN 27 27 5757 1 . ARG 28 28 5757 1 . PHE 29 29 5757 1 . THR 30 30 5757 1 . SER 31 31 5757 1 . ASP 32 32 5757 1 . VAL 33 33 5757 1 . PHE 34 34 5757 1 . LEU 35 35 5757 1 . GLU 36 36 5757 1 . LYS 37 37 5757 1 . ASP 38 38 5757 1 . GLY 39 39 5757 1 . LYS 40 40 5757 1 . LYS 41 41 5757 1 . VAL 42 42 5757 1 . ASN 43 43 5757 1 . ALA 44 44 5757 1 . LYS 45 45 5757 1 . SER 46 46 5757 1 . ILE 47 47 5757 1 . MET 48 48 5757 1 . GLY 49 49 5757 1 . LEU 50 50 5757 1 . MET 51 51 5757 1 . SER 52 52 5757 1 . LEU 53 53 5757 1 . ALA 54 54 5757 1 . VAL 55 55 5757 1 . SER 56 56 5757 1 . THR 57 57 5757 1 . GLY 58 58 5757 1 . THR 59 59 5757 1 . GLU 60 60 5757 1 . VAL 61 61 5757 1 . THR 62 62 5757 1 . LEU 63 63 5757 1 . ILE 64 64 5757 1 . ALA 65 65 5757 1 . GLN 66 66 5757 1 . GLY 67 67 5757 1 . GLU 68 68 5757 1 . ASP 69 69 5757 1 . GLU 70 70 5757 1 . GLN 71 71 5757 1 . GLU 72 72 5757 1 . ALA 73 73 5757 1 . LEU 74 74 5757 1 . GLU 75 75 5757 1 . LYS 76 76 5757 1 . LEU 77 77 5757 1 . ALA 78 78 5757 1 . ALA 79 79 5757 1 . TYR 80 80 5757 1 . VAL 81 81 5757 1 . GLN 82 82 5757 1 . GLU 83 83 5757 1 . GLU 84 84 5757 1 . VAL 85 85 5757 1 . LEU 86 86 5757 1 . GLN 87 87 5757 1 . HIS 88 88 5757 1 . HIS 89 89 5757 1 . HIS 90 90 5757 1 . HIS 91 91 5757 1 . HIS 92 92 5757 1 . HIS 93 93 5757 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 5757 _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 $Crh . 1423 organism . 'Bacillus subtilis' 'Bacillus subtilis' . . Eubacteria . Bacillus subtilis . . . . . . . . . . . . . . . . . . . . . 5757 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 5757 _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 $Crh . 'recombinant technology' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5757 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5757 _Sample.ID 1 _Sample.Type solid _Sample.Sub_type . _Sample.Details 'Microcrystallin solid protein obtained by slow precipitation with PEG' _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 'catabolite repression HPr' '[U-98% 13C; U-98% 15N]' . . 1 $Crh . . . 4 20 mg . . . . 5757 1 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_1 _Sample_condition_list.Entry_ID 5757 _Sample_condition_list.ID 1 _Sample_condition_list.Details ; The actual sample temperature is around 278K, which is not read out probe T. MAS speed is around 10 kHz. ; 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 6.9 0.2 n/a 5757 1 temperature 278 1 K 5757 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 5757 _Software.ID 1 _Software.Name NMRPipe _Software.Version 2.0 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data processing' 5757 1 stop_ save_ save_NMRVIEW _Software.Sf_category software _Software.Sf_framecode NMRVIEW _Software.Entry_ID 5757 _Software.ID 2 _Software.Name NMRVIEW _Software.Version 5.0 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID assignments 5757 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 5757 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer BRUKER _NMR_spectrometer.Model DSX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer _NMR_spectrometer.Entry_ID 5757 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer BRUKER _NMR_spectrometer.Model DSX _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 5757 _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 spectrometer_1 BRUKER DSX . 500 . . . 5757 1 2 spectrometer_2 BRUKER DSX . 600 . . . 5757 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 5757 _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 '13C-13C proton driven spin diffusion (PDSD)' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 5757 1 2 '13C-13C CO selective J-decoupled PDSD' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 5757 1 3 '13C-13C RFDR' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 5757 1 4 '13C-13C DQ SPC-5' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 5757 1 5 '15N-13C NCACO' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 5757 1 6 '15N-13C NCOCACB' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 5757 1 stop_ 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 5757 _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 external direct . external_to_the_sample . . . . . . . . 5757 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5757 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5757 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_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5757 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-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 . 5757 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 2 2 VAL N N 15 116.5 0.1 . 1 . . . . . . . . 5757 1 2 . 1 1 2 2 VAL CA C 13 58.0 0.1 . 1 . . . . . . . . 5757 1 3 . 1 1 2 2 VAL CB C 13 35.1 0.1 . 1 . . . . . . . . 5757 1 4 . 1 1 2 2 VAL CG1 C 13 21.5 0.1 . 1 . . . . . . . . 5757 1 5 . 1 1 2 2 VAL CG2 C 13 21.5 0.1 . 1 . . . . . . . . 5757 1 6 . 1 1 2 2 VAL C C 13 174.0 0.1 . 1 . . . . . . . . 5757 1 7 . 1 1 3 3 GLN N N 15 82.6 0.1 . 1 . . . . . . . . 5757 1 8 . 1 1 3 3 GLN CA C 13 54.9 0.1 . 1 . . . . . . . . 5757 1 9 . 1 1 3 3 GLN CB C 13 32.7 0.1 . 1 . . . . . . . . 5757 1 10 . 1 1 3 3 GLN CG C 13 30.9 0.1 . 1 . . . . . . . . 5757 1 11 . 1 1 3 3 GLN C C 13 172.2 0.1 . 1 . . . . . . . . 5757 1 12 . 1 1 4 4 GLN N N 15 125.5 0.1 . 1 . . . . . . . . 5757 1 13 . 1 1 4 4 GLN CA C 13 55.5 0.1 . 1 . . . . . . . . 5757 1 14 . 1 1 4 4 GLN CB C 13 32.2 0.1 . 1 . . . . . . . . 5757 1 15 . 1 1 4 4 GLN CG C 13 33.2 0.1 . 1 . . . . . . . . 5757 1 16 . 1 1 4 4 GLN CD C 13 180.2 0.1 . 1 . . . . . . . . 5757 1 17 . 1 1 4 4 GLN C C 13 174.1 0.1 . 1 . . . . . . . . 5757 1 18 . 1 1 5 5 LYS N N 15 115.2 0.1 . 1 . . . . . . . . 5757 1 19 . 1 1 5 5 LYS CA C 13 53.5 0.1 . 1 . . . . . . . . 5757 1 20 . 1 1 5 5 LYS CB C 13 33.2 0.1 . 1 . . . . . . . . 5757 1 21 . 1 1 5 5 LYS CG C 13 24.5 0.1 . 1 . . . . . . . . 5757 1 22 . 1 1 5 5 LYS CD C 13 28.8 0.1 . 1 . . . . . . . . 5757 1 23 . 1 1 5 5 LYS CE C 13 40.1 0.1 . 1 . . . . . . . . 5757 1 24 . 1 1 5 5 LYS C C 13 174.9 0.1 . 1 . . . . . . . . 5757 1 25 . 1 1 6 6 VAL N N 15 117.4 0.1 . 1 . . . . . . . . 5757 1 26 . 1 1 6 6 VAL CA C 13 55.5 0.1 . 1 . . . . . . . . 5757 1 27 . 1 1 6 6 VAL CB C 13 35.6 0.1 . 1 . . . . . . . . 5757 1 28 . 1 1 6 6 VAL CG1 C 13 19.8 0.1 . 2 . . . . . . . . 5757 1 29 . 1 1 6 6 VAL CG2 C 13 22.9 0.1 . 2 . . . . . . . . 5757 1 30 . 1 1 6 6 VAL C C 13 175.6 0.1 . 1 . . . . . . . . 5757 1 31 . 1 1 7 7 GLU N N 15 123.3 0.1 . 1 . . . . . . . . 5757 1 32 . 1 1 7 7 GLU CA C 13 54.5 0.1 . 1 . . . . . . . . 5757 1 33 . 1 1 7 7 GLU CB C 13 31.3 0.1 . 1 . . . . . . . . 5757 1 34 . 1 1 7 7 GLU CG C 13 36.8 0.1 . 1 . . . . . . . . 5757 1 35 . 1 1 7 7 GLU CD C 13 182.9 0.1 . 1 . . . . . . . . 5757 1 36 . 1 1 7 7 GLU C C 13 175.4 0.1 . 1 . . . . . . . . 5757 1 37 . 1 1 8 8 VAL N N 15 122.7 0.1 . 1 . . . . . . . . 5757 1 38 . 1 1 8 8 VAL CA C 13 63.7 0.1 . 1 . . . . . . . . 5757 1 39 . 1 1 8 8 VAL CB C 13 31.1 0.1 . 1 . . . . . . . . 5757 1 40 . 1 1 8 8 VAL CG1 C 13 21.6 0.1 . 2 . . . . . . . . 5757 1 41 . 1 1 8 8 VAL CG2 C 13 22.4 0.1 . 2 . . . . . . . . 5757 1 42 . 1 1 8 8 VAL C C 13 176.8 0.1 . 1 . . . . . . . . 5757 1 43 . 1 1 9 9 ARG N N 15 126.8 0.1 . 1 . . . . . . . . 5757 1 44 . 1 1 9 9 ARG CA C 13 54.1 0.1 . 1 . . . . . . . . 5757 1 45 . 1 1 9 9 ARG CB C 13 28.0 0.1 . 1 . . . . . . . . 5757 1 46 . 1 1 10 10 LEU N N 15 116.7 0.1 . 1 . . . . . . . . 5757 1 47 . 1 1 10 10 LEU CA C 13 52.9 0.1 . 1 . . . . . . . . 5757 1 48 . 1 1 10 10 LEU CB C 13 43.0 0.1 . 1 . . . . . . . . 5757 1 49 . 1 1 10 10 LEU CG C 13 25.5 0.1 . 1 . . . . . . . . 5757 1 50 . 1 1 10 10 LEU CD1 C 13 21.0 0.1 . 1 . . . . . . . . 5757 1 51 . 1 1 10 10 LEU CD2 C 13 21.0 0.1 . 1 . . . . . . . . 5757 1 52 . 1 1 11 11 LYS N N 15 118.6 0.1 . 1 . . . . . . . . 5757 1 53 . 1 1 11 11 LYS CA C 13 58.1 0.1 . 1 . . . . . . . . 5757 1 54 . 1 1 11 11 LYS CB C 13 33.3 0.1 . 1 . . . . . . . . 5757 1 55 . 1 1 11 11 LYS C C 13 174.1 0.1 . 1 . . . . . . . . 5757 1 56 . 1 1 12 12 THR N N 15 109.5 0.1 . 1 . . . . . . . . 5757 1 57 . 1 1 12 12 THR CA C 13 59.1 0.1 . 1 . . . . . . . . 5757 1 58 . 1 1 12 12 THR CB C 13 73.4 0.1 . 1 . . . . . . . . 5757 1 59 . 1 1 12 12 THR CG2 C 13 20.7 0.1 . 1 . . . . . . . . 5757 1 60 . 1 1 12 12 THR C C 13 173.8 0.1 . 1 . . . . . . . . 5757 1 61 . 1 1 13 13 GLY N N 15 106.4 0.1 . 1 . . . . . . . . 5757 1 62 . 1 1 13 13 GLY CA C 13 44.9 0.1 . 1 . . . . . . . . 5757 1 63 . 1 1 13 13 GLY C C 13 172.1 0.1 . 1 . . . . . . . . 5757 1 64 . 1 1 14 14 LEU N N 15 120.0 0.1 . 1 . . . . . . . . 5757 1 65 . 1 1 14 14 LEU CA C 13 56.2 0.1 . 1 . . . . . . . . 5757 1 66 . 1 1 14 14 LEU CB C 13 43.4 0.1 . 1 . . . . . . . . 5757 1 67 . 1 1 14 14 LEU CG C 13 26.6 0.1 . 1 . . . . . . . . 5757 1 68 . 1 1 14 14 LEU CD1 C 13 24.8 0.1 . 1 . . . . . . . . 5757 1 69 . 1 1 14 14 LEU CD2 C 13 24.8 0.1 . 1 . . . . . . . . 5757 1 70 . 1 1 14 14 LEU C C 13 177.2 0.1 . 1 . . . . . . . . 5757 1 71 . 1 1 15 15 GLN N N 15 118.4 0.1 . 1 . . . . . . . . 5757 1 72 . 1 1 15 15 GLN CA C 13 55.3 0.1 . 1 . . . . . . . . 5757 1 73 . 1 1 15 15 GLN CB C 13 33.8 0.1 . 1 . . . . . . . . 5757 1 74 . 1 1 15 15 GLN CG C 13 32.1 0.1 . 1 . . . . . . . . 5757 1 75 . 1 1 15 15 GLN CD C 13 180.1 0.1 . 1 . . . . . . . . 5757 1 76 . 1 1 15 15 GLN C C 13 174.1 0.1 . 1 . . . . . . . . 5757 1 77 . 1 1 16 16 ALA N N 15 118.2 0.1 . 1 . . . . . . . . 5757 1 78 . 1 1 16 16 ALA CA C 13 54.9 0.1 . 1 . . . . . . . . 5757 1 79 . 1 1 16 16 ALA CB C 13 16.9 0.1 . 1 . . . . . . . . 5757 1 80 . 1 1 16 16 ALA C C 13 179.1 0.1 . 1 . . . . . . . . 5757 1 81 . 1 1 17 17 ARG N N 15 121.4 0.1 . 1 . . . . . . . . 5757 1 82 . 1 1 17 17 ARG CA C 13 61.4 0.1 . 1 . . . . . . . . 5757 1 83 . 1 1 17 17 ARG CB C 13 27.2 0.1 . 1 . . . . . . . . 5757 1 84 . 1 1 17 17 ARG C C 13 177.5 0.1 . 1 . . . . . . . . 5757 1 85 . 1 1 18 18 PRO N N 15 133.6 0.1 . 1 . . . . . . . . 5757 1 86 . 1 1 18 18 PRO CA C 13 65.1 0.1 . 1 . . . . . . . . 5757 1 87 . 1 1 18 18 PRO CB C 13 31.6 0.1 . 1 . . . . . . . . 5757 1 88 . 1 1 18 18 PRO CG C 13 28.2 0.1 . 1 . . . . . . . . 5757 1 89 . 1 1 18 18 PRO CD C 13 49.2 0.1 . 1 . . . . . . . . 5757 1 90 . 1 1 18 18 PRO C C 13 180.0 0.1 . 1 . . . . . . . . 5757 1 91 . 1 1 19 19 ALA N N 15 119.8 0.1 . 1 . . . . . . . . 5757 1 92 . 1 1 19 19 ALA CA C 13 55.5 0.1 . 1 . . . . . . . . 5757 1 93 . 1 1 19 19 ALA CB C 13 18.3 0.1 . 1 . . . . . . . . 5757 1 94 . 1 1 20 20 ALA N N 15 121.5 0.1 . 1 . . . . . . . . 5757 1 95 . 1 1 20 20 ALA CA C 13 54.8 0.1 . 1 . . . . . . . . 5757 1 96 . 1 1 20 20 ALA CB C 13 18.3 0.1 . 1 . . . . . . . . 5757 1 97 . 1 1 21 21 LEU N N 15 119.6 0.1 . 1 . . . . . . . . 5757 1 98 . 1 1 21 21 LEU CA C 13 56.9 0.1 . 1 . . . . . . . . 5757 1 99 . 1 1 21 21 LEU CB C 13 40.6 0.1 . 1 . . . . . . . . 5757 1 100 . 1 1 21 21 LEU CG C 13 26.9 0.1 . 1 . . . . . . . . 5757 1 101 . 1 1 21 21 LEU CD1 C 13 20.8 0.1 . 1 . . . . . . . . 5757 1 102 . 1 1 21 21 LEU CD2 C 13 20.8 0.1 . 1 . . . . . . . . 5757 1 103 . 1 1 21 21 LEU C C 13 178.6 0.1 . 1 . . . . . . . . 5757 1 104 . 1 1 22 22 PHE N N 15 122.6 0.1 . 1 . . . . . . . . 5757 1 105 . 1 1 22 22 PHE CA C 13 61.1 0.1 . 1 . . . . . . . . 5757 1 106 . 1 1 22 22 PHE CB C 13 38.4 0.1 . 1 . . . . . . . . 5757 1 107 . 1 1 22 22 PHE CG C 13 138.9 0.1 . 1 . . . . . . . . 5757 1 108 . 1 1 22 22 PHE CD1 C 13 131.6 0.1 . 1 . . . . . . . . 5757 1 109 . 1 1 22 22 PHE CD2 C 13 131.6 0.1 . 1 . . . . . . . . 5757 1 110 . 1 1 22 22 PHE C C 13 177.6 0.1 . 1 . . . . . . . . 5757 1 111 . 1 1 23 23 VAL N N 15 120.2 0.1 . 1 . . . . . . . . 5757 1 112 . 1 1 23 23 VAL CA C 13 66.6 0.1 . 1 . . . . . . . . 5757 1 113 . 1 1 23 23 VAL CB C 13 31.5 0.1 . 1 . . . . . . . . 5757 1 114 . 1 1 23 23 VAL CG1 C 13 22.0 0.1 . 2 . . . . . . . . 5757 1 115 . 1 1 23 23 VAL CG2 C 13 23.3 0.1 . 2 . . . . . . . . 5757 1 116 . 1 1 23 23 VAL C C 13 177.0 0.1 . 1 . . . . . . . . 5757 1 117 . 1 1 24 24 GLN N N 15 118.2 0.1 . 1 . . . . . . . . 5757 1 118 . 1 1 24 24 GLN CA C 13 58.7 0.1 . 1 . . . . . . . . 5757 1 119 . 1 1 24 24 GLN CB C 13 29.0 0.1 . 1 . . . . . . . . 5757 1 120 . 1 1 24 24 GLN CG C 13 34.2 0.1 . 1 . . . . . . . . 5757 1 121 . 1 1 24 24 GLN CD C 13 180.1 0.1 . 1 . . . . . . . . 5757 1 122 . 1 1 25 25 GLU N N 15 117.9 0.1 . 1 . . . . . . . . 5757 1 123 . 1 1 25 25 GLU CA C 13 57.8 0.1 . 1 . . . . . . . . 5757 1 124 . 1 1 25 25 GLU CB C 13 28.6 0.1 . 1 . . . . . . . . 5757 1 125 . 1 1 25 25 GLU CG C 13 34.4 0.1 . 1 . . . . . . . . 5757 1 126 . 1 1 25 25 GLU CD C 13 182.7 0.1 . 1 . . . . . . . . 5757 1 127 . 1 1 26 26 ALA N N 15 118.2 0.1 . 1 . . . . . . . . 5757 1 128 . 1 1 26 26 ALA CA C 13 54.6 0.1 . 1 . . . . . . . . 5757 1 129 . 1 1 26 26 ALA CB C 13 17.8 0.1 . 1 . . . . . . . . 5757 1 130 . 1 1 27 27 ASN N N 15 113.9 0.1 . 1 . . . . . . . . 5757 1 131 . 1 1 27 27 ASN CA C 13 53.8 0.1 . 1 . . . . . . . . 5757 1 132 . 1 1 27 27 ASN CB C 13 38.4 0.1 . 1 . . . . . . . . 5757 1 133 . 1 1 27 27 ASN CG C 13 176.1 0.1 . 1 . . . . . . . . 5757 1 134 . 1 1 27 27 ASN ND2 N 15 110.3 0.1 . 1 . . . . . . . . 5757 1 135 . 1 1 28 28 ARG N N 15 117.9 0.1 . 1 . . . . . . . . 5757 1 136 . 1 1 28 28 ARG CA C 13 57.2 0.1 . 1 . . . . . . . . 5757 1 137 . 1 1 28 28 ARG CB C 13 28.9 0.1 . 1 . . . . . . . . 5757 1 138 . 1 1 28 28 ARG CG C 13 27.4 0.1 . 1 . . . . . . . . 5757 1 139 . 1 1 28 28 ARG CD C 13 42.8 0.1 . 1 . . . . . . . . 5757 1 140 . 1 1 29 29 PHE N N 15 118.5 0.1 . 1 . . . . . . . . 5757 1 141 . 1 1 29 29 PHE CA C 13 56.8 0.1 . 1 . . . . . . . . 5757 1 142 . 1 1 29 29 PHE CB C 13 39.6 0.1 . 1 . . . . . . . . 5757 1 143 . 1 1 29 29 PHE CG C 13 140.5 0.1 . 1 . . . . . . . . 5757 1 144 . 1 1 29 29 PHE CD1 C 13 131.5 0.1 . 1 . . . . . . . . 5757 1 145 . 1 1 29 29 PHE CD2 C 13 131.5 0.1 . 1 . . . . . . . . 5757 1 146 . 1 1 29 29 PHE C C 13 175.8 0.1 . 1 . . . . . . . . 5757 1 147 . 1 1 30 30 THR N N 15 119.8 0.1 . 1 . . . . . . . . 5757 1 148 . 1 1 30 30 THR CA C 13 63.8 0.1 . 1 . . . . . . . . 5757 1 149 . 1 1 30 30 THR CB C 13 68.7 0.1 . 1 . . . . . . . . 5757 1 150 . 1 1 30 30 THR CG2 C 13 21.9 0.1 . 1 . . . . . . . . 5757 1 151 . 1 1 30 30 THR C C 13 177.7 0.1 . 1 . . . . . . . . 5757 1 152 . 1 1 31 31 SER N N 15 121.6 0.1 . 1 . . . . . . . . 5757 1 153 . 1 1 31 31 SER CA C 13 61.6 0.1 . 1 . . . . . . . . 5757 1 154 . 1 1 31 31 SER CB C 13 64.9 0.1 . 1 . . . . . . . . 5757 1 155 . 1 1 31 31 SER C C 13 173.7 0.1 . 1 . . . . . . . . 5757 1 156 . 1 1 32 32 ASP N N 15 121.5 0.1 . 1 . . . . . . . . 5757 1 157 . 1 1 32 32 ASP CA C 13 54.2 0.1 . 1 . . . . . . . . 5757 1 158 . 1 1 32 32 ASP CB C 13 42.2 0.1 . 1 . . . . . . . . 5757 1 159 . 1 1 32 32 ASP CG C 13 180.2 0.1 . 1 . . . . . . . . 5757 1 160 . 1 1 32 32 ASP C C 13 175.5 0.1 . 1 . . . . . . . . 5757 1 161 . 1 1 33 33 VAL N N 15 120.8 0.1 . 1 . . . . . . . . 5757 1 162 . 1 1 33 33 VAL CA C 13 59.6 0.1 . 1 . . . . . . . . 5757 1 163 . 1 1 33 33 VAL CB C 13 35.2 0.1 . 1 . . . . . . . . 5757 1 164 . 1 1 33 33 VAL CG1 C 13 22.2 0.1 . 2 . . . . . . . . 5757 1 165 . 1 1 33 33 VAL CG2 C 13 20.0 0.1 . 2 . . . . . . . . 5757 1 166 . 1 1 33 33 VAL C C 13 173.9 0.1 . 1 . . . . . . . . 5757 1 167 . 1 1 34 34 PHE N N 15 122.0 0.1 . 1 . . . . . . . . 5757 1 168 . 1 1 34 34 PHE CA C 13 55.0 0.1 . 1 . . . . . . . . 5757 1 169 . 1 1 34 34 PHE CB C 13 43.1 0.1 . 1 . . . . . . . . 5757 1 170 . 1 1 34 34 PHE CG C 13 138.7 0.1 . 1 . . . . . . . . 5757 1 171 . 1 1 34 34 PHE CD1 C 13 131.6 0.1 . 1 . . . . . . . . 5757 1 172 . 1 1 34 34 PHE CD2 C 13 131.6 0.1 . 1 . . . . . . . . 5757 1 173 . 1 1 34 34 PHE C C 13 174.9 0.1 . 1 . . . . . . . . 5757 1 174 . 1 1 35 35 LEU N N 15 117.7 0.1 . 1 . . . . . . . . 5757 1 175 . 1 1 35 35 LEU CA C 13 53.2 0.1 . 1 . . . . . . . . 5757 1 176 . 1 1 35 35 LEU CB C 13 46.3 0.1 . 1 . . . . . . . . 5757 1 177 . 1 1 35 35 LEU CG C 13 27.6 0.1 . 1 . . . . . . . . 5757 1 178 . 1 1 35 35 LEU CD1 C 13 24.2 0.1 . 2 . . . . . . . . 5757 1 179 . 1 1 35 35 LEU CD2 C 13 25.4 0.1 . 2 . . . . . . . . 5757 1 180 . 1 1 35 35 LEU C C 13 175.6 0.1 . 1 . . . . . . . . 5757 1 181 . 1 1 36 36 GLU N N 15 122.9 0.1 . 1 . . . . . . . . 5757 1 182 . 1 1 36 36 GLU CA C 13 53.8 0.1 . 1 . . . . . . . . 5757 1 183 . 1 1 36 36 GLU CB C 13 34.3 0.1 . 1 . . . . . . . . 5757 1 184 . 1 1 36 36 GLU CG C 13 36.3 0.1 . 1 . . . . . . . . 5757 1 185 . 1 1 36 36 GLU CD C 13 182.0 0.1 . 1 . . . . . . . . 5757 1 186 . 1 1 36 36 GLU C C 13 174.7 0.1 . 1 . . . . . . . . 5757 1 187 . 1 1 37 37 LYS N N 15 123.8 0.1 . 1 . . . . . . . . 5757 1 188 . 1 1 37 37 LYS CA C 13 55.8 0.1 . 1 . . . . . . . . 5757 1 189 . 1 1 37 37 LYS CB C 13 36.1 0.1 . 1 . . . . . . . . 5757 1 190 . 1 1 37 37 LYS CG C 13 25.0 0.1 . 1 . . . . . . . . 5757 1 191 . 1 1 37 37 LYS CD C 13 28.9 0.1 . 1 . . . . . . . . 5757 1 192 . 1 1 37 37 LYS CE C 13 42.1 0.1 . 1 . . . . . . . . 5757 1 193 . 1 1 38 38 ASP N N 15 129.9 0.1 . 1 . . . . . . . . 5757 1 194 . 1 1 38 38 ASP CA C 13 55.4 0.1 . 1 . . . . . . . . 5757 1 195 . 1 1 38 38 ASP CB C 13 39.6 0.1 . 1 . . . . . . . . 5757 1 196 . 1 1 38 38 ASP CG C 13 180.9 0.1 . 1 . . . . . . . . 5757 1 197 . 1 1 38 38 ASP C C 13 175.5 0.1 . 1 . . . . . . . . 5757 1 198 . 1 1 39 39 GLY N N 15 105.0 0.1 . 1 . . . . . . . . 5757 1 199 . 1 1 39 39 GLY CA C 13 45.0 0.1 . 1 . . . . . . . . 5757 1 200 . 1 1 39 39 GLY C C 13 173.8 0.1 . 1 . . . . . . . . 5757 1 201 . 1 1 40 40 LYS N N 15 122.6 0.1 . 1 . . . . . . . . 5757 1 202 . 1 1 40 40 LYS CA C 13 54.0 0.1 . 1 . . . . . . . . 5757 1 203 . 1 1 40 40 LYS CB C 13 33.3 0.1 . 1 . . . . . . . . 5757 1 204 . 1 1 40 40 LYS CG C 13 25.0 0.1 . 1 . . . . . . . . 5757 1 205 . 1 1 40 40 LYS CD C 13 28.9 0.1 . 1 . . . . . . . . 5757 1 206 . 1 1 40 40 LYS CE C 13 42.1 0.1 . 1 . . . . . . . . 5757 1 207 . 1 1 41 41 LYS N N 15 126.0 0.1 . 1 . . . . . . . . 5757 1 208 . 1 1 41 41 LYS CA C 13 54.1 0.1 . 1 . . . . . . . . 5757 1 209 . 1 1 41 41 LYS CB C 13 35.4 0.1 . 1 . . . . . . . . 5757 1 210 . 1 1 41 41 LYS CG C 13 25.2 0.1 . 1 . . . . . . . . 5757 1 211 . 1 1 41 41 LYS CD C 13 28.9 0.1 . 1 . . . . . . . . 5757 1 212 . 1 1 41 41 LYS CE C 13 40.7 0.1 . 1 . . . . . . . . 5757 1 213 . 1 1 42 42 VAL N N 15 118.8 0.1 . 1 . . . . . . . . 5757 1 214 . 1 1 42 42 VAL CA C 13 57.9 0.1 . 1 . . . . . . . . 5757 1 215 . 1 1 42 42 VAL CB C 13 35.0 0.1 . 1 . . . . . . . . 5757 1 216 . 1 1 42 42 VAL CG1 C 13 18.4 0.1 . 2 . . . . . . . . 5757 1 217 . 1 1 42 42 VAL CG2 C 13 21.6 0.1 . 2 . . . . . . . . 5757 1 218 . 1 1 43 43 ASN N N 15 121.4 0.1 . 1 . . . . . . . . 5757 1 219 . 1 1 43 43 ASN CA C 13 53.0 0.1 . 1 . . . . . . . . 5757 1 220 . 1 1 43 43 ASN CB C 13 38.1 0.1 . 1 . . . . . . . . 5757 1 221 . 1 1 43 43 ASN CG C 13 176.7 0.1 . 1 . . . . . . . . 5757 1 222 . 1 1 43 43 ASN C C 13 174.9 0.1 . 1 . . . . . . . . 5757 1 223 . 1 1 43 43 ASN ND2 N 15 111.0 0.1 . 1 . . . . . . . . 5757 1 224 . 1 1 44 44 ALA N N 15 128.4 0.1 . 1 . . . . . . . . 5757 1 225 . 1 1 44 44 ALA CA C 13 51.8 0.1 . 1 . . . . . . . . 5757 1 226 . 1 1 44 44 ALA CB C 13 18.9 0.1 . 1 . . . . . . . . 5757 1 227 . 1 1 44 44 ALA C C 13 173.8 0.1 . 1 . . . . . . . . 5757 1 228 . 1 1 45 45 LYS N N 15 110.2 0.1 . 1 . . . . . . . . 5757 1 229 . 1 1 45 45 LYS CA C 13 55.6 0.1 . 1 . . . . . . . . 5757 1 230 . 1 1 45 45 LYS CB C 13 31.5 0.1 . 1 . . . . . . . . 5757 1 231 . 1 1 45 45 LYS CG C 13 27.4 0.1 . 1 . . . . . . . . 5757 1 232 . 1 1 45 45 LYS CD C 13 29.5 0.1 . 1 . . . . . . . . 5757 1 233 . 1 1 45 45 LYS CE C 13 42.8 0.1 . 1 . . . . . . . . 5757 1 234 . 1 1 45 45 LYS C C 13 175.5 0.1 . 1 . . . . . . . . 5757 1 235 . 1 1 46 46 SER N N 15 114.9 0.1 . 1 . . . . . . . . 5757 1 236 . 1 1 46 46 SER CA C 13 54.2 0.1 . 1 . . . . . . . . 5757 1 237 . 1 1 46 46 SER CB C 13 64.6 0.1 . 1 . . . . . . . . 5757 1 238 . 1 1 46 46 SER C C 13 174.4 0.1 . 1 . . . . . . . . 5757 1 239 . 1 1 47 47 ILE N N 15 131.0 0.1 . 1 . . . . . . . . 5757 1 240 . 1 1 47 47 ILE CA C 13 66.4 0.1 . 1 . . . . . . . . 5757 1 241 . 1 1 47 47 ILE CB C 13 37.7 0.1 . 1 . . . . . . . . 5757 1 242 . 1 1 47 47 ILE CG1 C 13 30.4 0.1 . 1 . . . . . . . . 5757 1 243 . 1 1 47 47 ILE CG2 C 13 17.8 0.1 . 1 . . . . . . . . 5757 1 244 . 1 1 47 47 ILE CD1 C 13 14.1 0.1 . 1 . . . . . . . . 5757 1 245 . 1 1 47 47 ILE C C 13 178.0 0.1 . 1 . . . . . . . . 5757 1 246 . 1 1 48 48 MET N N 15 117.7 0.1 . 1 . . . . . . . . 5757 1 247 . 1 1 48 48 MET CA C 13 58.3 0.1 . 1 . . . . . . . . 5757 1 248 . 1 1 48 48 MET CB C 13 32.3 0.1 . 1 . . . . . . . . 5757 1 249 . 1 1 48 48 MET CG C 13 32.2 0.1 . 1 . . . . . . . . 5757 1 250 . 1 1 48 48 MET CE C 13 15.9 0.1 . 1 . . . . . . . . 5757 1 251 . 1 1 49 49 GLY N N 15 107.9 0.1 . 1 . . . . . . . . 5757 1 252 . 1 1 49 49 GLY CA C 13 46.9 0.1 . 1 . . . . . . . . 5757 1 253 . 1 1 49 49 GLY C C 13 176.9 0.1 . 1 . . . . . . . . 5757 1 254 . 1 1 50 50 LEU N N 15 124.8 0.1 . 1 . . . . . . . . 5757 1 255 . 1 1 50 50 LEU CA C 13 58.2 0.1 . 1 . . . . . . . . 5757 1 256 . 1 1 50 50 LEU CB C 13 43.3 0.1 . 1 . . . . . . . . 5757 1 257 . 1 1 50 50 LEU C C 13 179.7 0.1 . 1 . . . . . . . . 5757 1 258 . 1 1 51 51 MET N N 15 114.3 0.1 . 1 . . . . . . . . 5757 1 259 . 1 1 51 51 MET CA C 13 59.1 0.1 . 1 . . . . . . . . 5757 1 260 . 1 1 51 51 MET CB C 13 33.6 0.1 . 1 . . . . . . . . 5757 1 261 . 1 1 51 51 MET CG C 13 33.5 0.1 . 1 . . . . . . . . 5757 1 262 . 1 1 51 51 MET CE C 13 15.8 0.1 . 1 . . . . . . . . 5757 1 263 . 1 1 52 52 SER N N 15 112.3 0.1 . 1 . . . . . . . . 5757 1 264 . 1 1 52 52 SER CA C 13 59.8 0.1 . 1 . . . . . . . . 5757 1 265 . 1 1 52 52 SER CB C 13 63.8 0.1 . 1 . . . . . . . . 5757 1 266 . 1 1 52 52 SER C C 13 175.2 0.1 . 1 . . . . . . . . 5757 1 267 . 1 1 53 53 LEU N N 15 122.0 0.1 . 1 . . . . . . . . 5757 1 268 . 1 1 53 53 LEU CA C 13 54.2 0.1 . 1 . . . . . . . . 5757 1 269 . 1 1 53 53 LEU CB C 13 42.8 0.1 . 1 . . . . . . . . 5757 1 270 . 1 1 53 53 LEU CG C 13 26.1 0.1 . 1 . . . . . . . . 5757 1 271 . 1 1 53 53 LEU CD1 C 13 22.4 0.1 . 1 . . . . . . . . 5757 1 272 . 1 1 53 53 LEU CD2 C 13 22.4 0.1 . 1 . . . . . . . . 5757 1 273 . 1 1 54 54 ALA N N 15 131.2 0.1 . 1 . . . . . . . . 5757 1 274 . 1 1 54 54 ALA CA C 13 51.8 0.1 . 1 . . . . . . . . 5757 1 275 . 1 1 54 54 ALA CB C 13 17.1 0.1 . 1 . . . . . . . . 5757 1 276 . 1 1 54 54 ALA C C 13 176.8 0.1 . 1 . . . . . . . . 5757 1 277 . 1 1 55 55 VAL N N 15 121.2 0.1 . 1 . . . . . . . . 5757 1 278 . 1 1 55 55 VAL CA C 13 60.2 0.1 . 1 . . . . . . . . 5757 1 279 . 1 1 55 55 VAL CB C 13 37.1 0.1 . 1 . . . . . . . . 5757 1 280 . 1 1 55 55 VAL CG1 C 13 20.0 0.1 . 2 . . . . . . . . 5757 1 281 . 1 1 55 55 VAL CG2 C 13 22.9 0.1 . 2 . . . . . . . . 5757 1 282 . 1 1 55 55 VAL C C 13 180.9 0.1 . 1 . . . . . . . . 5757 1 283 . 1 1 56 56 SER N N 15 118.0 0.1 . 1 . . . . . . . . 5757 1 284 . 1 1 56 56 SER CA C 13 56.7 0.1 . 1 . . . . . . . . 5757 1 285 . 1 1 56 56 SER CB C 13 65.9 0.1 . 1 . . . . . . . . 5757 1 286 . 1 1 56 56 SER C C 13 173.5 0.1 . 1 . . . . . . . . 5757 1 287 . 1 1 57 57 THR N N 15 122.4 0.1 . 1 . . . . . . . . 5757 1 288 . 1 1 57 57 THR CA C 13 65.8 0.1 . 1 . . . . . . . . 5757 1 289 . 1 1 57 57 THR CB C 13 68.4 0.1 . 1 . . . . . . . . 5757 1 290 . 1 1 57 57 THR CG2 C 13 22.4 0.1 . 1 . . . . . . . . 5757 1 291 . 1 1 57 57 THR C C 13 175.8 0.1 . 1 . . . . . . . . 5757 1 292 . 1 1 58 58 GLY N N 15 117.1 0.1 . 1 . . . . . . . . 5757 1 293 . 1 1 58 58 GLY CA C 13 44.4 0.1 . 1 . . . . . . . . 5757 1 294 . 1 1 58 58 GLY C C 13 173.9 0.1 . 1 . . . . . . . . 5757 1 295 . 1 1 59 59 THR N N 15 117.2 0.1 . 1 . . . . . . . . 5757 1 296 . 1 1 59 59 THR CA C 13 63.0 0.1 . 1 . . . . . . . . 5757 1 297 . 1 1 59 59 THR CB C 13 68.8 0.1 . 1 . . . . . . . . 5757 1 298 . 1 1 59 59 THR CG2 C 13 22.4 0.1 . 1 . . . . . . . . 5757 1 299 . 1 1 59 59 THR C C 13 172.4 0.1 . 1 . . . . . . . . 5757 1 300 . 1 1 60 60 GLU N N 15 121.8 0.1 . 1 . . . . . . . . 5757 1 301 . 1 1 60 60 GLU CA C 13 54.3 0.1 . 1 . . . . . . . . 5757 1 302 . 1 1 60 60 GLU CB C 13 32.7 0.1 . 1 . . . . . . . . 5757 1 303 . 1 1 60 60 GLU CG C 13 36.3 0.1 . 1 . . . . . . . . 5757 1 304 . 1 1 60 60 GLU CD C 13 183.2 0.1 . 1 . . . . . . . . 5757 1 305 . 1 1 61 61 VAL N N 15 118.9 0.1 . 1 . . . . . . . . 5757 1 306 . 1 1 61 61 VAL CA C 13 58.4 0.1 . 1 . . . . . . . . 5757 1 307 . 1 1 61 61 VAL CB C 13 34.8 0.1 . 1 . . . . . . . . 5757 1 308 . 1 1 61 61 VAL CG1 C 13 22.9 0.1 . 2 . . . . . . . . 5757 1 309 . 1 1 61 61 VAL CG2 C 13 19.8 0.1 . 2 . . . . . . . . 5757 1 310 . 1 1 62 62 THR N N 15 117.2 0.1 . 1 . . . . . . . . 5757 1 311 . 1 1 62 62 THR CA C 13 62.6 0.1 . 1 . . . . . . . . 5757 1 312 . 1 1 62 62 THR CB C 13 69.1 0.1 . 1 . . . . . . . . 5757 1 313 . 1 1 62 62 THR CG2 C 13 22.5 0.1 . 1 . . . . . . . . 5757 1 314 . 1 1 62 62 THR C C 13 172.6 0.1 . 1 . . . . . . . . 5757 1 315 . 1 1 63 63 LEU N N 15 131.0 0.1 . 1 . . . . . . . . 5757 1 316 . 1 1 63 63 LEU CA C 13 53.8 0.1 . 1 . . . . . . . . 5757 1 317 . 1 1 63 63 LEU CB C 13 45.0 0.1 . 1 . . . . . . . . 5757 1 318 . 1 1 63 63 LEU CG C 13 27.6 0.1 . 1 . . . . . . . . 5757 1 319 . 1 1 63 63 LEU CD1 C 13 24.2 0.1 . 1 . . . . . . . . 5757 1 320 . 1 1 63 63 LEU CD2 C 13 24.2 0.1 . 1 . . . . . . . . 5757 1 321 . 1 1 64 64 ILE N N 15 125.8 0.1 . 1 . . . . . . . . 5757 1 322 . 1 1 64 64 ILE CA C 13 59.8 0.1 . 1 . . . . . . . . 5757 1 323 . 1 1 64 64 ILE CB C 13 42.6 0.1 . 1 . . . . . . . . 5757 1 324 . 1 1 64 64 ILE CG1 C 13 28.0 0.1 . 1 . . . . . . . . 5757 1 325 . 1 1 64 64 ILE CG2 C 13 17.8 0.1 . 1 . . . . . . . . 5757 1 326 . 1 1 64 64 ILE CD1 C 13 15.0 0.1 . 1 . . . . . . . . 5757 1 327 . 1 1 64 64 ILE C C 13 173.9 0.1 . 1 . . . . . . . . 5757 1 328 . 1 1 65 65 ALA N N 15 126.4 0.1 . 1 . . . . . . . . 5757 1 329 . 1 1 65 65 ALA CA C 13 50.0 0.1 . 1 . . . . . . . . 5757 1 330 . 1 1 65 65 ALA CB C 13 23.0 0.1 . 1 . . . . . . . . 5757 1 331 . 1 1 65 65 ALA C C 13 175.9 0.1 . 1 . . . . . . . . 5757 1 332 . 1 1 66 66 GLN N N 15 120.1 0.1 . 1 . . . . . . . . 5757 1 333 . 1 1 66 66 GLN CA C 13 53.7 0.1 . 1 . . . . . . . . 5757 1 334 . 1 1 66 66 GLN CB C 13 32.1 0.1 . 1 . . . . . . . . 5757 1 335 . 1 1 66 66 GLN CG C 13 33.4 0.1 . 1 . . . . . . . . 5757 1 336 . 1 1 66 66 GLN CD C 13 179.1 0.1 . 1 . . . . . . . . 5757 1 337 . 1 1 66 66 GLN C C 13 174.2 0.1 . 1 . . . . . . . . 5757 1 338 . 1 1 67 67 GLY N N 15 119.5 0.1 . 1 . . . . . . . . 5757 1 339 . 1 1 67 67 GLY CA C 13 45.2 0.1 . 1 . . . . . . . . 5757 1 340 . 1 1 67 67 GLY C C 13 174.9 0.1 . 1 . . . . . . . . 5757 1 341 . 1 1 68 68 GLU N N 15 118.7 0.1 . 1 . . . . . . . . 5757 1 342 . 1 1 68 68 GLU CA C 13 59.2 0.1 . 1 . . . . . . . . 5757 1 343 . 1 1 68 68 GLU CB C 13 29.9 0.1 . 1 . . . . . . . . 5757 1 344 . 1 1 68 68 GLU CG C 13 36.2 0.1 . 1 . . . . . . . . 5757 1 345 . 1 1 68 68 GLU CD C 13 183.3 0.1 . 1 . . . . . . . . 5757 1 346 . 1 1 69 69 ASP N N 15 114.8 0.1 . 1 . . . . . . . . 5757 1 347 . 1 1 69 69 ASP CA C 13 51.1 0.1 . 1 . . . . . . . . 5757 1 348 . 1 1 69 69 ASP CB C 13 39.4 0.1 . 1 . . . . . . . . 5757 1 349 . 1 1 69 69 ASP CG C 13 179.6 0.1 . 1 . . . . . . . . 5757 1 350 . 1 1 69 69 ASP C C 13 176.2 0.1 . 1 . . . . . . . . 5757 1 351 . 1 1 70 70 GLU N N 15 116.3 0.1 . 1 . . . . . . . . 5757 1 352 . 1 1 70 70 GLU CA C 13 57.4 0.1 . 1 . . . . . . . . 5757 1 353 . 1 1 70 70 GLU CB C 13 27.2 0.1 . 1 . . . . . . . . 5757 1 354 . 1 1 70 70 GLU CG C 13 36.9 0.1 . 1 . . . . . . . . 5757 1 355 . 1 1 70 70 GLU CD C 13 184.5 0.1 . 1 . . . . . . . . 5757 1 356 . 1 1 70 70 GLU C C 13 175.1 0.1 . 1 . . . . . . . . 5757 1 357 . 1 1 71 71 GLN N N 15 121.4 0.1 . 1 . . . . . . . . 5757 1 358 . 1 1 71 71 GLN CA C 13 59.5 0.1 . 1 . . . . . . . . 5757 1 359 . 1 1 71 71 GLN CB C 13 27.7 0.1 . 1 . . . . . . . . 5757 1 360 . 1 1 71 71 GLN CG C 13 33.8 0.1 . 1 . . . . . . . . 5757 1 361 . 1 1 71 71 GLN CD C 13 179.7 0.1 . 1 . . . . . . . . 5757 1 362 . 1 1 72 72 GLU N N 15 117.1 0.1 . 1 . . . . . . . . 5757 1 363 . 1 1 72 72 GLU CA C 13 59.3 0.1 . 1 . . . . . . . . 5757 1 364 . 1 1 72 72 GLU CB C 13 26.8 0.1 . 1 . . . . . . . . 5757 1 365 . 1 1 72 72 GLU CG C 13 34.2 0.1 . 1 . . . . . . . . 5757 1 366 . 1 1 72 72 GLU CD C 13 183.2 0.1 . 1 . . . . . . . . 5757 1 367 . 1 1 73 73 ALA N N 15 122.4 0.1 . 1 . . . . . . . . 5757 1 368 . 1 1 73 73 ALA CA C 13 53.5 0.1 . 1 . . . . . . . . 5757 1 369 . 1 1 73 73 ALA CB C 13 17.9 0.1 . 1 . . . . . . . . 5757 1 370 . 1 1 73 73 ALA C C 13 178.7 0.1 . 1 . . . . . . . . 5757 1 371 . 1 1 74 74 LEU N N 15 116.5 0.1 . 1 . . . . . . . . 5757 1 372 . 1 1 74 74 LEU CA C 13 58.0 0.1 . 1 . . . . . . . . 5757 1 373 . 1 1 74 74 LEU CB C 13 42.1 0.1 . 1 . . . . . . . . 5757 1 374 . 1 1 74 74 LEU CG C 13 26.0 0.1 . 1 . . . . . . . . 5757 1 375 . 1 1 74 74 LEU CD1 C 13 24.3 0.1 . 1 . . . . . . . . 5757 1 376 . 1 1 74 74 LEU CD2 C 13 24.3 0.1 . 1 . . . . . . . . 5757 1 377 . 1 1 75 75 GLU N N 15 116.9 0.1 . 1 . . . . . . . . 5757 1 378 . 1 1 75 75 GLU CA C 13 58.9 0.1 . 1 . . . . . . . . 5757 1 379 . 1 1 75 75 GLU CB C 13 29.4 0.1 . 1 . . . . . . . . 5757 1 380 . 1 1 75 75 GLU CG C 13 36.2 0.1 . 1 . . . . . . . . 5757 1 381 . 1 1 75 75 GLU CD C 13 182.6 0.1 . 1 . . . . . . . . 5757 1 382 . 1 1 75 75 GLU C C 13 176.2 0.1 . 1 . . . . . . . . 5757 1 383 . 1 1 76 76 LYS N N 15 118.9 0.1 . 1 . . . . . . . . 5757 1 384 . 1 1 76 76 LYS CA C 13 59.0 0.1 . 1 . . . . . . . . 5757 1 385 . 1 1 76 76 LYS CB C 13 32.2 0.1 . 1 . . . . . . . . 5757 1 386 . 1 1 76 76 LYS CG C 13 24.8 0.1 . 1 . . . . . . . . 5757 1 387 . 1 1 76 76 LYS CD C 13 28.6 0.1 . 1 . . . . . . . . 5757 1 388 . 1 1 76 76 LYS CE C 13 42.1 0.1 . 1 . . . . . . . . 5757 1 389 . 1 1 77 77 LEU N N 15 119.3 0.1 . 1 . . . . . . . . 5757 1 390 . 1 1 77 77 LEU CA C 13 57.5 0.1 . 1 . . . . . . . . 5757 1 391 . 1 1 77 77 LEU CB C 13 40.9 0.1 . 1 . . . . . . . . 5757 1 392 . 1 1 77 77 LEU CG C 13 26.8 0.1 . 1 . . . . . . . . 5757 1 393 . 1 1 77 77 LEU CD1 C 13 22.5 0.1 . 1 . . . . . . . . 5757 1 394 . 1 1 77 77 LEU CD2 C 13 22.5 0.1 . 1 . . . . . . . . 5757 1 395 . 1 1 77 77 LEU C C 13 179.1 0.1 . 1 . . . . . . . . 5757 1 396 . 1 1 78 78 ALA N N 15 121.1 0.1 . 1 . . . . . . . . 5757 1 397 . 1 1 78 78 ALA CA C 13 55.1 0.1 . 1 . . . . . . . . 5757 1 398 . 1 1 78 78 ALA CB C 13 18.2 0.1 . 1 . . . . . . . . 5757 1 399 . 1 1 78 78 ALA C C 13 181.5 0.1 . 1 . . . . . . . . 5757 1 400 . 1 1 79 79 ALA N N 15 120.1 0.1 . 1 . . . . . . . . 5757 1 401 . 1 1 79 79 ALA CA C 13 55.6 0.1 . 1 . . . . . . . . 5757 1 402 . 1 1 79 79 ALA CB C 13 18.7 0.1 . 1 . . . . . . . . 5757 1 403 . 1 1 79 79 ALA C C 13 180.9 0.1 . 1 . . . . . . . . 5757 1 404 . 1 1 80 80 TYR N N 15 116.8 0.1 . 1 . . . . . . . . 5757 1 405 . 1 1 80 80 TYR CA C 13 61.3 0.1 . 1 . . . . . . . . 5757 1 406 . 1 1 80 80 TYR CB C 13 38.0 0.1 . 1 . . . . . . . . 5757 1 407 . 1 1 80 80 TYR CG C 13 129.7 0.1 . 1 . . . . . . . . 5757 1 408 . 1 1 80 80 TYR CD1 C 13 132.8 0.1 . 1 . . . . . . . . 5757 1 409 . 1 1 80 80 TYR CD2 C 13 132.8 0.1 . 1 . . . . . . . . 5757 1 410 . 1 1 80 80 TYR CE1 C 13 118.2 0.1 . 1 . . . . . . . . 5757 1 411 . 1 1 80 80 TYR CE2 C 13 118.2 0.1 . 1 . . . . . . . . 5757 1 412 . 1 1 80 80 TYR CZ C 13 157.3 0.1 . 1 . . . . . . . . 5757 1 413 . 1 1 80 80 TYR C C 13 176.8 0.1 . 1 . . . . . . . . 5757 1 414 . 1 1 81 81 VAL N N 15 117.8 0.1 . 1 . . . . . . . . 5757 1 415 . 1 1 81 81 VAL CA C 13 64.6 0.1 . 1 . . . . . . . . 5757 1 416 . 1 1 81 81 VAL CB C 13 32.2 0.1 . 1 . . . . . . . . 5757 1 417 . 1 1 81 81 VAL CG1 C 13 22.1 0.1 . 2 . . . . . . . . 5757 1 418 . 1 1 81 81 VAL CG2 C 13 23.5 0.1 . 2 . . . . . . . . 5757 1 419 . 1 1 81 81 VAL C C 13 174.6 0.1 . 1 . . . . . . . . 5757 1 420 . 1 1 82 82 GLN N N 15 113.4 0.1 . 1 . . . . . . . . 5757 1 421 . 1 1 82 82 GLN CA C 13 55.7 0.1 . 1 . . . . . . . . 5757 1 422 . 1 1 82 82 GLN CB C 13 29.9 0.1 . 1 . . . . . . . . 5757 1 423 . 1 1 82 82 GLN CG C 13 35.1 0.1 . 1 . . . . . . . . 5757 1 424 . 1 1 82 82 GLN CD C 13 179.0 0.1 . 1 . . . . . . . . 5757 1 425 . 1 1 83 83 GLU N N 15 114.9 0.1 . 1 . . . . . . . . 5757 1 426 . 1 1 83 83 GLU CA C 13 55.7 0.1 . 1 . . . . . . . . 5757 1 427 . 1 1 83 83 GLU CB C 13 30.0 0.1 . 1 . . . . . . . . 5757 1 428 . 1 1 83 83 GLU CG C 13 36.2 0.1 . 1 . . . . . . . . 5757 1 429 . 1 1 83 83 GLU CD C 13 181.7 0.1 . 1 . . . . . . . . 5757 1 430 . 1 1 84 84 GLU N N 15 114.9 0.1 . 1 . . . . . . . . 5757 1 431 . 1 1 84 84 GLU CA C 13 55.3 0.1 . 1 . . . . . . . . 5757 1 432 . 1 1 84 84 GLU CB C 13 29.8 0.1 . 1 . . . . . . . . 5757 1 433 . 1 1 84 84 GLU CG C 13 36.2 0.1 . 1 . . . . . . . . 5757 1 434 . 1 1 84 84 GLU CD C 13 181.7 0.1 . 1 . . . . . . . . 5757 1 435 . 1 1 85 85 VAL N N 15 93.4 0.1 . 1 . . . . . . . . 5757 1 436 . 1 1 85 85 VAL CA C 13 60.6 0.1 . 1 . . . . . . . . 5757 1 437 . 1 1 85 85 VAL CB C 13 32.7 0.1 . 1 . . . . . . . . 5757 1 438 . 1 1 85 85 VAL CG2 C 13 19.3 0.1 . 2 . . . . . . . . 5757 1 439 . 1 1 85 85 VAL CG1 C 13 21.3 0.1 . 2 . . . . . . . . 5757 1 440 . 1 1 85 85 VAL C C 13 171.1 0.1 . 1 . . . . . . . . 5757 1 stop_ save_ save_shift_set_2 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_2 _Assigned_chem_shift_list.Entry_ID 5757 _Assigned_chem_shift_list.ID 2 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-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 ; Peak doubling has been observed for a limited number of signals, indicating conformational or dynamic disorder. The minor signals are reported in this list. ; _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 . 5757 2 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 10 10 LEU CA C 13 53.1 0.1 . 1 . . . . . . . . 5757 2 2 . 1 1 10 10 LEU CB C 13 42.6 0.1 . 1 . . . . . . . . 5757 2 3 . 1 1 12 12 THR N N 15 111.0 0.1 . 1 . . . . . . . . 5757 2 4 . 1 1 18 18 PRO C C 13 178.8 0.1 . 1 . . . . . . . . 5757 2 5 . 1 1 38 38 ASP CB C 13 40.0 0.1 . 1 . . . . . . . . 5757 2 6 . 1 1 38 38 ASP CG C 13 181.7 0.1 . 1 . . . . . . . . 5757 2 7 . 1 1 49 49 GLY N N 15 109.5 0.1 . 1 . . . . . . . . 5757 2 8 . 1 1 52 52 SER N N 15 113.1 0.1 . 1 . . . . . . . . 5757 2 9 . 1 1 54 54 ALA C C 13 175.7 0.1 . 1 . . . . . . . . 5757 2 10 . 1 1 67 67 GLY N N 15 117.1 0.1 . 1 . . . . . . . . 5757 2 stop_ save_