data_5669 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5669 _Entry.Title ; Structure and Ubiquitin Interactions of the Conserved NZF Domain of Npl4 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2003-01-23 _Entry.Accession_date 2003-01-23 _Entry.Last_release_date 2003-06-10 _Entry.Original_release_date 2003-06-10 _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 B. Wang . . . 5669 2 S. Alam . L. . 5669 3 H. Meyer . H. . 5669 4 M. Payne . . . 5669 5 T. Stemmler . L. . 5669 6 D. Davis . R. . 5669 7 W. Sundquist . I. . 5669 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5669 coupling_constants 1 5669 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 109 5669 '15N chemical shifts' 30 5669 '1H chemical shifts' 164 5669 'coupling constants' 13 5669 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 . . 2003-06-10 2003-01-23 original author . 5669 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 1NJ3 'BMRB Entry Tracking System' 5669 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5669 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 22651060 _Citation.DOI . _Citation.PubMed_ID 12644454 _Citation.Full_citation . _Citation.Title ; Structure and Ubiquitin Interactions of the Conserved Zinc Finger Domain of Npl4 ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full . _Citation.Journal_volume 278 _Citation.Journal_issue 22 _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 20225 _Citation.Page_last 20234 _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 B. Wang . . . 5669 1 2 S. Alam . L. . 5669 1 3 H. Meyer . H. . 5669 1 4 M. Payne . . . 5669 1 5 T. Stemmler . L. . 5669 1 6 D. Davis . R. . 5669 1 7 W. Sundquist . I. . 5669 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID beta-ribbon 5669 1 Npl4 5669 1 'NZF domain' 5669 1 'rubredoxin knuckle' 5669 1 ubiquitin 5669 1 zinc-finger 5669 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5669 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 12411482 _Citation.Full_citation ; Meyer HH, Wang Y, Warren G. Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4. EMBO J. 2002 Nov 1;21(21):5645-52. ; _Citation.Title 'Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'EMBO J.' _Citation.Journal_name_full 'The EMBO journal' _Citation.Journal_volume 21 _Citation.Journal_issue 21 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0261-4189 _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 5645 _Citation.Page_last 5652 _Citation.Year 2002 _Citation.Details ; The multiple functions of the p97/Cdc48p ATPase can be explained largely by adaptors that link its activity to different cellular pathways, but how these adaptors recognize different substrates is unclear. Here we present evidence that the mammalian adaptors, p47 and Ufd1-Npl4, both bind ubiquitin conjugates directly and so link p97 to ubiquitylated substrates. In the case of Ufd1-Npl4, which is involved in endoplasmic reticulum (ER)-associated degradation and nuclear envelope reassembly, binding to ubiquitin is mediated through a putative zinc finger in Npl4. This novel domain (NZF) is conserved in metazoa and is both present and functional in other proteins. In the case of p47, which is involved in the reassembly of the ER, the nuclear envelope and the Golgi apparatus, binding is mediated by a UBA domain. Unlike Ufd1-Npl4, it binds ubiquitin only when complexed with p97, and binds mono- rather than polyubiquitin conjugates. The UBA domain is required for the function of p47 in mitotic Golgi reassembly. Together, these data suggest that ubiquitin recognition is a common feature of p97-mediated reactions. ; 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 'Hemmo H.' Meyer H. H. . 5669 2 2 Yanzhuang Wang Y. . . 5669 2 3 Graham Warren G. . . 5669 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 5669 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11781570 _Citation.Full_citation ; Hetzer M, Meyer HH, Walther TC, Bilbao-Cortes D, Warren G, Mattaj IW. Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly. Nat Cell Biol. 2001 Dec;3(12):1086-91. ; _Citation.Title 'Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Nat. Cell Biol.' _Citation.Journal_name_full 'Nature cell biology' _Citation.Journal_volume 3 _Citation.Journal_issue 12 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1465-7392 _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 1086 _Citation.Page_last 1091 _Citation.Year 2001 _Citation.Details ; Although nuclear envelope (NE) assembly is known to require the GTPase Ran, the membrane fusion machinery involved is uncharacterized. NE assembly involves formation of a reticular network on chromatin, fusion of this network into a closed NE and subsequent expansion. Here we show that p97, an AAA-ATPase previously implicated in fusion of Golgi and transitional endoplasmic reticulum (ER) membranes together with the adaptor p47, has two discrete functions in NE assembly. Formation of a closed NE requires the p97-Ufd1-Npl4 complex, not previously implicated in membrane fusion. Subsequent NE growth involves a p97-p47 complex. This study provides the first insights into the molecular mechanisms and specificity of fusion events involved in NE formation. ; 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. Hetzer M. . . 5669 3 2 'H. H.' Meyer H. H. . 5669 3 3 'T. C.' Walther T. C. . 5669 3 4 D. Bilbao-Cortes D. . . 5669 3 5 G. Warren G. . . 5669 3 6 'I. W.' Mattaj I. W. . 5669 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 5669 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11740563 _Citation.Full_citation ; Ye Y, Meyer HH, Rapoport TA. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature. 2001 Dec 6;414(6864):652-6. ; _Citation.Title 'The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Nature _Citation.Journal_name_full Nature _Citation.Journal_volume 414 _Citation.Journal_issue 6864 _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 652 _Citation.Page_last 656 _Citation.Year 2001 _Citation.Details ; In eukaryotic cells, incorrectly folded proteins in the endoplasmic reticulum (ER) are exported into the cytosol and degraded by the proteasome. This pathway is co-opted by some viruses. For example, the US11 protein of the human cytomegalovirus targets the major histocompatibility complex class I heavy chain for cytosolic degradation. How proteins are extracted from the ER membrane is unknown. In bacteria and mitochondria, members of the AAA ATPase family are involved in extracting and degrading membrane proteins. Here we demonstrate that another member of this family, Cdc48 in yeast and p97 in mammals, is required for the export of ER proteins into the cytosol. Whereas Cdc48/p97 was previously known to function in a complex with the cofactor p47 (ref. 5) in membrane fusion, we demonstrate that its role in ER protein export requires the interacting partners Ufd1 and Npl4. The AAA ATPase interacts with substrates at the ER membrane and is needed to release them as polyubiquitinated species into the cytosol. We propose that the Cdc48/p97-Ufd1-Npl4 complex extracts proteins from the ER membrane for cytosolic degradation. ; 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 Y. Ye Y. . . 5669 4 2 'H. H.' Meyer H. H. . 5669 4 3 'T. A.' Rapoport T. A. . 5669 4 stop_ save_ save_ref_4 _Citation.Sf_category citations _Citation.Sf_framecode ref_4 _Citation.Entry_ID 5669 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10811609 _Citation.Full_citation ; Meyer HH, Shorter JG, Seemann J, Pappin D, Warren G. A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J. 2000 May 15;19(10):2181-92. ; _Citation.Title 'A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'EMBO J.' _Citation.Journal_name_full 'The EMBO journal' _Citation.Journal_volume 19 _Citation.Journal_issue 10 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0261-4189 _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 2181 _Citation.Page_last 2192 _Citation.Year 2000 _Citation.Details ; The AAA-ATPase, p97/Cdc48p, has been implicated in many different pathways ranging from membrane fusion to ubiquitin-dependent protein degradation. Binding of the p47 complex directs p97 to act in the post-mitotic fusion of Golgi membranes. We now describe another binding complex comprising mammalian Ufd1 and Npl4. Yeast Ufd1p is required for ubiquitin-dependent protein degradation whereas yeast Npl4p has been implicated in nuclear transport. In rat liver cytosol, Ufd1 and Npl4 form a binary complex, which exists either alone or bound to p97. Ufd1/Npl4 competes with p47 for binding to p97 and so inhibits Golgi membrane fusion. This suggests that it is involved in another cellular function catalysed by p97, the most likely being ubiquitin-dependent events during mitosis. The fact that the binding of p47 and Ufd1/Npl4 is mutually exclusive suggests that these protein complexes act as adapters, directing a basic p97 activity into different cellular pathways. ; 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 'H. H.' Meyer H. H. . 5669 5 2 'J. G.' Shorter J. G. . 5669 5 3 J. Seemann J. . . 5669 5 4 D. Pappin D. . . 5669 5 5 G. Warren G. . . 5669 5 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_NZF _Assembly.Sf_category assembly _Assembly.Sf_framecode system_NZF _Assembly.Entry_ID 5669 _Assembly.ID 1 _Assembly.Name 'Npl4 Zinc Finger domain' _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 'all other bound' _Assembly.Molecular_mass 3438.35 _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 5669 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 'Npl4 Zinc Finger domain' 1 $NPL4-NZF . . . native . . . . . 5669 1 2 'ZINC ION' 2 $ZN . . . native . . . . . 5669 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 'metal coordination' single . 1 . 1 CYS 9 9 SG . 2 . 2 ZN 1 1 ZN . . . . . . . . . . 5669 1 2 'metal coordination' single . 1 . 1 CYS 12 12 SG . 2 . 2 ZN 1 1 ZN . . . . . . . . . . 5669 1 3 'metal coordination' single . 1 . 1 CYS 23 23 SG . 2 . 2 ZN 1 1 ZN . . . . . . . . . . 5669 1 4 'metal coordination' single . 1 . 1 CYS 26 26 SG . 2 . 2 ZN 1 1 ZN . . . . . . . . . . 5669 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 1NJ3 . . . . . . 5669 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Npl4 Zinc Finger domain' system 5669 1 NZF abbreviation 5669 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'ubiquitin binding domain' 5669 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_NPL4-NZF _Entity.Sf_category entity _Entity.Sf_framecode NPL4-NZF _Entity.Entry_ID 5669 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Npl4 Zinc Finger' _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 ; GSTSAMWACQHCTFMNQPGT GHCEMCSLPRT ; _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 31 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all other bound' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 3373 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details 'Contains zinc-ion coordinated by four cysteine residues.' _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Npl4 Zinc Finger' common 5669 1 NZF abbreviation 5669 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 . GLY . 5669 1 2 . SER . 5669 1 3 . THR . 5669 1 4 . SER . 5669 1 5 . ALA . 5669 1 6 . MET . 5669 1 7 . TRP . 5669 1 8 . ALA . 5669 1 9 . CYS . 5669 1 10 . GLN . 5669 1 11 . HIS . 5669 1 12 . CYS . 5669 1 13 . THR . 5669 1 14 . PHE . 5669 1 15 . MET . 5669 1 16 . ASN . 5669 1 17 . GLN . 5669 1 18 . PRO . 5669 1 19 . GLY . 5669 1 20 . THR . 5669 1 21 . GLY . 5669 1 22 . HIS . 5669 1 23 . CYS . 5669 1 24 . GLU . 5669 1 25 . MET . 5669 1 26 . CYS . 5669 1 27 . SER . 5669 1 28 . LEU . 5669 1 29 . PRO . 5669 1 30 . ARG . 5669 1 31 . THR . 5669 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 . GLY 1 1 5669 1 . SER 2 2 5669 1 . THR 3 3 5669 1 . SER 4 4 5669 1 . ALA 5 5 5669 1 . MET 6 6 5669 1 . TRP 7 7 5669 1 . ALA 8 8 5669 1 . CYS 9 9 5669 1 . GLN 10 10 5669 1 . HIS 11 11 5669 1 . CYS 12 12 5669 1 . THR 13 13 5669 1 . PHE 14 14 5669 1 . MET 15 15 5669 1 . ASN 16 16 5669 1 . GLN 17 17 5669 1 . PRO 18 18 5669 1 . GLY 19 19 5669 1 . THR 20 20 5669 1 . GLY 21 21 5669 1 . HIS 22 22 5669 1 . CYS 23 23 5669 1 . GLU 24 24 5669 1 . MET 25 25 5669 1 . CYS 26 26 5669 1 . SER 27 27 5669 1 . LEU 28 28 5669 1 . PRO 29 29 5669 1 . ARG 30 30 5669 1 . THR 31 31 5669 1 stop_ save_ save_ZN _Entity.Sf_category entity _Entity.Sf_framecode ZN _Entity.Entry_ID 5669 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name ZN _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer . _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID ZN _Entity.Nonpolymer_comp_label $chem_comp_ZN _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 2 _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 . 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 . ZN . 5669 2 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 5669 _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 $NPL4-NZF . 10116 organism . 'Rattus norvegicus' Rat . . Eukaryota Metazoa Rattus norvegicus . . . . . . . . . . . . . . . . . . . . . 5669 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 5669 _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 $NPL4-NZF . 'recombinant technology' . . . . . . . . . . . . . . . . . . . . . . PGEX . . . . . . 5669 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_ZN _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_ZN _Chem_comp.Entry_ID 5669 _Chem_comp.ID ZN _Chem_comp.Provenance . _Chem_comp.Name 'ZINC ION' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code ZN _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code ZN _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 2 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula Zn _Chem_comp.Formula_weight 65.409 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Jul 26 11:33:38 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID InChI=1S/Zn/q+2 InChI InChI 1.03 5669 ZN PTFCDOFLOPIGGS-UHFFFAOYSA-N InChIKey InChI 1.03 5669 ZN [Zn++] SMILES CACTVS 3.341 5669 ZN [Zn++] SMILES_CANONICAL CACTVS 3.341 5669 ZN [Zn+2] SMILES ACDLabs 10.04 5669 ZN [Zn+2] SMILES 'OpenEye OEToolkits' 1.5.0 5669 ZN [Zn+2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 5669 ZN stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID zinc 'SYSTEMATIC NAME' ACDLabs 10.04 5669 ZN 'zinc(+2) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 5669 ZN stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID ZN . ZN . . ZN . . N 2 . . . . no no . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 1 . 5669 ZN stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5669 _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 'Npl4 Zinc Finger' '[U-15N; U-13C]' . . 1 $NPL4-NZF . . 1 . . mM . . . . 5669 1 2 'sodium phosphate' . . . . . . . 20 . . mM . . . . 5669 1 3 NaCl . . . . . . . 50 . . mM . . . . 5669 1 4 BME . . . . . . . 5 . . mM . . . . 5669 1 5 H2O . . . . . . . 90 . . % . . . . 5669 1 6 D2O . . . . . . . 10 . . % . . . . 5669 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 5669 _Sample.ID 2 _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 'Npl4 Zinc Finger' '[U-95% 15N]' . . 1 $NPL4-NZF . . 1 0.9 1.1 mM . . . . 5669 2 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 5669 _Sample_condition_list.ID 1 _Sample_condition_list.Details 'tube sealed under argon' 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 'ionic strength' 75 . mM 5669 1 pH 5.5 0.1 n/a 5669 1 pressure 1 . atm 5669 1 temperature 291 0.1 K 5669 1 stop_ save_ ############################ # Computer software used # ############################ save_CNS _Software.Sf_category software _Software.Sf_framecode CNS _Software.Entry_ID 5669 _Software.ID 1 _Software.Name CNS _Software.Version 1.1 _Software.Details ; BRUNGER, ADAMS, CLORE, DELANO, GROS, GROSSE-KUNSTLEVE, JIANG, KUSZEWSKI, NILGES, PANNU, READ, RICE, SIMONSON, WARREN. ; loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 5669 1 stop_ save_ save_DYANA _Software.Sf_category software _Software.Sf_framecode DYANA _Software.Entry_ID 5669 _Software.ID 2 _Software.Name DYANA _Software.Version 1.5 _Software.Details 'Guntert, P., Mumenthaler, C., Wuthrich, K.' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 5669 2 stop_ save_ save_FELIX _Software.Sf_category software _Software.Sf_framecode FELIX _Software.Entry_ID 5669 _Software.ID 3 _Software.Name FELIX _Software.Version 97 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 5669 3 stop_ save_ save_Sparky _Software.Sf_category software _Software.Sf_framecode Sparky _Software.Entry_ID 5669 _Software.ID 4 _Software.Name SPARKY _Software.Version 3.106 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 5669 4 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 5669 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model UNITYplus _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 5669 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model Inova _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 5669 _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 Varian UNITYplus . 500 . . . 5669 1 2 NMR_spectrometer_2 Varian Inova . 600 . . . 5669 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 5669 _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 HNCACB . . . . . . . . . . . . . . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 5669 1 2 HN(CA)CO . . . . . . . . . . . . . . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 5669 1 3 H(CCO)NH-TOCSY . . . . . . . . . . . . . . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 5669 1 4 (H)C(CO)NH-TOCSY . . . . . . . . . . . . . . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 5669 1 5 '3D 13C-separated NOESY' . . . . . . . . . . . . . . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 5669 1 6 '3D 15N-separated NOESY' . . . . . . . . . . . . . . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 5669 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 5669 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name HNCACB _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 5669 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name HN(CA)CO _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 5669 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name H(CCO)NH-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 5669 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name (H)C(CO)NH-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_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 5669 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name '3D 13C-separated 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_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 5669 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name '3D 15N-separated 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_ #################### # 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 5669 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5669 1 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 5669 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5669 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 5669 _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 'Residues 1-3 are unassigned.' _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 . 5669 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 GLY H H 1 8.256 0.03 . 1 . . . . . . . . 5669 1 2 . 1 1 1 1 GLY N N 15 110.878 0.1 . 1 . . . . . . . . 5669 1 3 . 1 1 3 3 THR CB C 13 69.542 0.1 . 1 . . . . . . . . 5669 1 4 . 1 1 3 3 THR HB H 1 4.231 0.03 . 1 . . . . . . . . 5669 1 5 . 1 1 3 3 THR CG2 C 13 21.544 0.1 . 1 . . . . . . . . 5669 1 6 . 1 1 3 3 THR HG21 H 1 1.132 0.03 . 1 . . . . . . . . 5669 1 7 . 1 1 3 3 THR HG22 H 1 1.132 0.03 . 1 . . . . . . . . 5669 1 8 . 1 1 3 3 THR HG23 H 1 1.132 0.03 . 1 . . . . . . . . 5669 1 9 . 1 1 4 4 SER CA C 13 58.361 0.1 . 1 . . . . . . . . 5669 1 10 . 1 1 4 4 SER HA H 1 4.393 0.03 . 1 . . . . . . . . 5669 1 11 . 1 1 4 4 SER CB C 13 63.787 0.1 . 1 . . . . . . . . 5669 1 12 . 1 1 4 4 SER HB2 H 1 3.806 0.03 . 2 . . . . . . . . 5669 1 13 . 1 1 5 5 ALA H H 1 8.071 0.03 . 1 . . . . . . . . 5669 1 14 . 1 1 5 5 ALA N N 15 125.442 0.1 . 1 . . . . . . . . 5669 1 15 . 1 1 5 5 ALA CA C 13 51.884 0.1 . 1 . . . . . . . . 5669 1 16 . 1 1 5 5 ALA HA H 1 4.432 0.03 . 1 . . . . . . . . 5669 1 17 . 1 1 5 5 ALA C C 13 177.651 0.1 . 1 . . . . . . . . 5669 1 18 . 1 1 5 5 ALA CB C 13 20.017 0.1 . 1 . . . . . . . . 5669 1 19 . 1 1 5 5 ALA HB1 H 1 1.371 0.03 . 1 . . . . . . . . 5669 1 20 . 1 1 5 5 ALA HB2 H 1 1.371 0.03 . 1 . . . . . . . . 5669 1 21 . 1 1 5 5 ALA HB3 H 1 1.371 0.03 . 1 . . . . . . . . 5669 1 22 . 1 1 6 6 MET H H 1 7.996 0.03 . 1 . . . . . . . . 5669 1 23 . 1 1 6 6 MET N N 15 118.760 0.1 . 1 . . . . . . . . 5669 1 24 . 1 1 6 6 MET CA C 13 56.813 0.1 . 1 . . . . . . . . 5669 1 25 . 1 1 6 6 MET HA H 1 4.366 0.03 . 1 . . . . . . . . 5669 1 26 . 1 1 6 6 MET C C 13 175.598 0.1 . 1 . . . . . . . . 5669 1 27 . 1 1 6 6 MET CB C 13 34.395 0.1 . 1 . . . . . . . . 5669 1 28 . 1 1 6 6 MET HB2 H 1 1.861 0.03 . 1 . . . . . . . . 5669 1 29 . 1 1 6 6 MET HB3 H 1 1.674 0.03 . 1 . . . . . . . . 5669 1 30 . 1 1 6 6 MET CG C 13 33.053 0.1 . 1 . . . . . . . . 5669 1 31 . 1 1 6 6 MET HG2 H 1 2.574 0.03 . 2 . . . . . . . . 5669 1 32 . 1 1 6 6 MET HG3 H 1 2.238 0.03 . 2 . . . . . . . . 5669 1 33 . 1 1 7 7 TRP H H 1 8.151 0.03 . 1 . . . . . . . . 5669 1 34 . 1 1 7 7 TRP N N 15 118.508 0.1 . 1 . . . . . . . . 5669 1 35 . 1 1 7 7 TRP CA C 13 53.617 0.1 . 1 . . . . . . . . 5669 1 36 . 1 1 7 7 TRP HA H 1 4.914 0.03 . 1 . . . . . . . . 5669 1 37 . 1 1 7 7 TRP C C 13 173.294 0.1 . 1 . . . . . . . . 5669 1 38 . 1 1 7 7 TRP CB C 13 31.267 0.1 . 1 . . . . . . . . 5669 1 39 . 1 1 7 7 TRP HB2 H 1 3.155 0.03 . 1 . . . . . . . . 5669 1 40 . 1 1 7 7 TRP HB3 H 1 2.879 0.03 . 1 . . . . . . . . 5669 1 41 . 1 1 7 7 TRP CD1 C 13 127.147 0.1 . 1 . . . . . . . . 5669 1 42 . 1 1 7 7 TRP HD1 H 1 6.833 0.03 . 1 . . . . . . . . 5669 1 43 . 1 1 7 7 TRP NE1 N 15 131.314 0.1 . 1 . . . . . . . . 5669 1 44 . 1 1 7 7 TRP HE1 H 1 9.559 0.03 . 1 . . . . . . . . 5669 1 45 . 1 1 7 7 TRP CE3 C 13 121.085 0.1 . 1 . . . . . . . . 5669 1 46 . 1 1 7 7 TRP HE3 H 1 7.225 0.03 . 1 . . . . . . . . 5669 1 47 . 1 1 7 7 TRP CZ2 C 13 114.522 0.1 . 1 . . . . . . . . 5669 1 48 . 1 1 7 7 TRP HZ2 H 1 6.854 0.03 . 1 . . . . . . . . 5669 1 49 . 1 1 7 7 TRP CZ3 C 13 121.918 0.1 . 1 . . . . . . . . 5669 1 50 . 1 1 7 7 TRP HZ3 H 1 7.208 0.03 . 1 . . . . . . . . 5669 1 51 . 1 1 7 7 TRP CH2 C 13 123.625 0.1 . 1 . . . . . . . . 5669 1 52 . 1 1 7 7 TRP HH2 H 1 6.749 0.03 . 1 . . . . . . . . 5669 1 53 . 1 1 8 8 ALA H H 1 8.744 0.03 . 1 . . . . . . . . 5669 1 54 . 1 1 8 8 ALA N N 15 126.281 0.1 . 1 . . . . . . . . 5669 1 55 . 1 1 8 8 ALA CA C 13 50.593 0.1 . 1 . . . . . . . . 5669 1 56 . 1 1 8 8 ALA HA H 1 4.579 0.03 . 1 . . . . . . . . 5669 1 57 . 1 1 8 8 ALA C C 13 177.697 0.1 . 1 . . . . . . . . 5669 1 58 . 1 1 8 8 ALA CB C 13 19.566 0.1 . 1 . . . . . . . . 5669 1 59 . 1 1 8 8 ALA HB1 H 1 1.101 0.03 . 1 . . . . . . . . 5669 1 60 . 1 1 8 8 ALA HB2 H 1 1.101 0.03 . 1 . . . . . . . . 5669 1 61 . 1 1 8 8 ALA HB3 H 1 1.101 0.03 . 1 . . . . . . . . 5669 1 62 . 1 1 9 9 CYS H H 1 8.830 0.03 . 1 . . . . . . . . 5669 1 63 . 1 1 9 9 CYS N N 15 128.000 0.1 . 1 . . . . . . . . 5669 1 64 . 1 1 9 9 CYS CA C 13 59.725 0.1 . 1 . . . . . . . . 5669 1 65 . 1 1 9 9 CYS HA H 1 4.577 0.03 . 1 . . . . . . . . 5669 1 66 . 1 1 9 9 CYS C C 13 178.806 0.1 . 1 . . . . . . . . 5669 1 67 . 1 1 9 9 CYS CB C 13 31.731 0.1 . 1 . . . . . . . . 5669 1 68 . 1 1 9 9 CYS HB2 H 1 3.176 0.03 . 1 . . . . . . . . 5669 1 69 . 1 1 9 9 CYS HB3 H 1 2.775 0.03 . 1 . . . . . . . . 5669 1 70 . 1 1 10 10 GLN H H 1 9.700 0.03 . 1 . . . . . . . . 5669 1 71 . 1 1 10 10 GLN N N 15 130.963 0.1 . 1 . . . . . . . . 5669 1 72 . 1 1 10 10 GLN CA C 13 57.668 0.1 . 1 . . . . . . . . 5669 1 73 . 1 1 10 10 GLN HA H 1 3.999 0.03 . 1 . . . . . . . . 5669 1 74 . 1 1 10 10 GLN C C 13 175.298 0.1 . 1 . . . . . . . . 5669 1 75 . 1 1 10 10 GLN CB C 13 28.726 0.1 . 1 . . . . . . . . 5669 1 76 . 1 1 10 10 GLN HB2 H 1 1.884 0.03 . 2 . . . . . . . . 5669 1 77 . 1 1 10 10 GLN HB3 H 1 1.811 0.03 . 2 . . . . . . . . 5669 1 78 . 1 1 10 10 GLN CG C 13 33.731 0.1 . 1 . . . . . . . . 5669 1 79 . 1 1 10 10 GLN HG2 H 1 2.230 0.03 . 2 . . . . . . . . 5669 1 80 . 1 1 10 10 GLN HG3 H 1 2.050 0.03 . 2 . . . . . . . . 5669 1 81 . 1 1 10 10 GLN NE2 N 15 113.175 0.1 . 1 . . . . . . . . 5669 1 82 . 1 1 10 10 GLN HE21 H 1 7.413 0.03 . 1 . . . . . . . . 5669 1 83 . 1 1 10 10 GLN HE22 H 1 6.873 0.03 . 1 . . . . . . . . 5669 1 84 . 1 1 11 11 HIS H H 1 9.166 0.03 . 1 . . . . . . . . 5669 1 85 . 1 1 11 11 HIS N N 15 121.319 0.1 . 1 . . . . . . . . 5669 1 86 . 1 1 11 11 HIS CA C 13 57.819 0.1 . 1 . . . . . . . . 5669 1 87 . 1 1 11 11 HIS HA H 1 4.531 0.03 . 1 . . . . . . . . 5669 1 88 . 1 1 11 11 HIS C C 13 177.073 0.1 . 1 . . . . . . . . 5669 1 89 . 1 1 11 11 HIS CB C 13 31.791 0.1 . 1 . . . . . . . . 5669 1 90 . 1 1 11 11 HIS HB2 H 1 3.160 0.03 . 2 . . . . . . . . 5669 1 91 . 1 1 11 11 HIS CD2 C 13 121.640 0.1 . 1 . . . . . . . . 5669 1 92 . 1 1 11 11 HIS HD2 H 1 7.175 0.03 . 1 . . . . . . . . 5669 1 93 . 1 1 12 12 CYS H H 1 8.991 0.03 . 1 . . . . . . . . 5669 1 94 . 1 1 12 12 CYS N N 15 119.535 0.1 . 1 . . . . . . . . 5669 1 95 . 1 1 12 12 CYS CA C 13 58.896 0.1 . 1 . . . . . . . . 5669 1 96 . 1 1 12 12 CYS HA H 1 5.102 0.03 . 1 . . . . . . . . 5669 1 97 . 1 1 12 12 CYS C C 13 178.285 0.1 . 1 . . . . . . . . 5669 1 98 . 1 1 12 12 CYS CB C 13 32.503 0.1 . 1 . . . . . . . . 5669 1 99 . 1 1 12 12 CYS HB2 H 1 3.230 0.03 . 1 . . . . . . . . 5669 1 100 . 1 1 12 12 CYS HB3 H 1 2.550 0.03 . 1 . . . . . . . . 5669 1 101 . 1 1 13 13 THR H H 1 7.703 0.03 . 1 . . . . . . . . 5669 1 102 . 1 1 13 13 THR N N 15 117.369 0.1 . 1 . . . . . . . . 5669 1 103 . 1 1 13 13 THR CA C 13 66.037 0.1 . 1 . . . . . . . . 5669 1 104 . 1 1 13 13 THR HA H 1 4.187 0.03 . 1 . . . . . . . . 5669 1 105 . 1 1 13 13 THR C C 13 172.060 0.1 . 1 . . . . . . . . 5669 1 106 . 1 1 13 13 THR CB C 13 69.884 0.1 . 1 . . . . . . . . 5669 1 107 . 1 1 13 13 THR HB H 1 4.392 0.03 . 1 . . . . . . . . 5669 1 108 . 1 1 13 13 THR CG2 C 13 21.669 0.1 . 1 . . . . . . . . 5669 1 109 . 1 1 13 13 THR HG21 H 1 1.071 0.03 . 1 . . . . . . . . 5669 1 110 . 1 1 13 13 THR HG22 H 1 1.071 0.03 . 1 . . . . . . . . 5669 1 111 . 1 1 13 13 THR HG23 H 1 1.071 0.03 . 1 . . . . . . . . 5669 1 112 . 1 1 14 14 PHE H H 1 8.804 0.03 . 1 . . . . . . . . 5669 1 113 . 1 1 14 14 PHE N N 15 126.671 0.1 . 1 . . . . . . . . 5669 1 114 . 1 1 14 14 PHE CA C 13 60.620 0.1 . 1 . . . . . . . . 5669 1 115 . 1 1 14 14 PHE HA H 1 4.042 0.03 . 1 . . . . . . . . 5669 1 116 . 1 1 14 14 PHE C C 13 174.323 0.1 . 1 . . . . . . . . 5669 1 117 . 1 1 14 14 PHE CB C 13 41.026 0.1 . 1 . . . . . . . . 5669 1 118 . 1 1 14 14 PHE HB2 H 1 3.266 0.03 . 1 . . . . . . . . 5669 1 119 . 1 1 14 14 PHE HB3 H 1 2.630 0.03 . 1 . . . . . . . . 5669 1 120 . 1 1 14 14 PHE CD1 C 13 131.961 0.1 . 1 . . . . . . . . 5669 1 121 . 1 1 14 14 PHE HD1 H 1 6.985 0.03 . 3 . . . . . . . . 5669 1 122 . 1 1 14 14 PHE CE1 C 13 131.939 0.1 . 1 . . . . . . . . 5669 1 123 . 1 1 14 14 PHE HE1 H 1 7.142 0.03 . 3 . . . . . . . . 5669 1 124 . 1 1 14 14 PHE CZ C 13 129.618 0.1 . 1 . . . . . . . . 5669 1 125 . 1 1 14 14 PHE HZ H 1 7.098 0.03 . 1 . . . . . . . . 5669 1 126 . 1 1 15 15 MET H H 1 6.973 0.03 . 1 . . . . . . . . 5669 1 127 . 1 1 15 15 MET N N 15 124.237 0.1 . 1 . . . . . . . . 5669 1 128 . 1 1 15 15 MET CA C 13 53.154 0.1 . 1 . . . . . . . . 5669 1 129 . 1 1 15 15 MET HA H 1 4.391 0.03 . 1 . . . . . . . . 5669 1 130 . 1 1 15 15 MET C C 13 173.514 0.1 . 1 . . . . . . . . 5669 1 131 . 1 1 15 15 MET CB C 13 30.370 0.1 . 1 . . . . . . . . 5669 1 132 . 1 1 15 15 MET HB2 H 1 1.517 0.03 . 1 . . . . . . . . 5669 1 133 . 1 1 15 15 MET HB3 H 1 1.364 0.03 . 1 . . . . . . . . 5669 1 134 . 1 1 15 15 MET CG C 13 31.269 0.1 . 1 . . . . . . . . 5669 1 135 . 1 1 15 15 MET HG2 H 1 2.244 0.03 . 2 . . . . . . . . 5669 1 136 . 1 1 16 16 ASN H H 1 8.656 0.03 . 1 . . . . . . . . 5669 1 137 . 1 1 16 16 ASN N N 15 124.204 0.1 . 1 . . . . . . . . 5669 1 138 . 1 1 16 16 ASN CA C 13 53.286 0.1 . 1 . . . . . . . . 5669 1 139 . 1 1 16 16 ASN HA H 1 4.364 0.03 . 1 . . . . . . . . 5669 1 140 . 1 1 16 16 ASN C C 13 174.332 0.1 . 1 . . . . . . . . 5669 1 141 . 1 1 16 16 ASN CB C 13 43.086 0.1 . 1 . . . . . . . . 5669 1 142 . 1 1 16 16 ASN HB2 H 1 1.802 0.03 . 1 . . . . . . . . 5669 1 143 . 1 1 16 16 ASN HB3 H 1 0.142 0.03 . 1 . . . . . . . . 5669 1 144 . 1 1 16 16 ASN ND2 N 15 115.639 0.1 . 1 . . . . . . . . 5669 1 145 . 1 1 16 16 ASN HD21 H 1 7.417 0.03 . 1 . . . . . . . . 5669 1 146 . 1 1 16 16 ASN HD22 H 1 7.417 0.03 . 1 . . . . . . . . 5669 1 147 . 1 1 17 17 GLN H H 1 8.608 0.03 . 1 . . . . . . . . 5669 1 148 . 1 1 17 17 GLN N N 15 116.599 0.1 . 1 . . . . . . . . 5669 1 149 . 1 1 17 17 GLN CA C 13 53.915 0.1 . 1 . . . . . . . . 5669 1 150 . 1 1 17 17 GLN HA H 1 4.236 0.03 . 1 . . . . . . . . 5669 1 151 . 1 1 17 17 GLN CB C 13 27.836 0.1 . 1 . . . . . . . . 5669 1 152 . 1 1 17 17 GLN HB2 H 1 2.262 0.03 . 1 . . . . . . . . 5669 1 153 . 1 1 17 17 GLN HB3 H 1 1.828 0.03 . 1 . . . . . . . . 5669 1 154 . 1 1 17 17 GLN CG C 13 33.206 0.1 . 1 . . . . . . . . 5669 1 155 . 1 1 17 17 GLN HG2 H 1 2.539 0.03 . 2 . . . . . . . . 5669 1 156 . 1 1 17 17 GLN HG3 H 1 2.500 0.03 . 2 . . . . . . . . 5669 1 157 . 1 1 17 17 GLN NE2 N 15 114.465 0.1 . 1 . . . . . . . . 5669 1 158 . 1 1 17 17 GLN HE21 H 1 7.896 0.03 . 1 . . . . . . . . 5669 1 159 . 1 1 17 17 GLN HE22 H 1 6.793 0.03 . 1 . . . . . . . . 5669 1 160 . 1 1 18 18 PRO CA C 13 63.827 0.1 . 1 . . . . . . . . 5669 1 161 . 1 1 18 18 PRO HA H 1 4.417 0.03 . 1 . . . . . . . . 5669 1 162 . 1 1 18 18 PRO CB C 13 31.892 0.1 . 1 . . . . . . . . 5669 1 163 . 1 1 18 18 PRO HB2 H 1 2.230 0.03 . 2 . . . . . . . . 5669 1 164 . 1 1 18 18 PRO HB3 H 1 1.866 0.03 . 2 . . . . . . . . 5669 1 165 . 1 1 18 18 PRO CG C 13 27.658 0.1 . 1 . . . . . . . . 5669 1 166 . 1 1 18 18 PRO HG2 H 1 1.990 0.03 . 2 . . . . . . . . 5669 1 167 . 1 1 18 18 PRO HG3 H 1 1.795 0.03 . 2 . . . . . . . . 5669 1 168 . 1 1 18 18 PRO CD C 13 50.445 0.1 . 1 . . . . . . . . 5669 1 169 . 1 1 18 18 PRO HD2 H 1 3.767 0.03 . 2 . . . . . . . . 5669 1 170 . 1 1 18 18 PRO HD3 H 1 3.494 0.03 . 2 . . . . . . . . 5669 1 171 . 1 1 19 19 GLY H H 1 8.675 0.03 . 1 . . . . . . . . 5669 1 172 . 1 1 19 19 GLY N N 15 107.111 0.1 . 1 . . . . . . . . 5669 1 173 . 1 1 19 19 GLY CA C 13 45.429 0.1 . 1 . . . . . . . . 5669 1 174 . 1 1 19 19 GLY HA2 H 1 3.842 0.03 . 2 . . . . . . . . 5669 1 175 . 1 1 19 19 GLY HA3 H 1 3.955 0.03 . 2 . . . . . . . . 5669 1 176 . 1 1 19 19 GLY C C 13 174.543 0.1 . 1 . . . . . . . . 5669 1 177 . 1 1 20 20 THR H H 1 7.531 0.03 . 1 . . . . . . . . 5669 1 178 . 1 1 20 20 THR N N 15 112.095 0.1 . 1 . . . . . . . . 5669 1 179 . 1 1 20 20 THR CA C 13 60.702 0.1 . 1 . . . . . . . . 5669 1 180 . 1 1 20 20 THR HA H 1 4.578 0.03 . 1 . . . . . . . . 5669 1 181 . 1 1 20 20 THR C C 13 174.861 0.1 . 1 . . . . . . . . 5669 1 182 . 1 1 20 20 THR CB C 13 71.022 0.1 . 1 . . . . . . . . 5669 1 183 . 1 1 20 20 THR HB H 1 4.442 0.03 . 1 . . . . . . . . 5669 1 184 . 1 1 20 20 THR CG2 C 13 22.357 0.1 . 1 . . . . . . . . 5669 1 185 . 1 1 20 20 THR HG21 H 1 1.421 0.03 . 1 . . . . . . . . 5669 1 186 . 1 1 20 20 THR HG22 H 1 1.421 0.03 . 1 . . . . . . . . 5669 1 187 . 1 1 20 20 THR HG23 H 1 1.421 0.03 . 1 . . . . . . . . 5669 1 188 . 1 1 21 21 GLY H H 1 8.803 0.03 . 1 . . . . . . . . 5669 1 189 . 1 1 21 21 GLY N N 15 109.950 0.1 . 1 . . . . . . . . 5669 1 190 . 1 1 21 21 GLY CA C 13 45.108 0.1 . 1 . . . . . . . . 5669 1 191 . 1 1 21 21 GLY HA2 H 1 3.634 0.03 . 2 . . . . . . . . 5669 1 192 . 1 1 21 21 GLY HA3 H 1 4.086 0.03 . 2 . . . . . . . . 5669 1 193 . 1 1 21 21 GLY C C 13 173.774 0.1 . 1 . . . . . . . . 5669 1 194 . 1 1 22 22 HIS H H 1 7.752 0.03 . 1 . . . . . . . . 5669 1 195 . 1 1 22 22 HIS N N 15 118.346 0.1 . 1 . . . . . . . . 5669 1 196 . 1 1 22 22 HIS CA C 13 55.411 0.1 . 1 . . . . . . . . 5669 1 197 . 1 1 22 22 HIS HA H 1 4.970 0.03 . 1 . . . . . . . . 5669 1 198 . 1 1 22 22 HIS C C 13 173.108 0.1 . 1 . . . . . . . . 5669 1 199 . 1 1 22 22 HIS CB C 13 33.222 0.1 . 1 . . . . . . . . 5669 1 200 . 1 1 22 22 HIS HB2 H 1 2.792 0.03 . 1 . . . . . . . . 5669 1 201 . 1 1 22 22 HIS HB3 H 1 2.688 0.03 . 1 . . . . . . . . 5669 1 202 . 1 1 22 22 HIS CD2 C 13 119.788 0.1 . 1 . . . . . . . . 5669 1 203 . 1 1 22 22 HIS HD2 H 1 6.821 0.03 . 1 . . . . . . . . 5669 1 204 . 1 1 23 23 CYS H H 1 8.752 0.03 . 1 . . . . . . . . 5669 1 205 . 1 1 23 23 CYS N N 15 123.825 0.1 . 1 . . . . . . . . 5669 1 206 . 1 1 23 23 CYS CA C 13 58.886 0.1 . 1 . . . . . . . . 5669 1 207 . 1 1 23 23 CYS HA H 1 4.191 0.03 . 1 . . . . . . . . 5669 1 208 . 1 1 23 23 CYS C C 13 178.097 0.1 . 1 . . . . . . . . 5669 1 209 . 1 1 23 23 CYS CB C 13 31.479 0.1 . 1 . . . . . . . . 5669 1 210 . 1 1 23 23 CYS HB2 H 1 3.308 0.03 . 1 . . . . . . . . 5669 1 211 . 1 1 23 23 CYS HB3 H 1 3.061 0.03 . 1 . . . . . . . . 5669 1 212 . 1 1 24 24 GLU H H 1 9.220 0.03 . 1 . . . . . . . . 5669 1 213 . 1 1 24 24 GLU N N 15 131.223 0.1 . 1 . . . . . . . . 5669 1 214 . 1 1 24 24 GLU CA C 13 58.688 0.1 . 1 . . . . . . . . 5669 1 215 . 1 1 24 24 GLU HA H 1 3.946 0.03 . 1 . . . . . . . . 5669 1 216 . 1 1 24 24 GLU C C 13 176.445 0.1 . 1 . . . . . . . . 5669 1 217 . 1 1 24 24 GLU CB C 13 30.938 0.1 . 1 . . . . . . . . 5669 1 218 . 1 1 24 24 GLU HB2 H 1 2.114 0.03 . 1 . . . . . . . . 5669 1 219 . 1 1 24 24 GLU HB3 H 1 1.934 0.03 . 1 . . . . . . . . 5669 1 220 . 1 1 24 24 GLU CG C 13 36.688 0.1 . 1 . . . . . . . . 5669 1 221 . 1 1 24 24 GLU HG2 H 1 2.292 0.03 . 2 . . . . . . . . 5669 1 222 . 1 1 24 24 GLU HG3 H 1 2.144 0.03 . 2 . . . . . . . . 5669 1 223 . 1 1 25 25 MET H H 1 8.752 0.03 . 1 . . . . . . . . 5669 1 224 . 1 1 25 25 MET N N 15 119.906 0.1 . 1 . . . . . . . . 5669 1 225 . 1 1 25 25 MET CA C 13 55.887 0.1 . 1 . . . . . . . . 5669 1 226 . 1 1 25 25 MET HA H 1 4.332 0.03 . 1 . . . . . . . . 5669 1 227 . 1 1 25 25 MET C C 13 177.440 0.1 . 1 . . . . . . . . 5669 1 228 . 1 1 25 25 MET CB C 13 32.652 0.1 . 1 . . . . . . . . 5669 1 229 . 1 1 25 25 MET HB2 H 1 1.854 0.03 . 2 . . . . . . . . 5669 1 230 . 1 1 25 25 MET HB3 H 1 1.107 0.03 . 2 . . . . . . . . 5669 1 231 . 1 1 25 25 MET CG C 13 31.762 0.1 . 1 . . . . . . . . 5669 1 232 . 1 1 25 25 MET HG2 H 1 1.898 0.03 . 2 . . . . . . . . 5669 1 233 . 1 1 25 25 MET HG3 H 1 1.541 0.03 . 2 . . . . . . . . 5669 1 234 . 1 1 26 26 CYS H H 1 8.539 0.03 . 1 . . . . . . . . 5669 1 235 . 1 1 26 26 CYS N N 15 119.610 0.1 . 1 . . . . . . . . 5669 1 236 . 1 1 26 26 CYS CA C 13 59.160 0.1 . 1 . . . . . . . . 5669 1 237 . 1 1 26 26 CYS HA H 1 4.918 0.03 . 1 . . . . . . . . 5669 1 238 . 1 1 26 26 CYS C C 13 176.653 0.1 . 1 . . . . . . . . 5669 1 239 . 1 1 26 26 CYS CB C 13 31.792 0.1 . 1 . . . . . . . . 5669 1 240 . 1 1 26 26 CYS HB2 H 1 3.157 0.03 . 1 . . . . . . . . 5669 1 241 . 1 1 26 26 CYS HB3 H 1 2.647 0.03 . 1 . . . . . . . . 5669 1 242 . 1 1 27 27 SER H H 1 7.636 0.03 . 1 . . . . . . . . 5669 1 243 . 1 1 27 27 SER N N 15 115.915 0.1 . 1 . . . . . . . . 5669 1 244 . 1 1 27 27 SER CA C 13 61.815 0.1 . 1 . . . . . . . . 5669 1 245 . 1 1 27 27 SER HA H 1 4.397 0.03 . 1 . . . . . . . . 5669 1 246 . 1 1 27 27 SER C C 13 173.387 0.1 . 1 . . . . . . . . 5669 1 247 . 1 1 27 27 SER CB C 13 63.024 0.1 . 1 . . . . . . . . 5669 1 248 . 1 1 27 27 SER HB2 H 1 4.139 0.03 . 2 . . . . . . . . 5669 1 249 . 1 1 27 27 SER HB3 H 1 3.893 0.03 . 2 . . . . . . . . 5669 1 250 . 1 1 28 28 LEU H H 1 8.141 0.03 . 1 . . . . . . . . 5669 1 251 . 1 1 28 28 LEU N N 15 125.111 0.1 . 1 . . . . . . . . 5669 1 252 . 1 1 28 28 LEU CA C 13 54.499 0.1 . 1 . . . . . . . . 5669 1 253 . 1 1 28 28 LEU HA H 1 4.576 0.03 . 1 . . . . . . . . 5669 1 254 . 1 1 28 28 LEU C C 13 176.468 0.1 . 1 . . . . . . . . 5669 1 255 . 1 1 28 28 LEU CB C 13 39.741 0.1 . 1 . . . . . . . . 5669 1 256 . 1 1 28 28 LEU HB2 H 1 1.831 0.03 . 1 . . . . . . . . 5669 1 257 . 1 1 28 28 LEU HB3 H 1 1.257 0.03 . 1 . . . . . . . . 5669 1 258 . 1 1 28 28 LEU CG C 13 27.518 0.1 . 1 . . . . . . . . 5669 1 259 . 1 1 28 28 LEU CD1 C 13 22.246 0.1 . 1 . . . . . . . . 5669 1 260 . 1 1 28 28 LEU HD11 H 1 0.712 0.03 . 2 . . . . . . . . 5669 1 261 . 1 1 28 28 LEU HD12 H 1 0.712 0.03 . 2 . . . . . . . . 5669 1 262 . 1 1 28 28 LEU HD13 H 1 0.712 0.03 . 2 . . . . . . . . 5669 1 263 . 1 1 28 28 LEU CD2 C 13 24.277 0.1 . 1 . . . . . . . . 5669 1 264 . 1 1 28 28 LEU HD21 H 1 0.410 0.03 . 2 . . . . . . . . 5669 1 265 . 1 1 28 28 LEU HD22 H 1 0.410 0.03 . 2 . . . . . . . . 5669 1 266 . 1 1 28 28 LEU HD23 H 1 0.410 0.03 . 2 . . . . . . . . 5669 1 267 . 1 1 28 28 LEU HG H 1 1.652 0.03 . 1 . . . . . . . . 5669 1 268 . 1 1 29 29 PRO CA C 13 62.595 0.1 . 1 . . . . . . . . 5669 1 269 . 1 1 29 29 PRO HA H 1 4.446 0.03 . 1 . . . . . . . . 5669 1 270 . 1 1 29 29 PRO C C 13 175.859 0.1 . 1 . . . . . . . . 5669 1 271 . 1 1 29 29 PRO CB C 13 32.200 0.1 . 1 . . . . . . . . 5669 1 272 . 1 1 29 29 PRO HB2 H 1 2.010 0.03 . 2 . . . . . . . . 5669 1 273 . 1 1 29 29 PRO HB3 H 1 1.816 0.03 . 2 . . . . . . . . 5669 1 274 . 1 1 29 29 PRO CG C 13 27.370 0.1 . 1 . . . . . . . . 5669 1 275 . 1 1 29 29 PRO HG2 H 1 2.007 0.03 . 2 . . . . . . . . 5669 1 276 . 1 1 29 29 PRO CD C 13 50.791 0.1 . 1 . . . . . . . . 5669 1 277 . 1 1 29 29 PRO HD2 H 1 3.886 0.03 . 2 . . . . . . . . 5669 1 278 . 1 1 29 29 PRO HD3 H 1 3.648 0.03 . 2 . . . . . . . . 5669 1 279 . 1 1 30 30 ARG H H 1 7.594 0.03 . 1 . . . . . . . . 5669 1 280 . 1 1 30 30 ARG N N 15 121.538 0.1 . 1 . . . . . . . . 5669 1 281 . 1 1 30 30 ARG CA C 13 57.072 0.1 . 1 . . . . . . . . 5669 1 282 . 1 1 30 30 ARG HA H 1 3.756 0.03 . 1 . . . . . . . . 5669 1 283 . 1 1 30 30 ARG C C 13 175.709 0.1 . 1 . . . . . . . . 5669 1 284 . 1 1 30 30 ARG CB C 13 30.718 0.1 . 1 . . . . . . . . 5669 1 285 . 1 1 30 30 ARG HB2 H 1 0.984 0.03 . 1 . . . . . . . . 5669 1 286 . 1 1 30 30 ARG HB3 H 1 0.488 0.03 . 1 . . . . . . . . 5669 1 287 . 1 1 30 30 ARG CG C 13 25.804 0.1 . 1 . . . . . . . . 5669 1 288 . 1 1 30 30 ARG HG2 H 1 0.841 0.03 . 2 . . . . . . . . 5669 1 289 . 1 1 30 30 ARG HG3 H 1 0.293 0.03 . 2 . . . . . . . . 5669 1 290 . 1 1 30 30 ARG CD C 13 43.197 0.1 . 1 . . . . . . . . 5669 1 291 . 1 1 30 30 ARG HD2 H 1 2.068 0.03 . 2 . . . . . . . . 5669 1 292 . 1 1 30 30 ARG HD3 H 1 1.234 0.03 . 2 . . . . . . . . 5669 1 293 . 1 1 31 31 THR H H 1 7.483 0.03 . 1 . . . . . . . . 5669 1 294 . 1 1 31 31 THR N N 15 122.118 0.1 . 1 . . . . . . . . 5669 1 295 . 1 1 31 31 THR CA C 13 62.794 0.1 . 1 . . . . . . . . 5669 1 296 . 1 1 31 31 THR HA H 1 4.016 0.03 . 1 . . . . . . . . 5669 1 297 . 1 1 31 31 THR C C 13 178.807 0.1 . 1 . . . . . . . . 5669 1 298 . 1 1 31 31 THR CB C 13 70.928 0.1 . 1 . . . . . . . . 5669 1 299 . 1 1 31 31 THR HB H 1 4.100 0.03 . 1 . . . . . . . . 5669 1 300 . 1 1 31 31 THR CG2 C 13 22.075 0.1 . 1 . . . . . . . . 5669 1 301 . 1 1 31 31 THR HG21 H 1 1.040 0.03 . 1 . . . . . . . . 5669 1 302 . 1 1 31 31 THR HG22 H 1 1.040 0.03 . 1 . . . . . . . . 5669 1 303 . 1 1 31 31 THR HG23 H 1 1.040 0.03 . 1 . . . . . . . . 5669 1 stop_ save_