data_18397 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18397 _Entry.Title ; nanocrystalline GB1 1H, 13C, 15N assignments ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2012-04-13 _Entry.Accession_date 2012-04-13 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype SOLID-STATE _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 Donghua Zhou . . . 18397 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18397 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 186 18397 '15N chemical shifts' 61 18397 '1H chemical shifts' 66 18397 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 2 . . 2013-02-11 2012-04-13 update BMRB 'update entry citation' 18397 1 . . 2012-09-24 2012-04-13 original author 'original release' 18397 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 18397 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 22986689 _Citation.Full_citation . _Citation.Title 'Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 54 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 291 _Citation.Page_last 305 _Citation.Year 2012 _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 Donghua Zhou . H. . 18397 1 2 Andrew Nieuwkoop . J. . 18397 1 3 Deborah Berthold . A. . 18397 1 4 Gemma Comellas . . . 18397 1 5 Lindsay Sperling . J. . 18397 1 6 Ming Tang . . . 18397 1 7 Gautam Shah . J. . 18397 1 8 Elliott Brea . J. . 18397 1 9 Luisel Lemkau . R. . 18397 1 10 Chad Rienstra . M. . 18397 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18397 _Assembly.ID 1 _Assembly.Name GB1 _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 . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . 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 GB1 1 $GB1 A . yes native no no . . . 18397 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_GB1 _Entity.Sf_category entity _Entity.Sf_framecode GB1 _Entity.Entry_ID 18397 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name GB1 _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 ; MQYKLILNGKTLKGETTTEA VDAATAEKVFKQYANDNGVD GEWTYDDATKTFTVTE ; _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 no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 56 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 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 15156 . GB1 . . . . . 100.00 56 100.00 100.00 3.57e-30 . . . . 18397 1 2 no BMRB 15380 . GB1 . . . . . 100.00 56 100.00 100.00 3.57e-30 . . . . 18397 1 3 no BMRB 16444 . SC35 . . . . . 100.00 158 100.00 100.00 2.62e-30 . . . . 18397 1 4 no BMRB 16627 . Protein_GB1_(2Q6I) . . . . . 100.00 56 100.00 100.00 3.57e-30 . . . . 18397 1 5 no BMRB 16755 . N40 . . . . . 67.86 40 100.00 100.00 2.37e-16 . . . . 18397 1 6 no BMRB 16873 . GB1 . . . . . 100.00 56 100.00 100.00 3.57e-30 . . . . 18397 1 7 no BMRB 16882 . "Ubiquitin-Binding Motif" . . . . . 100.00 108 100.00 100.00 2.69e-30 . . . . 18397 1 8 no BMRB 16958 . ZCCHC9 . . . . . 100.00 164 100.00 100.00 1.84e-30 . . . . 18397 1 9 no BMRB 17810 . entity . . . . . 100.00 56 100.00 100.00 3.57e-30 . . . . 18397 1 10 no BMRB 19394 . GB1-UBM1 . . . . . 100.00 106 100.00 100.00 1.30e-30 . . . . 18397 1 11 no BMRB 26630 . Protein_G_Domain_Beta-1_Wild_Type . . . . . 100.00 64 98.21 98.21 1.28e-29 . . . . 18397 1 12 no PDB 1GB1 . "A Novel, Highly Stable Fold Of The Immunoglobulin Binding Domain Of Streptococcal Protein G" . . . . . 100.00 56 98.21 98.21 4.28e-29 . . . . 18397 1 13 no PDB 1IBX . "Nmr Structure Of Dff40 And Dff45 N-Terminal Domain Complex" . . . . . 100.00 145 100.00 100.00 4.67e-30 . . . . 18397 1 14 no PDB 1PGA . "Two Crystal Structures Of The B1 Immunoglobulin-Binding Domain Of Streptococcal Protein G And Comparison With Nmr" . . . . . 100.00 56 98.21 98.21 4.28e-29 . . . . 18397 1 15 no PDB 1PGB . "Two Crystal Structures Of The B1 Immunoglobulin-Binding Domain Of Streptoccocal Protein G And Comparison With Nmr" . . . . . 100.00 56 98.21 98.21 4.28e-29 . . . . 18397 1 16 no PDB 1PN5 . "Nmr Structure Of The Nalp1 Pyrin Domain (Pyd)" . . . . . 100.00 159 100.00 100.00 3.09e-30 . . . . 18397 1 17 no PDB 2CWB . "Solution Structure Of The Ubiquitin-Associated Domain Of Human Bmsc-Ubp And Its Complex With Ubiquitin" . . . . . 98.21 108 98.18 98.18 1.53e-28 . . . . 18397 1 18 no PDB 2DEN . "Solution Structure Of The Ubiquitin-Associated Domain Of Human Bmsc-Ubp And Its Complex With Ubiquitin" . . . . . 98.21 108 98.18 98.18 1.53e-28 . . . . 18397 1 19 no PDB 2GB1 . "A Novel, Highly Stable Fold Of The Immunoglobulin Binding Domain Of Streptococcal Protein G" . . . . . 100.00 56 98.21 98.21 4.28e-29 . . . . 18397 1 20 no PDB 2GI9 . "Backbone Conformational Constraints In A Microcrystalline U- 15n-Labeled Protein By 3d Dipolar-Shift Solid-State Nmr Spectrosco" . . . . . 100.00 56 100.00 100.00 3.57e-30 . . . . 18397 1 21 no PDB 2I2Y . "Solution Structure Of The Rrm Of Srp20 Bound To The Rna Cauc" . . . . . 100.00 150 100.00 100.00 5.99e-30 . . . . 18397 1 22 no PDB 2I38 . "Solution Structure Of The Rrm Of Srp20" . . . . . 100.00 150 100.00 100.00 6.32e-30 . . . . 18397 1 23 no PDB 2JSV . "Dipole Tensor-Based Refinement For Atomic-Resolution Structure Determination Of A Nanocrystalline Protein By Solid-State Nmr Sp" . . . . . 100.00 56 100.00 100.00 3.57e-30 . . . . 18397 1 24 no PDB 2JU6 . "Solid-State Protein Structure Determination With Proton- Detected Triple Resonance 3d Magic-Angle Spinning Nmr Spectroscopy" . . . . . 100.00 56 100.00 100.00 3.57e-30 . . . . 18397 1 25 no PDB 2K0P . "Determination Of A Protein Structure In The Solid State From Nmr Chemical Shifts" . . . . . 100.00 56 100.00 100.00 3.57e-30 . . . . 18397 1 26 no PDB 2KBT . "Attachment Of An Nmr-Invisible Solubility Enhancement Tag (Inset) Using A Sortase-Mediated Protein Ligation Method" . . . . . 100.00 142 98.21 98.21 1.34e-28 . . . . 18397 1 27 no PDB 2KHU . "Solution Structure Of The Ubiquitin-Binding Motif Of Human Polymerase Iota" . . . . . 100.00 108 100.00 100.00 2.69e-30 . . . . 18397 1 28 no PDB 2KHW . "Solution Structure Of The Human Polymerase Iota Ubm2- Ubiquitin Complex" . . . . . 100.00 108 100.00 100.00 2.69e-30 . . . . 18397 1 29 no PDB 2KLK . "Solution Structure Of Gb1 A34f Mutant With Rdc And Saxs" . . . . . 100.00 56 98.21 98.21 4.14e-29 . . . . 18397 1 30 no PDB 2KN4 . "The Structure Of The Rrm Domain Of Sc35" . . . . . 100.00 158 100.00 100.00 2.62e-30 . . . . 18397 1 31 no PDB 2KQ4 . "Atomic Resolution Protein Structure Determination By Three- Dimensional Transferred Echo Double Resonance Solid-State Nuclear M" . . . . . 100.00 56 100.00 100.00 3.57e-30 . . . . 18397 1 32 no PDB 2KWD . "Supramolecular Protein Structure Determination By Site-Speci Range Intermolecular Solid State Nmr Spectroscopy" . . . . . 100.00 56 100.00 100.00 3.57e-30 . . . . 18397 1 33 no PDB 2LGI . "Atomic Resolution Protein Structures Using Nmr Chemical Shift Tensors" . . . . . 100.00 56 100.00 100.00 3.57e-30 . . . . 18397 1 34 no PDB 2MBB . "Solution Structure Of The Human Polymerase Iota Ubm1-ubiquitin Complex" . . . . . 100.00 106 100.00 100.00 1.30e-30 . . . . 18397 1 35 no PDB 2PLP . "Ultra High Resolution Backbone Conformation Of Protein Gb1 From Residual Dipolar Couplings Alone" . . . . . 94.64 54 100.00 100.00 1.58e-27 . . . . 18397 1 36 no PDB 2QMT . "Crystal Polymorphism Of Protein Gb1 Examined By Solid-State Nmr And X-Ray Diffraction" . . . . . 100.00 56 100.00 100.00 3.57e-30 . . . . 18397 1 37 no PDB 2RMM . "Solution Structure Of Gb1 A34f Mutant" . . . . . 100.00 56 98.21 98.21 4.14e-29 . . . . 18397 1 38 no PDB 3GB1 . "Structures Of B1 Domain Of Streptococcal Protein G" . . . . . 100.00 56 98.21 98.21 4.28e-29 . . . . 18397 1 39 no PDB 3MP9 . "Structure Of Streptococcal Protein G B1 Domain At Ph 3.0" . . . . . 96.43 64 100.00 100.00 7.39e-29 . . . . 18397 1 40 no PDB 3UI3 . "Structural And Biochemical Characterization Of Hp0315 From Helicobacter Pylori As A Vapd Protein With An Endoribonuclease Activ" . . . . . 98.21 160 100.00 100.00 1.17e-28 . . . . 18397 1 41 no PDB 4Q0C . "3.1 A Resolution Crystal Structure Of The B. Pertussis Bvgs Periplasmic Domain" . . . . . 100.00 584 98.21 98.21 1.62e-27 . . . . 18397 1 42 no EMBL CAA37410 . "Protein G' [Streptococcus sp. 'group G']" . . . . . 80.36 185 97.78 100.00 8.64e-20 . . . . 18397 1 43 no GB AAY41168 . "protein G/SspDnaE fusion protein [Expression vector pJJDuet30]" . . . . . 100.00 201 98.21 100.00 2.83e-29 . . . . 18397 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 . 18397 1 2 . GLN . 18397 1 3 . TYR . 18397 1 4 . LYS . 18397 1 5 . LEU . 18397 1 6 . ILE . 18397 1 7 . LEU . 18397 1 8 . ASN . 18397 1 9 . GLY . 18397 1 10 . LYS . 18397 1 11 . THR . 18397 1 12 . LEU . 18397 1 13 . LYS . 18397 1 14 . GLY . 18397 1 15 . GLU . 18397 1 16 . THR . 18397 1 17 . THR . 18397 1 18 . THR . 18397 1 19 . GLU . 18397 1 20 . ALA . 18397 1 21 . VAL . 18397 1 22 . ASP . 18397 1 23 . ALA . 18397 1 24 . ALA . 18397 1 25 . THR . 18397 1 26 . ALA . 18397 1 27 . GLU . 18397 1 28 . LYS . 18397 1 29 . VAL . 18397 1 30 . PHE . 18397 1 31 . LYS . 18397 1 32 . GLN . 18397 1 33 . TYR . 18397 1 34 . ALA . 18397 1 35 . ASN . 18397 1 36 . ASP . 18397 1 37 . ASN . 18397 1 38 . GLY . 18397 1 39 . VAL . 18397 1 40 . ASP . 18397 1 41 . GLY . 18397 1 42 . GLU . 18397 1 43 . TRP . 18397 1 44 . THR . 18397 1 45 . TYR . 18397 1 46 . ASP . 18397 1 47 . ASP . 18397 1 48 . ALA . 18397 1 49 . THR . 18397 1 50 . LYS . 18397 1 51 . THR . 18397 1 52 . PHE . 18397 1 53 . THR . 18397 1 54 . VAL . 18397 1 55 . THR . 18397 1 56 . GLU . 18397 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 18397 1 . GLN 2 2 18397 1 . TYR 3 3 18397 1 . LYS 4 4 18397 1 . LEU 5 5 18397 1 . ILE 6 6 18397 1 . LEU 7 7 18397 1 . ASN 8 8 18397 1 . GLY 9 9 18397 1 . LYS 10 10 18397 1 . THR 11 11 18397 1 . LEU 12 12 18397 1 . LYS 13 13 18397 1 . GLY 14 14 18397 1 . GLU 15 15 18397 1 . THR 16 16 18397 1 . THR 17 17 18397 1 . THR 18 18 18397 1 . GLU 19 19 18397 1 . ALA 20 20 18397 1 . VAL 21 21 18397 1 . ASP 22 22 18397 1 . ALA 23 23 18397 1 . ALA 24 24 18397 1 . THR 25 25 18397 1 . ALA 26 26 18397 1 . GLU 27 27 18397 1 . LYS 28 28 18397 1 . VAL 29 29 18397 1 . PHE 30 30 18397 1 . LYS 31 31 18397 1 . GLN 32 32 18397 1 . TYR 33 33 18397 1 . ALA 34 34 18397 1 . ASN 35 35 18397 1 . ASP 36 36 18397 1 . ASN 37 37 18397 1 . GLY 38 38 18397 1 . VAL 39 39 18397 1 . ASP 40 40 18397 1 . GLY 41 41 18397 1 . GLU 42 42 18397 1 . TRP 43 43 18397 1 . THR 44 44 18397 1 . TYR 45 45 18397 1 . ASP 46 46 18397 1 . ASP 47 47 18397 1 . ALA 48 48 18397 1 . THR 49 49 18397 1 . LYS 50 50 18397 1 . THR 51 51 18397 1 . PHE 52 52 18397 1 . THR 53 53 18397 1 . VAL 54 54 18397 1 . THR 55 55 18397 1 . GLU 56 56 18397 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 18397 _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 $GB1 . 1301 organism . 'Streptococcal bacteria' 'Streptococcal bacteria' . . Bacteria . Streptococcal bacteria . . . . . . . . . . . . . . . . . . . . . 18397 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 18397 _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 $GB1 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . NA . . . . . . 18397 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18397 _Sample.ID 1 _Sample.Type solid _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '100% H2O' _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 GB1 '[U-98% 13C; U-98% 15N]' . . 1 $GB1 . . 5 . . mg . . . . 18397 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 18397 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pressure 1 . atm 18397 1 temperature 273 . K 18397 1 stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 18397 _Software.ID 1 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 18397 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 18397 1 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 18397 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 18397 _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 Varian INOVA . 750 . . . 18397 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 18397 _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 NH no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18397 1 2 CANH no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18397 1 3 CA(CO)NH no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18397 1 4 CANH no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18397 1 5 CONH no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18397 1 6 CO(CA)NH no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18397 1 7 CBCANH no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18397 1 8 CBCA(CO)NH no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18397 1 stop_ save_ save_NMR_spectrometer_expt _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spectrometer_expt _NMR_spec_expt.Entry_ID 18397 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name . _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $spectrometer_1 _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 1 _NMR_spec_expt.Software_label $SPARKY _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_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 18397 _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 0.00 na indirect 0.251449530 . . . . . . . . . 18397 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 18397 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 18397 1 P 31 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.404808636 . . . . . . . . . 18397 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_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 18397 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _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 NH . . . 18397 1 2 CANH . . . 18397 1 3 CA(CO)NH . . . 18397 1 5 CONH . . . 18397 1 6 CO(CA)NH . . . 18397 1 7 CBCANH . . . 18397 1 8 CBCA(CO)NH . . . 18397 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 MET C C 13 171.092 0.016 . 1 . . . . 1 M C . 18397 1 2 . 1 1 1 1 MET CA C 13 54.539 0.022 . 1 . . . . 1 M CA . 18397 1 3 . 1 1 1 1 MET CB C 13 32.307 0.084 . 1 . . . . 1 M CB . 18397 1 4 . 1 1 1 1 MET CG C 13 29.999 0.000 . 1 . . . . 1 M CG . 18397 1 5 . 1 1 2 2 GLN H H 1 8.614 0.033 . 1 . . . . 2 Q HN . 18397 1 6 . 1 1 2 2 GLN HE21 H 1 7.936 0.000 . . . . . . 2 Q HE1 . 18397 1 7 . 1 1 2 2 GLN HE22 H 1 7.085 0.000 . . . . . . 2 Q HE2 . 18397 1 8 . 1 1 2 2 GLN C C 13 174.871 0.013 . 1 . . . . 2 Q C . 18397 1 9 . 1 1 2 2 GLN CA C 13 56.087 0.012 . 1 . . . . 2 Q CA . 18397 1 10 . 1 1 2 2 GLN CB C 13 30.327 0.129 . 1 . . . . 2 Q CB . 18397 1 11 . 1 1 2 2 GLN CG C 13 35.600 0.000 . 1 . . . . 2 Q CG . 18397 1 12 . 1 1 2 2 GLN CD C 13 180.276 0.008 . 1 . . . . 2 Q CD . 18397 1 13 . 1 1 2 2 GLN N N 15 125.492 0.115 . 1 . . . . 2 Q N . 18397 1 14 . 1 1 2 2 GLN NE2 N 15 113.194 0.447 . 1 . . . . 2 Q NE2 . 18397 1 15 . 1 1 3 3 TYR H H 1 9.227 0.079 . 1 . . . . 3 Y HN . 18397 1 16 . 1 1 3 3 TYR C C 13 174.879 0.002 . 1 . . . . 3 Y C . 18397 1 17 . 1 1 3 3 TYR CA C 13 57.198 0.026 . 1 . . . . 3 Y CA . 18397 1 18 . 1 1 3 3 TYR CB C 13 43.525 0.000 . 1 . . . . 3 Y CB . 18397 1 19 . 1 1 3 3 TYR N N 15 123.694 0.160 . 1 . . . . 3 Y N . 18397 1 20 . 1 1 4 4 LYS H H 1 9.393 0.019 . 1 . . . . 4 K HN . 18397 1 21 . 1 1 4 4 LYS C C 13 173.307 0.008 . 1 . . . . 4 K C . 18397 1 22 . 1 1 4 4 LYS CA C 13 55.200 0.056 . 1 . . . . 4 K CA . 18397 1 23 . 1 1 4 4 LYS CB C 13 36.295 0.075 . 1 . . . . 4 K CB . 18397 1 24 . 1 1 4 4 LYS CG C 13 25.665 0.000 . 1 . . . . 4 K CG . 18397 1 25 . 1 1 4 4 LYS CD C 13 29.060 0.000 . 1 . . . . 4 K CD . 18397 1 26 . 1 1 4 4 LYS N N 15 122.412 0.123 . 1 . . . . 4 K N . 18397 1 27 . 1 1 5 5 LEU H H 1 9.300 0.054 . 1 . . . . 5 L HN . 18397 1 28 . 1 1 5 5 LEU C C 13 174.665 0.012 . 1 . . . . 5 L C . 18397 1 29 . 1 1 5 5 LEU CA C 13 53.053 0.031 . 1 . . . . 5 L CA . 18397 1 30 . 1 1 5 5 LEU N N 15 126.229 0.203 . 1 . . . . 5 L N . 18397 1 31 . 1 1 6 6 ILE H H 1 9.170 0.062 . 1 . . . . 6 I HN . 18397 1 32 . 1 1 6 6 ILE C C 13 175.075 0.013 . 1 . . . . 6 I C . 18397 1 33 . 1 1 6 6 ILE CA C 13 60.035 0.022 . 1 . . . . 6 I CA . 18397 1 34 . 1 1 6 6 ILE CB C 13 37.888 0.000 . 1 . . . . 6 I CB . 18397 1 35 . 1 1 6 6 ILE N N 15 126.087 0.060 . 1 . . . . 6 I N . 18397 1 36 . 1 1 7 7 LEU H H 1 9.381 0.054 . 1 . . . . 7 L HN . 18397 1 37 . 1 1 7 7 LEU C C 13 174.878 0.016 . 1 . . . . 7 L C . 18397 1 38 . 1 1 7 7 LEU CA C 13 54.844 0.061 . 1 . . . . 7 L CA . 18397 1 39 . 1 1 7 7 LEU CB C 13 42.990 0.000 . 1 . . . . 7 L CB . 18397 1 40 . 1 1 7 7 LEU CD1 C 13 26.065 0.000 . 1 . . . . 7 L CD1 . 18397 1 41 . 1 1 7 7 LEU CD2 C 13 25.090 0.000 . 1 . . . . 7 L CD2 . 18397 1 42 . 1 1 7 7 LEU N N 15 126.765 0.469 . 1 . . . . 7 L N . 18397 1 43 . 1 1 8 8 ASN H H 1 9.184 0.054 . 1 . . . . 8 N HN . 18397 1 44 . 1 1 8 8 ASN HD21 H 1 7.786 0.000 . 1 . . . . 8 N HD21 . 18397 1 45 . 1 1 8 8 ASN HD22 H 1 6.878 0.113 . 1 . . . . 8 N HD22 . 18397 1 46 . 1 1 8 8 ASN C C 13 176.222 0.012 . 1 . . . . 8 N C . 18397 1 47 . 1 1 8 8 ASN CA C 13 50.786 0.023 . 1 . . . . 8 N CA . 18397 1 48 . 1 1 8 8 ASN CB C 13 38.353 0.056 . 1 . . . . 8 N CB . 18397 1 49 . 1 1 8 8 ASN CG C 13 176.302 0.022 . 1 . . . . 8 N CG . 18397 1 50 . 1 1 8 8 ASN N N 15 124.871 0.028 . 1 . . . . 8 N N . 18397 1 51 . 1 1 8 8 ASN ND2 N 15 110.606 0.212 . 1 . . . . 8 N ND2 . 18397 1 52 . 1 1 9 9 GLY H H 1 8.320 0.047 . 1 . . . . 9 G HN . 18397 1 53 . 1 1 9 9 GLY C C 13 173.028 0.019 . 1 . . . . 9 G C . 18397 1 54 . 1 1 9 9 GLY CA C 13 44.719 0.043 . 1 . . . . 9 G CA . 18397 1 55 . 1 1 9 9 GLY N N 15 109.488 0.176 . 1 . . . . 9 G N . 18397 1 56 . 1 1 10 10 LYS H H 1 10.024 0.034 . 1 . . . . 10 K HN . 18397 1 57 . 1 1 10 10 LYS C C 13 178.983 0.008 . 1 . . . . 10 K C . 18397 1 58 . 1 1 10 10 LYS CA C 13 59.396 0.032 . 1 . . . . 10 K CA . 18397 1 59 . 1 1 10 10 LYS CB C 13 32.854 0.060 . 1 . . . . 10 K CB . 18397 1 60 . 1 1 10 10 LYS CG C 13 25.641 0.000 . 1 . . . . 10 K CG . 18397 1 61 . 1 1 10 10 LYS CD C 13 29.293 0.000 . 1 . . . . 10 K CD . 18397 1 62 . 1 1 10 10 LYS N N 15 120.801 0.064 . 1 . . . . 10 K N . 18397 1 63 . 1 1 11 11 THR H H 1 9.030 0.044 . 1 . . . . 11 T HN . 18397 1 64 . 1 1 11 11 THR C C 13 173.192 0.011 . 1 . . . . 11 T C . 18397 1 65 . 1 1 11 11 THR CA C 13 62.244 0.047 . 1 . . . . 11 T CA . 18397 1 66 . 1 1 11 11 THR CB C 13 69.802 0.000 . 1 . . . . 11 T CB . 18397 1 67 . 1 1 11 11 THR CG2 C 13 22.702 0.076 . 1 . . . . 11 T CG2 . 18397 1 68 . 1 1 11 11 THR N N 15 106.632 0.090 . 1 . . . . 11 T N . 18397 1 69 . 1 1 12 12 LEU H H 1 7.528 0.078 . 1 . . . . 12 L HN . 18397 1 70 . 1 1 12 12 LEU C C 13 173.605 0.008 . 1 . . . . 12 L C . 18397 1 71 . 1 1 12 12 LEU CA C 13 54.604 0.085 . 1 . . . . 12 L CA . 18397 1 72 . 1 1 12 12 LEU CB C 13 43.300 0.003 . 1 . . . . 12 L CB . 18397 1 73 . 1 1 12 12 LEU CD1 C 13 26.127 0.000 . 2 . . . . 12 L CD1 . 18397 1 74 . 1 1 12 12 LEU N N 15 127.355 0.072 . 1 . . . . 12 L N . 18397 1 75 . 1 1 13 13 LYS H H 1 8.880 0.051 . 1 . . . . 13 K HN . 18397 1 76 . 1 1 13 13 LYS C C 13 175.588 0.006 . 1 . . . . 13 K C . 18397 1 77 . 1 1 13 13 LYS CA C 13 53.559 0.057 . 1 . . . . 13 K CA . 18397 1 78 . 1 1 13 13 LYS N N 15 123.029 0.076 . 1 . . . . 13 K N . 18397 1 79 . 1 1 14 14 GLY H H 1 8.732 0.030 . 1 . . . . 14 G HN . 18397 1 80 . 1 1 14 14 GLY C C 13 171.138 0.011 . 1 . . . . 14 G C . 18397 1 81 . 1 1 14 14 GLY CA C 13 45.095 0.056 . 1 . . . . 14 G CA . 18397 1 82 . 1 1 14 14 GLY N N 15 105.536 0.044 . 1 . . . . 14 G N . 18397 1 83 . 1 1 15 15 GLU H H 1 8.814 0.043 . 1 . . . . 15 E HN . 18397 1 84 . 1 1 15 15 GLU C C 13 173.758 0.039 . 1 . . . . 15 E C . 18397 1 85 . 1 1 15 15 GLU CA C 13 53.930 0.019 . 1 . . . . 15 E CA . 18397 1 86 . 1 1 15 15 GLU CB C 13 33.480 0.048 . 1 . . . . 15 E CB . 18397 1 87 . 1 1 15 15 GLU N N 15 121.276 0.151 . 1 . . . . 15 E N . 18397 1 88 . 1 1 16 16 THR H H 1 8.985 0.018 . 1 . . . . 16 T HN . 18397 1 89 . 1 1 16 16 THR C C 13 171.771 0.002 . 1 . . . . 16 T C . 18397 1 90 . 1 1 16 16 THR CA C 13 60.277 0.078 . 1 . . . . 16 T CA . 18397 1 91 . 1 1 16 16 THR CB C 13 70.630 0.071 . 1 . . . . 16 T CB . 18397 1 92 . 1 1 16 16 THR CG2 C 13 20.033 0.030 . 1 . . . . 16 T CG2 . 18397 1 93 . 1 1 16 16 THR N N 15 115.485 0.373 . 1 . . . . 16 T N . 18397 1 94 . 1 1 17 17 THR H H 1 8.384 0.214 . 1 . . . . 17 T HN . 18397 1 95 . 1 1 17 17 THR C C 13 173.808 0.036 . 1 . . . . 17 T C . 18397 1 96 . 1 1 17 17 THR CA C 13 60.371 0.060 . 1 . . . . 17 T CA . 18397 1 97 . 1 1 17 17 THR CB C 13 73.011 0.068 . 1 . . . . 17 T CB . 18397 1 98 . 1 1 17 17 THR CG2 C 13 21.462 0.183 . 1 . . . . 17 T CG2 . 18397 1 99 . 1 1 17 17 THR N N 15 115.452 0.332 . 1 . . . . 17 T N . 18397 1 100 . 1 1 18 18 THR H H 1 9.332 0.070 . 1 . . . . 18 T HN . 18397 1 101 . 1 1 18 18 THR C C 13 171.025 0.012 . 1 . . . . 18 T C . 18397 1 102 . 1 1 18 18 THR CA C 13 61.681 0.041 . 1 . . . . 18 T CA . 18397 1 103 . 1 1 18 18 THR CB C 13 70.986 0.045 . 1 . . . . 18 T CB . 18397 1 104 . 1 1 18 18 THR CG2 C 13 18.719 0.051 . 1 . . . . 18 T CG2 . 18397 1 105 . 1 1 18 18 THR N N 15 115.981 0.053 . 1 . . . . 18 T N . 18397 1 106 . 1 1 19 19 GLU H H 1 7.958 0.012 . 1 . . . . 19 E HN . 18397 1 107 . 1 1 19 19 GLU C C 13 175.629 0.005 . 1 . . . . 19 E C . 18397 1 108 . 1 1 19 19 GLU CA C 13 54.326 0.037 . 1 . . . . 19 E CA . 18397 1 109 . 1 1 19 19 GLU N N 15 125.042 0.064 . 1 . . . . 19 E N . 18397 1 110 . 1 1 20 20 ALA H H 1 9.585 0.026 . 1 . . . . 20 A HN . 18397 1 111 . 1 1 20 20 ALA C C 13 177.610 0.004 . 1 . . . . 20 A C . 18397 1 112 . 1 1 20 20 ALA CA C 13 50.812 0.021 . 1 . . . . 20 A CA . 18397 1 113 . 1 1 20 20 ALA CB C 13 23.712 0.044 . 1 . . . . 20 A CB . 18397 1 114 . 1 1 20 20 ALA N N 15 125.338 0.130 . 1 . . . . 20 A N . 18397 1 115 . 1 1 21 21 VAL H H 1 8.839 0.035 . 1 . . . . 21 V HN . 18397 1 116 . 1 1 21 21 VAL C C 13 174.702 0.005 . 1 . . . . 21 V C . 18397 1 117 . 1 1 21 21 VAL CA C 13 63.727 0.044 . 1 . . . . 21 V CA . 18397 1 118 . 1 1 21 21 VAL CB C 13 31.962 0.000 . 1 . . . . 21 V CB . 18397 1 119 . 1 1 21 21 VAL CG1 C 13 20.989 0.000 . 2 . . . . 21 V CG1 . 18397 1 120 . 1 1 21 21 VAL N N 15 116.466 0.184 . 1 . . . . 21 V N . 18397 1 121 . 1 1 22 22 ASP H H 1 7.381 0.029 . 1 . . . . 22 D HN . 18397 1 122 . 1 1 22 22 ASP C C 13 174.903 0.010 . 1 . . . . 22 D C . 18397 1 123 . 1 1 22 22 ASP CA C 13 52.472 0.023 . 1 . . . . 22 D CA . 18397 1 124 . 1 1 22 22 ASP CB C 13 42.674 0.456 . 1 . . . . 22 D CB . 18397 1 125 . 1 1 22 22 ASP N N 15 115.526 0.160 . 1 . . . . 22 D N . 18397 1 126 . 1 1 23 23 ALA H H 1 9.379 0.033 . 1 . . . . 23 A HN . 18397 1 127 . 1 1 23 23 ALA C C 13 179.756 0.010 . 1 . . . . 23 A C . 18397 1 128 . 1 1 23 23 ALA CA C 13 54.754 0.029 . 1 . . . . 23 A CA . 18397 1 129 . 1 1 23 23 ALA CB C 13 18.233 0.041 . 1 . . . . 23 A CB . 18397 1 130 . 1 1 23 23 ALA N N 15 122.995 0.280 . 1 . . . . 23 A N . 18397 1 131 . 1 1 24 24 ALA H H 1 8.282 0.016 . 1 . . . . 24 A HN . 18397 1 132 . 1 1 24 24 ALA C C 13 181.382 0.042 . 1 . . . . 24 A C . 18397 1 133 . 1 1 24 24 ALA CA C 13 54.717 0.030 . 1 . . . . 24 A CA . 18397 1 134 . 1 1 24 24 ALA CB C 13 18.136 0.041 . 1 . . . . 24 A CB . 18397 1 135 . 1 1 24 24 ALA N N 15 120.606 0.170 . 1 . . . . 24 A N . 18397 1 136 . 1 1 25 25 THR H H 1 8.537 0.040 . 1 . . . . 25 T HN . 18397 1 137 . 1 1 25 25 THR C C 13 175.655 0.011 . 1 . . . . 25 T C . 18397 1 138 . 1 1 25 25 THR CA C 13 67.566 0.030 . 1 . . . . 25 T CA . 18397 1 139 . 1 1 25 25 THR CB C 13 67.595 0.000 . 1 . . . . 25 T CB . 18397 1 140 . 1 1 25 25 THR CG2 C 13 21.293 0.026 . 1 . . . . 25 T CG2 . 18397 1 141 . 1 1 25 25 THR N N 15 117.026 0.039 . 1 . . . . 25 T N . 18397 1 142 . 1 1 26 26 ALA H H 1 7.441 0.032 . 1 . . . . 26 A HN . 18397 1 143 . 1 1 26 26 ALA C C 13 177.254 0.177 . 1 . . . . 26 A C . 18397 1 144 . 1 1 26 26 ALA CA C 13 55.243 0.033 . 1 . . . . 26 A CA . 18397 1 145 . 1 1 26 26 ALA CB C 13 17.563 0.068 . 1 . . . . 26 A CB . 18397 1 146 . 1 1 26 26 ALA N N 15 123.886 0.148 . 1 . . . . 26 A N . 18397 1 147 . 1 1 27 27 GLU H H 1 8.848 0.034 . 1 . . . . 27 E HN . 18397 1 148 . 1 1 27 27 GLU C C 13 177.705 0.011 . 1 . . . . 27 E C . 18397 1 149 . 1 1 27 27 GLU CA C 13 59.304 0.080 . 1 . . . . 27 E CA . 18397 1 150 . 1 1 27 27 GLU CB C 13 29.137 0.006 . 1 . . . . 27 E CB . 18397 1 151 . 1 1 27 27 GLU N N 15 116.190 0.025 . 1 . . . . 27 E N . 18397 1 152 . 1 1 28 28 LYS H H 1 7.047 0.053 . 1 . . . . 28 K HN . 18397 1 153 . 1 1 28 28 LYS C C 13 178.784 0.004 . 1 . . . . 28 K C . 18397 1 154 . 1 1 28 28 LYS CA C 13 60.492 0.072 . 1 . . . . 28 K CA . 18397 1 155 . 1 1 28 28 LYS CB C 13 32.794 0.031 . 1 . . . . 28 K CB . 18397 1 156 . 1 1 28 28 LYS N N 15 117.225 0.088 . 1 . . . . 28 K N . 18397 1 157 . 1 1 29 29 VAL H H 1 7.651 0.029 . 1 . . . . 29 V HN . 18397 1 158 . 1 1 29 29 VAL C C 13 178.587 0.023 . 1 . . . . 29 V C . 18397 1 159 . 1 1 29 29 VAL CA C 13 66.603 0.009 . 1 . . . . 29 V CA . 18397 1 160 . 1 1 29 29 VAL CB C 13 32.004 0.011 . 1 . . . . 29 V CB . 18397 1 161 . 1 1 29 29 VAL CG1 C 13 22.242 0.000 . 1 . . . . 29 V CG1 . 18397 1 162 . 1 1 29 29 VAL CG2 C 13 21.093 0.000 . 1 . . . . 29 V CG2 . 18397 1 163 . 1 1 29 29 VAL N N 15 119.031 0.148 . 1 . . . . 29 V N . 18397 1 164 . 1 1 30 30 PHE H H 1 8.795 0.012 . 1 . . . . 30 F HN . 18397 1 165 . 1 1 30 30 PHE C C 13 178.919 0.003 . 1 . . . . 30 F C . 18397 1 166 . 1 1 30 30 PHE CA C 13 57.407 0.118 . 1 . . . . 30 F CA . 18397 1 167 . 1 1 30 30 PHE N N 15 118.349 0.065 . 1 . . . . 30 F N . 18397 1 168 . 1 1 31 31 LYS H H 1 9.199 0.039 . 1 . . . . 31 K HN . 18397 1 169 . 1 1 31 31 LYS C C 13 179.592 0.031 . 1 . . . . 31 K C . 18397 1 170 . 1 1 31 31 LYS CA C 13 60.311 0.033 . 1 . . . . 31 K CA . 18397 1 171 . 1 1 31 31 LYS CB C 13 31.855 0.000 . 1 . . . . 31 K CB . 18397 1 172 . 1 1 31 31 LYS CD C 13 29.227 0.000 . 1 . . . . 31 K CD . 18397 1 173 . 1 1 31 31 LYS N N 15 120.627 0.104 . 1 . . . . 31 K N . 18397 1 174 . 1 1 32 32 GLN H H 1 7.999 0.044 . 1 . . . . 32 Q HN . 18397 1 175 . 1 1 32 32 GLN HE21 H 1 8.153 0.000 . 1 . . . . 32 Q HE21 . 18397 1 176 . 1 1 32 32 GLN HE22 H 1 7.044 0.000 . 1 . . . . 32 Q HE22 . 18397 1 177 . 1 1 32 32 GLN C C 13 177.398 0.009 . 1 . . . . 32 Q C . 18397 1 178 . 1 1 32 32 GLN CA C 13 59.045 0.010 . 1 . . . . 32 Q CA . 18397 1 179 . 1 1 32 32 GLN CB C 13 28.971 0.030 . 1 . . . . 32 Q CB . 18397 1 180 . 1 1 32 32 GLN CD C 13 179.759 0.008 . 1 . . . . 32 Q CD . 18397 1 181 . 1 1 32 32 GLN N N 15 121.124 0.090 . 1 . . . . 32 Q N . 18397 1 182 . 1 1 32 32 GLN NE2 N 15 115.639 0.601 . 1 . . . . 32 Q NE2 . 18397 1 183 . 1 1 33 33 TYR H H 1 8.765 0.055 . 1 . . . . 33 Y HN . 18397 1 184 . 1 1 33 33 TYR C C 13 178.535 0.013 . 1 . . . . 33 Y C . 18397 1 185 . 1 1 33 33 TYR CA C 13 61.876 0.046 . 1 . . . . 33 Y CA . 18397 1 186 . 1 1 33 33 TYR CB C 13 38.895 0.000 . 1 . . . . 33 Y CB . 18397 1 187 . 1 1 33 33 TYR N N 15 120.732 0.058 . 1 . . . . 33 Y N . 18397 1 188 . 1 1 34 34 ALA H H 1 9.351 0.023 . 1 . . . . 34 A HN . 18397 1 189 . 1 1 34 34 ALA C C 13 179.403 0.007 . 1 . . . . 34 A C . 18397 1 190 . 1 1 34 34 ALA CA C 13 56.301 0.051 . 1 . . . . 34 A CA . 18397 1 191 . 1 1 34 34 ALA CB C 13 17.980 0.031 . 1 . . . . 34 A CB . 18397 1 192 . 1 1 34 34 ALA N N 15 122.513 0.061 . 1 . . . . 34 A N . 18397 1 193 . 1 1 35 35 ASN H H 1 8.490 0.019 . 1 . . . . 35 N HN . 18397 1 194 . 1 1 35 35 ASN HD21 H 1 7.725 0.000 . 1 . . . . 35 N HD21 . 18397 1 195 . 1 1 35 35 ASN HD22 H 1 7.104 0.128 . 1 . . . . 35 N HD22 . 18397 1 196 . 1 1 35 35 ASN C C 13 179.449 0.100 . 1 . . . . 35 N C . 18397 1 197 . 1 1 35 35 ASN CA C 13 57.277 0.013 . 1 . . . . 35 N CA . 18397 1 198 . 1 1 35 35 ASN CB C 13 39.420 0.043 . 1 . . . . 35 N CB . 18397 1 199 . 1 1 35 35 ASN CG C 13 175.980 0.013 . 1 . . . . 35 N CG . 18397 1 200 . 1 1 35 35 ASN N N 15 118.069 0.101 . 1 . . . . 35 N N . 18397 1 201 . 1 1 35 35 ASN ND2 N 15 113.083 0.461 . 1 . . . . 35 N ND2 . 18397 1 202 . 1 1 36 36 ASP H H 1 9.138 0.022 . 1 . . . . 36 D HN . 18397 1 203 . 1 1 36 36 ASP C C 13 175.893 0.001 . 1 . . . . 36 D C . 18397 1 204 . 1 1 36 36 ASP CA C 13 56.078 0.029 . 1 . . . . 36 D CA . 18397 1 205 . 1 1 36 36 ASP CB C 13 38.448 0.090 . 1 . . . . 36 D CB . 18397 1 206 . 1 1 36 36 ASP N N 15 120.981 0.032 . 1 . . . . 36 D N . 18397 1 207 . 1 1 37 37 ASN H H 1 7.390 0.083 . 1 . . . . 37 N HN . 18397 1 208 . 1 1 37 37 ASN HD21 H 1 6.709 0.000 . 1 . . . . 37 N HD21 . 18397 1 209 . 1 1 37 37 ASN HD22 H 1 6.013 0.086 . 1 . . . . 37 N HD22 . 18397 1 210 . 1 1 37 37 ASN C C 13 174.041 0.008 . 1 . . . . 37 N C . 18397 1 211 . 1 1 37 37 ASN CA C 13 53.696 0.018 . 1 . . . . 37 N CA . 18397 1 212 . 1 1 37 37 ASN CB C 13 40.478 0.116 . 1 . . . . 37 N CB . 18397 1 213 . 1 1 37 37 ASN CG C 13 176.605 0.016 . 1 . . . . 37 N CG . 18397 1 214 . 1 1 37 37 ASN N N 15 114.744 0.098 . 1 . . . . 37 N N . 18397 1 215 . 1 1 37 37 ASN ND2 N 15 113.876 0.442 . 1 . . . . 37 N ND2 . 18397 1 216 . 1 1 38 38 GLY H H 1 8.015 0.022 . 1 . . . . 38 G HN . 18397 1 217 . 1 1 38 38 GLY C C 13 173.849 0.027 . 1 . . . . 38 G C . 18397 1 218 . 1 1 38 38 GLY CA C 13 47.033 0.069 . 1 . . . . 38 G CA . 18397 1 219 . 1 1 38 38 GLY N N 15 108.276 0.074 . 1 . . . . 38 G N . 18397 1 220 . 1 1 39 39 VAL H H 1 8.336 0.028 . 1 . . . . 39 V HN . 18397 1 221 . 1 1 39 39 VAL C C 13 174.959 0.007 . 1 . . . . 39 V C . 18397 1 222 . 1 1 39 39 VAL CA C 13 61.952 0.014 . 1 . . . . 39 V CA . 18397 1 223 . 1 1 39 39 VAL CB C 13 31.827 0.094 . 1 . . . . 39 V CB . 18397 1 224 . 1 1 39 39 VAL CG1 C 13 22.015 0.080 . 2 . . . . 39 V CG1 . 18397 1 225 . 1 1 39 39 VAL N N 15 121.642 0.046 . 1 . . . . 39 V N . 18397 1 226 . 1 1 40 40 ASP H H 1 9.221 0.040 . 1 . . . . 40 D HN . 18397 1 227 . 1 1 40 40 ASP C C 13 174.739 0.048 . 1 . . . . 40 D C . 18397 1 228 . 1 1 40 40 ASP CA C 13 52.637 0.074 . 1 . . . . 40 D CA . 18397 1 229 . 1 1 40 40 ASP CB C 13 41.176 0.007 . 1 . . . . 40 D CB . 18397 1 230 . 1 1 40 40 ASP N N 15 130.657 0.072 . 1 . . . . 40 D N . 18397 1 231 . 1 1 41 41 GLY H H 1 8.174 0.014 . 1 . . . . 41 G HN . 18397 1 232 . 1 1 41 41 GLY C C 13 172.643 0.014 . 1 . . . . 41 G C . 18397 1 233 . 1 1 41 41 GLY CA C 13 45.256 0.025 . 1 . . . . 41 G CA . 18397 1 234 . 1 1 41 41 GLY N N 15 108.113 0.142 . 1 . . . . 41 G N . 18397 1 235 . 1 1 42 42 GLU H H 1 8.678 0.018 . 1 . . . . 42 E HN . 18397 1 236 . 1 1 42 42 GLU C C 13 177.760 0.009 . 1 . . . . 42 E C . 18397 1 237 . 1 1 42 42 GLU CA C 13 54.921 0.023 . 1 . . . . 42 E CA . 18397 1 238 . 1 1 42 42 GLU CB C 13 31.053 0.000 . 1 . . . . 42 E CB . 18397 1 239 . 1 1 42 42 GLU N N 15 118.256 0.325 . 1 . . . . 42 E N . 18397 1 240 . 1 1 43 43 TRP H H 1 9.310 0.061 . 1 . . . . 43 W HN . 18397 1 241 . 1 1 43 43 TRP HE1 H 1 10.645 0.000 . 1 . . . . 43 W HE1 . 18397 1 242 . 1 1 43 43 TRP C C 13 177.163 0.013 . 1 . . . . 43 W C . 18397 1 243 . 1 1 43 43 TRP CA C 13 57.710 0.040 . 1 . . . . 43 W CA . 18397 1 244 . 1 1 43 43 TRP CB C 13 33.649 0.000 . 1 . . . . 43 W CB . 18397 1 245 . 1 1 43 43 TRP N N 15 124.691 0.102 . 1 . . . . 43 W N . 18397 1 246 . 1 1 43 43 TRP NE1 N 15 130.989 0.000 . 1 . . . . 43 W NE1 . 18397 1 247 . 1 1 44 44 THR H H 1 9.172 0.143 . 1 . . . . 44 T HN . 18397 1 248 . 1 1 44 44 THR C C 13 173.743 0.011 . 1 . . . . 44 T C . 18397 1 249 . 1 1 44 44 THR CA C 13 61.162 0.064 . 1 . . . . 44 T CA . 18397 1 250 . 1 1 44 44 THR CG2 C 13 20.900 0.000 . 1 . . . . 44 T CG2 . 18397 1 251 . 1 1 44 44 THR N N 15 109.013 0.084 . 1 . . . . 44 T N . 18397 1 252 . 1 1 45 45 TYR H H 1 9.461 0.018 . 1 . . . . 45 Y HN . 18397 1 253 . 1 1 45 45 TYR C C 13 171.761 0.016 . 1 . . . . 45 Y C . 18397 1 254 . 1 1 45 45 TYR CA C 13 58.067 0.015 . 1 . . . . 45 Y CA . 18397 1 255 . 1 1 45 45 TYR N N 15 118.389 0.099 . 1 . . . . 45 Y N . 18397 1 256 . 1 1 46 46 ASP H H 1 7.597 0.057 . 1 . . . . 46 D HN . 18397 1 257 . 1 1 46 46 ASP C C 13 175.751 0.069 . 1 . . . . 46 D C . 18397 1 258 . 1 1 46 46 ASP CA C 13 50.843 0.041 . 1 . . . . 46 D CA . 18397 1 259 . 1 1 46 46 ASP CB C 13 42.096 0.109 . 1 . . . . 46 D CB . 18397 1 260 . 1 1 46 46 ASP N N 15 126.303 0.063 . 1 . . . . 46 D N . 18397 1 261 . 1 1 47 47 ASP H H 1 8.920 0.028 . 1 . . . . 47 D HN . 18397 1 262 . 1 1 47 47 ASP C C 13 177.013 0.006 . 1 . . . . 47 D C . 18397 1 263 . 1 1 47 47 ASP CA C 13 54.694 0.036 . 1 . . . . 47 D CA . 18397 1 264 . 1 1 47 47 ASP CB C 13 42.930 0.142 . 1 . . . . 47 D CB . 18397 1 265 . 1 1 47 47 ASP N N 15 123.239 0.048 . 1 . . . . 47 D N . 18397 1 266 . 1 1 48 48 ALA H H 1 8.485 0.042 . 1 . . . . 48 A HN . 18397 1 267 . 1 1 48 48 ALA C C 13 179.369 0.053 . 1 . . . . 48 A C . 18397 1 268 . 1 1 48 48 ALA CA C 13 54.027 0.096 . 1 . . . . 48 A CA . 18397 1 269 . 1 1 48 48 ALA CB C 13 19.069 0.032 . 1 . . . . 48 A CB . 18397 1 270 . 1 1 48 48 ALA N N 15 118.389 0.204 . 1 . . . . 48 A N . 18397 1 271 . 1 1 49 49 THR H H 1 7.041 0.017 . 1 . . . . 49 T HN . 18397 1 272 . 1 1 49 49 THR C C 13 175.691 0.005 . 1 . . . . 49 T C . 18397 1 273 . 1 1 49 49 THR CA C 13 60.457 0.029 . 1 . . . . 49 T CA . 18397 1 274 . 1 1 49 49 THR CB C 13 69.903 0.013 . 1 . . . . 49 T CB . 18397 1 275 . 1 1 49 49 THR CG2 C 13 21.600 0.017 . 1 . . . . 49 T CG2 . 18397 1 276 . 1 1 49 49 THR N N 15 104.191 0.068 . 1 . . . . 49 T N . 18397 1 277 . 1 1 50 50 LYS H H 1 7.980 0.112 . 1 . . . . 50 K HN . 18397 1 278 . 1 1 50 50 LYS C C 13 175.244 0.004 . 1 . . . . 50 K C . 18397 1 279 . 1 1 50 50 LYS CA C 13 55.502 0.028 . 1 . . . . 50 K CA . 18397 1 280 . 1 1 50 50 LYS N N 15 119.386 0.080 . 1 . . . . 50 K N . 18397 1 281 . 1 1 51 51 THR H H 1 7.563 0.044 . 1 . . . . 51 T HN . 18397 1 282 . 1 1 51 51 THR C C 13 174.145 0.005 . 1 . . . . 51 T C . 18397 1 283 . 1 1 51 51 THR CA C 13 62.662 0.030 . 1 . . . . 51 T CA . 18397 1 284 . 1 1 51 51 THR CB C 13 71.835 0.128 . 1 . . . . 51 T CB . 18397 1 285 . 1 1 51 51 THR CG2 C 13 21.019 0.101 . 1 . . . . 51 T CG2 . 18397 1 286 . 1 1 51 51 THR N N 15 111.885 0.160 . 1 . . . . 51 T N . 18397 1 287 . 1 1 52 52 PHE H H 1 10.846 0.032 . 1 . . . . 52 F HN . 18397 1 288 . 1 1 52 52 PHE C C 13 175.577 0.011 . 1 . . . . 52 F C . 18397 1 289 . 1 1 52 52 PHE CA C 13 56.675 0.100 . 1 . . . . 52 F CA . 18397 1 290 . 1 1 52 52 PHE CB C 13 43.466 0.114 . 1 . . . . 52 F CB . 18397 1 291 . 1 1 52 52 PHE N N 15 130.269 0.120 . 1 . . . . 52 F N . 18397 1 292 . 1 1 53 53 THR H H 1 9.386 0.098 . 1 . . . . 53 T HN . 18397 1 293 . 1 1 53 53 THR C C 13 171.904 0.007 . 1 . . . . 53 T C . 18397 1 294 . 1 1 53 53 THR CA C 13 60.435 0.028 . 1 . . . . 53 T CA . 18397 1 295 . 1 1 53 53 THR CG2 C 13 20.975 0.000 . 1 . . . . 53 T CG2 . 18397 1 296 . 1 1 53 53 THR N N 15 111.920 0.167 . 1 . . . . 53 T N . 18397 1 297 . 1 1 54 54 VAL H H 1 8.353 0.098 . 1 . . . . 54 V HN . 18397 1 298 . 1 1 54 54 VAL C C 13 172.442 0.006 . 1 . . . . 54 V C . 18397 1 299 . 1 1 54 54 VAL CA C 13 58.666 0.019 . 1 . . . . 54 V CA . 18397 1 300 . 1 1 54 54 VAL CB C 13 32.588 0.049 . 1 . . . . 54 V CB . 18397 1 301 . 1 1 54 54 VAL CG1 C 13 21.876 0.027 . 2 . . . . 54 V CG1 . 18397 1 302 . 1 1 54 54 VAL N N 15 118.136 0.037 . 1 . . . . 54 V N . 18397 1 303 . 1 1 55 55 THR H H 1 8.548 0.028 . 1 . . . . 55 T HN . 18397 1 304 . 1 1 55 55 THR C C 13 174.055 0.006 . 1 . . . . 55 T C . 18397 1 305 . 1 1 55 55 THR CA C 13 61.514 0.056 . 1 . . . . 55 T CA . 18397 1 306 . 1 1 55 55 THR CB C 13 72.302 0.042 . 1 . . . . 55 T CB . 18397 1 307 . 1 1 55 55 THR CG2 C 13 21.298 0.078 . 1 . . . . 55 T CG2 . 18397 1 308 . 1 1 55 55 THR N N 15 123.794 0.043 . 1 . . . . 55 T N . 18397 1 309 . 1 1 56 56 GLU H H 1 8.046 0.025 . 1 . . . . 56 E HN . 18397 1 310 . 1 1 56 56 GLU C C 13 180.103 0.001 . 1 . . . . 56 E C . 18397 1 311 . 1 1 56 56 GLU CA C 13 57.562 0.029 . 1 . . . . 56 E CA . 18397 1 312 . 1 1 56 56 GLU CB C 13 33.192 0.019 . 1 . . . . 56 E CB . 18397 1 313 . 1 1 56 56 GLU N N 15 131.081 0.103 . 1 . . . . 56 E N . 18397 1 stop_ save_