data_7350 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 7350 _Entry.Title ; NMR SOLUTION STRUCTURE OF A PROTEIN ASPARTIC ACID PHOSPHATE PHOSPHATASE FROM BACILLUS ANTHRACIS ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2006-12-01 _Entry.Accession_date 2006-12-05 _Entry.Last_release_date 2008-08-14 _Entry.Original_release_date 2008-08-14 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version . _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _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 R. Grenha R. . . 7350 2 N. Rzechorzek N. . . 7350 3 J. Brannigan J. A. . 7350 4 E. Ab E. . . 7350 5 G. Folkers G. . . 7350 6 R. Dejong R. . . 7350 7 T. Diercks T. . . 7350 8 A. Wilkinson A. J. . 7350 9 R. Kaptein R. . . 7350 10 K. Wilson K. S. . 7350 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID ANTHRACIS ANTHRACIS 7350 ANTITHETICAL ANTITHETICAL 7350 BACILLUS BACILLUS 7350 NEGATIVE NEGATIVE 7350 PHOSPHATASE PHOSPHATASE 7350 PHOSPHORYLATION PHOSPHORYLATION 7350 REGULATOR REGULATOR 7350 SPINE SPINE 7350 SPORULATION SPORULATION 7350 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 7350 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 257 7350 '15N chemical shifts' 59 7350 '1H chemical shifts' 433 7350 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 . . 2008-08-14 2006-12-01 original author . 7350 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2BZB 'BMRB Entry Tracking System' 7350 stop_ save_ ############### # Citations # ############### save_citations _Citation.Sf_category citations _Citation.Sf_framecode citations _Citation.Entry_ID 7350 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 17001075 _Citation.Full_citation . _Citation.Title 'Structural characterization of Spo0E-like protein-aspartic acid phosphatases that regulate sporulation in bacilli.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full 'The Journal of Biological Chemistry' _Citation.Journal_volume 281 _Citation.Journal_issue 49 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD 9999 _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 37993 _Citation.Page_last 38003 _Citation.Year 2006 _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 Rosa Grenha . . . 7350 1 2 Neil Rzechorzek . J. . 7350 1 3 James Brannigan . A. . 7350 1 4 Rob 'de Jong' . N. . 7350 1 5 Eiso AB . . . 7350 1 6 Tammo Diercks . . . 7350 1 7 Vincent Truffault . . . 7350 1 8 Joanne Ladds . C. . 7350 1 9 Mark Fogg . J. . 7350 1 10 Christina Bongiorni . . . 7350 1 11 Marta Perego . . . 7350 1 12 Robert Kaptein . . . 7350 1 13 Keith Wilson . S. . 7350 1 14 Gert Folkers . E. . 7350 1 15 Anthony Wilkinson . J. . 7350 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 7350 _Assembly.ID 1 _Assembly.Name CONSERVED_DOMAIN_PROTEIN _Assembly.BMRB_code . _Assembly.Number_of_components 1 _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 CONSERVED_DOMAIN_PROTEIN 1 $CONSERVED_DOMAIN_PROTEIN A . yes native no no . . . 7350 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_CONSERVED_DOMAIN_PROTEIN _Entity.Sf_category entity _Entity.Sf_framecode CONSERVED_DOMAIN_PROTEIN _Entity.Entry_ID 7350 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name CONSERVED_DOMAIN_PROTEIN _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; MEMGQLKNKIENKKKELIQL VARHGLDHDKVLLFSRDLDK LINKFMNVKDKVHK ; _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 yes _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 54 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID 1 _Entity.Fragment 'SMALL ASPARTIC ACID PHOSPHATE PHOSPHATASE' _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 2BZB . "Nmr Solution Structure Of A Protein Aspartic Acid Phosphate Phosphatase From Bacillus Anthracis" . . . . . 100.00 62 100.00 100.00 3.38e-27 . . . . 7350 1 2 no DBJ BAL17403 . "conserved domain protein [Bacillus cereus NC7401]" . . . . . 100.00 72 98.15 98.15 1.12e-26 . . . . 7350 1 3 no DBJ GAE97096 . "stage 0 sporulation regulatory protein [Bacillus anthracis CZC5]" . . . . . 100.00 63 100.00 100.00 1.86e-27 . . . . 7350 1 4 no EMBL CCW06493 . "Stage 0 sporulation regulatory protein [Bacillus sp. GeD10]" . . . . . 100.00 54 98.15 98.15 2.20e-26 . . . . 7350 1 5 no GB AAP25588 . "stage 0 sporulation regulatory protein [Bacillus anthracis str. Ames]" . . . . . 100.00 72 100.00 100.00 1.13e-27 . . . . 7350 1 6 no GB AAT30765 . "conserved domain protein [Bacillus anthracis str. 'Ames Ancestor']" . . . . . 100.00 72 100.00 100.00 1.13e-27 . . . . 7350 1 7 no GB AAT53854 . "conserved domain protein [Bacillus anthracis str. Sterne]" . . . . . 100.00 72 100.00 100.00 1.13e-27 . . . . 7350 1 8 no GB AAT63164 . "possible stage 0 sporulation regulatory protein [Bacillus thuringiensis serovar konkukian str. 97-27]" . . . . . 100.00 72 98.15 98.15 1.12e-26 . . . . 7350 1 9 no GB AAU18752 . "possible stage 0 sporulation regulatory protein [Bacillus cereus E33L]" . . . . . 100.00 72 98.15 98.15 1.12e-26 . . . . 7350 1 10 no REF NP_844102 . "stage 0 sporulation regulatory protein [Bacillus anthracis str. Ames]" . . . . . 100.00 72 100.00 100.00 1.13e-27 . . . . 7350 1 11 no REF WP_000291689 . "MULTISPECIES: hypothetical protein [Bacillus]" . . . . . 100.00 72 98.15 98.15 1.14e-26 . . . . 7350 1 12 no REF WP_000425177 . "hypothetical protein [Bacillus cereus]" . . . . . 100.00 54 98.15 98.15 2.20e-26 . . . . 7350 1 13 no REF WP_000515272 . "MULTISPECIES: hypothetical protein [Bacillus cereus group]" . . . . . 100.00 63 98.15 98.15 1.98e-26 . . . . 7350 1 14 no REF WP_000515273 . "hypothetical protein [Bacillus anthracis]" . . . . . 100.00 63 100.00 100.00 1.86e-27 . . . . 7350 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 . 7350 1 2 . GLU . 7350 1 3 . MET . 7350 1 4 . GLY . 7350 1 5 . GLN . 7350 1 6 . LEU . 7350 1 7 . LYS . 7350 1 8 . ASN . 7350 1 9 . LYS . 7350 1 10 . ILE . 7350 1 11 . GLU . 7350 1 12 . ASN . 7350 1 13 . LYS . 7350 1 14 . LYS . 7350 1 15 . LYS . 7350 1 16 . GLU . 7350 1 17 . LEU . 7350 1 18 . ILE . 7350 1 19 . GLN . 7350 1 20 . LEU . 7350 1 21 . VAL . 7350 1 22 . ALA . 7350 1 23 . ARG . 7350 1 24 . HIS . 7350 1 25 . GLY . 7350 1 26 . LEU . 7350 1 27 . ASP . 7350 1 28 . HIS . 7350 1 29 . ASP . 7350 1 30 . LYS . 7350 1 31 . VAL . 7350 1 32 . LEU . 7350 1 33 . LEU . 7350 1 34 . PHE . 7350 1 35 . SER . 7350 1 36 . ARG . 7350 1 37 . ASP . 7350 1 38 . LEU . 7350 1 39 . ASP . 7350 1 40 . LYS . 7350 1 41 . LEU . 7350 1 42 . ILE . 7350 1 43 . ASN . 7350 1 44 . LYS . 7350 1 45 . PHE . 7350 1 46 . MET . 7350 1 47 . ASN . 7350 1 48 . VAL . 7350 1 49 . LYS . 7350 1 50 . ASP . 7350 1 51 . LYS . 7350 1 52 . VAL . 7350 1 53 . HIS . 7350 1 54 . LYS . 7350 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 7350 1 . GLU 2 2 7350 1 . MET 3 3 7350 1 . GLY 4 4 7350 1 . GLN 5 5 7350 1 . LEU 6 6 7350 1 . LYS 7 7 7350 1 . ASN 8 8 7350 1 . LYS 9 9 7350 1 . ILE 10 10 7350 1 . GLU 11 11 7350 1 . ASN 12 12 7350 1 . LYS 13 13 7350 1 . LYS 14 14 7350 1 . LYS 15 15 7350 1 . GLU 16 16 7350 1 . LEU 17 17 7350 1 . ILE 18 18 7350 1 . GLN 19 19 7350 1 . LEU 20 20 7350 1 . VAL 21 21 7350 1 . ALA 22 22 7350 1 . ARG 23 23 7350 1 . HIS 24 24 7350 1 . GLY 25 25 7350 1 . LEU 26 26 7350 1 . ASP 27 27 7350 1 . HIS 28 28 7350 1 . ASP 29 29 7350 1 . LYS 30 30 7350 1 . VAL 31 31 7350 1 . LEU 32 32 7350 1 . LEU 33 33 7350 1 . PHE 34 34 7350 1 . SER 35 35 7350 1 . ARG 36 36 7350 1 . ASP 37 37 7350 1 . LEU 38 38 7350 1 . ASP 39 39 7350 1 . LYS 40 40 7350 1 . LEU 41 41 7350 1 . ILE 42 42 7350 1 . ASN 43 43 7350 1 . LYS 44 44 7350 1 . PHE 45 45 7350 1 . MET 46 46 7350 1 . ASN 47 47 7350 1 . VAL 48 48 7350 1 . LYS 49 49 7350 1 . ASP 50 50 7350 1 . LYS 51 51 7350 1 . VAL 52 52 7350 1 . HIS 53 53 7350 1 . LYS 54 54 7350 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 7350 _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 $CONSERVED_DOMAIN_PROTEIN . 1392 organism . 'BACILLUS ANTHRACIS' 'BACILLUS ANTHRACIS' . . Bacteria . Bacillus anthracis AMES . . . . . . . . . . . . . . . . . . . . 7350 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 7350 _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 $CONSERVED_DOMAIN_PROTEIN . 'recombinant technology' 'ESCHERICHIA COLI' . . . ESCHERICHIA COLI BL21 . . . . . . . . . . . . . . . PET28A . . . . . . 7350 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample _Sample.Sf_category sample _Sample.Sf_framecode sample _Sample.Entry_ID 7350 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details '90% WATER/10% D2O' _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 CONSERVED_DOMAIN_PROTEIN 'natural abundance' . . 1 $CONSERVED_DOMAIN_PROTEIN . . . . . mM . . . . 7350 1 2 D2O . . . . . . . 10 . . % . . . . 7350 1 3 H2O 'natural abundance' . . . . . . 90 . . % . . . . 7350 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 7350 _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 'ionic strength' 150 . mM 7350 1 pH 7.0 . pH 7350 1 pressure 1.0 . ATM 7350 1 temperature 298.0 . K 7350 1 stop_ save_ ############################ # Computer software used # ############################ save_CNS _Software.Sf_category software _Software.Sf_framecode CNS _Software.Entry_ID 7350 _Software.ID 1 _Software.Name CNS _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,SIMONSON,WARREN' . . 7350 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 7350 1 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 7350 _Software.ID 2 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 7350 2 stop_ save_ save_CYANA2.1 _Software.Sf_category software _Software.Sf_framecode CYANA2.1 _Software.Entry_ID 7350 _Software.ID 3 _Software.Name CYANA2.1 _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 7350 3 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 7350 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer BRUKER _NMR_spectrometer.Model OTHER _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 save_ save_700 _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode 700 _NMR_spectrometer_list.Entry_ID 7350 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 BRUKER OTHER . 700 . . . 7350 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 7350 _Experiment_list.ID 1 _Experiment_list.Details 'THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 15N- AND 13C, 15N-LABELED HIS-TAGGED' 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 HNCO no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7350 1 2 HNCACO no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7350 1 3 HNCACB no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7350 1 4 CBCACONH no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7350 1 5 HNCA no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7350 1 6 HBHACONH no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7350 1 7 HNCAHA no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7350 1 8 CCH-COSY no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7350 1 9 HCCH-TOCSY no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7350 1 10 HNH-NOESY no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7350 1 11 HCH-NOESY no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7350 1 12 'CNH- NOESY' no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7350 1 13 HH-NOESY no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7350 1 stop_ 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 7350 _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 . . . . . . . . . . . . 1 . . . 1 $citations . . 1 $citations 7350 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 7350 _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 HNCO . . . 7350 1 2 HNCACO . . . 7350 1 3 HNCACB . . . 7350 1 4 CBCACONH . . . 7350 1 5 HNCA . . . 7350 1 6 HBHACONH . . . 7350 1 7 HNCAHA . . . 7350 1 8 CCH-COSY . . . 7350 1 9 HCCH-TOCSY . . . 7350 1 10 HNH-NOESY . . . 7350 1 11 HCH-NOESY . . . 7350 1 12 'CNH- NOESY' . . . 7350 1 13 HH-NOESY . . . 7350 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 MET HA H 1 4.026 0.004 . . . . . . 1 MET HA . 7350 1 2 . 1 1 1 1 MET HB2 H 1 2.112 0.004 . . . . . . 1 MET HB1 . 7350 1 3 . 1 1 1 1 MET HB3 H 1 2.058 0.004 . . . . . . 1 MET HB2 . 7350 1 4 . 1 1 1 1 MET HE1 H 1 2.043 0.010 . . . . . . 1 MET QE . 7350 1 5 . 1 1 1 1 MET HE2 H 1 2.043 0.010 . . . . . . 1 MET QE . 7350 1 6 . 1 1 1 1 MET HE3 H 1 2.043 0.010 . . . . . . 1 MET QE . 7350 1 7 . 1 1 1 1 MET HG2 H 1 2.567 0.010 . . . . . . 1 MET HG1 . 7350 1 8 . 1 1 1 1 MET HG3 H 1 2.534 0.030 . . . . . . 1 MET HG2 . 7350 1 9 . 1 1 1 1 MET CB C 13 30.995 0.100 . . . . . . 1 MET CB . 7350 1 10 . 1 1 1 1 MET CE C 13 71.156 0.100 . . . . . . 1 MET CE . 7350 1 11 . 1 1 1 1 MET CG C 13 28.274 0.100 . . . . . . 1 MET CG . 7350 1 12 . 1 1 2 2 GLU HA H 1 4.380 0.015 . . . . . . 2 GLU HA . 7350 1 13 . 1 1 2 2 GLU HB2 H 1 2.120 0.005 . . . . . . 2 GLU HB1 . 7350 1 14 . 1 1 2 2 GLU HB3 H 1 1.944 0.008 . . . . . . 2 GLU HB2 . 7350 1 15 . 1 1 2 2 GLU HG2 H 1 2.317 0.010 . . . . . . 2 GLU HG1 . 7350 1 16 . 1 1 2 2 GLU HG3 H 1 2.301 0.015 . . . . . . 2 GLU HG2 . 7350 1 17 . 1 1 2 2 GLU CA C 13 53.725 0.100 . . . . . . 2 GLU CA . 7350 1 18 . 1 1 2 2 GLU CB C 13 27.594 0.100 . . . . . . 2 GLU CB . 7350 1 19 . 1 1 2 2 GLU CG C 13 33.553 0.100 . . . . . . 2 GLU CG . 7350 1 20 . 1 1 3 3 MET H H 1 8.786 0.010 . . . . . . 3 MET H . 7350 1 21 . 1 1 3 3 MET HA H 1 4.388 0.005 . . . . . . 3 MET HA . 7350 1 22 . 1 1 3 3 MET HB2 H 1 2.068 0.015 . . . . . . 3 MET HB1 . 7350 1 23 . 1 1 3 3 MET HB3 H 1 2.068 0.015 . . . . . . 3 MET HB2 . 7350 1 24 . 1 1 3 3 MET HE1 H 1 2.043 0.010 . . . . . . 3 MET QE . 7350 1 25 . 1 1 3 3 MET HE2 H 1 2.043 0.010 . . . . . . 3 MET QE . 7350 1 26 . 1 1 3 3 MET HE3 H 1 2.043 0.010 . . . . . . 3 MET QE . 7350 1 27 . 1 1 3 3 MET HG2 H 1 2.612 0.015 . . . . . . 3 MET HG1 . 7350 1 28 . 1 1 3 3 MET HG3 H 1 2.575 0.010 . . . . . . 3 MET HG2 . 7350 1 29 . 1 1 3 3 MET C C 13 174.957 0.100 . . . . . . 3 MET C . 7350 1 30 . 1 1 3 3 MET CA C 13 54.033 0.100 . . . . . . 3 MET CA . 7350 1 31 . 1 1 3 3 MET CB C 13 29.754 0.100 . . . . . . 3 MET CB . 7350 1 32 . 1 1 3 3 MET CE C 13 71.156 0.100 . . . . . . 3 MET CE . 7350 1 33 . 1 1 3 3 MET CG C 13 29.544 0.100 . . . . . . 3 MET CG . 7350 1 34 . 1 1 3 3 MET N N 15 123.131 0.100 . . . . . . 3 MET N . 7350 1 35 . 1 1 4 4 GLY H H 1 8.695 0.010 . . . . . . 4 GLY H . 7350 1 36 . 1 1 4 4 GLY HA2 H 1 3.961 0.009 . . . . . . 4 GLY HA1 . 7350 1 37 . 1 1 4 4 GLY HA3 H 1 3.852 0.006 . . . . . . 4 GLY HA2 . 7350 1 38 . 1 1 4 4 GLY C C 13 172.952 0.100 . . . . . . 4 GLY C . 7350 1 39 . 1 1 4 4 GLY CA C 13 43.855 0.100 . . . . . . 4 GLY CA . 7350 1 40 . 1 1 4 4 GLY N N 15 109.240 0.100 . . . . . . 4 GLY N . 7350 1 41 . 1 1 5 5 GLN H H 1 8.028 0.010 . . . . . . 5 GLN H . 7350 1 42 . 1 1 5 5 GLN HA H 1 4.254 0.005 . . . . . . 5 GLN HA . 7350 1 43 . 1 1 5 5 GLN HB2 H 1 2.161 0.005 . . . . . . 5 GLN HB1 . 7350 1 44 . 1 1 5 5 GLN HB3 H 1 2.080 0.001 . . . . . . 5 GLN HB2 . 7350 1 45 . 1 1 5 5 GLN HE21 H 1 7.557 0.010 . . . . . . 5 GLN HE21 . 7350 1 46 . 1 1 5 5 GLN HE22 H 1 6.882 0.010 . . . . . . 5 GLN HE22 . 7350 1 47 . 1 1 5 5 GLN HG2 H 1 2.449 0.004 . . . . . . 5 GLN HG1 . 7350 1 48 . 1 1 5 5 GLN HG3 H 1 2.372 0.007 . . . . . . 5 GLN HG2 . 7350 1 49 . 1 1 5 5 GLN C C 13 175.185 0.100 . . . . . . 5 GLN C . 7350 1 50 . 1 1 5 5 GLN CA C 13 54.807 0.100 . . . . . . 5 GLN CA . 7350 1 51 . 1 1 5 5 GLN CB C 13 26.166 0.100 . . . . . . 5 GLN CB . 7350 1 52 . 1 1 5 5 GLN CG C 13 31.356 0.100 . . . . . . 5 GLN CG . 7350 1 53 . 1 1 5 5 GLN N N 15 119.958 0.100 . . . . . . 5 GLN N . 7350 1 54 . 1 1 5 5 GLN NE2 N 15 112.594 0.100 . . . . . . 5 GLN NE2 . 7350 1 55 . 1 1 6 6 LEU H H 1 8.166 0.010 . . . . . . 6 LEU H . 7350 1 56 . 1 1 6 6 LEU HA H 1 4.053 0.006 . . . . . . 6 LEU HA . 7350 1 57 . 1 1 6 6 LEU HB2 H 1 1.603 0.015 . . . . . . 6 LEU HB1 . 7350 1 58 . 1 1 6 6 LEU HB3 H 1 1.774 0.015 . . . . . . 6 LEU HB2 . 7350 1 59 . 1 1 6 6 LEU HD11 H 1 0.856 0.010 . . . . . . 6 LEU QD1 . 7350 1 60 . 1 1 6 6 LEU HD12 H 1 0.856 0.010 . . . . . . 6 LEU QD1 . 7350 1 61 . 1 1 6 6 LEU HD13 H 1 0.856 0.010 . . . . . . 6 LEU QD1 . 7350 1 62 . 1 1 6 6 LEU HD21 H 1 0.913 0.015 . . . . . . 6 LEU QD2 . 7350 1 63 . 1 1 6 6 LEU HD22 H 1 0.913 0.015 . . . . . . 6 LEU QD2 . 7350 1 64 . 1 1 6 6 LEU HD23 H 1 0.913 0.015 . . . . . . 6 LEU QD2 . 7350 1 65 . 1 1 6 6 LEU HG H 1 1.539 0.004 . . . . . . 6 LEU HG . 7350 1 66 . 1 1 6 6 LEU C C 13 175.765 0.100 . . . . . . 6 LEU C . 7350 1 67 . 1 1 6 6 LEU CA C 13 55.343 0.100 . . . . . . 6 LEU CA . 7350 1 68 . 1 1 6 6 LEU CB C 13 38.864 0.100 . . . . . . 6 LEU CB . 7350 1 69 . 1 1 6 6 LEU CD1 C 13 22.294 0.100 . . . . . . 6 LEU CD1 . 7350 1 70 . 1 1 6 6 LEU CD2 C 13 21.282 0.100 . . . . . . 6 LEU CD2 . 7350 1 71 . 1 1 6 6 LEU CG C 13 24.603 0.100 . . . . . . 6 LEU CG . 7350 1 72 . 1 1 6 6 LEU N N 15 122.147 0.100 . . . . . . 6 LEU N . 7350 1 73 . 1 1 7 7 LYS H H 1 8.379 0.010 . . . . . . 7 LYS H . 7350 1 74 . 1 1 7 7 LYS HA H 1 3.820 0.006 . . . . . . 7 LYS HA . 7350 1 75 . 1 1 7 7 LYS HB2 H 1 1.881 0.010 . . . . . . 7 LYS HB1 . 7350 1 76 . 1 1 7 7 LYS HB3 H 1 1.845 0.010 . . . . . . 7 LYS HB2 . 7350 1 77 . 1 1 7 7 LYS HD2 H 1 1.661 0.010 . . . . . . 7 LYS HD1 . 7350 1 78 . 1 1 7 7 LYS HD3 H 1 1.661 0.010 . . . . . . 7 LYS HD2 . 7350 1 79 . 1 1 7 7 LYS HE2 H 1 2.941 0.010 . . . . . . 7 LYS HE1 . 7350 1 80 . 1 1 7 7 LYS HE3 H 1 2.941 0.010 . . . . . . 7 LYS HE2 . 7350 1 81 . 1 1 7 7 LYS HG2 H 1 1.502 0.015 . . . . . . 7 LYS HG1 . 7350 1 82 . 1 1 7 7 LYS HG3 H 1 1.323 0.015 . . . . . . 7 LYS HG2 . 7350 1 83 . 1 1 7 7 LYS C C 13 175.996 0.100 . . . . . . 7 LYS C . 7350 1 84 . 1 1 7 7 LYS CA C 13 57.440 0.100 . . . . . . 7 LYS CA . 7350 1 85 . 1 1 7 7 LYS CB C 13 29.296 0.100 . . . . . . 7 LYS CB . 7350 1 86 . 1 1 7 7 LYS CD C 13 26.661 0.100 . . . . . . 7 LYS CD . 7350 1 87 . 1 1 7 7 LYS CE C 13 39.391 0.100 . . . . . . 7 LYS CE . 7350 1 88 . 1 1 7 7 LYS CG C 13 22.727 0.100 . . . . . . 7 LYS CG . 7350 1 89 . 1 1 7 7 LYS N N 15 118.349 0.100 . . . . . . 7 LYS N . 7350 1 90 . 1 1 8 8 ASN H H 1 7.797 0.010 . . . . . . 8 ASN H . 7350 1 91 . 1 1 8 8 ASN HA H 1 4.442 0.015 . . . . . . 8 ASN HA . 7350 1 92 . 1 1 8 8 ASN HB2 H 1 2.839 0.015 . . . . . . 8 ASN HB1 . 7350 1 93 . 1 1 8 8 ASN HB3 H 1 2.839 0.015 . . . . . . 8 ASN HB2 . 7350 1 94 . 1 1 8 8 ASN HD21 H 1 7.588 0.010 . . . . . . 8 ASN HD21 . 7350 1 95 . 1 1 8 8 ASN HD22 H 1 6.917 0.010 . . . . . . 8 ASN HD22 . 7350 1 96 . 1 1 8 8 ASN C C 13 174.791 0.100 . . . . . . 8 ASN C . 7350 1 97 . 1 1 8 8 ASN CA C 13 53.489 0.100 . . . . . . 8 ASN CA . 7350 1 98 . 1 1 8 8 ASN CB C 13 35.683 0.100 . . . . . . 8 ASN CB . 7350 1 99 . 1 1 8 8 ASN N N 15 117.612 0.100 . . . . . . 8 ASN N . 7350 1 100 . 1 1 8 8 ASN ND2 N 15 112.418 0.100 . . . . . . 8 ASN ND2 . 7350 1 101 . 1 1 9 9 LYS H H 1 8.028 0.010 . . . . . . 9 LYS H . 7350 1 102 . 1 1 9 9 LYS HA H 1 4.097 0.015 . . . . . . 9 LYS HA . 7350 1 103 . 1 1 9 9 LYS HB2 H 1 1.868 0.015 . . . . . . 9 LYS HB1 . 7350 1 104 . 1 1 9 9 LYS HB3 H 1 2.041 0.010 . . . . . . 9 LYS HB2 . 7350 1 105 . 1 1 9 9 LYS HD2 H 1 1.603 0.010 . . . . . . 9 LYS HD1 . 7350 1 106 . 1 1 9 9 LYS HD3 H 1 1.603 0.010 . . . . . . 9 LYS HD2 . 7350 1 107 . 1 1 9 9 LYS HE2 H 1 2.956 0.010 . . . . . . 9 LYS HE1 . 7350 1 108 . 1 1 9 9 LYS HE3 H 1 2.956 0.010 . . . . . . 9 LYS HE2 . 7350 1 109 . 1 1 9 9 LYS HG2 H 1 1.674 0.015 . . . . . . 9 LYS HG1 . 7350 1 110 . 1 1 9 9 LYS HG3 H 1 1.488 0.003 . . . . . . 9 LYS HG2 . 7350 1 111 . 1 1 9 9 LYS C C 13 177.275 0.100 . . . . . . 9 LYS C . 7350 1 112 . 1 1 9 9 LYS CA C 13 57.032 0.100 . . . . . . 9 LYS CA . 7350 1 113 . 1 1 9 9 LYS CB C 13 30.184 0.100 . . . . . . 9 LYS CB . 7350 1 114 . 1 1 9 9 LYS CD C 13 26.673 0.100 . . . . . . 9 LYS CD . 7350 1 115 . 1 1 9 9 LYS CE C 13 39.480 0.100 . . . . . . 9 LYS CE . 7350 1 116 . 1 1 9 9 LYS CG C 13 23.182 0.100 . . . . . . 9 LYS CG . 7350 1 117 . 1 1 9 9 LYS N N 15 120.506 0.100 . . . . . . 9 LYS N . 7350 1 118 . 1 1 10 10 ILE H H 1 8.526 0.010 . . . . . . 10 ILE H . 7350 1 119 . 1 1 10 10 ILE HA H 1 3.410 0.002 . . . . . . 10 ILE HA . 7350 1 120 . 1 1 10 10 ILE HB H 1 1.904 0.010 . . . . . . 10 ILE HB . 7350 1 121 . 1 1 10 10 ILE HD11 H 1 0.685 0.010 . . . . . . 10 ILE QD1 . 7350 1 122 . 1 1 10 10 ILE HD12 H 1 0.685 0.010 . . . . . . 10 ILE QD1 . 7350 1 123 . 1 1 10 10 ILE HD13 H 1 0.685 0.010 . . . . . . 10 ILE QD1 . 7350 1 124 . 1 1 10 10 ILE HG12 H 1 0.755 0.010 . . . . . . 10 ILE HG11 . 7350 1 125 . 1 1 10 10 ILE HG13 H 1 1.767 0.010 . . . . . . 10 ILE HG12 . 7350 1 126 . 1 1 10 10 ILE HG21 H 1 0.797 0.015 . . . . . . 10 ILE QG2 . 7350 1 127 . 1 1 10 10 ILE HG22 H 1 0.797 0.015 . . . . . . 10 ILE QG2 . 7350 1 128 . 1 1 10 10 ILE HG23 H 1 0.797 0.015 . . . . . . 10 ILE QG2 . 7350 1 129 . 1 1 10 10 ILE C C 13 174.342 0.100 . . . . . . 10 ILE C . 7350 1 130 . 1 1 10 10 ILE CA C 13 63.589 0.100 . . . . . . 10 ILE CA . 7350 1 131 . 1 1 10 10 ILE CB C 13 35.272 0.100 . . . . . . 10 ILE CB . 7350 1 132 . 1 1 10 10 ILE CD1 C 13 11.359 0.100 . . . . . . 10 ILE CD1 . 7350 1 133 . 1 1 10 10 ILE CG1 C 13 29.255 0.100 . . . . . . 10 ILE CG1 . 7350 1 134 . 1 1 10 10 ILE CG2 C 13 14.224 0.100 . . . . . . 10 ILE CG2 . 7350 1 135 . 1 1 10 10 ILE N N 15 121.427 0.100 . . . . . . 10 ILE N . 7350 1 136 . 1 1 11 11 GLU H H 1 8.086 0.010 . . . . . . 11 GLU H . 7350 1 137 . 1 1 11 11 GLU HA H 1 3.977 0.004 . . . . . . 11 GLU HA . 7350 1 138 . 1 1 11 11 GLU HB2 H 1 2.054 0.015 . . . . . . 11 GLU HB1 . 7350 1 139 . 1 1 11 11 GLU HB3 H 1 2.130 0.015 . . . . . . 11 GLU HB2 . 7350 1 140 . 1 1 11 11 GLU HG2 H 1 2.354 0.015 . . . . . . 11 GLU HG1 . 7350 1 141 . 1 1 11 11 GLU HG3 H 1 2.247 0.015 . . . . . . 11 GLU HG2 . 7350 1 142 . 1 1 11 11 GLU C C 13 176.315 0.100 . . . . . . 11 GLU C . 7350 1 143 . 1 1 11 11 GLU CA C 13 56.658 0.100 . . . . . . 11 GLU CA . 7350 1 144 . 1 1 11 11 GLU CB C 13 26.316 0.100 . . . . . . 11 GLU CB . 7350 1 145 . 1 1 11 11 GLU CG C 13 32.867 0.100 . . . . . . 11 GLU CG . 7350 1 146 . 1 1 11 11 GLU N N 15 119.831 0.100 . . . . . . 11 GLU N . 7350 1 147 . 1 1 12 12 ASN H H 1 8.005 0.010 . . . . . . 12 ASN H . 7350 1 148 . 1 1 12 12 ASN HA H 1 4.439 0.015 . . . . . . 12 ASN HA . 7350 1 149 . 1 1 12 12 ASN HB2 H 1 2.829 0.001 . . . . . . 12 ASN HB1 . 7350 1 150 . 1 1 12 12 ASN HB3 H 1 2.829 0.001 . . . . . . 12 ASN HB2 . 7350 1 151 . 1 1 12 12 ASN HD21 H 1 7.559 0.010 . . . . . . 12 ASN HD21 . 7350 1 152 . 1 1 12 12 ASN HD22 H 1 6.818 0.010 . . . . . . 12 ASN HD22 . 7350 1 153 . 1 1 12 12 ASN C C 13 174.898 0.100 . . . . . . 12 ASN C . 7350 1 154 . 1 1 12 12 ASN CA C 13 53.673 0.100 . . . . . . 12 ASN CA . 7350 1 155 . 1 1 12 12 ASN CB C 13 35.615 0.100 . . . . . . 12 ASN CB . 7350 1 156 . 1 1 12 12 ASN N N 15 116.912 0.100 . . . . . . 12 ASN N . 7350 1 157 . 1 1 12 12 ASN ND2 N 15 112.560 0.100 . . . . . . 12 ASN ND2 . 7350 1 158 . 1 1 13 13 LYS H H 1 8.128 0.010 . . . . . . 13 LYS H . 7350 1 159 . 1 1 13 13 LYS HA H 1 4.123 0.004 . . . . . . 13 LYS HA . 7350 1 160 . 1 1 13 13 LYS HB2 H 1 1.785 0.009 . . . . . . 13 LYS HB1 . 7350 1 161 . 1 1 13 13 LYS HB3 H 1 1.909 0.022 . . . . . . 13 LYS HB2 . 7350 1 162 . 1 1 13 13 LYS HD2 H 1 1.764 0.010 . . . . . . 13 LYS HD1 . 7350 1 163 . 1 1 13 13 LYS HD3 H 1 1.963 0.008 . . . . . . 13 LYS HD2 . 7350 1 164 . 1 1 13 13 LYS HE2 H 1 3.002 0.003 . . . . . . 13 LYS HE1 . 7350 1 165 . 1 1 13 13 LYS HE3 H 1 2.711 0.003 . . . . . . 13 LYS HE2 . 7350 1 166 . 1 1 13 13 LYS HG2 H 1 1.409 0.011 . . . . . . 13 LYS HG1 . 7350 1 167 . 1 1 13 13 LYS HG3 H 1 1.530 0.032 . . . . . . 13 LYS HG2 . 7350 1 168 . 1 1 13 13 LYS C C 13 175.823 0.100 . . . . . . 13 LYS C . 7350 1 169 . 1 1 13 13 LYS CA C 13 54.224 0.100 . . . . . . 13 LYS CA . 7350 1 170 . 1 1 13 13 LYS CB C 13 27.493 0.100 . . . . . . 13 LYS CB . 7350 1 171 . 1 1 13 13 LYS CD C 13 23.602 0.100 . . . . . . 13 LYS CD . 7350 1 172 . 1 1 13 13 LYS CE C 13 38.765 0.100 . . . . . . 13 LYS CE . 7350 1 173 . 1 1 13 13 LYS CG C 13 21.872 0.100 . . . . . . 13 LYS CG . 7350 1 174 . 1 1 13 13 LYS N N 15 120.599 0.100 . . . . . . 13 LYS N . 7350 1 175 . 1 1 14 14 LYS H H 1 8.724 0.010 . . . . . . 14 LYS H . 7350 1 176 . 1 1 14 14 LYS HA H 1 3.707 0.010 . . . . . . 14 LYS HA . 7350 1 177 . 1 1 14 14 LYS HB2 H 1 2.002 0.010 . . . . . . 14 LYS HB1 . 7350 1 178 . 1 1 14 14 LYS HB3 H 1 1.860 0.010 . . . . . . 14 LYS HB2 . 7350 1 179 . 1 1 14 14 LYS HD2 H 1 1.706 0.010 . . . . . . 14 LYS HD1 . 7350 1 180 . 1 1 14 14 LYS HD3 H 1 1.528 0.015 . . . . . . 14 LYS HD2 . 7350 1 181 . 1 1 14 14 LYS HE2 H 1 2.791 0.008 . . . . . . 14 LYS HE1 . 7350 1 182 . 1 1 14 14 LYS HE3 H 1 2.704 0.004 . . . . . . 14 LYS HE2 . 7350 1 183 . 1 1 14 14 LYS HG2 H 1 1.122 0.010 . . . . . . 14 LYS HG1 . 7350 1 184 . 1 1 14 14 LYS HG3 H 1 1.534 0.015 . . . . . . 14 LYS HG2 . 7350 1 185 . 1 1 14 14 LYS C C 13 175.209 0.100 . . . . . . 14 LYS C . 7350 1 186 . 1 1 14 14 LYS CA C 13 57.717 0.100 . . . . . . 14 LYS CA . 7350 1 187 . 1 1 14 14 LYS CB C 13 29.301 0.100 . . . . . . 14 LYS CB . 7350 1 188 . 1 1 14 14 LYS CD C 13 26.806 0.100 . . . . . . 14 LYS CD . 7350 1 189 . 1 1 14 14 LYS CE C 13 38.604 0.100 . . . . . . 14 LYS CE . 7350 1 190 . 1 1 14 14 LYS CG C 13 21.995 0.100 . . . . . . 14 LYS CG . 7350 1 191 . 1 1 14 14 LYS N N 15 119.511 0.100 . . . . . . 14 LYS N . 7350 1 192 . 1 1 15 15 LYS H H 1 7.804 0.010 . . . . . . 15 LYS H . 7350 1 193 . 1 1 15 15 LYS HA H 1 3.881 0.015 . . . . . . 15 LYS HA . 7350 1 194 . 1 1 15 15 LYS HB2 H 1 2.009 0.010 . . . . . . 15 LYS HB1 . 7350 1 195 . 1 1 15 15 LYS HB3 H 1 1.925 0.010 . . . . . . 15 LYS HB2 . 7350 1 196 . 1 1 15 15 LYS HD2 H 1 1.697 0.010 . . . . . . 15 LYS HD1 . 7350 1 197 . 1 1 15 15 LYS HD3 H 1 1.697 0.010 . . . . . . 15 LYS HD2 . 7350 1 198 . 1 1 15 15 LYS HE2 H 1 2.958 0.010 . . . . . . 15 LYS HE1 . 7350 1 199 . 1 1 15 15 LYS HE3 H 1 2.958 0.010 . . . . . . 15 LYS HE2 . 7350 1 200 . 1 1 15 15 LYS HG2 H 1 1.689 0.015 . . . . . . 15 LYS HG1 . 7350 1 201 . 1 1 15 15 LYS HG3 H 1 1.386 0.015 . . . . . . 15 LYS HG2 . 7350 1 202 . 1 1 15 15 LYS C C 13 176.794 0.100 . . . . . . 15 LYS C . 7350 1 203 . 1 1 15 15 LYS CA C 13 57.640 0.100 . . . . . . 15 LYS CA . 7350 1 204 . 1 1 15 15 LYS CB C 13 29.434 0.100 . . . . . . 15 LYS CB . 7350 1 205 . 1 1 15 15 LYS CD C 13 26.768 0.100 . . . . . . 15 LYS CD . 7350 1 206 . 1 1 15 15 LYS CE C 13 39.504 0.100 . . . . . . 15 LYS CE . 7350 1 207 . 1 1 15 15 LYS CG C 13 23.114 0.100 . . . . . . 15 LYS CG . 7350 1 208 . 1 1 15 15 LYS N N 15 117.560 0.100 . . . . . . 15 LYS N . 7350 1 209 . 1 1 16 16 GLU H H 1 7.963 0.010 . . . . . . 16 GLU H . 7350 1 210 . 1 1 16 16 GLU HA H 1 3.993 0.015 . . . . . . 16 GLU HA . 7350 1 211 . 1 1 16 16 GLU HB2 H 1 1.872 0.010 . . . . . . 16 GLU HB1 . 7350 1 212 . 1 1 16 16 GLU HB3 H 1 2.372 0.015 . . . . . . 16 GLU HB2 . 7350 1 213 . 1 1 16 16 GLU HG2 H 1 2.232 0.010 . . . . . . 16 GLU HG1 . 7350 1 214 . 1 1 16 16 GLU HG3 H 1 2.663 0.010 . . . . . . 16 GLU HG2 . 7350 1 215 . 1 1 16 16 GLU C C 13 176.961 0.100 . . . . . . 16 GLU C . 7350 1 216 . 1 1 16 16 GLU CA C 13 56.539 0.100 . . . . . . 16 GLU CA . 7350 1 217 . 1 1 16 16 GLU CB C 13 27.543 0.100 . . . . . . 16 GLU CB . 7350 1 218 . 1 1 16 16 GLU CG C 13 33.711 0.100 . . . . . . 16 GLU CG . 7350 1 219 . 1 1 16 16 GLU N N 15 118.730 0.100 . . . . . . 16 GLU N . 7350 1 220 . 1 1 17 17 LEU H H 1 8.134 0.010 . . . . . . 17 LEU H . 7350 1 221 . 1 1 17 17 LEU HA H 1 4.040 0.015 . . . . . . 17 LEU HA . 7350 1 222 . 1 1 17 17 LEU HB2 H 1 2.141 0.015 . . . . . . 17 LEU HB1 . 7350 1 223 . 1 1 17 17 LEU HB3 H 1 1.494 0.003 . . . . . . 17 LEU HB2 . 7350 1 224 . 1 1 17 17 LEU HD11 H 1 0.939 0.008 . . . . . . 17 LEU QD1 . 7350 1 225 . 1 1 17 17 LEU HD12 H 1 0.939 0.008 . . . . . . 17 LEU QD1 . 7350 1 226 . 1 1 17 17 LEU HD13 H 1 0.939 0.008 . . . . . . 17 LEU QD1 . 7350 1 227 . 1 1 17 17 LEU HD21 H 1 0.940 0.004 . . . . . . 17 LEU QD2 . 7350 1 228 . 1 1 17 17 LEU HD22 H 1 0.940 0.004 . . . . . . 17 LEU QD2 . 7350 1 229 . 1 1 17 17 LEU HD23 H 1 0.940 0.004 . . . . . . 17 LEU QD2 . 7350 1 230 . 1 1 17 17 LEU HG H 1 1.663 0.007 . . . . . . 17 LEU HG . 7350 1 231 . 1 1 17 17 LEU C C 13 175.161 0.100 . . . . . . 17 LEU C . 7350 1 232 . 1 1 17 17 LEU CA C 13 55.965 0.100 . . . . . . 17 LEU CA . 7350 1 233 . 1 1 17 17 LEU CB C 13 39.231 0.100 . . . . . . 17 LEU CB . 7350 1 234 . 1 1 17 17 LEU CD1 C 13 23.968 0.100 . . . . . . 17 LEU CD1 . 7350 1 235 . 1 1 17 17 LEU CD2 C 13 21.652 0.100 . . . . . . 17 LEU CD2 . 7350 1 236 . 1 1 17 17 LEU CG C 13 24.826 0.100 . . . . . . 17 LEU CG . 7350 1 237 . 1 1 17 17 LEU N N 15 120.495 0.100 . . . . . . 17 LEU N . 7350 1 238 . 1 1 18 18 ILE H H 1 8.417 0.010 . . . . . . 18 ILE H . 7350 1 239 . 1 1 18 18 ILE HA H 1 3.513 0.012 . . . . . . 18 ILE HA . 7350 1 240 . 1 1 18 18 ILE HB H 1 1.850 0.010 . . . . . . 18 ILE HB . 7350 1 241 . 1 1 18 18 ILE HD11 H 1 0.800 0.010 . . . . . . 18 ILE QD1 . 7350 1 242 . 1 1 18 18 ILE HD12 H 1 0.800 0.010 . . . . . . 18 ILE QD1 . 7350 1 243 . 1 1 18 18 ILE HD13 H 1 0.800 0.010 . . . . . . 18 ILE QD1 . 7350 1 244 . 1 1 18 18 ILE HG12 H 1 0.773 0.008 . . . . . . 18 ILE HG11 . 7350 1 245 . 1 1 18 18 ILE HG13 H 1 1.768 0.005 . . . . . . 18 ILE HG12 . 7350 1 246 . 1 1 18 18 ILE HG21 H 1 0.864 0.010 . . . . . . 18 ILE QG2 . 7350 1 247 . 1 1 18 18 ILE HG22 H 1 0.864 0.010 . . . . . . 18 ILE QG2 . 7350 1 248 . 1 1 18 18 ILE HG23 H 1 0.864 0.010 . . . . . . 18 ILE QG2 . 7350 1 249 . 1 1 18 18 ILE C C 13 174.425 0.100 . . . . . . 18 ILE C . 7350 1 250 . 1 1 18 18 ILE CA C 13 63.610 0.100 . . . . . . 18 ILE CA . 7350 1 251 . 1 1 18 18 ILE CB C 13 35.687 0.100 . . . . . . 18 ILE CB . 7350 1 252 . 1 1 18 18 ILE CD1 C 13 12.105 0.100 . . . . . . 18 ILE CD1 . 7350 1 253 . 1 1 18 18 ILE CG1 C 13 27.338 0.100 . . . . . . 18 ILE CG1 . 7350 1 254 . 1 1 18 18 ILE CG2 C 13 15.007 0.100 . . . . . . 18 ILE CG2 . 7350 1 255 . 1 1 18 18 ILE N N 15 119.102 0.100 . . . . . . 18 ILE N . 7350 1 256 . 1 1 19 19 GLN H H 1 7.937 0.010 . . . . . . 19 GLN H . 7350 1 257 . 1 1 19 19 GLN HA H 1 3.968 0.004 . . . . . . 19 GLN HA . 7350 1 258 . 1 1 19 19 GLN HB2 H 1 2.127 0.015 . . . . . . 19 GLN HB1 . 7350 1 259 . 1 1 19 19 GLN HB3 H 1 2.092 0.005 . . . . . . 19 GLN HB2 . 7350 1 260 . 1 1 19 19 GLN HE21 H 1 7.428 0.010 . . . . . . 19 GLN HE21 . 7350 1 261 . 1 1 19 19 GLN HE22 H 1 6.864 0.010 . . . . . . 19 GLN HE22 . 7350 1 262 . 1 1 19 19 GLN HG2 H 1 2.383 0.015 . . . . . . 19 GLN HG1 . 7350 1 263 . 1 1 19 19 GLN HG3 H 1 2.521 0.015 . . . . . . 19 GLN HG2 . 7350 1 264 . 1 1 19 19 GLN C C 13 176.169 0.100 . . . . . . 19 GLN C . 7350 1 265 . 1 1 19 19 GLN CA C 13 56.108 0.100 . . . . . . 19 GLN CA . 7350 1 266 . 1 1 19 19 GLN CB C 13 25.865 0.100 . . . . . . 19 GLN CB . 7350 1 267 . 1 1 19 19 GLN CG C 13 31.618 0.100 . . . . . . 19 GLN CG . 7350 1 268 . 1 1 19 19 GLN N N 15 115.970 0.100 . . . . . . 19 GLN N . 7350 1 269 . 1 1 19 19 GLN NE2 N 15 111.760 0.100 . . . . . . 19 GLN NE2 . 7350 1 270 . 1 1 20 20 LEU H H 1 7.581 0.010 . . . . . . 20 LEU H . 7350 1 271 . 1 1 20 20 LEU HA H 1 4.046 0.015 . . . . . . 20 LEU HA . 7350 1 272 . 1 1 20 20 LEU HB2 H 1 1.970 0.010 . . . . . . 20 LEU HB1 . 7350 1 273 . 1 1 20 20 LEU HB3 H 1 1.374 0.008 . . . . . . 20 LEU HB2 . 7350 1 274 . 1 1 20 20 LEU HD11 H 1 0.820 0.001 . . . . . . 20 LEU QD1 . 7350 1 275 . 1 1 20 20 LEU HD12 H 1 0.820 0.001 . . . . . . 20 LEU QD1 . 7350 1 276 . 1 1 20 20 LEU HD13 H 1 0.820 0.001 . . . . . . 20 LEU QD1 . 7350 1 277 . 1 1 20 20 LEU HD21 H 1 0.771 0.003 . . . . . . 20 LEU QD2 . 7350 1 278 . 1 1 20 20 LEU HD22 H 1 0.771 0.003 . . . . . . 20 LEU QD2 . 7350 1 279 . 1 1 20 20 LEU HD23 H 1 0.771 0.003 . . . . . . 20 LEU QD2 . 7350 1 280 . 1 1 20 20 LEU HG H 1 1.870 0.009 . . . . . . 20 LEU HG . 7350 1 281 . 1 1 20 20 LEU C C 13 175.923 0.100 . . . . . . 20 LEU C . 7350 1 282 . 1 1 20 20 LEU CA C 13 55.370 0.100 . . . . . . 20 LEU CA . 7350 1 283 . 1 1 20 20 LEU CB C 13 40.426 0.100 . . . . . . 20 LEU CB . 7350 1 284 . 1 1 20 20 LEU CD1 C 13 20.878 0.100 . . . . . . 20 LEU CD1 . 7350 1 285 . 1 1 20 20 LEU CD2 C 13 23.966 0.100 . . . . . . 20 LEU CD2 . 7350 1 286 . 1 1 20 20 LEU CG C 13 24.225 0.100 . . . . . . 20 LEU CG . 7350 1 287 . 1 1 20 20 LEU N N 15 118.758 0.100 . . . . . . 20 LEU N . 7350 1 288 . 1 1 21 21 VAL H H 1 8.029 0.010 . . . . . . 21 VAL H . 7350 1 289 . 1 1 21 21 VAL HA H 1 3.500 0.009 . . . . . . 21 VAL HA . 7350 1 290 . 1 1 21 21 VAL HB H 1 1.813 0.015 . . . . . . 21 VAL HB . 7350 1 291 . 1 1 21 21 VAL HG11 H 1 0.291 0.004 . . . . . . 21 VAL QG1 . 7350 1 292 . 1 1 21 21 VAL HG12 H 1 0.291 0.004 . . . . . . 21 VAL QG1 . 7350 1 293 . 1 1 21 21 VAL HG13 H 1 0.291 0.004 . . . . . . 21 VAL QG1 . 7350 1 294 . 1 1 21 21 VAL HG21 H 1 0.690 0.005 . . . . . . 21 VAL QG2 . 7350 1 295 . 1 1 21 21 VAL HG22 H 1 0.690 0.005 . . . . . . 21 VAL QG2 . 7350 1 296 . 1 1 21 21 VAL HG23 H 1 0.690 0.005 . . . . . . 21 VAL QG2 . 7350 1 297 . 1 1 21 21 VAL C C 13 175.827 0.100 . . . . . . 21 VAL C . 7350 1 298 . 1 1 21 21 VAL CA C 13 63.833 0.100 . . . . . . 21 VAL CA . 7350 1 299 . 1 1 21 21 VAL CB C 13 28.699 0.100 . . . . . . 21 VAL CB . 7350 1 300 . 1 1 21 21 VAL CG1 C 13 18.077 0.100 . . . . . . 21 VAL CG1 . 7350 1 301 . 1 1 21 21 VAL CG2 C 13 19.692 0.100 . . . . . . 21 VAL CG2 . 7350 1 302 . 1 1 21 21 VAL N N 15 118.486 0.100 . . . . . . 21 VAL N . 7350 1 303 . 1 1 22 22 ALA H H 1 8.542 0.010 . . . . . . 22 ALA H . 7350 1 304 . 1 1 22 22 ALA HA H 1 3.986 0.006 . . . . . . 22 ALA HA . 7350 1 305 . 1 1 22 22 ALA HB1 H 1 1.498 0.015 . . . . . . 22 ALA QB . 7350 1 306 . 1 1 22 22 ALA HB2 H 1 1.498 0.015 . . . . . . 22 ALA QB . 7350 1 307 . 1 1 22 22 ALA HB3 H 1 1.498 0.015 . . . . . . 22 ALA QB . 7350 1 308 . 1 1 22 22 ALA C C 13 177.995 0.100 . . . . . . 22 ALA C . 7350 1 309 . 1 1 22 22 ALA CA C 13 52.408 0.100 . . . . . . 22 ALA CA . 7350 1 310 . 1 1 22 22 ALA CB C 13 15.900 0.100 . . . . . . 22 ALA CB . 7350 1 311 . 1 1 22 22 ALA N N 15 120.633 0.100 . . . . . . 22 ALA N . 7350 1 312 . 1 1 23 23 ARG H H 1 7.789 0.010 . . . . . . 23 ARG H . 7350 1 313 . 1 1 23 23 ARG HA H 1 4.128 0.015 . . . . . . 23 ARG HA . 7350 1 314 . 1 1 23 23 ARG HB2 H 1 1.994 0.015 . . . . . . 23 ARG HB1 . 7350 1 315 . 1 1 23 23 ARG HB3 H 1 2.079 0.015 . . . . . . 23 ARG HB2 . 7350 1 316 . 1 1 23 23 ARG HD2 H 1 3.166 0.006 . . . . . . 23 ARG HD1 . 7350 1 317 . 1 1 23 23 ARG HD3 H 1 3.166 0.006 . . . . . . 23 ARG HD2 . 7350 1 318 . 1 1 23 23 ARG HG2 H 1 1.924 0.002 . . . . . . 23 ARG HG1 . 7350 1 319 . 1 1 23 23 ARG HG3 H 1 1.755 0.007 . . . . . . 23 ARG HG2 . 7350 1 320 . 1 1 23 23 ARG C C 13 174.475 0.100 . . . . . . 23 ARG C . 7350 1 321 . 1 1 23 23 ARG CA C 13 55.242 0.100 . . . . . . 23 ARG CA . 7350 1 322 . 1 1 23 23 ARG CB C 13 27.249 0.100 . . . . . . 23 ARG CB . 7350 1 323 . 1 1 23 23 ARG CD C 13 41.043 0.100 . . . . . . 23 ARG CD . 7350 1 324 . 1 1 23 23 ARG CG C 13 24.831 0.100 . . . . . . 23 ARG CG . 7350 1 325 . 1 1 23 23 ARG N N 15 117.910 0.100 . . . . . . 23 ARG N . 7350 1 326 . 1 1 24 24 HIS H H 1 7.948 0.010 . . . . . . 24 HIS H . 7350 1 327 . 1 1 24 24 HIS HA H 1 4.387 0.008 . . . . . . 24 HIS HA . 7350 1 328 . 1 1 24 24 HIS HB2 H 1 2.946 0.004 . . . . . . 24 HIS HB1 . 7350 1 329 . 1 1 24 24 HIS HB3 H 1 3.376 0.015 . . . . . . 24 HIS HB2 . 7350 1 330 . 1 1 24 24 HIS HD2 H 1 6.925 0.007 . . . . . . 24 HIS HD2 . 7350 1 331 . 1 1 24 24 HIS C C 13 172.538 0.100 . . . . . . 24 HIS C . 7350 1 332 . 1 1 24 24 HIS CA C 13 54.831 0.100 . . . . . . 24 HIS CA . 7350 1 333 . 1 1 24 24 HIS CB C 13 27.176 0.100 . . . . . . 24 HIS CB . 7350 1 334 . 1 1 24 24 HIS CD2 C 13 119.161 0.100 . . . . . . 24 HIS CD2 . 7350 1 335 . 1 1 24 24 HIS N N 15 118.834 0.100 . . . . . . 24 HIS N . 7350 1 336 . 1 1 25 25 GLY H H 1 7.750 0.010 . . . . . . 25 GLY H . 7350 1 337 . 1 1 25 25 GLY HA2 H 1 4.194 0.004 . . . . . . 25 GLY HA1 . 7350 1 338 . 1 1 25 25 GLY HA3 H 1 3.666 0.003 . . . . . . 25 GLY HA2 . 7350 1 339 . 1 1 25 25 GLY C C 13 171.296 0.100 . . . . . . 25 GLY C . 7350 1 340 . 1 1 25 25 GLY CA C 13 43.048 0.100 . . . . . . 25 GLY CA . 7350 1 341 . 1 1 25 25 GLY N N 15 104.698 0.100 . . . . . . 25 GLY N . 7350 1 342 . 1 1 26 26 LEU H H 1 7.130 0.010 . . . . . . 26 LEU H . 7350 1 343 . 1 1 26 26 LEU HA H 1 4.383 0.001 . . . . . . 26 LEU HA . 7350 1 344 . 1 1 26 26 LEU HB2 H 1 1.437 0.015 . . . . . . 26 LEU HB1 . 7350 1 345 . 1 1 26 26 LEU HB3 H 1 1.614 0.001 . . . . . . 26 LEU HB2 . 7350 1 346 . 1 1 26 26 LEU HD11 H 1 0.871 0.010 . . . . . . 26 LEU QD1 . 7350 1 347 . 1 1 26 26 LEU HD12 H 1 0.871 0.010 . . . . . . 26 LEU QD1 . 7350 1 348 . 1 1 26 26 LEU HD13 H 1 0.871 0.010 . . . . . . 26 LEU QD1 . 7350 1 349 . 1 1 26 26 LEU HD21 H 1 0.794 0.001 . . . . . . 26 LEU QD2 . 7350 1 350 . 1 1 26 26 LEU HD22 H 1 0.794 0.001 . . . . . . 26 LEU QD2 . 7350 1 351 . 1 1 26 26 LEU HD23 H 1 0.794 0.001 . . . . . . 26 LEU QD2 . 7350 1 352 . 1 1 26 26 LEU HG H 1 1.771 0.002 . . . . . . 26 LEU HG . 7350 1 353 . 1 1 26 26 LEU C C 13 173.358 0.100 . . . . . . 26 LEU C . 7350 1 354 . 1 1 26 26 LEU CA C 13 52.546 0.100 . . . . . . 26 LEU CA . 7350 1 355 . 1 1 26 26 LEU CB C 13 41.273 0.100 . . . . . . 26 LEU CB . 7350 1 356 . 1 1 26 26 LEU CD1 C 13 22.283 0.100 . . . . . . 26 LEU CD1 . 7350 1 357 . 1 1 26 26 LEU CD2 C 13 21.968 0.100 . . . . . . 26 LEU CD2 . 7350 1 358 . 1 1 26 26 LEU CG C 13 25.220 0.100 . . . . . . 26 LEU CG . 7350 1 359 . 1 1 26 26 LEU N N 15 121.559 0.100 . . . . . . 26 LEU N . 7350 1 360 . 1 1 27 27 ASP H H 1 8.277 0.010 . . . . . . 27 ASP H . 7350 1 361 . 1 1 27 27 ASP HA H 1 4.566 0.008 . . . . . . 27 ASP HA . 7350 1 362 . 1 1 27 27 ASP HB2 H 1 2.901 0.001 . . . . . . 27 ASP HB1 . 7350 1 363 . 1 1 27 27 ASP HB3 H 1 2.818 0.015 . . . . . . 27 ASP HB2 . 7350 1 364 . 1 1 27 27 ASP C C 13 173.858 0.100 . . . . . . 27 ASP C . 7350 1 365 . 1 1 27 27 ASP CA C 13 51.007 0.100 . . . . . . 27 ASP CA . 7350 1 366 . 1 1 27 27 ASP CB C 13 39.077 0.100 . . . . . . 27 ASP CB . 7350 1 367 . 1 1 27 27 ASP N N 15 122.310 0.100 . . . . . . 27 ASP N . 7350 1 368 . 1 1 28 28 HIS H H 1 8.822 0.010 . . . . . . 28 HIS H . 7350 1 369 . 1 1 28 28 HIS HA H 1 4.162 0.003 . . . . . . 28 HIS HA . 7350 1 370 . 1 1 28 28 HIS HB2 H 1 3.308 0.015 . . . . . . 28 HIS HB1 . 7350 1 371 . 1 1 28 28 HIS HB3 H 1 3.184 0.015 . . . . . . 28 HIS HB2 . 7350 1 372 . 1 1 28 28 HIS C C 13 174.130 0.100 . . . . . . 28 HIS C . 7350 1 373 . 1 1 28 28 HIS CA C 13 57.469 0.100 . . . . . . 28 HIS CA . 7350 1 374 . 1 1 28 28 HIS CB C 13 26.847 0.100 . . . . . . 28 HIS CB . 7350 1 375 . 1 1 28 28 HIS N N 15 119.587 0.100 . . . . . . 28 HIS N . 7350 1 376 . 1 1 29 29 ASP H H 1 8.540 0.010 . . . . . . 29 ASP H . 7350 1 377 . 1 1 29 29 ASP HA H 1 4.292 0.007 . . . . . . 29 ASP HA . 7350 1 378 . 1 1 29 29 ASP HB2 H 1 2.670 0.015 . . . . . . 29 ASP HB1 . 7350 1 379 . 1 1 29 29 ASP HB3 H 1 2.720 0.015 . . . . . . 29 ASP HB2 . 7350 1 380 . 1 1 29 29 ASP C C 13 176.399 0.100 . . . . . . 29 ASP C . 7350 1 381 . 1 1 29 29 ASP CA C 13 54.711 0.100 . . . . . . 29 ASP CA . 7350 1 382 . 1 1 29 29 ASP CB C 13 37.220 0.100 . . . . . . 29 ASP CB . 7350 1 383 . 1 1 29 29 ASP N N 15 117.385 0.100 . . . . . . 29 ASP N . 7350 1 384 . 1 1 30 30 LYS H H 1 7.919 0.010 . . . . . . 30 LYS H . 7350 1 385 . 1 1 30 30 LYS HA H 1 4.252 0.008 . . . . . . 30 LYS HA . 7350 1 386 . 1 1 30 30 LYS HB2 H 1 2.147 0.015 . . . . . . 30 LYS HB1 . 7350 1 387 . 1 1 30 30 LYS HB3 H 1 1.981 0.015 . . . . . . 30 LYS HB2 . 7350 1 388 . 1 1 30 30 LYS HD2 H 1 1.862 0.010 . . . . . . 30 LYS HD1 . 7350 1 389 . 1 1 30 30 LYS HD3 H 1 1.774 0.015 . . . . . . 30 LYS HD2 . 7350 1 390 . 1 1 30 30 LYS HE2 H 1 3.051 0.015 . . . . . . 30 LYS HE1 . 7350 1 391 . 1 1 30 30 LYS HE3 H 1 3.051 0.015 . . . . . . 30 LYS HE2 . 7350 1 392 . 1 1 30 30 LYS HG2 H 1 1.657 0.003 . . . . . . 30 LYS HG1 . 7350 1 393 . 1 1 30 30 LYS HG3 H 1 1.850 0.008 . . . . . . 30 LYS HG2 . 7350 1 394 . 1 1 30 30 LYS C C 13 175.846 0.100 . . . . . . 30 LYS C . 7350 1 395 . 1 1 30 30 LYS CA C 13 56.226 0.100 . . . . . . 30 LYS CA . 7350 1 396 . 1 1 30 30 LYS CB C 13 30.424 0.100 . . . . . . 30 LYS CB . 7350 1 397 . 1 1 30 30 LYS CD C 13 26.591 0.100 . . . . . . 30 LYS CD . 7350 1 398 . 1 1 30 30 LYS CE C 13 39.624 0.100 . . . . . . 30 LYS CE . 7350 1 399 . 1 1 30 30 LYS CG C 13 23.446 0.100 . . . . . . 30 LYS CG . 7350 1 400 . 1 1 30 30 LYS N N 15 120.197 0.100 . . . . . . 30 LYS N . 7350 1 401 . 1 1 31 31 VAL H H 1 8.236 0.010 . . . . . . 31 VAL H . 7350 1 402 . 1 1 31 31 VAL HA H 1 3.352 0.007 . . . . . . 31 VAL HA . 7350 1 403 . 1 1 31 31 VAL HB H 1 2.158 0.010 . . . . . . 31 VAL HB . 7350 1 404 . 1 1 31 31 VAL HG11 H 1 0.927 0.014 . . . . . . 31 VAL QG1 . 7350 1 405 . 1 1 31 31 VAL HG12 H 1 0.927 0.014 . . . . . . 31 VAL QG1 . 7350 1 406 . 1 1 31 31 VAL HG13 H 1 0.927 0.014 . . . . . . 31 VAL QG1 . 7350 1 407 . 1 1 31 31 VAL HG21 H 1 0.838 0.010 . . . . . . 31 VAL QG2 . 7350 1 408 . 1 1 31 31 VAL HG22 H 1 0.838 0.010 . . . . . . 31 VAL QG2 . 7350 1 409 . 1 1 31 31 VAL HG23 H 1 0.838 0.010 . . . . . . 31 VAL QG2 . 7350 1 410 . 1 1 31 31 VAL C C 13 176.125 0.100 . . . . . . 31 VAL C . 7350 1 411 . 1 1 31 31 VAL CA C 13 64.757 0.100 . . . . . . 31 VAL CA . 7350 1 412 . 1 1 31 31 VAL CB C 13 28.581 0.100 . . . . . . 31 VAL CB . 7350 1 413 . 1 1 31 31 VAL CG1 C 13 21.779 0.100 . . . . . . 31 VAL CG1 . 7350 1 414 . 1 1 31 31 VAL CG2 C 13 18.849 0.100 . . . . . . 31 VAL CG2 . 7350 1 415 . 1 1 31 31 VAL N N 15 121.020 0.100 . . . . . . 31 VAL N . 7350 1 416 . 1 1 32 32 LEU H H 1 7.717 0.010 . . . . . . 32 LEU H . 7350 1 417 . 1 1 32 32 LEU HA H 1 3.940 0.006 . . . . . . 32 LEU HA . 7350 1 418 . 1 1 32 32 LEU HB2 H 1 1.769 0.015 . . . . . . 32 LEU HB1 . 7350 1 419 . 1 1 32 32 LEU HB3 H 1 1.512 0.010 . . . . . . 32 LEU HB2 . 7350 1 420 . 1 1 32 32 LEU HD11 H 1 0.812 0.015 . . . . . . 32 LEU QD1 . 7350 1 421 . 1 1 32 32 LEU HD12 H 1 0.812 0.015 . . . . . . 32 LEU QD1 . 7350 1 422 . 1 1 32 32 LEU HD13 H 1 0.812 0.015 . . . . . . 32 LEU QD1 . 7350 1 423 . 1 1 32 32 LEU HD21 H 1 0.788 0.009 . . . . . . 32 LEU QD2 . 7350 1 424 . 1 1 32 32 LEU HD22 H 1 0.788 0.009 . . . . . . 32 LEU QD2 . 7350 1 425 . 1 1 32 32 LEU HD23 H 1 0.788 0.009 . . . . . . 32 LEU QD2 . 7350 1 426 . 1 1 32 32 LEU HG H 1 1.491 0.015 . . . . . . 32 LEU HG . 7350 1 427 . 1 1 32 32 LEU C C 13 176.979 0.100 . . . . . . 32 LEU C . 7350 1 428 . 1 1 32 32 LEU CA C 13 55.433 0.100 . . . . . . 32 LEU CA . 7350 1 429 . 1 1 32 32 LEU CB C 13 38.631 0.100 . . . . . . 32 LEU CB . 7350 1 430 . 1 1 32 32 LEU CD1 C 13 22.183 0.100 . . . . . . 32 LEU CD1 . 7350 1 431 . 1 1 32 32 LEU CD2 C 13 20.340 0.100 . . . . . . 32 LEU CD2 . 7350 1 432 . 1 1 32 32 LEU CG C 13 24.068 0.100 . . . . . . 32 LEU CG . 7350 1 433 . 1 1 32 32 LEU N N 15 120.652 0.100 . . . . . . 32 LEU N . 7350 1 434 . 1 1 33 33 LEU H H 1 7.522 0.010 . . . . . . 33 LEU H . 7350 1 435 . 1 1 33 33 LEU HA H 1 4.040 0.018 . . . . . . 33 LEU HA . 7350 1 436 . 1 1 33 33 LEU HB2 H 1 1.875 0.014 . . . . . . 33 LEU HB1 . 7350 1 437 . 1 1 33 33 LEU HB3 H 1 1.971 0.007 . . . . . . 33 LEU HB2 . 7350 1 438 . 1 1 33 33 LEU HD11 H 1 1.026 0.010 . . . . . . 33 LEU QD1 . 7350 1 439 . 1 1 33 33 LEU HD12 H 1 1.026 0.010 . . . . . . 33 LEU QD1 . 7350 1 440 . 1 1 33 33 LEU HD13 H 1 1.026 0.010 . . . . . . 33 LEU QD1 . 7350 1 441 . 1 1 33 33 LEU HD21 H 1 0.953 0.015 . . . . . . 33 LEU QD2 . 7350 1 442 . 1 1 33 33 LEU HD22 H 1 0.953 0.015 . . . . . . 33 LEU QD2 . 7350 1 443 . 1 1 33 33 LEU HD23 H 1 0.953 0.015 . . . . . . 33 LEU QD2 . 7350 1 444 . 1 1 33 33 LEU HG H 1 1.930 0.010 . . . . . . 33 LEU HG . 7350 1 445 . 1 1 33 33 LEU C C 13 175.416 0.100 . . . . . . 33 LEU C . 7350 1 446 . 1 1 33 33 LEU CA C 13 55.456 0.100 . . . . . . 33 LEU CA . 7350 1 447 . 1 1 33 33 LEU CB C 13 39.047 0.100 . . . . . . 33 LEU CB . 7350 1 448 . 1 1 33 33 LEU CD1 C 13 22.168 0.100 . . . . . . 33 LEU CD1 . 7350 1 449 . 1 1 33 33 LEU CD2 C 13 20.871 0.100 . . . . . . 33 LEU CD2 . 7350 1 450 . 1 1 33 33 LEU CG C 13 24.036 0.100 . . . . . . 33 LEU CG . 7350 1 451 . 1 1 33 33 LEU N N 15 120.697 0.100 . . . . . . 33 LEU N . 7350 1 452 . 1 1 34 34 PHE H H 1 8.263 0.010 . . . . . . 34 PHE H . 7350 1 453 . 1 1 34 34 PHE HA H 1 3.434 0.009 . . . . . . 34 PHE HA . 7350 1 454 . 1 1 34 34 PHE HB2 H 1 2.613 0.015 . . . . . . 34 PHE HB1 . 7350 1 455 . 1 1 34 34 PHE HB3 H 1 1.847 0.015 . . . . . . 34 PHE HB2 . 7350 1 456 . 1 1 34 34 PHE HD1 H 1 6.700 0.004 . . . . . . 34 PHE QD . 7350 1 457 . 1 1 34 34 PHE HD2 H 1 6.700 0.004 . . . . . . 34 PHE QD . 7350 1 458 . 1 1 34 34 PHE HE1 H 1 6.883 0.006 . . . . . . 34 PHE QE . 7350 1 459 . 1 1 34 34 PHE HE2 H 1 6.883 0.006 . . . . . . 34 PHE QE . 7350 1 460 . 1 1 34 34 PHE HZ H 1 6.786 0.025 . . . . . . 34 PHE HZ . 7350 1 461 . 1 1 34 34 PHE C C 13 173.650 0.100 . . . . . . 34 PHE C . 7350 1 462 . 1 1 34 34 PHE CA C 13 58.060 0.100 . . . . . . 34 PHE CA . 7350 1 463 . 1 1 34 34 PHE CB C 13 35.396 0.100 . . . . . . 34 PHE CB . 7350 1 464 . 1 1 34 34 PHE CD1 C 13 128.814 0.100 . . . . . . 34 PHE CD1 . 7350 1 465 . 1 1 34 34 PHE CD2 C 13 128.814 0.100 . . . . . . 34 PHE CD2 . 7350 1 466 . 1 1 34 34 PHE CE1 C 13 127.331 0.100 . . . . . . 34 PHE CE1 . 7350 1 467 . 1 1 34 34 PHE CE2 C 13 127.331 0.100 . . . . . . 34 PHE CE2 . 7350 1 468 . 1 1 34 34 PHE CZ C 13 125.216 0.100 . . . . . . 34 PHE CZ . 7350 1 469 . 1 1 34 34 PHE N N 15 120.263 0.100 . . . . . . 34 PHE N . 7350 1 470 . 1 1 35 35 SER H H 1 8.306 0.011 . . . . . . 35 SER H . 7350 1 471 . 1 1 35 35 SER HA H 1 3.565 0.003 . . . . . . 35 SER HA . 7350 1 472 . 1 1 35 35 SER HB2 H 1 3.942 0.010 . . . . . . 35 SER HB1 . 7350 1 473 . 1 1 35 35 SER HB3 H 1 3.942 0.011 . . . . . . 35 SER HB2 . 7350 1 474 . 1 1 35 35 SER C C 13 173.163 0.100 . . . . . . 35 SER C . 7350 1 475 . 1 1 35 35 SER CA C 13 59.216 0.100 . . . . . . 35 SER CA . 7350 1 476 . 1 1 35 35 SER CB C 13 60.245 0.100 . . . . . . 35 SER CB . 7350 1 477 . 1 1 35 35 SER N N 15 112.662 0.100 . . . . . . 35 SER N . 7350 1 478 . 1 1 36 36 ARG H H 1 7.835 0.010 . . . . . . 36 ARG H . 7350 1 479 . 1 1 36 36 ARG HA H 1 4.054 0.015 . . . . . . 36 ARG HA . 7350 1 480 . 1 1 36 36 ARG HB2 H 1 1.973 0.004 . . . . . . 36 ARG HB1 . 7350 1 481 . 1 1 36 36 ARG HB3 H 1 1.973 0.004 . . . . . . 36 ARG HB2 . 7350 1 482 . 1 1 36 36 ARG HD2 H 1 3.162 0.005 . . . . . . 36 ARG HD1 . 7350 1 483 . 1 1 36 36 ARG HD3 H 1 3.162 0.005 . . . . . . 36 ARG HD2 . 7350 1 484 . 1 1 36 36 ARG HE H 1 7.143 0.010 . . . . . . 36 ARG HE . 7350 1 485 . 1 1 36 36 ARG HG2 H 1 1.860 0.010 . . . . . . 36 ARG HG1 . 7350 1 486 . 1 1 36 36 ARG HG3 H 1 1.570 0.009 . . . . . . 36 ARG HG2 . 7350 1 487 . 1 1 36 36 ARG C C 13 176.699 0.100 . . . . . . 36 ARG C . 7350 1 488 . 1 1 36 36 ARG CA C 13 56.465 0.100 . . . . . . 36 ARG CA . 7350 1 489 . 1 1 36 36 ARG CB C 13 27.471 0.100 . . . . . . 36 ARG CB . 7350 1 490 . 1 1 36 36 ARG CD C 13 40.950 0.100 . . . . . . 36 ARG CD . 7350 1 491 . 1 1 36 36 ARG CG C 13 24.406 0.100 . . . . . . 36 ARG CG . 7350 1 492 . 1 1 36 36 ARG N N 15 121.162 0.100 . . . . . . 36 ARG N . 7350 1 493 . 1 1 36 36 ARG NE N 15 112.524 0.100 . . . . . . 36 ARG NE . 7350 1 494 . 1 1 37 37 ASP H H 1 8.409 0.010 . . . . . . 37 ASP H . 7350 1 495 . 1 1 37 37 ASP HA H 1 4.406 0.004 . . . . . . 37 ASP HA . 7350 1 496 . 1 1 37 37 ASP HB2 H 1 2.566 0.006 . . . . . . 37 ASP HB1 . 7350 1 497 . 1 1 37 37 ASP HB3 H 1 2.717 0.015 . . . . . . 37 ASP HB2 . 7350 1 498 . 1 1 37 37 ASP C C 13 176.800 0.100 . . . . . . 37 ASP C . 7350 1 499 . 1 1 37 37 ASP CA C 13 54.726 0.100 . . . . . . 37 ASP CA . 7350 1 500 . 1 1 37 37 ASP CB C 13 37.597 0.100 . . . . . . 37 ASP CB . 7350 1 501 . 1 1 37 37 ASP N N 15 122.222 0.100 . . . . . . 37 ASP N . 7350 1 502 . 1 1 38 38 LEU H H 1 8.714 0.010 . . . . . . 38 LEU H . 7350 1 503 . 1 1 38 38 LEU HA H 1 3.795 0.008 . . . . . . 38 LEU HA . 7350 1 504 . 1 1 38 38 LEU HB2 H 1 0.775 0.010 . . . . . . 38 LEU HB1 . 7350 1 505 . 1 1 38 38 LEU HB3 H 1 1.536 0.015 . . . . . . 38 LEU HB2 . 7350 1 506 . 1 1 38 38 LEU HD11 H 1 0.626 0.015 . . . . . . 38 LEU QD1 . 7350 1 507 . 1 1 38 38 LEU HD12 H 1 0.626 0.015 . . . . . . 38 LEU QD1 . 7350 1 508 . 1 1 38 38 LEU HD13 H 1 0.626 0.015 . . . . . . 38 LEU QD1 . 7350 1 509 . 1 1 38 38 LEU HD21 H 1 0.669 0.015 . . . . . . 38 LEU QD2 . 7350 1 510 . 1 1 38 38 LEU HD22 H 1 0.669 0.015 . . . . . . 38 LEU QD2 . 7350 1 511 . 1 1 38 38 LEU HD23 H 1 0.669 0.015 . . . . . . 38 LEU QD2 . 7350 1 512 . 1 1 38 38 LEU HG H 1 1.333 0.010 . . . . . . 38 LEU HG . 7350 1 513 . 1 1 38 38 LEU C C 13 175.239 0.100 . . . . . . 38 LEU C . 7350 1 514 . 1 1 38 38 LEU CA C 13 55.026 0.100 . . . . . . 38 LEU CA . 7350 1 515 . 1 1 38 38 LEU CB C 13 38.413 0.100 . . . . . . 38 LEU CB . 7350 1 516 . 1 1 38 38 LEU CD1 C 13 20.928 0.100 . . . . . . 38 LEU CD1 . 7350 1 517 . 1 1 38 38 LEU CD2 C 13 24.231 0.100 . . . . . . 38 LEU CD2 . 7350 1 518 . 1 1 38 38 LEU CG C 13 24.183 0.100 . . . . . . 38 LEU CG . 7350 1 519 . 1 1 38 38 LEU N N 15 124.500 0.100 . . . . . . 38 LEU N . 7350 1 520 . 1 1 39 39 ASP H H 1 7.931 0.010 . . . . . . 39 ASP H . 7350 1 521 . 1 1 39 39 ASP HA H 1 4.190 0.006 . . . . . . 39 ASP HA . 7350 1 522 . 1 1 39 39 ASP HB2 H 1 2.831 0.010 . . . . . . 39 ASP HB1 . 7350 1 523 . 1 1 39 39 ASP HB3 H 1 2.574 0.010 . . . . . . 39 ASP HB2 . 7350 1 524 . 1 1 39 39 ASP C C 13 176.016 0.100 . . . . . . 39 ASP C . 7350 1 525 . 1 1 39 39 ASP CA C 13 55.136 0.100 . . . . . . 39 ASP CA . 7350 1 526 . 1 1 39 39 ASP CB C 13 38.043 0.100 . . . . . . 39 ASP CB . 7350 1 527 . 1 1 39 39 ASP N N 15 119.422 0.100 . . . . . . 39 ASP N . 7350 1 528 . 1 1 40 40 LYS H H 1 7.845 0.010 . . . . . . 40 LYS H . 7350 1 529 . 1 1 40 40 LYS HA H 1 3.954 0.015 . . . . . . 40 LYS HA . 7350 1 530 . 1 1 40 40 LYS HB2 H 1 1.925 0.010 . . . . . . 40 LYS HB1 . 7350 1 531 . 1 1 40 40 LYS HB3 H 1 1.899 0.010 . . . . . . 40 LYS HB2 . 7350 1 532 . 1 1 40 40 LYS HD2 H 1 1.711 0.010 . . . . . . 40 LYS HD1 . 7350 1 533 . 1 1 40 40 LYS HD3 H 1 1.711 0.010 . . . . . . 40 LYS HD2 . 7350 1 534 . 1 1 40 40 LYS HE2 H 1 2.953 0.010 . . . . . . 40 LYS HE1 . 7350 1 535 . 1 1 40 40 LYS HE3 H 1 2.953 0.010 . . . . . . 40 LYS HE2 . 7350 1 536 . 1 1 40 40 LYS HG2 H 1 1.654 0.010 . . . . . . 40 LYS HG1 . 7350 1 537 . 1 1 40 40 LYS HG3 H 1 1.457 0.010 . . . . . . 40 LYS HG2 . 7350 1 538 . 1 1 40 40 LYS C C 13 176.327 0.100 . . . . . . 40 LYS C . 7350 1 539 . 1 1 40 40 LYS CA C 13 57.018 0.100 . . . . . . 40 LYS CA . 7350 1 540 . 1 1 40 40 LYS CB C 13 30.020 0.100 . . . . . . 40 LYS CB . 7350 1 541 . 1 1 40 40 LYS CD C 13 26.867 0.100 . . . . . . 40 LYS CD . 7350 1 542 . 1 1 40 40 LYS CE C 13 39.395 0.100 . . . . . . 40 LYS CE . 7350 1 543 . 1 1 40 40 LYS CG C 13 22.665 0.100 . . . . . . 40 LYS CG . 7350 1 544 . 1 1 40 40 LYS N N 15 118.255 0.100 . . . . . . 40 LYS N . 7350 1 545 . 1 1 41 41 LEU H H 1 7.890 0.010 . . . . . . 41 LEU H . 7350 1 546 . 1 1 41 41 LEU HA H 1 4.318 0.006 . . . . . . 41 LEU HA . 7350 1 547 . 1 1 41 41 LEU HB2 H 1 2.060 0.010 . . . . . . 41 LEU HB1 . 7350 1 548 . 1 1 41 41 LEU HB3 H 1 1.769 0.010 . . . . . . 41 LEU HB2 . 7350 1 549 . 1 1 41 41 LEU HD11 H 1 0.726 0.010 . . . . . . 41 LEU QD1 . 7350 1 550 . 1 1 41 41 LEU HD12 H 1 0.726 0.010 . . . . . . 41 LEU QD1 . 7350 1 551 . 1 1 41 41 LEU HD13 H 1 0.726 0.010 . . . . . . 41 LEU QD1 . 7350 1 552 . 1 1 41 41 LEU HD21 H 1 1.233 0.015 . . . . . . 41 LEU QD2 . 7350 1 553 . 1 1 41 41 LEU HD22 H 1 1.233 0.015 . . . . . . 41 LEU QD2 . 7350 1 554 . 1 1 41 41 LEU HD23 H 1 1.233 0.015 . . . . . . 41 LEU QD2 . 7350 1 555 . 1 1 41 41 LEU HG H 1 1.839 0.010 . . . . . . 41 LEU HG . 7350 1 556 . 1 1 41 41 LEU C C 13 175.717 0.100 . . . . . . 41 LEU C . 7350 1 557 . 1 1 41 41 LEU CA C 13 55.570 0.100 . . . . . . 41 LEU CA . 7350 1 558 . 1 1 41 41 LEU CB C 13 39.544 0.100 . . . . . . 41 LEU CB . 7350 1 559 . 1 1 41 41 LEU CD1 C 13 23.255 0.100 . . . . . . 41 LEU CD1 . 7350 1 560 . 1 1 41 41 LEU CD2 C 13 22.547 0.100 . . . . . . 41 LEU CD2 . 7350 1 561 . 1 1 41 41 LEU CG C 13 24.903 0.100 . . . . . . 41 LEU CG . 7350 1 562 . 1 1 41 41 LEU N N 15 121.537 0.100 . . . . . . 41 LEU N . 7350 1 563 . 1 1 42 42 ILE H H 1 8.361 0.010 . . . . . . 42 ILE H . 7350 1 564 . 1 1 42 42 ILE HA H 1 3.576 0.002 . . . . . . 42 ILE HA . 7350 1 565 . 1 1 42 42 ILE HB H 1 1.929 0.015 . . . . . . 42 ILE HB . 7350 1 566 . 1 1 42 42 ILE HD11 H 1 0.831 0.003 . . . . . . 42 ILE QD1 . 7350 1 567 . 1 1 42 42 ILE HD12 H 1 0.831 0.003 . . . . . . 42 ILE QD1 . 7350 1 568 . 1 1 42 42 ILE HD13 H 1 0.831 0.003 . . . . . . 42 ILE QD1 . 7350 1 569 . 1 1 42 42 ILE HG12 H 1 1.069 0.010 . . . . . . 42 ILE HG11 . 7350 1 570 . 1 1 42 42 ILE HG13 H 1 1.907 0.010 . . . . . . 42 ILE HG12 . 7350 1 571 . 1 1 42 42 ILE HG21 H 1 0.786 0.015 . . . . . . 42 ILE QG2 . 7350 1 572 . 1 1 42 42 ILE HG22 H 1 0.786 0.015 . . . . . . 42 ILE QG2 . 7350 1 573 . 1 1 42 42 ILE HG23 H 1 0.786 0.015 . . . . . . 42 ILE QG2 . 7350 1 574 . 1 1 42 42 ILE C C 13 175.549 0.100 . . . . . . 42 ILE C . 7350 1 575 . 1 1 42 42 ILE CA C 13 63.399 0.100 . . . . . . 42 ILE CA . 7350 1 576 . 1 1 42 42 ILE CB C 13 35.192 0.100 . . . . . . 42 ILE CB . 7350 1 577 . 1 1 42 42 ILE CD1 C 13 11.497 0.100 . . . . . . 42 ILE CD1 . 7350 1 578 . 1 1 42 42 ILE CG1 C 13 27.616 0.100 . . . . . . 42 ILE CG1 . 7350 1 579 . 1 1 42 42 ILE CG2 C 13 15.241 0.100 . . . . . . 42 ILE CG2 . 7350 1 580 . 1 1 42 42 ILE N N 15 117.746 0.100 . . . . . . 42 ILE N . 7350 1 581 . 1 1 43 43 ASN H H 1 8.336 0.010 . . . . . . 43 ASN H . 7350 1 582 . 1 1 43 43 ASN HA H 1 4.267 0.007 . . . . . . 43 ASN HA . 7350 1 583 . 1 1 43 43 ASN HB2 H 1 2.822 0.010 . . . . . . 43 ASN HB1 . 7350 1 584 . 1 1 43 43 ASN HB3 H 1 2.722 0.010 . . . . . . 43 ASN HB2 . 7350 1 585 . 1 1 43 43 ASN HD21 H 1 7.413 0.010 . . . . . . 43 ASN HD21 . 7350 1 586 . 1 1 43 43 ASN HD22 H 1 6.813 0.010 . . . . . . 43 ASN HD22 . 7350 1 587 . 1 1 43 43 ASN C C 13 174.822 0.100 . . . . . . 43 ASN C . 7350 1 588 . 1 1 43 43 ASN CA C 13 53.620 0.100 . . . . . . 43 ASN CA . 7350 1 589 . 1 1 43 43 ASN CB C 13 35.375 0.100 . . . . . . 43 ASN CB . 7350 1 590 . 1 1 43 43 ASN N N 15 117.030 0.100 . . . . . . 43 ASN N . 7350 1 591 . 1 1 43 43 ASN ND2 N 15 112.151 0.100 . . . . . . 43 ASN ND2 . 7350 1 592 . 1 1 44 44 LYS H H 1 7.912 0.011 . . . . . . 44 LYS H . 7350 1 593 . 1 1 44 44 LYS HA H 1 3.937 0.003 . . . . . . 44 LYS HA . 7350 1 594 . 1 1 44 44 LYS HB2 H 1 2.018 0.010 . . . . . . 44 LYS HB1 . 7350 1 595 . 1 1 44 44 LYS HB3 H 1 1.924 0.010 . . . . . . 44 LYS HB2 . 7350 1 596 . 1 1 44 44 LYS HD2 H 1 1.580 0.010 . . . . . . 44 LYS HD1 . 7350 1 597 . 1 1 44 44 LYS HD3 H 1 1.523 0.010 . . . . . . 44 LYS HD2 . 7350 1 598 . 1 1 44 44 LYS HE2 H 1 2.709 0.008 . . . . . . 44 LYS HE1 . 7350 1 599 . 1 1 44 44 LYS HE3 H 1 2.709 0.008 . . . . . . 44 LYS HE2 . 7350 1 600 . 1 1 44 44 LYS HG2 H 1 0.757 0.015 . . . . . . 44 LYS HG1 . 7350 1 601 . 1 1 44 44 LYS HG3 H 1 1.226 0.010 . . . . . . 44 LYS HG2 . 7350 1 602 . 1 1 44 44 LYS C C 13 175.649 0.100 . . . . . . 44 LYS C . 7350 1 603 . 1 1 44 44 LYS CA C 13 56.487 0.100 . . . . . . 44 LYS CA . 7350 1 604 . 1 1 44 44 LYS CB C 13 29.495 0.100 . . . . . . 44 LYS CB . 7350 1 605 . 1 1 44 44 LYS CD C 13 26.944 0.100 . . . . . . 44 LYS CD . 7350 1 606 . 1 1 44 44 LYS CE C 13 39.414 0.100 . . . . . . 44 LYS CE . 7350 1 607 . 1 1 44 44 LYS CG C 13 21.869 0.100 . . . . . . 44 LYS CG . 7350 1 608 . 1 1 44 44 LYS N N 15 119.779 0.100 . . . . . . 44 LYS N . 7350 1 609 . 1 1 45 45 PHE H H 1 7.473 0.010 . . . . . . 45 PHE H . 7350 1 610 . 1 1 45 45 PHE HA H 1 4.219 0.008 . . . . . . 45 PHE HA . 7350 1 611 . 1 1 45 45 PHE HB2 H 1 2.844 0.015 . . . . . . 45 PHE HB1 . 7350 1 612 . 1 1 45 45 PHE HB3 H 1 2.518 0.015 . . . . . . 45 PHE HB2 . 7350 1 613 . 1 1 45 45 PHE HD1 H 1 7.511 0.008 . . . . . . 45 PHE QD . 7350 1 614 . 1 1 45 45 PHE HD2 H 1 7.511 0.008 . . . . . . 45 PHE QD . 7350 1 615 . 1 1 45 45 PHE HE1 H 1 7.281 0.001 . . . . . . 45 PHE QE . 7350 1 616 . 1 1 45 45 PHE HE2 H 1 7.281 0.001 . . . . . . 45 PHE QE . 7350 1 617 . 1 1 45 45 PHE HZ H 1 7.537 0.015 . . . . . . 45 PHE HZ . 7350 1 618 . 1 1 45 45 PHE C C 13 173.523 0.100 . . . . . . 45 PHE C . 7350 1 619 . 1 1 45 45 PHE CA C 13 58.213 0.100 . . . . . . 45 PHE CA . 7350 1 620 . 1 1 45 45 PHE CB C 13 37.021 0.100 . . . . . . 45 PHE CB . 7350 1 621 . 1 1 45 45 PHE CD1 C 13 129.226 0.100 . . . . . . 45 PHE CD1 . 7350 1 622 . 1 1 45 45 PHE CD2 C 13 129.226 0.100 . . . . . . 45 PHE CD2 . 7350 1 623 . 1 1 45 45 PHE CE1 C 13 127.353 0.100 . . . . . . 45 PHE CE1 . 7350 1 624 . 1 1 45 45 PHE CE2 C 13 127.353 0.100 . . . . . . 45 PHE CE2 . 7350 1 625 . 1 1 45 45 PHE CZ C 13 126.806 0.100 . . . . . . 45 PHE CZ . 7350 1 626 . 1 1 45 45 PHE N N 15 115.208 0.100 . . . . . . 45 PHE N . 7350 1 627 . 1 1 46 46 MET H H 1 8.092 0.010 . . . . . . 46 MET H . 7350 1 628 . 1 1 46 46 MET HA H 1 4.332 0.002 . . . . . . 46 MET HA . 7350 1 629 . 1 1 46 46 MET HB2 H 1 1.889 0.010 . . . . . . 46 MET HB1 . 7350 1 630 . 1 1 46 46 MET HB3 H 1 1.889 0.010 . . . . . . 46 MET HB2 . 7350 1 631 . 1 1 46 46 MET HE1 H 1 1.571 0.008 . . . . . . 46 MET QE . 7350 1 632 . 1 1 46 46 MET HE2 H 1 1.571 0.008 . . . . . . 46 MET QE . 7350 1 633 . 1 1 46 46 MET HE3 H 1 1.571 0.008 . . . . . . 46 MET QE . 7350 1 634 . 1 1 46 46 MET HG2 H 1 2.445 0.010 . . . . . . 46 MET HG1 . 7350 1 635 . 1 1 46 46 MET HG3 H 1 2.167 0.009 . . . . . . 46 MET HG2 . 7350 1 636 . 1 1 46 46 MET C C 13 173.398 0.100 . . . . . . 46 MET C . 7350 1 637 . 1 1 46 46 MET CA C 13 53.247 0.100 . . . . . . 46 MET CA . 7350 1 638 . 1 1 46 46 MET CB C 13 30.220 0.100 . . . . . . 46 MET CB . 7350 1 639 . 1 1 46 46 MET CE C 13 13.920 0.100 . . . . . . 46 MET CE . 7350 1 640 . 1 1 46 46 MET CG C 13 29.793 0.100 . . . . . . 46 MET CG . 7350 1 641 . 1 1 46 46 MET N N 15 116.651 0.100 . . . . . . 46 MET N . 7350 1 642 . 1 1 47 47 ASN H H 1 7.780 0.010 . . . . . . 47 ASN H . 7350 1 643 . 1 1 47 47 ASN HA H 1 4.708 0.010 . . . . . . 47 ASN HA . 7350 1 644 . 1 1 47 47 ASN HB2 H 1 2.693 0.002 . . . . . . 47 ASN HB1 . 7350 1 645 . 1 1 47 47 ASN HB3 H 1 2.866 0.015 . . . . . . 47 ASN HB2 . 7350 1 646 . 1 1 47 47 ASN HD21 H 1 7.515 0.010 . . . . . . 47 ASN HD21 . 7350 1 647 . 1 1 47 47 ASN HD22 H 1 6.785 0.010 . . . . . . 47 ASN HD22 . 7350 1 648 . 1 1 47 47 ASN C C 13 172.370 0.100 . . . . . . 47 ASN C . 7350 1 649 . 1 1 47 47 ASN CA C 13 50.699 0.100 . . . . . . 47 ASN CA . 7350 1 650 . 1 1 47 47 ASN CB C 13 35.877 0.100 . . . . . . 47 ASN CB . 7350 1 651 . 1 1 47 47 ASN N N 15 117.874 0.100 . . . . . . 47 ASN N . 7350 1 652 . 1 1 47 47 ASN ND2 N 15 112.529 0.100 . . . . . . 47 ASN ND2 . 7350 1 653 . 1 1 48 48 VAL H H 1 7.813 0.010 . . . . . . 48 VAL H . 7350 1 654 . 1 1 48 48 VAL HA H 1 4.025 0.002 . . . . . . 48 VAL HA . 7350 1 655 . 1 1 48 48 VAL HB H 1 2.057 0.010 . . . . . . 48 VAL HB . 7350 1 656 . 1 1 48 48 VAL HG11 H 1 0.882 0.010 . . . . . . 48 VAL QG1 . 7350 1 657 . 1 1 48 48 VAL HG12 H 1 0.882 0.010 . . . . . . 48 VAL QG1 . 7350 1 658 . 1 1 48 48 VAL HG13 H 1 0.882 0.010 . . . . . . 48 VAL QG1 . 7350 1 659 . 1 1 48 48 VAL HG21 H 1 0.885 0.010 . . . . . . 48 VAL QG2 . 7350 1 660 . 1 1 48 48 VAL HG22 H 1 0.885 0.010 . . . . . . 48 VAL QG2 . 7350 1 661 . 1 1 48 48 VAL HG23 H 1 0.885 0.010 . . . . . . 48 VAL QG2 . 7350 1 662 . 1 1 48 48 VAL C C 13 173.532 0.100 . . . . . . 48 VAL C . 7350 1 663 . 1 1 48 48 VAL CA C 13 59.912 0.100 . . . . . . 48 VAL CA . 7350 1 664 . 1 1 48 48 VAL CB C 13 29.855 0.100 . . . . . . 48 VAL CB . 7350 1 665 . 1 1 48 48 VAL CG1 C 13 18.652 0.100 . . . . . . 48 VAL CG1 . 7350 1 666 . 1 1 48 48 VAL CG2 C 13 18.151 0.100 . . . . . . 48 VAL CG2 . 7350 1 667 . 1 1 48 48 VAL N N 15 119.708 0.100 . . . . . . 48 VAL N . 7350 1 668 . 1 1 49 49 LYS H H 1 8.292 0.010 . . . . . . 49 LYS H . 7350 1 669 . 1 1 49 49 LYS HA H 1 4.276 0.002 . . . . . . 49 LYS HA . 7350 1 670 . 1 1 49 49 LYS HB2 H 1 1.722 0.010 . . . . . . 49 LYS HB1 . 7350 1 671 . 1 1 49 49 LYS HB3 H 1 1.797 0.010 . . . . . . 49 LYS HB2 . 7350 1 672 . 1 1 49 49 LYS HD2 H 1 1.631 0.010 . . . . . . 49 LYS HD1 . 7350 1 673 . 1 1 49 49 LYS HD3 H 1 1.631 0.010 . . . . . . 49 LYS HD2 . 7350 1 674 . 1 1 49 49 LYS HE2 H 1 2.954 0.010 . . . . . . 49 LYS HE1 . 7350 1 675 . 1 1 49 49 LYS HE3 H 1 2.954 0.010 . . . . . . 49 LYS HE2 . 7350 1 676 . 1 1 49 49 LYS HG2 H 1 1.411 0.015 . . . . . . 49 LYS HG1 . 7350 1 677 . 1 1 49 49 LYS HG3 H 1 1.375 0.010 . . . . . . 49 LYS HG2 . 7350 1 678 . 1 1 49 49 LYS C C 13 173.558 0.100 . . . . . . 49 LYS C . 7350 1 679 . 1 1 49 49 LYS CA C 13 53.631 0.100 . . . . . . 49 LYS CA . 7350 1 680 . 1 1 49 49 LYS CB C 13 30.358 0.100 . . . . . . 49 LYS CB . 7350 1 681 . 1 1 49 49 LYS CD C 13 26.381 0.100 . . . . . . 49 LYS CD . 7350 1 682 . 1 1 49 49 LYS CE C 13 39.442 0.100 . . . . . . 49 LYS CE . 7350 1 683 . 1 1 49 49 LYS CG C 13 22.017 0.100 . . . . . . 49 LYS CG . 7350 1 684 . 1 1 49 49 LYS N N 15 124.657 0.100 . . . . . . 49 LYS N . 7350 1 685 . 1 1 50 50 ASP H H 1 8.189 0.010 . . . . . . 50 ASP H . 7350 1 686 . 1 1 50 50 ASP HA H 1 4.524 0.015 . . . . . . 50 ASP HA . 7350 1 687 . 1 1 50 50 ASP HB2 H 1 2.562 0.004 . . . . . . 50 ASP HB1 . 7350 1 688 . 1 1 50 50 ASP HB3 H 1 2.641 0.001 . . . . . . 50 ASP HB2 . 7350 1 689 . 1 1 50 50 ASP C C 13 173.459 0.100 . . . . . . 50 ASP C . 7350 1 690 . 1 1 50 50 ASP CA C 13 51.871 0.100 . . . . . . 50 ASP CA . 7350 1 691 . 1 1 50 50 ASP CB C 13 38.662 0.100 . . . . . . 50 ASP CB . 7350 1 692 . 1 1 50 50 ASP N N 15 121.415 0.100 . . . . . . 50 ASP N . 7350 1 693 . 1 1 51 51 LYS H H 1 8.183 0.010 . . . . . . 51 LYS H . 7350 1 694 . 1 1 51 51 LYS HA H 1 4.233 0.005 . . . . . . 51 LYS HA . 7350 1 695 . 1 1 51 51 LYS HB2 H 1 1.698 0.010 . . . . . . 51 LYS HB1 . 7350 1 696 . 1 1 51 51 LYS HB3 H 1 1.756 0.015 . . . . . . 51 LYS HB2 . 7350 1 697 . 1 1 51 51 LYS HD2 H 1 1.636 0.010 . . . . . . 51 LYS HD1 . 7350 1 698 . 1 1 51 51 LYS HD3 H 1 1.636 0.010 . . . . . . 51 LYS HD2 . 7350 1 699 . 1 1 51 51 LYS HE2 H 1 2.952 0.010 . . . . . . 51 LYS HE1 . 7350 1 700 . 1 1 51 51 LYS HE3 H 1 2.952 0.010 . . . . . . 51 LYS HE2 . 7350 1 701 . 1 1 51 51 LYS HG2 H 1 1.329 0.010 . . . . . . 51 LYS HG1 . 7350 1 702 . 1 1 51 51 LYS HG3 H 1 1.367 0.010 . . . . . . 51 LYS HG2 . 7350 1 703 . 1 1 51 51 LYS C C 13 173.829 0.100 . . . . . . 51 LYS C . 7350 1 704 . 1 1 51 51 LYS CA C 13 53.701 0.100 . . . . . . 51 LYS CA . 7350 1 705 . 1 1 51 51 LYS CB C 13 30.361 0.100 . . . . . . 51 LYS CB . 7350 1 706 . 1 1 51 51 LYS CD C 13 26.424 0.100 . . . . . . 51 LYS CD . 7350 1 707 . 1 1 51 51 LYS CE C 13 39.438 0.100 . . . . . . 51 LYS CE . 7350 1 708 . 1 1 51 51 LYS CG C 13 22.043 0.100 . . . . . . 51 LYS CG . 7350 1 709 . 1 1 51 51 LYS N N 15 121.377 0.100 . . . . . . 51 LYS N . 7350 1 710 . 1 1 52 52 VAL H H 1 8.016 0.010 . . . . . . 52 VAL H . 7350 1 711 . 1 1 52 52 VAL HA H 1 3.960 0.004 . . . . . . 52 VAL HA . 7350 1 712 . 1 1 52 52 VAL HB H 1 1.967 0.010 . . . . . . 52 VAL HB . 7350 1 713 . 1 1 52 52 VAL HG11 H 1 0.849 0.015 . . . . . . 52 VAL QG1 . 7350 1 714 . 1 1 52 52 VAL HG12 H 1 0.849 0.015 . . . . . . 52 VAL QG1 . 7350 1 715 . 1 1 52 52 VAL HG13 H 1 0.849 0.015 . . . . . . 52 VAL QG1 . 7350 1 716 . 1 1 52 52 VAL HG21 H 1 0.794 0.015 . . . . . . 52 VAL QG2 . 7350 1 717 . 1 1 52 52 VAL HG22 H 1 0.794 0.015 . . . . . . 52 VAL QG2 . 7350 1 718 . 1 1 52 52 VAL HG23 H 1 0.794 0.015 . . . . . . 52 VAL QG2 . 7350 1 719 . 1 1 52 52 VAL C C 13 173.358 0.100 . . . . . . 52 VAL C . 7350 1 720 . 1 1 52 52 VAL CA C 13 59.907 0.100 . . . . . . 52 VAL CA . 7350 1 721 . 1 1 52 52 VAL CB C 13 29.929 0.100 . . . . . . 52 VAL CB . 7350 1 722 . 1 1 52 52 VAL CG1 C 13 18.107 0.100 . . . . . . 52 VAL CG1 . 7350 1 723 . 1 1 52 52 VAL CG2 C 13 18.362 0.100 . . . . . . 52 VAL CG2 . 7350 1 724 . 1 1 52 52 VAL N N 15 120.641 0.100 . . . . . . 52 VAL N . 7350 1 725 . 1 1 53 53 HIS H H 1 8.411 0.010 . . . . . . 53 HIS H . 7350 1 726 . 1 1 53 53 HIS HA H 1 4.618 0.015 . . . . . . 53 HIS HA . 7350 1 727 . 1 1 53 53 HIS HB2 H 1 3.143 0.010 . . . . . . 53 HIS HB1 . 7350 1 728 . 1 1 53 53 HIS HB3 H 1 3.056 0.010 . . . . . . 53 HIS HB2 . 7350 1 729 . 1 1 53 53 HIS C C 13 172.089 0.100 . . . . . . 53 HIS C . 7350 1 730 . 1 1 53 53 HIS CA C 13 53.096 0.100 . . . . . . 53 HIS CA . 7350 1 731 . 1 1 53 53 HIS CB C 13 27.271 0.100 . . . . . . 53 HIS CB . 7350 1 732 . 1 1 53 53 HIS N N 15 123.109 0.100 . . . . . . 53 HIS N . 7350 1 733 . 1 1 54 54 LYS H H 1 8.280 0.010 . . . . . . 54 LYS H . 7350 1 734 . 1 1 54 54 LYS HA H 1 4.223 0.015 . . . . . . 54 LYS HA . 7350 1 735 . 1 1 54 54 LYS HB2 H 1 1.752 0.010 . . . . . . 54 LYS HB1 . 7350 1 736 . 1 1 54 54 LYS HB3 H 1 1.632 0.010 . . . . . . 54 LYS HB2 . 7350 1 737 . 1 1 54 54 LYS HD2 H 1 1.685 0.010 . . . . . . 54 LYS HD1 . 7350 1 738 . 1 1 54 54 LYS HD3 H 1 1.685 0.010 . . . . . . 54 LYS HD2 . 7350 1 739 . 1 1 54 54 LYS HE2 H 1 2.941 0.010 . . . . . . 54 LYS HE1 . 7350 1 740 . 1 1 54 54 LYS HE3 H 1 2.941 0.010 . . . . . . 54 LYS HE2 . 7350 1 741 . 1 1 54 54 LYS HG2 H 1 1.365 0.010 . . . . . . 54 LYS HG1 . 7350 1 742 . 1 1 54 54 LYS HG3 H 1 1.316 0.010 . . . . . . 54 LYS HG2 . 7350 1 743 . 1 1 54 54 LYS C C 13 173.477 0.100 . . . . . . 54 LYS C . 7350 1 744 . 1 1 54 54 LYS CA C 13 53.736 0.100 . . . . . . 54 LYS CA . 7350 1 745 . 1 1 54 54 LYS CB C 13 30.462 0.100 . . . . . . 54 LYS CB . 7350 1 746 . 1 1 54 54 LYS CD C 13 26.416 0.100 . . . . . . 54 LYS CD . 7350 1 747 . 1 1 54 54 LYS CE C 13 39.441 0.100 . . . . . . 54 LYS CE . 7350 1 748 . 1 1 54 54 LYS CG C 13 22.045 0.100 . . . . . . 54 LYS CG . 7350 1 749 . 1 1 54 54 LYS N N 15 123.277 0.100 . . . . . . 54 LYS N . 7350 1 stop_ save_