data_4581 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4581 _Entry.Title ; Site-site Communication in the EF-hand Ca2+ Binding Protein Calbindin D9k ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2000-02-02 _Entry.Accession_date 2000-02-02 _Entry.Last_release_date 2000-12-18 _Entry.Original_release_date 2000-12-18 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 L. Maler . . . 4581 2 J. Blankenship . . . 4581 3 M. Rance . . . 4581 4 W. Chazin . J. . 4581 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4581 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 480 4581 '15N chemical shifts' 70 4581 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 . . 2000-12-18 2000-02-02 original author . 4581 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4581 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 20165185 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title 'Site-site Communication in the EF-hand Ca2+ Binding Protein Calbindin D9k' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Nat. Struct. Biol.' _Citation.Journal_name_full 'Nature Structural Biology' _Citation.Journal_volume 7 _Citation.Journal_issue . _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 245 _Citation.Page_last 250 _Citation.Year 2000 _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 L. Maler . . . 4581 1 2 J. Blankenship . . . 4581 1 3 M. Rance . . . 4581 1 4 W. Chazin . J. . 4581 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID EF-hand 4581 1 'Calcium-binding protein' 4581 1 NMR 4581 1 'signal transduction' 4581 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4581 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 7549869 _Citation.Full_citation ; Wimberly, B.; Thulin, E. and Chazin W.J. Protein Science (1995) 4 1045-1055 ; _Citation.Title 'Characterization of the N-terminal half-saturated state of calbindin D9k: NMR studies of the N56A mutant.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Sci.' _Citation.Journal_name_full 'Protein science : a publication of the Protein Society' _Citation.Journal_volume 4 _Citation.Journal_issue 6 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0961-8368 _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 1045 _Citation.Page_last 1055 _Citation.Year 1995 _Citation.Details ; Calbindin D9k is a small EF-hand protein that binds two calcium ions with positive cooperativity. The molecular basis of cooperativity for the binding pathway where the first ion binds in the N-terminal site (1) is investigated by NMR experiments on the half-saturated state of the N56A mutant, which exhibits sequential yet cooperative binding (Linse S, Chazin WJ, 1995, Protein Sci 4:1038-1044). Analysis of calcium-induced changes in chemical shifts, amide proton exchange rates, and NOEs indicates that ion binding to the N-terminal binding loop causes significant changes in conformation and/or dynamics throughout the protein. In particular, all three parameters indicate that the hydrophobic core undergoes a change in packing to a conformation very similar to the calcium-loaded state. These results are similar to those observed for the (Cd2+)1 state of the wild-type protein, a model for the complementary half-saturated state with an ion bound in the C-terminal site (II). Thus, with respect to cooperativity in either of the binding pathways, binding of the first ion drives the conformation and dynamics of the protein far toward the (Ca2+)2 state, thereby facilitating binding of the second ion. Comparison with the half-saturated state of the analogous E65Q mutant confirms that mutation of this critical bidentate calcium ligand at position 12 of the consensus EF-hand binding loop causes very significant structural perturbations. This result has important implications regarding numerous studies that have utilized mutation of this critical residue for site deactivation. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 B. Wimberly B. . . 4581 2 2 E. Thulin E. . . 4581 2 3 W.J. Chazin W. J. . 4581 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_N56A _Assembly.Sf_category assembly _Assembly.Sf_framecode system_N56A _Assembly.Entry_ID 4581 _Assembly.ID 1 _Assembly.Name 'CALBINDIN D9K' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'not present' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4581 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'CALBINDIN D9K' 1 $calbindin_N56A . . . native . . . . . 4581 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID . PDB 1D1OA . 'Chain A, Cooperativity In Ef-Hand Ca2+-Binding Proteins: Evidence Of Site-Site Communication From Binding-Induced Changes In Structure And Dynamics Of N56a Calbindin D9k' . . . . 4581 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'CALBINDIN D9K' system 4581 1 'calbindin N56A' abbreviation 4581 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_calbindin_N56A _Entity.Sf_category entity _Entity.Sf_framecode calbindin_N56A _Entity.Entry_ID 4581 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'CALBINDIN D9K' _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 ; KSPEELKGIFEKYAAKEGDP NQLSKEELKLLLQTEFPSLL KGMSTLDELFEELDKAGDGE VSFEEFQVLVKKISQ ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 75 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 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 15594 . calbindin_in_presence_of_Yb3+ . . . . . 100.00 75 98.67 98.67 6.04e-41 . . . . 4581 1 2 no BMRB 16340 . Calbindin_D9K . . . . . 100.00 76 97.33 97.33 1.21e-39 . . . . 4581 1 3 no BMRB 16758 . calbindin . . . . . 100.00 75 98.67 98.67 2.23e-40 . . . . 4581 1 4 no BMRB 247 . calbindin . . . . . 100.00 76 97.33 97.33 1.62e-39 . . . . 4581 1 5 no BMRB 325 . calbindin . . . . . 100.00 76 97.33 97.33 1.62e-39 . . . . 4581 1 6 no BMRB 326 . calbindin . . . . . 100.00 76 97.33 97.33 1.21e-39 . . . . 4581 1 7 no BMRB 327 . calbindin . . . . . 100.00 76 97.33 97.33 1.21e-39 . . . . 4581 1 8 no PDB 1B1G . "Solvated Refinement Of Ca-Loaded Calbindin D9k" . . . . . 100.00 75 97.33 97.33 1.68e-39 . . . . 4581 1 9 no PDB 1CDN . "Solution Structure Of (Cd2+)1-Calbindin D9k Reveals Details Of The Stepwise Structural Changes Along The Apo--> (Ca2+) Ii1--> (" . . . . . 100.00 76 97.33 97.33 1.21e-39 . . . . 4581 1 10 no PDB 1CLB . "Determination Of The Solution Structure Of Apo Calbindin D9k By Nmr Spectroscopy" . . . . . 100.00 76 97.33 97.33 1.21e-39 . . . . 4581 1 11 no PDB 1D1O . "Cooperativity In Ef-Hand Ca2+-Binding Proteins: Evidence Of Site-Site Communication From Binding-Induced Changes In Structure A" . . . . . 100.00 75 100.00 100.00 7.40e-42 . . . . 4581 1 12 no PDB 1HT9 . "Domain Swapping Ef-Hands" . . . . . 100.00 76 97.33 97.33 2.31e-40 . . . . 4581 1 13 no PDB 1IG5 . "Bovine Calbindin D9k Binding Mg2+" . . . . . 100.00 75 97.33 97.33 1.63e-39 . . . . 4581 1 14 no PDB 1IGV . "Bovine Calbindin D9k Binding Mn2+" . . . . . 100.00 75 97.33 97.33 1.63e-39 . . . . 4581 1 15 no PDB 1KCY . "Nmr Solution Structure Of Apo Calbindin D9k (F36g + P43m Mutant)" . . . . . 100.00 75 97.33 97.33 1.34e-39 . . . . 4581 1 16 no PDB 1KQV . "Family Of Nmr Solution Structures Of Ca Ln Calbindin D9k" . . . . . 100.00 79 98.67 98.67 3.74e-41 . . . . 4581 1 17 no PDB 1KSM . "Average Nmr Solution Structure Of Ca Ln Calbindin D9k" . . . . . 100.00 79 98.67 98.67 3.74e-41 . . . . 4581 1 18 no PDB 1N65 . "Family Of Nmr Solution Structures Of Ca Ce Calbindin D9k In Denaturating Conditions" . . . . . 100.00 75 98.67 98.67 6.04e-41 . . . . 4581 1 19 no PDB 2BCA . "High-Resolution Solution Structure Of Calcium-Loaded Calbindin D9k" . . . . . 100.00 76 97.33 97.33 1.21e-39 . . . . 4581 1 20 no PDB 2BCB . "High-Resolution Solution Structure Of Calcium-Loaded Calbindin D9k" . . . . . 100.00 75 97.33 97.33 1.68e-39 . . . . 4581 1 21 no PDB 2MAZ . "Backbone 1h, 13c, And 15n Chemical Shift Assignments For Bovine Apo Calbindin" . . . . . 100.00 75 98.67 98.67 6.04e-41 . . . . 4581 1 22 no PDB 3ICB . "The Refined Structure Of Vitamin D-Dependent Calcium- Binding Protein From Bovine Intestine. Molecular Details, Ion Binding, An" . . . . . 100.00 75 97.33 97.33 1.63e-39 . . . . 4581 1 23 no PDB 4ICB . "Proline Cis-trans Isomers In Calbindin D9k Observed By X-ray Crystallography" . . . . . 100.00 76 97.33 97.33 1.62e-39 . . . . 4581 1 24 no GB AAA30420 . "calcium-binding protein [Bos taurus]" . . . . . 100.00 79 97.33 97.33 1.11e-39 . . . . 4581 1 25 no GB AAA72542 . "intestinal calcium binding protein (ICaBP), minor A form [synthetic construct]" . . . . . 100.00 76 97.33 97.33 1.62e-39 . . . . 4581 1 26 no GB AAI18481 . "S100 calcium binding protein G [Bos taurus]" . . . . . 100.00 79 97.33 97.33 1.11e-39 . . . . 4581 1 27 no PRF 0707237A:PDB=3ICB . "protein,Ca binding" . . . . . 100.00 75 97.33 97.33 1.63e-39 . . . . 4581 1 28 no REF NP_776682 . "protein S100-G [Bos taurus]" . . . . . 100.00 79 97.33 97.33 1.11e-39 . . . . 4581 1 29 no REF XP_004021986 . "PREDICTED: protein S100-G [Ovis aries]" . . . . . 100.00 79 97.33 97.33 1.11e-39 . . . . 4581 1 30 no REF XP_005701114 . "PREDICTED: protein S100-G [Capra hircus]" . . . . . 100.00 79 97.33 97.33 1.11e-39 . . . . 4581 1 31 no REF XP_005888771 . "PREDICTED: protein S100-G [Bos mutus]" . . . . . 100.00 79 97.33 97.33 1.11e-39 . . . . 4581 1 32 no REF XP_005982038 . "PREDICTED: protein S100-G [Pantholops hodgsonii]" . . . . . 100.00 79 97.33 97.33 1.11e-39 . . . . 4581 1 33 no SP P02633 . "RecName: Full=Protein S100-G; AltName: Full=Calbindin-D9k; AltName: Full=S100 calcium-binding protein G; AltName: Full=Vitamin " . . . . . 100.00 79 97.33 97.33 1.11e-39 . . . . 4581 1 34 no TPG DAA12577 . "TPA: protein S100-G [Bos taurus]" . . . . . 100.00 79 97.33 97.33 1.11e-39 . . . . 4581 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'CALBINDIN D9K' common 4581 1 N56A variant 4581 1 'calbindin N56A' abbreviation 4581 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 . LYS . 4581 1 2 . SER . 4581 1 3 . PRO . 4581 1 4 . GLU . 4581 1 5 . GLU . 4581 1 6 . LEU . 4581 1 7 . LYS . 4581 1 8 . GLY . 4581 1 9 . ILE . 4581 1 10 . PHE . 4581 1 11 . GLU . 4581 1 12 . LYS . 4581 1 13 . TYR . 4581 1 14 . ALA . 4581 1 15 . ALA . 4581 1 16 . LYS . 4581 1 17 . GLU . 4581 1 18 . GLY . 4581 1 19 . ASP . 4581 1 20 . PRO . 4581 1 21 . ASN . 4581 1 22 . GLN . 4581 1 23 . LEU . 4581 1 24 . SER . 4581 1 25 . LYS . 4581 1 26 . GLU . 4581 1 27 . GLU . 4581 1 28 . LEU . 4581 1 29 . LYS . 4581 1 30 . LEU . 4581 1 31 . LEU . 4581 1 32 . LEU . 4581 1 33 . GLN . 4581 1 34 . THR . 4581 1 35 . GLU . 4581 1 36 . PHE . 4581 1 37 . PRO . 4581 1 38 . SER . 4581 1 39 . LEU . 4581 1 40 . LEU . 4581 1 41 . LYS . 4581 1 42 . GLY . 4581 1 43 . MET . 4581 1 44 . SER . 4581 1 45 . THR . 4581 1 46 . LEU . 4581 1 47 . ASP . 4581 1 48 . GLU . 4581 1 49 . LEU . 4581 1 50 . PHE . 4581 1 51 . GLU . 4581 1 52 . GLU . 4581 1 53 . LEU . 4581 1 54 . ASP . 4581 1 55 . LYS . 4581 1 56 . ALA . 4581 1 57 . GLY . 4581 1 58 . ASP . 4581 1 59 . GLY . 4581 1 60 . GLU . 4581 1 61 . VAL . 4581 1 62 . SER . 4581 1 63 . PHE . 4581 1 64 . GLU . 4581 1 65 . GLU . 4581 1 66 . PHE . 4581 1 67 . GLN . 4581 1 68 . VAL . 4581 1 69 . LEU . 4581 1 70 . VAL . 4581 1 71 . LYS . 4581 1 72 . LYS . 4581 1 73 . ILE . 4581 1 74 . SER . 4581 1 75 . GLN . 4581 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 . LYS 1 1 4581 1 . SER 2 2 4581 1 . PRO 3 3 4581 1 . GLU 4 4 4581 1 . GLU 5 5 4581 1 . LEU 6 6 4581 1 . LYS 7 7 4581 1 . GLY 8 8 4581 1 . ILE 9 9 4581 1 . PHE 10 10 4581 1 . GLU 11 11 4581 1 . LYS 12 12 4581 1 . TYR 13 13 4581 1 . ALA 14 14 4581 1 . ALA 15 15 4581 1 . LYS 16 16 4581 1 . GLU 17 17 4581 1 . GLY 18 18 4581 1 . ASP 19 19 4581 1 . PRO 20 20 4581 1 . ASN 21 21 4581 1 . GLN 22 22 4581 1 . LEU 23 23 4581 1 . SER 24 24 4581 1 . LYS 25 25 4581 1 . GLU 26 26 4581 1 . GLU 27 27 4581 1 . LEU 28 28 4581 1 . LYS 29 29 4581 1 . LEU 30 30 4581 1 . LEU 31 31 4581 1 . LEU 32 32 4581 1 . GLN 33 33 4581 1 . THR 34 34 4581 1 . GLU 35 35 4581 1 . PHE 36 36 4581 1 . PRO 37 37 4581 1 . SER 38 38 4581 1 . LEU 39 39 4581 1 . LEU 40 40 4581 1 . LYS 41 41 4581 1 . GLY 42 42 4581 1 . MET 43 43 4581 1 . SER 44 44 4581 1 . THR 45 45 4581 1 . LEU 46 46 4581 1 . ASP 47 47 4581 1 . GLU 48 48 4581 1 . LEU 49 49 4581 1 . PHE 50 50 4581 1 . GLU 51 51 4581 1 . GLU 52 52 4581 1 . LEU 53 53 4581 1 . ASP 54 54 4581 1 . LYS 55 55 4581 1 . ALA 56 56 4581 1 . GLY 57 57 4581 1 . ASP 58 58 4581 1 . GLY 59 59 4581 1 . GLU 60 60 4581 1 . VAL 61 61 4581 1 . SER 62 62 4581 1 . PHE 63 63 4581 1 . GLU 64 64 4581 1 . GLU 65 65 4581 1 . PHE 66 66 4581 1 . GLN 67 67 4581 1 . VAL 68 68 4581 1 . LEU 69 69 4581 1 . VAL 70 70 4581 1 . LYS 71 71 4581 1 . LYS 72 72 4581 1 . ILE 73 73 4581 1 . SER 74 74 4581 1 . GLN 75 75 4581 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 4581 _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 $calbindin_N56A . 9913 organism . 'Bos taurus' Bovine . . Eukaryota Metazoa Bos taurus . . . . . . . . . . . . . . . . . . . . . 4581 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 4581 _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 $calbindin_N56A . 'recombinant technology' . bacteria . . . . . . . . . . . . . . . . . . . . . . . . . . . 4581 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4581 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'CALBINDIN D9K' . . . 1 $calbindin_N56A . . 4 . . mM . . . . 4581 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 4581 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'CALBINDIN D9K' [U-15N] . . 1 $calbindin_N56A . . 4 . . mM . . . . 4581 2 stop_ save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_cond_1 _Sample_condition_list.Entry_ID 4581 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 6.0 0.2 n/a 4581 1 temperature 300 1 K 4581 1 'ionic strength' 0 . mM 4581 1 pressure 1 . atm 4581 1 stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Software.Sf_category software _Software.Sf_framecode FELIX _Software.Entry_ID 4581 _Software.ID 1 _Software.Name FELIX _Software.Version 97.0 _Software.Details 'MSI, SAN DIEGO, CA' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'resonance assignments, bookkeeping' 4581 1 stop_ save_ save_DIANA _Software.Sf_category software _Software.Sf_framecode DIANA _Software.Entry_ID 4581 _Software.ID 2 _Software.Name DIANA _Software.Version 2.8 _Software.Details 'GUNTERT, BRAUN, BILLETER, WUTHRICH' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 4581 2 stop_ save_ save_AMBER _Software.Sf_category software _Software.Sf_framecode AMBER _Software.Entry_ID 4581 _Software.ID 3 _Software.Name AMBER _Software.Version 4.1 _Software.Details 'PEARLMAN, CASE, CALDWELL, ROSS, CHEATHAM, FERGUSON, SEIBEL, SINGH, WEINER, KOLLMAN' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 4581 3 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer1 _NMR_spectrometer.Entry_ID 4581 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer2 _NMR_spectrometer.Entry_ID 4581 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer3 _NMR_spectrometer.Entry_ID 4581 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model Inova _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4581 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer1 Bruker AMX . 500 . . . 4581 1 2 NMR_spectrometer2 Bruker DRX . 600 . . . 4581 1 3 NMR_spectrometer3 Varian Inova . 600 . . . 4581 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 4581 _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 '2D NOESY' . . . . . . . . . . . . . . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 4581 1 2 '3D 15N-SEPARATED NOESY' . . . . . . . . . . . . . . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 4581 1 3 HSQC-J . . . . . . . . . . . . . . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 4581 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 4581 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '2D NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 4581 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '3D 15N-SEPARATED NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 4581 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name HSQC-J _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 4581 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 4581 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 4581 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_set_1 _Assigned_chem_shift_list.Entry_ID 4581 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_1 . 4581 1 . . 2 $sample_2 . 4581 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 LYS H H 1 7.94 0.01 . 1 . . . . . . . . 4581 1 2 . 1 1 1 1 LYS HA H 1 4.64 0.01 . 1 . . . . . . . . 4581 1 3 . 1 1 1 1 LYS HB2 H 1 1.80 0.01 . 2 . . . . . . . . 4581 1 4 . 1 1 1 1 LYS HB3 H 1 2.00 0.01 . 2 . . . . . . . . 4581 1 5 . 1 1 1 1 LYS HG2 H 1 1.50 0.01 . 2 . . . . . . . . 4581 1 6 . 1 1 1 1 LYS HG3 H 1 1.59 0.01 . 2 . . . . . . . . 4581 1 7 . 1 1 1 1 LYS HD2 H 1 1.71 0.01 . 2 . . . . . . . . 4581 1 8 . 1 1 1 1 LYS HE2 H 1 2.92 0.01 . 2 . . . . . . . . 4581 1 9 . 1 1 1 1 LYS N N 15 124.8 0.1 . 1 . . . . . . . . 4581 1 10 . 1 1 2 2 SER H H 1 9.02 0.01 . 1 . . . . . . . . 4581 1 11 . 1 1 2 2 SER HA H 1 4.70 0.01 . 1 . . . . . . . . 4581 1 12 . 1 1 2 2 SER HB2 H 1 4.09 0.01 . 2 . . . . . . . . 4581 1 13 . 1 1 2 2 SER HB3 H 1 4.39 0.01 . 2 . . . . . . . . 4581 1 14 . 1 1 2 2 SER N N 15 119.3 0.1 . 1 . . . . . . . . 4581 1 15 . 1 1 3 3 PRO HA H 1 4.32 0.01 . 1 . . . . . . . . 4581 1 16 . 1 1 3 3 PRO HB2 H 1 2.01 0.01 . 2 . . . . . . . . 4581 1 17 . 1 1 3 3 PRO HB3 H 1 2.48 0.01 . 2 . . . . . . . . 4581 1 18 . 1 1 3 3 PRO HG2 H 1 2.20 0.01 . 2 . . . . . . . . 4581 1 19 . 1 1 3 3 PRO HD2 H 1 3.73 0.01 . 2 . . . . . . . . 4581 1 20 . 1 1 4 4 GLU H H 1 8.79 0.01 . 1 . . . . . . . . 4581 1 21 . 1 1 4 4 GLU HA H 1 4.035 0.01 . 1 . . . . . . . . 4581 1 22 . 1 1 4 4 GLU HB2 H 1 1.97 0.01 . 2 . . . . . . . . 4581 1 23 . 1 1 4 4 GLU HB3 H 1 2.05 0.01 . 2 . . . . . . . . 4581 1 24 . 1 1 4 4 GLU HG2 H 1 2.255 0.01 . 2 . . . . . . . . 4581 1 25 . 1 1 4 4 GLU HG3 H 1 2.44 0.01 . 2 . . . . . . . . 4581 1 26 . 1 1 4 4 GLU N N 15 117.4 0.1 . 1 . . . . . . . . 4581 1 27 . 1 1 5 5 GLU H H 1 8.04 0.01 . 1 . . . . . . . . 4581 1 28 . 1 1 5 5 GLU HA H 1 4.14 0.01 . 1 . . . . . . . . 4581 1 29 . 1 1 5 5 GLU HB2 H 1 2.05 0.01 . 2 . . . . . . . . 4581 1 30 . 1 1 5 5 GLU HB3 H 1 2.26 0.01 . 2 . . . . . . . . 4581 1 31 . 1 1 5 5 GLU HG2 H 1 2.41 0.01 . 1 . . . . . . . . 4581 1 32 . 1 1 5 5 GLU HG3 H 1 2.41 0.01 . 1 . . . . . . . . 4581 1 33 . 1 1 5 5 GLU N N 15 122.4 0.1 . 1 . . . . . . . . 4581 1 34 . 1 1 6 6 LEU H H 1 8.60 0.01 . 1 . . . . . . . . 4581 1 35 . 1 1 6 6 LEU HA H 1 4.29 0.01 . 1 . . . . . . . . 4581 1 36 . 1 1 6 6 LEU HB2 H 1 1.80 0.01 . 2 . . . . . . . . 4581 1 37 . 1 1 6 6 LEU HB3 H 1 2.20 0.01 . 2 . . . . . . . . 4581 1 38 . 1 1 6 6 LEU HG H 1 1.90 0.01 . 1 . . . . . . . . 4581 1 39 . 1 1 6 6 LEU HD11 H 1 0.93 0.01 . 2 . . . . . . . . 4581 1 40 . 1 1 6 6 LEU HD12 H 1 0.93 0.01 . 2 . . . . . . . . 4581 1 41 . 1 1 6 6 LEU HD13 H 1 0.93 0.01 . 2 . . . . . . . . 4581 1 42 . 1 1 6 6 LEU HD21 H 1 0.98 0.01 . 2 . . . . . . . . 4581 1 43 . 1 1 6 6 LEU HD22 H 1 0.98 0.01 . 2 . . . . . . . . 4581 1 44 . 1 1 6 6 LEU HD23 H 1 0.98 0.01 . 2 . . . . . . . . 4581 1 45 . 1 1 6 6 LEU N N 15 120.1 0.1 . 1 . . . . . . . . 4581 1 46 . 1 1 7 7 LYS H H 1 8.39 0.01 . 1 . . . . . . . . 4581 1 47 . 1 1 7 7 LYS HA H 1 3.98 0.01 . 1 . . . . . . . . 4581 1 48 . 1 1 7 7 LYS HB2 H 1 1.645 0.01 . 2 . . . . . . . . 4581 1 49 . 1 1 7 7 LYS HB3 H 1 1.85 0.01 . 2 . . . . . . . . 4581 1 50 . 1 1 7 7 LYS HG2 H 1 0.83 0.01 . 1 . . . . . . . . 4581 1 51 . 1 1 7 7 LYS HG3 H 1 0.83 0.01 . 1 . . . . . . . . 4581 1 52 . 1 1 7 7 LYS HD2 H 1 1.23 0.01 . 2 . . . . . . . . 4581 1 53 . 1 1 7 7 LYS N N 15 121.7 0.1 . 1 . . . . . . . . 4581 1 54 . 1 1 8 8 GLY H H 1 7.855 0.01 . 1 . . . . . . . . 4581 1 55 . 1 1 8 8 GLY HA2 H 1 3.925 0.01 . 1 . . . . . . . . 4581 1 56 . 1 1 8 8 GLY HA3 H 1 3.925 0.01 . 1 . . . . . . . . 4581 1 57 . 1 1 8 8 GLY N N 15 105.6 0.1 . 1 . . . . . . . . 4581 1 58 . 1 1 9 9 ILE H H 1 7.96 0.01 . 1 . . . . . . . . 4581 1 59 . 1 1 9 9 ILE HA H 1 3.915 0.01 . 1 . . . . . . . . 4581 1 60 . 1 1 9 9 ILE HB H 1 2.19 0.01 . 1 . . . . . . . . 4581 1 61 . 1 1 9 9 ILE HG12 H 1 1.83 0.01 . 2 . . . . . . . . 4581 1 62 . 1 1 9 9 ILE HG21 H 1 1.19 0.01 . 1 . . . . . . . . 4581 1 63 . 1 1 9 9 ILE HG22 H 1 1.19 0.01 . 1 . . . . . . . . 4581 1 64 . 1 1 9 9 ILE HG23 H 1 1.19 0.01 . 1 . . . . . . . . 4581 1 65 . 1 1 9 9 ILE HD11 H 1 0.98 0.01 . 1 . . . . . . . . 4581 1 66 . 1 1 9 9 ILE HD12 H 1 0.98 0.01 . 1 . . . . . . . . 4581 1 67 . 1 1 9 9 ILE HD13 H 1 0.98 0.01 . 1 . . . . . . . . 4581 1 68 . 1 1 9 9 ILE N N 15 122.2 0.1 . 1 . . . . . . . . 4581 1 69 . 1 1 10 10 PHE H H 1 8.65 0.01 . 1 . . . . . . . . 4581 1 70 . 1 1 10 10 PHE HA H 1 3.535 0.01 . 1 . . . . . . . . 4581 1 71 . 1 1 10 10 PHE HB2 H 1 2.86 0.01 . 2 . . . . . . . . 4581 1 72 . 1 1 10 10 PHE HB3 H 1 3.36 0.01 . 2 . . . . . . . . 4581 1 73 . 1 1 10 10 PHE HD1 H 1 6.52 0.01 . 3 . . . . . . . . 4581 1 74 . 1 1 10 10 PHE HE1 H 1 7.13 0.01 . 3 . . . . . . . . 4581 1 75 . 1 1 10 10 PHE HZ H 1 7.46 0.01 . 1 . . . . . . . . 4581 1 76 . 1 1 10 10 PHE N N 15 120.1 0.1 . 1 . . . . . . . . 4581 1 77 . 1 1 11 11 GLU H H 1 8.60 0.01 . 1 . . . . . . . . 4581 1 78 . 1 1 11 11 GLU HA H 1 3.78 0.01 . 1 . . . . . . . . 4581 1 79 . 1 1 11 11 GLU HB2 H 1 1.95 0.01 . 2 . . . . . . . . 4581 1 80 . 1 1 11 11 GLU HB3 H 1 2.10 0.01 . 2 . . . . . . . . 4581 1 81 . 1 1 11 11 GLU HG2 H 1 2.34 0.01 . 2 . . . . . . . . 4581 1 82 . 1 1 11 11 GLU HG3 H 1 2.66 0.01 . 2 . . . . . . . . 4581 1 83 . 1 1 11 11 GLU N N 15 115.5 0.1 . 1 . . . . . . . . 4581 1 84 . 1 1 12 12 LYS H H 1 7.62 0.01 . 1 . . . . . . . . 4581 1 85 . 1 1 12 12 LYS HA H 1 3.84 0.01 . 1 . . . . . . . . 4581 1 86 . 1 1 12 12 LYS HB2 H 1 1.77 0.01 . 2 . . . . . . . . 4581 1 87 . 1 1 12 12 LYS HB3 H 1 1.85 0.01 . 2 . . . . . . . . 4581 1 88 . 1 1 12 12 LYS HG2 H 1 0.58 0.01 . 2 . . . . . . . . 4581 1 89 . 1 1 12 12 LYS HG3 H 1 1.14 0.01 . 2 . . . . . . . . 4581 1 90 . 1 1 12 12 LYS HD2 H 1 1.47 0.01 . 2 . . . . . . . . 4581 1 91 . 1 1 12 12 LYS N N 15 118.9 0.1 . 1 . . . . . . . . 4581 1 92 . 1 1 13 13 TYR H H 1 7.27 0.01 . 1 . . . . . . . . 4581 1 93 . 1 1 13 13 TYR HA H 1 4.03 0.01 . 1 . . . . . . . . 4581 1 94 . 1 1 13 13 TYR HB2 H 1 2.41 0.01 . 2 . . . . . . . . 4581 1 95 . 1 1 13 13 TYR HB3 H 1 2.815 0.01 . 2 . . . . . . . . 4581 1 96 . 1 1 13 13 TYR HD1 H 1 6.73 0.01 . 3 . . . . . . . . 4581 1 97 . 1 1 13 13 TYR HE1 H 1 7.44 0.01 . 3 . . . . . . . . 4581 1 98 . 1 1 13 13 TYR N N 15 115.1 0.1 . 1 . . . . . . . . 4581 1 99 . 1 1 14 14 ALA H H 1 8.37 0.01 . 1 . . . . . . . . 4581 1 100 . 1 1 14 14 ALA HA H 1 3.88 0.01 . 1 . . . . . . . . 4581 1 101 . 1 1 14 14 ALA HB1 H 1 0.425 0.01 . 1 . . . . . . . . 4581 1 102 . 1 1 14 14 ALA HB2 H 1 0.425 0.01 . 1 . . . . . . . . 4581 1 103 . 1 1 14 14 ALA HB3 H 1 0.425 0.01 . 1 . . . . . . . . 4581 1 104 . 1 1 14 14 ALA N N 15 119.5 0.1 . 1 . . . . . . . . 4581 1 105 . 1 1 15 15 ALA H H 1 6.935 0.01 . 1 . . . . . . . . 4581 1 106 . 1 1 15 15 ALA HA H 1 4.29 0.01 . 1 . . . . . . . . 4581 1 107 . 1 1 15 15 ALA HB1 H 1 1.39 0.01 . 1 . . . . . . . . 4581 1 108 . 1 1 15 15 ALA HB2 H 1 1.39 0.01 . 1 . . . . . . . . 4581 1 109 . 1 1 15 15 ALA HB3 H 1 1.39 0.01 . 1 . . . . . . . . 4581 1 110 . 1 1 15 15 ALA N N 15 117.2 0.1 . 1 . . . . . . . . 4581 1 111 . 1 1 16 16 LYS H H 1 7.225 0.01 . 1 . . . . . . . . 4581 1 112 . 1 1 16 16 LYS HA H 1 3.83 0.01 . 1 . . . . . . . . 4581 1 113 . 1 1 16 16 LYS HB2 H 1 1.95 0.01 . 2 . . . . . . . . 4581 1 114 . 1 1 16 16 LYS HB3 H 1 2.10 0.01 . 2 . . . . . . . . 4581 1 115 . 1 1 16 16 LYS HG2 H 1 1.49 0.01 . 2 . . . . . . . . 4581 1 116 . 1 1 16 16 LYS HD2 H 1 1.69 0.01 . 2 . . . . . . . . 4581 1 117 . 1 1 16 16 LYS HD3 H 1 1.82 0.01 . 2 . . . . . . . . 4581 1 118 . 1 1 16 16 LYS HE2 H 1 2.76 0.01 . 2 . . . . . . . . 4581 1 119 . 1 1 16 16 LYS N N 15 120.3 0.1 . 1 . . . . . . . . 4581 1 120 . 1 1 17 17 GLU H H 1 9.69 0.01 . 1 . . . . . . . . 4581 1 121 . 1 1 17 17 GLU HA H 1 4.70 0.01 . 1 . . . . . . . . 4581 1 122 . 1 1 17 17 GLU HB2 H 1 1.87 0.01 . 2 . . . . . . . . 4581 1 123 . 1 1 17 17 GLU HB3 H 1 1.95 0.01 . 2 . . . . . . . . 4581 1 124 . 1 1 17 17 GLU HG2 H 1 2.09 0.01 . 2 . . . . . . . . 4581 1 125 . 1 1 17 17 GLU HG3 H 1 2.15 0.01 . 2 . . . . . . . . 4581 1 126 . 1 1 17 17 GLU N N 15 116.4 0.1 . 1 . . . . . . . . 4581 1 127 . 1 1 18 18 GLY H H 1 8.98 0.01 . 1 . . . . . . . . 4581 1 128 . 1 1 18 18 GLY HA2 H 1 3.68 0.01 . 2 . . . . . . . . 4581 1 129 . 1 1 18 18 GLY HA3 H 1 3.94 0.01 . 2 . . . . . . . . 4581 1 130 . 1 1 18 18 GLY N N 15 113.2 0.1 . 1 . . . . . . . . 4581 1 131 . 1 1 19 19 ASP H H 1 8.25 0.01 . 1 . . . . . . . . 4581 1 132 . 1 1 19 19 ASP HA H 1 4.45 0.01 . 1 . . . . . . . . 4581 1 133 . 1 1 19 19 ASP HB2 H 1 2.48 0.01 . 2 . . . . . . . . 4581 1 134 . 1 1 19 19 ASP HB3 H 1 2.71 0.01 . 2 . . . . . . . . 4581 1 135 . 1 1 19 19 ASP N N 15 126.0 0.1 . 1 . . . . . . . . 4581 1 136 . 1 1 20 20 PRO HA H 1 4.85 0.01 . 1 . . . . . . . . 4581 1 137 . 1 1 20 20 PRO HB2 H 1 2.03 0.01 . 2 . . . . . . . . 4581 1 138 . 1 1 20 20 PRO HB3 H 1 2.20 0.01 . 2 . . . . . . . . 4581 1 139 . 1 1 20 20 PRO HG2 H 1 1.87 0.01 . 2 . . . . . . . . 4581 1 140 . 1 1 20 20 PRO HG3 H 1 2.06 0.01 . 2 . . . . . . . . 4581 1 141 . 1 1 20 20 PRO HD2 H 1 3.98 0.01 . 2 . . . . . . . . 4581 1 142 . 1 1 21 21 ASN H H 1 9.15 0.01 . 1 . . . . . . . . 4581 1 143 . 1 1 21 21 ASN HA H 1 4.99 0.01 . 1 . . . . . . . . 4581 1 144 . 1 1 21 21 ASN HB2 H 1 2.66 0.01 . 2 . . . . . . . . 4581 1 145 . 1 1 21 21 ASN HB3 H 1 3.02 0.01 . 2 . . . . . . . . 4581 1 146 . 1 1 21 21 ASN N N 15 115.9 0.1 . 1 . . . . . . . . 4581 1 147 . 1 1 22 22 GLN H H 1 7.27 0.01 . 1 . . . . . . . . 4581 1 148 . 1 1 22 22 GLN HA H 1 5.00 0.01 . 1 . . . . . . . . 4581 1 149 . 1 1 22 22 GLN HB2 H 1 1.68 0.01 . 2 . . . . . . . . 4581 1 150 . 1 1 22 22 GLN HB3 H 1 1.97 0.01 . 2 . . . . . . . . 4581 1 151 . 1 1 22 22 GLN HG2 H 1 2.02 0.01 . 2 . . . . . . . . 4581 1 152 . 1 1 22 22 GLN HG3 H 1 2.27 0.01 . 2 . . . . . . . . 4581 1 153 . 1 1 22 22 GLN N N 15 114.9 0.1 . 1 . . . . . . . . 4581 1 154 . 1 1 23 23 LEU H H 1 9.77 0.01 . 1 . . . . . . . . 4581 1 155 . 1 1 23 23 LEU HA H 1 5.36 0.01 . 1 . . . . . . . . 4581 1 156 . 1 1 23 23 LEU HB2 H 1 1.70 0.01 . 2 . . . . . . . . 4581 1 157 . 1 1 23 23 LEU HB3 H 1 1.83 0.01 . 2 . . . . . . . . 4581 1 158 . 1 1 23 23 LEU HG H 1 1.34 0.01 . 1 . . . . . . . . 4581 1 159 . 1 1 23 23 LEU HD11 H 1 0.42 0.01 . 1 . . . . . . . . 4581 1 160 . 1 1 23 23 LEU HD12 H 1 0.42 0.01 . 1 . . . . . . . . 4581 1 161 . 1 1 23 23 LEU HD13 H 1 0.42 0.01 . 1 . . . . . . . . 4581 1 162 . 1 1 23 23 LEU HD21 H 1 0.58 0.01 . 1 . . . . . . . . 4581 1 163 . 1 1 23 23 LEU HD22 H 1 0.58 0.01 . 1 . . . . . . . . 4581 1 164 . 1 1 23 23 LEU HD23 H 1 0.58 0.01 . 1 . . . . . . . . 4581 1 165 . 1 1 23 23 LEU N N 15 127.5 0.1 . 1 . . . . . . . . 4581 1 166 . 1 1 24 24 SER H H 1 10.21 0.01 . 1 . . . . . . . . 4581 1 167 . 1 1 24 24 SER HA H 1 4.95 0.01 . 1 . . . . . . . . 4581 1 168 . 1 1 24 24 SER HB2 H 1 4.08 0.01 . 2 . . . . . . . . 4581 1 169 . 1 1 24 24 SER HB3 H 1 4.39 0.01 . 2 . . . . . . . . 4581 1 170 . 1 1 24 24 SER N N 15 122.7 0.1 . 1 . . . . . . . . 4581 1 171 . 1 1 25 25 LYS H H 1 8.695 0.01 . 1 . . . . . . . . 4581 1 172 . 1 1 25 25 LYS HA H 1 3.50 0.01 . 1 . . . . . . . . 4581 1 173 . 1 1 25 25 LYS HB2 H 1 1.80 0.01 . 2 . . . . . . . . 4581 1 174 . 1 1 25 25 LYS N N 15 119.9 0.1 . 1 . . . . . . . . 4581 1 175 . 1 1 26 26 GLU H H 1 8.12 0.01 . 1 . . . . . . . . 4581 1 176 . 1 1 26 26 GLU HA H 1 3.925 0.01 . 1 . . . . . . . . 4581 1 177 . 1 1 26 26 GLU HB2 H 1 1.93 0.01 . 2 . . . . . . . . 4581 1 178 . 1 1 26 26 GLU HG2 H 1 2.22 0.01 . 2 . . . . . . . . 4581 1 179 . 1 1 26 26 GLU HG3 H 1 2.31 0.01 . 2 . . . . . . . . 4581 1 180 . 1 1 26 26 GLU N N 15 117.4 0.1 . 1 . . . . . . . . 4581 1 181 . 1 1 27 27 GLU H H 1 7.83 0.01 . 1 . . . . . . . . 4581 1 182 . 1 1 27 27 GLU HA H 1 3.925 0.01 . 1 . . . . . . . . 4581 1 183 . 1 1 27 27 GLU HB2 H 1 1.90 0.01 . 2 . . . . . . . . 4581 1 184 . 1 1 27 27 GLU HB3 H 1 2.54 0.01 . 2 . . . . . . . . 4581 1 185 . 1 1 27 27 GLU HG2 H 1 2.36 0.01 . 2 . . . . . . . . 4581 1 186 . 1 1 27 27 GLU HG3 H 1 2.54 0.01 . 2 . . . . . . . . 4581 1 187 . 1 1 27 27 GLU N N 15 120.8 0.1 . 1 . . . . . . . . 4581 1 188 . 1 1 28 28 LEU H H 1 8.77 0.01 . 1 . . . . . . . . 4581 1 189 . 1 1 28 28 LEU HA H 1 3.98 0.01 . 1 . . . . . . . . 4581 1 190 . 1 1 28 28 LEU HB2 H 1 1.54 0.01 . 2 . . . . . . . . 4581 1 191 . 1 1 28 28 LEU HB3 H 1 2.23 0.01 . 2 . . . . . . . . 4581 1 192 . 1 1 28 28 LEU HG H 1 1.68 0.01 . 1 . . . . . . . . 4581 1 193 . 1 1 28 28 LEU HD11 H 1 1.085 0.01 . 1 . . . . . . . . 4581 1 194 . 1 1 28 28 LEU HD12 H 1 1.085 0.01 . 1 . . . . . . . . 4581 1 195 . 1 1 28 28 LEU HD13 H 1 1.085 0.01 . 1 . . . . . . . . 4581 1 196 . 1 1 28 28 LEU HD21 H 1 1.085 0.01 . 1 . . . . . . . . 4581 1 197 . 1 1 28 28 LEU HD22 H 1 1.085 0.01 . 1 . . . . . . . . 4581 1 198 . 1 1 28 28 LEU HD23 H 1 1.085 0.01 . 1 . . . . . . . . 4581 1 199 . 1 1 28 28 LEU N N 15 119.3 0.1 . 1 . . . . . . . . 4581 1 200 . 1 1 29 29 LYS H H 1 8.42 0.01 . 1 . . . . . . . . 4581 1 201 . 1 1 29 29 LYS HA H 1 3.665 0.01 . 1 . . . . . . . . 4581 1 202 . 1 1 29 29 LYS HB2 H 1 1.84 0.01 . 2 . . . . . . . . 4581 1 203 . 1 1 29 29 LYS HB3 H 1 1.95 0.01 . 2 . . . . . . . . 4581 1 204 . 1 1 29 29 LYS HG2 H 1 1.39 0.01 . 2 . . . . . . . . 4581 1 205 . 1 1 29 29 LYS HD2 H 1 1.64 0.01 . 2 . . . . . . . . 4581 1 206 . 1 1 29 29 LYS HE2 H 1 2.96 0.01 . 1 . . . . . . . . 4581 1 207 . 1 1 29 29 LYS HE3 H 1 2.96 0.01 . 1 . . . . . . . . 4581 1 208 . 1 1 29 29 LYS N N 15 119.9 0.1 . 1 . . . . . . . . 4581 1 209 . 1 1 30 30 LEU H H 1 7.56 0.01 . 1 . . . . . . . . 4581 1 210 . 1 1 30 30 LEU HA H 1 4.035 0.01 . 1 . . . . . . . . 4581 1 211 . 1 1 30 30 LEU HB2 H 1 1.80 0.01 . 2 . . . . . . . . 4581 1 212 . 1 1 30 30 LEU HD11 H 1 1.01 0.01 . 1 . . . . . . . . 4581 1 213 . 1 1 30 30 LEU HD12 H 1 1.01 0.01 . 1 . . . . . . . . 4581 1 214 . 1 1 30 30 LEU HD13 H 1 1.01 0.01 . 1 . . . . . . . . 4581 1 215 . 1 1 30 30 LEU HD21 H 1 1.01 0.01 . 1 . . . . . . . . 4581 1 216 . 1 1 30 30 LEU HD22 H 1 1.01 0.01 . 1 . . . . . . . . 4581 1 217 . 1 1 30 30 LEU HD23 H 1 1.01 0.01 . 1 . . . . . . . . 4581 1 218 . 1 1 30 30 LEU N N 15 118.7 0.1 . 1 . . . . . . . . 4581 1 219 . 1 1 31 31 LEU H H 1 8.15 0.01 . 1 . . . . . . . . 4581 1 220 . 1 1 31 31 LEU HA H 1 2.31 0.01 . 1 . . . . . . . . 4581 1 221 . 1 1 31 31 LEU HB2 H 1 1.19 0.01 . 2 . . . . . . . . 4581 1 222 . 1 1 31 31 LEU HB3 H 1 1.75 0.01 . 2 . . . . . . . . 4581 1 223 . 1 1 31 31 LEU HD11 H 1 0.93 0.01 . 2 . . . . . . . . 4581 1 224 . 1 1 31 31 LEU HD12 H 1 0.93 0.01 . 2 . . . . . . . . 4581 1 225 . 1 1 31 31 LEU HD13 H 1 0.93 0.01 . 2 . . . . . . . . 4581 1 226 . 1 1 31 31 LEU HD21 H 1 0.98 0.01 . 2 . . . . . . . . 4581 1 227 . 1 1 31 31 LEU HD22 H 1 0.98 0.01 . 2 . . . . . . . . 4581 1 228 . 1 1 31 31 LEU HD23 H 1 0.98 0.01 . 2 . . . . . . . . 4581 1 229 . 1 1 31 31 LEU N N 15 124.35 0.1 . 1 . . . . . . . . 4581 1 230 . 1 1 32 32 LEU H H 1 8.875 0.01 . 1 . . . . . . . . 4581 1 231 . 1 1 32 32 LEU HA H 1 3.88 0.01 . 1 . . . . . . . . 4581 1 232 . 1 1 32 32 LEU HB2 H 1 1.34 0.01 . 2 . . . . . . . . 4581 1 233 . 1 1 32 32 LEU HB3 H 1 1.97 0.01 . 2 . . . . . . . . 4581 1 234 . 1 1 32 32 LEU HG H 1 2.15 0.01 . 1 . . . . . . . . 4581 1 235 . 1 1 32 32 LEU HD11 H 1 0.93 0.01 . 1 . . . . . . . . 4581 1 236 . 1 1 32 32 LEU HD12 H 1 0.93 0.01 . 1 . . . . . . . . 4581 1 237 . 1 1 32 32 LEU HD13 H 1 0.93 0.01 . 1 . . . . . . . . 4581 1 238 . 1 1 32 32 LEU HD21 H 1 1.14 0.01 . 1 . . . . . . . . 4581 1 239 . 1 1 32 32 LEU HD22 H 1 1.14 0.01 . 1 . . . . . . . . 4581 1 240 . 1 1 32 32 LEU HD23 H 1 1.14 0.01 . 1 . . . . . . . . 4581 1 241 . 1 1 32 32 LEU N N 15 120.35 0.1 . 1 . . . . . . . . 4581 1 242 . 1 1 33 33 GLN H H 1 8.44 0.01 . 1 . . . . . . . . 4581 1 243 . 1 1 33 33 GLN HA H 1 3.88 0.01 . 2 . . . . . . . . 4581 1 244 . 1 1 33 33 GLN HB2 H 1 1.95 0.01 . 2 . . . . . . . . 4581 1 245 . 1 1 33 33 GLN HB3 H 1 2.15 0.01 . 2 . . . . . . . . 4581 1 246 . 1 1 33 33 GLN HG2 H 1 2.36 0.01 . 2 . . . . . . . . 4581 1 247 . 1 1 33 33 GLN HG3 H 1 2.51 0.01 . 2 . . . . . . . . 4581 1 248 . 1 1 33 33 GLN N N 15 114.5 0.1 . 1 . . . . . . . . 4581 1 249 . 1 1 34 34 THR H H 1 7.67 0.01 . 1 . . . . . . . . 4581 1 250 . 1 1 34 34 THR HA H 1 4.035 0.01 . 1 . . . . . . . . 4581 1 251 . 1 1 34 34 THR HB H 1 4.19 0.01 . 1 . . . . . . . . 4581 1 252 . 1 1 34 34 THR HG21 H 1 1.235 0.01 . 1 . . . . . . . . 4581 1 253 . 1 1 34 34 THR HG22 H 1 1.235 0.01 . 1 . . . . . . . . 4581 1 254 . 1 1 34 34 THR HG23 H 1 1.235 0.01 . 1 . . . . . . . . 4581 1 255 . 1 1 34 34 THR N N 15 111.5 0.1 . 1 . . . . . . . . 4581 1 256 . 1 1 35 35 GLU H H 1 8.56 0.01 . 1 . . . . . . . . 4581 1 257 . 1 1 35 35 GLU HA H 1 4.19 0.01 . 1 . . . . . . . . 4581 1 258 . 1 1 35 35 GLU HB2 H 1 1.43 0.01 . 2 . . . . . . . . 4581 1 259 . 1 1 35 35 GLU HB3 H 1 1.495 0.01 . 2 . . . . . . . . 4581 1 260 . 1 1 35 35 GLU HG2 H 1 2.36 0.01 . 2 . . . . . . . . 4581 1 261 . 1 1 35 35 GLU N N 15 116.4 0.1 . 1 . . . . . . . . 4581 1 262 . 1 1 36 36 PHE H H 1 7.87 0.01 . 1 . . . . . . . . 4581 1 263 . 1 1 36 36 PHE HA H 1 5.15 0.01 . 1 . . . . . . . . 4581 1 264 . 1 1 36 36 PHE HB2 H 1 2.815 0.01 . 2 . . . . . . . . 4581 1 265 . 1 1 36 36 PHE HB3 H 1 3.32 0.01 . 2 . . . . . . . . 4581 1 266 . 1 1 36 36 PHE HD1 H 1 7.13 0.01 . 3 . . . . . . . . 4581 1 267 . 1 1 36 36 PHE HE1 H 1 7.18 0.01 . 3 . . . . . . . . 4581 1 268 . 1 1 36 36 PHE HZ H 1 7.02 0.01 . 1 . . . . . . . . 4581 1 269 . 1 1 36 36 PHE N N 15 115.7 0.1 . 1 . . . . . . . . 4581 1 270 . 1 1 37 37 PRO HA H 1 4.24 0.01 . 1 . . . . . . . . 4581 1 271 . 1 1 37 37 PRO HB2 H 1 2.44 0.01 . 2 . . . . . . . . 4581 1 272 . 1 1 38 38 SER H H 1 8.375 0.01 . 1 . . . . . . . . 4581 1 273 . 1 1 38 38 SER HA H 1 4.24 0.01 . 1 . . . . . . . . 4581 1 274 . 1 1 38 38 SER HB2 H 1 3.93 0.01 . 2 . . . . . . . . 4581 1 275 . 1 1 38 38 SER HB3 H 1 4.00 0.01 . 2 . . . . . . . . 4581 1 276 . 1 1 38 38 SER N N 15 113.4 0.1 . 1 . . . . . . . . 4581 1 277 . 1 1 39 39 LEU H H 1 7.94 0.01 . 1 . . . . . . . . 4581 1 278 . 1 1 39 39 LEU HA H 1 4.13 0.01 . 1 . . . . . . . . 4581 1 279 . 1 1 39 39 LEU HB2 H 1 1.78 0.01 . 2 . . . . . . . . 4581 1 280 . 1 1 39 39 LEU HB3 H 1 1.90 0.01 . 2 . . . . . . . . 4581 1 281 . 1 1 39 39 LEU HG H 1 1.44 0.01 . 1 . . . . . . . . 4581 1 282 . 1 1 39 39 LEU HD11 H 1 0.73 0.01 . 1 . . . . . . . . 4581 1 283 . 1 1 39 39 LEU HD12 H 1 0.73 0.01 . 1 . . . . . . . . 4581 1 284 . 1 1 39 39 LEU HD13 H 1 0.73 0.01 . 1 . . . . . . . . 4581 1 285 . 1 1 39 39 LEU HD21 H 1 0.73 0.01 . 1 . . . . . . . . 4581 1 286 . 1 1 39 39 LEU HD22 H 1 0.73 0.01 . 1 . . . . . . . . 4581 1 287 . 1 1 39 39 LEU HD23 H 1 0.73 0.01 . 1 . . . . . . . . 4581 1 288 . 1 1 39 39 LEU N N 15 123.1 0.1 . 1 . . . . . . . . 4581 1 289 . 1 1 40 40 LEU H H 1 7.69 0.01 . 1 . . . . . . . . 4581 1 290 . 1 1 40 40 LEU HA H 1 4.295 0.01 . 1 . . . . . . . . 4581 1 291 . 1 1 40 40 LEU HB2 H 1 1.75 0.01 . 2 . . . . . . . . 4581 1 292 . 1 1 40 40 LEU HB3 H 1 1.90 0.01 . 2 . . . . . . . . 4581 1 293 . 1 1 40 40 LEU HG H 1 1.44 0.01 . 1 . . . . . . . . 4581 1 294 . 1 1 40 40 LEU HD11 H 1 0.81 0.01 . 1 . . . . . . . . 4581 1 295 . 1 1 40 40 LEU HD12 H 1 0.81 0.01 . 1 . . . . . . . . 4581 1 296 . 1 1 40 40 LEU HD13 H 1 0.81 0.01 . 1 . . . . . . . . 4581 1 297 . 1 1 40 40 LEU HD21 H 1 0.90 0.01 . 1 . . . . . . . . 4581 1 298 . 1 1 40 40 LEU HD22 H 1 0.90 0.01 . 1 . . . . . . . . 4581 1 299 . 1 1 40 40 LEU HD23 H 1 0.90 0.01 . 1 . . . . . . . . 4581 1 300 . 1 1 40 40 LEU N N 15 120.2 0.1 . 1 . . . . . . . . 4581 1 301 . 1 1 41 41 LYS H H 1 7.46 0.01 . 1 . . . . . . . . 4581 1 302 . 1 1 41 41 LYS HA H 1 4.36 0.01 . 1 . . . . . . . . 4581 1 303 . 1 1 41 41 LYS HB2 H 1 1.80 0.01 . 2 . . . . . . . . 4581 1 304 . 1 1 41 41 LYS HB3 H 1 1.98 0.01 . 2 . . . . . . . . 4581 1 305 . 1 1 41 41 LYS HG2 H 1 1.38 0.01 . 2 . . . . . . . . 4581 1 306 . 1 1 41 41 LYS HG3 H 1 1.45 0.01 . 2 . . . . . . . . 4581 1 307 . 1 1 41 41 LYS HE2 H 1 3.01 0.01 . 1 . . . . . . . . 4581 1 308 . 1 1 41 41 LYS HE3 H 1 3.01 0.01 . 1 . . . . . . . . 4581 1 309 . 1 1 41 41 LYS N N 15 119.9 0.1 . 1 . . . . . . . . 4581 1 310 . 1 1 42 42 GLY H H 1 8.07 0.01 . 1 . . . . . . . . 4581 1 311 . 1 1 42 42 GLY HA2 H 1 3.93 0.01 . 2 . . . . . . . . 4581 1 312 . 1 1 42 42 GLY HA3 H 1 4.18 0.01 . 2 . . . . . . . . 4581 1 313 . 1 1 42 42 GLY N N 15 108.6 0.1 . 1 . . . . . . . . 4581 1 314 . 1 1 43 43 MET H H 1 8.00 0.01 . 1 . . . . . . . . 4581 1 315 . 1 1 43 43 MET HA H 1 4.68 0.01 . 1 . . . . . . . . 4581 1 316 . 1 1 43 43 MET HB2 H 1 2.09 0.01 . 2 . . . . . . . . 4581 1 317 . 1 1 43 43 MET HG2 H 1 2.58 0.01 . 2 . . . . . . . . 4581 1 318 . 1 1 43 43 MET HG3 H 1 2.63 0.01 . 2 . . . . . . . . 4581 1 319 . 1 1 44 44 SER H H 1 8.40 0.01 . 1 . . . . . . . . 4581 1 320 . 1 1 44 44 SER HA H 1 4.56 0.01 . 1 . . . . . . . . 4581 1 321 . 1 1 44 44 SER HB2 H 1 3.88 0.01 . 1 . . . . . . . . 4581 1 322 . 1 1 44 44 SER HB3 H 1 3.88 0.01 . 1 . . . . . . . . 4581 1 323 . 1 1 44 44 SER N N 15 115.9 0.1 . 1 . . . . . . . . 4581 1 324 . 1 1 45 45 THR H H 1 7.96 0.01 . 1 . . . . . . . . 4581 1 325 . 1 1 45 45 THR HA H 1 4.39 0.01 . 1 . . . . . . . . 4581 1 326 . 1 1 45 45 THR HB H 1 4.54 0.01 . 1 . . . . . . . . 4581 1 327 . 1 1 45 45 THR HG21 H 1 1.29 0.01 . 1 . . . . . . . . 4581 1 328 . 1 1 45 45 THR HG22 H 1 1.29 0.01 . 1 . . . . . . . . 4581 1 329 . 1 1 45 45 THR HG23 H 1 1.29 0.01 . 1 . . . . . . . . 4581 1 330 . 1 1 45 45 THR N N 15 114.0 0.1 . 1 . . . . . . . . 4581 1 331 . 1 1 46 46 LEU H H 1 8.08 0.01 . 1 . . . . . . . . 4581 1 332 . 1 1 46 46 LEU HA H 1 4.14 0.01 . 1 . . . . . . . . 4581 1 333 . 1 1 46 46 LEU HB2 H 1 1.79 0.01 . 2 . . . . . . . . 4581 1 334 . 1 1 46 46 LEU HG H 1 1.95 0.01 . 1 . . . . . . . . 4581 1 335 . 1 1 46 46 LEU HD11 H 1 0.97 0.01 . 1 . . . . . . . . 4581 1 336 . 1 1 46 46 LEU HD12 H 1 0.97 0.01 . 1 . . . . . . . . 4581 1 337 . 1 1 46 46 LEU HD13 H 1 0.97 0.01 . 1 . . . . . . . . 4581 1 338 . 1 1 46 46 LEU HD21 H 1 0.97 0.01 . 1 . . . . . . . . 4581 1 339 . 1 1 46 46 LEU HD22 H 1 0.97 0.01 . 1 . . . . . . . . 4581 1 340 . 1 1 46 46 LEU HD23 H 1 0.97 0.01 . 1 . . . . . . . . 4581 1 341 . 1 1 46 46 LEU N N 15 122.0 0.1 . 1 . . . . . . . . 4581 1 342 . 1 1 47 47 ASP H H 1 8.21 0.01 . 1 . . . . . . . . 4581 1 343 . 1 1 47 47 ASP HA H 1 4.035 0.01 . 1 . . . . . . . . 4581 1 344 . 1 1 47 47 ASP HB2 H 1 2.48 0.01 . 2 . . . . . . . . 4581 1 345 . 1 1 47 47 ASP HB3 H 1 2.71 0.01 . 2 . . . . . . . . 4581 1 346 . 1 1 47 47 ASP N N 15 114.5 0.1 . 1 . . . . . . . . 4581 1 347 . 1 1 48 48 GLU H H 1 7.895 0.01 . 1 . . . . . . . . 4581 1 348 . 1 1 48 48 GLU HA H 1 4.035 0.01 . 1 . . . . . . . . 4581 1 349 . 1 1 48 48 GLU HB2 H 1 2.15 0.01 . 2 . . . . . . . . 4581 1 350 . 1 1 48 48 GLU HG2 H 1 2.31 0.01 . 2 . . . . . . . . 4581 1 351 . 1 1 48 48 GLU N N 15 119.5 0.1 . 1 . . . . . . . . 4581 1 352 . 1 1 49 49 LEU H H 1 8.08 0.01 . 1 . . . . . . . . 4581 1 353 . 1 1 49 49 LEU HA H 1 4.23 0.01 . 1 . . . . . . . . 4581 1 354 . 1 1 49 49 LEU HB2 H 1 1.55 0.01 . 2 . . . . . . . . 4581 1 355 . 1 1 49 49 LEU HB3 H 1 1.65 0.01 . 2 . . . . . . . . 4581 1 356 . 1 1 49 49 LEU HG H 1 1.63 0.01 . 1 . . . . . . . . 4581 1 357 . 1 1 49 49 LEU HD11 H 1 0.72 0.01 . 2 . . . . . . . . 4581 1 358 . 1 1 49 49 LEU HD12 H 1 0.72 0.01 . 2 . . . . . . . . 4581 1 359 . 1 1 49 49 LEU HD13 H 1 0.72 0.01 . 2 . . . . . . . . 4581 1 360 . 1 1 49 49 LEU HD21 H 1 0.78 0.01 . 2 . . . . . . . . 4581 1 361 . 1 1 49 49 LEU HD22 H 1 0.78 0.01 . 2 . . . . . . . . 4581 1 362 . 1 1 49 49 LEU HD23 H 1 0.78 0.01 . 2 . . . . . . . . 4581 1 363 . 1 1 49 49 LEU N N 15 121.0 0.01 . 1 . . . . . . . . 4581 1 364 . 1 1 50 50 PHE H H 1 8.65 0.01 . 1 . . . . . . . . 4581 1 365 . 1 1 50 50 PHE HA H 1 3.83 0.01 . 1 . . . . . . . . 4581 1 366 . 1 1 50 50 PHE HB2 H 1 3.07 0.01 . 2 . . . . . . . . 4581 1 367 . 1 1 50 50 PHE HB3 H 1 3.17 0.01 . 2 . . . . . . . . 4581 1 368 . 1 1 50 50 PHE HD1 H 1 7.14 0.01 . 3 . . . . . . . . 4581 1 369 . 1 1 50 50 PHE HE1 H 1 7.14 0.01 . 3 . . . . . . . . 4581 1 370 . 1 1 50 50 PHE HZ H 1 7.14 0.01 . 1 . . . . . . . . 4581 1 371 . 1 1 50 50 PHE N N 15 118.9 0.1 . 1 . . . . . . . . 4581 1 372 . 1 1 51 51 GLU H H 1 7.92 0.01 . 1 . . . . . . . . 4581 1 373 . 1 1 51 51 GLU HA H 1 4.035 0.01 . 2 . . . . . . . . 4581 1 374 . 1 1 51 51 GLU HB2 H 1 2.10 0.01 . 2 . . . . . . . . 4581 1 375 . 1 1 51 51 GLU HG2 H 1 2.31 0.01 . 2 . . . . . . . . 4581 1 376 . 1 1 51 51 GLU HG3 H 1 2.46 0.01 . 2 . . . . . . . . 4581 1 377 . 1 1 51 51 GLU N N 15 117.2 0.1 . 1 . . . . . . . . 4581 1 378 . 1 1 52 52 GLU H H 1 7.71 0.01 . 1 . . . . . . . . 4581 1 379 . 1 1 52 52 GLU HA H 1 3.98 0.01 . 1 . . . . . . . . 4581 1 380 . 1 1 52 52 GLU HB2 H 1 2.10 0.01 . 2 . . . . . . . . 4581 1 381 . 1 1 52 52 GLU HG2 H 1 2.05 0.01 . 2 . . . . . . . . 4581 1 382 . 1 1 52 52 GLU HG3 H 1 2.31 0.01 . 2 . . . . . . . . 4581 1 383 . 1 1 52 52 GLU N N 15 118.5 0.1 . 1 . . . . . . . . 4581 1 384 . 1 1 53 53 LEU H H 1 7.67 0.01 . 1 . . . . . . . . 4581 1 385 . 1 1 53 53 LEU HA H 1 4.14 0.01 . 1 . . . . . . . . 4581 1 386 . 1 1 53 53 LEU HB2 H 1 1.295 0.01 . 2 . . . . . . . . 4581 1 387 . 1 1 53 53 LEU HB3 H 1 1.65 0.01 . 2 . . . . . . . . 4581 1 388 . 1 1 53 53 LEU HG H 1 1.92 0.01 . 1 . . . . . . . . 4581 1 389 . 1 1 53 53 LEU HD11 H 1 0.80 0.01 . 1 . . . . . . . . 4581 1 390 . 1 1 53 53 LEU HD12 H 1 0.80 0.01 . 1 . . . . . . . . 4581 1 391 . 1 1 53 53 LEU HD13 H 1 0.80 0.01 . 1 . . . . . . . . 4581 1 392 . 1 1 53 53 LEU HD21 H 1 0.73 0.01 . 1 . . . . . . . . 4581 1 393 . 1 1 53 53 LEU HD22 H 1 0.73 0.01 . 1 . . . . . . . . 4581 1 394 . 1 1 53 53 LEU HD23 H 1 0.73 0.01 . 1 . . . . . . . . 4581 1 395 . 1 1 53 53 LEU N N 15 117.3 0.1 . 1 . . . . . . . . 4581 1 396 . 1 1 54 54 ASP H H 1 8.10 0.01 . 1 . . . . . . . . 4581 1 397 . 1 1 54 54 ASP HA H 1 4.445 0.01 . 1 . . . . . . . . 4581 1 398 . 1 1 54 54 ASP HB2 H 1 2.56 0.01 . 2 . . . . . . . . 4581 1 399 . 1 1 54 54 ASP HB3 H 1 2.67 0.01 . 2 . . . . . . . . 4581 1 400 . 1 1 54 54 ASP N N 15 119.5 0.1 . 1 . . . . . . . . 4581 1 401 . 1 1 55 55 LYS H H 1 8.145 0.01 . 1 . . . . . . . . 4581 1 402 . 1 1 55 55 LYS HA H 1 4.14 0.01 . 1 . . . . . . . . 4581 1 403 . 1 1 55 55 LYS HB2 H 1 1.64 0.01 . 2 . . . . . . . . 4581 1 404 . 1 1 55 55 LYS HG2 H 1 1.79 0.01 . 2 . . . . . . . . 4581 1 405 . 1 1 55 55 LYS HE2 H 1 3.06 0.01 . 2 . . . . . . . . 4581 1 406 . 1 1 55 55 LYS N N 15 121.2 0.1 . 1 . . . . . . . . 4581 1 407 . 1 1 56 56 ALA H H 1 8.04 0.01 . 1 . . . . . . . . 4581 1 408 . 1 1 56 56 ALA HA H 1 4.24 0.01 . 1 . . . . . . . . 4581 1 409 . 1 1 56 56 ALA HB1 H 1 1.49 0.01 . 1 . . . . . . . . 4581 1 410 . 1 1 56 56 ALA HB2 H 1 1.49 0.01 . 1 . . . . . . . . 4581 1 411 . 1 1 56 56 ALA HB3 H 1 1.49 0.01 . 1 . . . . . . . . 4581 1 412 . 1 1 56 56 ALA N N 15 119.7 0.1 . 1 . . . . . . . . 4581 1 413 . 1 1 57 57 GLY H H 1 8.00 0.01 . 1 . . . . . . . . 4581 1 414 . 1 1 57 57 GLY HA2 H 1 3.88 0.01 . 1 . . . . . . . . 4581 1 415 . 1 1 57 57 GLY HA3 H 1 3.88 0.01 . 1 . . . . . . . . 4581 1 416 . 1 1 57 57 GLY N N 15 107.5 0.1 . 1 . . . . . . . . 4581 1 417 . 1 1 58 58 ASP H H 1 8.52 0.01 . 1 . . . . . . . . 4581 1 418 . 1 1 58 58 ASP HA H 1 4.70 0.01 . 1 . . . . . . . . 4581 1 419 . 1 1 58 58 ASP HB2 H 1 2.61 0.01 . 2 . . . . . . . . 4581 1 420 . 1 1 58 58 ASP HB3 H 1 2.92 0.01 . 2 . . . . . . . . 4581 1 421 . 1 1 58 58 ASP N N 15 119.3 0.1 . 1 . . . . . . . . 4581 1 422 . 1 1 59 59 GLY H H 1 8.71 0.01 . 1 . . . . . . . . 4581 1 423 . 1 1 59 59 GLY HA2 H 1 3.75 0.01 . 2 . . . . . . . . 4581 1 424 . 1 1 59 59 GLY HA3 H 1 4.14 0.01 . 2 . . . . . . . . 4581 1 425 . 1 1 59 59 GLY N N 15 112.4 0.1 . 1 . . . . . . . . 4581 1 426 . 1 1 60 60 GLU H H 1 7.83 0.01 . 1 . . . . . . . . 4581 1 427 . 1 1 60 60 GLU HA H 1 5.05 0.01 . 1 . . . . . . . . 4581 1 428 . 1 1 60 60 GLU HB2 H 1 1.645 0.01 . 2 . . . . . . . . 4581 1 429 . 1 1 60 60 GLU HB3 H 1 1.95 0.01 . 2 . . . . . . . . 4581 1 430 . 1 1 60 60 GLU HG2 H 1 2.15 0.01 . 2 . . . . . . . . 4581 1 431 . 1 1 60 60 GLU N N 15 118.2 0.1 . 1 . . . . . . . . 4581 1 432 . 1 1 61 61 VAL H H 1 9.55 0.01 . 1 . . . . . . . . 4581 1 433 . 1 1 61 61 VAL HA H 1 5.05 0.01 . 1 . . . . . . . . 4581 1 434 . 1 1 61 61 VAL HB H 1 2.36 0.01 . 1 . . . . . . . . 4581 1 435 . 1 1 61 61 VAL HG11 H 1 0.57 0.01 . 2 . . . . . . . . 4581 1 436 . 1 1 61 61 VAL HG12 H 1 0.57 0.01 . 2 . . . . . . . . 4581 1 437 . 1 1 61 61 VAL HG13 H 1 0.57 0.01 . 2 . . . . . . . . 4581 1 438 . 1 1 61 61 VAL HG21 H 1 1.04 0.01 . 2 . . . . . . . . 4581 1 439 . 1 1 61 61 VAL HG22 H 1 1.04 0.01 . 2 . . . . . . . . 4581 1 440 . 1 1 61 61 VAL HG23 H 1 1.04 0.01 . 2 . . . . . . . . 4581 1 441 . 1 1 61 61 VAL N N 15 121.4 0.1 . 1 . . . . . . . . 4581 1 442 . 1 1 62 62 SER H H 1 9.33 0.01 . 1 . . . . . . . . 4581 1 443 . 1 1 62 62 SER HA H 1 4.86 0.01 . 1 . . . . . . . . 4581 1 444 . 1 1 62 62 SER HB2 H 1 4.18 0.01 . 2 . . . . . . . . 4581 1 445 . 1 1 62 62 SER HB3 H 1 4.49 0.01 . 2 . . . . . . . . 4581 1 446 . 1 1 62 62 SER N N 15 123.7 0.1 . 1 . . . . . . . . 4581 1 447 . 1 1 63 63 PHE H H 1 9.38 0.01 . 1 . . . . . . . . 4581 1 448 . 1 1 63 63 PHE HA H 1 3.37 0.01 . 1 . . . . . . . . 4581 1 449 . 1 1 63 63 PHE HB2 H 1 2.255 0.01 . 2 . . . . . . . . 4581 1 450 . 1 1 63 63 PHE HB3 H 1 2.56 0.01 . 2 . . . . . . . . 4581 1 451 . 1 1 63 63 PHE HD1 H 1 6.67 0.01 . 3 . . . . . . . . 4581 1 452 . 1 1 63 63 PHE HE1 H 1 7.13 0.01 . 3 . . . . . . . . 4581 1 453 . 1 1 63 63 PHE HZ H 1 7.34 0.01 . 1 . . . . . . . . 4581 1 454 . 1 1 63 63 PHE N N 15 122.7 0.1 . 1 . . . . . . . . 4581 1 455 . 1 1 64 64 GLU H H 1 8.60 0.01 . 1 . . . . . . . . 4581 1 456 . 1 1 64 64 GLU HA H 1 3.73 0.01 . 1 . . . . . . . . 4581 1 457 . 1 1 64 64 GLU HB2 H 1 1.85 0.01 . 2 . . . . . . . . 4581 1 458 . 1 1 64 64 GLU HB3 H 1 2.00 0.01 . 2 . . . . . . . . 4581 1 459 . 1 1 64 64 GLU HG2 H 1 2.255 0.01 . 2 . . . . . . . . 4581 1 460 . 1 1 64 64 GLU N N 15 118.7 0.1 . 1 . . . . . . . . 4581 1 461 . 1 1 65 65 GLU H H 1 7.69 0.01 . 1 . . . . . . . . 4581 1 462 . 1 1 65 65 GLU HA H 1 3.98 0.01 . 1 . . . . . . . . 4581 1 463 . 1 1 65 65 GLU HB2 H 1 1.85 0.01 . 2 . . . . . . . . 4581 1 464 . 1 1 65 65 GLU HG2 H 1 2.08 0.01 . 2 . . . . . . . . 4581 1 465 . 1 1 65 65 GLU HG3 H 1 2.41 0.01 . 2 . . . . . . . . 4581 1 466 . 1 1 65 65 GLU N N 15 120.1 0.1 . 1 . . . . . . . . 4581 1 467 . 1 1 66 66 PHE H H 1 8.85 0.01 . 1 . . . . . . . . 4581 1 468 . 1 1 66 66 PHE HA H 1 4.035 0.01 . 1 . . . . . . . . 4581 1 469 . 1 1 66 66 PHE HB2 H 1 3.17 0.01 . 2 . . . . . . . . 4581 1 470 . 1 1 66 66 PHE HB3 H 1 3.27 0.01 . 2 . . . . . . . . 4581 1 471 . 1 1 66 66 PHE HD1 H 1 7.03 0.01 . 3 . . . . . . . . 4581 1 472 . 1 1 66 66 PHE HE1 H 1 7.12 0.01 . 3 . . . . . . . . 4581 1 473 . 1 1 66 66 PHE HZ H 1 7.35 0.01 . 1 . . . . . . . . 4581 1 474 . 1 1 66 66 PHE N N 15 120.8 0.1 . 1 . . . . . . . . 4581 1 475 . 1 1 67 67 GLN H H 1 7.87 0.01 . 1 . . . . . . . . 4581 1 476 . 1 1 67 67 GLN HA H 1 3.22 0.01 . 1 . . . . . . . . 4581 1 477 . 1 1 67 67 GLN HB2 H 1 1.70 0.01 . 2 . . . . . . . . 4581 1 478 . 1 1 67 67 GLN HB3 H 1 1.95 0.01 . 2 . . . . . . . . 4581 1 479 . 1 1 67 67 GLN HG2 H 1 2.10 0.01 . 2 . . . . . . . . 4581 1 480 . 1 1 67 67 GLN HG3 H 1 2.30 0.01 . 2 . . . . . . . . 4581 1 481 . 1 1 67 67 GLN N N 15 117.4 0.1 . 1 . . . . . . . . 4581 1 482 . 1 1 68 68 VAL H H 1 7.10 0.01 . 1 . . . . . . . . 4581 1 483 . 1 1 68 68 VAL HA H 1 3.49 0.01 . 1 . . . . . . . . 4581 1 484 . 1 1 68 68 VAL HB H 1 2.10 0.01 . 1 . . . . . . . . 4581 1 485 . 1 1 68 68 VAL HG11 H 1 0.98 0.01 . 1 . . . . . . . . 4581 1 486 . 1 1 68 68 VAL HG12 H 1 0.98 0.01 . 1 . . . . . . . . 4581 1 487 . 1 1 68 68 VAL HG13 H 1 0.98 0.01 . 1 . . . . . . . . 4581 1 488 . 1 1 68 68 VAL HG21 H 1 0.84 0.01 . 1 . . . . . . . . 4581 1 489 . 1 1 68 68 VAL HG22 H 1 0.84 0.01 . 1 . . . . . . . . 4581 1 490 . 1 1 68 68 VAL HG23 H 1 0.84 0.01 . 1 . . . . . . . . 4581 1 491 . 1 1 68 68 VAL N N 15 118.7 0.1 . 1 . . . . . . . . 4581 1 492 . 1 1 69 69 LEU H H 1 7.13 0.01 . 1 . . . . . . . . 4581 1 493 . 1 1 69 69 LEU HA H 1 3.73 0.01 . 1 . . . . . . . . 4581 1 494 . 1 1 69 69 LEU HB2 H 1 1.20 0.01 . 2 . . . . . . . . 4581 1 495 . 1 1 69 69 LEU HB3 H 1 1.34 0.01 . 2 . . . . . . . . 4581 1 496 . 1 1 69 69 LEU HG H 1 1.38 0.01 . 1 . . . . . . . . 4581 1 497 . 1 1 69 69 LEU HD11 H 1 0.80 0.01 . 2 . . . . . . . . 4581 1 498 . 1 1 69 69 LEU HD12 H 1 0.80 0.01 . 2 . . . . . . . . 4581 1 499 . 1 1 69 69 LEU HD13 H 1 0.80 0.01 . 2 . . . . . . . . 4581 1 500 . 1 1 69 69 LEU HD21 H 1 0.70 0.01 . 2 . . . . . . . . 4581 1 501 . 1 1 69 69 LEU HD22 H 1 0.70 0.01 . 2 . . . . . . . . 4581 1 502 . 1 1 69 69 LEU HD23 H 1 0.70 0.01 . 2 . . . . . . . . 4581 1 503 . 1 1 69 69 LEU N N 15 120.5 0.1 . 1 . . . . . . . . 4581 1 504 . 1 1 70 70 VAL H H 1 7.64 0.01 . 1 . . . . . . . . 4581 1 505 . 1 1 70 70 VAL HA H 1 3.12 0.01 . 1 . . . . . . . . 4581 1 506 . 1 1 70 70 VAL HB H 1 1.85 0.01 . 1 . . . . . . . . 4581 1 507 . 1 1 70 70 VAL HG11 H 1 0.51 0.01 . 1 . . . . . . . . 4581 1 508 . 1 1 70 70 VAL HG12 H 1 0.51 0.01 . 1 . . . . . . . . 4581 1 509 . 1 1 70 70 VAL HG13 H 1 0.51 0.01 . 1 . . . . . . . . 4581 1 510 . 1 1 70 70 VAL HG21 H 1 0.68 0.01 . 1 . . . . . . . . 4581 1 511 . 1 1 70 70 VAL HG22 H 1 0.68 0.01 . 1 . . . . . . . . 4581 1 512 . 1 1 70 70 VAL HG23 H 1 0.68 0.01 . 1 . . . . . . . . 4581 1 513 . 1 1 70 70 VAL N N 15 116.3 0.1 . 1 . . . . . . . . 4581 1 514 . 1 1 71 71 LYS H H 1 7.44 0.01 . 1 . . . . . . . . 4581 1 515 . 1 1 71 71 LYS HA H 1 3.93 0.01 . 1 . . . . . . . . 4581 1 516 . 1 1 71 71 LYS HB2 H 1 1.75 0.01 . 2 . . . . . . . . 4581 1 517 . 1 1 71 71 LYS HB3 H 1 1.80 0.01 . 2 . . . . . . . . 4581 1 518 . 1 1 71 71 LYS HG2 H 1 1.44 0.01 . 2 . . . . . . . . 4581 1 519 . 1 1 71 71 LYS HD2 H 1 1.59 0.01 . 2 . . . . . . . . 4581 1 520 . 1 1 71 71 LYS HE2 H 1 2.91 0.01 . 2 . . . . . . . . 4581 1 521 . 1 1 71 71 LYS N N 15 119.5 0.1 . 1 . . . . . . . . 4581 1 522 . 1 1 72 72 LYS H H 1 7.51 0.01 . 1 . . . . . . . . 4581 1 523 . 1 1 72 72 LYS HA H 1 4.15 0.01 . 1 . . . . . . . . 4581 1 524 . 1 1 72 72 LYS HB2 H 1 1.85 0.01 . 2 . . . . . . . . 4581 1 525 . 1 1 72 72 LYS HG2 H 1 1.49 0.01 . 2 . . . . . . . . 4581 1 526 . 1 1 72 72 LYS HD2 H 1 1.46 0.01 . 2 . . . . . . . . 4581 1 527 . 1 1 72 72 LYS HE2 H 1 2.72 0.01 . 2 . . . . . . . . 4581 1 528 . 1 1 73 73 ILE H H 1 7.54 0.01 . 1 . . . . . . . . 4581 1 529 . 1 1 73 73 ILE HA H 1 4.18 0.01 . 1 . . . . . . . . 4581 1 530 . 1 1 73 73 ILE HB H 1 1.85 0.01 . 1 . . . . . . . . 4581 1 531 . 1 1 73 73 ILE HG12 H 1 0.92 0.01 . 2 . . . . . . . . 4581 1 532 . 1 1 73 73 ILE HG13 H 1 1.23 0.01 . 2 . . . . . . . . 4581 1 533 . 1 1 73 73 ILE HG21 H 1 0.64 0.01 . 1 . . . . . . . . 4581 1 534 . 1 1 73 73 ILE HG22 H 1 0.64 0.01 . 1 . . . . . . . . 4581 1 535 . 1 1 73 73 ILE HG23 H 1 0.64 0.01 . 1 . . . . . . . . 4581 1 536 . 1 1 73 73 ILE HD11 H 1 0.30 0.01 . 1 . . . . . . . . 4581 1 537 . 1 1 73 73 ILE HD12 H 1 0.30 0.01 . 1 . . . . . . . . 4581 1 538 . 1 1 73 73 ILE HD13 H 1 0.30 0.01 . 1 . . . . . . . . 4581 1 539 . 1 1 73 73 ILE N N 15 113.0 0.1 . 1 . . . . . . . . 4581 1 540 . 1 1 74 74 SER H H 1 7.64 0.01 . 1 . . . . . . . . 4581 1 541 . 1 1 74 74 SER HA H 1 4.44 0.01 . 1 . . . . . . . . 4581 1 542 . 1 1 74 74 SER HB2 H 1 4.13 0.01 . 2 . . . . . . . . 4581 1 543 . 1 1 74 74 SER HB3 H 1 4.83 0.01 . 2 . . . . . . . . 4581 1 544 . 1 1 74 74 SER N N 15 117.0 0.1 . 1 . . . . . . . . 4581 1 545 . 1 1 75 75 GLN H H 1 7.60 0.01 . 1 . . . . . . . . 4581 1 546 . 1 1 75 75 GLN HA H 1 4.14 0.01 . 1 . . . . . . . . 4581 1 547 . 1 1 75 75 GLN HB2 H 1 1.93 0.01 . 2 . . . . . . . . 4581 1 548 . 1 1 75 75 GLN HB3 H 1 2.10 0.01 . 2 . . . . . . . . 4581 1 549 . 1 1 75 75 GLN HG2 H 1 2.31 0.01 . 2 . . . . . . . . 4581 1 550 . 1 1 75 75 GLN N N 15 126.4 0.1 . 1 . . . . . . . . 4581 1 stop_ save_