data_5508 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5508 _Entry.Title ; Native State Hydrogen Exchange Study of Suppressor and Pathogenic Variants of Transthyretin ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2002-08-25 _Entry.Accession_date 2002-08-26 _Entry.Last_release_date 2003-01-27 _Entry.Original_release_date 2003-01-27 _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 Kai Liu . . . 5508 2 Jeffery Kelly . . . 5508 3 David Wemmer . . . 5508 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5508 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 128 5508 '15N chemical shifts' 121 5508 '1H chemical shifts' 121 5508 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2003-01-27 2002-08-25 original author . 5508 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 5507 'wild type transthyretin' 5508 BMRB 5509 'mutant v30m' 5508 BMRB 5510 'mutant l55p' 5508 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5508 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 22090787 _Citation.DOI . _Citation.PubMed_ID 12095258 _Citation.Full_citation . _Citation.Title ; Native State Hydrogen Exchange Study of Suppressor and Pathogenic Variants of Transthyretin ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full . _Citation.Journal_volume 320 _Citation.Journal_issue 4 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 821 _Citation.Page_last 832 _Citation.Year 2002 _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 Kai Liu . . . 5508 1 2 Jeffery Kelly . . . 5508 1 3 David Wemmer . . . 5508 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID amyloid 5508 1 'hydrogen exchange' 5508 1 'NMR spectroscopy' 5508 1 'protection factor' 5508 1 transthyretin 5508 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_TTR _Assembly.Sf_category assembly _Assembly.Sf_framecode system_TTR _Assembly.Entry_ID 5508 _Assembly.ID 1 _Assembly.Name Transthyretin _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'all free' _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 tetramer 5508 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 'TTR subunit 1' 1 $TTR_T119M . . . native . . 1 . . 5508 1 2 'TTR subunit 2' 1 $TTR_T119M . . . native . . 1 . . 5508 1 3 'TTR subunit 3' 1 $TTR_T119M . . . native . . 1 . . 5508 1 4 'TTR subunit 4' 1 $TTR_T119M . . . native . . 1 . . 5508 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1F41 . . . . . . 5508 1 yes PDB 1F86 . . . . . . 5508 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID Transthyretin system 5508 1 TTR abbreviation 5508 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_TTR_T119M _Entity.Sf_category entity _Entity.Sf_framecode TTR_T119M _Entity.Entry_ID 5508 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Transthyretin _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 ; MGPTGTGESKCPLMVKVLDA VRGSPAINVAVHVFRKAADD TWEPFASGKTSESGELHGLT TEEEFVEGIYKVEIDTKSYW KALGISPFHEHAEVVFTAND SGPRRYTIAALLSPYSYSTM AVVTNPKE ; _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 128 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all free' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 2476 . "pancreatic polypeptide" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 2 no BMRB 5507 . TTR . . . . . 100.00 128 99.22 99.22 3.73e-87 . . . . 5508 1 3 no BMRB 5509 . TTR_v30m . . . . . 100.00 128 98.44 99.22 1.28e-86 . . . . 5508 1 4 no BMRB 5510 . TTR_L55P . . . . . 100.00 128 98.44 98.44 9.04e-86 . . . . 5508 1 5 no PDB 1BM7 . "Human Transthyretin (Prealbumin) Complex With Flufenamic Acid (2-[[3-(Trifluoromethyl)phenyl]amino] Benzoic Acid)" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 6 no PDB 1BMZ . "Human Transthyretin (Prealbumin)" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 7 no PDB 1BZ8 . "Transthyretin (Del Val122)" . . . . . 99.22 126 98.43 98.43 1.29e-83 . . . . 5508 1 8 no PDB 1BZD . "Tertiary Structures Of Three Amyloidogenic Transthyretin Variants And Implications For Amyloid Fibril Formation" . . . . . 99.22 127 98.43 98.43 2.66e-85 . . . . 5508 1 9 no PDB 1BZE . "Tertiary Structures Of Three Amyloidogenic Transthyretin Variants And Implications For Amyloid Fibril Formation" . . . . . 99.22 127 100.00 100.00 4.49e-87 . . . . 5508 1 10 no PDB 1DVQ . "Crystal Structure Of Human Transthyretin" . . . . . 96.88 124 98.39 99.19 1.69e-83 . . . . 5508 1 11 no PDB 1DVS . "Crystal Structure Of Human Transthyretin In Complex With Resveratrol" . . . . . 96.88 124 98.39 99.19 1.69e-83 . . . . 5508 1 12 no PDB 1DVT . "Crystal Structure Of Human Transthyretin In Complex With Flurbiprofen" . . . . . 96.88 124 98.39 99.19 1.69e-83 . . . . 5508 1 13 no PDB 1DVU . "Crystal Structure Of Human Transthyretin In Complex With Dibenzofuran- 4,6-Dicarboxylic Acid" . . . . . 96.88 124 98.39 99.19 1.69e-83 . . . . 5508 1 14 no PDB 1DVX . "Crystal Structure Of Human Transthyretin In Complex With Diclofenac" . . . . . 96.88 124 98.39 99.19 1.69e-83 . . . . 5508 1 15 no PDB 1DVY . "Crystal Structure Of Transthyretin In Complex With N-(M- Trifluoromethylphenyl) Phenoxazine-4,6-Dicarboxylic Acid" . . . . . 96.88 124 98.39 99.19 1.69e-83 . . . . 5508 1 16 no PDB 1DVZ . "Crystal Structure Of Human Transthyretin In Complex With O- Trifluoromethylphenyl Anthranilic Acid" . . . . . 96.88 124 98.39 99.19 1.69e-83 . . . . 5508 1 17 no PDB 1E3F . "Structure Of Human Transthyretin Complexed With Bromophenols: A New Mode Of Binding" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 18 no PDB 1E4H . "Structure Of Human Transthyretin Complexed With Bromophenols: A New Mode Of Binding" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 19 no PDB 1E5A . "Structure Of Human Transthyretin Complexed With Bromophenols: A New Mode Of Binding" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 20 no PDB 1ETA . "The X-Ray Crystal Structure Refinements Of Normal Human Transthyretin And The Amyloidogenic Val 30-->met Variant To 1.7 Angstro" . . . . . 100.00 128 98.44 98.44 2.17e-84 . . . . 5508 1 21 no PDB 1ETB . "The X-Ray Crystal Structure Refinements Of Normal Human Transthyretin And The Amyloidogenic Val 30-->met Variant To 1.7 Angstro" . . . . . 99.22 127 98.43 98.43 1.98e-85 . . . . 5508 1 22 no PDB 1F41 . "Crystal Structure Of Human Transthyretin At 1.5a Resolution" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 23 no PDB 1F86 . "Transthyretin Thr119met Protein Stabilisation" . . . . . 89.84 115 100.00 100.00 5.31e-78 . . . . 5508 1 24 no PDB 1FH2 . "Transthyretin Stability As A Key Factor In Amyloidogenesis" . . . . . 90.63 116 98.28 98.28 1.63e-73 . . . . 5508 1 25 no PDB 1FHN . "Transthyretin Stability As A Key Factor In Amyloidogenesis" . . . . . 99.22 127 100.00 100.00 4.49e-87 . . . . 5508 1 26 no PDB 1GKO . "An Engineered Transthyretin Monomer That Is Non-Amyloidogenic - Unless Partially Denatured" . . . . . 99.22 127 97.64 98.43 5.02e-85 . . . . 5508 1 27 no PDB 1ICT . "Monoclinic Form Of Human Transthyretin Complexed With Thyroxine (T4)" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 28 no PDB 1III . "Crystal Structure Of The Transthyretin Mutant Ttr Y114c-data Collected At Room Temperature" . . . . . 99.22 127 98.43 98.43 9.45e-85 . . . . 5508 1 29 no PDB 1IIK . "Crystal Structure Of The Transthyretin Mutant Ttr Y114c-Data Collected At Cryo Temperature" . . . . . 99.22 127 98.43 98.43 9.45e-85 . . . . 5508 1 30 no PDB 1IJN . "Crystal Structure Of The Transthyretin Mutant Ttr C10aY114C" . . . . . 99.22 127 97.64 97.64 2.39e-83 . . . . 5508 1 31 no PDB 1QAB . "The Structure Of Human Retinol Binding Protein With Its Carrier Protein Transthyretin Reveals Interaction With The Carboxy Term" . . . . . 99.22 127 98.43 99.21 7.26e-86 . . . . 5508 1 32 no PDB 1QWH . "A Covalent Dimer Of Transthyretin That Affects The Amyloid Pathway" . . . . . 91.41 117 99.15 99.15 9.44e-78 . . . . 5508 1 33 no PDB 1RLB . "Retinol Binding Protein Complexed With Transthyretin" . . . . . 99.22 127 98.43 99.21 7.26e-86 . . . . 5508 1 34 no PDB 1SOK . "Crystal Structure Of The Transthyretin Mutant A108yL110E SOLVED IN Space Group P21212" . . . . . 99.22 127 97.64 97.64 7.20e-84 . . . . 5508 1 35 no PDB 1SOQ . "Crystal Structure Of The Transthyretin Mutant A108yL110E SOLVED IN Space Group C2" . . . . . 99.22 127 97.64 97.64 7.20e-84 . . . . 5508 1 36 no PDB 1THA . "Mechanism Of Molecular Recognition. Structural Aspects Of 3, 3'-Diiodo-L-Thyronine Binding To Human Serum Transthyretin" . . . . . 99.22 127 98.43 99.21 7.26e-86 . . . . 5508 1 37 no PDB 1THC . "Crystal Structure Determination At 2.3a Of Human Transthyretin-3',5'- Dibromo-2',4,4',6-Tetra-Hydroxyaurone Complex" . . . . . 99.22 127 98.43 99.21 7.26e-86 . . . . 5508 1 38 no PDB 1TLM . "Structural Aspects Of Inotropic Bipyridine Binding: Crystal Structure Determination To 1.9 Angstroms Of The Human Serum Transth" . . . . . 99.22 127 98.43 99.21 7.26e-86 . . . . 5508 1 39 no PDB 1TSH . "Tertiary Structures Of Three Amyloidogenic Transthyretin Variants And Implications For Amyloid Fibril Formation" . . . . . 99.22 127 98.43 98.43 2.34e-85 . . . . 5508 1 40 no PDB 1TT6 . "The Orthorhombic Crystal Structure Of Transthyretin In Complex With Diethylstilbestrol" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 41 no PDB 1TTA . "The X-Ray Crystal Structure Refinements Of Normal Human Transthyretin And The Amyloidogenic Val30met Variant To 1.7 Angstroms R" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 42 no PDB 1TTB . "The X-Ray Crystal Structure Refinements Of Normal Human Transthyretin And The Amyloidogenic Val30met Variant To 1.7 Angstroms R" . . . . . 99.22 127 98.43 98.43 1.98e-85 . . . . 5508 1 43 no PDB 1TTC . "The X-Ray Crystal Structure Refinements Of Normal Human Transthyretin And The Amyloidogenic Val30met Variant To 1.7 Angstroms R" . . . . . 99.22 127 98.43 99.21 1.10e-85 . . . . 5508 1 44 no PDB 1TTR . "Transthyretin-V122I CARDIOMYOPATHIC MUTANT" . . . . . 99.22 127 98.43 99.21 5.97e-86 . . . . 5508 1 45 no PDB 1TYR . "Transthyretin Complex With Retinoic Acid" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 46 no PDB 1TZ8 . "The Monoclinic Crystal Struture Of Transthyretin In Complex With Diethylstilbestrol" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 47 no PDB 1U21 . "Transthyretin With Tethered Inhibitor On One Monomer." . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 48 no PDB 1X7S . "The X-Ray Crystallographic Structure Of The Amyloidogenic Variant Ttr Tyr78phe" . . . . . 99.22 127 98.43 99.21 1.53e-85 . . . . 5508 1 49 no PDB 1X7T . "Structure Of Ttr R104h: A Non-Amyloidogenic Variant With Protective Clinical Effects" . . . . . 99.22 127 98.43 98.43 5.36e-85 . . . . 5508 1 50 no PDB 1Y1D . "Crystal Structure Of Transthyretin In Complex With Iododiflunisal" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 51 no PDB 1Z7J . "Human Transthyretin (Also Called Prealbumin) Complex With 3, 3',5,5'- Tetraiodothyroacetic Acid (T4ac)" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 52 no PDB 1ZCR . "Crystal Structure Of Human Transthyretin With Bound Iodide" . . . . . 100.00 128 99.22 99.22 3.73e-87 . . . . 5508 1 53 no PDB 1ZD6 . "Crystal Structure Of Human Transthyretin With Bound Chloride" . . . . . 100.00 128 99.22 99.22 3.73e-87 . . . . 5508 1 54 no PDB 2B14 . "The Crystal Structure Of 2,4-Dinitrophenol In Complex With The Amyloidogenic Variant Transthyretin Leu 55 Pro" . . . . . 99.22 127 98.43 98.43 1.02e-84 . . . . 5508 1 55 no PDB 2B15 . "The Crystal Structure Of 2,4-Dinitrophenol In Complex With Human Transthyretin" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 56 no PDB 2B16 . "The Crystal Structure Of 2,4-Dinitrophenol In Complex With The Amyloidogenic Variant Transthyretin Tyr78phe" . . . . . 99.22 127 98.43 99.21 1.53e-85 . . . . 5508 1 57 no PDB 2B77 . "Human Transthyretin (ttr) Complexed With Diflunisal Analogues- Ttr.2', 4'-dichloro-4-hydroxy-1,1'-biphenyl-3-carboxylic Acid" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 58 no PDB 2B9A . "Human Transthyretin (ttr) Complexed With Diflunisal Analogues- Ttr.3', 5'-difluorobiphenyl-4-carboxylic Acid" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 59 no PDB 2F7I . "Human Transthyretin (Ttr) Complexed With Diflunisal Analogues- Ttr. 2',6'-Difluorobiphenyl-4-Carboxylic Acid" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 60 no PDB 2F8I . "Human Transthyretin (Ttr) Complexed With Benzoxazole" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 61 no PDB 2FBR . "Human Transthyretin (Ttr) Complexed With Bivalant Amyloid Inhibitor (4 Carbon Linker)" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 62 no PDB 2FLM . "Human Transthyretin (Ttr) Complexed With Bivalant Amyloid Inhibitor (6 Carbon Linker)" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 63 no PDB 2G3X . "Crystal Structure Of Transthyretin Mutant I84s At Acidic Ph" . . . . . 99.22 127 98.43 98.43 4.26e-85 . . . . 5508 1 64 no PDB 2G3Z . "Crystal Structure Of Transthyretin Mutant I84a At Low Ph" . . . . . 99.22 127 98.43 98.43 2.94e-85 . . . . 5508 1 65 no PDB 2G4E . "Crystal Structure Of Transthyretin Mutant I84a At Neutral Ph" . . . . . 99.22 127 98.43 98.43 2.94e-85 . . . . 5508 1 66 no PDB 2G4G . "Crystal Structure Of Human Transthyretin At Ph 4.6" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 67 no PDB 2G5U . "Human Transthyretin (Ttr) Complexed With Hydroxylated Polychlorinated Biphenyl-4,4'-Dihydroxy-3,3',5,5'-Tetrachlorobiphenyl" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 68 no PDB 2G9K . "Human Transthyretin (Ttr) Complexed With Hydroxylated Polychlorinated Biphenyl-4-Hydroxy-2',3,3',4',5-Pentachlorobiphenyl" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 69 no PDB 2GAB . "Human Transthyretin (Ttr) Complexed With Hydroxylated Polychlorinated Biphenyl-4-Hydroxy-3,3',5,4'-Tetrachlorobiphenyl" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 70 no PDB 2H4E . "Crystal Structure Of Cys10 Sulfonated Transthyretin" . . . . . 99.22 127 98.43 98.43 1.74e-84 . . . . 5508 1 71 no PDB 2NOY . "Crystal Structure Of Transthyretin Mutant I84s At Ph 7.5" . . . . . 99.22 127 98.43 98.43 4.26e-85 . . . . 5508 1 72 no PDB 2PAB . "Structure Of Prealbumin, Secondary, Tertiary And Quaternary Interactions Determined By Fourier Refinement At 1.8 Angstroms" . . . . . 99.22 127 98.43 99.21 7.26e-86 . . . . 5508 1 73 no PDB 2QGB . "Human Transthyretin (Ttr) In Apo-Form" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 74 no PDB 2QGC . "Human Transthyretin (Ttr) Complexed With 2-(3,5-Dimethyl-4- Hydroxyphenyl)benzoxazole" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 75 no PDB 2QGD . "Human Transthyretin (Ttr) Complexed With 2-(3,5-Dibromo-4- Hydroxyphenyl)benzoxazole" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 76 no PDB 2QGE . "Human Transthyretin (Ttr) Complexed With 2-(3,5-Dimethylphenyl) Benzoxazole" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 77 no PDB 2ROX . "Transthyretin (Also Called Prealbumin) Complex With Thyroxine (T4)" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 78 no PDB 2ROY . "Transthyretin (Also Called Prealbumin) Complex With 3',5'-Dinitro-N- Acetyl-L-Thyronine" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 79 no PDB 2TRH . "Tertiary Structures Of Three Amyloidogenic Transthyretin Variants And Implications For Amyloid Fibril Formation" . . . . . 99.22 127 98.43 98.43 2.17e-84 . . . . 5508 1 80 no PDB 2TRY . "Tertiary Structures Of Three Amyloidogenic Transthyretin Variants And Implications For Amyloid Fibril Formation" . . . . . 99.22 127 98.43 98.43 4.21e-85 . . . . 5508 1 81 no PDB 2WQA . "Complex Of Ttr And Rbp4 And Oleic Acid" . . . . . 99.22 129 99.21 99.21 4.12e-86 . . . . 5508 1 82 no PDB 3A4D . "Crystal Structure Of Human Transthyretin (Wild-Type)" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 83 no PDB 3A4E . "Crystal Structure Of Human Transthyretin (e54g)" . . . . . 99.22 127 98.43 98.43 6.59e-85 . . . . 5508 1 84 no PDB 3A4F . "Crystal Structure Of Human Transthyretin (e54k)" . . . . . 99.22 127 98.43 99.21 1.65e-85 . . . . 5508 1 85 no PDB 3B56 . "Crystal Structure Of Transthyretin In Complex With 3,5- Diiodosalicylic Acid" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 86 no PDB 3BSZ . "Crystal Structure Of The Transthyretin-retinol Binding Protein-fab Complex" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 87 no PDB 3BT0 . "Crystal Structure Of Transthyretin Variant V20s" . . . . . 99.22 127 98.43 98.43 3.21e-85 . . . . 5508 1 88 no PDB 3CBR . "Crystal Structure Of Human Transthyretin (Ttr) At Ph3.5" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 89 no PDB 3CFM . "Crystal Structure Of The Apo Form Of Human Wild-Type Transthyretin" . . . . . 92.19 118 99.15 99.15 2.69e-79 . . . . 5508 1 90 no PDB 3CFN . "Crystal Structure Of Human Transthyretin In Complex With 1-Anilino-8- Naphthalene Sulfonate" . . . . . 92.19 118 99.15 99.15 2.69e-79 . . . . 5508 1 91 no PDB 3CFQ . "Crystal Structure Of Human Wild-Type Transthyretin In Complex With Diclofenac" . . . . . 92.19 118 99.15 99.15 2.69e-79 . . . . 5508 1 92 no PDB 3CFT . "Crystal Structure Of Human Transthyretin In Complex With 1- Amino-5-Naphthalene Sulfonate" . . . . . 92.19 118 99.15 99.15 2.69e-79 . . . . 5508 1 93 no PDB 3CN0 . "Human Transthyretin (Ttr) In Complex With 3,5-Dimethyl-4- Hydroxystilbene" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 94 no PDB 3CN1 . "Human Transthyretin (Ttr) In Complex With 3,5-Dibromo-4- Hydroxystilbene" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 95 no PDB 3CN2 . "Human Transthyretin (Ttr) In Complex With 3,5-Dibromo-4- Hydroxybiphenyl" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 96 no PDB 3CN3 . "Human Transthyretin (Ttr) In Complex With 1,3-Dibromo-2- Hydroxy-5-Phenoxybenzene" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 97 no PDB 3CN4 . "Human Transthyretin (Ttr) In Complex With N-(3,5-Dibromo-4- Hydroxyphenyl)benzamide" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 98 no PDB 3CXF . "Crystal Structure Of Transthyretin Variant Y114h" . . . . . 99.22 127 98.43 99.21 2.47e-85 . . . . 5508 1 99 no PDB 3D2T . "Human Transthyretin (ttr) Complexed With Diflunisal" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 100 no PDB 3D7P . "Crystal Structure Of Human Transthyretin (Ttr) At Ph 4.0" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 101 no PDB 3DGD . "Crystal Structure Of The F87mL110M MUTANT OF HUMAN TRANSTHYRETIN AT Ph 4.6" . . . . . 99.22 127 97.64 98.43 5.02e-85 . . . . 5508 1 102 no PDB 3DID . "Crystal Structure Of The F87mL110M MUTANT OF HUMAN TRANSTHYRETIN AT Ph 4.6 Soaked" . . . . . 99.22 127 97.64 98.43 5.02e-85 . . . . 5508 1 103 no PDB 3DJR . "Crystal Structure Of Transthyretin Variant L58h At Neutral Ph" . . . . . 99.22 127 98.43 98.43 8.66e-85 . . . . 5508 1 104 no PDB 3DJS . "Crystal Structure Of Transthyretin Variant L58h At Acidic Ph" . . . . . 99.22 127 98.43 98.43 8.66e-85 . . . . 5508 1 105 no PDB 3DJT . "Crystal Structure Of Transthyretin Variant V30m At Acidic Ph" . . . . . 99.22 127 98.43 99.21 1.10e-85 . . . . 5508 1 106 no PDB 3DJZ . "Crystal Structure Of Transthyretin Variant L55p At Neutral Ph" . . . . . 99.22 127 98.43 98.43 1.02e-84 . . . . 5508 1 107 no PDB 3DK0 . "Crystal Structure Of Transthyretin Variant L55p At Acidic Ph" . . . . . 99.22 127 98.43 98.43 1.02e-84 . . . . 5508 1 108 no PDB 3DK2 . "Crystal Structure Of Transthyretin Variant Y114h At Acidic Ph" . . . . . 99.22 127 98.43 99.21 2.47e-85 . . . . 5508 1 109 no PDB 3DO4 . "Crystal Structure Of Transthyretin Variant T60a At Acidic Ph" . . . . . 99.22 127 98.43 98.43 2.34e-85 . . . . 5508 1 110 no PDB 3ESN . "Human Transthyretin (Ttr) Complexed With N-(3,5-Dibromo-4- Hydroxyphenyl)-2,6-Dimethylbenzamide" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 111 no PDB 3ESO . "Human Transthyretin (Ttr) Complexed With N-(3,5-Dibromo-4- Hydroxyphenyl)-2,5-Dichlorobenzamide" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 112 no PDB 3ESP . "Human Transthyretin (Ttr) Complexed With N-(3,5-Dibromo-4- Hydroxyphenyl)-3,5-Dimethyl-4-Hydroxybenzamide" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 113 no PDB 3FC8 . "Crystal Structure Of Transthyretin In Complex With Iododiflunisal-Betaalaome" . . . . . 96.88 124 99.19 99.19 9.90e-84 . . . . 5508 1 114 no PDB 3FCB . "Crystal Structure Of Transthyretin In Complex With Iododiflunisal-Betaalaoh" . . . . . 96.88 124 99.19 99.19 9.90e-84 . . . . 5508 1 115 no PDB 3GLZ . "Human Transthyretin (Ttr) Complexed With(E)-3-(2- (Trifluoromethyl)benzylideneaminooxy)propanoic Acid (Inhibitor 11)" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 116 no PDB 3GPS . "Crystal Structure Of The F87mL110M MUTANT OF HUMAN TRANSTHYRETIN AT Ph 5.5" . . . . . 99.22 127 97.64 98.43 5.02e-85 . . . . 5508 1 117 no PDB 3GRB . "Crystal Structure Of The F87mL110M MUTANT OF HUMAN TRANSTHYRETIN AT Ph 6.5" . . . . . 99.22 127 97.64 98.43 5.02e-85 . . . . 5508 1 118 no PDB 3GRG . "Crystal Structure Of The F87mL110M MUTANT OF HUMAN TRANSTHYRETIN AT Ph 7.5" . . . . . 99.22 127 97.64 98.43 5.02e-85 . . . . 5508 1 119 no PDB 3GS0 . "Human Transthyretin (Ttr) Complexed With (S)-3-(9h-Fluoren- 9-Ylideneaminooxy)-2-Methylpropanoic Acid (Inhibitor 16)" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 120 no PDB 3GS4 . "Human Transthyretin (Ttr) Complexed With 3-(9h-Fluoren-9- Ylideneaminooxy)propanoic Acid (Inhibitor 15)" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 121 no PDB 3GS7 . "Human Transthyretin (Ttr) Complexed With (E)-3-(2- Methoxybenzylideneaminooxy)propanoic Acid (Inhibitor 13)" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 122 no PDB 3HJ0 . "Transthyretin In Complex With A Covalent Small Molecule Kinetic Stabilizer" . . . . . 99.22 127 98.43 98.43 1.74e-84 . . . . 5508 1 123 no PDB 3I9A . "Crystal Structure Of Human Transthyretin Variant A25t - #1" . . . . . 99.22 127 98.43 98.43 1.98e-85 . . . . 5508 1 124 no PDB 3I9I . "Crystal Structure Of Human Transthyretin Variant A25t - #2" . . . . . 90.63 116 98.28 98.28 3.95e-77 . . . . 5508 1 125 no PDB 3I9P . "Crystal Structure Of Human Transthyretin - Wild Type" . . . . . 90.63 116 99.14 99.14 8.38e-78 . . . . 5508 1 126 no PDB 3IMR . "Transthyretin In Complex With (E)-2,6-Dibromo-4-(2,6- Dichlorostyryl)phenol" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 127 no PDB 3IMS . "Transthyretin In Complex With 2,6-Dibromo-4-(2,6- Dichlorophenethyl)phenol" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 128 no PDB 3IMT . "Transthyretin In Complex With (E)-4-(4-Aminostyryl)-2,6- Dibromophenol" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 129 no PDB 3IMU . "Transthyretin In Complex With (E)-4-(3-Aminostyryl)-2,6- Dibromoaniline" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 130 no PDB 3IMV . "Transthyretin In Complex With (E)-4-(4-Aminostyryl)-2,6- Dibromoaniline" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 131 no PDB 3IMW . "Transthyretin In Complex With (E)-2,6-Dibromo-4-(2,6- Dimethoxystyryl)aniline" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 132 no PDB 3IPB . "Human Transthyretin (Ttr) Complexed With A Palindromic Bivalent Amyloid Inhibitor (11 Carbon Linker)." . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 133 no PDB 3IPE . "Human Transthyretin (Ttr) Complexed With A Palindromic Bivalent Amyloid Inhibitor (7 Carbon Linker)." . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 134 no PDB 3KGS . "V30m Mutant Human Transthyretin (Ttr) (Apov30m) Ph 7.5" . . . . . 99.22 127 98.43 99.21 1.10e-85 . . . . 5508 1 135 no PDB 3KGT . "V30m Mutant Human Transthyretin (Ttr) Complexed With Geniste (V30m:gen) Ph 7.5" . . . . . 99.22 127 98.43 99.21 1.10e-85 . . . . 5508 1 136 no PDB 3KGU . "Wild Type Human Transthyretin (Ttr) Complexed With Genistein (Ttrwt:gen) Ph 7.5" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 137 no PDB 3M1O . "Human Transthyretin (Ttr) Complexed With 2-((3,5-Dichloro-4- Hydroxyphenyl)amino)benzoic Acid" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 138 no PDB 3NEE . "Wild Type Human Transthyretin (Ttr) Complexed With Gc-1 (Ttrwt:gc-1)" . . . . . 90.63 116 99.14 99.14 8.38e-78 . . . . 5508 1 139 no PDB 3NEO . "Wild Type Human Transthyretin (Ttr) Complexed With Gc-24 (Ttrwt:gc-24)" . . . . . 90.63 116 99.14 99.14 8.38e-78 . . . . 5508 1 140 no PDB 3NES . "V30m Mutant Human Transthyretin (Ttr) Complexed With Gc-1 (V30m:gc-1)" . . . . . 90.63 116 98.28 99.14 2.42e-77 . . . . 5508 1 141 no PDB 3NEX . "V30m Mutant Human Transthyretin (Ttr) Complexed With Gc-24 (V30m:gc- 24)" . . . . . 90.63 116 98.28 99.14 2.42e-77 . . . . 5508 1 142 no PDB 3NG5 . "Crystal Structure Of V30m Transthyretin Complexed With (-)- Epigallocatechin Gallate (Egcg)" . . . . . 99.22 127 98.43 99.21 1.10e-85 . . . . 5508 1 143 no PDB 3OZK . "Crystal Structure Of Human Transthyretin Variant A25t In Complex With Thyroxine (T4)" . . . . . 99.22 127 98.43 98.43 1.98e-85 . . . . 5508 1 144 no PDB 3OZL . "Crystal Structure Of Human Transthyretin Variant A25t In Complex With Flufenamic Acid" . . . . . 99.22 127 98.43 98.43 1.98e-85 . . . . 5508 1 145 no PDB 3P3R . "Transthyretin In Complex With (3,4-Dihydroxy-5-Nitrophenyl)(2- Fluorophenyl)methanone" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 146 no PDB 3P3S . "Human Transthyretin (Ttr) Complexed With (Z)-5-(3,5-Dibromo-4- Hydroxybenzylidene)-Imino-1-Methylimidazolidin-4-One" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 147 no PDB 3P3T . "Human Transthyretin (Ttr) Complexed With 4-(3-(2-Flourophenoxy) Propyl)-3,5-Dimethyl-1h-Pyrazole" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 148 no PDB 3P3U . "Human Transthyretin (Ttr) Complexed With 5-(2-Ethoxyphenyl)-3- (Pyridin-4-Yl)-1,2,4-Oxadiazole" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 149 no PDB 3SSG . "Structure Of Transthyretin L55p In Complex With Zn" . . . . . 99.22 127 98.43 98.43 1.02e-84 . . . . 5508 1 150 no PDB 3TCT . "Structure Of Wild-Type Ttr In Complex With Tafamidis" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 151 no PDB 3TFB . "Transthyretin Natural Mutant A25t" . . . . . 90.63 116 98.28 98.28 3.95e-77 . . . . 5508 1 152 no PDB 3U2I . "X-Ray Crystal Structure Of Human Transthyretin At Room Temperature" . . . . . 90.63 117 99.14 99.14 5.97e-77 . . . . 5508 1 153 no PDB 3U2J . "Neutron Crystal Structure Of Human Transthyretin" . . . . . 90.63 117 99.14 99.14 5.97e-77 . . . . 5508 1 154 no PDB 3W3B . "Crystal Structure Of Wild-type Human Transthyretin" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 155 no PDB 4ABQ . "Crystal Structure Of Transthyretin In Complex With Ligand C-1" . . . . . 96.88 124 99.19 99.19 9.90e-84 . . . . 5508 1 156 no PDB 4ABU . "Crystal Structure Of Transthyretin In Complex With Ligand C-2" . . . . . 96.88 124 99.19 99.19 9.90e-84 . . . . 5508 1 157 no PDB 4ABV . "Crystal Structure Of Transthyretin In Complex With Ligand C-3" . . . . . 96.88 124 99.19 99.19 9.90e-84 . . . . 5508 1 158 no PDB 4ABW . "Crystal Structure Of Transthyretin In Complex With Ligand C-6" . . . . . 96.88 124 99.19 99.19 9.90e-84 . . . . 5508 1 159 no PDB 4AC2 . "Crystal Structure Of Transthyretin In Complex With Ligand C-7" . . . . . 96.88 124 99.19 99.19 9.90e-84 . . . . 5508 1 160 no PDB 4AC4 . "Crystal Structure Of Transthyretin In Complex With Ligand C-18" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 161 no PDB 4ACT . "Crystal Structure Of Transthyretin In Complex With Ligand C-17" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 162 no PDB 4ANK . "Crystallographic Study Of Novel Transthyretin Ligands Exhibiting Negative-Cooperativity Between Two T4 Binding Sites." . . . . . 99.22 147 99.21 99.21 3.73e-86 . . . . 5508 1 163 no PDB 4DER . "Crystal Structure Of The Wild Type Ttr Binding Apigenin (Ttrwt:api)" . . . . . 90.63 116 99.14 99.14 8.38e-78 . . . . 5508 1 164 no PDB 4DES . "Crystal Structure Of The Wild Type Ttr Binding Chrysin (Ttrwt:chr)" . . . . . 90.63 116 99.14 99.14 8.38e-78 . . . . 5508 1 165 no PDB 4DET . "Crystal Structure Of The Wild Type Ttr Binding Kaempferol (Ttrwt:kae)" . . . . . 90.63 116 99.14 99.14 8.38e-78 . . . . 5508 1 166 no PDB 4DEU . "Crystal Structure Of The Wild Type Ttr Binding Naringenin (Ttrwt:nar)" . . . . . 90.63 117 99.14 99.14 6.81e-78 . . . . 5508 1 167 no PDB 4DEW . "Crystal Structure Of The Wild Type Ttr Binding Luteolin (Ttrwt:lut)" . . . . . 99.22 147 99.21 99.21 3.73e-86 . . . . 5508 1 168 no PDB 4FI6 . "Kinetic Stabilization Of Transthyretin Through Covalent Modification Of K15 By 3-(5-(3,5-dichlorophenyl)-1,3,4-oxadiazol-2-yl)-" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 169 no PDB 4FI7 . "Kinetic Stabilization Of Transthyretin Through Covalent Modification Of K15 By 3-(5-(3,5-dichloro-4-hydroxyphenyl)-1,3,4-oxadia" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 170 no PDB 4FI8 . "Kinetic Stabilization Of Transthyretin Through Covalent Modification Of K15 By 4-bromo-3-(5-(3,5-dichloro-4-hydroxyphenyl)-1,3," . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 171 no PDB 4HIQ . "The Structure Of V122i Mutant Transthyretin In Complex With Ag10" . . . . . 99.22 127 98.43 99.21 5.97e-86 . . . . 5508 1 172 no PDB 4HIS . "The Structure Of V122i Mutant Transthyretin In Complex With Tafamidis" . . . . . 99.22 127 98.43 99.21 5.97e-86 . . . . 5508 1 173 no PDB 4HJS . "Kinetic Stabilization Of Transthyretin Through Covalent Modification Of K15 By (e)-n-(4-(4-hydroxy-3,5-dimethylstyryl)ethanesul" . . . . . 90.63 116 99.14 99.14 8.38e-78 . . . . 5508 1 174 no PDB 4HJT . "Kinetic Stabilization Of Transthyretin Through Covalent Modification Of K15 By (e)-n-(4-(4-hydroxy-3,5-dimethylstyryl)phenyl)pr" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 175 no PDB 4HJU . "Transthyretin In Complex With (e)-n-(3-(4-hydroxy-3,5-dimethylstyryl) Phenyl)acrylamide" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 176 no PDB 4I85 . "Crystal Structure Of Transthyretin In Complex With Chf5074 At Neutral Ph" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 177 no PDB 4I87 . "Crystal Structure Of Ttr Variant I84s In Complex With Chf5074 At Acidic Ph" . . . . . 99.22 127 98.43 98.43 4.26e-85 . . . . 5508 1 178 no PDB 4I89 . "Crystal Structure Of Transthyretin In Complex With Diflunisal At Acidic Ph" . . . . . 99.22 127 98.43 98.43 4.26e-85 . . . . 5508 1 179 no PDB 4IIZ . "Crystal Structure Of Wild-type Human Transthyretin In Complex With Lumiracoxib" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 180 no PDB 4IK6 . "Crystal Structure Of Human Transthyretin In Complex With Lumiracoxib" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 181 no PDB 4IK7 . "Crystal Structure Of Human Transthyretin In Complex With Indomethacin" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 182 no PDB 4IKI . "Crystal Structure Of Wild-type Human Transthyretin In Complex With Indomethacin" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 183 no PDB 4IKJ . "Crystal Structure Of Wild-type Human Transthyretin In Complex With Sulindac" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 184 no PDB 4IKK . "Crystal Structure Of Wild-type Human Transthyretin In Complex With Sulindac" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 185 no PDB 4IKL . "Crystal Structure Of Wild-type Human Transthyretin In Complex With Sulindac" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 186 no PDB 4KY2 . "Transthyretin In Complex With The Fluorescent Folding Sensor (e)-7- Hydroxy-3-(4-hydroxy-3,5-dimethylstyryl)-4-methyl-2h-chrome" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 187 no PDB 4L1S . "Covalent Modification Of Transthyretin K15 By Yielding The Fluorescent Conjugate (e)-3-(dimethylamino)-5-(4-hydroxy-3,5-dimethy" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 188 no PDB 4L1T . "Transthyretin In Complex With (e)-3-(dimethylamino)-5-(4-hydroxy-3,5- Dimethylstyryl)benzoic Acid" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 189 no PDB 4MAS . "High Resolution Structure Of Wild Type Human Transthyretin In Complex With 3,3',5,5'-tetrachloro-[1,1'-biphenyl]-4,4'diol" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 190 no PDB 4MRB . "Wild Type Human Transthyretin Ph 7.5" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 191 no PDB 4MRC . "Human Transthyretin Ser52pro Mutant" . . . . . 98.44 126 98.41 98.41 2.79e-84 . . . . 5508 1 192 no PDB 4N85 . "Crystal Structure Of Human Transthyretin" . . . . . 99.22 159 99.21 99.21 6.19e-86 . . . . 5508 1 193 no PDB 4N86 . "Crystal Structure Of Human Transthyretin Complexed With Glabridin" . . . . . 99.22 159 99.21 99.21 6.19e-86 . . . . 5508 1 194 no PDB 4N87 . "Crystal Structure Of V30m Mutant Human Transthyretin Complexed With Glabridin" . . . . . 99.22 159 98.43 99.21 1.67e-85 . . . . 5508 1 195 no PDB 4PM1 . "Human Transthyretin (ttr) Complexed With 16-alpha-bromo-estradiol" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 196 no PDB 4PME . "Human Transthyretin (ttr) Complexed With Ferulic Acid And Curcumin" . . . . . 92.19 118 99.15 99.15 2.41e-79 . . . . 5508 1 197 no PDB 4PMF . "Human Transthyretin (ttr) Complexed With Curcumin" . . . . . 91.41 117 99.15 99.15 1.31e-78 . . . . 5508 1 198 no PDB 4PVL . "X-ray Structure Of Human Transthyretin (ttr) At Room Temperature To 1.9a Resolution" . . . . . 100.00 130 99.22 99.22 5.11e-87 . . . . 5508 1 199 no PDB 4PVM . "Neutron Structure Of Human Transthyretin (ttr) At Room Temperature To 2.0a Resolution (laue)" . . . . . 100.00 130 99.22 99.22 5.11e-87 . . . . 5508 1 200 no PDB 4PVN . "Neutron Structure Of Human Transthyretin (ttr) At Room Temperature To 2.3a Resolution (monochromatic)" . . . . . 100.00 130 99.22 99.22 5.11e-87 . . . . 5508 1 201 no PDB 4PWE . "Crystal Structure Of V30m Mutant Human Transthyretin" . . . . . 99.22 159 98.43 99.21 1.67e-85 . . . . 5508 1 202 no PDB 4PWF . "Crystal Structure Of V30m Mutant Human Transthyretin Complexed With Ferulic Acid Phenethyl Ester" . . . . . 99.22 159 98.43 99.21 1.67e-85 . . . . 5508 1 203 no PDB 4PWG . "Crystal Structure Of V30m Mutant Human Transthyretin Complexed With Caffeic Acid Ethyl Ester" . . . . . 99.22 159 98.43 99.21 1.67e-85 . . . . 5508 1 204 no PDB 4PWH . "Crystal Structure Of V30m Mutant Human Transthyretin Complexed With Caffeic Acid 1,1-dimethylallyl Ester" . . . . . 99.22 159 98.43 99.21 1.67e-85 . . . . 5508 1 205 no PDB 4PWI . "Crystal Structure Of V30m Mutant Human Transthyretin Complexed With Rosmarinic Acid" . . . . . 99.22 159 98.43 99.21 1.67e-85 . . . . 5508 1 206 no PDB 4PWJ . "Crystal Structure Of V30m Mutant Human Transthyretin Complexed With Nordihydroguaiaretic Acid" . . . . . 99.22 159 98.43 99.21 1.67e-85 . . . . 5508 1 207 no PDB 4PWK . "Crystal Structure Of V30m Mutant Human Transthyretin Complexed With Dihydroguaiaretic Acid" . . . . . 99.22 159 98.43 99.21 1.67e-85 . . . . 5508 1 208 no PDB 4QRF . "Crystal Structure Of V30m Mutant Human Transthyretin Complexed With Caffeic Acid Phenethyl Ester" . . . . . 99.22 159 98.43 99.21 1.67e-85 . . . . 5508 1 209 no PDB 5TTR . "Leu 55 Pro Transthyretin Crystal Structure" . . . . . 99.22 127 98.43 98.43 1.02e-84 . . . . 5508 1 210 no DBJ BAA00059 . "prealbumin [Homo sapiens]" . . . . . 99.22 147 98.43 99.21 1.02e-85 . . . . 5508 1 211 no DBJ BAG34987 . "unnamed protein product [Homo sapiens]" . . . . . 99.22 147 99.21 99.21 3.73e-86 . . . . 5508 1 212 no EMBL CAA42087 . "transthyretin [Homo sapiens]" . . . . . 99.22 147 99.21 99.21 3.73e-86 . . . . 5508 1 213 no EMBL CAG33189 . "TTR [Homo sapiens]" . . . . . 99.22 147 98.43 99.21 1.02e-85 . . . . 5508 1 214 no GB AAA60011 . "prealbumin [Homo sapiens]" . . . . . 99.22 147 99.21 99.21 3.73e-86 . . . . 5508 1 215 no GB AAA60012 . "prealbumin [Homo sapiens]" . . . . . 99.22 147 99.21 99.21 3.73e-86 . . . . 5508 1 216 no GB AAA60013 . "prealbumin precursor, partial [Homo sapiens]" . . . . . 99.22 147 99.21 99.21 3.73e-86 . . . . 5508 1 217 no GB AAA60018 . "prealbumin [Homo sapiens]" . . . . . 99.22 147 98.43 99.21 1.02e-85 . . . . 5508 1 218 no GB AAA61181 . "transthyretin, partial [Homo sapiens]" . . . . . 91.41 117 99.15 99.15 9.44e-78 . . . . 5508 1 219 no PRF 0908191A . "prealbumin,thyroxine binding" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 220 no PRF 1008142A . "prealbumin variant" . . . . . 99.22 127 97.64 98.43 4.41e-84 . . . . 5508 1 221 no PRF 1101213A . "protein,amyloid fibril" . . . . . 99.22 127 99.21 99.21 4.40e-86 . . . . 5508 1 222 no PRF 1709210A . transthyretin . . . . . 99.22 147 99.21 99.21 3.73e-86 . . . . 5508 1 223 no REF NP_000362 . "transthyretin precursor [Homo sapiens]" . . . . . 99.22 147 99.21 99.21 3.73e-86 . . . . 5508 1 224 no SP P02766 . "RecName: Full=Transthyretin; AltName: Full=ATTR; AltName: Full=Prealbumin; AltName: Full=TBPA; Flags: Precursor [Homo sapiens]" . . . . . 99.22 147 99.21 99.21 3.73e-86 . . . . 5508 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID T119M variant 5508 1 Transthyretin common 5508 1 TTR abbreviation 5508 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 . 5508 1 2 . GLY . 5508 1 3 . PRO . 5508 1 4 . THR . 5508 1 5 . GLY . 5508 1 6 . THR . 5508 1 7 . GLY . 5508 1 8 . GLU . 5508 1 9 . SER . 5508 1 10 . LYS . 5508 1 11 . CYS . 5508 1 12 . PRO . 5508 1 13 . LEU . 5508 1 14 . MET . 5508 1 15 . VAL . 5508 1 16 . LYS . 5508 1 17 . VAL . 5508 1 18 . LEU . 5508 1 19 . ASP . 5508 1 20 . ALA . 5508 1 21 . VAL . 5508 1 22 . ARG . 5508 1 23 . GLY . 5508 1 24 . SER . 5508 1 25 . PRO . 5508 1 26 . ALA . 5508 1 27 . ILE . 5508 1 28 . ASN . 5508 1 29 . VAL . 5508 1 30 . ALA . 5508 1 31 . VAL . 5508 1 32 . HIS . 5508 1 33 . VAL . 5508 1 34 . PHE . 5508 1 35 . ARG . 5508 1 36 . LYS . 5508 1 37 . ALA . 5508 1 38 . ALA . 5508 1 39 . ASP . 5508 1 40 . ASP . 5508 1 41 . THR . 5508 1 42 . TRP . 5508 1 43 . GLU . 5508 1 44 . PRO . 5508 1 45 . PHE . 5508 1 46 . ALA . 5508 1 47 . SER . 5508 1 48 . GLY . 5508 1 49 . LYS . 5508 1 50 . THR . 5508 1 51 . SER . 5508 1 52 . GLU . 5508 1 53 . SER . 5508 1 54 . GLY . 5508 1 55 . GLU . 5508 1 56 . LEU . 5508 1 57 . HIS . 5508 1 58 . GLY . 5508 1 59 . LEU . 5508 1 60 . THR . 5508 1 61 . THR . 5508 1 62 . GLU . 5508 1 63 . GLU . 5508 1 64 . GLU . 5508 1 65 . PHE . 5508 1 66 . VAL . 5508 1 67 . GLU . 5508 1 68 . GLY . 5508 1 69 . ILE . 5508 1 70 . TYR . 5508 1 71 . LYS . 5508 1 72 . VAL . 5508 1 73 . GLU . 5508 1 74 . ILE . 5508 1 75 . ASP . 5508 1 76 . THR . 5508 1 77 . LYS . 5508 1 78 . SER . 5508 1 79 . TYR . 5508 1 80 . TRP . 5508 1 81 . LYS . 5508 1 82 . ALA . 5508 1 83 . LEU . 5508 1 84 . GLY . 5508 1 85 . ILE . 5508 1 86 . SER . 5508 1 87 . PRO . 5508 1 88 . PHE . 5508 1 89 . HIS . 5508 1 90 . GLU . 5508 1 91 . HIS . 5508 1 92 . ALA . 5508 1 93 . GLU . 5508 1 94 . VAL . 5508 1 95 . VAL . 5508 1 96 . PHE . 5508 1 97 . THR . 5508 1 98 . ALA . 5508 1 99 . ASN . 5508 1 100 . ASP . 5508 1 101 . SER . 5508 1 102 . GLY . 5508 1 103 . PRO . 5508 1 104 . ARG . 5508 1 105 . ARG . 5508 1 106 . TYR . 5508 1 107 . THR . 5508 1 108 . ILE . 5508 1 109 . ALA . 5508 1 110 . ALA . 5508 1 111 . LEU . 5508 1 112 . LEU . 5508 1 113 . SER . 5508 1 114 . PRO . 5508 1 115 . TYR . 5508 1 116 . SER . 5508 1 117 . TYR . 5508 1 118 . SER . 5508 1 119 . THR . 5508 1 120 . MET . 5508 1 121 . ALA . 5508 1 122 . VAL . 5508 1 123 . VAL . 5508 1 124 . THR . 5508 1 125 . ASN . 5508 1 126 . PRO . 5508 1 127 . LYS . 5508 1 128 . GLU . 5508 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 5508 1 . GLY 2 2 5508 1 . PRO 3 3 5508 1 . THR 4 4 5508 1 . GLY 5 5 5508 1 . THR 6 6 5508 1 . GLY 7 7 5508 1 . GLU 8 8 5508 1 . SER 9 9 5508 1 . LYS 10 10 5508 1 . CYS 11 11 5508 1 . PRO 12 12 5508 1 . LEU 13 13 5508 1 . MET 14 14 5508 1 . VAL 15 15 5508 1 . LYS 16 16 5508 1 . VAL 17 17 5508 1 . LEU 18 18 5508 1 . ASP 19 19 5508 1 . ALA 20 20 5508 1 . VAL 21 21 5508 1 . ARG 22 22 5508 1 . GLY 23 23 5508 1 . SER 24 24 5508 1 . PRO 25 25 5508 1 . ALA 26 26 5508 1 . ILE 27 27 5508 1 . ASN 28 28 5508 1 . VAL 29 29 5508 1 . ALA 30 30 5508 1 . VAL 31 31 5508 1 . HIS 32 32 5508 1 . VAL 33 33 5508 1 . PHE 34 34 5508 1 . ARG 35 35 5508 1 . LYS 36 36 5508 1 . ALA 37 37 5508 1 . ALA 38 38 5508 1 . ASP 39 39 5508 1 . ASP 40 40 5508 1 . THR 41 41 5508 1 . TRP 42 42 5508 1 . GLU 43 43 5508 1 . PRO 44 44 5508 1 . PHE 45 45 5508 1 . ALA 46 46 5508 1 . SER 47 47 5508 1 . GLY 48 48 5508 1 . LYS 49 49 5508 1 . THR 50 50 5508 1 . SER 51 51 5508 1 . GLU 52 52 5508 1 . SER 53 53 5508 1 . GLY 54 54 5508 1 . GLU 55 55 5508 1 . LEU 56 56 5508 1 . HIS 57 57 5508 1 . GLY 58 58 5508 1 . LEU 59 59 5508 1 . THR 60 60 5508 1 . THR 61 61 5508 1 . GLU 62 62 5508 1 . GLU 63 63 5508 1 . GLU 64 64 5508 1 . PHE 65 65 5508 1 . VAL 66 66 5508 1 . GLU 67 67 5508 1 . GLY 68 68 5508 1 . ILE 69 69 5508 1 . TYR 70 70 5508 1 . LYS 71 71 5508 1 . VAL 72 72 5508 1 . GLU 73 73 5508 1 . ILE 74 74 5508 1 . ASP 75 75 5508 1 . THR 76 76 5508 1 . LYS 77 77 5508 1 . SER 78 78 5508 1 . TYR 79 79 5508 1 . TRP 80 80 5508 1 . LYS 81 81 5508 1 . ALA 82 82 5508 1 . LEU 83 83 5508 1 . GLY 84 84 5508 1 . ILE 85 85 5508 1 . SER 86 86 5508 1 . PRO 87 87 5508 1 . PHE 88 88 5508 1 . HIS 89 89 5508 1 . GLU 90 90 5508 1 . HIS 91 91 5508 1 . ALA 92 92 5508 1 . GLU 93 93 5508 1 . VAL 94 94 5508 1 . VAL 95 95 5508 1 . PHE 96 96 5508 1 . THR 97 97 5508 1 . ALA 98 98 5508 1 . ASN 99 99 5508 1 . ASP 100 100 5508 1 . SER 101 101 5508 1 . GLY 102 102 5508 1 . PRO 103 103 5508 1 . ARG 104 104 5508 1 . ARG 105 105 5508 1 . TYR 106 106 5508 1 . THR 107 107 5508 1 . ILE 108 108 5508 1 . ALA 109 109 5508 1 . ALA 110 110 5508 1 . LEU 111 111 5508 1 . LEU 112 112 5508 1 . SER 113 113 5508 1 . PRO 114 114 5508 1 . TYR 115 115 5508 1 . SER 116 116 5508 1 . TYR 117 117 5508 1 . SER 118 118 5508 1 . THR 119 119 5508 1 . MET 120 120 5508 1 . ALA 121 121 5508 1 . VAL 122 122 5508 1 . VAL 123 123 5508 1 . THR 124 124 5508 1 . ASN 125 125 5508 1 . PRO 126 126 5508 1 . LYS 127 127 5508 1 . GLU 128 128 5508 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 5508 _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 $TTR_T119M . 9606 . . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 5508 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 5508 _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 $TTR_T119M . 'recombinant technology' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5508 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5508 _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 Transthyretin '[U-C13; U-N15]' . . 1 $TTR_T119M . . . 0.3 1.5 mM . . . . 5508 1 2 D2O . . . . . . . 100 . . % . . . . 5508 1 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 5508 _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 7.0 0.1 n/a 5508 1 temperature 298 2 K 5508 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 5508 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _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 5508 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer Bruker DRX . 600 . . . 5508 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 5508 _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 HSQC . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5508 1 2 HNCA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5508 1 3 HNCACB . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5508 1 4 '1H-15N NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5508 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 5508 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name HSQC _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 5508 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name HNCA _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 5508 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name HNCACB _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 5508 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name '1H-15N NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5508 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5508 1 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 5508 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5508 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_cs _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode cs _Assigned_chem_shift_list.Entry_ID 5508 _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 . 5508 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 CA C 13 53.500 0.100 . 1 . . . . . . . . 5508 1 2 . 1 1 2 2 GLY N N 15 108.708 0.250 . 1 . . . . . . . . 5508 1 3 . 1 1 2 2 GLY H H 1 8.425 0.049 . 1 . . . . . . . . 5508 1 4 . 1 1 2 2 GLY CA C 13 46.070 0.100 . 1 . . . . . . . . 5508 1 5 . 1 1 3 3 PRO CA C 13 63.022 0.100 . 1 . . . . . . . . 5508 1 6 . 1 1 4 4 THR N N 15 113.369 0.044 . 1 . . . . . . . . 5508 1 7 . 1 1 4 4 THR H H 1 8.155 0.005 . 1 . . . . . . . . 5508 1 8 . 1 1 4 4 THR CA C 13 61.503 0.100 . 1 . . . . . . . . 5508 1 9 . 1 1 5 5 GLY N N 15 110.812 0.017 . 1 . . . . . . . . 5508 1 10 . 1 1 5 5 GLY H H 1 8.277 0.005 . 1 . . . . . . . . 5508 1 11 . 1 1 5 5 GLY CA C 13 45.060 0.100 . 1 . . . . . . . . 5508 1 12 . 1 1 6 6 THR N N 15 112.850 0.070 . 1 . . . . . . . . 5508 1 13 . 1 1 6 6 THR H H 1 8.028 0.002 . 1 . . . . . . . . 5508 1 14 . 1 1 6 6 THR CA C 13 61.451 0.100 . 1 . . . . . . . . 5508 1 15 . 1 1 7 7 GLY N N 15 110.882 0.025 . 1 . . . . . . . . 5508 1 16 . 1 1 7 7 GLY H H 1 8.352 0.001 . 1 . . . . . . . . 5508 1 17 . 1 1 7 7 GLY CA C 13 45.076 0.100 . 1 . . . . . . . . 5508 1 18 . 1 1 8 8 GLU N N 15 120.423 0.033 . 1 . . . . . . . . 5508 1 19 . 1 1 8 8 GLU H H 1 8.154 0.002 . 1 . . . . . . . . 5508 1 20 . 1 1 8 8 GLU CA C 13 56.054 0.100 . 1 . . . . . . . . 5508 1 21 . 1 1 9 9 SER N N 15 116.653 0.074 . 1 . . . . . . . . 5508 1 22 . 1 1 9 9 SER H H 1 8.251 0.006 . 1 . . . . . . . . 5508 1 23 . 1 1 9 9 SER CA C 13 58.019 0.100 . 1 . . . . . . . . 5508 1 24 . 1 1 10 10 LYS N N 15 122.558 0.126 . 1 . . . . . . . . 5508 1 25 . 1 1 10 10 LYS H H 1 8.301 0.002 . 1 . . . . . . . . 5508 1 26 . 1 1 10 10 LYS CA C 13 55.327 0.100 . 1 . . . . . . . . 5508 1 27 . 1 1 11 11 CYS N N 15 119.602 0.003 . 1 . . . . . . . . 5508 1 28 . 1 1 11 11 CYS H H 1 8.202 0.002 . 1 . . . . . . . . 5508 1 29 . 1 1 11 11 CYS CA C 13 50.540 0.100 . 1 . . . . . . . . 5508 1 30 . 1 1 12 12 PRO CA C 13 64.258 0.100 . 1 . . . . . . . . 5508 1 31 . 1 1 13 13 LEU N N 15 115.696 0.066 . 1 . . . . . . . . 5508 1 32 . 1 1 13 13 LEU H H 1 6.804 0.001 . 1 . . . . . . . . 5508 1 33 . 1 1 13 13 LEU CA C 13 53.446 0.100 . 1 . . . . . . . . 5508 1 34 . 1 1 14 14 MET N N 15 126.866 0.040 . 1 . . . . . . . . 5508 1 35 . 1 1 14 14 MET H H 1 8.595 0.005 . 1 . . . . . . . . 5508 1 36 . 1 1 14 14 MET CA C 13 54.464 0.100 . 1 . . . . . . . . 5508 1 37 . 1 1 15 15 VAL N N 15 121.923 0.213 . 1 . . . . . . . . 5508 1 38 . 1 1 15 15 VAL H H 1 7.498 0.051 . 1 . . . . . . . . 5508 1 39 . 1 1 15 15 VAL CA C 13 59.250 0.100 . 1 . . . . . . . . 5508 1 40 . 1 1 16 16 LYS N N 15 127.557 0.081 . 1 . . . . . . . . 5508 1 41 . 1 1 16 16 LYS H H 1 8.854 0.001 . 1 . . . . . . . . 5508 1 42 . 1 1 16 16 LYS CA C 13 54.194 0.100 . 1 . . . . . . . . 5508 1 43 . 1 1 17 17 VAL N N 15 124.502 0.069 . 1 . . . . . . . . 5508 1 44 . 1 1 17 17 VAL H H 1 9.096 0.004 . 1 . . . . . . . . 5508 1 45 . 1 1 17 17 VAL CA C 13 60.389 0.015 . 1 . . . . . . . . 5508 1 46 . 1 1 18 18 LEU N N 15 126.044 0.009 . 1 . . . . . . . . 5508 1 47 . 1 1 18 18 LEU H H 1 8.620 0.010 . 1 . . . . . . . . 5508 1 48 . 1 1 18 18 LEU CA C 13 53.382 0.100 . 1 . . . . . . . . 5508 1 49 . 1 1 19 19 ASP N N 15 121.655 0.019 . 1 . . . . . . . . 5508 1 50 . 1 1 19 19 ASP H H 1 8.765 0.001 . 1 . . . . . . . . 5508 1 51 . 1 1 19 19 ASP CA C 13 52.992 0.100 . 1 . . . . . . . . 5508 1 52 . 1 1 20 20 ALA N N 15 127.054 0.077 . 1 . . . . . . . . 5508 1 53 . 1 1 20 20 ALA H H 1 9.113 0.008 . 1 . . . . . . . . 5508 1 54 . 1 1 20 20 ALA CA C 13 53.382 0.100 . 1 . . . . . . . . 5508 1 55 . 1 1 21 21 VAL N N 15 120.697 0.004 . 1 . . . . . . . . 5508 1 56 . 1 1 21 21 VAL H H 1 9.730 0.012 . 1 . . . . . . . . 5508 1 57 . 1 1 21 21 VAL CA C 13 65.076 0.100 . 1 . . . . . . . . 5508 1 58 . 1 1 22 22 ARG N N 15 116.621 0.013 . 1 . . . . . . . . 5508 1 59 . 1 1 22 22 ARG H H 1 8.234 0.001 . 1 . . . . . . . . 5508 1 60 . 1 1 22 22 ARG CA C 13 55.185 0.100 . 1 . . . . . . . . 5508 1 61 . 1 1 23 23 GLY N N 15 109.817 0.019 . 1 . . . . . . . . 5508 1 62 . 1 1 23 23 GLY H H 1 7.600 0.002 . 1 . . . . . . . . 5508 1 63 . 1 1 23 23 GLY CA C 13 47.036 0.100 . 1 . . . . . . . . 5508 1 64 . 1 1 24 24 SER N N 15 111.372 0.067 . 1 . . . . . . . . 5508 1 65 . 1 1 24 24 SER H H 1 7.459 0.003 . 1 . . . . . . . . 5508 1 66 . 1 1 24 24 SER CA C 13 54.950 0.100 . 1 . . . . . . . . 5508 1 67 . 1 1 25 25 PRO CA C 13 62.380 0.100 . 1 . . . . . . . . 5508 1 68 . 1 1 26 26 ALA N N 15 127.173 0.104 . 1 . . . . . . . . 5508 1 69 . 1 1 26 26 ALA H H 1 8.227 0.002 . 1 . . . . . . . . 5508 1 70 . 1 1 26 26 ALA CA C 13 50.320 0.100 . 1 . . . . . . . . 5508 1 71 . 1 1 27 27 ILE N N 15 126.949 0.072 . 1 . . . . . . . . 5508 1 72 . 1 1 27 27 ILE H H 1 7.849 0.001 . 1 . . . . . . . . 5508 1 73 . 1 1 27 27 ILE CA C 13 61.464 0.100 . 1 . . . . . . . . 5508 1 74 . 1 1 28 28 ASN N N 15 122.230 0.025 . 1 . . . . . . . . 5508 1 75 . 1 1 28 28 ASN H H 1 7.801 0.001 . 1 . . . . . . . . 5508 1 76 . 1 1 28 28 ASN CA C 13 53.994 0.100 . 1 . . . . . . . . 5508 1 77 . 1 1 29 29 VAL N N 15 119.733 0.094 . 1 . . . . . . . . 5508 1 78 . 1 1 29 29 VAL H H 1 8.352 0.004 . 1 . . . . . . . . 5508 1 79 . 1 1 29 29 VAL CA C 13 61.237 0.100 . 1 . . . . . . . . 5508 1 80 . 1 1 30 30 ALA N N 15 130.634 0.082 . 1 . . . . . . . . 5508 1 81 . 1 1 30 30 ALA H H 1 9.129 0.002 . 1 . . . . . . . . 5508 1 82 . 1 1 30 30 ALA CA C 13 52.420 0.100 . 1 . . . . . . . . 5508 1 83 . 1 1 31 31 VAL N N 15 122.056 0.143 . 1 . . . . . . . . 5508 1 84 . 1 1 31 31 VAL H H 1 8.453 0.002 . 1 . . . . . . . . 5508 1 85 . 1 1 31 31 VAL CA C 13 60.065 0.100 . 1 . . . . . . . . 5508 1 86 . 1 1 32 32 HIS N N 15 123.656 0.080 . 1 . . . . . . . . 5508 1 87 . 1 1 32 32 HIS H H 1 9.029 0.004 . 1 . . . . . . . . 5508 1 88 . 1 1 32 32 HIS CA C 13 54.520 0.100 . 1 . . . . . . . . 5508 1 89 . 1 1 33 33 VAL N N 15 122.155 0.035 . 1 . . . . . . . . 5508 1 90 . 1 1 33 33 VAL H H 1 9.233 0.003 . 1 . . . . . . . . 5508 1 91 . 1 1 33 33 VAL CA C 13 59.751 0.100 . 1 . . . . . . . . 5508 1 92 . 1 1 34 34 PHE N N 15 128.199 0.109 . 1 . . . . . . . . 5508 1 93 . 1 1 34 34 PHE H H 1 9.902 0.003 . 1 . . . . . . . . 5508 1 94 . 1 1 34 34 PHE CA C 13 55.758 0.100 . 1 . . . . . . . . 5508 1 95 . 1 1 35 35 ARG N N 15 122.378 0.110 . 1 . . . . . . . . 5508 1 96 . 1 1 35 35 ARG H H 1 9.527 0.010 . 1 . . . . . . . . 5508 1 97 . 1 1 35 35 ARG CA C 13 53.820 0.100 . 1 . . . . . . . . 5508 1 98 . 1 1 36 36 LYS N N 15 129.891 0.128 . 1 . . . . . . . . 5508 1 99 . 1 1 36 36 LYS H H 1 8.614 0.002 . 1 . . . . . . . . 5508 1 100 . 1 1 36 36 LYS CA C 13 56.730 0.100 . 1 . . . . . . . . 5508 1 101 . 1 1 37 37 ALA N N 15 131.235 0.049 . 1 . . . . . . . . 5508 1 102 . 1 1 37 37 ALA H H 1 8.784 0.004 . 1 . . . . . . . . 5508 1 103 . 1 1 37 37 ALA CA C 13 50.643 0.100 . 1 . . . . . . . . 5508 1 104 . 1 1 38 38 ALA N N 15 121.970 0.021 . 1 . . . . . . . . 5508 1 105 . 1 1 38 38 ALA H H 1 8.315 0.007 . 1 . . . . . . . . 5508 1 106 . 1 1 38 38 ALA CA C 13 53.545 0.100 . 1 . . . . . . . . 5508 1 107 . 1 1 39 39 ASP N N 15 115.691 0.058 . 1 . . . . . . . . 5508 1 108 . 1 1 39 39 ASP H H 1 7.764 0.010 . 1 . . . . . . . . 5508 1 109 . 1 1 39 39 ASP CA C 13 53.083 0.100 . 1 . . . . . . . . 5508 1 110 . 1 1 40 40 ASP N N 15 113.317 0.024 . 1 . . . . . . . . 5508 1 111 . 1 1 40 40 ASP H H 1 7.942 0.012 . 1 . . . . . . . . 5508 1 112 . 1 1 40 40 ASP CA C 13 55.554 0.100 . 1 . . . . . . . . 5508 1 113 . 1 1 41 41 THR N N 15 110.870 0.042 . 1 . . . . . . . . 5508 1 114 . 1 1 41 41 THR H H 1 7.286 0.002 . 1 . . . . . . . . 5508 1 115 . 1 1 41 41 THR CA C 13 61.011 0.100 . 1 . . . . . . . . 5508 1 116 . 1 1 42 42 TRP N N 15 120.416 0.022 . 1 . . . . . . . . 5508 1 117 . 1 1 42 42 TRP H H 1 8.376 0.001 . 1 . . . . . . . . 5508 1 118 . 1 1 42 42 TRP CA C 13 55.161 0.100 . 1 . . . . . . . . 5508 1 119 . 1 1 42 42 TRP NE1 N 15 129.009 0.100 . 1 . . . . . . . . 5508 1 120 . 1 1 42 42 TRP HE1 H 1 9.888 0.010 . 1 . . . . . . . . 5508 1 121 . 1 1 43 43 GLU N N 15 126.111 0.063 . 1 . . . . . . . . 5508 1 122 . 1 1 43 43 GLU H H 1 9.309 0.002 . 1 . . . . . . . . 5508 1 123 . 1 1 43 43 GLU CA C 13 52.743 0.100 . 1 . . . . . . . . 5508 1 124 . 1 1 44 44 PRO CA C 13 64.148 0.100 . 1 . . . . . . . . 5508 1 125 . 1 1 45 45 PHE N N 15 124.938 0.054 . 1 . . . . . . . . 5508 1 126 . 1 1 45 45 PHE H H 1 8.829 0.003 . 1 . . . . . . . . 5508 1 127 . 1 1 45 45 PHE CA C 13 58.719 0.100 . 1 . . . . . . . . 5508 1 128 . 1 1 46 46 ALA N N 15 118.453 0.075 . 1 . . . . . . . . 5508 1 129 . 1 1 46 46 ALA H H 1 7.919 0.001 . 1 . . . . . . . . 5508 1 130 . 1 1 46 46 ALA CA C 13 51.882 0.100 . 1 . . . . . . . . 5508 1 131 . 1 1 47 47 SER N N 15 113.207 0.010 . 1 . . . . . . . . 5508 1 132 . 1 1 47 47 SER H H 1 8.529 0.010 . 1 . . . . . . . . 5508 1 133 . 1 1 47 47 SER CA C 13 57.284 0.100 . 1 . . . . . . . . 5508 1 134 . 1 1 48 48 GLY N N 15 106.099 0.002 . 1 . . . . . . . . 5508 1 135 . 1 1 48 48 GLY H H 1 8.374 0.002 . 1 . . . . . . . . 5508 1 136 . 1 1 48 48 GLY CA C 13 45.421 0.100 . 1 . . . . . . . . 5508 1 137 . 1 1 49 49 LYS N N 15 119.937 0.037 . 1 . . . . . . . . 5508 1 138 . 1 1 49 49 LYS H H 1 8.435 0.001 . 1 . . . . . . . . 5508 1 139 . 1 1 49 49 LYS CA C 13 53.498 0.100 . 1 . . . . . . . . 5508 1 140 . 1 1 50 50 THR N N 15 111.433 0.047 . 1 . . . . . . . . 5508 1 141 . 1 1 50 50 THR H H 1 8.647 0.005 . 1 . . . . . . . . 5508 1 142 . 1 1 50 50 THR CA C 13 61.738 0.100 . 1 . . . . . . . . 5508 1 143 . 1 1 51 51 SER N N 15 118.071 0.030 . 1 . . . . . . . . 5508 1 144 . 1 1 51 51 SER H H 1 8.511 0.003 . 1 . . . . . . . . 5508 1 145 . 1 1 51 51 SER CA C 13 56.780 0.100 . 1 . . . . . . . . 5508 1 146 . 1 1 52 52 GLU N N 15 118.554 0.077 . 1 . . . . . . . . 5508 1 147 . 1 1 52 52 GLU H H 1 9.052 0.002 . 1 . . . . . . . . 5508 1 148 . 1 1 52 52 GLU CA C 13 58.769 0.100 . 1 . . . . . . . . 5508 1 149 . 1 1 53 53 SER N N 15 111.428 0.040 . 1 . . . . . . . . 5508 1 150 . 1 1 53 53 SER H H 1 8.081 0.004 . 1 . . . . . . . . 5508 1 151 . 1 1 53 53 SER CA C 13 57.140 0.100 . 1 . . . . . . . . 5508 1 152 . 1 1 54 54 GLY N N 15 111.823 0.032 . 1 . . . . . . . . 5508 1 153 . 1 1 54 54 GLY H H 1 8.569 0.003 . 1 . . . . . . . . 5508 1 154 . 1 1 54 54 GLY CA C 13 45.185 0.100 . 1 . . . . . . . . 5508 1 155 . 1 1 55 55 GLU N N 15 115.224 0.034 . 1 . . . . . . . . 5508 1 156 . 1 1 55 55 GLU H H 1 7.243 0.003 . 1 . . . . . . . . 5508 1 157 . 1 1 55 55 GLU CA C 13 54.006 0.100 . 1 . . . . . . . . 5508 1 158 . 1 1 56 56 LEU N N 15 123.719 0.027 . 1 . . . . . . . . 5508 1 159 . 1 1 56 56 LEU H H 1 8.742 0.004 . 1 . . . . . . . . 5508 1 160 . 1 1 56 56 LEU CA C 13 53.604 0.100 . 1 . . . . . . . . 5508 1 161 . 1 1 57 57 HIS N N 15 124.226 0.037 . 1 . . . . . . . . 5508 1 162 . 1 1 57 57 HIS H H 1 8.677 0.010 . 1 . . . . . . . . 5508 1 163 . 1 1 57 57 HIS CA C 13 53.873 0.100 . 1 . . . . . . . . 5508 1 164 . 1 1 58 58 GLY N N 15 108.959 0.100 . 1 . . . . . . . . 5508 1 165 . 1 1 58 58 GLY H H 1 9.085 0.008 . 1 . . . . . . . . 5508 1 166 . 1 1 58 58 GLY CA C 13 46.229 0.100 . 1 . . . . . . . . 5508 1 167 . 1 1 59 59 LEU N N 15 119.505 0.078 . 1 . . . . . . . . 5508 1 168 . 1 1 59 59 LEU H H 1 8.124 0.010 . 1 . . . . . . . . 5508 1 169 . 1 1 59 59 LEU CA C 13 56.640 0.003 . 1 . . . . . . . . 5508 1 170 . 1 1 60 60 THR N N 15 109.438 0.174 . 1 . . . . . . . . 5508 1 171 . 1 1 60 60 THR H H 1 7.839 0.077 . 1 . . . . . . . . 5508 1 172 . 1 1 60 60 THR CA C 13 58.826 0.100 . 1 . . . . . . . . 5508 1 173 . 1 1 61 61 THR N N 15 111.192 0.008 . 1 . . . . . . . . 5508 1 174 . 1 1 61 61 THR H H 1 8.378 0.010 . 1 . . . . . . . . 5508 1 175 . 1 1 61 61 THR CA C 13 59.223 0.100 . 1 . . . . . . . . 5508 1 176 . 1 1 62 62 GLU N N 15 121.328 0.039 . 1 . . . . . . . . 5508 1 177 . 1 1 62 62 GLU H H 1 9.244 0.004 . 1 . . . . . . . . 5508 1 178 . 1 1 62 62 GLU CA C 13 59.674 0.100 . 1 . . . . . . . . 5508 1 179 . 1 1 63 63 GLU N N 15 115.907 0.001 . 1 . . . . . . . . 5508 1 180 . 1 1 63 63 GLU H H 1 8.651 0.004 . 1 . . . . . . . . 5508 1 181 . 1 1 63 63 GLU CA C 13 58.617 0.100 . 1 . . . . . . . . 5508 1 182 . 1 1 64 64 GLU N N 15 115.287 0.018 . 1 . . . . . . . . 5508 1 183 . 1 1 64 64 GLU H H 1 7.230 0.002 . 1 . . . . . . . . 5508 1 184 . 1 1 64 64 GLU CA C 13 56.414 0.100 . 1 . . . . . . . . 5508 1 185 . 1 1 65 65 PHE N N 15 123.726 0.037 . 1 . . . . . . . . 5508 1 186 . 1 1 65 65 PHE H H 1 7.826 0.018 . 1 . . . . . . . . 5508 1 187 . 1 1 65 65 PHE CA C 13 53.918 0.100 . 1 . . . . . . . . 5508 1 188 . 1 1 66 66 VAL N N 15 115.143 0.010 . 1 . . . . . . . . 5508 1 189 . 1 1 66 66 VAL H H 1 7.179 0.010 . 1 . . . . . . . . 5508 1 190 . 1 1 66 66 VAL CA C 13 59.824 0.100 . 1 . . . . . . . . 5508 1 191 . 1 1 67 67 GLU N N 15 121.796 0.031 . 1 . . . . . . . . 5508 1 192 . 1 1 67 67 GLU H H 1 8.561 0.003 . 1 . . . . . . . . 5508 1 193 . 1 1 67 67 GLU CA C 13 56.458 0.100 . 1 . . . . . . . . 5508 1 194 . 1 1 68 68 GLY N N 15 110.975 0.035 . 1 . . . . . . . . 5508 1 195 . 1 1 68 68 GLY H H 1 7.922 0.011 . 1 . . . . . . . . 5508 1 196 . 1 1 68 68 GLY CA C 13 44.291 0.100 . 1 . . . . . . . . 5508 1 197 . 1 1 69 69 ILE N N 15 120.580 0.100 . 1 . . . . . . . . 5508 1 198 . 1 1 69 69 ILE H H 1 8.332 0.002 . 1 . . . . . . . . 5508 1 199 . 1 1 69 69 ILE CA C 13 60.398 0.100 . 1 . . . . . . . . 5508 1 200 . 1 1 70 70 TYR N N 15 124.719 0.098 . 1 . . . . . . . . 5508 1 201 . 1 1 70 70 TYR H H 1 8.678 0.004 . 1 . . . . . . . . 5508 1 202 . 1 1 70 70 TYR CA C 13 55.973 0.100 . 1 . . . . . . . . 5508 1 203 . 1 1 71 71 LYS N N 15 118.551 0.005 . 1 . . . . . . . . 5508 1 204 . 1 1 71 71 LYS H H 1 8.718 0.003 . 1 . . . . . . . . 5508 1 205 . 1 1 71 71 LYS CA C 13 53.337 0.100 . 1 . . . . . . . . 5508 1 206 . 1 1 72 72 VAL N N 15 127.339 0.091 . 1 . . . . . . . . 5508 1 207 . 1 1 72 72 VAL H H 1 9.635 0.012 . 1 . . . . . . . . 5508 1 208 . 1 1 72 72 VAL CA C 13 60.783 0.100 . 1 . . . . . . . . 5508 1 209 . 1 1 73 73 GLU N N 15 128.168 0.066 . 1 . . . . . . . . 5508 1 210 . 1 1 73 73 GLU H H 1 9.665 0.005 . 1 . . . . . . . . 5508 1 211 . 1 1 73 73 GLU CA C 13 54.859 0.100 . 1 . . . . . . . . 5508 1 212 . 1 1 74 74 ILE N N 15 126.079 0.041 . 1 . . . . . . . . 5508 1 213 . 1 1 74 74 ILE H H 1 9.176 0.001 . 1 . . . . . . . . 5508 1 214 . 1 1 74 74 ILE CA C 13 59.903 0.100 . 1 . . . . . . . . 5508 1 215 . 1 1 75 75 ASP N N 15 128.431 0.044 . 1 . . . . . . . . 5508 1 216 . 1 1 75 75 ASP H H 1 8.950 0.100 . 1 . . . . . . . . 5508 1 217 . 1 1 75 75 ASP CA C 13 53.335 0.100 . 1 . . . . . . . . 5508 1 218 . 1 1 76 76 THR N N 15 117.142 0.011 . 1 . . . . . . . . 5508 1 219 . 1 1 76 76 THR H H 1 8.226 0.003 . 1 . . . . . . . . 5508 1 220 . 1 1 76 76 THR CA C 13 64.063 0.100 . 1 . . . . . . . . 5508 1 221 . 1 1 77 77 LYS N N 15 124.486 0.100 . 1 . . . . . . . . 5508 1 222 . 1 1 77 77 LYS H H 1 7.521 0.002 . 1 . . . . . . . . 5508 1 223 . 1 1 77 77 LYS CA C 13 59.946 0.100 . 1 . . . . . . . . 5508 1 224 . 1 1 78 78 SER N N 15 112.878 0.066 . 1 . . . . . . . . 5508 1 225 . 1 1 78 78 SER H H 1 8.183 0.003 . 1 . . . . . . . . 5508 1 226 . 1 1 78 78 SER CA C 13 61.393 0.100 . 1 . . . . . . . . 5508 1 227 . 1 1 79 79 TYR N N 15 121.137 0.008 . 1 . . . . . . . . 5508 1 228 . 1 1 79 79 TYR H H 1 6.793 0.001 . 1 . . . . . . . . 5508 1 229 . 1 1 79 79 TYR CA C 13 60.791 0.100 . 1 . . . . . . . . 5508 1 230 . 1 1 80 80 TRP N N 15 117.167 0.094 . 1 . . . . . . . . 5508 1 231 . 1 1 80 80 TRP H H 1 7.879 0.002 . 1 . . . . . . . . 5508 1 232 . 1 1 80 80 TRP CA C 13 58.826 0.100 . 1 . . . . . . . . 5508 1 233 . 1 1 80 80 TRP NE1 N 15 126.516 0.100 . 1 . . . . . . . . 5508 1 234 . 1 1 80 80 TRP HE1 H 1 10.245 0.010 . 1 . . . . . . . . 5508 1 235 . 1 1 81 81 LYS N N 15 118.114 0.041 . 1 . . . . . . . . 5508 1 236 . 1 1 81 81 LYS H H 1 8.707 0.003 . 1 . . . . . . . . 5508 1 237 . 1 1 81 81 LYS CA C 13 59.398 0.100 . 1 . . . . . . . . 5508 1 238 . 1 1 82 82 ALA N N 15 122.107 0.100 . 1 . . . . . . . . 5508 1 239 . 1 1 82 82 ALA H H 1 7.528 0.003 . 1 . . . . . . . . 5508 1 240 . 1 1 82 82 ALA CA C 13 53.989 0.100 . 1 . . . . . . . . 5508 1 241 . 1 1 83 83 LEU N N 15 117.500 0.100 . 1 . . . . . . . . 5508 1 242 . 1 1 83 83 LEU H H 1 7.310 0.010 . 1 . . . . . . . . 5508 1 243 . 1 1 83 83 LEU CA C 13 54.145 0.100 . 1 . . . . . . . . 5508 1 244 . 1 1 84 84 GLY N N 15 107.394 0.008 . 1 . . . . . . . . 5508 1 245 . 1 1 84 84 GLY H H 1 7.955 0.001 . 1 . . . . . . . . 5508 1 246 . 1 1 84 84 GLY CA C 13 45.248 0.100 . 1 . . . . . . . . 5508 1 247 . 1 1 85 85 ILE N N 15 122.783 0.047 . 1 . . . . . . . . 5508 1 248 . 1 1 85 85 ILE H H 1 7.919 0.001 . 1 . . . . . . . . 5508 1 249 . 1 1 85 85 ILE CA C 13 59.338 0.100 . 1 . . . . . . . . 5508 1 250 . 1 1 86 86 SER N N 15 121.809 0.012 . 1 . . . . . . . . 5508 1 251 . 1 1 86 86 SER H H 1 8.415 0.001 . 1 . . . . . . . . 5508 1 252 . 1 1 86 86 SER CA C 13 54.520 0.100 . 1 . . . . . . . . 5508 1 253 . 1 1 87 87 PRO CA C 13 60.932 0.100 . 1 . . . . . . . . 5508 1 254 . 1 1 88 88 PHE N N 15 115.921 0.041 . 1 . . . . . . . . 5508 1 255 . 1 1 88 88 PHE H H 1 7.365 0.001 . 1 . . . . . . . . 5508 1 256 . 1 1 88 88 PHE CA C 13 59.844 0.100 . 1 . . . . . . . . 5508 1 257 . 1 1 89 89 HIS N N 15 112.936 0.122 . 1 . . . . . . . . 5508 1 258 . 1 1 89 89 HIS H H 1 7.673 0.001 . 1 . . . . . . . . 5508 1 259 . 1 1 89 89 HIS CA C 13 57.696 0.100 . 1 . . . . . . . . 5508 1 260 . 1 1 90 90 GLU N N 15 122.540 0.100 . 1 . . . . . . . . 5508 1 261 . 1 1 90 90 GLU H H 1 8.356 0.002 . 1 . . . . . . . . 5508 1 262 . 1 1 90 90 GLU CA C 13 52.991 0.100 . 1 . . . . . . . . 5508 1 263 . 1 1 91 91 HIS N N 15 116.662 0.060 . 1 . . . . . . . . 5508 1 264 . 1 1 91 91 HIS H H 1 8.095 0.004 . 1 . . . . . . . . 5508 1 265 . 1 1 91 91 HIS CA C 13 54.217 0.100 . 1 . . . . . . . . 5508 1 266 . 1 1 92 92 ALA N N 15 119.989 0.125 . 1 . . . . . . . . 5508 1 267 . 1 1 92 92 ALA H H 1 8.512 0.002 . 1 . . . . . . . . 5508 1 268 . 1 1 92 92 ALA CA C 13 51.380 0.100 . 1 . . . . . . . . 5508 1 269 . 1 1 93 93 GLU N N 15 120.656 0.079 . 1 . . . . . . . . 5508 1 270 . 1 1 93 93 GLU H H 1 8.156 0.003 . 1 . . . . . . . . 5508 1 271 . 1 1 93 93 GLU CA C 13 54.207 0.100 . 1 . . . . . . . . 5508 1 272 . 1 1 94 94 VAL N N 15 121.743 0.081 . 1 . . . . . . . . 5508 1 273 . 1 1 94 94 VAL H H 1 8.869 0.002 . 1 . . . . . . . . 5508 1 274 . 1 1 94 94 VAL CA C 13 61.024 0.100 . 1 . . . . . . . . 5508 1 275 . 1 1 95 95 VAL N N 15 127.920 0.056 . 1 . . . . . . . . 5508 1 276 . 1 1 95 95 VAL H H 1 9.303 0.004 . 1 . . . . . . . . 5508 1 277 . 1 1 95 95 VAL CA C 13 60.701 0.100 . 1 . . . . . . . . 5508 1 278 . 1 1 96 96 PHE N N 15 124.663 0.047 . 1 . . . . . . . . 5508 1 279 . 1 1 96 96 PHE H H 1 9.052 0.007 . 1 . . . . . . . . 5508 1 280 . 1 1 96 96 PHE CA C 13 55.721 0.100 . 1 . . . . . . . . 5508 1 281 . 1 1 97 97 THR N N 15 118.285 0.049 . 1 . . . . . . . . 5508 1 282 . 1 1 97 97 THR H H 1 8.572 0.013 . 1 . . . . . . . . 5508 1 283 . 1 1 97 97 THR CA C 13 62.518 0.100 . 1 . . . . . . . . 5508 1 284 . 1 1 98 98 ALA N N 15 129.359 0.084 . 1 . . . . . . . . 5508 1 285 . 1 1 98 98 ALA H H 1 9.157 0.004 . 1 . . . . . . . . 5508 1 286 . 1 1 98 98 ALA CA C 13 49.649 0.100 . 1 . . . . . . . . 5508 1 287 . 1 1 99 99 ASN N N 15 111.956 0.079 . 1 . . . . . . . . 5508 1 288 . 1 1 99 99 ASN H H 1 8.593 0.001 . 1 . . . . . . . . 5508 1 289 . 1 1 99 99 ASN CA C 13 54.162 0.100 . 1 . . . . . . . . 5508 1 290 . 1 1 100 100 ASP N N 15 117.117 0.025 . 1 . . . . . . . . 5508 1 291 . 1 1 100 100 ASP H H 1 8.876 0.004 . 1 . . . . . . . . 5508 1 292 . 1 1 100 100 ASP CA C 13 55.331 0.100 . 1 . . . . . . . . 5508 1 293 . 1 1 101 101 SER N N 15 117.103 0.004 . 1 . . . . . . . . 5508 1 294 . 1 1 101 101 SER H H 1 8.781 0.010 . 1 . . . . . . . . 5508 1 295 . 1 1 101 101 SER CA C 13 56.869 0.100 . 1 . . . . . . . . 5508 1 296 . 1 1 102 102 GLY N N 15 109.998 0.003 . 1 . . . . . . . . 5508 1 297 . 1 1 102 102 GLY H H 1 7.190 0.010 . 1 . . . . . . . . 5508 1 298 . 1 1 102 102 GLY CA C 13 43.409 0.100 . 1 . . . . . . . . 5508 1 299 . 1 1 103 103 PRO CA C 13 57.500 0.100 . 1 . . . . . . . . 5508 1 300 . 1 1 104 104 ARG N N 15 121.255 0.045 . 1 . . . . . . . . 5508 1 301 . 1 1 104 104 ARG H H 1 8.908 0.012 . 1 . . . . . . . . 5508 1 302 . 1 1 104 104 ARG CA C 13 57.750 0.100 . 1 . . . . . . . . 5508 1 303 . 1 1 105 105 ARG N N 15 106.009 0.013 . 1 . . . . . . . . 5508 1 304 . 1 1 105 105 ARG H H 1 7.268 0.002 . 1 . . . . . . . . 5508 1 305 . 1 1 105 105 ARG CA C 13 54.217 0.100 . 1 . . . . . . . . 5508 1 306 . 1 1 106 106 TYR N N 15 121.207 0.081 . 1 . . . . . . . . 5508 1 307 . 1 1 106 106 TYR H H 1 8.858 0.001 . 1 . . . . . . . . 5508 1 308 . 1 1 106 106 TYR CA C 13 57.616 0.100 . 1 . . . . . . . . 5508 1 309 . 1 1 107 107 THR N N 15 120.710 0.156 . 1 . . . . . . . . 5508 1 310 . 1 1 107 107 THR H H 1 8.896 0.002 . 1 . . . . . . . . 5508 1 311 . 1 1 107 107 THR CA C 13 61.486 0.100 . 1 . . . . . . . . 5508 1 312 . 1 1 108 108 ILE N N 15 127.039 0.055 . 1 . . . . . . . . 5508 1 313 . 1 1 108 108 ILE H H 1 8.798 0.011 . 1 . . . . . . . . 5508 1 314 . 1 1 108 108 ILE CA C 13 58.161 0.011 . 1 . . . . . . . . 5508 1 315 . 1 1 109 109 ALA N N 15 127.767 0.046 . 1 . . . . . . . . 5508 1 316 . 1 1 109 109 ALA H H 1 8.749 0.004 . 1 . . . . . . . . 5508 1 317 . 1 1 109 109 ALA CA C 13 48.820 0.100 . 1 . . . . . . . . 5508 1 318 . 1 1 110 110 ALA N N 15 124.025 0.035 . 1 . . . . . . . . 5508 1 319 . 1 1 110 110 ALA H H 1 8.891 0.004 . 1 . . . . . . . . 5508 1 320 . 1 1 110 110 ALA CA C 13 50.266 0.100 . 1 . . . . . . . . 5508 1 321 . 1 1 111 111 LEU N N 15 124.016 0.023 . 1 . . . . . . . . 5508 1 322 . 1 1 111 111 LEU H H 1 8.933 0.005 . 1 . . . . . . . . 5508 1 323 . 1 1 111 111 LEU CA C 13 53.658 0.100 . 1 . . . . . . . . 5508 1 324 . 1 1 112 112 LEU N N 15 123.152 0.074 . 1 . . . . . . . . 5508 1 325 . 1 1 112 112 LEU H H 1 9.183 0.005 . 1 . . . . . . . . 5508 1 326 . 1 1 112 112 LEU CA C 13 55.327 0.100 . 1 . . . . . . . . 5508 1 327 . 1 1 113 113 SER N N 15 116.654 0.006 . 1 . . . . . . . . 5508 1 328 . 1 1 113 113 SER H H 1 8.991 0.005 . 1 . . . . . . . . 5508 1 329 . 1 1 113 113 SER CA C 13 57.750 0.100 . 1 . . . . . . . . 5508 1 330 . 1 1 114 114 PRO CA C 13 61.411 0.100 . 1 . . . . . . . . 5508 1 331 . 1 1 115 115 TYR N N 15 113.362 0.003 . 1 . . . . . . . . 5508 1 332 . 1 1 115 115 TYR H H 1 8.369 0.005 . 1 . . . . . . . . 5508 1 333 . 1 1 115 115 TYR CA C 13 57.965 0.100 . 1 . . . . . . . . 5508 1 334 . 1 1 116 116 SER N N 15 112.029 0.012 . 1 . . . . . . . . 5508 1 335 . 1 1 116 116 SER H H 1 7.560 0.010 . 1 . . . . . . . . 5508 1 336 . 1 1 116 116 SER CA C 13 56.761 0.100 . 1 . . . . . . . . 5508 1 337 . 1 1 117 117 TYR N N 15 120.275 0.318 . 1 . . . . . . . . 5508 1 338 . 1 1 117 117 TYR H H 1 8.330 0.018 . 1 . . . . . . . . 5508 1 339 . 1 1 117 117 TYR CA C 13 54.834 0.100 . 1 . . . . . . . . 5508 1 340 . 1 1 118 118 SER N N 15 114.751 0.001 . 1 . . . . . . . . 5508 1 341 . 1 1 118 118 SER H H 1 8.472 0.006 . 1 . . . . . . . . 5508 1 342 . 1 1 118 118 SER CA C 13 56.190 0.003 . 1 . . . . . . . . 5508 1 343 . 1 1 119 119 THR N N 15 115.772 0.032 . 1 . . . . . . . . 5508 1 344 . 1 1 119 119 THR H H 1 8.954 0.007 . 1 . . . . . . . . 5508 1 345 . 1 1 119 119 THR CA C 13 57.898 0.004 . 1 . . . . . . . . 5508 1 346 . 1 1 120 120 MET N N 15 122.065 0.062 . 1 . . . . . . . . 5508 1 347 . 1 1 120 120 MET H H 1 8.288 0.009 . 1 . . . . . . . . 5508 1 348 . 1 1 120 120 MET CA C 13 53.500 0.054 . 1 . . . . . . . . 5508 1 349 . 1 1 121 121 ALA N N 15 128.173 0.043 . 1 . . . . . . . . 5508 1 350 . 1 1 121 121 ALA H H 1 8.233 0.010 . 1 . . . . . . . . 5508 1 351 . 1 1 121 121 ALA CA C 13 49.810 0.100 . 1 . . . . . . . . 5508 1 352 . 1 1 122 122 VAL N N 15 118.902 0.241 . 1 . . . . . . . . 5508 1 353 . 1 1 122 122 VAL H H 1 8.318 0.004 . 1 . . . . . . . . 5508 1 354 . 1 1 122 122 VAL CA C 13 59.934 0.100 . 1 . . . . . . . . 5508 1 355 . 1 1 123 123 VAL N N 15 128.360 0.039 . 1 . . . . . . . . 5508 1 356 . 1 1 123 123 VAL H H 1 8.274 0.002 . 1 . . . . . . . . 5508 1 357 . 1 1 123 123 VAL CA C 13 60.495 0.100 . 1 . . . . . . . . 5508 1 358 . 1 1 124 124 THR N N 15 119.919 0.028 . 1 . . . . . . . . 5508 1 359 . 1 1 124 124 THR H H 1 8.726 0.001 . 1 . . . . . . . . 5508 1 360 . 1 1 124 124 THR CA C 13 59.962 0.100 . 1 . . . . . . . . 5508 1 361 . 1 1 125 125 ASN N N 15 121.716 0.025 . 1 . . . . . . . . 5508 1 362 . 1 1 125 125 ASN H H 1 8.677 0.002 . 1 . . . . . . . . 5508 1 363 . 1 1 125 125 ASN CA C 13 50.266 0.100 . 1 . . . . . . . . 5508 1 364 . 1 1 126 126 PRO CA C 13 63.026 0.100 . 1 . . . . . . . . 5508 1 365 . 1 1 127 127 LYS N N 15 120.320 0.036 . 1 . . . . . . . . 5508 1 366 . 1 1 127 127 LYS H H 1 8.022 0.003 . 1 . . . . . . . . 5508 1 367 . 1 1 127 127 LYS CA C 13 55.704 0.100 . 1 . . . . . . . . 5508 1 368 . 1 1 128 128 GLU N N 15 126.566 0.022 . 1 . . . . . . . . 5508 1 369 . 1 1 128 128 GLU H H 1 7.667 0.010 . 1 . . . . . . . . 5508 1 370 . 1 1 128 128 GLU CA C 13 57.626 0.100 . 1 . . . . . . . . 5508 1 stop_ save_