data_4472 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4472 _Entry.Title ; 1H, 13C, and 15N signal assignments for BeFx-activated CheY from E. coli ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 1999-12-03 _Entry.Accession_date 1999-12-03 _Entry.Last_release_date 2000-12-15 _Entry.Original_release_date 2000-12-15 _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 Ho Cho . S . 4472 2 Seok-Yong Lee . . . 4472 3 Dalai Yan . . . 4472 4 Xiaoyu Pan . . . 4472 5 John Parkinson . S . 4472 6 Sydney Kustu . . . 4472 7 David Wemmer . E . 4472 8 Jeffrey Pelton . G . 4472 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4472 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 822 4472 '13C chemical shifts' 405 4472 '15N chemical shifts' 123 4472 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 . . 2000-12-15 1999-12-03 original author . 4472 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4472 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 20198307 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Cho, H.S., Lee, S-Y., Yan, D., Pan, X., Parkinson, J.S., Kustu, S., Wemmer, D.E., and Pelton, J.G., "NMR Structure of Activated CheY," J. Mol. Biol. 297, 543-551 (2000). ; _Citation.Title 'NMR Structure of Activated CheY' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of Molecular Biology' _Citation.Journal_volume 297 _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 543 _Citation.Page_last 551 _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 Ho Cho . S . 4472 1 2 Seok-Yong Lee . . . 4472 1 3 Dalai Yan . . . 4472 1 4 Xiaoyu Pan . . . 4472 1 5 John Parkinson . S . 4472 1 6 Sydney Kustu . . . 4472 1 7 David Wemmer . E . 4472 1 8 Jeffrey Pelton . G . 4472 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID BeFx 4472 1 CheY 4472 1 'response regulator' 4472 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_CheY _Assembly.Sf_category assembly _Assembly.Sf_framecode system_CheY _Assembly.Entry_ID 4472 _Assembly.ID 1 _Assembly.Name 'BeFx-activated CheY from E. coli' _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 4472 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 CheY 1 $CheY . . . native . . . . . 4472 1 2 beryllofluoride 2 $entity_BF2 . . . native . . . . . 4472 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'BeFx-activated CheY from E. coli' system 4472 1 CheY abbreviation 4472 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'Chemotaxis response regulator' 4472 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_CheY _Entity.Sf_category entity _Entity.Sf_framecode CheY _Entity.Entry_ID 4472 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Chemotaxis protein Y' _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 ; MADKELKFLVVDDFSTMRRI VRNLLKELGFNNVEEAEDGV DALNKLQAGGYGFVISDWNM PNMDGLELLKTIRADGAMSA LPVLMVTAEAKKENIIAAAQ AGASGYVVKPFTAATLEEKL NKIFEKLGM ; _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 BF2 _Entity.Nonpolymer_comp_label $chem_comp_BF2 _Entity.Number_of_monomers 129 _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 14097 _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 2950 . "che Y protein" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 2 no BMRB 2951 . "che Y protein" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 3 no BMRB 3440 . "che Y protein" . . . . . 99.22 129 99.22 100.00 1.78e-84 . . . . 4472 1 4 no BMRB 4083 . "E. coli CheY" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 4472 1 5 no PDB 1A0O . "Chey-Binding Domain Of Chea In Complex With Chey" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 4472 1 6 no PDB 1AB5 . "Structure Of Chey Mutant F14n, V21t" . . . . . 96.90 125 98.40 98.40 1.65e-80 . . . . 4472 1 7 no PDB 1AB6 . "Structure Of Chey Mutant F14n, V86t" . . . . . 96.90 125 98.40 98.40 1.65e-80 . . . . 4472 1 8 no PDB 1BDJ . "Complex Structure Of Hpt Domain And Chey" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 4472 1 9 no PDB 1C4W . "1.9 A Structure Of A-Thiophosphonate Modified Chey D57c" . . . . . 99.22 128 99.22 99.22 1.11e-83 . . . . 4472 1 10 no PDB 1CEY . "Assignments, Secondary Structure, Global Fold, And Dynamics Of Chemotaxis Y Protein Using Three-And Four-Dimensional Heteronucl" . . . . . 98.45 128 100.00 100.00 3.78e-84 . . . . 4472 1 11 no PDB 1CHN . "Magnesium Binding To The Bacterial Chemotaxis Protein Chey Results In Large Conformational Changes Involving Its Functional Sur" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 4472 1 12 no PDB 1CYE . "Three Dimensional Structure Of Chemotactic Che Y Protein In Aqueous Solution By Nuclear Magnetic Resonance Methods" . . . . . 99.22 129 99.22 100.00 1.78e-84 . . . . 4472 1 13 no PDB 1D4Z . "Crystal Structure Of Chey-95iv, A Hyperactive Chey Mutant" . . . . . 99.22 128 99.22 100.00 1.53e-84 . . . . 4472 1 14 no PDB 1DJM . "Solution Structure Of Bef3-Activated Chey From Escherichia Coli" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 15 no PDB 1E6K . "Two-Component Signal Transduction System D12a Mutant Of Chey" . . . . . 99.22 130 98.44 99.22 2.85e-83 . . . . 4472 1 16 no PDB 1E6L . "Two-Component Signal Transduction System D13a Mutant Of Chey" . . . . . 98.45 127 99.21 99.21 5.25e-83 . . . . 4472 1 17 no PDB 1E6M . "Two-Component Signal Transduction System D57a Mutant Of Chey" . . . . . 99.22 128 98.44 99.22 3.47e-83 . . . . 4472 1 18 no PDB 1EAY . "Chey-Binding (P2) Domain Of Chea In Complex With Chey From Escherichia Coli" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 4472 1 19 no PDB 1EHC . "Structure Of Signal Transduction Protein Chey" . . . . . 99.22 128 99.22 99.22 8.29e-84 . . . . 4472 1 20 no PDB 1F4V . "Crystal Structure Of Activated Chey Bound To The N-Terminus Of Flim" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 4472 1 21 no PDB 1FFG . "Chey-binding Domain Of Chea In Complex With Chey At 2.1 A Resolution" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 4472 1 22 no PDB 1FFS . "Chey-Binding Domain Of Chea In Complex With Chey From Crystals Soaked In Acetyl Phosphate" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 4472 1 23 no PDB 1FFW . "Chey-Binding Domain Of Chea In Complex With Chey With A Bound Imido Diphosphate" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 4472 1 24 no PDB 1FQW . "Crystal Structure Of Activated Chey" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 4472 1 25 no PDB 1JBE . "1.08 A Structure Of Apo-Chey Reveals Meta-Active Conformation" . . . . . 99.22 128 98.44 98.44 1.26e-82 . . . . 4472 1 26 no PDB 1KMI . "Crystal Structure Of An E.Coli Chemotaxis Protein, Chez" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 27 no PDB 1MIH . "A Role For Chey Glu 89 In Chez-Mediated Dephosphorylation Of The E. Coli Chemotaxis Response Regulator Chey" . . . . . 100.00 129 99.22 99.22 1.12e-84 . . . . 4472 1 28 no PDB 1VLZ . "Uncoupled Phosphorylation And Activation In Bacterial Chemotaxis: The 2.1 Angstrom Structure Of A Threonine To Isoleucine Mutan" . . . . . 99.22 128 99.22 99.22 6.59e-84 . . . . 4472 1 29 no PDB 1YMU . "Signal Transduction Protein Chey Mutant With Met 17 Replaced By Gly (M17g)" . . . . . 99.22 130 98.44 99.22 3.82e-83 . . . . 4472 1 30 no PDB 1ZDM . "Crystal Structure Of Activated Chey Bound To Xe" . . . . . 100.00 129 99.22 99.22 1.54e-84 . . . . 4472 1 31 no PDB 2B1J . "Crystal Structure Of Unphosphorylated Chey Bound To The N- Terminus Of Flim" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 4472 1 32 no PDB 2CHE . "Structure Of The Mg2+-Bound Form Of Chey And Mechanism Of Phosphoryl Transfer In Bacterial Chemotaxis" . . . . . 99.22 128 97.66 99.22 3.35e-83 . . . . 4472 1 33 no PDB 2CHF . "Structure Of The Mg2+-Bound Form Of Chey And The Mechanism Of Phosphoryl Transfer In Bacterial Chemotaxis" . . . . . 99.22 128 97.66 99.22 3.35e-83 . . . . 4472 1 34 no PDB 2FKA . "Crystal Structure Of Mg(2+) And Bef(3)(-)-Bound Chey In Complex With Chez(200-214) Solved From A F432 Crystal Grown In Caps (Ph" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 4472 1 35 no PDB 2FLK . "Crystal Structure Of Chey In Complex With Chez(200-214) Solved From A F432 Crystal Grown In Caps (Ph 10.5)" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 4472 1 36 no PDB 2FLW . "Crystal Structure Of Mg2+ And Bef3- Ound Chey In Complex With Chez 200-214 Solved From A F432 Crystal Grown In Hepes (ph 7.5)" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 4472 1 37 no PDB 2FMF . "Crystal Structure Of Chey In Complex With Chez 200-214 Solved From A F432 Crystal Grown In Hepes (ph 7.5)" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 4472 1 38 no PDB 2FMH . "Crystal Structure Of Mg2+ And Bef3- Bound Chey In Complex With Chez 200-214 Solved From A F432 Crystal Grown In Tris (Ph 8.4)" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 4472 1 39 no PDB 2FMI . "Crystal Structure Of Chey In Complex With Chez 200-214 Solved From A F432 Crystal Grown In Tris (Ph 8.4)" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 4472 1 40 no PDB 2FMK . "Crystal Structure Of Mg2+ And Bef3- Bound Chey In Complex With Chez 200-214 Solved From A P2(1)2(1)2 Crystal Grown In Mes (Ph 6" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 4472 1 41 no PDB 2ID7 . "1.75 A Structure Of T87i Phosphono-Chey" . . . . . 99.22 128 98.44 98.44 1.06e-82 . . . . 4472 1 42 no PDB 2ID9 . "1.85 A Structure Of T87i/y106w Phosphono-chey" . . . . . 99.22 128 97.66 98.44 6.53e-82 . . . . 4472 1 43 no PDB 2IDM . "2.00 A Structure Of T87iY106W PHOSPHONO-Chey" . . . . . 99.22 128 97.66 98.44 6.53e-82 . . . . 4472 1 44 no PDB 2LP4 . "Solution Structure Of P1-CheyP2 COMPLEX IN BACTERIAL CHEMOTAXIS" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 4472 1 45 no PDB 2PL9 . "Crystal Structure Of Chey-mg(2+)-bef(3)(-) In Complex With Chez(c19) Peptide Solved From A P2(1)2(1)2 Crystal" . . . . . 99.22 128 97.66 99.22 3.35e-83 . . . . 4472 1 46 no PDB 2PMC . "Crystal Structure Of Chey-mg(2+) In Complex With Chez(c15) Peptide Solved From A P1 Crystal" . . . . . 99.22 128 97.66 99.22 3.35e-83 . . . . 4472 1 47 no PDB 3CHY . "Crystal Structure Of Escherichia Coli Chey Refined At 1.7- Angstrom Resolution" . . . . . 99.22 128 100.00 100.00 7.67e-85 . . . . 4472 1 48 no PDB 3F7N . "Crystal Structure Of Chey Triple Mutant F14e, N59m, E89l Complexed With Bef3- And Mn2+" . . . . . 99.22 128 97.66 97.66 8.22e-81 . . . . 4472 1 49 no PDB 3FFT . "Crystal Structure Of Chey Double Mutant F14e, E89r Complexed With Bef3- And Mn2+" . . . . . 99.22 128 98.44 98.44 1.30e-82 . . . . 4472 1 50 no PDB 3FFW . "Crystal Structure Of Chey Triple Mutant F14q, N59k, E89y Complexed With Bef3- And Mn2+" . . . . . 99.22 128 97.66 97.66 1.97e-81 . . . . 4472 1 51 no PDB 3FFX . "Crystal Structure Of Chey Triple Mutant F14e, N59r, E89h Complexed With Bef3- And Mn2+" . . . . . 99.22 128 97.66 97.66 7.13e-82 . . . . 4472 1 52 no PDB 3FGZ . "Crystal Structure Of Chey Triple Mutant F14e, N59m, E89r Complexed With Bef3- And Mn2+" . . . . . 99.22 128 97.66 97.66 2.53e-81 . . . . 4472 1 53 no PDB 3MYY . "Structure Of E. Coli Chey Mutant A113p Bound To Beryllium Fluoride" . . . . . 99.22 128 99.22 99.22 5.72e-84 . . . . 4472 1 54 no PDB 3OLV . "Structural And Functional Effects Of Substitution At Position T+1 In Chey: Cheya88v-Bef3-Mg Complex" . . . . . 100.00 129 99.22 99.22 6.30e-85 . . . . 4472 1 55 no PDB 3OLW . "Structural And Functional Effects Of Substitution At Position T+1 In Chey: Cheya88t-Bef3-Mn Complex" . . . . . 100.00 129 99.22 99.22 5.65e-85 . . . . 4472 1 56 no PDB 3OLX . "Structural And Functional Effects Of Substitution At Position T+1 In Chey: Cheya88s-Bef3-Mn Complex" . . . . . 100.00 129 99.22 100.00 3.57e-85 . . . . 4472 1 57 no PDB 3OLY . "Structural And Functional Effects Of Substitution At Position T+1 In Chey: Cheya88m-Bef3-Mn Complex" . . . . . 100.00 129 99.22 99.22 1.11e-84 . . . . 4472 1 58 no PDB 3OO0 . "Structure Of Apo Chey A113p" . . . . . 100.00 129 99.22 99.22 7.93e-85 . . . . 4472 1 59 no PDB 3OO1 . "Structure Of E. Coli Chey Mutant A113p In The Absence Of Sulfate" . . . . . 100.00 129 99.22 99.22 7.93e-85 . . . . 4472 1 60 no PDB 3RVJ . "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89q" . . . . . 100.00 132 98.45 100.00 1.25e-84 . . . . 4472 1 61 no PDB 3RVK . "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89q" . . . . . 100.00 132 98.45 100.00 1.25e-84 . . . . 4472 1 62 no PDB 3RVL . "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89r" . . . . . 100.00 132 98.45 99.22 3.42e-84 . . . . 4472 1 63 no PDB 3RVM . "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d And E89r" . . . . . 100.00 132 98.45 99.22 3.42e-84 . . . . 4472 1 64 no PDB 3RVN . "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89y" . . . . . 100.00 132 98.45 99.22 5.91e-84 . . . . 4472 1 65 no PDB 3RVO . "Structure Of Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89y" . . . . . 100.00 132 98.45 99.22 5.91e-84 . . . . 4472 1 66 no PDB 3RVP . "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89k" . . . . . 100.00 132 98.45 100.00 2.78e-84 . . . . 4472 1 67 no PDB 3RVQ . "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89k" . . . . . 100.00 132 98.45 100.00 2.78e-84 . . . . 4472 1 68 no PDB 3RVR . "Structure Of The Cheyn59dE89R MOLYBDATE COMPLEX" . . . . . 100.00 132 98.45 99.22 3.42e-84 . . . . 4472 1 69 no PDB 3RVS . "Structure Of The Cheyn59dE89R TUNGSTATE COMPLEX" . . . . . 100.00 132 98.45 99.22 3.42e-84 . . . . 4472 1 70 no PDB 5CHY . "Structure Of Chemotaxis Protein Chey" . . . . . 99.22 128 99.22 100.00 8.48e-84 . . . . 4472 1 71 no PDB 6CHY . "Structure Of Chemotaxis Protein Chey" . . . . . 99.22 128 98.44 99.22 7.05e-83 . . . . 4472 1 72 no DBJ BAA15698 . "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli str. K12 substr. W3110]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 73 no DBJ BAB36015 . "chemotaxis protein CheY [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 74 no DBJ BAG77641 . "chemotactic response regulator CheY [Escherichia coli SE11]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 75 no DBJ BAI25973 . "chemotaxis regulator CheY, transmitting signal to flagellar motor component [Escherichia coli O26:H11 str. 11368]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 76 no DBJ BAI30936 . "chemotaxis regulator CheY, transmitting signal to flagellar motor component [Escherichia coli O103:H2 str. 12009]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 77 no EMBL CAD05667 . "chemotaxis protein CheY [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 4472 1 78 no EMBL CAP76371 . "chemotaxis protein cheY [Escherichia coli LF82]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 79 no EMBL CAQ32359 . "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli BL21(DE3)]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 80 no EMBL CAQ98822 . "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli IAI1]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 81 no EMBL CAR03242 . "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli S88]" . . . . . 100.00 129 99.22 100.00 4.49e-85 . . . . 4472 1 82 no GB AAA23570 . "cheY protein [Escherichia coli]" . . . . . 100.00 129 99.22 99.22 7.93e-85 . . . . 4472 1 83 no GB AAA23577 . "CheY [Escherichia coli]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 84 no GB AAA27037 . "CheY [Salmonella enterica subsp. enterica serovar Typhimurium]" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 4472 1 85 no GB AAC74952 . "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 86 no GB AAG56872 . "chemotaxis regulator transmits chemoreceptor signals to flagelllar motor components [Escherichia coli O157:H7 str. EDL933]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 87 no PIR AH0745 . "chemotaxis protein CheY [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 4472 1 88 no REF NP_310619 . "chemotaxis regulatory protein CheY [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 89 no REF NP_416396 . "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 90 no REF NP_456482 . "chemotaxis protein CheY [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 4472 1 91 no REF NP_460873 . "chemotaxis regulatory protein CheY [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 4472 1 92 no REF NP_707777 . "chemotaxis regulatory protein CheY [Shigella flexneri 2a str. 301]" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 93 no SP P0A2D5 . "RecName: Full=Chemotaxis protein CheY" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 4472 1 94 no SP P0A2D6 . "RecName: Full=Chemotaxis protein CheY" . . . . . 100.00 129 97.67 99.22 5.36e-84 . . . . 4472 1 95 no SP P0AE67 . "RecName: Full=Chemotaxis protein CheY" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 96 no SP P0AE68 . "RecName: Full=Chemotaxis protein CheY" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 97 no SP P0AE69 . "RecName: Full=Chemotaxis protein CheY" . . . . . 100.00 129 100.00 100.00 1.46e-85 . . . . 4472 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Chemotaxis protein Y' common 4472 1 CheY abbreviation 4472 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 . 4472 1 2 . ALA . 4472 1 3 . ASP . 4472 1 4 . LYS . 4472 1 5 . GLU . 4472 1 6 . LEU . 4472 1 7 . LYS . 4472 1 8 . PHE . 4472 1 9 . LEU . 4472 1 10 . VAL . 4472 1 11 . VAL . 4472 1 12 . ASP . 4472 1 13 . ASP . 4472 1 14 . PHE . 4472 1 15 . SER . 4472 1 16 . THR . 4472 1 17 . MET . 4472 1 18 . ARG . 4472 1 19 . ARG . 4472 1 20 . ILE . 4472 1 21 . VAL . 4472 1 22 . ARG . 4472 1 23 . ASN . 4472 1 24 . LEU . 4472 1 25 . LEU . 4472 1 26 . LYS . 4472 1 27 . GLU . 4472 1 28 . LEU . 4472 1 29 . GLY . 4472 1 30 . PHE . 4472 1 31 . ASN . 4472 1 32 . ASN . 4472 1 33 . VAL . 4472 1 34 . GLU . 4472 1 35 . GLU . 4472 1 36 . ALA . 4472 1 37 . GLU . 4472 1 38 . ASP . 4472 1 39 . GLY . 4472 1 40 . VAL . 4472 1 41 . ASP . 4472 1 42 . ALA . 4472 1 43 . LEU . 4472 1 44 . ASN . 4472 1 45 . LYS . 4472 1 46 . LEU . 4472 1 47 . GLN . 4472 1 48 . ALA . 4472 1 49 . GLY . 4472 1 50 . GLY . 4472 1 51 . TYR . 4472 1 52 . GLY . 4472 1 53 . PHE . 4472 1 54 . VAL . 4472 1 55 . ILE . 4472 1 56 . SER . 4472 1 57 . ASP . 4472 1 58 . TRP . 4472 1 59 . ASN . 4472 1 60 . MET . 4472 1 61 . PRO . 4472 1 62 . ASN . 4472 1 63 . MET . 4472 1 64 . ASP . 4472 1 65 . GLY . 4472 1 66 . LEU . 4472 1 67 . GLU . 4472 1 68 . LEU . 4472 1 69 . LEU . 4472 1 70 . LYS . 4472 1 71 . THR . 4472 1 72 . ILE . 4472 1 73 . ARG . 4472 1 74 . ALA . 4472 1 75 . ASP . 4472 1 76 . GLY . 4472 1 77 . ALA . 4472 1 78 . MET . 4472 1 79 . SER . 4472 1 80 . ALA . 4472 1 81 . LEU . 4472 1 82 . PRO . 4472 1 83 . VAL . 4472 1 84 . LEU . 4472 1 85 . MET . 4472 1 86 . VAL . 4472 1 87 . THR . 4472 1 88 . ALA . 4472 1 89 . GLU . 4472 1 90 . ALA . 4472 1 91 . LYS . 4472 1 92 . LYS . 4472 1 93 . GLU . 4472 1 94 . ASN . 4472 1 95 . ILE . 4472 1 96 . ILE . 4472 1 97 . ALA . 4472 1 98 . ALA . 4472 1 99 . ALA . 4472 1 100 . GLN . 4472 1 101 . ALA . 4472 1 102 . GLY . 4472 1 103 . ALA . 4472 1 104 . SER . 4472 1 105 . GLY . 4472 1 106 . TYR . 4472 1 107 . VAL . 4472 1 108 . VAL . 4472 1 109 . LYS . 4472 1 110 . PRO . 4472 1 111 . PHE . 4472 1 112 . THR . 4472 1 113 . ALA . 4472 1 114 . ALA . 4472 1 115 . THR . 4472 1 116 . LEU . 4472 1 117 . GLU . 4472 1 118 . GLU . 4472 1 119 . LYS . 4472 1 120 . LEU . 4472 1 121 . ASN . 4472 1 122 . LYS . 4472 1 123 . ILE . 4472 1 124 . PHE . 4472 1 125 . GLU . 4472 1 126 . LYS . 4472 1 127 . LEU . 4472 1 128 . GLY . 4472 1 129 . MET . 4472 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 4472 1 . ALA 2 2 4472 1 . ASP 3 3 4472 1 . LYS 4 4 4472 1 . GLU 5 5 4472 1 . LEU 6 6 4472 1 . LYS 7 7 4472 1 . PHE 8 8 4472 1 . LEU 9 9 4472 1 . VAL 10 10 4472 1 . VAL 11 11 4472 1 . ASP 12 12 4472 1 . ASP 13 13 4472 1 . PHE 14 14 4472 1 . SER 15 15 4472 1 . THR 16 16 4472 1 . MET 17 17 4472 1 . ARG 18 18 4472 1 . ARG 19 19 4472 1 . ILE 20 20 4472 1 . VAL 21 21 4472 1 . ARG 22 22 4472 1 . ASN 23 23 4472 1 . LEU 24 24 4472 1 . LEU 25 25 4472 1 . LYS 26 26 4472 1 . GLU 27 27 4472 1 . LEU 28 28 4472 1 . GLY 29 29 4472 1 . PHE 30 30 4472 1 . ASN 31 31 4472 1 . ASN 32 32 4472 1 . VAL 33 33 4472 1 . GLU 34 34 4472 1 . GLU 35 35 4472 1 . ALA 36 36 4472 1 . GLU 37 37 4472 1 . ASP 38 38 4472 1 . GLY 39 39 4472 1 . VAL 40 40 4472 1 . ASP 41 41 4472 1 . ALA 42 42 4472 1 . LEU 43 43 4472 1 . ASN 44 44 4472 1 . LYS 45 45 4472 1 . LEU 46 46 4472 1 . GLN 47 47 4472 1 . ALA 48 48 4472 1 . GLY 49 49 4472 1 . GLY 50 50 4472 1 . TYR 51 51 4472 1 . GLY 52 52 4472 1 . PHE 53 53 4472 1 . VAL 54 54 4472 1 . ILE 55 55 4472 1 . SER 56 56 4472 1 . ASP 57 57 4472 1 . TRP 58 58 4472 1 . ASN 59 59 4472 1 . MET 60 60 4472 1 . PRO 61 61 4472 1 . ASN 62 62 4472 1 . MET 63 63 4472 1 . ASP 64 64 4472 1 . GLY 65 65 4472 1 . LEU 66 66 4472 1 . GLU 67 67 4472 1 . LEU 68 68 4472 1 . LEU 69 69 4472 1 . LYS 70 70 4472 1 . THR 71 71 4472 1 . ILE 72 72 4472 1 . ARG 73 73 4472 1 . ALA 74 74 4472 1 . ASP 75 75 4472 1 . GLY 76 76 4472 1 . ALA 77 77 4472 1 . MET 78 78 4472 1 . SER 79 79 4472 1 . ALA 80 80 4472 1 . LEU 81 81 4472 1 . PRO 82 82 4472 1 . VAL 83 83 4472 1 . LEU 84 84 4472 1 . MET 85 85 4472 1 . VAL 86 86 4472 1 . THR 87 87 4472 1 . ALA 88 88 4472 1 . GLU 89 89 4472 1 . ALA 90 90 4472 1 . LYS 91 91 4472 1 . LYS 92 92 4472 1 . GLU 93 93 4472 1 . ASN 94 94 4472 1 . ILE 95 95 4472 1 . ILE 96 96 4472 1 . ALA 97 97 4472 1 . ALA 98 98 4472 1 . ALA 99 99 4472 1 . GLN 100 100 4472 1 . ALA 101 101 4472 1 . GLY 102 102 4472 1 . ALA 103 103 4472 1 . SER 104 104 4472 1 . GLY 105 105 4472 1 . TYR 106 106 4472 1 . VAL 107 107 4472 1 . VAL 108 108 4472 1 . LYS 109 109 4472 1 . PRO 110 110 4472 1 . PHE 111 111 4472 1 . THR 112 112 4472 1 . ALA 113 113 4472 1 . ALA 114 114 4472 1 . THR 115 115 4472 1 . LEU 116 116 4472 1 . GLU 117 117 4472 1 . GLU 118 118 4472 1 . LYS 119 119 4472 1 . LEU 120 120 4472 1 . ASN 121 121 4472 1 . LYS 122 122 4472 1 . ILE 123 123 4472 1 . PHE 124 124 4472 1 . GLU 125 125 4472 1 . LYS 126 126 4472 1 . LEU 127 127 4472 1 . GLY 128 128 4472 1 . MET 129 129 4472 1 stop_ save_ save_entity_BF2 _Entity.Sf_category entity _Entity.Sf_framecode entity_BF2 _Entity.Entry_ID 4472 _Entity.ID 2 _Entity.BMRB_code BF2 _Entity.Name 'BERYLLIUM DIFLUORIDE' _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID BF2 _Entity.Nonpolymer_comp_label $chem_comp_BF2 _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components 1 _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 2 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 47.009 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'BERYLLIUM DIFLUORIDE' BMRB 4472 2 stop_ loop_ _Entity_systematic_name.Name _Entity_systematic_name.Naming_system _Entity_systematic_name.Entry_ID _Entity_systematic_name.Entity_ID 'BERYLLIUM DIFLUORIDE' BMRB 4472 2 BF2 'Three letter code' 4472 2 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 1 BF2 $chem_comp_BF2 4472 2 stop_ loop_ _Entity_atom_list.ID _Entity_atom_list.Comp_index_ID _Entity_atom_list.Comp_ID _Entity_atom_list.Atom_ID _Entity_atom_list.Entry_ID _Entity_atom_list.Entity_ID 1 1 BF2 BE 4472 2 2 1 BF2 F1 4472 2 3 1 BF2 F2 4472 2 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 4472 _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 $CheY . 562 . . 'Escherichia coli' 'Escherichia coli' . . Eubacteria . Escherichia coli . . . . . . . . . . . . . . . . . . . . . 4472 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 4472 _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 $CheY . 'recombinant technology' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4472 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_BF2 _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_BF2 _Chem_comp.Entry_ID 4472 _Chem_comp.ID BF2 _Chem_comp.Provenance PDB _Chem_comp.Name 'BERYLLIUM DIFLUORIDE' _Chem_comp.Type NON-POLYMER _Chem_comp.BMRB_code BF2 _Chem_comp.PDB_code BF2 _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-12-14 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code BF2 _Chem_comp.Number_atoms_all 3 _Chem_comp.Number_atoms_nh 3 _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code InChI=1S/Be.2FH/h;2*1H/q+2;;/p-2 _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula 'Be F2' _Chem_comp.Formula_weight 47.009 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code 4UKD _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details . _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID InChI=1S/Be.2FH/h;2*1H/q+2;;/p-2 InChI InChI 1.03 4472 BF2 JZKFIPKXQBZXMW-UHFFFAOYSA-L InChIKey InChI 1.03 4472 BF2 F[Be]F SMILES ACDLabs 10.04 4472 BF2 F[Be]F SMILES CACTVS 3.341 4472 BF2 [Be](F)F SMILES 'OpenEye OEToolkits' 1.5.0 4472 BF2 F[Be]F SMILES_CANONICAL CACTVS 3.341 4472 BF2 [Be](F)F SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 4472 BF2 stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID 'beryllium difluoride' 'SYSTEMATIC NAME' ACDLabs 10.04 4472 BF2 difluoroberyllium 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 4472 BF2 stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID BE BE BE BE . BE . . N 0 . . . 0 no no . . . . 37.170 . 68.362 . -12.729 . 0.000 0.000 0.000 1 . 4472 BF2 F1 F1 F1 F1 . F . . N 0 . . . 1 no no . . . . 35.781 . 68.849 . -12.699 . 0.000 0.000 -1.390 2 . 4472 BF2 F2 F2 F2 F2 . F . . N 0 . . . 1 no no . . . . 38.050 . 69.248 . -11.913 . 0.000 0.000 1.390 3 . 4472 BF2 stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING BE F1 no N 1 . 4472 BF2 2 . SING BE F2 no N 2 . 4472 BF2 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4472 _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 'Chemotaxis protein Y' '[U-99% 13C; U-99% 15N]' . . 1 $CheY . . . 1 4 mM . . . . 4472 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 4472 _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 'Chemotaxis protein Y' '[U-99% 15N]' . . 1 $CheY . . . 1 4 mM . . . . 4472 2 stop_ save_ save_sample_3 _Sample.Sf_category sample _Sample.Sf_framecode sample_3 _Sample.Entry_ID 4472 _Sample.ID 3 _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 'Chemotaxis protein Y' '[U-10% 13C]' . . 1 $CheY . . . 1 4 mM . . . . 4472 3 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_1 _Sample_condition_list.Entry_ID 4472 _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 6.7 0.2 n/a 4472 1 temperature 298 1 K 4472 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 4472 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AMX _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 4472 _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 AMX . 600 . . . 4472 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 4472 _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 HNCA . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4472 1 2 CBCACONH . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4472 1 3 '1H-15N NOESY' . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4472 1 4 '1H-15N TOCSY' . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4472 1 5 HCCH-TOCSY . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4472 1 6 '4D 1H-13C HMQC-NOESY-HMQC' . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4472 1 7 '4D 1H-15N HMQC-NOESY-HSQC' . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4472 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 4472 _NMR_spec_expt.ID 1 _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 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _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 4472 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name CBCACONH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _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 4472 _NMR_spec_expt.ID 3 _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 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _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 4472 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name '1H-15N TOCSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 4472 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name HCCH-TOCSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 4472 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name '4D 1H-13C HMQC-NOESY-HMQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _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_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 4472 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name '4D 1H-15N HMQC-NOESY-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 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _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 4472 _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 . . . 1 $entry_citation . . 1 $entry_citation 4472 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . 1 $entry_citation . . 1 $entry_citation 4472 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . 1 $entry_citation . . 1 $entry_citation 4472 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_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 4472 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-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 . 4472 1 . . 2 $sample_2 . 4472 1 . . 3 $sample_3 . 4472 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 2 2 ALA HB1 H 1 0.81 0.02 . 1 . . . . . . . . 4472 1 2 . 1 1 2 2 ALA HB2 H 1 0.81 0.02 . 1 . . . . . . . . 4472 1 3 . 1 1 2 2 ALA HB3 H 1 0.81 0.02 . 1 . . . . . . . . 4472 1 4 . 1 1 2 2 ALA CB C 13 18.1 0.2 . 1 . . . . . . . . 4472 1 5 . 1 1 3 3 ASP N N 15 121.4 0.2 . 1 . . . . . . . . 4472 1 6 . 1 1 3 3 ASP H H 1 8.64 0.02 . 1 . . . . . . . . 4472 1 7 . 1 1 3 3 ASP CA C 13 53.9 0.2 . 1 . . . . . . . . 4472 1 8 . 1 1 3 3 ASP HA H 1 4.5 0.02 . 1 . . . . . . . . 4472 1 9 . 1 1 3 3 ASP CB C 13 41.3 0.2 . 1 . . . . . . . . 4472 1 10 . 1 1 3 3 ASP HB2 H 1 2.72 0.02 . 2 . . . . . . . . 4472 1 11 . 1 1 3 3 ASP HB3 H 1 2.66 0.02 . 2 . . . . . . . . 4472 1 12 . 1 1 4 4 LYS N N 15 122.5 0.2 . 1 . . . . . . . . 4472 1 13 . 1 1 4 4 LYS H H 1 8.55 0.02 . 1 . . . . . . . . 4472 1 14 . 1 1 4 4 LYS CA C 13 57.1 0.2 . 1 . . . . . . . . 4472 1 15 . 1 1 4 4 LYS HA H 1 4.26 0.02 . 1 . . . . . . . . 4472 1 16 . 1 1 4 4 LYS CB C 13 30.6 0.2 . 1 . . . . . . . . 4472 1 17 . 1 1 4 4 LYS HB2 H 1 1.95 0.02 . 2 . . . . . . . . 4472 1 18 . 1 1 4 4 LYS HB3 H 1 1.79 0.02 . 2 . . . . . . . . 4472 1 19 . 1 1 4 4 LYS CG C 13 24.2 0.2 . 1 . . . . . . . . 4472 1 20 . 1 1 4 4 LYS HG2 H 1 1.38 0.02 . 2 . . . . . . . . 4472 1 21 . 1 1 4 4 LYS HG3 H 1 1.32 0.02 . 2 . . . . . . . . 4472 1 22 . 1 1 4 4 LYS CD C 13 27.6 0.2 . 1 . . . . . . . . 4472 1 23 . 1 1 4 4 LYS HD2 H 1 1.24 0.02 . 2 . . . . . . . . 4472 1 24 . 1 1 4 4 LYS HD3 H 1 1.18 0.02 . 2 . . . . . . . . 4472 1 25 . 1 1 4 4 LYS CE C 13 42.1 0.2 . 1 . . . . . . . . 4472 1 26 . 1 1 4 4 LYS HE2 H 1 2.81 0.02 . 1 . . . . . . . . 4472 1 27 . 1 1 4 4 LYS HE3 H 1 2.81 0.02 . 1 . . . . . . . . 4472 1 28 . 1 1 5 5 GLU N N 15 118.9 0.2 . 1 . . . . . . . . 4472 1 29 . 1 1 5 5 GLU H H 1 8.71 0.02 . 1 . . . . . . . . 4472 1 30 . 1 1 5 5 GLU CA C 13 55.5 0.2 . 1 . . . . . . . . 4472 1 31 . 1 1 5 5 GLU HA H 1 4.48 0.02 . 1 . . . . . . . . 4472 1 32 . 1 1 5 5 GLU CB C 13 29.1 0.2 . 1 . . . . . . . . 4472 1 33 . 1 1 5 5 GLU HB2 H 1 2.28 0.02 . 2 . . . . . . . . 4472 1 34 . 1 1 5 5 GLU HB3 H 1 1.96 0.02 . 2 . . . . . . . . 4472 1 35 . 1 1 5 5 GLU CG C 13 36.1 0.2 . 1 . . . . . . . . 4472 1 36 . 1 1 5 5 GLU HG2 H 1 2.35 0.02 . 2 . . . . . . . . 4472 1 37 . 1 1 5 5 GLU HG3 H 1 2.2 0.02 . 2 . . . . . . . . 4472 1 38 . 1 1 6 6 LEU N N 15 124.1 0.2 . 1 . . . . . . . . 4472 1 39 . 1 1 6 6 LEU H H 1 7.58 0.02 . 1 . . . . . . . . 4472 1 40 . 1 1 6 6 LEU CA C 13 56.3 0.2 . 1 . . . . . . . . 4472 1 41 . 1 1 6 6 LEU HA H 1 3.84 0.02 . 1 . . . . . . . . 4472 1 42 . 1 1 6 6 LEU CB C 13 42.9 0.2 . 1 . . . . . . . . 4472 1 43 . 1 1 6 6 LEU HB2 H 1 1.78 0.02 . 2 . . . . . . . . 4472 1 44 . 1 1 6 6 LEU HB3 H 1 1.61 0.02 . 2 . . . . . . . . 4472 1 45 . 1 1 6 6 LEU CG C 13 26.1 0.2 . 1 . . . . . . . . 4472 1 46 . 1 1 6 6 LEU HG H 1 1.17 0.02 . 1 . . . . . . . . 4472 1 47 . 1 1 6 6 LEU HD11 H 1 0.8 0.02 . 1 . . . . . . . . 4472 1 48 . 1 1 6 6 LEU HD12 H 1 0.8 0.02 . 1 . . . . . . . . 4472 1 49 . 1 1 6 6 LEU HD13 H 1 0.8 0.02 . 1 . . . . . . . . 4472 1 50 . 1 1 6 6 LEU HD21 H 1 0.61 0.02 . 1 . . . . . . . . 4472 1 51 . 1 1 6 6 LEU HD22 H 1 0.61 0.02 . 1 . . . . . . . . 4472 1 52 . 1 1 6 6 LEU HD23 H 1 0.61 0.02 . 1 . . . . . . . . 4472 1 53 . 1 1 6 6 LEU CD1 C 13 24.6 0.2 . 1 . . . . . . . . 4472 1 54 . 1 1 6 6 LEU CD2 C 13 26.1 0.2 . 1 . . . . . . . . 4472 1 55 . 1 1 7 7 LYS N N 15 126.1 0.2 . 1 . . . . . . . . 4472 1 56 . 1 1 7 7 LYS H H 1 8.51 0.02 . 1 . . . . . . . . 4472 1 57 . 1 1 7 7 LYS CA C 13 56 0.2 . 1 . . . . . . . . 4472 1 58 . 1 1 7 7 LYS HA H 1 5.12 0.02 . 1 . . . . . . . . 4472 1 59 . 1 1 7 7 LYS CB C 13 33.5 0.2 . 1 . . . . . . . . 4472 1 60 . 1 1 7 7 LYS HB2 H 1 1.88 0.02 . 2 . . . . . . . . 4472 1 61 . 1 1 7 7 LYS HB3 H 1 1.49 0.02 . 2 . . . . . . . . 4472 1 62 . 1 1 7 7 LYS CG C 13 25 0.2 . 1 . . . . . . . . 4472 1 63 . 1 1 7 7 LYS HG2 H 1 1.09 0.02 . 1 . . . . . . . . 4472 1 64 . 1 1 7 7 LYS HG3 H 1 1.09 0.02 . 1 . . . . . . . . 4472 1 65 . 1 1 7 7 LYS CD C 13 29.1 0.2 . 1 . . . . . . . . 4472 1 66 . 1 1 7 7 LYS HD2 H 1 1.15 0.02 . 2 . . . . . . . . 4472 1 67 . 1 1 7 7 LYS HD3 H 1 0.8 0.02 . 2 . . . . . . . . 4472 1 68 . 1 1 7 7 LYS CE C 13 41.3 0.2 . 1 . . . . . . . . 4472 1 69 . 1 1 7 7 LYS HE2 H 1 2.45 0.02 . 2 . . . . . . . . 4472 1 70 . 1 1 7 7 LYS HE3 H 1 2.19 0.02 . 2 . . . . . . . . 4472 1 71 . 1 1 8 8 PHE N N 15 128.1 0.2 . 1 . . . . . . . . 4472 1 72 . 1 1 8 8 PHE H H 1 9.22 0.02 . 1 . . . . . . . . 4472 1 73 . 1 1 8 8 PHE CA C 13 56.8 0.2 . 1 . . . . . . . . 4472 1 74 . 1 1 8 8 PHE HA H 1 5.46 0.02 . 1 . . . . . . . . 4472 1 75 . 1 1 8 8 PHE CB C 13 43.2 0.2 . 1 . . . . . . . . 4472 1 76 . 1 1 8 8 PHE HB2 H 1 3.19 0.02 . 2 . . . . . . . . 4472 1 77 . 1 1 8 8 PHE HB3 H 1 2.53 0.02 . 2 . . . . . . . . 4472 1 78 . 1 1 8 8 PHE CD1 C 13 130.6 0.2 . 3 . . . . . . . . 4472 1 79 . 1 1 8 8 PHE HD1 H 1 7 0.02 . 3 . . . . . . . . 4472 1 80 . 1 1 8 8 PHE CE1 C 13 131.1 0.2 . 3 . . . . . . . . 4472 1 81 . 1 1 8 8 PHE HE1 H 1 6.21 0.02 . 3 . . . . . . . . 4472 1 82 . 1 1 8 8 PHE CZ C 13 127.7 0.2 . 1 . . . . . . . . 4472 1 83 . 1 1 8 8 PHE HZ H 1 5.66 0.02 . 1 . . . . . . . . 4472 1 84 . 1 1 9 9 LEU N N 15 121.5 0.2 . 1 . . . . . . . . 4472 1 85 . 1 1 9 9 LEU H H 1 8.74 0.02 . 1 . . . . . . . . 4472 1 86 . 1 1 9 9 LEU CA C 13 52.9 0.2 . 1 . . . . . . . . 4472 1 87 . 1 1 9 9 LEU HA H 1 5.14 0.02 . 1 . . . . . . . . 4472 1 88 . 1 1 9 9 LEU CB C 13 43.6 0.2 . 1 . . . . . . . . 4472 1 89 . 1 1 9 9 LEU HB2 H 1 1.67 0.02 . 2 . . . . . . . . 4472 1 90 . 1 1 9 9 LEU HB3 H 1 1.08 0.02 . 2 . . . . . . . . 4472 1 91 . 1 1 9 9 LEU CG C 13 26.8 0.2 . 1 . . . . . . . . 4472 1 92 . 1 1 9 9 LEU HG H 1 1.17 0.02 . 1 . . . . . . . . 4472 1 93 . 1 1 9 9 LEU HD21 H 1 0.38 0.02 . 1 . . . . . . . . 4472 1 94 . 1 1 9 9 LEU HD22 H 1 0.38 0.02 . 1 . . . . . . . . 4472 1 95 . 1 1 9 9 LEU HD23 H 1 0.38 0.02 . 1 . . . . . . . . 4472 1 96 . 1 1 9 9 LEU HD11 H 1 0.56 0.02 . 1 . . . . . . . . 4472 1 97 . 1 1 9 9 LEU HD12 H 1 0.56 0.02 . 1 . . . . . . . . 4472 1 98 . 1 1 9 9 LEU HD13 H 1 0.56 0.02 . 1 . . . . . . . . 4472 1 99 . 1 1 9 9 LEU CD2 C 13 26.8 0.2 . 1 . . . . . . . . 4472 1 100 . 1 1 9 9 LEU CD1 C 13 22.7 0.2 . 1 . . . . . . . . 4472 1 101 . 1 1 10 10 VAL N N 15 127.3 0.2 . 1 . . . . . . . . 4472 1 102 . 1 1 10 10 VAL H H 1 9.08 0.02 . 1 . . . . . . . . 4472 1 103 . 1 1 10 10 VAL CA C 13 61.3 0.2 . 1 . . . . . . . . 4472 1 104 . 1 1 10 10 VAL HA H 1 4.82 0.02 . 1 . . . . . . . . 4472 1 105 . 1 1 10 10 VAL CB C 13 33.2 0.2 . 1 . . . . . . . . 4472 1 106 . 1 1 10 10 VAL HB H 1 1.98 0.02 . 1 . . . . . . . . 4472 1 107 . 1 1 10 10 VAL HG11 H 1 0.98 0.02 . 1 . . . . . . . . 4472 1 108 . 1 1 10 10 VAL HG12 H 1 0.98 0.02 . 1 . . . . . . . . 4472 1 109 . 1 1 10 10 VAL HG13 H 1 0.98 0.02 . 1 . . . . . . . . 4472 1 110 . 1 1 10 10 VAL HG21 H 1 0.88 0.02 . 1 . . . . . . . . 4472 1 111 . 1 1 10 10 VAL HG22 H 1 0.88 0.02 . 1 . . . . . . . . 4472 1 112 . 1 1 10 10 VAL HG23 H 1 0.88 0.02 . 1 . . . . . . . . 4472 1 113 . 1 1 10 10 VAL CG1 C 13 20.9 0.2 . 1 . . . . . . . . 4472 1 114 . 1 1 10 10 VAL CG2 C 13 22 0.2 . 1 . . . . . . . . 4472 1 115 . 1 1 11 11 VAL N N 15 127.2 0.2 . 1 . . . . . . . . 4472 1 116 . 1 1 11 11 VAL H H 1 9.22 0.02 . 1 . . . . . . . . 4472 1 117 . 1 1 11 11 VAL CA C 13 59.5 0.2 . 1 . . . . . . . . 4472 1 118 . 1 1 11 11 VAL HA H 1 4.9 0.02 . 1 . . . . . . . . 4472 1 119 . 1 1 11 11 VAL CB C 13 32.8 0.2 . 1 . . . . . . . . 4472 1 120 . 1 1 11 11 VAL HB H 1 2.3 0.02 . 1 . . . . . . . . 4472 1 121 . 1 1 11 11 VAL HG21 H 1 0.67 0.02 . 1 . . . . . . . . 4472 1 122 . 1 1 11 11 VAL HG22 H 1 0.67 0.02 . 1 . . . . . . . . 4472 1 123 . 1 1 11 11 VAL HG23 H 1 0.67 0.02 . 1 . . . . . . . . 4472 1 124 . 1 1 11 11 VAL HG11 H 1 0.62 0.02 . 1 . . . . . . . . 4472 1 125 . 1 1 11 11 VAL HG12 H 1 0.62 0.02 . 1 . . . . . . . . 4472 1 126 . 1 1 11 11 VAL HG13 H 1 0.62 0.02 . 1 . . . . . . . . 4472 1 127 . 1 1 11 11 VAL CG2 C 13 21.2 0.2 . 1 . . . . . . . . 4472 1 128 . 1 1 11 11 VAL CG1 C 13 21.6 0.2 . 1 . . . . . . . . 4472 1 129 . 1 1 12 12 ASP N N 15 124.6 0.2 . 1 . . . . . . . . 4472 1 130 . 1 1 12 12 ASP H H 1 8.11 0.02 . 1 . . . . . . . . 4472 1 131 . 1 1 12 12 ASP CA C 13 55.2 0.2 . 1 . . . . . . . . 4472 1 132 . 1 1 12 12 ASP HA H 1 4.69 0.02 . 1 . . . . . . . . 4472 1 133 . 1 1 12 12 ASP CB C 13 44 0.2 . 1 . . . . . . . . 4472 1 134 . 1 1 12 12 ASP HB2 H 1 2.72 0.02 . 2 . . . . . . . . 4472 1 135 . 1 1 12 12 ASP HB3 H 1 2.53 0.02 . 2 . . . . . . . . 4472 1 136 . 1 1 13 13 ASP N N 15 123.3 0.2 . 1 . . . . . . . . 4472 1 137 . 1 1 13 13 ASP H H 1 9.54 0.02 . 1 . . . . . . . . 4472 1 138 . 1 1 13 13 ASP CA C 13 54.8 0.2 . 1 . . . . . . . . 4472 1 139 . 1 1 13 13 ASP HA H 1 5.07 0.02 . 1 . . . . . . . . 4472 1 140 . 1 1 13 13 ASP CB C 13 39.1 0.2 . 1 . . . . . . . . 4472 1 141 . 1 1 13 13 ASP HB2 H 1 2.94 0.02 . 2 . . . . . . . . 4472 1 142 . 1 1 13 13 ASP HB3 H 1 2.79 0.02 . 2 . . . . . . . . 4472 1 143 . 1 1 14 14 PHE N N 15 123.7 0.2 . 1 . . . . . . . . 4472 1 144 . 1 1 14 14 PHE H H 1 10.3 0.02 . 1 . . . . . . . . 4472 1 145 . 1 1 14 14 PHE CA C 13 54.2 0.2 . 1 . . . . . . . . 4472 1 146 . 1 1 14 14 PHE HA H 1 5.25 0.02 . 1 . . . . . . . . 4472 1 147 . 1 1 14 14 PHE CB C 13 38 0.2 . 1 . . . . . . . . 4472 1 148 . 1 1 14 14 PHE HB2 H 1 3.18 0.02 . 2 . . . . . . . . 4472 1 149 . 1 1 14 14 PHE HB3 H 1 3.13 0.02 . 2 . . . . . . . . 4472 1 150 . 1 1 14 14 PHE HD1 H 1 7.44 0.02 . 3 . . . . . . . . 4472 1 151 . 1 1 14 14 PHE CD1 C 13 130.6 0.2 . 3 . . . . . . . . 4472 1 152 . 1 1 15 15 SER CA C 13 61.8 0.2 . 1 . . . . . . . . 4472 1 153 . 1 1 15 15 SER HA H 1 4.03 0.02 . 1 . . . . . . . . 4472 1 154 . 1 1 15 15 SER CB C 13 61.8 0.2 . 1 . . . . . . . . 4472 1 155 . 1 1 16 16 THR CA C 13 65.1 0.2 . 1 . . . . . . . . 4472 1 156 . 1 1 16 16 THR HA H 1 3.82 0.02 . 1 . . . . . . . . 4472 1 157 . 1 1 16 16 THR CB C 13 68.1 0.2 . 1 . . . . . . . . 4472 1 158 . 1 1 16 16 THR HB H 1 3.5 0.02 . 1 . . . . . . . . 4472 1 159 . 1 1 16 16 THR HG21 H 1 1.2 0.02 . 1 . . . . . . . . 4472 1 160 . 1 1 16 16 THR HG22 H 1 1.2 0.02 . 1 . . . . . . . . 4472 1 161 . 1 1 16 16 THR HG23 H 1 1.2 0.02 . 1 . . . . . . . . 4472 1 162 . 1 1 16 16 THR CG2 C 13 21.6 0.2 . 1 . . . . . . . . 4472 1 163 . 1 1 17 17 MET N N 15 119.3 0.2 . 1 . . . . . . . . 4472 1 164 . 1 1 17 17 MET H H 1 6.69 0.02 . 1 . . . . . . . . 4472 1 165 . 1 1 17 17 MET CA C 13 56 0.2 . 1 . . . . . . . . 4472 1 166 . 1 1 17 17 MET HA H 1 4.55 0.02 . 1 . . . . . . . . 4472 1 167 . 1 1 17 17 MET CB C 13 30.9 0.2 . 1 . . . . . . . . 4472 1 168 . 1 1 17 17 MET HB2 H 1 2.29 0.02 . 2 . . . . . . . . 4472 1 169 . 1 1 17 17 MET HB3 H 1 2.14 0.02 . 2 . . . . . . . . 4472 1 170 . 1 1 17 17 MET CG C 13 32 0.2 . 1 . . . . . . . . 4472 1 171 . 1 1 17 17 MET HG2 H 1 2.65 0.02 . 2 . . . . . . . . 4472 1 172 . 1 1 17 17 MET HG3 H 1 2.6 0.02 . 2 . . . . . . . . 4472 1 173 . 1 1 18 18 ARG N N 15 117 0.2 . 1 . . . . . . . . 4472 1 174 . 1 1 18 18 ARG H H 1 7.61 0.02 . 1 . . . . . . . . 4472 1 175 . 1 1 18 18 ARG CA C 13 60.7 0.2 . 1 . . . . . . . . 4472 1 176 . 1 1 18 18 ARG HA H 1 3.84 0.02 . 1 . . . . . . . . 4472 1 177 . 1 1 18 18 ARG CB C 13 30.6 0.2 . 1 . . . . . . . . 4472 1 178 . 1 1 18 18 ARG HB2 H 1 2.07 0.02 . 1 . . . . . . . . 4472 1 179 . 1 1 18 18 ARG HB3 H 1 2.07 0.02 . 1 . . . . . . . . 4472 1 180 . 1 1 18 18 ARG CG C 13 23.3 0.2 . 1 . . . . . . . . 4472 1 181 . 1 1 18 18 ARG HG2 H 1 1.1 0.02 . 2 . . . . . . . . 4472 1 182 . 1 1 18 18 ARG HG3 H 1 0.86 0.02 . 2 . . . . . . . . 4472 1 183 . 1 1 19 19 ARG N N 15 117.1 0.2 . 1 . . . . . . . . 4472 1 184 . 1 1 19 19 ARG H H 1 7.72 0.02 . 1 . . . . . . . . 4472 1 185 . 1 1 19 19 ARG CA C 13 58.9 0.2 . 1 . . . . . . . . 4472 1 186 . 1 1 19 19 ARG HA H 1 3.94 0.02 . 1 . . . . . . . . 4472 1 187 . 1 1 19 19 ARG CB C 13 29.3 0.2 . 1 . . . . . . . . 4472 1 188 . 1 1 19 19 ARG HB2 H 1 1.94 0.02 . 1 . . . . . . . . 4472 1 189 . 1 1 19 19 ARG HB3 H 1 1.94 0.02 . 1 . . . . . . . . 4472 1 190 . 1 1 19 19 ARG CG C 13 26.8 0.2 . 1 . . . . . . . . 4472 1 191 . 1 1 19 19 ARG HG2 H 1 1.71 0.02 . 2 . . . . . . . . 4472 1 192 . 1 1 19 19 ARG HG3 H 1 1.65 0.02 . 2 . . . . . . . . 4472 1 193 . 1 1 19 19 ARG CD C 13 42.8 0.2 . 1 . . . . . . . . 4472 1 194 . 1 1 19 19 ARG HD2 H 1 3.22 0.02 . 1 . . . . . . . . 4472 1 195 . 1 1 19 19 ARG HD3 H 1 3.22 0.02 . 1 . . . . . . . . 4472 1 196 . 1 1 20 20 ILE N N 15 119.9 0.2 . 1 . . . . . . . . 4472 1 197 . 1 1 20 20 ILE H H 1 7.77 0.02 . 1 . . . . . . . . 4472 1 198 . 1 1 20 20 ILE CA C 13 65.3 0.2 . 1 . . . . . . . . 4472 1 199 . 1 1 20 20 ILE HA H 1 3.72 0.02 . 1 . . . . . . . . 4472 1 200 . 1 1 20 20 ILE CB C 13 37.9 0.2 . 1 . . . . . . . . 4472 1 201 . 1 1 20 20 ILE HB H 1 2.09 0.02 . 1 . . . . . . . . 4472 1 202 . 1 1 20 20 ILE HG21 H 1 0.83 0.02 . 1 . . . . . . . . 4472 1 203 . 1 1 20 20 ILE HG22 H 1 0.83 0.02 . 1 . . . . . . . . 4472 1 204 . 1 1 20 20 ILE HG23 H 1 0.83 0.02 . 1 . . . . . . . . 4472 1 205 . 1 1 20 20 ILE CG2 C 13 16.4 0.2 . 1 . . . . . . . . 4472 1 206 . 1 1 20 20 ILE CG1 C 13 29.4 0.2 . 1 . . . . . . . . 4472 1 207 . 1 1 20 20 ILE HG12 H 1 1.81 0.02 . 2 . . . . . . . . 4472 1 208 . 1 1 20 20 ILE HG13 H 1 1.08 0.02 . 2 . . . . . . . . 4472 1 209 . 1 1 20 20 ILE HD11 H 1 0.84 0.02 . 1 . . . . . . . . 4472 1 210 . 1 1 20 20 ILE HD12 H 1 0.84 0.02 . 1 . . . . . . . . 4472 1 211 . 1 1 20 20 ILE HD13 H 1 0.84 0.02 . 1 . . . . . . . . 4472 1 212 . 1 1 20 20 ILE CD1 C 13 13.1 0.2 . 1 . . . . . . . . 4472 1 213 . 1 1 21 21 VAL N N 15 118.8 0.2 . 1 . . . . . . . . 4472 1 214 . 1 1 21 21 VAL H H 1 8.05 0.02 . 1 . . . . . . . . 4472 1 215 . 1 1 21 21 VAL CA C 13 67.4 0.2 . 1 . . . . . . . . 4472 1 216 . 1 1 21 21 VAL HA H 1 3.45 0.02 . 1 . . . . . . . . 4472 1 217 . 1 1 21 21 VAL CB C 13 31.1 0.2 . 1 . . . . . . . . 4472 1 218 . 1 1 21 21 VAL HB H 1 2.13 0.02 . 1 . . . . . . . . 4472 1 219 . 1 1 21 21 VAL HG21 H 1 1.12 0.02 . 1 . . . . . . . . 4472 1 220 . 1 1 21 21 VAL HG22 H 1 1.12 0.02 . 1 . . . . . . . . 4472 1 221 . 1 1 21 21 VAL HG23 H 1 1.12 0.02 . 1 . . . . . . . . 4472 1 222 . 1 1 21 21 VAL HG11 H 1 0.88 0.02 . 1 . . . . . . . . 4472 1 223 . 1 1 21 21 VAL HG12 H 1 0.88 0.02 . 1 . . . . . . . . 4472 1 224 . 1 1 21 21 VAL HG13 H 1 0.88 0.02 . 1 . . . . . . . . 4472 1 225 . 1 1 21 21 VAL CG2 C 13 22.9 0.2 . 1 . . . . . . . . 4472 1 226 . 1 1 21 21 VAL CG1 C 13 22.7 0.2 . 1 . . . . . . . . 4472 1 227 . 1 1 22 22 ARG N N 15 119.4 0.2 . 1 . . . . . . . . 4472 1 228 . 1 1 22 22 ARG H H 1 8.74 0.02 . 1 . . . . . . . . 4472 1 229 . 1 1 22 22 ARG CA C 13 60.5 0.2 . 1 . . . . . . . . 4472 1 230 . 1 1 22 22 ARG HA H 1 3.78 0.02 . 1 . . . . . . . . 4472 1 231 . 1 1 22 22 ARG CB C 13 30.5 0.2 . 1 . . . . . . . . 4472 1 232 . 1 1 22 22 ARG HB2 H 1 2 0.02 . 2 . . . . . . . . 4472 1 233 . 1 1 22 22 ARG HB3 H 1 1.78 0.02 . 2 . . . . . . . . 4472 1 234 . 1 1 22 22 ARG CG C 13 27.2 0.2 . 1 . . . . . . . . 4472 1 235 . 1 1 22 22 ARG HG2 H 1 1.54 0.02 . 1 . . . . . . . . 4472 1 236 . 1 1 22 22 ARG HG3 H 1 1.54 0.02 . 1 . . . . . . . . 4472 1 237 . 1 1 22 22 ARG CD C 13 43.9 0.2 . 1 . . . . . . . . 4472 1 238 . 1 1 22 22 ARG HD2 H 1 3.27 0.02 . 2 . . . . . . . . 4472 1 239 . 1 1 22 22 ARG HD3 H 1 3.07 0.02 . 2 . . . . . . . . 4472 1 240 . 1 1 23 23 ASN N N 15 118.9 0.2 . 1 . . . . . . . . 4472 1 241 . 1 1 23 23 ASN H H 1 8.57 0.02 . 1 . . . . . . . . 4472 1 242 . 1 1 23 23 ASN CA C 13 55.9 0.2 . 1 . . . . . . . . 4472 1 243 . 1 1 23 23 ASN HA H 1 4.55 0.02 . 1 . . . . . . . . 4472 1 244 . 1 1 23 23 ASN CB C 13 37.6 0.2 . 1 . . . . . . . . 4472 1 245 . 1 1 23 23 ASN HB2 H 1 3.03 0.02 . 2 . . . . . . . . 4472 1 246 . 1 1 23 23 ASN HB3 H 1 2.86 0.02 . 2 . . . . . . . . 4472 1 247 . 1 1 24 24 LEU N N 15 122.8 0.2 . 1 . . . . . . . . 4472 1 248 . 1 1 24 24 LEU H H 1 8.32 0.02 . 1 . . . . . . . . 4472 1 249 . 1 1 24 24 LEU CA C 13 58 0.2 . 1 . . . . . . . . 4472 1 250 . 1 1 24 24 LEU HA H 1 4.17 0.02 . 1 . . . . . . . . 4472 1 251 . 1 1 24 24 LEU CB C 13 41.7 0.2 . 1 . . . . . . . . 4472 1 252 . 1 1 24 24 LEU HB2 H 1 1.97 0.02 . 2 . . . . . . . . 4472 1 253 . 1 1 24 24 LEU HB3 H 1 1.33 0.02 . 2 . . . . . . . . 4472 1 254 . 1 1 24 24 LEU HD21 H 1 0.89 0.02 . 1 . . . . . . . . 4472 1 255 . 1 1 24 24 LEU HD22 H 1 0.89 0.02 . 1 . . . . . . . . 4472 1 256 . 1 1 24 24 LEU HD23 H 1 0.89 0.02 . 1 . . . . . . . . 4472 1 257 . 1 1 24 24 LEU HD11 H 1 0.79 0.02 . 1 . . . . . . . . 4472 1 258 . 1 1 24 24 LEU HD12 H 1 0.79 0.02 . 1 . . . . . . . . 4472 1 259 . 1 1 24 24 LEU HD13 H 1 0.79 0.02 . 1 . . . . . . . . 4472 1 260 . 1 1 24 24 LEU CD2 C 13 22.4 0.2 . 1 . . . . . . . . 4472 1 261 . 1 1 24 24 LEU CD1 C 13 26.5 0.2 . 1 . . . . . . . . 4472 1 262 . 1 1 25 25 LEU N N 15 118.1 0.2 . 1 . . . . . . . . 4472 1 263 . 1 1 25 25 LEU H H 1 8.41 0.02 . 1 . . . . . . . . 4472 1 264 . 1 1 25 25 LEU CA C 13 58 0.2 . 1 . . . . . . . . 4472 1 265 . 1 1 25 25 LEU HA H 1 3.85 0.02 . 1 . . . . . . . . 4472 1 266 . 1 1 25 25 LEU CB C 13 39.9 0.2 . 1 . . . . . . . . 4472 1 267 . 1 1 25 25 LEU HB2 H 1 1.82 0.02 . 2 . . . . . . . . 4472 1 268 . 1 1 25 25 LEU HB3 H 1 1.3 0.02 . 2 . . . . . . . . 4472 1 269 . 1 1 25 25 LEU CG C 13 26.1 0.2 . 1 . . . . . . . . 4472 1 270 . 1 1 25 25 LEU HG H 1 1.44 0.02 . 1 . . . . . . . . 4472 1 271 . 1 1 25 25 LEU HD11 H 1 0.11 0.02 . 1 . . . . . . . . 4472 1 272 . 1 1 25 25 LEU HD12 H 1 0.11 0.02 . 1 . . . . . . . . 4472 1 273 . 1 1 25 25 LEU HD13 H 1 0.11 0.02 . 1 . . . . . . . . 4472 1 274 . 1 1 25 25 LEU HD21 H 1 -0.14 0.02 . 1 . . . . . . . . 4472 1 275 . 1 1 25 25 LEU HD22 H 1 -0.14 0.02 . 1 . . . . . . . . 4472 1 276 . 1 1 25 25 LEU HD23 H 1 -0.14 0.02 . 1 . . . . . . . . 4472 1 277 . 1 1 25 25 LEU CD1 C 13 26.1 0.2 . 1 . . . . . . . . 4472 1 278 . 1 1 25 25 LEU CD2 C 13 22 0.2 . 1 . . . . . . . . 4472 1 279 . 1 1 26 26 LYS N N 15 120.4 0.2 . 1 . . . . . . . . 4472 1 280 . 1 1 26 26 LYS H H 1 7.99 0.02 . 1 . . . . . . . . 4472 1 281 . 1 1 26 26 LYS CA C 13 59.6 0.2 . 1 . . . . . . . . 4472 1 282 . 1 1 26 26 LYS HA H 1 3.79 0.02 . 1 . . . . . . . . 4472 1 283 . 1 1 26 26 LYS CB C 13 31.6 0.2 . 1 . . . . . . . . 4472 1 284 . 1 1 26 26 LYS HB2 H 1 2.08 0.02 . 1 . . . . . . . . 4472 1 285 . 1 1 26 26 LYS HB3 H 1 2.08 0.02 . 1 . . . . . . . . 4472 1 286 . 1 1 26 26 LYS CG C 13 24.2 0.2 . 1 . . . . . . . . 4472 1 287 . 1 1 26 26 LYS HG2 H 1 1.61 0.02 . 1 . . . . . . . . 4472 1 288 . 1 1 26 26 LYS HG3 H 1 1.61 0.02 . 1 . . . . . . . . 4472 1 289 . 1 1 26 26 LYS CD C 13 29.4 0.2 . 1 . . . . . . . . 4472 1 290 . 1 1 26 26 LYS HD2 H 1 1.73 0.02 . 1 . . . . . . . . 4472 1 291 . 1 1 26 26 LYS HD3 H 1 1.73 0.02 . 1 . . . . . . . . 4472 1 292 . 1 1 26 26 LYS CE C 13 42.1 0.2 . 1 . . . . . . . . 4472 1 293 . 1 1 26 26 LYS HE2 H 1 3.02 0.02 . 1 . . . . . . . . 4472 1 294 . 1 1 26 26 LYS HE3 H 1 3.02 0.02 . 1 . . . . . . . . 4472 1 295 . 1 1 27 27 GLU N N 15 121.7 0.2 . 1 . . . . . . . . 4472 1 296 . 1 1 27 27 GLU H H 1 7.94 0.02 . 1 . . . . . . . . 4472 1 297 . 1 1 27 27 GLU CA C 13 59.1 0.2 . 1 . . . . . . . . 4472 1 298 . 1 1 27 27 GLU HA H 1 4.02 0.02 . 1 . . . . . . . . 4472 1 299 . 1 1 27 27 GLU CB C 13 28.7 0.2 . 1 . . . . . . . . 4472 1 300 . 1 1 27 27 GLU HB2 H 1 2.29 0.02 . 2 . . . . . . . . 4472 1 301 . 1 1 27 27 GLU HB3 H 1 2.19 0.02 . 2 . . . . . . . . 4472 1 302 . 1 1 27 27 GLU CG C 13 36.1 0.2 . 1 . . . . . . . . 4472 1 303 . 1 1 27 27 GLU HG2 H 1 2.47 0.02 . 2 . . . . . . . . 4472 1 304 . 1 1 27 27 GLU HG3 H 1 2.28 0.02 . 2 . . . . . . . . 4472 1 305 . 1 1 28 28 LEU N N 15 117.3 0.2 . 1 . . . . . . . . 4472 1 306 . 1 1 28 28 LEU H H 1 7.51 0.02 . 1 . . . . . . . . 4472 1 307 . 1 1 28 28 LEU CA C 13 54.7 0.2 . 1 . . . . . . . . 4472 1 308 . 1 1 28 28 LEU HA H 1 4.27 0.02 . 1 . . . . . . . . 4472 1 309 . 1 1 28 28 LEU CB C 13 42.1 0.2 . 1 . . . . . . . . 4472 1 310 . 1 1 28 28 LEU HB2 H 1 2.13 0.02 . 2 . . . . . . . . 4472 1 311 . 1 1 28 28 LEU HB3 H 1 1.83 0.02 . 2 . . . . . . . . 4472 1 312 . 1 1 28 28 LEU CG C 13 26.1 0.2 . 1 . . . . . . . . 4472 1 313 . 1 1 28 28 LEU HG H 1 2.03 0.02 . 1 . . . . . . . . 4472 1 314 . 1 1 28 28 LEU HD11 H 1 0.87 0.02 . 1 . . . . . . . . 4472 1 315 . 1 1 28 28 LEU HD12 H 1 0.87 0.02 . 1 . . . . . . . . 4472 1 316 . 1 1 28 28 LEU HD13 H 1 0.87 0.02 . 1 . . . . . . . . 4472 1 317 . 1 1 28 28 LEU HD21 H 1 0.86 0.02 . 1 . . . . . . . . 4472 1 318 . 1 1 28 28 LEU HD22 H 1 0.86 0.02 . 1 . . . . . . . . 4472 1 319 . 1 1 28 28 LEU HD23 H 1 0.86 0.02 . 1 . . . . . . . . 4472 1 320 . 1 1 28 28 LEU CD1 C 13 24.6 0.2 . 1 . . . . . . . . 4472 1 321 . 1 1 28 28 LEU CD2 C 13 21.6 0.2 . 1 . . . . . . . . 4472 1 322 . 1 1 29 29 GLY N N 15 106 0.2 . 1 . . . . . . . . 4472 1 323 . 1 1 29 29 GLY H H 1 7.75 0.02 . 1 . . . . . . . . 4472 1 324 . 1 1 29 29 GLY CA C 13 44.7 0.2 . 1 . . . . . . . . 4472 1 325 . 1 1 29 29 GLY HA2 H 1 3.95 0.02 . 2 . . . . . . . . 4472 1 326 . 1 1 29 29 GLY HA3 H 1 3.53 0.02 . 2 . . . . . . . . 4472 1 327 . 1 1 30 30 PHE N N 15 120.9 0.2 . 1 . . . . . . . . 4472 1 328 . 1 1 30 30 PHE H H 1 8.22 0.02 . 1 . . . . . . . . 4472 1 329 . 1 1 30 30 PHE CA C 13 57.3 0.2 . 1 . . . . . . . . 4472 1 330 . 1 1 30 30 PHE HA H 1 4.91 0.02 . 1 . . . . . . . . 4472 1 331 . 1 1 30 30 PHE CB C 13 38.4 0.2 . 1 . . . . . . . . 4472 1 332 . 1 1 30 30 PHE HB2 H 1 3.15 0.02 . 2 . . . . . . . . 4472 1 333 . 1 1 30 30 PHE HB3 H 1 2.47 0.02 . 2 . . . . . . . . 4472 1 334 . 1 1 30 30 PHE HD1 H 1 7.4 0.02 . 3 . . . . . . . . 4472 1 335 . 1 1 30 30 PHE CD1 C 13 131.3 0.2 . 3 . . . . . . . . 4472 1 336 . 1 1 30 30 PHE CE1 C 13 129.3 0.2 . 3 . . . . . . . . 4472 1 337 . 1 1 30 30 PHE HE1 H 1 7.31 0.02 . 3 . . . . . . . . 4472 1 338 . 1 1 31 31 ASN N N 15 118.3 0.2 . 1 . . . . . . . . 4472 1 339 . 1 1 31 31 ASN H H 1 8.37 0.02 . 1 . . . . . . . . 4472 1 340 . 1 1 31 31 ASN CA C 13 53.5 0.2 . 1 . . . . . . . . 4472 1 341 . 1 1 31 31 ASN HA H 1 4.71 0.02 . 1 . . . . . . . . 4472 1 342 . 1 1 31 31 ASN CB C 13 40.6 0.2 . 1 . . . . . . . . 4472 1 343 . 1 1 31 31 ASN HB2 H 1 2.82 0.02 . 2 . . . . . . . . 4472 1 344 . 1 1 31 31 ASN HB3 H 1 2.66 0.02 . 2 . . . . . . . . 4472 1 345 . 1 1 32 32 ASN N N 15 124.2 0.2 . 1 . . . . . . . . 4472 1 346 . 1 1 32 32 ASN H H 1 9.86 0.02 . 1 . . . . . . . . 4472 1 347 . 1 1 32 32 ASN CA C 13 52.1 0.2 . 1 . . . . . . . . 4472 1 348 . 1 1 32 32 ASN HA H 1 5 0.02 . 1 . . . . . . . . 4472 1 349 . 1 1 32 32 ASN CB C 13 36.4 0.2 . 1 . . . . . . . . 4472 1 350 . 1 1 32 32 ASN HB2 H 1 3.28 0.02 . 2 . . . . . . . . 4472 1 351 . 1 1 32 32 ASN HB3 H 1 2.88 0.02 . 2 . . . . . . . . 4472 1 352 . 1 1 33 33 VAL N N 15 122 0.2 . 1 . . . . . . . . 4472 1 353 . 1 1 33 33 VAL H H 1 7.53 0.02 . 1 . . . . . . . . 4472 1 354 . 1 1 33 33 VAL CA C 13 60.8 0.2 . 1 . . . . . . . . 4472 1 355 . 1 1 33 33 VAL HA H 1 5 0.02 . 1 . . . . . . . . 4472 1 356 . 1 1 33 33 VAL CB C 13 36.2 0.2 . 1 . . . . . . . . 4472 1 357 . 1 1 33 33 VAL HB H 1 1.84 0.02 . 1 . . . . . . . . 4472 1 358 . 1 1 33 33 VAL HG11 H 1 0.79 0.02 . 2 . . . . . . . . 4472 1 359 . 1 1 33 33 VAL HG12 H 1 0.79 0.02 . 2 . . . . . . . . 4472 1 360 . 1 1 33 33 VAL HG13 H 1 0.79 0.02 . 2 . . . . . . . . 4472 1 361 . 1 1 33 33 VAL CG1 C 13 22.4 0.2 . 2 . . . . . . . . 4472 1 362 . 1 1 34 34 GLU N N 15 126.6 0.2 . 1 . . . . . . . . 4472 1 363 . 1 1 34 34 GLU H H 1 9.06 0.02 . 1 . . . . . . . . 4472 1 364 . 1 1 34 34 GLU CA C 13 53.8 0.2 . 1 . . . . . . . . 4472 1 365 . 1 1 34 34 GLU HA H 1 4.94 0.02 . 1 . . . . . . . . 4472 1 366 . 1 1 34 34 GLU CB C 13 33.8 0.2 . 1 . . . . . . . . 4472 1 367 . 1 1 34 34 GLU HB2 H 1 2.29 0.02 . 2 . . . . . . . . 4472 1 368 . 1 1 34 34 GLU HB3 H 1 2.15 0.02 . 2 . . . . . . . . 4472 1 369 . 1 1 34 34 GLU CG C 13 35.7 0.2 . 1 . . . . . . . . 4472 1 370 . 1 1 34 34 GLU HG2 H 1 2.57 0.02 . 2 . . . . . . . . 4472 1 371 . 1 1 34 34 GLU HG3 H 1 2.46 0.02 . 2 . . . . . . . . 4472 1 372 . 1 1 35 35 GLU N N 15 120.9 0.2 . 1 . . . . . . . . 4472 1 373 . 1 1 35 35 GLU H H 1 8.98 0.02 . 1 . . . . . . . . 4472 1 374 . 1 1 35 35 GLU CA C 13 54.7 0.2 . 1 . . . . . . . . 4472 1 375 . 1 1 35 35 GLU HA H 1 5.48 0.02 . 1 . . . . . . . . 4472 1 376 . 1 1 35 35 GLU CB C 13 34.6 0.2 . 1 . . . . . . . . 4472 1 377 . 1 1 35 35 GLU HB2 H 1 1.92 0.02 . 2 . . . . . . . . 4472 1 378 . 1 1 35 35 GLU HB3 H 1 1.87 0.02 . 2 . . . . . . . . 4472 1 379 . 1 1 35 35 GLU CG C 13 36.9 0.2 . 1 . . . . . . . . 4472 1 380 . 1 1 35 35 GLU HG2 H 1 2.14 0.02 . 2 . . . . . . . . 4472 1 381 . 1 1 35 35 GLU HG3 H 1 2.05 0.02 . 2 . . . . . . . . 4472 1 382 . 1 1 36 36 ALA N N 15 120.1 0.2 . 1 . . . . . . . . 4472 1 383 . 1 1 36 36 ALA H H 1 8.89 0.02 . 1 . . . . . . . . 4472 1 384 . 1 1 36 36 ALA CA C 13 50.3 0.2 . 1 . . . . . . . . 4472 1 385 . 1 1 36 36 ALA HA H 1 4.82 0.02 . 1 . . . . . . . . 4472 1 386 . 1 1 36 36 ALA HB1 H 1 1.29 0.02 . 1 . . . . . . . . 4472 1 387 . 1 1 36 36 ALA HB2 H 1 1.29 0.02 . 1 . . . . . . . . 4472 1 388 . 1 1 36 36 ALA HB3 H 1 1.29 0.02 . 1 . . . . . . . . 4472 1 389 . 1 1 36 36 ALA CB C 13 22.4 0.2 . 1 . . . . . . . . 4472 1 390 . 1 1 37 37 GLU N N 15 117 0.2 . 1 . . . . . . . . 4472 1 391 . 1 1 37 37 GLU H H 1 9.47 0.02 . 1 . . . . . . . . 4472 1 392 . 1 1 37 37 GLU CA C 13 56.3 0.2 . 1 . . . . . . . . 4472 1 393 . 1 1 37 37 GLU HA H 1 4.67 0.02 . 1 . . . . . . . . 4472 1 394 . 1 1 37 37 GLU CB C 13 31.8 0.2 . 1 . . . . . . . . 4472 1 395 . 1 1 37 37 GLU HB2 H 1 2.07 0.02 . 1 . . . . . . . . 4472 1 396 . 1 1 37 37 GLU HB3 H 1 2.07 0.02 . 1 . . . . . . . . 4472 1 397 . 1 1 37 37 GLU CG C 13 35 0.2 . 1 . . . . . . . . 4472 1 398 . 1 1 37 37 GLU HG2 H 1 2.25 0.02 . 2 . . . . . . . . 4472 1 399 . 1 1 37 37 GLU HG3 H 1 2.18 0.02 . 2 . . . . . . . . 4472 1 400 . 1 1 38 38 ASP N N 15 110.9 0.2 . 1 . . . . . . . . 4472 1 401 . 1 1 38 38 ASP H H 1 7.55 0.02 . 1 . . . . . . . . 4472 1 402 . 1 1 38 38 ASP CA C 13 53.8 0.2 . 1 . . . . . . . . 4472 1 403 . 1 1 38 38 ASP HA H 1 5.42 0.02 . 1 . . . . . . . . 4472 1 404 . 1 1 38 38 ASP CB C 13 41.3 0.2 . 1 . . . . . . . . 4472 1 405 . 1 1 38 38 ASP HB2 H 1 3.62 0.02 . 2 . . . . . . . . 4472 1 406 . 1 1 38 38 ASP HB3 H 1 3.23 0.02 . 2 . . . . . . . . 4472 1 407 . 1 1 39 39 GLY N N 15 101.6 0.2 . 1 . . . . . . . . 4472 1 408 . 1 1 39 39 GLY H H 1 8 0.02 . 1 . . . . . . . . 4472 1 409 . 1 1 39 39 GLY CA C 13 48.4 0.2 . 1 . . . . . . . . 4472 1 410 . 1 1 39 39 GLY HA2 H 1 3.75 0.02 . 2 . . . . . . . . 4472 1 411 . 1 1 39 39 GLY HA3 H 1 3.58 0.02 . 2 . . . . . . . . 4472 1 412 . 1 1 40 40 VAL N N 15 122.7 0.2 . 1 . . . . . . . . 4472 1 413 . 1 1 40 40 VAL H H 1 8.01 0.02 . 1 . . . . . . . . 4472 1 414 . 1 1 40 40 VAL CA C 13 66.2 0.2 . 1 . . . . . . . . 4472 1 415 . 1 1 40 40 VAL HA H 1 3.5 0.02 . 1 . . . . . . . . 4472 1 416 . 1 1 40 40 VAL CB C 13 31.3 0.2 . 1 . . . . . . . . 4472 1 417 . 1 1 40 40 VAL HB H 1 2.25 0.02 . 1 . . . . . . . . 4472 1 418 . 1 1 40 40 VAL HG11 H 1 0.9 0.02 . 1 . . . . . . . . 4472 1 419 . 1 1 40 40 VAL HG12 H 1 0.9 0.02 . 1 . . . . . . . . 4472 1 420 . 1 1 40 40 VAL HG13 H 1 0.9 0.02 . 1 . . . . . . . . 4472 1 421 . 1 1 40 40 VAL HG21 H 1 0.9 0.02 . 1 . . . . . . . . 4472 1 422 . 1 1 40 40 VAL HG22 H 1 0.9 0.02 . 1 . . . . . . . . 4472 1 423 . 1 1 40 40 VAL HG23 H 1 0.9 0.02 . 1 . . . . . . . . 4472 1 424 . 1 1 40 40 VAL CG1 C 13 20.9 0.2 . 1 . . . . . . . . 4472 1 425 . 1 1 40 40 VAL CG2 C 13 22.7 0.2 . 1 . . . . . . . . 4472 1 426 . 1 1 41 41 ASP N N 15 121.1 0.2 . 1 . . . . . . . . 4472 1 427 . 1 1 41 41 ASP H H 1 8.66 0.02 . 1 . . . . . . . . 4472 1 428 . 1 1 41 41 ASP CA C 13 56.3 0.2 . 1 . . . . . . . . 4472 1 429 . 1 1 41 41 ASP HA H 1 4.4 0.02 . 1 . . . . . . . . 4472 1 430 . 1 1 41 41 ASP CB C 13 42.4 0.2 . 1 . . . . . . . . 4472 1 431 . 1 1 41 41 ASP HB2 H 1 2.99 0.02 . 2 . . . . . . . . 4472 1 432 . 1 1 41 41 ASP HB3 H 1 2.61 0.02 . 2 . . . . . . . . 4472 1 433 . 1 1 42 42 ALA N N 15 116.7 0.2 . 1 . . . . . . . . 4472 1 434 . 1 1 42 42 ALA H H 1 8.29 0.02 . 1 . . . . . . . . 4472 1 435 . 1 1 42 42 ALA CA C 13 55.1 0.2 . 1 . . . . . . . . 4472 1 436 . 1 1 42 42 ALA HA H 1 3.62 0.02 . 1 . . . . . . . . 4472 1 437 . 1 1 42 42 ALA HB1 H 1 1.35 0.02 . 1 . . . . . . . . 4472 1 438 . 1 1 42 42 ALA HB2 H 1 1.35 0.02 . 1 . . . . . . . . 4472 1 439 . 1 1 42 42 ALA HB3 H 1 1.35 0.02 . 1 . . . . . . . . 4472 1 440 . 1 1 42 42 ALA CB C 13 19.5 0.2 . 1 . . . . . . . . 4472 1 441 . 1 1 43 43 LEU N N 15 118.3 0.2 . 1 . . . . . . . . 4472 1 442 . 1 1 43 43 LEU H H 1 8.17 0.02 . 1 . . . . . . . . 4472 1 443 . 1 1 43 43 LEU CA C 13 58 0.2 . 1 . . . . . . . . 4472 1 444 . 1 1 43 43 LEU HA H 1 3.76 0.02 . 1 . . . . . . . . 4472 1 445 . 1 1 43 43 LEU CB C 13 41 0.2 . 1 . . . . . . . . 4472 1 446 . 1 1 43 43 LEU HB2 H 1 1.74 0.02 . 2 . . . . . . . . 4472 1 447 . 1 1 43 43 LEU HB3 H 1 1.53 0.02 . 2 . . . . . . . . 4472 1 448 . 1 1 43 43 LEU CG C 13 26.5 0.2 . 1 . . . . . . . . 4472 1 449 . 1 1 43 43 LEU HG H 1 1.68 0.02 . 1 . . . . . . . . 4472 1 450 . 1 1 43 43 LEU HD21 H 1 0.8 0.02 . 1 . . . . . . . . 4472 1 451 . 1 1 43 43 LEU HD22 H 1 0.8 0.02 . 1 . . . . . . . . 4472 1 452 . 1 1 43 43 LEU HD23 H 1 0.8 0.02 . 1 . . . . . . . . 4472 1 453 . 1 1 43 43 LEU HD11 H 1 0.72 0.02 . 1 . . . . . . . . 4472 1 454 . 1 1 43 43 LEU HD12 H 1 0.72 0.02 . 1 . . . . . . . . 4472 1 455 . 1 1 43 43 LEU HD13 H 1 0.72 0.02 . 1 . . . . . . . . 4472 1 456 . 1 1 43 43 LEU CD2 C 13 25.3 0.2 . 1 . . . . . . . . 4472 1 457 . 1 1 43 43 LEU CD1 C 13 23.5 0.2 . 1 . . . . . . . . 4472 1 458 . 1 1 44 44 ASN N N 15 116.6 0.2 . 1 . . . . . . . . 4472 1 459 . 1 1 44 44 ASN H H 1 7.94 0.02 . 1 . . . . . . . . 4472 1 460 . 1 1 44 44 ASN CA C 13 56 0.2 . 1 . . . . . . . . 4472 1 461 . 1 1 44 44 ASN HA H 1 4.39 0.02 . 1 . . . . . . . . 4472 1 462 . 1 1 44 44 ASN CB C 13 38 0.2 . 1 . . . . . . . . 4472 1 463 . 1 1 44 44 ASN HB2 H 1 3.06 0.02 . 2 . . . . . . . . 4472 1 464 . 1 1 44 44 ASN HB3 H 1 2.87 0.02 . 2 . . . . . . . . 4472 1 465 . 1 1 45 45 LYS N N 15 120.2 0.2 . 1 . . . . . . . . 4472 1 466 . 1 1 45 45 LYS H H 1 7.94 0.02 . 1 . . . . . . . . 4472 1 467 . 1 1 45 45 LYS CA C 13 60 0.2 . 1 . . . . . . . . 4472 1 468 . 1 1 45 45 LYS HA H 1 4.11 0.02 . 1 . . . . . . . . 4472 1 469 . 1 1 45 45 LYS CB C 13 31.7 0.2 . 1 . . . . . . . . 4472 1 470 . 1 1 45 45 LYS HB2 H 1 1.78 0.02 . 1 . . . . . . . . 4472 1 471 . 1 1 45 45 LYS HB3 H 1 1.78 0.02 . 1 . . . . . . . . 4472 1 472 . 1 1 45 45 LYS CG C 13 26.8 0.2 . 1 . . . . . . . . 4472 1 473 . 1 1 45 45 LYS HG2 H 1 1.71 0.02 . 2 . . . . . . . . 4472 1 474 . 1 1 45 45 LYS HG3 H 1 1.49 0.02 . 2 . . . . . . . . 4472 1 475 . 1 1 45 45 LYS CD C 13 29.1 0.2 . 1 . . . . . . . . 4472 1 476 . 1 1 45 45 LYS HD2 H 1 1.62 0.02 . 2 . . . . . . . . 4472 1 477 . 1 1 45 45 LYS HD3 H 1 1.48 0.02 . 2 . . . . . . . . 4472 1 478 . 1 1 45 45 LYS CE C 13 42.4 0.2 . 1 . . . . . . . . 4472 1 479 . 1 1 45 45 LYS HE2 H 1 3.2 0.02 . 2 . . . . . . . . 4472 1 480 . 1 1 45 45 LYS HE3 H 1 3.11 0.02 . 2 . . . . . . . . 4472 1 481 . 1 1 46 46 LEU N N 15 118.7 0.2 . 1 . . . . . . . . 4472 1 482 . 1 1 46 46 LEU H H 1 8.75 0.02 . 1 . . . . . . . . 4472 1 483 . 1 1 46 46 LEU CA C 13 57.4 0.2 . 1 . . . . . . . . 4472 1 484 . 1 1 46 46 LEU HA H 1 3.85 0.02 . 1 . . . . . . . . 4472 1 485 . 1 1 46 46 LEU CB C 13 42.1 0.2 . 1 . . . . . . . . 4472 1 486 . 1 1 46 46 LEU HB2 H 1 1.72 0.02 . 2 . . . . . . . . 4472 1 487 . 1 1 46 46 LEU HB3 H 1 1.4 0.02 . 2 . . . . . . . . 4472 1 488 . 1 1 46 46 LEU CG C 13 30.9 0.2 . 1 . . . . . . . . 4472 1 489 . 1 1 46 46 LEU HG H 1 1.4 0.02 . 1 . . . . . . . . 4472 1 490 . 1 1 46 46 LEU HD11 H 1 0.53 0.02 . 1 . . . . . . . . 4472 1 491 . 1 1 46 46 LEU HD12 H 1 0.53 0.02 . 1 . . . . . . . . 4472 1 492 . 1 1 46 46 LEU HD13 H 1 0.53 0.02 . 1 . . . . . . . . 4472 1 493 . 1 1 46 46 LEU HD21 H 1 0.34 0.02 . 1 . . . . . . . . 4472 1 494 . 1 1 46 46 LEU HD22 H 1 0.34 0.02 . 1 . . . . . . . . 4472 1 495 . 1 1 46 46 LEU HD23 H 1 0.34 0.02 . 1 . . . . . . . . 4472 1 496 . 1 1 46 46 LEU CD1 C 13 25 0.2 . 1 . . . . . . . . 4472 1 497 . 1 1 46 46 LEU CD2 C 13 22.4 0.2 . 1 . . . . . . . . 4472 1 498 . 1 1 47 47 GLN N N 15 116.5 0.2 . 1 . . . . . . . . 4472 1 499 . 1 1 47 47 GLN H H 1 7.88 0.02 . 1 . . . . . . . . 4472 1 500 . 1 1 47 47 GLN CA C 13 57.6 0.2 . 1 . . . . . . . . 4472 1 501 . 1 1 47 47 GLN HA H 1 4.04 0.02 . 1 . . . . . . . . 4472 1 502 . 1 1 47 47 GLN CB C 13 27.9 0.2 . 1 . . . . . . . . 4472 1 503 . 1 1 47 47 GLN CG C 13 33.5 0.2 . 1 . . . . . . . . 4472 1 504 . 1 1 48 48 ALA N N 15 120.4 0.2 . 1 . . . . . . . . 4472 1 505 . 1 1 48 48 ALA H H 1 7.64 0.02 . 1 . . . . . . . . 4472 1 506 . 1 1 48 48 ALA CA C 13 53.3 0.2 . 1 . . . . . . . . 4472 1 507 . 1 1 48 48 ALA HA H 1 4.33 0.02 . 1 . . . . . . . . 4472 1 508 . 1 1 48 48 ALA HB1 H 1 1.67 0.02 . 1 . . . . . . . . 4472 1 509 . 1 1 48 48 ALA HB2 H 1 1.67 0.02 . 1 . . . . . . . . 4472 1 510 . 1 1 48 48 ALA HB3 H 1 1.67 0.02 . 1 . . . . . . . . 4472 1 511 . 1 1 48 48 ALA CB C 13 19 0.2 . 1 . . . . . . . . 4472 1 512 . 1 1 49 49 GLY N N 15 104 0.2 . 1 . . . . . . . . 4472 1 513 . 1 1 49 49 GLY H H 1 7.61 0.02 . 1 . . . . . . . . 4472 1 514 . 1 1 49 49 GLY CA C 13 44.3 0.2 . 1 . . . . . . . . 4472 1 515 . 1 1 49 49 GLY HA2 H 1 4.32 0.02 . 2 . . . . . . . . 4472 1 516 . 1 1 49 49 GLY HA3 H 1 4.08 0.02 . 2 . . . . . . . . 4472 1 517 . 1 1 50 50 GLY N N 15 103.6 0.2 . 1 . . . . . . . . 4472 1 518 . 1 1 50 50 GLY H H 1 8.38 0.02 . 1 . . . . . . . . 4472 1 519 . 1 1 50 50 GLY CA C 13 45.1 0.2 . 1 . . . . . . . . 4472 1 520 . 1 1 50 50 GLY HA2 H 1 3.94 0.02 . 2 . . . . . . . . 4472 1 521 . 1 1 50 50 GLY HA3 H 1 3.67 0.02 . 2 . . . . . . . . 4472 1 522 . 1 1 51 51 TYR N N 15 118.5 0.2 . 1 . . . . . . . . 4472 1 523 . 1 1 51 51 TYR H H 1 8.11 0.02 . 1 . . . . . . . . 4472 1 524 . 1 1 51 51 TYR CA C 13 60.7 0.2 . 1 . . . . . . . . 4472 1 525 . 1 1 51 51 TYR HA H 1 4.04 0.02 . 1 . . . . . . . . 4472 1 526 . 1 1 51 51 TYR CB C 13 38.8 0.2 . 1 . . . . . . . . 4472 1 527 . 1 1 51 51 TYR HB2 H 1 3.04 0.02 . 2 . . . . . . . . 4472 1 528 . 1 1 51 51 TYR HB3 H 1 2.51 0.02 . 2 . . . . . . . . 4472 1 529 . 1 1 51 51 TYR CD1 C 13 132.2 0.2 . 3 . . . . . . . . 4472 1 530 . 1 1 51 51 TYR HD1 H 1 6.78 0.02 . 3 . . . . . . . . 4472 1 531 . 1 1 51 51 TYR CE1 C 13 117.9 0.2 . 3 . . . . . . . . 4472 1 532 . 1 1 51 51 TYR HE1 H 1 6.66 0.02 . 3 . . . . . . . . 4472 1 533 . 1 1 52 52 GLY N N 15 106.8 0.2 . 1 . . . . . . . . 4472 1 534 . 1 1 52 52 GLY H H 1 9.52 0.02 . 1 . . . . . . . . 4472 1 535 . 1 1 52 52 GLY CA C 13 44.3 0.2 . 1 . . . . . . . . 4472 1 536 . 1 1 52 52 GLY HA2 H 1 4.51 0.02 . 2 . . . . . . . . 4472 1 537 . 1 1 52 52 GLY HA3 H 1 3.45 0.02 . 2 . . . . . . . . 4472 1 538 . 1 1 53 53 PHE N N 15 121.4 0.2 . 1 . . . . . . . . 4472 1 539 . 1 1 53 53 PHE H H 1 7.58 0.02 . 1 . . . . . . . . 4472 1 540 . 1 1 53 53 PHE CA C 13 58 0.2 . 1 . . . . . . . . 4472 1 541 . 1 1 53 53 PHE HA H 1 4.06 0.02 . 1 . . . . . . . . 4472 1 542 . 1 1 53 53 PHE CB C 13 43.2 0.2 . 1 . . . . . . . . 4472 1 543 . 1 1 53 53 PHE HB2 H 1 2.1 0.02 . 2 . . . . . . . . 4472 1 544 . 1 1 53 53 PHE HB3 H 1 1.98 0.02 . 2 . . . . . . . . 4472 1 545 . 1 1 53 53 PHE HD1 H 1 6.91 0.02 . 3 . . . . . . . . 4472 1 546 . 1 1 53 53 PHE CD1 C 13 132 0.2 . 3 . . . . . . . . 4472 1 547 . 1 1 54 54 VAL N N 15 127 0.2 . 1 . . . . . . . . 4472 1 548 . 1 1 54 54 VAL H H 1 8.25 0.02 . 1 . . . . . . . . 4472 1 549 . 1 1 54 54 VAL CA C 13 60.9 0.2 . 1 . . . . . . . . 4472 1 550 . 1 1 54 54 VAL HA H 1 5.08 0.02 . 1 . . . . . . . . 4472 1 551 . 1 1 54 54 VAL CB C 13 34.3 0.2 . 1 . . . . . . . . 4472 1 552 . 1 1 54 54 VAL HB H 1 2.1 0.02 . 1 . . . . . . . . 4472 1 553 . 1 1 54 54 VAL HG21 H 1 0.82 0.02 . 1 . . . . . . . . 4472 1 554 . 1 1 54 54 VAL HG22 H 1 0.82 0.02 . 1 . . . . . . . . 4472 1 555 . 1 1 54 54 VAL HG23 H 1 0.82 0.02 . 1 . . . . . . . . 4472 1 556 . 1 1 54 54 VAL HG11 H 1 0.74 0.02 . 1 . . . . . . . . 4472 1 557 . 1 1 54 54 VAL HG12 H 1 0.74 0.02 . 1 . . . . . . . . 4472 1 558 . 1 1 54 54 VAL HG13 H 1 0.74 0.02 . 1 . . . . . . . . 4472 1 559 . 1 1 54 54 VAL CG2 C 13 22.4 0.2 . 1 . . . . . . . . 4472 1 560 . 1 1 54 54 VAL CG1 C 13 20.5 0.2 . 1 . . . . . . . . 4472 1 561 . 1 1 55 55 ILE N N 15 128.6 0.2 . 1 . . . . . . . . 4472 1 562 . 1 1 55 55 ILE H H 1 9.36 0.02 . 1 . . . . . . . . 4472 1 563 . 1 1 55 55 ILE CA C 13 60.3 0.2 . 1 . . . . . . . . 4472 1 564 . 1 1 55 55 ILE HA H 1 5.07 0.02 . 1 . . . . . . . . 4472 1 565 . 1 1 55 55 ILE CB C 13 39.7 0.2 . 1 . . . . . . . . 4472 1 566 . 1 1 55 55 ILE HB H 1 1.88 0.02 . 1 . . . . . . . . 4472 1 567 . 1 1 55 55 ILE HG21 H 1 0.93 0.02 . 1 . . . . . . . . 4472 1 568 . 1 1 55 55 ILE HG22 H 1 0.93 0.02 . 1 . . . . . . . . 4472 1 569 . 1 1 55 55 ILE HG23 H 1 0.93 0.02 . 1 . . . . . . . . 4472 1 570 . 1 1 55 55 ILE CG2 C 13 16.8 0.2 . 1 . . . . . . . . 4472 1 571 . 1 1 55 55 ILE CG1 C 13 27.9 0.2 . 1 . . . . . . . . 4472 1 572 . 1 1 55 55 ILE HG12 H 1 1.97 0.02 . 2 . . . . . . . . 4472 1 573 . 1 1 55 55 ILE HG13 H 1 1.21 0.02 . 2 . . . . . . . . 4472 1 574 . 1 1 55 55 ILE HD11 H 1 0.77 0.02 . 1 . . . . . . . . 4472 1 575 . 1 1 55 55 ILE HD12 H 1 0.77 0.02 . 1 . . . . . . . . 4472 1 576 . 1 1 55 55 ILE HD13 H 1 0.77 0.02 . 1 . . . . . . . . 4472 1 577 . 1 1 55 55 ILE CD1 C 13 13.8 0.2 . 1 . . . . . . . . 4472 1 578 . 1 1 56 56 SER N N 15 118.9 0.2 . 1 . . . . . . . . 4472 1 579 . 1 1 56 56 SER H H 1 9.07 0.02 . 1 . . . . . . . . 4472 1 580 . 1 1 56 56 SER CA C 13 56.6 0.2 . 1 . . . . . . . . 4472 1 581 . 1 1 56 56 SER HA H 1 5.37 0.02 . 1 . . . . . . . . 4472 1 582 . 1 1 56 56 SER CB C 13 65.5 0.2 . 1 . . . . . . . . 4472 1 583 . 1 1 56 56 SER HB2 H 1 3.51 0.02 . 2 . . . . . . . . 4472 1 584 . 1 1 56 56 SER HB3 H 1 3 0.02 . 2 . . . . . . . . 4472 1 585 . 1 1 57 57 ASP N N 15 126.3 0.2 . 1 . . . . . . . . 4472 1 586 . 1 1 57 57 ASP H H 1 8.33 0.02 . 1 . . . . . . . . 4472 1 587 . 1 1 57 57 ASP CA C 13 52.4 0.2 . 1 . . . . . . . . 4472 1 588 . 1 1 57 57 ASP HA H 1 5.66 0.02 . 1 . . . . . . . . 4472 1 589 . 1 1 57 57 ASP CB C 13 43.9 0.2 . 1 . . . . . . . . 4472 1 590 . 1 1 57 57 ASP HB2 H 1 3.76 0.02 . 2 . . . . . . . . 4472 1 591 . 1 1 57 57 ASP HB3 H 1 3.11 0.02 . 2 . . . . . . . . 4472 1 592 . 1 1 58 58 TRP N N 15 120.8 0.2 . 1 . . . . . . . . 4472 1 593 . 1 1 58 58 TRP H H 1 8.1 0.02 . 1 . . . . . . . . 4472 1 594 . 1 1 58 58 TRP CA C 13 59.4 0.2 . 1 . . . . . . . . 4472 1 595 . 1 1 58 58 TRP HA H 1 4.45 0.02 . 1 . . . . . . . . 4472 1 596 . 1 1 58 58 TRP CB C 13 29.8 0.2 . 1 . . . . . . . . 4472 1 597 . 1 1 58 58 TRP HB2 H 1 3.59 0.02 . 2 . . . . . . . . 4472 1 598 . 1 1 58 58 TRP HB3 H 1 3.11 0.02 . 2 . . . . . . . . 4472 1 599 . 1 1 58 58 TRP CD1 C 13 124.5 0.2 . 1 . . . . . . . . 4472 1 600 . 1 1 58 58 TRP CE3 C 13 119.7 0.2 . 1 . . . . . . . . 4472 1 601 . 1 1 58 58 TRP NE1 N 15 130.4 0.2 . 1 . . . . . . . . 4472 1 602 . 1 1 58 58 TRP HD1 H 1 7.11 0.02 . 1 . . . . . . . . 4472 1 603 . 1 1 58 58 TRP HE3 H 1 7.58 0.02 . 1 . . . . . . . . 4472 1 604 . 1 1 58 58 TRP CZ3 C 13 121.6 0.2 . 1 . . . . . . . . 4472 1 605 . 1 1 58 58 TRP CZ2 C 13 115.3 0.2 . 1 . . . . . . . . 4472 1 606 . 1 1 58 58 TRP HE1 H 1 10.32 0.02 . 1 . . . . . . . . 4472 1 607 . 1 1 58 58 TRP HZ3 H 1 7.28 0.02 . 1 . . . . . . . . 4472 1 608 . 1 1 58 58 TRP CH2 C 13 124.4 0.2 . 1 . . . . . . . . 4472 1 609 . 1 1 58 58 TRP HZ2 H 1 7.51 0.02 . 1 . . . . . . . . 4472 1 610 . 1 1 58 58 TRP HH2 H 1 7.38 0.02 . 1 . . . . . . . . 4472 1 611 . 1 1 59 59 ASN N N 15 117 0.2 . 1 . . . . . . . . 4472 1 612 . 1 1 59 59 ASN H H 1 9.27 0.02 . 1 . . . . . . . . 4472 1 613 . 1 1 59 59 ASN CA C 13 54.8 0.2 . 1 . . . . . . . . 4472 1 614 . 1 1 59 59 ASN HA H 1 4.89 0.02 . 1 . . . . . . . . 4472 1 615 . 1 1 59 59 ASN CB C 13 37.2 0.2 . 1 . . . . . . . . 4472 1 616 . 1 1 59 59 ASN HB2 H 1 3.12 0.02 . 2 . . . . . . . . 4472 1 617 . 1 1 59 59 ASN HB3 H 1 3.07 0.02 . 2 . . . . . . . . 4472 1 618 . 1 1 60 60 MET N N 15 128.6 0.2 . 1 . . . . . . . . 4472 1 619 . 1 1 60 60 MET H H 1 7.53 0.02 . 1 . . . . . . . . 4472 1 620 . 1 1 60 60 MET CA C 13 53.8 0.2 . 1 . . . . . . . . 4472 1 621 . 1 1 60 60 MET HA H 1 4.69 0.02 . 1 . . . . . . . . 4472 1 622 . 1 1 60 60 MET CB C 13 32.8 0.2 . 1 . . . . . . . . 4472 1 623 . 1 1 60 60 MET CG C 13 29.1 0.2 . 1 . . . . . . . . 4472 1 624 . 1 1 61 61 PRO CD C 13 50.3 0.2 . 1 . . . . . . . . 4472 1 625 . 1 1 61 61 PRO CA C 13 62.2 0.2 . 1 . . . . . . . . 4472 1 626 . 1 1 61 61 PRO HA H 1 4.48 0.02 . 1 . . . . . . . . 4472 1 627 . 1 1 61 61 PRO CB C 13 32.4 0.2 . 1 . . . . . . . . 4472 1 628 . 1 1 61 61 PRO HB2 H 1 2.33 0.02 . 2 . . . . . . . . 4472 1 629 . 1 1 61 61 PRO HB3 H 1 1.94 0.02 . 2 . . . . . . . . 4472 1 630 . 1 1 61 61 PRO CG C 13 26.8 0.2 . 1 . . . . . . . . 4472 1 631 . 1 1 61 61 PRO HD2 H 1 3.83 0.02 . 2 . . . . . . . . 4472 1 632 . 1 1 61 61 PRO HD3 H 1 3.68 0.02 . 2 . . . . . . . . 4472 1 633 . 1 1 62 62 ASN N N 15 111.1 0.2 . 1 . . . . . . . . 4472 1 634 . 1 1 62 62 ASN H H 1 8.66 0.02 . 1 . . . . . . . . 4472 1 635 . 1 1 62 62 ASN CA C 13 58.7 0.2 . 1 . . . . . . . . 4472 1 636 . 1 1 62 62 ASN HA H 1 4.05 0.02 . 1 . . . . . . . . 4472 1 637 . 1 1 62 62 ASN CB C 13 37.6 0.2 . 1 . . . . . . . . 4472 1 638 . 1 1 62 62 ASN HB2 H 1 3.3 0.02 . 2 . . . . . . . . 4472 1 639 . 1 1 62 62 ASN HB3 H 1 2.58 0.02 . 2 . . . . . . . . 4472 1 640 . 1 1 63 63 MET N N 15 123.1 0.2 . 1 . . . . . . . . 4472 1 641 . 1 1 63 63 MET H H 1 9.43 0.02 . 1 . . . . . . . . 4472 1 642 . 1 1 63 63 MET CA C 13 56.6 0.2 . 1 . . . . . . . . 4472 1 643 . 1 1 63 63 MET HA H 1 4.27 0.02 . 1 . . . . . . . . 4472 1 644 . 1 1 63 63 MET CB C 13 35.7 0.2 . 1 . . . . . . . . 4472 1 645 . 1 1 63 63 MET CG C 13 30.9 0.2 . 1 . . . . . . . . 4472 1 646 . 1 1 63 63 MET HG2 H 1 2.52 0.02 . 2 . . . . . . . . 4472 1 647 . 1 1 63 63 MET HG3 H 1 2.39 0.02 . 2 . . . . . . . . 4472 1 648 . 1 1 64 64 ASP N N 15 127.1 0.2 . 1 . . . . . . . . 4472 1 649 . 1 1 64 64 ASP H H 1 8.72 0.02 . 1 . . . . . . . . 4472 1 650 . 1 1 64 64 ASP CA C 13 53.1 0.2 . 1 . . . . . . . . 4472 1 651 . 1 1 64 64 ASP HA H 1 4.57 0.02 . 1 . . . . . . . . 4472 1 652 . 1 1 64 64 ASP CB C 13 41 0.2 . 1 . . . . . . . . 4472 1 653 . 1 1 64 64 ASP HB2 H 1 3.82 0.02 . 2 . . . . . . . . 4472 1 654 . 1 1 64 64 ASP HB3 H 1 2.87 0.02 . 2 . . . . . . . . 4472 1 655 . 1 1 65 65 GLY N N 15 103.1 0.2 . 1 . . . . . . . . 4472 1 656 . 1 1 65 65 GLY H H 1 9.75 0.02 . 1 . . . . . . . . 4472 1 657 . 1 1 65 65 GLY CA C 13 46.5 0.2 . 1 . . . . . . . . 4472 1 658 . 1 1 65 65 GLY HA2 H 1 4.21 0.02 . 2 . . . . . . . . 4472 1 659 . 1 1 65 65 GLY HA3 H 1 3.5 0.02 . 2 . . . . . . . . 4472 1 660 . 1 1 66 66 LEU N N 15 122.2 0.2 . 1 . . . . . . . . 4472 1 661 . 1 1 66 66 LEU H H 1 7.11 0.02 . 1 . . . . . . . . 4472 1 662 . 1 1 66 66 LEU CA C 13 56.6 0.2 . 1 . . . . . . . . 4472 1 663 . 1 1 66 66 LEU HA H 1 3.64 0.02 . 1 . . . . . . . . 4472 1 664 . 1 1 66 66 LEU CB C 13 39.8 0.2 . 1 . . . . . . . . 4472 1 665 . 1 1 66 66 LEU HB2 H 1 1.64 0.02 . 2 . . . . . . . . 4472 1 666 . 1 1 66 66 LEU HB3 H 1 0.19 0.02 . 2 . . . . . . . . 4472 1 667 . 1 1 66 66 LEU CG C 13 26.8 0.2 . 1 . . . . . . . . 4472 1 668 . 1 1 66 66 LEU HG H 1 1.3 0.02 . 1 . . . . . . . . 4472 1 669 . 1 1 66 66 LEU HD21 H 1 0.91 0.02 . 1 . . . . . . . . 4472 1 670 . 1 1 66 66 LEU HD22 H 1 0.91 0.02 . 1 . . . . . . . . 4472 1 671 . 1 1 66 66 LEU HD23 H 1 0.91 0.02 . 1 . . . . . . . . 4472 1 672 . 1 1 66 66 LEU HD11 H 1 0.56 0.02 . 1 . . . . . . . . 4472 1 673 . 1 1 66 66 LEU HD12 H 1 0.56 0.02 . 1 . . . . . . . . 4472 1 674 . 1 1 66 66 LEU HD13 H 1 0.56 0.02 . 1 . . . . . . . . 4472 1 675 . 1 1 66 66 LEU CD2 C 13 24.6 0.2 . 1 . . . . . . . . 4472 1 676 . 1 1 66 66 LEU CD1 C 13 22.4 0.2 . 1 . . . . . . . . 4472 1 677 . 1 1 67 67 GLU N N 15 120.1 0.2 . 1 . . . . . . . . 4472 1 678 . 1 1 67 67 GLU H H 1 8.35 0.02 . 1 . . . . . . . . 4472 1 679 . 1 1 67 67 GLU CA C 13 58.9 0.2 . 1 . . . . . . . . 4472 1 680 . 1 1 67 67 GLU HA H 1 3.85 0.02 . 1 . . . . . . . . 4472 1 681 . 1 1 67 67 GLU CB C 13 28.7 0.2 . 1 . . . . . . . . 4472 1 682 . 1 1 67 67 GLU HB2 H 1 1.98 0.02 . 2 . . . . . . . . 4472 1 683 . 1 1 67 67 GLU HB3 H 1 1.85 0.02 . 2 . . . . . . . . 4472 1 684 . 1 1 67 67 GLU CG C 13 35.7 0.2 . 1 . . . . . . . . 4472 1 685 . 1 1 67 67 GLU HG2 H 1 2.3 0.02 . 1 . . . . . . . . 4472 1 686 . 1 1 67 67 GLU HG3 H 1 2.3 0.02 . 1 . . . . . . . . 4472 1 687 . 1 1 68 68 LEU N N 15 123.2 0.2 . 1 . . . . . . . . 4472 1 688 . 1 1 68 68 LEU H H 1 8.4 0.02 . 1 . . . . . . . . 4472 1 689 . 1 1 68 68 LEU CA C 13 58.5 0.2 . 1 . . . . . . . . 4472 1 690 . 1 1 68 68 LEU HA H 1 4.01 0.02 . 1 . . . . . . . . 4472 1 691 . 1 1 68 68 LEU CB C 13 41 0.2 . 1 . . . . . . . . 4472 1 692 . 1 1 68 68 LEU HB2 H 1 1.98 0.02 . 2 . . . . . . . . 4472 1 693 . 1 1 68 68 LEU HB3 H 1 1.13 0.02 . 2 . . . . . . . . 4472 1 694 . 1 1 68 68 LEU CG C 13 27.2 0.2 . 1 . . . . . . . . 4472 1 695 . 1 1 68 68 LEU HG H 1 1.35 0.02 . 1 . . . . . . . . 4472 1 696 . 1 1 68 68 LEU HD11 H 1 0.88 0.02 . 1 . . . . . . . . 4472 1 697 . 1 1 68 68 LEU HD12 H 1 0.88 0.02 . 1 . . . . . . . . 4472 1 698 . 1 1 68 68 LEU HD13 H 1 0.88 0.02 . 1 . . . . . . . . 4472 1 699 . 1 1 68 68 LEU HD21 H 1 0.78 0.02 . 1 . . . . . . . . 4472 1 700 . 1 1 68 68 LEU HD22 H 1 0.78 0.02 . 1 . . . . . . . . 4472 1 701 . 1 1 68 68 LEU HD23 H 1 0.78 0.02 . 1 . . . . . . . . 4472 1 702 . 1 1 68 68 LEU CD1 C 13 22.7 0.2 . 1 . . . . . . . . 4472 1 703 . 1 1 68 68 LEU CD2 C 13 25.3 0.2 . 1 . . . . . . . . 4472 1 704 . 1 1 69 69 LEU N N 15 120.8 0.2 . 1 . . . . . . . . 4472 1 705 . 1 1 69 69 LEU H H 1 8.11 0.02 . 1 . . . . . . . . 4472 1 706 . 1 1 69 69 LEU CA C 13 58.3 0.2 . 1 . . . . . . . . 4472 1 707 . 1 1 69 69 LEU HA H 1 3.74 0.02 . 1 . . . . . . . . 4472 1 708 . 1 1 69 69 LEU CB C 13 41 0.2 . 1 . . . . . . . . 4472 1 709 . 1 1 69 69 LEU HB2 H 1 2.1 0.02 . 2 . . . . . . . . 4472 1 710 . 1 1 69 69 LEU HB3 H 1 1.52 0.02 . 2 . . . . . . . . 4472 1 711 . 1 1 69 69 LEU CG C 13 26.1 0.2 . 1 . . . . . . . . 4472 1 712 . 1 1 69 69 LEU HG H 1 1.36 0.02 . 1 . . . . . . . . 4472 1 713 . 1 1 69 69 LEU HD21 H 1 0.82 0.02 . 1 . . . . . . . . 4472 1 714 . 1 1 69 69 LEU HD22 H 1 0.82 0.02 . 1 . . . . . . . . 4472 1 715 . 1 1 69 69 LEU HD23 H 1 0.82 0.02 . 1 . . . . . . . . 4472 1 716 . 1 1 69 69 LEU HD11 H 1 0.63 0.02 . 1 . . . . . . . . 4472 1 717 . 1 1 69 69 LEU HD12 H 1 0.63 0.02 . 1 . . . . . . . . 4472 1 718 . 1 1 69 69 LEU HD13 H 1 0.63 0.02 . 1 . . . . . . . . 4472 1 719 . 1 1 69 69 LEU CD2 C 13 27.2 0.2 . 1 . . . . . . . . 4472 1 720 . 1 1 69 69 LEU CD1 C 13 22 0.2 . 1 . . . . . . . . 4472 1 721 . 1 1 70 70 LYS N N 15 115.9 0.2 . 1 . . . . . . . . 4472 1 722 . 1 1 70 70 LYS H H 1 8.45 0.02 . 1 . . . . . . . . 4472 1 723 . 1 1 70 70 LYS CA C 13 59.9 0.2 . 1 . . . . . . . . 4472 1 724 . 1 1 70 70 LYS HA H 1 3.8 0.02 . 1 . . . . . . . . 4472 1 725 . 1 1 70 70 LYS CB C 13 32 0.2 . 1 . . . . . . . . 4472 1 726 . 1 1 70 70 LYS HB2 H 1 1.88 0.02 . 2 . . . . . . . . 4472 1 727 . 1 1 70 70 LYS HB3 H 1 1.77 0.02 . 2 . . . . . . . . 4472 1 728 . 1 1 70 70 LYS CG C 13 24.2 0.2 . 1 . . . . . . . . 4472 1 729 . 1 1 70 70 LYS HG2 H 1 1.44 0.02 . 1 . . . . . . . . 4472 1 730 . 1 1 70 70 LYS HG3 H 1 1.44 0.02 . 1 . . . . . . . . 4472 1 731 . 1 1 70 70 LYS CD C 13 28.7 0.2 . 1 . . . . . . . . 4472 1 732 . 1 1 70 70 LYS HD2 H 1 1.67 0.02 . 1 . . . . . . . . 4472 1 733 . 1 1 70 70 LYS HD3 H 1 1.67 0.02 . 1 . . . . . . . . 4472 1 734 . 1 1 70 70 LYS CE C 13 41.3 0.2 . 1 . . . . . . . . 4472 1 735 . 1 1 70 70 LYS HE2 H 1 2.95 0.02 . 1 . . . . . . . . 4472 1 736 . 1 1 70 70 LYS HE3 H 1 2.95 0.02 . 1 . . . . . . . . 4472 1 737 . 1 1 71 71 THR N N 15 117.4 0.2 . 1 . . . . . . . . 4472 1 738 . 1 1 71 71 THR H H 1 8.08 0.02 . 1 . . . . . . . . 4472 1 739 . 1 1 71 71 THR CA C 13 67.1 0.2 . 1 . . . . . . . . 4472 1 740 . 1 1 71 71 THR HA H 1 3.78 0.02 . 1 . . . . . . . . 4472 1 741 . 1 1 71 71 THR CB C 13 68.3 0.2 . 1 . . . . . . . . 4472 1 742 . 1 1 71 71 THR HB H 1 4.35 0.02 . 1 . . . . . . . . 4472 1 743 . 1 1 71 71 THR HG21 H 1 1.18 0.02 . 1 . . . . . . . . 4472 1 744 . 1 1 71 71 THR HG22 H 1 1.18 0.02 . 1 . . . . . . . . 4472 1 745 . 1 1 71 71 THR HG23 H 1 1.18 0.02 . 1 . . . . . . . . 4472 1 746 . 1 1 71 71 THR CG2 C 13 21.6 0.2 . 1 . . . . . . . . 4472 1 747 . 1 1 72 72 ILE N N 15 123.4 0.2 . 1 . . . . . . . . 4472 1 748 . 1 1 72 72 ILE H H 1 8.47 0.02 . 1 . . . . . . . . 4472 1 749 . 1 1 72 72 ILE CA C 13 66 0.2 . 1 . . . . . . . . 4472 1 750 . 1 1 72 72 ILE HA H 1 3.36 0.02 . 1 . . . . . . . . 4472 1 751 . 1 1 72 72 ILE CB C 13 38.5 0.2 . 1 . . . . . . . . 4472 1 752 . 1 1 72 72 ILE HB H 1 1.87 0.02 . 1 . . . . . . . . 4472 1 753 . 1 1 72 72 ILE HG21 H 1 0.75 0.02 . 1 . . . . . . . . 4472 1 754 . 1 1 72 72 ILE HG22 H 1 0.75 0.02 . 1 . . . . . . . . 4472 1 755 . 1 1 72 72 ILE HG23 H 1 0.75 0.02 . 1 . . . . . . . . 4472 1 756 . 1 1 72 72 ILE CG2 C 13 17.2 0.2 . 1 . . . . . . . . 4472 1 757 . 1 1 72 72 ILE CG1 C 13 29.1 0.2 . 1 . . . . . . . . 4472 1 758 . 1 1 72 72 ILE HG12 H 1 1.68 0.02 . 2 . . . . . . . . 4472 1 759 . 1 1 72 72 ILE HG13 H 1 1.14 0.02 . 2 . . . . . . . . 4472 1 760 . 1 1 72 72 ILE HD11 H 1 0.56 0.02 . 1 . . . . . . . . 4472 1 761 . 1 1 72 72 ILE HD12 H 1 0.56 0.02 . 1 . . . . . . . . 4472 1 762 . 1 1 72 72 ILE HD13 H 1 0.56 0.02 . 1 . . . . . . . . 4472 1 763 . 1 1 72 72 ILE CD1 C 13 14.5 0.2 . 1 . . . . . . . . 4472 1 764 . 1 1 73 73 ARG N N 15 113.4 0.2 . 1 . . . . . . . . 4472 1 765 . 1 1 73 73 ARG H H 1 8.16 0.02 . 1 . . . . . . . . 4472 1 766 . 1 1 73 73 ARG CA C 13 57.3 0.2 . 1 . . . . . . . . 4472 1 767 . 1 1 73 73 ARG HA H 1 4.04 0.02 . 1 . . . . . . . . 4472 1 768 . 1 1 73 73 ARG CB C 13 29 0.2 . 1 . . . . . . . . 4472 1 769 . 1 1 73 73 ARG HB2 H 1 1.99 0.02 . 1 . . . . . . . . 4472 1 770 . 1 1 73 73 ARG HB3 H 1 1.99 0.02 . 1 . . . . . . . . 4472 1 771 . 1 1 74 74 ALA N N 15 118.7 0.2 . 1 . . . . . . . . 4472 1 772 . 1 1 74 74 ALA H H 1 7.3 0.02 . 1 . . . . . . . . 4472 1 773 . 1 1 74 74 ALA CA C 13 51.7 0.2 . 1 . . . . . . . . 4472 1 774 . 1 1 74 74 ALA HA H 1 4.36 0.02 . 1 . . . . . . . . 4472 1 775 . 1 1 74 74 ALA HB1 H 1 1.4 0.02 . 1 . . . . . . . . 4472 1 776 . 1 1 74 74 ALA HB2 H 1 1.4 0.02 . 1 . . . . . . . . 4472 1 777 . 1 1 74 74 ALA HB3 H 1 1.4 0.02 . 1 . . . . . . . . 4472 1 778 . 1 1 74 74 ALA CB C 13 19.2 0.2 . 1 . . . . . . . . 4472 1 779 . 1 1 75 75 ASP N N 15 121.8 0.2 . 1 . . . . . . . . 4472 1 780 . 1 1 75 75 ASP H H 1 7.42 0.02 . 1 . . . . . . . . 4472 1 781 . 1 1 75 75 ASP CA C 13 54 0.2 . 1 . . . . . . . . 4472 1 782 . 1 1 75 75 ASP HA H 1 4.56 0.02 . 1 . . . . . . . . 4472 1 783 . 1 1 75 75 ASP CB C 13 43.6 0.2 . 1 . . . . . . . . 4472 1 784 . 1 1 75 75 ASP HB2 H 1 2.89 0.02 . 2 . . . . . . . . 4472 1 785 . 1 1 75 75 ASP HB3 H 1 2.6 0.02 . 2 . . . . . . . . 4472 1 786 . 1 1 76 76 GLY N N 15 112.1 0.2 . 1 . . . . . . . . 4472 1 787 . 1 1 76 76 GLY H H 1 8.75 0.02 . 1 . . . . . . . . 4472 1 788 . 1 1 76 76 GLY CA C 13 47.2 0.2 . 1 . . . . . . . . 4472 1 789 . 1 1 77 77 ALA N N 15 121.8 0.2 . 1 . . . . . . . . 4472 1 790 . 1 1 77 77 ALA H H 1 8.56 0.02 . 1 . . . . . . . . 4472 1 791 . 1 1 77 77 ALA CA C 13 53.3 0.2 . 1 . . . . . . . . 4472 1 792 . 1 1 77 77 ALA HA H 1 4.49 0.02 . 1 . . . . . . . . 4472 1 793 . 1 1 77 77 ALA HB1 H 1 1.39 0.02 . 1 . . . . . . . . 4472 1 794 . 1 1 77 77 ALA HB2 H 1 1.39 0.02 . 1 . . . . . . . . 4472 1 795 . 1 1 77 77 ALA HB3 H 1 1.39 0.02 . 1 . . . . . . . . 4472 1 796 . 1 1 77 77 ALA CB C 13 20.1 0.2 . 1 . . . . . . . . 4472 1 797 . 1 1 78 78 MET N N 15 116 0.2 . 1 . . . . . . . . 4472 1 798 . 1 1 78 78 MET H H 1 8.56 0.02 . 1 . . . . . . . . 4472 1 799 . 1 1 78 78 MET CA C 13 55.7 0.2 . 1 . . . . . . . . 4472 1 800 . 1 1 78 78 MET HA H 1 4.59 0.02 . 1 . . . . . . . . 4472 1 801 . 1 1 78 78 MET CB C 13 34.3 0.2 . 1 . . . . . . . . 4472 1 802 . 1 1 78 78 MET HB2 H 1 2.22 0.02 . 2 . . . . . . . . 4472 1 803 . 1 1 78 78 MET HB3 H 1 2.15 0.02 . 2 . . . . . . . . 4472 1 804 . 1 1 78 78 MET CG C 13 31.7 0.2 . 1 . . . . . . . . 4472 1 805 . 1 1 78 78 MET HG2 H 1 2.61 0.02 . 2 . . . . . . . . 4472 1 806 . 1 1 78 78 MET HG3 H 1 2.39 0.02 . 2 . . . . . . . . 4472 1 807 . 1 1 79 79 SER N N 15 112.6 0.2 . 1 . . . . . . . . 4472 1 808 . 1 1 79 79 SER H H 1 7.46 0.02 . 1 . . . . . . . . 4472 1 809 . 1 1 79 79 SER CA C 13 61.7 0.2 . 1 . . . . . . . . 4472 1 810 . 1 1 79 79 SER HA H 1 4.43 0.02 . 1 . . . . . . . . 4472 1 811 . 1 1 79 79 SER CB C 13 65.5 0.2 . 1 . . . . . . . . 4472 1 812 . 1 1 79 79 SER HB2 H 1 4.07 0.02 . 2 . . . . . . . . 4472 1 813 . 1 1 79 79 SER HB3 H 1 3.97 0.02 . 2 . . . . . . . . 4472 1 814 . 1 1 80 80 ALA N N 15 123 0.2 . 1 . . . . . . . . 4472 1 815 . 1 1 80 80 ALA H H 1 8.25 0.02 . 1 . . . . . . . . 4472 1 816 . 1 1 80 80 ALA CA C 13 50.9 0.2 . 1 . . . . . . . . 4472 1 817 . 1 1 80 80 ALA HA H 1 4.44 0.02 . 1 . . . . . . . . 4472 1 818 . 1 1 80 80 ALA HB1 H 1 1.34 0.02 . 1 . . . . . . . . 4472 1 819 . 1 1 80 80 ALA HB2 H 1 1.34 0.02 . 1 . . . . . . . . 4472 1 820 . 1 1 80 80 ALA HB3 H 1 1.34 0.02 . 1 . . . . . . . . 4472 1 821 . 1 1 80 80 ALA CB C 13 18.7 0.2 . 1 . . . . . . . . 4472 1 822 . 1 1 81 81 LEU N N 15 124.1 0.2 . 1 . . . . . . . . 4472 1 823 . 1 1 81 81 LEU H H 1 7.93 0.02 . 1 . . . . . . . . 4472 1 824 . 1 1 81 81 LEU CA C 13 53.5 0.2 . 1 . . . . . . . . 4472 1 825 . 1 1 81 81 LEU HA H 1 4.14 0.02 . 1 . . . . . . . . 4472 1 826 . 1 1 81 81 LEU CB C 13 42.8 0.2 . 1 . . . . . . . . 4472 1 827 . 1 1 81 81 LEU HB2 H 1 1.53 0.02 . 2 . . . . . . . . 4472 1 828 . 1 1 81 81 LEU HB3 H 1 1.28 0.02 . 2 . . . . . . . . 4472 1 829 . 1 1 81 81 LEU CG C 13 26.1 0.2 . 1 . . . . . . . . 4472 1 830 . 1 1 81 81 LEU HG H 1 1.54 0.02 . 1 . . . . . . . . 4472 1 831 . 1 1 81 81 LEU HD21 H 1 0.7 0.02 . 1 . . . . . . . . 4472 1 832 . 1 1 81 81 LEU HD22 H 1 0.7 0.02 . 1 . . . . . . . . 4472 1 833 . 1 1 81 81 LEU HD23 H 1 0.7 0.02 . 1 . . . . . . . . 4472 1 834 . 1 1 81 81 LEU HD11 H 1 0.7 0.02 . 1 . . . . . . . . 4472 1 835 . 1 1 81 81 LEU HD12 H 1 0.7 0.02 . 1 . . . . . . . . 4472 1 836 . 1 1 81 81 LEU HD13 H 1 0.7 0.02 . 1 . . . . . . . . 4472 1 837 . 1 1 81 81 LEU CD1 C 13 25.3 0.2 . 1 . . . . . . . . 4472 1 838 . 1 1 81 81 LEU CD2 C 13 24.6 0.2 . 1 . . . . . . . . 4472 1 839 . 1 1 82 82 PRO CD C 13 50.4 0.2 . 1 . . . . . . . . 4472 1 840 . 1 1 82 82 PRO CA C 13 62.5 0.2 . 1 . . . . . . . . 4472 1 841 . 1 1 82 82 PRO HA H 1 3.96 0.02 . 1 . . . . . . . . 4472 1 842 . 1 1 82 82 PRO CB C 13 31.4 0.2 . 1 . . . . . . . . 4472 1 843 . 1 1 82 82 PRO HB2 H 1 1.35 0.02 . 2 . . . . . . . . 4472 1 844 . 1 1 82 82 PRO HB3 H 1 0.33 0.02 . 2 . . . . . . . . 4472 1 845 . 1 1 82 82 PRO CG C 13 28.1 0.2 . 1 . . . . . . . . 4472 1 846 . 1 1 82 82 PRO HG2 H 1 1.83 0.02 . 2 . . . . . . . . 4472 1 847 . 1 1 82 82 PRO HG3 H 1 1.7 0.02 . 2 . . . . . . . . 4472 1 848 . 1 1 82 82 PRO HD2 H 1 3.92 0.02 . 2 . . . . . . . . 4472 1 849 . 1 1 82 82 PRO HD3 H 1 3.62 0.02 . 2 . . . . . . . . 4472 1 850 . 1 1 83 83 VAL N N 15 119 0.2 . 1 . . . . . . . . 4472 1 851 . 1 1 83 83 VAL H H 1 7.74 0.02 . 1 . . . . . . . . 4472 1 852 . 1 1 83 83 VAL CA C 13 60.2 0.2 . 1 . . . . . . . . 4472 1 853 . 1 1 83 83 VAL HA H 1 4.78 0.02 . 1 . . . . . . . . 4472 1 854 . 1 1 83 83 VAL CB C 13 35 0.2 . 1 . . . . . . . . 4472 1 855 . 1 1 83 83 VAL HB H 1 1.67 0.02 . 1 . . . . . . . . 4472 1 856 . 1 1 83 83 VAL HG11 H 1 0.69 0.02 . 1 . . . . . . . . 4472 1 857 . 1 1 83 83 VAL HG12 H 1 0.69 0.02 . 1 . . . . . . . . 4472 1 858 . 1 1 83 83 VAL HG13 H 1 0.69 0.02 . 1 . . . . . . . . 4472 1 859 . 1 1 83 83 VAL HG21 H 1 0.62 0.02 . 1 . . . . . . . . 4472 1 860 . 1 1 83 83 VAL HG22 H 1 0.62 0.02 . 1 . . . . . . . . 4472 1 861 . 1 1 83 83 VAL HG23 H 1 0.62 0.02 . 1 . . . . . . . . 4472 1 862 . 1 1 83 83 VAL CG1 C 13 20.1 0.2 . 1 . . . . . . . . 4472 1 863 . 1 1 83 83 VAL CG2 C 13 20.5 0.2 . 1 . . . . . . . . 4472 1 864 . 1 1 84 84 LEU N N 15 130.5 0.2 . 1 . . . . . . . . 4472 1 865 . 1 1 84 84 LEU H H 1 9.17 0.02 . 1 . . . . . . . . 4472 1 866 . 1 1 84 84 LEU CA C 13 52.4 0.2 . 1 . . . . . . . . 4472 1 867 . 1 1 84 84 LEU HA H 1 4.47 0.02 . 1 . . . . . . . . 4472 1 868 . 1 1 84 84 LEU CB C 13 45.4 0.2 . 1 . . . . . . . . 4472 1 869 . 1 1 84 84 LEU HB2 H 1 2.09 0.02 . 2 . . . . . . . . 4472 1 870 . 1 1 84 84 LEU HB3 H 1 1.14 0.02 . 2 . . . . . . . . 4472 1 871 . 1 1 84 84 LEU CG C 13 26.1 0.2 . 1 . . . . . . . . 4472 1 872 . 1 1 84 84 LEU HG H 1 1.26 0.02 . 1 . . . . . . . . 4472 1 873 . 1 1 84 84 LEU HD21 H 1 0.53 0.02 . 1 . . . . . . . . 4472 1 874 . 1 1 84 84 LEU HD22 H 1 0.53 0.02 . 1 . . . . . . . . 4472 1 875 . 1 1 84 84 LEU HD23 H 1 0.53 0.02 . 1 . . . . . . . . 4472 1 876 . 1 1 84 84 LEU HD11 H 1 0.57 0.02 . 1 . . . . . . . . 4472 1 877 . 1 1 84 84 LEU HD12 H 1 0.57 0.02 . 1 . . . . . . . . 4472 1 878 . 1 1 84 84 LEU HD13 H 1 0.57 0.02 . 1 . . . . . . . . 4472 1 879 . 1 1 84 84 LEU CD2 C 13 25.3 0.2 . 1 . . . . . . . . 4472 1 880 . 1 1 84 84 LEU CD1 C 13 22.7 0.2 . 1 . . . . . . . . 4472 1 881 . 1 1 85 85 MET N N 15 125.9 0.2 . 1 . . . . . . . . 4472 1 882 . 1 1 85 85 MET H H 1 7.96 0.02 . 1 . . . . . . . . 4472 1 883 . 1 1 85 85 MET CA C 13 53.2 0.2 . 1 . . . . . . . . 4472 1 884 . 1 1 85 85 MET HA H 1 5.54 0.02 . 1 . . . . . . . . 4472 1 885 . 1 1 85 85 MET CB C 13 32 0.2 . 1 . . . . . . . . 4472 1 886 . 1 1 85 85 MET HB2 H 1 1.83 0.02 . 2 . . . . . . . . 4472 1 887 . 1 1 85 85 MET HB3 H 1 1.86 0.02 . 2 . . . . . . . . 4472 1 888 . 1 1 85 85 MET CG C 13 32 0.2 . 1 . . . . . . . . 4472 1 889 . 1 1 85 85 MET HG2 H 1 2.41 0.02 . 2 . . . . . . . . 4472 1 890 . 1 1 86 86 VAL N N 15 122.4 0.2 . 1 . . . . . . . . 4472 1 891 . 1 1 86 86 VAL H H 1 8.77 0.02 . 1 . . . . . . . . 4472 1 892 . 1 1 86 86 VAL CA C 13 59.4 0.2 . 1 . . . . . . . . 4472 1 893 . 1 1 86 86 VAL HA H 1 5.13 0.02 . 1 . . . . . . . . 4472 1 894 . 1 1 86 86 VAL CB C 13 33.6 0.2 . 1 . . . . . . . . 4472 1 895 . 1 1 86 86 VAL HB H 1 1.78 0.02 . 1 . . . . . . . . 4472 1 896 . 1 1 86 86 VAL HG11 H 1 0.58 0.02 . 1 . . . . . . . . 4472 1 897 . 1 1 86 86 VAL HG12 H 1 0.58 0.02 . 1 . . . . . . . . 4472 1 898 . 1 1 86 86 VAL HG13 H 1 0.58 0.02 . 1 . . . . . . . . 4472 1 899 . 1 1 86 86 VAL HG21 H 1 0.58 0.02 . 1 . . . . . . . . 4472 1 900 . 1 1 86 86 VAL HG22 H 1 0.58 0.02 . 1 . . . . . . . . 4472 1 901 . 1 1 86 86 VAL HG23 H 1 0.58 0.02 . 1 . . . . . . . . 4472 1 902 . 1 1 86 86 VAL CG1 C 13 22.4 0.2 . 1 . . . . . . . . 4472 1 903 . 1 1 86 86 VAL CG2 C 13 20.9 0.2 . 1 . . . . . . . . 4472 1 904 . 1 1 87 87 THR N N 15 115.1 0.2 . 1 . . . . . . . . 4472 1 905 . 1 1 87 87 THR H H 1 8.18 0.02 . 1 . . . . . . . . 4472 1 906 . 1 1 87 87 THR CA C 13 58.9 0.2 . 1 . . . . . . . . 4472 1 907 . 1 1 87 87 THR HA H 1 5.29 0.02 . 1 . . . . . . . . 4472 1 908 . 1 1 87 87 THR CB C 13 68.8 0.2 . 1 . . . . . . . . 4472 1 909 . 1 1 87 87 THR HB H 1 4.39 0.02 . 1 . . . . . . . . 4472 1 910 . 1 1 87 87 THR HG21 H 1 1.07 0.02 . 1 . . . . . . . . 4472 1 911 . 1 1 87 87 THR HG22 H 1 1.07 0.02 . 1 . . . . . . . . 4472 1 912 . 1 1 87 87 THR HG23 H 1 1.07 0.02 . 1 . . . . . . . . 4472 1 913 . 1 1 87 87 THR CG2 C 13 18.3 0.2 . 1 . . . . . . . . 4472 1 914 . 1 1 88 88 ALA N N 15 128.4 0.2 . 1 . . . . . . . . 4472 1 915 . 1 1 88 88 ALA H H 1 8.44 0.02 . 1 . . . . . . . . 4472 1 916 . 1 1 88 88 ALA CA C 13 52.8 0.2 . 1 . . . . . . . . 4472 1 917 . 1 1 88 88 ALA HA H 1 4.57 0.02 . 1 . . . . . . . . 4472 1 918 . 1 1 88 88 ALA HB1 H 1 1.56 0.02 . 1 . . . . . . . . 4472 1 919 . 1 1 88 88 ALA HB2 H 1 1.56 0.02 . 1 . . . . . . . . 4472 1 920 . 1 1 88 88 ALA HB3 H 1 1.56 0.02 . 1 . . . . . . . . 4472 1 921 . 1 1 88 88 ALA CB C 13 19.2 0.2 . 1 . . . . . . . . 4472 1 922 . 1 1 89 89 GLU N N 15 120.2 0.2 . 1 . . . . . . . . 4472 1 923 . 1 1 89 89 GLU H H 1 8.7 0.02 . 1 . . . . . . . . 4472 1 924 . 1 1 89 89 GLU CA C 13 55.9 0.2 . 1 . . . . . . . . 4472 1 925 . 1 1 89 89 GLU HA H 1 4.21 0.02 . 1 . . . . . . . . 4472 1 926 . 1 1 89 89 GLU CB C 13 29 0.2 . 1 . . . . . . . . 4472 1 927 . 1 1 89 89 GLU HB2 H 1 1.79 0.02 . 1 . . . . . . . . 4472 1 928 . 1 1 89 89 GLU HB3 H 1 1.79 0.02 . 1 . . . . . . . . 4472 1 929 . 1 1 89 89 GLU CG C 13 35.4 0.2 . 1 . . . . . . . . 4472 1 930 . 1 1 89 89 GLU HG2 H 1 1.89 0.02 . 1 . . . . . . . . 4472 1 931 . 1 1 89 89 GLU HG3 H 1 1.89 0.02 . 1 . . . . . . . . 4472 1 932 . 1 1 90 90 ALA N N 15 129.4 0.2 . 1 . . . . . . . . 4472 1 933 . 1 1 90 90 ALA H H 1 8.48 0.02 . 1 . . . . . . . . 4472 1 934 . 1 1 90 90 ALA CA C 13 51.2 0.2 . 1 . . . . . . . . 4472 1 935 . 1 1 90 90 ALA HA H 1 4.48 0.02 . 1 . . . . . . . . 4472 1 936 . 1 1 90 90 ALA HB1 H 1 1.39 0.02 . 1 . . . . . . . . 4472 1 937 . 1 1 90 90 ALA HB2 H 1 1.39 0.02 . 1 . . . . . . . . 4472 1 938 . 1 1 90 90 ALA HB3 H 1 1.39 0.02 . 1 . . . . . . . . 4472 1 939 . 1 1 90 90 ALA CB C 13 19.9 0.2 . 1 . . . . . . . . 4472 1 940 . 1 1 91 91 LYS N N 15 119.9 0.2 . 1 . . . . . . . . 4472 1 941 . 1 1 91 91 LYS H H 1 7.72 0.02 . 1 . . . . . . . . 4472 1 942 . 1 1 91 91 LYS CA C 13 56.4 0.2 . 1 . . . . . . . . 4472 1 943 . 1 1 91 91 LYS HA H 1 4.3 0.02 . 1 . . . . . . . . 4472 1 944 . 1 1 91 91 LYS CB C 13 32.8 0.2 . 1 . . . . . . . . 4472 1 945 . 1 1 91 91 LYS HB2 H 1 1.87 0.02 . 2 . . . . . . . . 4472 1 946 . 1 1 91 91 LYS HB3 H 1 1.71 0.02 . 2 . . . . . . . . 4472 1 947 . 1 1 91 91 LYS CG C 13 25 0.2 . 1 . . . . . . . . 4472 1 948 . 1 1 91 91 LYS HG2 H 1 1.44 0.02 . 1 . . . . . . . . 4472 1 949 . 1 1 91 91 LYS HG3 H 1 1.44 0.02 . 1 . . . . . . . . 4472 1 950 . 1 1 91 91 LYS CD C 13 29.1 0.2 . 1 . . . . . . . . 4472 1 951 . 1 1 91 91 LYS HD2 H 1 1.65 0.02 . 1 . . . . . . . . 4472 1 952 . 1 1 91 91 LYS HD3 H 1 1.65 0.02 . 1 . . . . . . . . 4472 1 953 . 1 1 91 91 LYS CE C 13 41.7 0.2 . 1 . . . . . . . . 4472 1 954 . 1 1 91 91 LYS HE2 H 1 2.94 0.02 . 1 . . . . . . . . 4472 1 955 . 1 1 91 91 LYS HE3 H 1 2.94 0.02 . 1 . . . . . . . . 4472 1 956 . 1 1 92 92 LYS N N 15 126 0.2 . 1 . . . . . . . . 4472 1 957 . 1 1 92 92 LYS H H 1 8.94 0.02 . 1 . . . . . . . . 4472 1 958 . 1 1 92 92 LYS CA C 13 59.6 0.2 . 1 . . . . . . . . 4472 1 959 . 1 1 92 92 LYS HA H 1 3.8 0.02 . 1 . . . . . . . . 4472 1 960 . 1 1 92 92 LYS CB C 13 31.7 0.2 . 1 . . . . . . . . 4472 1 961 . 1 1 92 92 LYS HB2 H 1 1.9 0.02 . 2 . . . . . . . . 4472 1 962 . 1 1 92 92 LYS HB3 H 1 1.8 0.02 . 2 . . . . . . . . 4472 1 963 . 1 1 93 93 GLU N N 15 116.1 0.2 . 1 . . . . . . . . 4472 1 964 . 1 1 93 93 GLU H H 1 9.57 0.02 . 1 . . . . . . . . 4472 1 965 . 1 1 93 93 GLU CA C 13 59.8 0.2 . 1 . . . . . . . . 4472 1 966 . 1 1 93 93 GLU HA H 1 3.94 0.02 . 1 . . . . . . . . 4472 1 967 . 1 1 93 93 GLU CB C 13 28.4 0.2 . 1 . . . . . . . . 4472 1 968 . 1 1 93 93 GLU HB2 H 1 1.92 0.02 . 1 . . . . . . . . 4472 1 969 . 1 1 93 93 GLU HB3 H 1 1.92 0.02 . 1 . . . . . . . . 4472 1 970 . 1 1 93 93 GLU CG C 13 36.5 0.2 . 1 . . . . . . . . 4472 1 971 . 1 1 93 93 GLU HG2 H 1 2.38 0.02 . 2 . . . . . . . . 4472 1 972 . 1 1 93 93 GLU HG3 H 1 2.25 0.02 . 2 . . . . . . . . 4472 1 973 . 1 1 94 94 ASN N N 15 119.1 0.2 . 1 . . . . . . . . 4472 1 974 . 1 1 94 94 ASN H H 1 7.32 0.02 . 1 . . . . . . . . 4472 1 975 . 1 1 94 94 ASN CA C 13 55.6 0.2 . 1 . . . . . . . . 4472 1 976 . 1 1 94 94 ASN HA H 1 4.52 0.02 . 1 . . . . . . . . 4472 1 977 . 1 1 94 94 ASN CB C 13 37.5 0.2 . 1 . . . . . . . . 4472 1 978 . 1 1 94 94 ASN HB2 H 1 2.59 0.02 . 2 . . . . . . . . 4472 1 979 . 1 1 94 94 ASN HB3 H 1 2.36 0.02 . 2 . . . . . . . . 4472 1 980 . 1 1 95 95 ILE N N 15 121.5 0.2 . 1 . . . . . . . . 4472 1 981 . 1 1 95 95 ILE H H 1 7.28 0.02 . 1 . . . . . . . . 4472 1 982 . 1 1 95 95 ILE CA C 13 65.3 0.2 . 1 . . . . . . . . 4472 1 983 . 1 1 95 95 ILE HA H 1 2.97 0.02 . 1 . . . . . . . . 4472 1 984 . 1 1 95 95 ILE CB C 13 37.5 0.2 . 1 . . . . . . . . 4472 1 985 . 1 1 95 95 ILE HB H 1 1.58 0.02 . 1 . . . . . . . . 4472 1 986 . 1 1 95 95 ILE HG21 H 1 0.51 0.02 . 1 . . . . . . . . 4472 1 987 . 1 1 95 95 ILE HG22 H 1 0.51 0.02 . 1 . . . . . . . . 4472 1 988 . 1 1 95 95 ILE HG23 H 1 0.51 0.02 . 1 . . . . . . . . 4472 1 989 . 1 1 95 95 ILE CG2 C 13 16.4 0.2 . 1 . . . . . . . . 4472 1 990 . 1 1 95 95 ILE CG1 C 13 27.6 0.2 . 1 . . . . . . . . 4472 1 991 . 1 1 95 95 ILE HG12 H 1 1.05 0.02 . 2 . . . . . . . . 4472 1 992 . 1 1 95 95 ILE HG13 H 1 0.02 0.02 . 2 . . . . . . . . 4472 1 993 . 1 1 95 95 ILE HD11 H 1 0.52 0.02 . 1 . . . . . . . . 4472 1 994 . 1 1 95 95 ILE HD12 H 1 0.52 0.02 . 1 . . . . . . . . 4472 1 995 . 1 1 95 95 ILE HD13 H 1 0.52 0.02 . 1 . . . . . . . . 4472 1 996 . 1 1 95 95 ILE CD1 C 13 12.7 0.2 . 1 . . . . . . . . 4472 1 997 . 1 1 96 96 ILE N N 15 119.2 0.2 . 1 . . . . . . . . 4472 1 998 . 1 1 96 96 ILE H H 1 7.88 0.02 . 1 . . . . . . . . 4472 1 999 . 1 1 96 96 ILE CA C 13 64.1 0.2 . 1 . . . . . . . . 4472 1 1000 . 1 1 96 96 ILE HA H 1 3.75 0.02 . 1 . . . . . . . . 4472 1 1001 . 1 1 96 96 ILE CB C 13 37.9 0.2 . 1 . . . . . . . . 4472 1 1002 . 1 1 96 96 ILE HB H 1 1.76 0.02 . 1 . . . . . . . . 4472 1 1003 . 1 1 96 96 ILE HG21 H 1 0.89 0.02 . 1 . . . . . . . . 4472 1 1004 . 1 1 96 96 ILE HG22 H 1 0.89 0.02 . 1 . . . . . . . . 4472 1 1005 . 1 1 96 96 ILE HG23 H 1 0.89 0.02 . 1 . . . . . . . . 4472 1 1006 . 1 1 96 96 ILE CG2 C 13 16.8 0.2 . 1 . . . . . . . . 4472 1 1007 . 1 1 96 96 ILE CG1 C 13 28.7 0.2 . 1 . . . . . . . . 4472 1 1008 . 1 1 96 96 ILE HG12 H 1 1.58 0.02 . 2 . . . . . . . . 4472 1 1009 . 1 1 96 96 ILE HG13 H 1 1.14 0.02 . 2 . . . . . . . . 4472 1 1010 . 1 1 96 96 ILE HD11 H 1 0.79 0.02 . 1 . . . . . . . . 4472 1 1011 . 1 1 96 96 ILE HD12 H 1 0.79 0.02 . 1 . . . . . . . . 4472 1 1012 . 1 1 96 96 ILE HD13 H 1 0.79 0.02 . 1 . . . . . . . . 4472 1 1013 . 1 1 96 96 ILE CD1 C 13 12.7 0.2 . 1 . . . . . . . . 4472 1 1014 . 1 1 97 97 ALA N N 15 122.2 0.2 . 1 . . . . . . . . 4472 1 1015 . 1 1 97 97 ALA H H 1 7.82 0.02 . 1 . . . . . . . . 4472 1 1016 . 1 1 97 97 ALA CA C 13 55 0.2 . 1 . . . . . . . . 4472 1 1017 . 1 1 97 97 ALA HA H 1 4.2 0.02 . 1 . . . . . . . . 4472 1 1018 . 1 1 97 97 ALA HB1 H 1 1.73 0.02 . 1 . . . . . . . . 4472 1 1019 . 1 1 97 97 ALA HB2 H 1 1.73 0.02 . 1 . . . . . . . . 4472 1 1020 . 1 1 97 97 ALA HB3 H 1 1.73 0.02 . 1 . . . . . . . . 4472 1 1021 . 1 1 97 97 ALA CB C 13 17.5 0.2 . 1 . . . . . . . . 4472 1 1022 . 1 1 98 98 ALA N N 15 119.6 0.2 . 1 . . . . . . . . 4472 1 1023 . 1 1 98 98 ALA H H 1 8.62 0.02 . 1 . . . . . . . . 4472 1 1024 . 1 1 98 98 ALA CA C 13 54.6 0.2 . 1 . . . . . . . . 4472 1 1025 . 1 1 98 98 ALA HA H 1 3.88 0.02 . 1 . . . . . . . . 4472 1 1026 . 1 1 98 98 ALA HB1 H 1 1.62 0.02 . 1 . . . . . . . . 4472 1 1027 . 1 1 98 98 ALA HB2 H 1 1.62 0.02 . 1 . . . . . . . . 4472 1 1028 . 1 1 98 98 ALA HB3 H 1 1.62 0.02 . 1 . . . . . . . . 4472 1 1029 . 1 1 98 98 ALA CB C 13 17.2 0.2 . 1 . . . . . . . . 4472 1 1030 . 1 1 99 99 ALA N N 15 121.8 0.2 . 1 . . . . . . . . 4472 1 1031 . 1 1 99 99 ALA H H 1 8.11 0.02 . 1 . . . . . . . . 4472 1 1032 . 1 1 99 99 ALA CA C 13 55.4 0.2 . 1 . . . . . . . . 4472 1 1033 . 1 1 99 99 ALA HA H 1 4.17 0.02 . 1 . . . . . . . . 4472 1 1034 . 1 1 99 99 ALA HB1 H 1 1.55 0.02 . 1 . . . . . . . . 4472 1 1035 . 1 1 99 99 ALA HB2 H 1 1.55 0.02 . 1 . . . . . . . . 4472 1 1036 . 1 1 99 99 ALA HB3 H 1 1.55 0.02 . 1 . . . . . . . . 4472 1 1037 . 1 1 99 99 ALA CB C 13 18.6 0.2 . 1 . . . . . . . . 4472 1 1038 . 1 1 100 100 GLN N N 15 119 0.2 . 1 . . . . . . . . 4472 1 1039 . 1 1 100 100 GLN H H 1 8.77 0.02 . 1 . . . . . . . . 4472 1 1040 . 1 1 100 100 GLN CA C 13 58.4 0.2 . 1 . . . . . . . . 4472 1 1041 . 1 1 100 100 GLN HA H 1 4.03 0.02 . 1 . . . . . . . . 4472 1 1042 . 1 1 100 100 GLN CB C 13 27.9 0.2 . 1 . . . . . . . . 4472 1 1043 . 1 1 100 100 GLN HB2 H 1 2.19 0.02 . 2 . . . . . . . . 4472 1 1044 . 1 1 100 100 GLN HB3 H 1 2.11 0.02 . 2 . . . . . . . . 4472 1 1045 . 1 1 100 100 GLN CG C 13 33.9 0.2 . 1 . . . . . . . . 4472 1 1046 . 1 1 100 100 GLN HG2 H 1 2.61 0.02 . 2 . . . . . . . . 4472 1 1047 . 1 1 100 100 GLN HG3 H 1 2.43 0.02 . 2 . . . . . . . . 4472 1 1048 . 1 1 101 101 ALA N N 15 118.4 0.2 . 1 . . . . . . . . 4472 1 1049 . 1 1 101 101 ALA H H 1 7.61 0.02 . 1 . . . . . . . . 4472 1 1050 . 1 1 101 101 ALA CA C 13 51.7 0.2 . 1 . . . . . . . . 4472 1 1051 . 1 1 101 101 ALA HA H 1 4.35 0.02 . 1 . . . . . . . . 4472 1 1052 . 1 1 101 101 ALA HB1 H 1 1.39 0.02 . 1 . . . . . . . . 4472 1 1053 . 1 1 101 101 ALA HB2 H 1 1.39 0.02 . 1 . . . . . . . . 4472 1 1054 . 1 1 101 101 ALA HB3 H 1 1.39 0.02 . 1 . . . . . . . . 4472 1 1055 . 1 1 101 101 ALA CB C 13 19.2 0.2 . 1 . . . . . . . . 4472 1 1056 . 1 1 102 102 GLY N N 15 102.3 0.2 . 1 . . . . . . . . 4472 1 1057 . 1 1 102 102 GLY H H 1 7.62 0.02 . 1 . . . . . . . . 4472 1 1058 . 1 1 102 102 GLY CA C 13 45.5 0.2 . 1 . . . . . . . . 4472 1 1059 . 1 1 102 102 GLY HA2 H 1 4.23 0.02 . 2 . . . . . . . . 4472 1 1060 . 1 1 102 102 GLY HA3 H 1 3.85 0.02 . 2 . . . . . . . . 4472 1 1061 . 1 1 103 103 ALA N N 15 125 0.2 . 1 . . . . . . . . 4472 1 1062 . 1 1 103 103 ALA H H 1 8.73 0.02 . 1 . . . . . . . . 4472 1 1063 . 1 1 103 103 ALA CA C 13 53.6 0.2 . 1 . . . . . . . . 4472 1 1064 . 1 1 103 103 ALA HA H 1 3.97 0.02 . 1 . . . . . . . . 4472 1 1065 . 1 1 103 103 ALA HB1 H 1 1.38 0.02 . 1 . . . . . . . . 4472 1 1066 . 1 1 103 103 ALA HB2 H 1 1.38 0.02 . 1 . . . . . . . . 4472 1 1067 . 1 1 103 103 ALA HB3 H 1 1.38 0.02 . 1 . . . . . . . . 4472 1 1068 . 1 1 103 103 ALA CB C 13 17.9 0.2 . 1 . . . . . . . . 4472 1 1069 . 1 1 104 104 SER N N 15 118.5 0.2 . 1 . . . . . . . . 4472 1 1070 . 1 1 104 104 SER H H 1 9.31 0.02 . 1 . . . . . . . . 4472 1 1071 . 1 1 104 104 SER CA C 13 59.8 0.2 . 1 . . . . . . . . 4472 1 1072 . 1 1 104 104 SER HA H 1 4.39 0.02 . 1 . . . . . . . . 4472 1 1073 . 1 1 104 104 SER CB C 13 61.4 0.2 . 1 . . . . . . . . 4472 1 1074 . 1 1 104 104 SER HB2 H 1 3.96 0.02 . 2 . . . . . . . . 4472 1 1075 . 1 1 104 104 SER HB3 H 1 3.21 0.02 . 2 . . . . . . . . 4472 1 1076 . 1 1 105 105 GLY N N 15 102.4 0.2 . 1 . . . . . . . . 4472 1 1077 . 1 1 105 105 GLY H H 1 7.64 0.02 . 1 . . . . . . . . 4472 1 1078 . 1 1 105 105 GLY CA C 13 45.1 0.2 . 1 . . . . . . . . 4472 1 1079 . 1 1 105 105 GLY HA2 H 1 4.16 0.02 . 2 . . . . . . . . 4472 1 1080 . 1 1 105 105 GLY HA3 H 1 3.73 0.02 . 2 . . . . . . . . 4472 1 1081 . 1 1 106 106 TYR N N 15 124.3 0.2 . 1 . . . . . . . . 4472 1 1082 . 1 1 106 106 TYR H H 1 8.63 0.02 . 1 . . . . . . . . 4472 1 1083 . 1 1 106 106 TYR CA C 13 57.3 0.2 . 1 . . . . . . . . 4472 1 1084 . 1 1 106 106 TYR HA H 1 5.33 0.02 . 1 . . . . . . . . 4472 1 1085 . 1 1 106 106 TYR CB C 13 42.4 0.2 . 1 . . . . . . . . 4472 1 1086 . 1 1 106 106 TYR HB2 H 1 2.98 0.02 . 2 . . . . . . . . 4472 1 1087 . 1 1 106 106 TYR HB3 H 1 2.62 0.02 . 2 . . . . . . . . 4472 1 1088 . 1 1 106 106 TYR CD1 C 13 133.2 0.2 . 3 . . . . . . . . 4472 1 1089 . 1 1 106 106 TYR HD1 H 1 6.96 0.02 . 3 . . . . . . . . 4472 1 1090 . 1 1 106 106 TYR CE1 C 13 118.3 0.2 . 3 . . . . . . . . 4472 1 1091 . 1 1 106 106 TYR HE1 H 1 6.71 0.02 . 3 . . . . . . . . 4472 1 1092 . 1 1 107 107 VAL N N 15 128.8 0.2 . 1 . . . . . . . . 4472 1 1093 . 1 1 107 107 VAL H H 1 9.07 0.02 . 1 . . . . . . . . 4472 1 1094 . 1 1 107 107 VAL CA C 13 60.7 0.2 . 1 . . . . . . . . 4472 1 1095 . 1 1 107 107 VAL HA H 1 4.3 0.02 . 1 . . . . . . . . 4472 1 1096 . 1 1 107 107 VAL CB C 13 34.9 0.2 . 1 . . . . . . . . 4472 1 1097 . 1 1 107 107 VAL HB H 1 1.68 0.02 . 1 . . . . . . . . 4472 1 1098 . 1 1 107 107 VAL HG21 H 1 0.64 0.02 . 1 . . . . . . . . 4472 1 1099 . 1 1 107 107 VAL HG22 H 1 0.64 0.02 . 1 . . . . . . . . 4472 1 1100 . 1 1 107 107 VAL HG23 H 1 0.64 0.02 . 1 . . . . . . . . 4472 1 1101 . 1 1 107 107 VAL HG11 H 1 0.46 0.02 . 1 . . . . . . . . 4472 1 1102 . 1 1 107 107 VAL HG12 H 1 0.46 0.02 . 1 . . . . . . . . 4472 1 1103 . 1 1 107 107 VAL HG13 H 1 0.46 0.02 . 1 . . . . . . . . 4472 1 1104 . 1 1 107 107 VAL CG2 C 13 22 0.2 . 1 . . . . . . . . 4472 1 1105 . 1 1 107 107 VAL CG1 C 13 21.2 0.2 . 1 . . . . . . . . 4472 1 1106 . 1 1 108 108 VAL N N 15 125.7 0.2 . 1 . . . . . . . . 4472 1 1107 . 1 1 108 108 VAL H H 1 8.09 0.02 . 1 . . . . . . . . 4472 1 1108 . 1 1 108 108 VAL CA C 13 60.3 0.2 . 1 . . . . . . . . 4472 1 1109 . 1 1 108 108 VAL HA H 1 4.96 0.02 . 1 . . . . . . . . 4472 1 1110 . 1 1 108 108 VAL CB C 13 32.7 0.2 . 1 . . . . . . . . 4472 1 1111 . 1 1 108 108 VAL HB H 1 1.94 0.02 . 1 . . . . . . . . 4472 1 1112 . 1 1 108 108 VAL HG11 H 1 1.08 0.02 . 1 . . . . . . . . 4472 1 1113 . 1 1 108 108 VAL HG12 H 1 1.08 0.02 . 1 . . . . . . . . 4472 1 1114 . 1 1 108 108 VAL HG13 H 1 1.08 0.02 . 1 . . . . . . . . 4472 1 1115 . 1 1 108 108 VAL HG21 H 1 1.08 0.02 . 1 . . . . . . . . 4472 1 1116 . 1 1 108 108 VAL HG22 H 1 1.08 0.02 . 1 . . . . . . . . 4472 1 1117 . 1 1 108 108 VAL HG23 H 1 1.08 0.02 . 1 . . . . . . . . 4472 1 1118 . 1 1 108 108 VAL CG1 C 13 21.2 0.2 . 1 . . . . . . . . 4472 1 1119 . 1 1 108 108 VAL CG2 C 13 21.6 0.2 . 1 . . . . . . . . 4472 1 1120 . 1 1 109 109 LYS N N 15 124.4 0.2 . 1 . . . . . . . . 4472 1 1121 . 1 1 109 109 LYS H H 1 8.01 0.02 . 1 . . . . . . . . 4472 1 1122 . 1 1 109 109 LYS CA C 13 54.7 0.2 . 1 . . . . . . . . 4472 1 1123 . 1 1 109 109 LYS HA H 1 4.26 0.02 . 1 . . . . . . . . 4472 1 1124 . 1 1 109 109 LYS CB C 13 32.6 0.2 . 1 . . . . . . . . 4472 1 1125 . 1 1 109 109 LYS HB2 H 1 2.04 0.02 . 2 . . . . . . . . 4472 1 1126 . 1 1 109 109 LYS HB3 H 1 1.87 0.02 . 2 . . . . . . . . 4472 1 1127 . 1 1 110 110 PRO CD C 13 49.9 0.2 . 1 . . . . . . . . 4472 1 1128 . 1 1 110 110 PRO CA C 13 62.2 0.2 . 1 . . . . . . . . 4472 1 1129 . 1 1 110 110 PRO HA H 1 4.46 0.02 . 1 . . . . . . . . 4472 1 1130 . 1 1 110 110 PRO CB C 13 34.3 0.2 . 1 . . . . . . . . 4472 1 1131 . 1 1 110 110 PRO HB2 H 1 2.26 0.02 . 2 . . . . . . . . 4472 1 1132 . 1 1 110 110 PRO HB3 H 1 1.96 0.02 . 2 . . . . . . . . 4472 1 1133 . 1 1 110 110 PRO CG C 13 23.8 0.2 . 1 . . . . . . . . 4472 1 1134 . 1 1 110 110 PRO HG2 H 1 1.92 0.02 . 1 . . . . . . . . 4472 1 1135 . 1 1 110 110 PRO HG3 H 1 1.92 0.02 . 1 . . . . . . . . 4472 1 1136 . 1 1 110 110 PRO HD2 H 1 3.67 0.02 . 2 . . . . . . . . 4472 1 1137 . 1 1 110 110 PRO HD3 H 1 3.45 0.02 . 2 . . . . . . . . 4472 1 1138 . 1 1 111 111 PHE N N 15 114.8 0.2 . 1 . . . . . . . . 4472 1 1139 . 1 1 111 111 PHE H H 1 7.73 0.02 . 1 . . . . . . . . 4472 1 1140 . 1 1 111 111 PHE CA C 13 53.8 0.2 . 1 . . . . . . . . 4472 1 1141 . 1 1 111 111 PHE HA H 1 5.45 0.02 . 1 . . . . . . . . 4472 1 1142 . 1 1 111 111 PHE CB C 13 41.3 0.2 . 1 . . . . . . . . 4472 1 1143 . 1 1 111 111 PHE HB2 H 1 3.2 0.02 . 2 . . . . . . . . 4472 1 1144 . 1 1 111 111 PHE HB3 H 1 2.96 0.02 . 2 . . . . . . . . 4472 1 1145 . 1 1 111 111 PHE HD1 H 1 7 0.02 . 3 . . . . . . . . 4472 1 1146 . 1 1 111 111 PHE CD1 C 13 130.3 0.2 . 3 . . . . . . . . 4472 1 1147 . 1 1 112 112 THR N N 15 109.1 0.2 . 1 . . . . . . . . 4472 1 1148 . 1 1 112 112 THR H H 1 8.02 0.02 . 1 . . . . . . . . 4472 1 1149 . 1 1 112 112 THR CA C 13 59.2 0.2 . 1 . . . . . . . . 4472 1 1150 . 1 1 112 112 THR HA H 1 4.57 0.02 . 1 . . . . . . . . 4472 1 1151 . 1 1 112 112 THR CB C 13 68.5 0.2 . 1 . . . . . . . . 4472 1 1152 . 1 1 112 112 THR HB H 1 4.83 0.02 . 1 . . . . . . . . 4472 1 1153 . 1 1 112 112 THR HG21 H 1 1.31 0.02 . 1 . . . . . . . . 4472 1 1154 . 1 1 112 112 THR HG22 H 1 1.31 0.02 . 1 . . . . . . . . 4472 1 1155 . 1 1 112 112 THR HG23 H 1 1.31 0.02 . 1 . . . . . . . . 4472 1 1156 . 1 1 112 112 THR CG2 C 13 21.6 0.2 . 1 . . . . . . . . 4472 1 1157 . 1 1 113 113 ALA N N 15 123.5 0.2 . 1 . . . . . . . . 4472 1 1158 . 1 1 113 113 ALA H H 1 9.15 0.02 . 1 . . . . . . . . 4472 1 1159 . 1 1 113 113 ALA CA C 13 55.6 0.2 . 1 . . . . . . . . 4472 1 1160 . 1 1 113 113 ALA HA H 1 4 0.02 . 1 . . . . . . . . 4472 1 1161 . 1 1 113 113 ALA HB1 H 1 1.5 0.02 . 1 . . . . . . . . 4472 1 1162 . 1 1 113 113 ALA HB2 H 1 1.5 0.02 . 1 . . . . . . . . 4472 1 1163 . 1 1 113 113 ALA HB3 H 1 1.5 0.02 . 1 . . . . . . . . 4472 1 1164 . 1 1 113 113 ALA CB C 13 17.5 0.2 . 1 . . . . . . . . 4472 1 1165 . 1 1 114 114 ALA N N 15 118.4 0.2 . 1 . . . . . . . . 4472 1 1166 . 1 1 114 114 ALA H H 1 8.28 0.02 . 1 . . . . . . . . 4472 1 1167 . 1 1 114 114 ALA CA C 13 54.7 0.2 . 1 . . . . . . . . 4472 1 1168 . 1 1 114 114 ALA HA H 1 4.23 0.02 . 1 . . . . . . . . 4472 1 1169 . 1 1 114 114 ALA HB1 H 1 1.48 0.02 . 1 . . . . . . . . 4472 1 1170 . 1 1 114 114 ALA HB2 H 1 1.48 0.02 . 1 . . . . . . . . 4472 1 1171 . 1 1 114 114 ALA HB3 H 1 1.48 0.02 . 1 . . . . . . . . 4472 1 1172 . 1 1 114 114 ALA CB C 13 18 0.2 . 1 . . . . . . . . 4472 1 1173 . 1 1 115 115 THR N N 15 116.7 0.2 . 1 . . . . . . . . 4472 1 1174 . 1 1 115 115 THR H H 1 7.9 0.02 . 1 . . . . . . . . 4472 1 1175 . 1 1 115 115 THR CA C 13 65.9 0.2 . 1 . . . . . . . . 4472 1 1176 . 1 1 115 115 THR HA H 1 4.07 0.02 . 1 . . . . . . . . 4472 1 1177 . 1 1 115 115 THR CB C 13 68.5 0.2 . 1 . . . . . . . . 4472 1 1178 . 1 1 115 115 THR HB H 1 4.4 0.02 . 1 . . . . . . . . 4472 1 1179 . 1 1 115 115 THR HG21 H 1 1.3 0.02 . 1 . . . . . . . . 4472 1 1180 . 1 1 115 115 THR HG22 H 1 1.3 0.02 . 1 . . . . . . . . 4472 1 1181 . 1 1 115 115 THR HG23 H 1 1.3 0.02 . 1 . . . . . . . . 4472 1 1182 . 1 1 115 115 THR CG2 C 13 22 0.2 . 1 . . . . . . . . 4472 1 1183 . 1 1 116 116 LEU N N 15 121.7 0.2 . 1 . . . . . . . . 4472 1 1184 . 1 1 116 116 LEU H H 1 8.06 0.02 . 1 . . . . . . . . 4472 1 1185 . 1 1 116 116 LEU CA C 13 58.1 0.2 . 1 . . . . . . . . 4472 1 1186 . 1 1 116 116 LEU HA H 1 3.74 0.02 . 1 . . . . . . . . 4472 1 1187 . 1 1 116 116 LEU CB C 13 41 0.2 . 1 . . . . . . . . 4472 1 1188 . 1 1 116 116 LEU HB2 H 1 1.99 0.02 . 2 . . . . . . . . 4472 1 1189 . 1 1 116 116 LEU HB3 H 1 1.36 0.02 . 2 . . . . . . . . 4472 1 1190 . 1 1 116 116 LEU CG C 13 26.1 0.2 . 1 . . . . . . . . 4472 1 1191 . 1 1 116 116 LEU HG H 1 1.35 0.02 . 1 . . . . . . . . 4472 1 1192 . 1 1 116 116 LEU HD21 H 1 0.68 0.02 . 1 . . . . . . . . 4472 1 1193 . 1 1 116 116 LEU HD22 H 1 0.68 0.02 . 1 . . . . . . . . 4472 1 1194 . 1 1 116 116 LEU HD23 H 1 0.68 0.02 . 1 . . . . . . . . 4472 1 1195 . 1 1 116 116 LEU HD11 H 1 0.46 0.02 . 1 . . . . . . . . 4472 1 1196 . 1 1 116 116 LEU HD12 H 1 0.46 0.02 . 1 . . . . . . . . 4472 1 1197 . 1 1 116 116 LEU HD13 H 1 0.46 0.02 . 1 . . . . . . . . 4472 1 1198 . 1 1 116 116 LEU CD2 C 13 25.7 0.2 . 1 . . . . . . . . 4472 1 1199 . 1 1 116 116 LEU CD1 C 13 22 0.2 . 1 . . . . . . . . 4472 1 1200 . 1 1 117 117 GLU N N 15 118.4 0.2 . 1 . . . . . . . . 4472 1 1201 . 1 1 117 117 GLU H H 1 8.76 0.02 . 1 . . . . . . . . 4472 1 1202 . 1 1 117 117 GLU CA C 13 59.2 0.2 . 1 . . . . . . . . 4472 1 1203 . 1 1 117 117 GLU HA H 1 3.86 0.02 . 1 . . . . . . . . 4472 1 1204 . 1 1 117 117 GLU CB C 13 29.6 0.2 . 1 . . . . . . . . 4472 1 1205 . 1 1 117 117 GLU HB2 H 1 2.22 0.02 . 1 . . . . . . . . 4472 1 1206 . 1 1 117 117 GLU HB3 H 1 2.22 0.02 . 1 . . . . . . . . 4472 1 1207 . 1 1 117 117 GLU CG C 13 35.7 0.2 . 1 . . . . . . . . 4472 1 1208 . 1 1 117 117 GLU HG2 H 1 2.29 0.02 . 1 . . . . . . . . 4472 1 1209 . 1 1 117 117 GLU HG3 H 1 2.29 0.02 . 1 . . . . . . . . 4472 1 1210 . 1 1 118 118 GLU N N 15 117.9 0.2 . 1 . . . . . . . . 4472 1 1211 . 1 1 118 118 GLU H H 1 7.88 0.02 . 1 . . . . . . . . 4472 1 1212 . 1 1 118 118 GLU CA C 13 59.3 0.2 . 1 . . . . . . . . 4472 1 1213 . 1 1 118 118 GLU HA H 1 4.09 0.02 . 1 . . . . . . . . 4472 1 1214 . 1 1 118 118 GLU CB C 13 29.3 0.2 . 1 . . . . . . . . 4472 1 1215 . 1 1 118 118 GLU HB2 H 1 2.22 0.02 . 1 . . . . . . . . 4472 1 1216 . 1 1 118 118 GLU HB3 H 1 2.22 0.02 . 1 . . . . . . . . 4472 1 1217 . 1 1 118 118 GLU CG C 13 35.7 0.2 . 1 . . . . . . . . 4472 1 1218 . 1 1 118 118 GLU HG2 H 1 2.47 0.02 . 1 . . . . . . . . 4472 1 1219 . 1 1 118 118 GLU HG3 H 1 2.47 0.02 . 1 . . . . . . . . 4472 1 1220 . 1 1 119 119 LYS N N 15 117.1 0.2 . 1 . . . . . . . . 4472 1 1221 . 1 1 119 119 LYS H H 1 7.91 0.02 . 1 . . . . . . . . 4472 1 1222 . 1 1 119 119 LYS CA C 13 57.5 0.2 . 1 . . . . . . . . 4472 1 1223 . 1 1 119 119 LYS HA H 1 4.01 0.02 . 1 . . . . . . . . 4472 1 1224 . 1 1 119 119 LYS CB C 13 31.2 0.2 . 1 . . . . . . . . 4472 1 1225 . 1 1 119 119 LYS HB2 H 1 1.91 0.02 . 2 . . . . . . . . 4472 1 1226 . 1 1 119 119 LYS HB3 H 1 1.53 0.02 . 2 . . . . . . . . 4472 1 1227 . 1 1 119 119 LYS CG C 13 24.6 0.2 . 1 . . . . . . . . 4472 1 1228 . 1 1 119 119 LYS HG2 H 1 1.29 0.02 . 1 . . . . . . . . 4472 1 1229 . 1 1 119 119 LYS HG3 H 1 1.29 0.02 . 1 . . . . . . . . 4472 1 1230 . 1 1 119 119 LYS CD C 13 27.6 0.2 . 1 . . . . . . . . 4472 1 1231 . 1 1 119 119 LYS HD2 H 1 1.5 0.02 . 1 . . . . . . . . 4472 1 1232 . 1 1 119 119 LYS HD3 H 1 1.5 0.02 . 1 . . . . . . . . 4472 1 1233 . 1 1 120 120 LEU N N 15 118.4 0.2 . 1 . . . . . . . . 4472 1 1234 . 1 1 120 120 LEU H H 1 8.49 0.02 . 1 . . . . . . . . 4472 1 1235 . 1 1 120 120 LEU CA C 13 58.1 0.2 . 1 . . . . . . . . 4472 1 1236 . 1 1 120 120 LEU HA H 1 3.45 0.02 . 1 . . . . . . . . 4472 1 1237 . 1 1 120 120 LEU CB C 13 40.6 0.2 . 1 . . . . . . . . 4472 1 1238 . 1 1 120 120 LEU HB2 H 1 1.63 0.02 . 2 . . . . . . . . 4472 1 1239 . 1 1 120 120 LEU HB3 H 1 0.91 0.02 . 2 . . . . . . . . 4472 1 1240 . 1 1 120 120 LEU CG C 13 26.1 0.2 . 1 . . . . . . . . 4472 1 1241 . 1 1 120 120 LEU HG H 1 1.35 0.02 . 1 . . . . . . . . 4472 1 1242 . 1 1 120 120 LEU HD11 H 1 0.34 0.02 . 1 . . . . . . . . 4472 1 1243 . 1 1 120 120 LEU HD12 H 1 0.34 0.02 . 1 . . . . . . . . 4472 1 1244 . 1 1 120 120 LEU HD13 H 1 0.34 0.02 . 1 . . . . . . . . 4472 1 1245 . 1 1 120 120 LEU HD21 H 1 0.15 0.02 . 1 . . . . . . . . 4472 1 1246 . 1 1 120 120 LEU HD22 H 1 0.15 0.02 . 1 . . . . . . . . 4472 1 1247 . 1 1 120 120 LEU HD23 H 1 0.15 0.02 . 1 . . . . . . . . 4472 1 1248 . 1 1 120 120 LEU CD1 C 13 25.3 0.2 . 1 . . . . . . . . 4472 1 1249 . 1 1 120 120 LEU CD2 C 13 23.8 0.2 . 1 . . . . . . . . 4472 1 1250 . 1 1 121 121 ASN N N 15 115.4 0.2 . 1 . . . . . . . . 4472 1 1251 . 1 1 121 121 ASN H H 1 8.48 0.02 . 1 . . . . . . . . 4472 1 1252 . 1 1 121 121 ASN CA C 13 56 0.2 . 1 . . . . . . . . 4472 1 1253 . 1 1 121 121 ASN HA H 1 4.57 0.02 . 1 . . . . . . . . 4472 1 1254 . 1 1 121 121 ASN CB C 13 37.5 0.2 . 1 . . . . . . . . 4472 1 1255 . 1 1 121 121 ASN HB2 H 1 3.02 0.02 . 2 . . . . . . . . 4472 1 1256 . 1 1 121 121 ASN HB3 H 1 2.85 0.02 . 2 . . . . . . . . 4472 1 1257 . 1 1 122 122 LYS N N 15 119.4 0.2 . 1 . . . . . . . . 4472 1 1258 . 1 1 122 122 LYS H H 1 7.94 0.02 . 1 . . . . . . . . 4472 1 1259 . 1 1 122 122 LYS CA C 13 58.5 0.2 . 1 . . . . . . . . 4472 1 1260 . 1 1 122 122 LYS HA H 1 4.19 0.02 . 1 . . . . . . . . 4472 1 1261 . 1 1 122 122 LYS CB C 13 31.9 0.2 . 1 . . . . . . . . 4472 1 1262 . 1 1 122 122 LYS HB2 H 1 2.04 0.02 . 1 . . . . . . . . 4472 1 1263 . 1 1 122 122 LYS HB3 H 1 2.04 0.02 . 1 . . . . . . . . 4472 1 1264 . 1 1 122 122 LYS CD C 13 28.7 0.2 . 1 . . . . . . . . 4472 1 1265 . 1 1 122 122 LYS HD2 H 1 1.78 0.02 . 1 . . . . . . . . 4472 1 1266 . 1 1 122 122 LYS HD3 H 1 1.78 0.02 . 1 . . . . . . . . 4472 1 1267 . 1 1 122 122 LYS CE C 13 41.7 0.2 . 1 . . . . . . . . 4472 1 1268 . 1 1 122 122 LYS HE2 H 1 3.04 0.02 . 1 . . . . . . . . 4472 1 1269 . 1 1 122 122 LYS HE3 H 1 3.04 0.02 . 1 . . . . . . . . 4472 1 1270 . 1 1 123 123 ILE N N 15 121.9 0.2 . 1 . . . . . . . . 4472 1 1271 . 1 1 123 123 ILE H H 1 7.68 0.02 . 1 . . . . . . . . 4472 1 1272 . 1 1 123 123 ILE CA C 13 65.5 0.2 . 1 . . . . . . . . 4472 1 1273 . 1 1 123 123 ILE HA H 1 3.74 0.02 . 1 . . . . . . . . 4472 1 1274 . 1 1 123 123 ILE CB C 13 37.5 0.2 . 1 . . . . . . . . 4472 1 1275 . 1 1 123 123 ILE HB H 1 1.91 0.02 . 1 . . . . . . . . 4472 1 1276 . 1 1 123 123 ILE HG21 H 1 0.94 0.02 . 1 . . . . . . . . 4472 1 1277 . 1 1 123 123 ILE HG22 H 1 0.94 0.02 . 1 . . . . . . . . 4472 1 1278 . 1 1 123 123 ILE HG23 H 1 0.94 0.02 . 1 . . . . . . . . 4472 1 1279 . 1 1 123 123 ILE CG2 C 13 17.5 0.2 . 1 . . . . . . . . 4472 1 1280 . 1 1 123 123 ILE CG1 C 13 29.4 0.2 . 1 . . . . . . . . 4472 1 1281 . 1 1 123 123 ILE HD11 H 1 0.71 0.02 . 1 . . . . . . . . 4472 1 1282 . 1 1 123 123 ILE HD12 H 1 0.71 0.02 . 1 . . . . . . . . 4472 1 1283 . 1 1 123 123 ILE HD13 H 1 0.71 0.02 . 1 . . . . . . . . 4472 1 1284 . 1 1 123 123 ILE CD1 C 13 15.3 0.2 . 1 . . . . . . . . 4472 1 1285 . 1 1 124 124 PHE N N 15 118.4 0.2 . 1 . . . . . . . . 4472 1 1286 . 1 1 124 124 PHE H H 1 9.03 0.02 . 1 . . . . . . . . 4472 1 1287 . 1 1 124 124 PHE CA C 13 58.7 0.2 . 1 . . . . . . . . 4472 1 1288 . 1 1 124 124 PHE HA H 1 4.67 0.02 . 1 . . . . . . . . 4472 1 1289 . 1 1 124 124 PHE CB C 13 37.1 0.2 . 1 . . . . . . . . 4472 1 1290 . 1 1 124 124 PHE HB2 H 1 3.47 0.02 . 2 . . . . . . . . 4472 1 1291 . 1 1 124 124 PHE HB3 H 1 3.32 0.02 . 2 . . . . . . . . 4472 1 1292 . 1 1 124 124 PHE HD1 H 1 7.52 0.02 . 3 . . . . . . . . 4472 1 1293 . 1 1 124 124 PHE CD1 C 13 130.3 0.2 . 3 . . . . . . . . 4472 1 1294 . 1 1 124 124 PHE CE1 C 13 130.7 0.2 . 3 . . . . . . . . 4472 1 1295 . 1 1 124 124 PHE HE1 H 1 7.26 0.02 . 3 . . . . . . . . 4472 1 1296 . 1 1 124 124 PHE CZ C 13 128.4 0.2 . 1 . . . . . . . . 4472 1 1297 . 1 1 124 124 PHE HZ H 1 6.66 0.02 . 1 . . . . . . . . 4472 1 1298 . 1 1 125 125 GLU N N 15 117.6 0.2 . 1 . . . . . . . . 4472 1 1299 . 1 1 125 125 GLU H H 1 8.34 0.02 . 1 . . . . . . . . 4472 1 1300 . 1 1 125 125 GLU CA C 13 58.9 0.2 . 1 . . . . . . . . 4472 1 1301 . 1 1 125 125 GLU HA H 1 4.23 0.02 . 1 . . . . . . . . 4472 1 1302 . 1 1 125 125 GLU CB C 13 29.7 0.2 . 1 . . . . . . . . 4472 1 1303 . 1 1 125 125 GLU HB2 H 1 2.28 0.02 . 2 . . . . . . . . 4472 1 1304 . 1 1 125 125 GLU HB3 H 1 2.21 0.02 . 2 . . . . . . . . 4472 1 1305 . 1 1 125 125 GLU CG C 13 36.1 0.2 . 1 . . . . . . . . 4472 1 1306 . 1 1 125 125 GLU HG2 H 1 2.49 0.02 . 1 . . . . . . . . 4472 1 1307 . 1 1 125 125 GLU HG3 H 1 2.49 0.02 . 1 . . . . . . . . 4472 1 1308 . 1 1 126 126 LYS N N 15 120.2 0.2 . 1 . . . . . . . . 4472 1 1309 . 1 1 126 126 LYS H H 1 7.88 0.02 . 1 . . . . . . . . 4472 1 1310 . 1 1 126 126 LYS CA C 13 58.3 0.2 . 1 . . . . . . . . 4472 1 1311 . 1 1 126 126 LYS HA H 1 4.2 0.02 . 1 . . . . . . . . 4472 1 1312 . 1 1 126 126 LYS CB C 13 32.1 0.2 . 1 . . . . . . . . 4472 1 1313 . 1 1 126 126 LYS HB2 H 1 2.1 0.02 . 2 . . . . . . . . 4472 1 1314 . 1 1 126 126 LYS HB3 H 1 1.95 0.02 . 2 . . . . . . . . 4472 1 1315 . 1 1 126 126 LYS CD C 13 28.3 0.2 . 1 . . . . . . . . 4472 1 1316 . 1 1 126 126 LYS HD2 H 1 1.76 0.02 . 1 . . . . . . . . 4472 1 1317 . 1 1 126 126 LYS HD3 H 1 1.76 0.02 . 1 . . . . . . . . 4472 1 1318 . 1 1 126 126 LYS CE C 13 41.7 0.2 . 1 . . . . . . . . 4472 1 1319 . 1 1 126 126 LYS HE2 H 1 3.04 0.02 . 1 . . . . . . . . 4472 1 1320 . 1 1 126 126 LYS HE3 H 1 3.04 0.02 . 1 . . . . . . . . 4472 1 1321 . 1 1 127 127 LEU N N 15 116.3 0.2 . 1 . . . . . . . . 4472 1 1322 . 1 1 127 127 LEU H H 1 8.04 0.02 . 1 . . . . . . . . 4472 1 1323 . 1 1 127 127 LEU CA C 13 54.7 0.2 . 1 . . . . . . . . 4472 1 1324 . 1 1 127 127 LEU HA H 1 4.43 0.02 . 1 . . . . . . . . 4472 1 1325 . 1 1 127 127 LEU CB C 13 42.4 0.2 . 1 . . . . . . . . 4472 1 1326 . 1 1 127 127 LEU HB2 H 1 1.86 0.02 . 2 . . . . . . . . 4472 1 1327 . 1 1 127 127 LEU HB3 H 1 1.75 0.02 . 2 . . . . . . . . 4472 1 1328 . 1 1 127 127 LEU CG C 13 26.8 0.2 . 1 . . . . . . . . 4472 1 1329 . 1 1 127 127 LEU HG H 1 1.94 0.02 . 1 . . . . . . . . 4472 1 1330 . 1 1 127 127 LEU HD11 H 1 0.96 0.02 . 1 . . . . . . . . 4472 1 1331 . 1 1 127 127 LEU HD12 H 1 0.96 0.02 . 1 . . . . . . . . 4472 1 1332 . 1 1 127 127 LEU HD13 H 1 0.96 0.02 . 1 . . . . . . . . 4472 1 1333 . 1 1 127 127 LEU HD21 H 1 0.9 0.02 . 1 . . . . . . . . 4472 1 1334 . 1 1 127 127 LEU HD22 H 1 0.9 0.02 . 1 . . . . . . . . 4472 1 1335 . 1 1 127 127 LEU HD23 H 1 0.9 0.02 . 1 . . . . . . . . 4472 1 1336 . 1 1 127 127 LEU CD1 C 13 25.7 0.2 . 1 . . . . . . . . 4472 1 1337 . 1 1 127 127 LEU CD2 C 13 22 0.2 . 1 . . . . . . . . 4472 1 1338 . 1 1 128 128 GLY N N 15 109.9 0.2 . 1 . . . . . . . . 4472 1 1339 . 1 1 128 128 GLY H H 1 7.97 0.02 . 1 . . . . . . . . 4472 1 1340 . 1 1 128 128 GLY CA C 13 46.5 0.2 . 1 . . . . . . . . 4472 1 1341 . 1 1 129 129 MET N N 15 124.1 0.2 . 1 . . . . . . . . 4472 1 1342 . 1 1 129 129 MET H H 1 8.3 0.02 . 1 . . . . . . . . 4472 1 1343 . 1 1 129 129 MET CA C 13 57.1 0.2 . 1 . . . . . . . . 4472 1 1344 . 1 1 129 129 MET HA H 1 4.2 0.02 . 1 . . . . . . . . 4472 1 1345 . 1 1 129 129 MET CB C 13 35.4 0.2 . 1 . . . . . . . . 4472 1 1346 . 1 1 129 129 MET HB2 H 1 2.2 0.02 . 2 . . . . . . . . 4472 1 1347 . 1 1 129 129 MET HB3 H 1 1.85 0.02 . 2 . . . . . . . . 4472 1 1348 . 1 1 129 129 MET CG C 13 32.4 0.2 . 1 . . . . . . . . 4472 1 1349 . 1 1 129 129 MET HG2 H 1 2.6 0.02 . 2 . . . . . . . . 4472 1 1350 . 1 1 129 129 MET HG3 H 1 2.46 0.02 . 2 . . . . . . . . 4472 1 stop_ save_