data_4083 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignments, Secondary Structure, Global Fold, and Dynamics of Chemotaxis Y Protein Using Three- and Four-Dimensional Heteronuclear (13C, 15N) NMR Spectroscopy ; _BMRB_accession_number 4083 _BMRB_flat_file_name bmr4083.str _Entry_type update _Submission_date 1997-12-23 _Accession_date 1997-12-23 _Entry_origination BMRB _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Moy Frankln L. . 2 Lowry David F. . 3 Matsumura Philip . . 4 Dahlquist Frederick W. . 5 Krywko James E. . 6 Domaille Peter J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 722 "13C chemical shifts" 423 "15N chemical shifts" 127 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-02-17 reformat BMRB 'Format updated to NMR-STAR version 2.1' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Moy, F. L., Lowry, D. F., Matsumura, P., Dahlquist, F. W., Krywko, J. E., and Domaille, P. J., "Assignments, Secondary Structure, Global Fold, and Dynamics of Chemotaxis Y Protein Using Three- and Four-Dimensional Heteronuclear (13C, 15N) NMR Spectroscopy," Biochemistry 33, 10731-10742 (1994). ; _Citation_title ; Assignments, Secondary Structure, Global Fold, and Dynamics of Chemotaxis Y Protein Using Three- and Four-Dimensional Heteronuclear (13C, 15N) NMR Spectroscopy ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Moy Frankln L. . 2 Lowry David F. . 3 Matsumura Philip . . 4 Dahlquist Frederick W. . 5 Krywko James E. . 6 Domaille Peter J. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 33 _Journal_issue 35 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 10731 _Page_last 10742 _Year 1994 _Details . loop_ _Keyword 'chemotaxis Y protein' CheY NMR 'nuclear magnetic resonance' stop_ save_ ################################## # Molecular system description # ################################## save_system_CheY _Saveframe_category molecular_system _Mol_system_name CheY _Abbreviation_common CheY _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CheY $CheY stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function ; Recombinant E. coli CheY, a 128 residue protein is involved in regulating bacterial chemotaxis by binding to the flagellar motor of a bacteria. ; stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CheY _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'E. coli CheY' _Abbreviation_common CheY _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 128 _Mol_residue_sequence ; ADKELKFLVVDDFSTMRRIV RNLLKELGFNNVEEAEDGVD ALNKLQAGGYGFVISDWNMP NMDGLELLKTIRADGAMSAL PVLMVTAEAKKENIIAAAQA GASGYVVKPFTAATLEEKLN KIFEKLGM ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 ALA 2 3 ASP 3 4 LYS 4 5 GLU 5 6 LEU 6 7 LYS 7 8 PHE 8 9 LEU 9 10 VAL 10 11 VAL 11 12 ASP 12 13 ASP 13 14 PHE 14 15 SER 15 16 THR 16 17 MET 17 18 ARG 18 19 ARG 19 20 ILE 20 21 VAL 21 22 ARG 22 23 ASN 23 24 LEU 24 25 LEU 25 26 LYS 26 27 GLU 27 28 LEU 28 29 GLY 29 30 PHE 30 31 ASN 31 32 ASN 32 33 VAL 33 34 GLU 34 35 GLU 35 36 ALA 36 37 GLU 37 38 ASP 38 39 GLY 39 40 VAL 40 41 ASP 41 42 ALA 42 43 LEU 43 44 ASN 44 45 LYS 45 46 LEU 46 47 GLN 47 48 ALA 48 49 GLY 49 50 GLY 50 51 TYR 51 52 GLY 52 53 PHE 53 54 VAL 54 55 ILE 55 56 SER 56 57 ASP 57 58 TRP 58 59 ASN 59 60 MET 60 61 PRO 61 62 ASN 62 63 MET 63 64 ASP 64 65 GLY 65 66 LEU 66 67 GLU 67 68 LEU 68 69 LEU 69 70 LYS 70 71 THR 71 72 ILE 72 73 ARG 73 74 ALA 74 75 ASP 75 76 GLY 76 77 ALA 77 78 MET 78 79 SER 79 80 ALA 80 81 LEU 81 82 PRO 82 83 VAL 83 84 LEU 84 85 MET 85 86 VAL 86 87 THR 87 88 ALA 88 89 GLU 89 90 ALA 90 91 LYS 91 92 LYS 92 93 GLU 93 94 ASN 94 95 ILE 95 96 ILE 96 97 ALA 97 98 ALA 98 99 ALA 99 100 GLN 100 101 ALA 101 102 GLY 102 103 ALA 103 104 SER 104 105 GLY 105 106 TYR 106 107 VAL 107 108 VAL 108 109 LYS 109 110 PRO 110 111 PHE 111 112 THR 112 113 ALA 113 114 ALA 114 115 THR 115 116 LEU 116 117 GLU 117 118 GLU 118 119 LYS 119 120 LEU 120 121 ASN 121 122 LYS 122 123 ILE 123 124 PHE 124 125 GLU 125 126 LYS 126 127 LEU 127 128 GLY 128 129 MET stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-07 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 2950 "che Y protein" 100.00 129 100.00 100.00 7.19e-85 BMRB 2951 "che Y protein" 100.00 129 100.00 100.00 7.19e-85 BMRB 3440 "che Y protein" 100.00 129 99.22 100.00 1.92e-84 BMRB 4472 "Chemotaxis protein Y" 100.00 129 100.00 100.00 7.19e-85 PDB 1A0O "Chey-Binding Domain Of Chea In Complex With Chey" 100.00 128 100.00 100.00 1.20e-84 PDB 1AB5 "Structure Of Chey Mutant F14n, V21t" 97.66 125 98.40 98.40 1.29e-80 PDB 1AB6 "Structure Of Chey Mutant F14n, V86t" 97.66 125 98.40 98.40 1.29e-80 PDB 1BDJ "Complex Structure Of Hpt Domain And Chey" 100.00 128 100.00 100.00 1.20e-84 PDB 1C4W "1.9 A Structure Of A-Thiophosphonate Modified Chey D57c" 100.00 128 99.22 99.22 9.99e-84 PDB 1CEY "Assignments, Secondary Structure, Global Fold, And Dynamics Of Chemotaxis Y Protein Using Three-And Four-Dimensional Heteronucl" 99.22 128 100.00 100.00 3.70e-84 PDB 1CHN "Magnesium Binding To The Bacterial Chemotaxis Protein Chey Results In Large Conformational Changes Involving Its Functional Sur" 100.00 128 100.00 100.00 1.20e-84 PDB 1CYE "Three Dimensional Structure Of Chemotactic Che Y Protein In Aqueous Solution By Nuclear Magnetic Resonance Methods" 100.00 129 99.22 100.00 1.92e-84 PDB 1D4Z "Crystal Structure Of Chey-95iv, A Hyperactive Chey Mutant" 100.00 128 99.22 100.00 1.90e-84 PDB 1DJM "Solution Structure Of Bef3-Activated Chey From Escherichia Coli" 100.00 129 100.00 100.00 7.19e-85 PDB 1E6K "Two-Component Signal Transduction System D12a Mutant Of Chey" 100.00 130 98.44 99.22 2.52e-83 PDB 1E6L "Two-Component Signal Transduction System D13a Mutant Of Chey" 99.22 127 99.21 99.21 4.66e-83 PDB 1E6M "Two-Component Signal Transduction System D57a Mutant Of Chey" 100.00 128 98.44 99.22 2.98e-83 PDB 1EAY "Chey-Binding (P2) Domain Of Chea In Complex With Chey From Escherichia Coli" 100.00 128 100.00 100.00 1.20e-84 PDB 1EHC "Structure Of Signal Transduction Protein Chey" 100.00 128 99.22 99.22 9.46e-84 PDB 1F4V "Crystal Structure Of Activated Chey Bound To The N-Terminus Of Flim" 100.00 128 100.00 100.00 1.20e-84 PDB 1FFG "Chey-binding Domain Of Chea In Complex With Chey At 2.1 A Resolution" 100.00 128 100.00 100.00 1.20e-84 PDB 1FFS "Chey-Binding Domain Of Chea In Complex With Chey From Crystals Soaked In Acetyl Phosphate" 100.00 128 100.00 100.00 1.20e-84 PDB 1FFW "Chey-Binding Domain Of Chea In Complex With Chey With A Bound Imido Diphosphate" 100.00 128 100.00 100.00 1.20e-84 PDB 1FQW "Crystal Structure Of Activated Chey" 100.00 128 100.00 100.00 1.20e-84 PDB 1JBE "1.08 A Structure Of Apo-Chey Reveals Meta-Active Conformation" 100.00 128 98.44 98.44 1.13e-82 PDB 1KMI "Crystal Structure Of An E.Coli Chemotaxis Protein, Chez" 100.00 129 100.00 100.00 7.19e-85 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 5.66e-84 PDB 1VLZ "Uncoupled Phosphorylation And Activation In Bacterial Chemotaxis: The 2.1 Angstrom Structure Of A Threonine To Isoleucine Mutan" 100.00 128 99.22 99.22 9.46e-84 PDB 1YMU "Signal Transduction Protein Chey Mutant With Met 17 Replaced By Gly (M17g)" 100.00 130 98.44 99.22 5.60e-83 PDB 1ZDM "Crystal Structure Of Activated Chey Bound To Xe" 100.00 129 99.22 99.22 1.03e-83 PDB 2B1J "Crystal Structure Of Unphosphorylated Chey Bound To The N- Terminus Of Flim" 100.00 128 100.00 100.00 1.20e-84 PDB 2CHE "Structure Of The Mg2+-Bound Form Of Chey And Mechanism Of Phosphoryl Transfer In Bacterial Chemotaxis" 100.00 128 97.66 99.22 5.02e-83 PDB 2CHF "Structure Of The Mg2+-Bound Form Of Chey And The Mechanism Of Phosphoryl Transfer In Bacterial Chemotaxis" 100.00 128 97.66 99.22 5.02e-83 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 97.66 99.22 3.11e-83 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 97.66 99.22 3.11e-83 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 97.66 99.22 3.11e-83 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 97.66 99.22 3.11e-83 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 97.66 99.22 3.11e-83 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 97.66 99.22 3.11e-83 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 97.66 99.22 3.11e-83 PDB 2ID7 "1.75 A Structure Of T87i Phosphono-Chey" 100.00 128 98.44 98.44 8.39e-83 PDB 2ID9 "1.85 A Structure Of T87i/y106w Phosphono-chey" 100.00 128 97.66 98.44 6.61e-82 PDB 2IDM "2.00 A Structure Of T87iY106W PHOSPHONO-Chey" 100.00 128 97.66 98.44 6.61e-82 PDB 2LP4 "Solution Structure Of P1-CheyP2 COMPLEX IN BACTERIAL CHEMOTAXIS" 100.00 128 100.00 100.00 1.20e-84 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" 100.00 128 97.66 99.22 5.02e-83 PDB 2PMC "Crystal Structure Of Chey-mg(2+) In Complex With Chez(c15) Peptide Solved From A P1 Crystal" 100.00 128 97.66 99.22 5.02e-83 PDB 3CHY "Crystal Structure Of Escherichia Coli Chey Refined At 1.7- Angstrom Resolution" 100.00 128 100.00 100.00 1.20e-84 PDB 3F7N "Crystal Structure Of Chey Triple Mutant F14e, N59m, E89l Complexed With Bef3- And Mn2+" 100.00 128 97.66 97.66 7.45e-81 PDB 3FFT "Crystal Structure Of Chey Double Mutant F14e, E89r Complexed With Bef3- And Mn2+" 100.00 128 98.44 98.44 1.73e-82 PDB 3FFW "Crystal Structure Of Chey Triple Mutant F14q, N59k, E89y Complexed With Bef3- And Mn2+" 100.00 128 97.66 97.66 1.78e-81 PDB 3FFX "Crystal Structure Of Chey Triple Mutant F14e, N59r, E89h Complexed With Bef3- And Mn2+" 100.00 128 97.66 97.66 6.46e-82 PDB 3FGZ "Crystal Structure Of Chey Triple Mutant F14e, N59m, E89r Complexed With Bef3- And Mn2+" 100.00 128 97.66 97.66 2.61e-81 PDB 3MYY "Structure Of E. Coli Chey Mutant A113p Bound To Beryllium Fluoride" 100.00 128 99.22 99.22 6.04e-84 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 3.31e-84 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 2.88e-84 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 2.01e-84 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 4.40e-84 PDB 3OO0 "Structure Of Apo Chey A113p" 100.00 129 99.22 99.22 5.36e-84 PDB 3OO1 "Structure Of E. Coli Chey Mutant A113p In The Absence Of Sulfate" 100.00 129 99.22 99.22 5.36e-84 PDB 3RVJ "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89q" 100.00 132 98.44 100.00 7.93e-84 PDB 3RVK "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89q" 100.00 132 98.44 100.00 7.93e-84 PDB 3RVL "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89r" 100.00 132 98.44 99.22 1.80e-83 PDB 3RVM "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d And E89r" 100.00 132 98.44 99.22 1.80e-83 PDB 3RVN "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89y" 100.00 132 98.44 99.22 3.07e-83 PDB 3RVO "Structure Of Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89y" 100.00 132 98.44 99.22 3.07e-83 PDB 3RVP "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89k" 100.00 132 98.44 100.00 1.45e-83 PDB 3RVQ "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89k" 100.00 132 98.44 100.00 1.45e-83 PDB 3RVR "Structure Of The Cheyn59dE89R MOLYBDATE COMPLEX" 100.00 132 98.44 99.22 1.80e-83 PDB 3RVS "Structure Of The Cheyn59dE89R TUNGSTATE COMPLEX" 100.00 132 98.44 99.22 1.80e-83 PDB 5CHY "Structure Of Chemotaxis Protein Chey" 100.00 128 99.22 100.00 6.31e-84 PDB 6CHY "Structure Of Chemotaxis Protein Chey" 100.00 128 98.44 99.22 5.36e-83 DBJ BAA15698 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli str. K12 substr. W3110]" 100.00 129 100.00 100.00 7.19e-85 DBJ BAB36015 "chemotaxis protein CheY [Escherichia coli O157:H7 str. Sakai]" 100.00 129 100.00 100.00 7.19e-85 DBJ BAG77641 "chemotactic response regulator CheY [Escherichia coli SE11]" 100.00 129 100.00 100.00 7.19e-85 DBJ BAI25973 "chemotaxis regulator CheY, transmitting signal to flagellar motor component [Escherichia coli O26:H11 str. 11368]" 100.00 129 100.00 100.00 7.19e-85 DBJ BAI30936 "chemotaxis regulator CheY, transmitting signal to flagellar motor component [Escherichia coli O103:H2 str. 12009]" 100.00 129 100.00 100.00 7.19e-85 EMBL CAD05667 "chemotaxis protein CheY [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 129 97.66 99.22 3.11e-83 EMBL CAP76371 "chemotaxis protein cheY [Escherichia coli LF82]" 100.00 129 100.00 100.00 7.19e-85 EMBL CAQ32359 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli BL21(DE3)]" 100.00 129 100.00 100.00 7.19e-85 EMBL CAQ98822 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli IAI1]" 100.00 129 100.00 100.00 7.19e-85 EMBL CAR03242 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli S88]" 100.00 129 99.22 100.00 2.26e-84 GB AAA23570 "cheY protein [Escherichia coli]" 100.00 129 99.22 99.22 5.36e-84 GB AAA23577 "CheY [Escherichia coli]" 100.00 129 100.00 100.00 7.19e-85 GB AAA27037 "CheY [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 129 97.66 99.22 3.11e-83 GB AAC74952 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli str. K-12 substr. MG1655]" 100.00 129 100.00 100.00 7.19e-85 GB AAG56872 "chemotaxis regulator transmits chemoreceptor signals to flagelllar motor components [Escherichia coli O157:H7 str. EDL933]" 100.00 129 100.00 100.00 7.19e-85 PIR AH0745 "chemotaxis protein CheY [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 129 97.66 99.22 3.11e-83 REF NP_310619 "chemotaxis regulatory protein CheY [Escherichia coli O157:H7 str. Sakai]" 100.00 129 100.00 100.00 7.19e-85 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 7.19e-85 REF NP_456482 "chemotaxis protein CheY [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 129 97.66 99.22 3.11e-83 REF NP_460873 "chemotaxis regulatory protein CheY [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 129 97.66 99.22 3.11e-83 REF NP_707777 "chemotaxis regulatory protein CheY [Shigella flexneri 2a str. 301]" 100.00 129 100.00 100.00 7.19e-85 SP P0A2D5 "RecName: Full=Chemotaxis protein CheY" 100.00 129 97.66 99.22 3.11e-83 SP P0A2D6 "RecName: Full=Chemotaxis protein CheY" 100.00 129 97.66 99.22 3.11e-83 SP P0AE67 "RecName: Full=Chemotaxis protein CheY" 100.00 129 100.00 100.00 7.19e-85 SP P0AE68 "RecName: Full=Chemotaxis protein CheY" 100.00 129 100.00 100.00 7.19e-85 SP P0AE69 "RecName: Full=Chemotaxis protein CheY" 100.00 129 100.00 100.00 7.19e-85 stop_ save_ ############# # Ligands # ############# save_MG _Saveframe_category ligand _Mol_type non-polymer _Name_common "MG (MAGNESIUM ION)" _BMRB_code . _PDB_code MG _Molecular_mass 24.305 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jun 23 09:23:39 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons MG MG MG . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CheY 'E. coli' 562 Eubacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $CheY 'recombinant technology' 'E. coli' Escherichia coli . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CheY . mM 1.0 4.0 [U-15N] 'sodium phosphate' 100 mM . . . 'magnesium chloride' . mM 4 5 . 'sodium azide' 0.02 % . . . D2O 10 % . . . H2O 90 % . . . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CheY . mM 1.0 4.0 '[U-13C; U-15N]' 'sodium phosphate' 100 mM . . . 'magnesium chloride' . mM 4 5 . 'sodium azide' 0.02 % . . . D2O 10 % . . . H2O 90 % . . . stop_ save_ save_sample_three _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CheY . mM 1.0 4.0 '[U-13C; U-15N]' 'sodium phosphate' 100 mM . . . 'magnesium chloride' . mM 4 5 . 'sodium azide' 0.02 % . . . D2O 99.8 % . . . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.75 0.05 n/a temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio_citation_label _Correction_value_citation_label TSP C 13 'methyl carbons' ppm 0.00 external . . . . $entry_citation $entry_citation TSP H 1 'methyl protons' ppm 0.00 external . . . . $entry_citation $entry_citation 'liquid ammonia' N 15 nitrogen ppm 0.00 external . . . . $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_three stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chem_shift_reference _Mol_system_component_name CheY _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 ALA HA H 3.90 . 1 2 . 1 ALA HB H 0.81 . 1 3 . 1 ALA CA C 50.9 . 1 4 . 1 ALA CB C 18.5 . 1 5 . 2 ASP HA H 4.49 . 1 6 . 2 ASP HB2 H 2.73 . 2 7 . 2 ASP HB3 H 2.64 . 2 8 . 2 ASP CA C 53.7 . 1 9 . 2 ASP CB C 41.6 . 1 10 . 3 LYS H H 8.48 . 1 11 . 3 LYS HA H 4.26 . 1 12 . 3 LYS HB2 H 1.98 . 2 13 . 3 LYS HB3 H 1.77 . 2 14 . 3 LYS HG2 H 1.38 . 2 15 . 3 LYS HG3 H 1.27 . 2 16 . 3 LYS HD2 H 1.19 . 2 17 . 3 LYS HD3 H 1.15 . 2 18 . 3 LYS HE2 H 2.78 . 1 19 . 3 LYS HE3 H 2.78 . 1 20 . 3 LYS CA C 57.0 . 1 21 . 3 LYS CB C 30.5 . 1 22 . 3 LYS CG C 24.5 . 1 23 . 3 LYS CD C 27.8 . 1 24 . 3 LYS CE C 42.0 . 1 25 . 3 LYS N N 120.8 . 1 26 . 4 GLU H H 8.68 . 1 27 . 4 GLU HA H 4.48 . 1 28 . 4 GLU HB2 H 2.27 . 2 29 . 4 GLU HB3 H 1.97 . 2 30 . 4 GLU HG2 H 2.35 . 1 31 . 4 GLU HG3 H 2.35 . 1 32 . 4 GLU CA C 55.7 . 1 33 . 4 GLU CB C 29.0 . 1 34 . 4 GLU CG C 36.3 . 1 35 . 4 GLU N N 117.9 . 1 36 . 5 LEU H H 7.51 . 1 37 . 5 LEU HA H 3.84 . 1 38 . 5 LEU HB2 H 1.80 . 2 39 . 5 LEU HB3 H 1.63 . 2 40 . 5 LEU HG H 1.21 . 1 41 . 5 LEU HD1 H 0.81 . 2 42 . 5 LEU HD2 H 0.65 . 2 43 . 5 LEU CA C 56.4 . 1 44 . 5 LEU CB C 43.1 . 1 45 . 5 LEU CG C 26.2 . 1 46 . 5 LEU CD1 C 25.0 . 2 47 . 5 LEU CD2 C 26.5 . 2 48 . 5 LEU N N 122.7 . 1 49 . 6 LYS H H 8.47 . 1 50 . 6 LYS HA H 5.10 . 1 51 . 6 LYS HB2 H 1.88 . 2 52 . 6 LYS HB3 H 1.50 . 2 53 . 6 LYS HG2 H 1.13 . 1 54 . 6 LYS HG3 H 1.13 . 1 55 . 6 LYS HD2 H 1.16 . 2 56 . 6 LYS HD3 H 0.83 . 2 57 . 6 LYS HE2 H 2.47 . 2 58 . 6 LYS HE3 H 2.22 . 2 59 . 6 LYS CA C 56.1 . 1 60 . 6 LYS CB C 33.5 . 1 61 . 6 LYS CD C 29.1 . 1 62 . 6 LYS CE C 41.2 . 1 63 . 6 LYS N N 124.7 . 1 64 . 7 PHE H H 9.20 . 1 65 . 7 PHE HA H 5.41 . 1 66 . 7 PHE HB2 H 3.21 . 2 67 . 7 PHE HB3 H 2.54 . 2 68 . 7 PHE HD1 H 7.02 . 1 69 . 7 PHE HD2 H 7.02 . 1 70 . 7 PHE HE1 H 6.21 . 1 71 . 7 PHE HE2 H 6.21 . 1 72 . 7 PHE HZ H 5.66 . 1 73 . 7 PHE CA C 57.1 . 1 74 . 7 PHE CB C 43.4 . 1 75 . 7 PHE CD1 C 130.9 . 1 76 . 7 PHE CD2 C 130.9 . 1 77 . 7 PHE CE1 C 131.2 . 1 78 . 7 PHE CE2 C 131.2 . 1 79 . 7 PHE CZ C 128.0 . 1 80 . 7 PHE N N 127.2 . 1 81 . 8 LEU H H 8.78 . 1 82 . 8 LEU HA H 5.13 . 1 83 . 8 LEU HB2 H 1.70 . 2 84 . 8 LEU HB3 H 1.09 . 2 85 . 8 LEU HG H 1.16 . 1 86 . 8 LEU HD1 H 0.56 . 2 87 . 8 LEU HD2 H 0.38 . 2 88 . 8 LEU CA C 52.9 . 1 89 . 8 LEU CB C 43.9 . 1 90 . 8 LEU CD1 C 22.7 . 2 91 . 8 LEU CD2 C 27.1 . 2 92 . 8 LEU N N 120.5 . 1 93 . 9 VAL H H 9.04 . 1 94 . 9 VAL HA H 4.80 . 1 95 . 9 VAL HB H 1.99 . 1 96 . 9 VAL HG1 H 0.99 . 1 97 . 9 VAL HG2 H 0.99 . 1 98 . 9 VAL CA C 61.4 . 1 99 . 9 VAL CB C 33.0 . 1 100 . 9 VAL CG1 C 21.1 . 1 101 . 9 VAL CG2 C 21.1 . 1 102 . 9 VAL N N 126.1 . 1 103 . 10 VAL H H 9.21 . 1 104 . 10 VAL HA H 4.82 . 1 105 . 10 VAL HB H 2.27 . 1 106 . 10 VAL HG1 H 0.65 . 2 107 . 10 VAL HG2 H 0.68 . 2 108 . 10 VAL CA C 59.7 . 1 109 . 10 VAL CB C 32.6 . 1 110 . 10 VAL CG1 C 21.4 . 2 111 . 10 VAL CG2 C 21.3 . 2 112 . 10 VAL N N 126.2 . 1 113 . 11 ASP H H 8.11 . 1 114 . 11 ASP HA H 4.65 . 1 115 . 11 ASP HB2 H 2.74 . 2 116 . 11 ASP HB3 H 2.53 . 2 117 . 11 ASP CA C 55.4 . 1 118 . 11 ASP CB C 43.6 . 1 119 . 11 ASP N N 123.4 . 1 120 . 12 ASP H H 9.38 . 1 121 . 12 ASP HA H 5.08 . 1 122 . 12 ASP HB2 H 2.98 . 2 123 . 12 ASP HB3 H 2.80 . 2 124 . 12 ASP CA C 55.0 . 1 125 . 12 ASP CB C 40.1 . 1 126 . 12 ASP N N 122.9 . 1 127 . 13 PHE HA H 5.26 . 1 128 . 13 PHE HB2 H 3.22 . 1 129 . 13 PHE HB3 H 3.22 . 1 130 . 13 PHE HD1 H 7.42 . 1 131 . 13 PHE HD2 H 7.42 . 1 132 . 13 PHE HE1 H 7.36 . 1 133 . 13 PHE HE2 H 7.36 . 1 134 . 13 PHE HZ H 6.71 . 1 135 . 13 PHE CA C 54.3 . 1 136 . 13 PHE CB C 38.1 . 1 137 . 13 PHE CD1 C 130.5 . 1 138 . 13 PHE CD2 C 130.5 . 1 139 . 13 PHE CE1 C 128.8 . 1 140 . 13 PHE CE2 C 128.8 . 1 141 . 13 PHE CZ C 128.5 . 1 142 . 15 THR HA H 3.77 . 1 143 . 15 THR HB H 3.23 . 1 144 . 15 THR HG2 H 1.15 . 1 145 . 15 THR CA C 65.4 . 1 146 . 15 THR CB C 68.1 . 1 147 . 15 THR CG2 C 21.5 . 1 148 . 16 MET H H 6.49 . 1 149 . 16 MET HA H 4.51 . 1 150 . 16 MET HB2 H 2.18 . 1 151 . 16 MET HB3 H 2.18 . 1 152 . 16 MET HG2 H 2.76 . 2 153 . 16 MET HG3 H 2.66 . 2 154 . 16 MET CA C 55.9 . 1 155 . 16 MET CB C 31.1 . 1 156 . 16 MET CG C 32.6 . 1 157 . 16 MET N N 117.8 . 1 158 . 17 ARG H H 7.57 . 1 159 . 17 ARG HA H 3.82 . 1 160 . 17 ARG HB2 H 2.03 . 2 161 . 17 ARG HB3 H 1.81 . 2 162 . 17 ARG HG2 H 1.38 . 2 163 . 17 ARG HG3 H 1.28 . 2 164 . 17 ARG HD2 H 2.92 . 1 165 . 17 ARG HD3 H 2.92 . 1 166 . 17 ARG CA C 60.5 . 1 167 . 17 ARG CB C 30.5 . 1 168 . 17 ARG CG C 24.3 . 1 169 . 17 ARG CD C 41.4 . 1 170 . 17 ARG N N 115.8 . 1 171 . 18 ARG H H 7.62 . 1 172 . 18 ARG HA H 3.93 . 1 173 . 18 ARG HB2 H 1.93 . 1 174 . 18 ARG HB3 H 1.93 . 1 175 . 18 ARG HG2 H 1.70 . 2 176 . 18 ARG HG3 H 1.63 . 2 177 . 18 ARG HD2 H 3.22 . 2 178 . 18 ARG HD3 H 3.05 . 2 179 . 18 ARG CA C 58.8 . 1 180 . 18 ARG CB C 29.4 . 1 181 . 18 ARG CG C 27.2 . 1 182 . 18 ARG CD C 43.1 . 1 183 . 18 ARG N N 115.6 . 1 184 . 19 ILE H H 7.76 . 1 185 . 19 ILE HA H 3.72 . 1 186 . 19 ILE HB H 2.11 . 1 187 . 19 ILE HG12 H 1.80 . 2 188 . 19 ILE HG13 H 1.09 . 2 189 . 19 ILE HG2 H 0.79 . 1 190 . 19 ILE HD1 H 0.81 . 1 191 . 19 ILE CA C 65.4 . 1 192 . 19 ILE CB C 37.8 . 1 193 . 19 ILE CG1 C 29.3 . 1 194 . 19 ILE CG2 C 16.3 . 1 195 . 19 ILE CD1 C 13.2 . 1 196 . 19 ILE N N 119.0 . 1 197 . 20 VAL H H 8.28 . 1 198 . 20 VAL HA H 3.43 . 1 199 . 20 VAL HB H 2.15 . 1 200 . 20 VAL HG1 H 1.16 . 2 201 . 20 VAL HG2 H 0.94 . 2 202 . 20 VAL CA C 67.2 . 1 203 . 20 VAL CB C 31.0 . 1 204 . 20 VAL CG1 C 23.4 . 2 205 . 20 VAL CG2 C 22.6 . 2 206 . 20 VAL N N 117.8 . 1 207 . 21 ARG H H 8.60 . 1 208 . 21 ARG HA H 3.82 . 1 209 . 21 ARG HB2 H 2.03 . 2 210 . 21 ARG HB3 H 1.80 . 2 211 . 21 ARG HG2 H 1.52 . 1 212 . 21 ARG HG3 H 1.52 . 1 213 . 21 ARG HD2 H 3.27 . 2 214 . 21 ARG HD3 H 3.10 . 2 215 . 21 ARG CA C 60.4 . 1 216 . 21 ARG CB C 30.5 . 1 217 . 21 ARG CG C 27.4 . 1 218 . 21 ARG CD C 43.8 . 1 219 . 21 ARG N N 118.2 . 1 220 . 22 ASN H H 8.42 . 1 221 . 22 ASN HA H 4.56 . 1 222 . 22 ASN HB2 H 3.03 . 2 223 . 22 ASN HB3 H 2.84 . 2 224 . 22 ASN HD21 H 7.53 . 2 225 . 22 ASN HD22 H 7.02 . 2 226 . 22 ASN CA C 55.7 . 1 227 . 22 ASN CB C 37.5 . 1 228 . 22 ASN N N 117.7 . 1 229 . 22 ASN ND2 N 109.7 . 1 230 . 23 LEU H H 8.44 . 1 231 . 23 LEU HA H 4.16 . 1 232 . 23 LEU HB2 H 2.06 . 2 233 . 23 LEU HB3 H 1.16 . 2 234 . 23 LEU HD1 H 0.73 . 2 235 . 23 LEU HD2 H 0.87 . 2 236 . 23 LEU CA C 58.0 . 1 237 . 23 LEU CB C 42.3 . 1 238 . 23 LEU CD1 C 26.5 . 2 239 . 23 LEU CD2 C 22.4 . 2 240 . 23 LEU N N 121.8 . 1 241 . 24 LEU H H 8.33 . 1 242 . 24 LEU HA H 3.83 . 1 243 . 24 LEU HB2 H 1.83 . 2 244 . 24 LEU HB3 H 1.34 . 2 245 . 24 LEU HG H 1.42 . 1 246 . 24 LEU HD1 H 0.17 . 2 247 . 24 LEU HD2 H -0.14 . 2 248 . 24 LEU CA C 58.2 . 1 249 . 24 LEU CB C 40.1 . 1 250 . 24 LEU CG C 26.5 . 1 251 . 24 LEU CD1 C 26.7 . 2 252 . 24 LEU CD2 C 22.3 . 2 253 . 24 LEU N N 116.6 . 1 254 . 25 LYS H H 7.94 . 1 255 . 25 LYS HA H 3.75 . 1 256 . 25 LYS HB2 H 2.07 . 1 257 . 25 LYS HB3 H 2.07 . 1 258 . 25 LYS HG2 H 1.63 . 2 259 . 25 LYS HG3 H 1.41 . 2 260 . 25 LYS HD2 H 1.79 . 1 261 . 25 LYS HD3 H 1.79 . 1 262 . 25 LYS HE2 H 2.98 . 1 263 . 25 LYS HE3 H 2.98 . 1 264 . 25 LYS CA C 59.8 . 1 265 . 25 LYS CB C 31.6 . 1 266 . 25 LYS CG C 24.7 . 1 267 . 25 LYS CD C 29.6 . 1 268 . 25 LYS CE C 41.4 . 1 269 . 25 LYS N N 119.2 . 1 270 . 26 GLU H H 7.95 . 1 271 . 26 GLU HA H 3.99 . 1 272 . 26 GLU HB2 H 2.3 . 2 273 . 26 GLU HB3 H 2.17 . 2 274 . 26 GLU HG2 H 2.45 . 1 275 . 26 GLU HG3 H 2.45 . 1 276 . 26 GLU CA C 59.3 . 1 277 . 26 GLU CB C 28.8 . 1 278 . 26 GLU CG C 36.0 . 1 279 . 26 GLU N N 120.9 . 1 280 . 27 LEU H H 7.43 . 1 281 . 27 LEU HA H 4.28 . 1 282 . 27 LEU HB2 H 2.16 . 2 283 . 27 LEU HB3 H 1.83 . 2 284 . 27 LEU HD1 H 0.88 . 1 285 . 27 LEU HD2 H 0.88 . 1 286 . 27 LEU CA C 54.3 . 1 287 . 27 LEU CB C 42.2 . 1 288 . 27 LEU CG C 26.1 . 1 289 . 27 LEU CD1 C 24.8 . 2 290 . 27 LEU CD2 C 21.8 . 2 291 . 27 LEU N N 115.7 . 1 292 . 28 GLY H H 7.74 . 1 293 . 28 GLY HA2 H 3.94 . 2 294 . 28 GLY HA3 H 3.54 . 2 295 . 28 GLY CA C 44.6 . 1 296 . 28 GLY N N 104.9 . 1 297 . 29 PHE H H 8.17 . 1 298 . 29 PHE HA H 4.86 . 1 299 . 29 PHE HB2 H 3.08 . 2 300 . 29 PHE HB3 H 2.45 . 2 301 . 29 PHE HD1 H 7.29 . 1 302 . 29 PHE HD2 H 7.29 . 1 303 . 29 PHE HE1 H 7.31 . 1 304 . 29 PHE HE2 H 7.31 . 1 305 . 29 PHE CA C 57.1 . 1 306 . 29 PHE CB C 38.6 . 1 307 . 29 PHE CD1 C 132.9 . 1 308 . 29 PHE CD2 C 132.9 . 1 309 . 29 PHE CE1 C 130.8 . 1 310 . 29 PHE CE2 C 130.8 . 1 311 . 29 PHE N N 119.7 . 1 312 . 30 ASN H H 8.28 . 1 313 . 30 ASN HA H 4.68 . 1 314 . 30 ASN HB2 H 2.83 . 2 315 . 30 ASN HB3 H 2.66 . 2 316 . 30 ASN HD21 H 7.39 . 2 317 . 30 ASN HD22 H 6.88 . 2 318 . 30 ASN CA C 53.6 . 1 319 . 30 ASN CB C 40.5 . 1 320 . 30 ASN N N 116.8 . 1 321 . 30 ASN ND2 N 111.8 . 1 322 . 31 ASN H H 9.82 . 1 323 . 31 ASN HA H 5.01 . 1 324 . 31 ASN HB2 H 3.27 . 2 325 . 31 ASN HB3 H 2.88 . 2 326 . 31 ASN HD21 H 7.56 . 2 327 . 31 ASN HD22 H 7.00 . 2 328 . 31 ASN CA C 52.1 . 1 329 . 31 ASN CB C 36.4 . 1 330 . 31 ASN N N 123.0 . 1 331 . 31 ASN ND2 N 109.2 . 1 332 . 32 VAL H H 7.53 . 1 333 . 32 VAL HA H 4.99 . 1 334 . 32 VAL HB H 1.85 . 1 335 . 32 VAL HG1 H 0.83 . 1 336 . 32 VAL HG2 H 0.83 . 1 337 . 32 VAL CA C 60.8 . 1 338 . 32 VAL CB C 36.3 . 1 339 . 32 VAL CG1 C 22.6 . 1 340 . 32 VAL CG2 C 22.6 . 1 341 . 32 VAL N N 120.8 . 1 342 . 33 GLU H H 9.06 . 1 343 . 33 GLU HA H 4.93 . 1 344 . 33 GLU HB2 H 2.31 . 2 345 . 33 GLU HB3 H 2.16 . 2 346 . 33 GLU HG2 H 2.57 . 1 347 . 33 GLU HG3 H 2.45 . 2 348 . 33 GLU CA C 53.8 . 1 349 . 33 GLU CB C 34.0 . 1 350 . 33 GLU CG C 36.2 . 1 351 . 33 GLU N N 125.4 . 1 352 . 34 GLU H H 8.92 . 1 353 . 34 GLU HA H 5.44 . 1 354 . 34 GLU HB2 H 1.90 . 1 355 . 34 GLU HB3 H 1.90 . 1 356 . 34 GLU HG2 H 2.15 . 1 357 . 34 GLU HG3 H 2.06 . 2 358 . 34 GLU CA C 54.7 . 1 359 . 34 GLU CB C 34.8 . 1 360 . 34 GLU CG C 35.5 . 1 361 . 34 GLU N N 119.6 . 1 362 . 35 ALA H H 8.84 . 1 363 . 35 ALA HA H 4.81 . 1 364 . 35 ALA HB H 1.30 . 1 365 . 35 ALA CA C 50.1 . 1 366 . 35 ALA CB C 22.7 . 1 367 . 35 ALA N N 119.0 . 1 368 . 36 GLU H H 9.48 . 1 369 . 36 GLU HA H 4.62 . 1 370 . 36 GLU HB2 H 2.06 . 1 371 . 36 GLU HB3 H 2.06 . 1 372 . 36 GLU HG2 H 2.20 . 1 373 . 36 GLU HG3 H 2.20 . 1 374 . 36 GLU CA C 56.7 . 1 375 . 36 GLU CB C 31.8 . 1 376 . 36 GLU CG C 35.7 . 1 377 . 36 GLU N N 116.1 . 1 378 . 37 ASP H H 7.49 . 1 379 . 37 ASP HA H 5.30 . 1 380 . 37 ASP HB2 H 3.51 . 2 381 . 37 ASP HB3 H 3.30 . 2 382 . 37 ASP CA C 53.7 . 1 383 . 37 ASP CB C 41.3 . 1 384 . 37 ASP N N 108.9 . 1 385 . 38 GLY H H 8.08 . 1 386 . 38 GLY HA2 H 3.75 . 2 387 . 38 GLY HA3 H 3.61 . 2 388 . 38 GLY CA C 48.4 . 1 389 . 38 GLY N N 100.8 . 1 390 . 39 VAL H H 7.95 . 1 391 . 39 VAL HA H 3.50 . 1 392 . 39 VAL HB H 2.26 . 1 393 . 39 VAL HG1 H 0.90 . 1 394 . 39 VAL HG2 H 0.90 . 1 395 . 39 VAL CA C 65.9 . 1 396 . 39 VAL CB C 31.4 . 1 397 . 39 VAL CG1 C 21.1 . 1 398 . 39 VAL CG2 C 21.1 . 1 399 . 39 VAL N N 121.4 . 1 400 . 40 ASP H H 8.57 . 1 401 . 40 ASP HA H 4.44 . 1 402 . 40 ASP HB2 H 2.97 . 2 403 . 40 ASP HB3 H 2.60 . 2 404 . 40 ASP CA C 56.4 . 1 405 . 40 ASP CB C 42.4 . 1 406 . 40 ASP N N 119.8 . 1 407 . 41 ALA H H 8.30 . 1 408 . 41 ALA HA H 3.61 . 1 409 . 41 ALA HB H 1.36 . 1 410 . 41 ALA CA C 55.0 . 1 411 . 41 ALA CB C 19.8 . 1 412 . 41 ALA N N 115.6 . 1 413 . 42 LEU H H 8.12 . 1 414 . 42 LEU HA H 3.75 . 1 415 . 42 LEU HB2 H 1.74 . 2 416 . 42 LEU HB3 H 1.51 . 2 417 . 42 LEU CA C 58.2 . 1 418 . 42 LEU CB C 41.2 . 1 419 . 42 LEU N N 117.1 . 1 420 . 43 ASN H H 7.85 . 1 421 . 43 ASN HA H 4.39 . 1 422 . 43 ASN HB2 H 3.05 . 2 423 . 43 ASN HB3 H 2.88 . 2 424 . 43 ASN HD21 H 7.78 . 2 425 . 43 ASN HD22 H 6.83 . 2 426 . 43 ASN CA C 56.0 . 1 427 . 43 ASN CB C 38.0 . 1 428 . 43 ASN N N 115.6 . 1 429 . 43 ASN ND2 N 111.1 . 1 430 . 44 LYS H H 7.92 . 1 431 . 44 LYS HA H 4.11 . 1 432 . 44 LYS HB2 H 1.76 . 1 433 . 44 LYS HB3 H 1.76 . 1 434 . 44 LYS HG2 H 1.43 . 1 435 . 44 LYS HG3 H 1.43 . 1 436 . 44 LYS HD2 H 1.69 . 1 437 . 44 LYS HD3 H 1.69 . 1 438 . 44 LYS HE2 H 2.96 . 1 439 . 44 LYS HE3 H 2.96 . 1 440 . 44 LYS CA C 60.0 . 1 441 . 44 LYS CB C 31.9 . 1 442 . 44 LYS CG C 24.5 . 1 443 . 44 LYS CD C 29.0 . 1 444 . 44 LYS CE C 41.7 . 1 445 . 44 LYS N N 119.0 . 1 446 . 45 LEU H H 8.75 . 1 447 . 45 LEU HA H 3.83 . 1 448 . 45 LEU HB2 H 1.75 . 2 449 . 45 LEU HB3 H 1.41 . 2 450 . 45 LEU HD1 H 0.53 . 2 451 . 45 LEU HD2 H 0.36 . 2 452 . 45 LEU CA C 57.2 . 1 453 . 45 LEU CB C 42.1 . 1 454 . 45 LEU CD1 C 25.3 . 2 455 . 45 LEU CD2 C 22.6 . 2 456 . 45 LEU N N 117.3 . 1 457 . 46 GLN H H 7.84 . 1 458 . 46 GLN HA H 4.03 . 1 459 . 46 GLN HB2 H 2.15 . 1 460 . 46 GLN HB3 H 2.15 . 1 461 . 46 GLN HG2 H 2.56 . 1 462 . 46 GLN HG3 H 2.56 . 1 463 . 46 GLN HE21 H 6.83 . 2 464 . 46 GLN HE22 H 6.78 . 2 465 . 46 GLN CA C 57.7 . 1 466 . 46 GLN CB C 28.1 . 1 467 . 46 GLN CG C 33.8 . 1 468 . 46 GLN N N 115.3 . 1 469 . 46 GLN NE2 N 107.9 . 1 470 . 47 ALA H H 7.60 . 1 471 . 47 ALA HA H 4.31 . 1 472 . 47 ALA HB H 1.67 . 1 473 . 47 ALA CA C 53.3 . 1 474 . 47 ALA CB C 19.0 . 1 475 . 47 ALA N N 119.1 . 1 476 . 48 GLY H H 7.58 . 1 477 . 48 GLY HA2 H 4.31 . 2 478 . 48 GLY HA3 H 4.08 . 2 479 . 48 GLY CA C 44.5 . 1 480 . 48 GLY N N 102.7 . 1 481 . 49 GLY H H 8.34 . 1 482 . 49 GLY HA2 H 3.94 . 2 483 . 49 GLY HA3 H 3.67 . 2 484 . 49 GLY CA C 45.2 . 1 485 . 49 GLY N N 102.5 . 1 486 . 50 TYR H H 8.07 . 1 487 . 50 TYR HA H 4.07 . 1 488 . 50 TYR HB2 H 3.05 . 2 489 . 50 TYR HB3 H 2.53 . 2 490 . 50 TYR HD1 H 6.93 . 1 491 . 50 TYR HD2 H 6.93 . 1 492 . 50 TYR HE1 H 6.69 . 1 493 . 50 TYR HE2 H 6.69 . 1 494 . 50 TYR CA C 60.6 . 1 495 . 50 TYR CB C 39.0 . 1 496 . 50 TYR N N 117.2 . 1 497 . 51 GLY H H 9.53 . 1 498 . 51 GLY HA2 H 4.51 . 2 499 . 51 GLY HA3 H 3.44 . 2 500 . 51 GLY CA C 44.3 . 1 501 . 51 GLY N N 105.7 . 1 502 . 52 PHE H H 7.55 . 1 503 . 52 PHE HA H 4.10 . 1 504 . 52 PHE HB2 H 2.01 . 1 505 . 52 PHE HB3 H 2.01 . 1 506 . 52 PHE HD1 H 6.89 . 1 507 . 52 PHE HD2 H 6.89 . 1 508 . 52 PHE HE1 H 6.87 . 1 509 . 52 PHE HE2 H 6.87 . 1 510 . 52 PHE HZ H 6.79 . 1 511 . 52 PHE CA C 58.0 . 1 512 . 52 PHE CB C 43.4 . 1 513 . 52 PHE CD1 C 132.0 . 1 514 . 52 PHE CD2 C 132.0 . 1 515 . 52 PHE CE1 C 130.0 . 1 516 . 52 PHE CE2 C 130.0 . 1 517 . 52 PHE CZ C 128.4 . 1 518 . 52 PHE N N 120.1 . 1 519 . 53 VAL H H 8.21 . 1 520 . 53 VAL HA H 5.13 . 1 521 . 53 VAL HB H 2.09 . 1 522 . 53 VAL HG1 H 0.83 . 2 523 . 53 VAL HG2 H 0.74 . 2 524 . 53 VAL CA C 61.1 . 1 525 . 53 VAL CB C 34.6 . 1 526 . 53 VAL CG1 C 22.3 . 2 527 . 53 VAL CG2 C 20.6 . 2 528 . 53 VAL N N 125.6 . 1 529 . 54 ILE H H 9.23 . 1 530 . 54 ILE HA H 5.10 . 1 531 . 54 ILE HB H 1.87 . 1 532 . 54 ILE HG12 H 2.01 . 2 533 . 54 ILE HG13 H 1.21 . 2 534 . 54 ILE HG2 H 0.91 . 1 535 . 54 ILE HD1 H 0.77 . 1 536 . 54 ILE CA C 60.4 . 1 537 . 54 ILE CB C 40.1 . 1 538 . 54 ILE CG1 C 27.8 . 1 539 . 54 ILE CG2 C 17.7 . 1 540 . 54 ILE CD1 C 14.0 . 1 541 . 54 ILE N N 126.7 . 1 542 . 55 SER H H 8.93 . 1 543 . 55 SER HA H 5.40 . 1 544 . 55 SER HB2 H 3.64 . 2 545 . 55 SER HB3 H 3.06 . 2 546 . 55 SER CA C 56.2 . 1 547 . 55 SER CB C 65.8 . 1 548 . 55 SER N N 117.4 . 1 549 . 56 ASP H H 8.44 . 1 550 . 56 ASP HA H 5.10 . 1 551 . 56 ASP HB2 H 3.26 . 2 552 . 56 ASP HB3 H 2.92 . 2 553 . 56 ASP CA C 54.5 . 1 554 . 56 ASP CB C 38.7 . 1 555 . 56 ASP N N 125.4 . 1 556 . 57 TRP HA H 4.21 . 1 557 . 57 TRP HB2 H 3.60 . 2 558 . 57 TRP HB3 H 3.51 . 2 559 . 57 TRP HD1 H 7.27 . 1 560 . 57 TRP HE1 H 10.3 . 1 561 . 57 TRP HE3 H 7.42 . 1 562 . 57 TRP HZ2 H 7.47 . 3 563 . 57 TRP HZ3 H 6.79 . 3 564 . 57 TRP HH2 H 7.28 . 1 565 . 57 TRP CA C 59.8 . 1 566 . 57 TRP CB C 30.6 . 1 567 . 57 TRP CD1 C 126.6 . 1 568 . 57 TRP CD2 C 126.6 . 1 569 . 57 TRP CE2 C 118.5 . 1 570 . 57 TRP CZ2 C 114.7 . 1 571 . 57 TRP CZ3 C 120.0 . 1 572 . 57 TRP CH2 C 124.2 . 1 573 . 57 TRP NE1 N 129.4 . 1 574 . 58 ASN H H 8.14 . 1 575 . 58 ASN HA H 5.12 . 1 576 . 58 ASN HB2 H 2.86 . 1 577 . 58 ASN HB3 H 2.86 . 1 578 . 58 ASN CA C 54.7 . 1 579 . 58 ASN N N 115.0 . 1 580 . 59 MET H H 7.36 . 1 581 . 59 MET HA H 4.80 . 1 582 . 59 MET HB2 H 2.20 . 2 583 . 59 MET HB3 H 2.07 . 2 584 . 59 MET CA C 53.8 . 1 585 . 59 MET CB C 34.3 . 1 586 . 59 MET N N 122.5 . 1 587 . 60 PRO HA H 4.42 . 1 588 . 60 PRO HB2 H 1.94 . 1 589 . 60 PRO HB3 H 1.94 . 1 590 . 60 PRO HG2 H 2.14 . 1 591 . 60 PRO HG3 H 2.14 . 1 592 . 60 PRO HD2 H 3.80 . 2 593 . 60 PRO HD3 H 3.64 . 2 594 . 60 PRO CA C 62.1 . 1 595 . 60 PRO CB C 32.7 . 1 596 . 60 PRO CG C 26.8 . 1 597 . 60 PRO CD C 50.2 . 1 598 . 61 ASN H H 8.62 . 1 599 . 61 ASN HA H 4.05 . 1 600 . 61 ASN HB2 H 3.28 . 2 601 . 61 ASN HB3 H 2.65 . 2 602 . 61 ASN HD21 H 7.91 . 2 603 . 61 ASN HD22 H 7.02 . 2 604 . 61 ASN CA C 59.0 . 1 605 . 61 ASN CB C 37.5 . 1 606 . 61 ASN N N 110.6 . 1 607 . 61 ASN ND2 N 115.1 . 1 608 . 62 MET H H 9.27 . 1 609 . 62 MET HA H 4.21 . 1 610 . 62 MET HB2 H 2.19 . 1 611 . 62 MET HB3 H 2.19 . 1 612 . 62 MET HE H 2.41 . 1 613 . 62 MET CA C 56.9 . 1 614 . 62 MET CB C 35.5 . 1 615 . 62 MET CG C 31.0 . 1 616 . 62 MET N N 121.7 . 1 617 . 63 ASP H H 8.60 . 1 618 . 63 ASP HA H 4.49 . 1 619 . 63 ASP HB2 H 3.72 . 2 620 . 63 ASP HB3 H 2.92 . 2 621 . 63 ASP CA C 53.0 . 1 622 . 63 ASP CB C 40.5 . 1 623 . 63 ASP N N 125.8 . 1 624 . 64 GLY H H 8.63 . 1 625 . 64 GLY HA2 H 3.99 . 2 626 . 64 GLY HA3 H 3.48 . 2 627 . 64 GLY CA C 47.2 . 1 628 . 64 GLY N N 102.1 . 1 629 . 65 LEU H H 7.56 . 1 630 . 65 LEU HA H 3.74 . 1 631 . 65 LEU HB2 H 1.49 . 2 632 . 65 LEU HB3 H 0.86 . 2 633 . 65 LEU HG H 1.16 . 1 634 . 65 LEU HD1 H 0.73 . 1 635 . 65 LEU HD2 H 0.73 . 1 636 . 65 LEU CA C 56.9 . 1 637 . 65 LEU CB C 40.5 . 1 638 . 65 LEU CG C 26.8 . 1 639 . 65 LEU CD1 C 24.3 . 1 640 . 65 LEU CD2 C 24.3 . 1 641 . 65 LEU N N 120.5 . 1 642 . 66 GLU H H 8.19 . 1 643 . 66 GLU HA H 3.84 . 1 644 . 66 GLU HB2 H 1.97 . 2 645 . 66 GLU HB3 H 1.86 . 2 646 . 66 GLU HG2 H 2.31 . 1 647 . 66 GLU HG3 H 2.31 . 1 648 . 66 GLU CA C 58.9 . 1 649 . 66 GLU CB C 28.9 . 1 650 . 66 GLU CG C 36.0 . 1 651 . 66 GLU N N 118.5 . 1 652 . 67 LEU H H 8.32 . 1 653 . 67 LEU HA H 4.09 . 1 654 . 67 LEU HB2 H 2.07 . 2 655 . 67 LEU HB3 H 1.15 . 2 656 . 67 LEU HG H 1.35 . 1 657 . 67 LEU HD1 H 0.78 . 2 658 . 67 LEU HD2 H 0.90 . 2 659 . 67 LEU CA C 58.6 . 1 660 . 67 LEU CB C 41.0 . 1 661 . 67 LEU CG C 26.7 . 1 662 . 67 LEU CD1 C 25.9 . 2 663 . 67 LEU CD2 C 22.4 . 2 664 . 67 LEU N N 122.4 . 1 665 . 68 LEU H H 8.20 . 1 666 . 68 LEU HA H 3.78 . 1 667 . 68 LEU HB2 H 2.11 . 2 668 . 68 LEU HB3 H 1.60 . 2 669 . 68 LEU HD1 H 0.83 . 2 670 . 68 LEU HD2 H 0.65 . 2 671 . 68 LEU CA C 58.3 . 1 672 . 68 LEU CB C 41.0 . 1 673 . 68 LEU CD1 C 27.5 . 2 674 . 68 LEU CD2 C 22.2 . 2 675 . 68 LEU N N 119.4 . 1 676 . 69 LYS H H 8.36 . 1 677 . 69 LYS HA H 3.80 . 1 678 . 69 LYS HB2 H 1.86 . 2 679 . 69 LYS HB3 H 1.77 . 2 680 . 69 LYS HG2 H 1.41 . 1 681 . 69 LYS HG3 H 1.41 . 1 682 . 69 LYS HD2 H 1.67 . 1 683 . 69 LYS HD3 H 1.67 . 1 684 . 69 LYS HE2 H 2.96 . 1 685 . 69 LYS HE3 H 2.96 . 1 686 . 69 LYS CA C 59.8 . 1 687 . 69 LYS CB C 32.0 . 1 688 . 69 LYS CG C 24.5 . 1 689 . 69 LYS CD C 29.0 . 1 690 . 69 LYS CE C 41.7 . 1 691 . 69 LYS N N 114.7 . 1 692 . 70 THR H H 8.00 . 1 693 . 70 THR HA H 3.81 . 1 694 . 70 THR HB H 4.35 . 1 695 . 70 THR HG2 H 1.20 . 1 696 . 70 THR CA C 67.1 . 1 697 . 70 THR CB C 68.1 . 1 698 . 70 THR CG2 C 22.2 . 1 699 . 70 THR N N 116.0 . 1 700 . 71 ILE H H 8.45 . 1 701 . 71 ILE HA H 3.39 . 1 702 . 71 ILE HB H 1.88 . 1 703 . 71 ILE HG12 H 1.68 . 2 704 . 71 ILE HG13 H 0.81 . 2 705 . 71 ILE HG2 H 0.74 . 1 706 . 71 ILE HD1 H 0.56 . 1 707 . 71 ILE CA C 65.7 . 1 708 . 71 ILE CB C 38.6 . 1 709 . 71 ILE CG1 C 29.3 . 1 710 . 71 ILE CG2 C 17.1 . 1 711 . 71 ILE CD1 C 14.5 . 1 712 . 71 ILE N N 122.2 . 1 713 . 72 ARG H H 8.12 . 1 714 . 72 ARG HA H 4.01 . 1 715 . 72 ARG HB2 H 1.98 . 2 716 . 72 ARG HB3 H 1.64 . 2 717 . 72 ARG CA C 57.0 . 1 718 . 72 ARG CB C 29.0 . 1 719 . 72 ARG N N 112.0 . 1 720 . 73 ALA H H 7.28 . 1 721 . 73 ALA HA H 4.34 . 1 722 . 73 ALA HB H 1.42 . 1 723 . 73 ALA CA C 51.7 . 1 724 . 73 ALA CB C 19.1 . 1 725 . 73 ALA N N 117.6 . 1 726 . 74 ASP H H 7.40 . 1 727 . 74 ASP HA H 4.58 . 1 728 . 74 ASP HB2 H 2.90 . 1 729 . 74 ASP HB3 H 2.60 . 1 730 . 74 ASP CA C 53.8 . 1 731 . 74 ASP CB C 43.8 . 1 732 . 74 ASP N N 120.4 . 1 733 . 75 GLY H H 8.74 . 1 734 . 75 GLY HA2 H 3.90 . 1 735 . 75 GLY HA3 H 3.90 . 1 736 . 75 GLY CA C 47.2 . 1 737 . 75 GLY N N 111.1 . 1 738 . 76 ALA H H 8.57 . 1 739 . 76 ALA HA H 4.50 . 1 740 . 76 ALA HB H 1.49 . 1 741 . 76 ALA CA C 53.3 . 1 742 . 76 ALA CB C 19.4 . 1 743 . 76 ALA N N 120.5 . 1 744 . 77 MET H H 8.48 . 1 745 . 77 MET HA H 4.59 . 1 746 . 77 MET HB2 H 2.23 . 2 747 . 77 MET HB3 H 2.13 . 2 748 . 77 MET HG2 H 2.62 . 2 749 . 77 MET HG3 H 2.39 . 2 750 . 77 MET CA C 55.8 . 1 751 . 77 MET CB C 34.2 . 1 752 . 77 MET CG C 34.0 . 1 753 . 77 MET N N 114.7 . 1 754 . 78 SER H H 7.45 . 1 755 . 78 SER HA H 4.38 . 1 756 . 78 SER HB2 H 4.07 . 2 757 . 78 SER HB3 H 3.98 . 2 758 . 78 SER CA C 61.8 . 1 759 . 78 SER CB C 63.3 . 1 760 . 78 SER N N 111.3 . 1 761 . 79 ALA H H 8.20 . 1 762 . 79 ALA HA H 4.45 . 1 763 . 79 ALA HB H 1.33 . 1 764 . 79 ALA CA C 50.9 . 1 765 . 79 ALA CB C 18.7 . 1 766 . 79 ALA N N 121.8 . 1 767 . 80 LEU H H 7.83 . 1 768 . 80 LEU HA H 4.16 . 1 769 . 80 LEU HB2 H 1.54 . 2 770 . 80 LEU HB3 H 1.29 . 2 771 . 80 LEU HG H 1.54 . 1 772 . 80 LEU HD1 H 0.71 . 1 773 . 80 LEU HD2 H 0.71 . 1 774 . 80 LEU CA C 53.6 . 1 775 . 80 LEU CB C 42.8 . 1 776 . 80 LEU CG C 26.5 . 1 777 . 80 LEU CD1 C 25.0 . 1 778 . 80 LEU CD2 C 25.0 . 1 779 . 80 LEU N N 122.6 . 1 780 . 81 PRO HA H 4.01 . 1 781 . 81 PRO HB2 H 1.39 . 2 782 . 81 PRO HB3 H 0.42 . 2 783 . 81 PRO HG2 H 1.86 . 2 784 . 81 PRO HG3 H 1.68 . 2 785 . 81 PRO HD2 H 3.88 . 2 786 . 81 PRO HD3 H 3.56 . 2 787 . 81 PRO CA C 62.3 . 1 788 . 81 PRO CB C 31.4 . 1 789 . 81 PRO CG C 27.8 . 1 790 . 81 PRO CD C 51.1 . 1 791 . 82 VAL H H 7.68 . 1 792 . 82 VAL HA H 4.79 . 1 793 . 82 VAL HB H 1.68 . 1 794 . 82 VAL HG1 H 0.68 . 1 795 . 82 VAL HG2 H 0.68 . 1 796 . 82 VAL CA C 60.2 . 1 797 . 82 VAL CB C 35.9 . 1 798 . 82 VAL CG1 C 20.5 . 1 799 . 82 VAL CG2 C 20.5 . 1 800 . 82 VAL N N 117.5 . 1 801 . 83 LEU H H 9.10 . 1 802 . 83 LEU HA H 4.55 . 1 803 . 83 LEU HB2 H 2.11 . 2 804 . 83 LEU HB3 H 1.15 . 2 805 . 83 LEU HG H 1.31 . 1 806 . 83 LEU HD1 H 0.51 . 1 807 . 83 LEU HD2 H 0.51 . 1 808 . 83 LEU CA C 52.5 . 1 809 . 83 LEU CB C 45.4 . 1 810 . 83 LEU CG C 26.7 . 1 811 . 83 LEU CD1 C 25.8 . 1 812 . 83 LEU CD2 C 25.8 . 1 813 . 83 LEU N N 129.0 . 1 814 . 84 MET H H 8.09 . 1 815 . 84 MET HA H 5.53 . 1 816 . 84 MET HB2 H 2.14 . 2 817 . 84 MET HB3 H 2.06 . 2 818 . 84 MET HG2 H 2.45 . 1 819 . 84 MET HG3 H 2.45 . 1 820 . 84 MET CA C 52.7 . 1 821 . 84 MET CB C 31.9 . 1 822 . 84 MET CG C 31.9 . 1 823 . 84 MET N N 123.4 . 1 824 . 85 VAL H H 9.11 . 1 825 . 85 VAL HA H 4.99 . 1 826 . 85 VAL HB H 2.14 . 1 827 . 85 VAL HG1 H 1.11 . 2 828 . 85 VAL HG2 H 0.82 . 2 829 . 85 VAL CA C 60.9 . 1 830 . 85 VAL CB C 33.0 . 1 831 . 85 VAL CG1 C 22.7 . 2 832 . 85 VAL CG2 C 20.3 . 2 833 . 85 VAL N N 122.4 . 1 834 . 86 THR H H 8.50 . 1 835 . 86 THR HA H 5.10 . 1 836 . 86 THR HB H 4.07 . 1 837 . 86 THR HG2 H 0.92 . 1 838 . 86 THR CA C 58.6 . 1 839 . 86 THR CB C 70.4 . 1 840 . 86 THR CG2 C 19.4 . 1 841 . 86 THR N N 115.2 . 1 842 . 87 ALA H H 8.81 . 1 843 . 87 ALA HA H 4.63 . 1 844 . 87 ALA HB H 1.53 . 1 845 . 87 ALA CA C 52.5 . 1 846 . 87 ALA CB C 19.7 . 1 847 . 87 ALA N N 124.8 . 1 848 . 88 GLU H H 7.97 . 1 849 . 88 GLU HA H 4.32 . 1 850 . 88 GLU HB2 H 1.90 . 1 851 . 88 GLU HB3 H 1.90 . 1 852 . 88 GLU HG2 H 2.10 . 1 853 . 88 GLU HG3 H 2.10 . 1 854 . 88 GLU CA C 56.0 . 1 855 . 88 GLU CB C 29.2 . 1 856 . 88 GLU N N 115.3 . 1 857 . 89 ALA HA H 4.21 . 1 858 . 89 ALA HB H 1.28 . 1 859 . 89 ALA CA C 51.3 . 1 860 . 89 ALA CB C 17.4 . 1 861 . 90 LYS H H 7.38 . 1 862 . 90 LYS HA H 4.40 . 1 863 . 90 LYS HB2 H 1.78 . 2 864 . 90 LYS HB3 H 1.55 . 2 865 . 90 LYS HG2 H 1.30 . 1 866 . 90 LYS HG3 H 1.30 . 1 867 . 90 LYS HD2 H 1.60 . 1 868 . 90 LYS HD3 H 1.60 . 1 869 . 90 LYS HE2 H 2.90 . 1 870 . 90 LYS HE3 H 2.90 . 1 871 . 90 LYS CA C 55.1 . 1 872 . 90 LYS CB C 33.0 . 1 873 . 90 LYS CG C 24.8 . 1 874 . 90 LYS CD C 28.9 . 1 875 . 90 LYS CE C 41.7 . 1 876 . 90 LYS N N 119.8 . 1 877 . 91 LYS HA H 3.76 . 1 878 . 91 LYS HB2 H 1.87 . 2 879 . 91 LYS HB3 H 1.77 . 2 880 . 91 LYS HG2 H 1.40 . 1 881 . 91 LYS HG3 H 1.40 . 1 882 . 91 LYS HD2 H 1.66 . 1 883 . 91 LYS HD3 H 1.66 . 1 884 . 91 LYS HE2 H 2.92 . 1 885 . 91 LYS HE3 H 2.92 . 1 886 . 91 LYS CA C 59.8 . 1 887 . 91 LYS CB C 31.9 . 1 888 . 91 LYS CG C 24.5 . 1 889 . 91 LYS CD C 29.0 . 1 890 . 91 LYS CE C 41.8 . 1 891 . 92 GLU H H 9.59 . 1 892 . 92 GLU HA H 3.95 . 1 893 . 92 GLU HB2 H 1.93 . 1 894 . 92 GLU HB3 H 1.93 . 1 895 . 92 GLU HG2 H 2.27 . 1 896 . 92 GLU HG3 H 2.27 . 1 897 . 92 GLU CA C 59.8 . 1 898 . 92 GLU CB C 28.5 . 1 899 . 92 GLU CG C 36.3 . 1 900 . 92 GLU N N 114.9 . 1 901 . 93 ASN H H 7.23 . 1 902 . 93 ASN HA H 4.56 . 1 903 . 93 ASN HB2 H 2.56 . 2 904 . 93 ASN HB3 H 2.05 . 2 905 . 93 ASN HD21 H 7.30 . 2 906 . 93 ASN HD22 H 6.85 . 2 907 . 93 ASN CA C 54.7 . 1 908 . 93 ASN CB C 36.9 . 1 909 . 93 ASN N N 116.7 . 1 910 . 93 ASN ND2 N 109.4 . 1 911 . 94 ILE H H 7.44 . 1 912 . 94 ILE HA H 3.17 . 1 913 . 94 ILE HB H 1.67 . 1 914 . 94 ILE HG12 H 1.00 . 2 915 . 94 ILE HG13 H 0.26 . 2 916 . 94 ILE HG2 H 0.55 . 1 917 . 94 ILE HD1 H 0.38 . 1 918 . 94 ILE CA C 64.8 . 1 919 . 94 ILE CB C 37.3 . 1 920 . 94 ILE CG1 C 27.8 . 1 921 . 94 ILE CG2 C 16.7 . 1 922 . 94 ILE CD1 C 12.3 . 1 923 . 94 ILE N N 120.3 . 1 924 . 95 ILE H H 7.96 . 1 925 . 95 ILE HA H 3.79 . 1 926 . 95 ILE HB H 1.67 . 1 927 . 95 ILE HG12 H 1.59 . 2 928 . 95 ILE HG13 H 1.17 . 2 929 . 95 ILE HG2 H 0.90 . 1 930 . 95 ILE HD1 H 0.81 . 1 931 . 95 ILE CA C 64.3 . 1 932 . 95 ILE CB C 37.6 . 1 933 . 95 ILE CG1 C 28.6 . 1 934 . 95 ILE CG2 C 16.8 . 1 935 . 95 ILE CD1 C 12.8 . 1 936 . 95 ILE N N 118.3 . 1 937 . 96 ALA H H 7.64 . 1 938 . 96 ALA HA H 4.21 . 1 939 . 96 ALA HB H 1.72 . 1 940 . 96 ALA CA C 55.0 . 1 941 . 96 ALA CB C 18.1 . 1 942 . 96 ALA N N 120.5 . 1 943 . 97 ALA H H 8.46 . 1 944 . 97 ALA HA H 3.92 . 1 945 . 97 ALA HB H 1.53 . 1 946 . 97 ALA CA C 54.8 . 1 947 . 97 ALA CB C 16.9 . 1 948 . 97 ALA N N 117.9 . 1 949 . 98 ALA H H 8.16 . 1 950 . 98 ALA HA H 4.21 . 1 951 . 98 ALA HB H 1.59 . 1 952 . 98 ALA CA C 55.3 . 1 953 . 98 ALA CB C 17.7 . 1 954 . 98 ALA N N 120.5 . 1 955 . 99 GLN H H 8.70 . 1 956 . 99 GLN HA H 4.04 . 1 957 . 99 GLN HB2 H 2.19 . 2 958 . 99 GLN HB3 H 2.10 . 2 959 . 99 GLN HG2 H 2.63 . 2 960 . 99 GLN HG3 H 2.44 . 2 961 . 99 GLN HE21 H 7.36 . 2 962 . 99 GLN HE22 H 6.77 . 2 963 . 99 GLN CA C 58.5 . 1 964 . 99 GLN CB C 28.1 . 1 965 . 99 GLN CG C 34.2 . 1 966 . 99 GLN N N 117.5 . 1 967 . 99 GLN NE2 N 109.8 . 1 968 . 100 ALA H H 7.56 . 1 969 . 100 ALA HA H 4.35 . 1 970 . 100 ALA HB H 1.43 . 1 971 . 100 ALA CA C 51.7 . 1 972 . 100 ALA CB C 19.1 . 1 973 . 100 ALA N N 117.0 . 1 974 . 101 GLY H H 7.59 . 1 975 . 101 GLY HA2 H 4.22 . 2 976 . 101 GLY HA3 H 3.89 . 2 977 . 101 GLY CA C 45.6 . 1 978 . 101 GLY N N 101.1 . 1 979 . 102 ALA H H 8.72 . 1 980 . 102 ALA HA H 3.94 . 1 981 . 102 ALA HB H 1.37 . 1 982 . 102 ALA CA C 53.5 . 1 983 . 102 ALA CB C 18.4 . 1 984 . 102 ALA N N 123.6 . 1 985 . 103 SER H H 9.04 . 1 986 . 103 SER HA H 4.42 . 1 987 . 103 SER HB2 H 3.98 . 2 988 . 103 SER HB3 H 3.27 . 2 989 . 103 SER CA C 60.0 . 1 990 . 103 SER CB C 61.0 . 1 991 . 103 SER N N 116.6 . 1 992 . 104 GLY H H 7.64 . 1 993 . 104 GLY HA2 H 4.14 . 2 994 . 104 GLY HA3 H 3.85 . 2 995 . 104 GLY CA C 44.7 . 1 996 . 104 GLY N N 101.3 . 1 997 . 105 TYR H H 8.44 . 1 998 . 105 TYR HA H 5.88 . 1 999 . 105 TYR HB2 H 2.81 . 1 1000 . 105 TYR HB3 H 2.81 . 1 1001 . 105 TYR HD1 H 6.78 . 1 1002 . 105 TYR HD2 H 6.78 . 1 1003 . 105 TYR HE1 H 6.60 . 1 1004 . 105 TYR HE2 H 6.60 . 1 1005 . 105 TYR CA C 56.0 . 1 1006 . 105 TYR CB C 41.3 . 1 1007 . 105 TYR CD1 C 133.0 . 1 1008 . 105 TYR CD2 C 133.0 . 1 1009 . 105 TYR CE1 C 117.3 . 1 1010 . 105 TYR CE2 C 117.3 . 1 1011 . 105 TYR N N 117.9 . 1 1012 . 106 VAL H H 8.95 . 1 1013 . 106 VAL HA H 4.29 . 1 1014 . 106 VAL HB H 1.49 . 1 1015 . 106 VAL HG1 H 0.48 . 2 1016 . 106 VAL HG2 H 0.40 . 2 1017 . 106 VAL CA C 59.4 . 1 1018 . 106 VAL CB C 35.2 . 1 1019 . 106 VAL CG1 C 21.6 . 2 1020 . 106 VAL CG2 C 20.6 . 2 1021 . 106 VAL N N 118.9 . 1 1022 . 107 VAL H H 8.11 . 1 1023 . 107 VAL HA H 4.99 . 1 1024 . 107 VAL HB H 1.86 . 1 1025 . 107 VAL HG1 H 0.82 . 1 1026 . 107 VAL HG2 H 0.82 . 1 1027 . 107 VAL CA C 60.4 . 1 1028 . 107 VAL CB C 36.3 . 1 1029 . 107 VAL CG1 C 22.6 . 1 1030 . 107 VAL CG2 C 22.6 . 1 1031 . 107 VAL N N 125.1 . 1 1032 . 108 LYS H H 8.45 . 1 1033 . 108 LYS HA H 4.64 . 1 1034 . 108 LYS HB2 H 1.72 . 1 1035 . 108 LYS HB3 H 1.72 . 1 1036 . 108 LYS HG2 H 1.33 . 1 1037 . 108 LYS HG3 H 1.33 . 1 1038 . 108 LYS HD2 H 1.62 . 1 1039 . 108 LYS HD3 H 1.62 . 1 1040 . 108 LYS HE2 H 2.93 . 1 1041 . 108 LYS HE3 H 2.93 . 1 1042 . 108 LYS CA C 53.4 . 1 1043 . 108 LYS CB C 32.9 . 1 1044 . 108 LYS CG C 24.4 . 1 1045 . 108 LYS CD C 29.4 . 1 1046 . 108 LYS CE C 41.2 . 1 1047 . 108 LYS N N 122.5 . 1 1048 . 109 PRO HA H 4.39 . 1 1049 . 109 PRO HB2 H 2.27 . 2 1050 . 109 PRO HB3 H 1.99 . 2 1051 . 109 PRO HG2 H 1.93 . 1 1052 . 109 PRO HG3 H 1.93 . 1 1053 . 109 PRO HD2 H 3.67 . 2 1054 . 109 PRO HD3 H 3.48 . 2 1055 . 109 PRO CA C 62.2 . 1 1056 . 109 PRO CB C 34.4 . 1 1057 . 109 PRO CG C 24.4 . 1 1058 . 109 PRO CD C 50.0 . 1 1059 . 110 PHE H H 7.75 . 1 1060 . 110 PHE HA H 5.50 . 1 1061 . 110 PHE HB2 H 3.39 . 2 1062 . 110 PHE HB3 H 2.99 . 2 1063 . 110 PHE HD1 H 7.09 . 1 1064 . 110 PHE HD2 H 7.09 . 1 1065 . 110 PHE HE1 H 7.08 . 1 1066 . 110 PHE HE2 H 7.08 . 1 1067 . 110 PHE HZ H 7.00 . 1 1068 . 110 PHE CA C 53.6 . 1 1069 . 110 PHE CB C 40.6 . 1 1070 . 110 PHE CD1 C 133.0 . 1 1071 . 110 PHE CD2 C 133.0 . 1 1072 . 110 PHE CE1 C 130.3 . 1 1073 . 110 PHE CE2 C 130.3 . 1 1074 . 110 PHE CZ C 127.9 . 1 1075 . 110 PHE N N 114.5 . 1 1076 . 111 THR H H 7.86 . 1 1077 . 111 THR HA H 4.54 . 1 1078 . 111 THR HB H 4.80 . 1 1079 . 111 THR HG2 H 1.34 . 1 1080 . 111 THR CA C 59.3 . 1 1081 . 111 THR CB C 71.7 . 1 1082 . 111 THR CG2 C 21.6 . 1 1083 . 111 THR N N 107.3 . 1 1084 . 112 ALA H H 9.20 . 1 1085 . 112 ALA HA H 3.97 . 1 1086 . 112 ALA HB H 1.50 . 1 1087 . 112 ALA CA C 55.8 . 1 1088 . 112 ALA CB C 17.1 . 1 1089 . 112 ALA N N 121.7 . 1 1090 . 113 ALA H H 8.21 . 1 1091 . 113 ALA HA H 4.25 . 1 1092 . 113 ALA HB H 1.47 . 1 1093 . 113 ALA CA C 54.9 . 1 1094 . 113 ALA CB C 18.0 . 1 1095 . 113 ALA N N 117.1 . 1 1096 . 114 THR H H 7.81 . 1 1097 . 114 THR HA H 4.06 . 1 1098 . 114 THR HB H 4.30 . 1 1099 . 114 THR HG2 H 1.22 . 1 1100 . 114 THR CA C 65.8 . 1 1101 . 114 THR CB C 68.3 . 1 1102 . 114 THR CG2 C 22.3 . 1 1103 . 114 THR N N 115.5 . 1 1104 . 115 LEU H H 8.24 . 1 1105 . 115 LEU HA H 3.65 . 1 1106 . 115 LEU HB2 H 2.07 . 2 1107 . 115 LEU HB3 H 1.43 . 2 1108 . 115 LEU HG H 1.33 . 1 1109 . 115 LEU HD1 H 0.74 . 2 1110 . 115 LEU HD2 H 0.45 . 2 1111 . 115 LEU CA C 58.1 . 1 1112 . 115 LEU CB C 40.9 . 1 1113 . 115 LEU CG C 26.7 . 1 1114 . 115 LEU CD2 C 21.2 . 1 1115 . 115 LEU N N 120.7 . 1 1116 . 116 GLU H H 8.89 . 1 1117 . 116 GLU HA H 3.64 . 1 1118 . 116 GLU HB2 H 2.25 . 1 1119 . 116 GLU HB3 H 2.25 . 1 1120 . 116 GLU HG2 H 2.41 . 1 1121 . 116 GLU HG3 H 2.21 . 2 1122 . 116 GLU CA C 59.9 . 1 1123 . 116 GLU CB C 29.6 . 1 1124 . 116 GLU CG C 35.5 . 1 1125 . 116 GLU N N 117.7 . 1 1126 . 117 GLU H H 7.66 . 1 1127 . 117 GLU HA H 4.07 . 1 1128 . 117 GLU HB2 H 2.20 . 1 1129 . 117 GLU HB3 H 2.20 . 1 1130 . 117 GLU HG2 H 2.46 . 1 1131 . 117 GLU HG3 H 2.46 . 1 1132 . 117 GLU CA C 59.4 . 1 1133 . 117 GLU CB C 29.3 . 1 1134 . 117 GLU CG C 36.0 . 1 1135 . 117 GLU N N 116.6 . 1 1136 . 118 LYS H H 7.84 . 1 1137 . 118 LYS HA H 3.95 . 1 1138 . 118 LYS HB2 H 1.92 . 2 1139 . 118 LYS HB3 H 1.42 . 2 1140 . 118 LYS HG2 H 1.09 . 1 1141 . 118 LYS HG3 H 1.09 . 1 1142 . 118 LYS HD2 H 1.61 . 1 1143 . 118 LYS HD3 H 1.61 . 1 1144 . 118 LYS HE2 H 2.87 . 1 1145 . 118 LYS HE3 H 2.87 . 1 1146 . 118 LYS CA C 57.5 . 1 1147 . 118 LYS CB C 31.5 . 1 1148 . 118 LYS CG C 24.5 . 1 1149 . 118 LYS CD C 27.5 . 1 1150 . 118 LYS CE C 41.6 . 1 1151 . 118 LYS N N 115.6 . 1 1152 . 119 LEU H H 8.55 . 1 1153 . 119 LEU HA H 3.41 . 1 1154 . 119 LEU HB2 H 1.64 . 2 1155 . 119 LEU HB3 H 0.83 . 2 1156 . 119 LEU HG H 1.45 . 1 1157 . 119 LEU HD1 H 0.38 . 2 1158 . 119 LEU HD2 H 0.08 . 2 1159 . 119 LEU CA C 57.8 . 1 1160 . 119 LEU CB C 40.4 . 1 1161 . 119 LEU CG C 26.1 . 1 1162 . 119 LEU CD1 C 25.7 . 1 1163 . 119 LEU CD2 C 25.7 . 1 1164 . 119 LEU N N 116.8 . 1 1165 . 120 ASN H H 8.58 . 1 1166 . 120 ASN HA H 4.56 . 1 1167 . 120 ASN HB2 H 3.03 . 2 1168 . 120 ASN HB3 H 2.86 . 2 1169 . 120 ASN HD21 H 7.53 . 2 1170 . 120 ASN HD22 H 6.86 . 2 1171 . 120 ASN CA C 56.0 . 1 1172 . 120 ASN CB C 37.3 . 1 1173 . 120 ASN N N 114.5 . 1 1174 . 120 ASN ND2 N 110.1 . 1 1175 . 121 LYS H H 7.78 . 1 1176 . 121 LYS HA H 4.15 . 1 1177 . 121 LYS HB2 H 1.95 . 1 1178 . 121 LYS HB3 H 1.95 . 1 1179 . 121 LYS HD2 H 1.60 . 1 1180 . 121 LYS HD3 H 1.60 . 1 1181 . 121 LYS HE2 H 2.97 . 1 1182 . 121 LYS HE3 H 2.97 . 1 1183 . 121 LYS CA C 58.7 . 1 1184 . 121 LYS CB C 32.0 . 1 1185 . 121 LYS CG C 25.1 . 1 1186 . 121 LYS CD C 28.3 . 1 1187 . 121 LYS CE C 41.8 . 1 1188 . 121 LYS N N 117.9 . 1 1189 . 122 ILE H H 7.51 . 1 1190 . 122 ILE HA H 3.73 . 1 1191 . 122 ILE HB H 1.89 . 1 1192 . 122 ILE HG12 H 1.87 . 2 1193 . 122 ILE HG13 H 0.86 . 2 1194 . 122 ILE HG2 H 0.91 . 1 1195 . 122 ILE HD1 H 0.68 . 1 1196 . 122 ILE CA C 65.4 . 1 1197 . 122 ILE CB C 37.7 . 1 1198 . 122 ILE CG1 C 29.8 . 1 1199 . 122 ILE CG2 C 17.8 . 1 1200 . 122 ILE CD1 C 15.2 . 1 1201 . 122 ILE N N 120.5 . 1 1202 . 123 PHE H H 9.14 . 1 1203 . 123 PHE HA H 4.67 . 1 1204 . 123 PHE HB2 H 3.48 . 2 1205 . 123 PHE HB3 H 3.33 . 2 1206 . 123 PHE HD1 H 7.48 . 1 1207 . 123 PHE HD2 H 7.48 . 1 1208 . 123 PHE HE1 H 7.26 . 1 1209 . 123 PHE HE2 H 7.26 . 1 1210 . 123 PHE HZ H 6.69 . 1 1211 . 123 PHE CA C 58.7 . 1 1212 . 123 PHE CB C 37.2 . 1 1213 . 123 PHE CD1 C 130.8 . 1 1214 . 123 PHE CD2 C 130.8 . 1 1215 . 123 PHE CE1 C 130.8 . 1 1216 . 123 PHE CE2 C 130.8 . 1 1217 . 123 PHE CZ C 128.4 . 1 1218 . 123 PHE N N 117.3 . 1 1219 . 124 GLU H H 8.32 . 1 1220 . 124 GLU HA H 4.24 . 1 1221 . 124 GLU HB2 H 2.27 . 2 1222 . 124 GLU HB3 H 2.20 . 2 1223 . 124 GLU HG2 H 2.46 . 1 1224 . 124 GLU HG3 H 2.46 . 1 1225 . 124 GLU CA C 59.2 . 1 1226 . 124 GLU CB C 29.8 . 1 1227 . 124 GLU CG C 36.0 . 1 1228 . 124 GLU N N 116.5 . 1 1229 . 125 LYS H H 7.75 . 1 1230 . 125 LYS HA H 4.18 . 1 1231 . 125 LYS HB2 H 2.07 . 2 1232 . 125 LYS HB3 H 1.91 . 2 1233 . 125 LYS HG2 H 1.65 . 1 1234 . 125 LYS HG3 H 1.65 . 1 1235 . 125 LYS HD2 H 1.74 . 1 1236 . 125 LYS HD3 H 1.74 . 1 1237 . 125 LYS HE2 H 3.03 . 1 1238 . 125 LYS HE3 H 3.03 . 1 1239 . 125 LYS CA C 58.4 . 1 1240 . 125 LYS CB C 32.2 . 1 1241 . 125 LYS CG C 25.0 . 1 1242 . 125 LYS CD C 28.6 . 1 1243 . 125 LYS CE C 41.8 . 1 1244 . 125 LYS N N 118.7 . 1 1245 . 126 LEU H H 7.96 . 1 1246 . 126 LEU HA H 4.42 . 1 1247 . 126 LEU HB2 H 1.83 . 2 1248 . 126 LEU HB3 H 1.76 . 2 1249 . 126 LEU HG H 1.93 . 1 1250 . 126 LEU HD1 H 0.93 . 1 1251 . 126 LEU HD2 H 0.93 . 1 1252 . 126 LEU CA C 54.6 . 1 1253 . 126 LEU CB C 42.5 . 1 1254 . 126 LEU CG C 27.0 . 1 1255 . 126 LEU CD1 C 22.0 . 1 1256 . 126 LEU CD2 C 22.0 . 1 1257 . 126 LEU N N 115.1 . 1 1258 . 127 GLY H H 7.97 . 1 1259 . 127 GLY HA2 H 4.01 . 1 1260 . 127 GLY HA3 H 4.01 . 1 1261 . 127 GLY CA C 46.5 . 1 1262 . 127 GLY N N 108.8 . 1 1263 . 128 MET H H 8.25 . 1 1264 . 128 MET HA H 4.21 . 1 1265 . 128 MET HB2 H 2.18 . 2 1266 . 128 MET HB3 H 1.85 . 2 1267 . 128 MET HG2 H 2.60 . 2 1268 . 128 MET HG3 H 2.44 . 2 1269 . 128 MET CA C 57.0 . 1 1270 . 128 MET CB C 35.5 . 1 1271 . 128 MET CG C 32.4 . 1 1272 . 128 MET N N 123.1 . 1 stop_ save_