data_4472 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N signal assignments for BeFx-activated CheY from E. coli ; _BMRB_accession_number 4472 _BMRB_flat_file_name bmr4472.str _Entry_type original _Submission_date 1999-12-03 _Accession_date 1999-12-03 _Entry_origination author _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 Cho Ho S . 2 Lee Seok-Yong . . 3 Yan Dalai . . 4 Pan Xiaoyu . . 5 Parkinson John S . 6 Kustu Sydney . . 7 Wemmer David E . 8 Pelton Jeffrey G . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 658 "13C chemical shifts" 405 "15N chemical shifts" 123 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-12-15 original author . stop_ _Original_release_date 2000-12-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; 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 _CAS_abstract_code . _MEDLINE_UI_code 20198307 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cho Ho S . 2 Lee Seok-Yong . . 3 Yan Dalai . . 4 Pan Xiaoyu . . 5 Parkinson John S . 6 Kustu Sydney . . 7 Wemmer David E . 8 Pelton Jeffrey G . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume 297 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 543 _Page_last 551 _Year 2000 _Details . loop_ _Keyword BeFx CheY 'response regulator' stop_ save_ ################################## # Molecular system description # ################################## save_system_CheY _Saveframe_category molecular_system _Mol_system_name 'BeFx-activated CheY from E. coli' _Abbreviation_common CheY _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CheY $CheY beryllofluoride $entity_BF2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'Chemotaxis response regulator' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CheY _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Chemotaxis protein Y' _Abbreviation_common CheY _Molecular_mass 14097 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 129 _Mol_residue_sequence ; MADKELKFLVVDDFSTMRRI VRNLLKELGFNNVEEAEDGV DALNKLQAGGYGFVISDWNM PNMDGLELLKTIRADGAMSA LPVLMVTAEAKKENIIAAAQ AGASGYVVKPFTAATLEEKL NKIFEKLGM ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 ASP 4 LYS 5 GLU 6 LEU 7 LYS 8 PHE 9 LEU 10 VAL 11 VAL 12 ASP 13 ASP 14 PHE 15 SER 16 THR 17 MET 18 ARG 19 ARG 20 ILE 21 VAL 22 ARG 23 ASN 24 LEU 25 LEU 26 LYS 27 GLU 28 LEU 29 GLY 30 PHE 31 ASN 32 ASN 33 VAL 34 GLU 35 GLU 36 ALA 37 GLU 38 ASP 39 GLY 40 VAL 41 ASP 42 ALA 43 LEU 44 ASN 45 LYS 46 LEU 47 GLN 48 ALA 49 GLY 50 GLY 51 TYR 52 GLY 53 PHE 54 VAL 55 ILE 56 SER 57 ASP 58 TRP 59 ASN 60 MET 61 PRO 62 ASN 63 MET 64 ASP 65 GLY 66 LEU 67 GLU 68 LEU 69 LEU 70 LYS 71 THR 72 ILE 73 ARG 74 ALA 75 ASP 76 GLY 77 ALA 78 MET 79 SER 80 ALA 81 LEU 82 PRO 83 VAL 84 LEU 85 MET 86 VAL 87 THR 88 ALA 89 GLU 90 ALA 91 LYS 92 LYS 93 GLU 94 ASN 95 ILE 96 ILE 97 ALA 98 ALA 99 ALA 100 GLN 101 ALA 102 GLY 103 ALA 104 SER 105 GLY 106 TYR 107 VAL 108 VAL 109 LYS 110 PRO 111 PHE 112 THR 113 ALA 114 ALA 115 THR 116 LEU 117 GLU 118 GLU 119 LYS 120 LEU 121 ASN 122 LYS 123 ILE 124 PHE 125 GLU 126 LYS 127 LEU 128 GLY 129 MET stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 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 1.39e-85 BMRB 2951 "che Y protein" 100.00 129 100.00 100.00 1.39e-85 BMRB 3440 "che Y protein" 99.22 129 99.22 100.00 1.69e-84 BMRB 4083 "E. coli CheY" 99.22 128 100.00 100.00 7.30e-85 PDB 1A0O "Chey-Binding Domain Of Chea In Complex With Chey" 99.22 128 100.00 100.00 7.30e-85 PDB 1AB5 "Structure Of Chey Mutant F14n, V21t" 96.90 125 98.40 98.40 1.57e-80 PDB 1AB6 "Structure Of Chey Mutant F14n, V86t" 96.90 125 98.40 98.40 1.57e-80 PDB 1BDJ "Complex Structure Of Hpt Domain And Chey" 99.22 128 100.00 100.00 7.30e-85 PDB 1C4W "1.9 A Structure Of A-Thiophosphonate Modified Chey D57c" 99.22 128 99.22 99.22 1.06e-83 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 3.59e-84 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 7.30e-85 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 1.69e-84 PDB 1D4Z "Crystal Structure Of Chey-95iv, A Hyperactive Chey Mutant" 99.22 128 99.22 100.00 1.45e-84 PDB 1DJM "Solution Structure Of Bef3-Activated Chey From Escherichia Coli" 100.00 129 100.00 100.00 1.39e-85 PDB 1E6K "Two-Component Signal Transduction System D12a Mutant Of Chey" 99.22 130 98.44 99.22 2.71e-83 PDB 1E6L "Two-Component Signal Transduction System D13a Mutant Of Chey" 98.45 127 99.21 99.21 4.99e-83 PDB 1E6M "Two-Component Signal Transduction System D57a Mutant Of Chey" 99.22 128 98.44 99.22 3.30e-83 PDB 1EAY "Chey-Binding (P2) Domain Of Chea In Complex With Chey From Escherichia Coli" 99.22 128 100.00 100.00 7.30e-85 PDB 1EHC "Structure Of Signal Transduction Protein Chey" 99.22 128 99.22 99.22 7.89e-84 PDB 1F4V "Crystal Structure Of Activated Chey Bound To The N-Terminus Of Flim" 99.22 128 100.00 100.00 7.30e-85 PDB 1FFG "Chey-binding Domain Of Chea In Complex With Chey At 2.1 A Resolution" 99.22 128 100.00 100.00 7.30e-85 PDB 1FFS "Chey-Binding Domain Of Chea In Complex With Chey From Crystals Soaked In Acetyl Phosphate" 99.22 128 100.00 100.00 7.30e-85 PDB 1FFW "Chey-Binding Domain Of Chea In Complex With Chey With A Bound Imido Diphosphate" 99.22 128 100.00 100.00 7.30e-85 PDB 1FQW "Crystal Structure Of Activated Chey" 99.22 128 100.00 100.00 7.30e-85 PDB 1JBE "1.08 A Structure Of Apo-Chey Reveals Meta-Active Conformation" 99.22 128 98.44 98.44 1.20e-82 PDB 1KMI "Crystal Structure Of An E.Coli Chemotaxis Protein, Chez" 100.00 129 100.00 100.00 1.39e-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 1.07e-84 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 6.27e-84 PDB 1YMU "Signal Transduction Protein Chey Mutant With Met 17 Replaced By Gly (M17g)" 99.22 130 98.44 99.22 3.63e-83 PDB 1ZDM "Crystal Structure Of Activated Chey Bound To Xe" 100.00 129 99.22 99.22 1.47e-84 PDB 2B1J "Crystal Structure Of Unphosphorylated Chey Bound To The N- Terminus Of Flim" 99.22 128 100.00 100.00 7.30e-85 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 3.19e-83 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 3.19e-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 97.67 99.22 5.09e-84 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 5.09e-84 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 5.09e-84 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 5.09e-84 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 5.09e-84 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 5.09e-84 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 5.09e-84 PDB 2ID7 "1.75 A Structure Of T87i Phosphono-Chey" 99.22 128 98.44 98.44 1.00e-82 PDB 2ID9 "1.85 A Structure Of T87i/y106w Phosphono-chey" 99.22 128 97.66 98.44 6.21e-82 PDB 2IDM "2.00 A Structure Of T87iY106W PHOSPHONO-Chey" 99.22 128 97.66 98.44 6.21e-82 PDB 2LP4 "Solution Structure Of P1-CheyP2 COMPLEX IN BACTERIAL CHEMOTAXIS" 99.22 128 100.00 100.00 7.30e-85 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 3.19e-83 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 3.19e-83 PDB 3CHY "Crystal Structure Of Escherichia Coli Chey Refined At 1.7- Angstrom Resolution" 99.22 128 100.00 100.00 7.30e-85 PDB 3F7N "Crystal Structure Of Chey Triple Mutant F14e, N59m, E89l Complexed With Bef3- And Mn2+" 99.22 128 97.66 97.66 7.82e-81 PDB 3FFT "Crystal Structure Of Chey Double Mutant F14e, E89r Complexed With Bef3- And Mn2+" 99.22 128 98.44 98.44 1.23e-82 PDB 3FFW "Crystal Structure Of Chey Triple Mutant F14q, N59k, E89y Complexed With Bef3- And Mn2+" 99.22 128 97.66 97.66 1.87e-81 PDB 3FFX "Crystal Structure Of Chey Triple Mutant F14e, N59r, E89h Complexed With Bef3- And Mn2+" 99.22 128 97.66 97.66 6.78e-82 PDB 3FGZ "Crystal Structure Of Chey Triple Mutant F14e, N59m, E89r Complexed With Bef3- And Mn2+" 99.22 128 97.66 97.66 2.40e-81 PDB 3MYY "Structure Of E. Coli Chey Mutant A113p Bound To Beryllium Fluoride" 99.22 128 99.22 99.22 5.44e-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 5.99e-85 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 5.37e-85 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 3.40e-85 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 1.06e-84 PDB 3OO0 "Structure Of Apo Chey A113p" 100.00 129 99.22 99.22 7.54e-85 PDB 3OO1 "Structure Of E. Coli Chey Mutant A113p In The Absence Of Sulfate" 100.00 129 99.22 99.22 7.54e-85 PDB 3RVJ "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89q" 100.00 132 98.45 100.00 1.19e-84 PDB 3RVK "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89q" 100.00 132 98.45 100.00 1.19e-84 PDB 3RVL "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89r" 100.00 132 98.45 99.22 3.25e-84 PDB 3RVM "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d And E89r" 100.00 132 98.45 99.22 3.25e-84 PDB 3RVN "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89y" 100.00 132 98.45 99.22 5.62e-84 PDB 3RVO "Structure Of Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89y" 100.00 132 98.45 99.22 5.62e-84 PDB 3RVP "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89k" 100.00 132 98.45 100.00 2.64e-84 PDB 3RVQ "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89k" 100.00 132 98.45 100.00 2.64e-84 PDB 3RVR "Structure Of The Cheyn59dE89R MOLYBDATE COMPLEX" 100.00 132 98.45 99.22 3.25e-84 PDB 3RVS "Structure Of The Cheyn59dE89R TUNGSTATE COMPLEX" 100.00 132 98.45 99.22 3.25e-84 PDB 5CHY "Structure Of Chemotaxis Protein Chey" 99.22 128 99.22 100.00 8.06e-84 PDB 6CHY "Structure Of Chemotaxis Protein Chey" 99.22 128 98.44 99.22 6.70e-83 DBJ BAA15698 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli str. K12 substr. W3110]" 100.00 129 100.00 100.00 1.39e-85 DBJ BAB36015 "chemotaxis protein CheY [Escherichia coli O157:H7 str. Sakai]" 100.00 129 100.00 100.00 1.39e-85 DBJ BAG77641 "chemotactic response regulator CheY [Escherichia coli SE11]" 100.00 129 100.00 100.00 1.39e-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 1.39e-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 1.39e-85 EMBL CAD05667 "chemotaxis protein CheY [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 129 97.67 99.22 5.09e-84 EMBL CAP76371 "chemotaxis protein cheY [Escherichia coli LF82]" 100.00 129 100.00 100.00 1.39e-85 EMBL CAQ32359 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli BL21(DE3)]" 100.00 129 100.00 100.00 1.39e-85 EMBL CAQ98822 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli IAI1]" 100.00 129 100.00 100.00 1.39e-85 EMBL CAR03242 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli S88]" 100.00 129 99.22 100.00 4.27e-85 GB AAA23570 "cheY protein [Escherichia coli]" 100.00 129 99.22 99.22 7.54e-85 GB AAA23577 "CheY [Escherichia coli]" 100.00 129 100.00 100.00 1.39e-85 GB AAA27037 "CheY [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 129 97.67 99.22 5.09e-84 GB AAC74952 "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli str. K-12 substr. MG1655]" 100.00 129 100.00 100.00 1.39e-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 1.39e-85 PIR AH0745 "chemotaxis protein CheY [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 129 97.67 99.22 5.09e-84 REF NP_310619 "chemotaxis regulatory protein CheY [Escherichia coli O157:H7 str. Sakai]" 100.00 129 100.00 100.00 1.39e-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 1.39e-85 REF NP_456482 "chemotaxis protein CheY [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 129 97.67 99.22 5.09e-84 REF NP_460873 "chemotaxis regulatory protein CheY [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 129 97.67 99.22 5.09e-84 REF NP_707777 "chemotaxis regulatory protein CheY [Shigella flexneri 2a str. 301]" 100.00 129 100.00 100.00 1.39e-85 SP P0A2D5 "RecName: Full=Chemotaxis protein CheY" 100.00 129 97.67 99.22 5.09e-84 SP P0A2D6 "RecName: Full=Chemotaxis protein CheY" 100.00 129 97.67 99.22 5.09e-84 SP P0AE67 "RecName: Full=Chemotaxis protein CheY" 100.00 129 100.00 100.00 1.39e-85 SP P0AE68 "RecName: Full=Chemotaxis protein CheY" 100.00 129 100.00 100.00 1.39e-85 SP P0AE69 "RecName: Full=Chemotaxis protein CheY" 100.00 129 100.00 100.00 1.39e-85 stop_ save_ ############# # Ligands # ############# save_BF2 _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'BERYLLIUM DIFLUORIDE' _BMRB_code BF2 _PDB_code BF2 _Molecular_mass 47.009 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons BE BE BE . 0 . ? F1 F1 F . 0 . ? F2 F2 F . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING BE F1 ? ? SING BE F2 ? ? 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 'Escherichia 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' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _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 4 '[U-99% 13C; U-99% 15N]' stop_ save_ save_sample_2 _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 4 '[U-99% 15N]' stop_ save_ save_sample_3 _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 4 '[U-10% 13C]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_CBCACONH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label . save_ save_1H-15N_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_1H-15N_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_HCCH-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_4D_1H-13C_HMQC-NOESY-HMQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 1H-13C HMQC-NOESY-HMQC' _Sample_label . save_ save_4D_1H-15N_HMQC-NOESY-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 1H-15N HMQC-NOESY-HSQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 1H-13C HMQC-NOESY-HMQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 1H-15N HMQC-NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.7 0.2 n/a temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 $sample_3 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_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 . 2 ALA HB H 0.81 0.02 1 2 . 2 ALA CB C 18.1 0.2 1 3 . 3 ASP N N 121.4 0.2 1 4 . 3 ASP H H 8.64 0.02 1 5 . 3 ASP CA C 53.9 0.2 1 6 . 3 ASP HA H 4.5 0.02 1 7 . 3 ASP CB C 41.3 0.2 1 8 . 3 ASP HB2 H 2.72 0.02 2 9 . 3 ASP HB3 H 2.66 0.02 2 10 . 4 LYS N N 122.5 0.2 1 11 . 4 LYS H H 8.55 0.02 1 12 . 4 LYS CA C 57.1 0.2 1 13 . 4 LYS HA H 4.26 0.02 1 14 . 4 LYS CB C 30.6 0.2 1 15 . 4 LYS HB2 H 1.95 0.02 2 16 . 4 LYS HB3 H 1.79 0.02 2 17 . 4 LYS CG C 24.2 0.2 1 18 . 4 LYS HG2 H 1.38 0.02 2 19 . 4 LYS HG3 H 1.32 0.02 2 20 . 4 LYS CD C 27.6 0.2 1 21 . 4 LYS HD2 H 1.24 0.02 2 22 . 4 LYS HD3 H 1.18 0.02 2 23 . 4 LYS CE C 42.1 0.2 1 24 . 4 LYS HE2 H 2.81 0.02 1 25 . 4 LYS HE3 H 2.81 0.02 1 26 . 5 GLU N N 118.9 0.2 1 27 . 5 GLU H H 8.71 0.02 1 28 . 5 GLU CA C 55.5 0.2 1 29 . 5 GLU HA H 4.48 0.02 1 30 . 5 GLU CB C 29.1 0.2 1 31 . 5 GLU HB2 H 2.28 0.02 2 32 . 5 GLU HB3 H 1.96 0.02 2 33 . 5 GLU CG C 36.1 0.2 1 34 . 5 GLU HG2 H 2.35 0.02 2 35 . 5 GLU HG3 H 2.2 0.02 2 36 . 6 LEU N N 124.1 0.2 1 37 . 6 LEU H H 7.58 0.02 1 38 . 6 LEU CA C 56.3 0.2 1 39 . 6 LEU HA H 3.84 0.02 1 40 . 6 LEU CB C 42.9 0.2 1 41 . 6 LEU HB2 H 1.78 0.02 2 42 . 6 LEU HB3 H 1.61 0.02 2 43 . 6 LEU CG C 26.1 0.2 1 44 . 6 LEU HG H 1.17 0.02 1 45 . 6 LEU HD1 H 0.8 0.02 1 46 . 6 LEU HD2 H 0.61 0.02 1 47 . 6 LEU CD1 C 24.6 0.2 1 48 . 6 LEU CD2 C 26.1 0.2 1 49 . 7 LYS N N 126.1 0.2 1 50 . 7 LYS H H 8.51 0.02 1 51 . 7 LYS CA C 56 0.2 1 52 . 7 LYS HA H 5.12 0.02 1 53 . 7 LYS CB C 33.5 0.2 1 54 . 7 LYS HB2 H 1.88 0.02 2 55 . 7 LYS HB3 H 1.49 0.02 2 56 . 7 LYS CG C 25 0.2 1 57 . 7 LYS HG2 H 1.09 0.02 1 58 . 7 LYS HG3 H 1.09 0.02 1 59 . 7 LYS CD C 29.1 0.2 1 60 . 7 LYS HD2 H 1.15 0.02 2 61 . 7 LYS HD3 H 0.8 0.02 2 62 . 7 LYS CE C 41.3 0.2 1 63 . 7 LYS HE2 H 2.45 0.02 2 64 . 7 LYS HE3 H 2.19 0.02 2 65 . 8 PHE N N 128.1 0.2 1 66 . 8 PHE H H 9.22 0.02 1 67 . 8 PHE CA C 56.8 0.2 1 68 . 8 PHE HA H 5.46 0.02 1 69 . 8 PHE CB C 43.2 0.2 1 70 . 8 PHE HB2 H 3.19 0.02 2 71 . 8 PHE HB3 H 2.53 0.02 2 72 . 8 PHE CD1 C 130.6 0.2 3 73 . 8 PHE HD1 H 7 0.02 3 74 . 8 PHE CE1 C 131.1 0.2 3 75 . 8 PHE HE1 H 6.21 0.02 3 76 . 8 PHE CZ C 127.7 0.2 1 77 . 8 PHE HZ H 5.66 0.02 1 78 . 9 LEU N N 121.5 0.2 1 79 . 9 LEU H H 8.74 0.02 1 80 . 9 LEU CA C 52.9 0.2 1 81 . 9 LEU HA H 5.14 0.02 1 82 . 9 LEU CB C 43.6 0.2 1 83 . 9 LEU HB2 H 1.67 0.02 2 84 . 9 LEU HB3 H 1.08 0.02 2 85 . 9 LEU CG C 26.8 0.2 1 86 . 9 LEU HG H 1.17 0.02 1 87 . 9 LEU HD2 H 0.38 0.02 1 88 . 9 LEU HD1 H 0.56 0.02 1 89 . 9 LEU CD2 C 26.8 0.2 1 90 . 9 LEU CD1 C 22.7 0.2 1 91 . 10 VAL N N 127.3 0.2 1 92 . 10 VAL H H 9.08 0.02 1 93 . 10 VAL CA C 61.3 0.2 1 94 . 10 VAL HA H 4.82 0.02 1 95 . 10 VAL CB C 33.2 0.2 1 96 . 10 VAL HB H 1.98 0.02 1 97 . 10 VAL HG1 H 0.98 0.02 1 98 . 10 VAL HG2 H 0.88 0.02 1 99 . 10 VAL CG1 C 20.9 0.2 1 100 . 10 VAL CG2 C 22 0.2 1 101 . 11 VAL N N 127.2 0.2 1 102 . 11 VAL H H 9.22 0.02 1 103 . 11 VAL CA C 59.5 0.2 1 104 . 11 VAL HA H 4.9 0.02 1 105 . 11 VAL CB C 32.8 0.2 1 106 . 11 VAL HB H 2.3 0.02 1 107 . 11 VAL HG2 H 0.67 0.02 1 108 . 11 VAL HG1 H 0.62 0.02 1 109 . 11 VAL CG2 C 21.2 0.2 1 110 . 11 VAL CG1 C 21.6 0.2 1 111 . 12 ASP N N 124.6 0.2 1 112 . 12 ASP H H 8.11 0.02 1 113 . 12 ASP CA C 55.2 0.2 1 114 . 12 ASP HA H 4.69 0.02 1 115 . 12 ASP CB C 44 0.2 1 116 . 12 ASP HB2 H 2.72 0.02 2 117 . 12 ASP HB3 H 2.53 0.02 2 118 . 13 ASP N N 123.3 0.2 1 119 . 13 ASP H H 9.54 0.02 1 120 . 13 ASP CA C 54.8 0.2 1 121 . 13 ASP HA H 5.07 0.02 1 122 . 13 ASP CB C 39.1 0.2 1 123 . 13 ASP HB2 H 2.94 0.02 2 124 . 13 ASP HB3 H 2.79 0.02 2 125 . 14 PHE N N 123.7 0.2 1 126 . 14 PHE H H 10.3 0.02 1 127 . 14 PHE CA C 54.2 0.2 1 128 . 14 PHE HA H 5.25 0.02 1 129 . 14 PHE CB C 38 0.2 1 130 . 14 PHE HB2 H 3.18 0.02 2 131 . 14 PHE HB3 H 3.13 0.02 2 132 . 14 PHE HD1 H 7.44 0.02 3 133 . 14 PHE CD1 C 130.6 0.2 3 134 . 15 SER CA C 61.8 0.2 1 135 . 15 SER HA H 4.03 0.02 1 136 . 15 SER CB C 61.8 0.2 1 137 . 16 THR CA C 65.1 0.2 1 138 . 16 THR HA H 3.82 0.02 1 139 . 16 THR CB C 68.1 0.2 1 140 . 16 THR HB H 3.5 0.02 1 141 . 16 THR HG2 H 1.2 0.02 1 142 . 16 THR CG2 C 21.6 0.2 1 143 . 17 MET N N 119.3 0.2 1 144 . 17 MET H H 6.69 0.02 1 145 . 17 MET CA C 56 0.2 1 146 . 17 MET HA H 4.55 0.02 1 147 . 17 MET CB C 30.9 0.2 1 148 . 17 MET HB2 H 2.29 0.02 2 149 . 17 MET HB3 H 2.14 0.02 2 150 . 17 MET CG C 32 0.2 1 151 . 17 MET HG2 H 2.65 0.02 2 152 . 17 MET HG3 H 2.6 0.02 2 153 . 18 ARG N N 117 0.2 1 154 . 18 ARG H H 7.61 0.02 1 155 . 18 ARG CA C 60.7 0.2 1 156 . 18 ARG HA H 3.84 0.02 1 157 . 18 ARG CB C 30.6 0.2 1 158 . 18 ARG HB2 H 2.07 0.02 1 159 . 18 ARG HB3 H 2.07 0.02 1 160 . 18 ARG CG C 23.3 0.2 1 161 . 18 ARG HG2 H 1.1 0.02 2 162 . 18 ARG HG3 H 0.86 0.02 2 163 . 19 ARG N N 117.1 0.2 1 164 . 19 ARG H H 7.72 0.02 1 165 . 19 ARG CA C 58.9 0.2 1 166 . 19 ARG HA H 3.94 0.02 1 167 . 19 ARG CB C 29.3 0.2 1 168 . 19 ARG HB2 H 1.94 0.02 1 169 . 19 ARG HB3 H 1.94 0.02 1 170 . 19 ARG CG C 26.8 0.2 1 171 . 19 ARG HG2 H 1.71 0.02 2 172 . 19 ARG HG3 H 1.65 0.02 2 173 . 19 ARG CD C 42.8 0.2 1 174 . 19 ARG HD2 H 3.22 0.02 1 175 . 19 ARG HD3 H 3.22 0.02 1 176 . 20 ILE N N 119.9 0.2 1 177 . 20 ILE H H 7.77 0.02 1 178 . 20 ILE CA C 65.3 0.2 1 179 . 20 ILE HA H 3.72 0.02 1 180 . 20 ILE CB C 37.9 0.2 1 181 . 20 ILE HB H 2.09 0.02 1 182 . 20 ILE HG2 H 0.83 0.02 1 183 . 20 ILE CG2 C 16.4 0.2 1 184 . 20 ILE CG1 C 29.4 0.2 1 185 . 20 ILE HG12 H 1.81 0.02 2 186 . 20 ILE HG13 H 1.08 0.02 2 187 . 20 ILE HD1 H 0.84 0.02 1 188 . 20 ILE CD1 C 13.1 0.2 1 189 . 21 VAL N N 118.8 0.2 1 190 . 21 VAL H H 8.05 0.02 1 191 . 21 VAL CA C 67.4 0.2 1 192 . 21 VAL HA H 3.45 0.02 1 193 . 21 VAL CB C 31.1 0.2 1 194 . 21 VAL HB H 2.13 0.02 1 195 . 21 VAL HG2 H 1.12 0.02 1 196 . 21 VAL HG1 H 0.88 0.02 1 197 . 21 VAL CG2 C 22.9 0.2 1 198 . 21 VAL CG1 C 22.7 0.2 1 199 . 22 ARG N N 119.4 0.2 1 200 . 22 ARG H H 8.74 0.02 1 201 . 22 ARG CA C 60.5 0.2 1 202 . 22 ARG HA H 3.78 0.02 1 203 . 22 ARG CB C 30.5 0.2 1 204 . 22 ARG HB2 H 2 0.02 2 205 . 22 ARG HB3 H 1.78 0.02 2 206 . 22 ARG CG C 27.2 0.2 1 207 . 22 ARG HG2 H 1.54 0.02 1 208 . 22 ARG HG3 H 1.54 0.02 1 209 . 22 ARG CD C 43.9 0.2 1 210 . 22 ARG HD2 H 3.27 0.02 2 211 . 22 ARG HD3 H 3.07 0.02 2 212 . 23 ASN N N 118.9 0.2 1 213 . 23 ASN H H 8.57 0.02 1 214 . 23 ASN CA C 55.9 0.2 1 215 . 23 ASN HA H 4.55 0.02 1 216 . 23 ASN CB C 37.6 0.2 1 217 . 23 ASN HB2 H 3.03 0.02 2 218 . 23 ASN HB3 H 2.86 0.02 2 219 . 24 LEU N N 122.8 0.2 1 220 . 24 LEU H H 8.32 0.02 1 221 . 24 LEU CA C 58 0.2 1 222 . 24 LEU HA H 4.17 0.02 1 223 . 24 LEU CB C 41.7 0.2 1 224 . 24 LEU HB2 H 1.97 0.02 2 225 . 24 LEU HB3 H 1.33 0.02 2 226 . 24 LEU HD2 H 0.89 0.02 1 227 . 24 LEU HD1 H 0.79 0.02 1 228 . 24 LEU CD2 C 22.4 0.2 1 229 . 24 LEU CD1 C 26.5 0.2 1 230 . 25 LEU N N 118.1 0.2 1 231 . 25 LEU H H 8.41 0.02 1 232 . 25 LEU CA C 58 0.2 1 233 . 25 LEU HA H 3.85 0.02 1 234 . 25 LEU CB C 39.9 0.2 1 235 . 25 LEU HB2 H 1.82 0.02 2 236 . 25 LEU HB3 H 1.3 0.02 2 237 . 25 LEU CG C 26.1 0.2 1 238 . 25 LEU HG H 1.44 0.02 1 239 . 25 LEU HD1 H 0.11 0.02 1 240 . 25 LEU HD2 H -0.14 0.02 1 241 . 25 LEU CD1 C 26.1 0.2 1 242 . 25 LEU CD2 C 22 0.2 1 243 . 26 LYS N N 120.4 0.2 1 244 . 26 LYS H H 7.99 0.02 1 245 . 26 LYS CA C 59.6 0.2 1 246 . 26 LYS HA H 3.79 0.02 1 247 . 26 LYS CB C 31.6 0.2 1 248 . 26 LYS HB2 H 2.08 0.02 1 249 . 26 LYS HB3 H 2.08 0.02 1 250 . 26 LYS CG C 24.2 0.2 1 251 . 26 LYS HG2 H 1.61 0.02 1 252 . 26 LYS HG3 H 1.61 0.02 1 253 . 26 LYS CD C 29.4 0.2 1 254 . 26 LYS HD2 H 1.73 0.02 1 255 . 26 LYS HD3 H 1.73 0.02 1 256 . 26 LYS CE C 42.1 0.2 1 257 . 26 LYS HE2 H 3.02 0.02 1 258 . 26 LYS HE3 H 3.02 0.02 1 259 . 27 GLU N N 121.7 0.2 1 260 . 27 GLU H H 7.94 0.02 1 261 . 27 GLU CA C 59.1 0.2 1 262 . 27 GLU HA H 4.02 0.02 1 263 . 27 GLU CB C 28.7 0.2 1 264 . 27 GLU HB2 H 2.29 0.02 2 265 . 27 GLU HB3 H 2.19 0.02 2 266 . 27 GLU CG C 36.1 0.2 1 267 . 27 GLU HG2 H 2.47 0.02 2 268 . 27 GLU HG3 H 2.28 0.02 2 269 . 28 LEU N N 117.3 0.2 1 270 . 28 LEU H H 7.51 0.02 1 271 . 28 LEU CA C 54.7 0.2 1 272 . 28 LEU HA H 4.27 0.02 1 273 . 28 LEU CB C 42.1 0.2 1 274 . 28 LEU HB2 H 2.13 0.02 2 275 . 28 LEU HB3 H 1.83 0.02 2 276 . 28 LEU CG C 26.1 0.2 1 277 . 28 LEU HG H 2.03 0.02 1 278 . 28 LEU HD1 H 0.87 0.02 1 279 . 28 LEU HD2 H 0.86 0.02 1 280 . 28 LEU CD1 C 24.6 0.2 1 281 . 28 LEU CD2 C 21.6 0.2 1 282 . 29 GLY N N 106 0.2 1 283 . 29 GLY H H 7.75 0.02 1 284 . 29 GLY CA C 44.7 0.2 1 285 . 29 GLY HA2 H 3.95 0.02 2 286 . 29 GLY HA3 H 3.53 0.02 2 287 . 30 PHE N N 120.9 0.2 1 288 . 30 PHE H H 8.22 0.02 1 289 . 30 PHE CA C 57.3 0.2 1 290 . 30 PHE HA H 4.91 0.02 1 291 . 30 PHE CB C 38.4 0.2 1 292 . 30 PHE HB2 H 3.15 0.02 2 293 . 30 PHE HB3 H 2.47 0.02 2 294 . 30 PHE HD1 H 7.4 0.02 3 295 . 30 PHE CD1 C 131.3 0.2 3 296 . 30 PHE CE1 C 129.3 0.2 3 297 . 30 PHE HE1 H 7.31 0.02 3 298 . 31 ASN N N 118.3 0.2 1 299 . 31 ASN H H 8.37 0.02 1 300 . 31 ASN CA C 53.5 0.2 1 301 . 31 ASN HA H 4.71 0.02 1 302 . 31 ASN CB C 40.6 0.2 1 303 . 31 ASN HB2 H 2.82 0.02 2 304 . 31 ASN HB3 H 2.66 0.02 2 305 . 32 ASN N N 124.2 0.2 1 306 . 32 ASN H H 9.86 0.02 1 307 . 32 ASN CA C 52.1 0.2 1 308 . 32 ASN HA H 5 0.02 1 309 . 32 ASN CB C 36.4 0.2 1 310 . 32 ASN HB2 H 3.28 0.02 2 311 . 32 ASN HB3 H 2.88 0.02 2 312 . 33 VAL N N 122 0.2 1 313 . 33 VAL H H 7.53 0.02 1 314 . 33 VAL CA C 60.8 0.2 1 315 . 33 VAL HA H 5 0.02 1 316 . 33 VAL CB C 36.2 0.2 1 317 . 33 VAL HB H 1.84 0.02 1 318 . 33 VAL HG1 H 0.79 0.02 2 319 . 33 VAL CG1 C 22.4 0.2 2 320 . 34 GLU N N 126.6 0.2 1 321 . 34 GLU H H 9.06 0.02 1 322 . 34 GLU CA C 53.8 0.2 1 323 . 34 GLU HA H 4.94 0.02 1 324 . 34 GLU CB C 33.8 0.2 1 325 . 34 GLU HB2 H 2.29 0.02 2 326 . 34 GLU HB3 H 2.15 0.02 2 327 . 34 GLU CG C 35.7 0.2 1 328 . 34 GLU HG2 H 2.57 0.02 2 329 . 34 GLU HG3 H 2.46 0.02 2 330 . 35 GLU N N 120.9 0.2 1 331 . 35 GLU H H 8.98 0.02 1 332 . 35 GLU CA C 54.7 0.2 1 333 . 35 GLU HA H 5.48 0.02 1 334 . 35 GLU CB C 34.6 0.2 1 335 . 35 GLU HB2 H 1.92 0.02 2 336 . 35 GLU HB3 H 1.87 0.02 2 337 . 35 GLU CG C 36.9 0.2 1 338 . 35 GLU HG2 H 2.14 0.02 2 339 . 35 GLU HG3 H 2.05 0.02 2 340 . 36 ALA N N 120.1 0.2 1 341 . 36 ALA H H 8.89 0.02 1 342 . 36 ALA CA C 50.3 0.2 1 343 . 36 ALA HA H 4.82 0.02 1 344 . 36 ALA HB H 1.29 0.02 1 345 . 36 ALA CB C 22.4 0.2 1 346 . 37 GLU N N 117 0.2 1 347 . 37 GLU H H 9.47 0.02 1 348 . 37 GLU CA C 56.3 0.2 1 349 . 37 GLU HA H 4.67 0.02 1 350 . 37 GLU CB C 31.8 0.2 1 351 . 37 GLU HB2 H 2.07 0.02 1 352 . 37 GLU HB3 H 2.07 0.02 1 353 . 37 GLU CG C 35 0.2 1 354 . 37 GLU HG2 H 2.25 0.02 2 355 . 37 GLU HG3 H 2.18 0.02 2 356 . 38 ASP N N 110.9 0.2 1 357 . 38 ASP H H 7.55 0.02 1 358 . 38 ASP CA C 53.8 0.2 1 359 . 38 ASP HA H 5.42 0.02 1 360 . 38 ASP CB C 41.3 0.2 1 361 . 38 ASP HB2 H 3.62 0.02 2 362 . 38 ASP HB3 H 3.23 0.02 2 363 . 39 GLY N N 101.6 0.2 1 364 . 39 GLY H H 8 0.02 1 365 . 39 GLY CA C 48.4 0.2 1 366 . 39 GLY HA2 H 3.75 0.02 2 367 . 39 GLY HA3 H 3.58 0.02 2 368 . 40 VAL N N 122.7 0.2 1 369 . 40 VAL H H 8.01 0.02 1 370 . 40 VAL CA C 66.2 0.2 1 371 . 40 VAL HA H 3.5 0.02 1 372 . 40 VAL CB C 31.3 0.2 1 373 . 40 VAL HB H 2.25 0.02 1 374 . 40 VAL HG1 H 0.9 0.02 1 375 . 40 VAL HG2 H 0.9 0.02 1 376 . 40 VAL CG1 C 20.9 0.2 1 377 . 40 VAL CG2 C 22.7 0.2 1 378 . 41 ASP N N 121.1 0.2 1 379 . 41 ASP H H 8.66 0.02 1 380 . 41 ASP CA C 56.3 0.2 1 381 . 41 ASP HA H 4.4 0.02 1 382 . 41 ASP CB C 42.4 0.2 1 383 . 41 ASP HB2 H 2.99 0.02 2 384 . 41 ASP HB3 H 2.61 0.02 2 385 . 42 ALA N N 116.7 0.2 1 386 . 42 ALA H H 8.29 0.02 1 387 . 42 ALA CA C 55.1 0.2 1 388 . 42 ALA HA H 3.62 0.02 1 389 . 42 ALA HB H 1.35 0.02 1 390 . 42 ALA CB C 19.5 0.2 1 391 . 43 LEU N N 118.3 0.2 1 392 . 43 LEU H H 8.17 0.02 1 393 . 43 LEU CA C 58 0.2 1 394 . 43 LEU HA H 3.76 0.02 1 395 . 43 LEU CB C 41 0.2 1 396 . 43 LEU HB2 H 1.74 0.02 2 397 . 43 LEU HB3 H 1.53 0.02 2 398 . 43 LEU CG C 26.5 0.2 1 399 . 43 LEU HG H 1.68 0.02 1 400 . 43 LEU HD2 H 0.8 0.02 1 401 . 43 LEU HD1 H 0.72 0.02 1 402 . 43 LEU CD2 C 25.3 0.2 1 403 . 43 LEU CD1 C 23.5 0.2 1 404 . 44 ASN N N 116.6 0.2 1 405 . 44 ASN H H 7.94 0.02 1 406 . 44 ASN CA C 56 0.2 1 407 . 44 ASN HA H 4.39 0.02 1 408 . 44 ASN CB C 38 0.2 1 409 . 44 ASN HB2 H 3.06 0.02 2 410 . 44 ASN HB3 H 2.87 0.02 2 411 . 45 LYS N N 120.2 0.2 1 412 . 45 LYS H H 7.94 0.02 1 413 . 45 LYS CA C 60 0.2 1 414 . 45 LYS HA H 4.11 0.02 1 415 . 45 LYS CB C 31.7 0.2 1 416 . 45 LYS HB2 H 1.78 0.02 1 417 . 45 LYS HB3 H 1.78 0.02 1 418 . 45 LYS CG C 26.8 0.2 1 419 . 45 LYS HG2 H 1.71 0.02 2 420 . 45 LYS HG3 H 1.49 0.02 2 421 . 45 LYS CD C 29.1 0.2 1 422 . 45 LYS HD2 H 1.62 0.02 2 423 . 45 LYS HD3 H 1.48 0.02 2 424 . 45 LYS CE C 42.4 0.2 1 425 . 45 LYS HE2 H 3.2 0.02 2 426 . 45 LYS HE3 H 3.11 0.02 2 427 . 46 LEU N N 118.7 0.2 1 428 . 46 LEU H H 8.75 0.02 1 429 . 46 LEU CA C 57.4 0.2 1 430 . 46 LEU HA H 3.85 0.02 1 431 . 46 LEU CB C 42.1 0.2 1 432 . 46 LEU HB2 H 1.72 0.02 2 433 . 46 LEU HB3 H 1.4 0.02 2 434 . 46 LEU CG C 30.9 0.2 1 435 . 46 LEU HG H 1.4 0.02 1 436 . 46 LEU HD1 H 0.53 0.02 1 437 . 46 LEU HD2 H 0.34 0.02 1 438 . 46 LEU CD1 C 25 0.2 1 439 . 46 LEU CD2 C 22.4 0.2 1 440 . 47 GLN N N 116.5 0.2 1 441 . 47 GLN H H 7.88 0.02 1 442 . 47 GLN CA C 57.6 0.2 1 443 . 47 GLN HA H 4.04 0.02 1 444 . 47 GLN CB C 27.9 0.2 1 445 . 47 GLN CG C 33.5 0.2 1 446 . 48 ALA N N 120.4 0.2 1 447 . 48 ALA H H 7.64 0.02 1 448 . 48 ALA CA C 53.3 0.2 1 449 . 48 ALA HA H 4.33 0.02 1 450 . 48 ALA HB H 1.67 0.02 1 451 . 48 ALA CB C 19 0.2 1 452 . 49 GLY N N 104 0.2 1 453 . 49 GLY H H 7.61 0.02 1 454 . 49 GLY CA C 44.3 0.2 1 455 . 49 GLY HA2 H 4.32 0.02 2 456 . 49 GLY HA3 H 4.08 0.02 2 457 . 50 GLY N N 103.6 0.2 1 458 . 50 GLY H H 8.38 0.02 1 459 . 50 GLY CA C 45.1 0.2 1 460 . 50 GLY HA2 H 3.94 0.02 2 461 . 50 GLY HA3 H 3.67 0.02 2 462 . 51 TYR N N 118.5 0.2 1 463 . 51 TYR H H 8.11 0.02 1 464 . 51 TYR CA C 60.7 0.2 1 465 . 51 TYR HA H 4.04 0.02 1 466 . 51 TYR CB C 38.8 0.2 1 467 . 51 TYR HB2 H 3.04 0.02 2 468 . 51 TYR HB3 H 2.51 0.02 2 469 . 51 TYR CD1 C 132.2 0.2 3 470 . 51 TYR HD1 H 6.78 0.02 3 471 . 51 TYR CE1 C 117.9 0.2 3 472 . 51 TYR HE1 H 6.66 0.02 3 473 . 52 GLY N N 106.8 0.2 1 474 . 52 GLY H H 9.52 0.02 1 475 . 52 GLY CA C 44.3 0.2 1 476 . 52 GLY HA2 H 4.51 0.02 2 477 . 52 GLY HA3 H 3.45 0.02 2 478 . 53 PHE N N 121.4 0.2 1 479 . 53 PHE H H 7.58 0.02 1 480 . 53 PHE CA C 58 0.2 1 481 . 53 PHE HA H 4.06 0.02 1 482 . 53 PHE CB C 43.2 0.2 1 483 . 53 PHE HB2 H 2.1 0.02 2 484 . 53 PHE HB3 H 1.98 0.02 2 485 . 53 PHE HD1 H 6.91 0.02 3 486 . 53 PHE CD1 C 132 0.2 3 487 . 54 VAL N N 127 0.2 1 488 . 54 VAL H H 8.25 0.02 1 489 . 54 VAL CA C 60.9 0.2 1 490 . 54 VAL HA H 5.08 0.02 1 491 . 54 VAL CB C 34.3 0.2 1 492 . 54 VAL HB H 2.1 0.02 1 493 . 54 VAL HG2 H 0.82 0.02 1 494 . 54 VAL HG1 H 0.74 0.02 1 495 . 54 VAL CG2 C 22.4 0.2 1 496 . 54 VAL CG1 C 20.5 0.2 1 497 . 55 ILE N N 128.6 0.2 1 498 . 55 ILE H H 9.36 0.02 1 499 . 55 ILE CA C 60.3 0.2 1 500 . 55 ILE HA H 5.07 0.02 1 501 . 55 ILE CB C 39.7 0.2 1 502 . 55 ILE HB H 1.88 0.02 1 503 . 55 ILE HG2 H 0.93 0.02 1 504 . 55 ILE CG2 C 16.8 0.2 1 505 . 55 ILE CG1 C 27.9 0.2 1 506 . 55 ILE HG12 H 1.97 0.02 2 507 . 55 ILE HG13 H 1.21 0.02 2 508 . 55 ILE HD1 H 0.77 0.02 1 509 . 55 ILE CD1 C 13.8 0.2 1 510 . 56 SER N N 118.9 0.2 1 511 . 56 SER H H 9.07 0.02 1 512 . 56 SER CA C 56.6 0.2 1 513 . 56 SER HA H 5.37 0.02 1 514 . 56 SER CB C 65.5 0.2 1 515 . 56 SER HB2 H 3.51 0.02 2 516 . 56 SER HB3 H 3 0.02 2 517 . 57 ASP N N 126.3 0.2 1 518 . 57 ASP H H 8.33 0.02 1 519 . 57 ASP CA C 52.4 0.2 1 520 . 57 ASP HA H 5.66 0.02 1 521 . 57 ASP CB C 43.9 0.2 1 522 . 57 ASP HB2 H 3.76 0.02 2 523 . 57 ASP HB3 H 3.11 0.02 2 524 . 58 TRP N N 120.8 0.2 1 525 . 58 TRP H H 8.1 0.02 1 526 . 58 TRP CA C 59.4 0.2 1 527 . 58 TRP HA H 4.45 0.02 1 528 . 58 TRP CB C 29.8 0.2 1 529 . 58 TRP HB2 H 3.59 0.02 2 530 . 58 TRP HB3 H 3.11 0.02 2 531 . 58 TRP CD1 C 124.5 0.2 1 532 . 58 TRP CE3 C 119.7 0.2 1 533 . 58 TRP NE1 N 130.4 0.2 1 534 . 58 TRP HD1 H 7.11 0.02 1 535 . 58 TRP HE3 H 7.58 0.02 1 536 . 58 TRP CZ3 C 121.6 0.2 1 537 . 58 TRP CZ2 C 115.3 0.2 1 538 . 58 TRP HE1 H 10.32 0.02 1 539 . 58 TRP HZ3 H 7.28 0.02 1 540 . 58 TRP CH2 C 124.4 0.2 1 541 . 58 TRP HZ2 H 7.51 0.02 1 542 . 58 TRP HH2 H 7.38 0.02 1 543 . 59 ASN N N 117 0.2 1 544 . 59 ASN H H 9.27 0.02 1 545 . 59 ASN CA C 54.8 0.2 1 546 . 59 ASN HA H 4.89 0.02 1 547 . 59 ASN CB C 37.2 0.2 1 548 . 59 ASN HB2 H 3.12 0.02 2 549 . 59 ASN HB3 H 3.07 0.02 2 550 . 60 MET N N 128.6 0.2 1 551 . 60 MET H H 7.53 0.02 1 552 . 60 MET CA C 53.8 0.2 1 553 . 60 MET HA H 4.69 0.02 1 554 . 60 MET CB C 32.8 0.2 1 555 . 60 MET CG C 29.1 0.2 1 556 . 61 PRO CD C 50.3 0.2 1 557 . 61 PRO CA C 62.2 0.2 1 558 . 61 PRO HA H 4.48 0.02 1 559 . 61 PRO CB C 32.4 0.2 1 560 . 61 PRO HB2 H 2.33 0.02 2 561 . 61 PRO HB3 H 1.94 0.02 2 562 . 61 PRO CG C 26.8 0.2 1 563 . 61 PRO HD2 H 3.83 0.02 2 564 . 61 PRO HD3 H 3.68 0.02 2 565 . 62 ASN N N 111.1 0.2 1 566 . 62 ASN H H 8.66 0.02 1 567 . 62 ASN CA C 58.7 0.2 1 568 . 62 ASN HA H 4.05 0.02 1 569 . 62 ASN CB C 37.6 0.2 1 570 . 62 ASN HB2 H 3.3 0.02 2 571 . 62 ASN HB3 H 2.58 0.02 2 572 . 63 MET N N 123.1 0.2 1 573 . 63 MET H H 9.43 0.02 1 574 . 63 MET CA C 56.6 0.2 1 575 . 63 MET HA H 4.27 0.02 1 576 . 63 MET CB C 35.7 0.2 1 577 . 63 MET CG C 30.9 0.2 1 578 . 63 MET HG2 H 2.52 0.02 2 579 . 63 MET HG3 H 2.39 0.02 2 580 . 64 ASP N N 127.1 0.2 1 581 . 64 ASP H H 8.72 0.02 1 582 . 64 ASP CA C 53.1 0.2 1 583 . 64 ASP HA H 4.57 0.02 1 584 . 64 ASP CB C 41 0.2 1 585 . 64 ASP HB2 H 3.82 0.02 2 586 . 64 ASP HB3 H 2.87 0.02 2 587 . 65 GLY N N 103.1 0.2 1 588 . 65 GLY H H 9.75 0.02 1 589 . 65 GLY CA C 46.5 0.2 1 590 . 65 GLY HA2 H 4.21 0.02 2 591 . 65 GLY HA3 H 3.5 0.02 2 592 . 66 LEU N N 122.2 0.2 1 593 . 66 LEU H H 7.11 0.02 1 594 . 66 LEU CA C 56.6 0.2 1 595 . 66 LEU HA H 3.64 0.02 1 596 . 66 LEU CB C 39.8 0.2 1 597 . 66 LEU HB2 H 1.64 0.02 2 598 . 66 LEU HB3 H 0.19 0.02 2 599 . 66 LEU CG C 26.8 0.2 1 600 . 66 LEU HG H 1.3 0.02 1 601 . 66 LEU HD2 H 0.91 0.02 1 602 . 66 LEU HD1 H 0.56 0.02 1 603 . 66 LEU CD2 C 24.6 0.2 1 604 . 66 LEU CD1 C 22.4 0.2 1 605 . 67 GLU N N 120.1 0.2 1 606 . 67 GLU H H 8.35 0.02 1 607 . 67 GLU CA C 58.9 0.2 1 608 . 67 GLU HA H 3.85 0.02 1 609 . 67 GLU CB C 28.7 0.2 1 610 . 67 GLU HB2 H 1.98 0.02 2 611 . 67 GLU HB3 H 1.85 0.02 2 612 . 67 GLU CG C 35.7 0.2 1 613 . 67 GLU HG2 H 2.3 0.02 1 614 . 67 GLU HG3 H 2.3 0.02 1 615 . 68 LEU N N 123.2 0.2 1 616 . 68 LEU H H 8.4 0.02 1 617 . 68 LEU CA C 58.5 0.2 1 618 . 68 LEU HA H 4.01 0.02 1 619 . 68 LEU CB C 41 0.2 1 620 . 68 LEU HB2 H 1.98 0.02 2 621 . 68 LEU HB3 H 1.13 0.02 2 622 . 68 LEU CG C 27.2 0.2 1 623 . 68 LEU HG H 1.35 0.02 1 624 . 68 LEU HD1 H 0.88 0.02 1 625 . 68 LEU HD2 H 0.78 0.02 1 626 . 68 LEU CD1 C 22.7 0.2 1 627 . 68 LEU CD2 C 25.3 0.2 1 628 . 69 LEU N N 120.8 0.2 1 629 . 69 LEU H H 8.11 0.02 1 630 . 69 LEU CA C 58.3 0.2 1 631 . 69 LEU HA H 3.74 0.02 1 632 . 69 LEU CB C 41 0.2 1 633 . 69 LEU HB2 H 2.1 0.02 2 634 . 69 LEU HB3 H 1.52 0.02 2 635 . 69 LEU CG C 26.1 0.2 1 636 . 69 LEU HG H 1.36 0.02 1 637 . 69 LEU HD2 H 0.82 0.02 1 638 . 69 LEU HD1 H 0.63 0.02 1 639 . 69 LEU CD2 C 27.2 0.2 1 640 . 69 LEU CD1 C 22 0.2 1 641 . 70 LYS N N 115.9 0.2 1 642 . 70 LYS H H 8.45 0.02 1 643 . 70 LYS CA C 59.9 0.2 1 644 . 70 LYS HA H 3.8 0.02 1 645 . 70 LYS CB C 32 0.2 1 646 . 70 LYS HB2 H 1.88 0.02 2 647 . 70 LYS HB3 H 1.77 0.02 2 648 . 70 LYS CG C 24.2 0.2 1 649 . 70 LYS HG2 H 1.44 0.02 1 650 . 70 LYS HG3 H 1.44 0.02 1 651 . 70 LYS CD C 28.7 0.2 1 652 . 70 LYS HD2 H 1.67 0.02 1 653 . 70 LYS HD3 H 1.67 0.02 1 654 . 70 LYS CE C 41.3 0.2 1 655 . 70 LYS HE2 H 2.95 0.02 1 656 . 70 LYS HE3 H 2.95 0.02 1 657 . 71 THR N N 117.4 0.2 1 658 . 71 THR H H 8.08 0.02 1 659 . 71 THR CA C 67.1 0.2 1 660 . 71 THR HA H 3.78 0.02 1 661 . 71 THR CB C 68.3 0.2 1 662 . 71 THR HB H 4.35 0.02 1 663 . 71 THR HG2 H 1.18 0.02 1 664 . 71 THR CG2 C 21.6 0.2 1 665 . 72 ILE N N 123.4 0.2 1 666 . 72 ILE H H 8.47 0.02 1 667 . 72 ILE CA C 66 0.2 1 668 . 72 ILE HA H 3.36 0.02 1 669 . 72 ILE CB C 38.5 0.2 1 670 . 72 ILE HB H 1.87 0.02 1 671 . 72 ILE HG2 H 0.75 0.02 1 672 . 72 ILE CG2 C 17.2 0.2 1 673 . 72 ILE CG1 C 29.1 0.2 1 674 . 72 ILE HG12 H 1.68 0.02 2 675 . 72 ILE HG13 H 1.14 0.02 2 676 . 72 ILE HD1 H 0.56 0.02 1 677 . 72 ILE CD1 C 14.5 0.2 1 678 . 73 ARG N N 113.4 0.2 1 679 . 73 ARG H H 8.16 0.02 1 680 . 73 ARG CA C 57.3 0.2 1 681 . 73 ARG HA H 4.04 0.02 1 682 . 73 ARG CB C 29 0.2 1 683 . 73 ARG HB2 H 1.99 0.02 1 684 . 73 ARG HB3 H 1.99 0.02 1 685 . 74 ALA N N 118.7 0.2 1 686 . 74 ALA H H 7.3 0.02 1 687 . 74 ALA CA C 51.7 0.2 1 688 . 74 ALA HA H 4.36 0.02 1 689 . 74 ALA HB H 1.4 0.02 1 690 . 74 ALA CB C 19.2 0.2 1 691 . 75 ASP N N 121.8 0.2 1 692 . 75 ASP H H 7.42 0.02 1 693 . 75 ASP CA C 54 0.2 1 694 . 75 ASP HA H 4.56 0.02 1 695 . 75 ASP CB C 43.6 0.2 1 696 . 75 ASP HB2 H 2.89 0.02 2 697 . 75 ASP HB3 H 2.6 0.02 2 698 . 76 GLY N N 112.1 0.2 1 699 . 76 GLY H H 8.75 0.02 1 700 . 76 GLY CA C 47.2 0.2 1 701 . 77 ALA N N 121.8 0.2 1 702 . 77 ALA H H 8.56 0.02 1 703 . 77 ALA CA C 53.3 0.2 1 704 . 77 ALA HA H 4.49 0.02 1 705 . 77 ALA HB H 1.39 0.02 1 706 . 77 ALA CB C 20.1 0.2 1 707 . 78 MET N N 116 0.2 1 708 . 78 MET H H 8.56 0.02 1 709 . 78 MET CA C 55.7 0.2 1 710 . 78 MET HA H 4.59 0.02 1 711 . 78 MET CB C 34.3 0.2 1 712 . 78 MET HB2 H 2.22 0.02 2 713 . 78 MET HB3 H 2.15 0.02 2 714 . 78 MET CG C 31.7 0.2 1 715 . 78 MET HG2 H 2.61 0.02 2 716 . 78 MET HG3 H 2.39 0.02 2 717 . 79 SER N N 112.6 0.2 1 718 . 79 SER H H 7.46 0.02 1 719 . 79 SER CA C 61.7 0.2 1 720 . 79 SER HA H 4.43 0.02 1 721 . 79 SER CB C 65.5 0.2 1 722 . 79 SER HB2 H 4.07 0.02 2 723 . 79 SER HB3 H 3.97 0.02 2 724 . 80 ALA N N 123 0.2 1 725 . 80 ALA H H 8.25 0.02 1 726 . 80 ALA CA C 50.9 0.2 1 727 . 80 ALA HA H 4.44 0.02 1 728 . 80 ALA HB H 1.34 0.02 1 729 . 80 ALA CB C 18.7 0.2 1 730 . 81 LEU N N 124.1 0.2 1 731 . 81 LEU H H 7.93 0.02 1 732 . 81 LEU CA C 53.5 0.2 1 733 . 81 LEU HA H 4.14 0.02 1 734 . 81 LEU CB C 42.8 0.2 1 735 . 81 LEU HB2 H 1.53 0.02 2 736 . 81 LEU HB3 H 1.28 0.02 2 737 . 81 LEU CG C 26.1 0.2 1 738 . 81 LEU HG H 1.54 0.02 1 739 . 81 LEU HD2 H 0.7 0.02 1 740 . 81 LEU HD1 H 0.7 0.02 1 741 . 81 LEU CD1 C 25.3 0.2 1 742 . 81 LEU CD2 C 24.6 0.2 1 743 . 82 PRO CD C 50.4 0.2 1 744 . 82 PRO CA C 62.5 0.2 1 745 . 82 PRO HA H 3.96 0.02 1 746 . 82 PRO CB C 31.4 0.2 1 747 . 82 PRO HB2 H 1.35 0.02 2 748 . 82 PRO HB3 H 0.33 0.02 2 749 . 82 PRO CG C 28.1 0.2 1 750 . 82 PRO HG2 H 1.83 0.02 2 751 . 82 PRO HG3 H 1.7 0.02 2 752 . 82 PRO HD2 H 3.92 0.02 2 753 . 82 PRO HD3 H 3.62 0.02 2 754 . 83 VAL N N 119 0.2 1 755 . 83 VAL H H 7.74 0.02 1 756 . 83 VAL CA C 60.2 0.2 1 757 . 83 VAL HA H 4.78 0.02 1 758 . 83 VAL CB C 35 0.2 1 759 . 83 VAL HB H 1.67 0.02 1 760 . 83 VAL HG1 H 0.69 0.02 1 761 . 83 VAL HG2 H 0.62 0.02 1 762 . 83 VAL CG1 C 20.1 0.2 1 763 . 83 VAL CG2 C 20.5 0.2 1 764 . 84 LEU N N 130.5 0.2 1 765 . 84 LEU H H 9.17 0.02 1 766 . 84 LEU CA C 52.4 0.2 1 767 . 84 LEU HA H 4.47 0.02 1 768 . 84 LEU CB C 45.4 0.2 1 769 . 84 LEU HB2 H 2.09 0.02 2 770 . 84 LEU HB3 H 1.14 0.02 2 771 . 84 LEU CG C 26.1 0.2 1 772 . 84 LEU HG H 1.26 0.02 1 773 . 84 LEU HD2 H 0.53 0.02 1 774 . 84 LEU HD1 H 0.57 0.02 1 775 . 84 LEU CD2 C 25.3 0.2 1 776 . 84 LEU CD1 C 22.7 0.2 1 777 . 85 MET N N 125.9 0.2 1 778 . 85 MET H H 7.96 0.02 1 779 . 85 MET CA C 53.2 0.2 1 780 . 85 MET HA H 5.54 0.02 1 781 . 85 MET CB C 32 0.2 1 782 . 85 MET HB2 H 1.83 0.02 2 783 . 85 MET HB3 H 1.86 0.02 2 784 . 85 MET CG C 32 0.2 1 785 . 85 MET HG2 H 2.41 0.02 2 786 . 86 VAL N N 122.4 0.2 1 787 . 86 VAL H H 8.77 0.02 1 788 . 86 VAL CA C 59.4 0.2 1 789 . 86 VAL HA H 5.13 0.02 1 790 . 86 VAL CB C 33.6 0.2 1 791 . 86 VAL HB H 1.78 0.02 1 792 . 86 VAL HG1 H 0.58 0.02 1 793 . 86 VAL HG2 H 0.58 0.02 1 794 . 86 VAL CG1 C 22.4 0.2 1 795 . 86 VAL CG2 C 20.9 0.2 1 796 . 87 THR N N 115.1 0.2 1 797 . 87 THR H H 8.18 0.02 1 798 . 87 THR CA C 58.9 0.2 1 799 . 87 THR HA H 5.29 0.02 1 800 . 87 THR CB C 68.8 0.2 1 801 . 87 THR HB H 4.39 0.02 1 802 . 87 THR HG2 H 1.07 0.02 1 803 . 87 THR CG2 C 18.3 0.2 1 804 . 88 ALA N N 128.4 0.2 1 805 . 88 ALA H H 8.44 0.02 1 806 . 88 ALA CA C 52.8 0.2 1 807 . 88 ALA HA H 4.57 0.02 1 808 . 88 ALA HB H 1.56 0.02 1 809 . 88 ALA CB C 19.2 0.2 1 810 . 89 GLU N N 120.2 0.2 1 811 . 89 GLU H H 8.7 0.02 1 812 . 89 GLU CA C 55.9 0.2 1 813 . 89 GLU HA H 4.21 0.02 1 814 . 89 GLU CB C 29 0.2 1 815 . 89 GLU HB2 H 1.79 0.02 1 816 . 89 GLU HB3 H 1.79 0.02 1 817 . 89 GLU CG C 35.4 0.2 1 818 . 89 GLU HG2 H 1.89 0.02 1 819 . 89 GLU HG3 H 1.89 0.02 1 820 . 90 ALA N N 129.4 0.2 1 821 . 90 ALA H H 8.48 0.02 1 822 . 90 ALA CA C 51.2 0.2 1 823 . 90 ALA HA H 4.48 0.02 1 824 . 90 ALA HB H 1.39 0.02 1 825 . 90 ALA CB C 19.9 0.2 1 826 . 91 LYS N N 119.9 0.2 1 827 . 91 LYS H H 7.72 0.02 1 828 . 91 LYS CA C 56.4 0.2 1 829 . 91 LYS HA H 4.3 0.02 1 830 . 91 LYS CB C 32.8 0.2 1 831 . 91 LYS HB2 H 1.87 0.02 2 832 . 91 LYS HB3 H 1.71 0.02 2 833 . 91 LYS CG C 25 0.2 1 834 . 91 LYS HG2 H 1.44 0.02 1 835 . 91 LYS HG3 H 1.44 0.02 1 836 . 91 LYS CD C 29.1 0.2 1 837 . 91 LYS HD2 H 1.65 0.02 1 838 . 91 LYS HD3 H 1.65 0.02 1 839 . 91 LYS CE C 41.7 0.2 1 840 . 91 LYS HE2 H 2.94 0.02 1 841 . 91 LYS HE3 H 2.94 0.02 1 842 . 92 LYS N N 126 0.2 1 843 . 92 LYS H H 8.94 0.02 1 844 . 92 LYS CA C 59.6 0.2 1 845 . 92 LYS HA H 3.8 0.02 1 846 . 92 LYS CB C 31.7 0.2 1 847 . 92 LYS HB2 H 1.9 0.02 2 848 . 92 LYS HB3 H 1.8 0.02 2 849 . 93 GLU N N 116.1 0.2 1 850 . 93 GLU H H 9.57 0.02 1 851 . 93 GLU CA C 59.8 0.2 1 852 . 93 GLU HA H 3.94 0.02 1 853 . 93 GLU CB C 28.4 0.2 1 854 . 93 GLU HB2 H 1.92 0.02 1 855 . 93 GLU HB3 H 1.92 0.02 1 856 . 93 GLU CG C 36.5 0.2 1 857 . 93 GLU HG2 H 2.38 0.02 2 858 . 93 GLU HG3 H 2.25 0.02 2 859 . 94 ASN N N 119.1 0.2 1 860 . 94 ASN H H 7.32 0.02 1 861 . 94 ASN CA C 55.6 0.2 1 862 . 94 ASN HA H 4.52 0.02 1 863 . 94 ASN CB C 37.5 0.2 1 864 . 94 ASN HB2 H 2.59 0.02 2 865 . 94 ASN HB3 H 2.36 0.02 2 866 . 95 ILE N N 121.5 0.2 1 867 . 95 ILE H H 7.28 0.02 1 868 . 95 ILE CA C 65.3 0.2 1 869 . 95 ILE HA H 2.97 0.02 1 870 . 95 ILE CB C 37.5 0.2 1 871 . 95 ILE HB H 1.58 0.02 1 872 . 95 ILE HG2 H 0.51 0.02 1 873 . 95 ILE CG2 C 16.4 0.2 1 874 . 95 ILE CG1 C 27.6 0.2 1 875 . 95 ILE HG12 H 1.05 0.02 2 876 . 95 ILE HG13 H 0.02 0.02 2 877 . 95 ILE HD1 H 0.52 0.02 1 878 . 95 ILE CD1 C 12.7 0.2 1 879 . 96 ILE N N 119.2 0.2 1 880 . 96 ILE H H 7.88 0.02 1 881 . 96 ILE CA C 64.1 0.2 1 882 . 96 ILE HA H 3.75 0.02 1 883 . 96 ILE CB C 37.9 0.2 1 884 . 96 ILE HB H 1.76 0.02 1 885 . 96 ILE HG2 H 0.89 0.02 1 886 . 96 ILE CG2 C 16.8 0.2 1 887 . 96 ILE CG1 C 28.7 0.2 1 888 . 96 ILE HG12 H 1.58 0.02 2 889 . 96 ILE HG13 H 1.14 0.02 2 890 . 96 ILE HD1 H 0.79 0.02 1 891 . 96 ILE CD1 C 12.7 0.2 1 892 . 97 ALA N N 122.2 0.2 1 893 . 97 ALA H H 7.82 0.02 1 894 . 97 ALA CA C 55 0.2 1 895 . 97 ALA HA H 4.2 0.02 1 896 . 97 ALA HB H 1.73 0.02 1 897 . 97 ALA CB C 17.5 0.2 1 898 . 98 ALA N N 119.6 0.2 1 899 . 98 ALA H H 8.62 0.02 1 900 . 98 ALA CA C 54.6 0.2 1 901 . 98 ALA HA H 3.88 0.02 1 902 . 98 ALA HB H 1.62 0.02 1 903 . 98 ALA CB C 17.2 0.2 1 904 . 99 ALA N N 121.8 0.2 1 905 . 99 ALA H H 8.11 0.02 1 906 . 99 ALA CA C 55.4 0.2 1 907 . 99 ALA HA H 4.17 0.02 1 908 . 99 ALA HB H 1.55 0.02 1 909 . 99 ALA CB C 18.6 0.2 1 910 . 100 GLN N N 119 0.2 1 911 . 100 GLN H H 8.77 0.02 1 912 . 100 GLN CA C 58.4 0.2 1 913 . 100 GLN HA H 4.03 0.02 1 914 . 100 GLN CB C 27.9 0.2 1 915 . 100 GLN HB2 H 2.19 0.02 2 916 . 100 GLN HB3 H 2.11 0.02 2 917 . 100 GLN CG C 33.9 0.2 1 918 . 100 GLN HG2 H 2.61 0.02 2 919 . 100 GLN HG3 H 2.43 0.02 2 920 . 101 ALA N N 118.4 0.2 1 921 . 101 ALA H H 7.61 0.02 1 922 . 101 ALA CA C 51.7 0.2 1 923 . 101 ALA HA H 4.35 0.02 1 924 . 101 ALA HB H 1.39 0.02 1 925 . 101 ALA CB C 19.2 0.2 1 926 . 102 GLY N N 102.3 0.2 1 927 . 102 GLY H H 7.62 0.02 1 928 . 102 GLY CA C 45.5 0.2 1 929 . 102 GLY HA2 H 4.23 0.02 2 930 . 102 GLY HA3 H 3.85 0.02 2 931 . 103 ALA N N 125 0.2 1 932 . 103 ALA H H 8.73 0.02 1 933 . 103 ALA CA C 53.6 0.2 1 934 . 103 ALA HA H 3.97 0.02 1 935 . 103 ALA HB H 1.38 0.02 1 936 . 103 ALA CB C 17.9 0.2 1 937 . 104 SER N N 118.5 0.2 1 938 . 104 SER H H 9.31 0.02 1 939 . 104 SER CA C 59.8 0.2 1 940 . 104 SER HA H 4.39 0.02 1 941 . 104 SER CB C 61.4 0.2 1 942 . 104 SER HB2 H 3.96 0.02 2 943 . 104 SER HB3 H 3.21 0.02 2 944 . 105 GLY N N 102.4 0.2 1 945 . 105 GLY H H 7.64 0.02 1 946 . 105 GLY CA C 45.1 0.2 1 947 . 105 GLY HA2 H 4.16 0.02 2 948 . 105 GLY HA3 H 3.73 0.02 2 949 . 106 TYR N N 124.3 0.2 1 950 . 106 TYR H H 8.63 0.02 1 951 . 106 TYR CA C 57.3 0.2 1 952 . 106 TYR HA H 5.33 0.02 1 953 . 106 TYR CB C 42.4 0.2 1 954 . 106 TYR HB2 H 2.98 0.02 2 955 . 106 TYR HB3 H 2.62 0.02 2 956 . 106 TYR CD1 C 133.2 0.2 3 957 . 106 TYR HD1 H 6.96 0.02 3 958 . 106 TYR CE1 C 118.3 0.2 3 959 . 106 TYR HE1 H 6.71 0.02 3 960 . 107 VAL N N 128.8 0.2 1 961 . 107 VAL H H 9.07 0.02 1 962 . 107 VAL CA C 60.7 0.2 1 963 . 107 VAL HA H 4.3 0.02 1 964 . 107 VAL CB C 34.9 0.2 1 965 . 107 VAL HB H 1.68 0.02 1 966 . 107 VAL HG2 H 0.64 0.02 1 967 . 107 VAL HG1 H 0.46 0.02 1 968 . 107 VAL CG2 C 22 0.2 1 969 . 107 VAL CG1 C 21.2 0.2 1 970 . 108 VAL N N 125.7 0.2 1 971 . 108 VAL H H 8.09 0.02 1 972 . 108 VAL CA C 60.3 0.2 1 973 . 108 VAL HA H 4.96 0.02 1 974 . 108 VAL CB C 32.7 0.2 1 975 . 108 VAL HB H 1.94 0.02 1 976 . 108 VAL HG1 H 1.08 0.02 1 977 . 108 VAL HG2 H 1.08 0.02 1 978 . 108 VAL CG1 C 21.2 0.2 1 979 . 108 VAL CG2 C 21.6 0.2 1 980 . 109 LYS N N 124.4 0.2 1 981 . 109 LYS H H 8.01 0.02 1 982 . 109 LYS CA C 54.7 0.2 1 983 . 109 LYS HA H 4.26 0.02 1 984 . 109 LYS CB C 32.6 0.2 1 985 . 109 LYS HB2 H 2.04 0.02 2 986 . 109 LYS HB3 H 1.87 0.02 2 987 . 110 PRO CD C 49.9 0.2 1 988 . 110 PRO CA C 62.2 0.2 1 989 . 110 PRO HA H 4.46 0.02 1 990 . 110 PRO CB C 34.3 0.2 1 991 . 110 PRO HB2 H 2.26 0.02 2 992 . 110 PRO HB3 H 1.96 0.02 2 993 . 110 PRO CG C 23.8 0.2 1 994 . 110 PRO HG2 H 1.92 0.02 1 995 . 110 PRO HG3 H 1.92 0.02 1 996 . 110 PRO HD2 H 3.67 0.02 2 997 . 110 PRO HD3 H 3.45 0.02 2 998 . 111 PHE N N 114.8 0.2 1 999 . 111 PHE H H 7.73 0.02 1 1000 . 111 PHE CA C 53.8 0.2 1 1001 . 111 PHE HA H 5.45 0.02 1 1002 . 111 PHE CB C 41.3 0.2 1 1003 . 111 PHE HB2 H 3.2 0.02 2 1004 . 111 PHE HB3 H 2.96 0.02 2 1005 . 111 PHE HD1 H 7 0.02 3 1006 . 111 PHE CD1 C 130.3 0.2 3 1007 . 112 THR N N 109.1 0.2 1 1008 . 112 THR H H 8.02 0.02 1 1009 . 112 THR CA C 59.2 0.2 1 1010 . 112 THR HA H 4.57 0.02 1 1011 . 112 THR CB C 68.5 0.2 1 1012 . 112 THR HB H 4.83 0.02 1 1013 . 112 THR HG2 H 1.31 0.02 1 1014 . 112 THR CG2 C 21.6 0.2 1 1015 . 113 ALA N N 123.5 0.2 1 1016 . 113 ALA H H 9.15 0.02 1 1017 . 113 ALA CA C 55.6 0.2 1 1018 . 113 ALA HA H 4 0.02 1 1019 . 113 ALA HB H 1.5 0.02 1 1020 . 113 ALA CB C 17.5 0.2 1 1021 . 114 ALA N N 118.4 0.2 1 1022 . 114 ALA H H 8.28 0.02 1 1023 . 114 ALA CA C 54.7 0.2 1 1024 . 114 ALA HA H 4.23 0.02 1 1025 . 114 ALA HB H 1.48 0.02 1 1026 . 114 ALA CB C 18 0.2 1 1027 . 115 THR N N 116.7 0.2 1 1028 . 115 THR H H 7.9 0.02 1 1029 . 115 THR CA C 65.9 0.2 1 1030 . 115 THR HA H 4.07 0.02 1 1031 . 115 THR CB C 68.5 0.2 1 1032 . 115 THR HB H 4.4 0.02 1 1033 . 115 THR HG2 H 1.3 0.02 1 1034 . 115 THR CG2 C 22 0.2 1 1035 . 116 LEU N N 121.7 0.2 1 1036 . 116 LEU H H 8.06 0.02 1 1037 . 116 LEU CA C 58.1 0.2 1 1038 . 116 LEU HA H 3.74 0.02 1 1039 . 116 LEU CB C 41 0.2 1 1040 . 116 LEU HB2 H 1.99 0.02 2 1041 . 116 LEU HB3 H 1.36 0.02 2 1042 . 116 LEU CG C 26.1 0.2 1 1043 . 116 LEU HG H 1.35 0.02 1 1044 . 116 LEU HD2 H 0.68 0.02 1 1045 . 116 LEU HD1 H 0.46 0.02 1 1046 . 116 LEU CD2 C 25.7 0.2 1 1047 . 116 LEU CD1 C 22 0.2 1 1048 . 117 GLU N N 118.4 0.2 1 1049 . 117 GLU H H 8.76 0.02 1 1050 . 117 GLU CA C 59.2 0.2 1 1051 . 117 GLU HA H 3.86 0.02 1 1052 . 117 GLU CB C 29.6 0.2 1 1053 . 117 GLU HB2 H 2.22 0.02 1 1054 . 117 GLU HB3 H 2.22 0.02 1 1055 . 117 GLU CG C 35.7 0.2 1 1056 . 117 GLU HG2 H 2.29 0.02 1 1057 . 117 GLU HG3 H 2.29 0.02 1 1058 . 118 GLU N N 117.9 0.2 1 1059 . 118 GLU H H 7.88 0.02 1 1060 . 118 GLU CA C 59.3 0.2 1 1061 . 118 GLU HA H 4.09 0.02 1 1062 . 118 GLU CB C 29.3 0.2 1 1063 . 118 GLU HB2 H 2.22 0.02 1 1064 . 118 GLU HB3 H 2.22 0.02 1 1065 . 118 GLU CG C 35.7 0.2 1 1066 . 118 GLU HG2 H 2.47 0.02 1 1067 . 118 GLU HG3 H 2.47 0.02 1 1068 . 119 LYS N N 117.1 0.2 1 1069 . 119 LYS H H 7.91 0.02 1 1070 . 119 LYS CA C 57.5 0.2 1 1071 . 119 LYS HA H 4.01 0.02 1 1072 . 119 LYS CB C 31.2 0.2 1 1073 . 119 LYS HB2 H 1.91 0.02 2 1074 . 119 LYS HB3 H 1.53 0.02 2 1075 . 119 LYS CG C 24.6 0.2 1 1076 . 119 LYS HG2 H 1.29 0.02 1 1077 . 119 LYS HG3 H 1.29 0.02 1 1078 . 119 LYS CD C 27.6 0.2 1 1079 . 119 LYS HD2 H 1.5 0.02 1 1080 . 119 LYS HD3 H 1.5 0.02 1 1081 . 120 LEU N N 118.4 0.2 1 1082 . 120 LEU H H 8.49 0.02 1 1083 . 120 LEU CA C 58.1 0.2 1 1084 . 120 LEU HA H 3.45 0.02 1 1085 . 120 LEU CB C 40.6 0.2 1 1086 . 120 LEU HB2 H 1.63 0.02 2 1087 . 120 LEU HB3 H 0.91 0.02 2 1088 . 120 LEU CG C 26.1 0.2 1 1089 . 120 LEU HG H 1.35 0.02 1 1090 . 120 LEU HD1 H 0.34 0.02 1 1091 . 120 LEU HD2 H 0.15 0.02 1 1092 . 120 LEU CD1 C 25.3 0.2 1 1093 . 120 LEU CD2 C 23.8 0.2 1 1094 . 121 ASN N N 115.4 0.2 1 1095 . 121 ASN H H 8.48 0.02 1 1096 . 121 ASN CA C 56 0.2 1 1097 . 121 ASN HA H 4.57 0.02 1 1098 . 121 ASN CB C 37.5 0.2 1 1099 . 121 ASN HB2 H 3.02 0.02 2 1100 . 121 ASN HB3 H 2.85 0.02 2 1101 . 122 LYS N N 119.4 0.2 1 1102 . 122 LYS H H 7.94 0.02 1 1103 . 122 LYS CA C 58.5 0.2 1 1104 . 122 LYS HA H 4.19 0.02 1 1105 . 122 LYS CB C 31.9 0.2 1 1106 . 122 LYS HB2 H 2.04 0.02 1 1107 . 122 LYS HB3 H 2.04 0.02 1 1108 . 122 LYS CD C 28.7 0.2 1 1109 . 122 LYS HD2 H 1.78 0.02 1 1110 . 122 LYS HD3 H 1.78 0.02 1 1111 . 122 LYS CE C 41.7 0.2 1 1112 . 122 LYS HE2 H 3.04 0.02 1 1113 . 122 LYS HE3 H 3.04 0.02 1 1114 . 123 ILE N N 121.9 0.2 1 1115 . 123 ILE H H 7.68 0.02 1 1116 . 123 ILE CA C 65.5 0.2 1 1117 . 123 ILE HA H 3.74 0.02 1 1118 . 123 ILE CB C 37.5 0.2 1 1119 . 123 ILE HB H 1.91 0.02 1 1120 . 123 ILE HG2 H 0.94 0.02 1 1121 . 123 ILE CG2 C 17.5 0.2 1 1122 . 123 ILE CG1 C 29.4 0.2 1 1123 . 123 ILE HD1 H 0.71 0.02 1 1124 . 123 ILE CD1 C 15.3 0.2 1 1125 . 124 PHE N N 118.4 0.2 1 1126 . 124 PHE H H 9.03 0.02 1 1127 . 124 PHE CA C 58.7 0.2 1 1128 . 124 PHE HA H 4.67 0.02 1 1129 . 124 PHE CB C 37.1 0.2 1 1130 . 124 PHE HB2 H 3.47 0.02 2 1131 . 124 PHE HB3 H 3.32 0.02 2 1132 . 124 PHE HD1 H 7.52 0.02 3 1133 . 124 PHE CD1 C 130.3 0.2 3 1134 . 124 PHE CE1 C 130.7 0.2 3 1135 . 124 PHE HE1 H 7.26 0.02 3 1136 . 124 PHE CZ C 128.4 0.2 1 1137 . 124 PHE HZ H 6.66 0.02 1 1138 . 125 GLU N N 117.6 0.2 1 1139 . 125 GLU H H 8.34 0.02 1 1140 . 125 GLU CA C 58.9 0.2 1 1141 . 125 GLU HA H 4.23 0.02 1 1142 . 125 GLU CB C 29.7 0.2 1 1143 . 125 GLU HB2 H 2.28 0.02 2 1144 . 125 GLU HB3 H 2.21 0.02 2 1145 . 125 GLU CG C 36.1 0.2 1 1146 . 125 GLU HG2 H 2.49 0.02 1 1147 . 125 GLU HG3 H 2.49 0.02 1 1148 . 126 LYS N N 120.2 0.2 1 1149 . 126 LYS H H 7.88 0.02 1 1150 . 126 LYS CA C 58.3 0.2 1 1151 . 126 LYS HA H 4.2 0.02 1 1152 . 126 LYS CB C 32.1 0.2 1 1153 . 126 LYS HB2 H 2.1 0.02 2 1154 . 126 LYS HB3 H 1.95 0.02 2 1155 . 126 LYS CD C 28.3 0.2 1 1156 . 126 LYS HD2 H 1.76 0.02 1 1157 . 126 LYS HD3 H 1.76 0.02 1 1158 . 126 LYS CE C 41.7 0.2 1 1159 . 126 LYS HE2 H 3.04 0.02 1 1160 . 126 LYS HE3 H 3.04 0.02 1 1161 . 127 LEU N N 116.3 0.2 1 1162 . 127 LEU H H 8.04 0.02 1 1163 . 127 LEU CA C 54.7 0.2 1 1164 . 127 LEU HA H 4.43 0.02 1 1165 . 127 LEU CB C 42.4 0.2 1 1166 . 127 LEU HB2 H 1.86 0.02 2 1167 . 127 LEU HB3 H 1.75 0.02 2 1168 . 127 LEU CG C 26.8 0.2 1 1169 . 127 LEU HG H 1.94 0.02 1 1170 . 127 LEU HD1 H 0.96 0.02 1 1171 . 127 LEU HD2 H 0.9 0.02 1 1172 . 127 LEU CD1 C 25.7 0.2 1 1173 . 127 LEU CD2 C 22 0.2 1 1174 . 128 GLY N N 109.9 0.2 1 1175 . 128 GLY H H 7.97 0.02 1 1176 . 128 GLY CA C 46.5 0.2 1 1177 . 129 MET N N 124.1 0.2 1 1178 . 129 MET H H 8.3 0.02 1 1179 . 129 MET CA C 57.1 0.2 1 1180 . 129 MET HA H 4.2 0.02 1 1181 . 129 MET CB C 35.4 0.2 1 1182 . 129 MET HB2 H 2.2 0.02 2 1183 . 129 MET HB3 H 1.85 0.02 2 1184 . 129 MET CG C 32.4 0.2 1 1185 . 129 MET HG2 H 2.6 0.02 2 1186 . 129 MET HG3 H 2.46 0.02 2 stop_ save_