data_4896 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequential Assignment and Secondary Structure of the 14kDa chemotactic Protein CheY2 from Sinorhizobium meliloti ; _BMRB_accession_number 4896 _BMRB_flat_file_name bmr4896.str _Entry_type original _Submission_date 2000-11-08 _Accession_date 2000-11-08 _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 Riepl Hubert . . 2 Scharf Birgit . . 3 Schmitt Ruediger . . 4 Kalbitzer 'Hans Robert' . . 5 Maure Till . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 413 "13C chemical shifts" 344 "15N chemical shifts" 118 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-04-26 original author . stop_ _Original_release_date 2001-04-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Sequential Assignment and Secondary Structure of the 14 kDa Chemotactic Protein CheY2 from Sinorhizobium meliloti ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21228262 _PubMed_ID 11330820 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Riepl Hubert . . 2 Scharf Birgit . . 3 Schmitt Ruediger . . 4 Kalbitzer 'Hans Robert' . . 5 Maure Till . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 19 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 287 _Page_last 288 _Year 2001 _Details . loop_ _Keyword CheY2 NMR 'Protein Structure' stop_ save_ ################################## # Molecular system description # ################################## save_system_CheY2 _Saveframe_category molecular_system _Mol_system_name 'response-regulator protein CheY2' _Abbreviation_common CheY2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CheY2 $CheY2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'response-regulator protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CheY2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'response-regulator protein CheY2' _Abbreviation_common CheY2 _Molecular_mass 14000 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 129 _Mol_residue_sequence ; MSLAEKIKVLIVDDQVTSRL LLGDALQQLGFKQITAAGDG EQGMKIMAQNPHHLVISDFN MPKMDGLGLLQAVRANPATK KAAFIILTAQGDRALVQKAA ALGANNVLAKPFTIEKMKAA IEAVFGALK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 LEU 4 ALA 5 GLU 6 LYS 7 ILE 8 LYS 9 VAL 10 LEU 11 ILE 12 VAL 13 ASP 14 ASP 15 GLN 16 VAL 17 THR 18 SER 19 ARG 20 LEU 21 LEU 22 LEU 23 GLY 24 ASP 25 ALA 26 LEU 27 GLN 28 GLN 29 LEU 30 GLY 31 PHE 32 LYS 33 GLN 34 ILE 35 THR 36 ALA 37 ALA 38 GLY 39 ASP 40 GLY 41 GLU 42 GLN 43 GLY 44 MET 45 LYS 46 ILE 47 MET 48 ALA 49 GLN 50 ASN 51 PRO 52 HIS 53 HIS 54 LEU 55 VAL 56 ILE 57 SER 58 ASP 59 PHE 60 ASN 61 MET 62 PRO 63 LYS 64 MET 65 ASP 66 GLY 67 LEU 68 GLY 69 LEU 70 LEU 71 GLN 72 ALA 73 VAL 74 ARG 75 ALA 76 ASN 77 PRO 78 ALA 79 THR 80 LYS 81 LYS 82 ALA 83 ALA 84 PHE 85 ILE 86 ILE 87 LEU 88 THR 89 ALA 90 GLN 91 GLY 92 ASP 93 ARG 94 ALA 95 LEU 96 VAL 97 GLN 98 LYS 99 ALA 100 ALA 101 ALA 102 LEU 103 GLY 104 ALA 105 ASN 106 ASN 107 VAL 108 LEU 109 ALA 110 LYS 111 PRO 112 PHE 113 THR 114 ILE 115 GLU 116 LYS 117 MET 118 LYS 119 ALA 120 ALA 121 ILE 122 GLU 123 ALA 124 VAL 125 PHE 126 GLY 127 ALA 128 LEU 129 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-09-14 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 PDB 1P6Q "Nmr Structure Of The Response Regulator Chey2 From Sinorhizobium Meliloti, Complexed With Mg++" 100.00 129 100.00 100.00 2.93e-84 PDB 1P6U "Nmr Structure Of The Bef3-Activated Structure Of The Response Regulator Chey2-Mg2+ From Sinorhizobium Meliloti" 100.00 129 100.00 100.00 2.93e-84 EMBL CAC45215 "Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domain [Sinorhizobium meliloti 102" 100.00 129 100.00 100.00 2.93e-84 EMBL CCE94800 "chemotaxis regulator protein CheY-like [Sinorhizobium fredii HH103]" 100.00 129 97.67 99.22 1.03e-82 EMBL CCM66304 "putative chemotaxis protein CheY [Sinorhizobium meliloti Rm41]" 100.00 129 100.00 100.00 2.93e-84 EMBL CDH84541 "putative CheY2 [Sinorhizobium meliloti RU11/001]" 100.00 129 100.00 100.00 2.93e-84 GB AAA86678 "CheY2 [Sinorhizobium meliloti]" 100.00 129 100.00 100.00 2.93e-84 GB ABR59098 "response regulator receiver protein [Sinorhizobium medicae WSM419]" 100.00 129 99.22 100.00 1.14e-83 GB ACP24056 "predicted signal transduction response regulator, contains receiver domain [Sinorhizobium fredii NGR234]" 100.00 129 97.67 99.22 1.03e-82 GB AEG03193 "response regulator receiver protein [Sinorhizobium meliloti BL225C]" 100.00 129 100.00 100.00 2.93e-84 GB AEG52102 "response regulator receiver protein [Sinorhizobium meliloti AK83]" 100.00 129 100.00 100.00 2.93e-84 REF NP_384749 "chemotaxis regulator protein [Sinorhizobium meliloti 1021]" 100.00 129 100.00 100.00 2.93e-84 REF WP_003529938 "MULTISPECIES: chemotaxis protein CheY [Sinorhizobium/Ensifer group]" 100.00 129 100.00 100.00 2.93e-84 REF WP_011974449 "MULTISPECIES: chemotaxis protein CheY [Sinorhizobium]" 100.00 129 99.22 100.00 1.14e-83 REF WP_012706841 "MULTISPECIES: chemotaxis protein CheY [Sinorhizobium/Ensifer group]" 100.00 129 97.67 99.22 1.03e-82 REF WP_018324154 "chemotaxis protein CheY [Rhizobium giardinii]" 100.00 129 98.45 98.45 2.09e-82 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CheY2 'Sinorhizobium meliloti' 382 Eubacteria . Sinorhizobium meliloti stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $CheY2 'recombinant technology' 'E. coli' Escherichia coli ER2566 plasmid pTYB1 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 _Isotopic_labeling $CheY2 1.0 mM [U-15N] 'potassium phosphate' 20 mM . D2O 10 % . 'magnesium chloride' 5 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CheY2 1.0 mM '[U-15N; U-13C]' 'potassium phosphate' 20 mM . D2O 98 % . 'magnesium chloride' 5 mM . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version . loop_ _Task 'data collection and processing' stop_ _Details . save_ save_AURELIA _Saveframe_category software _Name AURELIA _Version . loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label . save_ save_1H-15N_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1H-15N_TOCSY-HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY-HSQC' _Sample_label . save_ save_1H-15N_NOESY-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _Sample_label . save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HCACO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCACO _Sample_label . save_ save_HNCA_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_CBCA(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HBHA(CO)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label . save_ save_HCCH-TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_1H-13C_HSQC_11 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _Sample_label . save_ save_1H-13C_NOESY-HSQC_12 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C NOESY-HSQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCACO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C 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 6.80 0.02 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_ _Experiment_label '1H-1H NOESY' '1H-15N HSQC' '1H-15N TOCSY-HSQC' '1H-15N NOESY-HSQC' HNCO HCACO HNCA CBCA(CO)NH HBHA(CO)NH HCCH-TOCSY '1H-13C HSQC' '1H-13C NOESY-HSQC' stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name CheY2 _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 SER HA H 4.49 0.05 1 2 . 2 SER HB2 H 3.97 0.05 1 3 . 2 SER HB3 H 3.97 0.05 1 4 . 2 SER C C 174.08 0.05 1 5 . 2 SER CA C 59.39 0.05 1 6 . 2 SER CB C 63.45 0.05 1 7 . 3 LEU H H 7.69 0.05 1 8 . 3 LEU HA H 4.04 0.05 1 9 . 3 LEU HB2 H 1.48 0.05 1 10 . 3 LEU HB3 H 1.48 0.05 1 11 . 3 LEU C C 177.70 0.05 1 12 . 3 LEU CA C 55.63 0.05 1 13 . 3 LEU CB C 44.30 0.05 1 14 . 3 LEU N N 120.75 0.05 1 15 . 4 ALA H H 7.99 0.05 1 16 . 4 ALA HA H 4.24 0.05 1 17 . 4 ALA C C 178.22 0.05 1 18 . 4 ALA CA C 55.71 0.05 1 19 . 4 ALA CB C 22.51 0.05 1 20 . 4 ALA N N 120.75 0.05 1 21 . 5 GLU H H 8.35 0.05 1 22 . 5 GLU HA H 3.98 0.05 1 23 . 5 GLU HB2 H 2.13 0.05 2 24 . 5 GLU C C 177.01 0.05 1 25 . 5 GLU CA C 58.59 0.05 1 26 . 5 GLU CB C 29.40 0.05 1 27 . 5 GLU N N 112.40 0.05 1 28 . 6 LYS H H 7.60 0.05 1 29 . 6 LYS HA H 4.26 0.05 1 30 . 6 LYS HB2 H 1.92 0.05 1 31 . 6 LYS HB3 H 1.92 0.05 1 32 . 6 LYS C C 175.98 0.05 1 33 . 6 LYS CA C 56.08 0.05 1 34 . 6 LYS CB C 33.38 0.05 1 35 . 6 LYS N N 116.90 0.05 1 36 . 7 ILE H H 7.15 0.05 1 37 . 7 ILE HA H 4.00 0.05 1 38 . 7 ILE HB H 1.94 0.05 1 39 . 7 ILE C C 175.11 0.05 1 40 . 7 ILE CA C 60.34 0.05 1 41 . 7 ILE CB C 38.11 0.05 1 42 . 7 ILE N N 120.75 0.05 1 43 . 8 LYS H H 11.06 0.05 1 44 . 8 LYS HA H 4.78 0.05 1 45 . 8 LYS HB2 H 1.39 0.05 1 46 . 8 LYS HB3 H 1.39 0.05 1 47 . 8 LYS C C 176.50 0.05 1 48 . 8 LYS CA C 56.20 0.05 1 49 . 8 LYS CB C 33.38 0.05 1 50 . 8 LYS N N 131.67 0.05 1 51 . 9 VAL H H 9.02 0.05 1 52 . 9 VAL HA H 5.18 0.05 1 53 . 9 VAL HB H 1.90 0.05 2 54 . 9 VAL C C 172.71 0.05 1 55 . 9 VAL CA C 60.44 0.05 1 56 . 9 VAL CB C 34.41 0.05 1 57 . 9 VAL N N 125.25 0.05 1 58 . 10 LEU H H 9.27 0.05 1 59 . 10 LEU HA H 5.14 0.05 1 60 . 10 LEU HB2 H 1.67 0.05 1 61 . 10 LEU HB3 H 1.67 0.05 1 62 . 10 LEU C C 174.25 0.05 1 63 . 10 LEU CA C 52.15 0.05 1 64 . 10 LEU CB C 43.88 0.05 1 65 . 10 LEU N N 131.03 0.05 1 66 . 11 ILE H H 9.06 0.05 1 67 . 11 ILE HA H 5.07 0.05 1 68 . 11 ILE HB H 1.66 0.05 1 69 . 11 ILE C C 176.84 0.05 1 70 . 11 ILE CA C 58.88 0.05 1 71 . 11 ILE CB C 40.21 0.05 1 72 . 11 ILE N N 122.04 0.05 1 73 . 12 VAL H H 8.58 0.05 1 74 . 12 VAL HA H 4.73 0.05 1 75 . 12 VAL HB H 2.12 0.05 1 76 . 12 VAL C C 174.42 0.05 1 77 . 12 VAL CA C 59.99 0.05 1 78 . 12 VAL CB C 32.00 0.05 1 79 . 12 VAL N N 123.96 0.05 1 80 . 13 ASP H H 8.02 0.05 1 81 . 13 ASP HA H 4.54 0.05 1 82 . 13 ASP HB2 H 2.69 0.05 2 83 . 13 ASP HB3 H 2.34 0.05 2 84 . 13 ASP C C 175.11 0.05 1 85 . 13 ASP CA C 54.76 0.05 1 86 . 13 ASP CB C 42.73 0.05 1 87 . 13 ASP N N 123.32 0.05 1 88 . 14 ASP H H 9.31 0.05 1 89 . 14 ASP HA H 4.80 0.05 1 90 . 14 ASP HB2 H 2.82 0.05 1 91 . 14 ASP HB3 H 2.82 0.05 1 92 . 14 ASP C C 175.87 0.05 1 93 . 14 ASP CA C 55.46 0.05 1 94 . 14 ASP CB C 41.20 0.05 1 95 . 14 ASP N N 125.89 0.05 1 96 . 15 GLN H H 9.07 0.05 1 97 . 15 GLN HA H 4.55 0.05 1 98 . 15 GLN HB2 H 2.19 0.05 1 99 . 15 GLN HB3 H 2.19 0.05 1 100 . 15 GLN C C 175.63 0.05 1 101 . 15 GLN CA C 54.12 0.05 1 102 . 15 GLN CB C 29.25 0.05 1 103 . 15 GLN N N 121.39 0.05 1 104 . 16 VAL H H 8.62 0.05 1 105 . 16 VAL HA H 3.46 0.05 1 106 . 16 VAL HB H 2.14 0.05 1 107 . 16 VAL C C 177.01 0.05 1 108 . 16 VAL CA C 66.52 0.05 1 109 . 16 VAL CB C 31.67 0.05 1 110 . 16 VAL N N 126.53 0.05 1 111 . 17 THR H H 8.25 0.05 1 112 . 17 THR HA H 4.21 0.05 1 113 . 17 THR HB H 3.89 0.05 1 114 . 17 THR C C 177.01 0.05 1 115 . 17 THR CA C 66.07 0.05 1 116 . 17 THR CB C 68.12 0.05 1 117 . 17 THR N N 111.76 0.05 1 118 . 18 SER H H 7.01 0.05 1 119 . 18 SER HA H 4.32 0.05 1 120 . 18 SER HB2 H 3.99 0.05 2 121 . 18 SER HB3 H 3.12 0.05 2 122 . 18 SER C C 176.84 0.05 1 123 . 18 SER CA C 62.02 0.05 1 124 . 18 SER CB C 62.02 0.05 1 125 . 18 SER N N 114.33 0.05 1 126 . 19 ARG H H 8.11 0.05 1 127 . 19 ARG HA H 3.95 0.05 1 128 . 19 ARG HB2 H 1.94 0.05 2 129 . 19 ARG C C 179.26 0.05 1 130 . 19 ARG CA C 60.49 0.05 1 131 . 19 ARG CB C 31.15 0.05 1 132 . 19 ARG N N 123.96 0.05 1 133 . 20 LEU H H 8.36 0.05 1 134 . 20 LEU HA H 4.15 0.05 1 135 . 20 LEU HB2 H 1.90 0.05 2 136 . 20 LEU HB3 H 1.62 0.05 2 137 . 20 LEU C C 179.43 0.05 1 138 . 20 LEU CA C 57.86 0.05 1 139 . 20 LEU CB C 41.41 0.05 1 140 . 20 LEU N N 119.47 0.05 1 141 . 21 LEU H H 7.59 0.05 1 142 . 21 LEU HA H 4.31 0.05 1 143 . 21 LEU HB2 H 2.26 0.05 2 144 . 21 LEU HB3 H 1.39 0.05 2 145 . 21 LEU C C 176.69 0.05 1 146 . 21 LEU CA C 57.86 0.05 1 147 . 21 LEU CB C 41.22 0.05 1 148 . 21 LEU N N 119.47 0.05 1 149 . 22 LEU H H 7.88 0.05 1 150 . 22 LEU HA H 4.09 0.05 1 151 . 22 LEU HB2 H 1.72 0.05 1 152 . 22 LEU HB3 H 1.72 0.05 1 153 . 22 LEU C C 178.22 0.05 1 154 . 22 LEU CA C 57.86 0.05 1 155 . 22 LEU CB C 41.27 0.05 1 156 . 22 LEU N N 120.75 0.05 1 157 . 23 GLY H H 8.34 0.05 1 158 . 23 GLY HA2 H 4.00 0.05 1 159 . 23 GLY HA3 H 3.54 0.05 1 160 . 23 GLY C C 175.64 0.05 1 161 . 23 GLY CA C 47.64 0.05 1 162 . 23 GLY N N 105.98 0.05 1 163 . 24 ASP H H 8.26 0.05 1 164 . 24 ASP HA H 4.43 0.05 1 165 . 24 ASP HB2 H 2.80 0.05 1 166 . 24 ASP HB3 H 2.80 0.05 1 167 . 24 ASP C C 178.40 0.05 1 168 . 24 ASP CA C 57.51 0.05 1 169 . 24 ASP CB C 41.03 0.05 1 170 . 24 ASP N N 121.39 0.05 1 171 . 25 ALA H H 7.97 0.05 1 172 . 25 ALA HA H 4.14 0.05 1 173 . 25 ALA HB H 1.62 0.05 1 174 . 25 ALA C C 179.42 0.05 1 175 . 25 ALA CA C 55.17 0.05 1 176 . 25 ALA CB C 21.00 0.05 1 177 . 25 ALA N N 122.04 0.05 1 178 . 26 LEU H H 8.33 0.05 1 179 . 26 LEU HA H 4.10 0.05 1 180 . 26 LEU HB2 H 2.01 0.05 2 181 . 26 LEU HB3 H 1.16 0.05 2 182 . 26 LEU C C 180.04 0.05 1 183 . 26 LEU CA C 57.67 0.05 1 184 . 26 LEU CB C 40.86 0.05 1 185 . 26 LEU N N 114.97 0.05 1 186 . 27 GLN H H 8.40 0.05 1 187 . 27 GLN HA H 4.11 0.05 1 188 . 27 GLN HB2 H 2.14 0.05 1 189 . 27 GLN HB3 H 2.14 0.05 1 190 . 27 GLN C C 179.06 0.05 1 191 . 27 GLN CA C 59.76 0.05 1 192 . 27 GLN CB C 33.37 0.05 1 193 . 27 GLN N N 120.11 0.05 1 194 . 28 GLN H H 8.07 0.05 1 195 . 28 GLN HA H 4.12 0.05 1 196 . 28 GLN HB2 H 1.83 0.05 1 197 . 28 GLN HB3 H 1.83 0.05 1 198 . 28 GLN C C 178.22 0.05 1 199 . 28 GLN CA C 59.24 0.05 1 200 . 28 GLN CB C 32.91 0.05 1 201 . 28 GLN N N 120.75 0.05 1 202 . 29 LEU H H 8.79 0.05 1 203 . 29 LEU HA H 4.32 0.05 1 204 . 29 LEU HB2 H 2.25 0.05 2 205 . 29 LEU HB3 H 1.70 0.05 2 206 . 29 LEU C C 175.63 0.05 1 207 . 29 LEU CA C 54.96 0.05 1 208 . 29 LEU CB C 42.67 0.05 1 209 . 29 LEU N N 119.47 0.05 1 210 . 30 GLY H H 7.58 0.05 1 211 . 30 GLY HA2 H 4.17 0.05 2 212 . 30 GLY HA3 H 3.57 0.05 2 213 . 30 GLY C C 174.46 0.05 1 214 . 30 GLY CA C 44.26 0.05 1 215 . 30 GLY N N 103.41 0.05 1 216 . 31 PHE H H 7.88 0.05 1 217 . 31 PHE HA H 4.23 0.05 1 218 . 31 PHE HB2 H 2.69 0.05 1 219 . 31 PHE HB3 H 2.69 0.05 1 220 . 31 PHE C C 175.30 0.05 1 221 . 31 PHE CA C 59.16 0.05 1 222 . 31 PHE CB C 38.46 0.05 1 223 . 31 PHE N N 117.54 0.05 1 224 . 32 LYS H H 8.25 0.05 1 225 . 32 LYS HA H 4.67 0.05 1 226 . 32 LYS HB2 H 2.01 0.05 2 227 . 32 LYS HB3 H 1.72 0.05 2 228 . 32 LYS C C 176.47 0.05 1 229 . 32 LYS CA C 56.20 0.05 1 230 . 32 LYS CB C 36.04 0.05 1 231 . 32 LYS N N 118.18 0.05 1 232 . 33 GLN H H 8.82 0.05 1 233 . 33 GLN HA H 4.63 0.05 1 234 . 33 GLN HB2 H 2.14 0.05 1 235 . 33 GLN HB3 H 2.14 0.05 1 236 . 33 GLN C C 172.90 0.05 1 237 . 33 GLN CA C 55.45 0.05 1 238 . 33 GLN CB C 28.89 0.05 1 239 . 33 GLN N N 122.04 0.05 1 240 . 34 ILE H H 7.73 0.05 1 241 . 34 ILE HA H 5.09 0.05 1 242 . 34 ILE HB H 1.61 0.05 1 243 . 34 ILE C C 175.65 0.05 1 244 . 34 ILE CA C 59.70 0.05 1 245 . 34 ILE CB C 41.28 0.05 1 246 . 34 ILE N N 123.32 0.05 1 247 . 35 THR H H 9.52 0.05 1 248 . 35 THR HA H 4.54 0.05 1 249 . 35 THR HB H 3.77 0.05 1 250 . 35 THR C C 171.64 0.05 1 251 . 35 THR CA C 61.33 0.05 1 252 . 35 THR CB C 68.70 0.05 1 253 . 35 THR N N 127.82 0.05 1 254 . 36 ALA H H 8.73 0.05 1 255 . 36 ALA HA H 5.41 0.05 1 256 . 36 ALA HB H 1.24 0.05 1 257 . 36 ALA C C 175.47 0.05 1 258 . 36 ALA CA C 50.12 0.05 1 259 . 36 ALA CB C 22.05 0.05 1 260 . 36 ALA N N 127.82 0.05 1 261 . 37 ALA H H 9.03 0.05 1 262 . 37 ALA HA H 4.58 0.05 1 263 . 37 ALA HB H 1.28 0.05 1 264 . 37 ALA C C 175.97 0.05 1 265 . 37 ALA CA C 50.09 0.05 1 266 . 37 ALA CB C 22.93 0.05 1 267 . 37 ALA N N 122.04 0.05 1 268 . 38 GLY H H 8.36 0.05 1 269 . 38 GLY HA2 H 4.54 0.05 2 270 . 38 GLY HA3 H 3.67 0.05 2 271 . 38 GLY C C 172.87 0.05 1 272 . 38 GLY CA C 44.82 0.05 1 273 . 38 GLY N N 104.05 0.05 1 274 . 39 ASP H H 7.21 0.05 1 275 . 39 ASP HA H 4.89 0.05 1 276 . 39 ASP HB2 H 3.39 0.05 2 277 . 39 ASP HB3 H 2.96 0.05 2 278 . 39 ASP C C 176.32 0.05 1 279 . 39 ASP CA C 53.98 0.05 1 280 . 39 ASP CB C 42.78 0.05 1 281 . 39 ASP N N 109.83 0.05 1 282 . 40 GLY H H 7.84 0.05 1 283 . 40 GLY HA2 H 3.99 0.05 2 284 . 40 GLY HA3 H 3.67 0.05 2 285 . 40 GLY C C 174.27 0.05 1 286 . 40 GLY CA C 48.47 0.05 1 287 . 40 GLY N N 104.05 0.05 1 288 . 41 GLU H H 8.46 0.05 1 289 . 41 GLU HA H 4.08 0.05 1 290 . 41 GLU HB2 H 2.04 0.05 1 291 . 41 GLU HB3 H 2.04 0.05 1 292 . 41 GLU C C 179.26 0.05 1 293 . 41 GLU CA C 59.81 0.05 1 294 . 41 GLU CB C 29.76 0.05 1 295 . 41 GLU N N 123.32 0.05 1 296 . 42 GLN H H 9.24 0.05 1 297 . 42 GLN HA H 4.00 0.05 1 298 . 42 GLN HB2 H 2.10 0.05 1 299 . 42 GLN HB3 H 2.10 0.05 1 300 . 42 GLN C C 179.16 0.05 1 301 . 42 GLN CA C 58.51 0.05 1 302 . 42 GLN CB C 28.68 0.05 1 303 . 42 GLN N N 121.39 0.05 1 304 . 43 GLY H H 8.25 0.05 1 305 . 43 GLY HA2 H 4.00 0.05 2 306 . 43 GLY HA3 H 3.53 0.05 2 307 . 43 GLY C C 173.39 0.05 1 308 . 43 GLY CA C 47.32 0.05 1 309 . 43 GLY N N 102.77 0.05 1 310 . 44 MET H H 8.30 0.05 1 311 . 44 MET HA H 4.31 0.05 1 312 . 44 MET HB2 H 2.24 0.05 2 313 . 44 MET HB3 H 1.91 0.05 2 314 . 44 MET C C 177.71 0.05 1 315 . 44 MET CA C 57.23 0.05 1 316 . 44 MET CB C 31.38 0.05 1 317 . 44 MET N N 121.39 0.05 1 318 . 45 LYS H H 7.99 0.05 1 319 . 45 LYS HA H 4.02 0.05 1 320 . 45 LYS HB2 H 1.92 0.05 1 321 . 45 LYS HB3 H 1.92 0.05 1 322 . 45 LYS C C 179.96 0.05 1 323 . 45 LYS CA C 59.71 0.05 1 324 . 45 LYS CB C 32.15 0.05 1 325 . 45 LYS N N 120.11 0.05 1 326 . 46 ILE H H 7.86 0.05 1 327 . 46 ILE HA H 3.77 0.05 1 328 . 46 ILE HB H 1.81 0.05 1 329 . 46 ILE C C 177.52 0.05 1 330 . 46 ILE CA C 65.05 0.05 1 331 . 46 ILE CB C 38.06 0.05 1 332 . 46 ILE N N 118.18 0.05 1 333 . 47 MET H H 7.94 0.05 1 334 . 47 MET HA H 4.19 0.05 1 335 . 47 MET HB2 H 2.33 0.05 2 336 . 47 MET HB3 H 2.02 0.05 2 337 . 47 MET C C 176.33 0.05 1 338 . 47 MET CA C 56.74 0.05 1 339 . 47 MET CB C 30.84 0.05 1 340 . 47 MET N N 115.61 0.05 1 341 . 48 ALA H H 8.17 0.05 1 342 . 48 ALA HA H 3.90 0.05 1 343 . 48 ALA HB H 1.48 0.05 1 344 . 48 ALA C C 179.08 0.05 1 345 . 48 ALA CA C 54.16 0.05 1 346 . 48 ALA CB C 21.50 0.05 1 347 . 48 ALA N N 115.61 0.05 1 348 . 49 GLN H H 7.32 0.05 1 349 . 49 GLN HA H 4.35 0.05 1 350 . 49 GLN HB2 H 2.14 0.05 1 351 . 49 GLN HB3 H 2.14 0.05 1 352 . 49 GLN C C 176.15 0.05 1 353 . 49 GLN CA C 56.34 0.05 1 354 . 49 GLN CB C 29.92 0.05 1 355 . 49 GLN N N 113.69 0.05 1 356 . 50 ASN H H 8.55 0.05 1 357 . 50 ASN N N 116.26 0.05 1 358 . 51 PRO HA H 4.54 0.05 1 359 . 51 PRO HB2 H 2.25 0.05 2 360 . 51 PRO HB3 H 1.93 0.05 2 361 . 51 PRO C C 176.49 0.05 1 362 . 51 PRO CA C 65.10 0.05 1 363 . 51 PRO CB C 32.05 0.05 1 364 . 52 HIS H H 7.42 0.05 1 365 . 52 HIS HA H 4.34 0.05 1 366 . 52 HIS HB2 H 3.22 0.05 2 367 . 52 HIS HB3 H 2.80 0.05 2 368 . 52 HIS C C 173.21 0.05 1 369 . 52 HIS CA C 54.63 0.05 1 370 . 52 HIS CB C 29.72 0.05 1 371 . 52 HIS N N 122.04 0.05 1 372 . 53 HIS H H 8.23 0.05 1 373 . 53 HIS HA H 4.52 0.05 1 374 . 53 HIS HB2 H 3.23 0.05 1 375 . 53 HIS HB3 H 3.23 0.05 1 376 . 53 HIS C C 175.29 0.05 1 377 . 53 HIS CA C 59.75 0.05 1 378 . 53 HIS CB C 33.48 0.05 1 379 . 53 HIS N N 118.82 0.05 1 380 . 54 LEU H H 8.07 0.05 1 381 . 54 LEU HA H 5.31 0.05 1 382 . 54 LEU HB2 H 1.62 0.05 1 383 . 54 LEU HB3 H 1.62 0.05 1 384 . 54 LEU C C 172.35 0.05 1 385 . 54 LEU CA C 53.15 0.05 1 386 . 54 LEU CB C 44.79 0.05 1 387 . 54 LEU N N 119.47 0.05 1 388 . 55 VAL H H 9.00 0.05 1 389 . 55 VAL HA H 4.98 0.05 1 390 . 55 VAL HB H 1.48 0.05 1 391 . 55 VAL C C 174.08 0.05 1 392 . 55 VAL CA C 59.77 0.05 1 393 . 55 VAL CB C 33.44 0.05 1 394 . 55 VAL N N 126.53 0.05 1 395 . 56 ILE H H 8.81 0.05 1 396 . 56 ILE HA H 4.78 0.05 1 397 . 56 ILE HB H 1.58 0.05 1 398 . 56 ILE C C 174.08 0.05 1 399 . 56 ILE CA C 59.80 0.05 1 400 . 56 ILE CB C 39.11 0.05 1 401 . 56 ILE N N 125.25 0.05 1 402 . 57 SER H H 8.45 0.05 1 403 . 57 SER N N 118.18 0.05 1 404 . 62 PRO HA H 3.68 0.05 1 405 . 62 PRO HB2 H 2.36 0.05 2 406 . 62 PRO HB3 H 1.80 0.05 2 407 . 62 PRO C C 177.37 0.05 1 408 . 62 PRO CA C 61.90 0.05 1 409 . 62 PRO CB C 31.37 0.05 1 410 . 63 LYS H H 9.24 0.05 1 411 . 63 LYS HA H 4.33 0.05 1 412 . 63 LYS HB2 H 2.14 0.05 2 413 . 63 LYS HB3 H 1.69 0.05 2 414 . 63 LYS C C 173.73 0.05 1 415 . 63 LYS CA C 56.20 0.05 1 416 . 63 LYS CB C 35.98 0.05 1 417 . 63 LYS N N 123.32 0.05 1 418 . 64 MET H H 8.23 0.05 1 419 . 64 MET N N 123.96 0.05 1 420 . 65 ASP HA H 4.56 0.05 1 421 . 65 ASP HB2 H 3.35 0.05 2 422 . 65 ASP HB3 H 2.70 0.05 2 423 . 65 ASP C C 176.50 0.05 1 424 . 65 ASP CA C 53.00 0.05 1 425 . 65 ASP CB C 41.22 0.05 1 426 . 66 GLY H H 9.53 0.05 1 427 . 66 GLY HA2 H 4.36 0.05 2 428 . 66 GLY HA3 H 3.97 0.05 2 429 . 66 GLY C C 176.32 0.05 1 430 . 66 GLY CA C 47.59 0.05 1 431 . 66 GLY N N 102.77 0.05 1 432 . 67 LEU H H 8.05 0.05 1 433 . 67 LEU HA H 4.29 0.05 1 434 . 67 LEU HB2 H 2.15 0.05 2 435 . 67 LEU HB3 H 1.37 0.05 2 436 . 67 LEU C C 179.77 0.05 1 437 . 67 LEU CA C 56.89 0.05 1 438 . 67 LEU CB C 40.42 0.05 1 439 . 67 LEU N N 117.54 0.05 1 440 . 68 GLY H H 8.73 0.05 1 441 . 68 GLY HA2 H 4.22 0.05 2 442 . 68 GLY HA3 H 3.70 0.05 2 443 . 68 GLY C C 174.43 0.05 1 444 . 68 GLY CA C 46.92 0.05 1 445 . 68 GLY N N 111.76 0.05 1 446 . 69 LEU H H 8.57 0.05 1 447 . 69 LEU HA H 4.22 0.05 1 448 . 69 LEU HB2 H 1.71 0.05 1 449 . 69 LEU HB3 H 1.71 0.05 1 450 . 69 LEU C C 180.47 0.05 1 451 . 69 LEU CA C 58.05 0.05 1 452 . 69 LEU CB C 42.19 0.05 1 453 . 69 LEU N N 123.96 0.05 1 454 . 70 LEU H H 8.22 0.05 1 455 . 70 LEU HA H 3.03 0.05 1 456 . 70 LEU HB2 H 1.80 0.05 1 457 . 70 LEU HB3 H 1.80 0.05 1 458 . 70 LEU C C 177.19 0.05 1 459 . 70 LEU CA C 58.16 0.05 1 460 . 70 LEU CB C 40.77 0.05 1 461 . 70 LEU N N 120.75 0.05 1 462 . 71 GLN H H 8.01 0.05 1 463 . 71 GLN HA H 3.89 0.05 1 464 . 71 GLN HB2 H 2.15 0.05 1 465 . 71 GLN HB3 H 2.15 0.05 1 466 . 71 GLN C C 178.40 0.05 1 467 . 71 GLN CA C 59.17 0.05 1 468 . 71 GLN CB C 29.29 0.05 1 469 . 71 GLN N N 115.61 0.05 1 470 . 72 ALA H H 7.97 0.05 1 471 . 72 ALA HA H 4.12 0.05 1 472 . 72 ALA HB H 1.60 0.05 1 473 . 72 ALA C C 180.81 0.05 1 474 . 72 ALA CA C 55.19 0.05 1 475 . 72 ALA CB C 21.54 0.05 1 476 . 72 ALA N N 122.04 0.05 1 477 . 73 VAL H H 8.85 0.05 1 478 . 73 VAL HA H 4.14 0.05 1 479 . 73 VAL HB H 2.02 0.05 1 480 . 73 VAL C C 179.10 0.05 1 481 . 73 VAL CA C 65.42 0.05 1 482 . 73 VAL CB C 31.05 0.05 1 483 . 73 VAL N N 119.47 0.05 1 484 . 74 ARG H H 8.15 0.05 1 485 . 74 ARG HA H 4.10 0.05 1 486 . 74 ARG HB2 H 2.03 0.05 2 487 . 74 ARG HB3 H 1.71 0.05 2 488 . 74 ARG C C 176.32 0.05 1 489 . 74 ARG CA C 57.10 0.05 1 490 . 74 ARG CB C 29.37 0.05 1 491 . 74 ARG N N 115.61 0.05 1 492 . 75 ALA H H 7.52 0.05 1 493 . 75 ALA HA H 4.31 0.05 1 494 . 75 ALA HB H 1.49 0.05 1 495 . 75 ALA C C 177.35 0.05 1 496 . 75 ALA CA C 52.67 0.05 1 497 . 75 ALA CB C 20.50 0.05 1 498 . 75 ALA N N 118.18 0.05 1 499 . 76 ASN H H 6.96 0.05 1 500 . 76 ASN N N 119.47 0.05 1 501 . 77 PRO HA H 4.20 0.05 1 502 . 77 PRO HB2 H 2.47 0.05 2 503 . 77 PRO HB3 H 2.13 0.05 2 504 . 77 PRO C C 177.87 0.05 1 505 . 77 PRO CA C 65.52 0.05 1 506 . 77 PRO CB C 32.18 0.05 1 507 . 78 ALA H H 8.40 0.05 1 508 . 78 ALA HA H 4.41 0.05 1 509 . 78 ALA HB H 1.60 0.05 1 510 . 78 ALA C C 179.25 0.05 1 511 . 78 ALA CA C 53.66 0.05 1 512 . 78 ALA CB C 20.19 0.05 1 513 . 78 ALA N N 116.26 0.05 1 514 . 79 THR H H 7.82 0.05 1 515 . 79 THR HA H 4.64 0.05 1 516 . 79 THR C C 175.76 0.05 1 517 . 79 THR CA C 61.51 0.05 1 518 . 79 THR CB C 69.22 0.05 1 519 . 79 THR N N 104.69 0.05 1 520 . 80 LYS H H 7.47 0.05 1 521 . 80 LYS HA H 4.36 0.05 1 522 . 80 LYS HB2 H 1.94 0.05 1 523 . 80 LYS HB3 H 1.94 0.05 1 524 . 80 LYS C C 177.36 0.05 1 525 . 80 LYS CA C 59.80 0.05 1 526 . 80 LYS CB C 32.59 0.05 1 527 . 80 LYS N N 120.11 0.05 1 528 . 81 LYS H H 8.29 0.05 1 529 . 81 LYS HA H 4.40 0.05 1 530 . 81 LYS HB2 H 2.13 0.05 2 531 . 81 LYS HB3 H 1.78 0.05 2 532 . 81 LYS C C 176.66 0.05 1 533 . 81 LYS CA C 55.76 0.05 1 534 . 81 LYS CB C 31.84 0.05 1 535 . 81 LYS N N 117.54 0.05 1 536 . 82 ALA H H 7.94 0.05 1 537 . 82 ALA HA H 4.22 0.05 1 538 . 82 ALA HB H 1.40 0.05 1 539 . 82 ALA C C 177.89 0.05 1 540 . 82 ALA CA C 53.42 0.05 1 541 . 82 ALA CB C 21.39 0.05 1 542 . 82 ALA N N 122.64 0.05 1 543 . 83 ALA H H 8.34 0.05 1 544 . 83 ALA HA H 4.73 0.05 1 545 . 83 ALA HB H 1.48 0.05 1 546 . 83 ALA C C 176.50 0.05 1 547 . 83 ALA CA C 51.30 0.05 1 548 . 83 ALA CB C 21.52 0.05 1 549 . 83 ALA N N 125.25 0.05 1 550 . 84 PHE H H 9.57 0.05 1 551 . 84 PHE HA H 5.43 0.05 1 552 . 84 PHE HB2 H 3.32 0.05 2 553 . 84 PHE HB3 H 2.50 0.05 2 554 . 84 PHE C C 174.61 0.05 1 555 . 84 PHE CA C 56.24 0.05 1 556 . 84 PHE CB C 45.03 0.05 1 557 . 84 PHE N N 125.25 0.05 1 558 . 85 ILE H H 9.24 0.05 1 559 . 85 ILE HA H 4.79 0.05 1 560 . 85 ILE HB H 1.59 0.05 1 561 . 85 ILE C C 173.73 0.05 1 562 . 85 ILE CA C 59.83 0.05 1 563 . 85 ILE CB C 41.16 0.05 1 564 . 85 ILE N N 129.75 0.05 1 565 . 86 ILE H H 7.96 0.05 1 566 . 86 ILE HA H 5.30 0.05 1 567 . 86 ILE HB H 1.80 0.05 1 568 . 86 ILE C C 173.05 0.05 1 569 . 86 ILE CA C 57.83 0.05 1 570 . 86 ILE CB C 40.11 0.05 1 571 . 86 ILE N N 125.89 0.05 1 572 . 87 LEU H H 8.72 0.05 1 573 . 87 LEU HA H 5.40 0.05 1 574 . 87 LEU HB2 H 1.49 0.05 1 575 . 87 LEU HB3 H 1.49 0.05 1 576 . 87 LEU C C 175.45 0.05 1 577 . 87 LEU CA C 52.61 0.05 1 578 . 87 LEU CB C 43.85 0.05 1 579 . 87 LEU N N 129.10 0.05 1 580 . 88 THR H H 8.49 0.05 1 581 . 88 THR HA H 5.08 0.05 1 582 . 88 THR HB H 4.10 0.05 1 583 . 88 THR C C 172.87 0.05 1 584 . 88 THR CA C 59.41 0.05 1 585 . 88 THR CB C 70.74 0.05 1 586 . 88 THR N N 113.69 0.05 1 587 . 89 ALA H H 9.56 0.05 1 588 . 89 ALA HA H 4.77 0.05 1 589 . 89 ALA HB H 1.60 0.05 1 590 . 89 ALA C C 178.23 0.05 1 591 . 89 ALA CA C 52.10 0.05 1 592 . 89 ALA CB C 19.98 0.05 1 593 . 89 ALA N N 129.10 0.05 1 594 . 90 GLN H H 8.83 0.05 1 595 . 90 GLN HA H 4.38 0.05 1 596 . 90 GLN HB2 H 2.24 0.05 1 597 . 90 GLN HB3 H 2.24 0.05 1 598 . 90 GLN C C 176.32 0.05 1 599 . 90 GLN CA C 56.22 0.05 1 600 . 90 GLN CB C 28.84 0.05 1 601 . 90 GLN N N 120.75 0.05 1 602 . 91 GLY H H 8.64 0.05 1 603 . 91 GLY HA2 H 3.90 0.05 1 604 . 91 GLY HA3 H 3.90 0.05 1 605 . 91 GLY C C 173.90 0.05 1 606 . 91 GLY CA C 45.66 0.05 1 607 . 91 GLY N N 109.83 0.05 1 608 . 92 ASP H H 7.62 0.05 1 609 . 92 ASP HA H 4.68 0.05 1 610 . 92 ASP HB2 H 2.90 0.05 1 611 . 92 ASP HB3 H 2.90 0.05 1 612 . 92 ASP C C 175.80 0.05 1 613 . 92 ASP CA C 53.22 0.05 1 614 . 92 ASP CB C 41.20 0.05 1 615 . 92 ASP N N 120.11 0.05 1 616 . 93 ARG H H 8.43 0.05 1 617 . 93 ARG HA H 4.01 0.05 1 618 . 93 ARG HB2 H 1.93 0.05 1 619 . 93 ARG HB3 H 1.93 0.05 1 620 . 93 ARG C C 178.04 0.05 1 621 . 93 ARG CA C 58.92 0.05 1 622 . 93 ARG CB C 29.98 0.05 1 623 . 93 ARG N N 122.04 0.05 1 624 . 94 ALA H H 8.31 0.05 1 625 . 94 ALA HA H 4.21 0.05 1 626 . 94 ALA HB H 1.48 0.05 1 627 . 94 ALA C C 180.11 0.05 1 628 . 94 ALA CA C 54.73 0.05 1 629 . 94 ALA CB C 21.54 0.05 1 630 . 94 ALA N N 120.75 0.05 1 631 . 95 LEU H H 7.75 0.05 1 632 . 95 LEU HA H 4.00 0.05 1 633 . 95 LEU HB2 H 1.59 0.05 1 634 . 95 LEU HB3 H 1.59 0.05 1 635 . 95 LEU C C 178.25 0.05 1 636 . 95 LEU CA C 57.62 0.05 1 637 . 95 LEU CB C 40.84 0.05 1 638 . 95 LEU N N 120.11 0.05 1 639 . 96 VAL H H 7.68 0.05 1 640 . 96 VAL HA H 3.46 0.05 1 641 . 96 VAL HB H 2.15 0.05 1 642 . 96 VAL C C 178.20 0.05 1 643 . 96 VAL CA C 67.17 0.05 1 644 . 96 VAL CB C 31.42 0.05 1 645 . 96 VAL N N 117.54 0.05 1 646 . 97 GLN H H 7.95 0.05 1 647 . 97 GLN HA H 4.53 0.05 1 648 . 97 GLN HB2 H 2.32 0.05 1 649 . 97 GLN HB3 H 2.32 0.05 1 650 . 97 GLN C C 180.99 0.05 1 651 . 97 GLN CA C 59.27 0.05 1 652 . 97 GLN CB C 28.18 0.05 1 653 . 97 GLN N N 116.90 0.05 1 654 . 98 LYS H H 8.24 0.05 1 655 . 98 LYS HA H 4.11 0.05 1 656 . 98 LYS HB2 H 2.35 0.05 1 657 . 98 LYS HB3 H 2.35 0.05 1 658 . 98 LYS C C 178.10 0.05 1 659 . 98 LYS CA C 59.11 0.05 1 660 . 98 LYS CB C 28.32 0.05 1 661 . 98 LYS N N 120.75 0.05 1 662 . 99 ALA H H 7.67 0.05 1 663 . 99 ALA HA H 4.14 0.05 1 664 . 99 ALA HB H 1.56 0.05 1 665 . 99 ALA C C 179.43 0.05 1 666 . 99 ALA CA C 54.68 0.05 1 667 . 99 ALA CB C 21.74 0.05 1 668 . 99 ALA N N 116.90 0.05 1 669 . 100 ALA H H 7.59 0.05 1 670 . 100 ALA HA H 3.76 0.05 1 671 . 100 ALA HB H 1.27 0.05 1 672 . 100 ALA C C 179.45 0.05 1 673 . 100 ALA CA C 54.69 0.05 1 674 . 100 ALA CB C 22.07 0.05 1 675 . 100 ALA N N 116.26 0.05 1 676 . 101 ALA H H 8.03 0.05 1 677 . 101 ALA HA H 4.20 0.05 1 678 . 101 ALA HB H 1.58 0.05 1 679 . 101 ALA C C 181.33 0.05 1 680 . 101 ALA CA C 55.10 0.05 1 681 . 101 ALA CB C 22.05 0.05 1 682 . 101 ALA N N 119.47 0.05 1 683 . 102 LEU H H 7.85 0.05 1 684 . 102 LEU HA H 4.31 0.05 1 685 . 102 LEU HB2 H 2.24 0.05 2 686 . 102 LEU HB3 H 1.70 0.05 2 687 . 102 LEU C C 176.67 0.05 1 688 . 102 LEU CA C 54.77 0.05 1 689 . 102 LEU CB C 42.72 0.05 1 690 . 102 LEU N N 121.39 0.05 1 691 . 103 GLY H H 7.59 0.05 1 692 . 103 GLY HA2 H 4.23 0.05 2 693 . 103 GLY HA3 H 3.82 0.05 2 694 . 103 GLY C C 175.98 0.05 1 695 . 103 GLY CA C 45.84 0.05 1 696 . 103 GLY N N 103.41 0.05 1 697 . 104 ALA H H 8.56 0.05 1 698 . 104 ALA HA H 4.11 0.05 1 699 . 104 ALA HB H 1.27 0.05 1 700 . 104 ALA C C 176.67 0.05 1 701 . 104 ALA CA C 53.10 0.05 1 702 . 104 ALA CB C 21.89 0.05 1 703 . 104 ALA N N 123.96 0.05 1 704 . 105 ASN H H 9.37 0.05 1 705 . 105 ASN HA H 4.61 0.05 1 706 . 105 ASN HB2 H 2.89 0.05 2 707 . 105 ASN HB3 H 2.23 0.05 2 708 . 105 ASN C C 174.66 0.05 1 709 . 105 ASN CA C 56.17 0.05 1 710 . 105 ASN CB C 39.07 0.05 1 711 . 105 ASN N N 120.11 0.05 1 712 . 106 ASN H H 7.77 0.05 1 713 . 106 ASN HA H 4.78 0.05 1 714 . 106 ASN HB2 H 2.80 0.05 2 715 . 106 ASN HB3 H 2.36 0.05 2 716 . 106 ASN C C 172.87 0.05 1 717 . 106 ASN CA C 52.04 0.05 1 718 . 106 ASN CB C 41.86 0.05 1 719 . 106 ASN N N 111.12 0.05 1 720 . 107 VAL H H 8.47 0.05 1 721 . 107 VAL HA H 4.99 0.05 1 722 . 107 VAL HB H 2.03 0.05 1 723 . 107 VAL C C 173.90 0.05 1 724 . 107 VAL CA C 60.96 0.05 1 725 . 107 VAL CB C 33.87 0.05 1 726 . 107 VAL N N 118.18 0.05 1 727 . 108 LEU H H 9.18 0.05 1 728 . 108 LEU HA H 4.65 0.05 1 729 . 108 LEU HB2 H 1.55 0.05 2 730 . 108 LEU HB3 H 1.26 0.05 2 731 . 108 LEU C C 174.26 0.05 1 732 . 108 LEU CA C 53.27 0.05 1 733 . 108 LEU CB C 45.54 0.05 1 734 . 108 LEU N N 127.18 0.05 1 735 . 109 ALA H H 8.24 0.05 1 736 . 109 ALA HA H 4.97 0.05 1 737 . 109 ALA HB H 1.34 0.05 1 738 . 109 ALA C C 176.66 0.05 1 739 . 109 ALA CA C 51.05 0.05 1 740 . 109 ALA CB C 19.98 0.05 1 741 . 109 ALA N N 124.61 0.05 1 742 . 110 LYS H H 7.63 0.05 1 743 . 110 LYS N N 118.82 0.05 1 744 . 111 PRO HA H 4.54 0.05 1 745 . 111 PRO HB2 H 2.34 0.05 2 746 . 111 PRO C C 175.44 0.05 1 747 . 111 PRO CA C 62.05 0.05 1 748 . 111 PRO CB C 34.32 0.05 1 749 . 112 PHE H H 7.82 0.05 1 750 . 112 PHE HA H 5.12 0.05 1 751 . 112 PHE HB2 H 3.23 0.05 1 752 . 112 PHE HB3 H 3.23 0.05 1 753 . 112 PHE C C 174.76 0.05 1 754 . 112 PHE CA C 55.78 0.05 1 755 . 112 PHE CB C 40.34 0.05 1 756 . 112 PHE N N 118.18 0.05 1 757 . 113 THR H H 7.31 0.05 1 758 . 113 THR HA H 4.75 0.05 1 759 . 113 THR C C 175.81 0.05 1 760 . 113 THR CA C 58.84 0.05 1 761 . 113 THR CB C 71.29 0.05 1 762 . 113 THR N N 109.19 0.05 1 763 . 114 ILE H H 9.29 0.05 1 764 . 114 ILE HA H 3.90 0.05 1 765 . 114 ILE HB H 2.04 0.05 1 766 . 114 ILE C C 177.02 0.05 1 767 . 114 ILE CA C 64.97 0.05 1 768 . 114 ILE CB C 37.2 0.05 1 769 . 114 ILE N N 124.61 0.05 1 770 . 115 GLU H H 8.93 0.05 1 771 . 115 GLU HA H 4.08 0.05 1 772 . 115 GLU HB2 H 2.07 0.05 1 773 . 115 GLU HB3 H 2.07 0.05 1 774 . 115 GLU C C 179.77 0.05 1 775 . 115 GLU CA C 60.40 0.05 1 776 . 115 GLU CB C 28.91 0.05 1 777 . 115 GLU N N 119.47 0.05 1 778 . 116 LYS H H 7.73 0.05 1 779 . 116 LYS HA H 4.00 0.05 1 780 . 116 LYS HB2 H 2.04 0.05 1 781 . 116 LYS HB3 H 2.04 0.05 1 782 . 116 LYS C C 179.62 0.05 1 783 . 116 LYS CA C 58.90 0.05 1 784 . 116 LYS CB C 32.76 0.05 1 785 . 116 LYS N N 119.47 0.05 1 786 . 117 MET H H 8.26 0.05 1 787 . 117 MET HA H 4.23 0.05 1 788 . 117 MET HB2 H 2.14 0.05 1 789 . 117 MET HB3 H 2.14 0.05 1 790 . 117 MET C C 176.84 0.05 1 791 . 117 MET CA C 57.83 0.05 1 792 . 117 MET CB C 31.50 0.05 1 793 . 117 MET N N 120.11 0.05 1 794 . 118 LYS H H 9.01 0.05 1 795 . 118 LYS HA H 3.71 0.05 1 796 . 118 LYS HB2 H 1.93 0.05 1 797 . 118 LYS HB3 H 1.93 0.05 1 798 . 118 LYS C C 177.53 0.05 1 799 . 118 LYS CA C 60.51 0.05 1 800 . 118 LYS CB C 32.86 0.05 1 801 . 118 LYS N N 119.47 0.05 1 802 . 119 ALA H H 7.79 0.05 1 803 . 119 ALA HA H 4.31 0.05 1 804 . 119 ALA HB H 1.58 0.05 1 805 . 119 ALA C C 180.59 0.05 1 806 . 119 ALA CA C 54.67 0.05 1 807 . 119 ALA CB C 21.36 0.05 1 808 . 119 ALA N N 118.18 0.05 1 809 . 120 ALA H H 7.87 0.05 1 810 . 120 ALA HA H 4.22 0.05 1 811 . 120 ALA HB H 1.48 0.05 1 812 . 120 ALA C C 179.61 0.05 1 813 . 120 ALA CA C 54.41 0.05 1 814 . 120 ALA CB C 21.11 0.05 1 815 . 120 ALA N N 120.11 0.05 1 816 . 121 ILE H H 8.11 0.05 1 817 . 121 ILE HA H 3.68 0.05 1 818 . 121 ILE HB H 1.91 0.05 1 819 . 121 ILE C C 179.26 0.05 1 820 . 121 ILE CA C 65.80 0.05 1 821 . 121 ILE CB C 38.32 0.05 1 822 . 121 ILE N N 116.90 0.05 1 823 . 122 GLU H H 9.14 0.05 1 824 . 122 GLU HA H 4.39 0.05 1 825 . 122 GLU HB2 H 2.13 0.05 2 826 . 122 GLU HB3 H 1.74 0.05 2 827 . 122 GLU C C 179.80 0.05 1 828 . 122 GLU CA C 58.99 0.05 1 829 . 122 GLU CB C 29.30 0.05 1 830 . 122 GLU N N 120.75 0.05 1 831 . 123 ALA H H 7.81 0.05 1 832 . 123 ALA HA H 4.20 0.05 1 833 . 123 ALA HB H 1.58 0.05 1 834 . 123 ALA C C 178.42 0.05 1 835 . 123 ALA CA C 54.65 0.05 1 836 . 123 ALA CB C 21.52 0.05 1 837 . 123 ALA N N 120.75 0.05 1 838 . 124 VAL H H 7.22 0.05 1 839 . 124 VAL HA H 3.89 0.05 1 840 . 124 VAL HB H 1.94 0.05 1 841 . 124 VAL C C 177.17 0.05 1 842 . 124 VAL CA C 64.11 0.05 1 843 . 124 VAL CB C 32.89 0.05 1 844 . 124 VAL N N 114.33 0.05 1 845 . 125 PHE H H 8.11 0.05 1 846 . 125 PHE HA H 4.34 0.05 1 847 . 125 PHE HB2 H 2.14 0.05 1 848 . 125 PHE HB3 H 2.14 0.05 1 849 . 125 PHE C C 176.15 0.05 1 850 . 125 PHE CA C 59.74 0.05 1 851 . 125 PHE CB C 41.70 0.05 1 852 . 125 PHE N N 114.33 0.05 1 853 . 126 GLY H H 8.51 0.05 1 854 . 126 GLY HA2 H 4.31 0.05 2 855 . 126 GLY HA3 H 3.68 0.05 2 856 . 126 GLY C C 170.80 0.05 1 857 . 126 GLY CA C 43.80 0.05 1 858 . 126 GLY N N 109.83 0.05 1 859 . 127 ALA H H 7.78 0.05 1 860 . 127 ALA HA H 4.01 0.05 1 861 . 127 ALA HB H 1.38 0.05 1 862 . 127 ALA C C 179.25 0.05 1 863 . 127 ALA CA C 52.63 0.05 1 864 . 127 ALA CB C 20.46 0.05 1 865 . 127 ALA N N 118.18 0.05 1 866 . 128 LEU H H 9.19 0.05 1 867 . 128 LEU HA H 4.21 0.05 1 868 . 128 LEU HB2 H 1.82 0.05 2 869 . 128 LEU HB3 H 1.49 0.05 2 870 . 128 LEU C C 176.33 0.05 1 871 . 128 LEU CA C 55.67 0.05 1 872 . 128 LEU CB C 42.17 0.05 1 873 . 128 LEU N N 122.04 0.05 1 874 . 129 LYS H H 7.52 0.05 1 875 . 129 LYS N N 123.96 0.05 1 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