data_4348 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C Chemical Shift Assignments for NtrC-C-term-3Ala ; _BMRB_accession_number 4348 _BMRB_flat_file_name bmr4348.str _Entry_type original _Submission_date 1999-05-18 _Accession_date 1999-05-19 _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 Pelton Jeffrey G. . 2 Kustu Sydney . . 3 Wemmer David E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 330 "13C chemical shifts" 281 "15N chemical shifts" 77 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-10-06 original author . stop_ _Original_release_date 1999-10-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Pelton, J. G., Kustu, S., and Wemmer, D. E., "Solution Structure of the DNA-binding Domain of NtrC with Three Alanine Substitutions," J. Mol. Biol., in preparation. ; _Citation_title ; Solution Structure of the DNA-binding Domain of NtrC with Three Alanine Substitutions ; _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pelton Jeffrey G. . 2 Kustu Sydney . . 3 Wemmer David E. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume . _Journal_issue na _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword 'DNA-binding protein' FIS 'four-helix bundle' helix-turn-helix 'NMR spectroscopy' 'protein structure' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Porter, S. C., North, A. K., Wedel, A. B., Kustu, S. (1993). Oligomerization of NtrC at the GlnA Enhancer Is Required for Transcriptional Activation. Genes Dev. 7, 2258-2273. ; _Citation_title 'Oligomerization of NTRC at the glnA enhancer is required for transcriptional activation.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 7901122 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Porter 'S C' C. . 2 North 'A K' K. . 3 Wedel 'A B' B. . 4 Kustu S . . stop_ _Journal_abbreviation 'Genes Dev.' _Journal_name_full 'Genes & development' _Journal_volume 7 _Journal_issue 11 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 2258 _Page_last 2273 _Year 1993 _Details ; To activate transcription of the glnA gene, the dimeric NTRC protein (nitrogen regulatory protein C) of enteric bacteria binds to an enhancer located approximately 100 bp upstream of the promoter. The enhancer is composed of two binding sites for NTRC that are three turns of the DNA helix apart. One role of the enhancer is to tether NTRC in high local concentration near the promoter to allow for its frequent interaction with sigma 54 holoenzyme by DNA looping. We have found that a second role of the enhancer is to ensure oligomerization of NTRC into a complex of at least two dimers that is required for transcriptional activation. Formation of this complex is greatly facilitated by a protein-protein interaction between NTRC dimers that is increased when the protein is phosphorylated. ; save_ ################################## # Molecular system description # ################################## save_system_NtrC-C-term-3Ala _Saveframe_category molecular_system _Mol_system_name 'Nitrogen Regulatory protein C-C-term-3Ala' _Abbreviation_common NtrC-C-term-3Ala _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'NtrC-C-term-3Ala subunit 1' $NtrC 'NtrC-C-term-3Ala subunit 2' $NtrC stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'NtrC-C-term-3Ala subunit 1' 1 'NtrC-C-term-3Ala subunit 2' stop_ loop_ _Biological_function DNA-binding stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_NtrC _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Nitrogen regulatory protein C' _Name_variant NtrC-C-term-3Ala _Abbreviation_common NtrC _Molecular_mass 19962 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 91 _Mol_residue_sequence ; MDLPGELFEASTPDSPSHLP PDSWATLLAQWADRALRSGH QNLLSEAQPELERTLLTTAL RHTQGHKQEAARLLGWGAAT LTAKLKELGME ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 LEU 4 PRO 5 GLY 6 GLU 7 LEU 8 PHE 9 GLU 10 ALA 11 SER 12 THR 13 PRO 14 ASP 15 SER 16 PRO 17 SER 18 HIS 19 LEU 20 PRO 21 PRO 22 ASP 23 SER 24 TRP 25 ALA 26 THR 27 LEU 28 LEU 29 ALA 30 GLN 31 TRP 32 ALA 33 ASP 34 ARG 35 ALA 36 LEU 37 ARG 38 SER 39 GLY 40 HIS 41 GLN 42 ASN 43 LEU 44 LEU 45 SER 46 GLU 47 ALA 48 GLN 49 PRO 50 GLU 51 LEU 52 GLU 53 ARG 54 THR 55 LEU 56 LEU 57 THR 58 THR 59 ALA 60 LEU 61 ARG 62 HIS 63 THR 64 GLN 65 GLY 66 HIS 67 LYS 68 GLN 69 GLU 70 ALA 71 ALA 72 ARG 73 LEU 74 LEU 75 GLY 76 TRP 77 GLY 78 ALA 79 ALA 80 THR 81 LEU 82 THR 83 ALA 84 LYS 85 LEU 86 LYS 87 GLU 88 LEU 89 GLY 90 MET 91 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-02 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 1NTC "Solution Structure Of The Dna-Binding Domain Of Ntrc With Three Alanine Substitutions" 100.00 91 100.00 100.00 1.36e-55 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $NtrC 'Salmonella typhimurium' 602 Eubacteria . Salmonella typhimurium 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 _Details $NtrC 'recombinant technology' 'E. coli' Escherichia coli pLys-S plasmid pJES1092 ; Reference for plasmid: Porter, S. C., North, A. K., Wedel, A. B., Kustu, S.1993 Genes Dev. 7, 2258-2273 C-terminus of NtrC with 3 alanine substitutions R456A, N457A, R461A ; 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 $NtrC . mM 0.5 1.5 '[U-98% 13C; U-95% 15N]' sodium_phosphate 20 mM . . . potassium_chloride 50 mM . . . EDTA 0.1 mM . . . sodium_azide 0.02 'w/v %' . . . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N__NOESY-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _Sample_label . save_ save_1H-15N__TOCSY-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY-HSQC' _Sample_label . save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HCACO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HCACO _Sample_label . save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name HA(CO)NH _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HCACO _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 HA(CO)NH _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 6.1 0.2 n/a temperature 308 2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details ; proton chemical shifts were referenced indirectly to DSS using the water peak as 4.73 ppm at 37C ; 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 C 13 'methyl protons' ppm 0 internal indirect . . . 0.25144953 water H 1 protons ppm 4.73 internal direct . internal . . DSS N 15 'methyl protons' ppm 0 internal indirect . . . 0.101329118 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_NtrC-C-term-3Ala _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N NOESY-HSQC' '1H-15N TOCSY-HSQC' HNCA HCACO HNCO HA(CO)NH stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'NtrC-C-term-3Ala subunit 1' _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 . 5 GLY H H 8.35 0.02 1 2 . 5 GLY N N 108.8 0.2 1 3 . 5 GLY HA2 H 3.93 0.02 2 4 . 5 GLY CA C 45.5 0.2 1 5 . 5 GLY C C 174.2 0.2 1 6 . 6 GLU H H 8.19 0.02 1 7 . 6 GLU N N 120 0.2 1 8 . 6 GLU HA H 4.26 0.02 1 9 . 6 GLU CA C 56.7 0.2 1 10 . 6 GLU C C 176.3 0.2 1 11 . 7 LEU H H 8.1 0.02 1 12 . 7 LEU N N 122 0.2 1 13 . 7 LEU HA H 4.3 0.02 1 14 . 7 LEU CA C 55.2 0.2 1 15 . 7 LEU HG H 1.56 0.02 1 16 . 7 LEU CG C 26.8 0.2 1 17 . 7 LEU HD1 H 0.93 0.02 1 18 . 7 LEU CD1 C 24.8 0.2 1 19 . 7 LEU HD2 H 0.86 0.02 1 20 . 7 LEU CD2 C 23.4 0.2 1 21 . 7 LEU C C 176.8 0.2 1 22 . 8 PHE H H 8.09 0.02 1 23 . 8 PHE N N 120.4 0.2 1 24 . 8 PHE HA H 4.62 0.02 1 25 . 8 PHE CA C 57.6 0.2 1 26 . 8 PHE HB2 H 3.05 0.02 2 27 . 8 PHE HB3 H 3.17 0.02 2 28 . 8 PHE CB C 39.7 0.2 1 29 . 8 PHE C C 175.4 0.2 1 30 . 9 GLU H H 8.21 0.02 1 31 . 9 GLU N N 122.5 0.2 1 32 . 9 GLU HA H 4.26 0.02 1 33 . 9 GLU CA C 56.3 0.2 1 34 . 9 GLU C C 175.7 0.2 1 35 . 10 ALA H H 8.21 0.02 1 36 . 10 ALA N N 125.1 0.2 1 37 . 10 ALA HA H 4.36 0.02 1 38 . 10 ALA CA C 52.5 0.2 1 39 . 10 ALA HB H 1.45 0.02 1 40 . 10 ALA CB C 19.3 0.2 1 41 . 10 ALA C C 177.5 0.2 1 42 . 11 SER H H 8.23 0.02 1 43 . 11 SER N N 114.8 0.2 1 44 . 11 SER HA H 4.5 0.02 1 45 . 11 SER CA C 58.3 0.2 1 46 . 11 SER HB2 H 3.86 0.02 2 47 . 11 SER C C 174.3 0.2 1 48 . 12 THR H H 8.31 0.02 1 49 . 12 THR N N 117.1 0.2 1 50 . 12 THR HA H 4.71 0.02 1 51 . 12 THR CA C 59.6 0.2 1 52 . 12 THR HB H 4.26 0.02 1 53 . 12 THR CB C 69.6 0.2 1 54 . 12 THR HG2 H 1.27 0.02 1 55 . 12 THR CG2 C 21.1 0.2 1 56 . 22 ASP H H 8.2 0.02 1 57 . 22 ASP N N 115.8 0.2 1 58 . 22 ASP HA H 4.62 0.02 1 59 . 22 ASP CA C 55.1 0.2 1 60 . 22 ASP HB2 H 2.65 0.02 2 61 . 22 ASP HB3 H 2.71 0.02 2 62 . 22 ASP C C 176.4 0.2 1 63 . 23 SER H H 8.28 0.02 1 64 . 23 SER N N 115 0.2 1 65 . 23 SER HA H 4.67 0.02 1 66 . 23 SER CA C 58.4 0.2 1 67 . 23 SER C C 175.8 0.2 1 68 . 24 TRP H H 8.41 0.02 1 69 . 24 TRP N N 122.5 0.2 1 70 . 24 TRP HA H 4.42 0.02 1 71 . 24 TRP CA C 60 0.2 1 72 . 24 TRP HB2 H 3.86 0.02 2 73 . 24 TRP HB3 H 3.15 0.02 2 74 . 24 TRP CB C 27.9 0.2 1 75 . 24 TRP HD1 H 7.34 0.02 1 76 . 24 TRP CD1 C 127.6 0.2 1 77 . 24 TRP HE3 H 7.38 0.02 1 78 . 24 TRP CE3 C 119.4 0.2 1 79 . 24 TRP HZ2 H 6.87 0.02 1 80 . 24 TRP CZ2 C 114.2 0.2 1 81 . 24 TRP HZ3 H 6.71 0.02 1 82 . 24 TRP CZ3 C 121.1 0.2 1 83 . 24 TRP HH2 H 7.01 0.02 1 84 . 24 TRP CH2 C 123.5 0.2 1 85 . 24 TRP C C 177.1 0.2 1 86 . 25 ALA H H 6.99 0.02 1 87 . 25 ALA N N 124.2 0.2 1 88 . 25 ALA HA H 3.49 0.02 1 89 . 25 ALA CA C 54.9 0.2 1 90 . 25 ALA HB H 0.51 0.02 1 91 . 25 ALA CB C 16.6 0.2 1 92 . 25 ALA C C 179.5 0.2 1 93 . 26 THR H H 7.63 0.02 1 94 . 26 THR N N 116 0.2 1 95 . 26 THR HA H 3.97 0.02 1 96 . 26 THR CA C 66.1 0.2 1 97 . 26 THR HB H 4.3 0.02 1 98 . 26 THR CB C 68.3 0.2 1 99 . 26 THR HG2 H 1.26 0.02 1 100 . 26 THR CG2 C 22 0.2 1 101 . 26 THR C C 177.1 0.2 1 102 . 27 LEU H H 7.39 0.02 1 103 . 27 LEU N N 121.8 0.2 1 104 . 27 LEU HA H 4.37 0.02 1 105 . 27 LEU CA C 57.6 0.2 1 106 . 27 LEU HB2 H 1.88 0.02 2 107 . 27 LEU HB3 H 1.99 0.02 2 108 . 27 LEU CB C 41.5 0.2 1 109 . 27 LEU HG H 1.9 0.02 1 110 . 27 LEU CG C 27.9 0.2 1 111 . 27 LEU HD1 H 1 0.02 1 112 . 27 LEU CD1 C 25.5 0.2 1 113 . 27 LEU HD2 H 0.91 0.02 1 114 . 27 LEU CD2 C 23.4 0.2 1 115 . 27 LEU C C 179.5 0.2 1 116 . 28 LEU H H 8.37 0.02 1 117 . 28 LEU N N 124.6 0.2 1 118 . 28 LEU HA H 3.82 0.02 1 119 . 28 LEU CA C 58.1 0.2 1 120 . 28 LEU HB2 H 1.99 0.02 2 121 . 28 LEU HB3 H 1.12 0.02 2 122 . 28 LEU CB C 40.8 0.2 1 123 . 28 LEU HG H 1.14 0.02 1 124 . 28 LEU CG C 26.8 0.2 1 125 . 28 LEU HD1 H -0.56 0.02 1 126 . 28 LEU CD1 C 20.7 0.2 1 127 . 28 LEU HD2 H 0.69 0.02 1 128 . 28 LEU CD2 C 27.5 0.2 1 129 . 28 LEU C C 177.8 0.2 1 130 . 29 ALA H H 7.96 0.02 1 131 . 29 ALA N N 121.8 0.2 1 132 . 29 ALA HA H 3.8 0.02 1 133 . 29 ALA CA C 55.4 0.2 1 134 . 29 ALA HB H 1.51 0.02 1 135 . 29 ALA CB C 17.7 0.2 1 136 . 29 ALA C C 179.7 0.2 1 137 . 30 GLN H H 7.48 0.02 1 138 . 30 GLN N N 117 0.2 1 139 . 30 GLN HA H 4.18 0.02 1 140 . 30 GLN CA C 59.1 0.2 1 141 . 30 GLN HG2 H 2.49 0.02 2 142 . 30 GLN HG3 H 2.75 0.02 2 143 . 30 GLN CG C 34.1 0.2 1 144 . 30 GLN C C 178.9 0.2 1 145 . 31 TRP H H 8.59 0.02 1 146 . 31 TRP N N 122.6 0.2 1 147 . 31 TRP HA H 4.04 0.02 1 148 . 31 TRP CA C 62.1 0.2 1 149 . 31 TRP HB2 H 3.62 0.02 2 150 . 31 TRP HB3 H 3.76 0.02 2 151 . 31 TRP CB C 28.1 0.2 1 152 . 31 TRP HD1 H 7.46 0.02 1 153 . 31 TRP CD1 C 127.5 0.2 1 154 . 31 TRP HE3 H 7.46 0.02 1 155 . 31 TRP CE3 C 121.1 0.2 1 156 . 31 TRP HZ2 H 7.59 0.02 1 157 . 31 TRP CZ2 C 114.3 0.2 1 158 . 31 TRP HZ3 H 6.65 0.02 1 159 . 31 TRP CZ3 C 119.8 0.2 1 160 . 31 TRP HH2 H 7.16 0.02 1 161 . 31 TRP CH2 C 123.7 0.2 1 162 . 31 TRP HE1 H 10.33 0.02 1 163 . 31 TRP NE1 N 130.5 0.2 1 164 . 31 TRP C C 178.9 0.2 1 165 . 32 ALA H H 9.02 0.02 1 166 . 32 ALA N N 122 0.2 1 167 . 32 ALA HA H 3.05 0.02 1 168 . 32 ALA CA C 54.3 0.2 1 169 . 32 ALA HB H 1.36 0.02 1 170 . 32 ALA CB C 18.4 0.2 1 171 . 32 ALA C C 178.1 0.2 1 172 . 33 ASP H H 8.24 0.02 1 173 . 33 ASP N N 118.4 0.2 1 174 . 33 ASP HA H 4.1 0.02 1 175 . 33 ASP CA C 57.7 0.2 1 176 . 33 ASP HB2 H 2.78 0.02 2 177 . 33 ASP CB C 42.5 0.2 1 178 . 33 ASP C C 177.7 0.2 1 179 . 34 ARG H H 7.52 0.02 1 180 . 34 ARG N N 117.4 0.2 1 181 . 34 ARG HA H 3.79 0.02 1 182 . 34 ARG CA C 59.5 0.2 1 183 . 34 ARG HD2 H 3.26 0.02 2 184 . 34 ARG CD C 43.6 0.2 1 185 . 34 ARG C C 179.2 0.2 1 186 . 35 ALA H H 8.18 0.02 1 187 . 35 ALA N N 123.8 0.2 1 188 . 35 ALA HA H 3.45 0.02 1 189 . 35 ALA CA C 54.7 0.2 1 190 . 35 ALA HB H 0.42 0.02 1 191 . 35 ALA CB C 16.6 0.2 1 192 . 35 ALA C C 180.3 0.2 1 193 . 36 LEU H H 8.41 0.02 1 194 . 36 LEU N N 118.9 0.2 1 195 . 36 LEU HA H 3.94 0.02 1 196 . 36 LEU CA C 57.5 0.2 1 197 . 36 LEU HB2 H 0.3 0.02 2 198 . 36 LEU HB3 H 1.51 0.02 2 199 . 36 LEU CB C 40.4 0.2 2 200 . 36 LEU HG H 1.43 0.02 1 201 . 36 LEU CG C 28.2 0.2 1 202 . 36 LEU HD1 H 0.45 0.02 1 203 . 36 LEU CD1 C 25.5 0.2 1 204 . 36 LEU HD2 H 0.74 0.02 1 205 . 36 LEU CD2 C 24.2 0.2 1 206 . 36 LEU C C 181.4 0.2 1 207 . 37 ARG H H 8.09 0.02 1 208 . 37 ARG N N 119.5 0.2 1 209 . 37 ARG HA H 4.19 0.02 1 210 . 37 ARG CA C 59.1 0.2 1 211 . 37 ARG C C 177.4 0.2 1 212 . 38 SER H H 7.61 0.02 1 213 . 38 SER N N 112.3 0.2 1 214 . 38 SER HA H 4.68 0.02 1 215 . 38 SER CA C 58.2 0.2 1 216 . 38 SER C C 174.6 0.2 1 217 . 39 GLY H H 7.64 0.02 1 218 . 39 GLY N N 107.6 0.2 1 219 . 39 GLY HA2 H 4.22 0.02 2 220 . 39 GLY HA3 H 3.86 0.02 2 221 . 39 GLY CA C 46 0.2 1 222 . 39 GLY C C 175.1 0.2 1 223 . 40 HIS H H 8.18 0.02 1 224 . 40 HIS N N 118.8 0.2 1 225 . 40 HIS HA H 4.53 0.02 1 226 . 40 HIS CA C 56.7 0.2 1 227 . 40 HIS HB2 H 3.06 0.02 2 228 . 40 HIS HB3 H 2.62 0.02 2 229 . 40 HIS CB C 29.4 0.2 1 230 . 40 HIS C C 174.3 0.2 1 231 . 41 GLN H H 8.32 0.02 1 232 . 41 GLN N N 117.2 0.2 1 233 . 41 GLN HA H 4.54 0.02 1 234 . 41 GLN CA C 54.6 0.2 1 235 . 41 GLN C C 174.5 0.2 1 236 . 42 ASN H H 8 0.02 1 237 . 42 ASN N N 116.2 0.2 1 238 . 42 ASN HA H 4.18 0.02 1 239 . 42 ASN CA C 53.5 0.2 1 240 . 42 ASN HB2 H 2.82 0.02 2 241 . 42 ASN HB3 H 3.18 0.02 2 242 . 42 ASN CB C 37.1 0.2 1 243 . 42 ASN C C 176.9 0.2 1 244 . 43 LEU H H 8.52 0.02 1 245 . 43 LEU N N 117.7 0.2 1 246 . 43 LEU HA H 4.1 0.02 1 247 . 43 LEU CA C 58.4 0.2 1 248 . 43 LEU HB2 H 1.63 0.02 2 249 . 43 LEU CB C 43.7 0.2 1 250 . 43 LEU HG H 1.81 0.02 1 251 . 43 LEU CG C 27.1 0.2 1 252 . 43 LEU HD1 H 0.7 0.02 1 253 . 43 LEU CD1 C 25.2 0.2 1 254 . 43 LEU HD2 H 0.59 0.02 1 255 . 43 LEU CD2 C 22.9 0.2 1 256 . 43 LEU C C 180.1 0.2 1 257 . 44 LEU H H 8.31 0.02 1 258 . 44 LEU N N 117.6 0.2 1 259 . 44 LEU HA H 4 0.02 1 260 . 44 LEU CA C 58.6 0.2 1 261 . 44 LEU HB2 H 1.68 0.02 2 262 . 44 LEU HB3 H 1.76 0.02 2 263 . 44 LEU CB C 41.1 0.2 1 264 . 44 LEU HG H 1.49 0.02 1 265 . 44 LEU CG C 27.8 0.2 1 266 . 44 LEU HD1 H 0.46 0.02 1 267 . 44 LEU CD1 C 24.8 0.2 1 268 . 44 LEU HD2 H 0.82 0.02 1 269 . 44 LEU CD2 C 24.5 0.2 1 270 . 44 LEU C C 178.6 0.2 1 271 . 45 SER H H 7.78 0.02 1 272 . 45 SER N N 113 0.2 1 273 . 45 SER HA H 4.31 0.02 1 274 . 45 SER CA C 61 0.2 1 275 . 45 SER C C 174.9 0.2 1 276 . 46 GLU H H 7.32 0.02 1 277 . 46 GLU N N 118 0.2 1 278 . 46 GLU HA H 4.58 0.02 1 279 . 46 GLU CA C 57.6 0.2 1 280 . 46 GLU HB2 H 2.47 0.02 2 281 . 46 GLU CB C 31 0.2 1 282 . 46 GLU HG2 H 2.45 0.02 2 283 . 46 GLU HG3 H 2.61 0.02 2 284 . 46 GLU CG C 36.6 0.2 1 285 . 46 GLU C C 178 0.2 1 286 . 47 ALA H H 8.28 0.02 1 287 . 47 ALA N N 120.4 0.2 1 288 . 47 ALA HA H 4.39 0.02 1 289 . 47 ALA CA C 54.9 0.2 1 290 . 47 ALA HB H 1.41 0.02 1 291 . 47 ALA CB C 20.3 0.2 1 292 . 47 ALA C C 178.1 0.2 1 293 . 48 GLN H H 8.94 0.02 1 294 . 48 GLN N N 118 0.2 1 295 . 48 GLN HA H 4.2 0.02 1 296 . 48 GLN CA C 61.2 0.2 1 297 . 48 GLN HB2 H 2.36 0.02 2 298 . 48 GLN HB3 H 2.41 0.02 2 299 . 48 GLN CB C 25.2 0.2 1 300 . 48 GLN HG2 H 2.34 0.02 2 301 . 48 GLN HG3 H 2.45 0.02 2 302 . 48 GLN CG C 33.3 0.2 1 303 . 49 PRO HA H 4.47 0.02 1 304 . 49 PRO CA C 66 0.2 1 305 . 49 PRO HD2 H 3.67 0.02 2 306 . 49 PRO HD3 H 3.82 0.02 2 307 . 49 PRO CD C 50.8 0.2 1 308 . 49 PRO C C 178.5 0.2 1 309 . 50 GLU H H 6.73 0.02 1 310 . 50 GLU N N 116.1 0.2 1 311 . 50 GLU HA H 4.17 0.02 1 312 . 50 GLU CA C 58.7 0.2 1 313 . 50 GLU HB2 H 2.03 0.02 2 314 . 50 GLU HB3 H 2.17 0.02 2 315 . 50 GLU CB C 29.4 0.2 1 316 . 50 GLU HG2 H 1.82 0.02 2 317 . 50 GLU HG3 H 1.9 0.02 2 318 . 50 GLU CG C 35.2 0.2 1 319 . 51 LEU H H 8.44 0.02 1 320 . 51 LEU N N 124.4 0.2 1 321 . 51 LEU HA H 3.82 0.02 1 322 . 51 LEU CA C 59.2 0.2 1 323 . 51 LEU HB2 H 1.9 0.02 2 324 . 51 LEU HB3 H 2.43 0.02 2 325 . 51 LEU CB C 41.7 0.2 1 326 . 51 LEU HG H 1.55 0.02 1 327 . 51 LEU CG C 26.6 0.2 1 328 . 51 LEU HD1 H 0.94 0.02 1 329 . 51 LEU CD1 C 27.8 0.2 1 330 . 51 LEU HD2 H 1.02 0.02 1 331 . 51 LEU CD2 C 26.6 0.2 1 332 . 51 LEU C C 178.1 0.2 1 333 . 52 GLU H H 8.52 0.02 1 334 . 52 GLU N N 118.1 0.2 1 335 . 52 GLU HA H 3.71 0.02 1 336 . 52 GLU CA C 60.9 0.2 1 337 . 52 GLU HB2 H 2.19 0.02 2 338 . 52 GLU HB3 H 2.45 0.02 2 339 . 52 GLU CB C 30.7 0.2 1 340 . 52 GLU C C 178.2 0.2 1 341 . 53 ARG H H 9.1 0.02 1 342 . 53 ARG N N 118.3 0.2 1 343 . 53 ARG HA H 3.92 0.02 1 344 . 53 ARG CA C 60.3 0.2 1 345 . 53 ARG HB2 H 1.92 0.02 2 346 . 53 ARG HB3 H 2.08 0.02 2 347 . 53 ARG CB C 30.5 0.2 1 348 . 53 ARG C C 179.5 0.2 1 349 . 54 THR H H 8.12 0.02 1 350 . 54 THR N N 117.6 0.2 1 351 . 54 THR HA H 3.86 0.02 1 352 . 54 THR CA C 67.5 0.2 1 353 . 54 THR HB H 4.16 0.02 1 354 . 54 THR CB C 67.9 0.2 1 355 . 54 THR HG2 H 1.12 0.02 1 356 . 54 THR CG2 C 21 0.2 1 357 . 55 LEU H H 8.33 0.02 1 358 . 55 LEU N N 122.3 0.2 1 359 . 55 LEU HA H 3.81 0.02 1 360 . 55 LEU CA C 58.6 0.2 1 361 . 55 LEU HB2 H 1.2 0.02 2 362 . 55 LEU HB3 H 1.8 0.02 2 363 . 55 LEU CB C 40.6 0.2 1 364 . 55 LEU HG H 1.98 0.02 1 365 . 55 LEU CG C 27 0.2 1 366 . 55 LEU HD1 H 0.78 0.02 1 367 . 55 LEU CD1 C 25.9 0.2 1 368 . 55 LEU HD2 H 0.77 0.02 1 369 . 55 LEU CD2 C 23.7 0.2 1 370 . 55 LEU C C 178 0.2 1 371 . 56 LEU H H 8.82 0.02 1 372 . 56 LEU N N 120.6 0.2 1 373 . 56 LEU HA H 4 0.02 1 374 . 56 LEU CA C 58.8 0.2 1 375 . 56 LEU HB2 H 1.72 0.02 2 376 . 56 LEU HB3 H 1.86 0.02 2 377 . 56 LEU CB C 41.8 0.2 1 378 . 56 LEU HG H 1.68 0.02 1 379 . 56 LEU CG C 27.7 0.2 1 380 . 56 LEU HD1 H 0.98 0.02 1 381 . 56 LEU CD1 C 23.9 0.2 1 382 . 56 LEU HD2 H 1.05 0.02 1 383 . 56 LEU CD2 C 26.2 0.2 1 384 . 56 LEU C C 178.6 0.2 1 385 . 57 THR H H 8.39 0.02 1 386 . 57 THR N N 114.1 0.2 1 387 . 57 THR HA H 3.81 0.02 1 388 . 57 THR CA C 67.3 0.2 1 389 . 57 THR HB H 4.31 0.02 1 390 . 57 THR CB C 68.2 0.2 1 391 . 57 THR HG2 H 1.29 0.02 1 392 . 57 THR CG2 C 21.2 0.2 1 393 . 57 THR C C 177.1 0.2 1 394 . 58 THR H H 7.77 0.02 1 395 . 58 THR N N 117.9 0.2 1 396 . 58 THR HA H 3.86 0.02 1 397 . 58 THR CA C 67.7 0.2 1 398 . 58 THR HB H 4.1 0.02 1 399 . 58 THR CB C 68.4 0.2 1 400 . 58 THR HG2 H 1.26 0.02 1 401 . 58 THR CG2 C 20.9 0.2 1 402 . 58 THR C C 176.2 0.2 1 403 . 59 ALA H H 8.68 0.02 1 404 . 59 ALA N N 124.5 0.2 1 405 . 59 ALA HA H 3.94 0.02 1 406 . 59 ALA CA C 55.8 0.2 1 407 . 59 ALA HB H 1.45 0.02 1 408 . 59 ALA CB C 18.1 0.2 1 409 . 59 ALA C C 178.9 0.2 1 410 . 60 LEU H H 8.57 0.02 1 411 . 60 LEU N N 117.1 0.2 1 412 . 60 LEU HA H 4.11 0.02 1 413 . 60 LEU CA C 57.4 0.2 1 414 . 60 LEU HB2 H 1.43 0.02 2 415 . 60 LEU HB3 H 1.92 0.02 2 416 . 60 LEU CB C 41.7 0.2 1 417 . 60 LEU HG H 1.68 0.02 1 418 . 60 LEU CG C 27.6 0.2 1 419 . 60 LEU HD1 H 0.85 0.02 1 420 . 60 LEU CD1 C 25.8 0.2 1 421 . 60 LEU HD2 H 0.72 0.02 1 422 . 60 LEU CD2 C 23.7 0.2 1 423 . 60 LEU C C 179.5 0.2 1 424 . 61 ARG H H 7.79 0.02 1 425 . 61 ARG N N 119.7 0.2 1 426 . 61 ARG HA H 4.15 0.02 1 427 . 61 ARG CA C 59.5 0.2 1 428 . 61 ARG C C 180 0.2 1 429 . 62 HIS H H 8.07 0.02 1 430 . 62 HIS N N 120.1 0.2 1 431 . 62 HIS HA H 4.28 0.02 1 432 . 62 HIS CA C 60 0.2 1 433 . 62 HIS HB2 H 3.38 0.02 2 434 . 62 HIS HB3 H 3.21 0.02 2 435 . 62 HIS CB C 31.2 0.2 1 436 . 62 HIS C C 176.8 0.2 1 437 . 63 THR H H 8.15 0.02 1 438 . 63 THR N N 106.4 0.2 1 439 . 63 THR HA H 4.48 0.02 1 440 . 63 THR CA C 61 0.2 1 441 . 63 THR HB H 4.91 0.02 1 442 . 63 THR CB C 68.3 0.2 1 443 . 63 THR HG2 H 1.31 0.02 1 444 . 63 THR CG2 C 22.2 0.2 1 445 . 63 THR C C 175 0.2 1 446 . 64 GLN H H 7.84 0.02 1 447 . 64 GLN N N 118.5 0.2 1 448 . 64 GLN HA H 3.98 0.02 1 449 . 64 GLN CA C 56.8 0.2 1 450 . 64 GLN HG2 H 2.33 0.02 2 451 . 64 GLN CG C 34.2 0.2 1 452 . 64 GLN C C 176.3 0.2 1 453 . 65 GLY H H 8.99 0.02 1 454 . 65 GLY N N 103.9 0.2 1 455 . 65 GLY HA2 H 4.14 0.02 2 456 . 65 GLY HA3 H 3.41 0.02 2 457 . 65 GLY CA C 45.4 0.2 1 458 . 65 GLY C C 173.9 0.2 1 459 . 66 HIS H H 7.59 0.02 1 460 . 66 HIS N N 120.3 0.2 1 461 . 66 HIS HA H 3.57 0.02 1 462 . 66 HIS CA C 56.2 0.2 1 463 . 66 HIS HB2 H 3.26 0.02 2 464 . 66 HIS HB3 H 3.56 0.02 2 465 . 66 HIS CB C 29.1 0.2 1 466 . 67 LYS HA H 3.79 0.02 1 467 . 67 LYS CA C 61.1 0.2 1 468 . 67 LYS C C 177.5 0.2 1 469 . 68 GLN H H 8.82 0.02 1 470 . 68 GLN N N 118.9 0.2 1 471 . 68 GLN HA H 4.05 0.02 1 472 . 68 GLN CA C 60 0.2 1 473 . 68 GLN HB2 H 2.23 0.02 2 474 . 68 GLN HB3 H 2.28 0.02 2 475 . 68 GLN CB C 27.8 0.2 1 476 . 68 GLN HG2 H 2.54 0.02 2 477 . 68 GLN CG C 34.5 0.2 1 478 . 68 GLN C C 179.2 0.2 1 479 . 69 GLU H H 8.6 0.02 1 480 . 69 GLU N N 120.2 0.2 1 481 . 69 GLU HA H 4.29 0.02 1 482 . 69 GLU CA C 58.9 0.2 1 483 . 69 GLU HB2 H 2.05 0.02 2 484 . 69 GLU HB3 H 1.95 0.02 2 485 . 69 GLU CB C 30.7 0.2 1 486 . 69 GLU HG2 H 2.25 0.02 2 487 . 69 GLU CG C 34.1 0.2 1 488 . 69 GLU C C 178.3 0.2 1 489 . 70 ALA H H 7.88 0.02 1 490 . 70 ALA N N 121 0.2 1 491 . 70 ALA HA H 3.9 0.02 1 492 . 70 ALA CA C 55.5 0.2 1 493 . 70 ALA HB H 1.41 0.02 1 494 . 70 ALA CB C 17.6 0.2 1 495 . 70 ALA C C 178.4 0.2 1 496 . 71 ALA H H 8.23 0.02 1 497 . 71 ALA N N 118.4 0.2 1 498 . 71 ALA HA H 3.95 0.02 1 499 . 71 ALA CA C 56 0.2 1 500 . 71 ALA HB H 1.72 0.02 1 501 . 71 ALA CB C 17.7 0.2 1 502 . 71 ALA C C 179.5 0.2 1 503 . 72 ARG H H 7.68 0.02 1 504 . 72 ARG N N 118.4 0.2 1 505 . 72 ARG HA H 4.2 0.02 1 506 . 72 ARG CA C 59.4 0.2 1 507 . 72 ARG HB2 H 2.06 0.02 2 508 . 72 ARG CB C 30.1 0.2 1 509 . 72 ARG C C 179.6 0.2 1 510 . 73 LEU H H 7.8 0.02 1 511 . 73 LEU N N 118.1 0.2 1 512 . 73 LEU HA H 4.15 0.02 1 513 . 73 LEU CA C 57.4 0.2 1 514 . 73 LEU HB2 H 1.42 0.02 2 515 . 73 LEU HB3 H 1.98 0.02 2 516 . 73 LEU CB C 41 0.2 1 517 . 73 LEU HD1 H 1 0.02 1 518 . 73 LEU CD1 C 26.2 0.2 1 519 . 73 LEU HD2 H 0.97 0.02 1 520 . 73 LEU CD2 C 22 0.2 1 521 . 73 LEU C C 177.8 0.2 1 522 . 74 LEU H H 7.67 0.02 1 523 . 74 LEU N N 117.2 0.2 1 524 . 74 LEU HA H 3.95 0.02 1 525 . 74 LEU CA C 56.7 0.2 1 526 . 74 LEU HB2 H 1.35 0.02 2 527 . 74 LEU HB3 H 0.74 0.02 2 528 . 74 LEU CB C 42 0.2 1 529 . 74 LEU HG H 1.72 0.02 1 530 . 74 LEU CG C 26 0.2 1 531 . 74 LEU HD1 H 0.46 0.02 1 532 . 74 LEU CD1 C 25.5 0.2 1 533 . 74 LEU HD2 H 0.36 0.02 1 534 . 74 LEU CD2 C 23.8 0.2 1 535 . 74 LEU C C 176.1 0.2 1 536 . 75 GLY H H 8.06 0.02 1 537 . 75 GLY N N 104.7 0.2 1 538 . 75 GLY HA2 H 4.42 0.02 2 539 . 75 GLY HA3 H 3.85 0.02 2 540 . 75 GLY CA C 45.2 0.2 1 541 . 75 GLY C C 174.6 0.2 1 542 . 76 TRP H H 7.96 0.02 1 543 . 76 TRP N N 121.4 0.2 1 544 . 76 TRP HA H 5.33 0.02 1 545 . 76 TRP CA C 53.4 0.2 1 546 . 76 TRP HB2 H 3.33 0.02 2 547 . 76 TRP HB3 H 3.07 0.02 2 548 . 76 TRP CB C 32.8 0.2 1 549 . 76 TRP HD1 H 7.2 0.02 1 550 . 76 TRP CD1 C 124.7 0.2 1 551 . 76 TRP HE3 H 7.13 0.02 1 552 . 76 TRP CE3 C 118.5 0.2 1 553 . 76 TRP HZ2 H 7.32 0.02 1 554 . 76 TRP CZ2 C 114.2 0.2 1 555 . 76 TRP HZ3 H 6.88 0.02 1 556 . 76 TRP CZ3 C 120.8 0.2 1 557 . 76 TRP HH2 H 6.89 0.02 1 558 . 76 TRP CH2 C 122.8 0.2 1 559 . 76 TRP HE1 H 10.17 0.02 1 560 . 76 TRP NE1 N 129.2 0.2 1 561 . 76 TRP C C 177 0.2 1 562 . 77 GLY H H 8.53 0.02 1 563 . 77 GLY N N 106.6 0.2 1 564 . 77 GLY HA2 H 4.39 0.02 2 565 . 77 GLY HA3 H 3.98 0.02 2 566 . 77 GLY CA C 44.3 0.2 1 567 . 77 GLY C C 175 0.2 1 568 . 78 ALA H H 8.74 0.02 1 569 . 78 ALA N N 124 0.2 1 570 . 78 ALA HA H 4 0.02 1 571 . 78 ALA CA C 56 0.2 1 572 . 78 ALA HB H 1.54 0.02 1 573 . 78 ALA CB C 18.1 0.2 1 574 . 79 ALA HA H 4.22 0.02 1 575 . 79 ALA CA C 55 0.2 1 576 . 79 ALA HB H 1.48 0.02 1 577 . 79 ALA CB C 17.7 0.2 1 578 . 79 ALA C C 180.8 0.2 1 579 . 80 THR H H 7.52 0.02 1 580 . 80 THR N N 116.9 0.2 1 581 . 80 THR HA H 3.8 0.02 1 582 . 80 THR CA C 65.8 0.2 1 583 . 80 THR HB H 3.96 0.02 1 584 . 80 THR CB C 68.7 0.2 1 585 . 80 THR HG2 H 0.33 0.02 1 586 . 80 THR CG2 C 21.1 0.2 1 587 . 80 THR C C 175 0.2 1 588 . 81 LEU H H 7.92 0.02 1 589 . 81 LEU N N 121.3 0.2 1 590 . 81 LEU HA H 3.86 0.02 1 591 . 81 LEU CA C 59.5 0.2 1 592 . 81 LEU HB2 H 1.71 0.02 2 593 . 81 LEU HB3 H 2.17 0.02 2 594 . 81 LEU CB C 41.1 0.2 1 595 . 81 LEU HG H 1.82 0.02 1 596 . 81 LEU CG C 27.5 0.2 1 597 . 81 LEU HD1 H 1.11 0.02 1 598 . 81 LEU CD1 C 25.6 0.2 1 599 . 81 LEU HD2 H 1.02 0.02 1 600 . 81 LEU CD2 C 26.3 0.2 1 601 . 81 LEU C C 177.5 0.2 1 602 . 82 THR H H 8.06 0.02 1 603 . 82 THR N N 113.9 0.2 1 604 . 82 THR HA H 3.74 0.02 1 605 . 82 THR CA C 67.3 0.2 1 606 . 82 THR HB H 4.22 0.02 1 607 . 82 THR CB C 68.7 0.2 1 608 . 82 THR HG2 H 1.29 0.02 1 609 . 82 THR CG2 C 21.8 0.2 1 610 . 82 THR C C 176.1 0.2 1 611 . 83 ALA H H 7.46 0.02 1 612 . 83 ALA N N 123.1 0.2 1 613 . 83 ALA HA H 4.11 0.02 1 614 . 83 ALA CA C 55.1 0.2 1 615 . 83 ALA HB H 1.47 0.02 1 616 . 83 ALA CB C 17.9 0.2 1 617 . 83 ALA C C 180.8 0.2 1 618 . 84 LYS H H 8.46 0.02 1 619 . 84 LYS N N 120.4 0.2 1 620 . 84 LYS HA H 3.93 0.02 1 621 . 84 LYS CA C 57.5 0.2 1 622 . 84 LYS C C 178.5 0.2 1 623 . 85 LEU H H 8.37 0.02 1 624 . 85 LEU N N 118.7 0.2 1 625 . 85 LEU HA H 3.9 0.02 1 626 . 85 LEU CA C 58.7 0.2 1 627 . 85 LEU HB2 H 1.36 0.02 2 628 . 85 LEU HB3 H 2.01 0.02 2 629 . 85 LEU CB C 41.7 0.2 1 630 . 85 LEU HD1 H 0.93 0.02 1 631 . 85 LEU CD1 C 26.5 0.2 1 632 . 85 LEU HD2 H 0.93 0.02 1 633 . 85 LEU CD2 C 24 0.2 1 634 . 85 LEU C C 179 0.2 1 635 . 86 LYS H H 7.06 0.02 1 636 . 86 LYS N N 116.1 0.2 1 637 . 86 LYS HA H 4.26 0.02 1 638 . 86 LYS CA C 58.6 0.2 1 639 . 86 LYS HB2 H 2.02 0.02 2 640 . 86 LYS CB C 32 0.2 1 641 . 86 LYS C C 180.1 0.2 1 642 . 87 GLU H H 8.34 0.02 1 643 . 87 GLU N N 122.1 0.2 1 644 . 87 GLU HA H 3.98 0.02 1 645 . 87 GLU CA C 59.3 0.2 1 646 . 87 GLU HB2 H 2.14 0.02 2 647 . 87 GLU HB3 H 2.2 0.02 2 648 . 87 GLU CB C 30.7 0.2 1 649 . 87 GLU HG2 H 2.2 0.02 2 650 . 87 GLU HG3 H 2.44 0.02 2 651 . 87 GLU CG C 36 0.2 1 652 . 87 GLU C C 178.1 0.2 1 653 . 88 LEU H H 8.39 0.02 1 654 . 88 LEU N N 114.5 0.2 1 655 . 88 LEU HA H 4.4 0.02 1 656 . 88 LEU CA C 54.5 0.2 1 657 . 88 LEU HB2 H 1.85 0.02 2 658 . 88 LEU HB3 H 1.6 0.02 2 659 . 88 LEU CB C 42.3 0.2 1 660 . 88 LEU HG H 1.96 0.02 1 661 . 88 LEU CG C 27.2 0.2 1 662 . 88 LEU HD1 H 0.97 0.02 1 663 . 88 LEU CD1 C 26.2 0.2 1 664 . 88 LEU HD2 H 1.09 0.02 1 665 . 88 LEU CD2 C 22.2 0.2 1 666 . 88 LEU C C 177.6 0.2 1 667 . 89 GLY H H 7.77 0.02 1 668 . 89 GLY N N 108.5 0.2 1 669 . 89 GLY HA2 H 4.04 0.02 2 670 . 89 GLY HA3 H 4.06 0.02 2 671 . 89 GLY CA C 46.8 0.2 1 672 . 89 GLY C C 175.2 0.2 1 673 . 90 MET H H 8.33 0.02 1 674 . 90 MET N N 118.1 0.2 1 675 . 90 MET HA H 4.43 0.02 1 676 . 90 MET CA C 56 0.2 1 677 . 90 MET C C 174.7 0.2 1 678 . 91 GLU H H 7.64 0.02 1 679 . 91 GLU N N 124.2 0.2 1 680 . 91 GLU HA H 4.06 0.02 1 681 . 91 GLU CA C 57.9 0.2 1 682 . 91 GLU HB2 H 1.82 0.02 2 683 . 91 GLU HB3 H 2.02 0.02 2 684 . 91 GLU CB C 33.2 0.2 1 685 . 91 GLU HG2 H 2.12 0.02 2 686 . 91 GLU HG3 H 2.18 0.02 2 687 . 91 GLU CG C 37.2 0.2 1 688 . 91 GLU C C 180.3 0.2 1 stop_ save_