data_19377 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N, 13C Backbone and 13Cbeta Chemical Shift Assignment of mouse Interleukin-10 ; _BMRB_accession_number 19377 _BMRB_flat_file_name bmr19377.str _Entry_type original _Submission_date 2013-07-19 _Accession_date 2013-07-19 _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 Kuenze Georg . . 2 Theisgen Stephan . . 3 Huster Daniel . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 214 "13C chemical shifts" 457 "15N chemical shifts" 152 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-07-23 original author . stop_ _Original_release_date 2013-07-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone 1H, 15N, 13C and side chain 13Cbeta NMR chemical shift assignment of murine interleukin-10' _Citation_status submitted _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 Kuenze Georg . . 2 Theisgen Stephan . . 3 Huster Daniel . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'IL10 dimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'IL-10, Chain A' $IL-10 'IL-10, Chain B' $IL-10 N-terminus $IL-10 stop_ _System_molecular_weight 40320 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'IL-10, Chain A' 1 'IL-10, Chain B' 2 N-terminus stop_ _Database_query_date . _Details dimer save_ ######################## # Monomeric polymers # ######################## save_IL-10 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common IL-10 _Molecular_mass 20160 _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function 'Cytokine, immune system' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 170 _Mol_residue_sequence ; SRGQYSREDNNCTHFPVGQS HMLLELRTAFSQVKTFFQTK DQLDNILLTDSLMQDFKGYL GCQALSEMIQFYLVEVMPQA EKHGPEIKEHLNSLGEKLKT LRMRLRRCHRFLPCENKSKA VEQVKSDFNKLQDQGVYKAM NEFDIFINYIEAYMMIKMKS LEHHHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 SER 2 ARG 3 GLY 4 GLN 5 TYR 6 SER 7 ARG 8 GLU 9 ASP 10 ASN 11 ASN 12 CYS 13 THR 14 HIS 15 PHE 16 PRO 17 VAL 18 GLY 19 GLN 20 SER 21 HIS 22 MET 23 LEU 24 LEU 25 GLU 26 LEU 27 ARG 28 THR 29 ALA 30 PHE 31 SER 32 GLN 33 VAL 34 LYS 35 THR 36 PHE 37 PHE 38 GLN 39 THR 40 LYS 41 ASP 42 GLN 43 LEU 44 ASP 45 ASN 46 ILE 47 LEU 48 LEU 49 THR 50 ASP 51 SER 52 LEU 53 MET 54 GLN 55 ASP 56 PHE 57 LYS 58 GLY 59 TYR 60 LEU 61 GLY 62 CYS 63 GLN 64 ALA 65 LEU 66 SER 67 GLU 68 MET 69 ILE 70 GLN 71 PHE 72 TYR 73 LEU 74 VAL 75 GLU 76 VAL 77 MET 78 PRO 79 GLN 80 ALA 81 GLU 82 LYS 83 HIS 84 GLY 85 PRO 86 GLU 87 ILE 88 LYS 89 GLU 90 HIS 91 LEU 92 ASN 93 SER 94 LEU 95 GLY 96 GLU 97 LYS 98 LEU 99 LYS 100 THR 101 LEU 102 ARG 103 MET 104 ARG 105 LEU 106 ARG 107 ARG 108 CYS 109 HIS 110 ARG 111 PHE 112 LEU 113 PRO 114 CYS 115 GLU 116 ASN 117 LYS 118 SER 119 LYS 120 ALA 121 VAL 122 GLU 123 GLN 124 VAL 125 LYS 126 SER 127 ASP 128 PHE 129 ASN 130 LYS 131 LEU 132 GLN 133 ASP 134 GLN 135 GLY 136 VAL 137 TYR 138 LYS 139 ALA 140 MET 141 ASN 142 GLU 143 PHE 144 ASP 145 ILE 146 PHE 147 ILE 148 ASN 149 TYR 150 ILE 151 GLU 152 ALA 153 TYR 154 MET 155 MET 156 ILE 157 LYS 158 MET 159 LYS 160 SER 161 LEU 162 GLU 163 HIS 164 HIS 165 HIS 166 HIS 167 HIS 168 HIS 169 HIS 170 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 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 4X51 "X-ray Structure Of Mouse Interleukin-10 Mutant - S1_e8del, C149y" 95.29 162 100.00 100.00 4.57e-116 DBJ BAE31139 "unnamed protein product [Mus musculus]" 94.12 178 98.75 98.75 4.39e-112 GB AAA39274 "interleukin 10 precursor [Mus musculus]" 94.12 178 99.38 99.38 5.22e-113 GB AAA39275 "interleukin 10 [Mus musculus domesticus]" 94.12 178 99.38 99.38 5.22e-113 GB AAI20613 "Interleukin 10 [Mus musculus]" 94.12 178 99.38 99.38 5.22e-113 GB AAI37845 "Interleukin 10 [Mus musculus]" 94.12 178 99.38 99.38 5.22e-113 GB EDL39722 "interleukin 10 [Mus musculus]" 94.12 178 99.38 99.38 5.22e-113 REF NP_034678 "interleukin-10 precursor [Mus musculus]" 94.12 178 99.38 99.38 5.22e-113 SP P18893 "RecName: Full=Interleukin-10; Short=IL-10; AltName: Full=Cytokine synthesis inhibitory factor; Short=CSIF; Flags: Precursor" 94.12 178 99.38 99.38 5.22e-113 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $IL-10 Mouse 10090 Eukaryota Metazoa Mus musculus IL10 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 $IL-10 'recombinant technology' . Escherichia coli Rosetta(DE3) pET41b(+) stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; Partially deuterated and uniformly 15N, 13C-labelled samples were produced by growing cells at 37 C in a minimal salt medium (75% D2O, 25% H2O) containing 9.29 g/L sodium sulphate, 29.2 g/L di-potassium hydrogenphosphate, 8.14 g/L sodium dihydrogenphosphate dihydrate, 1.2 g/L magnesium sulphate, 5 g/L [U-13C]glucose (Cambridge Isotope Laboratories), 1 g/L 15N ammonium chloride (Cambridge Isotope Laboratories), 4.92 g/L 15N ammonium sulphate (Cambridge Isotope Laboratories), 100 mg/mL thiamin, 100 mg/mL kanamycin, and 34 mg/mL chloramphenicol. Protein expression was induced with 1 mM isopropyl-beta-D-thiogalactopyranoside (IPTG) and was conducted for 4 hours. The cell pellet was resuspended in 50 mM Tris-HCl, pH 7.4, 100 mM NaCl, 1 mM EDTA, 0.1 mM PMSF and cells were lysed by using a french press and by adding 0.3 mg/mL lysozyme. Collected inclusion bodies were washed three times in 50 mM Tris-HCl, pH 7.4, 1 M NaCl, 5% (v/v) Triton X-100, 1 mM EDTA and were finally dissolved in 50 M Tris-HCl, pH 7.4, 100 mM NaCl, 6 M Guanidine hydrochloride, 200 mM dithiothreitol, 1 mM EDTA. Prior to refolding dithiothreitol was removed by dialysis against 100 mM Tris-HCl, pH 9.0, 100 mM NaCl, 6 M guanidine hydrochloride. Protein refolding was initiated by rapid dilution into 100 mM Tris-HCl, pH 9.0, 100 mM NaCl, 1 M L-arginine, 5 mM reduced glutathione, 1 mM oxidized glutathione until a final protein concentration of 0.1 mg/mL was reached. The refolding was allowed to proceed for two further days. IL-10 was purified using a Ni-NTA agarose column (Machery-Nagel) equilibrated in 20 mM sodium phosphate, pH 7.4, 50 mM NaCl and was eluted using the same buffer containing 600 mM imidazole. The native IL-10 dimer was separated from the monomer and higher molecular aggregates, which form during protein refolding, using a S-200 HR (GE Healthcare) preparative gelfiltration column equilibrated in 20 mM sodium phosphate, pH 7.4, 50 mM NaCl. NMR samples used for assignment contained between 1-2 mM IL-10 in 20 mM potassium phosphate, pH 6.2, 50 mM NaCl (95% H2O, 5% D2O). ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $IL-10 . mM 1 2 '[U-100% 13C; U-100% 15N; U-80% 2H]' 'potassium phosphate' 25 mM . . 'natural abundance' 'sodium chloride' 50 mM . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_TALOS _Saveframe_category software _Name TALOS _Version . loop_ _Vendor _Address _Electronic_address 'Cornilescu, Delaglio and Bax' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(COCA)CB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.05 . M pH 6.2 . pH pressure 1 . atm temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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_assigned_chem_shift_list_1_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCA' '3D HNCACB' '3D HBHA(CO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'IL-10, Chain A' _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 2 ARG HA H 4.16 0.10 1 2 2 2 ARG HB2 H 1.79 0.10 2 3 2 2 ARG C C 176.24 0.20 1 4 2 2 ARG CA C 57.00 0.25 1 5 2 2 ARG CB C 30.53 0.50 1 6 3 3 GLY H H 8.50 0.01 1 7 3 3 GLY HA2 H 4.38 0.10 2 8 3 3 GLY HA3 H 4.38 0.10 2 9 3 3 GLY C C 173.51 0.20 1 10 3 3 GLY CA C 45.53 0.25 1 11 3 3 GLY N N 111.49 0.10 1 12 4 4 GLN H H 8.15 0.01 1 13 4 4 GLN HA H 4.21 0.10 1 14 4 4 GLN HB2 H 1.86 0.10 2 15 4 4 GLN C C 175.25 0.20 1 16 4 4 GLN CA C 56.19 0.25 1 17 4 4 GLN CB C 29.68 0.50 1 18 4 4 GLN N N 121.15 0.10 1 19 5 5 TYR H H 8.22 0.01 1 20 5 5 TYR HA H 4.60 0.10 1 21 5 5 TYR HB2 H 3.06 0.10 2 22 5 5 TYR HB3 H 2.90 0.10 2 23 5 5 TYR C C 175.26 0.20 1 24 5 5 TYR CA C 57.95 0.25 1 25 5 5 TYR CB C 41.40 0.50 1 26 5 5 TYR N N 122.07 0.10 1 27 6 6 SER H H 8.24 0.01 1 28 6 6 SER HA H 4.43 0.10 1 29 6 6 SER HB2 H 3.83 0.10 2 30 6 6 SER C C 173.94 0.20 1 31 6 6 SER CA C 58.42 0.25 1 32 6 6 SER CB C 64.25 0.50 1 33 6 6 SER N N 118.93 0.10 1 34 7 7 ARG H H 8.38 0.01 1 35 7 7 ARG HA H 4.27 0.10 1 36 7 7 ARG HB2 H 1.78 0.10 2 37 7 7 ARG C C 176.02 0.20 1 38 7 7 ARG CA C 56.78 0.25 1 39 7 7 ARG CB C 30.46 0.50 1 40 7 7 ARG N N 124.43 0.10 1 41 8 8 GLU H H 8.41 0.01 1 42 8 8 GLU HA H 4.22 0.10 1 43 8 8 GLU HB2 H 2.00 0.10 2 44 8 8 GLU HB3 H 1.86 0.10 2 45 8 8 GLU C C 175.81 0.20 1 46 8 8 GLU CA C 57.00 0.25 1 47 8 8 GLU CB C 30.11 0.50 1 48 8 8 GLU N N 122.41 0.10 1 49 9 9 ASP H H 8.30 0.01 1 50 9 9 ASP HA H 4.54 0.10 1 51 9 9 ASP HB2 H 2.68 0.10 2 52 9 9 ASP C C 176.02 0.20 1 53 9 9 ASP CA C 54.67 0.25 1 54 9 9 ASP CB C 41.40 0.50 1 55 9 9 ASP N N 122.41 0.10 1 56 10 10 ASN H H 8.39 0.01 1 57 10 10 ASN HA H 4.54 0.10 1 58 10 10 ASN HB2 H 2.74 0.10 2 59 10 10 ASN C C 175.09 0.20 1 60 10 10 ASN CA C 54.43 0.25 1 61 10 10 ASN CB C 39.05 0.50 1 62 10 10 ASN N N 121.04 0.10 1 63 11 11 ASN H H 8.48 0.01 1 64 11 11 ASN HB2 H 2.89 0.10 2 65 11 11 ASN HB3 H 2.79 0.10 2 66 11 11 ASN C C 175.19 0.20 1 67 11 11 ASN CA C 54.43 0.25 1 68 11 11 ASN CB C 39.04 0.50 1 69 11 11 ASN N N 119.40 0.10 1 70 16 16 PRO C C 176.46 0.20 1 71 16 16 PRO CA C 63.59 0.25 1 72 16 16 PRO CB C 31.89 0.50 1 73 17 17 VAL H H 8.08 0.01 1 74 17 17 VAL C C 176.68 0.20 1 75 17 17 VAL CA C 63.58 0.25 1 76 17 17 VAL CB C 32.05 0.50 1 77 17 17 VAL N N 120.37 0.10 1 78 18 18 GLY H H 8.47 0.01 1 79 18 18 GLY C C 174.16 0.20 1 80 18 18 GLY CA C 45.76 0.25 1 81 18 18 GLY N N 112.63 0.10 1 82 19 19 GLN H H 8.12 0.01 1 83 19 19 GLN C C 175.81 0.20 1 84 19 19 GLN CA C 56.54 0.25 1 85 19 19 GLN CB C 29.22 0.50 1 86 19 19 GLN N N 120.60 0.10 1 87 20 20 SER H H 8.33 0.01 1 88 20 20 SER CA C 59.60 0.25 1 89 20 20 SER CB C 63.79 0.50 1 90 20 20 SER N N 116.52 0.10 1 91 21 21 HIS H H 8.04 0.01 1 92 21 21 HIS C C 175.36 0.20 1 93 21 21 HIS CA C 54.67 0.25 1 94 21 21 HIS N N 124.42 0.10 1 95 22 22 MET H H 8.28 0.01 1 96 22 22 MET C C 173.62 0.20 1 97 22 22 MET CA C 53.72 0.25 1 98 22 22 MET N N 120.14 0.10 1 99 23 23 LEU H H 8.25 0.01 1 100 23 23 LEU C C 177.00 0.20 1 101 23 23 LEU CA C 55.37 0.25 1 102 23 23 LEU CB C 41.06 0.50 1 103 23 23 LEU N N 124.92 0.10 1 104 24 24 LEU H H 7.50 0.01 1 105 24 24 LEU C C 179.30 0.20 1 106 24 24 LEU CA C 58.89 0.25 1 107 24 24 LEU CB C 41.40 0.50 1 108 24 24 LEU N N 122.82 0.10 1 109 25 25 GLU H H 8.62 0.01 1 110 25 25 GLU C C 179.42 0.20 1 111 25 25 GLU CA C 60.18 0.25 1 112 25 25 GLU CB C 29.22 0.50 1 113 25 25 GLU N N 120.39 0.10 1 114 26 26 LEU H H 8.11 0.01 1 115 26 26 LEU C C 179.42 0.20 1 116 26 26 LEU CA C 58.65 0.25 1 117 26 26 LEU CB C 42.49 0.50 1 118 26 26 LEU N N 122.88 0.10 1 119 27 27 ARG H H 8.39 0.01 1 120 27 27 ARG C C 179.84 0.20 1 121 27 27 ARG CA C 61.23 0.25 1 122 27 27 ARG CB C 30.14 0.50 1 123 27 27 ARG N N 119.30 0.10 1 124 28 28 THR H H 8.91 0.01 1 125 28 28 THR C C 176.79 0.20 1 126 28 28 THR CA C 66.86 0.25 1 127 28 28 THR CB C 68.59 0.50 1 128 28 28 THR N N 119.13 0.10 1 129 29 29 ALA H H 8.12 0.01 1 130 29 29 ALA C C 180.51 0.20 1 131 29 29 ALA CA C 55.14 0.25 1 132 29 29 ALA CB C 18.43 0.50 1 133 29 29 ALA N N 125.79 0.10 1 134 30 30 PHE H H 8.70 0.01 1 135 30 30 PHE C C 176.88 0.20 1 136 30 30 PHE CA C 60.76 0.25 1 137 30 30 PHE CB C 38.59 0.50 1 138 30 30 PHE N N 119.95 0.10 1 139 31 31 SER H H 8.25 0.01 1 140 31 31 SER HB2 H 4.05 0.10 2 141 31 31 SER C C 175.04 0.20 1 142 31 31 SER CA C 62.17 0.25 1 143 31 31 SER CB C 62.97 0.50 1 144 31 31 SER N N 116.71 0.10 1 145 32 32 GLN H H 7.03 0.01 1 146 32 32 GLN C C 176.46 0.20 1 147 32 32 GLN CA C 57.25 0.25 1 148 32 32 GLN CB C 28.74 0.50 1 149 32 32 GLN N N 117.44 0.10 1 150 33 33 VAL H H 7.52 0.01 1 151 33 33 VAL C C 174.93 0.20 1 152 33 33 VAL CA C 60.76 0.25 1 153 33 33 VAL CB C 32.94 0.50 1 154 33 33 VAL N N 109.80 0.10 1 155 34 34 LYS H H 6.97 0.01 1 156 34 34 LYS C C 177.11 0.20 1 157 34 34 LYS CA C 59.82 0.25 1 158 34 34 LYS CB C 32.02 0.50 1 159 34 34 LYS N N 124.15 0.10 1 160 35 35 THR H H 8.42 0.01 1 161 35 35 THR C C 175.68 0.20 1 162 35 35 THR CA C 66.62 0.25 1 163 35 35 THR CB C 68.12 0.50 1 164 35 35 THR N N 113.24 0.10 1 165 36 36 PHE H H 7.76 0.01 1 166 36 36 PHE C C 176.68 0.20 1 167 36 36 PHE CA C 61.70 0.25 1 168 36 36 PHE CB C 38.60 0.50 1 169 36 36 PHE N N 123.72 0.10 1 170 37 37 PHE H H 7.44 0.01 1 171 37 37 PHE C C 176.24 0.20 1 172 37 37 PHE CA C 62.87 0.25 1 173 37 37 PHE CB C 38.59 0.50 1 174 37 37 PHE N N 115.33 0.10 1 175 38 38 GLN H H 9.06 0.01 1 176 38 38 GLN C C 178.11 0.20 1 177 38 38 GLN CA C 59.36 0.25 1 178 38 38 GLN CB C 29.21 0.50 1 179 38 38 GLN N N 123.24 0.10 1 180 39 39 THR H H 7.62 0.01 1 181 39 39 THR C C 175.15 0.20 1 182 39 39 THR CA C 64.75 0.25 1 183 39 39 THR CB C 69.06 0.50 1 184 39 39 THR N N 110.91 0.10 1 185 40 40 LYS H H 6.86 0.01 1 186 40 40 LYS C C 175.48 0.20 1 187 40 40 LYS CA C 56.31 0.25 1 188 40 40 LYS CB C 32.96 0.50 1 189 40 40 LYS N N 119.57 0.10 1 190 41 41 ASP H H 7.50 0.01 1 191 41 41 ASP C C 174.93 0.20 1 192 41 41 ASP CA C 53.73 0.25 1 193 41 41 ASP CB C 39.61 0.50 1 194 41 41 ASP N N 119.68 0.10 1 195 42 42 GLN H H 8.34 0.01 1 196 42 42 GLN C C 175.91 0.20 1 197 42 42 GLN CA C 56.07 0.25 1 198 42 42 GLN CB C 29.68 0.50 1 199 42 42 GLN N N 124.89 0.10 1 200 43 43 LEU H H 8.08 0.01 1 201 43 43 LEU C C 178.05 0.20 1 202 43 43 LEU CA C 54.66 0.25 1 203 43 43 LEU CB C 43.03 0.50 1 204 43 43 LEU N N 122.00 0.10 1 205 44 44 ASP H H 8.80 0.01 1 206 44 44 ASP HB2 H 2.65 0.10 2 207 44 44 ASP C C 175.48 0.20 1 208 44 44 ASP CA C 54.91 0.25 1 209 44 44 ASP CB C 40.68 0.50 1 210 44 44 ASP N N 124.49 0.10 1 211 45 45 ASN H H 8.03 0.01 1 212 45 45 ASN HB2 H 2.63 0.10 2 213 45 45 ASN C C 172.53 0.20 1 214 45 45 ASN CA C 53.97 0.25 1 215 45 45 ASN CB C 39.06 0.50 1 216 45 45 ASN N N 117.39 0.10 1 217 46 46 ILE H H 7.96 0.01 1 218 46 46 ILE HB H 1.75 0.10 1 219 46 46 ILE C C 175.59 0.20 1 220 46 46 ILE CA C 59.38 0.25 1 221 46 46 ILE CB C 39.06 0.50 1 222 46 46 ILE N N 120.50 0.10 1 223 48 48 LEU H H 8.53 0.01 1 224 48 48 LEU C C 174.93 0.20 1 225 48 48 LEU CA C 54.42 0.25 1 226 48 48 LEU CB C 39.78 0.50 1 227 48 48 LEU N N 125.85 0.10 1 228 49 49 THR H H 7.57 0.01 1 229 49 49 THR C C 175.26 0.20 1 230 49 49 THR CA C 60.99 0.25 1 231 49 49 THR CB C 72.35 0.50 1 232 49 49 THR N N 113.46 0.10 1 233 50 50 ASP H H 8.77 0.01 1 234 50 50 ASP HB2 H 2.63 0.10 2 235 50 50 ASP HB3 H 2.57 0.10 2 236 50 50 ASP C C 177.33 0.20 1 237 50 50 ASP CA C 57.02 0.25 1 238 50 50 ASP CB C 41.07 0.50 1 239 50 50 ASP N N 120.11 0.10 1 240 51 51 SER H H 7.97 0.01 1 241 51 51 SER HB2 H 3.72 0.10 2 242 51 51 SER C C 176.02 0.20 1 243 51 51 SER CA C 61.93 0.25 1 244 51 51 SER CB C 62.78 0.50 1 245 51 51 SER N N 115.88 0.10 1 246 52 52 LEU H H 7.58 0.01 1 247 52 52 LEU C C 176.57 0.20 1 248 52 52 LEU CA C 57.71 0.25 1 249 52 52 LEU CB C 41.39 0.50 1 250 52 52 LEU N N 123.29 0.10 1 251 53 53 MET H H 6.24 0.01 1 252 53 53 MET C C 177.78 0.20 1 253 53 53 MET CA C 56.78 0.25 1 254 53 53 MET CB C 30.62 0.50 1 255 53 53 MET N N 118.63 0.10 1 256 54 54 GLN H H 8.09 0.01 1 257 54 54 GLN C C 179.19 0.20 1 258 54 54 GLN CA C 58.89 0.25 1 259 54 54 GLN CB C 27.34 0.50 1 260 54 54 GLN N N 117.81 0.10 1 261 55 55 ASP H H 7.52 0.01 1 262 55 55 ASP C C 179.52 0.20 1 263 55 55 ASP CA C 57.24 0.25 1 264 55 55 ASP CB C 40.00 0.50 1 265 55 55 ASP N N 122.13 0.10 1 266 56 56 PHE H H 8.31 0.01 1 267 56 56 PHE C C 176.46 0.20 1 268 56 56 PHE CA C 59.12 0.25 1 269 56 56 PHE CB C 37.66 0.50 1 270 56 56 PHE N N 121.12 0.10 1 271 57 57 LYS H H 7.59 0.01 1 272 57 57 LYS HB2 H 1.86 0.10 2 273 57 57 LYS HB3 H 1.80 0.10 2 274 57 57 LYS C C 176.57 0.20 1 275 57 57 LYS CA C 57.95 0.25 1 276 57 57 LYS CB C 33.44 0.50 1 277 57 57 LYS N N 115.89 0.10 1 278 58 58 GLY H H 7.23 0.01 1 279 58 58 GLY C C 176.55 0.20 1 280 58 58 GLY CA C 45.06 0.25 1 281 58 58 GLY N N 107.86 0.10 1 282 59 59 TYR H H 8.55 0.01 1 283 59 59 TYR C C 176.57 0.20 1 284 59 59 TYR CA C 60.75 0.25 1 285 59 59 TYR CB C 38.04 0.50 1 286 59 59 TYR N N 120.95 0.10 1 287 60 60 LEU H H 8.73 0.01 1 288 60 60 LEU C C 177.11 0.20 1 289 60 60 LEU CA C 53.96 0.25 1 290 60 60 LEU CB C 40.94 0.50 1 291 60 60 LEU N N 122.84 0.10 1 292 61 61 GLY H H 7.91 0.01 1 293 61 61 GLY C C 174.15 0.20 1 294 61 61 GLY CA C 49.98 0.25 1 295 61 61 GLY N N 109.03 0.10 1 296 62 62 CYS H H 8.71 0.01 1 297 62 62 CYS C C 175.06 0.20 1 298 62 62 CYS CA C 60.76 0.25 1 299 62 62 CYS CB C 38.92 0.50 1 300 62 62 CYS N N 119.75 0.10 1 301 63 63 GLN C C 178.21 0.20 1 302 63 63 GLN CA C 59.83 0.25 1 303 63 63 GLN CB C 27.57 0.50 1 304 64 64 ALA H H 8.54 0.01 1 305 64 64 ALA C C 178.10 0.20 1 306 64 64 ALA CA C 55.36 0.25 1 307 64 64 ALA CB C 18.43 0.50 1 308 64 64 ALA N N 123.76 0.10 1 309 65 65 LEU H H 8.21 0.01 1 310 65 65 LEU C C 177.88 0.20 1 311 65 65 LEU CA C 58.65 0.25 1 312 65 65 LEU CB C 39.06 0.50 1 313 65 65 LEU N N 120.84 0.10 1 314 66 66 SER H H 8.63 0.01 1 315 66 66 SER C C 177.98 0.20 1 316 66 66 SER CA C 61.70 0.25 1 317 66 66 SER CB C 63.59 0.50 1 318 66 66 SER N N 114.07 0.10 1 319 67 67 GLU H H 8.45 0.01 1 320 67 67 GLU C C 179.96 0.20 1 321 67 67 GLU CA C 59.82 0.25 1 322 67 67 GLU CB C 30.15 0.50 1 323 67 67 GLU N N 118.63 0.10 1 324 68 68 MET H H 8.38 0.01 1 325 68 68 MET C C 178.54 0.20 1 326 68 68 MET CA C 55.84 0.25 1 327 68 68 MET CB C 30.16 0.50 1 328 68 68 MET N N 120.75 0.10 1 329 69 69 ILE H H 8.90 0.01 1 330 69 69 ILE C C 177.00 0.20 1 331 69 69 ILE CA C 67.57 0.25 1 332 69 69 ILE CB C 37.66 0.50 1 333 69 69 ILE N N 122.41 0.10 1 334 70 70 GLN H H 7.82 0.01 1 335 70 70 GLN C C 176.46 0.20 1 336 70 70 GLN CA C 59.35 0.25 1 337 70 70 GLN CB C 28.74 0.50 1 338 70 70 GLN N N 119.36 0.10 1 339 71 71 PHE H H 8.41 0.01 1 340 71 71 PHE C C 177.88 0.20 1 341 71 71 PHE CA C 60.29 0.25 1 342 71 71 PHE CB C 39.09 0.50 1 343 71 71 PHE N N 121.17 0.10 1 344 72 72 TYR H H 8.11 0.01 1 345 72 72 TYR C C 177.44 0.20 1 346 72 72 TYR CA C 64.66 0.25 1 347 72 72 TYR CB C 38.60 0.50 1 348 72 72 TYR N N 119.70 0.10 1 349 73 73 LEU H H 8.27 0.01 1 350 73 73 LEU C C 177.98 0.20 1 351 73 73 LEU CA C 58.42 0.25 1 352 73 73 LEU CB C 42.82 0.50 1 353 73 73 LEU N N 117.64 0.10 1 354 74 74 VAL H H 8.78 0.01 1 355 74 74 VAL C C 175.90 0.20 1 356 74 74 VAL CA C 63.81 0.25 1 357 74 74 VAL CB C 32.53 0.50 1 358 74 74 VAL N N 114.70 0.10 1 359 75 75 GLU H H 7.58 0.01 1 360 75 75 GLU C C 176.66 0.20 1 361 75 75 GLU CA C 57.95 0.25 1 362 75 75 GLU CB C 30.15 0.50 1 363 75 75 GLU N N 118.47 0.10 1 364 76 76 VAL H H 7.15 0.01 1 365 76 76 VAL C C 177.45 0.20 1 366 76 76 VAL CA C 66.15 0.25 1 367 76 76 VAL CB C 32.53 0.50 1 368 76 76 VAL N N 117.44 0.10 1 369 77 77 MET H H 8.89 0.01 1 370 77 77 MET C C 175.15 0.20 1 371 77 77 MET CA C 61.94 0.25 1 372 77 77 MET CB C 29.69 0.50 1 373 77 77 MET N N 119.22 0.10 1 374 78 78 PRO C C 179.74 0.20 1 375 78 78 PRO CA C 66.16 0.25 1 376 79 79 GLN H H 6.79 0.01 1 377 79 79 GLN C C 178.00 0.20 1 378 79 79 GLN CA C 58.42 0.25 1 379 79 79 GLN CB C 29.68 0.50 1 380 79 79 GLN N N 114.68 0.10 1 381 80 80 ALA H H 8.60 0.01 1 382 80 80 ALA C C 178.42 0.20 1 383 80 80 ALA CA C 55.59 0.25 1 384 80 80 ALA CB C 18.23 0.50 1 385 80 80 ALA N N 125.10 0.10 1 386 81 81 GLU H H 8.06 0.01 1 387 81 81 GLU HB2 H 1.98 0.10 2 388 81 81 GLU C C 177.78 0.20 1 389 81 81 GLU CA C 59.59 0.25 1 390 81 81 GLU CB C 29.68 0.50 1 391 81 81 GLU N N 117.10 0.10 1 392 82 82 LYS H H 7.19 0.01 1 393 82 82 LYS HB2 H 1.79 0.10 2 394 82 82 LYS C C 177.55 0.20 1 395 82 82 LYS CA C 58.66 0.25 1 396 82 82 LYS CB C 32.03 0.50 1 397 82 82 LYS N N 118.73 0.10 1 398 83 83 HIS H H 7.60 0.01 1 399 83 83 HIS C C 174.05 0.20 1 400 83 83 HIS CA C 57.48 0.25 1 401 83 83 HIS CB C 31.08 0.50 1 402 83 83 HIS N N 115.67 0.10 1 403 84 84 GLY H H 7.71 0.01 1 404 84 84 GLY C C 170.88 0.20 1 405 84 84 GLY CA C 46.94 0.25 1 406 84 84 GLY N N 109.42 0.10 1 407 85 85 PRO C C 178.97 0.20 1 408 85 85 PRO CA C 65.69 0.25 1 409 85 85 PRO CB C 31.47 0.50 1 410 86 86 GLU H H 9.66 0.01 1 411 86 86 GLU HB2 H 1.97 0.10 2 412 86 86 GLU C C 177.55 0.20 1 413 86 86 GLU CA C 59.12 0.25 1 414 86 86 GLU CB C 28.75 0.50 1 415 86 86 GLU N N 119.09 0.10 1 416 87 87 ILE H H 7.47 0.01 1 417 87 87 ILE C C 176.13 0.20 1 418 87 87 ILE CA C 60.53 0.25 1 419 87 87 ILE CB C 38.10 0.50 1 420 87 87 ILE N N 114.07 0.10 1 421 88 88 LYS H H 7.47 0.01 1 422 88 88 LYS C C 177.23 0.20 1 423 88 88 LYS CA C 61.23 0.25 1 424 88 88 LYS CB C 32.50 0.50 1 425 88 88 LYS N N 124.11 0.10 1 426 89 89 GLU H H 8.68 0.01 1 427 89 89 GLU HB2 H 1.81 0.10 2 428 89 89 GLU HB3 H 1.75 0.10 2 429 89 89 GLU C C 179.09 0.20 1 430 89 89 GLU CA C 59.83 0.25 1 431 89 89 GLU CB C 28.48 0.50 1 432 89 89 GLU N N 119.58 0.10 1 433 90 90 HIS H H 7.46 0.01 1 434 90 90 HIS C C 179.09 0.20 1 435 90 90 HIS CA C 58.41 0.25 1 436 90 90 HIS CB C 31.09 0.50 1 437 90 90 HIS N N 119.66 0.10 1 438 91 91 LEU H H 8.48 0.01 1 439 91 91 LEU C C 178.59 0.20 1 440 91 91 LEU CA C 57.94 0.25 1 441 91 91 LEU CB C 40.94 0.50 1 442 91 91 LEU N N 122.69 0.10 1 443 92 92 ASN H H 8.73 0.01 1 444 92 92 ASN HB2 H 2.85 0.10 2 445 92 92 ASN C C 177.45 0.20 1 446 92 92 ASN CA C 57.01 0.25 1 447 92 92 ASN CB C 38.43 0.50 1 448 92 92 ASN N N 121.55 0.10 1 449 93 93 SER H H 7.79 0.01 1 450 93 93 SER HB2 H 4.05 0.10 2 451 93 93 SER C C 176.13 0.20 1 452 93 93 SER CA C 61.23 0.25 1 453 93 93 SER CB C 62.97 0.50 1 454 93 93 SER N N 115.55 0.10 1 455 94 94 LEU H H 7.97 0.01 1 456 94 94 LEU C C 177.88 0.20 1 457 94 94 LEU CA C 58.65 0.25 1 458 94 94 LEU CB C 41.89 0.50 1 459 94 94 LEU N N 121.78 0.10 1 460 95 95 GLY H H 8.51 0.01 1 461 95 95 GLY C C 175.48 0.20 1 462 95 95 GLY CA C 47.86 0.25 1 463 95 95 GLY N N 106.93 0.10 1 464 96 96 GLU H H 8.16 0.01 1 465 96 96 GLU HB2 H 2.19 0.10 2 466 96 96 GLU HB3 H 2.14 0.10 2 467 96 96 GLU C C 179.52 0.20 1 468 96 96 GLU CA C 59.82 0.25 1 469 96 96 GLU CB C 29.21 0.50 1 470 96 96 GLU N N 122.61 0.10 1 471 97 97 LYS H H 8.33 0.01 1 472 97 97 LYS C C 179.52 0.20 1 473 97 97 LYS CA C 59.13 0.25 1 474 97 97 LYS CB C 31.56 0.50 1 475 97 97 LYS N N 120.22 0.10 1 476 98 98 LEU H H 8.52 0.01 1 477 98 98 LEU C C 177.32 0.20 1 478 98 98 LEU CA C 58.17 0.25 1 479 98 98 LEU CB C 41.26 0.50 1 480 98 98 LEU N N 124.95 0.10 1 481 99 99 LYS H H 8.65 0.01 1 482 99 99 LYS C C 179.74 0.20 1 483 99 99 LYS CA C 61.00 0.25 1 484 99 99 LYS CB C 32.04 0.50 1 485 99 99 LYS N N 122.09 0.10 1 486 100 100 THR H H 8.60 0.01 1 487 100 100 THR C C 175.58 0.20 1 488 100 100 THR CA C 67.10 0.25 1 489 100 100 THR CB C 68.59 0.50 1 490 100 100 THR N N 119.20 0.10 1 491 101 101 LEU H H 7.97 0.01 1 492 101 101 LEU C C 177.45 0.20 1 493 101 101 LEU CA C 58.66 0.25 1 494 101 101 LEU CB C 40.46 0.50 1 495 101 101 LEU N N 124.24 0.10 1 496 102 102 ARG H H 8.32 0.01 1 497 102 102 ARG C C 176.68 0.20 1 498 102 102 ARG CA C 60.65 0.25 1 499 102 102 ARG CB C 31.55 0.50 1 500 102 102 ARG N N 119.75 0.10 1 501 103 103 MET H H 7.86 0.01 1 502 103 103 MET C C 178.54 0.20 1 503 103 103 MET CA C 58.89 0.25 1 504 103 103 MET CB C 31.09 0.50 1 505 103 103 MET N N 117.52 0.10 1 506 104 104 ARG H H 8.27 0.01 1 507 104 104 ARG C C 179.42 0.20 1 508 104 104 ARG CA C 59.59 0.25 1 509 104 104 ARG CB C 30.58 0.50 1 510 104 104 ARG N N 120.79 0.10 1 511 105 105 LEU H H 8.83 0.01 1 512 105 105 LEU C C 178.38 0.20 1 513 105 105 LEU CA C 58.19 0.25 1 514 105 105 LEU CB C 41.40 0.50 1 515 105 105 LEU N N 120.18 0.10 1 516 106 106 ARG H H 8.17 0.01 1 517 106 106 ARG C C 177.51 0.20 1 518 106 106 ARG CA C 59.12 0.25 1 519 106 106 ARG N N 118.06 0.10 1 520 113 113 PRO C C 177.55 0.20 1 521 113 113 PRO CA C 65.92 0.25 1 522 113 113 PRO CB C 34.97 0.50 1 523 114 114 CYS H H 8.06 0.01 1 524 114 114 CYS C C 173.73 0.20 1 525 114 114 CYS CA C 60.76 0.25 1 526 114 114 CYS CB C 39.36 0.50 1 527 114 114 CYS N N 110.62 0.10 1 528 115 115 GLU H H 7.26 0.01 1 529 115 115 GLU C C 175.03 0.20 1 530 115 115 GLU CA C 57.02 0.25 1 531 115 115 GLU CB C 30.15 0.50 1 532 115 115 GLU N N 121.56 0.10 1 533 116 116 ASN H H 7.67 0.01 1 534 116 116 ASN C C 173.06 0.20 1 535 116 116 ASN CA C 53.26 0.25 1 536 116 116 ASN CB C 41.88 0.50 1 537 116 116 ASN N N 119.64 0.10 1 538 117 117 LYS H H 8.34 0.01 1 539 117 117 LYS C C 176.03 0.20 1 540 117 117 LYS CA C 54.67 0.25 1 541 117 117 LYS CB C 34.37 0.50 1 542 117 117 LYS N N 119.36 0.10 1 543 118 118 SER H H 8.88 0.01 1 544 118 118 SER C C 176.13 0.20 1 545 118 118 SER CA C 57.73 0.25 1 546 118 118 SER CB C 62.61 0.50 1 547 118 118 SER N N 116.71 0.10 1 548 119 119 LYS H H 9.20 0.01 1 549 119 119 LYS C C 178.54 0.20 1 550 119 119 LYS CA C 58.64 0.25 1 551 119 119 LYS CB C 31.56 0.50 1 552 119 119 LYS N N 134.07 0.10 1 553 120 120 ALA H H 7.94 0.01 1 554 120 120 ALA C C 179.96 0.20 1 555 120 120 ALA CA C 55.13 0.25 1 556 120 120 ALA CB C 18.43 0.50 1 557 120 120 ALA N N 123.16 0.10 1 558 121 121 VAL H H 7.83 0.01 1 559 121 121 VAL C C 176.68 0.20 1 560 121 121 VAL CA C 66.61 0.25 1 561 121 121 VAL CB C 31.22 0.50 1 562 121 121 VAL N N 120.05 0.10 1 563 122 122 GLU H H 7.33 0.01 1 564 122 122 GLU HB2 H 1.97 0.10 2 565 122 122 GLU C C 178.75 0.20 1 566 122 122 GLU CA C 59.82 0.25 1 567 122 122 GLU CB C 29.21 0.50 1 568 122 122 GLU N N 119.86 0.10 1 569 123 123 GLN H H 7.82 0.01 1 570 123 123 GLN C C 176.79 0.20 1 571 123 123 GLN CA C 58.66 0.25 1 572 123 123 GLN CB C 28.04 0.50 1 573 123 123 GLN N N 121.15 0.10 1 574 124 124 VAL H H 7.79 0.01 1 575 124 124 VAL C C 177.66 0.20 1 576 124 124 VAL CA C 66.62 0.25 1 577 124 124 VAL CB C 31.10 0.50 1 578 124 124 VAL N N 122.42 0.10 1 579 125 125 LYS H H 7.96 0.01 1 580 125 125 LYS C C 178.54 0.20 1 581 125 125 LYS CA C 60.77 0.25 1 582 125 125 LYS CB C 31.57 0.50 1 583 125 125 LYS N N 118.06 0.10 1 584 126 126 SER H H 8.07 0.01 1 585 126 126 SER HB2 H 3.99 0.10 2 586 126 126 SER HB3 H 3.94 0.10 2 587 126 126 SER C C 177.44 0.20 1 588 126 126 SER CA C 61.70 0.25 1 589 126 126 SER CB C 62.97 0.50 1 590 126 126 SER N N 115.94 0.10 1 591 127 127 ASP H H 8.83 0.01 1 592 127 127 ASP C C 177.88 0.20 1 593 127 127 ASP CA C 57.74 0.25 1 594 127 127 ASP CB C 40.01 0.50 1 595 127 127 ASP N N 124.66 0.10 1 596 128 128 PHE H H 8.89 0.01 1 597 128 128 PHE C C 177.12 0.20 1 598 128 128 PHE CA C 62.16 0.25 1 599 128 128 PHE CB C 40.00 0.50 1 600 128 128 PHE N N 121.35 0.10 1 601 129 129 ASN H H 8.25 0.01 1 602 129 129 ASN C C 178.32 0.20 1 603 129 129 ASN CA C 56.55 0.25 1 604 129 129 ASN CB C 39.06 0.50 1 605 129 129 ASN N N 118.92 0.10 1 606 130 130 LYS H H 8.05 0.01 1 607 130 130 LYS C C 177.78 0.20 1 608 130 130 LYS CA C 59.12 0.25 1 609 130 130 LYS CB C 32.45 0.50 1 610 130 130 LYS N N 121.84 0.10 1 611 131 131 LEU H H 7.49 0.01 1 612 131 131 LEU C C 176.79 0.20 1 613 131 131 LEU CA C 55.60 0.25 1 614 131 131 LEU CB C 42.34 0.50 1 615 131 131 LEU N N 117.75 0.10 1 616 132 132 GLN H H 7.59 0.01 1 617 132 132 GLN C C 177.77 0.20 1 618 132 132 GLN CA C 57.48 0.25 1 619 132 132 GLN CB C 26.40 0.50 1 620 132 132 GLN N N 117.53 0.10 1 621 133 133 ASP H H 8.73 0.01 1 622 133 133 ASP HB2 H 2.52 0.10 2 623 133 133 ASP HB3 H 2.41 0.10 2 624 133 133 ASP C C 176.68 0.20 1 625 133 133 ASP CA C 57.96 0.25 1 626 133 133 ASP CB C 39.06 0.50 1 627 133 133 ASP N N 125.92 0.10 1 628 134 134 GLN H H 7.65 0.01 1 629 134 134 GLN C C 178.21 0.20 1 630 134 134 GLN CA C 58.19 0.25 1 631 134 134 GLN CB C 28.28 0.50 1 632 134 134 GLN N N 115.13 0.10 1 633 135 135 GLY H H 7.68 0.01 1 634 135 135 GLY C C 174.17 0.20 1 635 135 135 GLY CA C 47.87 0.25 1 636 135 135 GLY N N 110.47 0.10 1 637 136 136 VAL H H 7.24 0.01 1 638 136 136 VAL C C 176.57 0.20 1 639 136 136 VAL CA C 66.85 0.25 1 640 136 136 VAL CB C 31.08 0.50 1 641 136 136 VAL N N 123.05 0.10 1 642 137 137 TYR H H 6.95 0.01 1 643 137 137 TYR C C 177.23 0.20 1 644 137 137 TYR CA C 59.83 0.25 1 645 137 137 TYR CB C 36.72 0.50 1 646 137 137 TYR N N 117.53 0.10 1 647 138 138 LYS H H 8.01 0.01 1 648 138 138 LYS C C 177.01 0.20 1 649 138 138 LYS CA C 59.36 0.25 1 650 138 138 LYS CB C 29.69 0.50 1 651 138 138 LYS N N 119.75 0.10 1 652 139 139 ALA H H 8.66 0.01 1 653 139 139 ALA C C 180.95 0.20 1 654 139 139 ALA CA C 55.61 0.25 1 655 139 139 ALA CB C 17.96 0.50 1 656 139 139 ALA N N 119.36 0.10 1 657 140 140 MET H H 7.74 0.01 1 658 140 140 MET C C 178.10 0.20 1 659 140 140 MET CA C 55.13 0.25 1 660 140 140 MET CB C 27.81 0.50 1 661 140 140 MET N N 114.67 0.10 1 662 141 141 ASN H H 8.54 0.01 1 663 141 141 ASN C C 175.69 0.20 1 664 141 141 ASN CA C 56.31 0.25 1 665 141 141 ASN CB C 39.05 0.50 1 666 141 141 ASN N N 119.66 0.10 1 667 142 142 GLU H H 7.65 0.01 1 668 142 142 GLU C C 175.58 0.20 1 669 142 142 GLU CA C 56.31 0.25 1 670 142 142 GLU CB C 29.19 0.50 1 671 142 142 GLU N N 112.64 0.10 1 672 143 143 PHE H H 7.70 0.01 1 673 143 143 PHE C C 175.58 0.20 1 674 143 143 PHE CA C 61.46 0.25 1 675 143 143 PHE CB C 39.07 0.50 1 676 143 143 PHE N N 123.04 0.10 1 677 144 144 ASP H H 7.57 0.01 1 678 144 144 ASP C C 177.55 0.20 1 679 144 144 ASP CA C 56.31 0.25 1 680 144 144 ASP CB C 39.06 0.50 1 681 144 144 ASP N N 114.29 0.10 1 682 145 145 ILE H H 7.59 0.01 1 683 145 145 ILE C C 176.90 0.20 1 684 145 145 ILE CA C 64.60 0.25 1 685 145 145 ILE CB C 36.25 0.50 1 686 145 145 ILE N N 126.03 0.10 1 687 146 146 PHE H H 7.23 0.01 1 688 146 146 PHE C C 176.46 0.20 1 689 146 146 PHE CA C 59.59 0.25 1 690 146 146 PHE CB C 37.17 0.50 1 691 146 146 PHE N N 119.06 0.10 1 692 147 147 ILE H H 7.95 0.01 1 693 147 147 ILE C C 176.95 0.20 1 694 147 147 ILE CA C 65.92 0.25 1 695 147 147 ILE CB C 37.18 0.50 1 696 147 147 ILE N N 117.67 0.10 1 697 148 148 ASN H H 7.71 0.01 1 698 148 148 ASN C C 178.75 0.20 1 699 148 148 ASN CA C 56.08 0.25 1 700 148 148 ASN CB C 36.95 0.50 1 701 148 148 ASN N N 119.52 0.10 1 702 149 149 TYR H H 8.57 0.01 1 703 149 149 TYR C C 178.10 0.20 1 704 149 149 TYR CA C 57.95 0.25 1 705 149 149 TYR CB C 35.77 0.50 1 706 149 149 TYR N N 124.01 0.10 1 707 150 150 ILE H H 8.42 0.01 1 708 150 150 ILE C C 177.77 0.20 1 709 150 150 ILE CA C 66.86 0.25 1 710 150 150 ILE CB C 37.19 0.50 1 711 150 150 ILE N N 123.13 0.10 1 712 151 151 GLU H H 8.61 0.01 1 713 151 151 GLU C C 177.88 0.20 1 714 151 151 GLU CA C 60.53 0.25 1 715 151 151 GLU N N 121.49 0.10 1 716 152 152 ALA H H 8.16 0.01 1 717 152 152 ALA C C 179.85 0.20 1 718 152 152 ALA CA C 55.60 0.25 1 719 152 152 ALA CB C 18.42 0.50 1 720 152 152 ALA N N 122.00 0.10 1 721 153 153 TYR H H 8.48 0.01 1 722 153 153 TYR HA H 4.54 0.10 1 723 153 153 TYR HB2 H 3.04 0.10 2 724 153 153 TYR C C 176.45 0.20 1 725 153 153 TYR CA C 61.94 0.25 1 726 153 153 TYR CB C 38.13 0.50 1 727 153 153 TYR N N 121.19 0.10 1 728 154 154 MET H H 8.71 0.01 1 729 154 154 MET HB2 H 1.86 0.10 2 730 154 154 MET HB3 H 1.81 0.10 2 731 154 154 MET C C 177.67 0.20 1 732 154 154 MET CA C 60.05 0.25 1 733 154 154 MET CB C 33.22 0.50 1 734 154 154 MET N N 118.96 0.10 1 735 155 155 MET H H 8.21 0.01 1 736 155 155 MET C C 178.87 0.20 1 737 155 155 MET CA C 58.89 0.25 1 738 155 155 MET CB C 31.10 0.50 1 739 155 155 MET N N 118.28 0.10 1 740 156 156 ILE H H 7.90 0.01 1 741 156 156 ILE HA H 4.27 0.10 1 742 156 156 ILE HB H 1.64 0.10 1 743 156 156 ILE C C 178.98 0.20 1 744 156 156 ILE CA C 64.98 0.25 1 745 156 156 ILE CB C 37.86 0.50 1 746 156 156 ILE N N 121.05 0.10 1 747 157 157 LYS H H 7.88 0.01 1 748 157 157 LYS HA H 4.11 0.10 1 749 157 157 LYS HB2 H 1.91 0.10 2 750 157 157 LYS C C 178.65 0.20 1 751 157 157 LYS CA C 56.54 0.25 1 752 157 157 LYS CB C 31.46 0.50 1 753 157 157 LYS N N 119.43 0.10 1 754 158 158 MET H H 8.13 0.01 1 755 158 158 MET HA H 4.54 0.10 1 756 158 158 MET HB2 H 3.04 0.10 2 757 158 158 MET C C 177.00 0.20 1 758 158 158 MET CA C 57.36 0.25 1 759 158 158 MET CB C 32.37 0.50 1 760 158 158 MET N N 118.93 0.10 1 761 159 159 LYS H H 7.65 0.01 1 762 159 159 LYS C C 177.11 0.20 1 763 159 159 LYS CA C 57.95 0.25 1 764 159 159 LYS CB C 32.09 0.50 1 765 159 159 LYS N N 120.50 0.10 1 766 160 160 SER H H 7.88 0.01 1 767 160 160 SER C C 174.49 0.20 1 768 160 160 SER CA C 59.59 0.25 1 769 160 160 SER CB C 63.91 0.50 1 770 160 160 SER N N 115.78 0.10 1 771 161 161 LEU H H 7.94 0.01 1 772 161 161 LEU C C 177.01 0.20 1 773 161 161 LEU CA C 55.84 0.25 1 774 161 161 LEU CB C 42.34 0.50 1 775 161 161 LEU N N 124.12 0.10 1 776 162 162 GLU H H 8.05 0.01 1 777 162 162 GLU C C 175.81 0.20 1 778 162 162 GLU CA C 57.01 0.25 1 779 162 162 GLU N N 121.47 0.10 1 780 163 163 HIS H H 8.24 0.01 1 781 163 163 HIS C C 174.38 0.20 1 782 163 163 HIS CA C 56.09 0.25 1 783 163 163 HIS CB C 29.94 0.50 1 784 163 163 HIS N N 120.50 0.10 1 stop_ save_ save_assigned_chem_shift_list_1_3 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCA' '3D HNCACB' '3D HBHA(CO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name N-terminus _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 3 3 GLY H H 8.44 0.01 1 2 3 3 GLY C C 173.18 0.20 1 3 3 3 GLY CA C 45.31 0.25 1 4 3 3 GLY N N 111.76 0.10 1 5 4 4 GLN H H 8.08 0.01 1 6 4 4 GLN C C 174.16 0.20 1 7 4 4 GLN CA C 56.08 0.25 1 8 4 4 GLN CB C 29.64 0.50 1 9 4 4 GLN N N 121.40 0.10 1 10 5 5 TYR H H 7.72 0.01 1 11 5 5 TYR HB2 H 3.78 0.10 1 12 5 5 TYR C C 173.77 0.20 1 13 5 5 TYR CA C 59.36 0.25 1 14 5 5 TYR CB C 39.53 0.50 1 15 5 5 TYR N N 126.98 0.10 1 16 7 7 ARG H H 8.34 0.01 1 17 7 7 ARG HA H 4.38 0.10 1 18 7 7 ARG HB2 H 1.81 0.10 1 19 7 7 ARG C C 175.82 0.20 1 20 7 7 ARG CA C 56.58 0.25 1 21 7 7 ARG N N 124.16 0.10 1 22 8 8 GLU H H 8.44 0.01 1 23 8 8 GLU HA H 4.27 0.10 1 24 8 8 GLU HB2 H 1.97 0.10 1 25 8 8 GLU C C 175.52 0.20 1 26 8 8 GLU CA C 56.99 0.25 1 27 8 8 GLU N N 122.41 0.10 1 28 9 9 ASP H H 8.26 0.01 1 29 9 9 ASP HA H 4.58 0.10 1 30 9 9 ASP HB2 H 2.68 0.10 1 31 9 9 ASP C C 174.39 0.20 1 32 9 9 ASP CA C 54.67 0.25 1 33 9 9 ASP CB C 41.40 0.50 1 34 9 9 ASP N N 122.39 0.10 1 35 10 10 ASN H H 7.98 0.01 1 36 10 10 ASN C C 178.86 0.20 1 37 10 10 ASN CA C 55.61 0.25 1 38 10 10 ASN CB C 41.40 0.50 1 39 10 10 ASN N N 125.08 0.10 1 stop_ save_