data_26709 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone Assignment of Human linear diubiquitin ; _BMRB_accession_number 26709 _BMRB_flat_file_name bmr26709.str _Entry_type original _Submission_date 2015-11-26 _Accession_date 2015-11-26 _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 Halander Jenny . . 2 Messias Ana C. . 3 Geerlof Arie . . 4 Sattler Michael . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 132 "13C chemical shifts" 255 "15N chemical shifts" 132 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-01-14 original BMRB . stop_ _Original_release_date 2016-01-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Inhibition of Canonical NF-kB Signaling by a Small Molecule Targeting NEMO-Ubiquitin Interaction ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26740240 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vincendeau Michelle . . 2 Kamyar Hadian . . 3 Messias Ana C. . 4 Brenke Jara K. . 5 Halander Jenny . . 6 Griesbach Richard . . 7 Greczmiel Ute . . 8 Bertossi Arianna . . 9 Stehle Ralf . . 10 Nagel Daniel . . 11 Demski Kathrin . . 12 Velvarska Hana . . 13 Niessing Dierk . . 14 Geerlof Arie . . 15 Sattler Michael . . 16 Krappmann Daniel . . stop_ _Journal_abbreviation 'Sci. Rep.' _Journal_volume 6 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 18934 _Page_last 18934 _Year 2016 _Details . loop_ _Keyword NEMO NMR 'linear diubiquitin' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'linear diubiquitin' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'linear diubiquitin' $linear_diubiquitin stop_ _System_molecular_weight 18220.8 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'activation of NF-kappaB-inducing kinase activity' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_linear_diubiquitin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common linear_diubiquitin _Molecular_mass 18220.8 _Mol_thiol_state 'not present' loop_ _Biological_function 'activation of NF-kappaB-inducing kinase activity' 'inflammatory response' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 162 _Mol_residue_sequence ; MASHHHHHHGAQIFVKTLTG KTITLEVEPSDTIENVKAKI QDKEGIPPDQQRLIFAGKQL EDGRTLSDYNIQKESTLHLV LRLRGGMQIFVKTLTGKTIT LEVEPSDTIENVKAKIQDKE GIPPDQQRLIFAGKQLEDGR TLSDYNIQKESTLHLVLRLR GG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 SER 4 HIS 5 HIS 6 HIS 7 HIS 8 HIS 9 HIS 10 GLY 11 ALA 12 GLN 13 ILE 14 PHE 15 VAL 16 LYS 17 THR 18 LEU 19 THR 20 GLY 21 LYS 22 THR 23 ILE 24 THR 25 LEU 26 GLU 27 VAL 28 GLU 29 PRO 30 SER 31 ASP 32 THR 33 ILE 34 GLU 35 ASN 36 VAL 37 LYS 38 ALA 39 LYS 40 ILE 41 GLN 42 ASP 43 LYS 44 GLU 45 GLY 46 ILE 47 PRO 48 PRO 49 ASP 50 GLN 51 GLN 52 ARG 53 LEU 54 ILE 55 PHE 56 ALA 57 GLY 58 LYS 59 GLN 60 LEU 61 GLU 62 ASP 63 GLY 64 ARG 65 THR 66 LEU 67 SER 68 ASP 69 TYR 70 ASN 71 ILE 72 GLN 73 LYS 74 GLU 75 SER 76 THR 77 LEU 78 HIS 79 LEU 80 VAL 81 LEU 82 ARG 83 LEU 84 ARG 85 GLY 86 GLY 87 MET 88 GLN 89 ILE 90 PHE 91 VAL 92 LYS 93 THR 94 LEU 95 THR 96 GLY 97 LYS 98 THR 99 ILE 100 THR 101 LEU 102 GLU 103 VAL 104 GLU 105 PRO 106 SER 107 ASP 108 THR 109 ILE 110 GLU 111 ASN 112 VAL 113 LYS 114 ALA 115 LYS 116 ILE 117 GLN 118 ASP 119 LYS 120 GLU 121 GLY 122 ILE 123 PRO 124 PRO 125 ASP 126 GLN 127 GLN 128 ARG 129 LEU 130 ILE 131 PHE 132 ALA 133 GLY 134 LYS 135 GLN 136 LEU 137 GLU 138 ASP 139 GLY 140 ARG 141 THR 142 LEU 143 SER 144 ASP 145 TYR 146 ASN 147 ILE 148 GLN 149 LYS 150 GLU 151 SER 152 THR 153 LEU 154 HIS 155 LEU 156 VAL 157 LEU 158 ARG 159 LEU 160 ARG 161 GLY 162 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 UNIPROT P0CG47 Polyubiquitin-B . . . . . PDB 2W9N 'CRYSTAL STRUCTURE OF LINEAR DI-UBIQUITIN' . . . . . PDB 3AXC 'CRYSTAL STRUCTURE OF LINEAR DI-UBIQUITIN' . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $linear_diubiquitin Human 9606 Eukaryota Metazoa Homo sapiens 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 $linear_diubiquitin 'recombinant technology' . Escherichia coli BL21(DE3) pASK-IBA-3plus 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 $linear_diubiquitin 0.9 mM '[U-100% 13C; U-100% 15N]' D2O 10 % 'natural abundance' Tris-HCl 20 mM [U-2H] 'sodium chloride' 50 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'AV III' _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_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '20 mM deuterated Tis-HCl pH 7.5, 50mM NaCl and 10% D2O' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.07 . M pH 7.5 . pH pressure 1 . atm temperature 298 . 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $CARA stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D 1H-15N NOESY' '3D 1H-15N TOCSY' 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 'linear diubiquitin' _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 10 10 GLY H H 8.321 0.020 1 2 10 10 GLY CA C 44.901 0.3 1 3 10 10 GLY N N 109.919 0.3 1 4 11 11 ALA H H 8.537 0.020 1 5 11 11 ALA CA C 51.295 0.3 1 6 11 11 ALA CB C 20.146 0.3 1 7 11 11 ALA N N 123.877 0.3 1 8 12 12 GLN H H 8.012 0.020 1 9 12 12 GLN CA C 54.082 0.3 1 10 12 12 GLN CB C 30.884 0.3 1 11 12 12 GLN N N 118.420 0.3 1 12 13 13 ILE H H 8.312 0.020 1 13 13 13 ILE CA C 59.246 0.3 1 14 13 13 ILE CB C 41.458 0.3 1 15 13 13 ILE N N 114.130 0.3 1 16 14 14 PHE H H 8.469 0.020 1 17 14 14 PHE CA C 54.902 0.3 1 18 14 14 PHE CB C 40.803 0.3 1 19 14 14 PHE N N 118.873 0.3 1 20 15 15 VAL H H 9.301 0.020 1 21 15 15 VAL CA C 60.312 0.3 1 22 15 15 VAL CB C 33.753 0.3 1 23 15 15 VAL N N 121.563 0.3 1 24 16 16 LYS H H 8.970 0.020 1 25 16 16 LYS CA C 54.328 0.3 1 26 16 16 LYS CB C 33.835 0.3 1 27 16 16 LYS N N 127.920 0.3 1 28 17 17 THR H H 8.723 0.020 1 29 17 17 THR CA C 60.312 0.3 1 30 17 17 THR CB C 70.230 0.3 1 31 17 17 THR N N 115.402 0.3 1 32 18 18 LEU H H 9.133 0.020 1 33 18 18 LEU CA C 57.361 0.3 1 34 18 18 LEU CB C 41.458 0.3 1 35 18 18 LEU N N 121.356 0.3 1 36 20 20 GLY H H 7.818 0.020 1 37 20 20 GLY CA C 45.065 0.3 1 38 20 20 GLY N N 109.258 0.3 1 39 21 21 LYS H H 7.260 0.020 1 40 21 21 LYS CA C 56.131 0.3 1 41 21 21 LYS CB C 33.015 0.3 1 42 21 21 LYS N N 121.903 0.3 1 43 22 22 THR H H 8.619 0.020 1 44 22 22 THR CA C 62.115 0.3 1 45 22 22 THR CB C 69.574 0.3 1 46 22 22 THR N N 120.564 0.3 1 47 23 23 ILE H H 9.545 0.020 1 48 23 23 ILE CA C 59.868 0.3 1 49 23 23 ILE CB C 40.402 0.3 1 50 23 23 ILE N N 127.773 0.3 1 51 24 24 THR H H 8.746 0.020 1 52 24 24 THR CA C 61.869 0.3 1 53 24 24 THR CB C 69.328 0.3 1 54 24 24 THR N N 121.969 0.3 1 55 25 25 LEU H H 8.801 0.020 1 56 25 25 LEU CA C 52.442 0.3 1 57 25 25 LEU CB C 46.213 0.3 1 58 25 25 LEU N N 125.354 0.3 1 59 26 26 GLU H H 8.157 0.020 1 60 26 26 GLU CA C 55.475 0.3 1 61 26 26 GLU CB C 29.573 0.3 1 62 26 26 GLU N N 122.065 0.3 1 63 27 27 VAL H H 8.410 0.020 1 64 27 27 VAL CA C 58.754 0.3 1 65 27 27 VAL CB C 36.048 0.3 1 66 27 27 VAL N N 115.901 0.3 1 67 28 28 GLU H H 8.481 0.020 1 68 28 28 GLU CA C 53.180 0.3 1 69 28 28 GLU CB C 30.884 0.3 1 70 28 28 GLU N N 119.805 0.3 1 71 30 30 SER H H 7.086 0.020 1 72 30 30 SER CA C 57.115 0.3 1 73 30 30 SER CB C 63.181 0.3 1 74 30 30 SER N N 103.720 0.3 1 75 31 31 ASP H H 8.020 0.020 1 76 31 31 ASP CA C 55.721 0.3 1 77 31 31 ASP CB C 40.557 0.3 1 78 31 31 ASP N N 123.870 0.3 1 79 32 32 THR H H 7.839 0.020 1 80 32 32 THR CA C 59.328 0.3 1 81 32 32 THR CB C 70.804 0.3 1 82 32 32 THR N N 109.168 0.3 1 83 33 33 ILE H H 8.505 0.020 1 84 33 33 ILE CA C 62.033 0.3 1 85 33 33 ILE CB C 34.245 0.3 1 86 33 33 ILE N N 121.305 0.3 1 87 35 35 ASN H H 7.931 0.020 1 88 35 35 ASN CA C 55.721 0.3 1 89 35 35 ASN CB C 38.098 0.3 1 90 35 35 ASN N N 121.377 0.3 1 91 36 36 VAL H H 8.108 0.020 1 92 36 36 VAL CA C 67.443 0.3 1 93 36 36 VAL CB C 30.392 0.3 1 94 36 36 VAL N N 122.199 0.3 1 95 37 37 LYS H H 8.550 0.020 1 96 37 37 LYS CA C 58.918 0.3 1 97 37 37 LYS CB C 33.261 0.3 1 98 37 37 LYS N N 119.056 0.3 1 99 38 38 ALA H H 7.984 0.020 1 100 38 38 ALA CA C 55.147 0.3 1 101 38 38 ALA CB C 17.277 0.3 1 102 38 38 ALA N N 123.538 0.3 1 103 39 39 LYS H H 7.937 0.020 1 104 39 39 LYS CA C 59.492 0.3 1 105 39 39 LYS CB C 33.097 0.3 1 106 39 39 LYS N N 120.414 0.3 1 107 40 40 ILE H H 8.281 0.020 1 108 40 40 ILE CA C 65.968 0.3 1 109 40 40 ILE CB C 36.458 0.3 1 110 40 40 ILE N N 121.324 0.3 1 111 41 41 GLN H H 8.536 0.020 1 112 41 41 GLN CA C 59.820 0.3 1 113 41 41 GLN CB C 27.441 0.3 1 114 41 41 GLN N N 123.554 0.3 1 115 42 42 ASP H H 8.021 0.020 1 116 42 42 ASP CA C 57.279 0.3 1 117 42 42 ASP CB C 40.721 0.3 1 118 42 42 ASP N N 119.811 0.3 1 119 43 43 LYS H H 7.441 0.020 1 120 43 43 LYS CA C 57.853 0.3 1 121 43 43 LYS CB C 33.589 0.3 1 122 43 43 LYS N N 115.525 0.3 1 123 44 44 GLU H H 8.710 0.020 1 124 44 44 GLU CA C 54.984 0.3 1 125 44 44 GLU CB C 33.097 0.3 1 126 44 44 GLU N N 114.348 0.3 1 127 45 45 GLY H H 8.485 0.020 1 128 45 45 GLY CA C 45.721 0.3 1 129 45 45 GLY N N 108.904 0.3 1 130 46 46 ILE H H 6.141 0.020 1 131 46 46 ILE CA C 57.689 0.3 1 132 46 46 ILE CB C 40.065 0.3 1 133 46 46 ILE N N 120.392 0.3 1 134 49 49 ASP H H 8.518 0.020 1 135 49 49 ASP CA C 55.557 0.3 1 136 49 49 ASP CB C 39.491 0.3 1 137 49 49 ASP N N 113.665 0.3 1 138 50 50 GLN H H 7.802 0.020 1 139 50 50 GLN CA C 55.311 0.3 1 140 50 50 GLN CB C 29.736 0.3 1 141 50 50 GLN N N 116.861 0.3 1 142 51 51 GLN H H 7.471 0.020 1 143 51 51 GLN CA C 56.377 0.3 1 144 51 51 GLN CB C 31.048 0.3 1 145 51 51 GLN N N 118.052 0.3 1 146 52 52 ARG H H 8.477 0.020 1 147 52 52 ARG CA C 54.902 0.3 1 148 52 52 ARG CB C 31.294 0.3 1 149 52 52 ARG N N 123.091 0.3 1 150 53 53 LEU H H 8.789 0.020 1 151 53 53 LEU CA C 52.770 0.3 1 152 53 53 LEU CB C 45.311 0.3 1 153 53 53 LEU N N 124.451 0.3 1 154 54 54 ILE H H 9.125 0.020 1 155 54 54 ILE CA C 58.754 0.3 1 156 54 54 ILE CB C 40.721 0.3 1 157 54 54 ILE N N 122.418 0.3 1 158 55 55 PHE H H 8.829 0.020 1 159 55 55 PHE CA C 56.213 0.3 1 160 55 55 PHE CB C 43.344 0.3 1 161 55 55 PHE N N 124.873 0.3 1 162 56 56 ALA H H 9.010 0.020 1 163 56 56 ALA CA C 52.278 0.3 1 164 56 56 ALA CB C 16.129 0.3 1 165 56 56 ALA N N 133.028 0.3 1 166 57 57 GLY H H 8.083 0.020 1 167 57 57 GLY CA C 45.065 0.3 1 168 57 57 GLY N N 102.487 0.3 1 169 58 58 LYS H H 7.952 0.020 1 170 58 58 LYS CA C 54.410 0.3 1 171 58 58 LYS CB C 33.999 0.3 1 172 58 58 LYS N N 122.006 0.3 1 173 59 59 GLN H H 8.641 0.020 1 174 59 59 GLN CA C 55.885 0.3 1 175 59 59 GLN CB C 28.835 0.3 1 176 59 59 GLN N N 123.188 0.3 1 177 60 60 LEU H H 8.544 0.020 1 178 60 60 LEU CA C 53.918 0.3 1 179 60 60 LEU CB C 41.130 0.3 1 180 60 60 LEU N N 125.731 0.3 1 181 61 61 GLU H H 8.403 0.020 1 182 61 61 GLU CA C 55.721 0.3 1 183 61 61 GLU CB C 31.540 0.3 1 184 61 61 GLU N N 123.070 0.3 1 185 62 62 ASP H H 8.159 0.020 1 186 62 62 ASP CA C 56.148 0.3 1 187 62 62 ASP CB C 40.311 0.3 1 188 62 62 ASP N N 120.350 0.3 1 189 63 63 GLY H H 7.825 0.020 1 190 63 63 GLY CA C 45.094 0.3 1 191 63 63 GLY N N 109.220 0.3 1 192 64 64 ARG H H 7.409 0.020 1 193 64 64 ARG CA C 54.000 0.3 1 194 64 64 ARG CB C 32.442 0.3 1 195 64 64 ARG N N 119.214 0.3 1 196 65 65 THR H H 8.827 0.020 1 197 65 65 THR CA C 59.328 0.3 1 198 65 65 THR CB C 72.034 0.3 1 199 65 65 THR N N 108.897 0.3 1 200 66 66 LEU H H 8.194 0.020 1 201 66 66 LEU CA C 58.590 0.3 1 202 66 66 LEU CB C 40.065 0.3 1 203 66 66 LEU N N 118.130 0.3 1 204 67 67 SER H H 8.372 0.020 1 205 67 67 SER CA C 60.803 0.3 1 206 67 67 SER CB C 62.279 0.3 1 207 67 67 SER N N 113.159 0.3 1 208 68 68 ASP H H 7.941 0.020 1 209 68 68 ASP CA C 57.197 0.3 1 210 68 68 ASP CB C 39.901 0.3 1 211 68 68 ASP N N 124.539 0.3 1 212 69 69 TYR H H 7.246 0.020 1 213 69 69 TYR CA C 58.016 0.3 1 214 69 69 TYR CB C 39.901 0.3 1 215 69 69 TYR N N 115.661 0.3 1 216 70 70 ASN H H 8.132 0.020 1 217 70 70 ASN CA C 53.918 0.3 1 218 70 70 ASN CB C 37.032 0.3 1 219 70 70 ASN N N 116.066 0.3 1 220 71 71 ILE H H 7.273 0.020 1 221 71 71 ILE CA C 62.115 0.3 1 222 71 71 ILE CB C 36.458 0.3 1 223 71 71 ILE N N 118.996 0.3 1 224 72 72 GLN H H 7.633 0.020 1 225 72 72 GLN CA C 53.344 0.3 1 226 72 72 GLN CB C 31.212 0.3 1 227 72 72 GLN N N 124.777 0.3 1 228 73 73 LYS H H 8.471 0.020 1 229 73 73 LYS CA C 57.771 0.3 1 230 73 73 LYS CB C 32.032 0.3 1 231 73 73 LYS N N 120.167 0.3 1 232 74 74 GLU H H 9.266 0.020 1 233 74 74 GLU CA C 57.935 0.3 1 234 74 74 GLU CB C 25.720 0.3 1 235 74 74 GLU N N 114.833 0.3 1 236 75 75 SER H H 7.679 0.020 1 237 75 75 SER CA C 60.640 0.3 1 238 75 75 SER CB C 64.656 0.3 1 239 75 75 SER N N 115.035 0.3 1 240 76 76 THR H H 8.689 0.020 1 241 76 76 THR CA C 62.279 0.3 1 242 76 76 THR CB C 69.984 0.3 1 243 76 76 THR N N 117.462 0.3 1 244 77 77 LEU H H 9.389 0.020 1 245 77 77 LEU CA C 53.590 0.3 1 246 77 77 LEU CB C 44.163 0.3 1 247 77 77 LEU N N 127.672 0.3 1 248 78 78 HIS H H 9.200 0.020 1 249 78 78 HIS CA C 56.213 0.3 1 250 78 78 HIS CB C 32.278 0.3 1 251 78 78 HIS N N 119.674 0.3 1 252 79 79 LEU H H 8.260 0.020 1 253 79 79 LEU CA C 53.508 0.3 1 254 79 79 LEU CB C 43.835 0.3 1 255 79 79 LEU N N 123.688 0.3 1 256 80 80 VAL H H 9.158 0.020 1 257 80 80 VAL CA C 60.476 0.3 1 258 80 80 VAL CB C 34.409 0.3 1 259 80 80 VAL N N 126.562 0.3 1 260 81 81 LEU H H 8.102 0.020 1 261 81 81 LEU CA C 53.754 0.3 1 262 81 81 LEU CB C 42.524 0.3 1 263 81 81 LEU N N 123.122 0.3 1 264 82 82 ARG H H 8.581 0.020 1 265 82 82 ARG CA C 55.475 0.3 1 266 82 82 ARG CB C 30.884 0.3 1 267 82 82 ARG N N 123.630 0.3 1 268 83 83 LEU H H 8.346 0.020 1 269 83 83 LEU CA C 54.738 0.3 1 270 83 83 LEU CB C 42.196 0.3 1 271 83 83 LEU N N 124.542 0.3 1 272 84 84 ARG H H 8.474 0.020 1 273 84 84 ARG CA C 55.967 0.3 1 274 84 84 ARG CB C 30.310 0.3 1 275 84 84 ARG N N 122.334 0.3 1 276 86 86 GLY H H 8.208 0.020 1 277 86 86 GLY CA C 45.065 0.3 1 278 86 86 GLY N N 108.326 0.3 1 279 87 87 MET H H 8.906 0.020 1 280 87 87 MET CA C 54.574 0.3 1 281 87 87 MET CB C 34.409 0.3 1 282 87 87 MET N N 119.714 0.3 1 283 88 88 GLN H H 8.288 0.020 1 284 88 88 GLN CA C 54.164 0.3 1 285 88 88 GLN CB C 30.474 0.3 1 286 88 88 GLN N N 121.468 0.3 1 287 89 89 ILE H H 8.286 0.020 1 288 89 89 ILE CA C 59.246 0.3 1 289 89 89 ILE CB C 41.622 0.3 1 290 89 89 ILE N N 114.217 0.3 1 291 90 90 PHE H H 8.598 0.020 1 292 90 90 PHE CA C 54.820 0.3 1 293 90 90 PHE CB C 40.966 0.3 1 294 90 90 PHE N N 118.685 0.3 1 295 91 91 VAL H H 9.285 0.020 1 296 91 91 VAL CA C 60.230 0.3 1 297 91 91 VAL CB C 33.835 0.3 1 298 91 91 VAL N N 121.324 0.3 1 299 92 92 LYS H H 8.968 0.020 1 300 92 92 LYS CA C 54.492 0.3 1 301 92 92 LYS CB C 33.835 0.3 1 302 92 92 LYS N N 127.982 0.3 1 303 93 93 THR H H 8.696 0.020 1 304 93 93 THR CA C 60.312 0.3 1 305 93 93 THR CB C 70.230 0.3 1 306 93 93 THR N N 115.121 0.3 1 307 94 94 LEU H H 9.130 0.020 1 308 94 94 LEU CA C 57.279 0.3 1 309 94 94 LEU CB C 41.458 0.3 1 310 94 94 LEU N N 121.311 0.3 1 311 97 97 LYS H H 7.261 0.020 1 312 97 97 LYS CA C 56.049 0.3 1 313 97 97 LYS CB C 33.015 0.3 1 314 97 97 LYS N N 121.864 0.3 1 315 99 99 ILE H H 9.597 0.020 1 316 99 99 ILE CA C 59.954 0.3 1 317 99 99 ILE CB C 40.402 0.3 1 318 99 99 ILE N N 128.299 0.3 1 319 100 100 THR H H 8.741 0.020 1 320 100 100 THR CA C 61.951 0.3 1 321 100 100 THR CB C 69.165 0.3 1 322 100 100 THR N N 122.005 0.3 1 323 101 101 LEU H H 8.707 0.020 1 324 101 101 LEU CA C 52.360 0.3 1 325 101 101 LEU CB C 45.967 0.3 1 326 101 101 LEU N N 125.041 0.3 1 327 102 102 GLU H H 8.158 0.020 1 328 102 102 GLU CA C 55.475 0.3 1 329 102 102 GLU CB C 29.573 0.3 1 330 102 102 GLU N N 122.020 0.3 1 331 103 103 VAL H H 8.668 0.020 1 332 103 103 VAL CA C 58.426 0.3 1 333 103 103 VAL CB C 35.966 0.3 1 334 103 103 VAL N N 116.682 0.3 1 335 104 104 GLU H H 8.500 0.020 1 336 104 104 GLU CA C 53.262 0.3 1 337 104 104 GLU CB C 31.048 0.3 1 338 104 104 GLU N N 118.054 0.3 1 339 106 106 SER H H 7.088 0.020 1 340 106 106 SER CA C 57.197 0.3 1 341 106 106 SER CB C 63.181 0.3 1 342 106 106 SER N N 103.864 0.3 1 343 107 107 ASP H H 8.021 0.020 1 344 107 107 ASP CA C 55.721 0.3 1 345 107 107 ASP CB C 40.557 0.3 1 346 107 107 ASP N N 123.830 0.3 1 347 108 108 THR H H 7.931 0.020 1 348 108 108 THR CA C 59.328 0.3 1 349 108 108 THR CB C 70.968 0.3 1 350 108 108 THR N N 109.618 0.3 1 351 109 109 ILE H H 8.505 0.020 1 352 109 109 ILE CA C 62.033 0.3 1 353 109 109 ILE CB C 34.081 0.3 1 354 109 109 ILE N N 121.278 0.3 1 355 111 111 ASN H H 7.950 0.020 1 356 111 111 ASN CA C 55.803 0.3 1 357 111 111 ASN CB C 38.016 0.3 1 358 111 111 ASN N N 121.250 0.3 1 359 112 112 VAL H H 8.134 0.020 1 360 112 112 VAL CA C 67.525 0.3 1 361 112 112 VAL CB C 30.064 0.3 1 362 112 112 VAL N N 122.132 0.3 1 363 113 113 LYS H H 8.516 0.020 1 364 113 113 LYS CA C 59.082 0.3 1 365 113 113 LYS CB C 33.261 0.3 1 366 113 113 LYS N N 118.978 0.3 1 367 114 114 ALA H H 7.962 0.020 1 368 114 114 ALA CA C 55.066 0.3 1 369 114 114 ALA CB C 17.359 0.3 1 370 114 114 ALA N N 123.448 0.3 1 371 115 115 LYS H H 7.867 0.020 1 372 115 115 LYS CA C 59.574 0.3 1 373 115 115 LYS CB C 33.097 0.3 1 374 115 115 LYS N N 120.278 0.3 1 375 116 116 ILE H H 8.277 0.020 1 376 116 116 ILE CA C 65.968 0.3 1 377 116 116 ILE CB C 36.376 0.3 1 378 116 116 ILE N N 121.372 0.3 1 379 117 117 GLN H H 8.536 0.020 1 380 117 117 GLN CA C 59.738 0.3 1 381 117 117 GLN CB C 27.441 0.3 1 382 117 117 GLN N N 123.941 0.3 1 383 118 118 ASP H H 8.051 0.020 1 384 118 118 ASP CA C 57.279 0.3 1 385 118 118 ASP CB C 40.721 0.3 1 386 118 118 ASP N N 119.875 0.3 1 387 119 119 LYS H H 7.437 0.020 1 388 119 119 LYS CA C 57.965 0.3 1 389 119 119 LYS CB C 33.518 0.3 1 390 119 119 LYS N N 115.524 0.3 1 391 120 120 GLU H H 8.706 0.020 1 392 120 120 GLU CA C 55.024 0.3 1 393 120 120 GLU CB C 32.941 0.3 1 394 120 120 GLU N N 114.352 0.3 1 395 121 121 GLY H H 8.488 0.020 1 396 121 121 GLY CA C 45.684 0.3 1 397 121 121 GLY N N 108.908 0.3 1 398 122 122 ILE H H 6.135 0.020 1 399 122 122 ILE CA C 57.734 0.3 1 400 122 122 ILE CB C 40.091 0.3 1 401 122 122 ILE N N 120.396 0.3 1 402 125 125 ASP H H 8.519 0.020 1 403 125 125 ASP CA C 55.543 0.3 1 404 125 125 ASP CB C 39.457 0.3 1 405 125 125 ASP N N 113.607 0.3 1 406 126 126 GLN H H 7.795 0.020 1 407 126 126 GLN CA C 55.255 0.3 1 408 126 126 GLN CB C 29.770 0.3 1 409 126 126 GLN N N 116.865 0.3 1 410 127 127 GLN H H 7.465 0.020 1 411 127 127 GLN CA C 56.350 0.3 1 412 127 127 GLN CB C 31.154 0.3 1 413 127 127 GLN N N 118.060 0.3 1 414 129 129 LEU H H 8.793 0.020 1 415 129 129 LEU CA C 52.718 0.3 1 416 129 129 LEU CB C 45.395 0.3 1 417 129 129 LEU N N 124.441 0.3 1 418 130 130 ILE H H 9.125 0.020 1 419 130 130 ILE CA C 58.772 0.3 1 420 130 130 ILE CB C 40.783 0.3 1 421 130 130 ILE N N 122.373 0.3 1 422 133 133 GLY H H 8.083 0.020 1 423 133 133 GLY CA C 45.049 0.3 1 424 133 133 GLY N N 102.419 0.3 1 425 134 134 LYS H H 7.952 0.020 1 426 134 134 LYS CA C 54.328 0.3 1 427 134 134 LYS CB C 33.999 0.3 1 428 134 134 LYS N N 122.039 0.3 1 429 135 135 GLN H H 8.644 0.020 1 430 135 135 GLN CA C 55.967 0.3 1 431 135 135 GLN CB C 28.917 0.3 1 432 135 135 GLN N N 123.241 0.3 1 433 136 136 LEU H H 8.548 0.020 1 434 136 136 LEU CA C 53.918 0.3 1 435 136 136 LEU CB C 41.212 0.3 1 436 136 136 LEU N N 125.730 0.3 1 437 140 140 ARG H H 7.441 0.020 1 438 140 140 ARG CA C 54.000 0.3 1 439 140 140 ARG CB C 32.360 0.3 1 440 140 140 ARG N N 119.329 0.3 1 441 141 141 THR H H 8.832 0.020 1 442 141 141 THR CA C 59.328 0.3 1 443 141 141 THR CB C 72.034 0.3 1 444 141 141 THR N N 108.810 0.3 1 445 142 142 LEU H H 8.176 0.020 1 446 142 142 LEU CA C 58.508 0.3 1 447 142 142 LEU CB C 39.983 0.3 1 448 142 142 LEU N N 117.750 0.3 1 449 143 143 SER H H 8.366 0.020 1 450 143 143 SER CA C 60.803 0.3 1 451 143 143 SER CB C 62.197 0.3 1 452 143 143 SER N N 113.273 0.3 1 453 144 144 ASP H H 7.940 0.020 1 454 144 144 ASP CA C 57.279 0.3 1 455 144 144 ASP CB C 39.901 0.3 1 456 144 144 ASP N N 124.587 0.3 1 457 145 145 TYR H H 7.224 0.020 1 458 145 145 TYR CA C 58.016 0.3 1 459 145 145 TYR CB C 39.737 0.3 1 460 145 145 TYR N N 115.709 0.3 1 461 146 146 ASN H H 8.142 0.020 1 462 146 146 ASN CA C 53.918 0.3 1 463 146 146 ASN CB C 37.114 0.3 1 464 146 146 ASN N N 115.973 0.3 1 465 147 147 ILE H H 7.380 0.020 1 466 147 147 ILE CA C 61.869 0.3 1 467 147 147 ILE CB C 36.458 0.3 1 468 147 147 ILE N N 118.701 0.3 1 469 148 148 GLN H H 7.843 0.020 1 470 148 148 GLN CA C 53.508 0.3 1 471 148 148 GLN CB C 30.802 0.3 1 472 148 148 GLN N N 125.658 0.3 1 473 149 149 LYS H H 8.415 0.020 1 474 149 149 LYS CA C 57.771 0.3 1 475 149 149 LYS CB C 32.032 0.3 1 476 149 149 LYS N N 119.728 0.3 1 477 150 150 GLU H H 9.304 0.020 1 478 150 150 GLU CA C 58.016 0.3 1 479 150 150 GLU CB C 25.802 0.3 1 480 150 150 GLU N N 114.933 0.3 1 481 151 151 SER H H 7.631 0.020 1 482 151 151 SER CA C 60.558 0.3 1 483 151 151 SER CB C 64.574 0.3 1 484 151 151 SER N N 115.129 0.3 1 485 152 152 THR H H 8.659 0.020 1 486 152 152 THR CA C 62.197 0.3 1 487 152 152 THR CB C 69.984 0.3 1 488 152 152 THR N N 117.384 0.3 1 489 153 153 LEU H H 9.411 0.020 1 490 153 153 LEU CA C 53.590 0.3 1 491 153 153 LEU CB C 44.245 0.3 1 492 153 153 LEU N N 127.948 0.3 1 493 154 154 HIS H H 9.153 0.020 1 494 154 154 HIS CA C 56.131 0.3 1 495 154 154 HIS CB C 32.360 0.3 1 496 154 154 HIS N N 119.499 0.3 1 497 155 155 LEU H H 8.260 0.020 1 498 155 155 LEU CA C 53.508 0.3 1 499 155 155 LEU CB C 43.835 0.3 1 500 155 155 LEU N N 123.647 0.3 1 501 156 156 VAL H H 9.170 0.020 1 502 156 156 VAL CA C 60.394 0.3 1 503 156 156 VAL CB C 34.409 0.3 1 504 156 156 VAL N N 127.007 0.3 1 505 157 157 LEU H H 8.103 0.020 1 506 157 157 LEU CA C 53.672 0.3 1 507 157 157 LEU CB C 42.524 0.3 1 508 157 157 LEU N N 123.090 0.3 1 509 158 158 ARG H H 8.579 0.020 1 510 158 158 ARG CA C 55.393 0.3 1 511 158 158 ARG CB C 30.884 0.3 1 512 158 158 ARG N N 123.684 0.3 1 513 159 159 LEU H H 8.379 0.020 1 514 159 159 LEU CA C 54.902 0.3 1 515 159 159 LEU CB C 42.032 0.3 1 516 159 159 LEU N N 124.594 0.3 1 517 162 162 GLY H H 7.934 0.020 1 518 162 162 GLY CA C 45.557 0.3 1 519 162 162 GLY N N 115.104 0.3 1 stop_ save_