data_27358 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; DNA binding protein inhibitor ID2 in 8M urea pH2.3 ; _BMRB_accession_number 27358 _BMRB_flat_file_name bmr27358.str _Entry_type original _Submission_date 2018-01-15 _Accession_date 2018-01-15 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone assignment of full-length ID2 under denaturing conditions (8M urea pH2.3)' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Roschger Cornelia . . 2 Schubert Mario . . 3 Cabrele Chiara . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 129 "13C chemical shifts" 382 "15N chemical shifts" 124 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-04-18 original BMRB . stop_ _Original_release_date 2018-01-16 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The Recombinant Inhibitor of DNA Binding Id2 Forms Multimeric Structures via the Helix-Loop-Helix Domain and the Nuclear Export Signal ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29642431 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Roschger Cornelia . . 2 Schubert Mario . . 3 Regl Christof . . 4 Andosch Ancuela . . 5 'Marquez Macheda' Augusto . . 6 Berger Thomas . . 7 Huber Christian G. . 8 Lutz-Meindl Ursula . . 9 Cabrele Chiara . . stop_ _Journal_abbreviation 'Int. J. Mol. Sci.' _Journal_name_full 'International journal of molecular sciences' _Journal_volume 19 _Journal_issue 4 _Journal_ISSN 1422-0067 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first E1105 _Page_last E1105 _Year 2018 _Details . loop_ _Keyword helix-loop-helix 'inhibitor of DNA binding' 'intrinsic disorder' 'protein oligomerization' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Id2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Id2 $Id2 stop_ _System_molecular_weight . _System_physical_state denatured _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Id2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Id2 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function 'DNA binding inhibitor' stop_ _Details 'Both cysteines in the sequence are oxidized with beta-mercaptoethanol (-S-CH2-CH2-OH) according to mass spectrometry.' ############################## # Polymer residue sequence # ############################## _Residue_count 134 _Mol_residue_sequence ; MKAFSPVRSVRKNSLSDHSL GISRSKTPVDDPMSLLYNMN DCYSKLKELVPSIPQNKKVS KMEILQHVIDYILDLQIALD SHPTIVSLHHQRPGQNQASR TPLTTLNTDISILSLQASEF PSELMSNDSKALCG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 ALA 4 PHE 5 SER 6 PRO 7 VAL 8 ARG 9 SER 10 VAL 11 ARG 12 LYS 13 ASN 14 SER 15 LEU 16 SER 17 ASP 18 HIS 19 SER 20 LEU 21 GLY 22 ILE 23 SER 24 ARG 25 SER 26 LYS 27 THR 28 PRO 29 VAL 30 ASP 31 ASP 32 PRO 33 MET 34 SER 35 LEU 36 LEU 37 TYR 38 ASN 39 MET 40 ASN 41 ASP 42 CYS 43 TYR 44 SER 45 LYS 46 LEU 47 LYS 48 GLU 49 LEU 50 VAL 51 PRO 52 SER 53 ILE 54 PRO 55 GLN 56 ASN 57 LYS 58 LYS 59 VAL 60 SER 61 LYS 62 MET 63 GLU 64 ILE 65 LEU 66 GLN 67 HIS 68 VAL 69 ILE 70 ASP 71 TYR 72 ILE 73 LEU 74 ASP 75 LEU 76 GLN 77 ILE 78 ALA 79 LEU 80 ASP 81 SER 82 HIS 83 PRO 84 THR 85 ILE 86 VAL 87 SER 88 LEU 89 HIS 90 HIS 91 GLN 92 ARG 93 PRO 94 GLY 95 GLN 96 ASN 97 GLN 98 ALA 99 SER 100 ARG 101 THR 102 PRO 103 LEU 104 THR 105 THR 106 LEU 107 ASN 108 THR 109 ASP 110 ILE 111 SER 112 ILE 113 LEU 114 SER 115 LEU 116 GLN 117 ALA 118 SER 119 GLU 120 PHE 121 PRO 122 SER 123 GLU 124 LEU 125 MET 126 SER 127 ASN 128 ASP 129 SER 130 LYS 131 ALA 132 LEU 133 CYS 134 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 SP Q02363 'ID2_HUMAN DNA-binding protein inhibitor ID2' . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Id2 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 $Id2 'recombinant technology' . Escherichia coli . pET22b+ 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 $Id2 0.74 mM '[U-99% 13C; U-99% 15N]' urea 8 M 'natural abundance' chloride 180 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.2 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'Avance III HD' 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_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_(H)NCANH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (H)NCANH' _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' 180 . mM pH 2.3 . 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 . 'separate tube (no insert) similar to the experimental sample tube' . 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_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCACB' '3D CBCA(CO)NH' '3D HNCO' '3D HN(CA)CO' '3D (H)NCANH' 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 Id2 _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 1 1 MET CA C 55.104 0.2 1 2 1 1 MET CB C 33.049 0.2 1 3 2 2 LYS H H 8.749 0.01 1 4 2 2 LYS CA C 56.453 0.2 1 5 2 2 LYS CB C 33.317 0.2 1 6 2 2 LYS N N 125.124 0.2 1 7 3 3 ALA H H 8.378 0.01 1 8 3 3 ALA CA C 52.176 0.2 1 9 3 3 ALA CB C 19.435 0.2 1 10 3 3 ALA N N 126.268 0.2 1 11 4 4 PHE H H 8.304 0.01 1 12 4 4 PHE HB2 H 2.975 0.01 1 13 4 4 PHE HB3 H 2.975 0.01 1 14 4 4 PHE CA C 57.711 0.2 1 15 4 4 PHE CB C 39.904 0.2 1 16 4 4 PHE N N 120.603 0.2 1 17 5 5 SER H H 8.200 0.01 1 18 5 5 SER CA C 55.822 0.2 1 19 5 5 SER N N 119.515 0.2 1 20 6 6 PRO C C 176.579 0.2 1 21 6 6 PRO CA C 63.048 0.2 1 22 6 6 PRO CB C 32.108 0.2 1 23 7 7 VAL H H 8.128 0.01 1 24 7 7 VAL C C 176.134 0.2 1 25 7 7 VAL CA C 62.371 0.2 1 26 7 7 VAL CB C 32.653 0.2 1 27 7 7 VAL N N 120.534 0.2 1 28 8 8 ARG H H 8.380 0.01 1 29 8 8 ARG C C 176.050 0.2 1 30 8 8 ARG CA C 55.946 0.2 1 31 8 8 ARG CB C 31.041 0.2 1 32 8 8 ARG N N 125.294 0.2 1 33 9 9 SER H H 8.325 0.01 1 34 9 9 SER C C 174.324 0.2 1 35 9 9 SER CA C 58.035 0.2 1 36 9 9 SER CB C 63.985 0.2 1 37 9 9 SER N N 117.872 0.2 1 38 10 10 VAL H H 8.202 0.01 1 39 10 10 VAL C C 175.927 0.2 1 40 10 10 VAL CA C 62.108 0.2 1 41 10 10 VAL CB C 32.897 0.2 1 42 10 10 VAL N N 122.083 0.2 1 43 11 11 ARG H H 8.374 0.01 1 44 11 11 ARG C C 176.131 0.2 1 45 11 11 ARG CA C 55.946 0.2 1 46 11 11 ARG CB C 30.934 0.2 1 47 11 11 ARG N N 125.288 0.2 1 48 12 12 LYS H H 8.458 0.01 1 49 12 12 LYS C C 176.243 0.2 1 50 12 12 LYS CA C 56.382 0.2 1 51 12 12 LYS CB C 33.352 0.2 1 52 12 12 LYS N N 123.872 0.2 1 53 13 13 ASN H H 8.531 0.01 1 54 13 13 ASN C C 175.271 0.2 1 55 13 13 ASN CA C 53.204 0.2 1 56 13 13 ASN CB C 38.961 0.2 1 57 13 13 ASN N N 120.493 0.2 1 58 14 14 SER H H 8.322 0.01 1 59 14 14 SER C C 174.548 0.2 1 60 14 14 SER CA C 58.429 0.2 1 61 14 14 SER CB C 63.919 0.2 1 62 14 14 SER N N 116.524 0.2 1 63 15 15 LEU H H 8.277 0.01 1 64 15 15 LEU C C 177.361 0.2 1 65 15 15 LEU CA C 55.318 0.2 1 66 15 15 LEU CB C 42.295 0.2 1 67 15 15 LEU N N 123.981 0.2 1 68 16 16 SER H H 8.220 0.01 1 69 16 16 SER CA C 58.238 0.2 1 70 16 16 SER CB C 63.934 0.2 1 71 16 16 SER N N 115.850 0.2 1 72 17 17 ASP H H 8.383 0.01 1 73 17 17 ASP C C 174.968 0.2 1 74 17 17 ASP CA C 52.981 0.2 1 75 17 17 ASP CB C 38.061 0.2 1 76 17 17 ASP N N 120.911 0.2 1 77 18 18 HIS H H 8.442 0.01 1 78 18 18 HIS C C 174.324 0.2 1 79 18 18 HIS CA C 55.349 0.2 1 80 18 18 HIS CB C 28.922 0.2 1 81 18 18 HIS N N 119.060 0.2 1 82 19 19 SER H H 8.295 0.01 1 83 19 19 SER C C 174.469 0.2 1 84 19 19 SER CA C 58.468 0.2 1 85 19 19 SER CB C 63.900 0.2 1 86 19 19 SER N N 116.959 0.2 1 87 20 20 LEU H H 8.315 0.01 1 88 20 20 LEU C C 177.679 0.2 1 89 20 20 LEU CA C 55.334 0.2 1 90 20 20 LEU CB C 42.597 0.2 1 91 20 20 LEU N N 124.124 0.2 1 92 21 21 GLY H H 8.303 0.01 1 93 21 21 GLY C C 173.813 0.2 1 94 21 21 GLY CA C 45.233 0.2 1 95 21 21 GLY N N 109.330 0.2 1 96 22 22 ILE H H 7.937 0.01 1 97 22 22 ILE CA C 60.999 0.2 1 98 22 22 ILE CB C 39.037 0.2 1 99 22 22 ILE N N 119.705 0.2 1 100 23 23 SER H H 8.380 0.01 1 101 23 23 SER C C 174.491 0.2 1 102 23 23 SER CA C 58.263 0.2 1 103 23 23 SER CB C 63.953 0.2 1 104 23 23 SER N N 120.068 0.2 1 105 24 24 ARG H H 8.415 0.01 1 106 24 24 ARG C C 176.247 0.2 1 107 24 24 ARG CA C 56.085 0.2 1 108 24 24 ARG CB C 30.970 0.2 1 109 24 24 ARG N N 123.707 0.2 1 110 25 25 SER H H 8.310 0.01 1 111 25 25 SER C C 174.491 0.2 1 112 25 25 SER CA C 58.382 0.2 1 113 25 25 SER CB C 63.960 0.2 1 114 25 25 SER N N 117.037 0.2 1 115 26 26 LYS H H 8.410 0.01 1 116 26 26 LYS C C 176.417 0.2 1 117 26 26 LYS CA C 56.420 0.2 1 118 26 26 LYS CB C 33.220 0.2 1 119 26 26 LYS N N 123.570 0.2 1 120 27 27 THR H H 8.168 0.01 1 121 27 27 THR HA H 4.482 0.01 1 122 27 27 THR CA C 59.984 0.2 1 123 27 27 THR CB C 69.674 0.2 1 124 27 27 THR N N 117.639 0.2 1 125 28 28 PRO C C 176.627 0.2 1 126 28 28 PRO CA C 63.188 0.2 1 127 28 28 PRO CB C 32.279 0.2 1 128 29 29 VAL H H 8.150 0.01 1 129 29 29 VAL C C 175.786 0.2 1 130 29 29 VAL CA C 62.337 0.2 1 131 29 29 VAL CB C 32.839 0.2 1 132 29 29 VAL N N 120.135 0.2 1 133 30 30 ASP H H 8.445 0.01 1 134 30 30 ASP C C 174.207 0.2 1 135 30 30 ASP CA C 52.704 0.2 1 136 30 30 ASP CB C 38.307 0.2 1 137 30 30 ASP N N 122.130 0.2 1 138 31 31 ASP H H 8.400 0.01 1 139 31 31 ASP CA C 51.069 0.2 1 140 31 31 ASP CB C 38.131 0.2 1 141 31 31 ASP N N 120.025 0.2 1 142 32 32 PRO C C 176.850 0.2 1 143 32 32 PRO CA C 63.582 0.2 1 144 32 32 PRO CB C 32.064 0.2 1 145 33 33 MET H H 8.265 0.01 1 146 33 33 MET C C 176.366 0.2 1 147 33 33 MET CA C 55.811 0.2 1 148 33 33 MET CB C 32.738 0.2 1 149 33 33 MET N N 119.572 0.2 1 150 34 34 SER H H 8.156 0.01 1 151 34 34 SER C C 174.459 0.2 1 152 34 34 SER CA C 58.456 0.2 1 153 34 34 SER CB C 63.816 0.2 1 154 34 34 SER N N 116.423 0.2 1 155 35 35 LEU H H 8.149 0.01 1 156 35 35 LEU C C 176.914 0.2 1 157 35 35 LEU CA C 55.236 0.2 1 158 35 35 LEU CB C 42.248 0.2 1 159 35 35 LEU N N 124.184 0.2 1 160 36 36 LEU H H 8.039 0.01 1 161 36 36 LEU C C 176.885 0.2 1 162 36 36 LEU CA C 55.183 0.2 1 163 36 36 LEU CB C 42.411 0.2 1 164 36 36 LEU N N 121.982 0.2 1 165 37 37 TYR H H 8.027 0.01 1 166 37 37 TYR C C 175.353 0.2 1 167 37 37 TYR CA C 57.653 0.2 1 168 37 37 TYR CB C 38.968 0.2 1 169 37 37 TYR N N 120.226 0.2 1 170 38 38 ASN H H 8.326 0.01 1 171 38 38 ASN C C 175.247 0.2 1 172 38 38 ASN CA C 53.040 0.2 1 173 38 38 ASN CB C 38.923 0.2 1 174 38 38 ASN N N 120.380 0.2 1 175 39 39 MET H H 8.308 0.01 1 176 39 39 MET C C 176.052 0.2 1 177 39 39 MET CA C 55.911 0.2 1 178 39 39 MET CB C 32.504 0.2 1 179 39 39 MET N N 121.216 0.2 1 180 40 40 ASN H H 8.372 0.01 1 181 40 40 ASN C C 175.087 0.2 1 182 40 40 ASN CA C 53.611 0.2 1 183 40 40 ASN CB C 38.767 0.2 1 184 40 40 ASN N N 118.771 0.2 1 185 41 41 ASP H H 8.250 0.01 1 186 41 41 ASP C C 174.930 0.2 1 187 41 41 ASP CA C 53.036 0.2 1 188 41 41 ASP CB C 38.042 0.2 1 189 41 41 ASP N N 118.688 0.2 1 190 42 42 CYS H H 8.199 0.01 1 191 42 42 CYS C C 174.389 0.2 1 192 42 42 CYS CA C 55.873 0.2 1 193 42 42 CYS CB C 40.996 0.2 1 194 42 42 CYS N N 118.921 0.2 1 195 43 43 TYR H H 8.147 0.01 1 196 43 43 TYR C C 175.699 0.2 1 197 43 43 TYR CA C 58.110 0.2 1 198 43 43 TYR CB C 38.713 0.2 1 199 43 43 TYR N N 121.717 0.2 1 200 44 44 SER H H 8.127 0.01 1 201 44 44 SER C C 174.389 0.2 1 202 44 44 SER CA C 58.266 0.2 1 203 44 44 SER CB C 63.993 0.2 1 204 44 44 SER N N 117.037 0.2 1 205 45 45 LYS H H 8.250 0.01 1 206 45 45 LYS C C 176.420 0.2 1 207 45 45 LYS CA C 56.555 0.2 1 208 45 45 LYS CB C 33.005 0.2 1 209 45 45 LYS N N 123.568 0.2 1 210 46 46 LEU H H 8.112 0.01 1 211 46 46 LEU C C 177.219 0.2 1 212 46 46 LEU CA C 55.192 0.2 1 213 46 46 LEU CB C 42.383 0.2 1 214 46 46 LEU N N 122.850 0.2 1 215 47 47 LYS H H 8.341 0.01 1 216 47 47 LYS C C 176.290 0.2 1 217 47 47 LYS CA C 56.366 0.2 1 218 47 47 LYS CB C 33.089 0.2 1 219 47 47 LYS N N 122.690 0.2 1 220 48 48 GLU H H 8.287 0.01 1 221 48 48 GLU C C 175.589 0.2 1 222 48 48 GLU CA C 55.425 0.2 1 223 48 48 GLU CB C 28.969 0.2 1 224 48 48 GLU N N 121.794 0.2 1 225 49 49 LEU H H 8.329 0.01 1 226 49 49 LEU C C 176.829 0.2 1 227 49 49 LEU CA C 55.085 0.2 1 228 49 49 LEU CB C 42.262 0.2 1 229 49 49 LEU N N 124.531 0.2 1 230 50 50 VAL H H 8.190 0.01 1 231 50 50 VAL CA C 59.724 0.2 1 232 50 50 VAL CB C 32.608 0.2 1 233 50 50 VAL N N 122.477 0.2 1 234 51 51 PRO C C 176.562 0.2 1 235 51 51 PRO CA C 63.132 0.2 1 236 51 51 PRO CB C 32.205 0.2 1 237 52 52 SER H H 8.301 0.01 1 238 52 52 SER C C 174.159 0.2 1 239 52 52 SER CA C 58.097 0.2 1 240 52 52 SER CB C 63.887 0.2 1 241 52 52 SER N N 116.521 0.2 1 242 53 53 ILE H H 8.127 0.01 1 243 53 53 ILE CA C 58.724 0.2 1 244 53 53 ILE CB C 38.929 0.2 1 245 53 53 ILE N N 123.601 0.2 1 246 54 54 PRO C C 176.759 0.2 1 247 54 54 PRO CA C 63.264 0.2 1 248 54 54 PRO CB C 32.129 0.2 1 249 55 55 GLN H H 8.458 0.01 1 250 55 55 GLN C C 175.854 0.2 1 251 55 55 GLN CA C 55.952 0.2 1 252 55 55 GLN CB C 29.743 0.2 1 253 55 55 GLN N N 120.856 0.2 1 254 56 56 ASN H H 8.429 0.01 1 255 56 56 ASN C C 175.072 0.2 1 256 56 56 ASN CA C 53.145 0.2 1 257 56 56 ASN CB C 38.808 0.2 1 258 56 56 ASN N N 119.966 0.2 1 259 57 57 LYS H H 8.272 0.01 1 260 57 57 LYS C C 176.270 0.2 1 261 57 57 LYS CA C 56.382 0.2 1 262 57 57 LYS CB C 33.309 0.2 1 263 57 57 LYS N N 122.066 0.2 1 264 58 58 LYS H H 8.340 0.01 1 265 58 58 LYS C C 176.448 0.2 1 266 58 58 LYS CA C 56.421 0.2 1 267 58 58 LYS CB C 33.117 0.2 1 268 58 58 LYS N N 123.211 0.2 1 269 59 59 VAL H H 8.190 0.01 1 270 59 59 VAL C C 176.058 0.2 1 271 59 59 VAL CA C 61.978 0.2 1 272 59 59 VAL CB C 33.079 0.2 1 273 59 59 VAL N N 121.850 0.2 1 274 60 60 SER H H 8.375 0.01 1 275 60 60 SER C C 174.434 0.2 1 276 60 60 SER CA C 58.151 0.2 1 277 60 60 SER CB C 64.070 0.2 1 278 60 60 SER N N 120.227 0.2 1 279 61 61 LYS H H 8.393 0.01 1 280 61 61 LYS C C 176.342 0.2 1 281 61 61 LYS CA C 56.540 0.2 1 282 61 61 LYS CB C 33.243 0.2 1 283 61 61 LYS N N 123.851 0.2 1 284 62 62 MET H H 8.354 0.01 1 285 62 62 MET C C 175.988 0.2 1 286 62 62 MET CA C 55.530 0.2 1 287 62 62 MET CB C 33.091 0.2 1 288 62 62 MET N N 121.487 0.2 1 289 63 63 GLU H H 8.377 0.01 1 290 63 63 GLU C C 175.562 0.2 1 291 63 63 GLU CA C 55.665 0.2 1 292 63 63 GLU CB C 28.919 0.2 1 293 63 63 GLU N N 122.517 0.2 1 294 64 64 ILE H H 8.226 0.01 1 295 64 64 ILE C C 175.975 0.2 1 296 64 64 ILE CA C 60.980 0.2 1 297 64 64 ILE CB C 38.471 0.2 1 298 64 64 ILE N N 123.209 0.2 1 299 65 65 LEU H H 8.313 0.01 1 300 65 65 LEU C C 176.962 0.2 1 301 65 65 LEU CA C 54.941 0.2 1 302 65 65 LEU CB C 42.304 0.2 1 303 65 65 LEU N N 126.846 0.2 1 304 66 66 GLN H H 8.371 0.01 1 305 66 66 GLN C C 175.739 0.2 1 306 66 66 GLN CA C 55.706 0.2 1 307 66 66 GLN CB C 29.796 0.2 1 308 66 66 GLN N N 121.363 0.2 1 309 67 67 HIS H H 8.584 0.01 1 310 67 67 HIS C C 174.086 0.2 1 311 67 67 HIS CA C 55.178 0.2 1 312 67 67 HIS CB C 28.908 0.2 1 313 67 67 HIS N N 120.045 0.2 1 314 68 68 VAL H H 8.231 0.01 1 315 68 68 VAL C C 175.667 0.2 1 316 68 68 VAL CA C 62.366 0.2 1 317 68 68 VAL CB C 32.943 0.2 1 318 68 68 VAL N N 122.476 0.2 1 319 69 69 ILE H H 8.278 0.01 1 320 69 69 ILE C C 175.480 0.2 1 321 69 69 ILE CA C 60.908 0.2 1 322 69 69 ILE CB C 38.681 0.2 1 323 69 69 ILE N N 125.057 0.2 1 324 70 70 ASP H H 8.421 0.01 1 325 70 70 ASP C C 174.436 0.2 1 326 70 70 ASP CA C 52.571 0.2 1 327 70 70 ASP CB C 38.288 0.2 1 328 70 70 ASP N N 123.458 0.2 1 329 71 71 TYR H H 8.066 0.01 1 330 71 71 TYR C C 175.387 0.2 1 331 71 71 TYR CA C 58.216 0.2 1 332 71 71 TYR CB C 38.814 0.2 1 333 71 71 TYR N N 121.656 0.2 1 334 72 72 ILE H H 8.091 0.01 1 335 72 72 ILE C C 175.928 0.2 1 336 72 72 ILE CA C 61.083 0.2 1 337 72 72 ILE CB C 38.519 0.2 1 338 72 72 ILE N N 122.594 0.2 1 339 73 73 LEU H H 8.134 0.01 1 340 73 73 LEU C C 176.791 0.2 1 341 73 73 LEU CA C 55.307 0.2 1 342 73 73 LEU CB C 42.502 0.2 1 343 73 73 LEU N N 125.924 0.2 1 344 74 74 ASP H H 8.431 0.01 1 345 74 74 ASP C C 174.976 0.2 1 346 74 74 ASP CA C 52.832 0.2 1 347 74 74 ASP CB C 37.873 0.2 1 348 74 74 ASP N N 119.977 0.2 1 349 75 75 LEU H H 8.125 0.01 1 350 75 75 LEU C C 177.116 0.2 1 351 75 75 LEU CA C 55.383 0.2 1 352 75 75 LEU CB C 42.386 0.2 1 353 75 75 LEU N N 122.989 0.2 1 354 76 76 GLN H H 8.273 0.01 1 355 76 76 GLN C C 175.951 0.2 1 356 76 76 GLN CA C 56.138 0.2 1 357 76 76 GLN CB C 29.169 0.2 1 358 76 76 GLN N N 120.765 0.2 1 359 77 77 ILE H H 7.948 0.01 1 360 77 77 ILE C C 175.886 0.2 1 361 77 77 ILE CA C 61.246 0.2 1 362 77 77 ILE CB C 38.828 0.2 1 363 77 77 ILE N N 121.371 0.2 1 364 78 78 ALA H H 8.232 0.01 1 365 78 78 ALA C C 177.598 0.2 1 366 78 78 ALA CA C 52.457 0.2 1 367 78 78 ALA CB C 19.046 0.2 1 368 78 78 ALA N N 127.486 0.2 1 369 79 79 LEU H H 8.139 0.01 1 370 79 79 LEU C C 177.248 0.2 1 371 79 79 LEU CA C 55.271 0.2 1 372 79 79 LEU CB C 42.367 0.2 1 373 79 79 LEU N N 121.581 0.2 1 374 80 80 ASP H H 8.380 0.01 1 375 80 80 ASP C C 174.876 0.2 1 376 80 80 ASP CA C 52.825 0.2 1 377 80 80 ASP CB C 38.068 0.2 1 378 80 80 ASP N N 119.133 0.2 1 379 81 81 SER H H 8.085 0.01 1 380 81 81 SER C C 173.850 0.2 1 381 81 81 SER CA C 58.385 0.2 1 382 81 81 SER CB C 63.904 0.2 1 383 81 81 SER N N 115.931 0.2 1 384 82 82 HIS H H 8.377 0.01 1 385 82 82 HIS CA C 53.340 0.2 1 386 82 82 HIS CB C 28.595 0.2 1 387 82 82 HIS N N 119.958 0.2 1 388 83 83 PRO C C 176.885 0.2 1 389 83 83 PRO CA C 63.217 0.2 1 390 83 83 PRO CB C 32.224 0.2 1 391 84 84 THR H H 8.366 0.01 1 392 84 84 THR C C 174.350 0.2 1 393 84 84 THR CA C 62.143 0.2 1 394 84 84 THR CB C 70.022 0.2 1 395 84 84 THR N N 115.995 0.2 1 396 85 85 ILE H H 8.230 0.01 1 397 85 85 ILE C C 175.966 0.2 1 398 85 85 ILE CA C 60.925 0.2 1 399 85 85 ILE CB C 38.754 0.2 1 400 85 85 ILE N N 124.203 0.2 1 401 86 86 VAL H H 8.226 0.01 1 402 86 86 VAL C C 175.864 0.2 1 403 86 86 VAL CA C 62.172 0.2 1 404 86 86 VAL CB C 32.825 0.2 1 405 86 86 VAL N N 124.985 0.2 1 406 87 87 SER H H 8.318 0.01 1 407 87 87 SER C C 174.329 0.2 1 408 87 87 SER CA C 57.908 0.2 1 409 87 87 SER CB C 63.863 0.2 1 410 87 87 SER N N 119.868 0.2 1 411 88 88 LEU H H 8.250 0.01 1 412 88 88 LEU C C 177.028 0.2 1 413 88 88 LEU CA C 55.112 0.2 1 414 88 88 LEU CB C 42.458 0.2 1 415 88 88 LEU N N 124.737 0.2 1 416 89 89 HIS H H 8.502 0.01 1 417 89 89 HIS C C 174.236 0.2 1 418 89 89 HIS CA C 55.034 0.2 1 419 89 89 HIS CB C 28.894 0.2 1 420 89 89 HIS N N 118.727 0.2 1 421 90 90 HIS H H 8.608 0.01 1 422 90 90 HIS C C 174.127 0.2 1 423 90 90 HIS CA C 55.183 0.2 1 424 90 90 HIS CB C 29.130 0.2 1 425 90 90 HIS N N 120.378 0.2 1 426 91 91 GLN H H 8.551 0.01 1 427 91 91 GLN C C 175.614 0.2 1 428 91 91 GLN CA C 55.845 0.2 1 429 91 91 GLN CB C 29.895 0.2 1 430 91 91 GLN N N 122.490 0.2 1 431 92 92 ARG H H 8.545 0.01 1 432 92 92 ARG CA C 54.274 0.2 1 433 92 92 ARG CB C 30.043 0.2 1 434 92 92 ARG N N 124.042 0.2 1 435 93 93 PRO C C 177.237 0.2 1 436 93 93 PRO CA C 63.409 0.2 1 437 93 93 PRO CB C 32.213 0.2 1 438 94 94 GLY H H 8.411 0.01 1 439 94 94 GLY C C 174.008 0.2 1 440 94 94 GLY CA C 45.204 0.2 1 441 94 94 GLY N N 109.284 0.2 1 442 95 95 GLN H H 8.176 0.01 1 443 95 95 GLN C C 175.817 0.2 1 444 95 95 GLN CA C 55.918 0.2 1 445 95 95 GLN CB C 29.717 0.2 1 446 95 95 GLN N N 119.638 0.2 1 447 96 96 ASN H H 8.543 0.01 1 448 96 96 ASN C C 175.189 0.2 1 449 96 96 ASN CA C 53.416 0.2 1 450 96 96 ASN CB C 38.826 0.2 1 451 96 96 ASN N N 120.103 0.2 1 452 97 97 GLN H H 8.356 0.01 1 453 97 97 GLN C C 175.629 0.2 1 454 97 97 GLN CA C 55.989 0.2 1 455 97 97 GLN CB C 29.543 0.2 1 456 97 97 GLN N N 121.001 0.2 1 457 98 98 ALA H H 8.289 0.01 1 458 98 98 ALA C C 177.659 0.2 1 459 98 98 ALA CA C 52.598 0.2 1 460 98 98 ALA CB C 19.199 0.2 1 461 98 98 ALA N N 125.045 0.2 1 462 99 99 SER H H 8.209 0.01 1 463 99 99 SER C C 174.525 0.2 1 464 99 99 SER CA C 58.355 0.2 1 465 99 99 SER CB C 63.932 0.2 1 466 99 99 SER N N 115.146 0.2 1 467 100 100 ARG H H 8.352 0.01 1 468 100 100 ARG C C 176.095 0.2 1 469 100 100 ARG CA C 56.071 0.2 1 470 100 100 ARG CB C 31.042 0.2 1 471 100 100 ARG N N 123.022 0.2 1 472 101 101 THR H H 8.203 0.01 1 473 101 101 THR CA C 60.019 0.2 1 474 101 101 THR CB C 69.732 0.2 1 475 101 101 THR N N 117.791 0.2 1 476 102 102 PRO C C 176.603 0.2 1 477 102 102 PRO CA C 63.163 0.2 1 478 102 102 PRO CB C 32.172 0.2 1 479 103 103 LEU H H 8.326 0.01 1 480 103 103 LEU C C 177.581 0.2 1 481 103 103 LEU CA C 55.357 0.2 1 482 103 103 LEU CB C 42.411 0.2 1 483 103 103 LEU N N 122.746 0.2 1 484 104 104 THR H H 8.145 0.01 1 485 104 104 THR C C 174.586 0.2 1 486 104 104 THR CA C 61.667 0.2 1 487 104 104 THR CB C 70.066 0.2 1 488 104 104 THR N N 114.778 0.2 1 489 105 105 THR H H 8.127 0.01 1 490 105 105 THR C C 174.301 0.2 1 491 105 105 THR CA C 61.702 0.2 1 492 105 105 THR CB C 69.933 0.2 1 493 105 105 THR N N 116.206 0.2 1 494 106 106 LEU H H 8.204 0.01 1 495 106 106 LEU C C 176.857 0.2 1 496 106 106 LEU CA C 55.179 0.2 1 497 106 106 LEU CB C 42.590 0.2 1 498 106 106 LEU N N 124.411 0.2 1 499 107 107 ASN H H 8.489 0.01 1 500 107 107 ASN C C 175.432 0.2 1 501 107 107 ASN CA C 53.257 0.2 1 502 107 107 ASN CB C 38.803 0.2 1 503 107 107 ASN N N 120.114 0.2 1 504 108 108 THR H H 8.084 0.01 1 505 108 108 THR C C 174.299 0.2 1 506 108 108 THR CA C 61.895 0.2 1 507 108 108 THR CB C 69.655 0.2 1 508 108 108 THR N N 113.984 0.2 1 509 109 109 ASP H H 8.428 0.01 1 510 109 109 ASP C C 174.850 0.2 1 511 109 109 ASP CA C 53.016 0.2 1 512 109 109 ASP CB C 37.990 0.2 1 513 109 109 ASP N N 121.139 0.2 1 514 110 110 ILE H H 7.938 0.01 1 515 110 110 ILE C C 175.975 0.2 1 516 110 110 ILE CA C 61.228 0.2 1 517 110 110 ILE CB C 38.921 0.2 1 518 110 110 ILE N N 120.611 0.2 1 519 111 111 SER H H 8.291 0.01 1 520 111 111 SER C C 174.601 0.2 1 521 111 111 SER CA C 58.301 0.2 1 522 111 111 SER CB C 63.865 0.2 1 523 111 111 SER N N 119.603 0.2 1 524 112 112 ILE H H 8.130 0.01 1 525 112 112 ILE C C 176.168 0.2 1 526 112 112 ILE CA C 61.387 0.2 1 527 112 112 ILE CB C 38.598 0.2 1 528 112 112 ILE N N 123.025 0.2 1 529 113 113 LEU H H 8.162 0.01 1 530 113 113 LEU C C 177.399 0.2 1 531 113 113 LEU CA C 55.348 0.2 1 532 113 113 LEU CB C 42.272 0.2 1 533 113 113 LEU N N 125.235 0.2 1 534 114 114 SER H H 8.186 0.01 1 535 114 114 SER C C 174.692 0.2 1 536 114 114 SER CA C 58.414 0.2 1 537 114 114 SER CB C 63.795 0.2 1 538 114 114 SER N N 116.554 0.2 1 539 115 115 LEU H H 8.174 0.01 1 540 115 115 LEU C C 177.468 0.2 1 541 115 115 LEU CA C 55.522 0.2 1 542 115 115 LEU CB C 42.260 0.2 1 543 115 115 LEU N N 124.246 0.2 1 544 116 116 GLN H H 8.257 0.01 1 545 116 116 GLN C C 175.887 0.2 1 546 116 116 GLN CA C 56.134 0.2 1 547 116 116 GLN CB C 29.394 0.2 1 548 116 116 GLN N N 120.458 0.2 1 549 117 117 ALA H H 8.180 0.01 1 550 117 117 ALA C C 177.660 0.2 1 551 117 117 ALA CA C 52.793 0.2 1 552 117 117 ALA CB C 19.191 0.2 1 553 117 117 ALA N N 124.762 0.2 1 554 118 118 SER H H 8.132 0.01 1 555 118 118 SER C C 174.392 0.2 1 556 118 118 SER CA C 58.327 0.2 1 557 118 118 SER CB C 63.915 0.2 1 558 118 118 SER N N 114.366 0.2 1 559 119 119 GLU H H 8.155 0.01 1 560 119 119 GLU C C 175.190 0.2 1 561 119 119 GLU CA C 55.913 0.2 1 562 119 119 GLU CB C 28.981 0.2 1 563 119 119 GLU N N 121.735 0.2 1 564 120 120 PHE H H 8.106 0.01 1 565 120 120 PHE CA C 55.542 0.2 1 566 120 120 PHE CB C 39.110 0.2 1 567 120 120 PHE N N 120.597 0.2 1 568 121 121 PRO C C 176.832 0.2 1 569 121 121 PRO CA C 63.428 0.2 1 570 121 121 PRO CB C 32.037 0.2 1 571 122 122 SER H H 8.339 0.01 1 572 122 122 SER C C 174.814 0.2 1 573 122 122 SER CA C 58.689 0.2 1 574 122 122 SER CB C 63.831 0.2 1 575 122 122 SER N N 115.995 0.2 1 576 123 123 GLU H H 8.339 0.01 1 577 123 123 GLU C C 175.773 0.2 1 578 123 123 GLU CA C 55.899 0.2 1 579 123 123 GLU CB C 28.784 0.2 1 580 123 123 GLU N N 121.998 0.2 1 581 124 124 LEU H H 8.157 0.01 1 582 124 124 LEU C C 177.215 0.2 1 583 124 124 LEU CA C 55.241 0.2 1 584 124 124 LEU CB C 42.288 0.2 1 585 124 124 LEU N N 122.879 0.2 1 586 125 125 MET H H 8.338 0.01 1 587 125 125 MET C C 176.254 0.2 1 588 125 125 MET CA C 55.378 0.2 1 589 125 125 MET CB C 32.993 0.2 1 590 125 125 MET N N 121.269 0.2 1 591 126 126 SER H H 8.277 0.01 1 592 126 126 SER C C 174.354 0.2 1 593 126 126 SER CA C 58.393 0.2 1 594 126 126 SER CB C 63.867 0.2 1 595 126 126 SER N N 116.719 0.2 1 596 127 127 ASN H H 8.459 0.01 1 597 127 127 ASN C C 175.049 0.2 1 598 127 127 ASN CA C 53.374 0.2 1 599 127 127 ASN CB C 38.766 0.2 1 600 127 127 ASN N N 120.699 0.2 1 601 128 128 ASP H H 8.367 0.01 1 602 128 128 ASP C C 175.162 0.2 1 603 128 128 ASP CA C 52.960 0.2 1 604 128 128 ASP CB C 38.144 0.2 1 605 128 128 ASP N N 119.301 0.2 1 606 129 129 SER H H 8.191 0.01 1 607 129 129 SER C C 174.583 0.2 1 608 129 129 SER CA C 58.806 0.2 1 609 129 129 SER CB C 63.851 0.2 1 610 129 129 SER N N 116.335 0.2 1 611 130 130 LYS H H 8.220 0.01 1 612 130 130 LYS C C 176.203 0.2 1 613 130 130 LYS CA C 56.441 0.2 1 614 130 130 LYS CB C 33.061 0.2 1 615 130 130 LYS N N 123.029 0.2 1 616 131 131 ALA H H 8.137 0.01 1 617 131 131 ALA C C 177.530 0.2 1 618 131 131 ALA CA C 52.511 0.2 1 619 131 131 ALA CB C 19.127 0.2 1 620 131 131 ALA N N 124.696 0.2 1 621 132 132 LEU H H 8.143 0.01 1 622 132 132 LEU C C 177.296 0.2 1 623 132 132 LEU CA C 55.263 0.2 1 624 132 132 LEU CB C 42.387 0.2 1 625 132 132 LEU N N 121.428 0.2 1 626 133 133 CYS H H 8.391 0.01 1 627 133 133 CYS C C 174.969 0.2 1 628 133 133 CYS CA C 55.186 0.2 1 629 133 133 CYS CB C 41.581 0.2 1 630 133 133 CYS N N 119.172 0.2 1 631 134 134 GLY H H 8.358 0.01 1 632 134 134 GLY HA2 H 3.939 0.01 1 633 134 134 GLY HA3 H 3.939 0.01 1 634 134 134 GLY CA C 44.212 0.2 1 635 134 134 GLY N N 111.404 0.2 1 stop_ save_