data_27216 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignments of prothymosin alpha in complex with Histone H1 ; _BMRB_accession_number 27216 _BMRB_flat_file_name bmr27216.str _Entry_type original _Submission_date 2017-08-14 _Accession_date 2017-08-14 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Chemical shift assignments of prothymosin alpha in complex with Histone H1 at 10 degrees celcius, pH 7.4 and 165 mM ionic strength. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bugge Katrine . . 2 Kragelund Birthe B. . 3 Fernandes Catarina B. . 4 Borgia Alessandro . . 5 Borgia Madeleine B. . 6 Heidarsson Petur O. . 7 Schuler Benjamin . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 97 "13C chemical shifts" 172 "15N chemical shifts" 102 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-03-28 update BMRB 'update entry citation' 2018-02-12 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27215 'prothymosin alpha' stop_ _Original_release_date 2017-08-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Extreme disorder in an ultrahigh-affinity protein complex. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29466338 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Borgia Alessandro . . 2 Borgia Madeleine B. . 3 Bugge Katrine . . 4 Kissling Vera M. . 5 Heidarsson Petur O. . 6 Fernandes Catarina B. . 7 Sottini Andrea . . 8 Soranno Andrea . . 9 Buholzer Karin J. . 10 Nettels Daniel . . 11 Kragelund Birthe B. . 12 Best Robert B. . 13 Schuler Benjamin . . stop_ _Journal_abbreviation Nature _Journal_name_full Nature _Journal_volume 555 _Journal_issue 7694 _Journal_ISSN 1476-4687 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 61 _Page_last 66 _Year 2018 _Details . loop_ _Keyword 'high affinity' 'intrinsically disordered' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'prothymosin alpha in complex with Histone H1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Prothymosin alpha' $Prothymosin_alpha 'Histone H1' $Histone_H1 stop_ _System_molecular_weight . _System_physical_state 'intrinsically disordered' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Prothymosin_alpha _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Prothymosin_alpha _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 112 _Mol_residue_sequence ; GPMSDAAVDTSSEITTKDLK EKKEVVEEAENGRDAPANGN ANEENGEQEADNEVDEEEEE GGEEEEEEEEGDGEEEDGDE DEEAESATGKRAAEDDEDDD VDTKKQKTDEDD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 GLY 2 0 PRO 3 1 MET 4 2 SER 5 3 ASP 6 4 ALA 7 5 ALA 8 6 VAL 9 7 ASP 10 8 THR 11 9 SER 12 10 SER 13 11 GLU 14 12 ILE 15 13 THR 16 14 THR 17 15 LYS 18 16 ASP 19 17 LEU 20 18 LYS 21 19 GLU 22 20 LYS 23 21 LYS 24 22 GLU 25 23 VAL 26 24 VAL 27 25 GLU 28 26 GLU 29 27 ALA 30 28 GLU 31 29 ASN 32 30 GLY 33 31 ARG 34 32 ASP 35 33 ALA 36 34 PRO 37 35 ALA 38 36 ASN 39 37 GLY 40 38 ASN 41 39 ALA 42 40 ASN 43 41 GLU 44 42 GLU 45 43 ASN 46 44 GLY 47 45 GLU 48 46 GLN 49 47 GLU 50 48 ALA 51 49 ASP 52 50 ASN 53 51 GLU 54 52 VAL 55 53 ASP 56 54 GLU 57 55 GLU 58 56 GLU 59 57 GLU 60 58 GLU 61 59 GLY 62 60 GLY 63 61 GLU 64 62 GLU 65 63 GLU 66 64 GLU 67 65 GLU 68 66 GLU 69 67 GLU 70 68 GLU 71 69 GLY 72 70 ASP 73 71 GLY 74 72 GLU 75 73 GLU 76 74 GLU 77 75 ASP 78 76 GLY 79 77 ASP 80 78 GLU 81 79 ASP 82 80 GLU 83 81 GLU 84 82 ALA 85 83 GLU 86 84 SER 87 85 ALA 88 86 THR 89 87 GLY 90 88 LYS 91 89 ARG 92 90 ALA 93 91 ALA 94 92 GLU 95 93 ASP 96 94 ASP 97 95 GLU 98 96 ASP 99 97 ASP 100 98 ASP 101 99 VAL 102 100 ASP 103 101 THR 104 102 LYS 105 103 LYS 106 104 GLN 107 105 LYS 108 106 THR 109 107 ASP 110 108 GLU 111 109 ASP 112 110 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_Histone_H1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Histone_H1 _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 197 _Mol_residue_sequence ; TENSTSAPAAKPKRAKASKK STDHPKYSDMIVAAIQAEKN RAGSSRQSIQKYIKSHYKVG ENADSQIKLSIKRLVTTGVL KQTKGVGASGSFRLAKSDEP KKSVAFKKTKKEIKKVATPK KASKPKKAASKAPTKKPKAT PVKKAKKKLAATPKKAKKPK TVKAKPVKASKPKKAKPVKP KAKSSAKRAGKKKGGPR ; loop_ _Residue_seq_code _Residue_label 1 THR 2 GLU 3 ASN 4 SER 5 THR 6 SER 7 ALA 8 PRO 9 ALA 10 ALA 11 LYS 12 PRO 13 LYS 14 ARG 15 ALA 16 LYS 17 ALA 18 SER 19 LYS 20 LYS 21 SER 22 THR 23 ASP 24 HIS 25 PRO 26 LYS 27 TYR 28 SER 29 ASP 30 MET 31 ILE 32 VAL 33 ALA 34 ALA 35 ILE 36 GLN 37 ALA 38 GLU 39 LYS 40 ASN 41 ARG 42 ALA 43 GLY 44 SER 45 SER 46 ARG 47 GLN 48 SER 49 ILE 50 GLN 51 LYS 52 TYR 53 ILE 54 LYS 55 SER 56 HIS 57 TYR 58 LYS 59 VAL 60 GLY 61 GLU 62 ASN 63 ALA 64 ASP 65 SER 66 GLN 67 ILE 68 LYS 69 LEU 70 SER 71 ILE 72 LYS 73 ARG 74 LEU 75 VAL 76 THR 77 THR 78 GLY 79 VAL 80 LEU 81 LYS 82 GLN 83 THR 84 LYS 85 GLY 86 VAL 87 GLY 88 ALA 89 SER 90 GLY 91 SER 92 PHE 93 ARG 94 LEU 95 ALA 96 LYS 97 SER 98 ASP 99 GLU 100 PRO 101 LYS 102 LYS 103 SER 104 VAL 105 ALA 106 PHE 107 LYS 108 LYS 109 THR 110 LYS 111 LYS 112 GLU 113 ILE 114 LYS 115 LYS 116 VAL 117 ALA 118 THR 119 PRO 120 LYS 121 LYS 122 ALA 123 SER 124 LYS 125 PRO 126 LYS 127 LYS 128 ALA 129 ALA 130 SER 131 LYS 132 ALA 133 PRO 134 THR 135 LYS 136 LYS 137 PRO 138 LYS 139 ALA 140 THR 141 PRO 142 VAL 143 LYS 144 LYS 145 ALA 146 LYS 147 LYS 148 LYS 149 LEU 150 ALA 151 ALA 152 THR 153 PRO 154 LYS 155 LYS 156 ALA 157 LYS 158 LYS 159 PRO 160 LYS 161 THR 162 VAL 163 LYS 164 ALA 165 LYS 166 PRO 167 VAL 168 LYS 169 ALA 170 SER 171 LYS 172 PRO 173 LYS 174 LYS 175 ALA 176 LYS 177 PRO 178 VAL 179 LYS 180 PRO 181 LYS 182 ALA 183 LYS 184 SER 185 SER 186 ALA 187 LYS 188 ARG 189 ALA 190 GLY 191 LYS 192 LYS 193 LYS 194 GLY 195 GLY 196 PRO 197 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Prothymosin_alpha 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 $Prothymosin_alpha 'recombinant technology' . Escherichia coli . pET47b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'Labeled prothymosin alpha in complex with unlabeled Histone H1' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Prothymosin_alpha 100 uM '[U-100% 13C; U-100% 15N]' $Histone_H1 80 uM 'natural abundance' DSS 0.7 mM 'natural abundance' D2O 10 % '[U-100% 2H]' EDTA 0.1 mM 'natural abundance' 'TBS buffer' 165 mM 'natural abundance' Tris-HCl 10 mM 'natural abundance' KCl 155 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_Ccpnmr_Analysis _Saveframe_category software _Name Ccpnmr_Analysis _Version . loop_ _Vendor _Address _Electronic_address CCPN . . 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 . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _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_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _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)NNH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)NNH' _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' 165 . mM pH 7.4 . pH pressure 1 . atm temperature 283 . 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 $NMRPipe $Ccpnmr_Analysis stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D CBCA(CO)NH' '3D HN(CO)CA' '3D HNCO' '3D HN(CA)NNH' 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 'Prothymosin alpha' _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 3 MET CA C 55.619 0.000 1 2 1 3 MET CB C 32.604 0.000 1 3 1 3 MET H H 8.720 0.009 1 4 1 3 MET N N 120.539 0.047 1 5 2 4 SER CA C 58.604 0.000 1 6 2 4 SER CB C 63.811 0.000 1 7 2 4 SER H H 8.368 0.009 1 8 2 4 SER N N 117.038 0.051 1 9 3 5 ASP CA C 54.486 0.023 1 10 3 5 ASP CB C 41.085 0.017 1 11 3 5 ASP H H 8.442 0.008 1 12 3 5 ASP N N 122.872 0.062 1 13 4 6 ALA CA C 52.627 0.001 1 14 4 6 ALA CB C 19.338 0.015 1 15 4 6 ALA H H 8.188 0.006 1 16 4 6 ALA N N 124.164 0.048 1 17 5 7 ALA CA C 52.517 0.028 1 18 5 7 ALA CB C 19.221 0.020 1 19 5 7 ALA H H 8.318 0.007 1 20 5 7 ALA N N 123.538 0.047 1 21 6 8 VAL CA C 62.270 0.028 1 22 6 8 VAL CB C 33.025 0.021 1 23 6 8 VAL H H 8.132 0.007 1 24 6 8 VAL N N 119.553 0.048 1 25 7 9 ASP CA C 54.106 0.026 1 26 7 9 ASP CB C 41.314 0.081 1 27 7 9 ASP H H 8.550 0.008 1 28 7 9 ASP N N 124.566 0.054 1 29 8 10 THR CA C 62.029 0.082 1 30 8 10 THR CB C 69.417 0.016 1 31 8 10 THR H H 8.374 0.008 1 32 8 10 THR N N 115.803 0.048 1 33 9 11 SER CA C 59.227 0.023 1 34 9 11 SER CB C 63.803 0.014 1 35 9 11 SER H H 8.517 0.007 1 36 9 11 SER N N 118.625 0.048 1 37 10 12 SER CA C 58.683 0.000 1 38 10 12 SER CB C 63.802 0.028 1 39 10 12 SER H H 8.383 0.008 1 40 10 12 SER N N 117.889 0.067 1 41 11 13 GLU CA C 56.726 0.047 1 42 11 13 GLU CB C 30.296 0.014 1 43 11 13 GLU H H 8.387 0.010 1 44 11 13 GLU N N 122.841 0.052 1 45 12 14 ILE CA C 61.381 0.036 1 46 12 14 ILE CB C 38.492 0.046 1 47 12 14 ILE H H 8.286 0.007 1 48 12 14 ILE N N 122.364 0.049 1 49 13 15 THR CA C 62.001 0.091 1 50 13 15 THR CB C 69.936 0.025 1 51 13 15 THR H H 8.382 0.008 1 52 13 15 THR N N 118.646 0.042 1 53 14 16 THR CA C 62.250 0.015 1 54 14 16 THR CB C 69.703 0.054 1 55 14 16 THR H H 8.234 0.008 1 56 14 16 THR N N 116.813 0.048 1 57 15 17 LYS CA C 56.792 0.008 1 58 15 17 LYS CB C 33.055 0.014 1 59 15 17 LYS H H 8.355 0.008 1 60 15 17 LYS N N 123.782 0.058 1 61 16 18 ASP CA C 54.598 0.026 1 62 16 18 ASP CB C 41.169 0.051 1 63 16 18 ASP H H 8.395 0.007 1 64 16 18 ASP N N 121.444 0.052 1 65 17 19 LEU CA C 55.487 0.025 1 66 17 19 LEU CB C 42.127 0.043 1 67 17 19 LEU H H 8.254 0.007 1 68 17 19 LEU N N 123.158 0.048 1 69 18 20 LYS CA C 56.565 0.000 1 70 18 20 LYS CB C 32.763 0.001 1 71 18 20 LYS H H 8.348 0.009 1 72 18 20 LYS N N 121.753 0.059 1 73 19 21 GLU CA C 56.588 0.092 1 74 19 21 GLU CB C 30.441 0.020 1 75 19 21 GLU H H 8.360 0.009 1 76 19 21 GLU N N 121.785 0.061 1 77 20 22 LYS CA C 56.295 0.053 1 78 20 22 LYS CB C 33.056 0.084 1 79 20 22 LYS H H 8.420 0.008 1 80 20 22 LYS N N 123.438 0.051 1 81 21 23 LYS H H 8.451 0.007 1 82 21 23 LYS N N 123.958 0.050 1 83 22 24 GLU CA C 56.533 0.000 1 84 22 24 GLU CB C 30.458 0.000 1 85 22 24 GLU N N 123.160 0.005 1 86 23 25 VAL CA C 62.393 0.033 1 87 23 25 VAL CB C 32.927 0.071 1 88 23 25 VAL H H 8.370 0.008 1 89 23 25 VAL N N 122.858 0.053 1 90 24 26 VAL CA C 62.279 0.033 1 91 24 26 VAL CB C 32.877 0.025 1 92 24 26 VAL H H 8.409 0.006 1 93 24 26 VAL N N 125.760 0.038 1 94 25 27 GLU CA C 56.551 0.000 1 95 25 27 GLU CB C 30.543 0.013 1 96 25 27 GLU H H 8.637 0.008 1 97 25 27 GLU N N 125.852 0.033 1 98 26 28 GLU CA C 56.569 0.041 1 99 26 28 GLU CB C 30.519 0.008 1 100 26 28 GLU H H 8.579 0.008 1 101 26 28 GLU N N 123.102 0.059 1 102 27 29 ALA CA C 52.524 0.006 1 103 27 29 ALA CB C 19.628 0.077 1 104 27 29 ALA H H 8.482 0.006 1 105 27 29 ALA N N 125.662 0.122 1 106 28 30 GLU CA C 56.748 0.000 1 107 28 30 GLU CB C 30.200 0.000 1 108 28 30 GLU H H 8.538 0.007 1 109 28 30 GLU N N 120.559 0.114 1 110 29 31 ASN CB C 39.063 0.058 1 111 29 31 ASN H H 8.532 0.008 1 112 29 31 ASN N N 119.710 0.043 1 113 30 32 GLY CA C 45.621 0.000 1 114 30 32 GLY H H 8.518 0.009 1 115 30 32 GLY N N 109.586 0.040 1 116 31 33 ARG H H 8.195 0.008 1 117 31 33 ARG N N 120.460 0.033 1 118 32 34 ASP CA C 54.223 0.023 1 119 32 34 ASP CB C 41.153 0.000 1 120 32 34 ASP H H 8.475 0.008 1 121 32 34 ASP N N 121.169 0.033 1 122 33 35 ALA CA C 50.614 0.000 1 123 33 35 ALA CB C 18.234 0.000 1 124 33 35 ALA H H 8.218 0.003 1 125 33 35 ALA N N 125.472 0.039 1 126 34 36 PRO CA C 62.912 0.000 1 127 34 36 PRO CB C 32.218 0.000 1 128 35 37 ALA CA C 52.662 0.000 1 129 35 37 ALA CB C 19.206 0.000 1 130 35 37 ALA H H 8.597 0.008 1 131 35 37 ALA N N 124.919 0.048 1 132 36 38 ASN CB C 39.036 0.000 1 133 36 38 ASN H H 8.520 0.007 1 134 36 38 ASN N N 117.884 0.051 1 135 37 39 GLY CA C 45.500 0.000 1 136 37 39 GLY H H 8.427 0.008 1 137 37 39 GLY N N 109.462 0.061 1 138 38 40 ASN CA C 53.176 0.000 1 139 38 40 ASN CB C 39.154 0.000 1 140 38 40 ASN H H 8.411 0.009 1 141 38 40 ASN N N 118.849 0.059 1 142 39 41 ALA CA C 52.907 0.000 1 143 39 41 ALA CB C 19.174 0.030 1 144 39 41 ALA H H 8.452 0.008 1 145 39 41 ALA N N 124.742 0.046 1 146 40 42 ASN CA C 53.263 0.006 1 147 40 42 ASN CB C 38.971 0.000 1 148 40 42 ASN H H 8.505 0.009 1 149 40 42 ASN N N 117.689 0.043 1 150 41 43 GLU CA C 56.782 0.000 1 151 41 43 GLU CB C 30.427 0.000 1 152 41 43 GLU H H 8.487 0.008 1 153 41 43 GLU N N 121.572 0.143 1 154 42 44 GLU CA C 56.694 0.000 1 155 42 44 GLU CB C 30.237 0.000 1 156 42 44 GLU H H 8.518 0.007 1 157 42 44 GLU N N 121.856 0.046 1 158 43 45 ASN CA C 53.292 0.018 1 159 43 45 ASN CB C 39.163 0.007 1 160 43 45 ASN H H 8.571 0.007 1 161 43 45 ASN N N 119.835 0.056 1 162 44 46 GLY CA C 45.543 0.000 1 163 44 46 GLY H H 8.471 0.007 1 164 44 46 GLY N N 109.561 0.049 1 165 45 47 GLU CA C 56.513 0.019 1 166 45 47 GLU CB C 30.476 0.000 1 167 45 47 GLU H H 8.408 0.007 1 168 45 47 GLU N N 120.631 0.026 1 169 46 48 GLN CA C 55.715 0.000 1 170 46 48 GLN H H 8.552 0.009 1 171 46 48 GLN N N 121.594 0.048 1 172 47 49 GLU N N 123.154 0.000 1 173 48 50 ALA CA C 52.569 0.000 1 174 48 50 ALA CB C 19.580 0.000 1 175 48 50 ALA H H 8.489 0.009 1 176 48 50 ALA N N 125.836 0.110 1 177 49 51 ASP CA C 54.357 0.000 1 178 49 51 ASP CB C 41.148 0.000 1 179 49 51 ASP H H 8.450 0.007 1 180 49 51 ASP N N 120.148 0.053 1 181 50 52 ASN CA C 53.252 0.000 1 182 50 52 ASN CB C 39.325 0.052 1 183 50 52 ASN H H 8.423 0.008 1 184 50 52 ASN N N 119.335 0.048 1 185 51 53 GLU CA C 56.608 0.000 1 186 51 53 GLU CB C 30.351 0.000 1 187 51 53 GLU H H 8.484 0.006 1 188 51 53 GLU N N 121.764 0.046 1 189 52 54 VAL CA C 62.096 0.000 1 190 52 54 VAL CB C 33.280 0.000 1 191 52 54 VAL H H 8.258 0.007 1 192 52 54 VAL N N 121.273 0.069 1 193 53 55 ASP CA C 54.297 0.000 1 194 53 55 ASP CB C 41.408 0.000 1 195 53 55 ASP H H 8.550 0.009 1 196 53 55 ASP N N 125.094 0.076 1 197 54 56 GLU H H 8.529 0.009 1 198 54 56 GLU N N 122.332 0.072 1 199 55 57 GLU H H 8.569 0.006 1 200 55 57 GLU N N 122.205 0.107 1 201 57 59 GLU CA C 56.344 0.000 1 202 57 59 GLU CB C 30.714 0.000 1 203 57 59 GLU H H 8.609 0.006 1 204 57 59 GLU N N 123.178 0.053 1 205 58 60 GLU CA C 56.628 0.081 1 206 58 60 GLU CB C 30.666 0.055 1 207 58 60 GLU H H 8.677 0.012 1 208 58 60 GLU N N 123.297 0.057 1 209 59 61 GLY CA C 45.426 0.015 1 210 59 61 GLY H H 8.655 0.007 1 211 59 61 GLY N N 110.726 0.032 1 212 60 62 GLY CA C 45.262 0.015 1 213 60 62 GLY H H 8.442 0.008 1 214 60 62 GLY N N 109.085 0.046 1 215 61 63 GLU CA C 56.617 0.000 1 216 61 63 GLU CB C 30.531 0.000 1 217 61 63 GLU H H 8.556 0.009 1 218 61 63 GLU N N 120.573 0.034 1 219 62 64 GLU N N 122.195 0.000 1 220 67 69 GLU N N 123.370 0.000 1 221 68 70 GLU CA C 56.858 0.000 1 222 68 70 GLU CB C 30.668 0.000 1 223 68 70 GLU H H 8.707 0.007 1 224 68 70 GLU N N 123.394 0.057 1 225 69 71 GLY CA C 45.227 0.051 1 226 69 71 GLY H H 8.581 0.008 1 227 69 71 GLY N N 110.587 0.037 1 228 70 72 ASP CA C 54.398 0.023 1 229 70 72 ASP CB C 41.463 0.055 1 230 70 72 ASP H H 8.454 0.006 1 231 70 72 ASP N N 120.409 0.069 1 232 71 73 GLY CA C 45.436 0.021 1 233 71 73 GLY H H 8.567 0.009 1 234 71 73 GLY N N 109.579 0.043 1 235 72 74 GLU CA C 56.413 0.000 1 236 72 74 GLU CB C 30.565 0.000 1 237 72 74 GLU H H 8.406 0.006 1 238 72 74 GLU N N 120.490 0.022 1 239 73 75 GLU H H 8.651 0.008 1 240 73 75 GLU N N 122.219 0.057 1 241 74 76 GLU H H 8.608 0.009 1 242 74 76 GLU N N 122.635 0.056 1 243 75 77 ASP CA C 54.604 0.026 1 244 75 77 ASP CB C 41.475 0.029 1 245 75 77 ASP H H 8.589 0.006 1 246 75 77 ASP N N 122.373 0.064 1 247 76 78 GLY CA C 45.377 0.000 1 248 76 78 GLY H H 8.479 0.008 1 249 76 78 GLY N N 109.660 0.045 1 250 77 79 ASP CA C 54.280 0.013 1 251 77 79 ASP CB C 41.531 0.000 1 252 77 79 ASP H H 8.412 0.007 1 253 77 79 ASP N N 120.716 0.048 1 254 78 80 GLU H H 8.589 0.009 1 255 78 80 GLU N N 121.440 0.060 1 256 81 83 GLU CA C 56.707 0.000 1 257 81 83 GLU CB C 30.232 0.000 1 258 81 83 GLU H H 8.548 0.007 1 259 81 83 GLU N N 122.016 0.045 1 260 82 84 ALA CA C 52.923 0.037 1 261 82 84 ALA CB C 19.427 0.057 1 262 82 84 ALA H H 8.321 0.006 1 263 82 84 ALA N N 125.311 0.040 1 264 83 85 GLU CA C 56.923 0.000 1 265 83 85 GLU CB C 30.222 0.000 1 266 83 85 GLU H H 8.514 0.007 1 267 83 85 GLU N N 120.230 0.050 1 268 84 86 SER CA C 58.597 0.037 1 269 84 86 SER CB C 63.853 0.066 1 270 84 86 SER H H 8.374 0.006 1 271 84 86 SER N N 116.686 0.056 1 272 85 87 ALA CA C 53.144 0.000 1 273 85 87 ALA CB C 19.253 0.000 1 274 85 87 ALA H H 8.498 0.009 1 275 85 87 ALA N N 126.321 0.048 1 276 86 88 THR CA C 62.379 0.064 1 277 86 88 THR CB C 69.741 0.044 1 278 86 88 THR H H 8.161 0.007 1 279 86 88 THR N N 112.124 0.057 1 280 87 89 GLY CA C 45.397 0.013 1 281 87 89 GLY H H 8.373 0.008 1 282 87 89 GLY N N 111.240 0.044 1 283 88 90 LYS CA C 56.395 0.000 1 284 88 90 LYS CB C 33.226 0.038 1 285 88 90 LYS H H 8.188 0.008 1 286 88 90 LYS N N 121.263 0.046 1 287 89 91 ARG CA C 56.031 0.000 1 288 89 91 ARG CB C 30.999 0.000 1 289 89 91 ARG H H 8.521 0.008 1 290 89 91 ARG N N 123.442 0.083 1 291 90 92 ALA CA C 52.523 0.036 1 292 90 92 ALA CB C 19.259 0.053 1 293 90 92 ALA H H 8.551 0.007 1 294 90 92 ALA N N 126.382 0.050 1 295 91 93 ALA CA C 52.796 0.019 1 296 91 93 ALA CB C 19.328 0.000 1 297 91 93 ALA H H 8.444 0.008 1 298 91 93 ALA N N 123.719 0.044 1 299 92 94 GLU CA C 56.831 0.003 1 300 92 94 GLU CB C 30.148 0.050 1 301 92 94 GLU H H 8.519 0.008 1 302 92 94 GLU N N 119.443 0.048 1 303 93 95 ASP CA C 54.557 0.006 1 304 93 95 ASP CB C 41.279 0.000 1 305 93 95 ASP H H 8.308 0.008 1 306 93 95 ASP N N 120.596 0.056 1 307 94 96 ASP CB C 41.387 0.000 1 308 94 96 ASP H H 8.280 0.007 1 309 94 96 ASP N N 120.732 0.052 1 310 95 97 GLU CB C 33.230 0.000 1 311 95 97 GLU H H 8.401 0.008 1 312 95 97 GLU N N 121.231 0.033 1 313 96 98 ASP CA C 54.501 0.000 1 314 96 98 ASP CB C 41.420 0.007 1 315 96 98 ASP N N 121.783 0.004 1 316 97 99 ASP CA C 54.487 0.071 1 317 97 99 ASP CB C 41.423 0.000 1 318 97 99 ASP H H 8.389 0.010 1 319 97 99 ASP N N 121.384 0.070 1 320 98 100 ASP CA C 54.245 0.000 1 321 98 100 ASP CB C 41.200 0.000 1 322 98 100 ASP H H 8.420 0.008 1 323 98 100 ASP N N 120.972 0.042 1 324 99 101 VAL CA C 63.015 0.026 1 325 99 101 VAL CB C 32.586 0.000 1 326 99 101 VAL H H 8.077 0.008 1 327 99 101 VAL N N 120.143 0.040 1 328 100 102 ASP CA C 54.913 0.005 1 329 100 102 ASP CB C 41.159 0.029 1 330 100 102 ASP H H 8.510 0.009 1 331 100 102 ASP N N 122.947 0.095 1 332 101 103 THR CA C 62.708 0.005 1 333 101 103 THR CB C 69.429 0.034 1 334 101 103 THR H H 8.111 0.009 1 335 101 103 THR N N 115.103 0.053 1 336 102 104 LYS CA C 56.797 0.017 1 337 102 104 LYS CB C 32.594 0.040 1 338 102 104 LYS H H 8.289 0.009 1 339 102 104 LYS N N 123.259 0.046 1 340 103 105 LYS CA C 56.624 0.000 1 341 103 105 LYS CB C 32.924 0.024 1 342 103 105 LYS H H 8.217 0.008 1 343 103 105 LYS N N 122.280 0.053 1 344 104 106 GLN CA C 55.913 0.067 1 345 104 106 GLN CB C 29.546 0.048 1 346 104 106 GLN H H 8.451 0.008 1 347 104 106 GLN N N 122.054 0.040 1 348 105 107 LYS CA C 56.552 0.000 1 349 105 107 LYS CB C 33.198 0.000 1 350 105 107 LYS H H 8.530 0.009 1 351 105 107 LYS N N 123.748 0.072 1 352 106 108 THR CA C 61.615 0.034 1 353 106 108 THR CB C 70.162 0.024 1 354 106 108 THR H H 8.499 0.009 1 355 106 108 THR N N 115.764 0.045 1 356 107 109 ASP CA C 54.749 0.000 1 357 107 109 ASP CB C 41.184 0.000 1 358 107 109 ASP H H 8.493 0.009 1 359 107 109 ASP N N 122.146 0.048 1 360 108 110 GLU CA C 56.718 0.014 1 361 108 110 GLU CB C 30.533 0.004 1 362 108 110 GLU H H 8.347 0.008 1 363 108 110 GLU N N 120.207 0.053 1 364 109 111 ASP CA C 54.585 0.008 1 365 109 111 ASP CB C 41.494 0.008 1 366 109 111 ASP H H 8.333 0.009 1 367 109 111 ASP N N 121.468 0.048 1 368 110 112 ASP CA C 56.168 0.000 1 369 110 112 ASP CB C 42.131 0.000 1 370 110 112 ASP H H 7.991 0.007 1 371 110 112 ASP N N 126.035 0.040 1 stop_ save_