data_27215 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignments of free prothymosin alpha ; _BMRB_accession_number 27215 _BMRB_flat_file_name bmr27215.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 free prothymosin alpha in TBS buffer (pH 7.4), 0.1 mM EDTA, 10 degrees celcius.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bugge Katrine . . 2 Fernandes Catarina B. . 3 Kragelund Birthe 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" 169 "13C chemical shifts" 279 "15N chemical shifts" 105 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 27216 '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 . . 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 'intrinsically disordered' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'free prothymosin alpha' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'free prothymosin alpha' $Prothymosin_alpha stop_ _System_molecular_weight . _System_physical_state native _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 . 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 UNP P06454 . . . . . . stop_ 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 'TBS buffer (pH 7.4), 0.1mM EDTA, DSS, 10 degrees celcius' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Prothymosin_alpha 100 uM '[U-100% 13C; U-100% 15N]' Tris-HCl 10 mM 'natural abundance' KCL 155 mM 'natural abundance' EDTA 0.1 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_ _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 'free 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 H H 8.716 0.007 1 2 1 3 MET C C 176.360 0.000 1 3 1 3 MET N N 120.535 0.032 1 4 2 4 SER C C 174.158 0.000 1 5 2 4 SER CA C 58.609 0.000 1 6 2 4 SER CB C 63.697 0.000 1 7 2 4 SER H H 8.366 0.005 1 8 2 4 SER N N 117.007 0.034 1 9 3 5 ASP C C 175.816 0.016 1 10 3 5 ASP CA C 54.512 0.009 1 11 3 5 ASP CB C 41.097 0.077 1 12 3 5 ASP H H 8.440 0.005 1 13 3 5 ASP N N 122.869 0.034 1 14 4 6 ALA C C 177.285 0.014 1 15 4 6 ALA CA C 52.645 0.073 1 16 4 6 ALA CB C 19.278 0.017 1 17 4 6 ALA H H 8.189 0.005 1 18 4 6 ALA HA H 4.270 0.000 1 19 4 6 ALA N N 124.154 0.023 1 20 5 7 ALA C C 177.608 0.009 1 21 5 7 ALA CA C 52.646 0.000 1 22 5 7 ALA CB C 19.218 0.042 1 23 5 7 ALA H H 8.317 0.004 1 24 5 7 ALA HA H 4.285 0.000 1 25 5 7 ALA N N 123.527 0.021 1 26 6 8 VAL C C 175.646 0.000 1 27 6 8 VAL CA C 62.305 0.020 1 28 6 8 VAL CB C 33.165 0.000 1 29 6 8 VAL H H 8.129 0.005 1 30 6 8 VAL HA H 4.077 0.000 1 31 6 8 VAL N N 119.510 0.032 1 32 7 9 ASP C C 176.558 0.014 1 33 7 9 ASP CA C 54.185 0.026 1 34 7 9 ASP CB C 41.264 0.046 1 35 7 9 ASP H H 8.546 0.005 1 36 7 9 ASP HA H 4.712 0.000 1 37 7 9 ASP N N 124.507 0.055 1 38 8 10 THR C C 174.983 0.004 1 39 8 10 THR CA C 62.119 0.039 1 40 8 10 THR CB C 69.435 0.036 1 41 8 10 THR H H 8.371 0.008 1 42 8 10 THR HA H 4.384 0.000 1 43 8 10 THR N N 115.750 0.051 1 44 9 11 SER C C 174.751 0.009 1 45 9 11 SER CA C 59.452 0.000 1 46 9 11 SER CB C 63.872 0.000 1 47 9 11 SER H H 8.514 0.005 1 48 9 11 SER N N 118.596 0.047 1 49 10 12 SER CA C 58.756 0.000 1 50 10 12 SER CB C 63.945 0.000 1 51 10 12 SER H H 8.377 0.005 1 52 10 12 SER N N 117.856 0.050 1 53 11 13 GLU C C 176.313 0.015 1 54 11 13 GLU CA C 56.908 0.002 1 55 11 13 GLU CB C 30.249 0.098 1 56 11 13 GLU H H 8.383 0.005 1 57 11 13 GLU HA H 4.264 0.000 1 58 11 13 GLU N N 122.834 0.035 1 59 12 14 ILE C C 176.489 0.029 1 60 12 14 ILE CA C 61.445 0.094 1 61 12 14 ILE CB C 38.553 0.051 1 62 12 14 ILE H H 8.282 0.005 1 63 12 14 ILE HA H 4.196 0.000 1 64 12 14 ILE N N 122.330 0.035 1 65 13 15 THR C C 174.662 0.015 1 66 13 15 THR CA C 62.042 0.000 1 67 13 15 THR CB C 70.043 0.000 1 68 13 15 THR H H 8.376 0.006 1 69 13 15 THR N N 118.600 0.036 1 70 14 16 THR C C 174.470 0.000 1 71 14 16 THR CA C 62.307 0.000 1 72 14 16 THR CB C 69.755 0.099 1 73 14 16 THR H H 8.231 0.005 1 74 14 16 THR N N 116.785 0.034 1 75 15 17 LYS C C 175.997 0.041 1 76 15 17 LYS CA C 57.008 0.000 1 77 15 17 LYS CB C 33.121 0.018 1 78 15 17 LYS H H 8.351 0.005 1 79 15 17 LYS N N 123.752 0.046 1 80 16 18 ASP C C 176.134 0.000 1 81 16 18 ASP CA C 54.596 0.000 1 82 16 18 ASP CB C 41.124 0.000 1 83 16 18 ASP H H 8.396 0.007 1 84 16 18 ASP N N 121.413 0.040 1 85 17 19 LEU C C 177.472 0.014 1 86 17 19 LEU CA C 55.529 0.091 1 87 17 19 LEU CB C 42.243 0.026 1 88 17 19 LEU H H 8.252 0.005 1 89 17 19 LEU HA H 4.245 0.000 1 90 17 19 LEU N N 123.160 0.042 1 91 18 20 LYS C C 176.515 0.014 1 92 18 20 LYS CA C 56.624 0.000 1 93 18 20 LYS CB C 32.778 0.032 1 94 18 20 LYS H H 8.345 0.003 1 95 18 20 LYS HA H 4.262 0.000 1 96 18 20 LYS N N 121.703 0.037 1 97 19 21 GLU C C 176.152 0.003 1 98 19 21 GLU CA C 56.754 0.042 1 99 19 21 GLU CB C 30.438 0.027 1 100 19 21 GLU H H 8.356 0.005 1 101 19 21 GLU N N 121.753 0.039 1 102 20 22 LYS C C 176.143 0.034 1 103 20 22 LYS CA C 56.436 0.098 1 104 20 22 LYS CB C 33.057 0.069 1 105 20 22 LYS H H 8.416 0.006 1 106 20 22 LYS HA H 4.305 0.000 1 107 20 22 LYS N N 123.403 0.036 1 108 21 23 LYS CA C 56.389 0.000 1 109 21 23 LYS CB C 33.301 0.000 1 110 21 23 LYS H H 8.448 0.005 1 111 21 23 LYS N N 123.945 0.029 1 112 22 24 GLU C C 176.042 0.022 1 113 22 24 GLU CA C 56.650 0.024 1 114 22 24 GLU CB C 30.363 0.000 1 115 22 24 GLU H H 8.577 0.007 1 116 22 24 GLU N N 123.110 0.068 1 117 23 25 VAL C C 175.856 0.012 1 118 23 25 VAL CA C 62.551 0.000 1 119 23 25 VAL CB C 32.991 0.000 1 120 23 25 VAL H H 8.362 0.006 1 121 23 25 VAL HA H 4.080 0.000 1 122 23 25 VAL N N 122.784 0.036 1 123 24 26 VAL C C 175.867 0.008 1 124 24 26 VAL CA C 62.340 0.050 1 125 24 26 VAL CB C 32.906 0.003 1 126 24 26 VAL H H 8.399 0.005 1 127 24 26 VAL HA H 4.088 0.000 1 128 24 26 VAL N N 125.697 0.039 1 129 25 27 GLU C C 176.178 0.010 1 130 25 27 GLU CA C 56.650 0.000 1 131 25 27 GLU CB C 30.509 0.000 1 132 25 27 GLU H H 8.633 0.004 1 133 25 27 GLU HA H 4.276 0.000 1 134 25 27 GLU N N 125.800 0.031 1 135 26 28 GLU C C 176.939 0.000 1 136 26 28 GLU CA C 56.669 0.000 1 137 26 28 GLU CB C 30.484 0.000 1 138 26 28 GLU H H 8.574 0.006 1 139 26 28 GLU HA H 4.241 0.000 1 140 26 28 GLU N N 123.052 0.064 1 141 27 29 ALA C C 177.747 0.023 1 142 27 29 ALA CA C 52.707 0.000 1 143 27 29 ALA CB C 19.330 0.045 1 144 27 29 ALA H H 8.477 0.007 1 145 27 29 ALA N N 125.518 0.035 1 146 28 30 GLU C C 176.373 0.006 1 147 28 30 GLU CA C 56.659 0.000 1 148 28 30 GLU CB C 30.530 0.000 1 149 28 30 GLU H H 8.532 0.006 1 150 28 30 GLU N N 120.466 0.065 1 151 29 31 ASN C C 175.742 0.004 1 152 29 31 ASN CA C 53.647 0.055 1 153 29 31 ASN CB C 39.101 0.024 1 154 29 31 ASN H H 8.526 0.006 1 155 29 31 ASN N N 119.677 0.041 1 156 30 32 GLY C C 174.180 0.000 1 157 30 32 GLY CA C 45.752 0.046 1 158 30 32 GLY H H 8.516 0.005 1 159 30 32 GLY N N 109.556 0.045 1 160 31 33 ARG C C 175.994 0.000 1 161 31 33 ARG CA C 56.396 0.047 1 162 31 33 ARG CB C 30.963 0.040 1 163 31 33 ARG H H 8.190 0.005 1 164 31 33 ARG HA H 4.353 0.000 1 165 31 33 ARG N N 120.419 0.043 1 166 32 34 ASP C C 175.287 0.008 1 167 32 34 ASP CA C 54.414 0.000 1 168 32 34 ASP CB C 41.147 0.089 1 169 32 34 ASP H H 8.466 0.005 1 170 32 34 ASP N N 121.168 0.027 1 171 33 35 ALA C C 175.173 0.000 1 172 33 35 ALA CA C 50.770 0.000 1 173 33 35 ALA CB C 18.249 0.000 1 174 33 35 ALA H H 8.208 0.006 1 175 33 35 ALA N N 125.438 0.033 1 176 34 36 PRO C C 176.676 0.000 1 177 34 36 PRO CA C 63.114 0.000 1 178 35 37 ALA C C 177.530 0.019 1 179 35 37 ALA CA C 52.769 0.000 1 180 35 37 ALA CB C 19.260 0.000 1 181 35 37 ALA H H 8.595 0.008 1 182 35 37 ALA N N 124.915 0.030 1 183 36 38 ASN C C 175.633 0.002 1 184 36 38 ASN CB C 38.894 0.000 1 185 36 38 ASN H H 8.513 0.006 1 186 36 38 ASN N N 117.900 0.029 1 187 37 39 GLY C C 173.671 0.000 1 188 37 39 GLY CA C 45.574 0.000 1 189 37 39 GLY H H 8.420 0.007 1 190 37 39 GLY N N 109.438 0.045 1 191 38 40 ASN C C 174.975 0.010 1 192 38 40 ASN CA C 53.221 0.018 1 193 38 40 ASN CB C 39.133 0.006 1 194 38 40 ASN H H 8.407 0.007 1 195 38 40 ASN N N 118.836 0.052 1 196 39 41 ALA C C 177.391 0.009 1 197 39 41 ALA CA C 52.942 0.100 1 198 39 41 ALA CB C 19.156 0.000 1 199 39 41 ALA H H 8.450 0.010 1 200 39 41 ALA N N 124.759 0.038 1 201 40 42 ASN C C 175.119 0.006 1 202 40 42 ASN CA C 53.422 0.046 1 203 40 42 ASN CB C 38.948 0.070 1 204 40 42 ASN H H 8.504 0.006 1 205 40 42 ASN N N 117.677 0.029 1 206 41 43 GLU CA C 56.729 0.000 1 207 41 43 GLU CB C 30.271 0.000 1 208 41 43 GLU H H 8.407 0.005 1 209 41 43 GLU N N 121.240 0.030 1 210 42 44 GLU C C 176.206 0.018 1 211 42 44 GLU CA C 56.633 0.000 1 212 42 44 GLU CB C 30.179 0.000 1 213 42 44 GLU H H 8.503 0.006 1 214 42 44 GLU N N 121.826 0.031 1 215 43 45 ASN C C 175.635 0.004 1 216 43 45 ASN CA C 53.469 0.000 1 217 43 45 ASN CB C 39.170 0.072 1 218 43 45 ASN H H 8.570 0.005 1 219 43 45 ASN N N 119.827 0.032 1 220 44 46 GLY C C 174.011 0.015 1 221 44 46 GLY H H 8.419 0.000 1 222 44 46 GLY N N 109.591 0.029 1 223 45 47 GLU C C 176.369 0.000 1 224 45 47 GLU H H 8.408 0.005 1 225 45 47 GLU N N 120.642 0.038 1 226 46 48 GLN C C 175.834 0.010 1 227 46 48 GLN CA C 55.806 0.000 1 228 46 48 GLN CB C 29.804 0.025 1 229 46 48 GLN H H 8.548 0.006 1 230 46 48 GLN HA H 4.315 0.000 1 231 46 48 GLN N N 121.647 0.028 1 232 47 49 GLU C C 176.085 0.000 1 233 47 49 GLU CA C 56.682 0.075 1 234 47 49 GLU CB C 30.420 0.000 1 235 47 49 GLU H H 8.613 0.007 1 236 47 49 GLU N N 123.303 0.028 1 237 48 50 ALA C C 177.243 0.012 1 238 48 50 ALA CA C 52.621 0.017 1 239 48 50 ALA CB C 19.579 0.044 1 240 48 50 ALA H H 8.487 0.007 1 241 48 50 ALA HA H 4.327 0.000 1 242 48 50 ALA N N 125.668 0.047 1 243 49 51 ASP C C 175.822 0.010 1 244 49 51 ASP CA C 54.375 0.040 1 245 49 51 ASP CB C 41.209 0.074 1 246 49 51 ASP H H 8.453 0.005 1 247 49 51 ASP N N 120.295 0.039 1 248 50 52 ASN C C 174.950 0.000 1 249 50 52 ASN CA C 53.323 0.021 1 250 50 52 ASN CB C 39.348 0.094 1 251 50 52 ASN H H 8.437 0.005 1 252 50 52 ASN HA H 4.684 0.000 1 253 50 52 ASN N N 119.433 0.034 1 254 51 53 GLU C C 176.120 0.000 1 255 51 53 GLU CA C 56.547 0.000 1 256 51 53 GLU CB C 30.291 0.000 1 257 51 53 GLU H H 8.507 0.004 1 258 51 53 GLU HA H 4.283 0.000 1 259 51 53 GLU N N 121.940 0.032 1 260 52 54 VAL C C 175.497 0.004 1 261 52 54 VAL CA C 61.971 0.021 1 262 52 54 VAL CB C 33.318 0.066 1 263 52 54 VAL H H 8.271 0.006 1 264 52 54 VAL HA H 4.113 0.000 1 265 52 54 VAL N N 121.478 0.032 1 266 53 55 ASP C C 175.958 0.008 1 267 53 55 ASP CA C 54.325 0.045 1 268 53 55 ASP CB C 41.375 0.010 1 269 53 55 ASP H H 8.549 0.005 1 270 53 55 ASP HA H 4.614 0.000 1 271 53 55 ASP N N 125.320 0.039 1 272 54 56 GLU CB C 30.604 0.000 1 273 54 56 GLU H H 8.531 0.006 1 274 54 56 GLU HA H 4.284 0.000 1 275 54 56 GLU N N 122.426 0.025 1 276 55 57 GLU C C 176.266 0.000 1 277 55 57 GLU CA C 56.364 0.000 1 278 55 57 GLU H H 8.572 0.008 1 279 55 57 GLU HA H 4.281 0.000 1 280 55 57 GLU N N 122.495 0.031 1 281 56 58 GLU CB C 30.767 0.000 1 282 56 58 GLU H H 8.542 0.006 1 283 56 58 GLU HA H 4.250 0.000 1 284 56 58 GLU N N 122.994 0.029 1 285 57 59 GLU C C 176.252 0.000 1 286 57 59 GLU H H 8.622 0.006 1 287 57 59 GLU HA H 4.283 0.000 1 288 57 59 GLU N N 123.386 0.056 1 289 58 60 GLU C C 176.817 0.011 1 290 58 60 GLU CA C 56.766 0.082 1 291 58 60 GLU CB C 30.611 0.053 1 292 58 60 GLU H H 8.687 0.006 1 293 58 60 GLU N N 123.577 0.033 1 294 59 61 GLY C C 174.415 0.007 1 295 59 61 GLY CA C 45.439 0.035 1 296 59 61 GLY H H 8.656 0.007 1 297 59 61 GLY HA2 H 3.963 0.000 1 298 59 61 GLY N N 110.856 0.043 1 299 60 62 GLY C C 173.955 0.018 1 300 60 62 GLY CA C 45.146 0.000 1 301 60 62 GLY H H 8.435 0.005 1 302 60 62 GLY HA2 H 3.985 0.000 1 303 60 62 GLY N N 109.139 0.039 1 304 61 63 GLU H H 8.540 0.005 1 305 61 63 GLU HA H 4.298 0.000 1 306 61 63 GLU N N 120.609 0.033 1 307 62 64 GLU N N 122.461 0.000 1 308 67 69 GLU C C 176.248 0.000 1 309 67 69 GLU CA C 56.325 0.000 1 310 67 69 GLU CB C 30.715 0.046 1 311 67 69 GLU N N 123.670 0.000 1 312 68 70 GLU C C 176.824 0.000 1 313 68 70 GLU CA C 56.840 0.102 1 314 68 70 GLU CB C 30.583 0.000 1 315 68 70 GLU H H 8.722 0.004 1 316 68 70 GLU HA H 4.282 0.000 1 317 68 70 GLU N N 123.708 0.040 1 318 69 71 GLY C C 173.630 0.004 1 319 69 71 GLY CA C 45.239 0.078 1 320 69 71 GLY H H 8.574 0.006 1 321 69 71 GLY HA2 H 4.006 0.000 1 322 69 71 GLY N N 110.664 0.055 1 323 70 72 ASP C C 176.772 0.021 1 324 70 72 ASP CA C 54.420 0.000 1 325 70 72 ASP CB C 41.654 0.000 1 326 70 72 ASP H H 8.462 0.006 1 327 70 72 ASP HA H 4.594 0.000 1 328 70 72 ASP N N 120.449 0.042 1 329 71 73 GLY C C 173.977 0.000 1 330 71 73 GLY CA C 45.432 0.040 1 331 71 73 GLY H H 8.551 0.004 1 332 71 73 GLY HA2 H 3.953 0.000 1 333 71 73 GLY N N 109.613 0.028 1 334 72 74 GLU C C 176.433 0.000 1 335 72 74 GLU CA C 56.412 0.000 1 336 72 74 GLU CB C 30.505 0.014 1 337 72 74 GLU H H 8.410 0.006 1 338 72 74 GLU HA H 4.306 0.000 1 339 72 74 GLU N N 120.615 0.108 1 340 73 75 GLU C C 176.300 0.000 1 341 73 75 GLU CA C 56.487 0.056 1 342 73 75 GLU CB C 30.558 0.026 1 343 73 75 GLU H H 8.643 0.004 1 344 73 75 GLU HA H 4.274 0.000 1 345 73 75 GLU N N 122.471 0.038 1 346 74 76 GLU C C 176.075 0.000 1 347 74 76 GLU CA C 56.430 0.000 1 348 74 76 GLU CB C 30.703 0.001 1 349 74 76 GLU H H 8.608 0.007 1 350 74 76 GLU HA H 4.296 0.000 1 351 74 76 GLU N N 122.856 0.026 1 352 75 77 ASP C C 176.510 0.026 1 353 75 77 ASP CA C 54.555 0.041 1 354 75 77 ASP CB C 41.445 0.030 1 355 75 77 ASP H H 8.599 0.005 1 356 75 77 ASP HA H 4.583 0.000 1 357 75 77 ASP N N 122.590 0.031 1 358 76 78 GLY C C 173.640 0.009 1 359 76 78 GLY CA C 45.451 0.000 1 360 76 78 GLY H H 8.469 0.005 1 361 76 78 GLY HA2 H 3.962 0.000 1 362 76 78 GLY N N 109.711 0.036 1 363 77 79 ASP C C 176.194 0.000 1 364 77 79 ASP CA C 54.235 0.000 1 365 77 79 ASP CB C 41.513 0.000 1 366 77 79 ASP H H 8.411 0.006 1 367 77 79 ASP HA H 4.627 0.000 1 368 77 79 ASP N N 120.741 0.028 1 369 78 80 GLU C C 176.265 0.000 1 370 78 80 GLU CA C 56.827 0.000 1 371 78 80 GLU CB C 30.588 0.060 1 372 78 80 GLU H H 8.578 0.006 1 373 78 80 GLU HA H 4.256 0.000 1 374 78 80 GLU N N 121.553 0.026 1 375 79 81 ASP C C 176.263 0.000 1 376 79 81 ASP H H 8.531 0.006 1 377 79 81 ASP HA H 4.577 0.000 1 378 79 81 ASP N N 122.115 0.053 1 379 80 82 GLU C C 176.575 0.000 1 380 80 82 GLU H H 8.509 0.006 1 381 80 82 GLU HA H 4.238 0.000 1 382 80 82 GLU N N 122.360 0.035 1 383 81 83 GLU C C 176.379 0.013 1 384 81 83 GLU CA C 56.679 0.000 1 385 81 83 GLU CB C 30.157 0.000 1 386 81 83 GLU H H 8.552 0.006 1 387 81 83 GLU HA H 4.215 0.000 1 388 81 83 GLU N N 122.148 0.026 1 389 82 84 ALA C C 178.028 0.011 1 390 82 84 ALA CA C 52.967 0.032 1 391 82 84 ALA CB C 19.260 0.000 1 392 82 84 ALA H H 8.321 0.004 1 393 82 84 ALA HA H 4.306 0.000 1 394 82 84 ALA N N 125.453 0.024 1 395 83 85 GLU C C 176.716 0.015 1 396 83 85 GLU CA C 57.069 0.000 1 397 83 85 GLU CB C 30.110 0.000 1 398 83 85 GLU H H 8.518 0.005 1 399 83 85 GLU HA H 4.241 0.000 1 400 83 85 GLU N N 120.272 0.052 1 401 84 86 SER C C 174.659 0.019 1 402 84 86 SER CA C 58.687 0.000 1 403 84 86 SER CB C 63.893 0.000 1 404 84 86 SER H H 8.378 0.009 1 405 84 86 SER N N 116.752 0.047 1 406 85 87 ALA C C 178.198 0.015 1 407 85 87 ALA CA C 53.148 0.025 1 408 85 87 ALA CB C 19.182 0.000 1 409 85 87 ALA H H 8.492 0.006 1 410 85 87 ALA N N 126.366 0.047 1 411 86 88 THR C C 175.271 0.016 1 412 86 88 THR CA C 62.593 0.000 1 413 86 88 THR CB C 69.830 0.040 1 414 86 88 THR H H 8.161 0.004 1 415 86 88 THR HA H 4.287 0.000 1 416 86 88 THR N N 112.227 0.034 1 417 87 89 GLY C C 173.852 0.000 1 418 87 89 GLY CA C 45.483 0.024 1 419 87 89 GLY H H 8.374 0.006 1 420 87 89 GLY HA2 H 3.988 0.000 1 421 87 89 GLY N N 111.221 0.045 1 422 88 90 LYS C C 176.472 0.017 1 423 88 90 LYS CA C 56.434 0.025 1 424 88 90 LYS CB C 33.248 0.060 1 425 88 90 LYS H H 8.184 0.005 1 426 88 90 LYS N N 121.262 0.044 1 427 89 91 ARG C C 175.927 0.011 1 428 89 91 ARG CA C 56.056 0.052 1 429 89 91 ARG CB C 31.025 0.003 1 430 89 91 ARG H H 8.513 0.005 1 431 89 91 ARG HA H 4.311 0.000 1 432 89 91 ARG N N 123.509 0.034 1 433 90 92 ALA C C 177.430 0.021 1 434 90 92 ALA CA C 52.643 0.000 1 435 90 92 ALA CB C 19.242 0.018 1 436 90 92 ALA H H 8.550 0.005 1 437 90 92 ALA HA H 4.267 0.000 1 438 90 92 ALA N N 126.479 0.050 1 439 91 93 ALA C C 177.901 0.016 1 440 91 93 ALA CA C 52.817 0.048 1 441 91 93 ALA CB C 19.318 0.000 1 442 91 93 ALA H H 8.442 0.005 1 443 91 93 ALA HA H 4.286 0.000 1 444 91 93 ALA N N 123.774 0.033 1 445 92 94 GLU C C 176.207 0.013 1 446 92 94 GLU CA C 56.881 0.098 1 447 92 94 GLU CB C 30.153 0.079 1 448 92 94 GLU H H 8.520 0.004 1 449 92 94 GLU HA H 4.246 0.000 1 450 92 94 GLU N N 119.480 0.045 1 451 93 95 ASP C C 175.800 0.010 1 452 93 95 ASP CA C 54.558 0.012 1 453 93 95 ASP CB C 41.306 0.036 1 454 93 95 ASP H H 8.306 0.004 1 455 93 95 ASP HA H 4.573 0.000 1 456 93 95 ASP N N 120.599 0.029 1 457 94 96 ASP C C 176.152 0.025 1 458 94 96 ASP H H 8.280 0.006 1 459 94 96 ASP HA H 4.579 0.000 1 460 94 96 ASP N N 120.738 0.039 1 461 95 97 GLU C C 176.107 0.000 1 462 95 97 GLU CA C 56.617 0.000 1 463 95 97 GLU CB C 30.477 0.000 1 464 95 97 GLU H H 8.394 0.005 1 465 95 97 GLU N N 121.269 0.040 1 466 96 98 ASP CA C 54.416 0.011 1 467 96 98 ASP CB C 41.395 0.001 1 468 96 98 ASP H H 8.475 0.007 1 469 96 98 ASP HA H 4.581 0.000 1 470 96 98 ASP N N 121.848 0.039 1 471 97 99 ASP C C 175.918 0.000 1 472 97 99 ASP CA C 54.548 0.010 1 473 97 99 ASP CB C 41.398 0.000 1 474 97 99 ASP H H 8.393 0.005 1 475 97 99 ASP HA H 4.559 0.000 1 476 97 99 ASP N N 121.448 0.056 1 477 98 100 ASP C C 176.394 0.000 1 478 98 100 ASP CA C 54.322 0.000 1 479 98 100 ASP CB C 41.167 0.000 1 480 98 100 ASP H H 8.423 0.004 1 481 98 100 ASP HA H 4.606 0.000 1 482 98 100 ASP N N 121.021 0.030 1 483 99 101 VAL C C 176.232 0.006 1 484 99 101 VAL CA C 63.147 0.036 1 485 99 101 VAL CB C 32.613 0.000 1 486 99 101 VAL H H 8.074 0.006 1 487 99 101 VAL HA H 4.019 0.000 1 488 99 101 VAL N N 120.168 0.029 1 489 100 102 ASP C C 176.827 0.002 1 490 100 102 ASP CA C 55.002 0.036 1 491 100 102 ASP CB C 41.150 0.060 1 492 100 102 ASP H H 8.506 0.006 1 493 100 102 ASP HA H 4.666 0.000 1 494 100 102 ASP N N 122.881 0.051 1 495 101 103 THR C C 174.948 0.005 1 496 101 103 THR CA C 62.965 0.000 1 497 101 103 THR CB C 69.385 0.000 1 498 101 103 THR H H 8.103 0.005 1 499 101 103 THR HA H 4.189 0.000 1 500 101 103 THR N N 115.030 0.037 1 501 102 104 LYS C C 176.607 0.021 1 502 102 104 LYS CA C 56.758 0.011 1 503 102 104 LYS CB C 32.579 0.032 1 504 102 104 LYS H H 8.279 0.005 1 505 102 104 LYS HA H 4.230 0.000 1 506 102 104 LYS N N 123.226 0.036 1 507 103 105 LYS C C 176.393 0.004 1 508 103 105 LYS CA C 56.517 0.000 1 509 103 105 LYS CB C 33.018 0.024 1 510 103 105 LYS H H 8.206 0.004 1 511 103 105 LYS HA H 4.298 0.000 1 512 103 105 LYS N N 122.249 0.031 1 513 104 106 GLN C C 175.740 0.010 1 514 104 106 GLN CA C 55.911 0.038 1 515 104 106 GLN CB C 29.571 0.026 1 516 104 106 GLN H H 8.444 0.005 1 517 104 106 GLN HA H 4.284 0.000 1 518 104 106 GLN N N 122.053 0.033 1 519 105 107 LYS C C 176.607 0.020 1 520 105 107 LYS CA C 56.595 0.085 1 521 105 107 LYS CB C 33.270 0.007 1 522 105 107 LYS H H 8.522 0.006 1 523 105 107 LYS N N 123.760 0.030 1 524 106 108 THR C C 174.365 0.033 1 525 106 108 THR CA C 61.759 0.019 1 526 106 108 THR CB C 70.168 0.064 1 527 106 108 THR H H 8.506 0.006 1 528 106 108 THR HA H 4.472 0.000 1 529 106 108 THR N N 115.821 0.027 1 530 107 109 ASP C C 176.061 0.014 1 531 107 109 ASP CA C 54.780 0.037 1 532 107 109 ASP CB C 41.152 0.000 1 533 107 109 ASP H H 8.490 0.005 1 534 107 109 ASP HA H 4.602 0.000 1 535 107 109 ASP N N 122.120 0.029 1 536 108 110 GLU C C 176.018 0.000 1 537 108 110 GLU CA C 56.761 0.085 1 538 108 110 GLU CB C 30.491 0.084 1 539 108 110 GLU H H 8.343 0.004 1 540 108 110 GLU HA H 4.293 0.000 1 541 108 110 GLU N N 120.175 0.033 1 542 109 111 ASP C C 175.035 0.014 1 543 109 111 ASP CA C 54.588 0.009 1 544 109 111 ASP CB C 41.501 0.049 1 545 109 111 ASP H H 8.596 0.000 1 546 109 111 ASP HA H 4.628 0.000 1 547 109 111 ASP N N 121.489 0.022 1 548 110 112 ASP C C 180.956 0.000 1 549 110 112 ASP CA C 56.171 0.000 1 550 110 112 ASP CB C 42.240 0.000 1 551 110 112 ASP H H 7.993 0.004 1 552 110 112 ASP HA H 4.322 0.000 1 553 110 112 ASP N N 126.045 0.021 1 stop_ save_