data_26719 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and triple resonance 1H, 13C, and 15N Chemical Shift Assignments for residues 420-500 of Saccharomyces cerevisiae transcription factor Ash1 ; _BMRB_accession_number 26719 _BMRB_flat_file_name bmr26719.str _Entry_type original _Submission_date 2015-12-11 _Accession_date 2015-12-11 _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 Martin Erik W. . 2 Grace Christy R. . 3 Mittag Tanja . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 67 "13C chemical shifts" 198 "15N chemical shifts" 70 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-02-23 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 26720 'Phosphorylated Ash1 420-500' stop_ _Original_release_date 2015-12-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 27807972 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Martin Erik W. . 2 Holehouse Alex S. . 3 Grace Christy R. . 4 Hughes Alex . . 5 Pappu Rohit V. . 6 Mittag Tanja . . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full 'Journal of the American Chemical Society' _Journal_volume 138 _Journal_issue 47 _Journal_ISSN 1520-5126 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 15323 _Page_last 15335 _Year 2016 _Details . loop_ _Keyword ABSINTH SAXS SSP polymer proline stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Ash1 420-500' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Ash1 420-500' $Ash1_420-500 stop_ _System_molecular_weight 8830 _System_physical_state 'intrinsically disordered' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details ; Residues 420-500 of the yeast transcription factor Ash1. An additional N-terminal Gly-Ala was present from the affinity tag cleavage. ; save_ ######################## # Monomeric polymers # ######################## save_Ash1_420-500 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Ash1_420-500 _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'C-terminal disordered 80 amino acids of Yeast transcription factor.' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 83 _Mol_residue_sequence ; GASASSSPSPSTPTKSGKMR SRSSSPVRPKAYTPSPRSPN YHRFALDSPPQSPRRSSNSS ITKKGSRRSSGSSPTRHTTR VCV ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 GLY 2 2 ALA 3 3 SER 4 4 ALA 5 5 SER 6 6 SER 7 7 SER 8 8 PRO 9 9 SER 10 10 PRO 11 11 SER 12 12 THR 13 13 PRO 14 14 THR 15 15 LYS 16 16 SER 17 17 GLY 18 18 LYS 19 19 MET 20 20 ARG 21 21 SER 22 22 ARG 23 23 SER 24 24 SER 25 25 SER 26 26 PRO 27 27 VAL 28 28 ARG 29 29 PRO 30 30 LYS 31 31 ALA 32 32 TYR 33 33 THR 34 34 PRO 35 35 SER 36 36 PRO 37 37 ARG 38 38 SER 39 39 PRO 40 40 ASN 41 41 TYR 42 42 HIS 43 43 ARG 44 44 PHE 45 45 ALA 46 46 LEU 47 47 ASP 48 48 SER 49 49 PRO 50 50 PRO 51 51 GLN 52 52 SER 53 53 PRO 54 54 ARG 55 55 ARG 56 56 SER 57 57 SER 58 58 ASN 59 59 SER 60 60 SER 61 61 ILE 62 62 THR 63 63 LYS 64 64 LYS 65 65 GLY 66 66 SER 67 67 ARG 68 68 ARG 69 69 SER 70 70 SER 71 71 GLY 72 72 SER 73 73 SER 74 74 PRO 75 75 THR 76 76 ARG 77 77 HIS 78 78 THR 79 79 THR 80 80 ARG 81 81 VAL 82 82 CYS 83 83 VAL 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 $Ash1_420-500 "baker's yeast" 4932 Eukaryota Fungi Saccharomyces cerevisiae 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 $Ash1_420-500 'recombinant technology' . Escherichia coli . pET stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'PBS buffer w/ 10mM DTT' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Ash1_420-500 0.7 mM '[U-100% 13C; U-100% 15N]' DTT 10 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_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_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_(H)N(COCA)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (H)N(COCA)NH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1627 . M pH 6.95 0.05 pH pressure 1 . atm temperature 278 0.01 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_Ash1_420-500_reference _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 na indirect . . . 0.2514 DSS H 1 'methyl protons' ppm 0 na direct . . . 1 DSS N 15 'methyl protons' ppm 0 na indirect . . . 0.1013 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_Ash1_420-500_shift_list _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $TOPSPIN stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCACB' '3D CBCA(CO)NH' '3D HN(CA)CO' '3D (H)N(COCA)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $Ash1_420-500_reference _Mol_system_component_name 'Ash1 420-500' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 3 3 SER H H 8.323 0.020 1 2 3 3 SER C C 174.519 0.300 1 3 3 3 SER CA C 58.183 0.300 1 4 3 3 SER CB C 63.706 0.300 1 5 3 3 SER N N 115.801 0.300 1 6 4 4 ALA H H 8.335 0.020 1 7 4 4 ALA C C 177.939 0.300 1 8 4 4 ALA CA C 52.583 0.300 1 9 4 4 ALA CB C 18.984 0.300 1 10 4 4 ALA N N 126.372 0.300 1 11 5 5 SER H H 8.158 0.020 1 12 5 5 SER C C 174.620 0.300 1 13 5 5 SER CA C 58.260 0.300 1 14 5 5 SER CB C 63.629 0.300 1 15 5 5 SER N N 114.887 0.300 1 16 6 6 SER H H 8.132 0.020 1 17 6 6 SER C C 174.186 0.300 1 18 6 6 SER CA C 58.254 0.300 1 19 6 6 SER CB C 63.823 0.300 1 20 6 6 SER N N 117.768 0.300 1 21 7 7 SER H H 8.208 0.020 1 22 7 7 SER C C 172.397 0.300 1 23 7 7 SER CA C 56.467 0.300 1 24 7 7 SER CB C 63.048 0.300 1 25 7 7 SER N N 118.929 0.300 1 26 9 9 SER H H 8.288 0.020 1 27 9 9 SER C C 172.905 0.300 1 28 9 9 SER CA C 56.342 0.300 1 29 9 9 SER CB C 63.399 0.300 1 30 9 9 SER N N 118.004 0.300 1 31 10 10 PRO N N 137.774 0.300 1 32 11 11 SER H H 8.260 0.020 1 33 11 11 SER C C 174.406 0.300 1 34 11 11 SER CA C 58.106 0.300 1 35 11 11 SER CB C 63.706 0.300 1 36 11 11 SER N N 116.124 0.300 1 37 12 12 THR H H 8.012 0.020 1 38 12 12 THR C C 172.826 0.300 1 39 12 12 THR CA C 59.860 0.300 1 40 12 12 THR CB C 69.618 0.300 1 41 12 12 THR N N 118.496 0.300 1 42 14 14 THR H H 8.170 0.020 1 43 14 14 THR C C 174.778 0.300 1 44 14 14 THR CA C 62.095 0.300 1 45 14 14 THR CB C 69.766 0.300 1 46 14 14 THR N N 115.449 0.300 1 47 15 15 LYS H H 8.293 0.020 1 48 15 15 LYS C C 176.720 0.300 1 49 15 15 LYS CA C 56.265 0.300 1 50 15 15 LYS CB C 32.639 0.300 1 51 15 15 LYS N N 124.145 0.300 1 52 16 16 SER H H 8.222 0.020 1 53 16 16 SER C C 175.140 0.300 1 54 16 16 SER CA C 58.336 0.300 1 55 16 16 SER CB C 63.629 0.300 1 56 16 16 SER N N 117.113 0.300 1 57 17 17 GLY H H 8.273 0.020 1 58 17 17 GLY C C 174.180 0.300 1 59 17 17 GLY CA C 45.146 0.300 1 60 17 17 GLY N N 111.025 0.300 1 61 18 18 LYS H H 7.994 0.020 1 62 18 18 LYS C C 176.904 0.300 1 63 18 18 LYS CA C 56.342 0.300 1 64 18 18 LYS CB C 32.792 0.300 1 65 18 18 LYS N N 120.770 0.300 1 66 19 19 MET H H 8.244 0.020 1 67 19 19 MET C C 176.362 0.300 1 68 19 19 MET CA C 55.498 0.300 1 69 19 19 MET CB C 32.178 0.300 1 70 19 19 MET N N 121.672 0.300 1 71 20 20 ARG H H 8.229 0.020 1 72 20 20 ARG C C 176.449 0.300 1 73 20 20 ARG CA C 55.958 0.300 1 74 20 20 ARG CB C 30.491 0.300 1 75 20 20 ARG N N 122.996 0.300 1 76 21 21 SER H H 8.258 0.020 1 77 21 21 SER C C 174.699 0.300 1 78 21 21 SER CA C 58.336 0.300 1 79 21 21 SER CB C 63.553 0.300 1 80 21 21 SER N N 117.605 0.300 1 81 22 22 ARG H H 8.346 0.020 1 82 22 22 ARG C C 176.517 0.300 1 83 22 22 ARG CA C 56.035 0.300 1 84 22 22 ARG CB C 30.567 0.300 1 85 22 22 ARG N N 123.371 0.300 1 86 23 23 SER H H 8.239 0.020 1 87 23 23 SER C C 174.575 0.300 1 88 23 23 SER CA C 58.336 0.300 1 89 23 23 SER CB C 63.553 0.300 1 90 23 23 SER N N 117.080 0.300 1 91 24 24 SER H H 8.217 0.020 1 92 24 24 SER C C 174.203 0.300 1 93 24 24 SER CA C 58.493 0.300 1 94 24 24 SER CB C 63.427 0.300 1 95 24 24 SER N N 118.030 0.300 1 96 25 25 SER H H 8.148 0.020 1 97 25 25 SER C C 172.408 0.300 1 98 25 25 SER CA C 56.467 0.300 1 99 25 25 SER CB C 63.144 0.300 1 100 25 25 SER N N 118.903 0.300 1 101 27 27 VAL H H 8.123 0.020 1 102 27 27 VAL C C 176.179 0.300 1 103 27 27 VAL CA C 62.479 0.300 1 104 27 27 VAL CB C 32.219 0.300 1 105 27 27 VAL N N 121.449 0.300 1 106 28 28 ARG H H 8.311 0.020 1 107 28 28 ARG C C 174.056 0.300 1 108 28 28 ARG CA C 53.504 0.300 1 109 28 28 ARG CB C 29.800 0.300 1 110 28 28 ARG N N 127.075 0.300 1 111 29 29 PRO N N 136.611 0.300 1 112 30 30 LYS H H 8.255 0.020 1 113 30 30 LYS C C 176.362 0.300 1 114 30 30 LYS CA C 56.342 0.300 1 115 30 30 LYS CB C 32.562 0.300 1 116 30 30 LYS N N 122.136 0.300 1 117 31 31 ALA H H 8.162 0.020 1 118 31 31 ALA C C 177.059 0.300 1 119 31 31 ALA CA C 52.046 0.300 1 120 31 31 ALA CB C 18.984 0.300 1 121 31 31 ALA N N 125.320 0.300 1 122 32 32 TYR H H 8.106 0.020 1 123 32 32 TYR C C 175.366 0.300 1 124 32 32 TYR CA C 57.799 0.300 1 125 32 32 TYR CB C 38.775 0.300 1 126 32 32 TYR N N 120.910 0.300 1 127 33 33 THR H H 7.853 0.020 1 128 33 33 THR C C 175.357 0.300 1 129 33 33 THR CA C 59.027 0.300 1 130 33 33 THR CB C 70.073 0.300 1 131 33 33 THR N N 121.426 0.300 1 132 35 35 SER H H 8.362 0.020 1 133 35 35 SER C C 172.837 0.300 1 134 35 35 SER CA C 56.342 0.300 1 135 35 35 SER CB C 63.399 0.300 1 136 35 35 SER N N 118.145 0.300 1 137 37 37 ARG H H 8.141 0.020 1 138 37 37 ARG C C 176.280 0.300 1 139 37 37 ARG CA C 55.652 0.300 1 140 37 37 ARG CB C 30.567 0.300 1 141 37 37 ARG N N 120.465 0.300 1 142 38 38 SER H H 8.158 0.020 1 143 38 38 SER C C 173.266 0.300 1 144 38 38 SER CA C 56.265 0.300 1 145 38 38 SER CB C 63.092 0.300 1 146 38 38 SER N N 118.473 0.300 1 147 40 40 ASN H H 8.164 0.020 1 148 40 40 ASN C C 174.936 0.300 1 149 40 40 ASN CA C 52.967 0.300 1 150 40 40 ASN CB C 38.238 0.300 1 151 40 40 ASN N N 117.137 0.300 1 152 41 41 TYR H H 7.718 0.020 1 153 41 41 TYR C C 175.637 0.300 1 154 41 41 TYR CA C 58.643 0.300 1 155 41 41 TYR CB C 38.471 0.300 1 156 41 41 TYR N N 120.817 0.300 1 157 42 42 HIS H H 7.958 0.020 1 158 42 42 HIS C C 174.684 0.300 1 159 42 42 HIS CA C 55.805 0.300 1 160 42 42 HIS CB C 29.877 0.300 1 161 42 42 HIS N N 121.188 0.300 1 162 43 43 ARG H H 7.824 0.020 1 163 43 43 ARG C C 175.934 0.300 1 164 43 43 ARG CA C 56.235 0.300 1 165 43 43 ARG CB C 30.128 0.300 1 166 43 43 ARG N N 122.012 0.300 1 167 44 44 PHE H H 7.982 0.020 1 168 44 44 PHE C C 175.506 0.300 1 169 44 44 PHE CA C 57.493 0.300 1 170 44 44 PHE CB C 39.159 0.300 1 171 44 44 PHE N N 120.629 0.300 1 172 45 45 ALA H H 7.976 0.020 1 173 45 45 ALA C C 177.612 0.300 1 174 45 45 ALA CA C 52.276 0.300 1 175 45 45 ALA CB C 19.061 0.300 1 176 45 45 ALA N N 124.871 0.300 1 177 46 46 LEU H H 7.999 0.020 1 178 46 46 LEU C C 177.236 0.300 1 179 46 46 LEU CA C 55.038 0.300 1 180 46 46 LEU CB C 41.997 0.300 1 181 46 46 LEU N N 120.934 0.300 1 182 47 47 ASP H H 8.070 0.020 1 183 47 47 ASP C C 175.930 0.300 1 184 47 47 ASP CA C 54.117 0.300 1 185 47 47 ASP CB C 40.693 0.300 1 186 47 47 ASP N N 120.160 0.300 1 187 48 48 SER H H 7.906 0.020 1 188 48 48 SER C C 171.855 0.300 1 189 48 48 SER CA C 56.342 0.300 1 190 48 48 SER CB C 63.169 0.300 1 191 48 48 SER N N 116.809 0.300 1 192 49 49 PRO N N 138.991 0.300 1 193 51 51 GLN H H 8.370 0.020 1 194 51 51 GLN C C 175.969 0.300 1 195 51 51 GLN CA C 55.450 0.300 1 196 51 51 GLN CB C 29.274 0.300 1 197 51 51 GLN N N 120.465 0.300 1 198 52 52 SER H H 8.258 0.020 1 199 52 52 SER C C 172.690 0.300 1 200 52 52 SER CA C 56.419 0.300 1 201 52 52 SER CB C 63.092 0.300 1 202 52 52 SER N N 118.824 0.300 1 203 54 54 ARG H H 8.263 0.020 1 204 54 54 ARG C C 176.485 0.300 1 205 54 54 ARG CA C 56.024 0.300 1 206 54 54 ARG CB C 30.497 0.300 1 207 54 54 ARG N N 121.670 0.300 1 208 57 57 SER H H 8.322 0.020 1 209 57 57 SER C C 174.390 0.300 1 210 57 57 SER CA C 58.316 0.300 1 211 57 57 SER CB C 63.623 0.300 1 212 57 57 SER N N 117.987 0.300 1 213 58 58 ASN H H 8.322 0.020 1 214 58 58 ASN C C 175.482 0.300 1 215 58 58 ASN CA C 53.197 0.300 1 216 58 58 ASN CB C 38.545 0.300 1 217 58 58 ASN N N 120.777 0.300 1 218 59 59 SER H H 8.141 0.020 1 219 59 59 SER C C 174.745 0.300 1 220 59 59 SER CA C 58.643 0.300 1 221 59 59 SER CB C 63.553 0.300 1 222 59 59 SER N N 116.363 0.300 1 223 60 60 SER H H 8.205 0.020 1 224 60 60 SER C C 174.598 0.300 1 225 60 60 SER CA C 58.720 0.300 1 226 60 60 SER CB C 63.658 0.300 1 227 60 60 SER N N 118.002 0.300 1 228 61 61 ILE H H 7.935 0.020 1 229 61 61 ILE C C 176.642 0.300 1 230 61 61 ILE CA C 61.251 0.300 1 231 61 61 ILE CB C 38.392 0.300 1 232 61 61 ILE N N 122.246 0.300 1 233 62 62 THR H H 8.023 0.020 1 234 62 62 THR C C 174.519 0.300 1 235 62 62 THR CA C 61.865 0.300 1 236 62 62 THR CB C 69.536 0.300 1 237 62 62 THR N N 118.777 0.300 1 238 63 63 LYS H H 8.200 0.020 1 239 63 63 LYS C C 176.652 0.300 1 240 63 63 LYS CA C 56.265 0.300 1 241 63 63 LYS CB C 32.562 0.300 1 242 63 63 LYS N N 124.590 0.300 1 243 64 64 LYS H H 8.268 0.020 1 244 64 64 LYS C C 177.318 0.300 1 245 64 64 LYS CA C 56.649 0.300 1 246 64 64 LYS CB C 32.583 0.300 1 247 64 64 LYS N N 123.448 0.300 1 248 65 65 GLY H H 8.336 0.020 1 249 65 65 GLY C C 174.203 0.300 1 250 65 65 GLY CA C 45.146 0.300 1 251 65 65 GLY N N 110.626 0.300 1 252 66 66 SER H H 8.038 0.020 1 253 66 66 SER C C 174.688 0.300 1 254 66 66 SER CA C 58.260 0.300 1 255 66 66 SER CB C 63.783 0.300 1 256 66 66 SER N N 115.637 0.300 1 257 67 67 ARG H H 8.301 0.020 1 258 67 67 ARG C C 176.494 0.300 1 259 67 67 ARG CA C 55.936 0.300 1 260 67 67 ARG CB C 30.473 0.300 1 261 67 67 ARG N N 123.100 0.300 1 262 68 68 ARG H H 8.291 0.020 1 263 68 68 ARG C C 176.511 0.300 1 264 68 68 ARG CA C 56.164 0.300 1 265 68 68 ARG CB C 30.310 0.300 1 266 68 68 ARG N N 122.867 0.300 1 267 69 69 SER H H 8.311 0.020 1 268 69 69 SER C C 174.790 0.300 1 269 69 69 SER CA C 58.413 0.300 1 270 69 69 SER CB C 63.629 0.300 1 271 69 69 SER N N 117.629 0.300 1 272 70 70 SER H H 8.324 0.020 1 273 70 70 SER C C 175.086 0.300 1 274 70 70 SER CA C 58.490 0.300 1 275 70 70 SER CB C 63.246 0.300 1 276 70 70 SER N N 118.058 0.300 1 277 71 71 GLY H H 8.279 0.020 1 278 71 71 GLY C C 174.124 0.300 1 279 71 71 GLY CA C 45.142 0.300 1 280 71 71 GLY N N 110.758 0.300 1 281 72 72 SER H H 8.041 0.020 1 282 72 72 SER C C 174.327 0.300 1 283 72 72 SER CA C 58.106 0.300 1 284 72 72 SER CB C 63.936 0.300 1 285 72 72 SER N N 115.472 0.300 1 286 73 73 SER H H 8.242 0.020 1 287 73 73 SER C C 172.814 0.300 1 288 73 73 SER CA C 56.489 0.300 1 289 73 73 SER CB C 63.166 0.300 1 290 73 73 SER N N 118.909 0.300 1 291 75 75 THR H H 8.076 0.020 1 292 75 75 THR C C 174.519 0.300 1 293 75 75 THR CA C 61.942 0.300 1 294 75 75 THR CB C 69.613 0.300 1 295 75 75 THR N N 114.816 0.300 1 296 76 76 ARG H H 8.158 0.020 1 297 76 76 ARG C C 175.930 0.300 1 298 76 76 ARG CA C 55.805 0.300 1 299 76 76 ARG CB C 30.414 0.300 1 300 76 76 ARG N N 123.723 0.300 1 301 77 77 HIS H H 8.287 0.020 1 302 77 77 HIS C C 175.425 0.300 1 303 77 77 HIS CA C 55.946 0.300 1 304 77 77 HIS CB C 30.259 0.300 1 305 77 77 HIS N N 121.349 0.300 1 306 78 78 THR H H 8.023 0.020 1 307 78 78 THR C C 174.417 0.300 1 308 78 78 THR CA C 61.712 0.300 1 309 78 78 THR CB C 69.766 0.300 1 310 78 78 THR N N 116.199 0.300 1 311 79 79 THR H H 8.088 0.020 1 312 79 79 THR C C 174.248 0.300 1 313 79 79 THR CA C 61.869 0.300 1 314 79 79 THR CB C 69.400 0.300 1 315 79 79 THR N N 117.488 0.300 1 316 80 80 ARG H H 8.241 0.020 1 317 80 80 ARG C C 176.054 0.300 1 318 80 80 ARG CA C 55.921 0.300 1 319 80 80 ARG CB C 30.529 0.300 1 320 80 80 ARG N N 124.661 0.300 1 321 81 81 VAL H H 8.176 0.020 1 322 81 81 VAL C C 176.100 0.300 1 323 81 81 VAL CA C 62.344 0.300 1 324 81 81 VAL CB C 32.413 0.300 1 325 81 81 VAL N N 122.949 0.300 1 326 82 82 CYS H H 8.358 0.020 1 327 82 82 CYS C C 173.684 0.300 1 328 82 82 CYS CA C 58.335 0.300 1 329 82 82 CYS CB C 27.957 0.300 1 330 82 82 CYS N N 124.614 0.300 1 331 83 83 VAL H H 7.683 0.020 1 332 83 83 VAL C C 181.055 0.300 1 333 83 83 VAL CA C 63.659 0.300 1 334 83 83 VAL CB C 32.780 0.300 1 335 83 83 VAL N N 126.512 0.300 1 stop_ save_