data_4393 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N, and 13C NMR Backbone Assignments of the N Terminal Region of Human Erythrocyte Alpha Spectrin Including One Repeating Unit. ; _BMRB_accession_number 4393 _BMRB_flat_file_name bmr4393.str _Entry_type original _Submission_date 1999-09-08 _Accession_date 1999-09-09 _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 Park Sunghyouk . . 2 Liao Xiubei . . 3 Johnson Michael . . 4 Fung Leslie . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 298 "13C chemical shifts" 301 "15N chemical shifts" 149 "coupling constants" 96 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-12-07 original author 'original release' 2003-06-05 update author 'addition of coupling constants' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Park, S., Liao, X., Johnson, M.E., and Fung, L.W., "1H, 15N, and 13C NMR Backbone Assignments of the N-terminal Region of Human Erythrocyte alpha Spectrin Including one Structural Domain," J. Biomol. NMR 15, 345-346 (1999). ; _Citation_title ; 1H, 15N, and 13C NMR Backbone Assignments of the N-terminal Region of Human Erythrocyte alpha Spectrin Including one Structural Domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20149606 _PubMed_ID 10685345 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Park Sunghyouk . . 2 Liao Xiubei . . 3 Johnson Michael E. . 4 Fung Leslie W. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 15 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 345 _Page_last 346 _Year 1999 _Details . save_ ################################## # Molecular system description # ################################## save_system_Sp _Saveframe_category molecular_system _Mol_system_name spectrin _Abbreviation_common sp _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label spectrin $spectrin stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_spectrin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common spectrin _Abbreviation_common Sp _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 156 _Mol_residue_sequence ; MEQFPKETVVESSGPKVLET AEEIQERRQEVLTRYQSFKE RVAERGQKLEDSYHLQVFKR DADDLGKWIMEKVNILTDKS YEDPTNIQGKYQKHQSLEAE VQTKSRLMSELEKTREERFT MGHSAHEETKAHIEELRHLW DLLLELTLEKGDQLLR ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLU 3 GLN 4 PHE 5 PRO 6 LYS 7 GLU 8 THR 9 VAL 10 VAL 11 GLU 12 SER 13 SER 14 GLY 15 PRO 16 LYS 17 VAL 18 LEU 19 GLU 20 THR 21 ALA 22 GLU 23 GLU 24 ILE 25 GLN 26 GLU 27 ARG 28 ARG 29 GLN 30 GLU 31 VAL 32 LEU 33 THR 34 ARG 35 TYR 36 GLN 37 SER 38 PHE 39 LYS 40 GLU 41 ARG 42 VAL 43 ALA 44 GLU 45 ARG 46 GLY 47 GLN 48 LYS 49 LEU 50 GLU 51 ASP 52 SER 53 TYR 54 HIS 55 LEU 56 GLN 57 VAL 58 PHE 59 LYS 60 ARG 61 ASP 62 ALA 63 ASP 64 ASP 65 LEU 66 GLY 67 LYS 68 TRP 69 ILE 70 MET 71 GLU 72 LYS 73 VAL 74 ASN 75 ILE 76 LEU 77 THR 78 ASP 79 LYS 80 SER 81 TYR 82 GLU 83 ASP 84 PRO 85 THR 86 ASN 87 ILE 88 GLN 89 GLY 90 LYS 91 TYR 92 GLN 93 LYS 94 HIS 95 GLN 96 SER 97 LEU 98 GLU 99 ALA 100 GLU 101 VAL 102 GLN 103 THR 104 LYS 105 SER 106 ARG 107 LEU 108 MET 109 SER 110 GLU 111 LEU 112 GLU 113 LYS 114 THR 115 ARG 116 GLU 117 GLU 118 ARG 119 PHE 120 THR 121 MET 122 GLY 123 HIS 124 SER 125 ALA 126 HIS 127 GLU 128 GLU 129 THR 130 LYS 131 ALA 132 HIS 133 ILE 134 GLU 135 GLU 136 LEU 137 ARG 138 HIS 139 LEU 140 TRP 141 ASP 142 LEU 143 LEU 144 LEU 145 GLU 146 LEU 147 THR 148 LEU 149 GLU 150 LYS 151 GLY 152 ASP 153 GLN 154 LEU 155 LEU 156 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-12 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 PDB 1OWA "Solution Structural Studies On Human Erythrocyte Alpha Spectrin N Terminal Tetramerization Domain" 100.00 156 100.00 100.00 2.30e-107 PDB 3LBX "Crystal Structure Of The Erythrocyte Spectrin Tetramerization Domain Complex" 100.00 161 100.00 100.00 2.29e-107 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $spectrin 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 $spectrin 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $spectrin . mM 0.9 1.1 '[U-2H; U-15N; U-13C]' 'Phosphate Buffer' 5 mM . . . 'Sodium Chloride' 150 mM . . . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600.13 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.18 0.01 M pH 6.5 0.1 na temperature 293 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_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 0.00 external indirect cylindrical na parallel_to_Bo 0.251449530 DSS H 1 'methyl protons' ppm 0.00 external direct cylindrical na parallel_to_Bo . DSS N 15 'methyl protons' ppm 0.00 external indirect cylindrical na parallel_to_Bo 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_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name spectrin _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 MET H H 8.48 0.02 1 2 . 1 MET HA H 4.35 0.02 1 3 . 1 MET C C 176.5 0.1 1 4 . 1 MET CA C 55.5 0.1 1 5 . 1 MET N N 121.6 0.1 1 6 . 2 GLU H H 8.40 0.02 1 7 . 2 GLU HA H 4.20 0.02 1 8 . 2 GLU C C 175.8 0.1 1 9 . 2 GLU CA C 56.4 0.1 1 10 . 2 GLU N N 121.4 0.1 1 11 . 3 GLN H H 8.16 0.02 1 12 . 3 GLN HA H 4.06 0.02 1 13 . 3 GLN C C 175.0 0.1 1 14 . 3 GLN CA C 55.5 0.1 1 15 . 3 GLN N N 120.4 0.1 1 16 . 4 PHE H H 8.13 0.02 1 17 . 4 PHE HA H 4.75 0.02 1 18 . 4 PHE C C 173.4 0.1 1 19 . 4 PHE CA C 55.2 0.1 1 20 . 4 PHE N N 120.7 0.1 1 21 . 5 PRO HA H 4.26 0.02 1 22 . 5 PRO C C 176.7 0.1 1 23 . 5 PRO CA C 62.8 0.1 1 24 . 6 LYS H H 8.33 0.02 1 25 . 6 LYS HA H 4.17 0.02 1 26 . 6 LYS C C 176.4 0.1 1 27 . 6 LYS CA C 56.2 0.1 1 28 . 6 LYS N N 121.3 0.1 1 29 . 7 GLU H H 8.36 0.02 1 30 . 7 GLU HA H 4.19 0.02 1 31 . 7 GLU C C 176.3 0.1 1 32 . 7 GLU CA C 56.2 0.1 1 33 . 7 GLU N N 121.8 0.1 1 34 . 8 THR H H 8.18 0.02 1 35 . 8 THR HA H 4.16 0.02 1 36 . 8 THR C C 174.0 0.1 1 37 . 8 THR CA C 62.0 0.1 1 38 . 8 THR N N 116.4 0.1 1 39 . 9 VAL H H 8.17 0.02 1 40 . 9 VAL HA H 3.99 0.02 1 41 . 9 VAL C C 175.7 0.1 1 42 . 9 VAL CA C 62.0 0.1 1 43 . 9 VAL N N 123.6 0.1 1 44 . 10 VAL H H 8.21 0.02 1 45 . 10 VAL HA H 3.97 0.02 1 46 . 10 VAL C C 175.9 0.1 1 47 . 10 VAL CA C 61.9 0.1 1 48 . 10 VAL N N 124.6 0.1 1 49 . 11 GLU H H 8.45 0.02 1 50 . 11 GLU HA H 4.18 0.02 1 51 . 11 GLU C C 176.2 0.1 1 52 . 11 GLU CA C 56.2 0.1 1 53 . 11 GLU N N 125.1 0.1 1 54 . 12 SER H H 8.35 0.02 1 55 . 12 SER HA H 4.34 0.02 1 56 . 12 SER C C 174.4 0.1 1 57 . 12 SER CA C 58.1 0.1 1 58 . 12 SER N N 117.0 0.1 1 59 . 13 SER H H 8.33 0.02 1 60 . 13 SER HA H 4.38 0.02 1 61 . 13 SER C C 174.4 0.1 1 62 . 13 SER CA C 58.1 0.1 1 63 . 13 SER N N 117.5 0.1 1 64 . 14 GLY H H 8.12 0.02 1 65 . 14 GLY HA2 H 3.97 0.02 1 66 . 14 GLY C C 171.2 0.1 1 67 . 14 GLY CA C 44.5 0.1 1 68 . 14 GLY N N 110.0 0.1 1 69 . 15 PRO HA H 4.25 0.02 1 70 . 15 PRO C C 176.6 0.1 1 71 . 15 PRO CA C 62.7 0.1 1 72 . 16 LYS H H 8.29 0.02 1 73 . 16 LYS HA H 4.18 0.02 1 74 . 16 LYS C C 176.3 0.1 1 75 . 16 LYS CA C 55.9 0.1 1 76 . 16 LYS N N 121.5 0.1 1 77 . 17 VAL H H 8.14 0.02 1 78 . 17 VAL HA H 3.93 0.02 1 79 . 17 VAL C C 175.6 0.1 1 80 . 17 VAL CA C 62.0 0.1 1 81 . 17 VAL N N 122.4 0.1 1 82 . 18 LEU H H 8.25 0.02 1 83 . 18 LEU HA H 4.25 0.02 1 84 . 18 LEU C C 176.8 0.1 1 85 . 18 LEU CA C 54.7 0.1 1 86 . 18 LEU N N 126.0 0.1 1 87 . 19 GLU H H 8.15 0.02 1 88 . 19 GLU HA H 4.14 0.02 1 89 . 19 GLU C C 176.7 0.1 1 90 . 19 GLU CA C 55.6 0.1 1 91 . 19 GLU N N 122.0 0.1 1 92 . 20 THR H H 8.71 0.02 1 93 . 20 THR HA H 4.26 0.02 1 94 . 20 THR C C 174.8 0.1 1 95 . 20 THR CA C 60.8 0.1 1 96 . 20 THR N N 114.0 0.1 1 97 . 21 ALA H H 8.74 0.02 1 98 . 21 ALA HA H 3.91 0.02 1 99 . 21 ALA C C 180.4 0.1 1 100 . 21 ALA CA C 55.2 0.1 1 101 . 21 ALA N N 122.3 0.1 1 102 . 22 GLU H H 8.56 0.02 1 103 . 22 GLU HA H 3.90 0.02 1 104 . 22 GLU C C 178.8 0.1 1 105 . 22 GLU CA C 59.7 0.1 1 106 . 22 GLU N N 117.2 0.1 1 107 . 23 GLU H H 7.70 0.02 1 108 . 23 GLU HA H 3.89 0.02 1 109 . 23 GLU C C 179.7 0.1 1 110 . 23 GLU CA C 58.8 0.1 1 111 . 23 GLU N N 120.9 0.1 1 112 . 24 ILE H H 8.22 0.02 1 113 . 24 ILE HA H 3.45 0.02 1 114 . 24 ILE C C 177.5 0.1 1 115 . 24 ILE CA C 65.4 0.1 1 116 . 24 ILE N N 121.2 0.1 1 117 . 25 GLN H H 7.72 0.02 1 118 . 25 GLN HA H 3.88 0.02 1 119 . 25 GLN C C 178.5 0.1 1 120 . 25 GLN CA C 58.4 0.1 1 121 . 25 GLN N N 117.6 0.1 1 122 . 26 GLU H H 7.95 0.02 1 123 . 26 GLU HA H 3.88 0.02 1 124 . 26 GLU C C 178.7 0.1 1 125 . 26 GLU CA C 59.1 0.1 1 126 . 26 GLU N N 118.4 0.1 1 127 . 27 ARG H H 8.04 0.02 1 128 . 27 ARG HA H 4.06 0.02 1 129 . 27 ARG C C 179.5 0.1 1 130 . 27 ARG CA C 59.1 0.1 1 131 . 27 ARG N N 119.8 0.1 1 132 . 28 ARG H H 8.20 0.02 1 133 . 28 ARG HA H 3.85 0.02 1 134 . 28 ARG C C 178.0 0.1 1 135 . 28 ARG CA C 60.0 0.1 1 136 . 28 ARG N N 118.6 0.1 1 137 . 29 GLN H H 8.08 0.02 1 138 . 29 GLN HA H 3.86 0.02 1 139 . 29 GLN C C 178.5 0.1 1 140 . 29 GLN CA C 58.2 0.1 1 141 . 29 GLN N N 116.6 0.1 1 142 . 30 GLU H H 7.92 0.02 1 143 . 30 GLU HA H 4.04 0.02 1 144 . 30 GLU C C 178.5 0.1 1 145 . 30 GLU CA C 58.9 0.1 1 146 . 30 GLU N N 119.5 0.1 1 147 . 31 VAL H H 7.45 0.02 1 148 . 31 VAL HA H 3.51 0.02 1 149 . 31 VAL C C 179.1 0.1 1 150 . 31 VAL CA C 65.9 0.1 1 151 . 31 VAL N N 119.1 0.1 1 152 . 32 LEU H H 7.19 0.02 1 153 . 32 LEU HA H 3.95 0.02 1 154 . 32 LEU C C 179.2 0.1 1 155 . 32 LEU CA C 58.1 0.1 1 156 . 32 LEU N N 118.7 0.1 1 157 . 33 THR H H 8.68 0.02 1 158 . 33 THR HA H 3.85 0.02 1 159 . 33 THR C C 177.0 0.1 1 160 . 33 THR CA C 66.0 0.1 1 161 . 33 THR N N 116.1 0.1 1 162 . 34 ARG H H 8.42 0.02 1 163 . 34 ARG HA H 4.02 0.02 1 164 . 34 ARG CA C 59.6 0.1 1 165 . 34 ARG N N 122.6 0.1 1 166 . 37 SER H H 8.37 0.02 1 167 . 37 SER HA H 4.09 0.02 1 168 . 37 SER C C 176.4 0.1 1 169 . 37 SER CA C 61.5 0.1 1 170 . 37 SER N N 114.6 0.1 1 171 . 38 PHE H H 7.90 0.02 1 172 . 38 PHE HA H 3.76 0.02 1 173 . 38 PHE C C 176.4 0.1 1 174 . 38 PHE CA C 60.7 0.1 1 175 . 38 PHE N N 123.6 0.1 1 176 . 39 LYS H H 8.05 0.02 1 177 . 39 LYS HA H 3.21 0.02 1 178 . 39 LYS C C 179.4 0.1 1 179 . 39 LYS CA C 57.4 0.1 1 180 . 39 LYS N N 117.9 0.1 1 181 . 40 GLU H H 7.73 0.02 1 182 . 40 GLU HA H 3.86 0.02 1 183 . 40 GLU C C 178.2 0.1 1 184 . 40 GLU CA C 58.4 0.1 1 185 . 40 GLU N N 118.3 0.1 1 186 . 41 ARG H H 7.59 0.02 1 187 . 41 ARG HA H 3.99 0.02 1 188 . 41 ARG C C 178.8 0.1 1 189 . 41 ARG CA C 58.4 0.1 1 190 . 41 ARG N N 119.5 0.1 1 191 . 42 VAL H H 7.70 0.02 1 192 . 42 VAL HA H 3.57 0.02 1 193 . 42 VAL C C 177.8 0.1 1 194 . 42 VAL CA C 64.1 0.1 1 195 . 42 VAL N N 117.5 0.1 1 196 . 43 ALA H H 7.55 0.02 1 197 . 43 ALA HA H 3.99 0.02 1 198 . 43 ALA C C 179.0 0.1 1 199 . 43 ALA CA C 53.7 0.1 1 200 . 43 ALA N N 123.3 0.1 1 201 . 44 GLU H H 7.79 0.02 1 202 . 44 GLU HA H 3.99 0.02 1 203 . 44 GLU C C 177.2 0.1 1 204 . 44 GLU CA C 57.2 0.1 1 205 . 44 GLU N N 117.9 0.1 1 206 . 45 ARG H H 7.76 0.02 1 207 . 45 ARG HA H 4.12 0.02 1 208 . 45 ARG C C 177.2 0.1 1 209 . 45 ARG CA C 56.7 0.1 1 210 . 45 ARG N N 119.3 0.1 1 211 . 46 GLY H H 7.92 0.02 1 212 . 46 GLY HA2 H 3.81 0.02 1 213 . 46 GLY C C 173.8 0.1 1 214 . 46 GLY CA C 45.3 0.1 1 215 . 46 GLY N N 107.2 0.1 1 216 . 47 GLN H H 8.22 0.02 1 217 . 47 GLN HA H 4.21 0.02 1 218 . 47 GLN C C 175.7 0.1 1 219 . 47 GLN CA C 55.6 0.1 1 220 . 47 GLN N N 119.5 0.1 1 221 . 48 LYS H H 8.31 0.02 1 222 . 48 LYS HA H 4.26 0.02 1 223 . 48 LYS C C 176.4 0.1 1 224 . 48 LYS CA C 55.7 0.1 1 225 . 48 LYS N N 122.2 0.1 1 226 . 49 LEU H H 8.15 0.02 1 227 . 49 LEU HA H 4.18 0.02 1 228 . 49 LEU C C 177.1 0.1 1 229 . 49 LEU CA C 55.2 0.1 1 230 . 49 LEU N N 122.6 0.1 1 231 . 50 GLU H H 8.40 0.02 1 232 . 50 GLU HA H 4.12 0.02 1 233 . 50 GLU C C 176.8 0.1 1 234 . 50 GLU CA C 56.1 0.1 1 235 . 50 GLU N N 119.7 0.1 1 236 . 51 ASP H H 8.10 0.02 1 237 . 51 ASP HA H 4.53 0.02 1 238 . 51 ASP C C 176.4 0.1 1 239 . 51 ASP CA C 54.4 0.1 1 240 . 51 ASP N N 122.1 0.1 1 241 . 52 SER H H 8.24 0.02 1 242 . 52 SER HA H 4.40 0.02 1 243 . 52 SER C C 174.4 0.1 1 244 . 52 SER CA C 57.7 0.1 1 245 . 52 SER N N 116.3 0.1 1 246 . 53 TYR H H 8.87 0.02 1 247 . 53 TYR HA H 4.05 0.02 1 248 . 53 TYR C C 176.7 0.1 1 249 . 53 TYR CA C 61.8 0.1 1 250 . 53 TYR N N 123.4 0.1 1 251 . 54 HIS H H 8.08 0.02 1 252 . 54 HIS HA H 4.04 0.02 1 253 . 54 HIS C C 178.8 0.1 1 254 . 54 HIS CA C 59.9 0.1 1 255 . 54 HIS N N 113.4 0.1 1 256 . 55 LEU H H 7.88 0.02 1 257 . 55 LEU HA H 4.04 0.02 9 258 . 55 LEU C C 177.1 0.1 1 259 . 55 LEU CA C 57.3 0.1 1 260 . 55 LEU N N 121.6 0.1 1 261 . 56 GLN H H 8.29 0.02 1 262 . 56 GLN HA H 3.82 0.02 1 263 . 56 GLN C C 179.6 0.1 1 264 . 56 GLN CA C 59.2 0.1 1 265 . 56 GLN N N 118.9 0.1 1 266 . 57 VAL H H 7.93 0.02 1 267 . 57 VAL HA H 3.31 0.02 1 268 . 57 VAL C C 176.4 0.1 1 269 . 57 VAL CA C 66.3 0.1 1 270 . 57 VAL N N 118.8 0.1 1 271 . 58 PHE H H 7.68 0.02 1 272 . 58 PHE HA H 3.97 0.02 1 273 . 58 PHE C C 176.4 0.1 1 274 . 58 PHE CA C 61.4 0.1 1 275 . 58 PHE N N 119.7 0.1 1 276 . 59 LYS H H 8.42 0.02 1 277 . 59 LYS HA H 3.43 0.02 9 278 . 59 LYS C C 178.7 0.1 1 279 . 59 LYS CA C 60.0 0.1 1 280 . 59 LYS N N 116.2 0.1 1 281 . 60 ARG H H 7.73 0.02 1 282 . 60 ARG HA H 3.98 0.02 1 283 . 60 ARG C C 178.2 0.1 1 284 . 60 ARG CA C 58.7 0.1 1 285 . 60 ARG N N 120.0 0.1 1 286 . 61 ASP H H 8.46 0.02 1 287 . 61 ASP HA H 4.21 0.02 1 288 . 61 ASP C C 179.1 0.1 1 289 . 61 ASP CA C 57.2 0.1 1 290 . 61 ASP N N 120.7 0.1 1 291 . 62 ALA H H 8.59 0.02 1 292 . 62 ALA HA H 4.21 0.02 1 293 . 62 ALA C C 179.9 0.1 1 294 . 62 ALA CA C 54.7 0.1 1 295 . 62 ALA N N 122.7 0.1 1 296 . 63 ASP H H 8.27 0.02 1 297 . 63 ASP HA H 4.13 0.02 1 298 . 63 ASP C C 179.1 0.1 1 299 . 63 ASP CA C 57.1 0.1 1 300 . 63 ASP N N 119.6 0.1 1 301 . 64 ASP H H 8.52 0.02 1 302 . 64 ASP HA H 4.33 0.02 1 303 . 64 ASP C C 179.3 0.1 1 304 . 64 ASP CA C 57.4 0.1 1 305 . 64 ASP N N 119.8 0.1 1 306 . 65 LEU H H 8.06 0.02 1 307 . 65 LEU HA H 4.28 0.02 1 308 . 65 LEU C C 178.7 0.1 1 309 . 65 LEU CA C 57.8 0.1 1 310 . 65 LEU N N 121.7 0.1 1 311 . 66 GLY H H 8.41 0.02 1 312 . 66 GLY HA2 H 4.20 0.02 1 313 . 66 GLY C C 175.1 0.1 1 314 . 66 GLY CA C 47.5 0.1 1 315 . 66 GLY N N 106.0 0.1 1 316 . 67 LYS H H 8.17 0.02 1 317 . 67 LYS HA H 3.91 0.02 9 318 . 67 LYS C C 178.9 0.1 1 319 . 67 LYS CA C 59.7 0.1 1 320 . 67 LYS N N 119.9 0.1 1 321 . 68 TRP H H 7.96 0.02 1 322 . 68 TRP HA H 4.00 0.02 1 323 . 68 TRP C C 178.0 0.1 1 324 . 68 TRP CA C 62.1 0.1 1 325 . 68 TRP N N 120.9 0.1 1 326 . 69 ILE H H 8.92 0.02 1 327 . 69 ILE HA H 3.96 0.02 9 328 . 69 ILE C C 177.9 0.1 1 329 . 69 ILE CA C 65.8 0.1 1 330 . 69 ILE N N 117.5 0.1 1 331 . 70 MET H H 8.26 0.02 1 332 . 70 MET HA H 3.72 0.02 1 333 . 70 MET C C 178.0 0.1 1 334 . 70 MET CA C 58.8 0.1 1 335 . 70 MET N N 116.0 0.1 1 336 . 71 GLU H H 7.80 0.02 1 337 . 71 GLU HA H 3.81 0.02 1 338 . 71 GLU C C 179.1 0.1 1 339 . 71 GLU CA C 59.1 0.1 1 340 . 71 GLU N N 118.6 0.1 1 341 . 72 LYS H H 7.54 0.02 1 342 . 72 LYS HA H 3.59 0.02 1 343 . 72 LYS C C 178.6 0.1 1 344 . 72 LYS CA C 56.7 0.1 1 345 . 72 LYS N N 117.6 0.1 1 346 . 73 VAL H H 8.67 0.02 1 347 . 73 VAL HA H 3.68 0.02 1 348 . 73 VAL C C 178.2 0.1 1 349 . 73 VAL CA C 66.7 0.1 1 350 . 73 VAL N N 118.7 0.1 1 351 . 74 ASN H H 7.88 0.02 1 352 . 74 ASN HA H 4.13 0.02 1 353 . 74 ASN C C 177.1 0.1 1 354 . 74 ASN CA C 56.1 0.1 1 355 . 74 ASN N N 118.2 0.1 1 356 . 75 ILE H H 7.51 0.02 1 357 . 75 ILE HA H 3.69 0.02 5 358 . 75 ILE C C 178.3 0.1 1 359 . 75 ILE CA C 64.4 0.1 1 360 . 75 ILE N N 119.7 0.1 1 361 . 76 LEU H H 7.94 0.02 1 362 . 76 LEU HA H 3.58 0.02 9 363 . 76 LEU C C 177.6 0.1 1 364 . 76 LEU CA C 56.7 0.1 1 365 . 76 LEU N N 117.5 0.1 1 366 . 77 THR H H 7.52 0.02 1 367 . 77 THR HA H 4.12 0.02 1 368 . 77 THR C C 174.2 0.1 1 369 . 77 THR CA C 62.0 0.1 1 370 . 77 THR N N 106.5 0.1 1 371 . 78 ASP H H 7.22 0.02 1 372 . 78 ASP HA H 4.45 0.02 1 373 . 78 ASP C C 177.5 0.1 1 374 . 78 ASP CA C 54.4 0.1 1 375 . 78 ASP N N 122.9 0.1 1 376 . 79 LYS H H 8.65 0.02 1 377 . 79 LYS HA H 4.13 0.02 1 378 . 79 LYS C C 177.5 0.1 1 379 . 79 LYS CA C 57.7 0.1 1 380 . 79 LYS N N 125.6 0.1 1 381 . 80 SER H H 8.66 0.02 1 382 . 80 SER HA H 4.23 0.02 1 383 . 80 SER C C 175.0 0.1 1 384 . 80 SER CA C 59.4 0.1 1 385 . 80 SER N N 115.4 0.1 1 386 . 81 TYR H H 7.86 0.02 1 387 . 81 TYR HA H 4.07 0.02 1 388 . 81 TYR C C 176.0 0.1 1 389 . 81 TYR CA C 60.3 0.1 1 390 . 81 TYR N N 122.4 0.1 1 391 . 82 GLU H H 7.61 0.02 1 392 . 82 GLU HA H 4.12 0.02 1 393 . 82 GLU CA C 55.5 0.1 1 394 . 82 GLU N N 118.4 0.1 1 395 . 84 PRO HA H 4.27 0.02 1 396 . 84 PRO C C 177.3 0.1 1 397 . 84 PRO CA C 63.8 0.1 1 398 . 85 THR H H 8.24 0.02 1 399 . 85 THR HA H 4.15 0.02 1 400 . 85 THR C C 174.5 0.1 1 401 . 85 THR CA C 62.5 0.1 1 402 . 85 THR N N 110.8 0.1 1 403 . 86 ASN H H 7.81 0.02 1 404 . 86 ASN HA H 4.73 0.02 1 405 . 86 ASN C C 175.6 0.1 1 406 . 86 ASN CA C 52.4 0.1 1 407 . 86 ASN N N 119.8 0.1 1 408 . 87 ILE H H 8.09 0.02 1 409 . 87 ILE HA H 3.87 0.02 1 410 . 87 ILE C C 177.1 0.1 1 411 . 87 ILE CA C 62.8 0.1 1 412 . 87 ILE N N 121.5 0.1 1 413 . 88 GLN H H 8.35 0.02 1 414 . 88 GLN HA H 4.13 0.02 1 415 . 88 GLN C C 177.5 0.1 1 416 . 88 GLN CA C 57.2 0.1 1 417 . 88 GLN N N 120.3 0.1 1 418 . 89 GLY H H 8.04 0.02 1 419 . 89 GLY HA2 H 3.75 0.02 1 420 . 89 GLY C C 175.4 0.1 1 421 . 89 GLY CA C 45.8 0.1 1 422 . 89 GLY N N 108.1 0.1 1 423 . 90 LYS H H 7.92 0.02 1 424 . 90 LYS HA H 3.90 0.02 1 425 . 90 LYS C C 178.3 0.1 1 426 . 90 LYS CA C 58.8 0.1 1 427 . 90 LYS N N 120.5 0.1 1 428 . 91 TYR H H 8.21 0.02 1 429 . 91 TYR HA H 4.41 0.02 1 430 . 91 TYR C C 177.3 0.1 1 431 . 91 TYR CA C 60.5 0.1 1 432 . 91 TYR N N 119.5 0.1 1 433 . 92 GLN H H 8.17 0.02 1 434 . 92 GLN HA H 4.02 0.02 1 435 . 92 GLN C C 178.3 0.1 1 436 . 92 GLN CA C 58.0 0.1 1 437 . 92 GLN N N 119.8 0.1 1 438 . 93 LYS H H 8.11 0.02 1 439 . 93 LYS HA H 4.05 0.02 1 440 . 93 LYS C C 178.2 0.1 1 441 . 93 LYS CA C 58.5 0.1 1 442 . 93 LYS N N 119.9 0.1 1 443 . 94 HIS H H 8.09 0.02 1 444 . 94 HIS HA H 4.42 0.02 1 445 . 94 HIS C C 176.6 0.1 1 446 . 94 HIS CA C 59.3 0.1 1 447 . 94 HIS N N 120.1 0.1 1 448 . 95 GLN H H 8.26 0.02 1 449 . 95 GLN HA H 3.96 0.02 1 450 . 95 GLN C C 178.9 0.1 1 451 . 95 GLN CA C 58.1 0.1 1 452 . 95 GLN N N 118.2 0.1 1 453 . 96 SER H H 8.04 0.02 1 454 . 96 SER HA H 3.95 0.02 1 455 . 96 SER C C 176.1 0.1 1 456 . 96 SER CA C 60.7 0.1 1 457 . 96 SER N N 115.3 0.1 1 458 . 97 LEU H H 7.81 0.02 1 459 . 97 LEU HA H 4.20 0.02 1 460 . 97 LEU C C 178.1 0.1 1 461 . 97 LEU CA C 57.9 0.1 1 462 . 97 LEU N N 124.6 0.1 1 463 . 98 GLU H H 8.40 0.02 1 464 . 98 GLU HA H 3.63 0.02 1 465 . 98 GLU C C 179.1 0.1 1 466 . 98 GLU CA C 60.0 0.1 1 467 . 98 GLU N N 117.3 0.1 1 468 . 99 ALA H H 7.72 0.02 1 469 . 99 ALA HA H 4.11 0.02 1 470 . 99 ALA C C 180.5 0.1 1 471 . 99 ALA CA C 54.8 0.1 1 472 . 99 ALA N N 120.5 0.1 1 473 . 100 GLU H H 8.00 0.02 1 474 . 100 GLU HA H 4.04 0.02 1 475 . 100 GLU C C 179.3 0.1 1 476 . 100 GLU CA C 59.7 0.1 1 477 . 100 GLU N N 119.9 0.1 1 478 . 101 VAL H H 8.78 0.02 1 479 . 101 VAL HA H 3.65 0.02 1 480 . 101 VAL C C 178.3 0.1 1 481 . 101 VAL CA C 67.1 0.1 1 482 . 101 VAL N N 119.7 0.1 1 483 . 102 GLN H H 8.08 0.02 1 484 . 102 GLN HA H 4.04 0.02 1 485 . 102 GLN C C 179.6 0.1 1 486 . 102 GLN CA C 59.1 0.1 1 487 . 102 GLN N N 118.5 0.1 1 488 . 103 THR H H 7.94 0.02 1 489 . 103 THR HA H 3.80 0.02 1 490 . 103 THR C C 177.2 0.1 1 491 . 103 THR CA C 66.5 0.1 1 492 . 103 THR N N 116.7 0.1 1 493 . 104 LYS H H 8.17 0.02 1 494 . 104 LYS HA H 3.73 0.02 1 495 . 104 LYS C C 178.1 0.1 1 496 . 104 LYS CA C 56.7 0.1 1 497 . 104 LYS N N 120.7 0.1 1 498 . 105 SER H H 8.72 0.02 1 499 . 105 SER HA H 3.50 0.02 1 500 . 105 SER C C 176.9 0.1 1 501 . 105 SER CA C 61.2 0.1 1 502 . 105 SER N N 116.8 0.1 1 503 . 106 ARG H H 7.13 0.02 1 504 . 106 ARG HA H 3.99 0.02 1 505 . 106 ARG C C 178.3 0.1 1 506 . 106 ARG CA C 58.5 0.1 1 507 . 106 ARG N N 120.4 0.1 1 508 . 107 LEU H H 6.98 0.02 1 509 . 107 LEU HA H 3.96 0.02 1 510 . 107 LEU C C 178.9 0.1 1 511 . 107 LEU CA C 57.3 0.1 1 512 . 107 LEU N N 119.9 0.1 1 513 . 108 MET H H 7.55 0.02 1 514 . 108 MET HA H 4.10 0.02 1 515 . 108 MET C C 177.4 0.1 1 516 . 108 MET CA C 57.4 0.1 1 517 . 108 MET N N 118.9 0.1 1 518 . 109 SER H H 7.65 0.02 1 519 . 109 SER HA H 4.15 0.02 1 520 . 109 SER C C 177.1 0.1 1 521 . 109 SER CA C 61.4 0.1 1 522 . 109 SER N N 112.6 0.1 1 523 . 110 GLU H H 7.97 0.02 1 524 . 110 GLU HA H 3.94 0.02 1 525 . 110 GLU C C 176.0 0.1 1 526 . 110 GLU CA C 59.0 0.1 1 527 . 110 GLU N N 122.1 0.1 1 528 . 111 LEU H H 8.08 0.02 1 529 . 111 LEU HA H 4.08 0.02 1 530 . 111 LEU C C 179.3 0.1 1 531 . 111 LEU CA C 58.1 0.1 1 532 . 111 LEU N N 122.2 0.1 1 533 . 112 GLU H H 7.91 0.02 1 534 . 112 GLU C C 178.9 0.1 1 535 . 112 GLU CA C 59.8 0.1 1 536 . 112 GLU N N 118.1 0.1 1 537 . 113 LYS H H 7.97 0.02 1 538 . 113 LYS HA H 3.93 0.02 1 539 . 113 LYS C C 178.6 0.1 1 540 . 113 LYS CA C 58.9 0.1 1 541 . 113 LYS N N 119.9 0.1 1 542 . 114 THR H H 8.56 0.02 1 543 . 114 THR HA H 3.77 0.02 1 544 . 114 THR C C 176.0 0.1 1 545 . 114 THR CA C 66.4 0.1 1 546 . 114 THR N N 116.2 0.1 1 547 . 115 ARG H H 8.19 0.02 1 548 . 115 ARG HA H 4.01 0.02 9 549 . 115 ARG C C 179.2 0.1 1 550 . 115 ARG CA C 61.0 0.1 1 551 . 115 ARG N N 122.7 0.1 1 552 . 116 GLU H H 7.60 0.02 1 553 . 116 GLU HA H 3.69 0.02 1 554 . 116 GLU C C 177.6 0.1 1 555 . 116 GLU CA C 58.5 0.1 1 556 . 116 GLU N N 115.6 0.1 1 557 . 117 GLU H H 7.98 0.02 1 558 . 117 GLU HA H 4.20 0.02 1 559 . 117 GLU C C 177.7 0.1 1 560 . 117 GLU CA C 57.7 0.1 1 561 . 117 GLU N N 114.6 0.1 1 562 . 118 ARG H H 8.10 0.02 1 563 . 118 ARG HA H 3.99 0.02 1 564 . 118 ARG C C 176.3 0.1 1 565 . 118 ARG CA C 56.5 0.1 1 566 . 118 ARG N N 113.7 0.1 1 567 . 119 PHE H H 7.30 0.02 1 568 . 119 PHE HA H 4.72 0.02 1 569 . 119 PHE C C 175.9 0.1 1 570 . 119 PHE CA C 53.6 0.1 1 571 . 119 PHE N N 120.2 0.1 1 572 . 120 THR H H 7.42 0.02 1 573 . 120 THR HA H 4.11 0.02 1 574 . 120 THR C C 173.3 0.1 1 575 . 120 THR CA C 61.1 0.1 1 576 . 120 THR N N 113.2 0.1 1 577 . 121 MET H H 8.17 0.02 1 578 . 121 MET C C 176.2 0.1 1 579 . 121 MET CA C 57.8 0.1 1 580 . 121 MET N N 119.0 0.1 1 581 . 122 GLY H H 8.42 0.02 1 582 . 122 GLY HA2 H 3.52 0.02 1 583 . 122 GLY C C 174.2 0.1 1 584 . 122 GLY CA C 44.9 0.1 1 585 . 122 GLY N N 113.6 0.1 1 586 . 123 HIS H H 8.47 0.02 1 587 . 123 HIS HA H 4.34 0.02 1 588 . 123 HIS C C 178.2 0.1 1 589 . 123 HIS CA C 57.9 0.1 1 590 . 123 HIS N N 123.0 0.1 1 591 . 124 SER H H 8.79 0.02 1 592 . 124 SER CA C 61.7 0.1 1 593 . 124 SER N N 126.4 0.1 1 594 . 126 HIS H H 8.27 0.02 1 595 . 126 HIS HA H 3.85 0.02 9 596 . 126 HIS C C 175.4 0.1 1 597 . 126 HIS CA C 60.9 0.1 1 598 . 126 HIS N N 121.7 0.1 1 599 . 127 GLU H H 8.67 0.02 1 600 . 127 GLU HA H 3.62 0.02 1 601 . 127 GLU C C 179.8 0.1 1 602 . 127 GLU CA C 59.8 0.1 1 603 . 127 GLU N N 115.9 0.1 1 604 . 128 GLU H H 8.67 0.02 1 605 . 128 GLU HA H 4.10 0.02 1 606 . 128 GLU C C 179.2 0.1 1 607 . 128 GLU CA C 59.2 0.1 1 608 . 128 GLU N N 119.7 0.1 1 609 . 129 THR H H 7.81 0.02 1 610 . 129 THR HA H 3.92 0.02 1 611 . 129 THR C C 177.1 0.1 1 612 . 129 THR CA C 65.5 0.1 1 613 . 129 THR N N 109.9 0.1 1 614 . 130 LYS H H 7.79 0.02 1 615 . 130 LYS HA H 3.71 0.02 1 616 . 130 LYS C C 178.6 0.1 1 617 . 130 LYS CA C 59.9 0.1 1 618 . 130 LYS N N 123.4 0.1 1 619 . 131 ALA H H 7.79 0.02 1 620 . 131 ALA HA H 4.04 0.02 1 621 . 131 ALA C C 179.2 0.1 1 622 . 131 ALA CA C 54.7 0.1 1 623 . 131 ALA N N 120.2 0.1 1 624 . 132 HIS H H 7.83 0.02 1 625 . 132 HIS HA H 4.06 0.02 1 626 . 132 HIS C C 178.8 0.1 1 627 . 132 HIS CA C 59.7 0.1 1 628 . 132 HIS N N 116.0 0.1 1 629 . 133 ILE H H 7.90 0.02 1 630 . 133 ILE HA H 4.03 0.02 1 631 . 133 ILE C C 177.1 0.1 1 632 . 133 ILE CA C 62.0 0.1 1 633 . 133 ILE N N 117.1 0.1 1 634 . 134 GLU H H 8.01 0.02 1 635 . 134 GLU HA H 3.69 0.02 1 636 . 134 GLU C C 179.1 0.1 1 637 . 134 GLU CA C 59.3 0.1 1 638 . 134 GLU N N 119.4 0.1 1 639 . 135 GLU H H 7.96 0.02 1 640 . 135 GLU HA H 4.08 0.02 1 641 . 135 GLU C C 180.8 0.1 1 642 . 135 GLU CA C 58.0 0.1 1 643 . 135 GLU N N 115.9 0.1 1 644 . 136 LEU H H 8.32 0.02 1 645 . 136 LEU HA H 4.01 0.02 1 646 . 136 LEU C C 178.6 0.1 1 647 . 136 LEU CA C 58.0 0.1 1 648 . 136 LEU N N 120.5 0.1 1 649 . 137 ARG H H 8.66 0.02 1 650 . 137 ARG HA H 3.96 0.02 1 651 . 137 ARG C C 178.5 0.1 1 652 . 137 ARG CA C 58.8 0.1 1 653 . 137 ARG N N 118.7 0.1 1 654 . 138 HIS H H 7.43 0.02 1 655 . 138 HIS HA H 4.59 0.02 1 656 . 138 HIS C C 177.9 0.1 1 657 . 138 HIS CA C 58.2 0.1 1 658 . 138 HIS N N 114.6 0.1 1 659 . 139 LEU H H 7.41 0.02 1 660 . 139 LEU HA H 3.84 0.02 1 661 . 139 LEU C C 177.9 0.1 1 662 . 139 LEU CA C 57.6 0.1 1 663 . 139 LEU N N 119.6 0.1 1 664 . 140 TRP H H 9.04 0.02 1 665 . 140 TRP HA H 3.99 0.02 1 666 . 140 TRP C C 177.0 0.1 1 667 . 140 TRP CA C 60.3 0.1 1 668 . 140 TRP N N 120.9 0.1 1 669 . 141 ASP H H 8.44 0.02 1 670 . 141 ASP HA H 4.23 0.02 1 671 . 141 ASP C C 179.6 0.1 1 672 . 141 ASP CA C 57.2 0.1 1 673 . 141 ASP N N 116.2 0.1 1 674 . 142 LEU H H 7.23 0.02 1 675 . 142 LEU HA H 4.21 0.02 1 676 . 142 LEU C C 177.2 0.1 1 677 . 142 LEU CA C 57.4 0.1 1 678 . 142 LEU N N 121.5 0.1 1 679 . 143 LEU H H 7.82 0.02 1 680 . 143 LEU HA H 3.60 0.02 9 681 . 143 LEU C C 179.4 0.1 1 682 . 143 LEU CA C 58.0 0.1 1 683 . 143 LEU N N 120.2 0.1 1 684 . 144 LEU H H 8.38 0.02 1 685 . 144 LEU HA H 3.69 0.02 1 686 . 144 LEU C C 179.1 0.1 1 687 . 144 LEU CA C 57.7 0.1 1 688 . 144 LEU N N 119.7 0.1 1 689 . 145 GLU H H 7.75 0.02 1 690 . 145 GLU HA H 3.88 0.02 1 691 . 145 GLU C C 179.4 0.1 1 692 . 145 GLU CA C 59.2 0.1 1 693 . 145 GLU N N 120.6 0.1 1 694 . 146 LEU H H 8.23 0.02 1 695 . 146 LEU HA H 3.85 0.02 1 696 . 146 LEU C C 178.9 0.1 1 697 . 146 LEU CA C 60.0 0.1 1 698 . 146 LEU N N 118.8 0.1 1 699 . 147 THR H H 8.37 0.02 1 700 . 147 THR HA H 3.63 0.02 1 701 . 147 THR C C 176.8 0.1 1 702 . 147 THR CA C 66.9 0.1 1 703 . 147 THR N N 115.2 0.1 1 704 . 148 LEU H H 7.90 0.02 1 705 . 148 LEU HA H 4.09 0.02 1 706 . 148 LEU C C 178.9 0.1 1 707 . 148 LEU CA C 57.2 0.1 1 708 . 148 LEU N N 122.3 0.1 1 709 . 149 GLU H H 7.67 0.02 1 710 . 149 GLU HA H 3.96 0.02 1 711 . 149 GLU C C 178.4 0.1 1 712 . 149 GLU CA C 58.7 0.1 1 713 . 149 GLU N N 119.1 0.1 1 714 . 150 LYS H H 7.97 0.02 1 715 . 150 LYS HA H 3.82 0.02 1 716 . 150 LYS C C 178.8 0.1 1 717 . 150 LYS CA C 56.5 0.1 1 718 . 150 LYS N N 116.7 0.1 1 719 . 151 GLY H H 7.87 0.02 1 720 . 151 GLY HA2 H 4.08 0.02 1 721 . 151 GLY C C 175.5 0.1 1 722 . 151 GLY CA C 46.0 0.1 1 723 . 151 GLY N N 107.2 0.1 1 724 . 152 ASP H H 8.04 0.02 1 725 . 152 ASP HA H 4.38 0.02 1 726 . 152 ASP C C 177.8 0.1 1 727 . 152 ASP CA C 55.7 0.1 1 728 . 152 ASP N N 120.7 0.1 1 729 . 153 GLN H H 7.80 0.02 1 730 . 153 GLN HA H 4.00 0.02 1 731 . 153 GLN C C 176.8 0.1 1 732 . 153 GLN CA C 56.5 0.1 1 733 . 153 GLN N N 117.4 0.1 1 734 . 154 LEU H H 7.56 0.02 1 735 . 154 LEU HA H 4.08 0.02 1 736 . 154 LEU C C 177.0 0.1 1 737 . 154 LEU CA C 55.6 0.1 1 738 . 154 LEU N N 119.0 0.1 1 739 . 155 LEU H H 7.61 0.02 1 740 . 155 LEU HA H 4.24 0.02 1 741 . 155 LEU C C 176.2 0.1 1 742 . 155 LEU CA C 54.8 0.1 1 743 . 155 LEU N N 119.3 0.1 1 744 . 156 ARG H H 7.51 0.02 1 745 . 156 ARG HA H 4.02 0.02 1 746 . 156 ARG C C 175.6 0.1 1 747 . 156 ARG CA C 57.2 0.1 1 748 . 156 ARG N N 125.5 0.1 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants_set_1 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions _Spectrometer_frequency_1H 600 _Mol_system_component_name spectrin _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 2 GLU H 2 GLU HA 6.6 . . 1.5 2 3JHNHA 3 GLN H 3 GLN HA 6.3 . . 1.5 3 3JHNHA 4 PHE H 4 PHE HA 6.3 . . 1.5 4 3JHNHA 6 LYS H 6 LYS HA 6.3 . . 1.5 5 3JHNHA 8 THR H 8 THR HA 6.6 . . 1.5 6 3JHNHA 9 VAL H 9 VAL HA 7.6 . . 1.5 7 3JHNHA 10 VAL H 10 VAL HA 6.5 . . 1.5 8 3JHNHA 11 GLU H 11 GLU HA 6.5 . . 1.5 9 3JHNHA 12 SER H 12 SER HA 6.6 . . 1.5 10 3JHNHA 13 SER H 13 SER HA 6.3 . . 1.5 11 3JHNHA 16 LYS H 16 LYS HA 6.4 . . 1.5 12 3JHNHA 17 VAL H 17 VAL HA 6.1 . . 1.5 13 3JHNHA 18 LEU H 18 LEU HA 6.1 . . 1.5 14 3JHNHA 35 TYR H 35 TYR HA 2.8 . . 1.5 15 3JHNHA 23 GLU H 23 GLU HA 2.8 . . 1.5 16 3JHNHA 25 GLN H 25 GLN HA 3.5 . . 1.5 17 3JHNHA 29 GLN H 29 GLN HA 3.6 . . 1.5 18 3JHNHA 31 VAL H 31 VAL HA 2.7 . . 1.5 19 3JHNHA 32 LEU H 32 LEU HA 3.7 . . 1.5 20 3JHNHA 37 SER H 37 SER HA 4.9 . . 1.5 21 3JHNHA 40 GLU H 40 GLU HA 3.7 . . 1.5 22 3JHNHA 43 ALA H 43 ALA HA 3.9 . . 1.5 23 3JHNHA 44 GLU H 44 GLU HA 2.5 . . 1.5 24 3JHNHA 45 ARG H 45 ARG HA 2.9 . . 1.5 25 3JHNHA 47 GLN H 47 GLN HA 6.1 . . 1.5 26 3JHNHA 48 LYS H 48 LYS HA 7.2 . . 1.5 27 3JHNHA 49 LEU H 49 LEU HA 6.5 . . 1.5 28 3JHNHA 50 GLU H 50 GLU HA 5.0 . . 1.5 29 3JHNHA 51 ASP H 51 ASP HA 7.5 . . 1.5 30 3JHNHA 52 SER H 52 SER HA 4.2 . . 1.5 31 3JHNHA 54 HIS H 54 HIS HA 3.9 . . 1.5 32 3JHNHA 57 VAL H 57 VAL HA 3.5 . . 1.5 33 3JHNHA 59 LYS H 59 LYS HA 4.6 . . 1.5 34 3JHNHA 60 ARG H 60 ARG HA 4.6 . . 1.5 35 3JHNHA 61 ASP H 61 ASP HA 4.4 . . 1.5 36 3JHNHA 62 ALA H 62 ALA HA 3.3 . . 1.5 37 3JHNHA 64 ASP H 64 ASP HA 4.0 . . 1.5 38 3JHNHA 65 LEU H 65 LEU HA 4.1 . . 1.5 39 3JHNHA 67 LYS H 67 LYS HA 3.0 . . 1.5 40 3JHNHA 68 TRP H 68 TRP HA 3.2 . . 1.5 41 3JHNHA 70 MET H 70 MET HA 4.3 . . 1.5 42 3JHNHA 71 GLU H 71 GLU HA 4.9 . . 1.5 43 3JHNHA 72 LYS H 72 LYS HA 3.3 . . 1.5 44 3JHNHA 74 ASN H 74 ASN HA 4.4 . . 1.5 45 3JHNHA 75 ILE H 75 ILE HA 3.8 . . 1.5 46 3JHNHA 77 THR H 77 THR HA 3.2 . . 1.5 47 3JHNHA 78 ASP H 78 ASP HA 2.9 . . 1.5 48 3JHNHA 79 LYS H 79 LYS HA 4.1 . . 1.5 49 3JHNHA 80 SER H 80 SER HA 2.9 . . 1.5 50 3JHNHA 81 TYR H 81 TYR HA 2.7 . . 1.5 51 3JHNHA 85 THR H 85 THR HA 7.4 . . 1.5 52 3JHNHA 86 ASN H 86 ASN HA 7.1 . . 1.5 53 3JHNHA 87 ILE H 87 ILE HA 6.6 . . 1.5 54 3JHNHA 88 GLN H 88 GLN HA 4.0 . . 1.5 55 3JHNHA 89 GLY H 89 GLY HA 6.4 . . 1.5 56 3JHNHA 90 LYS H 90 LYS HA 4.3 . . 1.5 57 3JHNHA 91 TYR H 91 TYR HA 4.2 . . 1.5 58 3JHNHA 93 LYS H 93 LYS HA 3.0 . . 1.5 59 3JHNHA 95 GLN H 95 GLN HA 3.8 . . 1.5 60 3JHNHA 96 SER H 96 SER HA 3.0 . . 1.5 61 3JHNHA 98 GLU H 98 GLU HA 3.6 . . 1.5 62 3JHNHA 99 ALA H 99 ALA HA 4.2 . . 1.5 63 3JHNHA 101 VAL H 101 VAL HA 3.1 . . 1.5 64 3JHNHA 102 GLN H 102 GLN HA 4.4 . . 1.5 65 3JHNHA 104 LYS H 104 LYS HA 3.6 . . 1.5 66 3JHNHA 105 SER H 105 SER HA 3.0 . . 1.5 67 3JHNHA 107 LEU H 107 LEU HA 2.8 . . 1.5 68 3JHNHA 108 MET H 108 MET HA 4.8 . . 1.5 69 3JHNHA 109 SER H 109 SER HA 3.2 . . 1.5 70 3JHNHA 111 LEU H 111 LEU HA 3.8 . . 1.5 71 3JHNHA 113 LYS H 113 LYS HA 3.0 . . 1.5 72 3JHNHA 114 THR H 114 THR HA 3.8 . . 1.5 73 3JHNHA 115 ARG H 115 ARG HA 2.9 . . 1.5 74 3JHNHA 117 GLU H 117 GLU HA 3.5 . . 1.5 75 3JHNHA 119 PHE H 119 PHE HA 7.4 . . 1.5 76 3JHNHA 120 THR H 120 THR HA 6.9 . . 1.5 77 3JHNHA 121 MET H 121 MET HA 7.7 . . 1.5 78 3JHNHA 123 HIS H 123 HIS HA 5.4 . . 1.5 79 3JHNHA 126 HIS H 126 HIS HA 4.7 . . 1.5 80 3JHNHA 127 GLU H 127 GLU HA 4.1 . . 1.5 81 3JHNHA 130 LYS H 130 LYS HA 2.5 . . 1.5 82 3JHNHA 132 HIS H 132 HIS HA 3.2 . . 1.5 83 3JHNHA 134 GLU H 134 GLU HA 4.2 . . 1.5 84 3JHNHA 137 ARG H 137 ARG HA 4.2 . . 1.5 85 3JHNHA 138 HIS H 138 HIS HA 5.1 . . 1.5 86 3JHNHA 141 ASP H 141 ASP HA 3.8 . . 1.5 87 3JHNHA 142 LEU H 142 LEU HA 3.8 . . 1.5 88 3JHNHA 145 GLU H 145 GLU HA 3.1 . . 1.5 89 3JHNHA 146 LEU H 146 LEU HA 3.1 . . 1.5 90 3JHNHA 148 LEU H 148 LEU HA 3.4 . . 1.5 91 3JHNHA 149 GLU H 149 GLU HA 3.2 . . 1.5 92 3JHNHA 152 ASP H 152 ASP HA 4.0 . . 1.5 93 3JHNHA 153 GLN H 153 GLN HA 4.5 . . 1.5 94 3JHNHA 154 LEU H 154 LEU HA 4.0 . . 1.5 95 3JHNHA 155 LEU H 155 LEU HA 5.1 . . 1.5 96 3JHNHA 156 ARG H 156 ARG HA 8.0 . . 1.5 stop_ save_