data_4393 #Corrected using PDB structure: 1OWAA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 37 S HA 4.12 4.88 #114 T HA 3.80 4.52 #122 G HA 3.55 4.26 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted #124 S N 127.09 115.48 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.03 0.39 N/A 0.21 0.69 0.11 # #bmr4393.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4393.str file): #HA CA CB CO N HN #N/A +0.39 N/A +0.21 +0.69 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.02 +/-0.14 N/A +/-0.10 +/-0.33 +/-0.05 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.537 0.957 N/A 0.849 0.692 0.214 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.150 0.853 N/A 0.631 1.984 0.328 # ####################### # 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. ; 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_ _BMRB_accession_number 4393 _BMRB_flat_file_name bmr4393.str _Entry_type new _Submission_date 1999-09-08 _Accession_date 1999-09-09 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR 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 2003-06-05 update author "addition of coupling constants" 2000-12-07 original author "original release" 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 _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 _Page_first 345 _Page_last 346 _Year 1999 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_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state "not present" save_ ######################## # Monomeric polymers # ######################## save_spectrin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common spectrin _Abbreviation_common Sp ############################## # 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 2004-07-29 _Sequence_homology_query_revised_last_date 2004-05-28 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 "A Chain A, Solution Structural Studies OnHuman Erythrocyte Alpha Spectrin N TerminalTetramerization Domain" 100.00 156 100 100 2e-84 GenBank AAA60577.1 "erythroid alpha spectrin" 6.42 2429 100 100 2e-84 GenBank AAA60994.1 alpha-spectrin 6.42 2429 100 100 2e-84 PIR SJHUA "spectrin alpha chain - human" 6.42 2429 100 100 2e-84 REF NP_003117.1 "spectrin, alpha, erythrocytic 1(elliptocytosis 2); Spectrin, alpha, erythrocytic-1[Homo sapiens]" 6.42 2429 100 100 2e-84 SWISS-PROT P02549 "SPCA_HUMAN Spectrin alpha chain, erythrocyte(Erythroid alpha-spectrin)" 6.45 2418 100 100 2e-84 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 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 save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 na temperature 293 0.2 K 'ionic strength' 0.18 0.01 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference 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 H 1 'methyl protons' ppm 0.00 external direct cylindrical na parallel_to_Bo . DSS C 13 'methyl protons' ppm 0.00 external indirect cylindrical na parallel_to_Bo 0.251449530 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 # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name spectrin loop_ _Atom_shift_assign_ID _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 176.71 0.1 1 4 1 MET CA C 55.89 0.1 1 5 1 MET N N 122.29 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 176.01 0.1 1 9 2 GLU CA C 56.79 0.1 1 10 2 GLU N N 122.09 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 175.21 0.1 1 14 3 GLN CA C 55.89 0.1 1 15 3 GLN N N 121.09 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 173.61 0.1 1 19 4 PHE CA C 55.59 0.1 1 20 4 PHE N N 121.39 0.1 1 21 5 PRO HA H 4.26 0.02 1 22 5 PRO C C 176.91 0.1 1 23 5 PRO CA C 63.19 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 176.61 0.1 1 27 6 LYS CA C 56.59 0.1 1 28 6 LYS N N 121.99 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 176.51 0.1 1 32 7 GLU CA C 56.59 0.1 1 33 7 GLU N N 122.49 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 174.21 0.1 1 37 8 THR CA C 62.39 0.1 1 38 8 THR N N 117.09 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 175.91 0.1 1 42 9 VAL CA C 62.39 0.1 1 43 9 VAL N N 124.29 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 176.11 0.1 1 47 10 VAL CA C 62.29 0.1 1 48 10 VAL N N 125.29 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 176.41 0.1 1 52 11 GLU CA C 56.59 0.1 1 53 11 GLU N N 125.79 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 174.61 0.1 1 57 12 SER CA C 58.49 0.1 1 58 12 SER N N 117.69 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 174.61 0.1 1 62 13 SER CA C 58.49 0.1 1 63 13 SER N N 118.19 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 171.41 0.1 1 67 14 GLY CA C 44.89 0.1 1 68 14 GLY N N 110.69 0.1 1 69 15 PRO HA H 4.25 0.02 1 70 15 PRO C C 176.81 0.1 1 71 15 PRO CA C 63.09 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 176.51 0.1 1 75 16 LYS CA C 56.29 0.1 1 76 16 LYS N N 122.19 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 175.81 0.1 1 80 17 VAL CA C 62.39 0.1 1 81 17 VAL N N 123.09 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 177.01 0.1 1 85 18 LEU CA C 55.09 0.1 1 86 18 LEU N N 126.69 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 176.91 0.1 1 90 19 GLU CA C 55.99 0.1 1 91 19 GLU N N 122.69 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 175.01 0.1 1 95 20 THR CA C 61.19 0.1 1 96 20 THR N N 114.69 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 180.61 0.1 1 100 21 ALA CA C 55.59 0.1 1 101 21 ALA N N 122.99 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 179.01 0.1 1 105 22 GLU CA C 60.09 0.1 1 106 22 GLU N N 117.89 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 179.91 0.1 1 110 23 GLU CA C 59.19 0.1 1 111 23 GLU N N 121.59 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 177.71 0.1 1 115 24 ILE CA C 65.79 0.1 1 116 24 ILE N N 121.89 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 178.71 0.1 1 120 25 GLN CA C 58.79 0.1 1 121 25 GLN N N 118.29 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 178.91 0.1 1 125 26 GLU CA C 59.49 0.1 1 126 26 GLU N N 119.09 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 179.71 0.1 1 130 27 ARG CA C 59.49 0.1 1 131 27 ARG N N 120.49 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 178.21 0.1 1 135 28 ARG CA C 60.39 0.1 1 136 28 ARG N N 119.29 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 178.71 0.1 1 140 29 GLN CA C 58.59 0.1 1 141 29 GLN N N 117.29 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 178.71 0.1 1 145 30 GLU CA C 59.29 0.1 1 146 30 GLU N N 120.19 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 179.31 0.1 1 150 31 VAL CA C 66.29 0.1 1 151 31 VAL N N 119.79 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 179.41 0.1 1 155 32 LEU CA C 58.49 0.1 1 156 32 LEU N N 119.39 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 177.21 0.1 1 160 33 THR CA C 66.39 0.1 1 161 33 THR N N 116.79 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 59.99 0.1 1 165 34 ARG N N 123.29 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 176.61 0.1 1 169 37 SER CA C 61.89 0.1 1 170 37 SER N N 115.29 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 176.61 0.1 1 174 38 PHE CA C 61.09 0.1 1 175 38 PHE N N 124.29 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 179.61 0.1 1 179 39 LYS CA C 57.79 0.1 1 180 39 LYS N N 118.59 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 178.41 0.1 1 184 40 GLU CA C 58.79 0.1 1 185 40 GLU N N 118.99 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 179.01 0.1 1 189 41 ARG CA C 58.79 0.1 1 190 41 ARG N N 120.19 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 178.01 0.1 1 194 42 VAL CA C 64.49 0.1 1 195 42 VAL N N 118.19 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 179.21 0.1 1 199 43 ALA CA C 54.09 0.1 1 200 43 ALA N N 123.99 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 177.41 0.1 1 204 44 GLU CA C 57.59 0.1 1 205 44 GLU N N 118.59 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 177.41 0.1 1 209 45 ARG CA C 57.09 0.1 1 210 45 ARG N N 119.99 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 174.01 0.1 1 214 46 GLY CA C 45.69 0.1 1 215 46 GLY N N 107.89 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 175.91 0.1 1 219 47 GLN CA C 55.99 0.1 1 220 47 GLN N N 120.19 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 176.61 0.1 1 224 48 LYS CA C 56.09 0.1 1 225 48 LYS N N 122.89 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 177.31 0.1 1 229 49 LEU CA C 55.59 0.1 1 230 49 LEU N N 123.29 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 177.01 0.1 1 234 50 GLU CA C 56.49 0.1 1 235 50 GLU N N 120.39 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 176.61 0.1 1 239 51 ASP CA C 54.79 0.1 1 240 51 ASP N N 122.79 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 174.61 0.1 1 244 52 SER CA C 58.09 0.1 1 245 52 SER N N 116.99 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 176.91 0.1 1 249 53 TYR CA C 62.19 0.1 1 250 53 TYR N N 124.09 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 179.01 0.1 1 254 54 HIS CA C 60.29 0.1 1 255 54 HIS N N 114.09 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 177.31 0.1 1 259 55 LEU CA C 57.69 0.1 1 260 55 LEU N N 122.29 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 179.81 0.1 1 264 56 GLN CA C 59.59 0.1 1 265 56 GLN N N 119.59 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 176.61 0.1 1 269 57 VAL CA C 66.69 0.1 1 270 57 VAL N N 119.49 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 176.61 0.1 1 274 58 PHE CA C 61.79 0.1 1 275 58 PHE N N 120.39 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 178.91 0.1 1 279 59 LYS CA C 60.39 0.1 1 280 59 LYS N N 116.89 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 178.41 0.1 1 284 60 ARG CA C 59.09 0.1 1 285 60 ARG N N 120.69 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 179.31 0.1 1 289 61 ASP CA C 57.59 0.1 1 290 61 ASP N N 121.39 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 180.11 0.1 1 294 62 ALA CA C 55.09 0.1 1 295 62 ALA N N 123.39 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 179.31 0.1 1 299 63 ASP CA C 57.49 0.1 1 300 63 ASP N N 120.29 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 179.51 0.1 1 304 64 ASP CA C 57.79 0.1 1 305 64 ASP N N 120.49 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 178.91 0.1 1 309 65 LEU CA C 58.19 0.1 1 310 65 LEU N N 122.39 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 175.31 0.1 1 314 66 GLY CA C 47.89 0.1 1 315 66 GLY N N 106.69 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 179.11 0.1 1 319 67 LYS CA C 60.09 0.1 1 320 67 LYS N N 120.59 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 178.21 0.1 1 324 68 TRP CA C 62.49 0.1 1 325 68 TRP N N 121.59 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 178.11 0.1 1 329 69 ILE CA C 66.19 0.1 1 330 69 ILE N N 118.19 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 178.21 0.1 1 334 70 MET CA C 59.19 0.1 1 335 70 MET N N 116.69 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 179.31 0.1 1 339 71 GLU CA C 59.49 0.1 1 340 71 GLU N N 119.29 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 178.81 0.1 1 344 72 LYS CA C 57.09 0.1 1 345 72 LYS N N 118.29 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 178.41 0.1 1 349 73 VAL CA C 67.09 0.1 1 350 73 VAL N N 119.39 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 177.31 0.1 1 354 74 ASN CA C 56.49 0.1 1 355 74 ASN N N 118.89 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 178.51 0.1 1 359 75 ILE CA C 64.79 0.1 1 360 75 ILE N N 120.39 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 177.81 0.1 1 364 76 LEU CA C 57.09 0.1 1 365 76 LEU N N 118.19 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 174.41 0.1 1 369 77 THR CA C 62.39 0.1 1 370 77 THR N N 107.19 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 177.71 0.1 1 374 78 ASP CA C 54.79 0.1 1 375 78 ASP N N 123.59 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 177.71 0.1 1 379 79 LYS CA C 58.09 0.1 1 380 79 LYS N N 126.29 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 175.21 0.1 1 384 80 SER CA C 59.79 0.1 1 385 80 SER N N 116.09 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 176.21 0.1 1 389 81 TYR CA C 60.69 0.1 1 390 81 TYR N N 123.09 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 55.89 0.1 1 394 82 GLU N N 119.09 0.1 1 395 84 PRO HA H 4.27 0.02 1 396 84 PRO C C 177.51 0.1 1 397 84 PRO CA C 64.19 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 174.71 0.1 1 401 85 THR CA C 62.89 0.1 1 402 85 THR N N 111.49 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 175.81 0.1 1 406 86 ASN CA C 52.79 0.1 1 407 86 ASN N N 120.49 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 177.31 0.1 1 411 87 ILE CA C 63.19 0.1 1 412 87 ILE N N 122.19 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 177.71 0.1 1 416 88 GLN CA C 57.59 0.1 1 417 88 GLN N N 120.99 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 175.61 0.1 1 421 89 GLY CA C 46.19 0.1 1 422 89 GLY N N 108.79 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 178.51 0.1 1 426 90 LYS CA C 59.19 0.1 1 427 90 LYS N N 121.19 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 177.51 0.1 1 431 91 TYR CA C 60.89 0.1 1 432 91 TYR N N 120.19 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 178.51 0.1 1 436 92 GLN CA C 58.39 0.1 1 437 92 GLN N N 120.49 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 178.41 0.1 1 441 93 LYS CA C 58.89 0.1 1 442 93 LYS N N 120.59 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 176.81 0.1 1 446 94 HIS CA C 59.69 0.1 1 447 94 HIS N N 120.79 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 179.11 0.1 1 451 95 GLN CA C 58.49 0.1 1 452 95 GLN N N 118.89 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 176.31 0.1 1 456 96 SER CA C 61.09 0.1 1 457 96 SER N N 115.99 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 178.31 0.1 1 461 97 LEU CA C 58.29 0.1 1 462 97 LEU N N 125.29 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 179.31 0.1 1 466 98 GLU CA C 60.39 0.1 1 467 98 GLU N N 117.99 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 180.71 0.1 1 471 99 ALA CA C 55.19 0.1 1 472 99 ALA N N 121.19 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 179.51 0.1 1 476 100 GLU CA C 60.09 0.1 1 477 100 GLU N N 120.59 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 178.51 0.1 1 481 101 VAL CA C 67.49 0.1 1 482 101 VAL N N 120.39 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 179.81 0.1 1 486 102 GLN CA C 59.49 0.1 1 487 102 GLN N N 119.19 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 177.41 0.1 1 491 103 THR CA C 66.89 0.1 1 492 103 THR N N 117.39 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 178.31 0.1 1 496 104 LYS CA C 57.09 0.1 1 497 104 LYS N N 121.39 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 177.11 0.1 1 501 105 SER CA C 61.59 0.1 1 502 105 SER N N 117.49 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 178.51 0.1 1 506 106 ARG CA C 58.89 0.1 1 507 106 ARG N N 121.09 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 179.11 0.1 1 511 107 LEU CA C 57.69 0.1 1 512 107 LEU N N 120.59 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 177.61 0.1 1 516 108 MET CA C 57.79 0.1 1 517 108 MET N N 119.59 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 177.31 0.1 1 521 109 SER CA C 61.79 0.1 1 522 109 SER N N 113.29 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 176.21 0.1 1 526 110 GLU CA C 59.39 0.1 1 527 110 GLU N N 122.79 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 179.51 0.1 1 531 111 LEU CA C 58.49 0.1 1 532 111 LEU N N 122.89 0.1 1 533 112 GLU H H 7.91 0.02 1 534 112 GLU C C 179.11 0.1 1 535 112 GLU CA C 60.19 0.1 1 536 112 GLU N N 118.79 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 178.81 0.1 1 540 113 LYS CA C 59.29 0.1 1 541 113 LYS N N 120.59 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 176.21 0.1 1 545 114 THR CA C 66.79 0.1 1 546 114 THR N N 116.89 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 179.41 0.1 1 550 115 ARG CA C 61.39 0.1 1 551 115 ARG N N 123.39 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 177.81 0.1 1 555 116 GLU CA C 58.89 0.1 1 556 116 GLU N N 116.29 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 177.91 0.1 1 560 117 GLU CA C 58.09 0.1 1 561 117 GLU N N 115.29 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 176.51 0.1 1 565 118 ARG CA C 56.89 0.1 1 566 118 ARG N N 114.39 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 176.11 0.1 1 570 119 PHE CA C 53.99 0.1 1 571 119 PHE N N 120.89 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 173.51 0.1 1 575 120 THR CA C 61.49 0.1 1 576 120 THR N N 113.89 0.1 1 577 121 MET H H 8.17 0.02 1 578 121 MET C C 176.41 0.1 1 579 121 MET CA C 58.19 0.1 1 580 121 MET N N 119.69 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 174.41 0.1 1 584 122 GLY CA C 45.29 0.1 1 585 122 GLY N N 114.29 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 178.41 0.1 1 589 123 HIS CA C 58.29 0.1 1 590 123 HIS N N 123.69 0.1 1 591 124 SER H H 8.79 0.02 1 592 124 SER CA C 62.09 0.1 1 593 124 SER N N 127.09 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 175.61 0.1 1 597 126 HIS CA C 61.29 0.1 1 598 126 HIS N N 122.39 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 180.01 0.1 1 602 127 GLU CA C 60.19 0.1 1 603 127 GLU N N 116.59 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 179.41 0.1 1 607 128 GLU CA C 59.59 0.1 1 608 128 GLU N N 120.39 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 177.31 0.1 1 612 129 THR CA C 65.89 0.1 1 613 129 THR N N 110.59 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 178.81 0.1 1 617 130 LYS CA C 60.29 0.1 1 618 130 LYS N N 124.09 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 179.41 0.1 1 622 131 ALA CA C 55.09 0.1 1 623 131 ALA N N 120.89 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 179.01 0.1 1 627 132 HIS CA C 60.09 0.1 1 628 132 HIS N N 116.69 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 177.31 0.1 1 632 133 ILE CA C 62.39 0.1 1 633 133 ILE N N 117.79 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 179.31 0.1 1 637 134 GLU CA C 59.69 0.1 1 638 134 GLU N N 120.09 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 181.01 0.1 1 642 135 GLU CA C 58.39 0.1 1 643 135 GLU N N 116.59 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 178.81 0.1 1 647 136 LEU CA C 58.39 0.1 1 648 136 LEU N N 121.19 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 178.71 0.1 1 652 137 ARG CA C 59.19 0.1 1 653 137 ARG N N 119.39 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 178.11 0.1 1 657 138 HIS CA C 58.59 0.1 1 658 138 HIS N N 115.29 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 178.11 0.1 1 662 139 LEU CA C 57.99 0.1 1 663 139 LEU N N 120.29 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 177.21 0.1 1 667 140 TRP CA C 60.69 0.1 1 668 140 TRP N N 121.59 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 179.81 0.1 1 672 141 ASP CA C 57.59 0.1 1 673 141 ASP N N 116.89 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 177.41 0.1 1 677 142 LEU CA C 57.79 0.1 1 678 142 LEU N N 122.19 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 179.61 0.1 1 682 143 LEU CA C 58.39 0.1 1 683 143 LEU N N 120.89 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 179.31 0.1 1 687 144 LEU CA C 58.09 0.1 1 688 144 LEU N N 120.39 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 179.61 0.1 1 692 145 GLU CA C 59.59 0.1 1 693 145 GLU N N 121.29 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 179.11 0.1 1 697 146 LEU CA C 60.39 0.1 1 698 146 LEU N N 119.49 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 177.01 0.1 1 702 147 THR CA C 67.29 0.1 1 703 147 THR N N 115.89 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 179.11 0.1 1 707 148 LEU CA C 57.59 0.1 1 708 148 LEU N N 122.99 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 178.61 0.1 1 712 149 GLU CA C 59.09 0.1 1 713 149 GLU N N 119.79 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 179.01 0.1 1 717 150 LYS CA C 56.89 0.1 1 718 150 LYS N N 117.39 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 175.71 0.1 1 722 151 GLY CA C 46.39 0.1 1 723 151 GLY N N 107.89 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 178.01 0.1 1 727 152 ASP CA C 56.09 0.1 1 728 152 ASP N N 121.39 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 177.01 0.1 1 732 153 GLN CA C 56.89 0.1 1 733 153 GLN N N 118.09 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 177.21 0.1 1 737 154 LEU CA C 55.99 0.1 1 738 154 LEU N N 119.69 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 176.41 0.1 1 742 155 LEU CA C 55.19 0.1 1 743 155 LEU N N 119.99 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 175.81 0.1 1 747 156 ARG CA C 57.59 0.1 1 748 156 ARG N N 126.19 0.1 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants_set_1 _Saveframe_category coupling_constants loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions _Spectrometer_frequency_1H 600 _Mol_system_component_name spectrin loop_ _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_value_error 3JHNHA 2 GLU H 2 GLU HA 6.6 1.5 3JHNHA 3 GLN H 3 GLN HA 6.3 1.5 3JHNHA 4 PHE H 4 PHE HA 6.3 1.5 3JHNHA 6 LYS H 6 LYS HA 6.3 1.5 3JHNHA 8 THR H 8 THR HA 6.6 1.5 3JHNHA 9 VAL H 9 VAL HA 7.6 1.5 3JHNHA 10 VAL H 10 VAL HA 6.5 1.5 3JHNHA 11 GLU H 11 GLU HA 6.5 1.5 3JHNHA 12 SER H 12 SER HA 6.6 1.5 3JHNHA 13 SER H 13 SER HA 6.3 1.5 3JHNHA 16 LYS H 16 LYS HA 6.4 1.5 3JHNHA 17 VAL H 17 VAL HA 6.1 1.5 3JHNHA 18 LEU H 18 LEU HA 6.1 1.5 3JHNHA 35 TYR H 35 TYR HA 2.8 1.5 3JHNHA 23 GLU H 23 GLU HA 2.8 1.5 3JHNHA 25 GLN H 25 GLN HA 3.5 1.5 3JHNHA 29 GLN H 29 GLN HA 3.6 1.5 3JHNHA 31 VAL H 31 VAL HA 2.7 1.5 3JHNHA 32 LEU H 32 LEU HA 3.7 1.5 3JHNHA 37 SER H 37 SER HA 4.9 1.5 3JHNHA 40 GLU H 40 GLU HA 3.7 1.5 3JHNHA 43 ALA H 43 ALA HA 3.9 1.5 3JHNHA 44 GLU H 44 GLU HA 2.5 1.5 3JHNHA 45 ARG H 45 ARG HA 2.9 1.5 3JHNHA 47 GLN H 47 GLN HA 6.1 1.5 3JHNHA 48 LYS H 48 LYS HA 7.2 1.5 3JHNHA 49 LEU H 49 LEU HA 6.5 1.5 3JHNHA 50 GLU H 50 GLU HA 5.0 1.5 3JHNHA 51 ASP H 51 ASP HA 7.5 1.5 3JHNHA 52 SER H 52 SER HA 4.2 1.5 3JHNHA 54 HIS H 54 HIS HA 3.9 1.5 3JHNHA 57 VAL H 57 VAL HA 3.5 1.5 3JHNHA 59 LYS H 59 LYS HA 4.6 1.5 3JHNHA 60 ARG H 60 ARG HA 4.6 1.5 3JHNHA 61 ASP H 61 ASP HA 4.4 1.5 3JHNHA 62 ALA H 62 ALA HA 3.3 1.5 3JHNHA 64 ASP H 64 ASP HA 4.0 1.5 3JHNHA 65 LEU H 65 LEU HA 4.1 1.5 3JHNHA 67 LYS H 67 LYS HA 3.0 1.5 3JHNHA 68 TRP H 68 TRP HA 3.2 1.5 3JHNHA 70 MET H 70 MET HA 4.3 1.5 3JHNHA 71 GLU H 71 GLU HA 4.9 1.5 3JHNHA 72 LYS H 72 LYS HA 3.3 1.5 3JHNHA 74 ASN H 74 ASN HA 4.4 1.5 3JHNHA 75 ILE H 75 ILE HA 3.8 1.5 3JHNHA 77 THR H 77 THR HA 3.2 1.5 3JHNHA 78 ASP H 78 ASP HA 2.9 1.5 3JHNHA 79 LYS H 79 LYS HA 4.1 1.5 3JHNHA 80 SER H 80 SER HA 2.9 1.5 3JHNHA 81 TYR H 81 TYR HA 2.7 1.5 3JHNHA 85 THR H 85 THR HA 7.4 1.5 3JHNHA 86 ASN H 86 ASN HA 7.1 1.5 3JHNHA 87 ILE H 87 ILE HA 6.6 1.5 3JHNHA 88 GLN H 88 GLN HA 4.0 1.5 3JHNHA 89 GLY H 89 GLY HA 6.4 1.5 3JHNHA 90 LYS H 90 LYS HA 4.3 1.5 3JHNHA 91 TYR H 91 TYR HA 4.2 1.5 3JHNHA 93 LYS H 93 LYS HA 3.0 1.5 3JHNHA 95 GLN H 95 GLN HA 3.8 1.5 3JHNHA 96 SER H 96 SER HA 3.0 1.5 3JHNHA 98 GLU H 98 GLU HA 3.6 1.5 3JHNHA 99 ALA H 99 ALA HA 4.2 1.5 3JHNHA 101 VAL H 101 VAL HA 3.1 1.5 3JHNHA 102 GLN H 102 GLN HA 4.4 1.5 3JHNHA 104 LYS H 104 LYS HA 3.6 1.5 3JHNHA 105 SER H 105 SER HA 3.0 1.5 3JHNHA 107 LEU H 107 LEU HA 2.8 1.5 3JHNHA 108 MET H 108 MET HA 4.8 1.5 3JHNHA 109 SER H 109 SER HA 3.2 1.5 3JHNHA 111 LEU H 111 LEU HA 3.8 1.5 3JHNHA 113 LYS H 113 LYS HA 3.0 1.5 3JHNHA 114 THR H 114 THR HA 3.8 1.5 3JHNHA 115 ARG H 115 ARG HA 2.9 1.5 3JHNHA 117 GLU H 117 GLU HA 3.5 1.5 3JHNHA 119 PHE H 119 PHE HA 7.4 1.5 3JHNHA 120 THR H 120 THR HA 6.9 1.5 3JHNHA 121 MET H 121 MET HA 7.7 1.5 3JHNHA 123 HIS H 123 HIS HA 5.4 1.5 3JHNHA 126 HIS H 126 HIS HA 4.7 1.5 3JHNHA 127 GLU H 127 GLU HA 4.1 1.5 3JHNHA 130 LYS H 130 LYS HA 2.5 1.5 3JHNHA 132 HIS H 132 HIS HA 3.2 1.5 3JHNHA 134 GLU H 134 GLU HA 4.2 1.5 3JHNHA 137 ARG H 137 ARG HA 4.2 1.5 3JHNHA 138 HIS H 138 HIS HA 5.1 1.5 3JHNHA 141 ASP H 141 ASP HA 3.8 1.5 3JHNHA 142 LEU H 142 LEU HA 3.8 1.5 3JHNHA 145 GLU H 145 GLU HA 3.1 1.5 3JHNHA 146 LEU H 146 LEU HA 3.1 1.5 3JHNHA 148 LEU H 148 LEU HA 3.4 1.5 3JHNHA 149 GLU H 149 GLU HA 3.2 1.5 3JHNHA 152 ASP H 152 ASP HA 4.0 1.5 3JHNHA 153 GLN H 153 GLN HA 4.5 1.5 3JHNHA 154 LEU H 154 LEU HA 4.0 1.5 3JHNHA 155 LEU H 155 LEU HA 5.1 1.5 3JHNHA 156 ARG H 156 ARG HA 8.0 1.5 stop_ save_