data_5175 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, 15N and sidechain 1H Chemical shift of CPI-17 ; _BMRB_accession_number 5175 _BMRB_flat_file_name bmr5175.str _Entry_type original _Submission_date 2001-10-11 _Accession_date 2001-10-16 _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 Ohki Shin-ya . . 2 Eto Masumi . . 3 Kariya Eri . . 4 Hayano Toshiya . . 5 Hayashi Yuichiro . . 6 Yazawa Michio . . 7 Brautigan David . . 8 Kainosho Masatsune . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 505 "13C chemical shifts" 168 "15N chemical shifts" 84 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-05-06 original author . stop_ _Original_release_date 2002-05-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution NMR Structure of the Myosin Phosphatase Inhibitor Protein CPI-17 Shows Phosphorylation-induced Conformational Changes Responsible for Activation ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21592567 _PubMed_ID 11734001 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ohki Shin-ya . . 2 Eto Masumi . . 3 Kariya Eri . . 4 Hayano Toshiya . . 5 Hayashi Yuichiro . . 6 Yazawa Michio . . 7 Brautigan David . . 8 Kainosho Masatsune . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 314 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 839 _Page_last 849 _Year 2001 _Details . loop_ _Keyword CPI-17 stop_ save_ ################################## # Molecular system description # ################################## save_system_CPI-17 _Saveframe_category molecular_system _Mol_system_name 'CPI-17 (35-120) deletion mutant' _Abbreviation_common CPI-17 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CPI-17 $CPI-17 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CPI-17 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CPI-17 _Abbreviation_common CPI-17 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 86 _Mol_residue_sequence ; ARVTVKYDRRELQRRLDVEK WIDGRLEELYRGREADMPDE VNIDELLELESEEERSRKIQ GLLKSCTNPTENFVQELLVK LRGLHK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 35 ALA 2 36 ARG 3 37 VAL 4 38 THR 5 39 VAL 6 40 LYS 7 41 TYR 8 42 ASP 9 43 ARG 10 44 ARG 11 45 GLU 12 46 LEU 13 47 GLN 14 48 ARG 15 49 ARG 16 50 LEU 17 51 ASP 18 52 VAL 19 53 GLU 20 54 LYS 21 55 TRP 22 56 ILE 23 57 ASP 24 58 GLY 25 59 ARG 26 60 LEU 27 61 GLU 28 62 GLU 29 63 LEU 30 64 TYR 31 65 ARG 32 66 GLY 33 67 ARG 34 68 GLU 35 69 ALA 36 70 ASP 37 71 MET 38 72 PRO 39 73 ASP 40 74 GLU 41 75 VAL 42 76 ASN 43 77 ILE 44 78 ASP 45 79 GLU 46 80 LEU 47 81 LEU 48 82 GLU 49 83 LEU 50 84 GLU 51 85 SER 52 86 GLU 53 87 GLU 54 88 GLU 55 89 ARG 56 90 SER 57 91 ARG 58 92 LYS 59 93 ILE 60 94 GLN 61 95 GLY 62 96 LEU 63 97 LEU 64 98 LYS 65 99 SER 66 100 CYS 67 101 THR 68 102 ASN 69 103 PRO 70 104 THR 71 105 GLU 72 106 ASN 73 107 PHE 74 108 VAL 75 109 GLN 76 110 GLU 77 111 LEU 78 112 LEU 79 113 VAL 80 114 LYS 81 115 LEU 82 116 ARG 83 117 GLY 84 118 LEU 85 119 HIS 86 120 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 BMRB 5662 CPI-17_(22-120) 100.00 99 100.00 100.00 3.35e-52 BMRB 5663 CPI-17_(22-120)_T38D 100.00 99 98.84 98.84 4.28e-51 PDB 1J2M "Solution Structure Of Cpi-17(22-120)" 100.00 99 100.00 100.00 3.35e-52 PDB 1J2N "Solution Structure Of Cpi-17(22-120) T38d" 100.00 99 98.84 98.84 4.28e-51 PDB 1K5O "Cpi-17(35-120) Deletion Mutant" 100.00 86 100.00 100.00 2.10e-52 PDB 2RLT "Phosphorylated Cpi-17 (22-120)" 100.00 99 98.84 98.84 3.09e-51 DBJ BAA22995 "17-kDa PKC-potentiated inhibitory protein of PP1 [Sus scrofa]" 100.00 147 100.00 100.00 7.63e-53 REF NP_001179999 "protein phosphatase 1 regulatory subunit 14A [Bos taurus]" 100.00 147 97.67 98.84 1.64e-51 REF NP_999502 "protein phosphatase 1 regulatory subunit 14A [Sus scrofa]" 100.00 147 100.00 100.00 7.63e-53 REF XP_004015712 "PREDICTED: protein phosphatase 1 regulatory subunit 14A [Ovis aries]" 100.00 153 97.67 98.84 1.31e-51 REF XP_004284289 "PREDICTED: protein phosphatase 1 regulatory subunit 14A [Orcinus orca]" 100.00 147 97.67 98.84 1.25e-50 REF XP_004330765 "PREDICTED: protein phosphatase 1 regulatory subunit 14A-like, partial [Tursiops truncatus]" 69.77 99 98.33 98.33 2.09e-30 SP O18734 "RecName: Full=Protein phosphatase 1 regulatory subunit 14A; AltName: Full=17 kDa PKC-potentiated inhibitory protein of PP1; Alt" 100.00 147 100.00 100.00 7.63e-53 TPG DAA19818 "TPA: protein phosphatase 1, regulatory (inhibitor) subunit 14A-like [Bos taurus]" 100.00 147 97.67 98.84 1.64e-51 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ $CPI-17 9823 Pig Eukaryota Metazoa Sus scrofa aorta 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 $CPI-17 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CPI-17 . mM 0.8 1.3 . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 800 _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.05 n/a temperature 298 0.1 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 . ppm 0.0 . indirect . . . 0.101329112 DSS C 13 . ppm 0.0 . indirect . . . 0.251449519 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name CPI-17 _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 ALA H H 8.50 . 1 2 . 1 ALA HA H 4.31 . 1 3 . 1 ALA HB H 1.38 . 1 4 . 1 ALA N N 126.78 . 1 5 . 1 ALA CA C 51.20 . 1 6 . 1 ALA CB C 17.15 . 1 7 . 2 ARG H H 8.39 . 1 8 . 2 ARG HA H 4.35 . 1 9 . 2 ARG HB2 H 1.82 . 2 10 . 2 ARG HB3 H 1.77 . 2 11 . 2 ARG HG2 H 1.65 . 2 12 . 2 ARG HG3 H 1.59 . 2 13 . 2 ARG HD2 H 3.18 . 1 14 . 2 ARG HD3 H 3.18 . 1 15 . 2 ARG N N 121.41 . 1 16 . 2 ARG CA C 55.02 . 1 17 . 2 ARG CB C 29.19 . 1 18 . 3 VAL H H 8.26 . 1 19 . 3 VAL HA H 4.19 . 1 20 . 3 VAL HB H 2.07 . 1 21 . 3 VAL HG1 H 0.93 . 1 22 . 3 VAL HG2 H 0.93 . 1 23 . 3 VAL N N 122.21 . 1 24 . 3 VAL CA C 61.45 . 1 25 . 3 VAL CB C 31.08 . 1 26 . 4 THR H H 8.31 . 1 27 . 4 THR HA H 4.35 . 1 28 . 4 THR HB H 4.15 . 1 29 . 4 THR HG2 H 1.16 . 1 30 . 4 THR N N 119.13 . 1 31 . 4 THR CA C 61.18 . 1 32 . 4 THR CB C 69.11 . 1 33 . 5 VAL H H 8.11 . 1 34 . 5 VAL HA H 4.05 . 1 35 . 5 VAL HB H 1.95 . 1 36 . 5 VAL HG1 H 0.85 . 1 37 . 5 VAL HG2 H 0.77 . 1 38 . 5 VAL N N 123.22 . 1 39 . 5 VAL CA C 61.18 . 1 40 . 5 VAL CB C 31.33 . 1 41 . 6 LYS H H 8.23 . 1 42 . 6 LYS HA H 4.25 . 1 43 . 6 LYS HB2 H 1.61 . 1 44 . 6 LYS HB3 H 1.61 . 1 45 . 6 LYS HG2 H 1.29 . 2 46 . 6 LYS HG3 H 1.20 . 2 47 . 6 LYS HD2 H 0.93 . 1 48 . 6 LYS HD3 H 0.93 . 1 49 . 6 LYS HE2 H 2.93 . 1 50 . 6 LYS HE3 H 2.93 . 1 51 . 6 LYS N N 124.71 . 1 52 . 6 LYS CA C 55.24 . 1 53 . 6 LYS CB C 31.37 . 1 54 . 7 TYR H H 7.91 . 1 55 . 7 TYR HA H 4.66 . 1 56 . 7 TYR HB2 H 3.07 . 2 57 . 7 TYR HB3 H 2.82 . 2 58 . 7 TYR HD1 H 7.23 . 1 59 . 7 TYR HD2 H 7.23 . 1 60 . 7 TYR HE1 H 6.69 . 1 61 . 7 TYR HE2 H 6.69 . 1 62 . 7 TYR N N 121.09 . 1 63 . 7 TYR CA C 55.78 . 1 64 . 7 TYR CB C 38.25 . 1 65 . 8 ASP H H 8.47 . 1 66 . 8 ASP HA H 4.62 . 1 67 . 8 ASP HB2 H 2.83 . 2 68 . 8 ASP HB3 H 2.77 . 2 69 . 8 ASP N N 122.29 . 1 70 . 8 ASP CA C 52.46 . 1 71 . 8 ASP CB C 40.32 . 1 72 . 9 ARG H H 8.54 . 1 73 . 9 ARG HA H 4.10 . 1 74 . 9 ARG HB2 H 1.92 . 2 75 . 9 ARG HB3 H 1.39 . 2 76 . 9 ARG HG2 H 1.71 . 2 77 . 9 ARG HG3 H 1.67 . 2 78 . 9 ARG HD2 H 3.31 . 2 79 . 9 ARG HD3 H 3.23 . 2 80 . 9 ARG N N 121.93 . 1 81 . 9 ARG CA C 57.98 . 1 82 . 9 ARG CB C 28.11 . 1 83 . 10 ARG H H 8.34 . 1 84 . 10 ARG HA H 4.14 . 1 85 . 10 ARG HB2 H 2.01 . 1 86 . 10 ARG HB3 H 2.01 . 1 87 . 10 ARG HD2 H 3.31 . 2 88 . 10 ARG HD3 H 3.23 . 2 89 . 10 ARG N N 120.29 . 1 90 . 10 ARG CA C 60.80 . 1 91 . 10 ARG CB C 31.39 . 1 92 . 11 GLU H H 8.22 . 1 93 . 11 GLU HA H 4.07 . 1 94 . 11 GLU HB2 H 1.70 . 1 95 . 11 GLU HB3 H 1.70 . 1 96 . 11 GLU N N 118.59 . 1 97 . 11 GLU CA C 58.06 . 1 98 . 11 GLU CB C 30.72 . 1 99 . 12 LEU H H 8.26 . 1 100 . 12 LEU HA H 4.04 . 1 101 . 12 LEU HB2 H 1.89 . 2 102 . 12 LEU HB3 H 1.71 . 2 103 . 12 LEU HG H 1.65 . 1 104 . 12 LEU HD1 H 0.92 . 1 105 . 12 LEU HD2 H 0.92 . 1 106 . 12 LEU N N 120.96 . 1 107 . 12 LEU CA C 56.99 . 1 108 . 12 LEU CB C 39.86 . 1 109 . 13 GLN H H 8.00 . 1 110 . 13 GLN HA H 3.94 . 1 111 . 13 GLN HB2 H 2.18 . 1 112 . 13 GLN HB3 H 2.18 . 1 113 . 13 GLN HG2 H 2.43 . 1 114 . 13 GLN HG3 H 2.43 . 1 115 . 13 GLN N N 119.49 . 1 116 . 13 GLN CA C 56.53 . 1 117 . 13 GLN CB C 38.63 . 1 118 . 14 ARG H H 7.91 . 1 119 . 14 ARG HA H 4.17 . 1 120 . 14 ARG HB2 H 2.01 . 2 121 . 14 ARG HB3 H 1.79 . 2 122 . 14 ARG HG2 H 1.61 . 2 123 . 14 ARG HG3 H 1.57 . 2 124 . 14 ARG HD2 H 3.05 . 1 125 . 14 ARG N N 122.29 . 1 126 . 14 ARG CA C 66.70 . 1 127 . 14 ARG CB C 29.62 . 1 128 . 15 ARG H H 8.02 . 1 129 . 15 ARG HA H 3.89 . 1 130 . 15 ARG HB2 H 2.60 . 2 131 . 15 ARG HB3 H 2.41 . 2 132 . 15 ARG HD2 H 3.10 . 2 133 . 15 ARG HD3 H 2.94 . 2 134 . 15 ARG N N 121.52 . 1 135 . 15 ARG CA C 57.48 . 1 136 . 15 ARG CB C 28.83 . 1 137 . 16 LEU H H 8.30 . 1 138 . 16 LEU HA H 4.18 . 1 139 . 16 LEU HB2 H 1.87 . 1 140 . 16 LEU HB3 H 1.87 . 1 141 . 16 LEU HG H 1.78 . 1 142 . 16 LEU HD1 H 0.92 . 1 143 . 16 LEU HD2 H 0.92 . 1 144 . 16 LEU N N 121.45 . 1 145 . 16 LEU CA C 54.48 . 1 146 . 16 LEU CB C 30.88 . 1 147 . 17 ASP H H 8.38 . 1 148 . 17 ASP HA H 4.51 . 1 149 . 17 ASP HB2 H 2.90 . 2 150 . 17 ASP HB3 H 2.68 . 2 151 . 17 ASP N N 125.29 . 1 152 . 17 ASP CA C 61.47 . 1 153 . 17 ASP CB C 30.16 . 1 154 . 18 VAL H H 7.91 . 1 155 . 18 VAL HA H 3.89 . 1 156 . 18 VAL HB H 2.33 . 1 157 . 18 VAL HG1 H 1.07 . 1 158 . 18 VAL HG2 H 0.97 . 1 159 . 18 VAL N N 121.28 . 1 160 . 18 VAL CA C 54.79 . 1 161 . 18 VAL CB C 39.62 . 1 162 . 19 GLU H H 8.56 . 1 163 . 19 GLU HA H 4.00 . 1 164 . 19 GLU HB2 H 2.34 . 2 165 . 19 GLU HB3 H 2.16 . 2 166 . 19 GLU HG2 H 2.59 . 1 167 . 19 GLU HG3 H 2.59 . 1 168 . 19 GLU N N 114.27 . 1 169 . 19 GLU CA C 61.13 . 1 170 . 19 GLU CB C 30.29 . 1 171 . 20 LYS H H 8.44 . 1 172 . 20 LYS HA H 4.24 . 1 173 . 20 LYS HB2 H 2.05 . 2 174 . 20 LYS HB3 H 2.01 . 2 175 . 20 LYS HG2 H 1.70 . 2 176 . 20 LYS HG3 H 1.61 . 2 177 . 20 LYS HD2 H 1.80 . 1 178 . 20 LYS HD3 H 1.80 . 1 179 . 20 LYS HE2 H 3.03 . 1 180 . 20 LYS HE3 H 3.03 . 1 181 . 20 LYS N N 125.31 . 1 182 . 20 LYS CA C 57.78 . 1 183 . 20 LYS CB C 30.69 . 1 184 . 21 TRP H H 8.15 . 1 185 . 21 TRP HA H 4.27 . 1 186 . 21 TRP HB2 H 3.81 . 2 187 . 21 TRP HB3 H 3.43 . 2 188 . 21 TRP HD1 H 6.97 . 1 189 . 21 TRP HE3 H 7.68 . 1 190 . 21 TRP HZ2 H 6.74 . 1 191 . 21 TRP HZ3 H 7.05 . 1 192 . 21 TRP N N 123.32 . 1 193 . 21 TRP CA C 60.82 . 1 194 . 21 TRP CB C 26.32 . 1 195 . 22 ILE H H 9.10 . 1 196 . 22 ILE HA H 3.26 . 1 197 . 22 ILE HB H 2.32 . 1 198 . 22 ILE HG12 H 2.66 . 1 199 . 22 ILE HG13 H 2.34 . 1 200 . 22 ILE HG2 H 1.08 . 1 201 . 22 ILE HD1 H 1.03 . 1 202 . 22 ILE N N 120.98 . 1 203 . 22 ILE CA C 66.00 . 1 204 . 22 ILE CB C 36.83 . 1 205 . 23 ASP H H 7.98 . 1 206 . 23 ASP HA H 4.30 . 1 207 . 23 ASP HB2 H 2.80 . 2 208 . 23 ASP HB3 H 2.70 . 2 209 . 23 ASP N N 118.98 . 1 210 . 23 ASP CA C 56.97 . 1 211 . 23 ASP CB C 39.15 . 1 212 . 24 GLY H H 7.81 . 1 213 . 24 GLY HA2 H 3.89 . 2 214 . 24 GLY HA3 H 3.88 . 2 215 . 24 GLY N N 105.18 . 1 216 . 24 GLY CA C 45.73 . 1 217 . 25 ARG H H 7.84 . 1 218 . 25 ARG HA H 4.01 . 1 219 . 25 ARG HB2 H 1.47 . 2 220 . 25 ARG HB3 H 1.43 . 2 221 . 25 ARG HD2 H 2.96 . 2 222 . 25 ARG HD3 H 2.93 . 2 223 . 25 ARG N N 121.17 . 1 224 . 25 ARG CA C 55.98 . 1 225 . 25 ARG CB C 28.23 . 1 226 . 26 LEU H H 8.85 . 1 227 . 26 LEU HA H 3.85 . 1 228 . 26 LEU HB2 H 2.00 . 2 229 . 26 LEU HB3 H 1.33 . 2 230 . 26 LEU HG H 1.80 . 1 231 . 26 LEU HD1 H 0.59 . 1 232 . 26 LEU HD2 H 0.79 . 1 233 . 26 LEU N N 120.09 . 1 234 . 26 LEU CA C 57.45 . 1 235 . 26 LEU CB C 40.10 . 1 236 . 27 GLU H H 7.62 . 1 237 . 27 GLU HA H 3.87 . 1 238 . 27 GLU HB2 H 2.07 . 1 239 . 27 GLU HB3 H 2.07 . 1 240 . 27 GLU HG2 H 2.48 . 2 241 . 27 GLU HG3 H 2.19 . 2 242 . 27 GLU N N 117.75 . 1 243 . 27 GLU CA C 58.83 . 1 244 . 27 GLU CB C 27.43 . 1 245 . 28 GLU H H 6.88 . 1 246 . 28 GLU HA H 4.00 . 1 247 . 28 GLU HB2 H 2.17 . 2 248 . 28 GLU HB3 H 2.00 . 2 249 . 28 GLU HG2 H 2.36 . 2 250 . 28 GLU HG3 H 2.29 . 2 251 . 28 GLU N N 116.23 . 1 252 . 28 GLU CA C 57.77 . 1 253 . 28 GLU CB C 28.85 . 1 254 . 29 LEU H H 8.47 . 1 255 . 29 LEU HA H 3.79 . 1 256 . 29 LEU HB2 H 1.68 . 2 257 . 29 LEU HB3 H 1.29 . 2 258 . 29 LEU HG H 1.59 . 1 259 . 29 LEU HD1 H 0.74 . 1 260 . 29 LEU HD2 H 0.32 . 1 261 . 29 LEU N N 120.70 . 1 262 . 29 LEU CA C 56.73 . 1 263 . 29 LEU CB C 41.03 . 1 264 . 30 TYR H H 7.90 . 1 265 . 30 TYR HA H 4.27 . 1 266 . 30 TYR HB2 H 3.32 . 2 267 . 30 TYR HB3 H 2.58 . 2 268 . 30 TYR HD1 H 7.29 . 1 269 . 30 TYR HD2 H 7.29 . 1 270 . 30 TYR HE1 H 6.46 . 1 271 . 30 TYR HE2 H 6.46 . 1 272 . 30 TYR N N 114.58 . 1 273 . 30 TYR CA C 57.03 . 1 274 . 30 TYR CB C 35.17 . 1 275 . 31 ARG H H 6.84 . 1 276 . 31 ARG HA H 4.14 . 1 277 . 31 ARG HB2 H 2.14 . 2 278 . 31 ARG HB3 H 1.71 . 2 279 . 31 ARG HG2 H 1.39 . 1 280 . 31 ARG HG3 H 1.39 . 1 281 . 31 ARG HD2 H 3.23 . 1 282 . 31 ARG HD3 H 3.23 . 1 283 . 31 ARG N N 123.33 . 1 284 . 31 ARG CA C 57.76 . 1 285 . 31 ARG CB C 27.30 . 1 286 . 32 GLY H H 9.38 . 1 287 . 32 GLY HA2 H 4.34 . 2 288 . 32 GLY HA3 H 3.88 . 2 289 . 32 GLY N N 119.05 . 1 290 . 32 GLY CA C 44.58 . 1 291 . 33 ARG H H 8.72 . 1 292 . 33 ARG HA H 4.77 . 1 293 . 33 ARG HB2 H 2.34 . 2 294 . 33 ARG HB3 H 1.52 . 2 295 . 33 ARG HG2 H 1.64 . 1 296 . 33 ARG HG3 H 1.64 . 1 297 . 33 ARG HD2 H 3.29 . 1 298 . 33 ARG HD3 H 3.29 . 1 299 . 33 ARG N N 123.94 . 1 300 . 33 ARG CA C 53.28 . 1 301 . 33 ARG CB C 28.64 . 1 302 . 34 GLU H H 9.27 . 1 303 . 34 GLU HA H 3.77 . 1 304 . 34 GLU HB2 H 2.07 . 2 305 . 34 GLU HB3 H 1.94 . 2 306 . 34 GLU HG2 H 2.66 . 2 307 . 34 GLU HG3 H 2.32 . 2 308 . 34 GLU N N 121.51 . 1 309 . 34 GLU CA C 61.55 . 1 310 . 34 GLU CB C 26.33 . 1 311 . 35 ALA H H 8.56 . 1 312 . 35 ALA HA H 4.15 . 1 313 . 35 ALA HB H 1.39 . 1 314 . 35 ALA N N 120.62 . 1 315 . 35 ALA CA C 52.91 . 1 316 . 35 ALA CB C 16.33 . 1 317 . 36 ASP H H 7.95 . 1 318 . 36 ASP HA H 4.65 . 1 319 . 36 ASP HB2 H 2.93 . 1 320 . 36 ASP HB3 H 2.93 . 1 321 . 36 ASP N N 115.93 . 1 322 . 36 ASP CA C 53.11 . 1 323 . 36 ASP CB C 40.29 . 1 324 . 37 MET H H 7.12 . 1 325 . 37 MET HA H 2.60 . 1 326 . 37 MET HB2 H 1.71 . 2 327 . 37 MET HB3 H 1.52 . 2 328 . 37 MET HG2 H 2.12 . 1 329 . 37 MET HG3 H 2.12 . 1 330 . 37 MET N N 121.50 . 1 331 . 37 MET CA C 53.30 . 1 332 . 37 MET CB C 31.95 . 1 333 . 38 PRO HA H 4.39 . 1 334 . 38 PRO HB2 H 2.36 . 2 335 . 38 PRO HB3 H 1.71 . 2 336 . 38 PRO HG2 H 1.89 . 2 337 . 38 PRO HG3 H 1.73 . 2 338 . 38 PRO HD2 H 3.34 . 2 339 . 38 PRO HD3 H 2.96 . 2 340 . 38 PRO CA C 53.55 . 1 341 . 38 PRO CB C 29.88 . 1 342 . 39 ASP H H 8.41 . 1 343 . 39 ASP HA H 4.29 . 1 344 . 39 ASP HB2 H 2.64 . 1 345 . 39 ASP HB3 H 2.64 . 1 346 . 39 ASP N N 120.74 . 1 347 . 39 ASP CA C 56.98 . 1 348 . 39 ASP CB C 40.28 . 1 349 . 40 GLU H H 7.53 . 1 350 . 40 GLU HA H 4.40 . 1 351 . 40 GLU HB2 H 2.06 . 2 352 . 40 GLU HB3 H 1.89 . 2 353 . 40 GLU HG2 H 2.11 . 2 354 . 40 GLU HG3 H 2.05 . 2 355 . 40 GLU N N 118.72 . 1 356 . 40 GLU CA C 57.46 . 1 357 . 40 GLU CB C 26.73 . 1 358 . 41 VAL H H 8.74 . 1 359 . 41 VAL HA H 3.94 . 1 360 . 41 VAL HB H 2.18 . 1 361 . 41 VAL HG1 H 0.89 . 1 362 . 41 VAL HG2 H 0.82 . 1 363 . 41 VAL N N 118.73 . 1 364 . 41 VAL CA C 58.58 . 1 365 . 41 VAL CB C 28.86 . 1 366 . 42 ASN H H 8.79 . 1 367 . 42 ASN HA H 4.69 . 1 368 . 42 ASN HB2 H 2.99 . 2 369 . 42 ASN HB3 H 2.59 . 2 370 . 42 ASN N N 119.70 . 1 371 . 42 ASN CA C 52.05 . 1 372 . 42 ASN CB C 37.54 . 1 373 . 43 ILE H H 8.79 . 1 374 . 43 ILE HA H 3.60 . 1 375 . 43 ILE HB H 1.82 . 1 376 . 43 ILE HG12 H 1.68 . 1 377 . 43 ILE HG13 H 1.10 . 1 378 . 43 ILE HG2 H 0.80 . 1 379 . 43 ILE HD1 H 0.86 . 1 380 . 43 ILE N N 126.19 . 1 381 . 43 ILE CA C 64.38 . 1 382 . 43 ILE CB C 37.26 . 1 383 . 44 ASP H H 7.99 . 1 384 . 44 ASP HA H 4.34 . 1 385 . 44 ASP HB2 H 2.81 . 2 386 . 44 ASP HB3 H 2.65 . 2 387 . 44 ASP N N 120.31 . 1 388 . 44 ASP CA C 57.61 . 1 389 . 44 ASP CB C 38.66 . 1 390 . 45 GLU H H 7.82 . 1 391 . 45 GLU HA H 3.99 . 1 392 . 45 GLU HB2 H 2.00 . 1 393 . 45 GLU HB3 H 2.00 . 1 394 . 45 GLU HG2 H 2.17 . 1 395 . 45 GLU HG3 H 2.17 . 1 396 . 45 GLU N N 118.57 . 1 397 . 45 GLU CA C 57.82 . 1 398 . 45 GLU CB C 28.42 . 1 399 . 46 LEU H H 7.35 . 1 400 . 46 LEU HA H 4.10 . 1 401 . 46 LEU HB2 H 2.09 . 2 402 . 46 LEU HB3 H 1.12 . 2 403 . 46 LEU HG H 1.94 . 1 404 . 46 LEU HD1 H 0.78 . 1 405 . 46 LEU HD2 H 0.85 . 1 406 . 46 LEU N N 117.86 . 1 407 . 46 LEU CA C 56.63 . 1 408 . 46 LEU CB C 41.23 . 1 409 . 47 LEU H H 8.26 . 1 410 . 47 LEU HA H 4.10 . 1 411 . 47 LEU HB2 H 1.92 . 2 412 . 47 LEU HB3 H 1.40 . 2 413 . 47 LEU HG H 1.85 . 1 414 . 47 LEU HD1 H 0.85 . 1 415 . 47 LEU HD2 H 0.79 . 1 416 . 47 LEU N N 117.10 . 1 417 . 47 LEU CA C 55.27 . 1 418 . 47 LEU CB C 40.43 . 1 419 . 48 GLU H H 7.28 . 1 420 . 48 GLU HA H 4.05 . 1 421 . 48 GLU HB2 H 2.10 . 2 422 . 48 GLU HB3 H 2.07 . 2 423 . 48 GLU HG2 H 2.42 . 2 424 . 48 GLU HG3 H 2.34 . 2 425 . 48 GLU N N 116.30 . 1 426 . 48 GLU CA C 56.42 . 1 427 . 48 GLU CB C 28.37 . 1 428 . 49 LEU H H 7.15 . 1 429 . 49 LEU HA H 4.45 . 1 430 . 49 LEU HB2 H 2.13 . 2 431 . 49 LEU HB3 H 1.26 . 2 432 . 49 LEU HG H 2.00 . 1 433 . 49 LEU HD1 H 0.91 . 1 434 . 49 LEU HD2 H 0.91 . 1 435 . 49 LEU N N 119.86 . 1 436 . 49 LEU CA C 52.83 . 1 437 . 49 LEU CB C 40.29 . 1 438 . 50 GLU H H 8.75 . 1 439 . 50 GLU HA H 4.13 . 1 440 . 50 GLU HB2 H 2.13 . 2 441 . 50 GLU HB3 H 2.11 . 2 442 . 50 GLU HG2 H 2.35 . 2 443 . 50 GLU HG3 H 2.25 . 2 444 . 50 GLU N N 123.14 . 1 445 . 50 GLU CA C 57.50 . 1 446 . 50 GLU CB C 28.79 . 1 447 . 51 SER H H 7.81 . 1 448 . 51 SER HA H 4.77 . 1 449 . 51 SER HB2 H 4.25 . 2 450 . 51 SER HB3 H 3.92 . 2 451 . 51 SER N N 111.79 . 1 452 . 51 SER CA C 55.45 . 1 453 . 51 SER CB C 64.58 . 1 454 . 52 GLU H H 9.21 . 1 455 . 52 GLU HA H 3.94 . 1 456 . 52 GLU HB2 H 2.06 . 1 457 . 52 GLU HB3 H 2.06 . 1 458 . 52 GLU HG2 H 2.50 . 2 459 . 52 GLU HG3 H 2.23 . 2 460 . 52 GLU N N 126.54 . 1 461 . 52 GLU CA C 59.16 . 1 462 . 52 GLU CB C 27.50 . 1 463 . 53 GLU H H 8.69 . 1 464 . 53 GLU HA H 4.08 . 1 465 . 53 GLU HB2 H 2.07 . 2 466 . 53 GLU HB3 H 1.93 . 2 467 . 53 GLU HG2 H 2.31 . 1 468 . 53 GLU HG3 H 2.31 . 1 469 . 53 GLU N N 120.67 . 1 470 . 53 GLU CA C 58.76 . 1 471 . 53 GLU CB C 27.18 . 1 472 . 54 GLU H H 7.69 . 1 473 . 54 GLU HA H 4.05 . 1 474 . 54 GLU HB2 H 2.18 . 2 475 . 54 GLU HB3 H 2.00 . 2 476 . 54 GLU HG2 H 2.40 . 2 477 . 54 GLU HG3 H 2.32 . 2 478 . 54 GLU N N 119.08 . 1 479 . 54 GLU CA C 58.26 . 1 480 . 54 GLU CB C 28.84 . 1 481 . 55 ARG H H 8.12 . 1 482 . 55 ARG HA H 3.88 . 1 483 . 55 ARG HB2 H 2.05 . 2 484 . 55 ARG HB3 H 2.02 . 2 485 . 55 ARG HG2 H 1.86 . 2 486 . 55 ARG HG3 H 1.50 . 2 487 . 55 ARG HD2 H 2.93 . 2 488 . 55 ARG HD3 H 2.89 . 2 489 . 55 ARG N N 119.86 . 1 490 . 55 ARG CA C 59.69 . 1 491 . 55 ARG CB C 29.40 . 1 492 . 56 SER H H 8.65 . 1 493 . 56 SER HA H 3.89 . 1 494 . 56 SER HB2 H 4.02 . 2 495 . 56 SER HB3 H 3.98 . 2 496 . 56 SER N N 113.68 . 1 497 . 56 SER CA C 60.99 . 1 498 . 56 SER CB C 61.95 . 1 499 . 57 ARG H H 7.92 . 1 500 . 57 ARG HA H 4.05 . 1 501 . 57 ARG HB2 H 1.90 . 1 502 . 57 ARG HB3 H 1.90 . 1 503 . 57 ARG HD2 H 3.26 . 2 504 . 57 ARG HD3 H 3.19 . 2 505 . 57 ARG N N 119.61 . 1 506 . 57 ARG CA C 58.75 . 1 507 . 57 ARG CB C 29.86 . 1 508 . 58 LYS H H 7.89 . 1 509 . 58 LYS HA H 4.20 . 1 510 . 58 LYS HB2 H 1.81 . 2 511 . 58 LYS HB3 H 1.67 . 2 512 . 58 LYS HG2 H 0.93 . 1 513 . 58 LYS HG3 H 0.93 . 1 514 . 58 LYS HD2 H 1.89 . 1 515 . 58 LYS HD3 H 1.89 . 1 516 . 58 LYS HE2 H 2.93 . 1 517 . 58 LYS HE3 H 2.93 . 1 518 . 58 LYS N N 121.09 . 1 519 . 58 LYS CA C 57.89 . 1 520 . 58 LYS CB C 30.35 . 1 521 . 59 ILE H H 8.37 . 1 522 . 59 ILE HA H 3.67 . 1 523 . 59 ILE HB H 1.90 . 1 524 . 59 ILE HG12 H 2.05 . 1 525 . 59 ILE HG13 H 2.01 . 1 526 . 59 ILE HG2 H 1.07 . 1 527 . 59 ILE HD1 H 0.81 . 1 528 . 59 ILE N N 119.80 . 1 529 . 59 ILE CA C 64.86 . 1 530 . 59 ILE CB C 36.77 . 1 531 . 60 GLN H H 8.76 . 1 532 . 60 GLN HA H 3.89 . 1 533 . 60 GLN HB2 H 2.06 . 1 534 . 60 GLN HB3 H 2.06 . 1 535 . 60 GLN HG2 H 2.46 . 2 536 . 60 GLN HG3 H 2.19 . 2 537 . 60 GLN N N 117.64 . 1 538 . 60 GLN CA C 58.68 . 1 539 . 60 GLN CB C 26.86 . 1 540 . 61 GLY H H 8.00 . 1 541 . 61 GLY HA2 H 3.93 . 1 542 . 61 GLY HA3 H 3.93 . 1 543 . 61 GLY N N 105.99 . 1 544 . 61 GLY CA C 45.91 . 1 545 . 62 LEU H H 7.78 . 1 546 . 62 LEU HA H 4.31 . 1 547 . 62 LEU HB2 H 2.24 . 2 548 . 62 LEU HB3 H 1.51 . 2 549 . 62 LEU HG H 2.06 . 1 550 . 62 LEU HD1 H 1.06 . 1 551 . 62 LEU HD2 H 1.06 . 1 552 . 62 LEU N N 121.93 . 1 553 . 62 LEU CA C 56.16 . 1 554 . 62 LEU CB C 41.07 . 1 555 . 63 LEU H H 7.43 . 1 556 . 63 LEU HA H 4.81 . 1 557 . 63 LEU HB2 H 2.02 . 2 558 . 63 LEU HB3 H 1.78 . 2 559 . 63 LEU HG H 2.07 . 1 560 . 63 LEU HD1 H 0.90 . 1 561 . 63 LEU HD2 H 0.98 . 1 562 . 63 LEU N N 117.00 . 1 563 . 63 LEU CA C 52.75 . 1 564 . 63 LEU CB C 40.52 . 1 565 . 64 LYS H H 7.27 . 1 566 . 64 LYS HA H 4.18 . 1 567 . 64 LYS HB2 H 2.05 . 2 568 . 64 LYS HB3 H 2.03 . 2 569 . 64 LYS HE2 H 3.18 . 1 570 . 64 LYS HE3 H 3.18 . 1 571 . 64 LYS N N 121.51 . 1 572 . 64 LYS CA C 58.50 . 1 573 . 64 LYS CB C 30.67 . 1 574 . 65 SER H H 8.43 . 1 575 . 65 SER HA H 4.56 . 1 576 . 65 SER HB2 H 4.17 . 2 577 . 65 SER HB3 H 4.07 . 2 578 . 65 SER N N 111.96 . 1 579 . 65 SER CA C 56.75 . 1 580 . 65 SER CB C 62.72 . 1 581 . 66 CYS H H 8.12 . 1 582 . 66 CYS HA H 3.74 . 1 583 . 66 CYS HB2 H 3.14 . 2 584 . 66 CYS HB3 H 2.61 . 2 585 . 66 CYS N N 124.49 . 1 586 . 66 CYS CA C 60.02 . 1 587 . 66 CYS CB C 25.89 . 1 588 . 67 THR H H 8.91 . 1 589 . 67 THR HA H 4.41 . 1 590 . 67 THR HB H 4.10 . 1 591 . 67 THR HG2 H 1.17 . 1 592 . 67 THR N N 120.37 . 1 593 . 67 THR CA C 61.66 . 1 594 . 67 THR CB C 67.90 . 1 595 . 68 ASN H H 7.75 . 1 596 . 68 ASN HA H 5.24 . 1 597 . 68 ASN HB2 H 2.75 . 1 598 . 68 ASN HB3 H 2.34 . 1 599 . 68 ASN N N 122.59 . 1 600 . 68 ASN CA C 50.34 . 1 601 . 68 ASN CB C 38.90 . 1 602 . 69 PRO HA H 4.51 . 1 603 . 69 PRO HB2 H 2.55 . 2 604 . 69 PRO HB3 H 2.04 . 2 605 . 69 PRO HG2 H 2.19 . 2 606 . 69 PRO HG3 H 2.08 . 2 607 . 69 PRO HD2 H 3.66 . 1 608 . 69 PRO HD3 H 3.66 . 1 609 . 69 PRO CA C 60.93 . 1 610 . 69 PRO CB C 30.42 . 1 611 . 70 THR H H 8.48 . 1 612 . 70 THR HA H 4.49 . 1 613 . 70 THR HB H 4.59 . 1 614 . 70 THR HG2 H 1.37 . 1 615 . 70 THR N N 112.59 . 1 616 . 70 THR CA C 61.00 . 1 617 . 70 THR CB C 70.27 . 1 618 . 71 GLU H H 8.59 . 1 619 . 71 GLU HA H 3.99 . 1 620 . 71 GLU HB2 H 2.16 . 2 621 . 71 GLU HB3 H 2.02 . 2 622 . 71 GLU HG2 H 2.41 . 2 623 . 71 GLU HG3 H 2.35 . 2 624 . 71 GLU N N 124.08 . 1 625 . 71 GLU CA C 60.40 . 1 626 . 71 GLU CB C 27.23 . 1 627 . 72 ASN H H 8.76 . 1 628 . 72 ASN HA H 4.55 . 1 629 . 72 ASN HB2 H 2.87 . 1 630 . 72 ASN HB3 H 2.87 . 1 631 . 72 ASN N N 117.60 . 1 632 . 72 ASN CA C 55.55 . 1 633 . 72 ASN CB C 36.53 . 1 634 . 73 PHE H H 8.06 . 1 635 . 73 PHE HA H 4.51 . 1 636 . 73 PHE HB2 H 3.37 . 2 637 . 73 PHE HB3 H 3.07 . 2 638 . 73 PHE HD1 H 7.23 . 1 639 . 73 PHE HD2 H 7.23 . 1 640 . 73 PHE HE1 H 6.54 . 1 641 . 73 PHE HE2 H 6.54 . 1 642 . 73 PHE N N 121.67 . 1 643 . 73 PHE CA C 60.23 . 1 644 . 73 PHE CB C 38.00 . 1 645 . 74 VAL H H 8.39 . 1 646 . 74 VAL HA H 3.12 . 1 647 . 74 VAL HB H 2.20 . 1 648 . 74 VAL HG1 H 1.12 . 1 649 . 74 VAL HG2 H 0.94 . 1 650 . 74 VAL N N 118.36 . 1 651 . 74 VAL CA C 67.06 . 1 652 . 74 VAL CB C 30.61 . 1 653 . 75 GLN H H 7.92 . 1 654 . 75 GLN HA H 3.93 . 1 655 . 75 GLN HB2 H 2.19 . 1 656 . 75 GLN HB3 H 2.19 . 1 657 . 75 GLN HG2 H 2.51 . 1 658 . 75 GLN HG3 H 2.51 . 1 659 . 75 GLN N N 115.69 . 1 660 . 75 GLN CA C 58.10 . 1 661 . 75 GLN CB C 26.54 . 1 662 . 76 GLU H H 8.34 . 1 663 . 76 GLU HA H 3.94 . 1 664 . 76 GLU HB2 H 2.41 . 2 665 . 76 GLU HB3 H 2.07 . 2 666 . 76 GLU HG2 H 2.15 . 1 667 . 76 GLU HG3 H 2.15 . 1 668 . 76 GLU N N 118.69 . 1 669 . 76 GLU CA C 58.29 . 1 670 . 76 GLU CB C 28.29 . 1 671 . 77 LEU H H 8.83 . 1 672 . 77 LEU HA H 3.88 . 1 673 . 77 LEU HB2 H 1.84 . 2 674 . 77 LEU HB3 H 1.19 . 2 675 . 77 LEU HG H 1.40 . 1 676 . 77 LEU HD1 H 0.80 . 1 677 . 77 LEU HD2 H 0.99 . 1 678 . 77 LEU N N 122.51 . 1 679 . 77 LEU CA C 56.86 . 1 680 . 77 LEU CB C 38.39 . 1 681 . 78 LEU H H 8.32 . 1 682 . 78 LEU HA H 3.85 . 1 683 . 78 LEU HB2 H 1.97 . 2 684 . 78 LEU HB3 H 1.48 . 2 685 . 78 LEU HG H 1.94 . 1 686 . 78 LEU HD1 H 0.75 . 1 687 . 78 LEU HD2 H 0.83 . 1 688 . 78 LEU N N 118.97 . 1 689 . 78 LEU CA C 56.83 . 1 690 . 78 LEU CB C 39.53 . 1 691 . 79 VAL H H 7.33 . 1 692 . 79 VAL HA H 3.42 . 1 693 . 79 VAL HB H 2.10 . 1 694 . 79 VAL HG1 H 1.04 . 1 695 . 79 VAL HG2 H 0.83 . 1 696 . 79 VAL N N 118.55 . 1 697 . 79 VAL CA C 66.16 . 1 698 . 79 VAL CB C 30.01 . 1 699 . 80 LYS H H 7.87 . 1 700 . 80 LYS HA H 3.83 . 1 701 . 80 LYS HB2 H 1.74 . 2 702 . 80 LYS HB3 H 1.64 . 2 703 . 80 LYS HG2 H 1.01 . 2 704 . 80 LYS HG3 H 0.31 . 2 705 . 80 LYS HD2 H 1.08 . 2 706 . 80 LYS HD3 H 0.95 . 2 707 . 80 LYS N N 121.02 . 1 708 . 80 LYS CA C 58.96 . 1 709 . 80 LYS CB C 31.06 . 1 710 . 81 LEU H H 8.51 . 1 711 . 81 LEU HA H 3.93 . 1 712 . 81 LEU HB2 H 1.93 . 2 713 . 81 LEU HB3 H 1.33 . 2 714 . 81 LEU HG H 1.99 . 1 715 . 81 LEU HD1 H 0.78 . 1 716 . 81 LEU HD2 H 0.78 . 1 717 . 81 LEU N N 117.66 . 1 718 . 81 LEU CA C 56.43 . 1 719 . 81 LEU CB C 40.05 . 1 720 . 82 ARG H H 7.43 . 1 721 . 82 ARG HA H 4.79 . 1 722 . 82 ARG HB2 H 1.73 . 1 723 . 82 ARG HB3 H 1.73 . 1 724 . 82 ARG N N 117.78 . 1 725 . 82 ARG CA C 57.15 . 1 726 . 82 ARG CB C 28.24 . 1 727 . 83 GLY H H 7.48 . 1 728 . 83 GLY HA2 H 4.15 . 2 729 . 83 GLY HA3 H 3.77 . 2 730 . 83 GLY N N 104.55 . 1 731 . 83 GLY CA C 43.84 . 1 732 . 84 LEU H H 7.26 . 1 733 . 84 LEU HA H 4.52 . 1 734 . 84 LEU HB2 H 1.93 . 2 735 . 84 LEU HB3 H 1.54 . 2 736 . 84 LEU HG H 1.85 . 1 737 . 84 LEU HD1 H 0.76 . 1 738 . 84 LEU HD2 H 0.90 . 1 739 . 84 LEU N N 120.08 . 1 740 . 84 LEU CA C 53.07 . 1 741 . 84 LEU CB C 41.38 . 1 742 . 85 HIS H H 8.54 . 1 743 . 85 HIS HA H 4.64 . 1 744 . 85 HIS HB2 H 3.18 . 2 745 . 85 HIS HB3 H 3.06 . 2 746 . 85 HIS N N 118.82 . 1 747 . 85 HIS CA C 54.58 . 1 748 . 85 HIS CB C 29.03 . 1 749 . 86 LYS H H 8.19 . 1 750 . 86 LYS HA H 4.10 . 1 751 . 86 LYS HB2 H 1.73 . 1 752 . 86 LYS HB3 H 1.73 . 1 753 . 86 LYS HG2 H 1.66 . 2 754 . 86 LYS HG3 H 1.39 . 2 755 . 86 LYS N N 128.61 . 1 756 . 86 LYS CA C 57.28 . 1 757 . 86 LYS CB C 31.72 . 1 stop_ save_