data_4491 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the apo EH1 domain of mouse Eps15 ; _BMRB_accession_number 4491 _BMRB_flat_file_name bmr4491.str _Entry_type original _Submission_date 1999-06-02 _Accession_date 1999-12-06 _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 Whitehead B. . . 2 Tessari M. . . 3 Carotenuto A. . . 4 'van Bergen en Henegouwen' P. M.P. . 5 Vuister G. W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 616 "13C chemical shifts" 501 "15N chemical shifts" 124 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-06-17 original author . stop_ _Original_release_date 2000-06-17 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Sequence-specific 1H, 13C and 15N assignment of the EH1 domain of mouse Eps15' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99052122 _PubMed_ID 9835057 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Whitehead B. . . 2 Tessari M. . . 3 Versteeg H. H. . 4 'van Delft' S. . . 5 'van Bergen en Henegouwen' P. M.P. . 6 Vuister G. W. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 12 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 465 _Page_last 466 _Year 1998 _Details . loop_ _Keyword EF-hand 'EH domain' Eps15 'S100 protein' 'Solution structure' stop_ save_ ################################## # Molecular system description # ################################## save_system_Eps15 _Saveframe_category molecular_system _Mol_system_name Eps15 _Abbreviation_common Eps15 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Eps15 $Eps15 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Eps15 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Eps15 _Abbreviation_common Eps15 _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 120 _Mol_residue_sequence ; MAAAAQLSLTQLSSGNPVYE KYYRQVEAGNTGRVLALDAA AFLKKSGLPDLILGKIWDLA DTDGKGVLSKQEFFVALRLV ACAQNGLEVSLSSLSLAVPP PRFHDSSSPLLTSGPSVAEL ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 ALA 4 ALA 5 ALA 6 GLN 7 LEU 8 SER 9 LEU 10 THR 11 GLN 12 LEU 13 SER 14 SER 15 GLY 16 ASN 17 PRO 18 VAL 19 TYR 20 GLU 21 LYS 22 TYR 23 TYR 24 ARG 25 GLN 26 VAL 27 GLU 28 ALA 29 GLY 30 ASN 31 THR 32 GLY 33 ARG 34 VAL 35 LEU 36 ALA 37 LEU 38 ASP 39 ALA 40 ALA 41 ALA 42 PHE 43 LEU 44 LYS 45 LYS 46 SER 47 GLY 48 LEU 49 PRO 50 ASP 51 LEU 52 ILE 53 LEU 54 GLY 55 LYS 56 ILE 57 TRP 58 ASP 59 LEU 60 ALA 61 ASP 62 THR 63 ASP 64 GLY 65 LYS 66 GLY 67 VAL 68 LEU 69 SER 70 LYS 71 GLN 72 GLU 73 PHE 74 PHE 75 VAL 76 ALA 77 LEU 78 ARG 79 LEU 80 VAL 81 ALA 82 CYS 83 ALA 84 GLN 85 ASN 86 GLY 87 LEU 88 GLU 89 VAL 90 SER 91 LEU 92 SER 93 SER 94 LEU 95 SER 96 LEU 97 ALA 98 VAL 99 PRO 100 PRO 101 PRO 102 ARG 103 PHE 104 HIS 105 ASP 106 SER 107 SER 108 SER 109 PRO 110 LEU 111 LEU 112 THR 113 SER 114 GLY 115 PRO 116 SER 117 VAL 118 ALA 119 GLU 120 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-04 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 4140 "EH1 domain of mouse Eps15" 100.00 120 100.00 100.00 1.17e-78 PDB 1QJT "Solution Structure Of The Apo Eh1 Domain Of Mouse Epidermal Growth Factor Receptor Substrate 15, Eps15" 81.67 99 100.00 100.00 1.73e-63 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Eps15 'house mouse' 10090 Eukaryota Metazoa Mus musculus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Cell_line _Vector_type _Vector_name $Eps15 'recombinant technology' 'E. Coli' Escherichia Coli . K10 plasmid pGex-2T 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 _Isotopic_labeling $Eps15 1.0 mM [U-15N] 'potassium phosphate' 100 mM . 'sodium chloride' 100 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Eps15 1.0 mM '[U-15N; U-13C]' 'potassium phosphate' 100 mM . 'sodium chloride' 100 mM . H2O 90 % . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityInova _Field_strength 500 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityInova _Field_strength 750 _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 5.2 . n/a temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_ref _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 H2O C 13 proton ppm 43.2 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 external direct . . . . H2O N 15 proton ppm 118.04 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one $sample_two stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chem_shift_ref _Mol_system_component_name Eps15 _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 C C 176.1 . 1 2 . 2 ALA H H 8.33 . 1 3 . 2 ALA HA H 4.24 . 1 4 . 2 ALA HB H 1.38 . 1 5 . 2 ALA C C 177.8 . 1 6 . 2 ALA CA C 52.6 . 1 7 . 2 ALA CB C 18.7 . 1 8 . 2 ALA N N 125.6 . 1 9 . 3 ALA H H 8.22 . 1 10 . 3 ALA HA H 4.18 . 1 11 . 3 ALA HB H 1.39 . 1 12 . 3 ALA C C 178.3 . 1 13 . 3 ALA CA C 52.6 . 1 14 . 3 ALA CB C 18.9 . 1 15 . 3 ALA N N 123.2 . 1 16 . 4 ALA H H 8.27 . 1 17 . 4 ALA HA H 4.18 . 1 18 . 4 ALA HB H 1.39 . 1 19 . 4 ALA C C 178.0 . 1 20 . 4 ALA CA C 52.9 . 1 21 . 4 ALA CB C 18.6 . 1 22 . 4 ALA N N 122.2 . 1 23 . 5 ALA H H 7.98 . 1 24 . 5 ALA HA H 4.22 . 1 25 . 5 ALA HB H 1.39 . 1 26 . 5 ALA C C 178.0 . 1 27 . 5 ALA CA C 52.8 . 1 28 . 5 ALA CB C 18.7 . 1 29 . 5 ALA N N 120.4 . 1 30 . 6 GLN H H 8.01 . 1 31 . 6 GLN HA H 4.26 . 1 32 . 6 GLN HB2 H 1.95 . 2 33 . 6 GLN HB3 H 2.12 . 2 34 . 6 GLN HG2 H 2.34 . 2 35 . 6 GLN HE21 H 6.81 . 2 36 . 6 GLN HE22 H 7.47 . 2 37 . 6 GLN C C 175.9 . 1 38 . 6 GLN CA C 55.4 . 1 39 . 6 GLN CB C 28.8 . 1 40 . 6 GLN CG C 33.5 . 1 41 . 6 GLN CD C 180.5 . 1 42 . 6 GLN N N 117.6 . 1 43 . 6 GLN NE2 N 112.4 . 1 44 . 7 LEU H H 7.75 . 1 45 . 7 LEU HA H 4.43 . 1 46 . 7 LEU HB2 H 1.31 . 2 47 . 7 LEU HB3 H 1.59 . 2 48 . 7 LEU HG H 1.60 . 1 49 . 7 LEU HD1 H 0.81 . 1 50 . 7 LEU HD2 H 0.74 . 1 51 . 7 LEU C C 176.8 . 1 52 . 7 LEU CA C 54.5 . 1 53 . 7 LEU CB C 42.5 . 1 54 . 7 LEU CG C 27.3 . 1 55 . 7 LEU CD1 C 26.1 . 1 56 . 7 LEU CD2 C 23.0 . 1 57 . 7 LEU N N 122.5 . 1 58 . 8 SER H H 8.76 . 1 59 . 8 SER HA H 4.51 . 1 60 . 8 SER HB2 H 3.95 . 2 61 . 8 SER HB3 H 4.31 . 2 62 . 8 SER C C 175.3 . 1 63 . 8 SER CA C 56.6 . 1 64 . 8 SER CB C 64.9 . 1 65 . 8 SER N N 117.8 . 1 66 . 9 LEU H H 8.56 . 1 67 . 9 LEU HA H 3.97 . 1 68 . 9 LEU HB2 H 1.38 . 2 69 . 9 LEU HB3 H 1.76 . 2 70 . 9 LEU HG H 1.67 . 1 71 . 9 LEU HD1 H 0.57 . 1 72 . 9 LEU HD2 H 0.02 . 1 73 . 9 LEU C C 179.9 . 1 74 . 9 LEU CA C 58.3 . 1 75 . 9 LEU CB C 40.2 . 1 76 . 9 LEU CG C 26.2 . 1 77 . 9 LEU CD1 C 25.5 . 1 78 . 9 LEU CD2 C 21.4 . 1 79 . 9 LEU N N 119.8 . 1 80 . 10 THR H H 7.98 . 1 81 . 10 THR HA H 3.96 . 1 82 . 10 THR HB H 4.00 . 1 83 . 10 THR HG2 H 1.14 . 1 84 . 10 THR C C 177.0 . 1 85 . 10 THR CA C 65.5 . 1 86 . 10 THR CB C 68.2 . 1 87 . 10 THR CG2 C 21.7 . 1 88 . 10 THR N N 112.5 . 1 89 . 11 GLN H H 7.82 . 1 90 . 11 GLN HA H 4.02 . 1 91 . 11 GLN HB2 H 2.01 . 2 92 . 11 GLN HB3 H 2.25 . 2 93 . 11 GLN HG2 H 2.36 . 2 94 . 11 GLN HE21 H 6.83 . 2 95 . 11 GLN HE22 H 7.51 . 2 96 . 11 GLN C C 179.8 . 1 97 . 11 GLN CA C 58.6 . 1 98 . 11 GLN CB C 28.5 . 1 99 . 11 GLN CG C 34.5 . 1 100 . 11 GLN CD C 179.9 . 1 101 . 11 GLN N N 122.3 . 1 102 . 11 GLN NE2 N 112.2 . 1 103 . 12 LEU H H 8.36 . 1 104 . 12 LEU HA H 4.01 . 1 105 . 12 LEU HB2 H 1.37 . 2 106 . 12 LEU HB3 H 2.20 . 2 107 . 12 LEU HG H 1.61 . 1 108 . 12 LEU HD1 H 0.95 . 1 109 . 12 LEU HD2 H 0.94 . 1 110 . 12 LEU C C 176.9 . 1 111 . 12 LEU CA C 57.3 . 1 112 . 12 LEU CB C 43.4 . 1 113 . 12 LEU CG C 27.4 . 1 114 . 12 LEU CD1 C 26.9 . 1 115 . 12 LEU CD2 C 24.7 . 1 116 . 12 LEU N N 120.0 . 1 117 . 13 SER H H 7.99 . 1 118 . 13 SER HA H 2.47 . 1 119 . 13 SER HB2 H 3.23 . 2 120 . 13 SER HB3 H 3.88 . 2 121 . 13 SER C C 177.7 . 1 122 . 13 SER CA C 56.8 . 1 123 . 13 SER CB C 65.7 . 1 124 . 13 SER N N 108.9 . 1 125 . 14 SER H H 7.83 . 1 126 . 14 SER HA H 4.16 . 1 127 . 14 SER HB2 H 4.09 . 2 128 . 14 SER HB3 H 4.27 . 2 129 . 14 SER C C 174.8 . 1 130 . 14 SER CA C 59.2 . 1 131 . 14 SER CB C 62.2 . 1 132 . 14 SER N N 118.3 . 1 133 . 15 GLY H H 8.44 . 1 134 . 15 GLY HA2 H 4.05 . 2 135 . 15 GLY HA3 H 3.62 . 2 136 . 15 GLY C C 173.8 . 1 137 . 15 GLY CA C 45.0 . 1 138 . 15 GLY N N 107.2 . 1 139 . 16 ASN H H 7.84 . 1 140 . 16 ASN HA H 5.01 . 1 141 . 16 ASN HB2 H 2.85 . 2 142 . 16 ASN HB3 H 3.27 . 2 143 . 16 ASN HD21 H 7.39 . 2 144 . 16 ASN HD22 H 7.98 . 2 145 . 16 ASN CA C 51.2 . 1 146 . 16 ASN CB C 40.0 . 1 147 . 16 ASN N N 122.5 . 1 148 . 16 ASN ND2 N 113.8 . 1 149 . 17 PRO HA H 4.60 . 1 150 . 17 PRO HB2 H 2.04 . 2 151 . 17 PRO HB3 H 2.46 . 2 152 . 17 PRO HG2 H 2.04 . 2 153 . 17 PRO HD2 H 3.88 . 2 154 . 17 PRO HD3 H 4.19 . 2 155 . 17 PRO C C 177.7 . 1 156 . 17 PRO CA C 64.0 . 1 157 . 17 PRO CB C 32.5 . 1 158 . 17 PRO CG C 26.7 . 1 159 . 17 PRO CD C 51.9 . 1 160 . 18 VAL H H 8.64 . 1 161 . 18 VAL HA H 3.74 . 1 162 . 18 VAL HB H 1.96 . 1 163 . 18 VAL HG1 H 0.92 . 1 164 . 18 VAL HG2 H 0.81 . 1 165 . 18 VAL C C 176.1 . 1 166 . 18 VAL CA C 64.4 . 1 167 . 18 VAL CB C 31.0 . 1 168 . 18 VAL CG1 C 20.4 . 1 169 . 18 VAL CG2 C 20.4 . 1 170 . 18 VAL N N 118.0 . 1 171 . 19 TYR H H 7.30 . 1 172 . 19 TYR HA H 3.69 . 1 173 . 19 TYR HB2 H 1.32 . 2 174 . 19 TYR HB3 H 2.68 . 2 175 . 19 TYR HD1 H 6.55 . 1 176 . 19 TYR HE1 H 6.72 . 1 177 . 19 TYR C C 177.1 . 1 178 . 19 TYR CA C 62.4 . 1 179 . 19 TYR CB C 37.1 . 1 180 . 19 TYR CD1 C 132.0 . 1 181 . 19 TYR CE1 C 118.4 . 1 182 . 19 TYR N N 120.6 . 1 183 . 20 GLU H H 7.57 . 1 184 . 20 GLU HA H 4.28 . 1 185 . 20 GLU HB2 H 2.18 . 2 186 . 20 GLU HB3 H 2.27 . 2 187 . 20 GLU HG2 H 2.41 . 2 188 . 20 GLU HG3 H 2.53 . 2 189 . 20 GLU C C 178.2 . 1 190 . 20 GLU CA C 58.8 . 1 191 . 20 GLU CB C 29.0 . 1 192 . 20 GLU CG C 34.6 . 1 193 . 20 GLU N N 117.8 . 1 194 . 21 LYS H H 7.46 . 1 195 . 21 LYS HA H 3.91 . 1 196 . 21 LYS HB2 H 1.71 . 2 197 . 21 LYS HG2 H 1.13 . 2 198 . 21 LYS HG3 H 1.47 . 2 199 . 21 LYS HD2 H 1.47 . 2 200 . 21 LYS HD3 H 1.56 . 2 201 . 21 LYS HE2 H 2.86 . 2 202 . 21 LYS C C 179.7 . 1 203 . 21 LYS CA C 59.6 . 1 204 . 21 LYS CB C 31.8 . 1 205 . 21 LYS CG C 24.6 . 1 206 . 21 LYS CD C 29.3 . 1 207 . 21 LYS CE C 41.8 . 1 208 . 21 LYS N N 119.0 . 1 209 . 22 TYR H H 8.17 . 1 210 . 22 TYR HA H 4.40 . 1 211 . 22 TYR HB2 H 2.82 . 2 212 . 22 TYR HB3 H 2.98 . 2 213 . 22 TYR HD1 H 6.89 . 1 214 . 22 TYR HE1 H 6.84 . 1 215 . 22 TYR C C 177.8 . 1 216 . 22 TYR CA C 58.3 . 1 217 . 22 TYR CB C 36.7 . 1 218 . 22 TYR CD1 C 131.7 . 1 219 . 22 TYR CE1 C 117.9 . 1 220 . 22 TYR N N 118.6 . 1 221 . 23 TYR H H 8.28 . 1 222 . 23 TYR HA H 3.89 . 1 223 . 23 TYR HB2 H 3.40 . 2 224 . 23 TYR HD1 H 6.91 . 1 225 . 23 TYR HE1 H 6.49 . 1 226 . 23 TYR C C 176.3 . 1 227 . 23 TYR CA C 60.8 . 1 228 . 23 TYR CB C 38.3 . 1 229 . 23 TYR CD1 C 132.5 . 1 230 . 23 TYR CE1 C 117.8 . 1 231 . 23 TYR N N 118.6 . 1 232 . 24 ARG H H 8.45 . 1 233 . 24 ARG HA H 3.68 . 1 234 . 24 ARG HB2 H 1.87 . 2 235 . 24 ARG HB3 H 1.94 . 2 236 . 24 ARG HG2 H 1.77 . 2 237 . 24 ARG HG3 H 1.96 . 2 238 . 24 ARG HD2 H 3.18 . 2 239 . 24 ARG HD3 H 3.26 . 2 240 . 24 ARG HE H 7.68 . 1 241 . 24 ARG C C 178.6 . 1 242 . 24 ARG CA C 58.1 . 1 243 . 24 ARG CB C 29.4 . 1 244 . 24 ARG CG C 27.4 . 1 245 . 24 ARG CD C 42.8 . 1 246 . 24 ARG N N 117.4 . 1 247 . 24 ARG NE N 85.2 . 1 248 . 25 GLN H H 7.46 . 1 249 . 25 GLN HA H 4.02 . 1 250 . 25 GLN HB2 H 2.06 . 2 251 . 25 GLN HB3 H 2.21 . 2 252 . 25 GLN HG2 H 2.35 . 2 253 . 25 GLN HG3 H 2.57 . 2 254 . 25 GLN HE21 H 6.91 . 2 255 . 25 GLN HE22 H 7.32 . 2 256 . 25 GLN C C 177.4 . 1 257 . 25 GLN CA C 58.0 . 1 258 . 25 GLN CB C 28.5 . 1 259 . 25 GLN CG C 34.1 . 1 260 . 25 GLN CD C 180.0 . 1 261 . 25 GLN N N 116.4 . 1 262 . 25 GLN NE2 N 109.9 . 1 263 . 26 VAL H H 6.98 . 1 264 . 26 VAL HA H 4.16 . 1 265 . 26 VAL HB H 1.67 . 1 266 . 26 VAL HG1 H 0.44 . 1 267 . 26 VAL HG2 H 0.12 . 1 268 . 26 VAL C C 175.0 . 1 269 . 26 VAL CA C 61.1 . 1 270 . 26 VAL CB C 32.2 . 1 271 . 26 VAL CG1 C 21.8 . 1 272 . 26 VAL CG2 C 20.5 . 1 273 . 26 VAL N N 110.9 . 1 274 . 27 GLU H H 7.44 . 1 275 . 27 GLU HA H 3.61 . 1 276 . 27 GLU HB2 H 1.17 . 2 277 . 27 GLU HB3 H 1.45 . 2 278 . 27 GLU HG2 H 2.00 . 2 279 . 27 GLU HG3 H 2.08 . 2 280 . 27 GLU C C 175.0 . 1 281 . 27 GLU CA C 56.2 . 1 282 . 27 GLU CB C 27.8 . 1 283 . 27 GLU CG C 32.6 . 1 284 . 27 GLU N N 123.3 . 1 285 . 28 ALA H H 8.46 . 1 286 . 28 ALA HA H 4.41 . 1 287 . 28 ALA HB H 1.33 . 1 288 . 28 ALA C C 177.1 . 1 289 . 28 ALA CA C 51.2 . 1 290 . 28 ALA CB C 16.6 . 1 291 . 28 ALA N N 127.9 . 1 292 . 29 GLY H H 8.64 . 1 293 . 29 GLY HA2 H 3.90 . 2 294 . 29 GLY HA3 H 3.79 . 2 295 . 29 GLY C C 173.5 . 1 296 . 29 GLY CA C 46.6 . 1 297 . 29 GLY N N 115.6 . 1 298 . 30 ASN H H 8.67 . 1 299 . 30 ASN HA H 5.00 . 1 300 . 30 ASN HB2 H 2.75 . 2 301 . 30 ASN HB3 H 2.90 . 2 302 . 30 ASN HD21 H 6.88 . 2 303 . 30 ASN HD22 H 7.59 . 2 304 . 30 ASN C C 177.3 . 1 305 . 30 ASN CA C 52.1 . 1 306 . 30 ASN CB C 38.1 . 1 307 . 30 ASN CG C 178.0 . 1 308 . 30 ASN N N 122.7 . 1 309 . 30 ASN ND2 N 112.7 . 1 310 . 31 THR H H 8.19 . 1 311 . 31 THR HA H 4.20 . 1 312 . 31 THR HB H 4.34 . 1 313 . 31 THR HG2 H 1.35 . 1 314 . 31 THR C C 176.6 . 1 315 . 31 THR CA C 63.3 . 1 316 . 31 THR CB C 71.0 . 1 317 . 31 THR CG2 C 20.9 . 1 318 . 31 THR N N 108.6 . 1 319 . 32 GLY H H 8.92 . 1 320 . 32 GLY HA2 H 4.11 . 2 321 . 32 GLY HA3 H 3.95 . 2 322 . 32 GLY C C 173.9 . 1 323 . 32 GLY CA C 45.5 . 1 324 . 32 GLY N N 110.9 . 1 325 . 33 ARG H H 7.64 . 1 326 . 33 ARG HA H 4.91 . 1 327 . 33 ARG HB2 H 1.67 . 2 328 . 33 ARG HG2 H 1.52 . 2 329 . 33 ARG HD2 H 3.08 . 2 330 . 33 ARG HE H 7.16 . 1 331 . 33 ARG C C 174.0 . 1 332 . 33 ARG CA C 54.2 . 1 333 . 33 ARG CB C 32.9 . 1 334 . 33 ARG CG C 26.7 . 1 335 . 33 ARG CD C 43.4 . 1 336 . 33 ARG N N 118.1 . 1 337 . 33 ARG NE N 84.9 . 1 338 . 34 VAL H H 8.77 . 1 339 . 34 VAL HA H 4.13 . 1 340 . 34 VAL HB H 1.90 . 1 341 . 34 VAL HG1 H 0.67 . 1 342 . 34 VAL HG2 H 0.48 . 1 343 . 34 VAL C C 175.3 . 1 344 . 34 VAL CA C 60.7 . 1 345 . 34 VAL CB C 33.8 . 1 346 . 34 VAL CG1 C 21.4 . 1 347 . 34 VAL CG2 C 20.4 . 1 348 . 34 VAL N N 119.1 . 1 349 . 35 LEU H H 9.66 . 1 350 . 35 LEU HA H 4.54 . 1 351 . 35 LEU HB2 H 1.71 . 2 352 . 35 LEU HB3 H 1.87 . 2 353 . 35 LEU HG H 1.82 . 1 354 . 35 LEU HD1 H 0.97 . 1 355 . 35 LEU HD2 H 0.91 . 1 356 . 35 LEU C C 176.7 . 1 357 . 35 LEU CA C 55.4 . 1 358 . 35 LEU CB C 40.9 . 1 359 . 35 LEU CG C 27.2 . 1 360 . 35 LEU CD1 C 24.7 . 1 361 . 35 LEU CD2 C 22.8 . 1 362 . 35 LEU N N 127.9 . 1 363 . 36 ALA H H 8.36 . 1 364 . 36 ALA HA H 3.88 . 1 365 . 36 ALA HB H 1.30 . 1 366 . 36 ALA C C 179.5 . 1 367 . 36 ALA CA C 56.0 . 1 368 . 36 ALA CB C 18.0 . 1 369 . 36 ALA N N 125.6 . 1 370 . 37 LEU H H 8.57 . 1 371 . 37 LEU HA H 3.98 . 1 372 . 37 LEU HB2 H 1.48 . 2 373 . 37 LEU HB3 H 1.65 . 2 374 . 37 LEU HG H 1.64 . 1 375 . 37 LEU HD1 H 0.84 . 1 376 . 37 LEU HD2 H 0.89 . 1 377 . 37 LEU C C 179.7 . 1 378 . 37 LEU CA C 58.0 . 1 379 . 37 LEU CB C 41.6 . 1 380 . 37 LEU CG C 26.9 . 1 381 . 37 LEU CD1 C 23.7 . 1 382 . 37 LEU CD2 C 24.5 . 1 383 . 37 LEU N N 116.5 . 1 384 . 38 ASP H H 6.79 . 1 385 . 38 ASP HA H 4.51 . 1 386 . 38 ASP HB2 H 2.62 . 2 387 . 38 ASP HB3 H 2.82 . 2 388 . 38 ASP C C 179.1 . 1 389 . 38 ASP CA C 56.2 . 1 390 . 38 ASP CB C 40.0 . 1 391 . 38 ASP N N 117.9 . 1 392 . 39 ALA H H 8.55 . 1 393 . 39 ALA HA H 4.08 . 1 394 . 39 ALA HB H 1.66 . 1 395 . 39 ALA C C 179.8 . 1 396 . 39 ALA CA C 55.1 . 1 397 . 39 ALA CB C 18.6 . 1 398 . 39 ALA N N 122.1 . 1 399 . 40 ALA H H 8.70 . 1 400 . 40 ALA HA H 4.04 . 1 401 . 40 ALA HB H 1.18 . 1 402 . 40 ALA C C 180.1 . 1 403 . 40 ALA CA C 55.3 . 1 404 . 40 ALA CB C 17.3 . 1 405 . 40 ALA N N 120.2 . 1 406 . 41 ALA H H 7.51 . 1 407 . 41 ALA HA H 4.07 . 1 408 . 41 ALA HB H 1.53 . 1 409 . 41 ALA C C 180.0 . 1 410 . 41 ALA CA C 54.6 . 1 411 . 41 ALA CB C 17.8 . 1 412 . 41 ALA N N 119.1 . 1 413 . 42 PHE H H 7.76 . 1 414 . 42 PHE HA H 4.06 . 1 415 . 42 PHE HB2 H 3.03 . 2 416 . 42 PHE HB3 H 3.17 . 2 417 . 42 PHE HD1 H 6.79 . 1 418 . 42 PHE HE1 H 6.23 . 1 419 . 42 PHE C C 177.7 . 1 420 . 42 PHE CA C 61.3 . 1 421 . 42 PHE CB C 39.7 . 1 422 . 42 PHE CD1 C 130.4 . 1 423 . 42 PHE CE1 C 129.8 . 1 424 . 42 PHE N N 118.9 . 1 425 . 43 LEU H H 8.84 . 1 426 . 43 LEU HA H 3.99 . 1 427 . 43 LEU HB2 H 1.64 . 2 428 . 43 LEU HB3 H 2.12 . 2 429 . 43 LEU HG H 2.22 . 1 430 . 43 LEU HD1 H 0.99 . 1 431 . 43 LEU HD2 H 0.82 . 1 432 . 43 LEU C C 180.3 . 1 433 . 43 LEU CA C 57.9 . 1 434 . 43 LEU CB C 40.9 . 1 435 . 43 LEU CG C 27.4 . 1 436 . 43 LEU CD1 C 24.6 . 1 437 . 43 LEU CD2 C 22.6 . 1 438 . 43 LEU N N 117.1 . 1 439 . 44 LYS H H 7.77 . 1 440 . 44 LYS HA H 4.08 . 1 441 . 44 LYS HB2 H 1.96 . 2 442 . 44 LYS HG2 H 1.51 . 2 443 . 44 LYS HG3 H 1.66 . 2 444 . 44 LYS HD2 H 1.68 . 2 445 . 44 LYS HE2 H 2.95 . 2 446 . 44 LYS C C 178.9 . 1 447 . 44 LYS CA C 59.0 . 1 448 . 44 LYS CB C 32.0 . 1 449 . 44 LYS CG C 25.2 . 1 450 . 44 LYS CD C 29.0 . 1 451 . 44 LYS CE C 41.8 . 1 452 . 44 LYS N N 120.2 . 1 453 . 45 LYS H H 7.89 . 1 454 . 45 LYS HA H 4.26 . 1 455 . 45 LYS HB2 H 1.91 . 2 456 . 45 LYS HB3 H 2.11 . 2 457 . 45 LYS HG2 H 1.43 . 2 458 . 45 LYS HG3 H 1.64 . 2 459 . 45 LYS HD2 H 1.53 . 2 460 . 45 LYS HD3 H 1.62 . 2 461 . 45 LYS HE2 H 2.91 . 2 462 . 45 LYS C C 177.5 . 1 463 . 45 LYS CA C 57.9 . 1 464 . 45 LYS CB C 30.6 . 1 465 . 45 LYS CG C 25.5 . 1 466 . 45 LYS CD C 29.1 . 1 467 . 45 LYS CE C 41.9 . 1 468 . 45 LYS N N 118.7 . 1 469 . 46 SER H H 8.08 . 1 470 . 46 SER HA H 4.03 . 1 471 . 46 SER HB2 H 3.58 . 2 472 . 46 SER HB3 H 3.81 . 2 473 . 46 SER HG H 4.94 . 1 474 . 46 SER C C 175.8 . 1 475 . 46 SER CA C 59.5 . 1 476 . 46 SER CB C 65.1 . 1 477 . 46 SER N N 114.5 . 1 478 . 47 GLY H H 7.74 . 1 479 . 47 GLY HA2 H 4.15 . 2 480 . 47 GLY HA3 H 3.85 . 2 481 . 47 GLY C C 174.1 . 1 482 . 47 GLY CA C 45.5 . 1 483 . 47 GLY N N 109.2 . 1 484 . 48 LEU H H 7.36 . 1 485 . 48 LEU HA H 4.51 . 1 486 . 48 LEU HB2 H 1.15 . 2 487 . 48 LEU HB3 H 1.53 . 2 488 . 48 LEU HD1 H 0.93 . 1 489 . 48 LEU HD2 H 0.87 . 1 490 . 48 LEU CA C 52.8 . 1 491 . 48 LEU CB C 41.5 . 1 492 . 48 LEU CG C 27.0 . 1 493 . 48 LEU CD1 C 27.1 . 1 494 . 48 LEU CD2 C 22.7 . 1 495 . 48 LEU N N 120.5 . 1 496 . 49 PRO HA H 4.53 . 1 497 . 49 PRO HB2 H 1.92 . 2 498 . 49 PRO HB3 H 2.53 . 2 499 . 49 PRO HG2 H 2.08 . 2 500 . 49 PRO HG3 H 2.16 . 2 501 . 49 PRO HD2 H 3.41 . 2 502 . 49 PRO HD3 H 3.96 . 2 503 . 49 PRO C C 177.5 . 1 504 . 49 PRO CA C 62.0 . 1 505 . 49 PRO CB C 32.5 . 1 506 . 49 PRO CG C 27.5 . 1 507 . 49 PRO CD C 50.3 . 1 508 . 50 ASP H H 8.79 . 1 509 . 50 ASP HA H 4.29 . 1 510 . 50 ASP HB2 H 2.63 . 2 511 . 50 ASP C C 178.6 . 1 512 . 50 ASP CA C 57.8 . 1 513 . 50 ASP CB C 39.9 . 1 514 . 50 ASP N N 123.5 . 1 515 . 51 LEU H H 8.82 . 1 516 . 51 LEU HA H 4.13 . 1 517 . 51 LEU HB2 H 1.51 . 2 518 . 51 LEU HB3 H 1.75 . 2 519 . 51 LEU HG H 1.64 . 1 520 . 51 LEU HD1 H 0.94 . 1 521 . 51 LEU HD2 H 0.92 . 1 522 . 51 LEU C C 180.0 . 1 523 . 51 LEU CA C 58.1 . 1 524 . 51 LEU CB C 42.2 . 1 525 . 51 LEU CG C 26.9 . 1 526 . 51 LEU CD1 C 24.3 . 1 527 . 51 LEU CD2 C 24.0 . 1 528 . 51 LEU N N 119.5 . 1 529 . 52 ILE H H 6.91 . 1 530 . 52 ILE HA H 3.90 . 1 531 . 52 ILE HB H 2.01 . 1 532 . 52 ILE HG12 H 1.42 . 1 533 . 52 ILE HG13 H 1.63 . 1 534 . 52 ILE HG2 H 0.96 . 1 535 . 52 ILE HD1 H 0.86 . 1 536 . 52 ILE C C 177.8 . 1 537 . 52 ILE CA C 62.3 . 1 538 . 52 ILE CB C 36.7 . 1 539 . 52 ILE CG1 C 28.0 . 1 540 . 52 ILE CG2 C 18.0 . 1 541 . 52 ILE CD1 C 10.5 . 1 542 . 52 ILE N N 118.4 . 1 543 . 53 LEU H H 8.03 . 1 544 . 53 LEU HA H 3.95 . 1 545 . 53 LEU HB2 H 1.50 . 2 546 . 53 LEU HB3 H 1.93 . 2 547 . 53 LEU HD1 H 0.89 . 1 548 . 53 LEU HD2 H 0.79 . 1 549 . 53 LEU C C 179.6 . 1 550 . 53 LEU CA C 58.0 . 1 551 . 53 LEU CB C 40.5 . 1 552 . 53 LEU CG C 26.4 . 1 553 . 53 LEU CD1 C 26.1 . 1 554 . 53 LEU CD2 C 22.9 . 1 555 . 53 LEU N N 120.4 . 1 556 . 54 GLY H H 8.53 . 1 557 . 54 GLY HA3 H 3.96 . 2 558 . 54 GLY C C 175.9 . 1 559 . 54 GLY CA C 47.0 . 1 560 . 54 GLY N N 106.5 . 1 561 . 55 LYS H H 7.28 . 1 562 . 55 LYS HA H 4.21 . 1 563 . 55 LYS HB2 H 2.00 . 2 564 . 55 LYS HB3 H 2.05 . 2 565 . 55 LYS HG2 H 1.50 . 2 566 . 55 LYS HG3 H 1.65 . 2 567 . 55 LYS HD2 H 1.74 . 2 568 . 55 LYS HE2 H 3.02 . 2 569 . 55 LYS C C 179.0 . 1 570 . 55 LYS CA C 58.9 . 1 571 . 55 LYS CB C 32.3 . 1 572 . 55 LYS CG C 24.8 . 1 573 . 55 LYS CD C 29.1 . 1 574 . 55 LYS CE C 41.9 . 1 575 . 55 LYS N N 122.8 . 1 576 . 56 ILE H H 8.25 . 1 577 . 56 ILE HA H 3.35 . 1 578 . 56 ILE HB H 1.99 . 1 579 . 56 ILE HG12 H 1.97 . 1 580 . 56 ILE HG2 H 0.80 . 1 581 . 56 ILE HD1 H 0.66 . 1 582 . 56 ILE C C 177.2 . 1 583 . 56 ILE CA C 66.3 . 1 584 . 56 ILE CB C 37.6 . 1 585 . 56 ILE CG1 C 30.3 . 1 586 . 56 ILE CG2 C 15.8 . 1 587 . 56 ILE CD1 C 13.8 . 1 588 . 56 ILE N N 119.3 . 1 589 . 57 TRP H H 8.36 . 1 590 . 57 TRP HA H 4.02 . 1 591 . 57 TRP HB2 H 3.38 . 2 592 . 57 TRP HD1 H 7.32 . 1 593 . 57 TRP HE1 H 10.38 . 1 594 . 57 TRP HE3 H 7.48 . 1 595 . 57 TRP HZ2 H 7.26 . 1 596 . 57 TRP HZ3 H 6.79 . 1 597 . 57 TRP HH2 H 6.97 . 1 598 . 57 TRP C C 177.2 . 1 599 . 57 TRP CA C 60.7 . 1 600 . 57 TRP CB C 28.5 . 1 601 . 57 TRP CD1 C 128.0 . 1 602 . 57 TRP CE3 C 119.2 . 1 603 . 57 TRP CZ2 C 114.3 . 1 604 . 57 TRP CZ3 C 120.2 . 1 605 . 57 TRP CH2 C 123.1 . 1 606 . 57 TRP N N 119.3 . 1 607 . 57 TRP NE1 N 129.9 . 1 608 . 58 ASP H H 7.94 . 1 609 . 58 ASP HA H 4.38 . 1 610 . 58 ASP HB2 H 2.74 . 2 611 . 58 ASP HB3 H 2.88 . 2 612 . 58 ASP C C 178.0 . 1 613 . 58 ASP CA C 56.1 . 1 614 . 58 ASP CB C 40.0 . 1 615 . 58 ASP N N 115.9 . 1 616 . 59 LEU H H 7.60 . 1 617 . 59 LEU HA H 4.12 . 1 618 . 59 LEU HB2 H 1.14 . 2 619 . 59 LEU HB3 H 1.78 . 2 620 . 59 LEU HG H 1.84 . 1 621 . 59 LEU HD1 H 0.76 . 1 622 . 59 LEU HD2 H 0.86 . 1 623 . 59 LEU C C 177.7 . 1 624 . 59 LEU CA C 56.1 . 1 625 . 59 LEU CB C 42.5 . 1 626 . 59 LEU CG C 26.5 . 1 627 . 59 LEU CD1 C 25.9 . 1 628 . 59 LEU CD2 C 22.7 . 1 629 . 59 LEU N N 117.1 . 1 630 . 60 ALA H H 8.07 . 1 631 . 60 ALA HA H 4.12 . 1 632 . 60 ALA HB H 1.18 . 1 633 . 60 ALA C C 176.6 . 1 634 . 60 ALA CA C 53.4 . 1 635 . 60 ALA CB C 18.9 . 1 636 . 60 ALA N N 120.1 . 1 637 . 61 ASP H H 8.00 . 1 638 . 61 ASP HA H 4.56 . 1 639 . 61 ASP HB2 H 1.58 . 2 640 . 61 ASP HB3 H 2.69 . 2 641 . 61 ASP C C 176.7 . 1 642 . 61 ASP CA C 51.1 . 1 643 . 61 ASP CB C 37.1 . 1 644 . 61 ASP N N 114.5 . 1 645 . 62 THR H H 7.97 . 1 646 . 62 THR HA H 3.98 . 1 647 . 62 THR HB H 4.10 . 1 648 . 62 THR HG2 H 1.25 . 1 649 . 62 THR C C 175.8 . 1 650 . 62 THR CA C 64.7 . 1 651 . 62 THR CB C 69.0 . 1 652 . 62 THR CG2 C 21.7 . 1 653 . 62 THR N N 118.4 . 1 654 . 63 ASP H H 8.77 . 1 655 . 63 ASP HA H 4.68 . 1 656 . 63 ASP HB2 H 2.77 . 2 657 . 63 ASP HB3 H 2.87 . 2 658 . 63 ASP C C 177.0 . 1 659 . 63 ASP CA C 53.8 . 1 660 . 63 ASP CB C 40.6 . 1 661 . 63 ASP N N 118.7 . 1 662 . 64 GLY H H 8.14 . 1 663 . 64 GLY HA3 H 3.89 . 2 664 . 64 GLY CA C 46.8 . 1 665 . 64 GLY N N 109.7 . 1 666 . 65 LYS HA H 4.44 . 1 667 . 65 LYS HB2 H 2.00 . 2 668 . 65 LYS HG2 H 1.50 . 2 669 . 65 LYS HD2 H 1.74 . 2 670 . 65 LYS HE2 H 3.05 . 2 671 . 65 LYS C C 178.3 . 1 672 . 65 LYS CA C 56.1 . 1 673 . 65 LYS CB C 33.1 . 1 674 . 65 LYS CG C 24.5 . 1 675 . 65 LYS CD C 28.7 . 1 676 . 65 LYS CE C 41.8 . 1 677 . 66 GLY H H 10.02 . 1 678 . 66 GLY HA2 H 4.20 . 2 679 . 66 GLY HA3 H 3.97 . 2 680 . 66 GLY C C 173.5 . 1 681 . 66 GLY CA C 46.0 . 1 682 . 66 GLY N N 111.4 . 1 683 . 67 VAL H H 7.56 . 1 684 . 67 VAL HA H 4.84 . 1 685 . 67 VAL HB H 1.98 . 1 686 . 67 VAL HG1 H 0.91 . 1 687 . 67 VAL HG2 H 0.89 . 1 688 . 67 VAL C C 174.0 . 1 689 . 67 VAL CA C 60.0 . 1 690 . 67 VAL CB C 34.8 . 1 691 . 67 VAL CG1 C 21.3 . 1 692 . 67 VAL CG2 C 20.1 . 1 693 . 67 VAL N N 118.0 . 1 694 . 68 LEU H H 9.23 . 1 695 . 68 LEU HA H 5.04 . 1 696 . 68 LEU HB2 H 1.70 . 2 697 . 68 LEU HB3 H 1.84 . 2 698 . 68 LEU HG H 1.59 . 1 699 . 68 LEU HD1 H 0.69 . 1 700 . 68 LEU HD2 H 0.42 . 1 701 . 68 LEU C C 177.0 . 1 702 . 68 LEU CA C 53.3 . 1 703 . 68 LEU CB C 44.0 . 1 704 . 68 LEU CG C 27.5 . 1 705 . 68 LEU CD1 C 25.6 . 1 706 . 68 LEU CD2 C 22.1 . 1 707 . 68 LEU N N 124.0 . 1 708 . 69 SER H H 8.79 . 1 709 . 69 SER HA H 4.74 . 1 710 . 69 SER HB2 H 4.03 . 2 711 . 69 SER HB3 H 4.43 . 2 712 . 69 SER C C 174.4 . 1 713 . 69 SER CA C 56.2 . 1 714 . 69 SER CB C 65.5 . 1 715 . 69 SER N N 116.5 . 1 716 . 70 LYS H H 8.62 . 1 717 . 70 LYS HA H 3.60 . 1 718 . 70 LYS HB2 H 1.42 . 2 719 . 70 LYS HG2 H -0.45 . 2 720 . 70 LYS HG3 H 0.12 . 2 721 . 70 LYS HD2 H 0.98 . 2 722 . 70 LYS HD3 H 1.19 . 2 723 . 70 LYS HE2 H 2.18 . 2 724 . 70 LYS HE3 H 2.28 . 2 725 . 70 LYS C C 177.6 . 1 726 . 70 LYS CA C 60.8 . 1 727 . 70 LYS CB C 32.6 . 1 728 . 70 LYS CG C 24.4 . 1 729 . 70 LYS CD C 30.1 . 1 730 . 70 LYS CE C 42.0 . 1 731 . 70 LYS N N 121.4 . 1 732 . 71 GLN H H 8.27 . 1 733 . 71 GLN HA H 3.45 . 1 734 . 71 GLN HB2 H 1.96 . 2 735 . 71 GLN HG2 H 2.22 . 2 736 . 71 GLN HG3 H 2.28 . 2 737 . 71 GLN HE21 H 6.78 . 2 738 . 71 GLN HE22 H 7.37 . 2 739 . 71 GLN C C 177.7 . 1 740 . 71 GLN CA C 60.1 . 1 741 . 71 GLN CB C 27.1 . 1 742 . 71 GLN CG C 32.8 . 1 743 . 71 GLN CD C 178.9 . 1 744 . 71 GLN N N 116.6 . 1 745 . 71 GLN NE2 N 110.3 . 1 746 . 72 GLU H H 7.61 . 1 747 . 72 GLU HA H 3.93 . 1 748 . 72 GLU HB2 H 2.17 . 2 749 . 72 GLU HB3 H 2.33 . 2 750 . 72 GLU HG2 H 2.56 . 2 751 . 72 GLU HG3 H 2.81 . 2 752 . 72 GLU C C 179.0 . 1 753 . 72 GLU CA C 58.7 . 1 754 . 72 GLU CB C 29.7 . 1 755 . 72 GLU CG C 35.6 . 1 756 . 72 GLU N N 117.2 . 1 757 . 73 PHE H H 8.84 . 1 758 . 73 PHE HA H 4.29 . 1 759 . 73 PHE HB2 H 3.12 . 2 760 . 73 PHE HB3 H 3.40 . 2 761 . 73 PHE HD1 H 7.25 . 1 762 . 73 PHE HE1 H 7.04 . 1 763 . 73 PHE HZ H 6.71 . 1 764 . 73 PHE C C 176.6 . 1 765 . 73 PHE CA C 61.8 . 1 766 . 73 PHE CB C 38.9 . 1 767 . 73 PHE CD1 C 130.3 . 1 768 . 73 PHE CE1 C 130.3 . 1 769 . 73 PHE CZ C 130.3 . 1 770 . 73 PHE N N 119.7 . 1 771 . 74 PHE H H 8.97 . 1 772 . 74 PHE HA H 4.37 . 1 773 . 74 PHE HB2 H 3.00 . 2 774 . 74 PHE HB3 H 3.65 . 2 775 . 74 PHE HD1 H 7.38 . 1 776 . 74 PHE HE1 H 7.17 . 1 777 . 74 PHE HZ H 7.07 . 1 778 . 74 PHE C C 177.4 . 1 779 . 74 PHE CA C 61.0 . 1 780 . 74 PHE CB C 38.2 . 1 781 . 74 PHE CD1 C 130.1 . 1 782 . 74 PHE CE1 C 131.4 . 1 783 . 74 PHE CZ C 129.1 . 1 784 . 74 PHE N N 121.3 . 1 785 . 75 VAL H H 8.22 . 1 786 . 75 VAL HA H 3.54 . 1 787 . 75 VAL HB H 2.54 . 1 788 . 75 VAL HG1 H 0.83 . 1 789 . 75 VAL HG2 H 1.12 . 1 790 . 75 VAL C C 177.3 . 1 791 . 75 VAL CA C 67.6 . 1 792 . 75 VAL CB C 30.9 . 1 793 . 75 VAL CG1 C 20.7 . 1 794 . 75 VAL CG2 C 23.8 . 1 795 . 75 VAL N N 120.4 . 1 796 . 76 ALA H H 7.87 . 1 797 . 76 ALA HA H 3.69 . 1 798 . 76 ALA HB H 1.12 . 1 799 . 76 ALA C C 178.9 . 1 800 . 76 ALA CA C 55.4 . 1 801 . 76 ALA CB C 16.2 . 1 802 . 76 ALA N N 120.8 . 1 803 . 77 LEU H H 8.22 . 1 804 . 77 LEU HA H 3.59 . 1 805 . 77 LEU HB2 H 0.78 . 2 806 . 77 LEU HB3 H 2.00 . 2 807 . 77 LEU HG H 1.10 . 1 808 . 77 LEU HD1 H 0.55 . 1 809 . 77 LEU HD2 H 0.55 . 1 810 . 77 LEU C C 178.3 . 1 811 . 77 LEU CA C 57.9 . 1 812 . 77 LEU CB C 42.9 . 1 813 . 77 LEU CG C 26.0 . 1 814 . 77 LEU CD1 C 27.3 . 1 815 . 77 LEU CD2 C 23.3 . 1 816 . 77 LEU N N 115.7 . 1 817 . 78 ARG H H 8.41 . 1 818 . 78 ARG HA H 4.36 . 1 819 . 78 ARG HB2 H 1.76 . 2 820 . 78 ARG HB3 H 2.19 . 2 821 . 78 ARG HG2 H 1.72 . 2 822 . 78 ARG HG3 H 1.76 . 2 823 . 78 ARG HD2 H 3.39 . 2 824 . 78 ARG HD3 H 3.76 . 2 825 . 78 ARG HE H 7.91 . 1 826 . 78 ARG C C 174.1 . 1 827 . 78 ARG CA C 58.5 . 1 828 . 78 ARG CB C 29.7 . 1 829 . 78 ARG CG C 28.8 . 1 830 . 78 ARG CD C 43.2 . 1 831 . 78 ARG N N 120.7 . 1 832 . 78 ARG NE N 87.5 . 1 833 . 79 LEU H H 8.70 . 1 834 . 79 LEU HA H 4.10 . 1 835 . 79 LEU HB2 H 1.18 . 2 836 . 79 LEU HB3 H 2.19 . 2 837 . 79 LEU HG H 1.65 . 1 838 . 79 LEU HD1 H 0.77 . 1 839 . 79 LEU HD2 H 0.76 . 1 840 . 79 LEU C C 179.8 . 1 841 . 79 LEU CA C 58.1 . 1 842 . 79 LEU CB C 42.9 . 1 843 . 79 LEU CG C 27.0 . 1 844 . 79 LEU CD1 C 28.2 . 1 845 . 79 LEU CD2 C 22.5 . 1 846 . 79 LEU N N 120.0 . 1 847 . 80 VAL H H 8.36 . 1 848 . 80 VAL HA H 3.35 . 1 849 . 80 VAL HB H 2.49 . 1 850 . 80 VAL HG1 H 0.55 . 1 851 . 80 VAL HG2 H 1.08 . 1 852 . 80 VAL C C 177.6 . 1 853 . 80 VAL CA C 66.6 . 1 854 . 80 VAL CB C 30.0 . 1 855 . 80 VAL CG1 C 21.2 . 1 856 . 80 VAL CG2 C 23.5 . 1 857 . 80 VAL N N 121.3 . 1 858 . 81 ALA H H 7.71 . 1 859 . 81 ALA HA H 3.90 . 1 860 . 81 ALA HB H 1.64 . 1 861 . 81 ALA C C 181.5 . 1 862 . 81 ALA CA C 55.4 . 1 863 . 81 ALA CB C 17.2 . 1 864 . 81 ALA N N 122.3 . 1 865 . 82 CYS H H 8.62 . 1 866 . 82 CYS HA H 3.97 . 1 867 . 82 CYS HB2 H 2.47 . 2 868 . 82 CYS HB3 H 3.41 . 2 869 . 82 CYS C C 176.5 . 1 870 . 82 CYS CA C 65.1 . 1 871 . 82 CYS CB C 25.4 . 1 872 . 82 CYS N N 117.9 . 1 873 . 83 ALA H H 8.28 . 1 874 . 83 ALA HA H 4.11 . 1 875 . 83 ALA HB H 1.46 . 1 876 . 83 ALA C C 181.4 . 1 877 . 83 ALA CA C 54.4 . 1 878 . 83 ALA CB C 19.0 . 1 879 . 83 ALA N N 121.9 . 1 880 . 84 GLN H H 8.55 . 1 881 . 84 GLN HA H 4.05 . 1 882 . 84 GLN HB2 H 1.90 . 2 883 . 84 GLN HB3 H 2.14 . 2 884 . 84 GLN HG2 H 2.33 . 2 885 . 84 GLN HG3 H 2.70 . 2 886 . 84 GLN HE21 H 6.65 . 2 887 . 84 GLN HE22 H 8.11 . 2 888 . 84 GLN C C 176.7 . 1 889 . 84 GLN CA C 57.5 . 1 890 . 84 GLN CB C 28.7 . 1 891 . 84 GLN CG C 34.7 . 1 892 . 84 GLN CD C 177.5 . 1 893 . 84 GLN N N 115.8 . 1 894 . 84 GLN NE2 N 112.9 . 1 895 . 85 ASN H H 7.56 . 1 896 . 85 ASN HA H 4.96 . 1 897 . 85 ASN HB2 H 2.43 . 2 898 . 85 ASN HB3 H 2.93 . 2 899 . 85 ASN HD21 H 7.30 . 2 900 . 85 ASN HD22 H 8.53 . 2 901 . 85 ASN C C 174.3 . 1 902 . 85 ASN CA C 53.3 . 1 903 . 85 ASN CB C 39.9 . 1 904 . 85 ASN N N 115.6 . 1 905 . 85 ASN ND2 N 119.0 . 1 906 . 86 GLY H H 7.60 . 1 907 . 86 GLY HA2 H 4.01 . 2 908 . 86 GLY HA3 H 3.80 . 2 909 . 86 GLY C C 174.2 . 1 910 . 86 GLY CA C 46.4 . 1 911 . 86 GLY N N 106.1 . 1 912 . 87 LEU H H 8.08 . 1 913 . 87 LEU HA H 4.56 . 1 914 . 87 LEU HB2 H 1.49 . 2 915 . 87 LEU HG H 1.61 . 1 916 . 87 LEU HD1 H 0.96 . 1 917 . 87 LEU HD2 H 0.90 . 1 918 . 87 LEU C C 176.4 . 1 919 . 87 LEU CA C 53.1 . 1 920 . 87 LEU CB C 43.0 . 1 921 . 87 LEU CG C 27.5 . 1 922 . 87 LEU CD1 C 26.2 . 1 923 . 87 LEU CD2 C 23.1 . 1 924 . 87 LEU N N 120.4 . 1 925 . 88 GLU H H 8.34 . 1 926 . 88 GLU HA H 3.94 . 1 927 . 88 GLU HB2 H 1.70 . 2 928 . 88 GLU HB3 H 1.85 . 2 929 . 88 GLU HG2 H 2.10 . 2 930 . 88 GLU HG3 H 2.24 . 2 931 . 88 GLU C C 177.5 . 1 932 . 88 GLU CA C 56.2 . 1 933 . 88 GLU CB C 29.6 . 1 934 . 88 GLU CG C 35.5 . 1 935 . 88 GLU N N 119.6 . 1 936 . 89 VAL H H 8.89 . 1 937 . 89 VAL HA H 3.61 . 1 938 . 89 VAL HB H 2.11 . 1 939 . 89 VAL HG1 H 0.81 . 1 940 . 89 VAL HG2 H 0.96 . 1 941 . 89 VAL C C 173.0 . 1 942 . 89 VAL CA C 62.9 . 1 943 . 89 VAL CB C 29.3 . 1 944 . 89 VAL CG1 C 22.4 . 1 945 . 89 VAL CG2 C 21.6 . 1 946 . 89 VAL N N 126.7 . 1 947 . 90 SER H H 7.16 . 1 948 . 90 SER HA H 4.50 . 1 949 . 90 SER HB2 H 3.42 . 2 950 . 90 SER HB3 H 3.92 . 2 951 . 90 SER C C 174.6 . 1 952 . 90 SER CA C 55.5 . 1 953 . 90 SER CB C 64.2 . 1 954 . 90 SER N N 120.3 . 1 955 . 91 LEU H H 9.29 . 1 956 . 91 LEU HA H 4.13 . 1 957 . 91 LEU HB2 H 1.53 . 2 958 . 91 LEU HB3 H 1.85 . 2 959 . 91 LEU HG H 1.85 . 1 960 . 91 LEU HD1 H 1.00 . 1 961 . 91 LEU HD2 H 0.84 . 1 962 . 91 LEU C C 180.1 . 1 963 . 91 LEU CA C 57.4 . 1 964 . 91 LEU CB C 40.0 . 1 965 . 91 LEU CG C 26.9 . 1 966 . 91 LEU CD1 C 25.1 . 1 967 . 91 LEU CD2 C 22.3 . 1 968 . 91 LEU N N 124.6 . 1 969 . 92 SER H H 8.35 . 1 970 . 92 SER HA H 4.23 . 1 971 . 92 SER HB2 H 3.89 . 2 972 . 92 SER C C 176.3 . 1 973 . 92 SER CA C 60.7 . 1 974 . 92 SER CB C 62.4 . 1 975 . 92 SER N N 114.3 . 1 976 . 93 SER H H 7.62 . 1 977 . 93 SER HA H 4.43 . 1 978 . 93 SER HB2 H 4.15 . 2 979 . 93 SER HB3 H 4.24 . 2 980 . 93 SER C C 175.1 . 1 981 . 93 SER CA C 58.7 . 1 982 . 93 SER CB C 64.2 . 1 983 . 93 SER N N 116.5 . 1 984 . 94 LEU H H 7.41 . 1 985 . 94 LEU HA H 3.83 . 1 986 . 94 LEU HB2 H 1.39 . 2 987 . 94 LEU HB3 H 1.95 . 2 988 . 94 LEU HG H 1.97 . 1 989 . 94 LEU HD1 H 1.03 . 1 990 . 94 LEU HD2 H 0.84 . 1 991 . 94 LEU C C 176.3 . 1 992 . 94 LEU CA C 57.3 . 1 993 . 94 LEU CB C 41.6 . 1 994 . 94 LEU CG C 26.7 . 1 995 . 94 LEU CD1 C 26.7 . 1 996 . 94 LEU CD2 C 22.9 . 1 997 . 94 LEU N N 117.2 . 1 998 . 95 SER H H 7.42 . 1 999 . 95 SER HA H 4.33 . 1 1000 . 95 SER HB2 H 3.83 . 2 1001 . 95 SER HB3 H 3.94 . 2 1002 . 95 SER C C 174.5 . 1 1003 . 95 SER CA C 58.4 . 1 1004 . 95 SER CB C 63.3 . 1 1005 . 95 SER N N 108.7 . 1 1006 . 96 LEU H H 7.33 . 1 1007 . 96 LEU HA H 4.33 . 1 1008 . 96 LEU HB2 H 1.45 . 2 1009 . 96 LEU HB3 H 1.88 . 2 1010 . 96 LEU HG H 1.67 . 1 1011 . 96 LEU HD1 H 1.04 . 1 1012 . 96 LEU HD2 H 0.87 . 1 1013 . 96 LEU C C 178.6 . 1 1014 . 96 LEU CA C 54.0 . 1 1015 . 96 LEU CB C 41.6 . 1 1016 . 96 LEU CG C 27.2 . 1 1017 . 96 LEU CD1 C 25.8 . 1 1018 . 96 LEU CD2 C 22.2 . 1 1019 . 96 LEU N N 123.3 . 1 1020 . 97 ALA H H 8.36 . 1 1021 . 97 ALA HA H 4.16 . 1 1022 . 97 ALA HB H 1.31 . 1 1023 . 97 ALA C C 176.9 . 1 1024 . 97 ALA CA C 52.8 . 1 1025 . 97 ALA CB C 18.1 . 1 1026 . 97 ALA N N 125.3 . 1 1027 . 98 VAL H H 7.54 . 1 1028 . 98 VAL HA H 4.72 . 1 1029 . 98 VAL HB H 2.07 . 1 1030 . 98 VAL HG1 H 0.94 . 1 1031 . 98 VAL HG2 H 0.94 . 1 1032 . 98 VAL CA C 58.3 . 1 1033 . 98 VAL CB C 35.1 . 1 1034 . 98 VAL CG1 C 21.9 . 1 1035 . 98 VAL CG2 C 20.3 . 1 1036 . 98 VAL N N 118.8 . 1 1037 . 99 PRO HA H 4.76 . 1 1038 . 99 PRO HB2 H 1.85 . 2 1039 . 99 PRO HB3 H 2.49 . 2 1040 . 99 PRO HG2 H 1.91 . 2 1041 . 99 PRO HD2 H 3.34 . 2 1042 . 99 PRO HD3 H 3.81 . 2 1043 . 99 PRO CA C 62.0 . 1 1044 . 99 PRO CB C 30.7 . 1 1045 . 99 PRO CG C 27.1 . 1 1046 . 99 PRO CD C 50.9 . 1 1047 . 100 PRO HA H 4.86 . 1 1048 . 100 PRO HB2 H 1.88 . 2 1049 . 100 PRO HB3 H 2.26 . 2 1050 . 100 PRO HG2 H 2.10 . 2 1051 . 100 PRO HD2 H 3.68 . 2 1052 . 100 PRO HD3 H 3.77 . 2 1053 . 100 PRO CA C 61.0 . 1 1054 . 100 PRO CB C 30.2 . 1 1055 . 100 PRO CG C 27.6 . 1 1056 . 100 PRO CD C 49.5 . 1 1057 . 101 PRO HA H 4.13 . 1 1058 . 101 PRO HB2 H 1.57 . 2 1059 . 101 PRO HB3 H 2.01 . 2 1060 . 101 PRO HD2 H 3.44 . 2 1061 . 101 PRO HD3 H 3.68 . 2 1062 . 101 PRO C C 178.7 . 1 1063 . 101 PRO CA C 61.8 . 1 1064 . 101 PRO CB C 31.5 . 1 1065 . 101 PRO CD C 49.0 . 1 1066 . 102 ARG H H 8.69 . 1 1067 . 102 ARG HA H 4.44 . 1 1068 . 102 ARG HB2 H 1.45 . 2 1069 . 102 ARG HB3 H 1.51 . 2 1070 . 102 ARG HG2 H 1.40 . 2 1071 . 102 ARG HG3 H 1.52 . 2 1072 . 102 ARG HD2 H 3.08 . 2 1073 . 102 ARG HD3 H 3.14 . 2 1074 . 102 ARG HE H 7.15 . 1 1075 . 102 ARG C C 174.8 . 1 1076 . 102 ARG CA C 54.7 . 1 1077 . 102 ARG CB C 32.4 . 1 1078 . 102 ARG CG C 27.1 . 1 1079 . 102 ARG CD C 43.0 . 1 1080 . 102 ARG N N 120.5 . 1 1081 . 102 ARG NE N 84.6 . 1 1082 . 103 PHE H H 8.34 . 1 1083 . 103 PHE HA H 4.23 . 1 1084 . 103 PHE HB2 H 2.29 . 2 1085 . 103 PHE HB3 H 2.35 . 2 1086 . 103 PHE HD1 H 6.36 . 1 1087 . 103 PHE HE1 H 6.63 . 1 1088 . 103 PHE HZ H 6.63 . 1 1089 . 103 PHE C C 174.8 . 1 1090 . 103 PHE CA C 56.4 . 1 1091 . 103 PHE CB C 41.2 . 1 1092 . 103 PHE CD1 C 131.9 . 1 1093 . 103 PHE CE1 C 129.7 . 1 1094 . 103 PHE CZ C 127.4 . 1 1095 . 103 PHE N N 119.8 . 1 1096 . 104 HIS H H 8.27 . 1 1097 . 104 HIS HA H 4.74 . 1 1098 . 104 HIS HB2 H 3.19 . 2 1099 . 104 HIS HB3 H 3.26 . 2 1100 . 104 HIS HD2 H 7.28 . 1 1101 . 104 HIS HE1 H 8.51 . 1 1102 . 104 HIS C C 173.8 . 1 1103 . 104 HIS CA C 55.1 . 1 1104 . 104 HIS CB C 29.0 . 1 1105 . 104 HIS CD2 C 119.9 . 1 1106 . 104 HIS CE1 C 136.1 . 1 1107 . 104 HIS N N 119.8 . 1 1108 . 105 ASP H H 8.61 . 1 1109 . 105 ASP HA H 4.67 . 1 1110 . 105 ASP HB2 H 2.66 . 2 1111 . 105 ASP HB3 H 2.77 . 2 1112 . 105 ASP C C 177.2 . 1 1113 . 105 ASP CA C 53.8 . 1 1114 . 105 ASP CB C 41.2 . 1 1115 . 105 ASP N N 122.9 . 1 1116 . 106 SER H H 8.45 . 1 1117 . 106 SER HA H 4.47 . 1 1118 . 106 SER HB2 H 3.89 . 2 1119 . 106 SER C C 174.6 . 1 1120 . 106 SER CA C 58.4 . 1 1121 . 106 SER CB C 63.7 . 1 1122 . 106 SER N N 116.3 . 1 1123 . 107 SER H H 8.46 . 1 1124 . 107 SER HA H 4.49 . 1 1125 . 107 SER HB2 H 3.90 . 2 1126 . 107 SER C C 174.2 . 1 1127 . 107 SER CA C 58.3 . 1 1128 . 107 SER CB C 63.8 . 1 1129 . 107 SER N N 117.6 . 1 1130 . 108 SER H H 8.18 . 1 1131 . 108 SER HA H 4.78 . 1 1132 . 108 SER HB2 H 3.85 . 2 1133 . 108 SER CA C 56.3 . 1 1134 . 108 SER CB C 63.2 . 1 1135 . 108 SER N N 118.5 . 1 1136 . 109 PRO HA H 4.42 . 1 1137 . 109 PRO HB2 H 1.89 . 2 1138 . 109 PRO HB3 H 2.27 . 2 1139 . 109 PRO HG2 H 1.99 . 2 1140 . 109 PRO HD2 H 3.72 . 2 1141 . 109 PRO HD3 H 3.80 . 2 1142 . 109 PRO C C 176.8 . 1 1143 . 109 PRO CA C 62.9 . 1 1144 . 109 PRO CB C 31.7 . 1 1145 . 109 PRO CG C 27.0 . 1 1146 . 109 PRO CD C 50.5 . 1 1147 . 110 LEU H H 8.22 . 1 1148 . 110 LEU HA H 4.28 . 1 1149 . 110 LEU HB2 H 1.58 . 2 1150 . 110 LEU HG H 1.58 . 1 1151 . 110 LEU HD1 H 0.88 . 1 1152 . 110 LEU HD2 H 0.86 . 1 1153 . 110 LEU C C 177.3 . 1 1154 . 110 LEU CA C 55.2 . 1 1155 . 110 LEU CB C 42.0 . 1 1156 . 110 LEU CG C 27.1 . 1 1157 . 110 LEU CD1 C 24.7 . 1 1158 . 110 LEU CD2 C 23.3 . 1 1159 . 110 LEU N N 121.7 . 1 1160 . 111 LEU H H 8.20 . 1 1161 . 111 LEU HA H 4.43 . 1 1162 . 111 LEU HB2 H 1.60 . 2 1163 . 111 LEU HB3 H 1.66 . 2 1164 . 111 LEU HG H 1.60 . 1 1165 . 111 LEU HD1 H 0.91 . 1 1166 . 111 LEU HD2 H 0.84 . 1 1167 . 111 LEU C C 177.5 . 1 1168 . 111 LEU CA C 54.7 . 1 1169 . 111 LEU CB C 42.1 . 1 1170 . 111 LEU CG C 26.8 . 1 1171 . 111 LEU CD1 C 24.7 . 1 1172 . 111 LEU CD2 C 23.2 . 1 1173 . 111 LEU N N 123.0 . 1 1174 . 112 THR H H 8.07 . 1 1175 . 112 THR HA H 4.39 . 1 1176 . 112 THR HB H 4.26 . 1 1177 . 112 THR HG2 H 1.17 . 1 1178 . 112 THR C C 174.5 . 1 1179 . 112 THR CA C 61.3 . 1 1180 . 112 THR CB C 69.6 . 1 1181 . 112 THR CG2 C 21.1 . 1 1182 . 112 THR N N 114.1 . 1 1183 . 113 SER H H 8.26 . 1 1184 . 113 SER HA H 4.51 . 1 1185 . 113 SER HB2 H 3.88 . 2 1186 . 113 SER C C 174.5 . 1 1187 . 113 SER CA C 58.0 . 1 1188 . 113 SER CB C 63.8 . 1 1189 . 113 SER N N 117.5 . 1 1190 . 114 GLY H H 8.23 . 1 1191 . 114 GLY HA2 H 4.14 . 2 1192 . 114 GLY HA3 H 4.10 . 2 1193 . 114 GLY CA C 44.1 . 1 1194 . 114 GLY N N 110.6 . 1 1195 . 115 PRO HA H 4.47 . 1 1196 . 115 PRO HB2 H 2.00 . 2 1197 . 115 PRO HB3 H 2.26 . 2 1198 . 115 PRO HG2 H 2.00 . 2 1199 . 115 PRO HD2 H 3.61 . 2 1200 . 115 PRO C C 176.2 . 1 1201 . 115 PRO CA C 63.0 . 1 1202 . 115 PRO CB C 31.9 . 1 1203 . 115 PRO CG C 26.7 . 1 1204 . 115 PRO CD C 49.6 . 1 1205 . 116 SER H H 8.45 . 1 1206 . 116 SER HA H 4.48 . 1 1207 . 116 SER HB2 H 3.88 . 2 1208 . 116 SER C C 176.6 . 1 1209 . 116 SER CA C 58.1 . 1 1210 . 116 SER CB C 63.7 . 1 1211 . 116 SER N N 116.3 . 1 1212 . 117 VAL H H 8.11 . 1 1213 . 117 VAL HA H 4.16 . 1 1214 . 117 VAL HB H 2.08 . 1 1215 . 117 VAL HG1 H 0.91 . 1 1216 . 117 VAL HG2 H 0.90 . 1 1217 . 117 VAL C C 175.8 . 1 1218 . 117 VAL CA C 61.8 . 1 1219 . 117 VAL CB C 32.8 . 1 1220 . 117 VAL CG1 C 20.7 . 1 1221 . 117 VAL CG2 C 19.9 . 1 1222 . 117 VAL N N 121.5 . 1 1223 . 118 ALA H H 8.27 . 1 1224 . 118 ALA HA H 4.32 . 1 1225 . 118 ALA HB H 1.37 . 1 1226 . 118 ALA C C 178.2 . 1 1227 . 118 ALA CA C 52.2 . 1 1228 . 118 ALA CB C 18.8 . 1 1229 . 118 ALA N N 127.2 . 1 1230 . 119 GLU H H 8.25 . 1 1231 . 119 GLU HA H 4.28 . 1 1232 . 119 GLU HB2 H 1.95 . 2 1233 . 119 GLU HB3 H 2.11 . 2 1234 . 119 GLU HG3 H 2.34 . 2 1235 . 119 GLU C C 175.3 . 1 1236 . 119 GLU CA C 55.6 . 1 1237 . 119 GLU N N 120.6 . 1 1238 . 120 LEU H H 7.85 . 1 1239 . 120 LEU HA H 4.19 . 1 1240 . 120 LEU CA C 56.1 . 1 1241 . 120 LEU N N 128.8 . 1 stop_ save_