data_4288 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific 1H, 13C and 15N Assignment and Secondary Structure of the Apo EH2 Domain of Mouse Eps15. ; _BMRB_accession_number 4288 _BMRB_flat_file_name bmr4288.str _Entry_type original _Submission_date 1998-12-21 _Accession_date 1998-12-21 _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 Carotenuto Alfonso . . 2 Tessari Marco . . 3 Whitehead Brian G . 4 Aelen Jan M.A. . 5 'van Bergen en Henegouwen' Paul M.P. . 6 Vuister Geerten W . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 614 "13C chemical shifts" 447 "15N chemical shifts" 98 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-10-06 original author . stop_ _Original_release_date 1999-10-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Carotenuto, A., Tessari, M., Whitehead, B., Aelen, J.M.A., van Bergen en Henegouwen, P.M.P., Vuister, G.W., "Sequence-specific 1H, 13C and 15N Assignment and Secondary Structure of the Apo EH2 Domain of Mouse Eps15," J. Biomol. NMR 14, 97-98 (1999). ; _Citation_title ; Sequence-specific 1H, 13C and 15N Assignment and Secondary Structure of the Apo EH2 Domain of Mouse Eps15 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99311324 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Carotenuto Alfonso . . 2 Tessari Marco . . 3 Whitehead Brian G . 4 Aelen Jan M.A. . 5 'van Bergen en Henegouwen' Paul M.P. . 6 Vuister Geerten W . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 14 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 97 _Page_last 98 _Year 1999 _Details . loop_ _Keyword 'Ca2+ -binding protein' 'EH domain' 'NMR assignments' 'Secondary structure' stop_ save_ ################################## # Molecular system description # ################################## save_system_mEps15-EH2 _Saveframe_category molecular_system _Mol_system_name mEps15-EH2 _Abbreviation_common EH2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'mEps15 EH2' $mEps15-EH2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'EH2 domain of mouse Eps15' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_mEps15-EH2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'EH2 domain' _Abbreviation_common EH2 _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 105 _Mol_residue_sequence ; GSELPWAVKSEDKAKYDAIF DSLSPVDGFLSGDKVKPVLL NSKLPVEILGRVWELSDIDH DGKLDRDEFAVAMFLVYCAL EKEPVPMSLPPALVPPSKRK TWVVS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 117 GLY 2 118 SER 3 119 GLU 4 120 LEU 5 121 PRO 6 122 TRP 7 123 ALA 8 124 VAL 9 125 LYS 10 126 SER 11 127 GLU 12 128 ASP 13 129 LYS 14 130 ALA 15 131 LYS 16 132 TYR 17 133 ASP 18 134 ALA 19 135 ILE 20 136 PHE 21 137 ASP 22 138 SER 23 139 LEU 24 140 SER 25 141 PRO 26 142 VAL 27 143 ASP 28 144 GLY 29 145 PHE 30 146 LEU 31 147 SER 32 148 GLY 33 149 ASP 34 150 LYS 35 151 VAL 36 152 LYS 37 153 PRO 38 154 VAL 39 155 LEU 40 156 LEU 41 157 ASN 42 158 SER 43 159 LYS 44 160 LEU 45 161 PRO 46 162 VAL 47 163 GLU 48 164 ILE 49 165 LEU 50 166 GLY 51 167 ARG 52 168 VAL 53 169 TRP 54 170 GLU 55 171 LEU 56 172 SER 57 173 ASP 58 174 ILE 59 175 ASP 60 176 HIS 61 177 ASP 62 178 GLY 63 179 LYS 64 180 LEU 65 181 ASP 66 182 ARG 67 183 ASP 68 184 GLU 69 185 PHE 70 186 ALA 71 187 VAL 72 188 ALA 73 189 MET 74 190 PHE 75 191 LEU 76 192 VAL 77 193 TYR 78 194 CYS 79 195 ALA 80 196 LEU 81 197 GLU 82 198 LYS 83 199 GLU 84 200 PRO 85 201 VAL 86 202 PRO 87 203 MET 88 204 SER 89 205 LEU 90 206 PRO 91 207 PRO 92 208 ALA 93 209 LEU 94 210 VAL 95 211 PRO 96 212 PRO 97 213 SER 98 214 LYS 99 215 ARG 100 216 LYS 101 217 THR 102 218 TRP 103 219 VAL 104 220 VAL 105 221 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2008-01-16 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 SWISS-PROT P42567 'EP15_MOUSE Epidermal growth factor receptorsubstrate 15 (Protein Eps15) (AF-1p protein)' 11.71 897 99 100 4e-54 REF NP_031969.1 'epidermal growth factor receptorpathway substrate 15 [Mus musculus]' 11.71 897 99 100 4e-54 REF NP_001009424.1 'epidermal growth factor receptorpathway substrate 15 [Rattus norvegicus]' 13.26 792 99 100 4e-54 GenBank AAH48783.2 'Epidermal growth factor receptor pathwaysubstrate 15 [Mus musculus]' 11.71 897 99 100 4e-54 GenBank AAA02912.1 eps15 11.71 897 99 100 4e-54 GenBank AAP12672.1 'epidermal growth factor receptor pathwaysubstrate 15 isoform B [Mus musculus]' 13.24 793 99 100 4e-54 GenBank AAP12671.1 'epidermal growth factor receptor pathwaysubstrate 15 isoform B [Rattus norvegicus]' 13.26 792 99 100 4e-54 EMBL CAM23716.1 'epidermal growth factor receptorpathway substrate 15 [Mus musculus]' 11.71 897 99 100 4e-54 DBJ BAF74783.1 'epidermal growth factor receptorpathway substrate 15 [Rattus norvegicus]' 11.71 897 99 100 4e-54 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $mEps15-EH2 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 _Vector_type _Vector_name $mEps15-EH2 '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 $mEps15-EH2 1.5 mM [U-15N] H2O 95 % . D2O 5 % . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $mEps15-EH2 1.5 mM [U-15N,U-13C] H2O 95 % . D2O 5 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer . _Model . _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 . n/a temperature 288 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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_citation_label _Correction_value_citation_label H2O H 1 protons ppm 4.83 internal indirect . . . $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one $sample_two stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'mEps15 EH2' _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 GLY CA C 42.1 . 1 2 . 1 GLY HA2 H 3.98 . 2 3 . 1 GLY HA3 H 3.93 . 2 4 . 2 SER N N 114.8 . 1 5 . 2 SER H H 8.76 . 1 6 . 2 SER CA C 57.0 . 1 7 . 2 SER HA H 4.56 . 1 8 . 2 SER CB C 62.6 . 1 9 . 2 SER HB2 H 3.92 . 1 10 . 2 SER HB3 H 3.92 . 1 11 . 2 SER C C 169.0 . 1 12 . 3 GLU N N 122.1 . 1 13 . 3 GLU H H 8.71 . 1 14 . 3 GLU CA C 54.9 . 1 15 . 3 GLU HA H 4.35 . 1 16 . 3 GLU CB C 28.8 . 1 17 . 3 GLU HB2 H 2.03 . 2 18 . 3 GLU HB3 H 1.98 . 2 19 . 3 GLU CG C 34.2 . 1 20 . 3 GLU HG2 H 2.30 . 1 21 . 3 GLU HG3 H 2.30 . 1 22 . 3 GLU C C 172.9 . 1 23 . 4 LEU N N 124.5 . 1 24 . 4 LEU H H 8.64 . 1 25 . 4 LEU CA C 51.5 . 1 26 . 4 LEU HA H 4.70 . 1 27 . 4 LEU CB C 40.9 . 1 28 . 4 LEU HB2 H 1.68 . 2 29 . 4 LEU HB3 H 1.58 . 2 30 . 4 LEU CG C 25.6 . 1 31 . 4 LEU HG H 1.71 . 1 32 . 4 LEU HD1 H 1.00 . 2 33 . 4 LEU HD2 H 0.92 . 2 34 . 4 LEU CD1 C 23.6 . 1 35 . 4 LEU CD2 C 22.7 . 1 36 . 4 LEU C C 174.9 . 1 37 . 5 PRO CD C 49.5 . 1 38 . 5 PRO CA C 61.5 . 1 39 . 5 PRO HA H 4.54 . 1 40 . 5 PRO CB C 30.6 . 1 41 . 5 PRO HB2 H 2.44 . 2 42 . 5 PRO HB3 H 1.89 . 2 43 . 5 PRO CG C 26.1 . 1 44 . 5 PRO HG2 H 2.12 . 1 45 . 5 PRO HG3 H 2.12 . 1 46 . 5 PRO HD2 H 4.07 . 2 47 . 5 PRO HD3 H 3.72 . 2 48 . 6 TRP N N 121.8 . 1 49 . 6 TRP H H 9.08 . 1 50 . 6 TRP CA C 53.0 . 1 51 . 6 TRP HA H 5.12 . 1 52 . 6 TRP CB C 28.3 . 1 53 . 6 TRP HB2 H 3.53 . 2 54 . 6 TRP HB3 H 2.90 . 2 55 . 6 TRP CE3 C 121.1 . 1 56 . 6 TRP NE1 N 126.1 . 1 57 . 6 TRP HE3 H 7.69 . 1 58 . 6 TRP CZ3 C 117.7 . 1 59 . 6 TRP HE1 H 9.32 . 1 60 . 6 TRP HZ3 H 7.42 . 1 61 . 6 TRP CH2 C 119.9 . 1 62 . 6 TRP HZ2 H 7.11 . 1 63 . 6 TRP HH2 H 6.99 . 1 64 . 6 TRP C C 175.1 . 1 65 . 7 ALA N N 127.4 . 1 66 . 7 ALA H H 8.03 . 1 67 . 7 ALA CA C 52.1 . 1 68 . 7 ALA HA H 3.88 . 1 69 . 7 ALA HB H 0.99 . 1 70 . 7 ALA CB C 17.9 . 1 71 . 7 ALA C C 176.1 . 1 72 . 8 VAL N N 119.5 . 1 73 . 8 VAL H H 8.84 . 1 74 . 8 VAL CA C 60.2 . 1 75 . 8 VAL HA H 3.54 . 1 76 . 8 VAL CB C 28.5 . 1 77 . 8 VAL HB H -0.54 . 1 78 . 8 VAL HG1 H 0.52 . 2 79 . 8 VAL HG2 H 0.00 . 2 80 . 8 VAL CG1 C 20.6 . 1 81 . 8 VAL CG2 C 19.0 . 1 82 . 8 VAL C C 178.4 . 1 83 . 9 LYS N N 126.5 . 1 84 . 9 LYS H H 8.71 . 1 85 . 9 LYS CA C 54.2 . 1 86 . 9 LYS HA H 4.30 . 1 87 . 9 LYS CB C 31.3 . 1 88 . 9 LYS HB2 H 2.12 . 2 89 . 9 LYS HB3 H 1.89 . 2 90 . 9 LYS CG C 23.8 . 1 91 . 9 LYS HG2 H 1.64 . 2 92 . 9 LYS HG3 H 1.59 . 2 93 . 9 LYS CD C 27.6 . 1 94 . 9 LYS HD2 H 1.76 . 1 95 . 9 LYS HD3 H 1.76 . 1 96 . 9 LYS CE C 40.9 . 1 97 . 9 LYS HE2 H 3.09 . 1 98 . 9 LYS HE3 H 3.09 . 1 99 . 9 LYS C C 172.7 . 1 100 . 10 SER N N 117.4 . 1 101 . 10 SER H H 8.97 . 1 102 . 10 SER CA C 61.2 . 1 103 . 10 SER HA H 4.09 . 1 104 . 10 SER CB C 61.2 . 1 105 . 10 SER HB2 H 4.00 . 1 106 . 10 SER HB3 H 4.00 . 1 107 . 10 SER C C 177.2 . 1 108 . 11 GLU N N 120.3 . 1 109 . 11 GLU H H 9.51 . 1 110 . 11 GLU CA C 58.3 . 1 111 . 11 GLU HA H 4.12 . 1 112 . 11 GLU CB C 27.1 . 1 113 . 11 GLU HB2 H 1.98 . 1 114 . 11 GLU HB3 H 1.98 . 1 115 . 11 GLU CG C 34.6 . 1 116 . 11 GLU HG2 H 2.33 . 1 117 . 11 GLU HG3 H 2.33 . 1 118 . 12 ASP N N 119.1 . 1 119 . 12 ASP H H 6.94 . 1 120 . 12 ASP CA C 55.2 . 1 121 . 12 ASP HA H 4.12 . 1 122 . 12 ASP CB C 38.7 . 1 123 . 12 ASP HB2 H 2.48 . 2 124 . 12 ASP HB3 H 2.27 . 2 125 . 12 ASP C C 177.4 . 1 126 . 13 LYS N N 118.7 . 1 127 . 13 LYS H H 8.30 . 1 128 . 13 LYS CA C 57.2 . 1 129 . 13 LYS HA H 3.71 . 1 130 . 13 LYS CB C 31.1 . 1 131 . 13 LYS HB2 H 2.11 . 2 132 . 13 LYS HB3 H 1.57 . 2 133 . 13 LYS CG C 23.1 . 1 134 . 13 LYS HG2 H 1.70 . 1 135 . 13 LYS HG3 H 1.70 . 1 136 . 13 LYS CD C 26.9 . 1 137 . 13 LYS HD2 H 2.38 . 2 138 . 13 LYS HD3 H 1.56 . 2 139 . 13 LYS CE C 41.5 . 1 140 . 13 LYS HE2 H 3.37 . 2 141 . 13 LYS HE3 H 3.32 . 2 142 . 13 LYS C C 174.4 . 1 143 . 14 ALA N N 117.2 . 1 144 . 14 ALA H H 7.79 . 1 145 . 14 ALA CA C 53.9 . 1 146 . 14 ALA HA H 4.31 . 1 147 . 14 ALA HB H 1.49 . 1 148 . 14 ALA CB C 16.5 . 1 149 . 14 ALA C C 175.7 . 1 150 . 15 LYS N N 118.7 . 1 151 . 15 LYS H H 7.10 . 1 152 . 15 LYS CA C 58.1 . 1 153 . 15 LYS HA H 4.16 . 1 154 . 15 LYS CB C 30.7 . 1 155 . 15 LYS HB2 H 1.91 . 1 156 . 15 LYS HB3 H 1.91 . 1 157 . 15 LYS CG C 23.8 . 1 158 . 15 LYS HG2 H 1.68 . 2 159 . 15 LYS HG3 H 1.40 . 2 160 . 15 LYS CD C 28.3 . 1 161 . 15 LYS HD2 H 1.68 . 1 162 . 15 LYS HD3 H 1.68 . 1 163 . 15 LYS CE C 40.9 . 1 164 . 15 LYS HE2 H 2.94 . 1 165 . 15 LYS HE3 H 2.94 . 1 166 . 15 LYS C C 179.7 . 1 167 . 16 TYR N N 120.9 . 1 168 . 16 TYR H H 8.60 . 1 169 . 16 TYR CA C 56.7 . 1 170 . 16 TYR HA H 4.83 . 1 171 . 16 TYR CB C 34.4 . 1 172 . 16 TYR HB2 H 3.51 . 2 173 . 16 TYR HB3 H 3.30 . 2 174 . 16 TYR HD1 H 6.74 . 1 175 . 16 TYR HD2 H 6.74 . 1 176 . 16 TYR HE1 H 6.56 . 1 177 . 16 TYR HE2 H 6.56 . 1 178 . 16 TYR CD1 C 130.0 . 1 179 . 16 TYR CE1 C 116.9 . 1 180 . 16 TYR CE2 C 116.9 . 1 181 . 16 TYR CD2 C 130.0 . 1 182 . 16 TYR C C 178.6 . 1 183 . 17 ASP N N 119.9 . 1 184 . 17 ASP H H 9.44 . 1 185 . 17 ASP CA C 56.0 . 1 186 . 17 ASP HA H 4.51 . 1 187 . 17 ASP CB C 39.0 . 1 188 . 17 ASP HB2 H 3.02 . 2 189 . 17 ASP HB3 H 2.71 . 2 190 . 17 ASP C C 177.1 . 1 191 . 18 ALA N N 119.5 . 1 192 . 18 ALA H H 7.42 . 1 193 . 18 ALA CA C 53.6 . 1 194 . 18 ALA HA H 4.45 . 1 195 . 18 ALA HB H 1.68 . 1 196 . 18 ALA CB C 16.4 . 1 197 . 18 ALA C C 176.5 . 1 198 . 19 ILE N N 119.3 . 1 199 . 19 ILE H H 7.83 . 1 200 . 19 ILE CA C 63.8 . 1 201 . 19 ILE HA H 3.90 . 1 202 . 19 ILE CB C 37.3 . 1 203 . 19 ILE HB H 2.51 . 1 204 . 19 ILE HG2 H 1.28 . 1 205 . 19 ILE CG2 C 16.7 . 1 206 . 19 ILE CG1 C 26.9 . 1 207 . 19 ILE HG12 H 2.19 . 2 208 . 19 ILE HG13 H 1.28 . 2 209 . 19 ILE HD1 H 1.21 . 1 210 . 19 ILE CD1 C 12.6 . 1 211 . 19 ILE C C 180.2 . 1 212 . 20 PHE N N 122.9 . 1 213 . 20 PHE H H 9.32 . 1 214 . 20 PHE CA C 60.6 . 1 215 . 20 PHE HA H 3.25 . 1 216 . 20 PHE CB C 37.7 . 1 217 . 20 PHE HB2 H 3.43 . 2 218 . 20 PHE HB3 H 3.18 . 2 219 . 20 PHE C C 172.1 . 1 220 . 21 ASP N N 114.1 . 1 221 . 21 ASP H H 8.44 . 1 222 . 21 ASP CA C 56.0 . 1 223 . 21 ASP HA H 4.33 . 1 224 . 21 ASP CB C 39.0 . 1 225 . 21 ASP HB2 H 2.81 . 1 226 . 21 ASP HB3 H 2.81 . 1 227 . 21 ASP C C 175.8 . 1 228 . 22 SER N N 115.9 . 1 229 . 22 SER H H 7.99 . 1 230 . 22 SER CA C 59.2 . 1 231 . 22 SER HA H 4.54 . 1 232 . 22 SER CB C 62.2 . 1 233 . 22 SER HB2 H 4.17 . 1 234 . 22 SER HB3 H 4.17 . 1 235 . 22 SER C C 178.0 . 1 236 . 23 LEU N N 122.5 . 1 237 . 23 LEU H H 7.35 . 1 238 . 23 LEU CA C 53.5 . 1 239 . 23 LEU HA H 4.45 . 1 240 . 23 LEU CB C 40.9 . 1 241 . 23 LEU HB2 H 1.69 . 2 242 . 23 LEU HB3 H 1.49 . 2 243 . 23 LEU CG C 25.1 . 1 244 . 23 LEU HG H 1.86 . 1 245 . 23 LEU HD1 H 0.82 . 2 246 . 23 LEU HD2 H 0.89 . 2 247 . 23 LEU CD1 C 25.6 . 1 248 . 23 LEU CD2 C 21.0 . 1 249 . 23 LEU C C 173.5 . 1 250 . 24 SER N N 107.8 . 1 251 . 24 SER H H 7.74 . 1 252 . 24 SER CA C 56.7 . 1 253 . 24 SER HA H 4.12 . 1 254 . 24 SER CB C 59.8 . 1 255 . 24 SER HB2 H 4.06 . 1 256 . 24 SER HB3 H 4.06 . 1 257 . 24 SER C C 174.1 . 1 258 . 25 PRO CD C 49.1 . 1 259 . 25 PRO CA C 61.7 . 1 260 . 25 PRO HA H 4.19 . 1 261 . 25 PRO CB C 31.1 . 1 262 . 25 PRO HB2 H 1.57 . 2 263 . 25 PRO HB3 H 1.23 . 2 264 . 25 PRO CG C 26.0 . 1 265 . 25 PRO HG2 H 1.88 . 2 266 . 25 PRO HG3 H 1.54 . 2 267 . 25 PRO HD2 H 3.70 . 2 268 . 25 PRO HD3 H 3.62 . 2 269 . 26 VAL N N 120.0 . 1 270 . 26 VAL H H 8.51 . 1 271 . 26 VAL CA C 60.6 . 1 272 . 26 VAL HA H 5.69 . 1 273 . 26 VAL CB C 32.5 . 1 274 . 26 VAL HB H 2.05 . 1 275 . 26 VAL CG1 C 19.7 . 1 276 . 26 VAL HG1 H 1.05 . 1 277 . 26 VAL HG2 H 1.05 . 1 278 . 26 VAL C C 175.2 . 1 279 . 27 ASP N N 128.0 . 1 280 . 27 ASP H H 9.71 . 1 281 . 27 ASP CA C 54.1 . 1 282 . 27 ASP HA H 4.40 . 1 283 . 27 ASP CB C 38.2 . 1 284 . 27 ASP HB2 H 3.30 . 2 285 . 27 ASP HB3 H 2.99 . 2 286 . 27 ASP C C 175.5 . 1 287 . 28 GLY N N 98.8 . 1 288 . 28 GLY H H 8.54 . 1 289 . 28 GLY CA C 43.6 . 1 290 . 28 GLY HA2 H 4.00 . 2 291 . 28 GLY HA3 H 3.60 . 2 292 . 28 GLY C C 173.1 . 1 293 . 29 PHE N N 113.4 . 1 294 . 29 PHE H H 7.87 . 1 295 . 29 PHE CA C 55.2 . 1 296 . 29 PHE HA H 5.69 . 1 297 . 29 PHE CB C 42.9 . 1 298 . 29 PHE HB2 H 3.08 . 2 299 . 29 PHE HB3 H 2.86 . 2 300 . 29 PHE C C 172.4 . 1 301 . 30 LEU N N 119.8 . 1 302 . 30 LEU H H 9.60 . 1 303 . 30 LEU CA C 51.7 . 1 304 . 30 LEU HA H 4.81 . 1 305 . 30 LEU CB C 44.2 . 1 306 . 30 LEU HB2 H 1.79 . 2 307 . 30 LEU HB3 H 1.33 . 2 308 . 30 LEU CG C 27.6 . 1 309 . 30 LEU HG H 0.33 . 1 310 . 30 LEU HD1 H 0.89 . 2 311 . 30 LEU HD2 H 0.39 . 2 312 . 30 LEU CD1 C 24.4 . 1 313 . 30 LEU CD2 C 22.6 . 1 314 . 30 LEU C C 174.9 . 1 315 . 31 SER N N 116.0 . 1 316 . 31 SER H H 7.91 . 1 317 . 31 SER CA C 55.8 . 1 318 . 31 SER HA H 4.71 . 1 319 . 31 SER CB C 63.4 . 1 320 . 31 SER HB2 H 4.49 . 2 321 . 31 SER HB3 H 4.13 . 2 322 . 31 SER C C 174.5 . 1 323 . 32 GLY N N 107.9 . 1 324 . 32 GLY H H 9.05 . 1 325 . 32 GLY CA C 47.3 . 1 326 . 32 GLY HA2 H 3.70 . 2 327 . 32 GLY HA3 H 3.57 . 2 328 . 32 GLY C C 174.6 . 1 329 . 33 ASP N N 116.5 . 1 330 . 33 ASP H H 8.48 . 1 331 . 33 ASP CA C 55.2 . 1 332 . 33 ASP HA H 4.36 . 1 333 . 33 ASP CB C 38.8 . 1 334 . 33 ASP HB2 H 2.70 . 2 335 . 33 ASP HB3 H 2.60 . 2 336 . 33 ASP C C 174.1 . 1 337 . 34 LYS N N 116.3 . 1 338 . 34 LYS H H 7.55 . 1 339 . 34 LYS CA C 56.5 . 1 340 . 34 LYS HA H 4.36 . 1 341 . 34 LYS CB C 32.9 . 1 342 . 34 LYS HB2 H 2.04 . 2 343 . 34 LYS HB3 H 1.91 . 2 344 . 34 LYS CG C 24.8 . 1 345 . 34 LYS HG2 H 1.60 . 2 346 . 34 LYS HG3 H 1.54 . 2 347 . 34 LYS CD C 28.5 . 1 348 . 34 LYS HD2 H 1.95 . 2 349 . 34 LYS HD3 H 1.76 . 2 350 . 34 LYS CE C 41.3 . 1 351 . 34 LYS HE2 H 3.10 . 1 352 . 34 LYS HE3 H 3.10 . 1 353 . 34 LYS C C 176.4 . 1 354 . 35 VAL N N 115.4 . 1 355 . 35 VAL H H 7.75 . 1 356 . 35 VAL CA C 63.4 . 1 357 . 35 VAL HA H 4.01 . 1 358 . 35 VAL CB C 32.1 . 1 359 . 35 VAL HB H 2.31 . 1 360 . 35 VAL HG1 H 1.41 . 2 361 . 35 VAL HG2 H 1.33 . 2 362 . 35 VAL CG1 C 22.8 . 1 363 . 35 VAL CG2 C 20.4 . 1 364 . 35 VAL C C 176.6 . 1 365 . 36 LYS N N 119.4 . 1 366 . 36 LYS H H 8.43 . 1 367 . 36 LYS CA C 61.1 . 1 368 . 36 LYS HA H 4.01 . 1 369 . 36 LYS CB C 28.2 . 1 370 . 36 LYS HB2 H 1.47 . 2 371 . 36 LYS HB3 H 1.40 . 2 372 . 36 LYS CG C 24.4 . 1 373 . 36 LYS HG2 H 1.32 . 2 374 . 36 LYS HG3 H 1.25 . 2 375 . 36 LYS CD C 29.0 . 1 376 . 36 LYS HD2 H 1.87 . 1 377 . 36 LYS HD3 H 1.87 . 1 378 . 36 LYS CE C 40.1 . 1 379 . 36 LYS HE2 H 2.41 . 2 380 . 36 LYS HE3 H 2.29 . 2 381 . 36 LYS C C 175.7 . 1 382 . 37 PRO CD C 49.2 . 1 383 . 37 PRO CA C 65.0 . 1 384 . 37 PRO HA H 4.30 . 1 385 . 37 PRO CB C 30.0 . 1 386 . 37 PRO HB2 H 2.43 . 2 387 . 37 PRO HB3 H 1.87 . 2 388 . 37 PRO CG C 27.1 . 1 389 . 37 PRO HG2 H 2.18 . 2 390 . 37 PRO HG3 H 2.00 . 2 391 . 37 PRO HD2 H 3.65 . 2 392 . 37 PRO HD3 H 3.50 . 2 393 . 38 VAL N N 115.2 . 1 394 . 38 VAL H H 7.05 . 1 395 . 38 VAL CA C 64.0 . 1 396 . 38 VAL HA H 3.92 . 1 397 . 38 VAL CB C 30.5 . 1 398 . 38 VAL HB H 2.50 . 1 399 . 38 VAL HG1 H 1.28 . 2 400 . 38 VAL HG2 H 1.18 . 2 401 . 38 VAL CG1 C 21.7 . 1 402 . 38 VAL CG2 C 19.9 . 1 403 . 38 VAL C C 177.7 . 1 404 . 39 LEU N N 117.7 . 1 405 . 39 LEU H H 7.89 . 1 406 . 39 LEU CA C 56.6 . 1 407 . 39 LEU HA H 4.10 . 1 408 . 39 LEU CB C 39.2 . 1 409 . 39 LEU HB2 H 2.17 . 2 410 . 39 LEU HB3 H 1.58 . 2 411 . 39 LEU CG C 25.5 . 1 412 . 39 LEU HG H 1.97 . 1 413 . 39 LEU HD1 H 1.03 . 2 414 . 39 LEU HD2 H 0.77 . 2 415 . 39 LEU CD1 C 24.0 . 1 416 . 39 LEU CD2 C 20.9 . 1 417 . 39 LEU C C 178.0 . 1 418 . 40 LEU N N 119.8 . 1 419 . 40 LEU H H 8.73 . 1 420 . 40 LEU CA C 56.7 . 1 421 . 40 LEU HA H 4.05 . 1 422 . 40 LEU CB C 40.2 . 1 423 . 40 LEU HB2 H 1.87 . 2 424 . 40 LEU HB3 H 1.60 . 2 425 . 40 LEU CG C 25.6 . 1 426 . 40 LEU HG H 1.79 . 1 427 . 40 LEU HD1 H 0.91 . 2 428 . 40 LEU HD2 H 0.90 . 2 429 . 40 LEU CD1 C 24.0 . 1 430 . 40 LEU CD2 C 21.8 . 1 431 . 40 LEU C C 178.5 . 1 432 . 41 ASN N N 117.0 . 1 433 . 41 ASN H H 7.84 . 1 434 . 41 ASN CA C 53.6 . 1 435 . 41 ASN HA H 4.64 . 1 436 . 41 ASN CB C 37.0 . 1 437 . 41 ASN HB2 H 3.03 . 1 438 . 41 ASN HB3 H 3.03 . 1 439 . 41 ASN ND2 N 111.4 . 1 440 . 41 ASN HD21 H 7.76 . 2 441 . 41 ASN HD22 H 7.03 . 2 442 . 41 ASN C C 178.8 . 1 443 . 42 SER N N 113.3 . 1 444 . 42 SER H H 7.75 . 1 445 . 42 SER CA C 59.8 . 1 446 . 42 SER HA H 4.19 . 1 447 . 42 SER CB C 63.6 . 1 448 . 42 SER HB2 H 3.88 . 1 449 . 42 SER HB3 H 3.88 . 1 450 . 42 SER C C 174.4 . 1 451 . 43 LYS N N 111.5 . 1 452 . 43 LYS H H 7.92 . 1 453 . 43 LYS CA C 56.6 . 1 454 . 43 LYS HA H 4.05 . 1 455 . 43 LYS CB C 27.8 . 1 456 . 43 LYS HB2 H 2.27 . 2 457 . 43 LYS HB3 H 2.11 . 2 458 . 43 LYS CG C 23.6 . 1 459 . 43 LYS HG2 H 1.49 . 2 460 . 43 LYS HG3 H 1.42 . 2 461 . 43 LYS CD C 27.5 . 1 462 . 43 LYS HD2 H 1.79 . 2 463 . 43 LYS HD3 H 1.73 . 2 464 . 43 LYS CE C 41.0 . 1 465 . 43 LYS HE2 H 3.09 . 1 466 . 43 LYS HE3 H 3.09 . 1 467 . 43 LYS C C 173.4 . 1 468 . 44 LEU N N 119.9 . 1 469 . 44 LEU H H 7.59 . 1 470 . 44 LEU CA C 52.3 . 1 471 . 44 LEU HA H 4.52 . 1 472 . 44 LEU CB C 40.4 . 1 473 . 44 LEU HB2 H 1.61 . 2 474 . 44 LEU HB3 H 1.20 . 2 475 . 44 LEU CG C 25.9 . 1 476 . 44 LEU HG H 1.63 . 1 477 . 44 LEU HD1 H 0.98 . 2 478 . 44 LEU HD2 H 0.96 . 2 479 . 44 LEU CD1 C 25.3 . 1 480 . 44 LEU CD2 C 22.0 . 1 481 . 44 LEU C C 174.5 . 1 482 . 45 PRO CD C 49.2 . 1 483 . 45 PRO CA C 61.4 . 1 484 . 45 PRO HA H 4.54 . 1 485 . 45 PRO CB C 31.4 . 1 486 . 45 PRO HB2 H 2.63 . 2 487 . 45 PRO HB3 H 1.92 . 2 488 . 45 PRO CG C 26.7 . 1 489 . 45 PRO HG2 H 2.20 . 1 490 . 45 PRO HG3 H 2.20 . 1 491 . 45 PRO HD2 H 4.01 . 2 492 . 45 PRO HD3 H 3.48 . 2 493 . 46 VAL N N 121.4 . 1 494 . 46 VAL H H 8.78 . 1 495 . 46 VAL CA C 65.1 . 1 496 . 46 VAL HA H 3.71 . 1 497 . 46 VAL CB C 30.2 . 1 498 . 46 VAL HB H 2.19 . 1 499 . 46 VAL HG1 H 1.10 . 2 500 . 46 VAL HG2 H 1.07 . 2 501 . 46 VAL CG1 C 19.9 . 1 502 . 46 VAL CG2 C 19.7 . 1 503 . 46 VAL C C 177.3 . 1 504 . 47 GLU N N 120.2 . 1 505 . 47 GLU H H 9.55 . 1 506 . 47 GLU CA C 58.4 . 1 507 . 47 GLU HA H 4.24 . 1 508 . 47 GLU CB C 27.2 . 1 509 . 47 GLU HB2 H 2.13 . 2 510 . 47 GLU HB3 H 2.08 . 2 511 . 47 GLU CG C 34.6 . 1 512 . 47 GLU HG2 H 2.43 . 1 513 . 47 GLU HG3 H 2.43 . 1 514 . 48 ILE N N 118.3 . 1 515 . 48 ILE H H 7.17 . 1 516 . 48 ILE CA C 61.8 . 1 517 . 48 ILE HA H 3.95 . 1 518 . 48 ILE CB C 35.9 . 1 519 . 48 ILE HB H 2.14 . 1 520 . 48 ILE HG2 H 0.94 . 1 521 . 48 ILE CG2 C 16.4 . 1 522 . 48 ILE CG1 C 27.3 . 1 523 . 48 ILE HG12 H 1.71 . 2 524 . 48 ILE HG13 H 1.42 . 2 525 . 48 ILE HD1 H 0.95 . 1 526 . 48 ILE CD1 C 10.1 . 1 527 . 48 ILE C C 178.4 . 1 528 . 49 LEU N N 118.5 . 1 529 . 49 LEU H H 7.90 . 1 530 . 49 LEU CA C 56.6 . 1 531 . 49 LEU HA H 3.97 . 1 532 . 49 LEU CB C 39.9 . 1 533 . 49 LEU HB2 H 1.97 . 2 534 . 49 LEU HB3 H 1.47 . 2 535 . 49 LEU HG H 1.69 . 1 536 . 49 LEU CD1 C 24.9 . 1 537 . 49 LEU CD2 C 21.5 . 1 538 . 49 LEU HD1 H 0.84 . 1 539 . 49 LEU HD2 H 0.84 . 1 540 . 49 LEU C C 176.4 . 1 541 . 50 GLY N N 105.7 . 1 542 . 50 GLY H H 8.71 . 1 543 . 50 GLY CA C 46.0 . 1 544 . 50 GLY HA2 H 4.08 . 2 545 . 50 GLY HA3 H 4.01 . 2 546 . 50 GLY C C 178.7 . 1 547 . 51 ARG N N 121.7 . 1 548 . 51 ARG H H 7.34 . 1 549 . 51 ARG CA C 58.0 . 1 550 . 51 ARG HA H 4.34 . 1 551 . 51 ARG CB C 28.4 . 1 552 . 51 ARG HB2 H 2.11 . 2 553 . 51 ARG HB3 H 2.06 . 2 554 . 51 ARG CG C 26.3 . 1 555 . 51 ARG HG2 H 1.92 . 2 556 . 51 ARG HG3 H 1.75 . 2 557 . 51 ARG CD C 42.2 . 1 558 . 51 ARG HD2 H 3.35 . 1 559 . 51 ARG HD3 H 3.35 . 1 560 . 51 ARG C C 174.9 . 1 561 . 52 VAL N N 117.7 . 1 562 . 52 VAL H H 8.52 . 1 563 . 52 VAL CA C 66.2 . 1 564 . 52 VAL HA H 3.48 . 1 565 . 52 VAL CB C 29.9 . 1 566 . 52 VAL HB H 2.40 . 1 567 . 52 VAL HG1 H 1.05 . 2 568 . 52 VAL HG2 H 1.01 . 2 569 . 52 VAL CG1 C 21.8 . 1 570 . 52 VAL CG2 C 20.5 . 1 571 . 52 VAL C C 176.7 . 1 572 . 53 TRP N N 119.0 . 1 573 . 53 TRP H H 8.29 . 1 574 . 53 TRP CA C 60.1 . 1 575 . 53 TRP HA H 4.01 . 1 576 . 53 TRP CB C 27.2 . 1 577 . 53 TRP HB2 H 3.49 . 2 578 . 53 TRP HB3 H 3.33 . 2 579 . 53 TRP CE3 C 117.2 . 1 580 . 53 TRP NE1 N 129.4 . 1 581 . 53 TRP HE3 H 7.26 . 1 582 . 53 TRP CZ3 C 121.8 . 1 583 . 53 TRP CZ2 C 112.9 . 1 584 . 53 TRP HE1 H 10.48 . 1 585 . 53 TRP HZ3 H 6.80 . 1 586 . 53 TRP CH2 C 119.6 . 1 587 . 53 TRP HZ2 H 7.14 . 1 588 . 53 TRP HH2 H 6.77 . 1 589 . 53 TRP C C 177.3 . 1 590 . 54 GLU N N 114.1 . 1 591 . 54 GLU H H 7.90 . 1 592 . 54 GLU CA C 57.7 . 1 593 . 54 GLU HA H 3.92 . 1 594 . 54 GLU CB C 28.2 . 1 595 . 54 GLU HB2 H 2.33 . 2 596 . 54 GLU HB3 H 2.25 . 2 597 . 54 GLU CG C 34.2 . 1 598 . 54 GLU HG2 H 2.64 . 2 599 . 54 GLU HG3 H 2.59 . 2 600 . 54 GLU C C 174.1 . 1 601 . 55 LEU N N 115.2 . 1 602 . 55 LEU H H 8.38 . 1 603 . 55 LEU CA C 55.3 . 1 604 . 55 LEU HA H 4.06 . 1 605 . 55 LEU CB C 42.2 . 1 606 . 55 LEU HB2 H 1.82 . 2 607 . 55 LEU HB3 H 1.24 . 2 608 . 55 LEU CG C 25.6 . 1 609 . 55 LEU HG H 1.88 . 1 610 . 55 LEU CD1 C 24.7 . 1 611 . 55 LEU CD2 C 21.6 . 1 612 . 55 LEU HD1 H 0.77 . 1 613 . 55 LEU HD2 H 0.77 . 1 614 . 55 LEU C C 178.3 . 1 615 . 56 SER N N 110.9 . 1 616 . 56 SER H H 7.50 . 1 617 . 56 SER CA C 60.5 . 1 618 . 56 SER HA H 4.17 . 1 619 . 56 SER CB C 62.0 . 1 620 . 56 SER HB2 H 3.82 . 2 621 . 56 SER HB3 H 3.58 . 2 622 . 56 SER C C 176.6 . 1 623 . 57 ASP N N 116.0 . 1 624 . 57 ASP H H 7.17 . 1 625 . 57 ASP CA C 50.4 . 1 626 . 57 ASP HA H 4.57 . 1 627 . 57 ASP CB C 35.3 . 1 628 . 57 ASP HB2 H 2.34 . 2 629 . 57 ASP HB3 H 1.30 . 2 630 . 57 ASP C C 172.4 . 1 631 . 58 ILE N N 126.6 . 1 632 . 58 ILE H H 8.13 . 1 633 . 58 ILE CA C 63.4 . 1 634 . 58 ILE HA H 3.39 . 1 635 . 58 ILE CB C 38.5 . 1 636 . 58 ILE HB H 1.64 . 1 637 . 58 ILE HG2 H 0.96 . 1 638 . 58 ILE CG2 C 15.8 . 1 639 . 58 ILE CG1 C 28.4 . 1 640 . 58 ILE HG12 H 2.12 . 2 641 . 58 ILE HG13 H 1.29 . 2 642 . 58 ILE HD1 H 1.00 . 1 643 . 58 ILE CD1 C 13.9 . 1 644 . 58 ILE C C 176.6 . 1 645 . 59 ASP N N 112.2 . 1 646 . 59 ASP H H 7.85 . 1 647 . 59 ASP CA C 51.0 . 1 648 . 59 ASP HA H 4.45 . 1 649 . 59 ASP CB C 38.4 . 1 650 . 59 ASP HB2 H 3.14 . 2 651 . 59 ASP HB3 H 2.36 . 2 652 . 59 ASP C C 175.6 . 1 653 . 60 HIS N N 112.0 . 1 654 . 60 HIS H H 7.64 . 1 655 . 60 HIS CA C 55.4 . 1 656 . 60 HIS HA H 4.29 . 1 657 . 60 HIS CB C 25.1 . 1 658 . 60 HIS HB2 H 3.49 . 2 659 . 60 HIS HB3 H 3.44 . 2 660 . 60 HIS CD2 C 118.9 . 1 661 . 60 HIS CE1 C 135.2 . 1 662 . 60 HIS HD2 H 7.27 . 1 663 . 60 HIS HE1 H 8.68 . 1 664 . 60 HIS C C 174.7 . 1 665 . 61 ASP N N 117.9 . 1 666 . 61 ASP H H 8.51 . 1 667 . 61 ASP CA C 52.1 . 1 668 . 61 ASP HA H 4.77 . 1 669 . 61 ASP CB C 39.6 . 1 670 . 61 ASP HB2 H 2.99 . 2 671 . 61 ASP HB3 H 2.44 . 2 672 . 61 ASP C C 172.9 . 1 673 . 62 GLY N N 112.5 . 1 674 . 62 GLY H H 10.92 . 1 675 . 62 GLY CA C 44.9 . 1 676 . 62 GLY HA2 H 4.38 . 2 677 . 62 GLY HA3 H 3.94 . 2 678 . 62 GLY C C 177.1 . 1 679 . 63 LYS N N 117.6 . 1 680 . 63 LYS H H 8.24 . 1 681 . 63 LYS CA C 52.8 . 1 682 . 63 LYS HA H 5.22 . 1 683 . 63 LYS CB C 35.0 . 1 684 . 63 LYS HB2 H 1.76 . 2 685 . 63 LYS HB3 H 1.68 . 2 686 . 63 LYS CG C 22.4 . 1 687 . 63 LYS HG2 H 1.19 . 2 688 . 63 LYS HG3 H 1.06 . 2 689 . 63 LYS CD C 28.1 . 1 690 . 63 LYS HD2 H 1.33 . 2 691 . 63 LYS HD3 H 1.02 . 2 692 . 63 LYS CE C 40.3 . 1 693 . 63 LYS HE2 H 2.13 . 2 694 . 63 LYS HE3 H 2.06 . 2 695 . 63 LYS C C 171.7 . 1 696 . 64 LEU N N 119.9 . 1 697 . 64 LEU H H 9.54 . 1 698 . 64 LEU CA C 52.0 . 1 699 . 64 LEU HA H 6.02 . 1 700 . 64 LEU CB C 41.9 . 1 701 . 64 LEU HB2 H 2.13 . 2 702 . 64 LEU HB3 H 1.86 . 2 703 . 64 LEU CG C 25.6 . 1 704 . 64 LEU HG H 1.81 . 1 705 . 64 LEU HD1 H 1.02 . 2 706 . 64 LEU HD2 H 0.17 . 2 707 . 64 LEU CD1 C 25.9 . 1 708 . 64 LEU CD2 C 19.7 . 1 709 . 64 LEU C C 172.7 . 1 710 . 65 ASP N N 122.4 . 1 711 . 65 ASP H H 9.20 . 1 712 . 65 ASP CA C 50.5 . 1 713 . 65 ASP HA H 5.41 . 1 714 . 65 ASP CB C 39.2 . 1 715 . 65 ASP HB2 H 3.27 . 2 716 . 65 ASP HB3 H 2.91 . 2 717 . 65 ASP C C 176.2 . 1 718 . 66 ARG N N 116.4 . 1 719 . 66 ARG H H 8.21 . 1 720 . 66 ARG CA C 59.2 . 1 721 . 66 ARG HA H 2.88 . 1 722 . 66 ARG CB C 29.4 . 1 723 . 66 ARG HB2 H 1.31 . 1 724 . 66 ARG HB3 H 1.31 . 1 725 . 66 ARG CG C 26.6 . 1 726 . 66 ARG HG2 H 0.84 . 2 727 . 66 ARG HG3 H 0.80 . 2 728 . 66 ARG CD C 41.4 . 1 729 . 66 ARG HD2 H 3.20 . 2 730 . 66 ARG HD3 H 2.96 . 2 731 . 66 ARG C C 172.5 . 1 732 . 67 ASP N N 118.7 . 1 733 . 67 ASP H H 7.96 . 1 734 . 67 ASP CA C 56.3 . 1 735 . 67 ASP HA H 4.78 . 1 736 . 67 ASP CB C 39.1 . 1 737 . 67 ASP HB2 H 2.61 . 2 738 . 67 ASP HB3 H 2.29 . 2 739 . 67 ASP C C 177.7 . 1 740 . 68 GLU N N 119.6 . 1 741 . 68 GLU H H 8.78 . 1 742 . 68 GLU CA C 58.6 . 1 743 . 68 GLU HA H 4.03 . 1 744 . 68 GLU CB C 30.4 . 1 745 . 68 GLU HB2 H 2.64 . 2 746 . 68 GLU HB3 H 2.38 . 2 747 . 68 GLU CG C 36.7 . 1 748 . 68 GLU HG2 H 2.96 . 2 749 . 68 GLU HG3 H 2.40 . 2 750 . 68 GLU C C 177.0 . 1 751 . 69 PHE N N 117.6 . 1 752 . 69 PHE H H 9.38 . 1 753 . 69 PHE CA C 60.7 . 1 754 . 69 PHE HA H 4.24 . 1 755 . 69 PHE CB C 38.8 . 1 756 . 69 PHE HB2 H 3.35 . 1 757 . 69 PHE HB3 H 3.35 . 1 758 . 69 PHE C C 177.8 . 1 759 . 70 ALA N N 119.0 . 1 760 . 70 ALA H H 7.81 . 1 761 . 70 ALA CA C 53.8 . 1 762 . 70 ALA HA H 4.00 . 1 763 . 70 ALA HB H 2.06 . 1 764 . 70 ALA CB C 17.4 . 1 765 . 70 ALA C C 174.8 . 1 766 . 71 VAL N N 116.5 . 1 767 . 71 VAL H H 7.74 . 1 768 . 71 VAL CA C 66.2 . 1 769 . 71 VAL HA H 3.50 . 1 770 . 71 VAL CB C 30.0 . 1 771 . 71 VAL HB H 2.81 . 1 772 . 71 VAL HG1 H 1.59 . 2 773 . 71 VAL HG2 H 1.06 . 2 774 . 71 VAL CG1 C 22.8 . 1 775 . 71 VAL CG2 C 20.9 . 1 776 . 71 VAL C C 177.6 . 1 777 . 72 ALA N N 120.9 . 1 778 . 72 ALA H H 8.05 . 1 779 . 72 ALA CA C 54.5 . 1 780 . 72 ALA HA H 3.95 . 1 781 . 72 ALA HB H 1.21 . 1 782 . 72 ALA CB C 15.4 . 1 783 . 72 ALA C C 175.4 . 1 784 . 73 MET N N 112.8 . 1 785 . 73 MET H H 7.98 . 1 786 . 73 MET CA C 54.5 . 1 787 . 73 MET HA H 3.94 . 1 788 . 73 MET CB C 28.9 . 1 789 . 73 MET HB2 H 0.78 . 1 790 . 73 MET HB3 H 0.78 . 1 791 . 73 MET CG C 31.8 . 1 792 . 73 MET HG2 H 1.71 . 2 793 . 73 MET HG3 H 1.32 . 2 794 . 73 MET C C 178.3 . 1 795 . 74 PHE N N 121.7 . 1 796 . 74 PHE H H 8.45 . 1 797 . 74 PHE CA C 60.2 . 1 798 . 74 PHE HA H 4.38 . 1 799 . 74 PHE CB C 38.4 . 1 800 . 74 PHE HB2 H 3.43 . 2 801 . 74 PHE HB3 H 3.13 . 2 802 . 74 PHE C C 177.3 . 1 803 . 75 LEU N N 119.1 . 1 804 . 75 LEU H H 8.83 . 1 805 . 75 LEU CA C 56.8 . 1 806 . 75 LEU HA H 4.02 . 1 807 . 75 LEU CB C 42.3 . 1 808 . 75 LEU HB2 H 2.36 . 2 809 . 75 LEU HB3 H 1.26 . 2 810 . 75 LEU CG C 25.9 . 1 811 . 75 LEU HG H 2.22 . 1 812 . 75 LEU HD1 H 0.91 . 2 813 . 75 LEU HD2 H 0.96 . 2 814 . 75 LEU CD1 C 26.6 . 1 815 . 75 LEU CD2 C 21.6 . 1 816 . 75 LEU C C 177.6 . 1 817 . 76 VAL N N 119.4 . 1 818 . 76 VAL H H 8.39 . 1 819 . 76 VAL CA C 66.0 . 1 820 . 76 VAL HA H 3.37 . 1 821 . 76 VAL CB C 30.0 . 1 822 . 76 VAL HB H 2.19 . 1 823 . 76 VAL HG1 H 1.00 . 2 824 . 76 VAL HG2 H 0.74 . 2 825 . 76 VAL CG1 C 22.9 . 1 826 . 76 VAL CG2 C 20.0 . 1 827 . 77 TYR N N 118.0 . 1 828 . 77 TYR H H 8.42 . 1 829 . 77 TYR CA C 61.6 . 1 830 . 77 TYR HA H 4.12 . 1 831 . 77 TYR CB C 35.6 . 1 832 . 77 TYR HB2 H 3.05 . 1 833 . 77 TYR HB3 H 3.05 . 1 834 . 77 TYR HD1 H 7.21 . 1 835 . 77 TYR HE1 H 6.72 . 1 836 . 77 TYR HE2 H 6.73 . 1 837 . 77 TYR HD2 H 7.17 . 1 838 . 77 TYR C C 175.9 . 1 839 . 78 CYS N N 116.4 . 1 840 . 78 CYS H H 8.22 . 1 841 . 78 CYS CA C 62.2 . 1 842 . 78 CYS HA H 3.88 . 1 843 . 78 CYS CB C 25.0 . 1 844 . 78 CYS HB2 H 2.98 . 2 845 . 78 CYS HB3 H 2.63 . 2 846 . 78 CYS C C 171.5 . 1 847 . 79 ALA N N 122.3 . 1 848 . 79 ALA H H 8.23 . 1 849 . 79 ALA CA C 53.5 . 1 850 . 79 ALA HA H 4.45 . 1 851 . 79 ALA HB H 1.68 . 1 852 . 79 ALA CB C 16.7 . 1 853 . 79 ALA C C 175.7 . 1 854 . 80 LEU N N 121.6 . 1 855 . 80 LEU H H 8.77 . 1 856 . 80 LEU CA C 56.2 . 1 857 . 80 LEU HA H 4.18 . 1 858 . 80 LEU CB C 40.5 . 1 859 . 80 LEU HB2 H 2.08 . 2 860 . 80 LEU HB3 H 1.56 . 2 861 . 80 LEU CG C 25.9 . 1 862 . 80 LEU HG H 1.86 . 1 863 . 80 LEU HD1 H 0.81 . 2 864 . 80 LEU HD2 H 1.00 . 2 865 . 80 LEU CD1 C 24.6 . 1 866 . 80 LEU CD2 C 21.4 . 1 867 . 80 LEU C C 181.7 . 1 868 . 81 GLU N N 117.0 . 1 869 . 81 GLU H H 7.48 . 1 870 . 81 GLU CA C 54.1 . 1 871 . 81 GLU HA H 4.41 . 1 872 . 81 GLU CB C 26.7 . 1 873 . 81 GLU HB2 H 2.39 . 2 874 . 81 GLU HB3 H 2.05 . 2 875 . 81 GLU CG C 32.6 . 1 876 . 81 GLU HG2 H 2.46 . 2 877 . 81 GLU HG3 H 2.37 . 2 878 . 81 GLU C C 177.4 . 1 879 . 82 LYS N N 110.8 . 1 880 . 82 LYS H H 7.87 . 1 881 . 82 LYS CA C 56.2 . 1 882 . 82 LYS HA H 3.85 . 1 883 . 82 LYS CB C 27.6 . 1 884 . 82 LYS HB2 H 2.27 . 2 885 . 82 LYS HB3 H 2.07 . 2 886 . 82 LYS CG C 23.7 . 1 887 . 82 LYS HG2 H 1.40 . 1 888 . 82 LYS HG3 H 1.40 . 1 889 . 82 LYS CD C 27.6 . 1 890 . 82 LYS HD2 H 1.76 . 2 891 . 82 LYS HD3 H 1.70 . 2 892 . 82 LYS CE C 41.0 . 1 893 . 82 LYS HE2 H 3.07 . 1 894 . 82 LYS HE3 H 3.07 . 1 895 . 82 LYS C C 173.8 . 1 896 . 83 GLU N N 119.5 . 1 897 . 83 GLU H H 8.05 . 1 898 . 83 GLU CA C 52.2 . 1 899 . 83 GLU HA H 4.71 . 1 900 . 83 GLU HB2 H 1.99 . 2 901 . 83 GLU HB3 H 1.70 . 2 902 . 83 GLU CG C 33.2 . 1 903 . 83 GLU HG2 H 2.36 . 2 904 . 83 GLU HG3 H 2.31 . 2 905 . 83 GLU C C 174.6 . 1 906 . 84 PRO CD C 49.2 . 1 907 . 84 PRO CA C 61.0 . 1 908 . 84 PRO HA H 4.39 . 1 909 . 84 PRO CB C 30.6 . 1 910 . 84 PRO HB2 H 2.29 . 2 911 . 84 PRO HB3 H 1.78 . 2 912 . 84 PRO CG C 26.0 . 1 913 . 84 PRO HG2 H 3.90 . 2 914 . 84 PRO HG3 H 3.72 . 2 915 . 84 PRO HD2 H 3.89 . 2 916 . 84 PRO HD3 H 3.72 . 2 917 . 85 VAL N N 123.9 . 1 918 . 85 VAL H H 8.67 . 1 919 . 85 VAL CA C 58.7 . 1 920 . 85 VAL HA H 4.34 . 1 921 . 85 VAL CB C 31.0 . 1 922 . 85 VAL HB H 2.04 . 1 923 . 85 VAL HG1 H 1.02 . 2 924 . 85 VAL HG2 H 1.04 . 2 925 . 85 VAL CG1 C 20.8 . 1 926 . 85 VAL CG2 C 20.4 . 1 927 . 85 VAL C C 175.4 . 1 928 . 86 PRO CD C 49.5 . 1 929 . 86 PRO CA C 61.4 . 1 930 . 86 PRO HA H 4.62 . 1 931 . 86 PRO CB C 31.5 . 1 932 . 86 PRO HB2 H 2.45 . 1 933 . 86 PRO HB3 H 2.45 . 1 934 . 86 PRO CG C 25.4 . 1 935 . 86 PRO HG2 H 2.09 . 2 936 . 86 PRO HG3 H 1.84 . 2 937 . 86 PRO HD2 H 3.94 . 2 938 . 86 PRO HD3 H 3.55 . 2 939 . 87 MET N N 113.6 . 1 940 . 87 MET H H 8.61 . 1 941 . 87 MET CA C 54.9 . 1 942 . 87 MET HA H 4.44 . 1 943 . 87 MET CB C 31.0 . 1 944 . 87 MET HB2 H 2.19 . 2 945 . 87 MET HB3 H 2.12 . 2 946 . 87 MET CG C 31.1 . 1 947 . 87 MET HG2 H 2.81 . 2 948 . 87 MET HG3 H 2.66 . 2 949 . 87 MET C C 173.6 . 1 950 . 88 SER N N 109.3 . 1 951 . 88 SER H H 7.63 . 1 952 . 88 SER CA C 55.0 . 1 953 . 88 SER HA H 4.54 . 1 954 . 88 SER CB C 63.8 . 1 955 . 88 SER HB2 H 3.83 . 2 956 . 88 SER HB3 H 3.79 . 2 957 . 88 SER C C 175.2 . 1 958 . 89 LEU N N 123.0 . 1 959 . 89 LEU H H 9.31 . 1 960 . 89 LEU CA C 52.1 . 1 961 . 89 LEU HA H 4.37 . 1 962 . 89 LEU CB C 40.5 . 1 963 . 89 LEU HB2 H 1.70 . 2 964 . 89 LEU HB3 H 1.45 . 2 965 . 89 LEU CG C 25.3 . 1 966 . 89 LEU HG H 1.81 . 1 967 . 89 LEU HD1 H 1.01 . 2 968 . 89 LEU HD2 H 0.90 . 2 969 . 89 LEU CD1 C 25.2 . 1 970 . 89 LEU CD2 C 23.9 . 1 971 . 89 LEU C C 177.8 . 1 972 . 90 PRO CD C 49.3 . 1 973 . 90 PRO HA H 4.86 . 1 974 . 90 PRO CB C 29.9 . 1 975 . 90 PRO HB2 H 2.56 . 2 976 . 90 PRO HB3 H 2.01 . 2 977 . 90 PRO CG C 26.3 . 1 978 . 90 PRO HG2 H 2.23 . 1 979 . 90 PRO HG3 H 2.23 . 1 980 . 90 PRO HD2 H 4.21 . 2 981 . 90 PRO HD3 H 3.67 . 2 982 . 91 PRO CD C 48.9 . 1 983 . 91 PRO CA C 64.5 . 1 984 . 91 PRO HA H 4.18 . 1 985 . 91 PRO CB C 30.8 . 1 986 . 91 PRO HB2 H 2.42 . 2 987 . 91 PRO HB3 H 1.94 . 2 988 . 91 PRO CG C 26.2 . 1 989 . 91 PRO HG2 H 2.23 . 2 990 . 91 PRO HG3 H 2.15 . 2 991 . 91 PRO HD2 H 3.93 . 2 992 . 91 PRO HD3 H 3.89 . 2 993 . 92 ALA N N 114.4 . 1 994 . 92 ALA H H 8.79 . 1 995 . 92 ALA CA C 53.0 . 1 996 . 92 ALA HA H 4.07 . 1 997 . 92 ALA HB H 1.52 . 1 998 . 92 ALA CB C 17.4 . 1 999 . 92 ALA C C 177.9 . 1 1000 . 93 LEU N N 117.0 . 1 1001 . 93 LEU H H 8.21 . 1 1002 . 93 LEU CA C 53.5 . 1 1003 . 93 LEU HA H 4.32 . 1 1004 . 93 LEU CB C 41.8 . 1 1005 . 93 LEU HB2 H 1.95 . 2 1006 . 93 LEU HB3 H 1.40 . 2 1007 . 93 LEU CG C 26.2 . 1 1008 . 93 LEU HG H 1.82 . 1 1009 . 93 LEU HD1 H 0.79 . 2 1010 . 93 LEU HD2 H 0.53 . 2 1011 . 93 LEU CD1 C 24.7 . 1 1012 . 93 LEU CD2 C 22.6 . 1 1013 . 93 LEU C C 177.8 . 1 1014 . 94 VAL N N 121.3 . 1 1015 . 94 VAL H H 7.33 . 1 1016 . 94 VAL CA C 60.3 . 1 1017 . 94 VAL HA H 3.76 . 1 1018 . 94 VAL CB C 30.5 . 1 1019 . 94 VAL HB H 2.07 . 1 1020 . 94 VAL CG1 C 20.3 . 1 1021 . 94 VAL CG2 C 20.2 . 1 1022 . 94 VAL HG1 H 0.81 . 1 1023 . 94 VAL HG2 H 0.81 . 1 1024 . 94 VAL C C 175.4 . 1 1025 . 95 PRO CD C 49.4 . 1 1026 . 95 PRO CA C 59.1 . 1 1027 . 95 PRO HA H 2.69 . 1 1028 . 95 PRO CB C 29.1 . 1 1029 . 95 PRO HB2 H 1.34 . 2 1030 . 95 PRO HB3 H 1.28 . 2 1031 . 95 PRO CG C 27.0 . 1 1032 . 95 PRO HG2 H 1.99 . 2 1033 . 95 PRO HG3 H 1.64 . 2 1034 . 95 PRO HD2 H 4.37 . 2 1035 . 95 PRO HD3 H 3.25 . 2 1036 . 96 PRO CD C 48.2 . 1 1037 . 96 PRO CA C 65.1 . 1 1038 . 96 PRO HA H 3.63 . 1 1039 . 96 PRO CB C 30.7 . 1 1040 . 96 PRO HB2 H 2.30 . 2 1041 . 96 PRO HB3 H 1.81 . 2 1042 . 96 PRO CG C 26.2 . 1 1043 . 96 PRO HG2 H 2.19 . 2 1044 . 96 PRO HG3 H 1.74 . 2 1045 . 96 PRO HD2 H 2.97 . 2 1046 . 96 PRO HD3 H 2.82 . 2 1047 . 97 SER N N 110.4 . 1 1048 . 97 SER H H 8.52 . 1 1049 . 97 SER CA C 58.9 . 1 1050 . 97 SER HA H 4.05 . 1 1051 . 97 SER CB C 61.2 . 1 1052 . 97 SER HB2 H 3.90 . 2 1053 . 97 SER HB3 H 3.85 . 2 1054 . 97 SER C C 176.7 . 1 1055 . 98 LYS N N 117.8 . 1 1056 . 98 LYS H H 8.14 . 1 1057 . 98 LYS CA C 52.9 . 1 1058 . 98 LYS HA H 4.65 . 1 1059 . 98 LYS CB C 31.5 . 1 1060 . 98 LYS HB2 H 2.15 . 2 1061 . 98 LYS HB3 H 1.58 . 2 1062 . 98 LYS CG C 23.6 . 1 1063 . 98 LYS HG2 H 1.52 . 2 1064 . 98 LYS HG3 H 1.28 . 2 1065 . 98 LYS CD C 27.3 . 1 1066 . 98 LYS HD2 H 1.71 . 2 1067 . 98 LYS HD3 H 1.47 . 2 1068 . 98 LYS CE C 40.8 . 1 1069 . 98 LYS HE2 H 3.05 . 2 1070 . 98 LYS HE3 H 2.98 . 2 1071 . 98 LYS C C 174.0 . 1 1072 . 99 ARG N N 118.7 . 1 1073 . 99 ARG H H 7.23 . 1 1074 . 99 ARG CA C 56.5 . 1 1075 . 99 ARG HA H 4.14 . 1 1076 . 99 ARG CB C 29.4 . 1 1077 . 99 ARG HB2 H 1.95 . 2 1078 . 99 ARG HB3 H 1.74 . 2 1079 . 99 ARG CG C 26.0 . 1 1080 . 99 ARG HG2 H 1.92 . 2 1081 . 99 ARG HG3 H 1.52 . 2 1082 . 99 ARG CD C 43.1 . 1 1083 . 99 ARG HD2 H 3.23 . 2 1084 . 99 ARG HD3 H 3.00 . 2 1085 . 99 ARG C C 175.2 . 1 1086 . 100 LYS N N 119.6 . 1 1087 . 100 LYS H H 8.47 . 1 1088 . 100 LYS CA C 55.6 . 1 1089 . 100 LYS HA H 4.31 . 1 1090 . 100 LYS CB C 31.4 . 1 1091 . 100 LYS HB2 H 1.76 . 1 1092 . 100 LYS HB3 H 1.76 . 1 1093 . 100 LYS CG C 23.5 . 1 1094 . 100 LYS HG2 H 1.39 . 1 1095 . 100 LYS HG3 H 1.39 . 1 1096 . 100 LYS CD C 27.6 . 1 1097 . 100 LYS HD2 H 1.67 . 1 1098 . 100 LYS HD3 H 1.67 . 1 1099 . 100 LYS CE C 40.8 . 1 1100 . 100 LYS HE2 H 2.98 . 1 1101 . 100 LYS HE3 H 2.98 . 1 1102 . 100 LYS C C 175.4 . 1 1103 . 101 THR N N 111.6 . 1 1104 . 101 THR H H 7.89 . 1 1105 . 101 THR CA C 60.7 . 1 1106 . 101 THR HA H 4.31 . 1 1107 . 101 THR CB C 68.3 . 1 1108 . 101 THR HB H 4.23 . 1 1109 . 101 THR HG2 H 1.16 . 1 1110 . 101 THR CG2 C 20.4 . 1 1111 . 101 THR C C 175.5 . 1 1112 . 102 TRP N N 122.7 . 1 1113 . 102 TRP H H 8.06 . 1 1114 . 102 TRP CA C 56.1 . 1 1115 . 102 TRP HA H 4.72 . 1 1116 . 102 TRP CB C 28.5 . 1 1117 . 102 TRP HB2 H 3.34 . 2 1118 . 102 TRP HB3 H 3.27 . 2 1119 . 102 TRP CE3 C 119.5 . 1 1120 . 102 TRP NE1 N 128.2 . 1 1121 . 102 TRP HE3 H 7.58 . 1 1122 . 102 TRP CZ3 C 123.3 . 1 1123 . 102 TRP CZ2 C 113.4 . 1 1124 . 102 TRP HE1 H 10.21 . 1 1125 . 102 TRP HZ3 H 7.20 . 1 1126 . 102 TRP CH2 C 120.5 . 1 1127 . 102 TRP HZ2 H 7.47 . 1 1128 . 102 TRP HH2 H 7.11 . 1 1129 . 102 TRP C C 172.8 . 1 1130 . 103 VAL N N 121.9 . 1 1131 . 103 VAL H H 7.92 . 1 1132 . 103 VAL CA C 60.7 . 1 1133 . 103 VAL HA H 4.10 . 1 1134 . 103 VAL CB C 31.6 . 1 1135 . 103 VAL HB H 2.00 . 1 1136 . 103 VAL CG1 C 19.6 . 1 1137 . 103 VAL CG2 C 19.4 . 1 1138 . 103 VAL HG1 H 0.90 . 1 1139 . 103 VAL HG2 H 0.90 . 1 1140 . 103 VAL C C 174.2 . 1 1141 . 104 VAL N N 123.7 . 1 1142 . 104 VAL H H 8.22 . 1 1143 . 104 VAL CA C 60.9 . 1 1144 . 104 VAL HA H 4.10 . 1 1145 . 104 VAL CB C 31.4 . 1 1146 . 104 VAL HB H 2.11 . 1 1147 . 104 VAL CG1 C 19.7 . 1 1148 . 104 VAL CG2 C 19.4 . 1 1149 . 104 VAL HG1 H 0.99 . 1 1150 . 104 VAL HG2 H 0.99 . 1 1151 . 104 VAL C C 174.1 . 1 1152 . 105 SER N N 124.2 . 1 1153 . 105 SER H H 8.02 . 1 1154 . 105 SER CA C 58.5 . 1 1155 . 105 SER HA H 4.32 . 1 1156 . 105 SER CB C 63.7 . 1 1157 . 105 SER HB2 H 3.88 . 1 1158 . 105 SER HB3 H 3.88 . 1 1159 . 105 SER C C 174.0 . 1 stop_ save_