data_7362 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Structure of Protein UPF0165 protein AF_2212 from Archaeoglobus Fulgidus; Northeast Structural Genomics Consortium Target GR83 ; _BMRB_accession_number 7362 _BMRB_flat_file_name bmr7362.str _Entry_type original _Submission_date 2007-01-19 _Accession_date 2007-01-23 _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 Singarapu K. K. . 2 Sukumaran D. K. . 3 Parish D. . . 4 Atreya H. S. . 5 Liu G. . . 6 Eletsky A. . . 7 Chen C. X. . 8 Jiang M. . . 9 Cunningham K. . . 10 Xiao R. . . 11 Swapna G. V.T. . 12 Acton T. B. . 13 Rost B. . . 14 Montelione G. T. . 15 Szyperski T. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 397 "13C chemical shifts" 229 "15N chemical shifts" 62 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-03-04 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_citations _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR Structure of Protein Y2212_ARCFU from Archaeoglobus Fulgidus; Northeast Structural Genomics Consortium Target GR83' _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Singarapu K. K. . 2 Sukumaran D. K. . 3 Parish D. . . 4 Atreya H. S. . 5 Liu G. . . 6 Eletsky A. . . 7 Chen C. X. . 8 Jiang M. . . 9 Cunningham K. . . 10 Ma L. C. . 11 Xiao R. . . 12 Liu J. . . 13 Baran M. . . 14 Swapna G. V.T. . 15 Acton T. B. . 16 Rost B. . . 17 Montelione G. T. . 18 Szyperski T. . . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD 0353 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name UPF0165 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'UPF0165 chain A' $UPF0165_protein_AF_2212 'UPF0165 chain B' $UPF0165_protein_AF_2212 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_UPF0165_protein_AF_2212 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common UPF0165_protein_AF_2212 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 69 _Mol_residue_sequence ; MPKIIEAVYENGVFKPLQKV DLKEGERVKIKLELKVEPID LGEPVSVEEIKKIRDGTWMS SLEHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 PRO 3 LYS 4 ILE 5 ILE 6 GLU 7 ALA 8 VAL 9 TYR 10 GLU 11 ASN 12 GLY 13 VAL 14 PHE 15 LYS 16 PRO 17 LEU 18 GLN 19 LYS 20 VAL 21 ASP 22 LEU 23 LYS 24 GLU 25 GLY 26 GLU 27 ARG 28 VAL 29 LYS 30 ILE 31 LYS 32 LEU 33 GLU 34 LEU 35 LYS 36 VAL 37 GLU 38 PRO 39 ILE 40 ASP 41 LEU 42 GLY 43 GLU 44 PRO 45 VAL 46 SER 47 VAL 48 GLU 49 GLU 50 ILE 51 LYS 52 LYS 53 ILE 54 ARG 55 ASP 56 GLY 57 THR 58 TRP 59 MET 60 SER 61 SER 62 LEU 63 GLU 64 HIS 65 HIS 66 HIS 67 HIS 68 HIS 69 HIS 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 PDB 2NWT "Nmr Structure Of Protein Upf0165 Protein Af_2212 From Archaeoglobus Fulgidus; Northeast Structural Genomics Consortium Target G" 100.00 69 100.00 100.00 9.21e-40 GB AAB89054 "conserved hypothetical protein [Archaeoglobus fulgidus DSM 4304]" 88.41 61 100.00 100.00 1.87e-33 GB AIG99201 "hypothetical protein AFULGI_00024860 [Archaeoglobus fulgidus DSM 8774]" 88.41 61 98.36 98.36 4.07e-32 REF NP_071037 "hypothetical protein AF2212 [Archaeoglobus fulgidus DSM 4304]" 88.41 61 100.00 100.00 1.87e-33 REF WP_010879701 "antitoxin [Archaeoglobus fulgidus]" 88.41 61 100.00 100.00 1.87e-33 SP O28071 "RecName: Full=Putative antitoxin VapB21 [Archaeoglobus fulgidus DSM 4304]" 88.41 61 100.00 100.00 1.87e-33 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $UPF0165_protein_AF_2212 'Archaeoglobus fulgidus' 2234 Archaea . Archaeoglobus fulgidus XL-10 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 $UPF0165_protein_AF_2212 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample _Saveframe_category sample _Sample_type solution _Details '1.2 mM protein Y2212_ARCFU, U-15N,13C, 5mM CaCl, 100mM NaCl, 20mM NH4OAc, 10mM DTT, 0.02%NaN3, 5% D2O, 95% H2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $assembly 1.2 mM '[U-13C; U-15N]' NaCl 5 mM . NH4OAc 20 mM . DTT 10 mM . NaN3 0.02 % . D2O 5 % . H2O 95 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 2.3 loop_ _Vendor _Address _Electronic_address 'Delaglio et al' . . stop_ loop_ _Task processing stop_ _Details . save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Vendor _Address _Electronic_address 'Guntert et al' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Guntert et al' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version 1.1 loop_ _Vendor _Address _Electronic_address 'Brunget et al' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_4,3D,_GFT_HNNCABCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name '4,3D, GFT HNNCABCA' _Sample_label $sample save_ save_4,3D,_GFT_CABCACoNNH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '4,3D, GFT CABCACoNNH' _Sample_label $sample save_ save_4,3D,_GFT_HCCH_COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '4,3D, GFT HCCH COSY' _Sample_label $sample save_ save_3D,_15N-13C_resolved_simultanious_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D, 15N-13C resolved simultanious NOESY' _Sample_label $sample save_ save_3D,_15N,_13C_resolved_X-filtered_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D, 15N, 13C resolved X-filtered NOESY' _Sample_label $sample save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 5.5 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'UPF0165 chain A' _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 3 3 LYS HA H 4.47 . 1 2 3 3 LYS HB2 H 1.79 . 2 3 3 3 LYS HB3 H 1.73 . 2 4 3 3 LYS HD2 H 1.66 . 2 5 3 3 LYS HD3 H 1.64 . 2 6 3 3 LYS HE2 H 2.96 . 2 7 3 3 LYS HE3 H 2.96 . 2 8 3 3 LYS HG2 H 1.38 . 2 9 3 3 LYS HG3 H 1.40 . 2 10 3 3 LYS CA C 56.3 . 1 11 3 3 LYS CB C 34.1 . 1 12 3 3 LYS CD C 29.2 . 1 13 3 3 LYS CE C 42.1 . 1 14 3 3 LYS CG C 25.1 . 1 15 4 4 ILE H H 8.24 . 1 16 4 4 ILE HA H 4.76 . 1 17 4 4 ILE HB H 1.72 . 1 18 4 4 ILE HD1 H 0.78 . 1 19 4 4 ILE HG12 H 0.97 . 2 20 4 4 ILE HG13 H 1.47 . 2 21 4 4 ILE HG2 H 0.73 . 1 22 4 4 ILE CA C 59.9 . 1 23 4 4 ILE CB C 39.1 . 1 24 4 4 ILE CD1 C 13.1 . 1 25 4 4 ILE CG1 C 28.0 . 1 26 4 4 ILE CG2 C 18.1 . 1 27 4 4 ILE N N 123.7 . 1 28 5 5 ILE H H 8.96 . 1 29 5 5 ILE HA H 4.51 . 1 30 5 5 ILE HB H 1.75 . 1 31 5 5 ILE HD1 H 0.79 . 1 32 5 5 ILE HG12 H 0.96 . 2 33 5 5 ILE HG13 H 1.33 . 2 34 5 5 ILE HG2 H 0.83 . 1 35 5 5 ILE CA C 58.9 . 1 36 5 5 ILE CB C 42.0 . 1 37 5 5 ILE CD1 C 14.7 . 1 38 5 5 ILE CG1 C 27.1 . 1 39 5 5 ILE CG2 C 18.0 . 1 40 5 5 ILE N N 125.1 . 1 41 6 6 GLU H H 8.57 . 1 42 6 6 GLU HA H 4.91 . 1 43 6 6 GLU HB2 H 2.06 . 2 44 6 6 GLU HB3 H 1.93 . 2 45 6 6 GLU HG2 H 2.36 . 2 46 6 6 GLU HG3 H 2.17 . 2 47 6 6 GLU CA C 55.9 . 1 48 6 6 GLU CB C 31.5 . 1 49 6 6 GLU CG C 37.1 . 1 50 6 6 GLU N N 124.8 . 1 51 7 7 ALA H H 9.03 . 1 52 7 7 ALA HA H 5.27 . 1 53 7 7 ALA HB H 1.16 . 1 54 7 7 ALA CA C 51.0 . 1 55 7 7 ALA CB C 24.1 . 1 56 7 7 ALA N N 124.7 . 1 57 8 8 VAL H H 8.55 . 1 58 8 8 VAL HA H 5.09 . 1 59 8 8 VAL HB H 1.90 . 1 60 8 8 VAL HG1 H 0.91 . 2 61 8 8 VAL HG2 H 0.92 . 2 62 8 8 VAL CA C 59.8 . 1 63 8 8 VAL CB C 35.6 . 1 64 8 8 VAL CG1 C 21.8 . 1 65 8 8 VAL CG2 C 21.0 . 1 66 8 8 VAL N N 118.4 . 1 67 9 9 TYR H H 8.93 . 1 68 9 9 TYR HA H 5.04 . 1 69 9 9 TYR HB2 H 3.02 . 2 70 9 9 TYR HB3 H 2.41 . 2 71 9 9 TYR HD1 H 6.01 . 3 72 9 9 TYR HD2 H 6.01 . 3 73 9 9 TYR HE1 H 6.18 . 3 74 9 9 TYR HE2 H 6.18 . 3 75 9 9 TYR CA C 56.3 . 1 76 9 9 TYR CB C 38.7 . 1 77 9 9 TYR CD1 C 133.4 . 1 78 9 9 TYR CE1 C 116.8 . 1 79 9 9 TYR N N 129.8 . 1 80 10 10 GLU H H 8.53 . 1 81 10 10 GLU HA H 4.36 . 1 82 10 10 GLU HB2 H 1.81 . 2 83 10 10 GLU HB3 H 1.72 . 2 84 10 10 GLU HG2 H 2.03 . 2 85 10 10 GLU HG3 H 2.09 . 2 86 10 10 GLU CA C 55.0 . 1 87 10 10 GLU CB C 33.2 . 1 88 10 10 GLU CG C 35.9 . 1 89 10 10 GLU N N 126.5 . 1 90 11 11 ASN H H 10.40 . 1 91 11 11 ASN HA H 4.21 . 1 92 11 11 ASN HB2 H 2.96 . 2 93 11 11 ASN HB3 H 2.67 . 2 94 11 11 ASN HD21 H 7.49 . 2 95 11 11 ASN HD22 H 6.82 . 2 96 11 11 ASN CA C 54.1 . 1 97 11 11 ASN CB C 38.0 . 1 98 11 11 ASN N N 123.2 . 1 99 11 11 ASN ND2 N 112.4 . 1 100 12 12 GLY H H 8.16 . 1 101 12 12 GLY HA2 H 3.45 . 2 102 12 12 GLY HA3 H 3.97 . 2 103 12 12 GLY CA C 45.4 . 1 104 12 12 GLY N N 102.8 . 1 105 13 13 VAL H H 7.35 . 1 106 13 13 VAL HA H 4.89 . 1 107 13 13 VAL HB H 2.08 . 1 108 13 13 VAL HG1 H 0.94 . 2 109 13 13 VAL HG2 H 0.81 . 2 110 13 13 VAL CA C 58.6 . 1 111 13 13 VAL CB C 35.9 . 1 112 13 13 VAL CG1 C 22.3 . 1 113 13 13 VAL CG2 C 18.0 . 1 114 13 13 VAL N N 112.0 . 1 115 14 14 PHE H H 8.89 . 1 116 14 14 PHE HA H 5.31 . 1 117 14 14 PHE HB2 H 2.58 . 2 118 14 14 PHE HB3 H 3.33 . 2 119 14 14 PHE HD1 H 7.01 . 3 120 14 14 PHE HD2 H 7.01 . 3 121 14 14 PHE HE1 H 6.97 . 3 122 14 14 PHE HE2 H 6.97 . 3 123 14 14 PHE HZ H 6.83 . 1 124 14 14 PHE CA C 56.7 . 1 125 14 14 PHE CB C 40.6 . 1 126 14 14 PHE CD1 C 131.0 . 1 127 14 14 PHE CE1 C 130.4 . 1 128 14 14 PHE CZ C 129.3 . 1 129 14 14 PHE N N 114.2 . 1 130 15 15 LYS H H 9.75 . 1 131 15 15 LYS HA H 5.06 . 1 132 15 15 LYS HB2 H 2.01 . 2 133 15 15 LYS HB3 H 1.88 . 2 134 15 15 LYS HD2 H 1.63 . 2 135 15 15 LYS HD3 H 1.63 . 2 136 15 15 LYS HE2 H 2.83 . 2 137 15 15 LYS HE3 H 2.83 . 2 138 15 15 LYS HG2 H 1.52 . 2 139 15 15 LYS HG3 H 1.29 . 2 140 15 15 LYS CA C 53.2 . 1 141 15 15 LYS CB C 33.1 . 1 142 15 15 LYS CD C 29.7 . 1 143 15 15 LYS CE C 42.1 . 1 144 15 15 LYS CG C 25.2 . 1 145 15 15 LYS N N 127.7 . 1 146 16 16 PRO HA H 4.79 . 1 147 16 16 PRO HB2 H 2.23 . 2 148 16 16 PRO HB3 H 2.63 . 2 149 16 16 PRO HD2 H 4.48 . 2 150 16 16 PRO HD3 H 4.33 . 2 151 16 16 PRO HG2 H 2.48 . 2 152 16 16 PRO HG3 H 2.04 . 2 153 16 16 PRO CA C 62.3 . 1 154 16 16 PRO CB C 33.2 . 1 155 16 16 PRO CD C 52.1 . 1 156 16 16 PRO CG C 28.1 . 1 157 17 17 LEU H H 8.86 . 1 158 17 17 LEU HA H 4.44 . 1 159 17 17 LEU HB2 H 1.74 . 2 160 17 17 LEU HB3 H 1.51 . 2 161 17 17 LEU HD1 H 0.82 . 2 162 17 17 LEU HD2 H 0.84 . 2 163 17 17 LEU HG H 1.59 . 1 164 17 17 LEU CA C 55.0 . 1 165 17 17 LEU CB C 41.5 . 1 166 17 17 LEU CD1 C 25.4 . 1 167 17 17 LEU CD2 C 22.7 . 1 168 17 17 LEU CG C 27.9 . 1 169 17 17 LEU N N 122.5 . 1 170 18 18 GLN H H 7.45 . 1 171 18 18 GLN HA H 4.60 . 1 172 18 18 GLN HB2 H 2.19 . 2 173 18 18 GLN HB3 H 2.04 . 2 174 18 18 GLN HE21 H 7.70 . 2 175 18 18 GLN HE22 H 6.95 . 2 176 18 18 GLN HG2 H 2.25 . 2 177 18 18 GLN HG3 H 2.34 . 2 178 18 18 GLN CA C 53.7 . 1 179 18 18 GLN CB C 32.6 . 1 180 18 18 GLN CG C 34.4 . 1 181 18 18 GLN N N 115.6 . 1 182 18 18 GLN NE2 N 112.4 . 1 183 19 19 LYS H H 8.30 . 1 184 19 19 LYS HA H 4.15 . 1 185 19 19 LYS HB2 H 1.74 . 2 186 19 19 LYS HB3 H 1.76 . 2 187 19 19 LYS HD2 H 1.67 . 2 188 19 19 LYS HD3 H 1.67 . 2 189 19 19 LYS HG2 H 1.46 . 2 190 19 19 LYS HG3 H 1.35 . 2 191 19 19 LYS CA C 57.3 . 1 192 19 19 LYS CB C 32.9 . 1 193 19 19 LYS CD C 29.4 . 1 194 19 19 LYS CG C 24.9 . 1 195 19 19 LYS N N 120.3 . 1 196 20 20 VAL H H 8.41 . 1 197 20 20 VAL HA H 4.24 . 1 198 20 20 VAL HB H 1.89 . 1 199 20 20 VAL HG1 H 0.65 . 2 200 20 20 VAL HG2 H 0.80 . 2 201 20 20 VAL CA C 60.5 . 1 202 20 20 VAL CB C 34.3 . 1 203 20 20 VAL CG1 C 22.2 . 1 204 20 20 VAL CG2 C 21.1 . 1 205 20 20 VAL N N 121.7 . 1 206 21 21 ASP H H 8.56 . 1 207 21 21 ASP HA H 4.76 . 1 208 21 21 ASP HB2 H 2.48 . 2 209 21 21 ASP HB3 H 2.67 . 2 210 21 21 ASP CA C 53.0 . 1 211 21 21 ASP CB C 40.4 . 1 212 21 21 ASP N N 125.8 . 1 213 22 22 LEU H H 6.76 . 1 214 22 22 LEU HA H 4.41 . 1 215 22 22 LEU HB2 H 0.69 . 2 216 22 22 LEU HB3 H 1.18 . 2 217 22 22 LEU HD1 H 0.54 . 2 218 22 22 LEU HD2 H 0.75 . 2 219 22 22 LEU HG H 1.22 . 1 220 22 22 LEU CA C 53.4 . 1 221 22 22 LEU CB C 45.5 . 1 222 22 22 LEU CD1 C 26.6 . 1 223 22 22 LEU CD2 C 24.0 . 1 224 22 22 LEU CG C 27.2 . 1 225 22 22 LEU N N 121.2 . 1 226 23 23 LYS H H 8.70 . 1 227 23 23 LYS HA H 4.34 . 1 228 23 23 LYS HB2 H 1.78 . 2 229 23 23 LYS HB3 H 1.81 . 2 230 23 23 LYS HD2 H 1.69 . 2 231 23 23 LYS HD3 H 1.69 . 2 232 23 23 LYS HE2 H 3.00 . 2 233 23 23 LYS HE3 H 3.00 . 2 234 23 23 LYS HG2 H 1.53 . 2 235 23 23 LYS HG3 H 1.52 . 2 236 23 23 LYS CA C 55.6 . 1 237 23 23 LYS CB C 33.5 . 1 238 23 23 LYS CD C 29.3 . 1 239 23 23 LYS CE C 42.1 . 1 240 23 23 LYS CG C 25.0 . 1 241 23 23 LYS N N 121.3 . 1 242 24 24 GLU H H 8.41 . 1 243 24 24 GLU HA H 4.03 . 1 244 24 24 GLU HB2 H 2.02 . 2 245 24 24 GLU HB3 H 1.99 . 2 246 24 24 GLU HG2 H 2.39 . 2 247 24 24 GLU HG3 H 2.29 . 2 248 24 24 GLU CA C 58.3 . 1 249 24 24 GLU CB C 29.6 . 1 250 24 24 GLU CG C 35.5 . 1 251 24 24 GLU N N 122.1 . 1 252 25 25 GLY H H 9.63 . 1 253 25 25 GLY HA2 H 4.29 . 2 254 25 25 GLY HA3 H 3.55 . 2 255 25 25 GLY CA C 45.5 . 1 256 25 25 GLY N N 116.0 . 1 257 26 26 GLU H H 8.02 . 1 258 26 26 GLU HA H 4.16 . 1 259 26 26 GLU HB2 H 2.37 . 2 260 26 26 GLU HB3 H 2.00 . 2 261 26 26 GLU HG2 H 2.40 . 2 262 26 26 GLU HG3 H 2.26 . 2 263 26 26 GLU CA C 58.0 . 1 264 26 26 GLU CB C 30.9 . 1 265 26 26 GLU CG C 36.6 . 1 266 26 26 GLU N N 122.2 . 1 267 27 27 ARG H H 8.61 . 1 268 27 27 ARG HA H 5.07 . 1 269 27 27 ARG HB2 H 1.95 . 2 270 27 27 ARG HB3 H 1.85 . 2 271 27 27 ARG HD2 H 3.22 . 2 272 27 27 ARG HD3 H 3.22 . 2 273 27 27 ARG HE H 7.37 . 1 274 27 27 ARG HG2 H 1.78 . 2 275 27 27 ARG HG3 H 1.60 . 2 276 27 27 ARG CA C 55.3 . 1 277 27 27 ARG CB C 31.1 . 1 278 27 27 ARG CD C 43.4 . 1 279 27 27 ARG CG C 28.3 . 1 280 27 27 ARG N N 125.8 . 1 281 27 27 ARG NE N 92.5 . 1 282 28 28 VAL H H 8.96 . 1 283 28 28 VAL HA H 4.88 . 1 284 28 28 VAL HB H 2.05 . 1 285 28 28 VAL HG1 H 0.88 . 2 286 28 28 VAL HG2 H 0.69 . 2 287 28 28 VAL CA C 58.9 . 1 288 28 28 VAL CB C 36.0 . 1 289 28 28 VAL CG1 C 22.3 . 1 290 28 28 VAL CG2 C 19.5 . 1 291 28 28 VAL N N 116.9 . 1 292 29 29 LYS H H 8.46 . 1 293 29 29 LYS HA H 4.84 . 1 294 29 29 LYS HB2 H 1.66 . 2 295 29 29 LYS HB3 H 1.48 . 2 296 29 29 LYS HD2 H 1.57 . 2 297 29 29 LYS HD3 H 1.57 . 2 298 29 29 LYS HE2 H 2.87 . 2 299 29 29 LYS HE3 H 2.87 . 2 300 29 29 LYS HG2 H 1.40 . 2 301 29 29 LYS HG3 H 1.21 . 2 302 29 29 LYS CA C 55.2 . 1 303 29 29 LYS CB C 34.3 . 1 304 29 29 LYS CD C 29.6 . 1 305 29 29 LYS CE C 42.1 . 1 306 29 29 LYS CG C 25.7 . 1 307 29 29 LYS N N 121.3 . 1 308 30 30 ILE H H 9.02 . 1 309 30 30 ILE HA H 4.46 . 1 310 30 30 ILE HB H 1.40 . 1 311 30 30 ILE HD1 H -0.06 . 1 312 30 30 ILE HG12 H 0.47 . 2 313 30 30 ILE HG13 H 1.17 . 2 314 30 30 ILE HG2 H 0.23 . 1 315 30 30 ILE CA C 59.6 . 1 316 30 30 ILE CB C 40.8 . 1 317 30 30 ILE CD1 C 13.4 . 1 318 30 30 ILE CG1 C 26.8 . 1 319 30 30 ILE CG2 C 17.8 . 1 320 30 30 ILE N N 120.7 . 1 321 31 31 LYS H H 8.52 . 1 322 31 31 LYS HA H 4.85 . 1 323 31 31 LYS HB2 H 1.70 . 2 324 31 31 LYS HB3 H 1.56 . 2 325 31 31 LYS HD2 H 1.53 . 2 326 31 31 LYS HD3 H 1.53 . 2 327 31 31 LYS HE2 H 2.79 . 2 328 31 31 LYS HE3 H 2.79 . 2 329 31 31 LYS HG2 H 1.22 . 2 330 31 31 LYS HG3 H 1.18 . 2 331 31 31 LYS CA C 54.6 . 1 332 31 31 LYS CB C 34.9 . 1 333 31 31 LYS CD C 29.8 . 1 334 31 31 LYS CE C 42.0 . 1 335 31 31 LYS CG C 25.6 . 1 336 31 31 LYS N N 125.0 . 1 337 32 32 LEU H H 8.81 . 1 338 32 32 LEU HA H 4.61 . 1 339 32 32 LEU HB2 H 1.54 . 2 340 32 32 LEU HB3 H 1.30 . 2 341 32 32 LEU HD1 H 0.71 . 2 342 32 32 LEU HD2 H 0.49 . 2 343 32 32 LEU HG H 1.44 . 1 344 32 32 LEU CA C 54.2 . 1 345 32 32 LEU CB C 43.6 . 1 346 32 32 LEU CD1 C 25.9 . 1 347 32 32 LEU CD2 C 24.9 . 1 348 32 32 LEU CG C 27.0 . 1 349 32 32 LEU N N 125.8 . 1 350 33 33 GLU H H 8.61 . 1 351 33 33 GLU HA H 4.49 . 1 352 33 33 GLU HB2 H 1.95 . 2 353 33 33 GLU HB3 H 1.77 . 2 354 33 33 GLU HG2 H 2.08 . 2 355 33 33 GLU HG3 H 2.10 . 2 356 33 33 GLU CA C 55.3 . 1 357 33 33 GLU CB C 31.3 . 1 358 33 33 GLU CG C 35.8 . 1 359 33 33 GLU N N 123.8 . 1 360 34 34 LEU H H 8.43 . 1 361 34 34 LEU HA H 4.45 . 1 362 34 34 LEU HB2 H 1.59 . 2 363 34 34 LEU HB3 H 1.59 . 2 364 34 34 LEU HD1 H 0.89 . 2 365 34 34 LEU HD2 H 0.85 . 2 366 34 34 LEU HG H 1.59 . 1 367 34 34 LEU CA C 54.8 . 1 368 34 34 LEU CB C 42.8 . 1 369 34 34 LEU CD1 C 25.3 . 1 370 34 34 LEU CD2 C 23.9 . 1 371 34 34 LEU CG C 27.5 . 1 372 34 34 LEU N N 124.4 . 1 373 35 35 LYS H H 8.50 . 1 374 35 35 LYS HA H 4.27 . 1 375 35 35 LYS HB2 H 1.70 . 2 376 35 35 LYS HB3 H 1.80 . 2 377 35 35 LYS HD2 H 1.68 . 2 378 35 35 LYS HD3 H 1.67 . 2 379 35 35 LYS HG2 H 1.34 . 2 380 35 35 LYS HG3 H 1.41 . 2 381 35 35 LYS CA C 56.7 . 1 382 35 35 LYS CB C 33.0 . 1 383 35 35 LYS CD C 28.8 . 1 384 35 35 LYS CG C 25.1 . 1 385 35 35 LYS N N 122.8 . 1 386 36 36 VAL H H 8.16 . 1 387 36 36 VAL HA H 4.13 . 1 388 36 36 VAL HB H 2.00 . 1 389 36 36 VAL HG1 H 0.87 . 2 390 36 36 VAL HG2 H 0.88 . 2 391 36 36 VAL CA C 61.9 . 1 392 36 36 VAL CB C 33.0 . 1 393 36 36 VAL CG1 C 20.7 . 1 394 36 36 VAL CG2 C 21.2 . 1 395 36 36 VAL N N 121.9 . 1 396 37 37 GLU H H 8.48 . 1 397 37 37 GLU HA H 4.59 . 1 398 37 37 GLU HB2 H 1.85 . 2 399 37 37 GLU HB3 H 2.02 . 2 400 37 37 GLU HG2 H 2.28 . 2 401 37 37 GLU HG3 H 2.27 . 2 402 37 37 GLU CA C 54.1 . 1 403 37 37 GLU CB C 29.9 . 1 404 37 37 GLU CG C 35.8 . 1 405 37 37 GLU N N 126.8 . 1 406 38 38 PRO HA H 4.41 . 1 407 38 38 PRO HB2 H 2.25 . 2 408 38 38 PRO HB3 H 1.90 . 2 409 38 38 PRO HD2 H 3.72 . 2 410 38 38 PRO HD3 H 3.79 . 2 411 38 38 PRO HG2 H 2.03 . 2 412 38 38 PRO HG3 H 1.99 . 2 413 38 38 PRO CA C 63.1 . 1 414 38 38 PRO CB C 32.1 . 1 415 38 38 PRO CD C 50.6 . 1 416 38 38 PRO CG C 27.6 . 1 417 39 39 ILE H H 8.12 . 1 418 39 39 ILE HA H 4.11 . 1 419 39 39 ILE HB H 1.80 . 1 420 39 39 ILE HD1 H 0.84 . 1 421 39 39 ILE HG12 H 1.44 . 2 422 39 39 ILE HG13 H 1.15 . 2 423 39 39 ILE HG2 H 0.86 . 1 424 39 39 ILE CA C 61.3 . 1 425 39 39 ILE CB C 39.2 . 1 426 39 39 ILE CD1 C 13.4 . 1 427 39 39 ILE CG1 C 27.5 . 1 428 39 39 ILE CG2 C 17.7 . 1 429 39 39 ILE N N 120.4 . 1 430 40 40 ASP H H 8.37 . 1 431 40 40 ASP HA H 4.63 . 1 432 40 40 ASP HB2 H 2.58 . 2 433 40 40 ASP HB3 H 2.72 . 2 434 40 40 ASP CA C 53.7 . 1 435 40 40 ASP CB C 41.3 . 1 436 40 40 ASP N N 124.2 . 1 437 41 41 LEU H H 8.31 . 1 438 41 41 LEU HA H 4.29 . 1 439 41 41 LEU HB2 H 1.61 . 2 440 41 41 LEU HB3 H 1.64 . 2 441 41 41 LEU HD1 H 0.88 . 2 442 41 41 LEU HD2 H 0.82 . 2 443 41 41 LEU HG H 1.61 . 1 444 41 41 LEU CA C 55.3 . 1 445 41 41 LEU CB C 42.4 . 1 446 41 41 LEU CD1 C 25.3 . 1 447 41 41 LEU CD2 C 23.4 . 1 448 41 41 LEU CG C 26.9 . 1 449 42 42 GLY H H 8.40 . 1 450 42 42 GLY HA2 H 3.90 . 2 451 42 42 GLY HA3 H 3.90 . 2 452 42 42 GLY CA C 45.2 . 1 453 42 42 GLY N N 109.0 . 1 454 43 43 GLU H H 8.10 . 1 455 43 43 GLU HA H 4.58 . 1 456 43 43 GLU HB2 H 1.85 . 2 457 43 43 GLU HB3 H 2.02 . 2 458 43 43 GLU HG2 H 2.27 . 2 459 43 43 GLU HG3 H 2.27 . 2 460 43 43 GLU CA C 54.2 . 1 461 43 43 GLU CB C 29.8 . 1 462 43 43 GLU CG C 35.9 . 1 463 43 43 GLU N N 121.5 . 1 464 44 44 PRO HA H 4.43 . 1 465 44 44 PRO HB2 H 1.87 . 2 466 44 44 PRO HB3 H 2.23 . 2 467 44 44 PRO HD2 H 3.65 . 2 468 44 44 PRO HD3 H 3.72 . 2 469 44 44 PRO HG2 H 1.99 . 2 470 44 44 PRO HG3 H 1.99 . 2 471 44 44 PRO CA C 63.0 . 1 472 44 44 PRO CB C 32.1 . 1 473 44 44 PRO CD C 50.6 . 1 474 44 44 PRO CG C 27.5 . 1 475 45 45 VAL H H 8.23 . 1 476 45 45 VAL HA H 4.10 . 1 477 45 45 VAL HB H 2.03 . 1 478 45 45 VAL HG1 H 0.93 . 2 479 45 45 VAL HG2 H 0.93 . 2 480 45 45 VAL CA C 62.3 . 1 481 45 45 VAL CB C 33.1 . 1 482 45 45 VAL CG1 C 21.3 . 1 483 45 45 VAL CG2 C 20.8 . 1 484 45 45 VAL N N 120.4 . 1 485 46 46 SER H H 8.39 . 1 486 46 46 SER HA H 4.52 . 1 487 46 46 SER HB2 H 3.86 . 2 488 46 46 SER HB3 H 3.97 . 2 489 46 46 SER CA C 57.7 . 1 490 46 46 SER CB C 64.1 . 1 491 46 46 SER N N 119.9 . 1 492 47 47 VAL H H 8.34 . 1 493 47 47 VAL HA H 4.00 . 1 494 47 47 VAL HB H 2.10 . 1 495 47 47 VAL HG1 H 0.94 . 2 496 47 47 VAL HG2 H 0.92 . 2 497 47 47 VAL CA C 63.5 . 1 498 47 47 VAL CB C 32.4 . 1 499 47 47 VAL CG1 C 20.9 . 1 500 47 47 VAL CG2 C 21.0 . 1 501 47 47 VAL N N 122.2 . 1 502 48 48 GLU H H 8.39 . 1 503 48 48 GLU HA H 4.15 . 1 504 48 48 GLU HB2 H 1.99 . 2 505 48 48 GLU HB3 H 1.93 . 2 506 48 48 GLU HG2 H 2.25 . 2 507 48 48 GLU HG3 H 2.26 . 2 508 48 48 GLU CA C 57.5 . 1 509 48 48 GLU CB C 30.1 . 1 510 48 48 GLU CG C 36.4 . 1 511 48 48 GLU N N 122.5 . 1 512 49 49 GLU H H 8.15 . 1 513 49 49 GLU HA H 4.13 . 1 514 49 49 GLU HB2 H 2.00 . 2 515 49 49 GLU HB3 H 2.01 . 2 516 49 49 GLU HG2 H 2.22 . 2 517 49 49 GLU HG3 H 2.21 . 2 518 49 49 GLU CA C 57.6 . 1 519 49 49 GLU CB C 30.1 . 1 520 49 49 GLU CG C 36.3 . 1 521 49 49 GLU N N 121.4 . 1 522 50 50 ILE H H 8.04 . 1 523 50 50 ILE HA H 3.93 . 1 524 50 50 ILE HB H 1.85 . 1 525 50 50 ILE HD1 H 0.80 . 1 526 50 50 ILE HG12 H 1.15 . 2 527 50 50 ILE HG13 H 1.49 . 2 528 50 50 ILE HG2 H 0.86 . 1 529 50 50 ILE CA C 62.4 . 1 530 50 50 ILE CB C 38.4 . 1 531 50 50 ILE CD1 C 13.0 . 1 532 50 50 ILE CG1 C 28.1 . 1 533 50 50 ILE CG2 C 17.5 . 1 534 50 50 ILE N N 121.4 . 1 535 51 51 LYS H H 8.11 . 1 536 51 51 LYS HA H 4.14 . 1 537 51 51 LYS HB2 H 1.75 . 2 538 51 51 LYS HB3 H 1.79 . 2 539 51 51 LYS HD2 H 1.61 . 2 540 51 51 LYS HD3 H 1.61 . 2 541 51 51 LYS HG2 H 1.45 . 2 542 51 51 LYS HG3 H 1.35 . 2 543 51 51 LYS CA C 57.6 . 1 544 51 51 LYS CB C 33.0 . 1 545 51 51 LYS CD C 29.3 . 1 546 51 51 LYS CG C 25.1 . 1 547 51 51 LYS N N 123.3 . 1 548 52 52 LYS H H 7.94 . 1 549 52 52 LYS HA H 4.22 . 1 550 52 52 LYS HB2 H 1.76 . 2 551 52 52 LYS HB3 H 1.76 . 2 552 52 52 LYS HD2 H 1.61 . 2 553 52 52 LYS HD3 H 1.61 . 2 554 52 52 LYS HG2 H 1.45 . 2 555 52 52 LYS HG3 H 1.33 . 2 556 52 52 LYS CA C 57.2 . 1 557 52 52 LYS CB C 32.9 . 1 558 52 52 LYS CD C 29.4 . 1 559 52 52 LYS CG C 24.9 . 1 560 52 52 LYS N N 120.9 . 1 561 53 53 ILE H H 8.00 . 1 562 53 53 ILE HA H 4.03 . 1 563 53 53 ILE HB H 1.83 . 1 564 53 53 ILE HD1 H 0.76 . 1 565 53 53 ILE HG12 H 1.08 . 2 566 53 53 ILE HG13 H 1.47 . 2 567 53 53 ILE HG2 H 0.84 . 1 568 53 53 ILE CA C 62.0 . 1 569 53 53 ILE CB C 38.4 . 1 570 53 53 ILE CD1 C 13.1 . 1 571 53 53 ILE CG1 C 27.9 . 1 572 53 53 ILE CG2 C 17.6 . 1 573 53 53 ILE N N 121.4 . 1 574 54 54 ARG H H 8.30 . 1 575 54 54 ARG HA H 4.23 . 1 576 54 54 ARG HB2 H 1.82 . 2 577 54 54 ARG HB3 H 1.75 . 2 578 54 54 ARG HD2 H 3.03 . 2 579 54 54 ARG HD3 H 3.05 . 2 580 54 54 ARG HE H 7.14 . 1 581 54 54 ARG HG2 H 1.60 . 2 582 54 54 ARG HG3 H 1.50 . 2 583 54 54 ARG CA C 57.0 . 1 584 54 54 ARG CB C 30.8 . 1 585 54 54 ARG CD C 43.4 . 1 586 54 54 ARG CG C 27.3 . 1 587 54 54 ARG N N 124.1 . 1 588 54 54 ARG NE N 92.8 . 1 589 55 55 ASP HA H 4.60 . 1 590 55 55 ASP HB2 H 2.71 . 2 591 55 55 ASP HB3 H 2.72 . 2 592 55 55 ASP CA C 54.2 . 1 593 55 55 ASP CB C 41.2 . 1 594 56 56 GLY H H 8.25 . 1 595 56 56 GLY HA2 H 3.96 . 2 596 56 56 GLY HA3 H 3.97 . 2 597 56 56 GLY CA C 45.9 . 1 598 56 56 GLY N N 108.7 . 1 599 57 57 THR H H 8.18 . 1 600 57 57 THR HA H 4.29 . 1 601 57 57 THR HB H 4.21 . 1 602 57 57 THR HG2 H 1.13 . 1 603 57 57 THR CA C 62.5 . 1 604 57 57 THR CB C 69.5 . 1 605 57 57 THR CG2 C 21.8 . 1 606 57 57 THR N N 113.7 . 1 607 58 58 TRP H H 8.10 . 1 608 58 58 TRP HA H 4.55 . 1 609 58 58 TRP HB2 H 3.25 . 2 610 58 58 TRP HB3 H 3.25 . 2 611 58 58 TRP HD1 H 7.24 . 1 612 58 58 TRP HE1 H 10.18 . 1 613 58 58 TRP HH2 H 7.15 . 1 614 58 58 TRP HZ2 H 7.41 . 1 615 58 58 TRP HZ3 H 7.06 . 1 616 58 58 TRP CA C 58.0 . 1 617 58 58 TRP CB C 29.3 . 1 618 58 58 TRP CD1 C 126.9 . 1 619 58 58 TRP CH2 C 124.5 . 1 620 58 58 TRP CZ2 C 114.8 . 1 621 58 58 TRP CZ3 C 122.0 . 1 622 58 58 TRP N N 123.4 . 1 623 58 58 TRP NE1 N 129.8 . 1 624 59 59 MET H H 7.99 . 1 625 59 59 MET HA H 4.20 . 1 626 59 59 MET HB2 H 1.90 . 2 627 59 59 MET HB3 H 1.81 . 2 628 59 59 MET HG2 H 2.27 . 2 629 59 59 MET HG3 H 2.22 . 2 630 59 59 MET CA C 55.8 . 1 631 59 59 MET CB C 32.8 . 1 632 59 59 MET CG C 32.1 . 1 633 59 59 MET N N 121.3 . 1 634 60 60 SER H H 8.08 . 1 635 60 60 SER HA H 4.29 . 1 636 60 60 SER HB2 H 3.81 . 2 637 60 60 SER HB3 H 3.89 . 2 638 60 60 SER CA C 58.8 . 1 639 60 60 SER CB C 63.4 . 1 640 60 60 SER N N 116.1 . 1 641 61 61 SER H H 8.18 . 1 642 61 61 SER HA H 4.37 . 1 643 61 61 SER HB2 H 3.84 . 2 644 61 61 SER HB3 H 3.91 . 2 645 61 61 SER CA C 59.0 . 1 646 61 61 SER CB C 63.6 . 1 647 61 61 SER N N 117.4 . 1 648 62 62 LEU H H 8.03 . 1 649 62 62 LEU HA H 4.19 . 1 650 62 62 LEU HB2 H 1.50 . 2 651 62 62 LEU HB3 H 1.56 . 2 652 62 62 LEU HD1 H 0.79 . 2 653 62 62 LEU HD2 H 0.83 . 2 654 62 62 LEU HG H 1.54 . 1 655 62 62 LEU CA C 55.7 . 1 656 62 62 LEU CB C 42.3 . 1 657 62 62 LEU CD1 C 23.5 . 1 658 62 62 LEU CD2 C 25.1 . 1 659 62 62 LEU CG C 27.1 . 1 660 62 62 LEU N N 123.2 . 1 661 63 63 GLU H H 8.04 . 1 662 63 63 GLU HA H 4.11 . 1 663 63 63 GLU HB2 H 1.86 . 2 664 63 63 GLU HB3 H 1.85 . 2 665 63 63 GLU HG2 H 2.18 . 2 666 63 63 GLU HG3 H 2.12 . 2 667 63 63 GLU CA C 56.7 . 1 668 63 63 GLU CB C 30.1 . 1 669 63 63 GLU CG C 36.0 . 1 670 63 63 GLU N N 119.9 . 1 671 64 64 HIS H H 8.25 . 1 672 64 64 HIS HA H 4.61 . 1 673 64 64 HIS HB2 H 3.13 . 2 674 64 64 HIS HB3 H 3.05 . 2 675 64 64 HIS HD2 H 7.11 . 1 676 64 64 HIS CA C 55.6 . 1 677 64 64 HIS CB C 29.7 . 1 678 64 64 HIS CD2 C 119.8 . 1 679 64 64 HIS N N 118.7 . 1 680 65 65 HIS H H 8.29 . 1 681 65 65 HIS HA H 4.42 . 1 682 65 65 HIS HB2 H 3.20 . 2 683 65 65 HIS HB3 H 3.09 . 2 684 65 65 HIS HD2 H 7.08 . 1 685 65 65 HIS CA C 57.1 . 1 686 65 65 HIS CB C 29.6 . 1 687 65 65 HIS CD2 C 119.8 . 1 688 65 65 HIS N N 125.5 . 1 stop_ save_