data_4144 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, 15N Sequential Assignment of the RNA Polymerase 'H' Subunit from Methanococcus jannaschii ; _BMRB_accession_number 4144 _BMRB_flat_file_name bmr4144.str _Entry_type original _Submission_date 1998-05-26 _Accession_date 1998-05-26 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; The data reported here represent subunit H (rpb5) from Methanococcus jannaschii ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hodach Meri . . 2 Elorante Jyrki . . 3 Kostourou Vassiliki . . 4 Wienzierl Robert . . 5 Matthews Stephen . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 151 "13C chemical shifts" 219 "15N chemical shifts" 68 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1998-10-05 original author . stop_ _Original_release_date 1998-10-05 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Hodach, M., Elorante, J., Kostourou, V., Wienzierl, R., and Matthews, S., "1H, 13C, 15N Sequential Assignment of the RNA Polymerase 'H' Subunit from Methanococcus jannaschii," J. Biomol. NMR, submitted (1998). ; _Citation_title ; 1H, 13C, 15N Sequential Assignment of the RNA Polymerase 'H' Subunit from Methanococcus jannaschii ; _Citation_status submitted _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 Hodach Meri . . 2 Elorante Jyrki . . 3 Kostourou Vassiliki . . 4 Wienzierl Robert . . 5 Matthews Stephen . . stop_ _Journal_abbreviation 'J Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 1998 _Details . loop_ _Keyword NMR 'nuclear magnetic resonance' protein 'resonance assignments' rpb5 stop_ save_ ################################## # Molecular system description # ################################## save_system_rpb5 _Saveframe_category molecular_system _Mol_system_name 'subunit H, RPB5' _Abbreviation_common rpb5 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label rpb5 $rpb5 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'RNA polymerase subunit' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_rpb5 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common RPB5 _Name_variant 'subunit H' _Abbreviation_common rpb5 _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 78 _Mol_residue_sequence ; MKVTDHILVPKHEIVPKEEV EEILKRYNIKIQQLPKIYED DPVIQEIGAKEGDVVRVIRK SPTAGVSIAYRLVIKRII ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 VAL 4 THR 5 ASP 6 HIS 7 ILE 8 LEU 9 VAL 10 PRO 11 LYS 12 HIS 13 GLU 14 ILE 15 VAL 16 PRO 17 LYS 18 GLU 19 GLU 20 VAL 21 GLU 22 GLU 23 ILE 24 LEU 25 LYS 26 ARG 27 TYR 28 ASN 29 ILE 30 LYS 31 ILE 32 GLN 33 GLN 34 LEU 35 PRO 36 LYS 37 ILE 38 TYR 39 GLU 40 ASP 41 ASP 42 PRO 43 VAL 44 ILE 45 GLN 46 GLU 47 ILE 48 GLY 49 ALA 50 LYS 51 GLU 52 GLY 53 ASP 54 VAL 55 VAL 56 ARG 57 VAL 58 ILE 59 ARG 60 LYS 61 SER 62 PRO 63 THR 64 ALA 65 GLY 66 VAL 67 SER 68 ILE 69 ALA 70 TYR 71 ARG 72 LEU 73 VAL 74 ILE 75 LYS 76 ARG 77 ILE 78 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-15 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 1HMJ "Solution Structure Of Rna Polymerase Subunit H" 100.00 78 100.00 100.00 1.39e-44 GB AAB99042 "DNA-directed RNA polymerase, subunit H (rpoH) [Methanocaldococcus jannaschii DSM 2661]" 100.00 78 100.00 100.00 1.39e-44 SP Q58443 "RecName: Full=DNA-directed RNA polymerase subunit H" 100.00 78 100.00 100.00 1.39e-44 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $rpb5 'Methanococcus jannaschii' 2190 Archaea Euryarchaeota Methanococcus jannaschii 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 $rpb5 'recombinant technology' 'M. jannaschii' Methanoccocus jannaschii . 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 $rpb5 1.0 mM [U-13C;U-15N] H2O 90 % . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX-500 _Field_strength 500 _Details . 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 302 . 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 DSS C 13 . ppm 0.0 . indirect . . . 0.251449519 DSS H 1 methyl ppm 0.0 external direct . . . . DSS N 15 . ppm 0.0 . indirect . . . 0.101329122 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_one _Saveframe_category assigned_chemical_shifts _Details ; The chemical shifts recorded in this save frame are from amino acid residues where only a single set of shifts were observed. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name rpb5 _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 H H 8.33 0.01 1 2 . 1 MET N N 121.3 0.2 1 3 . 1 MET HA H 4.6 0.01 1 4 . 1 MET CA C 53.1 0.2 1 5 . 1 MET CB C 30.6 0.2 1 6 . 1 MET C C 173.4 0.2 1 7 . 2 LYS H H 8.44 0.01 1 8 . 2 LYS N N 123.8 0.2 1 9 . 2 LYS HA H 4.3 0.01 1 10 . 2 LYS CA C 53.9 0.2 1 11 . 2 LYS CB C 30.7 0.2 1 12 . 2 LYS C C 174.2 0.2 1 13 . 3 VAL H H 8.29 0.01 1 14 . 3 VAL N N 121.8 0.2 1 15 . 3 VAL HA H 4.1 0.01 1 16 . 3 VAL CA C 60.1 0.2 1 17 . 3 VAL CB C 30.3 0.2 1 18 . 3 VAL C C 174.0 0.2 1 19 . 4 THR H H 8.04 0.01 1 20 . 4 THR HA H 4.3 0.01 1 21 . 4 THR CA C 59.2 0.2 1 22 . 4 THR CB C 58.6 0.2 1 23 . 4 THR C C 171.7 0.2 1 24 . 5 ASP H H 8.11 0.01 1 25 . 5 ASP N N 122.1 0.2 1 26 . 5 ASP HA H 4.1 0.01 1 27 . 5 ASP CA C 51.9 0.2 1 28 . 5 ASP CB C 38.7 0.2 1 29 . 5 ASP C C 173.5 0.2 1 30 . 6 HIS H H 8.43 0.01 1 31 . 6 HIS N N 118.1 0.2 1 32 . 6 HIS HA H 4.6 0.01 1 33 . 6 HIS CA C 52.9 0.2 1 34 . 6 HIS CB C 26.5 0.2 1 35 . 6 HIS C C 171.8 0.2 1 36 . 7 ILE H H 8.10 0.01 1 37 . 7 ILE N N 120.8 0.2 1 38 . 7 ILE HA H 4.1 0.01 1 39 . 7 ILE CA C 58.9 0.2 1 40 . 7 ILE CB C 36.0 0.2 1 41 . 7 ILE C C 173.4 0.2 1 42 . 8 LEU H H 8.27 0.01 1 43 . 8 LEU N N 124.9 0.2 1 44 . 8 LEU HA H 4.4 0.01 1 45 . 8 LEU CA C 52.4 0.2 1 46 . 8 LEU CB C 39.7 0.2 1 47 . 8 LEU C C 174.2 0.2 1 48 . 9 VAL H H 7.98 0.01 1 49 . 9 VAL N N 122.1 0.2 1 50 . 9 VAL HA H 4.4 0.01 1 51 . 9 VAL CA C 57.3 0.2 1 52 . 10 PRO CA C 60.5 0.2 1 53 . 10 PRO CB C 29.5 0.2 1 54 . 10 PRO C C 173.5 0.2 1 55 . 11 LYS H H 8.18 0.01 1 56 . 11 LYS N N 126.7 0.2 1 57 . 11 LYS HA H 4.4 0.01 1 58 . 11 LYS CA C 53.5 0.2 1 59 . 11 LYS CB C 31.2 0.2 1 60 . 11 LYS C C 172.9 0.2 1 61 . 12 HIS H H 8.45 0.01 1 62 . 12 HIS N N 117.7 0.2 1 63 . 12 HIS HA H 5.4 0.01 1 64 . 12 HIS CA C 52.7 0.2 1 65 . 12 HIS CB C 28.7 0.2 1 66 . 12 HIS C C 171.9 0.2 1 67 . 13 GLU H H 8.73 0.01 1 68 . 13 GLU N N 117.7 0.2 1 69 . 13 GLU HA H 4.8 0.01 1 70 . 13 GLU CA C 52.2 0.2 1 71 . 13 GLU CB C 31.4 0.2 1 72 . 13 GLU C C 172.3 0.2 1 73 . 14 ILE H H 8.88 0.01 1 74 . 14 ILE N N 108.1 0.2 1 75 . 14 ILE HA H 4.1 0.01 1 76 . 14 ILE CA C 60.3 0.2 1 77 . 14 ILE CB C 36.3 0.2 1 78 . 14 ILE C C 173.8 0.2 1 79 . 15 VAL H H 9.01 0.01 1 80 . 15 VAL HA H 4.2 0.01 1 81 . 15 VAL CA C 59.7 0.2 1 82 . 16 PRO HA H 4.4 0.01 1 83 . 16 PRO CA C 60.5 0.2 1 84 . 16 PRO CB C 30.4 0.2 1 85 . 16 PRO C C 176.1 0.2 1 86 . 17 LYS H H 8.72 0.01 1 87 . 17 LYS N N 123.1 0.2 1 88 . 17 LYS HA H 3.9 0.01 1 89 . 17 LYS CA C 57.9 0.2 1 90 . 17 LYS CB C 29.9 0.2 1 91 . 17 LYS C C 176.5 0.2 1 92 . 18 GLU H H 9.51 0.01 1 93 . 18 GLU N N 116.8 0.2 1 94 . 18 GLU HA H 4.1 0.01 1 95 . 18 GLU CA C 57.0 0.2 1 96 . 18 GLU CB C 26.0 0.2 1 97 . 18 GLU C C 175.6 0.2 1 98 . 19 GLU H H 7.63 0.01 1 99 . 19 GLU N N 118.8 0.2 1 100 . 19 GLU HA H 4.3 0.01 1 101 . 19 GLU CA C 55.0 0.2 1 102 . 19 GLU CB C 27.9 0.2 1 103 . 19 GLU C C 175.5 0.2 1 104 . 20 VAL H H 7.65 0.01 1 105 . 20 VAL N N 119.8 0.2 1 106 . 20 VAL HA H 3.2 0.01 1 107 . 20 VAL CA C 65.1 0.2 1 108 . 20 VAL CB C 29.2 0.2 1 109 . 20 VAL C C 174.4 0.2 1 110 . 21 GLU H H 8.04 0.01 1 111 . 21 GLU N N 115.9 0.2 1 112 . 21 GLU HA H 3.8 0.01 1 113 . 21 GLU CA C 57.2 0.2 1 114 . 21 GLU CB C 26.6 0.2 1 115 . 21 GLU C C 176.4 0.2 1 116 . 22 GLU H H 7.40 0.01 1 117 . 22 GLU N N 117.1 0.2 1 118 . 22 GLU HA H 4.0 0.01 1 119 . 22 GLU CA C 56.6 0.2 1 120 . 22 GLU CB C 26.8 0.2 1 121 . 22 GLU C C 176.5 0.2 1 122 . 23 ILE H H 7.79 0.01 1 123 . 23 ILE N N 120.9 0.2 1 124 . 23 ILE HA H 3.5 0.01 1 125 . 23 ILE CA C 62.5 0.2 1 126 . 23 ILE CB C 35.5 0.2 1 127 . 23 ILE C C 175.3 0.2 1 128 . 24 LEU H H 8.12 0.01 1 129 . 24 LEU N N 117.2 0.2 1 130 . 24 LEU HA H 3.9 0.01 1 131 . 24 LEU CA C 55.6 0.2 1 132 . 24 LEU CB C 36.7 0.2 1 133 . 24 LEU C C 177.7 0.2 1 134 . 25 LYS H H 7.65 0.01 1 135 . 25 LYS N N 116.6 0.2 1 136 . 25 LYS HA H 4.1 0.01 1 137 . 25 LYS CA C 56.5 0.2 1 138 . 25 LYS CB C 30.2 0.2 1 139 . 25 LYS C C 177.2 0.2 1 140 . 26 ARG H H 8.01 0.01 1 141 . 26 ARG N N 119.6 0.2 1 142 . 26 ARG HA H 3.9 0.01 1 143 . 26 ARG CA C 56.5 0.2 1 144 . 26 ARG CB C 27.5 0.2 1 145 . 26 ARG C C 175.8 0.2 1 146 . 27 TYR H H 7.67 0.01 1 147 . 27 TYR N N 113.9 0.2 1 148 . 27 TYR HA H 4.5 0.01 1 149 . 27 TYR CA C 55.5 0.2 1 150 . 27 TYR CB C 36.2 0.2 1 151 . 27 TYR C C 172.3 0.2 1 152 . 28 ASN H H 7.95 0.01 1 153 . 28 ASN N N 118.7 0.2 1 154 . 28 ASN HA H 4.4 0.01 1 155 . 28 ASN CA C 51.6 0.2 1 156 . 28 ASN CB C 34.6 0.2 1 157 . 28 ASN C C 171.7 0.2 1 158 . 29 ILE H H 7.84 0.01 1 159 . 29 ILE N N 111.5 0.2 1 160 . 29 ILE HA H 4.7 0.01 1 161 . 29 ILE CA C 57.2 0.2 1 162 . 29 ILE CB C 40.1 0.2 1 163 . 29 ILE C C 176.2 0.2 1 164 . 30 LYS H H 8.07 0.01 1 165 . 30 LYS N N 119.1 0.2 1 166 . 30 LYS HA H 4.6 0.01 1 167 . 30 LYS CA C 51.9 0.2 1 168 . 30 LYS CB C 31.6 0.2 1 169 . 30 LYS C C 176.5 0.2 1 170 . 31 ILE H H 8.80 0.01 1 171 . 31 ILE N N 121.9 0.2 1 172 . 31 ILE HA H 3.7 0.01 1 173 . 31 ILE CA C 62.7 0.2 1 174 . 31 ILE CB C 35.5 0.2 1 175 . 31 ILE C C 173.7 0.2 1 176 . 32 GLN H H 7.98 0.01 1 177 . 32 GLN N N 114.5 0.2 1 178 . 32 GLN HA H 4.0 0.01 1 179 . 32 GLN CA C 55.6 0.2 1 180 . 32 GLN CB C 25.0 0.2 1 181 . 32 GLN C C 174.5 0.2 1 182 . 33 GLN H H 8.12 0.01 1 183 . 33 GLN HA H 3.9 0.01 1 184 . 33 GLN CA C 53.5 0.2 1 185 . 33 GLN CB C 27.5 0.2 1 186 . 33 GLN C C 174.8 0.2 1 187 . 34 LEU H H 7.41 0.01 1 188 . 34 LEU N N 121.7 0.2 1 189 . 34 LEU HA H 4.3 0.01 1 190 . 34 LEU CA C 51.4 0.2 1 191 . 35 PRO HA H 4.5 0.01 1 192 . 35 PRO CA C 60.2 0.2 1 193 . 35 PRO CB C 28.9 0.2 1 194 . 35 PRO C C 173.1 0.2 1 195 . 36 LYS H H 8.20 0.01 1 196 . 36 LYS N N 117.7 0.2 1 197 . 36 LYS HA H 5.2 0.01 1 198 . 36 LYS CA C 51.8 0.2 1 199 . 36 LYS CB C 31.5 0.2 1 200 . 36 LYS C C 174.5 0.2 1 201 . 37 ILE H H 8.61 0.01 1 202 . 37 ILE N N 121.9 0.2 1 203 . 37 ILE HA H 4.2 0.01 1 204 . 37 ILE CA C 57.7 0.2 1 205 . 37 ILE CB C 40.2 0.2 1 206 . 37 ILE C C 169.9 0.2 1 207 . 38 TYR H H 8.17 0.01 1 208 . 38 TYR N N 123.9 0.2 1 209 . 38 TYR HA H 5.2 0.01 1 210 . 38 TYR CA C 56.2 0.2 1 211 . 38 TYR CB C 37.5 0.2 1 212 . 38 TYR C C 176.0 0.2 1 213 . 39 GLU H H 8.54 0.01 1 214 . 39 GLU N N 117.9 0.2 1 215 . 39 GLU CA C 55.7 0.2 1 216 . 39 GLU CB C 28.0 0.2 1 217 . 39 GLU C C 172.0 0.2 1 218 . 40 ASP H H 7.68 0.01 1 219 . 40 ASP N N 110.6 0.2 1 220 . 40 ASP HA H 4.5 0.01 1 221 . 40 ASP CA C 50.0 0.2 1 222 . 40 ASP CB C 37.3 0.2 1 223 . 40 ASP C C 173.6 0.2 1 224 . 41 ASP H H 7.62 0.01 1 225 . 41 ASP N N 124.0 0.2 1 226 . 41 ASP HA H 4.7 0.01 1 227 . 41 ASP CA C 50.6 0.2 1 228 . 42 PRO HA H 4.3 0.01 1 229 . 42 PRO CA C 63.4 0.2 1 230 . 42 PRO CB C 30.2 0.2 1 231 . 42 PRO C C 176.8 0.2 1 232 . 43 VAL H H 8.37 0.01 1 233 . 43 VAL N N 114.0 0.2 1 234 . 43 VAL HA H 3.9 0.01 1 235 . 43 VAL CA C 62.5 0.2 1 236 . 43 VAL CB C 28.7 0.2 1 237 . 43 VAL C C 174.8 0.2 1 238 . 44 ILE H H 7.23 0.01 1 239 . 44 ILE N N 118.4 0.2 1 240 . 44 ILE HA H 3.9 0.01 1 241 . 44 ILE CA C 57.6 0.2 1 242 . 44 ILE CB C 31.9 0.2 1 243 . 44 ILE C C 176.2 0.2 1 244 . 45 GLN H H 8.07 0.01 1 245 . 45 GLN N N 118.5 0.2 1 246 . 45 GLN HA H 4.2 0.01 1 247 . 45 GLN CA C 56.3 0.2 1 248 . 45 GLN CB C 26.5 0.2 1 249 . 45 GLN C C 177.2 0.2 1 250 . 46 GLU H H 7.88 0.01 1 251 . 46 GLU N N 117.0 0.2 1 252 . 46 GLU HA H 4.1 0.01 1 253 . 46 GLU CA C 56.6 0.2 1 254 . 46 GLU CB C 27.0 0.2 1 255 . 46 GLU C C 175.7 0.2 1 256 . 47 ILE H H 7.13 0.01 1 257 . 47 ILE N N 108.2 0.2 1 258 . 47 ILE HA H 4.5 0.01 1 259 . 47 ILE CA C 59.0 0.2 1 260 . 47 ILE CB C 36.0 0.2 1 261 . 47 ILE C C 174.0 0.2 1 262 . 48 GLY H H 7.74 0.01 1 263 . 48 GLY N N 109.2 0.2 1 264 . 48 GLY HA2 H 3.9 0.01 1 265 . 48 GLY HA3 H 3.9 0.01 1 266 . 48 GLY CA C 44.0 0.2 1 267 . 48 GLY C C 172.5 0.2 1 268 . 49 ALA H H 7.07 0.01 1 269 . 49 ALA N N 120.5 0.2 1 270 . 49 ALA HA H 4.5 0.01 1 271 . 49 ALA CA C 49.0 0.2 1 272 . 49 ALA CB C 19.0 0.2 1 273 . 49 ALA C C 172.4 0.2 1 274 . 50 LYS H H 9.09 0.01 1 275 . 50 LYS N N 118.1 0.2 1 276 . 50 LYS HA H 4.7 0.01 1 277 . 50 LYS CA C 51.2 0.2 1 278 . 50 LYS CB C 28.8 0.2 1 279 . 50 LYS C C 171.9 0.2 1 280 . 51 GLU H H 8.73 0.01 1 281 . 51 GLU N N 115.4 0.2 1 282 . 51 GLU HA H 3.5 0.01 1 283 . 51 GLU CA C 55.3 0.2 1 284 . 51 GLU CB C 27.0 0.2 1 285 . 51 GLU C C 174.1 0.2 1 286 . 52 GLY H H 8.82 0.01 1 287 . 52 GLY N N 117.8 0.2 1 288 . 52 GLY HA2 H 4.5 0.01 1 289 . 52 GLY HA3 H 4.5 0.01 1 290 . 52 GLY CA C 42.4 0.2 1 291 . 52 GLY C C 172.0 0.2 1 292 . 53 ASP H H 8.46 0.01 1 293 . 53 ASP N N 120.5 0.2 1 294 . 53 ASP HA H 4.6 0.01 1 295 . 53 ASP CA C 52.6 0.2 1 296 . 53 ASP CB C 38.6 0.2 1 297 . 53 ASP C C 171.8 0.2 1 298 . 54 VAL H H 8.79 0.01 1 299 . 54 VAL N N 120.3 0.2 1 300 . 54 VAL HA H 4.9 0.01 1 301 . 54 VAL CA C 58.5 0.2 1 302 . 54 VAL CB C 30.4 0.2 1 303 . 54 VAL C C 172.5 0.2 1 304 . 55 VAL H H 9.15 0.01 1 305 . 55 VAL N N 122.0 0.2 1 306 . 55 VAL HA H 5.0 0.01 1 307 . 55 VAL CA C 56.4 0.2 1 308 . 55 VAL CB C 32.9 0.2 1 309 . 55 VAL C C 172.0 0.2 1 310 . 56 ARG H H 9.37 0.01 1 311 . 56 ARG N N 124.5 0.2 1 312 . 56 ARG HA H 4.8 0.01 1 313 . 56 ARG CA C 51.4 0.2 1 314 . 56 ARG CB C 30.4 0.2 1 315 . 56 ARG C C 172.0 0.2 1 316 . 57 VAL H H 8.68 0.01 1 317 . 57 VAL N N 124.4 0.2 1 318 . 57 VAL HA H 4.2 0.01 1 319 . 57 VAL CA C 58.2 0.2 1 320 . 57 VAL CB C 30.5 0.2 1 321 . 57 VAL C C 173.0 0.2 1 322 . 58 ILE H H 8.80 0.01 1 323 . 58 ILE N N 127.3 0.2 1 324 . 58 ILE HA H 4.5 0.01 1 325 . 58 ILE CA C 58.4 0.2 1 326 . 58 ILE CB C 37.1 0.2 1 327 . 58 ILE C C 173.0 0.2 1 328 . 59 ARG H H 8.60 0.01 1 329 . 59 ARG N N 126.3 0.2 1 330 . 59 ARG HA H 4.6 0.01 1 331 . 59 ARG CA C 52.3 0.2 1 332 . 59 ARG CB C 30.8 0.2 1 333 . 59 ARG C C 172.3 0.2 1 334 . 60 LYS H H 8.60 0.01 1 335 . 60 LYS HA H 4.6 0.01 1 336 . 60 LYS CA C 53.5 0.2 1 337 . 60 LYS CB C 31.5 0.2 1 338 . 60 LYS C C 173.1 0.2 1 339 . 61 SER H H 8.15 0.01 1 340 . 61 SER N N 118.9 0.2 1 341 . 61 SER HA H 5.0 0.01 1 342 . 61 SER CA C 52.4 0.2 1 343 . 62 PRO HA H 4.5 0.01 1 344 . 62 PRO CA C 62.2 0.2 1 345 . 62 PRO CB C 29.8 0.2 1 346 . 62 PRO C C 175.0 0.2 1 347 . 63 THR H H 7.65 0.01 1 348 . 63 THR N N 106.6 0.2 1 349 . 63 THR HA H 4.4 0.01 1 350 . 63 THR CA C 59.4 0.2 1 351 . 63 THR CB C 58.7 0.2 1 352 . 63 THR C C 172.5 0.2 1 353 . 64 ALA H H 7.79 0.01 1 354 . 64 ALA N N 122.7 0.2 1 355 . 64 ALA HA H 4.5 0.01 1 356 . 64 ALA CA C 49.9 0.2 1 357 . 64 ALA CB C 17.8 0.2 1 358 . 64 ALA C C 175.1 0.2 1 359 . 65 GLY H H 7.98 0.01 1 360 . 65 GLY N N 107.8 0.2 1 361 . 65 GLY HA2 H 4.0 0.01 1 362 . 65 GLY HA3 H 4.0 0.01 1 363 . 65 GLY CA C 42.7 0.2 1 364 . 65 GLY C C 171.6 0.2 1 365 . 66 VAL H H 8.31 0.01 1 366 . 66 VAL N N 120.4 0.2 1 367 . 66 VAL HA H 4.6 0.01 1 368 . 66 VAL CA C 59.3 0.2 1 369 . 66 VAL CB C 38.6 0.2 1 370 . 66 VAL C C 173.3 0.2 1 371 . 67 SER H H 8.79 0.01 1 372 . 67 SER N N 120.4 0.2 1 373 . 67 SER HA H 3.7 0.01 1 374 . 67 SER CA C 54.6 0.2 1 375 . 67 SER CB C 61.9 0.2 1 376 . 67 SER C C 170.5 0.2 1 377 . 68 ILE H H 8.33 0.01 1 378 . 68 ILE N N 123.6 0.2 1 379 . 68 ILE HA H 4.5 0.01 1 380 . 68 ILE CA C 57.9 0.2 1 381 . 68 ILE CB C 37.2 0.2 1 382 . 68 ILE C C 172.4 0.2 1 383 . 69 ALA H H 8.34 0.01 1 384 . 69 ALA N N 129.2 0.2 1 385 . 69 ALA HA H 4.5 0.01 1 386 . 69 ALA CA C 48.0 0.2 1 387 . 69 ALA CB C 20.1 0.2 1 388 . 69 ALA C C 172.2 0.2 1 389 . 70 TYR H H 7.93 0.01 1 390 . 70 TYR N N 115.8 0.2 1 391 . 70 TYR HA H 5.5 0.01 1 392 . 70 TYR CA C 54.8 0.2 1 393 . 70 TYR CB C 39.7 0.2 1 394 . 70 TYR C C 172.4 0.2 1 395 . 71 ARG H H 9.09 0.01 1 396 . 71 ARG N N 118.4 0.2 1 397 . 71 ARG HA H 5.0 0.01 1 398 . 71 ARG CA C 50.8 0.2 1 399 . 71 ARG CB C 32.2 0.2 1 400 . 71 ARG C C 171.4 0.2 1 401 . 72 LEU HA H 4.8 0.01 1 402 . 72 LEU CA C 51.1 0.2 1 403 . 72 LEU CB C 42.7 0.2 1 404 . 72 LEU C C 172.7 0.2 1 405 . 73 VAL H H 8.72 0.01 1 406 . 73 VAL N N 126.1 0.2 1 407 . 73 VAL HA H 4.5 0.01 1 408 . 73 VAL CA C 59.4 0.2 1 409 . 73 VAL CB C 31.6 0.2 1 410 . 73 VAL C C 174.4 0.2 1 411 . 74 ILE H H 8.80 0.01 1 412 . 74 ILE N N 122.7 0.2 1 413 . 74 ILE HA H 4.9 0.01 1 414 . 74 ILE CA C 56.7 0.2 1 415 . 74 ILE CB C 39.9 0.2 1 416 . 74 ILE C C 172.5 0.2 1 417 . 75 LYS H H 8.61 0.01 1 418 . 75 LYS N N 121.6 0.2 1 419 . 75 LYS HA H 4.4 0.01 1 420 . 75 LYS CA C 53.6 0.2 1 421 . 75 LYS CB C 31.6 0.2 1 422 . 75 LYS C C 173.8 0.2 1 423 . 76 ARG H H 8.87 0.01 1 424 . 76 ARG N N 123.6 0.2 1 425 . 76 ARG HA H 4.1 0.01 1 426 . 76 ARG CA C 54.0 0.2 1 427 . 76 ARG CB C 28.7 0.2 1 428 . 76 ARG C C 173.2 0.2 1 429 . 77 ILE H H 8.02 0.01 1 430 . 77 ILE N N 125.2 0.2 1 431 . 77 ILE HA H 4.2 0.01 1 432 . 77 ILE CA C 58.7 0.2 1 433 . 77 ILE CB C 35.8 0.2 1 434 . 77 ILE C C 172.8 0.2 1 435 . 78 ILE H H 7.70 0.01 1 436 . 78 ILE N N 129.5 0.2 1 437 . 78 ILE HA H 4.0 0.01 1 438 . 78 ILE CA C 60.3 0.2 1 stop_ save_