data_5936 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N, 13C Resonance Assignment of b-ADT ; _BMRB_accession_number 5936 _BMRB_flat_file_name bmr5936.str _Entry_type original _Submission_date 2003-09-08 _Accession_date 2003-09-08 _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 John Michael . . 2 Heller Markus . . 3 Coles Murray . . 4 Bosch Gundula . . 5 Baumeister Wolfgang . . 6 Kessler Horst . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 241 "13C chemical shifts" 248 "15N chemical shifts" 116 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-04-07 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5930 'chmeical shifts of a-ADT' stop_ _Original_release_date 2004-04-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone 1H, 15N and 13C resonance assignments of [agr]-ADT and [bgr]-ADT ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15014236 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 John Michael . . 2 Heller Markus . . 3 Coles Murray . . 4 Bosch Gundula . . 5 Baumeister Wolfgang . . 6 Kessler Horst . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 29 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 209 _Page_last 210 _Year 2004 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_citation_Wishart(1995) _Saveframe_category citation _Citation_full 'J. Biomol. NMR, 6 (1995) 135-140.' _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_bADT _Saveframe_category molecular_system _Mol_system_name bADT _Abbreviation_common bADT _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label bADT $bADT stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function chaperonin stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_bADT _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'apical domain of the Thermosome' _Name_variant C151S _Abbreviation_common bADT _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 159 _Mol_residue_sequence ; MSGIIVDKEKVHPGMPDVVK DAKIALLDAPLEIKKPEFDT NLRIEDPSMIQKFLAQEENM LREMVDKIKSVGANVVITQK GIDDMAQHYLSRAGIYAVRR VKKSDMDKLAKATGASIVST IDEISSSDLGTAERVEQVKV GEDYMTFVTGSKNHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 GLY 4 ILE 5 ILE 6 VAL 7 ASP 8 LYS 9 GLU 10 LYS 11 VAL 12 HIS 13 PRO 14 GLY 15 MET 16 PRO 17 ASP 18 VAL 19 VAL 20 LYS 21 ASP 22 ALA 23 LYS 24 ILE 25 ALA 26 LEU 27 LEU 28 ASP 29 ALA 30 PRO 31 LEU 32 GLU 33 ILE 34 LYS 35 LYS 36 PRO 37 GLU 38 PHE 39 ASP 40 THR 41 ASN 42 LEU 43 ARG 44 ILE 45 GLU 46 ASP 47 PRO 48 SER 49 MET 50 ILE 51 GLN 52 LYS 53 PHE 54 LEU 55 ALA 56 GLN 57 GLU 58 GLU 59 ASN 60 MET 61 LEU 62 ARG 63 GLU 64 MET 65 VAL 66 ASP 67 LYS 68 ILE 69 LYS 70 SER 71 VAL 72 GLY 73 ALA 74 ASN 75 VAL 76 VAL 77 ILE 78 THR 79 GLN 80 LYS 81 GLY 82 ILE 83 ASP 84 ASP 85 MET 86 ALA 87 GLN 88 HIS 89 TYR 90 LEU 91 SER 92 ARG 93 ALA 94 GLY 95 ILE 96 TYR 97 ALA 98 VAL 99 ARG 100 ARG 101 VAL 102 LYS 103 LYS 104 SER 105 ASP 106 MET 107 ASP 108 LYS 109 LEU 110 ALA 111 LYS 112 ALA 113 THR 114 GLY 115 ALA 116 SER 117 ILE 118 VAL 119 SER 120 THR 121 ILE 122 ASP 123 GLU 124 ILE 125 SER 126 SER 127 SER 128 ASP 129 LEU 130 GLY 131 THR 132 ALA 133 GLU 134 ARG 135 VAL 136 GLU 137 GLN 138 VAL 139 LYS 140 VAL 141 GLY 142 GLU 143 ASP 144 TYR 145 MET 146 THR 147 PHE 148 VAL 149 THR 150 GLY 151 SER 152 LYS 153 ASN 154 HIS 155 HIS 156 HIS 157 HIS 158 HIS 159 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 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 1A6D "Thermosome From T. Acidophilum" 96.23 543 98.04 99.35 1.42e-98 PDB 1A6E "Thermosome-Mg-Adp-Alf3 Complex" 96.23 543 98.04 99.35 1.42e-98 PDB 1E0R "Beta-Apical Domain Of Thermosome" 100.00 159 99.37 100.00 8.35e-110 EMBL CAA86611 "thermosome beta-subunit [Thermoplasma acidophilum]" 96.23 543 98.04 99.35 1.42e-98 EMBL CAC12400 "thermosome beta chain [Thermoplasma acidophilum]" 96.23 543 98.04 99.35 1.42e-98 REF NP_394733 "thermosome beta chain [Thermoplasma acidophilum DSM 1728]" 96.23 543 98.04 99.35 1.42e-98 REF WP_010901684 "thermosome subunit [Thermoplasma acidophilum]" 96.23 543 98.04 99.35 1.42e-98 SP P48425 "RecName: Full=Thermosome subunit beta; AltName: Full=Chaperonin subunit beta; AltName: Full=Thermosome subunit 2 [Thermoplasma " 96.23 543 98.04 99.35 1.42e-98 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $bADT 'Thermoplasma acidophilum' 2303 Archaea . Thermoplasma acidophilum 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 $bADT 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_15N _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $bADT . mM 0.7 1.0 [U-15N] 'Na Phosphate' 25 mM . . . NaCl 100 mM . . . stop_ save_ save_sample_CN _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $bADT . mM 0.7 1.0 '[U-13C; U-15N]' 'Na Phosphate' 25 mM . . . NaCl 100 mM . . . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_general_condition _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.8 0.2 n/a temperature 315 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 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_bADT_bb _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_15N $sample_CN stop_ _Sample_conditions_label $general_condition _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name bADT _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 GLY C C 172.1 0.1 1 2 . 3 GLY CA C 45.2 0.1 1 3 . 4 ILE H H 8.48 0.01 1 4 . 4 ILE HA H 4.29 0.01 1 5 . 4 ILE C C 174.4 0.1 1 6 . 4 ILE CA C 59.9 0.1 1 7 . 4 ILE N N 120.87 0.1 1 8 . 5 ILE H H 8.42 0.01 1 9 . 5 ILE HA H 4.76 0.01 1 10 . 5 ILE C C 175.5 0.1 1 11 . 5 ILE CA C 59.6 0.1 1 12 . 5 ILE N N 126.3 0.1 1 13 . 6 VAL H H 9.42 0.01 1 14 . 6 VAL HA H 4.28 0.01 1 15 . 6 VAL C C 176.5 0.1 1 16 . 6 VAL CA C 60.5 0.1 1 17 . 6 VAL N N 128.7 0.1 1 18 . 7 ASP H H 8.89 0.01 1 19 . 7 ASP HA H 4.67 0.01 1 20 . 7 ASP C C 175.9 0.1 1 21 . 7 ASP CA C 54.1 0.1 1 22 . 7 ASP N N 132 0.1 1 23 . 8 LYS H H 8.32 0.01 1 24 . 8 LYS HA H 4.74 0.01 1 25 . 8 LYS C C 174.5 0.1 1 26 . 8 LYS CA C 53.8 0.1 1 27 . 8 LYS N N 120.65 0.1 1 28 . 9 GLU H H 8.9 0.01 1 29 . 9 GLU HA H 4.15 0.01 1 30 . 9 GLU CA C 53.8 0.1 1 31 . 9 GLU N N 123.3 0.1 1 32 . 10 LYS HA H 4 0.01 1 33 . 10 LYS C C 179.06 0.1 1 34 . 10 LYS CA C 55.7 0.1 1 35 . 11 VAL H H 8.02 0.01 1 36 . 11 VAL HA H 3.88 0.01 1 37 . 11 VAL C C 173.5 0.1 1 38 . 11 VAL CA C 64 0.1 1 39 . 11 VAL N N 118.15 0.1 1 40 . 12 HIS H H 7.49 0.01 1 41 . 12 HIS HA H 5.13 0.01 1 42 . 12 HIS CA C 53.5 0.1 1 43 . 12 HIS N N 121.3 0.1 1 44 . 14 GLY C C 173 0.1 1 45 . 14 GLY CA C 45 0.1 1 46 . 15 MET H H 7.7 0.01 1 47 . 15 MET CA C 53.5 0.1 1 48 . 15 MET N N 129.2 0.1 1 49 . 16 PRO HA H 4.45 0.01 1 50 . 16 PRO C C 174.7 0.1 1 51 . 16 PRO CA C 62.9 0.1 1 52 . 17 ASP H H 8.15 0.01 1 53 . 17 ASP HA H 4.78 0.01 1 54 . 17 ASP C C 175.8 0.1 1 55 . 17 ASP CA C 55.9 0.1 1 56 . 17 ASP N N 115.6 0.1 1 57 . 18 VAL H H 7.4 0.01 1 58 . 18 VAL HA H 4.71 0.01 1 59 . 18 VAL C C 174.5 0.1 1 60 . 18 VAL CA C 60.5 0.1 1 61 . 18 VAL N N 114.3 0.1 1 62 . 19 VAL H H 9.29 0.01 1 63 . 19 VAL HA H 4.1 0.01 1 64 . 19 VAL C C 175 0.1 1 65 . 19 VAL CA C 61.4 0.1 1 66 . 19 VAL N N 127.9 0.1 1 67 . 20 LYS H H 8.32 0.01 1 68 . 20 LYS HA H 4.69 0.01 1 69 . 20 LYS C C 176.3 0.1 1 70 . 20 LYS CA C 55.1 0.1 1 71 . 20 LYS N N 126.8 0.1 1 72 . 21 ASP H H 8.56 0.01 1 73 . 21 ASP HA H 4.23 0.01 1 74 . 21 ASP C C 175.6 0.1 1 75 . 21 ASP CA C 55.6 0.1 1 76 . 21 ASP N N 122 0.1 1 77 . 22 ALA H H 7.53 0.01 1 78 . 22 ALA HA H 4.32 0.01 1 79 . 22 ALA C C 177.4 0.1 1 80 . 22 ALA CA C 51.6 0.1 1 81 . 22 ALA N N 121.4 0.1 1 82 . 23 LYS H H 9.43 0.01 1 83 . 23 LYS HA H 5.16 0.01 1 84 . 23 LYS C C 176.2 0.1 1 85 . 23 LYS CA C 54.3 0.1 1 86 . 23 LYS N N 125.7 0.1 1 87 . 24 ILE H H 8.8 0.01 1 88 . 24 ILE HA H 4.4 0.01 1 89 . 24 ILE C C 174.5 0.1 1 90 . 24 ILE CA C 60.9 0.1 1 91 . 24 ILE N N 122.8 0.1 1 92 . 25 ALA H H 8.98 0.01 1 93 . 25 ALA HA H 4.8 0.01 1 94 . 25 ALA C C 174.8 0.1 1 95 . 25 ALA CA C 49.7 0.1 1 96 . 25 ALA N N 130.05 0.1 1 97 . 26 LEU H H 9.57 0.01 1 98 . 26 LEU HA H 5.07 0.01 1 99 . 26 LEU C C 174.9 0.1 1 100 . 26 LEU CA C 52.5 0.1 1 101 . 26 LEU N N 125 0.1 1 102 . 27 LEU H H 8.89 0.01 1 103 . 27 LEU HA H 5.37 0.01 1 104 . 27 LEU C C 176 0.1 1 105 . 27 LEU CA C 52.3 0.1 1 106 . 27 LEU N N 120.43 0.1 1 107 . 28 ASP H H 8.32 0.01 1 108 . 28 ASP HA H 4.81 0.01 1 109 . 28 ASP C C 174.1 0.1 1 110 . 28 ASP CA C 52 0.1 1 111 . 28 ASP N N 120.4 0.1 1 112 . 29 ALA H H 6.36 0.01 1 113 . 29 ALA HA H 4.86 0.01 1 114 . 29 ALA CA C 49.3 0.1 1 115 . 29 ALA N N 118 0.1 1 116 . 30 PRO HA H 4.39 0.01 1 117 . 30 PRO C C 176.1 0.1 1 118 . 30 PRO CA C 61.4 0.1 1 119 . 31 LEU H H 8.13 0.01 1 120 . 31 LEU HA H 4.55 0.01 1 121 . 31 LEU C C 173.2 0.1 1 122 . 31 LEU CA C 53.6 0.1 1 123 . 31 LEU N N 122.2 0.1 1 124 . 32 GLU H H 7.44 0.01 1 125 . 32 GLU HA H 4.67 0.01 1 126 . 32 GLU C C 175.4 0.1 1 127 . 32 GLU CA C 53.4 0.1 1 128 . 32 GLU N N 116.3 0.1 1 129 . 33 ILE H H 9.17 0.01 1 130 . 33 ILE HA H 4.2 0.01 1 131 . 33 ILE C C 176.4 0.1 1 132 . 33 ILE CA C 60.5 0.1 1 133 . 33 ILE N N 122 0.1 1 134 . 34 LYS H H 8.53 0.01 1 135 . 34 LYS HA H 4.26 0.01 1 136 . 34 LYS C C 175.6 0.1 1 137 . 34 LYS CA C 56 0.1 1 138 . 34 LYS N N 127.65 0.1 1 139 . 35 LYS H H 7.97 0.01 1 140 . 35 LYS HA H 4.58 0.01 1 141 . 35 LYS CA C 53.7 0.1 1 142 . 35 LYS N N 121.7 0.1 1 143 . 39 ASP HA H 4.25 0.01 1 144 . 39 ASP C C 175.7 0.1 1 145 . 39 ASP CA C 60.8 0.1 1 146 . 40 THR H H 7.71 0.01 1 147 . 40 THR HA H 4.15 0.01 1 148 . 40 THR CA C 62.8 0.1 1 149 . 40 THR N N 123.8 0.1 1 150 . 43 ARG HA H 4.29 0.01 1 151 . 43 ARG C C 178.7 0.1 1 152 . 43 ARG CA C 57.3 0.1 1 153 . 44 ILE H H 7.71 0.01 1 154 . 44 ILE HA H 3.85 0.01 1 155 . 44 ILE C C 177.6 0.1 1 156 . 44 ILE CA C 63.6 0.1 1 157 . 44 ILE N N 119.99 0.1 1 158 . 45 GLU H H 7.85 0.01 1 159 . 45 GLU HA H 4.17 0.01 1 160 . 45 GLU CA C 58.5 0.1 1 161 . 45 GLU N N 118.7 0.1 1 162 . 47 PRO HA H 4.48 0.01 1 163 . 47 PRO C C 176.4 0.1 1 164 . 47 PRO CA C 63.4 0.1 1 165 . 48 SER H H 7.92 0.01 1 166 . 48 SER CA C 60.1 0.1 1 167 . 48 SER N N 121.7 0.1 1 168 . 52 LYS HA H 4.11 0.01 1 169 . 52 LYS C C 178.9 0.1 1 170 . 52 LYS CA C 59.2 0.1 1 171 . 53 PHE H H 8 0.01 1 172 . 53 PHE HA H 4.36 0.01 1 173 . 53 PHE C C 178 0.1 1 174 . 53 PHE CA C 60.5 0.1 1 175 . 53 PHE N N 120.9 0.1 1 176 . 54 LEU H H 8.52 0.01 1 177 . 54 LEU HA H 4.02 0.01 1 178 . 54 LEU C C 179.5 0.1 1 179 . 54 LEU CA C 57.4 0.1 1 180 . 54 LEU N N 119.9 0.1 1 181 . 55 ALA H H 8.08 0.01 1 182 . 55 ALA HA H 4.22 0.01 1 183 . 55 ALA C C 180.5 0.1 1 184 . 55 ALA CA C 54.7 0.1 1 185 . 55 ALA N N 122 0.1 1 186 . 56 GLN H H 7.85 0.01 1 187 . 56 GLN HA H 4.16 0.01 1 188 . 56 GLN C C 179 0.1 1 189 . 56 GLN CA C 58.2 0.1 1 190 . 56 GLN N N 118.5 0.1 1 191 . 57 GLU H H 8.17 0.01 1 192 . 57 GLU HA H 3.95 0.01 1 193 . 57 GLU C C 179.4 0.1 1 194 . 57 GLU CA C 58.7 0.1 1 195 . 57 GLU N N 120 0.1 1 196 . 58 GLU H H 8.42 0.01 1 197 . 58 GLU CA C 60 0.1 1 198 . 58 GLU N N 120.87 0.1 1 199 . 59 ASN HA H 4.3 0.01 1 200 . 59 ASN C C 177.6 0.1 1 201 . 59 ASN CA C 56 0.1 1 202 . 60 MET H H 8.02 0.01 1 203 . 60 MET C C 178.7 0.1 1 204 . 60 MET CA C 57.9 0.1 1 205 . 60 MET N N 118.7 0.1 1 206 . 61 LEU H H 7.94 0.01 1 207 . 61 LEU HA H 4.11 0.01 1 208 . 61 LEU C C 178.6 0.1 1 209 . 61 LEU CA C 57.6 0.1 1 210 . 61 LEU N N 121.5 0.1 1 211 . 62 ARG H H 8.09 0.01 1 212 . 62 ARG HA H 3.23 0.01 1 213 . 62 ARG C C 179.1 0.1 1 214 . 62 ARG CA C 60 0.1 1 215 . 62 ARG N N 119.3 0.1 1 216 . 63 GLU H H 7.98 0.01 1 217 . 63 GLU HA H 3.97 0.01 1 218 . 63 GLU C C 179.6 0.1 1 219 . 63 GLU CA C 59.2 0.1 1 220 . 63 GLU N N 118 0.1 1 221 . 64 MET H H 8.1 0.01 1 222 . 64 MET HA H 4.08 0.01 1 223 . 64 MET C C 178.3 0.1 1 224 . 64 MET CA C 59.2 0.1 1 225 . 64 MET N N 120.76 0.1 1 226 . 65 VAL H H 7.98 0.01 1 227 . 65 VAL HA H 3.36 0.01 1 228 . 65 VAL C C 177.5 0.1 1 229 . 65 VAL CA C 67.5 0.1 1 230 . 65 VAL N N 118.9 0.1 1 231 . 66 ASP H H 8.33 0.01 1 232 . 66 ASP HA H 4.38 0.01 1 233 . 66 ASP C C 179.6 0.1 1 234 . 66 ASP CA C 57.4 0.1 1 235 . 66 ASP N N 120.1 0.1 1 236 . 67 LYS H H 8.16 0.01 1 237 . 67 LYS HA H 4.04 0.01 1 238 . 67 LYS C C 179.2 0.1 1 239 . 67 LYS CA C 58.7 0.1 1 240 . 67 LYS N N 122.8 0.1 1 241 . 68 ILE H H 7.69 0.01 1 242 . 68 ILE HA H 3.47 0.01 1 243 . 68 ILE C C 177.3 0.1 1 244 . 68 ILE CA C 65.4 0.1 1 245 . 68 ILE N N 120.43 0.1 1 246 . 69 LYS H H 8.31 0.01 1 247 . 69 LYS HA H 4.17 0.01 1 248 . 69 LYS C C 179.9 0.1 1 249 . 69 LYS CA C 58.7 0.1 1 250 . 69 LYS N N 118 0.1 1 251 . 70 SER H H 8.66 0.01 1 252 . 70 SER HA H 4.21 0.01 1 253 . 70 SER C C 176.7 0.1 1 254 . 70 SER CA C 61.3 0.1 1 255 . 70 SER N N 116.7 0.1 1 256 . 71 VAL H H 7.46 0.01 1 257 . 71 VAL HA H 4.42 0.01 1 258 . 71 VAL C C 176.1 0.1 1 259 . 71 VAL CA C 61.6 0.1 1 260 . 71 VAL N N 113.65 0.1 1 261 . 72 GLY H H 7.75 0.01 1 262 . 72 GLY HA2 H 4.63 0.01 2 263 . 72 GLY C C 174.4 0.1 1 264 . 72 GLY CA C 44.5 0.1 1 265 . 72 GLY N N 106.65 0.1 1 266 . 73 ALA H H 7 0.01 1 267 . 73 ALA HA H 4.25 0.01 1 268 . 73 ALA C C 177.1 0.1 1 269 . 73 ALA CA C 52.3 0.1 1 270 . 73 ALA N N 120.65 0.1 1 271 . 74 ASN H H 8.93 0.01 1 272 . 74 ASN HA H 4.72 0.01 1 273 . 74 ASN CA C 52.1 0.1 1 274 . 74 ASN N N 116.1 0.1 1 275 . 75 VAL H H 7.95 0.01 1 276 . 75 VAL HA H 5.42 0.01 1 277 . 75 VAL C C 174.8 0.1 1 278 . 75 VAL CA C 60.5 0.1 1 279 . 75 VAL N N 120.65 0.1 1 280 . 76 VAL H H 9.21 0.01 1 281 . 76 VAL HA H 4.9 0.01 1 282 . 76 VAL C C 173.3 0.1 1 283 . 76 VAL CA C 60.2 0.1 1 284 . 76 VAL N N 127 0.1 1 285 . 77 ILE H H 8.88 0.01 1 286 . 77 ILE HA H 4.69 0.01 1 287 . 77 ILE C C 174.4 0.1 1 288 . 77 ILE CA C 59.6 0.1 1 289 . 77 ILE N N 127.65 0.1 1 290 . 78 THR H H 8.22 0.01 1 291 . 78 THR HA H 6.11 0.01 1 292 . 78 THR C C 172.5 0.1 1 293 . 78 THR CA C 55.6 0.1 1 294 . 78 THR N N 118.2 0.1 1 295 . 79 GLN H H 7.68 0.01 1 296 . 79 GLN HA H 4.97 0.01 1 297 . 79 GLN C C 177.5 0.1 1 298 . 79 GLN CA C 56 0.1 1 299 . 79 GLN N N 124.8 0.1 1 300 . 80 LYS H H 8.28 0.01 1 301 . 80 LYS HA H 4.57 0.01 1 302 . 80 LYS C C 174.3 0.1 1 303 . 80 LYS CA C 52.9 0.1 1 304 . 80 LYS N N 119.1 0.1 1 305 . 81 GLY H H 8.09 0.01 1 306 . 81 GLY CA C 45.4 0.1 1 307 . 81 GLY N N 105.56 0.1 1 308 . 82 ILE HA H 4.83 0.01 1 309 . 82 ILE C C 176.2 0.1 1 310 . 82 ILE CA C 61.1 0.1 1 311 . 83 ASP H H 8.42 0.01 1 312 . 83 ASP HA H 4.8 0.01 1 313 . 83 ASP CA C 53.3 0.1 1 314 . 83 ASP N N 128.1 0.1 1 315 . 84 ASP HA H 4.19 0.01 1 316 . 84 ASP C C 178.9 0.1 1 317 . 84 ASP CA C 58 0.1 1 318 . 85 MET H H 8.22 0.01 1 319 . 85 MET HA H 4.26 0.01 1 320 . 85 MET C C 178.4 0.1 1 321 . 85 MET CA C 57.6 0.1 1 322 . 85 MET N N 119.8 0.1 1 323 . 86 ALA H H 8.73 0.01 1 324 . 86 ALA HA H 3.9 0.01 1 325 . 86 ALA C C 180 0.1 1 326 . 86 ALA CA C 55.7 0.1 1 327 . 86 ALA N N 122.4 0.1 1 328 . 87 GLN H H 8.82 0.01 1 329 . 87 GLN HA H 3.49 0.01 1 330 . 87 GLN C C 177.7 0.1 1 331 . 87 GLN CA C 59.5 0.1 1 332 . 87 GLN N N 116.5 0.1 1 333 . 88 HIS H H 7.49 0.01 1 334 . 88 HIS HA H 3.85 0.01 1 335 . 88 HIS C C 177.8 0.1 1 336 . 88 HIS CA C 59.6 0.1 1 337 . 88 HIS N N 118.7 0.1 1 338 . 89 TYR H H 7.92 0.01 1 339 . 89 TYR HA H 4.01 0.01 1 340 . 89 TYR C C 179.7 0.1 1 341 . 89 TYR CA C 61.8 0.1 1 342 . 89 TYR N N 117.4 0.1 1 343 . 90 LEU H H 8.93 0.01 1 344 . 90 LEU HA H 3.85 0.01 1 345 . 90 LEU C C 178 0.1 1 346 . 90 LEU CA C 58 0.1 1 347 . 90 LEU N N 120.54 0.1 1 348 . 91 SER H H 8.04 0.01 1 349 . 91 SER HA H 3.85 0.01 1 350 . 91 SER C C 173.4 0.1 1 351 . 91 SER CA C 61.2 0.1 1 352 . 91 SER N N 113.9 0.1 1 353 . 92 ARG H H 8.03 0.01 1 354 . 92 ARG HA H 3.95 0.01 1 355 . 92 ARG C C 177.4 0.1 1 356 . 92 ARG CA C 58.2 0.1 1 357 . 92 ARG N N 122.18 0.1 1 358 . 93 ALA H H 7.24 0.01 1 359 . 93 ALA HA H 4.4 0.01 1 360 . 93 ALA C C 177.1 0.1 1 361 . 93 ALA CA C 51.6 0.1 1 362 . 93 ALA N N 118.7 0.1 1 363 . 94 GLY H H 7.84 0.01 1 364 . 94 GLY HA2 H 4.01 0.01 2 365 . 94 GLY C C 174.1 0.1 1 366 . 94 GLY CA C 45.43 0.1 1 367 . 94 GLY N N 107.64 0.1 1 368 . 95 ILE H H 7.64 0.01 1 369 . 95 ILE HA H 3.96 0.01 1 370 . 95 ILE C C 174.1 0.1 1 371 . 95 ILE CA C 60.4 0.1 1 372 . 95 ILE N N 120.87 0.1 1 373 . 96 TYR H H 7.6 0.01 1 374 . 96 TYR HA H 4.16 0.01 1 375 . 96 TYR C C 174.5 0.1 1 376 . 96 TYR CA C 57.8 0.1 1 377 . 96 TYR N N 127.4 0.1 1 378 . 97 ALA H H 7.88 0.01 1 379 . 97 ALA HA H 6.33 0.01 1 380 . 97 ALA C C 174.4 0.1 1 381 . 97 ALA CA C 49.1 0.1 1 382 . 97 ALA N N 131.4 0.1 1 383 . 98 VAL H H 8.05 0.01 1 384 . 98 VAL HA H 4.3 0.01 1 385 . 98 VAL C C 173.7 0.1 1 386 . 98 VAL CA C 60.7 0.1 1 387 . 98 VAL N N 116.9 0.1 1 388 . 99 ARG H H 8.68 0.01 1 389 . 99 ARG HA H 5.28 0.01 1 390 . 99 ARG C C 173.1 0.1 1 391 . 99 ARG CA C 52.5 0.1 1 392 . 99 ARG N N 120.9 0.1 1 393 . 100 ARG H H 7.93 0.01 1 394 . 100 ARG HA H 3.52 0.01 1 395 . 100 ARG C C 175.4 0.1 1 396 . 100 ARG CA C 55.6 0.1 1 397 . 100 ARG N N 112.45 0.1 1 398 . 101 VAL H H 8.06 0.01 1 399 . 101 VAL HA H 3.85 0.01 1 400 . 101 VAL C C 176.5 0.1 1 401 . 101 VAL CA C 63.2 0.1 1 402 . 101 VAL N N 120 0.1 1 403 . 102 LYS H H 8.82 0.01 1 404 . 102 LYS HA H 4.14 0.01 1 405 . 102 LYS CA C 56.5 0.1 1 406 . 102 LYS N N 125 0.1 1 407 . 104 SER HA H 4.19 0.01 1 408 . 104 SER C C 178 0.1 1 409 . 104 SER CA C 61.4 0.1 1 410 . 105 ASP H H 6.89 0.01 1 411 . 105 ASP HA H 4.58 0.01 1 412 . 105 ASP C C 178.2 0.1 1 413 . 105 ASP CA C 56.8 0.1 1 414 . 105 ASP N N 122.2 0.1 1 415 . 106 MET H H 8.02 0.01 1 416 . 106 MET HA H 4.06 0.01 1 417 . 106 MET C C 178.3 0.1 1 418 . 106 MET CA C 57.4 0.1 1 419 . 106 MET N N 120.65 0.1 1 420 . 107 ASP H H 8.26 0.01 1 421 . 107 ASP HA H 4.35 0.01 1 422 . 107 ASP C C 179.4 0.1 1 423 . 107 ASP CA C 57.4 0.1 1 424 . 107 ASP N N 119.1 0.1 1 425 . 108 LYS H H 7.4 0.01 1 426 . 108 LYS HA H 4 0.01 1 427 . 108 LYS C C 180 0.1 1 428 . 108 LYS CA C 59.2 0.1 1 429 . 108 LYS N N 119.88 0.1 1 430 . 109 LEU H H 8.51 0.01 1 431 . 109 LEU HA H 3.87 0.01 1 432 . 109 LEU C C 180.2 0.1 1 433 . 109 LEU CA C 57.7 0.1 1 434 . 109 LEU N N 119.6 0.1 1 435 . 110 ALA H H 8.86 0.01 1 436 . 110 ALA HA H 3.86 0.01 1 437 . 110 ALA C C 179.9 0.1 1 438 . 110 ALA CA C 56 0.1 1 439 . 110 ALA N N 127.4 0.1 1 440 . 111 LYS H H 7.5 0.01 1 441 . 111 LYS HA H 4.02 0.01 1 442 . 111 LYS C C 179.1 0.1 1 443 . 111 LYS CA C 58.8 0.1 1 444 . 111 LYS N N 116.9 0.1 1 445 . 112 ALA H H 7.99 0.01 1 446 . 112 ALA HA H 4.3 0.01 1 447 . 112 ALA C C 179.2 0.1 1 448 . 112 ALA CA C 53.9 0.1 1 449 . 112 ALA N N 117.9 0.1 1 450 . 113 THR H H 7.89 0.01 1 451 . 113 THR HA H 4.78 0.01 1 452 . 113 THR C C 176.2 0.1 1 453 . 113 THR CA C 61.3 0.1 1 454 . 113 THR N N 130.82 0.1 1 455 . 114 GLY H H 7.83 0.01 1 456 . 114 GLY HA2 H 4.19 0.01 2 457 . 114 GLY C C 173.9 0.1 1 458 . 114 GLY CA C 45.4 0.1 1 459 . 114 GLY N N 110.6 0.1 1 460 . 115 ALA H H 7.32 0.01 1 461 . 115 ALA HA H 4.18 0.01 1 462 . 115 ALA C C 176.9 0.1 1 463 . 115 ALA CA C 51.3 0.1 1 464 . 115 ALA N N 122.4 0.1 1 465 . 116 SER H H 8.36 0.01 1 466 . 116 SER HA H 4.68 0.01 1 467 . 116 SER C C 173.3 0.1 1 468 . 116 SER CA C 56.9 0.1 1 469 . 116 SER N N 115.4 0.1 1 470 . 117 ILE H H 8.41 0.01 1 471 . 117 ILE HA H 3.99 0.01 1 472 . 117 ILE C C 177 0.1 1 473 . 117 ILE CA C 62.2 0.1 1 474 . 117 ILE N N 123.5 0.1 1 475 . 118 VAL H H 8.75 0.01 1 476 . 118 VAL HA H 4.14 0.01 1 477 . 118 VAL CA C 61.7 0.1 1 478 . 118 VAL N N 130.7 0.1 1 479 . 119 SER HA H 4.58 0.01 1 480 . 119 SER C C 174 0.1 1 481 . 119 SER CA C 57.8 0.1 1 482 . 120 THR H H 7.75 0.01 1 483 . 120 THR HA H 4.13 0.01 1 484 . 120 THR CA C 63.2 0.1 1 485 . 120 THR N N 121.1 0.1 1 486 . 121 ILE HA H 3.37 0.01 1 487 . 121 ILE C C 176.7 0.1 1 488 . 121 ILE CA C 64.8 0.1 1 489 . 122 ASP H H 8.26 0.01 1 490 . 122 ASP HA H 4.26 0.01 1 491 . 122 ASP C C 176.9 0.1 1 492 . 122 ASP CA C 56.1 0.1 1 493 . 122 ASP N N 114.7 0.1 1 494 . 123 GLU H H 7.3 0.01 1 495 . 123 GLU HA H 4.36 0.01 1 496 . 123 GLU C C 176.9 0.1 1 497 . 123 GLU CA C 55.2 0.1 1 498 . 123 GLU N N 114.5 0.1 1 499 . 124 ILE H H 7.62 0.01 1 500 . 124 ILE HA H 4.14 0.01 1 501 . 124 ILE C C 172.7 0.1 1 502 . 124 ILE CA C 63.2 0.1 1 503 . 124 ILE N N 122.8 0.1 1 504 . 125 SER H H 9.04 0.01 1 505 . 125 SER HA H 4.96 0.01 1 506 . 125 SER CA C 56 0.1 1 507 . 125 SER N N 121.2 0.1 1 508 . 127 SER HA H 4.31 0.01 1 509 . 127 SER C C 175.1 0.1 1 510 . 127 SER CA C 59.6 0.1 1 511 . 128 ASP H H 7.73 0.01 1 512 . 128 ASP HA H 4.64 0.01 1 513 . 128 ASP C C 177.6 0.1 1 514 . 128 ASP CA C 56 0.1 1 515 . 128 ASP N N 119.3 0.1 1 516 . 129 LEU H H 7.26 0.01 1 517 . 129 LEU HA H 4.61 0.01 1 518 . 129 LEU C C 178 0.1 1 519 . 129 LEU CA C 54.2 0.1 1 520 . 129 LEU N N 117.8 0.1 1 521 . 130 GLY H H 9.35 0.01 1 522 . 130 GLY C C 173.8 0.1 1 523 . 130 GLY CA C 43.3 0.1 1 524 . 130 GLY N N 108.4 0.1 1 525 . 131 THR H H 8.75 0.01 1 526 . 131 THR HA H 5.32 0.01 1 527 . 131 THR C C 173.4 0.1 1 528 . 131 THR CA C 60.6 0.1 1 529 . 131 THR N N 113.2 0.1 1 530 . 132 ALA H H 8.02 0.01 1 531 . 132 ALA HA H 4.53 0.01 1 532 . 132 ALA C C 175.7 0.1 1 533 . 132 ALA CA C 51.1 0.1 1 534 . 132 ALA N N 122.3 0.1 1 535 . 133 GLU H H 8.09 0.01 1 536 . 133 GLU HA H 4.19 0.01 1 537 . 133 GLU C C 178.3 0.1 1 538 . 133 GLU CA C 59.3 0.1 1 539 . 133 GLU N N 122.2 0.1 1 540 . 134 ARG H H 7.84 0.01 1 541 . 134 ARG HA H 5.15 0.01 1 542 . 134 ARG C C 173.7 0.1 1 543 . 134 ARG CA C 55.7 0.1 1 544 . 134 ARG N N 133.9 0.1 1 545 . 135 VAL H H 8.42 0.01 1 546 . 135 VAL HA H 4.67 0.01 1 547 . 135 VAL C C 173.7 0.1 1 548 . 135 VAL CA C 61.1 0.1 1 549 . 135 VAL N N 123.9 0.1 1 550 . 136 GLU H H 8.9 0.01 1 551 . 136 GLU HA H 5.36 0.01 1 552 . 136 GLU C C 173.9 0.1 1 553 . 136 GLU CA C 53.7 0.1 1 554 . 136 GLU N N 123.9 0.1 1 555 . 137 GLN H H 8.89 0.01 1 556 . 137 GLN HA H 5.36 0.01 1 557 . 137 GLN C C 176.2 0.1 1 558 . 137 GLN CA C 55.7 0.1 1 559 . 137 GLN N N 124.15 0.1 1 560 . 138 VAL H H 9.1 0.01 1 561 . 138 VAL HA H 4.67 0.01 1 562 . 138 VAL C C 173.7 0.1 1 563 . 138 VAL CA C 59.2 0.1 1 564 . 138 VAL N N 124.6 0.1 1 565 . 139 LYS H H 8.42 0.01 1 566 . 139 LYS HA H 4.49 0.01 1 567 . 139 LYS C C 176 0.1 1 568 . 139 LYS CA C 55.6 0.1 1 569 . 139 LYS N N 125 0.1 1 570 . 140 VAL H H 8.73 0.01 1 571 . 140 VAL HA H 4.03 0.01 1 572 . 140 VAL CA C 61.1 0.1 1 573 . 140 VAL N N 129.8 0.1 1 574 . 142 GLU HA H 4.2 0.01 1 575 . 142 GLU C C 175.7 0.1 1 576 . 142 GLU CA C 55.4 0.1 1 577 . 143 ASP H H 7.61 0.01 1 578 . 143 ASP HA H 4.84 0.01 1 579 . 143 ASP C C 174.3 0.1 1 580 . 143 ASP CA C 53.4 0.1 1 581 . 143 ASP N N 118.9 0.1 1 582 . 144 TYR H H 8.49 0.01 1 583 . 144 TYR HA H 5.07 0.01 1 584 . 144 TYR C C 175.2 0.1 1 585 . 144 TYR CA C 57.8 0.1 1 586 . 144 TYR N N 119.3 0.1 1 587 . 145 MET H H 9.11 0.01 1 588 . 145 MET HA H 4.73 0.01 1 589 . 145 MET C C 174.2 0.1 1 590 . 145 MET CA C 54.2 0.1 1 591 . 145 MET N N 118.9 0.1 1 592 . 146 THR H H 8.73 0.01 1 593 . 146 THR HA H 5.04 0.01 1 594 . 146 THR C C 172.2 0.1 1 595 . 146 THR CA C 63.2 0.1 1 596 . 146 THR N N 117.6 0.1 1 597 . 147 PHE H H 9.87 0.01 1 598 . 147 PHE HA H 5.4 0.01 1 599 . 147 PHE C C 174.8 0.1 1 600 . 147 PHE CA C 55.2 0.1 1 601 . 147 PHE N N 129.4 0.1 1 602 . 148 VAL H H 8.87 0.01 1 603 . 148 VAL HA H 4.45 0.01 1 604 . 148 VAL CA C 61 0.1 1 605 . 148 VAL N N 128.5 0.1 1 stop_ save_