data_18202 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and partial sidechain assignment (13C only) of hNaa50p assignment ; _BMRB_accession_number 18202 _BMRB_flat_file_name bmr18202.str _Entry_type original _Submission_date 2012-01-19 _Accession_date 2012-01-19 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone and partial sidechain assignment of the human N-alpha acetyltransferase 50 protein at 310 K based upon HNCO, HN(CA)CO, HNCA, HN(CO)CA, HNCACB, CBCA(CO)NH, CC(CO)NH and several amino acid edited 2D experiments (MUSIC)' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Brenner Annette K. . 2 Lillehaug Johan R. . 3 Evjenth Rune H. . 4 Froeystein 'Nils Aage' . . 5 Thompson Paul R. . 6 Arnesen Thomas . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 140 "13C chemical shifts" 544 "15N chemical shifts" 140 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-18 update BMRB 'update entry citation' 2012-05-02 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Human protein N-terminal acetyltransferase hNaa50p (hNAT5/hSAN) follows ordered sequential catalytic mechanism: combined kinetic and NMR study.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22311970 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Evjenth Rune H. . 2 Brenner Annette K. . 3 Thompson Paul R. . 4 Arnesen Thomas . . 5 Frystein 'Nils Age' . . 6 Lillehaug Johan R. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 287 _Journal_issue 13 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 10081 _Page_last 10088 _Year 2012 _Details . loop_ _Keyword 'enzymatic assay' 'enzyme mechanism' NMR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name hNaa50p _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label hNaa50p $hNaa50p 'Acetyl-coenzyme A' $entity_ACO stop_ _System_molecular_weight 19576.8 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'acetyl-CoA is the first substrate of hNaa50p' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_hNaa50p _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common hNaa50p _Molecular_mass 19576.8 _Mol_thiol_state unknown loop_ _Biological_function 'N-alpha acetyltransferase' 'N-epsilon acetyltransferase' stop_ _Details 'methionines 75 and 92 are selenomethionines' ############################## # Polymer residue sequence # ############################## _Residue_count 173 _Mol_residue_sequence ; GAMVMKGSRIELGDVTPHNI KQLKRLNQVIFPVSYNDKFY KDVLEVGELAKLAYFNDIAV GAVCCRVDHSQNQKRLYIXT LGCLAPYRRLGIGTKXLNHV LNICEKDGTFDNIYLHVQIS NESAIDFYRKFGFEIIETKK NYYKRIEPADAHVLQKNLKV PSGQNADVQKTDN ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 GLY 2 -2 ALA 3 -1 MET 4 0 VAL 5 1 MET 6 2 LYS 7 3 GLY 8 4 SER 9 5 ARG 10 6 ILE 11 7 GLU 12 8 LEU 13 9 GLY 14 10 ASP 15 11 VAL 16 12 THR 17 13 PRO 18 14 HIS 19 15 ASN 20 16 ILE 21 17 LYS 22 18 GLN 23 19 LEU 24 20 LYS 25 21 ARG 26 22 LEU 27 23 ASN 28 24 GLN 29 25 VAL 30 26 ILE 31 27 PHE 32 28 PRO 33 29 VAL 34 30 SER 35 31 TYR 36 32 ASN 37 33 ASP 38 34 LYS 39 35 PHE 40 36 TYR 41 37 LYS 42 38 ASP 43 39 VAL 44 40 LEU 45 41 GLU 46 42 VAL 47 43 GLY 48 44 GLU 49 45 LEU 50 46 ALA 51 47 LYS 52 48 LEU 53 49 ALA 54 50 TYR 55 51 PHE 56 52 ASN 57 53 ASP 58 54 ILE 59 55 ALA 60 56 VAL 61 57 GLY 62 58 ALA 63 59 VAL 64 60 CYS 65 61 CYS 66 62 ARG 67 63 VAL 68 64 ASP 69 65 HIS 70 66 SER 71 67 GLN 72 68 ASN 73 69 GLN 74 70 LYS 75 71 ARG 76 72 LEU 77 73 TYR 78 74 ILE 79 75 MSE 80 76 THR 81 77 LEU 82 78 GLY 83 79 CYS 84 80 LEU 85 81 ALA 86 82 PRO 87 83 TYR 88 84 ARG 89 85 ARG 90 86 LEU 91 87 GLY 92 88 ILE 93 89 GLY 94 90 THR 95 91 LYS 96 92 MSE 97 93 LEU 98 94 ASN 99 95 HIS 100 96 VAL 101 97 LEU 102 98 ASN 103 99 ILE 104 100 CYS 105 101 GLU 106 102 LYS 107 103 ASP 108 104 GLY 109 105 THR 110 106 PHE 111 107 ASP 112 108 ASN 113 109 ILE 114 110 TYR 115 111 LEU 116 112 HIS 117 113 VAL 118 114 GLN 119 115 ILE 120 116 SER 121 117 ASN 122 118 GLU 123 119 SER 124 120 ALA 125 121 ILE 126 122 ASP 127 123 PHE 128 124 TYR 129 125 ARG 130 126 LYS 131 127 PHE 132 128 GLY 133 129 PHE 134 130 GLU 135 131 ILE 136 132 ILE 137 133 GLU 138 134 THR 139 135 LYS 140 136 LYS 141 137 ASN 142 138 TYR 143 139 TYR 144 140 LYS 145 141 ARG 146 142 ILE 147 143 GLU 148 144 PRO 149 145 ALA 150 146 ASP 151 147 ALA 152 148 HIS 153 149 VAL 154 150 LEU 155 151 GLN 156 152 LYS 157 153 ASN 158 154 LEU 159 155 LYS 160 156 VAL 161 157 PRO 162 158 SER 163 159 GLY 164 160 GLN 165 161 ASN 166 162 ALA 167 163 ASP 168 164 VAL 169 165 GLN 170 166 LYS 171 167 THR 172 168 ASP 173 169 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 2OB0 "Human Mak3 Homolog In Complex With Acetyl-Coa" 97.11 170 100.00 100.00 2.50e-117 PDB 2PSW "Human Mak3 Homolog In Complex With Coa" 97.11 170 100.00 100.00 2.50e-117 PDB 3TFY "Naa50p Amino-Terminal Acetyltransferase Bound To Substrate Peptide Fragment And Coa" 97.69 169 98.82 98.82 1.26e-118 DBJ BAB14397 "unnamed protein product [Homo sapiens]" 97.69 169 98.82 98.82 1.26e-118 DBJ BAB14490 "unnamed protein product [Homo sapiens]" 97.69 169 98.82 98.82 1.26e-118 DBJ BAB27439 "unnamed protein product [Mus musculus]" 97.69 168 97.04 97.63 5.95e-115 DBJ BAE22602 "unnamed protein product [Mus musculus]" 97.69 168 97.04 97.63 5.95e-115 DBJ BAE26378 "unnamed protein product [Mus musculus]" 97.69 168 97.04 97.63 5.95e-115 EMBL CAG30965 "hypothetical protein RCJMB04_1e13 [Gallus gallus]" 87.86 153 98.03 98.03 1.98e-104 EMBL CAH89629 "hypothetical protein [Pongo abelii]" 97.69 169 98.82 98.82 1.26e-118 GB AAH12731 "N-acetyltransferase 13 (GCN5-related) [Homo sapiens]" 97.69 169 98.82 98.82 1.26e-118 GB AAH57117 "N-acetyltransferase 13 [Mus musculus]" 97.69 169 97.63 98.22 1.46e-117 GB AAI22618 "N-acetyltransferase 13 (GCN5-related) [Bos taurus]" 97.69 169 98.82 98.82 1.26e-118 GB ABM84090 "N-acetyltransferase 13 [synthetic construct]" 97.69 169 98.82 98.82 1.26e-118 GB ABM87460 "N-acetyltransferase 13 [synthetic construct]" 97.69 169 98.82 98.82 1.26e-118 REF NP_001025949 "N-alpha-acetyltransferase 50, NatE catalytic subunit [Gallus gallus]" 87.86 153 98.03 98.03 1.98e-104 REF NP_001069218 "N-alpha-acetyltransferase 50 [Bos taurus]" 97.69 169 98.82 98.82 1.26e-118 REF NP_001124730 "N-alpha-acetyltransferase 50 [Pongo abelii]" 97.69 169 98.82 98.82 1.26e-118 REF NP_001231736 "N-alpha-acetyltransferase 50 [Sus scrofa]" 97.69 169 98.82 98.82 1.26e-118 REF NP_001248300 "N-alpha-acetyltransferase 50 [Macaca mulatta]" 97.69 169 98.82 98.82 1.26e-118 SP Q0IIJ0 "RecName: Full=N-alpha-acetyltransferase 50; AltName: Full=N-acetyltransferase 13; AltName: Full=NatE catalytic subunit" 97.69 169 98.82 98.82 1.26e-118 SP Q5RF28 "RecName: Full=N-alpha-acetyltransferase 50; AltName: Full=N-acetyltransferase NAT13; AltName: Full=NatE catalytic subunit" 97.69 169 98.82 98.82 1.26e-118 SP Q6PGB6 "RecName: Full=N-alpha-acetyltransferase 50; AltName: Full=N-acetyltransferase NAT13; AltName: Full=NatE catalytic subunit" 97.69 169 97.63 98.22 1.46e-117 SP Q9GZZ1 "RecName: Full=N-alpha-acetyltransferase 50; AltName: Full=N-acetyltransferase 13; AltName: Full=N-acetyltransferase 5; Short=hN" 97.69 169 98.82 98.82 1.26e-118 TPG DAA33506 "TPA: N-acetyltransferase 13 [Bos taurus]" 97.69 169 98.82 98.82 1.26e-118 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_MSE _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common SELENOMETHIONINE _BMRB_code MSE _PDB_code MSE _Standard_residue_derivative . _Molecular_mass 196.106 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? SE SE SE . 0 . ? CE CE C . 0 . ? H H H . 0 . ? HN2 HN2 H . 0 . ? HA HA H . 0 . ? HXT HXT H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG2 HG2 H . 0 . ? HG3 HG3 H . 0 . ? HE1 HE1 H . 0 . ? HE2 HE2 H . 0 . ? HE3 HE3 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H ? ? SING N HN2 ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG SE ? ? SING CG HG2 ? ? SING CG HG3 ? ? SING SE CE ? ? SING CE HE1 ? ? SING CE HE2 ? ? SING CE HE3 ? ? stop_ save_ ############# # Ligands # ############# save_ACO _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'ACETYL COENZYME *A' _BMRB_code ACO _PDB_code ACO _Molecular_mass 809.571 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N1A N1A N . 0 . ? C2A C2A C . 0 . ? N3A N3A N . 0 . ? C4A C4A C . 0 . ? C5A C5A C . 0 . ? C6A C6A C . 0 . ? N6A N6A N . 0 . ? N7A N7A N . 0 . ? C8A C8A C . 0 . ? N9A N9A N . 0 . ? C1B C1B C . 0 . ? C2B C2B C . 0 . ? O2B O2B O . 0 . ? C3B C3B C . 0 . ? O3B O3B O . 0 . ? P3B P3B P . 0 . ? O7A O7A O . 0 . ? O8A O8A O . 0 . ? O9A O9A O . 0 . ? C4B C4B C . 0 . ? O4B O4B O . 0 . ? C5B C5B C . 0 . ? O5B O5B O . 0 . ? P1A P1A P . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? O3A O3A O . 0 . ? P2A P2A P . 0 . ? O4A O4A O . 0 . ? O5A O5A O . 0 . ? O6A O6A O . 0 . ? CBP CBP C . 0 . ? CCP CCP C . 0 . ? CDP CDP C . 0 . ? CEP CEP C . 0 . ? CAP CAP C . 0 . ? OAP OAP O . 0 . ? C9P C9P C . 0 . ? O9P O9P O . 0 . ? N8P N8P N . 0 . ? C7P C7P C . 0 . ? C6P C6P C . 0 . ? C5P C5P C . 0 . ? O5P O5P O . 0 . ? N4P N4P N . 0 . ? C3P C3P C . 0 . ? C2P C2P C . 0 . ? S1P S1P S . 0 . ? C C C . 0 . ? O O O . 0 . ? CH3 CH3 C . 0 . ? H2A H2A H . 0 . ? H61A H61A H . 0 . ? H62A H62A H . 0 . ? H8A H8A H . 0 . ? H1B H1B H . 0 . ? H2B H2B H . 0 . ? HO2A HO2A H . 0 . ? H3B H3B H . 0 . ? HOA8 HOA8 H . 0 . ? HOA9 HOA9 H . 0 . ? H4B H4B H . 0 . ? H51A H51A H . 0 . ? H52A H52A H . 0 . ? HOA2 HOA2 H . 0 . ? HOA5 HOA5 H . 0 . ? H121 H121 H . 0 . ? H122 H122 H . 0 . ? H131 H131 H . 0 . ? H132 H132 H . 0 . ? H133 H133 H . 0 . ? H141 H141 H . 0 . ? H142 H142 H . 0 . ? H143 H143 H . 0 . ? H10 H10 H . 0 . ? HO1 HO1 H . 0 . ? HN8 HN8 H . 0 . ? H71 H71 H . 0 . ? H72 H72 H . 0 . ? H61 H61 H . 0 . ? H62 H62 H . 0 . ? HN4 HN4 H . 0 . ? H31 H31 H . 0 . ? H32 H32 H . 0 . ? H21 H21 H . 0 . ? H22 H22 H . 0 . ? HH31 HH31 H . 0 . ? HH32 HH32 H . 0 . ? HH33 HH33 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N1A C2A ? ? DOUB N1A C6A ? ? DOUB C2A N3A ? ? SING C2A H2A ? ? SING N3A C4A ? ? DOUB C4A C5A ? ? SING C4A N9A ? ? SING C5A C6A ? ? SING C5A N7A ? ? SING C6A N6A ? ? SING N6A H61A ? ? SING N6A H62A ? ? DOUB N7A C8A ? ? SING C8A N9A ? ? SING C8A H8A ? ? SING N9A C1B ? ? SING C1B C2B ? ? SING C1B O4B ? ? SING C1B H1B ? ? SING C2B O2B ? ? SING C2B C3B ? ? SING C2B H2B ? ? SING O2B HO2A ? ? SING C3B O3B ? ? SING C3B C4B ? ? SING C3B H3B ? ? SING O3B P3B ? ? DOUB P3B O7A ? ? SING P3B O8A ? ? SING P3B O9A ? ? SING O8A HOA8 ? ? SING O9A HOA9 ? ? SING C4B O4B ? ? SING C4B C5B ? ? SING C4B H4B ? ? SING C5B O5B ? ? SING C5B H51A ? ? SING C5B H52A ? ? SING O5B P1A ? ? DOUB P1A O1A ? ? SING P1A O2A ? ? SING P1A O3A ? ? SING O2A HOA2 ? ? SING O3A P2A ? ? DOUB P2A O4A ? ? SING P2A O5A ? ? SING P2A O6A ? ? SING O5A HOA5 ? ? SING O6A CCP ? ? SING CBP CCP ? ? SING CBP CDP ? ? SING CBP CEP ? ? SING CBP CAP ? ? SING CCP H121 ? ? SING CCP H122 ? ? SING CDP H131 ? ? SING CDP H132 ? ? SING CDP H133 ? ? SING CEP H141 ? ? SING CEP H142 ? ? SING CEP H143 ? ? SING CAP OAP ? ? SING CAP C9P ? ? SING CAP H10 ? ? SING OAP HO1 ? ? DOUB C9P O9P ? ? SING C9P N8P ? ? SING N8P C7P ? ? SING N8P HN8 ? ? SING C7P C6P ? ? SING C7P H71 ? ? SING C7P H72 ? ? SING C6P C5P ? ? SING C6P H61 ? ? SING C6P H62 ? ? DOUB C5P O5P ? ? SING C5P N4P ? ? SING N4P C3P ? ? SING N4P HN4 ? ? SING C3P C2P ? ? SING C3P H31 ? ? SING C3P H32 ? ? SING C2P S1P ? ? SING C2P H21 ? ? SING C2P H22 ? ? SING S1P C ? ? DOUB C O ? ? SING C CH3 ? ? SING CH3 HH31 ? ? SING CH3 HH32 ? ? SING CH3 HH33 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $hNaa50p Human 9606 Eukaryota Metazoa Homo sapiens 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 $hNaa50p 'recombinant technology' . Escherichia coli 'BL21 Star (DE3)' pETM-30 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $hNaa50p 0.2 mM '[U-98% 13C; U-98% 15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version . loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 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' 0.1 0.01 M pH 7.4 0.2 pH pressure 1 . atm temperature 310 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D C(CO)NH' '3D HNCO' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name hNaa50p _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 7 GLY C C 174.052 0.3 1 2 3 7 GLY CA C 45.229 0.3 1 3 4 8 SER H H 8.091 0.02 1 4 4 8 SER C C 173.428 0.3 1 5 4 8 SER CA C 57.483 0.3 1 6 4 8 SER CB C 64.012 0.3 1 7 4 8 SER N N 116.159 0.1 1 8 5 9 ARG H H 8.177 0.02 1 9 5 9 ARG C C 174.978 0.3 1 10 5 9 ARG CA C 55.874 0.3 1 11 5 9 ARG CB C 31.008 0.3 1 12 5 9 ARG CG C 27.617 0.3 1 13 5 9 ARG CD C 43.139 0.3 1 14 5 9 ARG N N 123.370 0.1 1 15 6 10 ILE H H 8.336 0.02 1 16 6 10 ILE C C 175.645 0.3 1 17 6 10 ILE CA C 60.125 0.3 1 18 6 10 ILE CB C 39.169 0.3 1 19 6 10 ILE CD1 C 18.047 0.3 1 20 6 10 ILE N N 124.967 0.1 1 21 7 11 GLU H H 8.749 0.02 1 22 7 11 GLU C C 174.353 0.3 1 23 7 11 GLU CA C 54.248 0.3 1 24 7 11 GLU CB C 34.173 0.3 1 25 7 11 GLU CG C 35.830 0.3 1 26 7 11 GLU N N 129.944 0.1 1 27 8 12 LEU H H 8.843 0.02 1 28 8 12 LEU C C 177.411 0.3 1 29 8 12 LEU CA C 52.849 0.3 1 30 8 12 LEU CB C 42.311 0.3 1 31 8 12 LEU CD1 C 26.939 0.3 2 32 8 12 LEU CD2 C 26.261 0.3 2 33 8 12 LEU N N 120.694 0.1 1 34 9 13 GLY H H 9.577 0.02 1 35 9 13 GLY C C 172.178 0.3 1 36 9 13 GLY CA C 44.032 0.3 1 37 9 13 GLY N N 109.290 0.1 1 38 10 14 ASP H H 8.420 0.02 1 39 10 14 ASP C C 176.442 0.3 1 40 10 14 ASP CA C 54.991 0.3 1 41 10 14 ASP CB C 41.105 0.3 1 42 10 14 ASP N N 119.798 0.1 1 43 11 15 VAL H H 9.152 0.02 1 44 11 15 VAL C C 175.172 0.3 1 45 11 15 VAL CA C 62.203 0.3 1 46 11 15 VAL CB C 31.460 0.3 1 47 11 15 VAL CG1 C 22.418 0.3 2 48 11 15 VAL CG2 C 21.589 0.3 2 49 11 15 VAL N N 123.208 0.1 1 50 12 16 THR H H 9.666 0.02 1 51 12 16 THR C C 173.371 0.3 1 52 12 16 THR CA C 58.824 0.3 1 53 12 16 THR CB C 69.717 0.3 1 54 12 16 THR CG2 C 21.137 0.3 1 55 12 16 THR N N 120.227 0.1 1 56 14 18 HIS C C 176.550 0.3 1 57 14 18 HIS CA C 56.875 0.3 1 58 14 18 HIS CB C 30.556 0.3 1 59 15 19 ASN H H 7.794 0.02 1 60 15 19 ASN C C 178.251 0.3 1 61 15 19 ASN CA C 52.580 0.3 1 62 15 19 ASN CB C 38.694 0.3 1 63 15 19 ASN N N 115.469 0.1 1 64 16 20 ILE H H 7.623 0.02 1 65 16 20 ILE C C 176.636 0.3 1 66 16 20 ILE CA C 63.015 0.3 1 67 16 20 ILE CB C 37.743 0.3 1 68 16 20 ILE CG2 C 17.746 0.3 1 69 16 20 ILE CD1 C 14.958 0.3 1 70 16 20 ILE N N 121.164 0.1 1 71 17 21 LYS H H 8.364 0.02 1 72 17 21 LYS C C 179.199 0.3 1 73 17 21 LYS CA C 59.620 0.3 1 74 17 21 LYS CB C 31.686 0.3 1 75 17 21 LYS CG C 24.527 0.3 1 76 17 21 LYS CE C 41.557 0.3 1 77 17 21 LYS N N 120.644 0.1 1 78 18 22 GLN H H 7.738 0.02 1 79 18 22 GLN C C 178.230 0.3 1 80 18 22 GLN CA C 58.339 0.3 1 81 18 22 GLN CB C 28.069 0.3 1 82 18 22 GLN N N 118.787 0.1 1 83 19 23 LEU H H 7.423 0.02 1 84 19 23 LEU C C 177.541 0.3 1 85 19 23 LEU CA C 58.484 0.3 1 86 19 23 LEU CB C 41.545 0.3 1 87 19 23 LEU CG C 27.014 0.3 1 88 19 23 LEU CD1 C 21.438 0.3 2 89 19 23 LEU CD2 C 20.308 0.3 2 90 19 23 LEU N N 120.456 0.1 1 91 20 24 LYS H H 8.062 0.02 1 92 20 24 LYS C C 178.424 0.3 1 93 20 24 LYS CA C 59.814 0.3 1 94 20 24 LYS CB C 32.063 0.3 1 95 20 24 LYS CE C 41.180 0.3 1 96 20 24 LYS N N 117.910 0.1 1 97 21 25 ARG H H 7.563 0.02 1 98 21 25 ARG C C 178.693 0.3 1 99 21 25 ARG CA C 59.039 0.3 1 100 21 25 ARG CB C 29.802 0.3 1 101 21 25 ARG CD C 43.064 0.3 1 102 21 25 ARG N N 117.892 0.1 1 103 22 26 LEU H H 8.006 0.02 1 104 22 26 LEU C C 178.897 0.3 1 105 22 26 LEU CA C 57.969 0.3 1 106 22 26 LEU CB C 41.946 0.3 1 107 22 26 LEU CG C 29.953 0.3 1 108 22 26 LEU CD1 C 27.010 0.3 2 109 22 26 LEU CD2 C 25.658 0.3 2 110 22 26 LEU N N 118.736 0.1 1 111 23 27 ASN H H 8.627 0.02 1 112 23 27 ASN C C 179.048 0.3 1 113 23 27 ASN CA C 55.438 0.3 1 114 23 27 ASN CB C 36.584 0.3 1 115 23 27 ASN N N 117.916 0.1 1 116 24 28 GLN H H 8.208 0.02 1 117 24 28 GLN C C 177.282 0.3 1 118 24 28 GLN CA C 58.371 0.3 1 119 24 28 GLN CB C 28.370 0.3 1 120 24 28 GLN N N 118.739 0.1 1 121 25 29 VAL H H 7.472 0.02 1 122 25 29 VAL C C 177.885 0.3 1 123 25 29 VAL CA C 64.275 0.3 1 124 25 29 VAL CB C 32.515 0.3 1 125 25 29 VAL CG1 C 21.815 0.3 2 126 25 29 VAL CG2 C 21.815 0.3 2 127 25 29 VAL N N 115.475 0.1 1 128 26 30 ILE H H 8.060 0.02 1 129 26 30 ILE C C 178.870 0.3 1 130 26 30 ILE CA C 66.018 0.3 1 131 26 30 ILE CB C 39.619 0.3 1 132 26 30 ILE N N 118.524 0.1 1 133 27 31 PHE H H 8.426 0.02 1 134 27 31 PHE CA C 56.984 0.3 1 135 27 31 PHE CB C 40.145 0.3 1 136 27 31 PHE N N 117.585 0.1 1 137 28 32 PRO C C 176.012 0.3 1 138 28 32 PRO CA C 63.545 0.3 1 139 28 32 PRO CB C 30.857 0.3 1 140 29 33 VAL H H 6.958 0.02 1 141 29 33 VAL C C 174.332 0.3 1 142 29 33 VAL CA C 60.285 0.3 1 143 29 33 VAL CB C 33.645 0.3 1 144 29 33 VAL CG1 C 22.794 0.3 2 145 29 33 VAL CG2 C 20.006 0.3 2 146 29 33 VAL N N 116.478 0.1 1 147 30 34 SER C C 173.674 0.3 1 148 30 34 SER CA C 57.493 0.3 1 149 30 34 SER CB C 63.562 0.3 1 150 31 35 TYR H H 8.092 0.02 1 151 31 35 TYR C C 176.744 0.3 1 152 31 35 TYR CA C 58.018 0.3 1 153 31 35 TYR N N 124.463 0.1 1 154 33 37 ASP C C 178.811 0.3 1 155 33 37 ASP CA C 57.712 0.3 1 156 33 37 ASP CB C 40.428 0.3 1 157 34 38 LYS H H 8.128 0.02 1 158 34 38 LYS C C 177.399 0.3 1 159 34 38 LYS CA C 59.129 0.3 1 160 34 38 LYS CB C 32.192 0.3 1 161 34 38 LYS CE C 42.235 0.3 1 162 34 38 LYS N N 120.897 0.1 1 163 35 39 PHE H H 7.779 0.02 1 164 35 39 PHE C C 179.306 0.3 1 165 35 39 PHE CA C 61.160 0.3 1 166 35 39 PHE CB C 38.568 0.3 1 167 35 39 PHE N N 119.918 0.1 1 168 37 41 LYS C C 179.056 0.3 1 169 37 41 LYS CA C 58.759 0.3 1 170 37 41 LYS CB C 32.339 0.3 1 171 38 42 ASP H H 8.365 0.02 1 172 38 42 ASP C C 179.910 0.3 1 173 38 42 ASP CA C 57.019 0.3 1 174 38 42 ASP CB C 39.523 0.3 1 175 38 42 ASP N N 120.39 0.1 1 176 39 43 VAL H H 7.699 0.02 1 177 39 43 VAL C C 176.383 0.3 1 178 39 43 VAL CA C 64.830 0.3 1 179 39 43 VAL CB C 31.782 0.3 1 180 39 43 VAL CG1 C 22.418 0.3 1 181 39 43 VAL CG2 C 21.438 0.3 1 182 39 43 VAL N N 117.505 0.1 1 183 40 44 LEU H H 7.110 0.02 1 184 40 44 LEU C C 178.144 0.3 1 185 40 44 LEU CA C 56.244 0.3 1 186 40 44 LEU CB C 41.406 0.3 1 187 40 44 LEU CD1 C 25.808 0.3 2 188 40 44 LEU CD2 C 25.808 0.3 2 189 40 44 LEU N N 117.545 0.1 1 190 41 45 GLU H H 7.710 0.02 1 191 41 45 GLU C C 177.912 0.3 1 192 41 45 GLU CA C 56.304 0.3 1 193 41 45 GLU CB C 30.480 0.3 1 194 41 45 GLU CG C 35.755 0.3 1 195 41 45 GLU N N 115.905 0.1 1 196 42 46 VAL H H 7.160 0.02 1 197 42 46 VAL C C 177.347 0.3 1 198 42 46 VAL CA C 61.859 0.3 1 199 42 46 VAL CB C 31.686 0.3 1 200 42 46 VAL CG1 C 20.458 0.3 2 201 42 46 VAL CG2 C 19.253 0.3 2 202 42 46 VAL N N 111.607 0.1 1 203 43 47 GLY H H 8.281 0.02 1 204 43 47 GLY C C 175.736 0.3 1 205 43 47 GLY CA C 47.117 0.3 1 206 43 47 GLY N N 113.940 0.1 1 207 44 48 GLU H H 8.838 0.02 1 208 44 48 GLU C C 175.344 0.3 1 209 44 48 GLU CA C 57.962 0.3 1 210 44 48 GLU CB C 29.727 0.3 1 211 44 48 GLU CG C 35.680 0.3 1 212 44 48 GLU N N 122.135 0.1 1 213 45 49 LEU H H 7.322 0.02 1 214 45 49 LEU C C 174.159 0.3 1 215 45 49 LEU CA C 56.025 0.3 1 216 45 49 LEU CB C 40.804 0.3 1 217 45 49 LEU CG C 28.069 0.3 1 218 45 49 LEU CD1 C 25.507 0.3 2 219 45 49 LEU CD2 C 23.473 0.3 2 220 45 49 LEU N N 118.188 0.1 1 221 46 50 ALA H H 7.885 0.02 1 222 46 50 ALA C C 175.904 0.3 1 223 46 50 ALA CA C 50.848 0.3 1 224 46 50 ALA CB C 21.966 0.3 1 225 46 50 ALA N N 121.516 0.1 1 226 47 51 LYS H H 8.839 0.02 1 227 47 51 LYS C C 175.713 0.3 1 228 47 51 LYS CA C 53.316 0.3 1 229 47 51 LYS CB C 37.111 0.3 1 230 47 51 LYS N N 117.201 0.1 1 231 48 52 LEU H H 8.583 0.02 1 232 48 52 LEU C C 174.719 0.3 1 233 48 52 LEU CA C 54.065 0.3 1 234 48 52 LEU CB C 45.475 0.3 1 235 48 52 LEU CG C 25.432 0.3 1 236 48 52 LEU N N 119.712 0.1 1 237 49 53 ALA H H 8.322 0.02 1 238 49 53 ALA C C 175.193 0.3 1 239 49 53 ALA CA C 50.255 0.3 1 240 49 53 ALA CB C 21.287 0.3 1 241 49 53 ALA N N 122.627 0.1 1 242 50 54 TYR H H 9.300 0.02 1 243 50 54 TYR C C 174.606 0.3 1 244 50 54 TYR CA C 56.598 0.3 1 245 50 54 TYR CB C 41.843 0.3 1 246 50 54 TYR N N 120.871 0.1 1 247 51 55 PHE H H 9.048 0.02 1 248 51 55 PHE C C 175.258 0.3 1 249 51 55 PHE CA C 56.045 0.3 1 250 51 55 PHE CB C 42.537 0.3 1 251 51 55 PHE N N 122.986 0.1 1 252 52 56 ASN H H 9.025 0.02 1 253 52 56 ASN C C 174.246 0.3 1 254 52 56 ASN CA C 54.593 0.3 1 255 52 56 ASN CB C 36.508 0.3 1 256 52 56 ASN N N 126.391 0.1 1 257 53 57 ASP H H 8.957 0.02 1 258 53 57 ASP C C 174.793 0.3 1 259 53 57 ASP CA C 56.553 0.3 1 260 53 57 ASP CB C 39.749 0.3 1 261 53 57 ASP N N 109.216 0.1 1 262 54 58 ILE H H 8.072 0.02 1 263 54 58 ILE C C 175.688 0.3 1 264 54 58 ILE CA C 60.083 0.3 1 265 54 58 ILE CB C 39.146 0.3 1 266 54 58 ILE CG1 C 26.637 0.3 1 267 54 58 ILE N N 121.951 0.1 1 268 55 59 ALA H H 8.759 0.02 1 269 55 59 ALA C C 176.894 0.3 1 270 55 59 ALA CA C 52.203 0.3 1 271 55 59 ALA CB C 17.294 0.3 1 272 55 59 ALA N N 130.493 0.1 1 273 56 60 VAL H H 8.480 0.02 1 274 56 60 VAL C C 174.426 0.3 1 275 56 60 VAL CA C 60.190 0.3 1 276 56 60 VAL CB C 37.097 0.3 1 277 56 60 VAL CG1 C 19.931 0.3 2 278 56 60 VAL CG2 C 18.650 0.3 2 279 56 60 VAL N N 113.270 0.1 1 280 57 61 GLY H H 7.754 0.02 1 281 57 61 GLY C C 170.175 0.3 1 282 57 61 GLY CA C 46.081 0.3 1 283 57 61 GLY N N 108.002 0.1 1 284 58 62 ALA H H 8.580 0.02 1 285 58 62 ALA C C 175.732 0.3 1 286 58 62 ALA CA C 52.655 0.3 1 287 58 62 ALA CB C 23.699 0.3 1 288 58 62 ALA N N 119.004 0.1 1 289 59 63 VAL H H 8.850 0.02 1 290 59 63 VAL C C 172.760 0.3 1 291 59 63 VAL CA C 58.012 0.3 1 292 59 63 VAL CB C 33.570 0.3 1 293 59 63 VAL N N 118.998 0.1 1 294 61 65 CYS C C 171.403 0.3 1 295 61 65 CYS CA C 56.531 0.3 1 296 61 65 CYS CB C 31.837 0.3 1 297 62 66 ARG H H 9.074 0.02 1 298 62 66 ARG C C 173.729 0.3 1 299 62 66 ARG CA C 54.819 0.3 1 300 62 66 ARG CB C 34.323 0.3 1 301 62 66 ARG CD C 43.667 0.3 1 302 62 66 ARG N N 116.200 0.1 1 303 63 67 VAL H H 8.870 0.02 1 304 63 67 VAL C C 175.021 0.3 1 305 63 67 VAL CA C 63.409 0.3 1 306 63 67 VAL CB C 31.761 0.3 1 307 63 67 VAL CG1 C 21.589 0.3 2 308 63 67 VAL CG2 C 21.589 0.3 2 309 63 67 VAL N N 123.336 0.1 1 310 64 68 ASP H H 9.419 0.02 1 311 64 68 ASP C C 174.741 0.3 1 312 64 68 ASP CA C 52.971 0.3 1 313 64 68 ASP CB C 43.818 0.3 1 314 64 68 ASP N N 129.356 0.1 1 315 65 69 HIS H H 8.752 0.02 1 316 65 69 HIS C C 175.085 0.3 1 317 65 69 HIS CA C 55.254 0.3 1 318 65 69 HIS CB C 30.301 0.3 1 319 65 69 HIS N N 124.956 0.1 1 320 66 70 SER H H 8.225 0.02 1 321 66 70 SER C C 174.395 0.3 1 322 66 70 SER CA C 58.133 0.3 1 323 66 70 SER CB C 64.012 0.3 1 324 66 70 SER N N 117.826 0.1 1 325 67 71 GLN H H 8.118 0.02 1 326 67 71 GLN C C 175.372 0.3 1 327 67 71 GLN CA C 57.062 0.3 1 328 67 71 GLN CB C 26.939 0.3 1 329 67 71 GLN N N 122.133 0.1 1 330 68 72 ASN H H 8.573 0.02 1 331 68 72 ASN C C 174.420 0.3 1 332 68 72 ASN CA C 54.356 0.3 1 333 68 72 ASN CB C 37.789 0.3 1 334 68 72 ASN N N 112.874 0.1 1 335 69 73 GLN H H 7.749 0.02 1 336 69 73 GLN C C 174.073 0.3 1 337 69 73 GLN CA C 54.647 0.3 1 338 69 73 GLN CB C 32.741 0.3 1 339 69 73 GLN CG C 33.794 0.3 1 340 69 73 GLN N N 117.507 0.1 1 341 70 74 LYS H H 9.395 0.02 1 342 70 74 LYS C C 174.999 0.3 1 343 70 74 LYS CA C 56.348 0.3 1 344 70 74 LYS CB C 33.268 0.3 1 345 70 74 LYS N N 125.172 0.1 1 346 71 75 ARG H H 8.986 0.02 1 347 71 75 ARG C C 174.461 0.3 1 348 71 75 ARG CA C 53.774 0.3 1 349 71 75 ARG CB C 34.878 0.3 1 350 71 75 ARG CD C 43.818 0.3 1 351 71 75 ARG N N 125.602 0.1 1 352 72 76 LEU H H 8.883 0.02 1 353 72 76 LEU C C 173.772 0.3 1 354 72 76 LEU CA C 53.165 0.3 1 355 72 76 LEU CB C 41.783 0.3 1 356 72 76 LEU CG C 27.316 0.3 1 357 72 76 LEU CD1 C 25.808 0.3 2 358 72 76 LEU CD2 C 24.527 0.3 2 359 72 76 LEU N N 125.716 0.1 1 360 73 77 TYR H H 9.275 0.02 1 361 73 77 TYR C C 175.818 0.3 1 362 73 77 TYR CA C 54.388 0.3 1 363 73 77 TYR CB C 39.781 0.3 1 364 73 77 TYR N N 128.124 0.1 1 365 74 78 ILE H H 8.084 0.02 1 366 74 78 ILE C C 172.626 0.3 1 367 74 78 ILE CA C 58.389 0.3 1 368 74 78 ILE CB C 37.368 0.3 1 369 74 78 ILE CG2 C 18.047 0.3 1 370 74 78 ILE CD1 C 13.677 0.3 1 371 74 78 ILE N N 127.915 0.1 1 372 75 79 MSE H H 9.022 0.02 1 373 75 79 MSE C C 176.571 0.3 1 374 75 79 MSE CA C 58.948 0.3 1 375 75 79 MSE CB C 33.570 0.3 1 376 75 79 MSE N N 122.865 0.1 1 377 76 80 THR H H 7.697 0.02 1 378 76 80 THR C C 172.393 0.3 1 379 76 80 THR CA C 59.900 0.3 1 380 76 80 THR CB C 70.643 0.3 1 381 76 80 THR CG2 C 22.893 0.3 1 382 76 80 THR N N 106.484 0.1 1 383 77 81 LEU H H 6.856 0.02 1 384 77 81 LEU C C 175.997 0.3 1 385 77 81 LEU CA C 57.381 0.3 1 386 77 81 LEU CB C 42.763 0.3 1 387 77 81 LEU N N 124.211 0.1 1 388 78 82 GLY H H 8.602 0.02 1 389 78 82 GLY C C 170.132 0.3 1 390 78 82 GLY CA C 46.559 0.3 1 391 78 82 GLY N N 112.465 0.1 1 392 79 83 CYS H H 8.950 0.02 1 393 79 83 CYS CA C 55.512 0.3 1 394 79 83 CYS CB C 31.495 0.3 1 395 79 83 CYS N N 116.069 0.1 1 396 80 84 LEU H H 8.883 0.02 1 397 80 84 LEU C C 176.076 0.3 1 398 80 84 LEU CA C 52.865 0.3 1 399 80 84 LEU CB C 43.972 0.3 1 400 80 84 LEU N N 125.245 0.1 1 401 81 85 ALA H H 9.233 0.02 1 402 81 85 ALA C C 174.181 0.3 1 403 81 85 ALA CA C 54.491 0.3 1 404 81 85 ALA CB C 17.252 0.3 1 405 81 85 ALA N N 119.762 0.1 1 406 82 86 PRO C C 176.076 0.3 1 407 82 86 PRO CA C 64.618 0.3 1 408 82 86 PRO CB C 30.480 0.3 1 409 82 86 PRO CD C 50.449 0.3 1 410 83 87 TYR H H 7.835 0.02 1 411 83 87 TYR C C 173.061 0.3 1 412 83 87 TYR CA C 56.875 0.3 1 413 83 87 TYR CB C 37.865 0.3 1 414 83 87 TYR N N 114.648 0.1 1 415 84 88 ARG H H 6.672 0.02 1 416 84 88 ARG C C 175.129 0.3 1 417 84 88 ARG CA C 57.019 0.3 1 418 84 88 ARG CB C 31.363 0.3 1 419 84 88 ARG N N 117.759 0.1 1 420 85 89 ARG H H 9.519 0.02 1 421 85 89 ARG C C 176.205 0.3 1 422 85 89 ARG CA C 57.326 0.3 1 423 85 89 ARG N N 116.958 0.1 1 424 86 90 LEU C C 178.057 0.3 1 425 86 90 LEU CA C 53.570 0.3 1 426 86 90 LEU CB C 43.667 0.3 1 427 86 90 LEU CD1 C 26.261 0.3 2 428 86 90 LEU CD2 C 25.507 0.3 2 429 87 91 GLY H H 9.565 0.02 1 430 87 91 GLY C C 177.196 0.3 1 431 87 91 GLY CA C 45.249 0.3 1 432 87 91 GLY N N 111.600 0.1 1 433 88 92 ILE H H 9.349 0.02 1 434 88 92 ILE C C 178.043 0.3 1 435 88 92 ILE CA C 66.419 0.3 1 436 88 92 ILE CB C 35.755 0.3 1 437 88 92 ILE CG1 C 28.973 0.3 1 438 88 92 ILE N N 125.470 0.1 1 439 89 93 GLY H H 9.690 0.02 1 440 89 93 GLY C C 176.593 0.3 1 441 89 93 GLY CA C 47.760 0.3 1 442 89 93 GLY N N 112.581 0.1 1 443 90 94 THR H H 9.448 0.02 1 444 90 94 THR C C 175.538 0.3 1 445 90 94 THR CA C 68.948 0.3 1 446 90 94 THR CG2 C 20.986 0.3 1 447 90 94 THR N N 121.041 0.1 1 448 91 95 LYS H H 7.854 0.02 1 449 91 95 LYS C C 180.233 0.3 1 450 91 95 LYS CA C 59.732 0.3 1 451 91 95 LYS CB C 31.888 0.3 1 452 91 95 LYS CE C 41.783 0.3 1 453 91 95 LYS N N 122.482 0.1 1 454 92 96 MSE H H 8.268 0.02 1 455 92 96 MSE C C 177.174 0.3 1 456 92 96 MSE CA C 61.052 0.3 1 457 92 96 MSE CB C 34.365 0.3 1 458 92 96 MSE N N 117.717 0.1 1 459 93 97 LEU H H 8.987 0.02 1 460 93 97 LEU C C 178.811 0.3 1 461 93 97 LEU CA C 57.176 0.3 1 462 93 97 LEU CB C 40.728 0.3 1 463 93 97 LEU CD1 C 25.582 0.3 2 464 93 97 LEU CD2 C 22.644 0.3 2 465 93 97 LEU N N 120.657 0.1 1 466 94 98 ASN H H 9.080 0.02 1 467 94 98 ASN C C 178.165 0.3 1 468 94 98 ASN CA C 56.165 0.3 1 469 94 98 ASN CB C 37.639 0.3 1 470 94 98 ASN N N 117.778 0.1 1 471 95 99 HIS H H 7.646 0.02 1 472 95 99 HIS C C 176.701 0.3 1 473 95 99 HIS CA C 60.460 0.3 1 474 95 99 HIS CB C 30.254 0.3 1 475 95 99 HIS N N 120.475 0.1 1 476 96 100 VAL H H 7.398 0.02 1 477 96 100 VAL C C 178.014 0.3 1 478 96 100 VAL CA C 66.552 0.3 1 479 96 100 VAL CB C 31.385 0.3 1 480 96 100 VAL CG1 C 22.506 0.3 2 481 96 100 VAL CG2 C 22.506 0.3 2 482 96 100 VAL N N 118.052 0.1 1 483 97 101 LEU H H 8.731 0.02 1 484 97 101 LEU C C 179.651 0.3 1 485 97 101 LEU CA C 58.484 0.3 1 486 97 101 LEU CB C 40.125 0.3 1 487 97 101 LEU CD1 C 26.035 0.3 2 488 97 101 LEU CD2 C 26.035 0.3 2 489 97 101 LEU N N 119.358 0.1 1 490 98 102 ASN H H 8.343 0.02 1 491 98 102 ASN C C 177.720 0.3 1 492 98 102 ASN CA C 56.423 0.3 1 493 98 102 ASN CB C 38.392 0.3 1 494 98 102 ASN N N 119.097 0.1 1 495 99 103 ILE H H 7.833 0.02 1 496 99 103 ILE C C 179.499 0.3 1 497 99 103 ILE CA C 64.496 0.3 1 498 99 103 ILE CG1 C 27.692 0.3 1 499 99 103 ILE CD1 C 16.616 0.3 1 500 99 103 ILE N N 120.512 0.1 1 501 100 104 CYS H H 7.734 0.02 1 502 100 104 CYS C C 177.713 0.3 1 503 100 104 CYS CA C 63.774 0.3 1 504 100 104 CYS CB C 26.713 0.3 1 505 100 104 CYS N N 117.407 0.1 1 506 101 105 GLU H H 8.539 0.02 1 507 101 105 GLU C C 178.445 0.3 1 508 101 105 GLU CA C 59.342 0.3 1 509 101 105 GLU CB C 29.425 0.3 1 510 101 105 GLU CG C 35.830 0.3 1 511 101 105 GLU N N 122.890 0.1 1 512 102 106 LYS H H 8.012 0.02 1 513 102 106 LYS C C 177.777 0.3 1 514 102 106 LYS CA C 58.360 0.3 1 515 102 106 LYS CB C 32.063 0.3 1 516 102 106 LYS CG C 24.678 0.3 1 517 102 106 LYS CE C 41.632 0.3 1 518 102 106 LYS N N 117.685 0.1 1 519 103 107 ASP H H 7.663 0.02 1 520 103 107 ASP C C 177.734 0.3 1 521 103 107 ASP CA C 56.832 0.3 1 522 103 107 ASP CB C 43.215 0.3 1 523 103 107 ASP N N 119.048 0.1 1 524 104 108 GLY H H 8.171 0.02 1 525 104 108 GLY C C 176.421 0.3 1 526 104 108 GLY CA C 46.380 0.3 1 527 104 108 GLY N N 102.779 0.1 1 528 105 109 THR H H 9.036 0.02 1 529 105 109 THR C C 175.042 0.3 1 530 105 109 THR CA C 61.858 0.3 1 531 105 109 THR CB C 69.513 0.3 1 532 105 109 THR CG2 C 20.986 0.3 1 533 105 109 THR N N 111.117 0.1 1 534 106 110 PHE H H 8.297 0.02 1 535 106 110 PHE C C 175.990 0.3 1 536 106 110 PHE CA C 59.168 0.3 1 537 106 110 PHE CB C 39.975 0.3 1 538 106 110 PHE N N 120.240 0.1 1 539 107 111 ASP H H 9.669 0.02 1 540 107 111 ASP C C 177.045 0.3 1 541 107 111 ASP CA C 57.435 0.3 1 542 107 111 ASP CB C 43.365 0.3 1 543 107 111 ASP N N 119.926 0.1 1 544 108 112 ASN H H 7.545 0.02 1 545 108 112 ASN C C 171.769 0.3 1 546 108 112 ASN CA C 52.940 0.3 1 547 108 112 ASN CB C 41.445 0.3 1 548 108 112 ASN N N 108.307 0.1 1 549 109 113 ILE H H 8.273 0.02 1 550 109 113 ILE C C 174.418 0.3 1 551 109 113 ILE CA C 58.828 0.3 1 552 109 113 ILE N N 118.038 0.1 1 553 110 114 TYR H H 9.747 0.02 1 554 110 114 TYR C C 171.166 0.3 1 555 110 114 TYR CA C 55.949 0.3 1 556 110 114 TYR CB C 42.009 0.3 1 557 110 114 TYR N N 126.350 0.1 1 558 111 115 LEU H H 8.503 0.02 1 559 111 115 LEU C C 174.112 0.3 1 560 111 115 LEU CA C 55.567 0.3 1 561 111 115 LEU CB C 43.215 0.3 1 562 111 115 LEU CD1 C 26.016 0.3 2 563 111 115 LEU CD2 C 26.016 0.3 2 564 111 115 LEU N N 114.579 0.1 1 565 112 116 HIS C C 175.631 0.3 1 566 112 116 HIS CA C 55.964 0.3 1 567 112 116 HIS CB C 33.784 0.3 1 568 113 117 VAL H H 7.860 0.02 1 569 113 117 VAL CA C 57.574 0.3 1 570 113 117 VAL N N 127.761 0.1 1 571 114 118 GLN C C 176.876 0.3 1 572 114 118 GLN CA C 57.541 0.3 1 573 114 118 GLN CB C 30.028 0.3 1 574 115 119 ILE H H 7.646 0.02 1 575 115 119 ILE C C 175.021 0.3 1 576 115 119 ILE CA C 64.814 0.3 1 577 115 119 ILE CD1 C 16.314 0.3 1 578 115 119 ILE N N 116.432 0.1 1 579 116 120 SER H H 7.059 0.02 1 580 116 120 SER C C 175.021 0.3 1 581 116 120 SER CA C 57.790 0.3 1 582 116 120 SER CB C 63.306 0.3 1 583 116 120 SER N N 109.610 0.1 1 584 117 121 ASN H H 8.020 0.02 1 585 117 121 ASN C C 174.964 0.3 1 586 117 121 ASN CA C 51.291 0.3 1 587 117 121 ASN CB C 36.358 0.3 1 588 117 121 ASN N N 123.712 0.1 1 589 118 122 GLU H H 8.095 0.02 1 590 118 122 GLU C C 178.359 0.3 1 591 118 122 GLU CA C 59.771 0.3 1 592 118 122 GLU CB C 29.802 0.3 1 593 118 122 GLU N N 123.983 0.1 1 594 119 123 SER H H 8.792 0.02 1 595 119 123 SER C C 177.153 0.3 1 596 119 123 SER CA C 61.267 0.3 1 597 119 123 SER CB C 62.430 0.3 1 598 119 123 SER N N 113.355 0.1 1 599 120 124 ALA H H 7.391 0.02 1 600 120 124 ALA C C 178.637 0.3 1 601 120 124 ALA CA C 54.806 0.3 1 602 120 124 ALA CB C 19.854 0.3 1 603 120 124 ALA N N 122.731 0.1 1 604 121 125 ILE H H 8.103 0.02 1 605 121 125 ILE C C 177.497 0.3 1 606 121 125 ILE CA C 66.970 0.3 1 607 121 125 ILE CB C 40.125 0.3 1 608 121 125 ILE CG1 C 25.658 0.3 1 609 121 125 ILE CG2 C 17.260 0.3 1 610 121 125 ILE CD1 C 14.322 0.3 1 611 121 125 ILE N N 118.941 0.1 1 612 122 126 ASP H H 8.329 0.02 1 613 122 126 ASP C C 178.187 0.3 1 614 122 126 ASP CA C 57.797 0.3 1 615 122 126 ASP CB C 40.804 0.3 1 616 122 126 ASP N N 118.193 0.1 1 617 123 127 PHE H H 7.461 0.02 1 618 123 127 PHE C C 176.205 0.3 1 619 123 127 PHE CA C 60.987 0.3 1 620 123 127 PHE CB C 38.694 0.3 1 621 123 127 PHE N N 119.563 0.1 1 622 124 128 TYR H H 8.232 0.02 1 623 124 128 TYR C C 180.474 0.3 1 624 124 128 TYR CA C 63.436 0.3 1 625 124 128 TYR CB C 36.887 0.3 1 626 124 128 TYR N N 114.754 0.1 1 627 125 129 ARG H H 8.952 0.02 1 628 125 129 ARG C C 180.541 0.3 1 629 125 129 ARG CA C 60.034 0.3 1 630 125 129 ARG CB C 29.651 0.3 1 631 125 129 ARG CG C 27.768 0.3 1 632 125 129 ARG CD C 43.447 0.3 1 633 125 129 ARG N N 121.974 0.1 1 634 126 130 LYS H H 7.576 0.02 1 635 126 130 LYS C C 177.454 0.3 1 636 126 130 LYS CA C 59.017 0.3 1 637 126 130 LYS CB C 31.309 0.3 1 638 126 130 LYS CE C 41.482 0.3 1 639 126 130 LYS N N 120.018 0.1 1 640 127 131 PHE H H 7.560 0.02 1 641 127 131 PHE C C 175.667 0.3 1 642 127 131 PHE CA C 57.747 0.3 1 643 127 131 PHE CB C 39.598 0.3 1 644 127 131 PHE N N 116.053 0.1 1 645 128 132 GLY H H 8.049 0.02 1 646 128 132 GLY C C 174.805 0.3 1 647 128 132 GLY CA C 45.908 0.3 1 648 128 132 GLY N N 106.706 0.1 1 649 129 133 PHE H H 7.670 0.02 1 650 129 133 PHE C C 175.064 0.3 1 651 129 133 PHE CA C 58.139 0.3 1 652 129 133 PHE CB C 39.899 0.3 1 653 129 133 PHE N N 118.105 0.1 1 654 130 134 GLU H H 8.539 0.02 1 655 130 134 GLU C C 175.732 0.3 1 656 130 134 GLU CA C 53.829 0.3 1 657 130 134 GLU CB C 33.268 0.3 1 658 130 134 GLU CG C 35.755 0.3 1 659 130 134 GLU N N 119.214 0.1 1 660 131 135 ILE H H 8.969 0.02 1 661 131 135 ILE C C 177.454 0.3 1 662 131 135 ILE CA C 62.602 0.3 1 663 131 135 ILE CB C 37.963 0.3 1 664 131 135 ILE CG1 C 27.617 0.3 1 665 131 135 ILE CD1 C 17.520 0.3 1 666 131 135 ILE N N 122.959 0.1 1 667 132 136 ILE H H 8.801 0.02 1 668 132 136 ILE C C 175.624 0.3 1 669 132 136 ILE CA C 61.024 0.3 1 670 132 136 ILE CB C 39.394 0.3 1 671 132 136 ILE CG1 C 26.487 0.3 1 672 132 136 ILE CD1 C 18.198 0.3 1 673 132 136 ILE N N 123.527 0.1 1 674 133 137 GLU H H 7.619 0.02 1 675 133 137 GLU C C 174.009 0.3 1 676 133 137 GLU CA C 55.684 0.3 1 677 133 137 GLU CB C 32.816 0.3 1 678 133 137 GLU N N 119.001 0.1 1 679 134 138 THR H H 8.853 0.02 1 680 134 138 THR C C 173.643 0.3 1 681 134 138 THR CA C 62.945 0.3 1 682 134 138 THR CB C 70.666 0.3 1 683 134 138 THR CG2 C 21.287 0.3 1 684 134 138 THR N N 120.41 0.1 1 685 135 139 LYS H H 9.759 0.02 1 686 135 139 LYS C C 175.322 0.3 1 687 135 139 LYS CA C 53.667 0.3 1 688 135 139 LYS CB C 32.967 0.3 1 689 135 139 LYS CE C 41.331 0.3 1 690 135 139 LYS N N 128.504 0.1 1 691 136 140 LYS H H 8.714 0.02 1 692 136 140 LYS C C 178.057 0.3 1 693 136 140 LYS CA C 55.099 0.3 1 694 136 140 LYS CB C 31.837 0.3 1 695 136 140 LYS CG C 24.075 0.3 1 696 136 140 LYS CE C 41.256 0.3 1 697 136 140 LYS N N 125.414 0.1 1 698 137 141 ASN H H 9.534 0.02 1 699 137 141 ASN C C 173.406 0.3 1 700 137 141 ASN CA C 54.564 0.3 1 701 137 141 ASN CB C 36.810 0.3 1 702 137 141 ASN N N 118.777 0.1 1 703 138 142 TYR H H 7.260 0.02 1 704 138 142 TYR C C 176.616 0.3 1 705 138 142 TYR CA C 60.998 0.3 1 706 138 142 TYR CB C 40.420 0.3 1 707 138 142 TYR N N 119.533 0.1 1 708 139 143 TYR H H 8.808 0.02 1 709 139 143 TYR C C 175.795 0.3 1 710 139 143 TYR CA C 57.392 0.3 1 711 139 143 TYR CB C 39.919 0.3 1 712 139 143 TYR N N 117.125 0.1 1 713 141 145 ARG C C 175.435 0.3 1 714 141 145 ARG CA C 57.359 0.3 1 715 141 145 ARG CB C 29.727 0.3 1 716 141 145 ARG CD C 42.922 0.3 1 717 142 146 ILE H H 7.231 0.02 1 718 142 146 ILE C C 173.492 0.3 1 719 142 146 ILE CA C 60.082 0.3 1 720 142 146 ILE CB C 40.653 0.3 1 721 142 146 ILE CG1 C 25.733 0.3 1 722 142 146 ILE CD1 C 17.821 0.3 1 723 142 146 ILE N N 113.641 0.1 1 724 143 147 GLU H H 7.976 0.02 1 725 143 147 GLU C C 174.999 0.3 1 726 143 147 GLU CA C 52.604 0.3 1 727 143 147 GLU CB C 32.414 0.3 1 728 143 147 GLU N N 119.438 0.1 1 729 144 148 PRO C C 176.485 0.3 1 730 144 148 PRO CA C 62.919 0.3 1 731 145 149 ALA H H 8.895 0.02 1 732 145 149 ALA C C 177.562 0.3 1 733 145 149 ALA CA C 52.946 0.3 1 734 145 149 ALA CB C 20.609 0.3 1 735 145 149 ALA N N 123.205 0.1 1 736 146 150 ASP H H 7.219 0.02 1 737 146 150 ASP C C 174.569 0.3 1 738 146 150 ASP CA C 54.528 0.3 1 739 146 150 ASP CB C 41.708 0.3 1 740 146 150 ASP N N 118.768 0.1 1 741 147 151 ALA H H 8.682 0.02 1 742 147 151 ALA C C 177.390 0.3 1 743 147 151 ALA CA C 50.034 0.3 1 744 147 151 ALA CB C 23.925 0.3 1 745 147 151 ALA N N 121.450 0.1 1 746 148 152 HIS H H 9.128 0.02 1 747 148 152 HIS C C 175.732 0.3 1 748 148 152 HIS CA C 54.753 0.3 1 749 148 152 HIS CB C 33.268 0.3 1 750 148 152 HIS N N 119.445 0.1 1 751 149 153 VAL H H 8.879 0.02 1 752 149 153 VAL C C 175.839 0.3 1 753 149 153 VAL CA C 61.547 0.3 1 754 149 153 VAL CB C 31.985 0.3 1 755 149 153 VAL CG1 C 20.911 0.3 2 756 149 153 VAL CG2 C 20.911 0.3 2 757 149 153 VAL N N 121.294 0.1 1 758 150 154 LEU H H 8.792 0.02 1 759 150 154 LEU C C 176.162 0.3 1 760 150 154 LEU CA C 52.679 0.3 1 761 150 154 LEU CB C 43.822 0.3 1 762 150 154 LEU N N 128.089 0.1 1 763 151 155 GLN C C 174.267 0.3 1 764 151 155 GLN CA C 54.538 0.3 1 765 151 155 GLN CB C 35.000 0.3 1 766 152 156 LYS H H 9.083 0.02 1 767 152 156 LYS C C 174.784 0.3 1 768 152 156 LYS CA C 54.134 0.3 1 769 152 156 LYS CB C 33.983 0.3 1 770 152 156 LYS N N 130.567 0.1 1 771 153 157 ASN H H 8.911 0.02 1 772 153 157 ASN C C 175.225 0.3 1 773 153 157 ASN CA C 53.722 0.3 1 774 153 157 ASN CB C 38.560 0.3 1 775 153 157 ASN N N 127.143 0.1 1 776 154 158 LEU H H 8.082 0.02 1 777 154 158 LEU C C 176.851 0.3 1 778 154 158 LEU CA C 54.819 0.3 1 779 154 158 LEU CB C 42.009 0.3 1 780 154 158 LEU CG C 27.165 0.3 1 781 154 158 LEU CD1 C 21.890 0.3 2 782 154 158 LEU CD2 C 20.835 0.3 2 783 154 158 LEU N N 123.228 0.1 1 784 155 159 LYS H H 8.057 0.02 1 785 155 159 LYS C C 175.968 0.3 1 786 155 159 LYS CA C 55.475 0.3 1 787 155 159 LYS CB C 32.967 0.3 1 788 155 159 LYS CG C 24.000 0.3 1 789 155 159 LYS CE C 42.009 0.3 1 790 155 159 LYS N N 120.203 0.1 1 791 156 160 VAL H H 8.049 0.02 1 792 156 160 VAL C C 174.612 0.3 1 793 156 160 VAL CA C 59.745 0.3 1 794 156 160 VAL CB C 32.114 0.3 1 795 156 160 VAL N N 122.325 0.1 1 796 157 161 PRO C C 176.894 0.3 1 797 157 161 PRO CA C 63.350 0.3 1 798 157 161 PRO CB C 32.157 0.3 1 799 157 161 PRO CD C 50.901 0.3 1 800 158 162 SER H H 8.404 0.02 1 801 158 162 SER C C 175.258 0.3 1 802 158 162 SER CA C 58.528 0.3 1 803 158 162 SER CB C 63.846 0.3 1 804 158 162 SER N N 116.381 0.1 1 805 159 163 GLY H H 8.448 0.02 1 806 159 163 GLY C C 173.944 0.3 1 807 159 163 GLY CA C 45.402 0.3 1 808 159 163 GLY N N 111.006 0.1 1 809 160 164 GLN H H 8.168 0.02 1 810 160 164 GLN C C 174.892 0.3 1 811 160 164 GLN CA C 55.723 0.3 1 812 160 164 GLN CB C 29.501 0.3 1 813 160 164 GLN CG C 33.946 0.3 1 814 160 164 GLN N N 119.881 0.1 1 815 161 165 ASN H H 8.051 0.02 1 816 161 165 ASN C C 173.729 0.3 1 817 161 165 ASN CA C 53.301 0.3 1 818 161 165 ASN CB C 38.995 0.3 1 819 161 165 ASN N N 125.425 0.1 1 820 162 166 ALA H H 7.828 0.02 1 821 162 166 ALA C C 182.365 0.3 1 822 162 166 ALA CA C 53.580 0.3 1 823 162 166 ALA CB C 19.804 0.3 1 824 162 166 ALA N N 129.638 0.1 1 stop_ save_