data_15714 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shift assignements for monomeric apoSOD1 - variant D90A ; _BMRB_accession_number 15714 _BMRB_flat_file_name bmr15714.str _Entry_type original _Submission_date 2008-04-03 _Accession_date 2008-04-03 _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 Teilum Kaare . . 2 Akke Mikael . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 146 "13C chemical shifts" 154 "15N chemical shifts" 146 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-11-05 update BMRB 'complete entry citation' 2009-10-01 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15711 'SOD1, wild type' 15712 'SOD1, mutant A4V' 15713 'SOD1, mutant G85R' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19828437 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Teilum Kaare . . 2 Smith Melanie H. . 3 Schulz Eike . . 4 Christensen Lea C. . 5 Solomentsev Gleb . . 6 Oliveberg Mikael . . 7 Akke Mikael . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Journal_volume 106 _Journal_issue 43 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 18273 _Page_last 18278 _Year 2009 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name SOD1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'chain 1, proline cis conformer' $SOD1 'chain 2, proline trans conformer' $SOD1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SOD1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common SOD1 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 153 _Mol_residue_sequence ; ATKAVAVLKGDGPVQGIINF EQKESNGPVKVWGSIKGLTE GLHGFHVHEEEDNTAGCTSA GPHFNPLSRKHGGPKDEERH VGDLGNVTAAKDGVADVSIE DSVISLSGDHAIIGRTLVVH EKADDLGKGGNEESTKTGNA GSRLACGVIGIAQ ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 THR 3 LYS 4 ALA 5 VAL 6 ALA 7 VAL 8 LEU 9 LYS 10 GLY 11 ASP 12 GLY 13 PRO 14 VAL 15 GLN 16 GLY 17 ILE 18 ILE 19 ASN 20 PHE 21 GLU 22 GLN 23 LYS 24 GLU 25 SER 26 ASN 27 GLY 28 PRO 29 VAL 30 LYS 31 VAL 32 TRP 33 GLY 34 SER 35 ILE 36 LYS 37 GLY 38 LEU 39 THR 40 GLU 41 GLY 42 LEU 43 HIS 44 GLY 45 PHE 46 HIS 47 VAL 48 HIS 49 GLU 50 GLU 51 GLU 52 ASP 53 ASN 54 THR 55 ALA 56 GLY 57 CYS 58 THR 59 SER 60 ALA 61 GLY 62 PRO 63 HIS 64 PHE 65 ASN 66 PRO 67 LEU 68 SER 69 ARG 70 LYS 71 HIS 72 GLY 73 GLY 74 PRO 75 LYS 76 ASP 77 GLU 78 GLU 79 ARG 80 HIS 81 VAL 82 GLY 83 ASP 84 LEU 85 GLY 86 ASN 87 VAL 88 THR 89 ALA 90 ALA 91 LYS 92 ASP 93 GLY 94 VAL 95 ALA 96 ASP 97 VAL 98 SER 99 ILE 100 GLU 101 ASP 102 SER 103 VAL 104 ILE 105 SER 106 LEU 107 SER 108 GLY 109 ASP 110 HIS 111 ALA 112 ILE 113 ILE 114 GLY 115 ARG 116 THR 117 LEU 118 VAL 119 VAL 120 HIS 121 GLU 122 LYS 123 ALA 124 ASP 125 ASP 126 LEU 127 GLY 128 LYS 129 GLY 130 GLY 131 ASN 132 GLU 133 GLU 134 SER 135 THR 136 LYS 137 THR 138 GLY 139 ASN 140 ALA 141 GLY 142 SER 143 ARG 144 LEU 145 ALA 146 CYS 147 GLY 148 VAL 149 ILE 150 GLY 151 ILE 152 ALA 153 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-05 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 BMRB 15711 SOD1 100.00 153 99.35 99.35 3.65e-102 BMRB 15712 SOD1 100.00 153 98.69 98.69 1.82e-101 BMRB 15713 SOD1 100.00 153 98.69 98.69 3.14e-101 BMRB 18509 Superoxide_dismutase_C6A-C111S_thermostable_mutant 100.00 153 97.39 98.04 2.20e-99 BMRB 18708 SUPEROXIDE_DISMUTASE_CU-ZN 100.00 153 97.39 98.04 2.20e-99 BMRB 18968 SOD1 100.00 153 99.35 99.35 3.65e-102 BMRB 26570 SOD1 100.00 153 97.39 98.04 2.20e-99 BMRB 4202 "Superoxide Dismutase" 100.00 153 98.04 99.35 2.32e-101 PDB 1BA9 "The Solution Structure Of Reduced Monomeric Superoxide Dismutase, Nmr, 36 Structures" 99.35 153 98.03 99.34 1.23e-100 PDB 1DSW "The Solution Structure Of A Monomeric, Reduced Form Of Human Copper, Zinc Superoxide Dismutase Bearing The Same Charge As The N" 99.35 153 97.37 98.03 5.00e-99 PDB 1KMG "The Solution Structure Of Monomeric Copper-Free Superoxide Dismutase" 100.00 153 98.04 99.35 2.32e-101 PDB 1L3N "The Solution Structure Of Reduced Dimeric Copper Zinc Sod: The Structural Effects Of Dimerization" 100.00 153 97.39 98.04 2.20e-99 PDB 1MFM "Monomeric Human Sod Mutant F50eG51EE133Q AT ATOMIC Resolution" 100.00 153 98.04 99.35 2.32e-101 PDB 1N18 "Thermostable Mutant Of Human Superoxide Dismutase, C6a, C111s" 100.00 154 97.39 98.04 2.18e-99 PDB 1RK7 "Solution Structure Of Apo Cu,Zn Superoxide Dismutase: Role Of Metal Ions In Protein Folding" 100.00 153 98.04 99.35 2.32e-101 PDB 1SOS "Atomic Structures Of Wild-type And Thermostable Mutant Recombinant Human Cu, Zn Superoxide Dismutase" 100.00 154 97.39 98.04 2.28e-99 PDB 2AF2 "Solution Structure Of Disulfide Reduced And Copper Depleted Human Superoxide Dismutase" 100.00 153 97.39 98.04 2.20e-99 PDB 2GBT "C6aC111A CUZN SUPEROXIDE DISMUTASE" 100.00 153 98.04 98.04 9.50e-100 PDB 2LU5 "Structure And Chemical Shifts Of Cu(I),Zn(Ii) Superoxide Dismutase By Solid-State Nmr" 100.00 153 97.39 98.04 2.20e-99 PDB 2XJK "Monomeric Human Cu,Zn Superoxide Dismutase" 100.00 153 99.35 99.35 3.65e-102 PDB 2XJL "Monomeric Human Cu,Zn Superoxide Dismutase Without Cu Ligands" 100.00 153 97.39 97.39 2.35e-99 PDB 4BCY "Monomeric Human Cu,zn Superoxide Dismutase, Mutation H43f" 100.00 153 98.69 98.69 3.87e-101 GB AAA72747 "CuZn superoxide dismutase [synthetic construct]" 100.00 154 97.39 98.04 2.18e-99 GB AAA80237 "HSOD-GlyProGly-A+, partial [synthetic construct]" 100.00 171 97.39 98.04 8.87e-99 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $SOD1 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 $SOD1 'recombinant technology' . Escherichia coli . N/A 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 $SOD1 1 mM '[U-100% 13C; U-100% 15N]' MES 10 mM 'natural abundance' EDTA 1 mM 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _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_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _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' 0.01 . M pH 6.3 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . 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 water H 1 protons ppm 4.773 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' 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 'chain 1, proline cis conformer' _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 1 ALA CA C 51.980 0.030 1 2 2 2 THR H H 8.531 0.001 1 3 2 2 THR CA C 62.551 0.003 1 4 2 2 THR N N 115.934 0.001 1 5 3 3 LYS H H 8.710 0.030 1 6 3 3 LYS CA C 54.986 0.005 1 7 3 3 LYS N N 125.823 0.004 1 8 4 4 ALA H H 9.120 0.001 1 9 4 4 ALA CA C 50.638 0.005 1 10 4 4 ALA N N 122.849 0.025 1 11 5 5 VAL H H 9.451 0.002 1 12 5 5 VAL CA C 60.356 0.003 1 13 5 5 VAL N N 120.799 0.003 1 14 6 6 ALA H H 9.401 0.001 1 15 6 6 ALA CA C 50.941 0.001 1 16 6 6 ALA N N 128.927 0.008 1 17 7 7 VAL H H 9.216 0.002 1 18 7 7 VAL CA C 62.000 0.003 1 19 7 7 VAL N N 125.372 0.009 1 20 8 8 LEU H H 8.771 0.002 1 21 8 8 LEU CA C 54.063 0.030 1 22 8 8 LEU N N 126.369 0.011 1 23 9 9 LYS H H 8.311 0.001 1 24 9 9 LYS CA C 55.302 0.005 1 25 9 9 LYS N N 121.402 0.037 1 26 10 10 GLY H H 8.647 0.002 1 27 10 10 GLY CA C 45.415 0.010 1 28 10 10 GLY N N 112.417 0.029 1 29 11 11 ASP H H 8.751 0.030 1 30 11 11 ASP CA C 54.624 0.005 1 31 11 11 ASP N N 121.170 0.023 1 32 12 12 GLY H H 8.158 0.030 1 33 12 12 GLY CA C 44.448 0.030 1 34 12 12 GLY N N 110.451 0.014 1 35 13 13 PRO CA C 63.423 0.030 1 36 14 14 VAL H H 7.407 0.003 1 37 14 14 VAL CA C 62.971 0.019 1 38 14 14 VAL N N 120.752 0.011 1 39 15 15 GLN H H 7.976 0.003 1 40 15 15 GLN CA C 54.105 0.006 1 41 15 15 GLN N N 123.427 0.015 1 42 16 16 GLY H H 8.268 0.002 1 43 16 16 GLY CA C 46.734 0.001 1 44 16 16 GLY N N 107.652 0.029 1 45 17 17 ILE H H 8.019 0.030 1 46 17 17 ILE CA C 61.268 0.003 1 47 17 17 ILE N N 120.774 0.011 1 48 18 18 ILE H H 8.822 0.001 1 49 18 18 ILE CA C 56.776 0.011 1 50 18 18 ILE N N 126.666 0.014 1 51 19 19 ASN H H 8.768 0.002 1 52 19 19 ASN CA C 52.352 0.004 1 53 19 19 ASN N N 124.415 0.019 1 54 20 20 PHE H H 8.504 0.030 1 55 20 20 PHE CA C 55.237 0.006 1 56 20 20 PHE N N 115.056 0.007 1 57 21 21 GLU H H 9.618 0.002 1 58 21 21 GLU CA C 56.182 0.002 1 59 21 21 GLU N N 122.214 0.009 1 60 22 22 GLN H H 9.170 0.001 1 61 22 22 GLN CA C 54.525 0.002 1 62 22 22 GLN N N 129.770 0.028 1 63 23 23 LYS H H 9.217 0.002 1 64 23 23 LYS CA C 59.688 0.003 1 65 23 23 LYS N N 130.103 0.006 1 66 24 24 GLU H H 8.141 0.030 1 67 24 24 GLU CA C 54.341 0.001 1 68 24 24 GLU N N 115.685 0.023 1 69 25 25 SER H H 8.839 0.002 1 70 25 25 SER CA C 61.115 0.006 1 71 25 25 SER N N 118.360 0.039 1 72 26 26 ASN H H 8.321 0.002 1 73 26 26 ASN CA C 52.927 0.004 1 74 26 26 ASN N N 117.023 0.017 1 75 27 27 GLY H H 7.927 0.002 1 76 27 27 GLY CA C 44.601 0.030 1 77 27 27 GLY N N 108.075 0.029 1 78 29 29 VAL H H 8.974 0.030 1 79 29 29 VAL CA C 61.138 0.030 1 80 29 29 VAL N N 121.516 0.030 1 81 30 30 LYS H H 9.163 0.001 1 82 30 30 LYS CA C 55.829 0.005 1 83 30 30 LYS N N 128.426 0.002 1 84 31 31 VAL H H 9.236 0.004 1 85 31 31 VAL CA C 60.469 0.002 1 86 31 31 VAL N N 126.703 0.026 1 87 32 32 TRP H H 9.024 0.002 1 88 32 32 TRP CA C 56.135 0.006 1 89 32 32 TRP N N 125.559 0.016 1 90 33 33 GLY H H 8.476 0.002 1 91 33 33 GLY CA C 44.748 0.008 1 92 33 33 GLY N N 108.424 0.015 1 93 34 34 SER H H 7.828 0.001 1 94 34 34 SER CA C 57.054 0.001 1 95 34 34 SER N N 114.167 0.013 1 96 35 35 ILE H H 8.670 0.004 1 97 35 35 ILE CA C 60.166 0.001 1 98 35 35 ILE N N 123.498 0.012 1 99 36 36 LYS H H 9.072 0.001 1 100 36 36 LYS CA C 54.536 0.004 1 101 36 36 LYS N N 124.322 0.005 1 102 37 37 GLY H H 8.161 0.030 1 103 37 37 GLY CA C 45.696 0.020 1 104 37 37 GLY N N 105.890 0.009 1 105 38 38 LEU H H 8.428 0.003 1 106 38 38 LEU CA C 53.611 0.003 1 107 38 38 LEU N N 120.903 0.019 1 108 39 39 THR H H 8.158 0.002 1 109 39 39 THR CA C 61.340 0.014 1 110 39 39 THR N N 111.209 0.021 1 111 40 40 GLU H H 8.609 0.152 1 112 40 40 GLU CA C 57.417 0.009 1 113 40 40 GLU N N 124.913 1.891 1 114 41 41 GLY H H 8.749 0.003 1 115 41 41 GLY CA C 43.276 0.005 1 116 41 41 GLY N N 113.480 0.014 1 117 42 42 LEU H H 8.249 0.002 1 118 42 42 LEU CA C 55.086 0.007 1 119 42 42 LEU N N 120.433 0.027 1 120 43 43 HIS H H 8.740 0.003 1 121 43 43 HIS CA C 54.517 0.007 1 122 43 43 HIS N N 116.196 0.035 1 123 44 44 GLY H H 8.688 0.005 1 124 44 44 GLY CA C 46.257 0.047 1 125 44 44 GLY N N 112.498 0.047 1 126 45 45 PHE H H 8.759 0.004 1 127 45 45 PHE CA C 54.936 0.008 1 128 45 45 PHE N N 127.634 0.045 1 129 46 46 HIS H H 8.806 0.002 1 130 46 46 HIS CA C 53.335 0.019 1 131 46 46 HIS N N 121.356 0.006 1 132 47 47 VAL H H 9.069 0.003 1 133 47 47 VAL CA C 61.381 0.030 1 134 47 47 VAL N N 121.864 0.018 1 135 48 48 HIS H H 9.677 0.005 1 136 48 48 HIS CA C 55.620 0.018 1 137 48 48 HIS N N 128.349 0.025 1 138 49 49 GLU H H 8.939 0.004 1 139 49 49 GLU CA C 56.530 0.005 1 140 49 49 GLU N N 123.586 0.072 1 141 50 50 GLU H H 8.727 0.005 1 142 50 50 GLU CA C 56.396 0.007 1 143 50 50 GLU N N 122.336 0.027 1 144 51 51 GLU H H 8.579 0.004 1 145 51 51 GLU CA C 56.671 0.024 1 146 51 51 GLU N N 121.672 0.045 1 147 52 52 ASP H H 8.286 0.005 1 148 52 52 ASP CA C 54.031 0.023 1 149 52 52 ASP N N 120.222 0.031 1 150 53 53 ASN H H 8.469 0.030 1 151 53 53 ASN CA C 53.665 0.006 1 152 53 53 ASN N N 119.460 0.028 1 153 54 54 THR H H 8.236 0.001 1 154 54 54 THR CA C 62.742 0.002 1 155 54 54 THR N N 113.449 0.012 1 156 55 55 ALA H H 8.177 0.001 1 157 55 55 ALA CA C 52.773 0.001 1 158 55 55 ALA N N 125.276 0.014 1 159 56 56 GLY H H 8.167 0.004 1 160 56 56 GLY CA C 45.490 0.001 1 161 56 56 GLY N N 107.445 0.012 1 162 57 57 CYS H H 8.542 0.002 1 163 57 57 CYS CA C 55.835 0.025 1 164 57 57 CYS N N 118.808 0.012 1 165 58 58 THR H H 8.167 0.001 1 166 58 58 THR CA C 62.012 0.019 1 167 58 58 THR N N 114.103 0.006 1 168 59 59 SER H H 8.381 0.002 1 169 59 59 SER CA C 58.516 0.002 1 170 59 59 SER N N 118.184 0.008 1 171 60 60 ALA H H 8.213 0.004 6 172 60 60 ALA CA C 52.411 0.004 6 173 60 60 ALA N N 125.358 0.032 6 174 61 61 GLY H H 8.125 0.002 6 175 61 61 GLY CA C 44.644 0.030 6 176 61 61 GLY N N 107.844 0.016 6 177 62 62 PRO CA C 62.654 0.030 6 178 63 63 HIS H H 8.593 0.012 6 179 63 63 HIS CA C 56.546 0.001 6 180 63 63 HIS N N 122.201 0.023 6 181 64 64 PHE H H 8.516 0.005 6 182 64 64 PHE CA C 55.115 0.305 6 183 64 64 PHE N N 121.926 0.034 6 184 66 66 PRO CA C 63.658 0.030 1 185 67 67 LEU H H 8.080 0.030 1 186 67 67 LEU CA C 55.323 0.003 1 187 67 67 LEU N N 119.625 0.017 1 188 68 68 SER H H 7.916 0.001 1 189 68 68 SER CA C 58.525 0.002 1 190 68 68 SER N N 115.342 0.017 1 191 69 69 ARG H H 8.174 0.004 1 192 69 69 ARG CA C 56.002 0.009 1 193 69 69 ARG N N 122.759 0.018 1 194 70 70 LYS H H 8.294 0.005 1 195 70 70 LYS CA C 56.389 0.030 1 196 70 70 LYS N N 122.217 0.055 1 197 71 71 HIS H H 8.235 0.202 1 198 71 71 HIS CA C 55.697 0.011 1 199 71 71 HIS N N 121.081 0.799 1 200 72 72 GLY H H 8.520 0.007 1 201 72 72 GLY CA C 45.179 0.001 1 202 72 72 GLY N N 110.626 0.023 1 203 73 73 GLY H H 8.303 0.005 1 204 73 73 GLY CA C 44.577 0.030 1 205 73 73 GLY N N 109.185 0.015 1 206 74 74 PRO CA C 63.585 0.030 1 207 75 75 LYS H H 8.479 0.004 1 208 75 75 LYS CA C 56.429 0.022 1 209 75 75 LYS N N 120.470 0.097 1 210 76 76 ASP H H 8.242 0.008 1 211 76 76 ASP CA C 54.922 0.001 1 212 76 76 ASP N N 121.054 0.010 1 213 77 77 GLU H H 8.331 0.001 1 214 77 77 GLU CA C 56.741 0.030 1 215 77 77 GLU N N 120.350 0.027 1 216 78 78 GLU H H 8.261 0.008 1 217 78 78 GLU CA C 56.602 0.020 1 218 78 78 GLU N N 121.371 0.025 1 219 79 79 ARG H H 8.195 0.001 1 220 79 79 ARG CA C 55.996 0.005 1 221 79 79 ARG N N 121.435 0.045 1 222 80 80 HIS H H 8.663 0.002 1 223 80 80 HIS CA C 55.496 0.010 1 224 80 80 HIS N N 120.191 0.053 1 225 81 81 VAL H H 8.139 0.002 1 226 81 81 VAL CA C 62.505 0.015 1 227 81 81 VAL N N 122.156 0.094 1 228 82 82 GLY H H 8.750 0.003 1 229 82 82 GLY CA C 45.106 0.030 1 230 82 82 GLY N N 112.625 0.045 1 231 84 84 LEU CA C 55.562 0.030 1 232 85 85 GLY H H 8.440 0.011 1 233 85 85 GLY CA C 44.706 0.012 1 234 85 85 GLY N N 108.927 0.099 1 235 86 86 ASN H H 8.301 0.002 1 236 86 86 ASN CA C 52.700 0.002 1 237 86 86 ASN N N 116.937 0.063 1 238 87 87 VAL H H 9.026 0.001 1 239 87 87 VAL CA C 59.200 0.001 1 240 87 87 VAL N N 114.986 0.042 1 241 88 88 THR H H 8.670 0.005 1 242 88 88 THR CA C 61.737 0.001 1 243 88 88 THR N N 118.645 0.018 1 244 89 89 ALA H H 9.216 0.004 1 245 89 89 ALA CA C 50.127 0.005 1 246 89 89 ALA N N 129.203 0.020 1 247 90 90 ALA H H 8.052 0.001 1 248 90 90 ALA CA C 51.184 0.007 1 249 90 90 ALA N N 126.935 0.024 1 250 91 91 LYS H H 8.389 0.030 1 251 91 91 LYS CA C 59.314 0.013 1 252 91 91 LYS N N 118.924 0.012 1 253 92 92 ASP H H 7.930 0.004 1 254 92 92 ASP CA C 53.291 0.024 1 255 92 92 ASP N N 115.773 0.017 1 256 93 93 GLY H H 8.347 0.030 1 257 93 93 GLY CA C 46.386 0.030 1 258 93 93 GLY N N 109.910 0.011 1 259 94 94 VAL H H 7.422 0.030 1 260 94 94 VAL CA C 61.511 0.002 1 261 94 94 VAL N N 118.208 0.002 1 262 95 95 ALA H H 9.600 0.001 1 263 95 95 ALA CA C 50.345 0.001 1 264 95 95 ALA N N 131.850 0.013 1 265 96 96 ASP H H 8.675 0.002 1 266 96 96 ASP CA C 54.151 0.001 1 267 96 96 ASP N N 124.955 0.019 1 268 97 97 VAL H H 8.631 0.007 1 269 97 97 VAL CA C 61.873 0.009 1 270 97 97 VAL N N 124.778 0.039 1 271 98 98 SER H H 8.845 0.002 1 272 98 98 SER CA C 58.272 0.019 1 273 98 98 SER N N 123.738 0.012 1 274 99 99 ILE H H 9.405 0.002 1 275 99 99 ILE CA C 60.279 0.005 1 276 99 99 ILE N N 126.337 0.020 1 277 100 100 GLU H H 8.641 0.001 1 278 100 100 GLU CA C 55.692 0.018 1 279 100 100 GLU N N 124.742 0.031 1 280 101 101 ASP H H 9.173 0.002 1 281 101 101 ASP CA C 53.965 0.004 1 282 101 101 ASP N N 126.747 0.019 1 283 102 102 SER H H 8.909 0.005 1 284 102 102 SER CA C 58.592 0.009 1 285 102 102 SER N N 119.343 0.009 1 286 103 103 VAL H H 8.830 0.006 1 287 103 103 VAL CA C 64.130 0.009 1 288 103 103 VAL N N 122.832 0.076 1 289 104 104 ILE H H 7.814 0.006 1 290 104 104 ILE CA C 61.441 0.007 1 291 104 104 ILE N N 113.550 0.042 1 292 105 105 SER H H 7.606 0.003 1 293 105 105 SER CA C 56.197 0.004 1 294 105 105 SER N N 108.679 0.008 1 295 106 106 LEU H H 8.441 0.002 1 296 106 106 LEU CA C 54.570 0.012 1 297 106 106 LEU N N 121.983 0.015 1 298 107 107 SER H H 8.213 0.002 1 299 107 107 SER CA C 57.281 0.001 1 300 107 107 SER N N 112.405 0.005 1 301 108 108 GLY H H 8.613 0.030 1 302 108 108 GLY CA C 44.790 0.001 1 303 108 108 GLY N N 108.551 0.020 1 304 109 109 ASP H H 8.606 0.001 1 305 109 109 ASP CA C 56.478 0.006 1 306 109 109 ASP N N 119.678 0.027 1 307 110 110 HIS H H 8.834 0.003 1 308 110 110 HIS CA C 53.686 0.003 1 309 110 110 HIS N N 116.781 0.016 1 310 111 111 ALA H H 7.078 0.002 1 311 111 111 ALA CA C 52.322 0.002 1 312 111 111 ALA N N 121.262 0.015 1 313 112 112 ILE H H 7.816 0.002 1 314 112 112 ILE CA C 61.847 0.006 1 315 112 112 ILE N N 108.760 0.009 1 316 113 113 ILE H H 6.226 0.001 1 317 113 113 ILE CA C 61.480 0.005 1 318 113 113 ILE N N 118.468 0.030 1 319 114 114 GLY H H 9.227 0.002 1 320 114 114 GLY CA C 45.117 0.008 1 321 114 114 GLY N N 116.895 0.013 1 322 115 115 ARG H H 7.793 0.002 1 323 115 115 ARG CA C 55.566 0.030 1 324 115 115 ARG N N 119.021 0.010 1 325 116 116 THR H H 8.418 0.030 1 326 116 116 THR CA C 62.179 0.001 1 327 116 116 THR N N 113.769 0.030 1 328 117 117 LEU H H 9.189 0.002 1 329 117 117 LEU CA C 53.652 0.001 1 330 117 117 LEU N N 129.501 0.074 1 331 118 118 VAL H H 9.031 0.002 1 332 118 118 VAL CA C 60.509 0.030 1 333 118 118 VAL N N 123.753 0.030 1 334 120 120 HIS H H 9.369 0.006 1 335 120 120 HIS CA C 56.337 0.011 1 336 120 120 HIS N N 128.038 0.004 1 337 121 121 GLU H H 8.845 0.003 1 338 121 121 GLU CA C 59.355 0.030 1 339 121 121 GLU N N 122.465 0.019 1 340 122 122 LYS H H 8.793 0.030 1 341 122 122 LYS CA C 54.950 0.007 1 342 122 122 LYS N N 118.777 0.083 1 343 123 123 ALA H H 8.275 0.001 1 344 123 123 ALA CA C 51.852 0.011 1 345 123 123 ALA N N 124.501 0.021 1 346 124 124 ASP H H 9.156 0.021 1 347 124 124 ASP CA C 54.432 0.009 1 348 124 124 ASP N N 120.848 0.018 1 349 125 125 ASP H H 8.534 0.006 1 350 125 125 ASP CA C 54.032 0.001 1 351 125 125 ASP N N 122.750 0.051 1 352 126 126 LEU H H 8.411 0.004 1 353 126 126 LEU CA C 55.602 0.002 1 354 126 126 LEU N N 122.452 0.006 1 355 127 127 GLY H H 8.506 0.001 1 356 127 127 GLY CA C 45.636 0.004 1 357 127 127 GLY N N 108.860 0.028 1 358 128 128 LYS H H 8.110 0.005 1 359 128 128 LYS CA C 56.331 0.002 1 360 128 128 LYS N N 120.427 0.031 1 361 129 129 GLY H H 8.513 0.001 1 362 129 129 GLY CA C 45.422 0.004 1 363 129 129 GLY N N 109.715 0.017 1 364 130 130 GLY H H 8.327 0.030 1 365 130 130 GLY CA C 45.365 0.001 1 366 130 130 GLY N N 108.761 0.005 1 367 131 131 ASN H H 8.373 0.002 1 368 131 131 ASN CA C 53.275 0.002 1 369 131 131 ASN N N 118.464 0.026 1 370 132 132 GLU H H 8.575 0.002 1 371 132 132 GLU CA C 57.340 0.030 1 372 132 132 GLU N N 120.893 0.008 1 373 133 133 GLU H H 8.447 0.006 1 374 133 133 GLU CA C 57.285 0.007 1 375 133 133 GLU N N 120.993 0.021 1 376 134 134 SER H H 8.295 0.003 1 377 134 134 SER CA C 59.168 0.006 1 378 134 134 SER N N 115.875 0.025 1 379 135 135 THR H H 8.038 0.009 1 380 135 135 THR CA C 62.361 0.002 1 381 135 135 THR N N 114.706 0.072 1 382 136 136 LYS H H 8.192 0.012 1 383 136 136 LYS CA C 56.758 0.003 1 384 136 136 LYS N N 122.749 0.031 1 385 137 137 THR H H 8.081 0.004 1 386 137 137 THR CA C 61.987 0.004 1 387 137 137 THR N N 113.224 0.082 1 388 138 138 GLY H H 8.379 0.006 1 389 138 138 GLY CA C 45.543 0.014 1 390 138 138 GLY N N 111.035 0.025 1 391 139 139 ASN H H 8.314 0.001 1 392 139 139 ASN CA C 53.325 0.011 1 393 139 139 ASN N N 118.490 0.025 1 394 140 140 ALA H H 8.340 0.007 1 395 140 140 ALA CA C 52.877 0.005 1 396 140 140 ALA N N 123.837 0.035 1 397 141 141 GLY H H 8.241 0.030 1 398 141 141 GLY CA C 45.242 0.030 1 399 141 141 GLY N N 106.420 0.028 1 400 142 142 SER H H 8.681 0.030 1 401 142 142 SER CA C 59.111 0.002 1 402 142 142 SER N N 117.205 0.030 1 403 143 143 ARG H H 8.675 0.002 1 404 143 143 ARG CA C 56.343 0.030 1 405 143 143 ARG N N 121.830 0.006 1 406 145 145 ALA CA C 51.539 0.030 1 407 146 146 CYS H H 8.674 0.002 1 408 146 146 CYS CA C 54.926 0.004 1 409 146 146 CYS N N 116.074 0.009 1 410 147 147 GLY H H 8.660 0.002 1 411 147 147 GLY CA C 46.630 0.003 1 412 147 147 GLY N N 110.766 0.032 1 413 148 148 VAL H H 8.788 0.002 1 414 148 148 VAL CA C 62.709 0.002 1 415 148 148 VAL N N 124.543 0.069 1 416 149 149 ILE H H 8.688 0.001 1 417 149 149 ILE CA C 62.294 0.003 1 418 149 149 ILE N N 128.706 0.014 1 419 150 150 GLY H H 8.896 0.001 1 420 150 150 GLY CA C 43.665 0.003 1 421 150 150 GLY N N 117.927 0.005 1 422 151 151 ILE H H 8.553 0.030 1 423 151 151 ILE CA C 61.447 0.003 1 424 151 151 ILE N N 121.167 0.017 1 425 152 152 ALA H H 8.270 0.001 1 426 152 152 ALA CA C 51.134 0.001 1 427 152 152 ALA N N 131.018 0.016 1 428 153 153 GLN H H 8.040 0.001 1 429 153 153 GLN CA C 57.354 0.030 1 430 153 153 GLN N N 124.887 0.015 1 stop_ save_ save_assigned_chem_shift_list_1_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' 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 'chain 2, proline trans conformer' _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 60 60 ALA H H 8.347 0.006 6 2 60 60 ALA CA C 52.624 0.003 6 3 60 60 ALA N N 125.576 0.010 6 4 61 61 GLY H H 8.048 0.003 6 5 61 61 GLY CA C 43.656 0.030 6 6 61 61 GLY N N 107.349 0.035 6 7 62 62 PRO CA C 63.222 0.030 6 8 63 63 HIS H H 8.452 0.042 6 9 63 63 HIS CA C 55.449 0.003 6 10 63 63 HIS N N 118.557 0.031 6 11 64 64 PHE H H 8.151 0.002 6 12 64 64 PHE CA C 57.597 0.002 6 13 64 64 PHE N N 121.825 0.014 6 14 65 65 ASN H H 8.431 0.002 6 15 65 65 ASN CA C 50.444 0.030 6 16 65 65 ASN N N 123.158 0.007 6 stop_ save_