data_6116 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C and 15N resonance assignment of the N-terminal domain of human eRF1 ; _BMRB_accession_number 6116 _BMRB_flat_file_name bmr6116.str _Entry_type original _Submission_date 2004-02-26 _Accession_date 2004-03-01 _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 Oda Yoshifumi . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 135 "13C chemical shifts" 273 "15N chemical shifts" 135 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-10-01 original author . stop_ _Original_release_date 2004-10-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone 1H, 13C and 15N resonance assignment of the N-terminal domain of human eRF1' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15452443 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Oda Yoshifumi . . 2 Muramatsu Tomonari . . 3 Yumoto Fumiaki . . 4 Ito Mie . . 5 Tanokura Masaru . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 30 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 109 _Page_last 110 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_system_NeRF1 _Saveframe_category molecular_system _Mol_system_name 'N-terminal domain of human eRF1' _Abbreviation_common NeRF1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'N-terminal domain of human eRF1' $NeRF1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_NeRF1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'N-terminal domain of human eRF1' _Abbreviation_common NeRF1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 142 _Mol_residue_sequence ; MADDPSAADRNVEIWKIKKL IKSLEAARGNGTSMISLIIP PKDQISRVAKMLADEFGTAS NIKSRVNRLSVLGAITSVQQ RLKLYNKVPPNGLVVYCGTI VTEEGKEKKVNIDFEPFKPI NTSLYLCDNKFHTEALTALL SD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ALA 3 3 ASP 4 4 ASP 5 5 PRO 6 6 SER 7 7 ALA 8 8 ALA 9 9 ASP 10 10 ARG 11 11 ASN 12 12 VAL 13 13 GLU 14 14 ILE 15 15 TRP 16 16 LYS 17 17 ILE 18 18 LYS 19 19 LYS 20 20 LEU 21 21 ILE 22 22 LYS 23 23 SER 24 24 LEU 25 25 GLU 26 26 ALA 27 27 ALA 28 28 ARG 29 29 GLY 30 30 ASN 31 31 GLY 32 32 THR 33 33 SER 34 34 MET 35 35 ILE 36 36 SER 37 37 LEU 38 38 ILE 39 39 ILE 40 40 PRO 41 41 PRO 42 42 LYS 43 43 ASP 44 44 GLN 45 45 ILE 46 46 SER 47 47 ARG 48 48 VAL 49 49 ALA 50 50 LYS 51 51 MET 52 52 LEU 53 53 ALA 54 54 ASP 55 55 GLU 56 56 PHE 57 57 GLY 58 58 THR 59 59 ALA 60 60 SER 61 61 ASN 62 62 ILE 63 63 LYS 64 64 SER 65 65 ARG 66 66 VAL 67 67 ASN 68 68 ARG 69 69 LEU 70 70 SER 71 71 VAL 72 72 LEU 73 73 GLY 74 74 ALA 75 75 ILE 76 76 THR 77 77 SER 78 78 VAL 79 79 GLN 80 80 GLN 81 81 ARG 82 82 LEU 83 83 LYS 84 84 LEU 85 85 TYR 86 86 ASN 87 87 LYS 88 88 VAL 89 89 PRO 90 90 PRO 91 91 ASN 92 92 GLY 93 93 LEU 94 94 VAL 95 95 VAL 96 96 TYR 97 97 CYS 98 98 GLY 99 99 THR 100 100 ILE 101 101 VAL 102 102 THR 103 103 GLU 104 104 GLU 105 105 GLY 106 106 LYS 107 107 GLU 108 108 LYS 109 109 LYS 110 110 VAL 111 111 ASN 112 112 ILE 113 113 ASP 114 114 PHE 115 115 GLU 116 116 PRO 117 117 PHE 118 118 LYS 119 119 PRO 120 120 ILE 121 121 ASN 122 122 THR 123 123 SER 124 124 LEU 125 125 TYR 126 126 LEU 127 127 CYS 128 128 ASP 129 129 ASN 130 130 LYS 131 131 PHE 132 132 HIS 133 133 THR 134 134 GLU 135 135 ALA 136 136 LEU 137 137 THR 138 138 ALA 139 139 LEU 140 140 LEU 141 141 SER 142 142 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 17822 entity 100.00 144 97.18 97.89 7.87e-96 BMRB 18092 NeRF1 100.00 150 100.00 100.00 9.15e-99 BMRB 19506 eRF1 100.00 445 100.00 100.00 1.81e-95 PDB 1DT9 "The Crystal Structure Of Human Eukaryotic Release Factor Erf1-Mechanism Of Stop Codon Recognition And Peptidyl-Trna Hydrolysis" 100.00 437 100.00 100.00 1.90e-95 PDB 2LGT "Backbone 1h, 13c, And 15n Chemical Shift Assignments For Qfm(Y)f" 100.00 144 97.18 97.89 7.87e-96 PDB 2LLX "Solution Structure Of The N-Terminal Domain Of Human Polypeptide Chain Release Factor Erf1" 100.00 150 100.00 100.00 9.15e-99 PDB 3E1Y "Crystal Structure Of Human Erf1ERF3 COMPLEX" 100.00 451 100.00 100.00 1.69e-95 PDB 3J5Y "Structure Of The Mammalian Ribosomal Pre-termination Complex Associated With Erf1-erf3-gdpnp" 95.77 414 100.00 100.00 1.12e-90 DBJ BAA85489 "eukaryotic polypeptide chain release factor 1 [Oryctolagus cuniculus]" 100.00 437 100.00 100.00 1.90e-95 DBJ BAC33839 "unnamed protein product [Mus musculus]" 100.00 437 100.00 100.00 1.74e-95 DBJ BAE31210 "unnamed protein product [Mus musculus]" 64.79 387 100.00 100.00 4.81e-57 DBJ BAE31619 "unnamed protein product [Mus musculus]" 64.79 387 100.00 100.00 4.81e-57 DBJ BAE37589 "unnamed protein product [Mus musculus]" 100.00 437 100.00 100.00 1.90e-95 EMBL CAA37987 "suppressor [Xenopus laevis]" 100.00 437 100.00 100.00 1.78e-95 EMBL CAA57281 "C11 protein [Homo sapiens]" 100.00 437 100.00 100.00 1.90e-95 EMBL CAA57282 "C11 protein [Mesocricetus auratus]" 100.00 437 100.00 100.00 1.90e-95 EMBL CAA78620 "XLCL1 [Xenopus laevis]" 100.00 437 100.00 100.00 1.78e-95 EMBL CAF90786 "unnamed protein product, partial [Tetraodon nigroviridis]" 100.00 443 100.00 100.00 2.96e-95 GB AAA36665 "TB3-1 [Homo sapiens]" 100.00 428 99.30 99.30 3.65e-94 GB AAB49726 "eukaryotic release factor 1 [Homo sapiens]" 100.00 437 100.00 100.00 1.90e-95 GB AAD43966 "eRF1 [Homo sapiens]" 100.00 437 100.00 100.00 1.90e-95 GB AAH13717 "Eukaryotic translation termination factor 1 [Mus musculus]" 100.00 437 99.30 99.30 1.92e-94 GB AAH14269 "ETF1 protein [Homo sapiens]" 76.76 404 100.00 100.00 8.14e-70 REF NP_001008345 "eukaryotic peptide chain release factor subunit 1 [Rattus norvegicus]" 100.00 437 100.00 100.00 1.90e-95 REF NP_001069722 "eukaryotic peptide chain release factor subunit 1 [Bos taurus]" 100.00 437 100.00 100.00 1.90e-95 REF NP_001076236 "eukaryotic peptide chain release factor subunit 1 [Oryctolagus cuniculus]" 100.00 437 100.00 100.00 1.90e-95 REF NP_001084363 "eukaryotic peptide chain release factor subunit 1 [Xenopus laevis]" 100.00 437 100.00 100.00 1.78e-95 REF NP_001126989 "eukaryotic peptide chain release factor subunit 1 [Pongo abelii]" 100.00 437 100.00 100.00 1.69e-95 SP P35615 "RecName: Full=Eukaryotic peptide chain release factor subunit 1; Short=Eukaryotic release factor 1; Short=eRF1; AltName: Full=O" 100.00 437 100.00 100.00 1.78e-95 SP P62495 "RecName: Full=Eukaryotic peptide chain release factor subunit 1; Short=Eukaryotic release factor 1; Short=eRF1; AltName: Full=P" 100.00 437 100.00 100.00 1.90e-95 SP P62496 "RecName: Full=Eukaryotic peptide chain release factor subunit 1; Short=Eukaryotic release factor 1; Short=Protein Cl1; Short=eR" 100.00 437 100.00 100.00 1.90e-95 SP P62497 "RecName: Full=Eukaryotic peptide chain release factor subunit 1; Short=Eukaryotic release factor 1; Short=eRF1 [Oryctolagus cun" 100.00 437 100.00 100.00 1.90e-95 SP P62498 "RecName: Full=Eukaryotic peptide chain release factor subunit 1; Short=Eukaryotic release factor 1; Short=eRF1 [Xenopus (Silura" 100.00 437 100.00 100.00 1.99e-95 TPG DAA27419 "TPA: eukaryotic peptide chain release factor subunit 1 [Bos taurus]" 100.00 437 100.00 100.00 1.90e-95 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $NeRF1 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 $NeRF1 'recombinant technology' . . . . . 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 $NeRF1 0.5 mM '[U-95% 13C; U-95% 15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY-INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.05 pH temperature 298 1 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'N-terminal domain of human eRF1' _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 MET H H 8.669 0.007 1 2 1 1 MET N N 122.697 0.081 1 3 1 1 MET CA C 55.882 0.066 1 4 1 1 MET CB C 33.275 0.081 1 5 2 2 ALA H H 8.377 0.006 1 6 2 2 ALA N N 124.806 0.05 1 7 2 2 ALA CA C 53.019 0.038 1 8 2 2 ALA CB C 19.598 0.091 1 9 3 3 ASP H H 8.215 0.006 1 10 3 3 ASP N N 119.042 0.054 1 11 3 3 ASP CA C 54.513 0.038 1 12 3 3 ASP CB C 41.491 0.129 1 13 4 4 ASP H H 8.11 0.006 1 14 4 4 ASP N N 121.188 0.039 1 15 4 4 ASP CA C 52.237 0.007 1 16 4 4 ASP CB C 41.665 0 1 17 5 5 PRO CA C 64.037 0.261 1 18 5 5 PRO CB C 32.399 0.062 1 19 6 6 SER H H 8.476 0.013 1 20 6 6 SER N N 115.493 0.272 1 21 6 6 SER CA C 58.992 0.249 1 22 6 6 SER CB C 64.143 0.116 1 23 7 7 ALA H H 8.064 0.076 1 24 7 7 ALA N N 125.933 0.263 1 25 7 7 ALA CA C 53.631 0.079 1 26 7 7 ALA CB C 19.52 0.115 1 27 8 8 ALA H H 8.07 0.01 1 28 8 8 ALA N N 122.217 0.055 1 29 8 8 ALA CA C 53.754 0.101 1 30 8 8 ALA CB C 19.249 0.13 1 31 9 9 ASP H H 8.148 0.013 1 32 9 9 ASP N N 118.935 0.091 1 33 9 9 ASP CA C 55.221 0.079 1 34 9 9 ASP CB C 41.335 0.095 1 35 10 10 ARG H H 8.239 0.01 1 36 10 10 ARG N N 122.033 0.055 1 37 10 10 ARG CA C 57.936 0.065 1 38 10 10 ARG CB C 30.605 0.115 1 39 11 11 ASN H H 8.28 0.01 1 40 11 11 ASN N N 117.947 0.092 1 41 11 11 ASN CA C 55.409 0.083 1 42 11 11 ASN CB C 38.551 0.143 1 43 12 12 VAL H H 7.934 0.008 1 44 12 12 VAL N N 121.555 0.053 1 45 12 12 VAL CA C 65.812 0.128 1 46 12 12 VAL CB C 32.226 0.131 1 47 13 13 GLU H H 7.949 0.014 1 48 13 13 GLU N N 120.008 0.11 1 49 13 13 GLU CA C 58.822 0.051 1 50 13 13 GLU CB C 29.025 0.054 1 51 14 14 ILE H H 7.88 0.007 1 52 14 14 ILE N N 120.384 0.108 1 53 14 14 ILE CA C 65.14 0.105 1 54 14 14 ILE CB C 37.954 0.074 1 55 15 15 TRP H H 7.958 0.009 1 56 15 15 TRP N N 120.646 0.087 1 57 15 15 TRP CA C 60.982 0.076 1 58 15 15 TRP CB C 29.014 0.114 1 59 16 16 LYS H H 8.066 0.01 1 60 16 16 LYS N N 118.704 0.079 1 61 16 16 LYS CA C 60.314 0.123 1 62 16 16 LYS CB C 32.995 0.156 1 63 17 17 ILE H H 7.769 0.012 1 64 17 17 ILE N N 120.554 0.074 1 65 17 17 ILE CA C 63.563 0.087 1 66 17 17 ILE CB C 37.055 0.064 1 67 18 18 LYS H H 8.457 0.008 1 68 18 18 LYS N N 121.268 0.051 1 69 18 18 LYS CA C 61.367 0.092 1 70 18 18 LYS CB C 32.626 0.145 1 71 19 19 LYS H H 7.838 0.01 1 72 19 19 LYS N N 118.673 0.053 1 73 19 19 LYS CA C 59.488 0.003 1 74 19 19 LYS CB C 32.587 0 1 75 20 20 LEU H H 7.773 0.015 1 76 20 20 LEU N N 122.444 0.151 1 77 20 20 LEU CA C 58.214 0.088 1 78 20 20 LEU CB C 42.148 0.037 1 79 21 21 ILE H H 8.656 0.011 1 80 21 21 ILE N N 119.253 0.082 1 81 21 21 ILE CA C 66.502 0.084 1 82 21 21 ILE CB C 38.388 0.091 1 83 22 22 LYS H H 7.556 0.007 1 84 22 22 LYS N N 117.532 0.09 1 85 22 22 LYS CA C 59.153 0.053 1 86 22 22 LYS CB C 32.071 0.074 1 87 23 23 SER H H 7.867 0.007 1 88 23 23 SER N N 114.909 0.102 1 89 23 23 SER CA C 61.313 0.707 1 90 23 23 SER CB C 63.693 0.429 1 91 24 24 LEU H H 8.269 0.005 1 92 24 24 LEU N N 121.607 0.133 1 93 24 24 LEU CA C 57.236 0.036 1 94 24 24 LEU CB C 42.262 0.13 1 95 25 25 GLU H H 8.449 0.009 1 96 25 25 GLU N N 119.923 0.067 1 97 25 25 GLU CA C 59.042 0.095 1 98 25 25 GLU CB C 30.023 0.108 1 99 26 26 ALA H H 7.366 0.006 1 100 26 26 ALA N N 118.488 0.065 1 101 26 26 ALA CA C 52.408 0.057 1 102 26 26 ALA CB C 19.716 0.113 1 103 27 27 ALA H H 7.052 0.009 1 104 27 27 ALA N N 120.979 0.035 1 105 27 27 ALA CA C 52.986 0.085 1 106 27 27 ALA CB C 19.736 0.102 1 107 28 28 ARG H H 8.926 0.014 1 108 28 28 ARG N N 123.754 0.054 1 109 28 28 ARG CA C 54.446 0.048 1 110 28 28 ARG CB C 33.792 0.15 1 111 29 29 GLY H H 8.156 0.01 1 112 29 29 GLY N N 108.904 0.123 1 113 29 29 GLY CA C 44.914 0.054 1 114 30 30 ASN H H 8.598 0.005 1 115 30 30 ASN N N 119.45 0.051 1 116 30 30 ASN CA C 52.228 0.046 1 117 30 30 ASN CB C 38.7 0.078 1 118 31 31 GLY H H 8.243 0.007 1 119 31 31 GLY N N 110.373 0.069 1 120 31 31 GLY CA C 45.544 0.05 1 121 32 32 THR H H 8.171 0.01 1 122 32 32 THR N N 113.611 0.071 1 123 32 32 THR CA C 60.165 0.073 1 124 32 32 THR CB C 68.793 0.023 1 125 33 33 SER H H 7.758 0.008 1 126 33 33 SER N N 114.867 0.058 1 127 33 33 SER CA C 58.183 0.03 1 128 33 33 SER CB C 64.845 0.022 1 129 34 34 MET H H 8.694 0.007 1 130 34 34 MET N N 121.036 0.085 1 131 34 34 MET CA C 55.232 0.073 1 132 34 34 MET CB C 35.074 0.046 1 133 35 35 ILE H H 9.74 0.01 1 134 35 35 ILE N N 126.546 0.07 1 135 35 35 ILE CA C 61.112 0.065 1 136 35 35 ILE CB C 40.521 0.14 1 137 36 36 SER H H 8.564 0.008 1 138 36 36 SER N N 122.039 0.085 1 139 36 36 SER CA C 57.587 0.064 1 140 36 36 SER CB C 65.223 0.063 1 141 37 37 LEU H H 8.841 0.008 1 142 37 37 LEU N N 127.881 0.079 1 143 37 37 LEU CA C 53.681 0.082 1 144 37 37 LEU CB C 45.714 0.14 1 145 38 38 ILE H H 9.287 0.009 1 146 38 38 ILE N N 126.001 0.114 1 147 38 38 ILE CA C 61.137 0.048 1 148 38 38 ILE CB C 40.329 0.234 1 149 39 39 ILE H H 9.3 0.009 1 150 39 39 ILE N N 129.368 0.052 1 151 39 39 ILE CA C 57.786 0.003 1 152 39 39 ILE CB C 40.907 0 1 153 41 41 PRO CA C 64.535 0.1 1 154 41 41 PRO CB C 32.584 0.157 1 155 42 42 LYS H H 8.107 0.012 1 156 42 42 LYS N N 113.004 0.065 1 157 42 42 LYS CA C 57.256 0.055 1 158 42 42 LYS CB C 31.08 0.13 1 159 43 43 ASP H H 7.514 0.008 1 160 43 43 ASP N N 121.23 0.054 1 161 43 43 ASP CA C 53.105 0.029 1 162 43 43 ASP CB C 42.687 0.034 1 163 44 44 GLN H H 9.442 0.007 1 164 44 44 GLN N N 117.141 0.049 1 165 44 44 GLN CA C 54.414 0.019 1 166 44 44 GLN CB C 31.938 0.094 1 167 45 45 ILE H H 8.937 0.006 1 168 45 45 ILE N N 126.5 0.025 1 169 45 45 ILE CA C 63.727 0.035 1 170 45 45 ILE CB C 36.689 0.105 1 171 46 46 SER H H 8.613 0.005 1 172 46 46 SER N N 113.207 0.032 1 173 46 46 SER CA C 61.052 0.089 1 174 46 46 SER CB C 61.887 0.149 1 175 47 47 ARG H H 7.013 0.01 1 176 47 47 ARG N N 124.062 0.081 1 177 47 47 ARG CA C 59.492 0.03 1 178 47 47 ARG CB C 30.508 0.114 1 179 48 48 VAL H H 7.452 0.006 1 180 48 48 VAL N N 121.624 0.079 1 181 48 48 VAL CA C 66.442 0.02 1 182 48 48 VAL CB C 32.01 0.057 1 183 49 49 ALA H H 8.919 0.006 1 184 49 49 ALA N N 121.546 0.045 1 185 49 49 ALA CA C 55.649 0.056 1 186 49 49 ALA CB C 18.299 0.132 1 187 50 50 LYS H H 7.584 0.008 1 188 50 50 LYS N N 120.112 0.06 1 189 50 50 LYS CA C 59.358 0.044 1 190 50 50 LYS CB C 32.356 0.009 1 191 51 51 MET H H 7.817 0.008 1 192 51 51 MET N N 121.403 0.108 1 193 51 51 MET CA C 59.376 0.035 1 194 51 51 MET CB C 31.424 0.106 1 195 52 52 LEU H H 8.4 0.006 1 196 52 52 LEU N N 119.345 0.042 1 197 52 52 LEU CA C 57.801 0.026 1 198 52 52 LEU CB C 42.142 0.1 1 199 53 53 ALA H H 7.891 0.008 1 200 53 53 ALA N N 122.82 0.07 1 201 53 53 ALA CA C 55.26 0.053 1 202 53 53 ALA CB C 18.054 0.105 1 203 54 54 ASP H H 8.396 0.008 1 204 54 54 ASP N N 122.526 0.03 1 205 54 54 ASP CA C 57.593 0.073 1 206 54 54 ASP CB C 39.98 0.091 1 207 55 55 GLU H H 8.445 0.007 1 208 55 55 GLU N N 121.651 0.094 1 209 55 55 GLU CA C 58.981 0.042 1 210 55 55 GLU CB C 29.307 0.098 1 211 56 56 PHE H H 8.881 0.007 1 212 56 56 PHE N N 122.912 0.062 1 213 56 56 PHE CA C 61.982 0.027 1 214 56 56 PHE CB C 39.601 0.166 1 215 57 57 GLY H H 8.158 0.008 1 216 57 57 GLY N N 106.882 0.049 1 217 57 57 GLY CA C 47.576 0.056 1 218 58 58 THR H H 8.182 0.006 1 219 58 58 THR N N 118.584 0.037 1 220 58 58 THR CA C 65.9 0.077 1 221 58 58 THR CB C 68.968 0.135 1 222 59 59 ALA H H 8.585 0.006 1 223 59 59 ALA N N 125.9 0.038 1 224 59 59 ALA CA C 54.298 0.105 1 225 59 59 ALA CB C 18.81 0.103 1 226 60 60 SER H H 7.696 0.01 1 227 60 60 SER N N 112.038 0.042 1 228 60 60 SER CA C 61.59 0.085 1 229 60 60 SER CB C 63.379 0.158 1 230 61 61 ASN H H 7.567 0.008 1 231 61 61 ASN N N 116.78 0.093 1 232 61 61 ASN CA C 53.457 0.028 1 233 61 61 ASN CB C 39.641 0.091 1 234 62 62 ILE H H 7.655 0.009 1 235 62 62 ILE N N 123.469 0.043 1 236 62 62 ILE CA C 63.66 0.043 1 237 62 62 ILE CB C 38.994 0.057 1 238 63 63 LYS H H 8.575 0.007 1 239 63 63 LYS N N 128.254 0.053 1 240 63 63 LYS CA C 59.047 0.037 1 241 63 63 LYS CB C 32.922 0.096 1 242 64 64 SER H H 7.767 0.005 1 243 64 64 SER N N 113.988 0.039 1 244 64 64 SER CA C 57.254 0.023 1 245 64 64 SER CB C 63.539 0.089 1 246 65 65 ARG H H 8.835 0.006 1 247 65 65 ARG N N 131.071 0.076 1 248 65 65 ARG CA C 60.196 0.059 1 249 65 65 ARG CB C 30.571 0.132 1 250 66 66 VAL H H 8.115 0.006 1 251 66 66 VAL N N 116.667 0.062 1 252 66 66 VAL CA C 65.805 0.06 1 253 66 66 VAL CB C 31.978 0.091 1 254 67 67 ASN H H 7.586 0.01 1 255 67 67 ASN N N 119.265 0.111 1 256 67 67 ASN CA C 55.74 0.05 1 257 67 67 ASN CB C 38.636 0.079 1 258 68 68 ARG H H 8.664 0.005 1 259 68 68 ARG N N 121.561 0.069 1 260 68 68 ARG CA C 60.161 0.042 1 261 68 68 ARG CB C 31.032 0.148 1 262 69 69 LEU H H 8.308 0.009 1 263 69 69 LEU N N 116.449 0.095 1 264 69 69 LEU CA C 58.424 0.071 1 265 69 69 LEU CB C 41.342 0.077 1 266 70 70 SER H H 7.835 0.01 1 267 70 70 SER N N 116.221 0.084 1 268 70 70 SER CA C 62.181 0.463 1 269 70 70 SER CB C 63.256 0.053 1 270 71 71 VAL H H 8.159 0.008 1 271 71 71 VAL N N 124.118 0.06 1 272 71 71 VAL CA C 67.177 0.071 1 273 71 71 VAL CB C 32.396 0.101 1 274 72 72 LEU H H 8.565 0.005 1 275 72 72 LEU N N 118.644 0.083 1 276 72 72 LEU CA C 58.645 0.119 1 277 72 72 LEU CB C 41.009 0.09 1 278 73 73 GLY H H 8.218 0.009 1 279 73 73 GLY N N 106.267 0.08 1 280 73 73 GLY CA C 47.426 0.035 1 281 74 74 ALA H H 7.879 0.007 1 282 74 74 ALA N N 126.842 0.042 1 283 74 74 ALA CA C 55.87 0.092 1 284 74 74 ALA CB C 18.42 0.081 1 285 75 75 ILE H H 8.832 0.008 1 286 75 75 ILE N N 119.245 0.074 1 287 75 75 ILE CA C 67.11 0.067 1 288 75 75 ILE CB C 39.147 0.123 1 289 76 76 THR H H 8.533 0.008 1 290 76 76 THR N N 115.449 0.06 1 291 76 76 THR CA C 67.105 0.083 1 292 76 76 THR CB C 69.029 0.125 1 293 77 77 SER H H 7.972 0.007 1 294 77 77 SER N N 118.237 0.09 1 295 77 77 SER CA C 62.983 0.167 1 296 77 77 SER CB C 63.978 0.041 1 297 78 78 VAL H H 8.333 0.009 1 298 78 78 VAL N N 123.984 0.067 1 299 78 78 VAL CA C 67.258 0.103 1 300 78 78 VAL CB C 31.483 0.136 1 301 79 79 GLN H H 8.831 0.006 1 302 79 79 GLN N N 119.157 0.059 1 303 79 79 GLN CA C 59.916 0.036 1 304 79 79 GLN CB C 29.571 0.227 1 305 80 80 GLN H H 8.06 0.006 1 306 80 80 GLN N N 116.479 0.069 1 307 80 80 GLN CA C 58.909 0.021 1 308 80 80 GLN CB C 28.518 0.142 1 309 81 81 ARG H H 7.724 0.008 1 310 81 81 ARG N N 118.742 0.037 1 311 81 81 ARG CA C 57.096 0.055 1 312 81 81 ARG CB C 28.959 0.073 1 313 82 82 LEU H H 8.326 0.011 1 314 82 82 LEU N N 116.944 0.081 1 315 82 82 LEU CA C 57.784 0.143 1 316 82 82 LEU CB C 41.649 0.09 1 317 83 83 LYS H H 7.264 0.009 1 318 83 83 LYS N N 114.707 0.043 1 319 83 83 LYS CA C 58.084 0.128 1 320 83 83 LYS CB C 32.565 0.122 1 321 84 84 LEU H H 7.442 0.008 1 322 84 84 LEU N N 117.436 0.053 1 323 84 84 LEU CA C 55.809 0.089 1 324 84 84 LEU CB C 41.285 0.17 1 325 85 85 TYR H H 7.847 0.008 1 326 85 85 TYR N N 119.259 0.064 1 327 85 85 TYR CA C 58.211 0.076 1 328 85 85 TYR CB C 40.146 0.031 1 329 86 86 ASN H H 8.798 0.008 1 330 86 86 ASN N N 119.103 0.062 1 331 86 86 ASN CA C 54.221 0.043 1 332 86 86 ASN CB C 39.492 0.081 1 333 87 87 LYS H H 7.812 0.009 1 334 87 87 LYS N N 116.038 0.064 1 335 87 87 LYS CA C 54.638 0.043 1 336 87 87 LYS CB C 35.278 0.087 1 337 88 88 VAL H H 8.537 0.007 1 338 88 88 VAL N N 124.9 0.054 1 339 88 88 VAL CA C 62.411 0.048 1 340 88 88 VAL CB C 32.929 0 1 341 90 90 PRO CA C 66.347 0.047 1 342 90 90 PRO CB C 32.416 0.151 1 343 91 91 ASN H H 9.25 0.009 1 344 91 91 ASN N N 112.289 0.03 1 345 91 91 ASN CA C 52.414 0.085 1 346 91 91 ASN CB C 38.041 0.07 1 347 92 92 GLY H H 8.012 0.011 1 348 92 92 GLY N N 108.384 0.087 1 349 92 92 GLY CA C 43.44 0.056 1 350 93 93 LEU H H 8.725 0.007 1 351 93 93 LEU N N 117.097 0.057 1 352 93 93 LEU CA C 54.24 0.09 1 353 93 93 LEU CB C 47.79 0.112 1 354 94 94 VAL H H 8.249 0.009 1 355 94 94 VAL N N 125.788 0.063 1 356 94 94 VAL CA C 60.665 0.038 1 357 94 94 VAL CB C 32.843 0.035 1 358 95 95 VAL H H 8.936 0.009 1 359 95 95 VAL N N 125.089 0.078 1 360 95 95 VAL CA C 60.717 0.092 1 361 95 95 VAL CB C 35.569 0.132 1 362 96 96 TYR H H 8.759 0.012 1 363 96 96 TYR N N 123.484 0.104 1 364 96 96 TYR CA C 56.719 0.053 1 365 96 96 TYR CB C 40.736 0.2 1 366 97 97 CYS H H 8.72 0.009 1 367 97 97 CYS N N 119.402 0.065 1 368 97 97 CYS CA C 56.731 0.044 1 369 97 97 CYS CB C 32.633 0.104 1 370 98 98 GLY H H 9.033 0.012 1 371 98 98 GLY N N 111.937 0.043 1 372 98 98 GLY CA C 46.445 0.064 1 373 99 99 THR H H 8.131 0.009 1 374 99 99 THR N N 118.411 0.056 1 375 99 99 THR CA C 62.345 0.727 1 376 99 99 THR CB C 70.316 0.043 1 377 100 100 ILE H H 9.029 0.007 1 378 100 100 ILE N N 122.267 0.132 1 379 100 100 ILE CA C 59.301 0.065 1 380 100 100 ILE CB C 40.758 0.118 1 381 101 101 VAL H H 8.493 0.006 1 382 101 101 VAL N N 120.533 0.047 1 383 101 101 VAL CA C 61.036 0.078 1 384 101 101 VAL CB C 33.484 0.097 1 385 102 102 THR H H 9.047 0.006 1 386 102 102 THR N N 118.34 0.048 1 387 102 102 THR CA C 61.033 0.041 1 388 102 102 THR CB C 71.77 0.015 1 389 103 103 GLU H H 9.431 0.007 1 390 103 103 GLU N N 121.524 0.035 1 391 103 103 GLU CA C 59.421 0.056 1 392 103 103 GLU CB C 29.369 0.08 1 393 104 104 GLU H H 7.923 0.007 1 394 104 104 GLU N N 115.744 0.055 1 395 104 104 GLU CA C 56.701 0.036 1 396 104 104 GLU CB C 30.14 0.078 1 397 105 105 GLY H H 8.245 0.007 1 398 105 105 GLY N N 108.643 0.043 1 399 105 105 GLY CA C 45.697 0.039 1 400 106 106 LYS H H 7.124 0.007 1 401 106 106 LYS N N 119.175 0.042 1 402 106 106 LYS CA C 54.959 0.033 1 403 106 106 LYS CB C 33.96 0.046 1 404 107 107 GLU H H 8.525 0.005 1 405 107 107 GLU N N 121.265 0.035 1 406 107 107 GLU CA C 55.968 0.085 1 407 107 107 GLU CB C 31.783 0.127 1 408 108 108 LYS H H 9.079 0.008 1 409 108 108 LYS N N 124.487 0.036 1 410 108 108 LYS CA C 55.351 0.061 1 411 108 108 LYS CB C 36.549 0.131 1 412 109 109 LYS H H 8.739 0.005 1 413 109 109 LYS N N 124.965 0.064 1 414 109 109 LYS CA C 56.458 0.054 1 415 109 109 LYS CB C 33.271 0.099 1 416 110 110 VAL H H 9.007 0.007 1 417 110 110 VAL N N 124.553 0.048 1 418 110 110 VAL CA C 61.771 0.074 1 419 110 110 VAL CB C 34.74 0.079 1 420 111 111 ASN H H 8.88 0.009 1 421 111 111 ASN N N 126.028 0.067 1 422 111 111 ASN CA C 53.614 0.028 1 423 111 111 ASN CB C 41.023 0.04 1 424 112 112 ILE H H 9.105 0.008 1 425 112 112 ILE N N 125.561 0.058 1 426 112 112 ILE CA C 60.337 0.106 1 427 112 112 ILE CB C 42.075 0.184 1 428 113 113 ASP H H 8.194 0.008 1 429 113 113 ASP N N 121.914 0.154 1 430 113 113 ASP CA C 52.445 0.084 1 431 113 113 ASP CB C 44.619 0.229 1 432 114 114 PHE H H 8.816 0.008 1 433 114 114 PHE N N 115.616 0.039 1 434 114 114 PHE CA C 57.02 0.062 1 435 114 114 PHE CB C 40.27 0.103 1 436 115 115 GLU H H 8.729 0.005 1 437 115 115 GLU N N 123.831 0.084 1 438 115 115 GLU CA C 52.206 0.025 1 439 115 115 GLU CB C 31.989 0 1 440 116 116 PRO CA C 62.85 0.192 1 441 116 116 PRO CB C 33.198 0.024 1 442 117 117 PHE H H 7.421 0.012 1 443 117 117 PHE N N 114.963 0.104 1 444 117 117 PHE CA C 58.631 0.132 1 445 117 117 PHE CB C 38.648 0.103 1 446 118 118 LYS H H 7.053 0.011 1 447 118 118 LYS N N 119.941 0.145 1 448 118 118 LYS CA C 53.585 0 1 449 118 118 LYS CB C 34.606 0 1 450 119 119 PRO CA C 63.239 0.052 1 451 119 119 PRO CB C 32.325 0.119 1 452 120 120 ILE H H 7.72 0.012 1 453 120 120 ILE N N 121.992 0.069 1 454 120 120 ILE CA C 59.68 0.118 1 455 120 120 ILE CB C 40.641 0.486 1 456 121 121 ASN H H 8.279 0.008 1 457 121 121 ASN N N 121.533 0.107 1 458 121 121 ASN CA C 53.358 0.032 1 459 121 121 ASN CB C 39.493 0.076 1 460 122 122 THR H H 7.117 0.008 1 461 122 122 THR N N 114.774 0.048 1 462 122 122 THR CA C 61.034 0.589 1 463 122 122 THR CB C 70.935 0.015 1 464 123 123 SER H H 7.911 0.007 1 465 123 123 SER N N 115.817 0.064 1 466 123 123 SER CA C 56.74 0.029 1 467 123 123 SER CB C 64.921 0.012 1 468 124 124 LEU H H 8.616 0.009 1 469 124 124 LEU N N 126.507 0.079 1 470 124 124 LEU CA C 55.399 0.095 1 471 124 124 LEU CB C 47.343 0.075 1 472 125 125 TYR H H 8.344 0.007 1 473 125 125 TYR N N 125.787 0.054 1 474 125 125 TYR CA C 58.71 0.049 1 475 125 125 TYR CB C 40.468 0.054 1 476 126 126 LEU H H 8.295 0.009 1 477 126 126 LEU N N 127.854 0.028 1 478 126 126 LEU CA C 54.348 0.096 1 479 126 126 LEU CB C 47.752 0.071 1 480 127 127 CYS H H 8.461 0.006 1 481 127 127 CYS N N 123.885 0.045 1 482 127 127 CYS CA C 57.419 0.059 1 483 127 127 CYS CB C 27.238 0.071 1 484 128 128 ASP H H 9.344 0.01 1 485 128 128 ASP N N 127.392 0.033 1 486 128 128 ASP CA C 52.928 0.038 1 487 128 128 ASP CB C 45.323 0.037 1 488 129 129 ASN H H 9.349 0.01 1 489 129 129 ASN N N 119.092 0.062 1 490 129 129 ASN CA C 53.256 0.081 1 491 129 129 ASN CB C 38.571 0.106 1 492 130 130 LYS H H 7.273 0.008 1 493 130 130 LYS N N 113.481 0.037 1 494 130 130 LYS CA C 54.675 0.048 1 495 130 130 LYS CB C 34.34 0.109 1 496 131 131 PHE H H 9.695 0.047 1 497 131 131 PHE N N 120.991 0.132 1 498 131 131 PHE CA C 57.062 0.156 1 499 131 131 PHE CB C 39.4 0.076 1 500 132 132 HIS H H 9.083 0.01 1 501 132 132 HIS N N 120.678 0.043 1 502 132 132 HIS CA C 56.743 0.097 1 503 132 132 HIS CB C 28.928 0.111 1 504 133 133 THR H H 8.825 0.022 1 505 133 133 THR N N 117.83 0.153 1 506 133 133 THR CA C 62.088 0.1 1 507 133 133 THR CB C 69.252 0.217 1 508 134 134 GLU H H 10.533 0.012 1 509 134 134 GLU N N 128.522 0.046 1 510 134 134 GLU CA C 60.807 0.061 1 511 134 134 GLU CB C 28.077 0.032 1 512 135 135 ALA H H 9.013 0.012 1 513 135 135 ALA N N 121.84 0.051 1 514 135 135 ALA CA C 54.489 0.04 1 515 135 135 ALA CB C 19.116 0.086 1 516 136 136 LEU H H 7.788 0.016 1 517 136 136 LEU N N 115.812 0.099 1 518 136 136 LEU CA C 56.145 0.086 1 519 136 136 LEU CB C 41.98 0.064 1 520 137 137 THR H H 7.985 0.007 1 521 137 137 THR N N 116.004 0.091 1 522 137 137 THR CA C 66.998 0.103 1 523 137 137 THR CB C 68.402 0.657 1 524 138 138 ALA H H 7.963 0.026 1 525 138 138 ALA N N 123.297 0.057 1 526 138 138 ALA CA C 55.048 0.027 1 527 138 138 ALA CB C 18.51 0.108 1 528 139 139 LEU H H 7.584 0.005 1 529 139 139 LEU N N 117.548 0.094 1 530 139 139 LEU CA C 56.804 0.087 1 531 139 139 LEU CB C 42.483 0.137 1 532 140 140 LEU H H 7.574 0.015 1 533 140 140 LEU N N 115.612 0.118 1 534 140 140 LEU CA C 55.731 0.081 1 535 140 140 LEU CB C 42.22 0.069 1 536 141 141 SER H H 7.594 0.009 1 537 141 141 SER N N 114.093 0.082 1 538 141 141 SER CA C 59.697 0.124 1 539 141 141 SER CB C 64.184 0.017 1 540 142 142 ASP H H 8.272 0.007 1 541 142 142 ASP N N 121.741 0.086 1 542 142 142 ASP CA C 54.66 0.038 1 543 142 142 ASP CB C 41.341 0.026 1 stop_ save_