data_25167 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for CS domain of human Shq1 ; _BMRB_accession_number 25167 _BMRB_flat_file_name bmr25167.str _Entry_type original _Submission_date 2014-08-20 _Accession_date 2014-08-20 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone 1H, 13C, and 15N Chemical Shift Assignments for CS domain of human Shq1' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Singh Mahavir . . 2 Wang Zhonghua . . 3 Cascio Duilio . . 4 Feigon Juli . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 86 "13C chemical shifts" 261 "15N chemical shifts" 86 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-10-23 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 19910 'Solution structure of the P22S mutant of N-terminal CS domain of human Shq1' stop_ _Original_release_date 2015-10-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure and interactions of the CS domain of human H/ACA RNP assembly protein Shq1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25553844 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Singh Mahavir . . 2 Wang Zhonghua . . 3 Cascio Duilio . . 4 Feigon Juli . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 427 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 807 _Page_last 823 _Year 2015 _Details . loop_ _Keyword 'Dyskeratosis Congenita' HADDOCK NMR RNP Shq1 stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Human Shq1 CS domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Human Shq1 CS domain' $Human_Shq1_CS_domain stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Assembly factor for H/ACA RNP' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Human_Shq1_CS_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Human_Shq1_CS_domain _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 133 _Mol_residue_sequence ; GSTAIGMKETAAAKFERQHM DSPDLGTGGGSGDDDDKMLT PAFDLSQDPDFLTIAIRVPY ARVSEFDVYFEGSDFKFYAK PYFLRLTLPGRIVENGSEQG SYDADKGIFTIRLPKETPGQ HFEGLNMLTALLA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -36 GLY 2 -35 SER 3 -34 THR 4 -33 ALA 5 -32 ILE 6 -31 GLY 7 -30 MET 8 -29 LYS 9 -28 GLU 10 -27 THR 11 -26 ALA 12 -25 ALA 13 -24 ALA 14 -23 LYS 15 -22 PHE 16 -21 GLU 17 -20 ARG 18 -19 GLN 19 -18 HIS 20 -17 MET 21 -16 ASP 22 -15 SER 23 -14 PRO 24 -13 ASP 25 -12 LEU 26 -11 GLY 27 -10 THR 28 -9 GLY 29 -8 GLY 30 -7 GLY 31 -6 SER 32 -5 GLY 33 -4 ASP 34 -3 ASP 35 -2 ASP 36 -1 ASP 37 0 LYS 38 1 MET 39 2 LEU 40 3 THR 41 4 PRO 42 5 ALA 43 6 PHE 44 7 ASP 45 8 LEU 46 9 SER 47 10 GLN 48 11 ASP 49 12 PRO 50 13 ASP 51 14 PHE 52 15 LEU 53 16 THR 54 17 ILE 55 18 ALA 56 19 ILE 57 20 ARG 58 21 VAL 59 22 PRO 60 23 TYR 61 24 ALA 62 25 ARG 63 26 VAL 64 27 SER 65 28 GLU 66 29 PHE 67 30 ASP 68 31 VAL 69 32 TYR 70 33 PHE 71 34 GLU 72 35 GLY 73 36 SER 74 37 ASP 75 38 PHE 76 39 LYS 77 40 PHE 78 41 TYR 79 42 ALA 80 43 LYS 81 44 PRO 82 45 TYR 83 46 PHE 84 47 LEU 85 48 ARG 86 49 LEU 87 50 THR 88 51 LEU 89 52 PRO 90 53 GLY 91 54 ARG 92 55 ILE 93 56 VAL 94 57 GLU 95 58 ASN 96 59 GLY 97 60 SER 98 61 GLU 99 62 GLN 100 63 GLY 101 64 SER 102 65 TYR 103 66 ASP 104 67 ALA 105 68 ASP 106 69 LYS 107 70 GLY 108 71 ILE 109 72 PHE 110 73 THR 111 74 ILE 112 75 ARG 113 76 LEU 114 77 PRO 115 78 LYS 116 79 GLU 117 80 THR 118 81 PRO 119 82 GLY 120 83 GLN 121 84 HIS 122 85 PHE 123 86 GLU 124 87 GLY 125 88 LEU 126 89 ASN 127 90 MET 128 91 LEU 129 92 THR 130 93 ALA 131 94 LEU 132 95 LEU 133 96 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 19910 P22S_mutant_of_human_Shq1_CS_domain 100.00 133 99.25 99.25 2.34e-89 PDB 2MNW "Solution Structure Of The P22s Mutant Of N-terminal Cs Domain Of Human Shq1" 100.00 133 99.25 99.25 2.34e-89 PDB 4PBD "Crystal Structure Of The N-terminal Cs Domain Of Human Shq1" 75.94 110 98.02 98.02 5.83e-64 PDB 4PCK "Crystal Structure Of The P22s Mutant Of N-terminal Cs Domain Of Human Shq1" 75.94 110 99.01 99.01 4.27e-65 GB AAH17204 "SHQ1 homolog (S. cerevisiae) [Homo sapiens]" 72.18 577 100.00 100.00 5.85e-59 GB AAH17274 "SHQ1 homolog (S. cerevisiae) [Homo sapiens]" 72.18 577 100.00 100.00 5.85e-59 GB AAH25270 "SHQ1 homolog (S. cerevisiae) [Homo sapiens]" 72.18 577 100.00 100.00 5.85e-59 GB AAH32671 "SHQ1 homolog (S. cerevisiae) [Homo sapiens]" 72.18 577 100.00 100.00 5.85e-59 GB AAH39830 "SHQ1 homolog (S. cerevisiae) [Homo sapiens]" 72.18 577 100.00 100.00 5.85e-59 REF NP_060600 "protein SHQ1 homolog [Homo sapiens]" 72.18 577 100.00 100.00 5.85e-59 REF XP_001082636 "PREDICTED: protein SHQ1 homolog isoform 2 [Macaca mulatta]" 72.18 577 100.00 100.00 5.85e-59 REF XP_001141951 "PREDICTED: protein SHQ1 homolog isoform X1 [Pan troglodytes]" 72.18 577 100.00 100.00 7.84e-59 REF XP_001493794 "PREDICTED: protein SHQ1 homolog [Equus caballus]" 72.18 590 97.92 98.96 2.88e-58 REF XP_003132372 "PREDICTED: protein SHQ1 homolog isoform X2 [Sus scrofa]" 72.18 579 97.92 97.92 2.40e-57 SP Q6PI26 "RecName: Full=Protein SHQ1 homolog" 72.18 577 100.00 100.00 5.85e-59 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Human_Shq1_CS_domain 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 $Human_Shq1_CS_domain 'recombinant technology' . Escherichia coli . pET46 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Human_Shq1_CS_domain . mM 0.2 1.0 '[U-100% 15N]' 'sodium phosphate' 20 mM . . 'natural abundance' 'sodium chloride' 100 mM . . 'natural abundance' DTT 2 mM . . 'natural abundance' H2O 93 % . . 'natural abundance' D2O 7 % . . 'natural abundance' 'sodium azide' 0.02 % . . 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Human_Shq1_CS_domain . mM 0.2 1.0 '[U-100% 13C; U-100% 15N]' 'sodium phosphate' 20 mM . . 'natural abundance' 'sodium chloride' 100 mM . . 'natural abundance' DTT 2 mM . . 'natural abundance' H2O 93 % . . 'natural abundance' D2O 7 % . . 'natural abundance' 'sodium azide' 0.02 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version Bruker loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection 'data analysis' processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _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_2 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_2 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_2 save_ save_3D_HCACO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7 . pH pressure 1 . atm temperature 295 . 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 HNCACB' '3D HNCO' '3D HCACO' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Human Shq1 CS domain' _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 40 THR H H 8.879 0.02 1 2 3 40 THR CA C 59.89 0.30 1 3 3 40 THR CB C 69.815 0.30 1 4 3 40 THR N N 120.977 0.30 1 5 4 41 PRO CA C 62.016 0.30 1 6 4 41 PRO CB C 32.099 0.30 1 7 5 42 ALA H H 8.525 0.02 1 8 5 42 ALA C C 176.022 0.30 1 9 5 42 ALA CA C 52.091 0.30 1 10 5 42 ALA CB C 19.196 0.30 1 11 5 42 ALA N N 122.664 0.30 1 12 6 43 PHE H H 7.739 0.02 1 13 6 43 PHE C C 172.576 0.30 1 14 6 43 PHE CA C 55.352 0.30 1 15 6 43 PHE CB C 42.308 0.30 1 16 6 43 PHE N N 115.208 0.30 1 17 7 44 ASP H H 8.917 0.02 1 18 7 44 ASP C C 174.599 0.30 1 19 7 44 ASP CA C 53.367 0.30 1 20 7 44 ASP CB C 45.285 0.30 1 21 7 44 ASP N N 118.886 0.30 1 22 8 45 LEU H H 8.755 0.02 1 23 8 45 LEU C C 175.484 0.30 1 24 8 45 LEU CA C 53.934 0.30 1 25 8 45 LEU CB C 45.852 0.30 1 26 8 45 LEU N N 123.458 0.30 1 27 9 46 SER H H 8.87 0.02 1 28 9 46 SER C C 171.818 0.30 1 29 9 46 SER CA C 57.054 0.30 1 30 9 46 SER CB C 65.419 0.30 1 31 9 46 SER N N 115.906 0.30 1 32 10 47 GLN H H 8.805 0.02 1 33 10 47 GLN C C 172.165 0.30 1 34 10 47 GLN CA C 54.218 0.30 1 35 10 47 GLN CB C 33.092 0.30 1 36 10 47 GLN N N 115.272 0.30 1 37 11 48 ASP H H 8.696 0.02 1 38 11 48 ASP CA C 52.658 0.30 1 39 11 48 ASP CB C 42.166 0.30 1 40 11 48 ASP N N 124.34 0.30 1 41 12 49 PRO C C 175.358 0.30 1 42 13 50 ASP H H 7.997 0.02 1 43 13 50 ASP C C 176.559 0.30 1 44 13 50 ASP CA C 55.069 0.30 1 45 13 50 ASP CB C 44.435 0.30 1 46 13 50 ASP N N 110.553 0.30 1 47 14 51 PHE H H 8.394 0.02 1 48 14 51 PHE C C 174.726 0.30 1 49 14 51 PHE CA C 57.479 0.30 1 50 14 51 PHE CB C 43.017 0.30 1 51 14 51 PHE N N 118.793 0.30 1 52 15 52 LEU H H 9.21 0.02 1 53 15 52 LEU C C 174.785 0.30 1 54 15 52 LEU CA C 53.225 0.30 1 55 15 52 LEU CB C 45.002 0.30 1 56 15 52 LEU N N 123.903 0.30 1 57 16 53 THR H H 9.011 0.02 1 58 16 53 THR C C 172.892 0.30 1 59 16 53 THR CA C 62.725 0.30 1 60 16 53 THR CB C 69.531 0.30 1 61 16 53 THR N N 122.968 0.30 1 62 17 54 ILE H H 8.684 0.02 1 63 17 54 ILE C C 172.671 0.30 1 64 17 54 ILE CA C 60.031 0.30 1 65 17 54 ILE CB C 39.614 0.30 1 66 17 54 ILE N N 126.385 0.30 1 67 18 55 ALA H H 8.5 0.02 1 68 18 55 ALA C C 176.685 0.30 1 69 18 55 ALA CA C 50.106 0.30 1 70 18 55 ALA CB C 20.756 0.30 1 71 18 55 ALA N N 130.208 0.30 1 72 19 56 ILE H H 9.624 0.02 1 73 19 56 ILE C C 174.82 0.30 1 74 19 56 ILE CA C 61.166 0.30 1 75 19 56 ILE CB C 40.606 0.30 1 76 19 56 ILE N N 124.661 0.30 1 77 20 57 ARG H H 8.673 0.02 1 78 20 57 ARG CA C 56.628 0.30 1 79 20 57 ARG CB C 29.547 0.30 1 80 20 57 ARG N N 128.739 0.30 1 81 22 59 PRO C C 177.191 0.30 1 82 22 59 PRO CA C 64.334 0.30 1 83 22 59 PRO CB C 31.264 0.30 1 84 23 60 TYR H H 8.058 0.02 1 85 23 60 TYR C C 175.453 0.30 1 86 23 60 TYR CA C 57.054 0.30 1 87 23 60 TYR CB C 36.636 0.30 1 88 23 60 TYR N N 115.263 0.30 1 89 24 61 ALA H H 7.627 0.02 1 90 24 61 ALA C C 177.349 0.30 1 91 24 61 ALA CA C 52.658 0.30 1 92 24 61 ALA CB C 19.763 0.30 1 93 24 61 ALA N N 121.899 0.30 1 94 25 62 ARG H H 8.719 0.02 1 95 25 62 ARG C C 175.863 0.30 1 96 25 62 ARG CA C 55.307 0.30 1 97 25 62 ARG CB C 30.619 0.30 1 98 25 62 ARG N N 120.767 0.30 1 99 26 63 VAL H H 7.527 0.02 1 100 26 63 VAL C C 175.642 0.30 1 101 26 63 VAL CA C 61.307 0.30 1 102 26 63 VAL CB C 33.375 0.30 1 103 26 63 VAL N N 116.766 0.30 1 104 27 64 SER H H 8.168 0.02 1 105 27 64 SER C C 173.777 0.30 1 106 27 64 SER CA C 58.439 0.30 1 107 27 64 SER CB C 63.307 0.30 1 108 27 64 SER N N 114.802 0.30 1 109 28 65 GLU H H 7.209 0.02 1 110 28 65 GLU C C 174.82 0.30 1 111 28 65 GLU CA C 55.215 0.30 1 112 28 65 GLU CB C 30.711 0.30 1 113 28 65 GLU N N 120.088 0.30 1 114 29 66 PHE H H 7.87 0.02 1 115 29 66 PHE C C 174.694 0.30 1 116 29 66 PHE CA C 55.675 0.30 1 117 29 66 PHE CB C 39.462 0.30 1 118 29 66 PHE N N 121.202 0.30 1 119 30 67 ASP H H 8.324 0.02 1 120 30 67 ASP C C 174.125 0.30 1 121 30 67 ASP CA C 53.741 0.30 1 122 30 67 ASP CB C 43.055 0.30 1 123 30 67 ASP N N 123.966 0.30 1 124 31 68 VAL H H 8.269 0.02 1 125 31 68 VAL C C 174.03 0.30 1 126 31 68 VAL CA C 60.373 0.30 1 127 31 68 VAL CB C 34.857 0.30 1 128 31 68 VAL N N 123.181 0.30 1 129 32 69 TYR H H 8.905 0.02 1 130 32 69 TYR C C 173.087 0.30 1 131 32 69 TYR CA C 56.619 0.30 1 132 32 69 TYR CB C 41.925 0.30 1 133 32 69 TYR N N 127.233 0.30 1 134 33 70 PHE H H 7.547 0.02 1 135 33 70 PHE C C 173.272 0.30 1 136 33 70 PHE CA C 55.307 0.30 1 137 33 70 PHE CB C 40.568 0.30 1 138 33 70 PHE N N 121.252 0.30 1 139 34 71 GLU H H 8.202 0.02 1 140 34 71 GLU C C 175.769 0.30 1 141 34 71 GLU CA C 56.77 0.30 1 142 34 71 GLU CB C 31.248 0.30 1 143 34 71 GLU N N 120.522 0.30 1 144 35 72 GLY H H 9.234 0.02 1 145 35 72 GLY C C 173.208 0.30 1 146 35 72 GLY CA C 47.696 0.30 1 147 35 72 GLY N N 117.27 0.30 1 148 36 73 SER H H 8.925 0.02 1 149 36 73 SER C C 172.766 0.30 1 150 36 73 SER CA C 57.333 0.30 1 151 36 73 SER CB C 64.518 0.30 1 152 36 73 SER N N 122.427 0.30 1 153 37 74 ASP H H 8.592 0.02 1 154 37 74 ASP C C 174.252 0.30 1 155 37 74 ASP CA C 54.643 0.30 1 156 37 74 ASP CB C 43.867 0.30 1 157 37 74 ASP N N 122.998 0.30 1 158 38 75 PHE H H 8.361 0.02 1 159 38 75 PHE C C 172.9 0.30 1 160 38 75 PHE CA C 56.933 0.30 1 161 38 75 PHE CB C 43.013 0.30 1 162 38 75 PHE N N 122.841 0.30 1 163 39 76 LYS H H 8.709 0.02 1 164 39 76 LYS C C 172.639 0.30 1 165 39 76 LYS CA C 54.83 0.30 1 166 39 76 LYS CB C 36.804 0.30 1 167 39 76 LYS N N 126.578 0.30 1 168 40 77 PHE H H 8.523 0.02 1 169 40 77 PHE C C 171.967 0.30 1 170 40 77 PHE CA C 55.932 0.30 1 171 40 77 PHE CB C 43.614 0.30 1 172 40 77 PHE N N 122.47 0.30 1 173 41 78 TYR H H 8.469 0.02 1 174 41 78 TYR C C 173.082 0.30 1 175 41 78 TYR CA C 55.778 0.30 1 176 41 78 TYR CB C 41.599 0.30 1 177 41 78 TYR N N 126.542 0.30 1 178 42 79 ALA H H 7.881 0.02 1 179 42 79 ALA C C 174.22 0.30 1 180 42 79 ALA CA C 51.382 0.30 1 181 42 79 ALA CB C 20.756 0.30 1 182 42 79 ALA N N 128.914 0.30 1 183 43 80 LYS H H 7.93 0.02 1 184 43 80 LYS CA C 56.203 0.30 1 185 43 80 LYS CB C 32.95 0.30 1 186 43 80 LYS N N 124.445 0.30 1 187 44 81 PRO C C 173.967 0.30 1 188 44 81 PRO CA C 64.427 0.30 1 189 44 81 PRO CB C 34.226 0.30 1 190 45 82 TYR H H 9.449 0.02 1 191 45 82 TYR C C 175.295 0.30 1 192 45 82 TYR CA C 58.188 0.30 1 193 45 82 TYR CB C 40.606 0.30 1 194 45 82 TYR N N 126.475 0.30 1 195 46 83 PHE H H 8.799 0.02 1 196 46 83 PHE C C 173.272 0.30 1 197 46 83 PHE CA C 56.628 0.30 1 198 46 83 PHE CB C 44.009 0.30 1 199 46 83 PHE N N 121.113 0.30 1 200 47 84 LEU H H 8.86 0.02 1 201 47 84 LEU C C 171.881 0.30 1 202 47 84 LEU CA C 53.188 0.30 1 203 47 84 LEU CB C 47.569 0.30 1 204 47 84 LEU N N 129.728 0.30 1 205 48 85 ARG H H 8.621 0.02 1 206 48 85 ARG C C 174.157 0.30 1 207 48 85 ARG CA C 54.218 0.30 1 208 48 85 ARG CB C 33.199 0.30 1 209 48 85 ARG N N 127.534 0.30 1 210 49 86 LEU H H 8.999 0.02 1 211 49 86 LEU C C 175.958 0.30 1 212 49 86 LEU CA C 52.912 0.30 1 213 49 86 LEU CB C 47.753 0.30 1 214 49 86 LEU N N 122.864 0.30 1 215 50 87 THR H H 8.671 0.02 1 216 50 87 THR C C 174.631 0.30 1 217 50 87 THR CA C 61.166 0.30 1 218 50 87 THR CB C 69.389 0.30 1 219 50 87 THR N N 118.625 0.30 1 220 51 88 LEU H H 9.547 0.02 1 221 51 88 LEU CA C 52.658 0.30 1 222 51 88 LEU CB C 42.024 0.30 1 223 51 88 LEU N N 126.27 0.30 1 224 52 89 PRO C C 174.346 0.30 1 225 52 89 PRO CA C 62.725 0.30 1 226 52 89 PRO CB C 30.681 0.30 1 227 53 90 GLY H H 6.566 0.02 1 228 53 90 GLY C C 170.585 0.30 1 229 53 90 GLY CA C 43.584 0.30 1 230 53 90 GLY N N 105.96 0.30 1 231 54 91 ARG H H 8.203 0.02 1 232 54 91 ARG C C 176.953 0.30 1 233 54 91 ARG CA C 55.778 0.30 1 234 54 91 ARG CB C 32.241 0.30 1 235 54 91 ARG N N 115.63 0.30 1 236 55 92 ILE H H 8.652 0.02 1 237 55 92 ILE C C 175.358 0.30 1 238 55 92 ILE CA C 58.613 0.30 1 239 55 92 ILE CB C 40.89 0.30 1 240 55 92 ILE N N 118.878 0.30 1 241 56 93 VAL H H 8.354 0.02 1 242 56 93 VAL C C 172.892 0.30 1 243 56 93 VAL CA C 60.465 0.30 1 244 56 93 VAL CB C 35.041 0.30 1 245 56 93 VAL N N 117.973 0.30 1 246 57 94 GLU H H 8.382 0.02 1 247 57 94 GLU C C 176.401 0.30 1 248 57 94 GLU CA C 55.951 0.30 1 249 57 94 GLU CB C 29.974 0.30 1 250 57 94 GLU N N 123.337 0.30 1 251 58 95 ASN H H 8.366 0.02 1 252 58 95 ASN C C 176.18 0.30 1 253 58 95 ASN CA C 52.819 0.30 1 254 58 95 ASN CB C 38.91 0.30 1 255 58 95 ASN N N 121.571 0.30 1 256 59 96 GLY H H 9.375 0.02 1 257 59 96 GLY C C 174.947 0.30 1 258 59 96 GLY CA C 45.542 0.30 1 259 59 96 GLY N N 112.032 0.30 1 260 60 97 SER H H 8.361 0.02 1 261 60 97 SER C C 174.188 0.30 1 262 60 97 SER CA C 58.807 0.30 1 263 60 97 SER CB C 64.15 0.30 1 264 60 97 SER N N 115.392 0.30 1 265 61 98 GLU H H 8.963 0.02 1 266 61 98 GLU C C 175.579 0.30 1 267 61 98 GLU CA C 56.32 0.30 1 268 61 98 GLU CB C 29.606 0.30 1 269 61 98 GLU N N 122.917 0.30 1 270 62 99 GLN H H 8.274 0.02 1 271 62 99 GLN C C 175.705 0.30 1 272 62 99 GLN CA C 55.494 0.30 1 273 62 99 GLN CB C 31.248 0.30 1 274 62 99 GLN N N 120.042 0.30 1 275 63 100 GLY H H 8.911 0.02 1 276 63 100 GLY C C 172.64 0.30 1 277 63 100 GLY CA C 44.713 0.30 1 278 63 100 GLY N N 111.703 0.30 1 279 64 101 SER H H 8.335 0.02 1 280 64 101 SER C C 171.881 0.30 1 281 64 101 SER CA C 57.196 0.30 1 282 64 101 SER CB C 65.277 0.30 1 283 64 101 SER N N 115.147 0.30 1 284 65 102 TYR H H 8.988 0.02 1 285 65 102 TYR C C 173.651 0.30 1 286 65 102 TYR CA C 55.491 0.30 1 287 65 102 TYR CB C 41.028 0.30 1 288 65 102 TYR N N 124.941 0.30 1 289 66 103 ASP H H 8.038 0.02 1 290 66 103 ASP C C 175.389 0.30 1 291 66 103 ASP CA C 51.622 0.30 1 292 66 103 ASP CB C 41.581 0.30 1 293 66 103 ASP N N 128.576 0.30 1 294 67 104 ALA H H 8.471 0.02 1 295 67 104 ALA C C 178.771 0.30 1 296 67 104 ALA CA C 53.934 0.30 1 297 67 104 ALA CB C 18.629 0.30 1 298 67 104 ALA N N 127.546 0.30 1 299 68 105 ASP H H 7.988 0.02 1 300 68 105 ASP C C 177.855 0.30 1 301 68 105 ASP CA C 56.781 0.30 1 302 68 105 ASP CB C 40.844 0.30 1 303 68 105 ASP N N 117.887 0.30 1 304 69 106 LYS H H 7.41 0.02 1 305 69 106 LYS C C 177.159 0.30 1 306 69 106 LYS CA C 56.061 0.30 1 307 69 106 LYS CB C 34.084 0.30 1 308 69 106 LYS N N 115.659 0.30 1 309 70 107 GLY H H 8.055 0.02 1 310 70 107 GLY C C 174.125 0.30 1 311 70 107 GLY CA C 47.108 0.30 1 312 70 107 GLY N N 109.987 0.30 1 313 71 108 ILE H H 7.006 0.02 1 314 71 108 ILE C C 175.263 0.30 1 315 71 108 ILE CA C 59.544 0.30 1 316 71 108 ILE CB C 42.226 0.30 1 317 71 108 ILE N N 116.311 0.30 1 318 72 109 PHE H H 9.592 0.02 1 319 72 109 PHE C C 173.208 0.30 1 320 72 109 PHE CA C 56.061 0.30 1 321 72 109 PHE CB C 42.024 0.30 1 322 72 109 PHE N N 132.401 0.30 1 323 73 110 THR H H 8.603 0.02 1 324 73 110 THR C C 172.576 0.30 1 325 73 110 THR CA C 61.307 0.30 1 326 73 110 THR CB C 69.956 0.30 1 327 73 110 THR N N 124.507 0.30 1 328 74 111 ILE H H 8.833 0.02 1 329 74 111 ILE C C 171.407 0.30 1 330 74 111 ILE CA C 58.897 0.30 1 331 74 111 ILE CB C 41.882 0.30 1 332 74 111 ILE N N 125.415 0.30 1 333 75 112 ARG H H 8.283 0.02 1 334 75 112 ARG C C 174.852 0.30 1 335 75 112 ARG CA C 54.502 0.30 1 336 75 112 ARG CB C 31.532 0.30 1 337 75 112 ARG N N 127.224 0.30 1 338 76 113 LEU H H 9.306 0.02 1 339 76 113 LEU CA C 50.531 0.30 1 340 76 113 LEU CB C 43.159 0.30 1 341 76 113 LEU N N 124.994 0.30 1 342 77 114 PRO C C 176.496 0.30 1 343 77 114 PRO CA C 62.158 0.30 1 344 77 114 PRO CB C 31.248 0.30 1 345 78 115 LYS H H 7.807 0.02 1 346 78 115 LYS C C 176.654 0.30 1 347 78 115 LYS CA C 54.479 0.30 1 348 78 115 LYS CB C 32.808 0.30 1 349 78 115 LYS N N 122.735 0.30 1 350 79 116 GLU H H 8.525 0.02 1 351 79 116 GLU C C 176.338 0.30 1 352 79 116 GLU CA C 59.176 0.30 1 353 79 116 GLU CB C 30.619 0.30 1 354 79 116 GLU N N 124.467 0.30 1 355 80 117 THR H H 9.064 0.02 1 356 80 117 THR CA C 59.039 0.30 1 357 80 117 THR CB C 69.389 0.30 1 358 80 117 THR N N 115.868 0.30 1 359 81 118 PRO C C 177.886 0.30 1 360 81 118 PRO CA C 63.86 0.30 1 361 81 118 PRO CB C 31.674 0.30 1 362 82 119 GLY H H 9.142 0.02 1 363 82 119 GLY C C 174.947 0.30 1 364 82 119 GLY CA C 45.082 0.30 1 365 82 119 GLY N N 113.451 0.30 1 366 83 120 GLN H H 7.963 0.02 1 367 83 120 GLN C C 175.231 0.30 1 368 83 120 GLN CA C 56.412 0.30 1 369 83 120 GLN CB C 29.422 0.30 1 370 83 120 GLN N N 122.713 0.30 1 371 84 121 HIS H H 9.224 0.02 1 372 84 121 HIS C C 175.326 0.30 1 373 84 121 HIS CA C 56.628 0.30 1 374 84 121 HIS CB C 30.965 0.30 1 375 84 121 HIS N N 131.209 0.30 1 376 85 122 PHE H H 9.129 0.02 1 377 85 122 PHE C C 175.01 0.30 1 378 85 122 PHE CA C 54.643 0.30 1 379 85 122 PHE CB C 36.494 0.30 1 380 85 122 PHE N N 130.213 0.30 1 381 86 123 GLU H H 8.911 0.02 1 382 86 123 GLU C C 176.97 0.30 1 383 86 123 GLU CA C 55.919 0.30 1 384 86 123 GLU CB C 30.581 0.30 1 385 86 123 GLU N N 125.926 0.30 1 386 87 124 GLY H H 8.636 0.02 1 387 87 124 GLY C C 177.349 0.30 1 388 87 124 GLY CA C 46.463 0.30 1 389 87 124 GLY N N 108.446 0.30 1 390 88 125 LEU H H 8.38 0.02 1 391 88 125 LEU C C 177.507 0.30 1 392 88 125 LEU CA C 57.61 0.30 1 393 88 125 LEU CB C 40.66 0.30 1 394 88 125 LEU N N 119.716 0.30 1 395 89 126 ASN H H 8.475 0.02 1 396 89 126 ASN C C 175.484 0.30 1 397 89 126 ASN CA C 54.385 0.30 1 398 89 126 ASN CB C 37.16 0.30 1 399 89 126 ASN N N 112.367 0.30 1 400 90 127 MET H H 7.47 0.02 1 401 90 127 MET C C 176.085 0.30 1 402 90 127 MET CA C 54.502 0.30 1 403 90 127 MET CB C 32.808 0.30 1 404 90 127 MET N N 117.461 0.30 1 405 91 128 LEU H H 7.311 0.02 1 406 91 128 LEU C C 176.938 0.30 1 407 91 128 LEU CA C 56.487 0.30 1 408 91 128 LEU CB C 42.502 0.30 1 409 91 128 LEU N N 121.323 0.30 1 410 92 129 THR H H 8.109 0.02 1 411 92 129 THR C C 173.303 0.30 1 412 92 129 THR CA C 60.457 0.30 1 413 92 129 THR CB C 71.233 0.30 1 414 92 129 THR N N 113.828 0.30 1 415 93 130 ALA H H 8.419 0.02 1 416 93 130 ALA C C 177.665 0.30 1 417 93 130 ALA CA C 52.819 0.30 1 418 93 130 ALA CB C 19.749 0.30 1 419 93 130 ALA N N 124.469 0.30 1 420 94 131 LEU H H 8.424 0.02 1 421 94 131 LEU C C 177.412 0.30 1 422 94 131 LEU CA C 55.069 0.30 1 423 94 131 LEU CB C 42.45 0.30 1 424 94 131 LEU N N 122.9 0.30 1 425 95 132 LEU H H 8.365 0.02 1 426 95 132 LEU C C 176.053 0.30 1 427 95 132 LEU CA C 55.03 0.30 1 428 95 132 LEU CB C 42.318 0.30 1 429 95 132 LEU N N 124.419 0.30 1 430 96 133 ALA H H 7.719 0.02 1 431 96 133 ALA CA C 53.651 0.30 1 432 96 133 ALA CB C 20.472 0.30 1 433 96 133 ALA N N 128.754 0.30 1 stop_ save_