data_11372 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, K138A mutant ; _BMRB_accession_number 11372 _BMRB_flat_file_name bmr11372.str _Entry_type original _Submission_date 2010-09-08 _Accession_date 2010-09-08 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Takahashi M. . . 2 Kuwasako K. . . 3 Abe C. . . 4 Tsuda K. . . 5 Inoue M. . . 6 Terada T. . . 7 Shirouzu M. . . 8 Kobayashi N. . . 9 Kigawa T. . . 10 Taguchi S. . . 11 Guntert P. . . 12 Hayashizaki Y. . . 13 Tanaka A. . . 14 Muto Y. . . 15 Yokoyama S. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 95 "13C chemical shifts" 293 "15N chemical shifts" 95 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-11-30 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 11370 'Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, C terminal truncated' 11371 'Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, D131A mutant' 11373 'Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, T134A mutant' 11374 'Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1 with RNA (CCCCC)' 11375 'Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1 with RNA (UUUUU)' 11376 'Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1' stop_ _Original_release_date 2010-11-30 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18500819 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kuwasako Kanako . . 2 Takahashi Mari . . 3 Tochio Naoya . . 4 Abe Chikage . . 5 Tsuda Kengo . . 6 Inoue Makoto . . 7 Terada Takaho . . 8 Shirouzu Mikako . . 9 Kobayashi Naohiro . . 10 Kigawa Takanori . . 11 Taguchi Seiichi . . 12 Tanaka Akiko . . 13 Hayashizaki Yoshihide . . 14 Guntert Peter . . 15 Muto Yutaka . . 16 Yokoyama Shigeyuki . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 47 _Journal_issue 24 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6437 _Page_last 6450 _Year 2008 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Tia1 protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'RRM domain K138A mutant' $entity_1 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_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'RRM domain K138A mutant' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 103 _Mol_residue_sequence ; GQKKDTSNHFHVFVGDLSPE ITTEDIKAAFAPFGRISDAR VVKDMATGKSAGYGFVSFFN KWDAENAIQQMGGQWLGGRQ IRTNWATRKPPAPKSTYESN TKQ ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 GLN 3 LYS 4 LYS 5 ASP 6 THR 7 SER 8 ASN 9 HIS 10 PHE 11 HIS 12 VAL 13 PHE 14 VAL 15 GLY 16 ASP 17 LEU 18 SER 19 PRO 20 GLU 21 ILE 22 THR 23 THR 24 GLU 25 ASP 26 ILE 27 LYS 28 ALA 29 ALA 30 PHE 31 ALA 32 PRO 33 PHE 34 GLY 35 ARG 36 ILE 37 SER 38 ASP 39 ALA 40 ARG 41 VAL 42 VAL 43 LYS 44 ASP 45 MET 46 ALA 47 THR 48 GLY 49 LYS 50 SER 51 ALA 52 GLY 53 TYR 54 GLY 55 PHE 56 VAL 57 SER 58 PHE 59 PHE 60 ASN 61 LYS 62 TRP 63 ASP 64 ALA 65 GLU 66 ASN 67 ALA 68 ILE 69 GLN 70 GLN 71 MET 72 GLY 73 GLY 74 GLN 75 TRP 76 LEU 77 GLY 78 GLY 79 ARG 80 GLN 81 ILE 82 ARG 83 THR 84 ASN 85 TRP 86 ALA 87 THR 88 ARG 89 LYS 90 PRO 91 PRO 92 ALA 93 PRO 94 LYS 95 SER 96 THR 97 TYR 98 GLU 99 SER 100 ASN 101 THR 102 LYS 103 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-07 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 11370 "RRM domain C terminal truncated" 84.47 87 98.85 98.85 8.50e-56 BMRB 11371 "RRM domain D131A mutant" 100.00 103 98.06 98.06 1.89e-67 BMRB 11373 "RRM domain T134A mutant" 100.00 103 98.06 98.06 8.83e-68 BMRB 11374 "RRM domain" 100.00 115 99.03 99.03 9.05e-69 BMRB 11375 "RRM domain" 100.00 115 99.03 99.03 9.05e-69 BMRB 11376 "RRM domain" 100.00 115 99.03 99.03 9.05e-69 PDB 2DGO "Solution Structure Of The Rna Binding Domain In Cytotoxic Granule-Associated Rna Binding Protein 1" 100.00 115 99.03 99.03 9.05e-69 PDB 2RNE "Solution Structure Of The Second Rna Recognition Motif (Rrm) Of Tia-1" 100.00 115 99.03 99.03 9.05e-69 GB EAW99825 "TIA1 cytotoxic granule-associated RNA binding protein, isoform CRA_c, partial [Homo sapiens]" 99.03 144 99.02 99.02 7.04e-68 REF XP_005430921 "PREDICTED: nucleolysin TIA-1 isoform p40 [Geospiza fortis]" 99.03 367 98.04 99.02 2.52e-64 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 Mouse 10090 Eukaryota Metazoa Mus musculus 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 $entity_1 'cell free synthesis' 'E. coli' Escherichia coli . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; 20mM [U-99% 2H] TRIS, 100mM sodium chloride, 1mM [U-98% 2H] DTT, 0.02% sodium azide, 1mM [U-99% 13C; U-99% 15N] protein, 90% H2O/10% D2O ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1 mM '[U-99% 13C; U-99% 15N]' TRIS 20 mM '[U-99% 2H]' 'sodium chloride' 100 mM 'natural abundance' DTT 1 mM '[U-98% 2H]' 'sodium azide' 0.02 % 'natural abundance' H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_OPAL _Saveframe_category software _Name OPAL _Version . loop_ _Vendor _Address _Electronic_address 'Luginbuhl, Guntert, Billeter and Wuthrich' . . stop_ loop_ _Task refinement 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 0.1 mM pH 7.0 0.05 pH pressure 1 0.001 atm temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_reference_1 _Saveframe_category chemical_shift_reference _Details ; Chemical shift reference of 1H was based on the proton of water (4.784ppm at 298K) and then those of 15N and 13C were calculated based on their gyromagnetic ratios. ; 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 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 . indirect . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_chemical_shift_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $OPAL stop_ loop_ _Experiment_label '3D 1H-15N NOESY' '3D 1H-13C NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $reference_1 _Mol_system_component_name 'RRM domain K138A mutant' _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 2 2 GLN C C 175.975 0.300 1 2 2 2 GLN CA C 55.936 0.300 1 3 2 2 GLN CB C 29.836 0.300 1 4 3 3 LYS H H 8.530 0.030 1 5 3 3 LYS C C 176.437 0.300 1 6 3 3 LYS CA C 56.550 0.300 1 7 3 3 LYS CB C 32.958 0.300 1 8 3 3 LYS N N 123.814 0.300 1 9 4 4 LYS H H 8.454 0.030 1 10 4 4 LYS C C 175.981 0.300 1 11 4 4 LYS CA C 56.410 0.300 1 12 4 4 LYS CB C 33.112 0.300 1 13 4 4 LYS N N 123.650 0.300 1 14 5 5 ASP H H 8.434 0.030 1 15 5 5 ASP C C 176.682 0.300 1 16 5 5 ASP CA C 54.247 0.300 1 17 5 5 ASP CB C 41.248 0.300 1 18 5 5 ASP N N 122.419 0.300 1 19 6 6 THR H H 8.217 0.030 1 20 6 6 THR C C 175.523 0.300 1 21 6 6 THR CA C 61.156 0.300 1 22 6 6 THR CB C 69.037 0.300 1 23 6 6 THR N N 114.831 0.300 1 24 7 7 SER H H 8.305 0.030 1 25 7 7 SER C C 174.470 0.300 1 26 7 7 SER CA C 60.183 0.300 1 27 7 7 SER CB C 63.407 0.300 1 28 7 7 SER N N 118.717 0.300 1 29 8 8 ASN H H 8.245 0.030 1 30 8 8 ASN C C 174.180 0.300 1 31 8 8 ASN CA C 53.069 0.300 1 32 8 8 ASN CB C 38.587 0.300 1 33 8 8 ASN N N 119.485 0.300 1 34 9 9 HIS H H 7.395 0.030 1 35 9 9 HIS C C 172.219 0.300 1 36 9 9 HIS CA C 53.790 0.300 1 37 9 9 HIS CB C 32.129 0.300 1 38 9 9 HIS N N 119.133 0.300 1 39 10 10 PHE H H 8.363 0.030 1 40 10 10 PHE C C 174.969 0.300 1 41 10 10 PHE CA C 58.410 0.300 1 42 10 10 PHE CB C 40.839 0.300 1 43 10 10 PHE N N 117.495 0.300 1 44 11 11 HIS H H 8.851 0.030 1 45 11 11 HIS C C 174.236 0.300 1 46 11 11 HIS CA C 56.550 0.300 1 47 11 11 HIS CB C 33.214 0.300 1 48 11 11 HIS N N 124.302 0.300 1 49 12 12 VAL H H 9.782 0.030 1 50 12 12 VAL C C 175.413 0.300 1 51 12 12 VAL CA C 62.179 0.300 1 52 12 12 VAL CB C 33.852 0.300 1 53 12 12 VAL N N 126.442 0.300 1 54 13 13 PHE H H 9.134 0.030 1 55 13 13 PHE C C 172.764 0.300 1 56 13 13 PHE CA C 57.215 0.300 1 57 13 13 PHE CB C 40.839 0.300 1 58 13 13 PHE N N 128.011 0.300 1 59 14 14 VAL H H 7.794 0.030 1 60 14 14 VAL C C 173.560 0.300 1 61 14 14 VAL CA C 59.620 0.300 1 62 14 14 VAL CB C 32.600 0.300 1 63 14 14 VAL N N 127.019 0.300 1 64 15 15 GLY H H 8.807 0.030 1 65 15 15 GLY C C 172.288 0.300 1 66 15 15 GLY CA C 43.603 0.300 1 67 15 15 GLY N N 111.366 0.300 1 68 16 16 ASP H H 8.404 0.030 1 69 16 16 ASP C C 173.922 0.300 1 70 16 16 ASP CA C 55.373 0.300 1 71 16 16 ASP CB C 38.843 0.300 1 72 16 16 ASP N N 115.476 0.300 1 73 17 17 LEU H H 7.521 0.030 1 74 17 17 LEU C C 178.277 0.300 1 75 17 17 LEU CA C 53.172 0.300 1 76 17 17 LEU CB C 42.886 0.300 1 77 17 17 LEU N N 112.279 0.300 1 78 18 18 SER H H 8.957 0.030 1 79 18 18 SER C C 174.804 0.300 1 80 18 18 SER CA C 57.062 0.300 1 81 18 18 SER CB C 63.407 0.300 1 82 18 18 SER N N 120.996 0.300 1 83 19 19 PRO C C 176.254 0.300 1 84 19 19 PRO CA C 65.557 0.300 1 85 19 19 PRO CB C 31.986 0.300 1 86 20 20 GLU H H 9.033 0.030 1 87 20 20 GLU C C 176.717 0.300 1 88 20 20 GLU CA C 56.776 0.300 1 89 20 20 GLU CB C 28.813 0.300 1 90 20 20 GLU N N 116.102 0.300 1 91 21 21 ILE H H 7.356 0.030 1 92 21 21 ILE C C 177.043 0.300 1 93 21 21 ILE CA C 59.467 0.300 1 94 21 21 ILE CB C 35.005 0.300 1 95 21 21 ILE N N 121.707 0.300 1 96 22 22 THR H H 9.408 0.030 1 97 22 22 THR C C 176.315 0.300 1 98 22 22 THR CA C 60.132 0.300 1 99 22 22 THR CB C 73.128 0.300 1 100 22 22 THR N N 121.202 0.300 1 101 23 23 THR H H 9.026 0.030 1 102 23 23 THR C C 175.349 0.300 1 103 23 23 THR CA C 67.165 0.300 1 104 23 23 THR CB C 69.139 0.300 1 105 23 23 THR N N 118.447 0.300 1 106 24 24 GLU H H 8.405 0.030 1 107 24 24 GLU C C 179.181 0.300 1 108 24 24 GLU CA C 60.388 0.300 1 109 24 24 GLU CB C 28.403 0.300 1 110 24 24 GLU N N 119.878 0.300 1 111 25 25 ASP H H 7.693 0.030 1 112 25 25 ASP C C 179.848 0.300 1 113 25 25 ASP CA C 57.471 0.300 1 114 25 25 ASP CB C 41.607 0.300 1 115 25 25 ASP N N 120.073 0.300 1 116 26 26 ILE H H 7.920 0.030 1 117 26 26 ILE C C 177.447 0.300 1 118 26 26 ILE CA C 64.321 0.300 1 119 26 26 ILE CB C 37.256 0.300 1 120 26 26 ILE N N 118.440 0.300 1 121 27 27 LYS H H 8.249 0.030 1 122 27 27 LYS C C 177.770 0.300 1 123 27 27 LYS CA C 60.951 0.300 1 124 27 27 LYS CB C 32.139 0.300 1 125 27 27 LYS N N 121.674 0.300 1 126 28 28 ALA H H 7.729 0.030 1 127 28 28 ALA C C 180.301 0.300 1 128 28 28 ALA CA C 54.861 0.300 1 129 28 28 ALA CB C 17.963 0.300 1 130 28 28 ALA N N 118.258 0.300 1 131 29 29 ALA H H 7.837 0.030 1 132 29 29 ALA C C 177.796 0.300 1 133 29 29 ALA CA C 53.940 0.300 1 134 29 29 ALA CB C 18.884 0.300 1 135 29 29 ALA N N 118.017 0.300 1 136 30 30 PHE H H 7.957 0.030 1 137 30 30 PHE C C 175.404 0.300 1 138 30 30 PHE CA C 59.518 0.300 1 139 30 30 PHE CB C 40.327 0.300 1 140 30 30 PHE N N 112.023 0.300 1 141 31 31 ALA H H 8.021 0.030 1 142 31 31 ALA C C 176.345 0.300 1 143 31 31 ALA CA C 55.629 0.300 1 144 31 31 ALA CB C 16.633 0.300 1 145 31 31 ALA N N 125.060 0.300 1 146 32 32 PRO C C 177.365 0.300 1 147 32 32 PRO CA C 64.943 0.300 1 148 32 32 PRO CB C 31.269 0.300 1 149 33 33 PHE H H 7.693 0.030 1 150 33 33 PHE C C 174.536 0.300 1 151 33 33 PHE CA C 59.723 0.300 1 152 33 33 PHE CB C 39.048 0.300 1 153 33 33 PHE N N 112.576 0.300 1 154 34 34 GLY H H 7.597 0.030 1 155 34 34 GLY C C 171.620 0.300 1 156 34 34 GLY CA C 44.421 0.300 1 157 34 34 GLY N N 104.613 0.300 1 158 35 35 ARG H H 8.242 0.030 1 159 35 35 ARG C C 176.984 0.300 1 160 35 35 ARG CA C 57.829 0.300 1 161 35 35 ARG CB C 30.911 0.300 1 162 35 35 ARG N N 117.025 0.300 1 163 36 36 ILE H H 8.507 0.030 1 164 36 36 ILE C C 176.745 0.300 1 165 36 36 ILE CA C 60.337 0.300 1 166 36 36 ILE CB C 40.769 0.300 1 167 36 36 ILE N N 128.024 0.300 1 168 37 37 SER H H 8.832 0.030 1 169 37 37 SER C C 174.618 0.300 1 170 37 37 SER CA C 57.880 0.300 1 171 37 37 SER CB C 63.203 0.300 1 172 37 37 SER N N 123.271 0.300 1 173 38 38 ASP H H 7.269 0.030 1 174 38 38 ASP C C 172.768 0.300 1 175 38 38 ASP CA C 53.684 0.300 1 176 38 38 ASP CB C 43.654 0.300 1 177 38 38 ASP N N 119.551 0.300 1 178 39 39 ALA H H 7.958 0.030 1 179 39 39 ALA C C 175.263 0.300 1 180 39 39 ALA CA C 51.790 0.300 1 181 39 39 ALA CB C 22.313 0.300 1 182 39 39 ALA N N 121.461 0.300 1 183 40 40 ARG H H 8.625 0.030 1 184 40 40 ARG C C 174.327 0.300 1 185 40 40 ARG CA C 55.833 0.300 1 186 40 40 ARG CB C 32.907 0.300 1 187 40 40 ARG N N 115.702 0.300 1 188 41 41 VAL H H 7.700 0.030 1 189 41 41 VAL C C 176.148 0.300 1 190 41 41 VAL CA C 63.123 0.300 1 191 41 41 VAL CB C 32.753 0.300 1 192 41 41 VAL N N 123.834 0.300 1 193 42 42 VAL H H 8.433 0.030 1 194 42 42 VAL C C 173.933 0.300 1 195 42 42 VAL CA C 63.816 0.300 1 196 42 42 VAL CB C 30.860 0.300 1 197 42 42 VAL N N 131.459 0.300 1 198 43 43 LYS H H 8.089 0.030 1 199 43 43 LYS C C 176.175 0.300 1 200 43 43 LYS CA C 54.502 0.300 1 201 43 43 LYS CB C 34.544 0.300 1 202 43 43 LYS N N 125.300 0.300 1 203 44 44 ASP H H 8.764 0.030 1 204 44 44 ASP C C 177.426 0.300 1 205 44 44 ASP CA C 53.787 0.300 1 206 44 44 ASP CB C 42.169 0.300 1 207 44 44 ASP N N 123.394 0.300 1 208 45 45 MET H H 8.954 0.030 1 209 45 45 MET C C 177.541 0.300 1 210 45 45 MET CA C 57.215 0.300 1 211 45 45 MET CB C 31.474 0.300 1 212 45 45 MET N N 126.634 0.300 1 213 46 46 ALA H H 8.587 0.030 1 214 46 46 ALA C C 179.599 0.300 1 215 46 46 ALA CA C 54.451 0.300 1 216 46 46 ALA CB C 19.243 0.300 1 217 46 46 ALA N N 120.750 0.300 1 218 47 47 THR H H 7.666 0.030 1 219 47 47 THR C C 176.642 0.300 1 220 47 47 THR CA C 61.514 0.300 1 221 47 47 THR CB C 71.372 0.300 1 222 47 47 THR N N 104.848 0.300 1 223 48 48 GLY H H 8.492 0.030 1 224 48 48 GLY C C 173.560 0.300 1 225 48 48 GLY CA C 45.957 0.300 1 226 48 48 GLY N N 111.246 0.300 1 227 49 49 LYS H H 7.816 0.030 1 228 49 49 LYS C C 175.433 0.300 1 229 49 49 LYS CA C 54.963 0.300 1 230 49 49 LYS CB C 34.084 0.300 1 231 49 49 LYS N N 119.606 0.300 1 232 50 50 SER H H 8.562 0.030 1 233 50 50 SER C C 176.523 0.300 1 234 50 50 SER CA C 58.750 0.300 1 235 50 50 SER CB C 63.714 0.300 1 236 50 50 SER N N 113.778 0.300 1 237 51 51 ALA H H 9.594 0.030 1 238 51 51 ALA C C 178.274 0.300 1 239 51 51 ALA CA C 52.148 0.300 1 240 51 51 ALA CB C 19.294 0.300 1 241 51 51 ALA N N 129.733 0.300 1 242 52 52 GLY H H 9.102 0.030 1 243 52 52 GLY C C 172.724 0.300 1 244 52 52 GLY CA C 45.598 0.300 1 245 52 52 GLY N N 105.938 0.300 1 246 53 53 TYR H H 7.138 0.030 1 247 53 53 TYR C C 172.154 0.300 1 248 53 53 TYR CA C 55.219 0.300 1 249 53 53 TYR CB C 40.327 0.300 1 250 53 53 TYR N N 113.343 0.300 1 251 54 54 GLY H H 8.837 0.030 1 252 54 54 GLY C C 169.416 0.300 1 253 54 54 GLY CA C 45.291 0.300 1 254 54 54 GLY N N 106.266 0.300 1 255 55 55 PHE H H 8.452 0.030 1 256 55 55 PHE C C 174.530 0.300 1 257 55 55 PHE CA C 55.782 0.300 1 258 55 55 PHE CB C 44.268 0.300 1 259 55 55 PHE N N 113.747 0.300 1 260 56 56 VAL H H 8.945 0.030 1 261 56 56 VAL C C 173.750 0.300 1 262 56 56 VAL CA C 61.412 0.300 1 263 56 56 VAL CB C 34.800 0.300 1 264 56 56 VAL N N 119.893 0.300 1 265 57 57 SER H H 8.770 0.030 1 266 57 57 SER C C 172.812 0.300 1 267 57 57 SER CA C 57.471 0.300 1 268 57 57 SER CB C 64.226 0.300 1 269 57 57 SER N N 122.362 0.300 1 270 58 58 PHE H H 9.261 0.030 1 271 58 58 PHE C C 175.787 0.300 1 272 58 58 PHE CA C 57.222 0.300 1 273 58 58 PHE CB C 42.579 0.300 1 274 58 58 PHE N N 122.038 0.300 1 275 59 59 PHE H H 7.709 0.030 1 276 59 59 PHE C C 175.835 0.300 1 277 59 59 PHE CA C 61.360 0.300 1 278 59 59 PHE CB C 40.072 0.300 1 279 59 59 PHE N N 117.919 0.300 1 280 60 60 ASN H H 8.656 0.030 1 281 60 60 ASN C C 174.811 0.300 1 282 60 60 ASN CA C 51.586 0.300 1 283 60 60 ASN CB C 40.634 0.300 1 284 60 60 ASN N N 114.228 0.300 1 285 61 61 LYS H H 8.161 0.030 1 286 61 61 LYS C C 177.112 0.300 1 287 61 61 LYS CA C 60.234 0.300 1 288 61 61 LYS CB C 32.139 0.300 1 289 61 61 LYS N N 126.632 0.300 1 290 62 62 TRP H H 7.570 0.030 1 291 62 62 TRP C C 177.848 0.300 1 292 62 62 TRP CA C 59.518 0.300 1 293 62 62 TRP CB C 27.738 0.300 1 294 62 62 TRP N N 116.602 0.300 1 295 63 63 ASP H H 6.875 0.030 1 296 63 63 ASP C C 176.510 0.300 1 297 63 63 ASP CA C 56.908 0.300 1 298 63 63 ASP CB C 40.685 0.300 1 299 63 63 ASP N N 121.266 0.300 1 300 64 64 ALA H H 6.591 0.030 1 301 64 64 ALA C C 177.950 0.300 1 302 64 64 ALA CA C 54.605 0.300 1 303 64 64 ALA CB C 19.243 0.300 1 304 64 64 ALA N N 119.705 0.300 1 305 65 65 GLU H H 8.304 0.030 1 306 65 65 GLU C C 178.936 0.300 1 307 65 65 GLU CA C 59.927 0.300 1 308 65 65 GLU CB C 30.041 0.300 1 309 65 65 GLU N N 117.151 0.300 1 310 66 66 ASN H H 7.913 0.030 1 311 66 66 ASN C C 176.325 0.300 1 312 66 66 ASN CA C 55.731 0.300 1 313 66 66 ASN CB C 38.127 0.300 1 314 66 66 ASN N N 117.917 0.300 1 315 67 67 ALA H H 7.869 0.030 1 316 67 67 ALA C C 179.373 0.300 1 317 67 67 ALA CA C 55.117 0.300 1 318 67 67 ALA CB C 18.914 0.300 1 319 67 67 ALA N N 121.673 0.300 1 320 68 68 ILE H H 8.081 0.030 1 321 68 68 ILE C C 179.137 0.300 1 322 68 68 ILE CA C 66.324 0.300 1 323 68 68 ILE CB C 38.331 0.300 1 324 68 68 ILE N N 116.555 0.300 1 325 69 69 GLN H H 7.622 0.030 1 326 69 69 GLN C C 178.496 0.300 1 327 69 69 GLN CA C 58.494 0.300 1 328 69 69 GLN CB C 28.608 0.300 1 329 69 69 GLN N N 117.109 0.300 1 330 70 70 GLN H H 8.417 0.030 1 331 70 70 GLN C C 178.298 0.300 1 332 70 70 GLN CA C 57.624 0.300 1 333 70 70 GLN CB C 29.069 0.300 1 334 70 70 GLN N N 114.721 0.300 1 335 71 71 MET H H 7.681 0.030 1 336 71 71 MET C C 177.429 0.300 1 337 71 71 MET CA C 53.786 0.300 1 338 71 71 MET CB C 30.809 0.300 1 339 71 71 MET N N 113.079 0.300 1 340 72 72 GLY H H 7.035 0.030 1 341 72 72 GLY C C 175.540 0.300 1 342 72 72 GLY CA C 48.976 0.300 1 343 72 72 GLY N N 106.980 0.300 1 344 73 73 GLY H H 8.449 0.030 1 345 73 73 GLY C C 174.467 0.300 1 346 73 73 GLY CA C 45.752 0.300 1 347 73 73 GLY N N 115.353 0.300 1 348 74 74 GLN H H 7.608 0.030 1 349 74 74 GLN C C 175.058 0.300 1 350 74 74 GLN CA C 55.354 0.300 1 351 74 74 GLN CB C 28.557 0.300 1 352 74 74 GLN N N 119.054 0.300 1 353 75 75 TRP H H 8.637 0.030 1 354 75 75 TRP C C 176.504 0.300 1 355 75 75 TRP CA C 57.829 0.300 1 356 75 75 TRP CB C 28.761 0.300 1 357 75 75 TRP N N 121.016 0.300 1 358 76 76 LEU H H 8.548 0.030 1 359 76 76 LEU C C 176.622 0.300 1 360 76 76 LEU CA C 54.928 0.300 1 361 76 76 LEU CB C 43.960 0.300 1 362 76 76 LEU N N 125.900 0.300 1 363 77 77 GLY H H 9.311 0.030 1 364 77 77 GLY C C 175.671 0.300 1 365 77 77 GLY CA C 47.287 0.300 1 366 77 77 GLY N N 115.413 0.300 1 367 78 78 GLY H H 8.740 0.030 1 368 78 78 GLY C C 173.694 0.300 1 369 78 78 GLY CA C 46.102 0.300 1 370 78 78 GLY N N 107.905 0.300 1 371 79 79 ARG H H 7.615 0.030 1 372 79 79 ARG C C 173.728 0.300 1 373 79 79 ARG CA C 55.219 0.300 1 374 79 79 ARG CB C 34.135 0.300 1 375 79 79 ARG N N 118.448 0.300 1 376 80 80 GLN H H 7.799 0.030 1 377 80 80 GLN C C 176.113 0.300 1 378 80 80 GLN CA C 55.014 0.300 1 379 80 80 GLN CB C 29.632 0.300 1 380 80 80 GLN N N 121.774 0.300 1 381 81 81 ILE H H 8.146 0.030 1 382 81 81 ILE C C 176.115 0.300 1 383 81 81 ILE CA C 61.002 0.300 1 384 81 81 ILE CB C 39.867 0.300 1 385 81 81 ILE N N 118.036 0.300 1 386 82 82 ARG H H 7.903 0.030 1 387 82 82 ARG C C 175.195 0.300 1 388 82 82 ARG CA C 53.786 0.300 1 389 82 82 ARG CB C 33.367 0.300 1 390 82 82 ARG N N 119.715 0.300 1 391 83 83 THR H H 8.423 0.030 1 392 83 83 THR C C 174.195 0.300 1 393 83 83 THR CA C 58.492 0.300 1 394 83 83 THR CB C 71.321 0.300 1 395 83 83 THR N N 110.630 0.300 1 396 84 84 ASN H H 8.627 0.030 1 397 84 84 ASN C C 174.297 0.300 1 398 84 84 ASN CA C 52.609 0.300 1 399 84 84 ASN CB C 42.221 0.300 1 400 84 84 ASN N N 114.876 0.300 1 401 85 85 TRP H H 8.772 0.030 1 402 85 85 TRP C C 177.313 0.300 1 403 85 85 TRP CA C 58.348 0.300 1 404 85 85 TRP CB C 30.218 0.300 1 405 85 85 TRP N N 121.990 0.300 1 406 86 86 ALA H H 8.922 0.030 1 407 86 86 ALA C C 177.526 0.300 1 408 86 86 ALA CA C 52.558 0.300 1 409 86 86 ALA CB C 19.703 0.300 1 410 86 86 ALA N N 125.745 0.300 1 411 87 87 THR H H 8.584 0.030 1 412 87 87 THR CA C 62.486 0.300 1 413 87 87 THR CB C 69.548 0.300 1 414 87 87 THR N N 114.822 0.300 1 415 88 88 ARG C C 175.151 0.300 1 416 88 88 ARG CA C 55.219 0.300 1 417 88 88 ARG CB C 31.167 0.300 1 418 89 89 LYS H H 8.210 0.030 1 419 89 89 LYS C C 173.759 0.300 1 420 89 89 LYS CA C 54.196 0.300 1 421 89 89 LYS CB C 31.986 0.300 1 422 89 89 LYS N N 123.608 0.300 1 423 91 91 PRO C C 176.058 0.300 1 424 91 91 PRO CA C 62.486 0.300 1 425 91 91 PRO CB C 31.986 0.300 1 426 92 92 ALA H H 8.295 0.030 1 427 92 92 ALA C C 175.584 0.300 1 428 92 92 ALA CA C 50.409 0.300 1 429 92 92 ALA CB C 17.964 0.300 1 430 92 92 ALA N N 125.495 0.300 1 431 93 93 PRO C C 176.866 0.300 1 432 93 93 PRO CA C 62.896 0.300 1 433 93 93 PRO CB C 32.088 0.300 1 434 94 94 LYS H H 8.412 0.030 1 435 94 94 LYS C C 176.708 0.300 1 436 94 94 LYS CA C 56.601 0.300 1 437 94 94 LYS CB C 32.958 0.300 1 438 94 94 LYS N N 121.633 0.300 1 439 95 95 SER H H 8.367 0.030 1 440 95 95 SER C C 174.733 0.300 1 441 95 95 SER CA C 58.492 0.300 1 442 95 95 SER CB C 64.022 0.300 1 443 95 95 SER N N 117.057 0.300 1 444 96 96 THR H H 8.134 0.030 1 445 96 96 THR C C 174.287 0.300 1 446 96 96 THR CA C 62.078 0.300 1 447 96 96 THR CB C 69.870 0.300 1 448 96 96 THR N N 115.608 0.300 1 449 97 97 TYR H H 8.121 0.030 1 450 97 97 TYR C C 175.690 0.300 1 451 97 97 TYR CA C 58.136 0.300 1 452 97 97 TYR CB C 38.740 0.300 1 453 97 97 TYR N N 121.832 0.300 1 454 98 98 GLU H H 8.207 0.030 1 455 98 98 GLU C C 176.095 0.300 1 456 98 98 GLU CA C 56.396 0.300 1 457 98 98 GLU CB C 30.450 0.300 1 458 98 98 GLU N N 122.648 0.300 1 459 99 99 SER H H 8.273 0.030 1 460 99 99 SER C C 174.394 0.300 1 461 99 99 SER CA C 58.341 0.300 1 462 99 99 SER CB C 63.919 0.300 1 463 99 99 SER N N 116.733 0.300 1 464 100 100 ASN H H 8.475 0.030 1 465 100 100 ASN C C 175.302 0.300 1 466 100 100 ASN CA C 53.377 0.300 1 467 100 100 ASN CB C 38.792 0.300 1 468 100 100 ASN N N 120.893 0.300 1 469 101 101 THR H H 8.058 0.030 1 470 101 101 THR C C 174.298 0.300 1 471 101 101 THR CA C 61.884 0.300 1 472 101 101 THR CB C 69.753 0.300 1 473 101 101 THR N N 114.266 0.300 1 474 102 102 LYS H H 8.274 0.030 1 475 102 102 LYS C C 175.522 0.300 1 476 102 102 LYS CA C 56.447 0.300 1 477 102 102 LYS CB C 32.907 0.300 1 478 102 102 LYS N N 124.389 0.300 1 479 103 103 GLN H H 8.003 0.030 1 480 103 103 GLN C C 180.509 0.300 1 481 103 103 GLN CA C 57.266 0.300 1 482 103 103 GLN CB C 30.348 0.300 1 483 103 103 GLN N N 127.258 0.300 1 stop_ save_