data_11373 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, T134A mutant ; _BMRB_accession_number 11373 _BMRB_flat_file_name bmr11373.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" 292 "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' 11372 'Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, K138A 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 T134A 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 T134A mutant' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 103 _Mol_residue_sequence ; GQKKDTSNHFHVFVGDLSPE ITTEDIKAAFAPFGRISDAR VVKDMAAGKSKGYGFVSFFN 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 ALA 48 GLY 49 LYS 50 SER 51 LYS 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 6.69e-56 BMRB 11371 "RRM domain D131A mutant" 100.00 103 98.06 98.06 1.43e-67 BMRB 11372 "RRM domain K138A mutant" 100.00 103 98.06 98.06 8.83e-68 BMRB 11374 "RRM domain" 100.00 115 99.03 99.03 7.86e-69 BMRB 11375 "RRM domain" 100.00 115 99.03 99.03 7.86e-69 BMRB 11376 "RRM domain" 100.00 115 99.03 99.03 7.86e-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 7.86e-69 PDB 2RNE "Solution Structure Of The Second Rna Recognition Motif (Rrm) Of Tia-1" 100.00 115 99.03 99.03 7.86e-69 GB EAW99825 "TIA1 cytotoxic granule-associated RNA binding protein, isoform CRA_c, partial [Homo sapiens]" 99.03 144 99.02 99.02 5.98e-68 REF XP_005430921 "PREDICTED: nucleolysin TIA-1 isoform p40 [Geospiza fortis]" 99.03 367 98.04 99.02 1.76e-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 T134A 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 175.989 0.300 1 2 2 2 GLN CA C 55.735 0.300 1 3 2 2 GLN CB C 29.743 0.300 1 4 3 3 LYS H H 8.531 0.030 1 5 3 3 LYS C C 176.496 0.300 1 6 3 3 LYS CA C 56.400 0.300 1 7 3 3 LYS CB C 33.305 0.300 1 8 3 3 LYS N N 123.812 0.300 1 9 4 4 LYS H H 8.456 0.030 1 10 4 4 LYS C C 175.979 0.300 1 11 4 4 LYS CA C 56.093 0.300 1 12 4 4 LYS CB C 33.169 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 176.722 0.300 1 16 5 5 ASP CA C 54.094 0.300 1 17 5 5 ASP CB C 41.204 0.300 1 18 5 5 ASP N N 122.424 0.300 1 19 6 6 THR H H 8.218 0.030 1 20 6 6 THR C C 175.545 0.300 1 21 6 6 THR CA C 61.014 0.300 1 22 6 6 THR CB C 69.021 0.300 1 23 6 6 THR N N 114.860 0.300 1 24 7 7 SER H H 8.306 0.030 1 25 7 7 SER C C 174.521 0.300 1 26 7 7 SER CA C 60.194 0.300 1 27 7 7 SER CB C 63.200 0.300 1 28 7 7 SER N N 118.741 0.300 1 29 8 8 ASN H H 8.246 0.030 1 30 8 8 ASN C C 174.160 0.300 1 31 8 8 ASN CA C 52.864 0.300 1 32 8 8 ASN CB C 38.681 0.300 1 33 8 8 ASN N N 119.452 0.300 1 34 9 9 HIS H H 7.390 0.030 1 35 9 9 HIS C C 172.174 0.300 1 36 9 9 HIS CA C 53.684 0.300 1 37 9 9 HIS CB C 32.293 0.300 1 38 9 9 HIS N N 119.165 0.300 1 39 10 10 PHE H H 8.360 0.030 1 40 10 10 PHE C C 175.069 0.300 1 41 10 10 PHE CA C 58.346 0.300 1 42 10 10 PHE CB C 40.844 0.300 1 43 10 10 PHE N N 117.495 0.300 1 44 11 11 HIS H H 8.840 0.030 1 45 11 11 HIS C C 174.293 0.300 1 46 11 11 HIS CA C 56.657 0.300 1 47 11 11 HIS CB C 33.221 0.300 1 48 11 11 HIS N N 124.295 0.300 1 49 12 12 VAL H H 9.762 0.030 1 50 12 12 VAL C C 175.246 0.300 1 51 12 12 VAL CA C 62.040 0.300 1 52 12 12 VAL CB C 33.620 0.300 1 53 12 12 VAL N N 126.434 0.300 1 54 13 13 PHE H H 9.130 0.030 1 55 13 13 PHE C C 172.805 0.300 1 56 13 13 PHE CA C 57.118 0.300 1 57 13 13 PHE CB C 40.895 0.300 1 58 13 13 PHE N N 127.950 0.300 1 59 14 14 VAL H H 7.841 0.030 1 60 14 14 VAL C C 173.613 0.300 1 61 14 14 VAL CA C 59.579 0.300 1 62 14 14 VAL CB C 32.757 0.300 1 63 14 14 VAL N N 126.945 0.300 1 64 15 15 GLY H H 8.792 0.030 1 65 15 15 GLY C C 172.333 0.300 1 66 15 15 GLY CA C 43.688 0.300 1 67 15 15 GLY N N 111.370 0.300 1 68 16 16 ASP H H 8.414 0.030 1 69 16 16 ASP CA C 55.323 0.300 1 70 16 16 ASP CB C 38.986 0.300 1 71 16 16 ASP N N 115.352 0.300 1 72 17 17 LEU C C 178.283 0.300 1 73 17 17 LEU CA C 53.074 0.300 1 74 17 17 LEU CB C 42.796 0.300 1 75 18 18 SER H H 8.891 0.030 1 76 18 18 SER CA C 56.863 0.300 1 77 18 18 SER CB C 63.253 0.300 1 78 18 18 SER N N 120.828 0.300 1 79 19 19 PRO C C 176.304 0.300 1 80 19 19 PRO CA C 65.254 0.300 1 81 19 19 PRO CB C 32.004 0.300 1 82 20 20 GLU H H 8.918 0.030 1 83 20 20 GLU C C 176.742 0.300 1 84 20 20 GLU CA C 56.606 0.300 1 85 20 20 GLU CB C 29.100 0.300 1 86 20 20 GLU N N 116.079 0.300 1 87 21 21 ILE H H 7.329 0.030 1 88 21 21 ILE C C 176.844 0.300 1 89 21 21 ILE CA C 59.425 0.300 1 90 21 21 ILE CB C 35.230 0.300 1 91 21 21 ILE N N 121.623 0.300 1 92 22 22 THR H H 9.331 0.030 1 93 22 22 THR C C 176.269 0.300 1 94 22 22 THR CA C 59.989 0.300 1 95 22 22 THR CB C 73.244 0.300 1 96 22 22 THR N N 120.719 0.300 1 97 23 23 THR H H 8.995 0.030 1 98 23 23 THR C C 175.527 0.300 1 99 23 23 THR CA C 66.602 0.300 1 100 23 23 THR CB C 68.815 0.300 1 101 23 23 THR N N 118.015 0.300 1 102 24 24 GLU H H 8.386 0.030 1 103 24 24 GLU C C 179.171 0.300 1 104 24 24 GLU CA C 60.399 0.300 1 105 24 24 GLU CB C 28.584 0.300 1 106 24 24 GLU N N 119.945 0.300 1 107 25 25 ASP H H 7.699 0.030 1 108 25 25 ASP C C 179.811 0.300 1 109 25 25 ASP CA C 57.323 0.300 1 110 25 25 ASP CB C 41.565 0.300 1 111 25 25 ASP N N 120.098 0.300 1 112 26 26 ILE H H 7.893 0.030 1 113 26 26 ILE C C 177.449 0.300 1 114 26 26 ILE CA C 64.197 0.300 1 115 26 26 ILE CB C 37.092 0.300 1 116 26 26 ILE N N 118.622 0.300 1 117 27 27 LYS H H 8.271 0.030 1 118 27 27 LYS C C 177.799 0.300 1 119 27 27 LYS CA C 60.809 0.300 1 120 27 27 LYS CB C 32.087 0.300 1 121 27 27 LYS N N 121.572 0.300 1 122 28 28 ALA H H 7.752 0.030 1 123 28 28 ALA C C 180.294 0.300 1 124 28 28 ALA CA C 54.863 0.300 1 125 28 28 ALA CB C 17.922 0.300 1 126 28 28 ALA N N 118.316 0.300 1 127 29 29 ALA H H 7.804 0.030 1 128 29 29 ALA C C 177.787 0.300 1 129 29 29 ALA CA C 53.735 0.300 1 130 29 29 ALA CB C 19.106 0.300 1 131 29 29 ALA N N 117.989 0.300 1 132 30 30 PHE H H 7.954 0.030 1 133 30 30 PHE C C 175.437 0.300 1 134 30 30 PHE CA C 59.630 0.300 1 135 30 30 PHE CB C 40.432 0.300 1 136 30 30 PHE N N 112.051 0.300 1 137 31 31 ALA H H 8.050 0.030 1 138 31 31 ALA C C 176.366 0.300 1 139 31 31 ALA CA C 55.528 0.300 1 140 31 31 ALA CB C 16.784 0.300 1 141 31 31 ALA N N 125.086 0.300 1 142 32 32 PRO C C 177.365 0.300 1 143 32 32 PRO CA C 64.947 0.300 1 144 32 32 PRO CB C 30.976 0.300 1 145 33 33 PHE H H 7.695 0.030 1 146 33 33 PHE C C 174.556 0.300 1 147 33 33 PHE CA C 59.528 0.300 1 148 33 33 PHE CB C 38.989 0.300 1 149 33 33 PHE N N 112.629 0.300 1 150 34 34 GLY H H 7.598 0.030 1 151 34 34 GLY C C 171.582 0.300 1 152 34 34 GLY CA C 44.456 0.300 1 153 34 34 GLY N N 104.637 0.300 1 154 35 35 ARG H H 8.238 0.030 1 155 35 35 ARG C C 176.974 0.300 1 156 35 35 ARG CA C 57.784 0.300 1 157 35 35 ARG CB C 30.902 0.300 1 158 35 35 ARG N N 117.006 0.300 1 159 36 36 ILE H H 8.504 0.030 1 160 36 36 ILE C C 176.786 0.300 1 161 36 36 ILE CA C 60.297 0.300 1 162 36 36 ILE CB C 40.742 0.300 1 163 36 36 ILE N N 127.962 0.300 1 164 37 37 SER H H 8.846 0.030 1 165 37 37 SER C C 174.673 0.300 1 166 37 37 SER CA C 57.990 0.300 1 167 37 37 SER CB C 63.148 0.300 1 168 37 37 SER N N 123.252 0.300 1 169 38 38 ASP H H 7.271 0.030 1 170 38 38 ASP C C 172.747 0.300 1 171 38 38 ASP CA C 53.581 0.300 1 172 38 38 ASP CB C 43.677 0.300 1 173 38 38 ASP N N 119.582 0.300 1 174 39 39 ALA H H 7.967 0.030 1 175 39 39 ALA C C 175.206 0.300 1 176 39 39 ALA CA C 51.633 0.300 1 177 39 39 ALA CB C 22.507 0.300 1 178 39 39 ALA N N 121.411 0.300 1 179 40 40 ARG H H 8.636 0.030 1 180 40 40 ARG C C 174.275 0.300 1 181 40 40 ARG CA C 55.632 0.300 1 182 40 40 ARG CB C 33.169 0.300 1 183 40 40 ARG N N 116.135 0.300 1 184 41 41 VAL H H 7.724 0.030 1 185 41 41 VAL C C 175.607 0.300 1 186 41 41 VAL CA C 62.552 0.300 1 187 41 41 VAL CB C 33.221 0.300 1 188 41 41 VAL N N 122.860 0.300 1 189 42 42 VAL H H 8.603 0.030 1 190 42 42 VAL C C 174.047 0.300 1 191 42 42 VAL CA C 63.424 0.300 1 192 42 42 VAL CB C 31.160 0.300 1 193 42 42 VAL N N 130.023 0.300 1 194 43 43 LYS H H 8.179 0.030 1 195 43 43 LYS C C 175.881 0.300 1 196 43 43 LYS CA C 54.811 0.300 1 197 43 43 LYS CB C 35.229 0.300 1 198 43 43 LYS N N 125.648 0.300 1 199 44 44 ASP H H 8.657 0.030 1 200 44 44 ASP C C 176.550 0.300 1 201 44 44 ASP CA C 53.632 0.300 1 202 44 44 ASP CB C 41.978 0.300 1 203 44 44 ASP N N 121.889 0.300 1 204 45 45 MET H H 8.683 0.030 1 205 45 45 MET C C 177.178 0.300 1 206 45 45 MET CA C 56.452 0.300 1 207 45 45 MET CB C 31.904 0.300 1 208 45 45 MET N N 123.190 0.300 1 209 46 46 ALA H H 8.306 0.030 1 210 46 46 ALA C C 178.406 0.300 1 211 46 46 ALA CA C 53.787 0.300 1 212 46 46 ALA CB C 18.746 0.300 1 213 46 46 ALA N N 123.148 0.300 1 214 47 47 ALA H H 8.143 0.030 1 215 47 47 ALA C C 178.418 0.300 1 216 47 47 ALA CA C 52.145 0.300 1 217 47 47 ALA CB C 19.467 0.300 1 218 47 47 ALA N N 119.675 0.300 1 219 48 48 GLY H H 8.151 0.030 1 220 48 48 GLY C C 174.106 0.300 1 221 48 48 GLY CA C 46.251 0.300 1 222 48 48 GLY N N 107.730 0.300 1 223 49 49 LYS H H 7.557 0.030 1 224 49 49 LYS C C 175.761 0.300 1 225 49 49 LYS CA C 55.017 0.300 1 226 49 49 LYS CB C 34.838 0.300 1 227 49 49 LYS N N 117.913 0.300 1 228 50 50 SER H H 8.718 0.030 1 229 50 50 SER C C 176.185 0.300 1 230 50 50 SER CA C 58.294 0.300 1 231 50 50 SER CB C 63.894 0.300 1 232 50 50 SER N N 116.073 0.300 1 233 51 51 LYS H H 9.059 0.030 1 234 51 51 LYS C C 176.928 0.300 1 235 51 51 LYS CA C 56.401 0.300 1 236 51 51 LYS CB C 32.706 0.300 1 237 51 51 LYS N N 124.763 0.300 1 238 52 52 GLY H H 9.057 0.030 1 239 52 52 GLY C C 172.698 0.300 1 240 52 52 GLY CA C 45.533 0.300 1 241 52 52 GLY N N 107.733 0.300 1 242 53 53 TYR H H 7.373 0.030 1 243 53 53 TYR C C 172.355 0.300 1 244 53 53 TYR CA C 55.324 0.300 1 245 53 53 TYR CB C 40.431 0.300 1 246 53 53 TYR N N 114.149 0.300 1 247 54 54 GLY H H 8.914 0.030 1 248 54 54 GLY C C 169.536 0.300 1 249 54 54 GLY CA C 45.174 0.300 1 250 54 54 GLY N N 106.484 0.300 1 251 55 55 PHE H H 8.485 0.030 1 252 55 55 PHE C C 174.629 0.300 1 253 55 55 PHE CA C 55.837 0.300 1 254 55 55 PHE CB C 44.192 0.300 1 255 55 55 PHE N N 114.302 0.300 1 256 56 56 VAL H H 8.942 0.030 1 257 56 56 VAL C C 173.768 0.300 1 258 56 56 VAL CA C 61.168 0.300 1 259 56 56 VAL CB C 34.845 0.300 1 260 56 56 VAL N N 120.267 0.300 1 261 57 57 SER H H 8.735 0.030 1 262 57 57 SER C C 172.784 0.300 1 263 57 57 SER CA C 57.272 0.300 1 264 57 57 SER CB C 64.028 0.300 1 265 57 57 SER N N 122.329 0.300 1 266 58 58 PHE H H 9.265 0.030 1 267 58 58 PHE C C 175.778 0.300 1 268 58 58 PHE CA C 56.965 0.300 1 269 58 58 PHE CB C 42.389 0.300 1 270 58 58 PHE N N 122.079 0.300 1 271 59 59 PHE H H 7.710 0.030 1 272 59 59 PHE C C 175.850 0.300 1 273 59 59 PHE CA C 61.373 0.300 1 274 59 59 PHE CB C 40.071 0.300 1 275 59 59 PHE N N 117.940 0.300 1 276 60 60 ASN H H 8.652 0.030 1 277 60 60 ASN C C 174.767 0.300 1 278 60 60 ASN CA C 51.531 0.300 1 279 60 60 ASN CB C 40.587 0.300 1 280 60 60 ASN N N 114.168 0.300 1 281 61 61 LYS H H 8.161 0.030 1 282 61 61 LYS C C 177.121 0.300 1 283 61 61 LYS CA C 60.143 0.300 1 284 61 61 LYS CB C 32.087 0.300 1 285 61 61 LYS N N 126.641 0.300 1 286 62 62 TRP H H 7.568 0.030 1 287 62 62 TRP C C 177.840 0.300 1 288 62 62 TRP CA C 59.476 0.300 1 289 62 62 TRP CB C 27.935 0.300 1 290 62 62 TRP N N 116.589 0.300 1 291 63 63 ASP H H 6.868 0.030 1 292 63 63 ASP C C 176.500 0.300 1 293 63 63 ASP CA C 56.605 0.300 1 294 63 63 ASP CB C 40.638 0.300 1 295 63 63 ASP N N 121.271 0.300 1 296 64 64 ALA H H 6.588 0.030 1 297 64 64 ALA C C 177.915 0.300 1 298 64 64 ALA CA C 54.401 0.300 1 299 64 64 ALA CB C 19.209 0.300 1 300 64 64 ALA N N 119.724 0.300 1 301 65 65 GLU H H 8.300 0.030 1 302 65 65 GLU C C 178.959 0.300 1 303 65 65 GLU CA C 59.630 0.300 1 304 65 65 GLU CB C 30.316 0.300 1 305 65 65 GLU N N 117.115 0.300 1 306 66 66 ASN H H 7.914 0.030 1 307 66 66 ASN C C 176.317 0.300 1 308 66 66 ASN CA C 55.632 0.300 1 309 66 66 ASN CB C 38.165 0.300 1 310 66 66 ASN N N 117.955 0.300 1 311 67 67 ALA H H 7.864 0.030 1 312 67 67 ALA C C 179.369 0.300 1 313 67 67 ALA CA C 54.965 0.300 1 314 67 67 ALA CB C 19.158 0.300 1 315 67 67 ALA N N 121.670 0.300 1 316 68 68 ILE H H 8.071 0.030 1 317 68 68 ILE C C 179.081 0.300 1 318 68 68 ILE CA C 66.243 0.300 1 319 68 68 ILE CB C 38.320 0.300 1 320 68 68 ILE N N 116.542 0.300 1 321 69 69 GLN H H 7.625 0.030 1 322 69 69 GLN C C 178.520 0.300 1 323 69 69 GLN CA C 58.493 0.300 1 324 69 69 GLN CB C 28.636 0.300 1 325 69 69 GLN N N 117.152 0.300 1 326 70 70 GLN H H 8.413 0.030 1 327 70 70 GLN C C 178.269 0.300 1 328 70 70 GLN CA C 57.436 0.300 1 329 70 70 GLN CB C 29.203 0.300 1 330 70 70 GLN N N 114.732 0.300 1 331 71 71 MET H H 7.683 0.030 1 332 71 71 MET C C 177.432 0.300 1 333 71 71 MET CA C 53.683 0.300 1 334 71 71 MET CB C 30.851 0.300 1 335 71 71 MET N N 113.171 0.300 1 336 72 72 GLY H H 7.040 0.030 1 337 72 72 GLY C C 175.497 0.300 1 338 72 72 GLY CA C 49.019 0.300 1 339 72 72 GLY N N 107.002 0.300 1 340 73 73 GLY H H 8.447 0.030 1 341 73 73 GLY C C 174.504 0.300 1 342 73 73 GLY CA C 45.840 0.300 1 343 73 73 GLY N N 115.302 0.300 1 344 74 74 GLN H H 7.605 0.030 1 345 74 74 GLN C C 174.930 0.300 1 346 74 74 GLN CA C 55.119 0.300 1 347 74 74 GLN CB C 28.687 0.300 1 348 74 74 GLN N N 119.020 0.300 1 349 75 75 TRP H H 8.627 0.030 1 350 75 75 TRP C C 176.495 0.300 1 351 75 75 TRP CA C 57.580 0.300 1 352 75 75 TRP CB C 28.842 0.300 1 353 75 75 TRP N N 120.919 0.300 1 354 76 76 LEU H H 8.604 0.030 1 355 76 76 LEU C C 176.718 0.300 1 356 76 76 LEU CA C 54.811 0.300 1 357 76 76 LEU CB C 43.986 0.300 1 358 76 76 LEU N N 125.820 0.300 1 359 77 77 GLY H H 9.336 0.030 1 360 77 77 GLY C C 175.656 0.300 1 361 77 77 GLY CA C 47.584 0.300 1 362 77 77 GLY N N 115.475 0.300 1 363 78 78 GLY H H 8.757 0.030 1 364 78 78 GLY C C 173.704 0.300 1 365 78 78 GLY CA C 45.738 0.300 1 366 78 78 GLY N N 107.580 0.300 1 367 79 79 ARG H H 7.619 0.030 1 368 79 79 ARG C C 173.686 0.300 1 369 79 79 ARG CA C 54.863 0.300 1 370 79 79 ARG CB C 33.942 0.300 1 371 79 79 ARG N N 118.454 0.300 1 372 80 80 GLN H H 7.826 0.030 1 373 80 80 GLN C C 176.138 0.300 1 374 80 80 GLN CA C 55.119 0.300 1 375 80 80 GLN CB C 29.666 0.300 1 376 80 80 GLN N N 121.784 0.300 1 377 81 81 ILE H H 8.161 0.030 1 378 81 81 ILE C C 176.070 0.300 1 379 81 81 ILE CA C 60.706 0.300 1 380 81 81 ILE CB C 40.020 0.300 1 381 81 81 ILE N N 118.282 0.300 1 382 82 82 ARG H H 7.888 0.030 1 383 82 82 ARG C C 175.262 0.300 1 384 82 82 ARG CA C 53.735 0.300 1 385 82 82 ARG CB C 33.376 0.300 1 386 82 82 ARG N N 119.739 0.300 1 387 83 83 THR H H 8.415 0.030 1 388 83 83 THR C C 174.176 0.300 1 389 83 83 THR CA C 58.400 0.300 1 390 83 83 THR CB C 71.132 0.300 1 391 83 83 THR N N 110.762 0.300 1 392 84 84 ASN H H 8.614 0.030 1 393 84 84 ASN C C 174.232 0.300 1 394 84 84 ASN CA C 52.608 0.300 1 395 84 84 ASN CB C 42.132 0.300 1 396 84 84 ASN N N 114.929 0.300 1 397 85 85 TRP H H 8.771 0.030 1 398 85 85 TRP C C 177.373 0.300 1 399 85 85 TRP CA C 58.144 0.300 1 400 85 85 TRP CB C 30.336 0.300 1 401 85 85 TRP N N 121.945 0.300 1 402 86 86 ALA H H 8.914 0.030 1 403 86 86 ALA C C 177.549 0.300 1 404 86 86 ALA CA C 52.407 0.300 1 405 86 86 ALA CB C 19.776 0.300 1 406 86 86 ALA N N 125.711 0.300 1 407 87 87 THR H H 8.559 0.030 1 408 87 87 THR C C 175.619 0.300 1 409 87 87 THR CA C 61.834 0.300 1 410 87 87 THR CB C 69.690 0.300 1 411 87 87 THR N N 114.758 0.300 1 412 88 88 ARG H H 8.137 0.030 1 413 88 88 ARG C C 175.178 0.300 1 414 88 88 ARG CA C 55.430 0.300 1 415 88 88 ARG CB C 31.212 0.300 1 416 88 88 ARG N N 122.174 0.300 1 417 89 89 LYS H H 8.225 0.030 1 418 89 89 LYS C C 173.782 0.300 1 419 89 89 LYS CA C 54.090 0.300 1 420 89 89 LYS CB C 32.067 0.300 1 421 89 89 LYS N N 123.636 0.300 1 422 91 91 PRO C C 176.057 0.300 1 423 91 91 PRO CA C 62.593 0.300 1 424 91 91 PRO CB C 31.901 0.300 1 425 92 92 ALA H H 8.294 0.030 1 426 92 92 ALA C C 175.569 0.300 1 427 92 92 ALA CA C 50.393 0.300 1 428 92 92 ALA CB C 18.126 0.300 1 429 92 92 ALA N N 125.531 0.300 1 430 93 93 PRO C C 176.874 0.300 1 431 93 93 PRO CA C 62.900 0.300 1 432 93 93 PRO CB C 32.004 0.300 1 433 94 94 LYS H H 8.412 0.030 1 434 94 94 LYS C C 176.734 0.300 1 435 94 94 LYS CA C 56.503 0.300 1 436 94 94 LYS CB C 32.757 0.300 1 437 94 94 LYS N N 121.644 0.300 1 438 95 95 SER H H 8.369 0.030 1 439 95 95 SER C C 174.699 0.300 1 440 95 95 SER CA C 58.339 0.300 1 441 95 95 SER CB C 63.817 0.300 1 442 95 95 SER N N 117.060 0.300 1 443 96 96 THR H H 8.133 0.030 1 444 96 96 THR C C 174.248 0.300 1 445 96 96 THR CA C 61.940 0.300 1 446 96 96 THR CB C 69.587 0.300 1 447 96 96 THR N N 115.615 0.300 1 448 97 97 TYR H H 8.116 0.030 1 449 97 97 TYR C C 175.704 0.300 1 450 97 97 TYR CA C 58.147 0.300 1 451 97 97 TYR CB C 38.835 0.300 1 452 97 97 TYR N N 121.812 0.300 1 453 98 98 GLU H H 8.206 0.030 1 454 98 98 GLU C C 176.099 0.300 1 455 98 98 GLU CA C 56.451 0.300 1 456 98 98 GLU CB C 30.490 0.300 1 457 98 98 GLU N N 122.628 0.300 1 458 99 99 SER H H 8.274 0.030 1 459 99 99 SER C C 174.394 0.300 1 460 99 99 SER CA C 58.335 0.300 1 461 99 99 SER CB C 63.715 0.300 1 462 99 99 SER N N 116.751 0.300 1 463 100 100 ASN H H 8.475 0.030 1 464 100 100 ASN C C 175.323 0.300 1 465 100 100 ASN CA C 53.325 0.300 1 466 100 100 ASN CB C 38.835 0.300 1 467 100 100 ASN N N 120.853 0.300 1 468 101 101 THR H H 8.056 0.030 1 469 101 101 THR C C 174.272 0.300 1 470 101 101 THR CA C 61.886 0.300 1 471 101 101 THR CB C 69.587 0.300 1 472 101 101 THR N N 114.282 0.300 1 473 102 102 LYS H H 8.275 0.030 1 474 102 102 LYS C C 175.515 0.300 1 475 102 102 LYS CA C 56.503 0.300 1 476 102 102 LYS CB C 32.963 0.300 1 477 102 102 LYS N N 124.403 0.300 1 478 103 103 GLN H H 8.005 0.030 1 479 103 103 GLN C C 180.494 0.300 1 480 103 103 GLN CA C 57.171 0.300 1 481 103 103 GLN CB C 30.518 0.300 1 482 103 103 GLN N N 127.262 0.300 1 stop_ save_