data_11371 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, D131A mutant ; _BMRB_accession_number 11371 _BMRB_flat_file_name bmr11371.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" 93 "13C chemical shifts" 290 "15N chemical shifts" 93 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' 11372 'Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, K138A 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 D131A 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 D131A mutant' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 103 _Mol_residue_sequence ; GQKKDTSNHFHVFVGDLSPE ITTEDIKAAFAPFGRISDAR VVKAMATGKSKGYGFVSFFN 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 ALA 45 MET 46 ALA 47 THR 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 1.63e-55 BMRB 11372 "RRM domain K138A mutant" 100.00 103 98.06 98.06 1.89e-67 BMRB 11373 "RRM domain T134A mutant" 100.00 103 98.06 98.06 1.43e-67 BMRB 11374 "RRM domain" 100.00 115 99.03 99.03 2.14e-68 BMRB 11375 "RRM domain" 100.00 115 99.03 99.03 2.14e-68 BMRB 11376 "RRM domain" 100.00 115 99.03 99.03 2.14e-68 PDB 2DGO "Solution Structure Of The Rna Binding Domain In Cytotoxic Granule-Associated Rna Binding Protein 1" 100.00 115 99.03 99.03 2.14e-68 PDB 2RNE "Solution Structure Of The Second Rna Recognition Motif (Rrm) Of Tia-1" 100.00 115 99.03 99.03 2.14e-68 GB EAW99825 "TIA1 cytotoxic granule-associated RNA binding protein, isoform CRA_c, partial [Homo sapiens]" 99.03 144 99.02 99.02 1.61e-67 REF XP_005430921 "PREDICTED: nucleolysin TIA-1 isoform p40 [Geospiza fortis]" 99.03 367 98.04 99.02 5.28e-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 D131A 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 175.994 0.300 1 2 2 2 GLN CA C 55.775 0.300 1 3 2 2 GLN CB C 30.106 0.300 1 4 3 3 LYS H H 8.533 0.030 1 5 3 3 LYS C C 176.444 0.300 1 6 3 3 LYS CA C 56.382 0.300 1 7 3 3 LYS CB C 33.077 0.300 1 8 3 3 LYS N N 123.810 0.300 1 9 4 4 LYS H H 8.457 0.030 1 10 4 4 LYS C C 175.973 0.300 1 11 4 4 LYS CA C 56.236 0.300 1 12 4 4 LYS CB C 33.129 0.300 1 13 4 4 LYS N N 123.655 0.300 1 14 5 5 ASP H H 8.437 0.030 1 15 5 5 ASP C C 176.757 0.300 1 16 5 5 ASP CA C 54.184 0.300 1 17 5 5 ASP CB C 41.259 0.300 1 18 5 5 ASP N N 122.429 0.300 1 19 6 6 THR H H 8.222 0.030 1 20 6 6 THR C C 175.539 0.300 1 21 6 6 THR CA C 61.144 0.300 1 22 6 6 THR CB C 69.191 0.300 1 23 6 6 THR N N 114.849 0.300 1 24 7 7 SER H H 8.311 0.030 1 25 7 7 SER C C 174.477 0.300 1 26 7 7 SER CA C 60.144 0.300 1 27 7 7 SER CB C 63.387 0.300 1 28 7 7 SER N N 118.739 0.300 1 29 8 8 ASN H H 8.252 0.030 1 30 8 8 ASN C C 174.169 0.300 1 31 8 8 ASN CA C 52.866 0.300 1 32 8 8 ASN CB C 38.705 0.300 1 33 8 8 ASN N N 119.472 0.300 1 34 9 9 HIS H H 7.393 0.030 1 35 9 9 HIS C C 172.238 0.300 1 36 9 9 HIS CA C 53.915 0.300 1 37 9 9 HIS CB C 32.206 0.300 1 38 9 9 HIS N N 119.150 0.300 1 39 10 10 PHE H H 8.368 0.030 1 40 10 10 PHE C C 175.087 0.300 1 41 10 10 PHE CA C 58.434 0.300 1 42 10 10 PHE CB C 40.842 0.300 1 43 10 10 PHE N N 117.509 0.300 1 44 11 11 HIS H H 8.839 0.030 1 45 11 11 HIS C C 174.253 0.300 1 46 11 11 HIS CA C 56.602 0.300 1 47 11 11 HIS CB C 33.233 0.300 1 48 11 11 HIS N N 124.319 0.300 1 49 12 12 VAL H H 9.776 0.030 1 50 12 12 VAL C C 175.278 0.300 1 51 12 12 VAL CA C 62.219 0.300 1 52 12 12 VAL CB C 33.915 0.300 1 53 12 12 VAL N N 126.476 0.300 1 54 13 13 PHE H H 9.132 0.030 1 55 13 13 PHE C C 172.825 0.300 1 56 13 13 PHE CA C 57.285 0.300 1 57 13 13 PHE CB C 40.841 0.300 1 58 13 13 PHE N N 127.970 0.300 1 59 14 14 VAL H H 7.824 0.030 1 60 14 14 VAL C C 173.619 0.300 1 61 14 14 VAL CA C 59.606 0.300 1 62 14 14 VAL CB C 32.660 0.300 1 63 14 14 VAL N N 126.964 0.300 1 64 15 15 GLY H H 8.796 0.030 1 65 15 15 GLY C C 172.331 0.300 1 66 15 15 GLY CA C 43.489 0.300 1 67 15 15 GLY N N 111.361 0.300 1 68 16 16 ASP H H 8.406 0.030 1 69 16 16 ASP C C 174.011 0.300 1 70 16 16 ASP CA C 55.524 0.300 1 71 16 16 ASP CB C 38.861 0.300 1 72 16 16 ASP N N 115.421 0.300 1 73 17 17 LEU C C 178.287 0.300 1 74 17 17 LEU CA C 53.194 0.300 1 75 17 17 LEU CB C 43.030 0.300 1 76 18 18 SER H H 8.887 0.030 1 77 18 18 SER C C 174.703 0.300 1 78 18 18 SER CA C 56.993 0.300 1 79 18 18 SER CB C 63.042 0.300 1 80 18 18 SER N N 120.856 0.300 1 81 19 19 PRO C C 176.260 0.300 1 82 19 19 PRO CA C 65.467 0.300 1 83 19 19 PRO CB C 31.982 0.300 1 84 20 20 GLU H H 8.913 0.030 1 85 20 20 GLU C C 176.757 0.300 1 86 20 20 GLU CA C 56.651 0.300 1 87 20 20 GLU CB C 29.116 0.300 1 88 20 20 GLU N N 116.021 0.300 1 89 21 21 ILE H H 7.334 0.030 1 90 21 21 ILE C C 176.899 0.300 1 91 21 21 ILE CA C 59.435 0.300 1 92 21 21 ILE CB C 35.213 0.300 1 93 21 21 ILE N N 121.577 0.300 1 94 22 22 THR H H 9.366 0.030 1 95 22 22 THR C C 176.276 0.300 1 96 22 22 THR CA C 60.046 0.300 1 97 22 22 THR CB C 73.657 0.300 1 98 22 22 THR N N 120.890 0.300 1 99 23 23 THR H H 9.003 0.030 1 100 23 23 THR C C 175.474 0.300 1 101 23 23 THR CA C 66.957 0.300 1 102 23 23 THR CB C 68.983 0.300 1 103 23 23 THR N N 118.103 0.300 1 104 24 24 GLU H H 8.399 0.030 1 105 24 24 GLU C C 179.186 0.300 1 106 24 24 GLU CA C 60.436 0.300 1 107 24 24 GLU CB C 28.595 0.300 1 108 24 24 GLU N N 119.972 0.300 1 109 25 25 ASP H H 7.708 0.030 1 110 25 25 ASP C C 179.813 0.300 1 111 25 25 ASP CA C 57.505 0.300 1 112 25 25 ASP CB C 41.675 0.300 1 113 25 25 ASP N N 120.119 0.300 1 114 26 26 ILE H H 7.890 0.030 1 115 26 26 ILE C C 177.464 0.300 1 116 26 26 ILE CA C 64.221 0.300 1 117 26 26 ILE CB C 37.142 0.300 1 118 26 26 ILE N N 118.420 0.300 1 119 27 27 LYS H H 8.285 0.030 1 120 27 27 LYS C C 177.780 0.300 1 121 27 27 LYS CA C 60.998 0.300 1 122 27 27 LYS CB C 32.139 0.300 1 123 27 27 LYS N N 121.557 0.300 1 124 28 28 ALA H H 7.759 0.030 1 125 28 28 ALA C C 180.283 0.300 1 126 28 28 ALA CA C 54.843 0.300 1 127 28 28 ALA CB C 18.225 0.300 1 128 28 28 ALA N N 118.306 0.300 1 129 29 29 ALA H H 7.814 0.030 1 130 29 29 ALA C C 177.793 0.300 1 131 29 29 ALA CA C 53.940 0.300 1 132 29 29 ALA CB C 18.931 0.300 1 133 29 29 ALA N N 118.004 0.300 1 134 30 30 PHE H H 7.967 0.030 1 135 30 30 PHE C C 175.416 0.300 1 136 30 30 PHE CA C 59.532 0.300 1 137 30 30 PHE CB C 40.321 0.300 1 138 30 30 PHE N N 112.047 0.300 1 139 31 31 ALA H H 8.049 0.030 1 140 31 31 ALA C C 176.379 0.300 1 141 31 31 ALA CA C 55.720 0.300 1 142 31 31 ALA CB C 16.765 0.300 1 143 31 31 ALA N N 125.067 0.300 1 144 32 32 PRO C C 177.374 0.300 1 145 32 32 PRO CA C 65.175 0.300 1 146 32 32 PRO CB C 31.461 0.300 1 147 33 33 PHE H H 7.699 0.030 1 148 33 33 PHE C C 174.558 0.300 1 149 33 33 PHE CA C 59.508 0.300 1 150 33 33 PHE CB C 39.018 0.300 1 151 33 33 PHE N N 112.643 0.300 1 152 34 34 GLY H H 7.600 0.030 1 153 34 34 GLY C C 171.592 0.300 1 154 34 34 GLY CA C 44.383 0.300 1 155 34 34 GLY N N 104.638 0.300 1 156 35 35 ARG H H 8.243 0.030 1 157 35 35 ARG C C 176.972 0.300 1 158 35 35 ARG CA C 57.897 0.300 1 159 35 35 ARG CB C 31.044 0.300 1 160 35 35 ARG N N 117.026 0.300 1 161 36 36 ILE H H 8.507 0.030 1 162 36 36 ILE C C 176.743 0.300 1 163 36 36 ILE CA C 60.412 0.300 1 164 36 36 ILE CB C 40.790 0.300 1 165 36 36 ILE N N 127.973 0.300 1 166 37 37 SER H H 8.843 0.030 1 167 37 37 SER C C 174.613 0.300 1 168 37 37 SER CA C 57.995 0.300 1 169 37 37 SER CB C 63.050 0.300 1 170 37 37 SER N N 123.260 0.300 1 171 38 38 ASP H H 7.271 0.030 1 172 38 38 ASP C C 172.760 0.300 1 173 38 38 ASP CA C 53.794 0.300 1 174 38 38 ASP CB C 43.708 0.300 1 175 38 38 ASP N N 119.571 0.300 1 176 39 39 ALA H H 7.971 0.030 1 177 39 39 ALA C C 175.238 0.300 1 178 39 39 ALA CA C 51.693 0.300 1 179 39 39 ALA CB C 22.602 0.300 1 180 39 39 ALA N N 121.400 0.300 1 181 40 40 ARG H H 8.642 0.030 1 182 40 40 ARG C C 174.267 0.300 1 183 40 40 ARG CA C 55.772 0.300 1 184 40 40 ARG CB C 33.129 0.300 1 185 40 40 ARG N N 115.941 0.300 1 186 41 41 VAL H H 7.681 0.030 1 187 41 41 VAL C C 175.716 0.300 1 188 41 41 VAL CA C 62.927 0.300 1 189 41 41 VAL CB C 32.985 0.300 1 190 41 41 VAL N N 123.134 0.300 1 191 42 42 VAL H H 8.518 0.030 1 192 42 42 VAL C C 174.160 0.300 1 193 42 42 VAL CA C 63.862 0.300 1 194 42 42 VAL CB C 30.893 0.300 1 195 42 42 VAL N N 130.219 0.300 1 196 43 43 LYS H H 8.162 0.030 1 197 43 43 LYS C C 176.211 0.300 1 198 43 43 LYS CA C 54.282 0.300 1 199 43 43 LYS CB C 35.161 0.300 1 200 43 43 LYS N N 125.490 0.300 1 201 44 44 ALA H H 8.630 0.030 1 202 44 44 ALA C C 178.291 0.300 1 203 44 44 ALA CA C 51.586 0.300 1 204 44 44 ALA CB C 18.850 0.300 1 205 44 44 ALA N N 125.018 0.300 1 206 46 46 ALA CA C 55.075 0.300 1 207 46 46 ALA CB C 19.026 0.300 1 208 47 47 THR H H 7.135 0.030 1 209 47 47 THR C C 176.020 0.300 1 210 47 47 THR CA C 60.900 0.300 1 211 47 47 THR CB C 70.918 0.300 1 212 47 47 THR N N 103.152 0.300 1 213 48 48 GLY H H 8.263 0.030 1 214 48 48 GLY C C 173.657 0.300 1 215 48 48 GLY CA C 45.784 0.300 1 216 48 48 GLY N N 110.824 0.300 1 217 49 49 LYS H H 7.755 0.030 1 218 49 49 LYS C C 176.450 0.300 1 219 49 49 LYS CA C 55.601 0.300 1 220 49 49 LYS CB C 33.546 0.300 1 221 49 49 LYS N N 119.158 0.300 1 222 50 50 SER H H 8.674 0.030 1 223 50 50 SER C C 176.609 0.300 1 224 50 50 SER CA C 58.242 0.300 1 225 50 50 SER CB C 64.217 0.300 1 226 50 50 SER N N 115.796 0.300 1 227 51 51 LYS H H 9.157 0.030 1 228 51 51 LYS C C 177.109 0.300 1 229 51 51 LYS CA C 56.431 0.300 1 230 51 51 LYS CB C 33.025 0.300 1 231 51 51 LYS N N 125.306 0.300 1 232 52 52 GLY H H 9.141 0.030 1 233 52 52 GLY C C 172.717 0.300 1 234 52 52 GLY CA C 45.662 0.300 1 235 52 52 GLY N N 107.582 0.300 1 236 53 53 TYR H H 7.220 0.030 1 237 53 53 TYR C C 172.310 0.300 1 238 53 53 TYR CA C 55.308 0.300 1 239 53 53 TYR CB C 40.425 0.300 1 240 53 53 TYR N N 113.435 0.300 1 241 54 54 GLY H H 8.870 0.030 1 242 54 54 GLY C C 169.495 0.300 1 243 54 54 GLY CA C 45.149 0.300 1 244 54 54 GLY N N 106.384 0.300 1 245 55 55 PHE H H 8.486 0.030 1 246 55 55 PHE C C 174.546 0.300 1 247 55 55 PHE CA C 55.967 0.300 1 248 55 55 PHE CB C 44.515 0.300 1 249 55 55 PHE N N 114.086 0.300 1 250 56 56 VAL H H 8.948 0.030 1 251 56 56 VAL C C 173.733 0.300 1 252 56 56 VAL CA C 61.290 0.300 1 253 56 56 VAL CB C 35.005 0.300 1 254 56 56 VAL N N 120.105 0.300 1 255 57 57 SER H H 8.742 0.030 1 256 57 57 SER C C 172.786 0.300 1 257 57 57 SER CA C 57.423 0.300 1 258 57 57 SER CB C 64.189 0.300 1 259 57 57 SER N N 122.302 0.300 1 260 58 58 PHE H H 9.261 0.030 1 261 58 58 PHE C C 175.784 0.300 1 262 58 58 PHE CA C 57.066 0.300 1 263 58 58 PHE CB C 42.561 0.300 1 264 58 58 PHE N N 122.081 0.300 1 265 59 59 PHE H H 7.718 0.030 1 266 59 59 PHE C C 175.844 0.300 1 267 59 59 PHE CA C 61.389 0.300 1 268 59 59 PHE CB C 40.060 0.300 1 269 59 59 PHE N N 117.945 0.300 1 270 60 60 ASN H H 8.649 0.030 1 271 60 60 ASN C C 174.809 0.300 1 272 60 60 ASN CA C 51.620 0.300 1 273 60 60 ASN CB C 40.737 0.300 1 274 60 60 ASN N N 114.173 0.300 1 275 61 61 LYS H H 8.168 0.030 1 276 61 61 LYS C C 177.094 0.300 1 277 61 61 LYS CA C 60.168 0.300 1 278 61 61 LYS CB C 32.347 0.300 1 279 61 61 LYS N N 126.585 0.300 1 280 62 62 TRP H H 7.571 0.030 1 281 62 62 TRP C C 177.868 0.300 1 282 62 62 TRP CA C 59.508 0.300 1 283 62 62 TRP CB C 27.813 0.300 1 284 62 62 TRP N N 116.614 0.300 1 285 63 63 ASP H H 6.880 0.030 1 286 63 63 ASP C C 176.509 0.300 1 287 63 63 ASP CA C 56.870 0.300 1 288 63 63 ASP CB C 40.685 0.300 1 289 63 63 ASP N N 121.286 0.300 1 290 64 64 ALA H H 6.595 0.030 1 291 64 64 ALA C C 177.978 0.300 1 292 64 64 ALA CA C 54.502 0.300 1 293 64 64 ALA CB C 19.163 0.300 1 294 64 64 ALA N N 119.718 0.300 1 295 65 65 GLU H H 8.303 0.030 1 296 65 65 GLU C C 178.936 0.300 1 297 65 65 GLU CA C 59.654 0.300 1 298 65 65 GLU CB C 30.159 0.300 1 299 65 65 GLU N N 117.123 0.300 1 300 66 66 ASN H H 7.921 0.030 1 301 66 66 ASN C C 176.316 0.300 1 302 66 66 ASN CA C 55.796 0.300 1 303 66 66 ASN CB C 38.463 0.300 1 304 66 66 ASN N N 117.954 0.300 1 305 67 67 ALA H H 7.873 0.030 1 306 67 67 ALA C C 179.337 0.300 1 307 67 67 ALA CA C 55.026 0.300 1 308 67 67 ALA CB C 18.798 0.300 1 309 67 67 ALA N N 121.676 0.300 1 310 68 68 ILE H H 8.079 0.030 1 311 68 68 ILE C C 179.105 0.300 1 312 68 68 ILE CA C 66.444 0.300 1 313 68 68 ILE CB C 38.288 0.300 1 314 68 68 ILE N N 116.549 0.300 1 315 69 69 GLN H H 7.628 0.030 1 316 69 69 GLN C C 178.515 0.300 1 317 69 69 GLN CA C 58.434 0.300 1 318 69 69 GLN CB C 28.751 0.300 1 319 69 69 GLN N N 117.146 0.300 1 320 70 70 GLN H H 8.416 0.030 1 321 70 70 GLN C C 178.320 0.300 1 322 70 70 GLN CA C 57.603 0.300 1 323 70 70 GLN CB C 29.116 0.300 1 324 70 70 GLN N N 114.733 0.300 1 325 71 71 MET H H 7.690 0.030 1 326 71 71 MET C C 177.412 0.300 1 327 71 71 MET CA C 53.794 0.300 1 328 71 71 MET CB C 30.836 0.300 1 329 71 71 MET N N 113.210 0.300 1 330 72 72 GLY H H 7.045 0.030 1 331 72 72 GLY C C 175.532 0.300 1 332 72 72 GLY CA C 48.838 0.300 1 333 72 72 GLY N N 106.997 0.300 1 334 73 73 GLY H H 8.450 0.030 1 335 73 73 GLY C C 174.395 0.300 1 336 73 73 GLY CA C 45.760 0.300 1 337 73 73 GLY N N 115.309 0.300 1 338 74 74 GLN H H 7.610 0.030 1 339 74 74 GLN C C 174.950 0.300 1 340 74 74 GLN CA C 55.186 0.300 1 341 74 74 GLN CB C 28.699 0.300 1 342 74 74 GLN N N 119.032 0.300 1 343 75 75 TRP H H 8.623 0.030 1 344 75 75 TRP C C 176.491 0.300 1 345 75 75 TRP CA C 57.654 0.300 1 346 75 75 TRP CB C 28.999 0.300 1 347 75 75 TRP N N 120.954 0.300 1 348 76 76 LEU H H 8.609 0.030 1 349 76 76 LEU C C 176.726 0.300 1 350 76 76 LEU CA C 54.814 0.300 1 351 76 76 LEU CB C 43.935 0.300 1 352 76 76 LEU N N 125.830 0.300 1 353 77 77 GLY H H 9.338 0.030 1 354 77 77 GLY C C 175.645 0.300 1 355 77 77 GLY CA C 47.252 0.300 1 356 77 77 GLY N N 115.406 0.300 1 357 78 78 GLY H H 8.758 0.030 1 358 78 78 GLY C C 173.677 0.300 1 359 78 78 GLY CA C 45.710 0.300 1 360 78 78 GLY N N 107.503 0.300 1 361 79 79 ARG H H 7.628 0.030 1 362 79 79 ARG C C 173.740 0.300 1 363 79 79 ARG CA C 55.099 0.300 1 364 79 79 ARG CB C 34.067 0.300 1 365 79 79 ARG N N 118.490 0.300 1 366 80 80 GLN H H 7.828 0.030 1 367 80 80 GLN C C 176.166 0.300 1 368 80 80 GLN CA C 55.185 0.300 1 369 80 80 GLN CB C 29.689 0.300 1 370 80 80 GLN N N 121.688 0.300 1 371 81 81 ILE H H 8.170 0.030 1 372 81 81 ILE C C 176.072 0.300 1 373 81 81 ILE CA C 60.998 0.300 1 374 81 81 ILE CB C 39.904 0.300 1 375 81 81 ILE N N 118.219 0.300 1 376 82 82 ARG H H 7.906 0.030 1 377 82 82 ARG C C 175.264 0.300 1 378 82 82 ARG CA C 53.892 0.300 1 379 82 82 ARG CB C 33.442 0.300 1 380 82 82 ARG N N 119.761 0.300 1 381 83 83 THR H H 8.419 0.030 1 382 83 83 THR C C 174.154 0.300 1 383 83 83 THR CA C 58.385 0.300 1 384 83 83 THR CB C 71.380 0.300 1 385 83 83 THR N N 110.761 0.300 1 386 84 84 ASN H H 8.618 0.030 1 387 84 84 ASN C C 174.242 0.300 1 388 84 84 ASN CA C 52.621 0.300 1 389 84 84 ASN CB C 42.145 0.300 1 390 84 84 ASN N N 114.962 0.300 1 391 85 85 TRP H H 8.780 0.030 1 392 85 85 TRP C C 177.387 0.300 1 393 85 85 TRP CA C 58.385 0.300 1 394 85 85 TRP CB C 30.315 0.300 1 395 85 85 TRP N N 121.948 0.300 1 396 86 86 ALA H H 8.914 0.030 1 397 86 86 ALA C C 177.513 0.300 1 398 86 86 ALA CA C 51.729 0.300 1 399 86 86 ALA CB C 19.880 0.300 1 400 86 86 ALA N N 125.707 0.300 1 401 87 87 THR H H 8.552 0.030 1 402 87 87 THR C C 174.203 0.300 1 403 87 87 THR CA C 62.136 0.300 1 404 87 87 THR CB C 69.621 0.300 1 405 87 87 THR N N 114.708 0.300 1 406 88 88 ARG H H 8.153 0.030 1 407 88 88 ARG C C 175.178 0.300 1 408 88 88 ARG CA C 55.382 0.300 1 409 88 88 ARG CB C 31.180 0.300 1 410 88 88 ARG N N 122.258 0.300 1 411 89 89 LYS H H 8.228 0.030 1 412 89 89 LYS C C 173.774 0.300 1 413 89 89 LYS CA C 53.981 0.300 1 414 89 89 LYS CB C 32.303 0.300 1 415 89 89 LYS N N 123.682 0.300 1 416 91 91 PRO C C 176.066 0.300 1 417 91 91 PRO CA C 62.519 0.300 1 418 91 91 PRO CB C 31.957 0.300 1 419 92 92 ALA H H 8.296 0.030 1 420 92 92 ALA C C 175.523 0.300 1 421 92 92 ALA CA C 50.286 0.300 1 422 92 92 ALA CB C 18.049 0.300 1 423 92 92 ALA N N 125.522 0.300 1 424 93 93 PRO C C 176.887 0.300 1 425 93 93 PRO CA C 62.941 0.300 1 426 93 93 PRO CB C 32.104 0.300 1 427 94 94 LYS H H 8.411 0.030 1 428 94 94 LYS C C 176.710 0.300 1 429 94 94 LYS CA C 56.504 0.300 1 430 94 94 LYS CB C 32.868 0.300 1 431 94 94 LYS N N 121.556 0.300 1 432 95 95 SER H H 8.362 0.030 1 433 95 95 SER C C 174.720 0.300 1 434 95 95 SER CA C 58.312 0.300 1 435 95 95 SER CB C 64.051 0.300 1 436 95 95 SER N N 117.026 0.300 1 437 96 96 THR H H 8.135 0.030 1 438 96 96 THR C C 174.270 0.300 1 439 96 96 THR CA C 62.052 0.300 1 440 96 96 THR CB C 69.590 0.300 1 441 96 96 THR N N 115.594 0.300 1 442 97 97 TYR H H 8.120 0.030 1 443 97 97 TYR C C 175.732 0.300 1 444 97 97 TYR CA C 58.066 0.300 1 445 97 97 TYR CB C 38.757 0.300 1 446 97 97 TYR N N 121.779 0.300 1 447 98 98 GLU H H 8.213 0.030 1 448 98 98 GLU C C 176.103 0.300 1 449 98 98 GLU CA C 56.480 0.300 1 450 98 98 GLU CB C 30.499 0.300 1 451 98 98 GLU N N 122.606 0.300 1 452 99 99 SER H H 8.276 0.030 1 453 99 99 SER C C 174.398 0.300 1 454 99 99 SER CA C 58.457 0.300 1 455 99 99 SER CB C 63.775 0.300 1 456 99 99 SER N N 116.731 0.300 1 457 100 100 ASN H H 8.477 0.030 1 458 100 100 ASN C C 175.333 0.300 1 459 100 100 ASN CA C 53.452 0.300 1 460 100 100 ASN CB C 38.792 0.300 1 461 100 100 ASN N N 120.825 0.300 1 462 101 101 THR H H 8.061 0.030 1 463 101 101 THR C C 174.307 0.300 1 464 101 101 THR CA C 61.950 0.300 1 465 101 101 THR CB C 69.802 0.300 1 466 101 101 THR N N 114.259 0.300 1 467 102 102 LYS H H 8.278 0.030 1 468 102 102 LYS C C 175.512 0.300 1 469 102 102 LYS CA C 56.382 0.300 1 470 102 102 LYS CB C 33.117 0.300 1 471 102 102 LYS N N 124.388 0.300 1 472 103 103 GLN H H 8.007 0.030 1 473 103 103 GLN C C 180.477 0.300 1 474 103 103 GLN CA C 57.336 0.300 1 475 103 103 GLN CB C 30.447 0.300 1 476 103 103 GLN N N 127.252 0.300 1 stop_ save_