data_6702 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Resonance assignments of 30 kDa complexes of TFIID subunit TAF1 with TATA-binding protein ; _BMRB_accession_number 6702 _BMRB_flat_file_name bmr6702.str _Entry_type original _Submission_date 2005-06-22 _Accession_date 2005-06-22 _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 Mal Tapas K. . 2 Liu Dingjiang . . 3 Masutomi Yutaka . . 4 Zheng Le . . 5 Nakatani Yoshihiro . . 6 Kokubo Tetsuro . . 7 Ikura Mitsuhiko . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 232 "13C chemical shifts" 462 "15N chemical shifts" 232 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-11-06 original author . stop_ _Original_release_date 2006-11-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Resonance Assignments of 30 kDa Complexes of TFIID Subunit TAF1 with TATA-binding Protein ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16222567 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mal Tapas K. . 2 Liu Dingjiang . . 3 Masutomi Yutaka . . 4 Zheng Le . . 5 Nakatani Yoshihiro . . 6 Kokubo Tetsuro . . 7 Ikura Mitsuhiko . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 33 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 76 _Page_last 76 _Year 2005 _Details . loop_ _Keyword NMR TBP stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'yeast TBP associated factor 1 (yTAF1)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label yTAF1c $yTAF1c yTBPc $yTBPc stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state 'protein-protein complex' _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details 'Protein complex of yTAF1 and TBP' save_ ######################## # Monomeric polymers # ######################## save_yTAF1c _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common yTAF1 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 64 _Mol_residue_sequence ; TNLANEDEAYEAIFGGEFGS LEIGSYIGGDEGANSKDYTE HLPDAVDFEDEDELADDDDD LPEE ; loop_ _Residue_seq_code _Residue_label 1 THR 2 ASN 3 LEU 4 ALA 5 ASN 6 GLU 7 ASP 8 GLU 9 ALA 10 TYR 11 GLU 12 ALA 13 ILE 14 PHE 15 GLY 16 GLY 17 GLU 18 PHE 19 GLY 20 SER 21 LEU 22 GLU 23 ILE 24 GLY 25 SER 26 TYR 27 ILE 28 GLY 29 GLY 30 ASP 31 GLU 32 GLY 33 ALA 34 ASN 35 SER 36 LYS 37 ASP 38 TYR 39 THR 40 GLU 41 HIS 42 LEU 43 PRO 44 ASP 45 ALA 46 VAL 47 ASP 48 PHE 49 GLU 50 ASP 51 GLU 52 ASP 53 GLU 54 LEU 55 ALA 56 ASP 57 ASP 58 ASP 59 ASP 60 ASP 61 LEU 62 PRO 63 GLU 64 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 6700 yTBP 100.00 192 100.00 100.00 5.47e-136 PDB 1NGM "Crystal Structure Of A Yeast Brf1-Tbp-Dna Ternary Complex" 93.75 180 100.00 100.00 7.38e-127 PDB 1NH2 "Crystal Structure Of A Yeast TfiiaTBPDNA COMPLEX" 93.75 180 100.00 100.00 7.38e-127 PDB 1RM1 "Structure Of A Yeast TfiiaTBPTATA-Box Dna Complex" 100.00 240 100.00 100.00 1.81e-135 PDB 1TBA "Solution Structure Of A Tbp-Tafii230 Complex: Protein Mimicry Of The Minor Groove Surface Of The Tata Box Unwound By Tbp, Nmr, " 93.75 180 100.00 100.00 7.38e-127 PDB 1TBP "Crystal Structure Of Yeast Tata-Binding Protein And Model For Interaction With Dna" 93.23 180 100.00 100.00 3.93e-126 PDB 1YTB "Crystal Structure Of A Yeast TbpTATA-Box Complex" 93.75 180 100.00 100.00 7.38e-127 PDB 1YTF "Yeast TfiiaTBPDNA COMPLEX" 93.75 180 100.00 100.00 7.38e-127 PDB 4B0A "The High-resolution Structure Of Ytbp-ytaf1 Identifies Conserved And Competing Interaction Surfaces In Transcriptional Activati" 95.31 278 98.36 98.91 7.10e-126 DBJ GAA22978 "K7_Spt15p [Saccharomyces cerevisiae Kyokai no. 7]" 100.00 240 100.00 100.00 1.81e-135 EMBL CAA34751 "unnamed protein product [Saccharomyces cerevisiae]" 100.00 240 100.00 100.00 1.81e-135 EMBL CAG60477 "unnamed protein product [Candida glabrata]" 94.27 233 99.45 99.45 9.38e-127 EMBL CAY79336 "Spt15p [Saccharomyces cerevisiae EC1118]" 100.00 240 100.00 100.00 1.81e-135 EMBL CCD25155 "hypothetical protein NDAI_0E03380 [Naumovozyma dairenensis CBS 421]" 98.44 264 97.88 97.88 5.85e-131 EMBL CCE61293 "hypothetical protein TPHA_0A02110 [Tetrapisispora phaffii CBS 4417]" 94.79 244 98.35 99.45 4.04e-127 GB AAA34458 "TATA box factor [Saccharomyces cerevisiae]" 100.00 240 100.00 100.00 1.81e-135 GB AAA35146 "tata-box factor protein [Saccharomyces cerevisiae]" 100.00 240 99.48 99.48 7.56e-135 GB AAA35147 "TATA-binding protein [Saccharomyces cerevisiae]" 100.00 240 100.00 100.00 1.81e-135 GB AAB64675 "Spt15p: TATA-box binding protein tfIId [Saccharomyces cerevisiae]" 100.00 240 100.00 100.00 1.81e-135 GB AEP68354 "TATA-binding protein [Saccharomyces cerevisiae]" 100.00 240 100.00 100.00 1.81e-135 PRF 1515352A "transcription initiation factor TFIID" 100.00 240 100.00 100.00 1.81e-135 REF NP_011075 "TATA-binding protein [Saccharomyces cerevisiae S288c]" 100.00 240 100.00 100.00 1.81e-135 REF XP_001646300 "hypothetical protein Kpol_1032p36 [Vanderwaltozyma polyspora DSM 70294]" 98.44 251 97.35 97.88 3.99e-130 REF XP_003670398 "hypothetical protein NDAI_0E03380 [Naumovozyma dairenensis CBS 421]" 98.44 264 97.88 97.88 5.85e-131 REF XP_003683727 "hypothetical protein TPHA_0A02110 [Tetrapisispora phaffii CBS 4417]" 94.79 244 98.35 99.45 4.04e-127 REF XP_003955666 "hypothetical protein KAFR_0B02330 [Kazachstania africana CBS 2517]" 97.40 230 97.33 98.93 8.50e-129 SP P13393 "RecName: Full=TATA-box-binding protein; AltName: Full=TATA sequence-binding protein; Short=TBP; AltName: Full=TATA-binding fact" 100.00 240 100.00 100.00 1.81e-135 TPG DAA07809 "TPA: TATA-binding protein [Saccharomyces cerevisiae S288c]" 100.00 240 100.00 100.00 1.81e-135 stop_ save_ save_yTBPc _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common yTBPc _Molecular_mass . _Mol_thiol_state 'all free' _Details . _Residue_count 192 _Mol_residue_sequence ; AAPESEKDTSATSGIVPTLQ NIVATVTLGCRLDLKTVALH ARNAEYNPKRFAAVIMRIRE PKTTALIFASGKMVVTGAKS EDDSKLASRKYARIIQKIGF AAKFTDFKIQNIVGSCDVKF PIRLEGLAFSHGTFSSYEPE LFPGLIYRMVKPKIVLLIFV SGKIVLTGAKQREEIYQAFE AIYPVLSEFRKM ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ALA 3 PRO 4 GLU 5 SER 6 GLU 7 LYS 8 ASP 9 THR 10 SER 11 ALA 12 THR 13 SER 14 GLY 15 ILE 16 VAL 17 PRO 18 THR 19 LEU 20 GLN 21 ASN 22 ILE 23 VAL 24 ALA 25 THR 26 VAL 27 THR 28 LEU 29 GLY 30 CYS 31 ARG 32 LEU 33 ASP 34 LEU 35 LYS 36 THR 37 VAL 38 ALA 39 LEU 40 HIS 41 ALA 42 ARG 43 ASN 44 ALA 45 GLU 46 TYR 47 ASN 48 PRO 49 LYS 50 ARG 51 PHE 52 ALA 53 ALA 54 VAL 55 ILE 56 MET 57 ARG 58 ILE 59 ARG 60 GLU 61 PRO 62 LYS 63 THR 64 THR 65 ALA 66 LEU 67 ILE 68 PHE 69 ALA 70 SER 71 GLY 72 LYS 73 MET 74 VAL 75 VAL 76 THR 77 GLY 78 ALA 79 LYS 80 SER 81 GLU 82 ASP 83 ASP 84 SER 85 LYS 86 LEU 87 ALA 88 SER 89 ARG 90 LYS 91 TYR 92 ALA 93 ARG 94 ILE 95 ILE 96 GLN 97 LYS 98 ILE 99 GLY 100 PHE 101 ALA 102 ALA 103 LYS 104 PHE 105 THR 106 ASP 107 PHE 108 LYS 109 ILE 110 GLN 111 ASN 112 ILE 113 VAL 114 GLY 115 SER 116 CYS 117 ASP 118 VAL 119 LYS 120 PHE 121 PRO 122 ILE 123 ARG 124 LEU 125 GLU 126 GLY 127 LEU 128 ALA 129 PHE 130 SER 131 HIS 132 GLY 133 THR 134 PHE 135 SER 136 SER 137 TYR 138 GLU 139 PRO 140 GLU 141 LEU 142 PHE 143 PRO 144 GLY 145 LEU 146 ILE 147 TYR 148 ARG 149 MET 150 VAL 151 LYS 152 PRO 153 LYS 154 ILE 155 VAL 156 LEU 157 LEU 158 ILE 159 PHE 160 VAL 161 SER 162 GLY 163 LYS 164 ILE 165 VAL 166 LEU 167 THR 168 GLY 169 ALA 170 LYS 171 GLN 172 ARG 173 GLU 174 GLU 175 ILE 176 TYR 177 GLN 178 ALA 179 PHE 180 GLU 181 ALA 182 ILE 183 TYR 184 PRO 185 VAL 186 LEU 187 SER 188 GLU 189 PHE 190 ARG 191 LYS 192 MET stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $yTAF1c 'Saccharomyces Cerevisiae' 4932 Eukaryota Fungi Saccharomyces cerevisiae $yTBPc 'Saccharomyces Cerevisiae' 4932 Eukaryota Fungi Saccharomyces cerevisiae 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 $yTAF1c 'recombinant technology' . . . . . $yTBPc 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $yTAF1c . mM . $yTBPc . mM . 'Tris buffer' 20 mM . stop_ save_ ############################# # NMR applied experiments # ############################# save_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _Sample_label . save_ save_HNCACA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACA _Sample_label . save_ save_CBCACONNH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONNH _Sample_label . save_ save_HCCTOCSYNNH_4 _Saveframe_category NMR_applied_experiment _Experiment_name HCCTOCSYNNH _Sample_label . save_ ####################### # Sample conditions # ####################### save_20_mM_Tris_buffer _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 0.2 pH temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 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_ytafc-STARch.txt_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $20_mM_Tris_buffer _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name yTAF1c _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 11 2 ASN H H 8.89 0.05 . 2 11 2 ASN CA C 51.56 0.4 . 3 11 2 ASN CB C 37.3 0.4 . 4 11 2 ASN N N 123.85 0.3 . 5 12 3 LEU H H 8.44 0.05 . 6 12 3 LEU CA C 54.71 0.4 . 7 12 3 LEU CB C 39.78 0.4 . 8 12 3 LEU N N 122.38 0.3 . 9 13 4 ALA H H 7.69 0.05 . 10 13 4 ALA CA C 52.26 0.4 . 11 13 4 ALA CB C 18.09 0.4 . 12 13 4 ALA N N 119.04 0.3 . 13 14 5 ASN H H 7.83 0.05 . 14 14 5 ASN CA C 51.5 0.4 . 15 14 5 ASN CB C 39.24 0.4 . 16 14 5 ASN N N 119.42 0.3 . 17 16 7 ASP H H 8.35 0.05 . 18 16 7 ASP CA C 56.8 0.4 . 19 16 7 ASP CB C 39.08 0.4 . 20 16 7 ASP N N 116.92 0.3 . 21 17 8 GLU H H 7.73 0.05 . 22 17 8 GLU CA C 58.62 0.4 . 23 17 8 GLU CB C 29.09 0.4 . 24 17 8 GLU N N 119.55 0.3 . 25 18 9 ALA H H 8.37 0.05 . 26 18 9 ALA CA C 54.78 0.4 . 27 18 9 ALA CB C 17.24 0.4 . 28 18 9 ALA N N 123.28 0.3 . 29 19 10 TYR H H 8.28 0.05 . 30 19 10 TYR CA C 61.63 0.4 . 31 19 10 TYR CB C 37.92 0.4 . 32 19 10 TYR N N 117.11 0.3 . 33 20 11 GLU H H 7.62 0.05 . 34 20 11 GLU CA C 57.69 0.4 . 35 20 11 GLU CB C 28.63 0.4 . 36 20 11 GLU N N 114.61 0.3 . 37 21 12 ALA H H 7.89 0.05 . 38 21 12 ALA CA C 54.08 0.4 . 39 21 12 ALA CB C 17.16 0.4 . 40 21 12 ALA N N 121.8 0.3 . 41 23 14 PHE H H 6.52 0.05 . 42 23 14 PHE CA C 57.59 0.4 . 43 23 14 PHE CB C 39.63 0.4 . 44 23 14 PHE N N 111.78 0.3 . 45 24 15 GLY H H 8 0.05 . 46 24 15 GLY CA C 44.82 0.4 . 47 24 15 GLY N N 109.98 0.3 . 48 25 16 GLY H H 8.18 0.05 . 49 25 16 GLY CA C 43.98 0.4 . 50 25 16 GLY N N 107.03 0.3 . 51 26 17 GLU H H 8.66 0.05 . 52 26 17 GLU CA C 58.39 0.4 . 53 26 17 GLU CB C 28.63 0.4 . 54 26 17 GLU N N 121.48 0.3 . 55 27 18 PHE H H 8.76 0.05 . 56 27 18 PHE CA C 54.51 0.4 . 57 27 18 PHE CB C 38.85 0.4 . 58 27 18 PHE N N 114.29 0.3 . 59 28 19 GLY H H 7.65 0.05 . 60 28 19 GLY CA C 46.3 0.4 . 61 28 19 GLY N N 111.85 0.3 . 62 30 21 LEU H H 7.57 0.05 . 63 30 21 LEU CA C 57.93 0.4 . 64 30 21 LEU CB C 41.72 0.4 . 65 30 21 LEU N N 124.62 0.3 . 66 31 22 GLU H H 7.79 0.05 . 67 31 22 GLU CA C 55.01 0.4 . 68 31 22 GLU CB C 28.32 0.4 . 69 31 22 GLU N N 114.03 0.3 . 70 32 23 ILE H H 7.32 0.05 . 71 32 23 ILE CA C 64.32 0.4 . 72 32 23 ILE CB C 37.53 0.4 . 73 32 23 ILE N N 121.03 0.3 . 74 33 24 GLY H H 8.71 0.05 . 75 33 24 GLY CA C 45.73 0.4 . 76 33 24 GLY N N 108.96 0.3 . 77 34 25 SER H H 8.04 0.05 . 78 34 25 SER CA C 60.04 0.4 . 79 34 25 SER CB C 62.48 0.4 . 80 34 25 SER N N 116.6 0.3 . 81 35 26 TYR H H 7.56 0.05 . 82 35 26 TYR CA C 58.68 0.4 . 83 35 26 TYR CB C 37.92 0.4 . 84 35 26 TYR N N 118.78 0.3 . 85 36 27 ILE H H 6.94 0.05 . 86 36 27 ILE CA C 61.2 0.4 . 87 36 27 ILE CB C 37.61 0.4 . 88 36 27 ILE N N 111.97 0.3 . 89 37 28 GLY H H 7.8 0.05 . 90 37 28 GLY CA C 44.77 0.4 . 91 37 28 GLY N N 109.15 0.3 . 92 38 29 GLY H H 8.2 0.05 . 93 38 29 GLY CA C 44.57 0.4 . 94 38 29 GLY N N 108.83 0.3 . 95 39 30 ASP H H 8.42 0.05 . 96 39 30 ASP CA C 53.98 0.4 . 97 39 30 ASP CB C 40.63 0.4 . 98 39 30 ASP N N 120.9 0.3 . 99 40 31 GLU H H 8.52 0.05 . 100 40 31 GLU CA C 56.47 0.4 . 101 40 31 GLU CB C 28.78 0.4 . 102 40 31 GLU N N 120.71 0.3 . 103 41 32 GLY H H 8.3 0.05 . 104 41 32 GLY CA C 44.84 0.4 . 105 41 32 GLY N N 109.6 0.3 . 106 42 33 ALA H H 8.12 0.05 . 107 42 33 ALA CA C 52.26 0.4 . 108 42 33 ALA CB C 18.25 0.4 . 109 42 33 ALA N N 123.66 0.3 . 110 44 35 SER H H 8.02 0.05 . 111 44 35 SER CA C 59.56 0.4 . 112 44 35 SER CB C 64.26 0.4 . 113 44 35 SER N N 123.4 0.3 . 114 45 36 LYS H H 8.31 0.05 . 115 45 36 LYS CA C 55.77 0.4 . 116 45 36 LYS CB C 31.72 0.4 . 117 45 36 LYS N N 122.83 0.3 . 118 47 38 TYR H H 8.18 0.05 . 119 47 38 TYR CA C 55.84 0.4 . 120 47 38 TYR CB C 40.94 0.4 . 121 47 38 TYR N N 120.96 0.3 . 122 48 39 THR H H 8.29 0.05 . 123 48 39 THR CA C 62.79 0.4 . 124 48 39 THR CB C 69.11 0.4 . 125 48 39 THR N N 121.2 0.3 . 126 49 40 GLU H H 8.47 0.05 . 127 49 40 GLU CA C 55.84 0.4 . 128 49 40 GLU CB C 29.25 0.4 . 129 49 40 GLU N N 127.64 0.3 . 130 50 41 HIS H H 8.34 0.05 . 131 50 41 HIS CA C 52.36 0.4 . 132 50 41 HIS CB C 30.25 0.4 . 133 50 41 HIS N N 118.46 0.3 . 134 51 42 LEU H H 9.05 0.05 . 135 51 42 LEU CA C 53.62 0.4 . 136 51 42 LEU CB C 39.55 0.4 . 137 51 42 LEU N N 123.85 0.3 . 138 53 44 ASP H H 8.08 0.05 . 139 53 44 ASP CA C 51.93 0.4 . 140 53 44 ASP CB C 38.85 0.4 . 141 53 44 ASP N N 112.94 0.3 . 142 54 45 ALA H H 7.49 0.05 . 143 54 45 ALA CA C 52.52 0.4 . 144 54 45 ALA CB C 19.19 0.4 . 145 54 45 ALA N N 122.38 0.3 . 146 55 46 VAL H H 8.04 0.05 . 147 55 46 VAL CA C 60.61 0.4 . 148 55 46 VAL CB C 33.82 0.4 . 149 55 46 VAL N N 122.63 0.3 . 150 56 47 ASP H H 8.67 0.05 . 151 56 47 ASP CA C 52.86 0.4 . 152 56 47 ASP CB C 40.4 0.4 . 153 56 47 ASP N N 124.75 0.3 . 154 57 48 PHE H H 7.14 0.05 . 155 57 48 PHE CA C 58.22 0.4 . 156 57 48 PHE CB C 38.54 0.4 . 157 57 48 PHE N N 125.01 0.3 . 158 58 49 GLU H H 8.62 0.05 . 159 58 49 GLU CA C 56.33 0.4 . 160 58 49 GLU CB C 29.09 0.4 . 161 58 49 GLU N N 120.26 0.3 . 162 59 50 ASP H H 8.16 0.05 . 163 59 50 ASP CA C 52.72 0.4 . 164 59 50 ASP CB C 40.01 0.4 . 165 59 50 ASP N N 117.69 0.3 . 166 60 51 GLU H H 7.45 0.05 . 167 60 51 GLU CA C 57.75 0.4 . 168 60 51 GLU CB C 30.25 0.4 . 169 60 51 GLU N N 121.73 0.3 . 170 61 52 ASP H H 8.38 0.05 . 171 61 52 ASP CA C 53.09 0.4 . 172 61 52 ASP CB C 41.87 0.4 . 173 61 52 ASP N N 123.79 0.3 . 174 62 53 GLU H H 9.81 0.05 . 175 62 53 GLU CA C 55.97 0.4 . 176 62 53 GLU CB C 31.1 0.4 . 177 62 53 GLU N N 124.43 0.3 . 178 63 54 LEU H H 7.9 0.05 . 179 63 54 LEU CA C 51.93 0.4 . 180 63 54 LEU CB C 42.96 0.4 . 181 63 54 LEU N N 112.94 0.3 . 182 64 55 ALA H H 7.49 0.05 . 183 64 55 ALA CA C 51.1 0.4 . 184 64 55 ALA CB C 18.87 0.4 . 185 64 55 ALA N N 125.07 0.3 . 186 65 56 ASP H H 8.83 0.05 . 187 65 56 ASP CA C 54.78 0.4 . 188 65 56 ASP CB C 40.17 0.4 . 189 65 56 ASP N N 123.28 0.3 . 190 66 57 ASP H H 8.57 0.05 . 191 66 57 ASP CA C 52.22 0.4 . 192 66 57 ASP CB C 40.25 0.4 . 193 66 57 ASP N N 120.64 0.3 . 194 67 58 ASP H H 8.54 0.05 . 195 67 58 ASP CA C 54.61 0.4 . 196 67 58 ASP CB C 40.55 0.4 . 197 67 58 ASP N N 123.98 0.3 . 198 68 59 ASP H H 8.46 0.05 . 199 68 59 ASP CA C 54.35 0.4 . 200 68 59 ASP CB C 40.63 0.4 . 201 68 59 ASP N N 120.84 0.3 . 202 69 60 ASP H H 8.1 0.05 . 203 69 60 ASP CA C 53.42 0.4 . 204 69 60 ASP CB C 40.71 0.4 . 205 69 60 ASP N N 120.51 0.3 . 206 70 61 LEU H H 8.02 0.05 . 207 70 61 LEU CA C 52.53 0.4 . 208 70 61 LEU CB C 40.71 0.4 . 209 70 61 LEU N N 123.42 0.3 . 210 72 63 GLU H H 8.68 0.05 . 211 72 63 GLU CA C 56.432 0.4 . 212 72 63 GLU CB C 29.01 0.4 . 213 72 63 GLU N N 120 0.3 . 214 73 64 GLU H H 8.34 0.05 . 215 73 64 GLU CA C 52.59 0.4 . 216 73 64 GLU CB C 38.23 0.4 . 217 73 64 GLU N N 119.74 0.3 . stop_ save_ save_ytafc-STARch.txt_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $20_mM_Tris_buffer _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name yTBPc _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 52 4 GLU H H 8.63 0.05 . 2 52 4 GLU CA C 56.35 0.4 . 3 52 4 GLU CB C 29.10 0.4 . 4 52 4 GLU N N 121.20 0.3 . 5 53 5 SER H H 8.26 0.05 . 6 53 5 SER CA C 58.00 0.4 . 7 53 5 SER CB C 63.37 0.4 . 8 53 5 SER N N 116.35 0.3 . 9 54 6 GLU H H 8.39 0.05 . 10 54 6 GLU CA C 56.08 0.4 . 11 54 6 GLU CB C 29.25 0.4 . 12 54 6 GLU N N 122.89 0.3 . 13 55 7 LYS H H 8.19 0.05 . 14 55 7 LYS CA C 55.76 0.4 . 15 55 7 LYS CB C 32.08 0.4 . 16 55 7 LYS N N 122.16 0.3 . 17 56 8 ASP H H 8.38 0.05 . 18 56 8 ASP CA C 53.75 0.4 . 19 56 8 ASP CB C 40.53 0.4 . 20 56 8 ASP N N 121.99 0.3 . 21 57 9 THR H H 8.21 0.05 . 22 57 9 THR CA C 61.08 0.4 . 23 57 9 THR CB C 68.58 0.4 . 24 57 9 THR N N 115.38 0.3 . 25 58 10 SER H H 8.45 0.05 . 26 58 10 SER CA C 58.80 0.4 . 27 58 10 SER CB C 63.33 0.4 . 28 58 10 SER N N 119.02 0.3 . 29 59 11 ALA H H 8.41 0.05 . 30 59 11 ALA CA C 52.55 0.4 . 31 59 11 ALA CB C 18.48 0.4 . 32 59 11 ALA N N 126.04 0.3 . 33 60 12 THR H H 7.92 0.05 . 34 60 12 THR CA C 60.55 0.4 . 35 60 12 THR CB C 68.58 0.4 . 36 60 12 THR N N 111.02 0.3 . 37 62 14 GLY H H 8.22 0.05 . 38 62 14 GLY CA C 44.60 0.4 . 39 62 14 GLY N N 109.33 0.3 . 40 63 15 ILE H H 7.96 0.05 . 41 63 15 ILE CA C 60.27 0.4 . 42 63 15 ILE CB C 37.59 0.4 . 43 63 15 ILE N N 122.41 0.3 . 44 64 16 VAL H H 7.98 0.05 . 45 64 16 VAL CA C 57.85 0.4 . 46 64 16 VAL CB C 33.51 0.4 . 47 64 16 VAL N N 124.59 0.3 . 48 65 17 PRO CA C 62.17 0.4 . 49 65 17 PRO CB C 31.35 0.4 . 50 66 18 THR H H 8.74 0.05 . 51 66 18 THR CA C 60.09 0.4 . 52 66 18 THR CB C 70.20 0.4 . 53 66 18 THR N N 116.59 0.3 . 54 67 19 LEU H H 8.85 0.05 . 55 67 19 LEU CA C 55.26 0.4 . 56 67 19 LEU CB C 38.83 0.4 . 57 67 19 LEU N N 124.34 0.3 . 58 68 20 GLN H H 9.43 0.05 . 59 68 20 GLN CA C 55.28 0.4 . 60 68 20 GLN CB C 30.17 0.4 . 61 68 20 GLN N N 122.95 0.3 . 62 69 21 ASN H H 7.65 0.05 . 63 69 21 ASN CA C 53.56 0.4 . 64 69 21 ASN CB C 40.66 0.4 . 65 69 21 ASN N N 112.72 0.3 . 66 70 22 ILE H H 7.87 0.05 . 67 70 22 ILE CA C 60.04 0.4 . 68 70 22 ILE CB C 40.26 0.4 . 69 70 22 ILE N N 124.83 0.3 . 70 71 23 VAL H H 9.31 0.05 . 71 71 23 VAL CA C 60.87 0.4 . 72 71 23 VAL CB C 32.93 0.4 . 73 71 23 VAL N N 128.95 0.3 . 74 72 24 ALA H H 9.34 0.05 . 75 72 24 ALA CA C 49.90 0.4 . 76 72 24 ALA CB C 23.98 0.4 . 77 72 24 ALA N N 131.37 0.3 . 78 73 25 THR H H 9.08 0.05 . 79 73 25 THR CA C 58.88 0.4 . 80 73 25 THR CB C 70.11 0.4 . 81 73 25 THR N N 110.54 0.3 . 82 74 26 VAL H H 8.38 0.05 . 83 74 26 VAL CA C 60.36 0.4 . 84 74 26 VAL CB C 37.12 0.4 . 85 74 26 VAL N N 118.05 0.3 . 86 75 27 THR H H 8.35 0.05 . 87 75 27 THR CA C 61.08 0.4 . 88 75 27 THR CB C 68.83 0.4 . 89 75 27 THR N N 123.13 0.3 . 90 76 28 LEU H H 8.87 0.05 . 91 76 28 LEU CA C 54.60 0.4 . 92 76 28 LEU CB C 40.82 0.4 . 93 76 28 LEU N N 125.31 0.3 . 94 77 29 GLY H H 7.71 0.05 . 95 77 29 GLY CA C 45.86 0.4 . 96 77 29 GLY N N 104.67 0.3 . 97 78 30 CYS H H 7.35 0.05 . 98 78 30 CYS CA C 53.55 0.4 . 99 78 30 CYS CB C 30.41 0.4 . 100 78 30 CYS N N 114.17 0.3 . 101 79 31 ARG H H 7.98 0.05 . 102 79 31 ARG CA C 54.88 0.4 . 103 79 31 ARG CB C 29.17 0.4 . 104 79 31 ARG N N 118.05 0.3 . 105 80 32 LEU H H 8.96 0.05 . 106 80 32 LEU CA C 52.47 0.4 . 107 80 32 LEU CB C 44.39 0.4 . 108 80 32 LEU N N 121.68 0.3 . 109 81 33 ASP H H 5.64 0.05 . 110 81 33 ASP CA C 52.34 0.4 . 111 81 33 ASP CB C 40.86 0.4 . 112 81 33 ASP N N 120.47 0.3 . 113 82 34 LEU H H 8.56 0.05 . 114 82 34 LEU CA C 57.01 0.4 . 115 82 34 LEU CB C 37.47 0.4 . 116 82 34 LEU N N 126.04 0.3 . 117 83 35 LYS H H 8.25 0.05 . 118 83 35 LYS CA C 58.57 0.4 . 119 83 35 LYS CB C 30.81 0.4 . 120 83 35 LYS N N 118.29 0.3 . 121 84 36 THR H H 7.60 0.05 . 122 84 36 THR CA C 67.05 0.4 . 123 84 36 THR CB C 67.70 0.4 . 124 84 36 THR N N 115.87 0.3 . 125 85 37 VAL H H 7.66 0.05 . 126 85 37 VAL CA C 66.56 0.4 . 127 85 37 VAL CB C 30.21 0.4 . 128 85 37 VAL N N 119.98 0.3 . 129 86 38 ALA H H 8.00 0.05 . 130 86 38 ALA CA C 54.22 0.4 . 131 86 38 ALA CB C 18.30 0.4 . 132 86 38 ALA N N 117.81 0.3 . 133 87 39 LEU H H 8.75 0.05 . 134 87 39 LEU CA C 57.21 0.4 . 135 87 39 LEU CB C 41.73 0.4 . 136 87 39 LEU N N 116.84 0.3 . 137 88 40 HIS H H 7.62 0.05 . 138 88 40 HIS CA C 58.27 0.4 . 139 88 40 HIS CB C 31.15 0.4 . 140 88 40 HIS N N 112.72 0.3 . 141 89 41 ALA H H 7.79 0.05 . 142 89 41 ALA CA C 49.80 0.4 . 143 89 41 ALA CB C 19.48 0.4 . 144 89 41 ALA N N 123.62 0.3 . 145 90 42 ARG H H 8.82 0.05 . 146 90 42 ARG CA C 57.44 0.4 . 147 90 42 ARG CB C 28.96 0.4 . 148 90 42 ARG N N 121.20 0.3 . 149 91 43 ASN H H 9.23 0.05 . 150 91 43 ASN CA C 52.72 0.4 . 151 91 43 ASN CB C 35.05 0.4 . 152 91 43 ASN N N 111.75 0.3 . 153 92 44 ALA H H 7.52 0.05 . 154 92 44 ALA CA C 49.91 0.4 . 155 92 44 ALA CB C 22.13 0.4 . 156 92 44 ALA N N 122.65 0.3 . 157 93 45 GLU H H 9.47 0.05 . 158 93 45 GLU CA C 53.54 0.4 . 159 93 45 GLU CB C 31.81 0.4 . 160 93 45 GLU N N 120.95 0.3 . 161 94 46 TYR H H 9.07 0.05 . 162 94 46 TYR CA C 55.80 0.4 . 163 94 46 TYR CB C 40.98 0.4 . 164 94 46 TYR N N 123.38 0.3 . 165 95 47 ASN H H 9.26 0.05 . 166 95 47 ASN CA C 49.14 0.4 . 167 95 47 ASN CB C 37.82 0.4 . 168 95 47 ASN N N 126.52 0.3 . 169 96 48 PRO CA C 62.67 0.4 . 170 96 48 PRO CB C 31.04 0.4 . 171 97 49 LYS H H 7.60 0.05 . 172 97 49 LYS CA C 57.00 0.4 . 173 97 49 LYS CB C 30.21 0.4 . 174 97 49 LYS N N 116.11 0.3 . 175 98 50 ARG H H 7.24 0.05 . 176 98 50 ARG CA C 56.02 0.4 . 177 98 50 ARG CB C 31.59 0.4 . 178 98 50 ARG N N 117.81 0.3 . 179 99 51 PHE H H 7.96 0.05 . 180 99 51 PHE CA C 57.62 0.4 . 181 99 51 PHE CB C 41.62 0.4 . 182 99 51 PHE N N 116.84 0.3 . 183 100 52 ALA H H 7.43 0.05 . 184 100 52 ALA CA C 51.86 0.4 . 185 100 52 ALA CB C 16.84 0.4 . 186 100 52 ALA N N 131.13 0.3 . 187 101 53 ALA H H 7.44 0.05 . 188 101 53 ALA CA C 51.32 0.4 . 189 101 53 ALA CB C 19.63 0.4 . 190 101 53 ALA N N 119.02 0.3 . 191 102 54 VAL H H 8.58 0.05 . 192 102 54 VAL CA C 61.41 0.4 . 193 102 54 VAL CB C 32.07 0.4 . 194 102 54 VAL N N 120.71 0.3 . 195 103 55 ILE H H 9.09 0.05 . 196 103 55 ILE CA C 59.25 0.4 . 197 103 55 ILE CB C 37.78 0.4 . 198 103 55 ILE N N 129.19 0.3 . 199 104 56 MET H H 9.61 0.05 . 200 104 56 MET CA C 53.57 0.4 . 201 104 56 MET CB C 37.21 0.4 . 202 104 56 MET N N 129.19 0.3 . 203 105 57 ARG H H 7.44 0.05 . 204 105 57 ARG CA C 55.19 0.4 . 205 105 57 ARG CB C 33.01 0.4 . 206 105 57 ARG N N 121.44 0.3 . 207 106 58 ILE H H 7.35 0.05 . 208 106 58 ILE CA C 59.29 0.4 . 209 106 58 ILE CB C 40.98 0.4 . 210 106 58 ILE N N 114.66 0.3 . 211 107 59 ARG H H 8.38 0.05 . 212 107 59 ARG CA C 57.55 0.4 . 213 107 59 ARG CB C 30.78 0.4 . 214 107 59 ARG N N 119.50 0.3 . 215 108 60 GLU H H 7.88 0.05 . 216 108 60 GLU CA C 51.94 0.4 . 217 108 60 GLU CB C 32.06 0.4 . 218 108 60 GLU N N 117.08 0.3 . 219 109 61 PRO CA C 61.79 0.4 . 220 109 61 PRO CB C 32.58 0.4 . 221 110 62 LYS H H 8.64 0.05 . 222 110 62 LYS CA C 57.97 0.4 . 223 110 62 LYS CB C 30.22 0.4 . 224 110 62 LYS N N 127.25 0.3 . 225 111 63 THR H H 7.74 0.05 . 226 111 63 THR CA C 59.45 0.4 . 227 111 63 THR CB C 15.57 0.4 . 228 111 63 THR N N 119.50 0.3 . 229 112 64 THR H H 8.85 0.05 . 230 112 64 THR CA C 61.97 0.4 . 231 112 64 THR CB C 71.00 0.4 . 232 112 64 THR N N 115.87 0.3 . 233 113 65 ALA H H 9.53 0.05 . 234 113 65 ALA CA C 48.75 0.4 . 235 113 65 ALA CB C 19.25 0.4 . 236 113 65 ALA N N 127.74 0.3 . 237 114 66 LEU H H 9.33 0.05 . 238 114 66 LEU CA C 53.00 0.4 . 239 114 66 LEU CB C 42.12 0.4 . 240 114 66 LEU N N 120.47 0.3 . 241 115 67 ILE H H 9.25 0.05 . 242 115 67 ILE CA C 60.68 0.4 . 243 115 67 ILE CB C 39.11 0.4 . 244 115 67 ILE N N 124.34 0.3 . 245 116 68 PHE H H 8.58 0.05 . 246 116 68 PHE CA C 57.31 0.4 . 247 116 68 PHE CB C 39.18 0.4 . 248 116 68 PHE N N 124.59 0.3 . 249 117 69 ALA H H 9.63 0.05 . 250 117 69 ALA CA C 54.58 0.4 . 251 117 69 ALA CB C 17.85 0.4 . 252 117 69 ALA N N 125.56 0.3 . 253 118 70 SER H H 8.41 0.05 . 254 118 70 SER CA C 58.59 0.4 . 255 118 70 SER CB C 62.71 0.4 . 256 118 70 SER N N 109.57 0.3 . 257 119 71 GLY H H 8.47 0.05 . 258 119 71 GLY CA C 44.96 0.4 . 259 119 71 GLY N N 111.02 0.3 . 260 120 72 LYS H H 7.20 0.05 . 261 120 72 LYS CA C 56.37 0.4 . 262 120 72 LYS CB C 32.07 0.4 . 263 120 72 LYS N N 119.98 0.3 . 264 121 73 MET H H 8.99 0.05 . 265 121 73 MET CA C 53.56 0.4 . 266 121 73 MET CB C 37.28 0.4 . 267 121 73 MET N N 120.71 0.3 . 268 122 74 VAL H H 9.37 0.05 . 269 122 74 VAL CA C 60.09 0.4 . 270 122 74 VAL CB C 34.00 0.4 . 271 122 74 VAL N N 127.49 0.3 . 272 123 75 VAL H H 9.58 0.05 . 273 123 75 VAL CA C 61.09 0.4 . 274 123 75 VAL CB C 33.96 0.4 . 275 123 75 VAL N N 127.49 0.3 . 276 124 76 THR H H 9.61 0.05 . 277 124 76 THR CA C 58.72 0.4 . 278 124 76 THR CB C 71.11 0.4 . 279 124 76 THR N N 124.34 0.3 . 280 125 77 GLY H H 8.89 0.05 . 281 125 77 GLY CA C 44.90 0.4 . 282 125 77 GLY N N 115.63 0.3 . 283 126 78 ALA H H 7.19 0.05 . 284 126 78 ALA CA C 50.83 0.4 . 285 126 78 ALA CB C 19.05 0.4 . 286 126 78 ALA N N 121.20 0.3 . 287 127 79 LYS H H 9.31 0.05 . 288 127 79 LYS CA C 54.36 0.4 . 289 127 79 LYS CB C 31.69 0.4 . 290 127 79 LYS N N 114.41 0.3 . 291 128 80 SER H H 7.43 0.05 . 292 128 80 SER CA C 56.20 0.4 . 293 128 80 SER CB C 66.35 0.4 . 294 128 80 SER N N 110.05 0.3 . 295 131 83 ASP H H 7.94 0.05 . 296 131 83 ASP CA C 56.41 0.4 . 297 131 83 ASP CB C 39.56 0.4 . 298 131 83 ASP N N 121.68 0.3 . 299 132 84 SER H H 8.08 0.05 . 300 132 84 SER CA C 62.06 0.4 . 301 132 84 SER CB C 63.09 0.4 . 302 132 84 SER N N 115.87 0.3 . 303 133 85 LYS H H 7.72 0.05 . 304 133 85 LYS CA C 59.56 0.4 . 305 133 85 LYS CB C 30.93 0.4 . 306 133 85 LYS N N 123.13 0.3 . 307 134 86 LEU H H 8.11 0.05 . 308 134 86 LEU CA C 58.03 0.4 . 309 134 86 LEU CB C 41.43 0.4 . 310 134 86 LEU N N 120.71 0.3 . 311 135 87 ALA H H 8.58 0.05 . 312 135 87 ALA CA C 54.58 0.4 . 313 135 87 ALA CB C 18.36 0.4 . 314 135 87 ALA N N 117.56 0.3 . 315 136 88 SER H H 7.99 0.05 . 316 136 88 SER CA C 63.73 0.4 . 317 136 88 SER CB C 63.08 0.4 . 318 136 88 SER N N 112.23 0.3 . 319 137 89 ARG H H 8.06 0.05 . 320 137 89 ARG CA C 59.26 0.4 . 321 137 89 ARG CB C 30.42 0.4 . 322 137 89 ARG N N 120.47 0.3 . 323 138 90 LYS H H 7.93 0.05 . 324 138 90 LYS CA C 59.65 0.4 . 325 138 90 LYS CB C 32.10 0.4 . 326 138 90 LYS N N 124.83 0.3 . 327 139 91 TYR H H 8.37 0.05 . 328 139 91 TYR CA C 62.52 0.4 . 329 139 91 TYR CB C 38.29 0.4 . 330 139 91 TYR N N 117.08 0.3 . 331 140 92 ALA H H 7.92 0.05 . 332 140 92 ALA CA C 54.65 0.4 . 333 140 92 ALA CB C 17.18 0.4 . 334 140 92 ALA N N 116.84 0.3 . 335 141 93 ARG H H 7.28 0.05 . 336 141 93 ARG CA C 56.40 0.4 . 337 141 93 ARG CB C 27.68 0.4 . 338 141 93 ARG N N 118.05 0.3 . 339 142 94 ILE H H 8.28 0.05 . 340 142 94 ILE CA C 65.37 0.4 . 341 142 94 ILE CB C 36.31 0.4 . 342 142 94 ILE N N 121.44 0.3 . 343 143 95 ILE H H 7.47 0.05 . 344 143 95 ILE CA C 62.08 0.4 . 345 143 95 ILE CB C 34.40 0.4 . 346 143 95 ILE N N 116.59 0.3 . 347 144 96 GLN H H 7.75 0.05 . 348 144 96 GLN CA C 57.45 0.4 . 349 144 96 GLN CB C 26.72 0.4 . 350 144 96 GLN N N 118.77 0.3 . 351 145 97 LYS H H 8.63 0.05 . 352 145 97 LYS CA C 59.70 0.4 . 353 145 97 LYS CB C 32.07 0.4 . 354 145 97 LYS N N 121.92 0.3 . 355 146 98 ILE H H 8.05 0.05 . 356 146 98 ILE CA C 63.09 0.4 . 357 146 98 ILE CB C 37.73 0.4 . 358 146 98 ILE N N 119.74 0.3 . 359 147 99 GLY H H 7.51 0.05 . 360 147 99 GLY CA C 44.27 0.4 . 361 147 99 GLY N N 104.48 0.3 . 362 148 100 PHE H H 7.39 0.05 . 363 148 100 PHE CA C 56.91 0.4 . 364 148 100 PHE CB C 39.98 0.4 . 365 148 100 PHE N N 119.02 0.3 . 366 149 101 ALA H H 9.06 0.05 . 367 149 101 ALA CA C 50.73 0.4 . 368 149 101 ALA CB C 15.60 0.4 . 369 149 101 ALA N N 130.58 0.3 . 370 150 102 ALA H H 7.95 0.05 . 371 150 102 ALA CA C 50.51 0.4 . 372 150 102 ALA CB C 21.16 0.4 . 373 150 102 ALA N N 123.86 0.3 . 374 151 103 LYS H H 9.36 0.05 . 375 151 103 LYS CA C 54.14 0.4 . 376 151 103 LYS CB C 35.20 0.4 . 377 151 103 LYS N N 123.62 0.3 . 378 152 104 PHE H H 8.80 0.05 . 379 152 104 PHE CA C 57.05 0.4 . 380 152 104 PHE CB C 38.68 0.4 . 381 152 104 PHE N N 121.20 0.3 . 382 153 105 THR H H 7.06 0.05 . 383 153 105 THR CA C 59.20 0.4 . 384 153 105 THR CB C 71.03 0.4 . 385 153 105 THR N N 118.05 0.3 . 386 154 106 ASP H H 8.86 0.05 . 387 154 106 ASP CA C 53.68 0.4 . 388 154 106 ASP CB C 39.25 0.4 . 389 154 106 ASP N N 119.74 0.3 . 390 155 107 PHE H H 8.22 0.05 . 391 155 107 PHE CA C 58.59 0.4 . 392 155 107 PHE CB C 38.70 0.4 . 393 155 107 PHE N N 118.53 0.3 . 394 156 108 LYS H H 8.41 0.05 . 395 156 108 LYS CA C 54.27 0.4 . 396 156 108 LYS CB C 34.93 0.4 . 397 156 108 LYS N N 128.95 0.3 . 398 157 109 ILE H H 8.38 0.05 . 399 157 109 ILE CA C 61.29 0.4 . 400 157 109 ILE CB C 35.39 0.4 . 401 157 109 ILE N N 122.89 0.3 . 402 158 110 GLN H H 9.39 0.05 . 403 158 110 GLN CA C 55.78 0.4 . 404 158 110 GLN CB C 28.27 0.4 . 405 158 110 GLN N N 129.67 0.3 . 406 159 111 ASN H H 7.87 0.05 . 407 159 111 ASN CA C 52.94 0.4 . 408 159 111 ASN CB C 40.28 0.4 . 409 159 111 ASN N N 114.66 0.3 . 410 160 112 ILE H H 8.28 0.05 . 411 160 112 ILE CA C 60.66 0.4 . 412 160 112 ILE CB C 39.73 0.4 . 413 160 112 ILE N N 127.74 0.3 . 414 161 113 VAL H H 8.68 0.05 . 415 161 113 VAL CA C 59.41 0.4 . 416 161 113 VAL CB C 33.51 0.4 . 417 161 113 VAL N N 124.59 0.3 . 418 162 114 GLY H H 9.77 0.05 . 419 162 114 GLY CA C 42.94 0.4 . 420 162 114 GLY N N 113.93 0.3 . 421 163 115 SER H H 9.09 0.05 . 422 163 115 SER CA C 56.41 0.4 . 423 163 115 SER CB C 66.04 0.4 . 424 163 115 SER N N 113.45 0.3 . 425 164 116 CYS H H 8.87 0.05 . 426 164 116 CYS CA C 56.41 0.4 . 427 164 116 CYS CB C 30.12 0.4 . 428 164 116 CYS N N 117.56 0.3 . 429 165 117 ASP H H 8.04 0.05 . 430 165 117 ASP CA C 51.89 0.4 . 431 165 117 ASP CB C 41.81 0.4 . 432 165 117 ASP N N 121.92 0.3 . 433 166 118 VAL H H 8.48 0.05 . 434 166 118 VAL CA C 61.42 0.4 . 435 166 118 VAL CB C 30.39 0.4 . 436 166 118 VAL N N 116.84 0.3 . 437 168 120 PHE H H 7.10 0.05 . 438 168 120 PHE CA C 53.77 0.4 . 439 168 120 PHE CB C 37.85 0.4 . 440 168 120 PHE N N 115.14 0.3 . 441 169 121 PRO CA C 60.46 0.4 . 442 169 121 PRO CB C 27.99 0.4 . 443 170 122 ILE H H 8.40 0.05 . 444 170 122 ILE CA C 59.47 0.4 . 445 170 122 ILE CB C 40.17 0.4 . 446 170 122 ILE N N 119.74 0.3 . 447 171 123 ARG H H 9.18 0.05 . 448 171 123 ARG CA C 54.22 0.4 . 449 171 123 ARG CB C 27.68 0.4 . 450 171 123 ARG N N 126.28 0.3 . 451 172 124 LEU H H 7.83 0.05 . 452 172 124 LEU CA C 57.23 0.4 . 453 172 124 LEU CB C 39.20 0.4 . 454 172 124 LEU N N 126.52 0.3 . 455 173 125 GLU H H 9.35 0.05 . 456 173 125 GLU CA C 59.06 0.4 . 457 173 125 GLU CB C 27.41 0.4 . 458 173 125 GLU N N 116.35 0.3 . 459 174 126 GLY H H 7.32 0.05 . 460 174 126 GLY CA C 46.43 0.4 . 461 174 126 GLY N N 107.09 0.3 . 462 175 127 LEU H H 7.13 0.05 . 463 175 127 LEU CA C 57.80 0.4 . 464 175 127 LEU CB C 40.55 0.4 . 465 175 127 LEU N N 127.49 0.3 . 466 176 128 ALA H H 8.22 0.05 . 467 176 128 ALA CA C 53.55 0.4 . 468 176 128 ALA CB C 17.38 0.4 . 469 176 128 ALA N N 119.50 0.3 . 470 177 129 PHE H H 7.44 0.05 . 471 177 129 PHE CA C 59.56 0.4 . 472 177 129 PHE CB C 38.66 0.4 . 473 177 129 PHE N N 114.90 0.3 . 474 178 130 SER H H 7.95 0.05 . 475 178 130 SER CA C 60.66 0.4 . 476 178 130 SER CB C 63.83 0.4 . 477 178 130 SER N N 114.41 0.3 . 478 179 131 HIS H H 8.43 0.05 . 479 179 131 HIS CA C 54.78 0.4 . 480 179 131 HIS CB C 29.19 0.4 . 481 179 131 HIS N N 121.92 0.3 . 482 180 132 GLY H H 7.68 0.05 . 483 180 132 GLY CA C 47.53 0.4 . 484 180 132 GLY N N 111.99 0.3 . 485 182 134 PHE H H 6.95 0.05 . 486 182 134 PHE CA C 56.44 0.4 . 487 182 134 PHE CB C 40.14 0.4 . 488 182 134 PHE N N 116.35 0.3 . 489 183 135 SER H H 7.31 0.05 . 490 183 135 SER CA C 57.84 0.4 . 491 183 135 SER CB C 67.20 0.4 . 492 183 135 SER N N 112.48 0.3 . 493 184 136 SER H H 9.03 0.05 . 494 184 136 SER CA C 57.00 0.4 . 495 184 136 SER CB C 64.79 0.4 . 496 184 136 SER N N 116.84 0.3 . 497 185 137 TYR H H 9.23 0.05 . 498 185 137 TYR CA C 56.02 0.4 . 499 185 137 TYR CB C 38.82 0.4 . 500 185 137 TYR N N 127.01 0.3 . 501 186 138 GLU H H 9.24 0.05 . 502 186 138 GLU CA C 52.34 0.4 . 503 186 138 GLU CB C 29.23 0.4 . 504 186 138 GLU N N 128.95 0.3 . 505 187 139 PRO CA C 63.50 0.4 . 506 187 139 PRO CB C 30.17 0.4 . 507 188 140 GLU H H 8.84 0.05 . 508 188 140 GLU CA C 57.60 0.4 . 509 188 140 GLU CB C 28.03 0.4 . 510 188 140 GLU N N 117.81 0.3 . 511 189 141 LEU H H 7.97 0.05 . 512 189 141 LEU CA C 55.19 0.4 . 513 189 141 LEU CB C 42.15 0.4 . 514 189 141 LEU N N 119.50 0.3 . 515 190 142 PHE H H 8.02 0.05 . 516 190 142 PHE CA C 54.90 0.4 . 517 190 142 PHE CB C 40.62 0.4 . 518 190 142 PHE N N 119.98 0.3 . 519 191 143 PRO CA C 63.50 0.4 . 520 191 143 PRO CB C 30.92 0.4 . 521 192 144 GLY H H 6.20 0.05 . 522 192 144 GLY CA C 43.22 0.4 . 523 192 144 GLY N N 105.65 0.3 . 524 193 145 LEU H H 9.09 0.05 . 525 193 145 LEU CA C 54.40 0.4 . 526 193 145 LEU CB C 44.39 0.4 . 527 193 145 LEU N N 124.34 0.3 . 528 194 146 ILE H H 8.94 0.05 . 529 194 146 ILE CA C 60.18 0.4 . 530 194 146 ILE CB C 38.21 0.4 . 531 194 146 ILE N N 127.49 0.3 . 532 195 147 TYR H H 10.05 0.05 . 533 195 147 TYR CA C 56.10 0.4 . 534 195 147 TYR CB C 41.07 0.4 . 535 195 147 TYR N N 133.98 0.3 . 536 196 148 ARG H H 8.92 0.05 . 537 196 148 ARG CA C 55.27 0.4 . 538 196 148 ARG CB C 28.07 0.4 . 539 196 148 ARG N N 129.65 0.3 . 540 197 149 MET H H 8.27 0.05 . 541 197 149 MET CA C 55.91 0.4 . 542 197 149 MET CB C 33.77 0.4 . 543 197 149 MET N N 125.07 0.3 . 544 198 150 VAL H H 8.03 0.05 . 545 198 150 VAL CA C 63.79 0.4 . 546 198 150 VAL CB C 31.61 0.4 . 547 198 150 VAL N N 122.16 0.3 . 548 199 151 LYS H H 7.29 0.05 . 549 199 151 LYS CA C 53.14 0.4 . 550 199 151 LYS CB C 33.97 0.4 . 551 199 151 LYS N N 119.98 0.3 . 552 200 152 PRO CA C 62.56 0.4 . 553 200 152 PRO CB C 33.01 0.4 . 554 201 153 LYS H H 8.25 0.05 . 555 201 153 LYS CA C 55.08 0.4 . 556 201 153 LYS CB C 29.71 0.4 . 557 201 153 LYS N N 120.47 0.3 . 558 202 154 ILE H H 7.62 0.05 . 559 202 154 ILE CA C 56.81 0.4 . 560 202 154 ILE CB C 40.10 0.4 . 561 202 154 ILE N N 127.98 0.3 . 562 203 155 VAL H H 8.75 0.05 . 563 203 155 VAL CA C 61.18 0.4 . 564 203 155 VAL CB C 32.15 0.4 . 565 203 155 VAL N N 126.52 0.3 . 566 204 156 LEU H H 9.65 0.05 . 567 204 156 LEU CA C 53.66 0.4 . 568 204 156 LEU CB C 42.25 0.4 . 569 204 156 LEU N N 126.52 0.3 . 570 205 157 LEU H H 9.56 0.05 . 571 205 157 LEU CA C 52.98 0.4 . 572 205 157 LEU CB C 41.16 0.4 . 573 205 157 LEU N N 123.62 0.3 . 574 206 158 ILE H H 9.13 0.05 . 575 206 158 ILE CA C 59.94 0.4 . 576 206 158 ILE CB C 38.73 0.4 . 577 206 158 ILE N N 123.38 0.3 . 578 207 159 PHE H H 8.49 0.05 . 579 207 159 PHE CA C 56.79 0.4 . 580 207 159 PHE CB C 39.68 0.4 . 581 207 159 PHE N N 124.34 0.3 . 582 208 160 VAL H H 9.35 0.05 . 583 208 160 VAL CA C 64.22 0.4 . 584 208 160 VAL CB C 31.15 0.4 . 585 208 160 VAL N N 121.20 0.3 . 586 209 161 SER H H 7.35 0.05 . 587 209 161 SER CA C 57.78 0.4 . 588 209 161 SER CB C 63.85 0.4 . 589 209 161 SER N N 109.33 0.3 . 590 210 162 GLY H H 8.22 0.05 . 591 210 162 GLY CA C 44.83 0.4 . 592 210 162 GLY N N 111.02 0.3 . 593 211 163 LYS H H 7.02 0.05 . 594 211 163 LYS CA C 56.18 0.4 . 595 211 163 LYS CB C 31.75 0.4 . 596 211 163 LYS N N 120.23 0.3 . 597 212 164 ILE H H 8.85 0.05 . 598 212 164 ILE CA C 58.22 0.4 . 599 212 164 ILE CB C 40.00 0.4 . 600 212 164 ILE N N 122.16 0.3 . 601 213 165 VAL H H 9.44 0.05 . 602 213 165 VAL CA C 60.82 0.4 . 603 213 165 VAL CB C 33.95 0.4 . 604 213 165 VAL N N 127.74 0.3 . 605 214 166 LEU H H 9.13 0.05 . 606 214 166 LEU CA C 54.77 0.4 . 607 214 166 LEU CB C 43.27 0.4 . 608 214 166 LEU N N 125.56 0.3 . 609 215 167 THR H H 9.49 0.05 . 610 215 167 THR CA C 59.76 0.4 . 611 215 167 THR CB C 70.34 0.4 . 612 215 167 THR N N 117.08 0.3 . 613 216 168 GLY H H 8.96 0.05 . 614 216 168 GLY CA C 43.92 0.4 . 615 216 168 GLY N N 114.90 0.3 . 616 217 169 ALA H H 7.26 0.05 . 617 217 169 ALA CA C 51.50 0.4 . 618 217 169 ALA CB C 20.68 0.4 . 619 217 169 ALA N N 122.41 0.3 . 620 218 170 LYS H H 8.96 0.05 . 621 218 170 LYS CA C 54.56 0.4 . 622 218 170 LYS CB C 32.54 0.4 . 623 218 170 LYS N N 115.87 0.3 . 624 219 171 GLN H H 7.56 0.05 . 625 219 171 GLN CA C 53.56 0.4 . 626 219 171 GLN CB C 31.55 0.4 . 627 219 171 GLN N N 115.38 0.3 . 628 220 172 ARG H H 9.85 0.05 . 629 220 172 ARG CA C 59.55 0.4 . 630 220 172 ARG CB C 29.24 0.4 . 631 220 172 ARG N N 125.56 0.3 . 632 221 173 GLU H H 9.44 0.05 . 633 221 173 GLU CA C 59.46 0.4 . 634 221 173 GLU CB C 27.80 0.4 . 635 221 173 GLU N N 118.77 0.3 . 636 222 174 GLU H H 7.55 0.05 . 637 222 174 GLU CA C 58.43 0.4 . 638 222 174 GLU CB C 29.59 0.4 . 639 222 174 GLU N N 116.35 0.3 . 640 223 175 ILE H H 7.04 0.05 . 641 223 175 ILE CA C 62.10 0.4 . 642 223 175 ILE CB C 34.91 0.4 . 643 223 175 ILE N N 117.08 0.3 . 644 224 176 TYR H H 6.89 0.05 . 645 224 176 TYR CA C 58.80 0.4 . 646 224 176 TYR CB C 35.45 0.4 . 647 224 176 TYR N N 118.53 0.3 . 648 225 177 GLN H H 8.70 0.05 . 649 225 177 GLN CA C 58.02 0.4 . 650 225 177 GLN CB C 27.79 0.4 . 651 225 177 GLN N N 119.26 0.3 . 652 226 178 ALA H H 8.17 0.05 . 653 226 178 ALA CA C 54.28 0.4 . 654 226 178 ALA CB C 19.20 0.4 . 655 226 178 ALA N N 121.92 0.3 . 656 227 179 PHE H H 8.09 0.05 . 657 227 179 PHE CA C 60.68 0.4 . 658 227 179 PHE CB C 38.29 0.4 . 659 227 179 PHE N N 116.84 0.3 . 660 228 180 GLU H H 8.27 0.05 . 661 228 180 GLU CA C 58.44 0.4 . 662 228 180 GLU CB C 28.39 0.4 . 663 228 180 GLU N N 117.81 0.3 . 664 229 181 ALA H H 7.60 0.05 . 665 229 181 ALA CA C 53.46 0.4 . 666 229 181 ALA CB C 17.80 0.4 . 667 229 181 ALA N N 118.29 0.3 . 668 230 182 ILE H H 7.83 0.05 . 669 230 182 ILE CA C 57.21 0.4 . 670 230 182 ILE CB C 38.63 0.4 . 671 230 182 ILE N N 116.59 0.3 . 672 231 183 TYR H H 8.12 0.05 . 673 231 183 TYR CA C 63.51 0.4 . 674 231 183 TYR CB C 34.32 0.4 . 675 231 183 TYR N N 126.04 0.3 . 676 232 184 PRO CA C 65.07 0.4 . 677 232 184 PRO CB C 30.14 0.4 . 678 233 185 VAL H H 6.98 0.05 . 679 233 185 VAL CA C 64.54 0.4 . 680 233 185 VAL CB C 30.60 0.4 . 681 233 185 VAL N N 119.02 0.3 . 682 234 186 LEU H H 7.91 0.05 . 683 234 186 LEU CA C 57.43 0.4 . 684 234 186 LEU CB C 38.75 0.4 . 685 234 186 LEU N N 117.08 0.3 . 686 235 187 SER H H 7.83 0.05 . 687 235 187 SER CA C 60.68 0.4 . 688 235 187 SER CB C 62.18 0.4 . 689 235 187 SER N N 108.84 0.3 . 690 236 188 GLU H H 7.52 0.05 . 691 236 188 GLU CA C 57.75 0.4 . 692 236 188 GLU CB C 28.21 0.4 . 693 236 188 GLU N N 122.41 0.3 . 694 237 189 PHE H H 7.44 0.05 . 695 237 189 PHE CA C 57.85 0.4 . 696 237 189 PHE CB C 37.29 0.4 . 697 237 189 PHE N N 115.87 0.3 . 698 238 190 ARG H H 6.96 0.05 . 699 238 190 ARG CA C 55.96 0.4 . 700 238 190 ARG CB C 30.16 0.4 . 701 238 190 ARG N N 121.44 0.3 . 702 239 191 LYS H H 8.67 0.05 . 703 239 191 LYS CA C 55.97 0.4 . 704 239 191 LYS CB C 32.20 0.4 . 705 239 191 LYS N N 128.62 0.3 . 706 240 192 MET H H 8.14 0.05 . 707 240 192 MET CA C 56.00 0.4 . 708 240 192 MET CB C 32.57 0.4 . 709 240 192 MET N N 131.23 0.3 . stop_ save_