data_6700 ####################### # 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 6700 _BMRB_flat_file_name bmr6700.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" 519 "13C chemical shifts" 600 "15N chemical shifts" 250 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-10-28 original author . stop_ 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 'TBP associated factor 1 (TAF1)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'TBP associated factor 1 (TAF1)' $dTAF1 'yeast TATA binding protein (y)TBP' $yTBP 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 'Drosophila (d)TAF1 was studied in complex with yeast (y)TBP' save_ ######################## # Monomeric polymers # ######################## save_dTAF1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common dTAF1 _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'Transcriptional regulation' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 67 _Mol_residue_sequence ; EGSIGNGLDLTGILFGNIDS EGRLLQDDDGEGRGGTGFDA ELRENIGSLSKLGLDSMLLE VIDLKEA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 11 GLU 2 12 GLY 3 13 SER 4 14 ILE 5 15 GLY 6 16 ASN 7 17 GLY 8 18 LEU 9 19 ASP 10 20 LEU 11 21 THR 12 22 GLY 13 23 ILE 14 24 LEU 15 25 PHE 16 26 GLY 17 27 ASN 18 28 ILE 19 29 ASP 20 30 SER 21 31 GLU 22 32 GLY 23 33 ARG 24 34 LEU 25 35 LEU 26 36 GLN 27 37 ASP 28 38 ASP 29 39 ASP 30 40 GLY 31 41 GLU 32 42 GLY 33 43 ARG 34 44 GLY 35 45 GLY 36 46 THR 37 47 GLY 38 48 PHE 39 49 ASP 40 50 ALA 41 51 GLU 42 52 LEU 43 53 ARG 44 54 GLU 45 55 ASN 46 56 ILE 47 57 GLY 48 58 SER 49 59 LEU 50 60 SER 51 61 LYS 52 62 LEU 53 63 GLY 54 64 LEU 55 65 ASP 56 66 SER 57 67 MET 58 68 LEU 59 69 LEU 60 70 GLU 61 71 VAL 62 72 ILE 63 73 ASP 64 74 LEU 65 75 LYS 66 76 GLU 67 77 ALA 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 6702 yTBPc 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_yTBP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TBPc _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'Transcriptional regulation' stop_ _Details . _Residue_count 192 _Mol_residue_sequence ; AAPESEKDTSATSGIVPTLQ NIVATVTLGCRLDLKTVALH ARNAEYNPKRFAAVIMRIRE PKTTALIFASGKMVVTGAKS EDDSKLASRKYARIIQKIGF AAKFTDFKIQNIVGSCDVKF PIRLEGLAFSHGTFSSYEPE LFPGLIYRMVKPKIVLLIFV SGKIVLTGAKQREEIYQAFE AIYPVLSEFRKM ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 49 ALA 2 50 ALA 3 51 PRO 4 52 GLU 5 53 SER 6 54 GLU 7 55 LYS 8 56 ASP 9 57 THR 10 58 SER 11 59 ALA 12 60 THR 13 61 SER 14 62 GLY 15 63 ILE 16 64 VAL 17 65 PRO 18 66 THR 19 67 LEU 20 68 GLN 21 69 ASN 22 70 ILE 23 71 VAL 24 72 ALA 25 73 THR 26 74 VAL 27 75 THR 28 76 LEU 29 77 GLY 30 78 CYS 31 79 ARG 32 80 LEU 33 81 ASP 34 82 LEU 35 83 LYS 36 84 THR 37 85 VAL 38 86 ALA 39 87 LEU 40 88 HIS 41 89 ALA 42 90 ARG 43 91 ASN 44 92 ALA 45 93 GLU 46 94 TYR 47 95 ASN 48 96 PRO 49 97 LYS 50 98 ARG 51 99 PHE 52 100 ALA 53 101 ALA 54 102 VAL 55 103 ILE 56 104 MET 57 105 ARG 58 106 ILE 59 107 ARG 60 108 GLU 61 109 PRO 62 110 LYS 63 111 THR 64 112 THR 65 113 ALA 66 114 LEU 67 115 ILE 68 116 PHE 69 117 ALA 70 118 SER 71 119 GLY 72 120 LYS 73 121 MET 74 122 VAL 75 123 VAL 76 124 THR 77 125 GLY 78 126 ALA 79 127 LYS 80 128 SER 81 129 GLU 82 130 ASP 83 131 ASP 84 132 SER 85 133 LYS 86 134 LEU 87 135 ALA 88 136 SER 89 137 ARG 90 138 LYS 91 139 TYR 92 140 ALA 93 141 ARG 94 142 ILE 95 143 ILE 96 144 GLN 97 145 LYS 98 146 ILE 99 147 GLY 100 148 PHE 101 149 ALA 102 150 ALA 103 151 LYS 104 152 PHE 105 153 THR 106 154 ASP 107 155 PHE 108 156 LYS 109 157 ILE 110 158 GLN 111 159 ASN 112 160 ILE 113 161 VAL 114 162 GLY 115 163 SER 116 164 CYS 117 165 ASP 118 166 VAL 119 167 LYS 120 168 PHE 121 169 PRO 122 170 ILE 123 171 ARG 124 172 LEU 125 173 GLU 126 174 GLY 127 175 LEU 128 176 ALA 129 177 PHE 130 178 SER 131 179 HIS 132 180 GLY 133 181 THR 134 182 PHE 135 183 SER 136 184 SER 137 185 TYR 138 186 GLU 139 187 PRO 140 188 GLU 141 189 LEU 142 190 PHE 143 191 PRO 144 192 GLY 145 193 LEU 146 194 ILE 147 195 TYR 148 196 ARG 149 197 MET 150 198 VAL 151 199 LYS 152 200 PRO 153 201 LYS 154 202 ILE 155 203 VAL 156 204 LEU 157 205 LEU 158 206 ILE 159 207 PHE 160 208 VAL 161 209 SER 162 210 GLY 163 211 LYS 164 212 ILE 165 213 VAL 166 214 LEU 167 215 THR 168 216 GLY 169 217 ALA 170 218 LYS 171 219 GLN 172 220 ARG 173 221 GLU 174 222 GLU 175 223 ILE 176 224 TYR 177 225 GLN 178 226 ALA 179 227 PHE 180 228 GLU 181 229 ALA 182 230 ILE 183 231 TYR 184 232 PRO 185 233 VAL 186 234 LEU 187 235 SER 188 236 GLU 189 237 PHE 190 238 ARG 191 239 LYS 192 240 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 $dTAF1 'Drosophila Melanogaster' 7227 Eukaryota Metazoa Drosophila melanogaster $yTBP '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 $dTAF1 'recombinant technology' 'E. Coli' . . . . $yTBP 'recombinant technology' 'E. Coli' . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_dTAF1(11-77) _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $dTAF1 . mM 0.8 1 '[U-15N; U-13C; U-2H]' $yTBP . mM 0.8 1 '[U-15N; U-13C; U-2H]' phosphate 20 mM . . . Glycerol 5 '% (v/v)' . . . Na2SO4 250 mM . . . MgCl2 5 mM . . . DTT 10 mM . . . NaN3 0.05 mM . . . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _Sample_label $dTAF1(11-77) save_ save_HNCACA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACA _Sample_label $dTAF1(11-77) save_ save_CBCACONNH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONNH _Sample_label $dTAF1(11-77) save_ save_HCCTOCSYNNH_4 _Saveframe_category NMR_applied_experiment _Experiment_name HCCTOCSYNNH _Sample_label $dTAF1(11-77) save_ ####################### # Sample conditions # ####################### save_20_mM_phosphate_buffer _Saveframe_category sample_conditions _Details '20 mM phosphate, 5% (v/v) Glycerol, 250 Na2SO4, 5 mM MgCl2, 10 mM DTT and 0.05 NaN3' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_assignment_of_dTAF1(11-77)_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $dTAF1(11-77) stop_ _Sample_conditions_label $20_mM_phosphate_buffer _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'TBP associated factor 1 (TAF1)' _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 12 2 GLY H H 8.66 0.05 . 2 12 2 GLY HA2 H 4.01 0.05 . 3 12 2 GLY HA3 H 4.01 0.05 . 4 12 2 GLY C C 174.24 0.4 . 5 12 2 GLY CA C 45.51 0.4 . 6 12 2 GLY N N 111.63 0.4 . 7 13 3 SER H H 8.22 0.05 . 8 13 3 SER HA H 4.51 0.05 . 9 13 3 SER HB2 H 3.88 0.05 . 10 13 3 SER C C 174.77 0.4 . 11 13 3 SER CA C 58.41 0.4 . 12 13 3 SER CB C 64.01 0.4 . 13 13 3 SER N N 116.11 0.4 . 14 14 4 ILE H H 8.25 0.05 . 15 14 4 ILE HA H 4.22 0.05 . 16 14 4 ILE HB H 1.94 0.05 . 17 14 4 ILE HG12 H 1.47 0.05 . 18 14 4 ILE HG13 H 1.19 0.05 . 19 14 4 ILE HG2 H 0.91 0.05 . 20 14 4 ILE HD1 H 0.82 0.05 . 21 14 4 ILE C C 176.74 0.4 . 22 14 4 ILE CA C 61.6 0.4 . 23 14 4 ILE CB C 38.74 0.4 . 24 14 4 ILE CG1 C 27.62 0.4 . 25 14 4 ILE CG2 C 17.67 0.4 . 26 14 4 ILE CD1 C 13.24 0.4 . 27 14 4 ILE N N 122.43 0.4 . 28 15 5 GLY H H 8.43 0.05 . 29 15 5 GLY HA2 H 3.98 0.05 . 30 15 5 GLY HA3 H 3.98 0.05 . 31 15 5 GLY C C 173.97 0.4 . 32 15 5 GLY CA C 45.51 0.4 . 33 15 5 GLY N N 112.57 0.4 . 34 16 6 ASN H H 8.4 0.05 . 35 16 6 ASN HA H 4.78 0.05 . 36 16 6 ASN HB2 H 2.78 0.05 . 37 16 6 ASN HB3 H 2.89 0.05 . 38 16 6 ASN HD21 H 7.61 0.05 . 39 16 6 ASN HD22 H 6.91 0.05 . 40 16 6 ASN C C 175.7 0.4 . 41 16 6 ASN CA C 53.24 0.4 . 42 16 6 ASN CB C 39.21 0.4 . 43 16 6 ASN N N 119.27 0.4 . 44 16 6 ASN ND2 N 113.06 0.4 . 45 17 7 GLY H H 8.44 0.05 . 46 17 7 GLY HA2 H 3.96 0.05 . 47 17 7 GLY HA3 H 3.96 0.05 . 48 17 7 GLY C C 173.57 0.4 . 49 17 7 GLY CA C 45.55 0.4 . 50 17 7 GLY N N 109.53 0.4 . 51 18 8 LEU H H 7.99 0.05 . 52 18 8 LEU HA H 4.3 0.05 . 53 18 8 LEU HB2 H 1.32 0.05 . 54 18 8 LEU HB3 H 1.45 0.05 . 55 18 8 LEU HG H 1.28 0.05 . 56 18 8 LEU HD1 H 0.67 0.05 . 57 18 8 LEU HD2 H 0.57 0.05 . 58 18 8 LEU C C 175.42 0.4 . 59 18 8 LEU CA C 54.92 0.4 . 60 18 8 LEU CB C 43.64 0.4 . 61 18 8 LEU CG C 27.16 0.4 . 62 18 8 LEU CD1 C 24.05 0.4 . 63 18 8 LEU CD2 C 24.75 0.4 . 64 18 8 LEU N N 122.35 0.4 . 65 19 9 ASP H H 8.46 0.05 . 66 19 9 ASP HA H 4.72 0.05 . 67 19 9 ASP HB2 H 2.66 0.05 . 68 19 9 ASP HB3 H 2.88 0.05 . 69 19 9 ASP C C 176.89 0.4 . 70 19 9 ASP CA C 53.74 0.4 . 71 19 9 ASP CB C 41.85 0.4 . 72 19 9 ASP N N 124.87 0.4 . 73 20 10 LEU H H 8.63 0.05 . 74 20 10 LEU HA H 4.38 0.05 . 75 20 10 LEU HB2 H 1.66 0.05 . 76 20 10 LEU HG H 1.32 0.05 . 77 20 10 LEU HD1 H 0.46 0.05 . 78 20 10 LEU HD2 H 0.34 0.05 . 79 20 10 LEU C C 176.52 0.4 . 80 20 10 LEU CA C 54.82 0.4 . 81 20 10 LEU CB C 42.47 0.4 . 82 20 10 LEU CG C 26.85 0.4 . 83 20 10 LEU CD1 C 25.55 0.4 . 84 20 10 LEU CD2 C 22.87 0.4 . 85 20 10 LEU N N 125.85 0.4 . 86 21 11 THR H H 8.26 0.05 . 87 21 11 THR HA H 3.92 0.05 . 88 21 11 THR HB H 3.53 0.05 . 89 21 11 THR HG2 H 1.17 0.05 . 90 21 11 THR C C 175.31 0.4 . 91 21 11 THR CA C 67.5 0.4 . 92 21 11 THR CB C 67.9 0.4 . 93 21 11 THR CG2 C 22.15 0.4 . 94 21 11 THR N N 117.45 0.4 . 95 22 12 GLY H H 9.27 0.05 . 96 22 12 GLY HA2 H 3.57 0.05 . 97 22 12 GLY HA3 H 3.57 0.05 . 98 22 12 GLY C C 174.95 0.4 . 99 22 12 GLY N N 106.28 0.4 . 100 23 13 ILE H H 8.05 0.05 . 101 23 13 ILE HA H 4.45 0.05 . 102 23 13 ILE HB H 1.89 0.05 . 103 23 13 ILE HG12 H 1.4 0.05 . 104 23 13 ILE HG13 H 1.4 0.05 . 105 23 13 ILE HG2 H 0.93 0.05 . 106 23 13 ILE HD1 H 0.73 0.05 . 107 23 13 ILE C C 177.58 0.4 . 108 23 13 ILE CA C 62.38 0.4 . 109 23 13 ILE CG1 C 27.14 0.4 . 110 23 13 ILE CG2 C 18.23 0.4 . 111 23 13 ILE CD1 C 15.35 0.4 . 112 23 13 ILE N N 115.31 0.4 . 113 24 14 LEU H H 7.72 0.05 . 114 24 14 LEU HA H 3.57 0.05 . 115 24 14 LEU HB2 H 1.4 0.05 . 116 24 14 LEU HG H 1.02 0.05 . 117 24 14 LEU HD1 H 0.73 0.05 . 118 24 14 LEU HD2 H 0.54 0.05 . 119 24 14 LEU C C 177.03 0.4 . 120 24 14 LEU CA C 56.93 0.4 . 121 24 14 LEU CB C 41.23 0.4 . 122 24 14 LEU CD1 C 25.63 0.4 . 123 24 14 LEU CD2 C 22.26 0.4 . 124 24 14 LEU N N 117.96 0.4 . 125 25 15 PHE H H 7.54 0.05 . 126 25 15 PHE HA H 4.27 0.05 . 127 25 15 PHE HB2 H 2.71 0.05 . 128 25 15 PHE HB3 H 3.12 0.05 . 129 25 15 PHE HD1 H 6.99 0.05 . 130 25 15 PHE HD2 H 6.99 0.05 . 131 25 15 PHE HE1 H 6.85 0.05 . 132 25 15 PHE HE2 H 6.85 0.05 . 133 25 15 PHE HZ H 6.80 0.05 . 134 25 15 PHE C C 174.31 0.4 . 135 25 15 PHE N N 112.58 0.4 . 136 26 16 GLY H H 7.56 0.05 . 137 26 16 GLY HA2 H 3.56 0.05 . 138 26 16 GLY HA3 H 3.56 0.05 . 139 26 16 GLY CA C 45.67 0.4 . 140 26 16 GLY N N 107.55 0.4 . 141 27 17 ASN H H 8.16 0.05 . 142 27 17 ASN HA H 4.2 0.05 . 143 27 17 ASN N N 112.83 0.4 . 144 28 18 ILE H H 6.2 0.05 . 145 28 18 ILE HA H 5.5 0.05 . 146 28 18 ILE HG2 H 0.6 0.05 . 147 28 18 ILE HD1 H 0.73 0.05 . 148 28 18 ILE CA C 57.9 0.4 . 149 28 18 ILE CG2 C 16.79 0.4 . 150 28 18 ILE CD1 C 14.19 0.4 . 151 28 18 ILE N N 107.98 0.4 . 152 29 19 ASP H H 8.55 0.05 . 153 29 19 ASP HB2 H 2.61 0.05 . 154 29 19 ASP HB3 H 3.36 0.05 . 155 29 19 ASP CA C 59.54 0.4 . 156 29 19 ASP CB C 41.77 0.4 . 157 29 19 ASP N N 122.18 0.4 . 158 30 20 SER H H 8.3 0.05 . 159 30 20 SER HA H 4.18 0.05 . 160 30 20 SER HB2 H 3.96 0.05 . 161 30 20 SER CA C 60.83 0.4 . 162 30 20 SER CB C 62.77 0.4 . 163 30 20 SER N N 111.36 0.4 . 164 31 21 GLU H H 8.09 0.05 . 165 31 21 GLU HA H 4.41 0.05 . 166 31 21 GLU HB2 H 1.9 0.05 . 167 31 21 GLU HB3 H 2.3 0.05 . 168 31 21 GLU HG2 H 2.09 0.05 . 169 31 21 GLU HG3 H 2.20 0.05 . 170 31 21 GLU CA C 55.27 0.4 . 171 31 21 GLU CB C 30.26 0.4 . 172 31 21 GLU CG C 36.78 0.4 . 173 31 21 GLU N N 118.04 0.4 . 174 32 22 GLY H H 8.16 0.05 . 175 32 22 GLY N N 108.05 0.4 . 176 33 23 ARG H H 8.48 0.05 . 177 33 23 ARG HA H 4.24 0.05 . 178 33 23 ARG HB2 H 1.89 0.05 . 179 33 23 ARG HB3 H 1.89 0.05 . 180 33 23 ARG HG2 H 1.46 0.05 . 181 33 23 ARG HG3 H 1.61 0.05 . 182 33 23 ARG HD2 H 3.13 0.05 . 183 33 23 ARG HD3 H 3.23 0.05 . 184 33 23 ARG HH11 H 7.73 0.05 . 185 33 23 ARG HH12 H 7.77 0.05 . 186 33 23 ARG CG C 28.24 0.4 . 187 33 23 ARG CD C 43.3 0.4 . 188 33 23 ARG N N 122.19 0.4 . 189 33 23 ARG NH1 N 86.37 0.4 . 190 34 24 LEU H H 8.29 0.05 . 191 34 24 LEU HA H 4.29 0.05 . 192 34 24 LEU HB2 H 1.4 0.05 . 193 34 24 LEU HB3 H 1.4 0.05 . 194 34 24 LEU HD1 H 0.7 0.05 . 195 34 24 LEU HD2 H 0.85 0.05 . 196 34 24 LEU C C 177.06 0.4 . 197 34 24 LEU CA C 54.5 0.4 . 198 34 24 LEU CB C 43.43 0.4 . 199 34 24 LEU CD1 C 25.62 0.4 . 200 34 24 LEU CD2 C 23.9 0.4 . 201 34 24 LEU N N 122.78 0.4 . 202 35 25 LEU H H 8.3 0.05 . 203 35 25 LEU HA H 4.28 0.05 . 204 35 25 LEU HB2 H 1.59 0.05 . 205 35 25 LEU HB3 H 1.59 0.05 . 206 35 25 LEU HG H 1.59 0.05 . 207 35 25 LEU HD1 H 0.69 0.05 . 208 35 25 LEU HD2 H 0.8 0.05 . 209 35 25 LEU C C 177.35 0.4 . 210 35 25 LEU CA C 54.51 0.4 . 211 35 25 LEU CB C 42.53 0.4 . 212 35 25 LEU CG C 27.62 0.4 . 213 35 25 LEU CD1 C 25.63 0.4 . 214 35 25 LEU CD2 C 23.05 0.4 . 215 35 25 LEU N N 127.23 0.4 . 216 36 26 GLN H H 8.63 0.05 . 217 36 26 GLN HA H 4.35 0.05 . 218 36 26 GLN HB2 H 1.91 0.05 . 219 36 26 GLN HB3 H 2.05 0.05 . 220 36 26 GLN HG2 H 2.3 0.05 . 221 36 26 GLN HG3 H 2.3 0.05 . 222 36 26 GLN HE21 H 7.68 0.05 . 223 36 26 GLN HE22 H 6.87 0.05 . 224 36 26 GLN C C 175.24 0.4 . 225 36 26 GLN CA C 55.66 0.4 . 226 36 26 GLN CB C 30.14 0.4 . 227 36 26 GLN CG C 34.15 0.4 . 228 36 26 GLN N N 122.71 0.4 . 229 36 26 GLN NE2 N 112.4 0.4 . 230 37 27 ASP H H 8.52 0.05 . 231 37 27 ASP HA H 4.63 0.05 . 232 37 27 ASP HB2 H 2.59 0.05 . 233 37 27 ASP HB3 H 2.71 0.05 . 234 37 27 ASP C C 175.81 0.4 . 235 37 27 ASP CA C 54.38 0.4 . 236 37 27 ASP CB C 41.68 0.4 . 237 37 27 ASP N N 124.01 0.4 . 238 38 28 ASP H H 8.4 0.05 . 239 38 28 ASP HA H 4.6 0.05 . 240 38 28 ASP HB2 H 2.71 0.05 . 241 38 28 ASP HB3 H 2.71 0.05 . 242 38 28 ASP C C 175.81 0.4 . 243 38 28 ASP CA C 54.54 0.4 . 244 38 28 ASP CB C 41.63 0.4 . 245 38 28 ASP N N 121.46 0.4 . 246 39 29 ASP H H 8.38 0.05 . 247 39 29 ASP HA H 4.59 0.05 . 248 39 29 ASP HB2 H 2.71 0.05 . 249 39 29 ASP HB3 H 2.71 0.05 . 250 39 29 ASP C C 177.08 0.4 . 251 39 29 ASP CA C 54.6 0.4 . 252 39 29 ASP CB C 41.33 0.4 . 253 39 29 ASP N N 121.25 0.4 . 254 40 30 GLY H H 8.44 0.05 . 255 40 30 GLY HA2 H 3.96 0.05 . 256 40 30 GLY HA3 H 3.96 0.05 . 257 40 30 GLY C C 174.81 0.4 . 258 40 30 GLY CA C 45.84 0.4 . 259 40 30 GLY N N 109.53 0.4 . 260 41 31 GLU H H 8.37 0.05 . 261 41 31 GLU HA H 4.27 0.05 . 262 41 31 GLU HB2 H 1.96 0.05 . 263 41 31 GLU HB3 H 2.09 0.05 . 264 41 31 GLU HG2 H 2.23 0.05 . 265 41 31 GLU HG3 H 2.26 0.05 . 266 41 31 GLU C C 177.4 0.4 . 267 41 31 GLU CA C 56.83 0.4 . 268 41 31 GLU CB C 30.11 0.4 . 269 41 31 GLU CG C 36.31 0.4 . 270 41 31 GLU N N 120.74 0.4 . 271 42 32 GLY H H 8.49 0.05 . 272 42 32 GLY HA2 H 3.97 0.05 . 273 42 32 GLY HA3 H 3.97 0.05 . 274 42 32 GLY C C 174.9 0.4 . 275 42 32 GLY CA C 45.87 0.4 . 276 42 32 GLY N N 110 0.4 . 277 43 33 ARG H H 8.25 0.05 . 278 43 33 ARG HA H 4.36 0.05 . 279 43 33 ARG HB2 H 1.93 0.05 . 280 43 33 ARG HB3 H 1.76 0.05 . 281 43 33 ARG HG2 H 1.6 0.05 . 282 43 33 ARG HG3 H 1.6 0.05 . 283 43 33 ARG HD2 H 3.17 0.05 . 284 43 33 ARG HD3 H 3.17 0.05 . 285 43 33 ARG C C 177.15 0.4 . 286 43 33 ARG CA C 56.4 0.4 . 287 43 33 ARG CB C 30.54 0.4 . 288 43 33 ARG CG C 27.31 0.4 . 289 43 33 ARG CD C 43.15 0.4 . 290 43 33 ARG N N 120.63 0.4 . 291 44 34 GLY H H 8.58 0.05 . 292 44 34 GLY HA2 H 3.98 0.05 . 293 44 34 GLY HA3 H 3.98 0.05 . 294 44 34 GLY C C 174.94 0.4 . 295 44 34 GLY CA C 45.62 0.4 . 296 44 34 GLY N N 110.18 0.4 . 297 45 35 GLY H H 8.31 0.05 . 298 45 35 GLY HA2 H 4.01 0.05 . 299 45 35 GLY HA3 H 4.01 0.05 . 300 45 35 GLY C C 174.6 0.4 . 301 45 35 GLY CA C 45.53 0.4 . 302 45 35 GLY N N 109.37 0.4 . 303 46 36 THR H H 8.11 0.05 . 304 46 36 THR HA H 4.35 0.05 . 305 46 36 THR HB H 4.18 0.05 . 306 46 36 THR HG2 H 1.16 0.05 . 307 46 36 THR C C 175.04 0.4 . 308 46 36 THR CA C 61.76 0.4 . 309 46 36 THR CB C 70.02 0.4 . 310 46 36 THR CG2 C 21.54 0.4 . 311 46 36 THR N N 112.75 0.4 . 312 47 37 GLY H H 8.33 0.05 . 313 47 37 GLY HA2 H 3.78 0.05 . 314 47 37 GLY HA3 H 3.78 0.05 . 315 47 37 GLY C C 173.99 0.4 . 316 47 37 GLY CA C 44.99 0.4 . 317 47 37 GLY N N 111.2 0.4 . 318 48 38 PHE H H 8.35 0.05 . 319 48 38 PHE HA H 4.64 0.05 . 320 48 38 PHE HB2 H 2.71 0.05 . 321 48 38 PHE HB3 H 3.09 0.05 . 322 48 38 PHE HD1 H 7.24 0.05 . 323 48 38 PHE HD2 H 7.24 0.05 . 324 48 38 PHE HE1 H 7.35 0.05 . 325 48 38 PHE HE2 H 7.35 0.05 . 326 48 38 PHE HZ H 7.4 0.05 . 327 48 38 PHE C C 175.85 0.4 . 328 48 38 PHE CA C 56.2 0.4 . 329 48 38 PHE CB C 42.53 0.4 . 330 48 38 PHE N N 119.8 0.4 . 331 49 39 ASP H H 8.63 0.05 . 332 49 39 ASP HA H 4.35 0.05 . 333 49 39 ASP HB2 H 2.2 0.05 . 334 49 39 ASP HB3 H 2.43 0.05 . 335 49 39 ASP C C 177.03 0.4 . 336 49 39 ASP CA C 53.73 0.4 . 337 49 39 ASP CB C 42.24 0.4 . 338 49 39 ASP N N 122.71 0.4 . 339 50 40 ALA H H 8.61 0.05 . 340 50 40 ALA HA H 3.83 0.05 . 341 50 40 ALA HB H 1.37 0.05 . 342 50 40 ALA C C 178.52 0.4 . 343 50 40 ALA CA C 55.82 0.4 . 344 50 40 ALA CB C 18.73 0.4 . 345 50 40 ALA N N 127.05 0.4 . 346 51 41 GLU H H 8.72 0.05 . 347 51 41 GLU HA H 3.82 0.05 . 348 51 41 GLU HB2 H 1.57 0.05 . 349 51 41 GLU HB3 H 1.69 0.05 . 350 51 41 GLU HG2 H 1.97 0.05 . 351 51 41 GLU HG3 H 2.1 0.05 . 352 51 41 GLU C C 178.27 0.4 . 353 51 41 GLU CA C 59.37 0.4 . 354 51 41 GLU CB C 29.47 0.4 . 355 51 41 GLU CG C 37.09 0.4 . 356 51 41 GLU N N 115.51 0.4 . 357 52 42 LEU H H 7.08 0.05 . 358 52 42 LEU HA H 4.18 0.05 . 359 52 42 LEU HB2 H 1.32 0.05 . 360 52 42 LEU HB3 H 1.55 0.05 . 361 52 42 LEU HG H 1.06 0.05 . 362 52 42 LEU HD1 H 0.4 0.05 . 363 52 42 LEU HD2 H 0.11 0.05 . 364 52 42 LEU C C 177.84 0.4 . 365 52 42 LEU CA C 57.84 0.4 . 366 52 42 LEU CG C 27.78 0.4 . 367 52 42 LEU CD1 C 24.4 0.4 . 368 52 42 LEU CD2 C 24.56 0.4 . 369 52 42 LEU N N 117.32 0.4 . 370 53 43 ARG H H 7.71 0.05 . 371 53 43 ARG HA H 3.6 0.05 . 372 53 43 ARG HB2 H 1.74 0.05 . 373 53 43 ARG HB3 H 1.77 0.05 . 374 53 43 ARG HG2 H 1.45 0.05 . 375 53 43 ARG HG3 H 1.6 0.05 . 376 53 43 ARG HD2 H 3.13 0.05 . 377 53 43 ARG HD3 H 3.13 0.05 . 378 53 43 ARG C C 178.47 0.4 . 379 53 43 ARG CA C 60.52 0.4 . 380 53 43 ARG CB C 30.99 0.4 . 381 53 43 ARG CG C 28.55 0.4 . 382 53 43 ARG CD C 43.31 0.4 . 383 53 43 ARG N N 115.87 0.4 . 384 54 44 GLU H H 8.5 0.05 . 385 54 44 GLU HA H 4.19 0.05 . 386 54 44 GLU HB2 H 1.86 0.05 . 387 54 44 GLU HB3 H 2.12 0.05 . 388 54 44 GLU HG2 H 2.27 0.05 . 389 54 44 GLU HG3 H 2.37 0.05 . 390 54 44 GLU C C 177.38 0.4 . 391 54 44 GLU CA C 57.58 0.4 . 392 54 44 GLU CB C 30 0.4 . 393 54 44 GLU CG C 36.63 0.4 . 394 54 44 GLU N N 114.65 0.4 . 395 55 45 ASN H H 7.46 0.05 . 396 55 45 ASN HA H 5.32 0.05 . 397 55 45 ASN HB2 H 2.69 0.05 . 398 55 45 ASN HB3 H 3.29 0.05 . 399 55 45 ASN C C 175.6 0.4 . 400 55 45 ASN CA C 53.82 0.4 . 401 55 45 ASN CB C 40.94 0.4 . 402 55 45 ASN N N 114.87 0.4 . 403 56 46 ILE H H 7.26 0.05 . 404 56 46 ILE HA H 3.72 0.05 . 405 56 46 ILE HB H 1.88 0.05 . 406 56 46 ILE HG12 H 1.13 0.05 . 407 56 46 ILE HG13 H 1.45 0.05 . 408 56 46 ILE HG2 H 0.81 0.05 . 409 56 46 ILE HD1 H 0.50 0.05 . 410 56 46 ILE C C 177.4 0.4 . 411 56 46 ILE CA C 63.86 0.4 . 412 56 46 ILE CB C 38.05 0.4 . 413 56 46 ILE CG1 C 28.24 0.4 . 414 56 46 ILE CG2 C 17.91 0.4 . 415 56 46 ILE CD1 C 13.63 0.4 . 416 56 46 ILE N N 120.68 0.4 . 417 57 47 GLY H H 8.81 0.05 . 418 57 47 GLY HA2 H 4.05 0.05 . 419 57 47 GLY HA3 H 4.05 0.05 . 420 57 47 GLY C C 175.99 0.4 . 421 57 47 GLY CA C 46.77 0.4 . 422 57 47 GLY N N 108.75 0.4 . 423 58 48 SER H H 7.85 0.05 . 424 58 48 SER HA H 4.18 0.05 . 425 58 48 SER HB2 H 4.51 0.05 . 426 58 48 SER C C 175.56 0.4 . 427 58 48 SER CA C 59.89 0.4 . 428 58 48 SER CB C 64.24 0.4 . 429 58 48 SER N N 115.83 0.4 . 430 59 49 LEU H H 7.69 0.05 . 431 59 49 LEU HA H 3.76 0.05 . 432 59 49 LEU HB2 H 1.8 0.05 . 433 59 49 LEU HG H 1.38 0.05 . 434 59 49 LEU HD1 H 0.56 0.05 . 435 59 49 LEU HD2 H -0.07 0.05 . 436 59 49 LEU C C 179.33 0.4 . 437 59 49 LEU CA C 56.35 0.4 . 438 59 49 LEU CB C 44.8 0.4 . 439 59 49 LEU CG C 27.0 0.4 . 440 59 49 LEU CD1 C 25.75 0.4 . 441 59 49 LEU CD2 C 22.01 0.4 . 442 59 49 LEU N N 120.22 0.4 . 443 60 50 SER H H 8.57 0.05 . 444 60 50 SER HA H 4.04 0.05 . 445 60 50 SER HB2 H 4.0 0.05 . 446 60 50 SER C C 176.82 0.4 . 447 60 50 SER CA C 62.56 0.4 . 448 60 50 SER CB C 62.56 0.4 . 449 60 50 SER N N 115.98 0.4 . 450 61 51 LYS H H 7.57 0.05 . 451 61 51 LYS HA H 4.32 0.05 . 452 61 51 LYS HB2 H 1.96 0.05 . 453 61 51 LYS HB3 H 2.01 0.05 . 454 61 51 LYS HG2 H 1.52 0.05 . 455 61 51 LYS HG3 H 1.52 0.05 . 456 61 51 LYS HD2 H 1.74 0.05 . 457 61 51 LYS HD3 H 1.74 0.05 . 458 61 51 LYS HE2 H 3.01 0.05 . 459 61 51 LYS HE3 H 3.01 0.05 . 460 61 51 LYS C C 177.47 0.4 . 461 61 51 LYS CA C 57.38 0.4 . 462 61 51 LYS CB C 32.34 0.4 . 463 61 51 LYS CG C 25.45 0.4 . 464 61 51 LYS CD C 29.49 0.4 . 465 61 51 LYS CE C 42.37 0.4 . 466 61 51 LYS N N 119.85 0.4 . 467 62 52 LEU H H 7.35 0.05 . 468 62 52 LEU HA H 4.43 0.05 . 469 62 52 LEU HB2 H 1.67 0.05 . 470 62 52 LEU HG H 1.61 0.05 . 471 62 52 LEU HD1 H 0.72 0.05 . 472 62 52 LEU HD2 H 0.86 0.05 . 473 62 52 LEU C C 176.87 0.4 . 474 62 52 LEU CA C 54.67 0.4 . 475 62 52 LEU CB C 42.11 0.4 . 476 62 52 LEU CD1 C 26.28 0.4 . 477 62 52 LEU CD2 C 25.14 0.4 . 478 62 52 LEU N N 119.03 0.4 . 479 63 53 GLY H H 7.84 0.05 . 480 63 53 GLY HA2 H 4.31 0.05 . 481 63 53 GLY HA3 H 4.31 0.05 . 482 63 53 GLY C C 175.99 0.4 . 483 63 53 GLY CA C 45.85 0.4 . 484 63 53 GLY N N 105.87 0.4 . 485 64 54 LEU H H 7.98 0.05 . 486 64 54 LEU HA H 4.38 0.05 . 487 64 54 LEU HB2 H 1.39 0.05 . 488 64 54 LEU HB3 H 1.69 0.05 . 489 64 54 LEU HG H 1.68 0.05 . 490 64 54 LEU HD1 H 0.85 0.05 . 491 64 54 LEU HD2 H 0.81 0.05 . 492 64 54 LEU C C 177.04 0.4 . 493 64 54 LEU CA C 56.3 0.4 . 494 64 54 LEU CB C 40.45 0.4 . 495 64 54 LEU CG C 29.18 0.4 . 496 64 54 LEU CD1 C 25.08 0.4 . 497 64 54 LEU CD2 C 24.21 0.4 . 498 64 54 LEU N N 120.87 0.4 . 499 65 55 ASP H H 8.9 0.05 . 500 65 55 ASP HA H 4.2 0.05 . 501 65 55 ASP HB2 H 2.67 0.05 . 502 65 55 ASP HB3 H 2.76 0.05 . 503 65 55 ASP C C 178.56 0.4 . 504 65 55 ASP CA C 56.63 0.4 . 505 65 55 ASP CB C 38.8 0.4 . 506 65 55 ASP N N 120.01 0.4 . 507 66 56 SER H H 7.96 0.05 . 508 66 56 SER HA H 4.07 0.05 . 509 66 56 SER HB2 H 4.37 0.05 . 510 66 56 SER C C 176.34 0.4 . 511 66 56 SER CA C 60.97 0.4 . 512 66 56 SER CB C 62.63 0.4 . 513 66 56 SER N N 116.41 0.4 . 514 67 57 MET H H 7.43 0.05 . 515 67 57 MET HA H 4.15 0.05 . 516 67 57 MET HB2 H 1.99 0.05 . 517 67 57 MET HB3 H 2.0 0.05 . 518 67 57 MET HG2 H 2.37 0.05 . 519 67 57 MET HG3 H 2.65 0.05 . 520 67 57 MET HE H 2.08 0.05 . 521 67 57 MET C C 177.99 0.4 . 522 67 57 MET CA C 58.58 0.4 . 523 67 57 MET CB C 32.96 0.4 . 524 67 57 MET CG C 32.44 0.4 . 525 67 57 MET CE C 17.22 0.4 . 526 67 57 MET N N 121.49 0.4 . 527 68 58 LEU H H 7.66 0.05 . 528 68 58 LEU HA H 4.01 0.05 . 529 68 58 LEU HB2 H 1.50 0.05 . 530 68 58 LEU HB3 H 1.86 0.05 . 531 68 58 LEU HG H 1.56 0.05 . 532 68 58 LEU HD1 H 0.8 0.05 . 533 68 58 LEU HD2 H 0.78 0.05 . 534 68 58 LEU C C 178.34 0.4 . 535 68 58 LEU CA C 57.06 0.4 . 536 68 58 LEU CB C 41.74 0.4 . 537 68 58 LEU CG C 27.16 0.4 . 538 68 58 LEU CD1 C 25.14 0.4 . 539 68 58 LEU CD2 C 24.36 0.4 . 540 68 58 LEU N N 119.74 0.4 . 541 69 59 LEU H H 7.83 0.05 . 542 69 59 LEU HA H 4.1 0.05 . 543 69 59 LEU HB2 H 1.56 0.05 . 544 69 59 LEU HB3 H 1.72 0.05 . 545 69 59 LEU HG H 1.72 0.05 . 546 69 59 LEU HD1 H 0.86 0.05 . 547 69 59 LEU HD2 H 0.86 0.05 . 548 69 59 LEU C C 178.38 0.4 . 549 69 59 LEU CA C 57.25 0.4 . 550 69 59 LEU CB C 41.59 0.4 . 551 69 59 LEU CG C 27.62 0.4 . 552 69 59 LEU CD1 C 24.92 0.4 . 553 69 59 LEU CD2 C 23.43 0.4 . 554 69 59 LEU N N 118.63 0.4 . 555 70 60 GLU H H 7.33 0.05 . 556 70 60 GLU HA H 4.02 0.05 . 557 70 60 GLU HB2 H 2.03 0.05 . 558 70 60 GLU HG2 H 2.2 0.05 . 559 70 60 GLU HG3 H 2.41 0.05 . 560 70 60 GLU C C 177.38 0.4 . 561 70 60 GLU CA C 58.2 0.4 . 562 70 60 GLU CB C 29.99 0.4 . 563 70 60 GLU CG C 36.63 0.4 . 564 70 60 GLU N N 116.12 0.4 . 565 71 61 VAL H H 7.46 0.05 . 566 71 61 VAL HA H 3.85 0.05 . 567 71 61 VAL HB H 2.13 0.05 . 568 71 61 VAL HG1 H 0.72 0.05 . 569 71 61 VAL HG2 H 0.83 0.05 . 570 71 61 VAL C C 175.23 0.4 . 571 71 61 VAL CA C 63.75 0.4 . 572 71 61 VAL CB C 32.75 0.4 . 573 71 61 VAL CG1 C 22.47 0.4 . 574 71 61 VAL CG2 C 21.46 0.4 . 575 71 61 VAL N N 114.87 0.4 . 576 72 62 ILE H H 7.77 0.05 . 577 72 62 ILE HA H 3.95 0.05 . 578 72 62 ILE HB H 1.74 0.05 . 579 72 62 ILE HG12 H 1.08 0.05 . 580 72 62 ILE HG13 H 1.32 0.05 . 581 72 62 ILE HG2 H 0.74 0.05 . 582 72 62 ILE HD1 H 0.73 0.05 . 583 72 62 ILE C C 173.75 0.4 . 584 72 62 ILE CA C 60.72 0.4 . 585 72 62 ILE CB C 39.32 0.4 . 586 72 62 ILE CG1 C 27.31 0.4 . 587 72 62 ILE CG2 C 17.79 0.4 . 588 72 62 ILE CD1 C 13.84 0.4 . 589 72 62 ILE N N 115.47 0.4 . 590 73 63 ASP H H 7.49 0.05 . 591 73 63 ASP HA H 4.5 0.05 . 592 73 63 ASP HB2 H 2.35 0.05 . 593 73 63 ASP HB3 H 2.63 0.05 . 594 73 63 ASP C C 176.08 0.4 . 595 73 63 ASP CA C 53.54 0.4 . 596 73 63 ASP CB C 40.99 0.4 . 597 73 63 ASP N N 122.16 0.4 . 598 74 64 LEU H H 8.11 0.05 . 599 74 64 LEU HA H 4.16 0.05 . 600 74 64 LEU HB2 H 1.56 0.05 . 601 74 64 LEU HB3 H 1.58 0.05 . 602 74 64 LEU HG H 1.55 0.05 . 603 74 64 LEU HD1 H 0.78 0.05 . 604 74 64 LEU HD2 H 0.86 0.05 . 605 74 64 LEU C C 177.46 0.4 . 606 74 64 LEU CA C 55.44 0.4 . 607 74 64 LEU CB C 42.28 0.4 . 608 74 64 LEU CG C 27.16 0.4 . 609 74 64 LEU CD1 C 23.78 0.4 . 610 74 64 LEU CD2 C 25.3 0.4 . 611 74 64 LEU N N 123.44 0.4 . 612 75 65 LYS H H 8.21 0.05 . 613 75 65 LYS HA H 4.23 0.05 . 614 75 65 LYS HB2 H 1.8 0.05 . 615 75 65 LYS HG2 H 1.4 0.05 . 616 75 65 LYS HG3 H 1.4 0.05 . 617 75 65 LYS HD2 H 1.66 0.05 . 618 75 65 LYS HD3 H 1.66 0.05 . 619 75 65 LYS HE2 H 2.98 0.05 . 620 75 65 LYS HE3 H 2.98 0.05 . 621 75 65 LYS C C 176.73 0.4 . 622 75 65 LYS CA C 56.89 0.4 . 623 75 65 LYS CB C 32.72 0.4 . 624 75 65 LYS CG C 24.98 0.4 . 625 75 65 LYS CD C 29.18 0.4 . 626 75 65 LYS CE C 41.45 0.4 . 627 75 65 LYS N N 121.09 0.4 . 628 76 66 GLU H H 8.11 0.05 . 629 76 66 GLU HA H 4.27 0.05 . 630 76 66 GLU HB2 H 1.88 0.05 . 631 76 66 GLU HB3 H 2.08 0.05 . 632 76 66 GLU HG2 H 2.2 0.05 . 633 76 66 GLU HG3 H 2.2 0.05 . 634 76 66 GLU C C 175.1 0.4 . 635 76 66 GLU CA C 56.36 0.4 . 636 76 66 GLU CB C 30.53 0.4 . 637 76 66 GLU CG C 36.63 0.4 . 638 76 66 GLU N N 121.48 0.4 . 639 77 67 ALA H H 7.77 0.05 . 640 77 67 ALA HA H 4.1 0.05 . 641 77 67 ALA HB H 1.3 0.05 . 642 77 67 ALA CA C 53.86 0.4 . 643 77 67 ALA CB C 20.47 0.4 . 644 77 67 ALA N N 130.44 0.4 . stop_ save_ save_Chemical_shift_assignment_of_dTAF1(11-77)_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $dTAF1(11-77) stop_ _Sample_conditions_label $20_mM_phosphate_buffer _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'yeast TATA binding protein (y)TBP' _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 8.62 0.05 . 2 52 4 GLU CA C 56.27 0.4 . 3 52 4 GLU CB C 29.49 0.4 . 4 52 4 GLU N N 121.02 0.3 . 5 53 5 SER H H 8.25 0.05 . 6 53 5 SER CA C 57.86 0.4 . 7 53 5 SER CB C 63.78 0.4 . 8 53 5 SER N N 116.15 0.3 . 9 54 6 GLU H H 8.37 0.05 . 10 54 6 GLU CA C 55.99 0.4 . 11 54 6 GLU CB C 29.63 0.4 . 12 54 6 GLU N N 122.87 0.3 . 13 55 7 LYS H H 8.17 0.05 . 14 55 7 LYS CA C 55.66 0.4 . 15 55 7 LYS CB C 32.56 0.4 . 16 55 7 LYS N N 121.86 0.3 . 17 56 8 ASP H H 8.36 0.05 . 18 56 8 ASP CA C 53.65 0.4 . 19 56 8 ASP CB C 40.85 0.4 . 20 56 8 ASP N N 121.86 0.3 . 21 57 9 THR H H 8.19 0.05 . 22 57 9 THR CA C 61.03 0.4 . 23 57 9 THR CB C 69.15 0.4 . 24 57 9 THR N N 115.09 0.3 . 25 58 10 SER H H 8.42 0.05 . 26 58 10 SER CA C 58.68 0.4 . 27 58 10 SER CB C 63.44 0.4 . 28 58 10 SER N N 118.71 0.3 . 29 59 11 ALA H H 8.40 0.05 . 30 59 11 ALA CA C 52.51 0.4 . 31 59 11 ALA CB C 18.80 0.4 . 32 59 11 ALA N N 126.04 0.3 . 33 60 12 THR H H 7.89 0.05 . 34 60 12 THR CA C 60.46 0.4 . 35 60 12 THR CB C 69.03 0.4 . 36 60 12 THR N N 110.75 0.3 . 37 61 13 SER H H 8.42 0.05 . 38 61 13 SER CA C 58.82 0.4 . 39 61 13 SER CB C 63.20 0.4 . 40 61 13 SER N N 117.33 0.3 . 41 62 14 GLY H H 8.20 0.05 . 42 62 14 GLY CA C 44.60 0.4 . 43 62 14 GLY N N 109.04 0.3 . 44 63 15 ILE H H 7.95 0.05 . 45 63 15 ILE CA C 60.28 0.4 . 46 63 15 ILE CB C 38.09 0.4 . 47 63 15 ILE N N 122.41 0.3 . 48 64 16 VAL H H 8.08 0.05 . 49 64 16 VAL CA C 57.90 0.4 . 50 64 16 VAL CB C 33.99 0.4 . 51 64 16 VAL N N 124.96 0.3 . 52 65 17 PRO CA C 62.09 0.4 . 53 65 17 PRO CB C 31.94 0.4 . 54 66 18 THR H H 8.81 0.05 . 55 66 18 THR CA C 60.40 0.4 . 56 66 18 THR CB C 70.68 0.4 . 57 66 18 THR N N 117.55 0.3 . 58 67 19 LEU H H 8.93 0.05 . 59 67 19 LEU CA C 55.53 0.4 . 60 67 19 LEU CB C 39.84 0.4 . 61 67 19 LEU N N 125.68 0.3 . 62 68 20 GLN H H 9.13 0.05 . 63 68 20 GLN CA C 54.06 0.4 . 64 68 20 GLN CB C 31.55 0.4 . 65 68 20 GLN N N 119.99 0.3 . 66 69 21 ASN H H 7.58 0.05 . 67 69 21 ASN CA C 54.26 0.4 . 68 69 21 ASN CB C 42.53 0.4 . 69 69 21 ASN N N 112.11 0.3 . 70 70 22 ILE H H 7.94 0.05 . 71 70 22 ILE CA C 59.30 0.4 . 72 70 22 ILE CB C 40.40 0.4 . 73 70 22 ILE N N 124.75 0.3 . 74 71 23 VAL H H 9.27 0.05 . 75 71 23 VAL CA C 59.86 0.4 . 76 71 23 VAL CB C 33.06 0.4 . 77 71 23 VAL N N 127.46 0.3 . 78 72 24 ALA H H 9.26 0.05 . 79 72 24 ALA CA C 49.83 0.4 . 80 72 24 ALA CB C 24.66 0.4 . 81 72 24 ALA N N 131.50 0.3 . 82 73 25 THR H H 8.82 0.05 . 83 73 25 THR CA C 58.68 0.4 . 84 73 25 THR CB C 71.14 0.4 . 85 73 25 THR N N 109.69 0.3 . 86 74 26 VAL H H 8.59 0.05 . 87 74 26 VAL CA C 60.11 0.4 . 88 74 26 VAL CB C 37.02 0.4 . 89 74 26 VAL N N 118.46 0.3 . 90 75 27 THR H H 8.36 0.05 . 91 75 27 THR CA C 60.72 0.4 . 92 75 27 THR CB C 69.56 0.4 . 93 75 27 THR N N 121.86 0.3 . 94 76 28 LEU H H 8.77 0.05 . 95 76 28 LEU CA C 54.71 0.4 . 96 76 28 LEU CB C 41.21 0.4 . 97 76 28 LEU N N 125.02 0.3 . 98 77 29 GLY H H 7.94 0.05 . 99 77 29 GLY CA C 45.79 0.4 . 100 77 29 GLY N N 129.28 0.3 . 101 78 30 CYS H H 7.38 0.05 . 102 78 30 CYS CA C 53.44 0.4 . 103 78 30 CYS CB C 30.93 0.4 . 104 78 30 CYS N N 113.98 0.3 . 105 79 31 ARG H H 7.99 0.05 . 106 79 31 ARG CA C 54.65 0.4 . 107 79 31 ARG CB C 29.89 0.4 . 108 79 31 ARG N N 117.60 0.3 . 109 80 32 LEU H H 8.72 0.05 . 110 80 32 LEU CA C 52.51 0.4 . 111 80 32 LEU CB C 44.90 0.4 . 112 80 32 LEU N N 121.06 0.3 . 113 81 33 ASP H H 5.80 0.05 . 114 81 33 ASP CA C 52.32 0.4 . 115 81 33 ASP CB C 41.37 0.4 . 116 81 33 ASP N N 120.29 0.3 . 117 82 34 LEU H H 8.58 0.05 . 118 82 34 LEU CA C 57.08 0.4 . 119 82 34 LEU CB C 37.81 0.4 . 120 82 34 LEU N N 126.33 0.3 . 121 83 35 LYS H H 8.19 0.05 . 122 83 35 LYS CA C 59.09 0.4 . 123 83 35 LYS CB C 31.14 0.4 . 124 83 35 LYS N N 117.58 0.3 . 125 84 36 THR H H 7.46 0.05 . 126 84 36 THR CA C 66.39 0.4 . 127 84 36 THR CB C 67.88 0.4 . 128 84 36 THR N N 116.57 0.3 . 129 85 37 VAL H H 7.76 0.05 . 130 85 37 VAL CA C 66.22 0.4 . 131 85 37 VAL CB C 30.85 0.4 . 132 85 37 VAL N N 120.64 0.3 . 133 86 38 ALA H H 8.01 0.05 . 134 86 38 ALA CA C 53.81 0.4 . 135 86 38 ALA CB C 18.26 0.4 . 136 86 38 ALA N N 117.67 0.3 . 137 87 39 LEU H H 7.66 0.05 . 138 87 39 LEU CA C 56.16 0.4 . 139 87 39 LEU CB C 42.20 0.4 . 140 87 39 LEU N N 116.09 0.3 . 141 88 40 HIS H H 7.38 0.05 . 142 88 40 HIS CA C 56.60 0.4 . 143 88 40 HIS CB C 32.02 0.4 . 144 88 40 HIS N N 113.98 0.3 . 145 89 41 ALA H H 8.02 0.05 . 146 89 41 ALA CA C 50.93 0.4 . 147 89 41 ALA CB C 19.32 0.4 . 148 89 41 ALA N N 123.31 0.3 . 149 90 42 ARG H H 8.54 0.05 . 150 90 42 ARG CA C 56.40 0.4 . 151 90 42 ARG CB C 29.71 0.4 . 152 90 42 ARG N N 122.60 0.3 . 153 91 43 ASN H H 8.89 0.05 . 154 91 43 ASN CA C 52.95 0.4 . 155 91 43 ASN CB C 37.30 0.4 . 156 91 43 ASN N N 116.65 0.3 . 157 92 44 ALA H H 7.90 0.05 . 158 92 44 ALA CA C 50.35 0.4 . 159 92 44 ALA CB C 22.09 0.4 . 160 92 44 ALA N N 121.14 0.3 . 161 93 45 GLU H H 9.11 0.05 . 162 93 45 GLU CA C 54.48 0.4 . 163 93 45 GLU CB C 32.72 0.4 . 164 93 45 GLU N N 120.65 0.3 . 165 94 46 TYR H H 8.92 0.05 . 166 94 46 TYR CA C 55.46 0.4 . 167 94 46 TYR CB C 40.89 0.4 . 168 94 46 TYR N N 123.17 0.3 . 169 95 47 ASN H H 9.13 0.05 . 170 95 47 ASN CA C 49.40 0.4 . 171 95 47 ASN CB C 38.63 0.4 . 172 95 47 ASN N N 125.23 0.3 . 173 96 48 PRO CA C 62.97 0.4 . 174 96 48 PRO CB C 30.65 0.4 . 175 97 49 LYS H H 7.78 0.05 . 176 97 49 LYS CA C 57.23 0.4 . 177 97 49 LYS CB C 31.23 0.4 . 178 97 49 LYS N N 117.01 0.3 . 179 98 50 ARG H H 7.56 0.05 . 180 98 50 ARG CA C 56.45 0.4 . 181 98 50 ARG CB C 31.45 0.4 . 182 98 50 ARG N N 117.63 0.3 . 183 99 51 PHE H H 7.81 0.05 . 184 99 51 PHE CA C 56.64 0.4 . 185 99 51 PHE CB C 40.97 0.4 . 186 99 51 PHE N N 114.93 0.3 . 187 100 52 ALA H H 8.52 0.05 . 188 100 52 ALA CA C 51.34 0.4 . 189 100 52 ALA CB C 16.84 0.4 . 190 100 52 ALA N N 131.11 0.3 . 191 101 53 ALA H H 7.41 0.05 . 192 101 53 ALA CA C 50.75 0.4 . 193 101 53 ALA CB C 20.29 0.4 . 194 101 53 ALA N N 119.78 0.3 . 195 102 54 VAL H H 8.46 0.05 . 196 102 54 VAL CA C 60.90 0.4 . 197 102 54 VAL CB C 32.61 0.4 . 198 102 54 VAL N N 120.79 0.3 . 199 103 55 ILE H H 8.85 0.05 . 200 103 55 ILE CA C 59.47 0.4 . 201 103 55 ILE CB C 38.55 0.4 . 202 103 55 ILE N N 127.22 0.3 . 203 104 56 MET H H 9.45 0.05 . 204 104 56 MET CA C 53.57 0.4 . 205 104 56 MET CB C 37.40 0.4 . 206 104 56 MET N N 127.72 0.3 . 207 105 57 ARG H H 7.75 0.05 . 208 105 57 ARG CA C 55.14 0.4 . 209 105 57 ARG CB C 33.62 0.4 . 210 105 57 ARG N N 118.60 0.3 . 211 106 58 ILE H H 7.33 0.05 . 212 106 58 ILE CA C 59.24 0.4 . 213 106 58 ILE CB C 40.64 0.4 . 214 106 58 ILE N N 116.75 0.3 . 215 107 59 ARG H H 8.50 0.05 . 216 107 59 ARG CA C 57.26 0.4 . 217 107 59 ARG CB C 30.55 0.4 . 218 107 59 ARG N N 120.16 0.3 . 219 108 60 GLU H H 7.25 0.05 . 220 108 60 GLU CA C 52.11 0.4 . 221 108 60 GLU CB C 32.35 0.4 . 222 108 60 GLU N N 116.12 0.3 . 223 109 61 PRO CA C 61.94 0.4 . 224 109 61 PRO CB C 33.24 0.4 . 225 110 62 LYS H H 8.60 0.05 . 226 110 62 LYS CA C 57.87 0.4 . 227 110 62 LYS CB C 30.70 0.4 . 228 110 62 LYS N N 126.29 0.3 . 229 111 63 THR H H 7.76 0.05 . 230 111 63 THR CA C 60.88 0.4 . 231 111 63 THR CB C 76.23 0.4 . 232 111 63 THR N N 120.25 0.3 . 233 112 64 THR H H 8.63 0.05 . 234 112 64 THR CA C 61.90 0.4 . 235 112 64 THR CB C 71.52 0.4 . 236 112 64 THR N N 115.37 0.3 . 237 113 65 ALA H H 9.40 0.05 . 238 113 65 ALA CA C 48.60 0.4 . 239 113 65 ALA CB C 19.71 0.4 . 240 113 65 ALA N N 128.06 0.3 . 241 114 66 LEU H H 9.13 0.05 . 242 114 66 LEU CA C 55.51 0.4 . 243 114 66 LEU CB C 39.73 0.4 . 244 114 66 LEU N N 119.99 0.3 . 245 115 67 ILE H H 8.90 0.05 . 246 115 67 ILE CA C 59.66 0.4 . 247 115 67 ILE CB C 39.19 0.4 . 248 115 67 ILE N N 123.02 0.3 . 249 116 68 PHE H H 8.39 0.05 . 250 116 68 PHE CA C 56.97 0.4 . 251 116 68 PHE CB C 40.20 0.4 . 252 116 68 PHE N N 123.70 0.3 . 253 117 69 ALA H H 9.50 0.05 . 254 117 69 ALA CA C 54.38 0.4 . 255 117 69 ALA CB C 18.16 0.4 . 256 117 69 ALA N N 124.70 0.3 . 257 118 70 SER H H 7.83 0.05 . 258 118 70 SER CA C 57.68 0.4 . 259 118 70 SER CB C 63.97 0.4 . 260 118 70 SER N N 108.32 0.3 . 261 119 71 GLY H H 8.38 0.05 . 262 119 71 GLY CA C 44.86 0.4 . 263 119 71 GLY N N 110.74 0.3 . 264 120 72 LYS H H 7.29 0.05 . 265 120 72 LYS CA C 55.64 0.4 . 266 120 72 LYS CB C 32.26 0.4 . 267 120 72 LYS N N 120.60 0.3 . 268 121 73 MET H H 8.89 0.05 . 269 121 73 MET CA C 53.16 0.4 . 270 121 73 MET CB C 37.47 0.4 . 271 121 73 MET N N 123.02 0.3 . 272 122 74 VAL H H 9.05 0.05 . 273 122 74 VAL CA C 59.53 0.4 . 274 122 74 VAL CB C 34.12 0.4 . 275 122 74 VAL N N 125.60 0.3 . 276 123 75 VAL H H 9.37 0.05 . 277 123 75 VAL CA C 60.68 0.4 . 278 123 75 VAL CB C 34.44 0.4 . 279 123 75 VAL N N 126.41 0.3 . 280 124 76 THR H H 9.62 0.05 . 281 124 76 THR CA C 57.87 0.4 . 282 124 76 THR CB C 71.17 0.4 . 283 124 76 THR N N 125.07 0.3 . 284 125 77 GLY H H 8.43 0.05 . 285 125 77 GLY CA C 45.04 0.4 . 286 125 77 GLY N N 113.08 0.3 . 287 126 78 ALA H H 6.95 0.05 . 288 126 78 ALA CA C 50.61 0.4 . 289 126 78 ALA CB C 19.49 0.4 . 290 126 78 ALA N N 120.40 0.3 . 291 127 79 LYS H H 9.38 0.05 . 292 127 79 LYS CA C 54.69 0.4 . 293 127 79 LYS CB C 32.17 0.4 . 294 127 79 LYS N N 114.97 0.3 . 295 128 80 SER H H 7.34 0.05 . 296 128 80 SER CA C 55.89 0.4 . 297 128 80 SER CB C 66.84 0.4 . 298 128 80 SER N N 108.77 0.3 . 299 129 81 GLU H H 8.75 0.05 . 300 129 81 GLU CB C 29.45 0.4 . 301 129 81 GLU N N 123.18 0.3 . 302 130 82 ASP H H 7.95 0.05 . 303 130 82 ASP CA C 56.76 0.4 . 304 130 82 ASP CB C 39.67 0.4 . 305 130 82 ASP N N 121.67 0.3 . 306 131 83 ASP H H 7.95 0.05 . 307 131 83 ASP CA C 56.45 0.4 . 308 131 83 ASP CB C 39.48 0.4 . 309 131 83 ASP N N 121.67 0.3 . 310 132 84 SER H H 8.08 0.05 . 311 132 84 SER CA C 61.70 0.4 . 312 132 84 SER CB C 63.36 0.4 . 313 132 84 SER N N 115.93 0.3 . 314 133 85 LYS H H 7.83 0.05 . 315 133 85 LYS CA C 59.51 0.4 . 316 133 85 LYS CB C 31.68 0.4 . 317 133 85 LYS N N 122.93 0.3 . 318 134 86 LEU H H 8.01 0.05 . 319 134 86 LEU CA C 57.47 0.4 . 320 134 86 LEU CB C 41.53 0.4 . 321 134 86 LEU N N 119.94 0.3 . 322 135 87 ALA H H 8.68 0.05 . 323 135 87 ALA CA C 54.57 0.4 . 324 135 87 ALA CB C 18.68 0.4 . 325 135 87 ALA N N 119.15 0.3 . 326 136 88 SER H H 8.10 0.05 . 327 136 88 SER CA C 63.74 0.4 . 328 136 88 SER CB C 63.25 0.4 . 329 136 88 SER N N 111.98 0.3 . 330 137 89 ARG H H 8.07 0.05 . 331 137 89 ARG CA C 58.96 0.4 . 332 137 89 ARG CB C 29.41 0.4 . 333 137 89 ARG N N 121.47 0.3 . 334 138 90 LYS H H 8.47 0.05 . 335 138 90 LYS CB C 30.97 0.4 . 336 138 90 LYS N N 118.10 0.3 . 337 139 91 TYR H H 8.47 0.05 . 338 139 91 TYR CB C 38.87 0.4 . 339 139 91 TYR N N 118.10 0.3 . 340 140 92 ALA H H 7.96 0.05 . 341 140 92 ALA CA C 55.03 0.4 . 342 140 92 ALA CB C 17.69 0.4 . 343 140 92 ALA N N 118.98 0.3 . 344 141 93 ARG H H 7.90 0.05 . 345 141 93 ARG CA C 57.80 0.4 . 346 141 93 ARG CB C 29.25 0.4 . 347 141 93 ARG N N 117.43 0.3 . 348 142 94 ILE H H 7.89 0.05 . 349 142 94 ILE CA C 65.20 0.4 . 350 142 94 ILE CB C 37.50 0.4 . 351 142 94 ILE N N 121.14 0.3 . 352 143 95 ILE H H 7.62 0.05 . 353 143 95 ILE CB C 35.83 0.4 . 354 143 95 ILE N N 118.35 0.3 . 355 144 96 GLN H H 8.36 0.05 . 356 144 96 GLN CA C 57.64 0.4 . 357 144 96 GLN CB C 28.28 0.4 . 358 144 96 GLN N N 119.80 0.3 . 359 145 97 LYS H H 8.42 0.05 . 360 145 97 LYS CA C 58.23 0.4 . 361 145 97 LYS CB C 31.49 0.4 . 362 145 97 LYS N N 120.21 0.3 . 363 146 98 ILE H H 7.66 0.05 . 364 146 98 ILE CA C 62.58 0.4 . 365 146 98 ILE CB C 37.62 0.4 . 366 146 98 ILE N N 117.46 0.3 . 367 147 99 GLY H H 7.58 0.05 . 368 147 99 GLY CA C 44.09 0.4 . 369 147 99 GLY N N 129.31 0.3 . 370 148 100 PHE H H 7.11 0.05 . 371 148 100 PHE CA C 57.02 0.4 . 372 148 100 PHE CB C 40.35 0.4 . 373 148 100 PHE N N 118.25 0.3 . 374 149 101 ALA H H 9.06 0.05 . 375 149 101 ALA CA C 50.61 0.4 . 376 149 101 ALA CB C 15.85 0.4 . 377 149 101 ALA N N 130.61 0.3 . 378 150 102 ALA H H 7.86 0.05 . 379 150 102 ALA CA C 50.32 0.4 . 380 150 102 ALA CB C 21.30 0.4 . 381 150 102 ALA N N 123.92 0.3 . 382 151 103 LYS H H 9.25 0.05 . 383 151 103 LYS CA C 54.21 0.4 . 384 151 103 LYS CB C 35.10 0.4 . 385 151 103 LYS N N 123.57 0.3 . 386 152 104 PHE H H 8.54 0.05 . 387 152 104 PHE CA C 57.05 0.4 . 388 152 104 PHE CB C 38.81 0.4 . 389 152 104 PHE N N 121.64 0.3 . 390 153 105 THR H H 7.45 0.05 . 391 153 105 THR CA C 60.26 0.4 . 392 153 105 THR CB C 70.98 0.4 . 393 153 105 THR N N 119.91 0.3 . 394 154 106 ASP H H 8.52 0.05 . 395 154 106 ASP CA C 53.81 0.4 . 396 154 106 ASP CB C 39.60 0.4 . 397 154 106 ASP N N 119.54 0.3 . 398 155 107 PHE H H 7.97 0.05 . 399 155 107 PHE CA C 58.49 0.4 . 400 155 107 PHE CB C 39.26 0.4 . 401 155 107 PHE N N 118.70 0.3 . 402 156 108 LYS H H 8.35 0.05 . 403 156 108 LYS CA C 54.47 0.4 . 404 156 108 LYS CB C 35.33 0.4 . 405 156 108 LYS N N 129.42 0.3 . 406 157 109 ILE H H 8.48 0.05 . 407 157 109 ILE CA C 61.71 0.4 . 408 157 109 ILE CB C 35.88 0.4 . 409 157 109 ILE N N 124.63 0.3 . 410 158 110 GLN H H 8.99 0.05 . 411 158 110 GLN CA C 54.18 0.4 . 412 158 110 GLN CB C 30.64 0.4 . 413 158 110 GLN N N 125.18 0.3 . 414 159 111 ASN H H 7.65 0.05 . 415 159 111 ASN CA C 53.81 0.4 . 416 159 111 ASN CB C 41.33 0.4 . 417 159 111 ASN N N 114.53 0.3 . 418 160 112 ILE H H 8.28 0.05 . 419 160 112 ILE CA C 60.32 0.4 . 420 160 112 ILE CB C 40.17 0.4 . 421 160 112 ILE N N 127.75 0.3 . 422 161 113 VAL H H 8.71 0.05 . 423 161 113 VAL CA C 58.85 0.4 . 424 161 113 VAL CB C 34.03 0.4 . 425 161 113 VAL N N 123.92 0.3 . 426 162 114 GLY H H 9.54 0.05 . 427 162 114 GLY CA C 42.99 0.4 . 428 162 114 GLY N N 113.31 0.3 . 429 163 115 SER H H 9.24 0.05 . 430 163 115 SER CA C 56.59 0.4 . 431 163 115 SER CB C 66.91 0.4 . 432 163 115 SER N N 114.44 0.3 . 433 164 116 CYS H H 8.92 0.05 . 434 164 116 CYS CA C 56.20 0.4 . 435 164 116 CYS CB C 30.47 0.4 . 436 164 116 CYS N N 116.48 0.3 . 437 165 117 ASP H H 8.17 0.05 . 438 165 117 ASP CA C 51.69 0.4 . 439 165 117 ASP CB C 42.30 0.4 . 440 165 117 ASP N N 121.86 0.3 . 441 166 118 VAL H H 8.52 0.05 . 442 166 118 VAL CA C 61.32 0.4 . 443 166 118 VAL CB C 30.97 0.4 . 444 166 118 VAL N N 116.99 0.3 . 445 167 119 LYS H H 8.63 0.05 . 446 167 119 LYS CA C 56.81 0.4 . 447 167 119 LYS CB C 28.24 0.4 . 448 167 119 LYS N N 111.77 0.3 . 449 168 120 PHE H H 7.11 0.05 . 450 168 120 PHE CA C 53.76 0.4 . 451 168 120 PHE CB C 38.32 0.4 . 452 168 120 PHE N N 115.14 0.3 . 453 169 121 PRO CA C 60.46 0.4 . 454 169 121 PRO CB C 31.50 0.4 . 455 170 122 ILE H H 8.36 0.05 . 456 170 122 ILE CA C 59.45 0.4 . 457 170 122 ILE CB C 40.54 0.4 . 458 170 122 ILE N N 119.80 0.3 . 459 171 123 ARG H H 9.08 0.05 . 460 171 123 ARG CA C 54.17 0.4 . 461 171 123 ARG CB C 28.18 0.4 . 462 171 123 ARG N N 126.01 0.3 . 463 172 124 LEU H H 7.79 0.05 . 464 172 124 LEU CA C 57.22 0.4 . 465 172 124 LEU CB C 39.68 0.4 . 466 172 124 LEU N N 126.17 0.3 . 467 173 125 GLU H H 9.25 0.05 . 468 173 125 GLU CA C 59.04 0.4 . 469 173 125 GLU CB C 27.91 0.4 . 470 173 125 GLU N N 116.17 0.3 . 471 174 126 GLY H H 7.36 0.05 . 472 174 126 GLY CA C 46.42 0.4 . 473 174 126 GLY N N 131.80 0.3 . 474 175 127 LEU H H 7.14 0.05 . 475 175 127 LEU CA C 57.50 0.4 . 476 175 127 LEU CB C 40.96 0.4 . 477 175 127 LEU N N 127.10 0.3 . 478 176 128 ALA H H 8.19 0.05 . 479 176 128 ALA CA C 53.54 0.4 . 480 176 128 ALA CB C 17.85 0.4 . 481 176 128 ALA N N 119.18 0.3 . 482 177 129 PHE H H 7.44 0.05 . 483 177 129 PHE CA C 59.45 0.4 . 484 177 129 PHE CB C 39.07 0.4 . 485 177 129 PHE N N 114.68 0.3 . 486 178 130 SER H H 7.99 0.05 . 487 178 130 SER CA C 60.62 0.4 . 488 178 130 SER CB C 64.06 0.4 . 489 178 130 SER N N 114.20 0.3 . 490 179 131 HIS H H 8.42 0.05 . 491 179 131 HIS CA C 54.61 0.4 . 492 179 131 HIS CB C 29.60 0.4 . 493 179 131 HIS N N 121.77 0.3 . 494 180 132 GLY H H 7.61 0.05 . 495 180 132 GLY CA C 47.52 0.4 . 496 180 132 GLY N N 111.85 0.3 . 497 181 133 THR H H 6.93 0.05 . 498 181 133 THR CA C 68.17 0.4 . 499 181 133 THR CB C 63.83 0.4 . 500 181 133 THR N N 116.35 0.3 . 501 182 134 PHE H H 6.93 0.05 . 502 182 134 PHE CA C 56.45 0.4 . 503 182 134 PHE CB C 40.56 0.4 . 504 182 134 PHE N N 116.35 0.3 . 505 183 135 SER H H 7.27 0.05 . 506 183 135 SER CA C 57.86 0.4 . 507 183 135 SER CB C 67.21 0.4 . 508 183 135 SER N N 112.36 0.3 . 509 184 136 SER H H 9.14 0.05 . 510 184 136 SER CA C 57.16 0.4 . 511 184 136 SER CB C 65.03 0.4 . 512 184 136 SER N N 117.27 0.3 . 513 185 137 TYR H H 9.20 0.05 . 514 185 137 TYR CA C 55.74 0.4 . 515 185 137 TYR CB C 39.20 0.4 . 516 185 137 TYR N N 127.20 0.3 . 517 186 138 GLU H H 9.60 0.05 . 518 186 138 GLU CA C 52.13 0.4 . 519 186 138 GLU CB C 29.83 0.4 . 520 186 138 GLU N N 129.34 0.3 . 521 187 139 PRO CA C 63.30 0.4 . 522 187 139 PRO CB C 30.58 0.4 . 523 188 140 GLU H H 8.73 0.05 . 524 188 140 GLU CA C 57.60 0.4 . 525 188 140 GLU CB C 28.45 0.4 . 526 188 140 GLU N N 117.80 0.3 . 527 189 141 LEU H H 7.96 0.05 . 528 189 141 LEU CA C 55.03 0.4 . 529 189 141 LEU CB C 43.55 0.4 . 530 189 141 LEU N N 118.98 0.3 . 531 190 142 PHE H H 8.02 0.05 . 532 190 142 PHE CA C 54.43 0.4 . 533 190 142 PHE CB C 41.81 0.4 . 534 190 142 PHE N N 118.79 0.3 . 535 191 143 PRO CA C 63.49 0.4 . 536 191 143 PRO CB C 31.30 0.4 . 537 192 144 GLY H H 5.99 0.05 . 538 192 144 GLY CA C 42.87 0.4 . 539 192 144 GLY N N 130.24 0.3 . 540 193 145 LEU H H 9.03 0.05 . 541 193 145 LEU CA C 54.22 0.4 . 542 193 145 LEU CB C 45.06 0.4 . 543 193 145 LEU N N 123.71 0.3 . 544 194 146 ILE H H 8.86 0.05 . 545 194 146 ILE CA C 59.67 0.4 . 546 194 146 ILE CB C 38.16 0.4 . 547 194 146 ILE N N 127.22 0.3 . 548 195 147 TYR H H 9.85 0.05 . 549 195 147 TYR CA C 56.01 0.4 . 550 195 147 TYR CB C 41.92 0.4 . 551 195 147 TYR N N 108.18 0.3 . 552 196 148 ARG H H 8.96 0.05 . 553 196 148 ARG CA C 55.02 0.4 . 554 196 148 ARG CB C 28.92 0.4 . 555 196 148 ARG N N 129.77 0.3 . 556 197 149 MET H H 8.34 0.05 . 557 197 149 MET CA C 55.64 0.4 . 558 197 149 MET CB C 34.27 0.4 . 559 197 149 MET N N 124.89 0.3 . 560 198 150 VAL H H 8.04 0.05 . 561 198 150 VAL CA C 63.74 0.4 . 562 198 150 VAL CB C 32.35 0.4 . 563 198 150 VAL N N 121.97 0.3 . 564 199 151 LYS H H 7.24 0.05 . 565 199 151 LYS CA C 53.11 0.4 . 566 199 151 LYS CB C 34.58 0.4 . 567 199 151 LYS N N 119.62 0.3 . 568 200 152 PRO CA C 62.51 0.4 . 569 200 152 PRO CB C 33.32 0.4 . 570 201 153 LYS H H 8.21 0.05 . 571 201 153 LYS CA C 55.22 0.4 . 572 201 153 LYS CB C 30.14 0.4 . 573 201 153 LYS N N 120.03 0.3 . 574 202 154 ILE H H 7.56 0.05 . 575 202 154 ILE CA C 56.51 0.4 . 576 202 154 ILE CB C 40.55 0.4 . 577 202 154 ILE N N 128.10 0.3 . 578 203 155 VAL H H 8.58 0.05 . 579 203 155 VAL CA C 60.90 0.4 . 580 203 155 VAL CB C 32.70 0.4 . 581 203 155 VAL N N 125.50 0.3 . 582 204 156 LEU H H 9.81 0.05 . 583 204 156 LEU CA C 53.72 0.4 . 584 204 156 LEU CB C 43.00 0.4 . 585 204 156 LEU N N 127.47 0.3 . 586 205 157 LEU H H 9.55 0.05 . 587 205 157 LEU CA C 56.70 0.4 . 588 205 157 LEU CB C 42.30 0.4 . 589 205 157 LEU N N 121.97 0.3 . 590 206 158 ILE H H 9.19 0.05 . 591 206 158 ILE CA C 60.68 0.4 . 592 206 158 ILE CB C 27.80 0.4 . 593 206 158 ILE N N 124.05 0.3 . 594 207 159 PHE H H 8.73 0.05 . 595 207 159 PHE CA C 56.69 0.4 . 596 207 159 PHE CB C 39.75 0.4 . 597 207 159 PHE N N 119.16 0.3 . 598 208 160 VAL H H 9.55 0.05 . 599 208 160 VAL CA C 64.22 0.4 . 600 208 160 VAL CB C 31.66 0.4 . 601 208 160 VAL N N 121.97 0.3 . 602 209 161 SER H H 7.56 0.05 . 603 209 161 SER CA C 57.84 0.4 . 604 209 161 SER CB C 64.23 0.4 . 605 209 161 SER N N 109.54 0.3 . 606 210 162 GLY H H 8.18 0.05 . 607 210 162 GLY CA C 44.81 0.4 . 608 210 162 GLY N N 111.06 0.3 . 609 211 163 LYS H H 7.28 0.05 . 610 211 163 LYS CA C 56.05 0.4 . 611 211 163 LYS CB C 32.06 0.4 . 612 211 163 LYS N N 119.80 0.3 . 613 212 164 ILE H H 8.86 0.05 . 614 212 164 ILE CA C 58.02 0.4 . 615 212 164 ILE CB C 39.99 0.4 . 616 212 164 ILE N N 120.06 0.3 . 617 213 165 VAL H H 9.49 0.05 . 618 213 165 VAL CA C 60.49 0.4 . 619 213 165 VAL CB C 34.33 0.4 . 620 213 165 VAL N N 126.32 0.3 . 621 214 166 LEU H H 9.33 0.05 . 622 214 166 LEU CA C 55.18 0.4 . 623 214 166 LEU CB C 43.59 0.4 . 624 214 166 LEU N N 126.28 0.3 . 625 215 167 THR H H 9.28 0.05 . 626 215 167 THR CA C 59.50 0.4 . 627 215 167 THR CB C 71.04 0.4 . 628 215 167 THR N N 115.82 0.3 . 629 216 168 GLY H H 8.58 0.05 . 630 216 168 GLY CA C 44.03 0.4 . 631 216 168 GLY N N 112.99 0.3 . 632 217 169 ALA H H 7.02 0.05 . 633 217 169 ALA CA C 51.31 0.4 . 634 217 169 ALA CB C 21.14 0.4 . 635 217 169 ALA N N 121.03 0.3 . 636 218 170 LYS H H 8.99 0.05 . 637 218 170 LYS CA C 54.57 0.4 . 638 218 170 LYS CB C 32.87 0.4 . 639 218 170 LYS N N 116.01 0.3 . 640 219 171 GLN H H 7.48 0.05 . 641 219 171 GLN CA C 53.40 0.4 . 642 219 171 GLN CB C 31.93 0.4 . 643 219 171 GLN N N 115.00 0.3 . 644 220 172 ARG H H 9.71 0.05 . 645 220 172 ARG CA C 59.63 0.4 . 646 220 172 ARG CB C 29.94 0.4 . 647 220 172 ARG N N 125.02 0.3 . 648 221 173 GLU H H 9.43 0.05 . 649 221 173 GLU CA C 59.50 0.4 . 650 221 173 GLU CB C 28.31 0.4 . 651 221 173 GLU N N 118.54 0.3 . 652 222 174 GLU H H 7.51 0.05 . 653 222 174 GLU CA C 58.26 0.4 . 654 222 174 GLU CB C 30.14 0.4 . 655 222 174 GLU N N 116.04 0.3 . 656 223 175 ILE H H 7.08 0.05 . 657 223 175 ILE CA C 61.72 0.4 . 658 223 175 ILE CB C 34.94 0.4 . 659 223 175 ILE N N 116.79 0.3 . 660 224 176 TYR H H 6.80 0.05 . 661 224 176 TYR CA C 58.78 0.4 . 662 224 176 TYR CB C 35.93 0.4 . 663 224 176 TYR N N 118.60 0.3 . 664 225 177 GLN H H 8.55 0.05 . 665 225 177 GLN CA C 57.87 0.4 . 666 225 177 GLN CB C 28.18 0.4 . 667 225 177 GLN N N 118.74 0.3 . 668 226 178 ALA H H 8.17 0.05 . 669 226 178 ALA CA C 54.17 0.4 . 670 226 178 ALA CB C 19.87 0.4 . 671 226 178 ALA N N 121.86 0.3 . 672 227 179 PHE H H 8.03 0.05 . 673 227 179 PHE CA C 60.49 0.4 . 674 227 179 PHE CB C 38.56 0.4 . 675 227 179 PHE N N 116.64 0.3 . 676 228 180 GLU H H 8.16 0.05 . 677 228 180 GLU CA C 58.41 0.4 . 678 228 180 GLU CB C 28.88 0.4 . 679 228 180 GLU N N 117.44 0.3 . 680 229 181 ALA H H 7.57 0.05 . 681 229 181 ALA CA C 53.42 0.4 . 682 229 181 ALA CB C 18.21 0.4 . 683 229 181 ALA N N 118.10 0.3 . 684 230 182 ILE H H 7.86 0.05 . 685 230 182 ILE CA C 57.05 0.4 . 686 230 182 ILE CB C 39.11 0.4 . 687 230 182 ILE N N 116.57 0.3 . 688 231 183 TYR H H 8.05 0.05 . 689 231 183 TYR CA C 63.53 0.4 . 690 231 183 TYR CB C 34.76 0.4 . 691 231 183 TYR N N 125.97 0.3 . 692 232 184 PRO CA C 64.55 0.4 . 693 232 184 PRO CB C 30.98 0.4 . 694 233 185 VAL H H 6.97 0.05 . 695 233 185 VAL CA C 64.55 0.4 . 696 233 185 VAL CB C 30.98 0.4 . 697 233 185 VAL N N 118.75 0.3 . 698 234 186 LEU H H 7.85 0.05 . 699 234 186 LEU CA C 57.40 0.4 . 700 234 186 LEU CB C 39.11 0.4 . 701 234 186 LEU N N 116.72 0.3 . 702 235 187 SER H H 7.81 0.05 . 703 235 187 SER CA C 60.54 0.4 . 704 235 187 SER CB C 62.61 0.4 . 705 235 187 SER N N 108.65 0.3 . 706 236 188 GLU H H 7.47 0.05 . 707 236 188 GLU CA C 57.65 0.4 . 708 236 188 GLU CB C 28.47 0.4 . 709 236 188 GLU N N 121.97 0.3 . 710 237 189 PHE H H 7.41 0.05 . 711 237 189 PHE CA C 57.65 0.4 . 712 237 189 PHE CB C 37.81 0.4 . 713 237 189 PHE N N 115.92 0.3 . 714 238 190 ARG H H 6.91 0.05 . 715 238 190 ARG CA C 55.77 0.4 . 716 238 190 ARG CB C 30.64 0.4 . 717 238 190 ARG N N 120.96 0.3 . 718 239 191 LYS H H 8.63 0.05 . 719 239 191 LYS CA C 55.89 0.4 . 720 239 191 LYS CB C 32.60 0.4 . 721 239 191 LYS N N 128.45 0.3 . 722 240 192 MET H H 8.11 0.05 . 723 240 192 MET CA C 56.00 0.4 . 724 240 192 MET CB C 32.97 0.4 . 725 240 192 MET N N 130.99 0.3 . stop_ save_