data_4223 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of a TBP-TAFII230 Complex: Protein Mimicry of the Minor Groove Surface of the TATA Box Unwound by TBP ; _BMRB_accession_number 4223 _BMRB_flat_file_name bmr4223.str _Entry_type original _Submission_date 1998-08-16 _Accession_date 1999-04-12 _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 Liu D. . . 2 Ishima R. . . 3 Tong K. I. . 4 Baby S. . . 5 Kokubo T. . . 6 Muhandiram D. R. . 7 Kay L. E. . 8 Nakatani Y. . . 9 Ikura M. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 318 "13C chemical shifts" 239 "15N chemical shifts" 69 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-12-06 original author . stop_ _Original_release_date 1999-12-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure of a TBP-TAFII230 Complex: Protein Mimicry of the Minor Groove Surface of the TATA Box Unwound by TB ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98412653 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liu Dingjiang . . 2 Ishima R. . . 3 Tong K. I. . 4 Bagby S. . . 5 Kokubo T. . . 6 Muhandiram D. R. . 7 Kay L. E. . 8 Nakatani Y. . . 9 Ikura M. . . stop_ _Journal_abbreviation Cell _Journal_volume 94 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 573 _Page_last 583 _Year 1998 _Details . loop_ _Keyword 'NMR solution structure' TAF TAFII230 TBP TFIID 'Transcription factors' stop_ save_ ################################## # Molecular system description # ################################## save_TAFII230 _Saveframe_category molecular_system _Mol_system_name 'TATA box binding protein associated factor II 230' _Abbreviation_common TAFII230 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label TAFII230 $TAF stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'transcription factor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TAF _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'TATA box binding protein associated factor' _Abbreviation_common TAF _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 67 _Mol_residue_sequence ; EGSIGNGLDLTGILFGNIDS EGRLLQDDDGEGRGGTGFDA ELRENIGSLSKLGLDSMLLE VIDLKEA ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 GLY 3 SER 4 ILE 5 GLY 6 ASN 7 GLY 8 LEU 9 ASP 10 LEU 11 THR 12 GLY 13 ILE 14 LEU 15 PHE 16 GLY 17 ASN 18 ILE 19 ASP 20 SER 21 GLU 22 GLY 23 ARG 24 LEU 25 LEU 26 GLN 27 ASP 28 ASP 29 ASP 30 GLY 31 GLU 32 GLY 33 ARG 34 GLY 35 GLY 36 THR 37 GLY 38 PHE 39 ASP 40 ALA 41 GLU 42 LEU 43 ARG 44 GLU 45 ASN 46 ILE 47 GLY 48 SER 49 LEU 50 SER 51 LYS 52 LEU 53 GLY 54 LEU 55 ASP 56 SER 57 MET 58 LEU 59 LEU 60 GLU 61 VAL 62 ILE 63 ASP 64 LEU 65 LYS 66 GLU 67 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 PDB 1TBA "Solution Structure Of A Tbp-Tafii230 Complex: Protein Mimicry Of The Minor Groove Surface Of The Tata Box Unwound By Tbp, Nmr, " 100.00 67 100.00 100.00 2.07e-34 GB AAB26991 "transcription factor TFIID 230 kda subunit [Drosophila melanogaster]" 100.00 2068 100.00 100.00 1.18e-33 GB AAD19815 "transcription factor [Drosophila melanogaster]" 100.00 2065 100.00 100.00 8.89e-34 GB AAF54102 "TBP-associated factor 1, isoform A [Drosophila melanogaster]" 100.00 2065 100.00 100.00 8.89e-34 GB AAO47866 "RE74933p [Drosophila melanogaster]" 100.00 2096 100.00 100.00 1.54e-33 GB AAS65116 "TBP-associated factor 1, isoform B [Drosophila melanogaster]" 100.00 2129 100.00 100.00 1.19e-33 REF NP_001163532 "TBP-associated factor 1, isoform D [Drosophila melanogaster]" 100.00 2096 100.00 100.00 1.33e-33 REF NP_001246952 "TBP-associated factor 1, isoform E [Drosophila melanogaster]" 100.00 2172 100.00 100.00 9.08e-34 REF NP_001287201 "TBP-associated factor 1, isoform F [Drosophila melanogaster]" 100.00 2097 100.00 100.00 1.33e-33 REF NP_476956 "TBP-associated factor 1, isoform A [Drosophila melanogaster]" 100.00 2065 100.00 100.00 8.89e-34 REF NP_996159 "TBP-associated factor 1, isoform C [Drosophila melanogaster]" 100.00 2098 100.00 100.00 8.70e-34 SP P51123 "RecName: Full=Transcription initiation factor TFIID subunit 1; AltName: Full=TAFII250; AltName: Full=TBP-associated factor 230 " 100.00 2129 100.00 100.00 1.19e-33 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TAF Drosophila 7215 Eukaryota Metazoa Drosophila . 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 $TAF 'recombinant technology' 'Escherichia coli' 'Escherichia coli' . BL21 . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $TAF 1.0 mM 0.6 1.25 '[U-13C; U-15N; U60%-2H]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TAF 1.0 mM '[U-13C; U-15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.75 . M pH 7.0 0.2 n/a temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation 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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name TAFII230 _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 . 4 ILE N N 122.43 . 1 2 . 4 ILE H H 8.25 . 1 3 . 4 ILE CA C 61.60 . 1 4 . 4 ILE HA H 4.22 . 1 5 . 4 ILE CB C 38.74 . 1 6 . 4 ILE HB H 1.94 . 1 7 . 4 ILE CG1 C 27.62 . 1 8 . 4 ILE HG12 H 1.47 . 1 9 . 4 ILE HG13 H 1.19 . 1 10 . 4 ILE CD1 C 13.24 . 1 11 . 4 ILE HD1 H 0.82 . 1 12 . 4 ILE CG2 C 17.67 . 1 13 . 4 ILE HG2 H 0.91 . 1 14 . 4 ILE C C 176.74 . 1 15 . 5 GLY N N 112.57 . 1 16 . 5 GLY H H 8.43 . 1 17 . 5 GLY CA C 45.51 . 1 18 . 5 GLY HA2 H 3.98 . 1 19 . 5 GLY HA3 H 3.98 . 1 20 . 5 GLY C C 173.97 . 1 21 . 6 ASN N N 119.27 . 1 22 . 6 ASN H H 8.40 . 1 23 . 6 ASN CA C 53.24 . 1 24 . 6 ASN HA H 4.78 . 1 25 . 6 ASN CB C 39.21 . 1 26 . 6 ASN HB2 H 2.89 . 1 27 . 6 ASN HB3 H 2.78 . 1 28 . 6 ASN ND2 N 113.06 . 1 29 . 6 ASN HD21 H 6.91 . 1 30 . 6 ASN HD22 H 7.61 . 1 31 . 6 ASN C C 175.70 . 1 32 . 7 GLY N N 109.53 . 1 33 . 7 GLY H H 8.44 . 1 34 . 7 GLY CA C 45.55 . 1 35 . 7 GLY HA2 H 3.96 . 1 36 . 7 GLY HA3 H 3.96 . 1 37 . 7 GLY C C 173.57 . 1 38 . 8 LEU N N 122.35 . 1 39 . 8 LEU H H 7.99 . 1 40 . 8 LEU CA C 54.92 . 1 41 . 8 LEU HA H 4.30 . 1 42 . 8 LEU CB C 43.64 . 1 43 . 8 LEU HB2 H 1.45 . 1 44 . 8 LEU HB3 H 1.32 . 1 45 . 8 LEU CG C 27.16 . 1 46 . 8 LEU HG H 1.28 . 1 47 . 8 LEU CD1 C 24.05 . 1 48 . 8 LEU HD1 H 0.67 . 1 49 . 8 LEU CD2 C 24.75 . 1 50 . 8 LEU HD2 H 0.57 . 1 51 . 8 LEU C C 175.42 . 1 52 . 9 ASP N N 124.87 . 1 53 . 9 ASP H H 8.46 . 1 54 . 9 ASP CA C 53.74 . 1 55 . 9 ASP HA H 4.72 . 1 56 . 9 ASP CB C 41.85 . 1 57 . 9 ASP HB2 H 2.88 . 1 58 . 9 ASP HB3 H 2.66 . 1 59 . 9 ASP C C 176.89 . 1 60 . 10 LEU N N 125.85 . 1 61 . 10 LEU H H 8.63 . 1 62 . 10 LEU CA C 54.82 . 1 63 . 10 LEU HA H 4.38 . 1 64 . 10 LEU CB C 42.47 . 1 65 . 10 LEU HB2 H 1.66 . 1 66 . 10 LEU CG C 26.85 . 1 67 . 10 LEU HG H 1.32 . 1 68 . 10 LEU CD1 C 25.55 . 1 69 . 10 LEU HD1 H 0.46 . 1 70 . 10 LEU CD2 C 22.87 . 1 71 . 10 LEU HD2 H 0.34 . 1 72 . 10 LEU C C 176.52 . 1 73 . 11 THR N N 117.45 . 1 74 . 11 THR H H 8.26 . 1 75 . 11 THR CA C 67.50 . 1 76 . 11 THR HA H 3.92 . 1 77 . 11 THR CB C 67.90 . 1 78 . 11 THR HB H 3.53 . 1 79 . 11 THR CG2 C 22.15 . 1 80 . 11 THR HG2 H 1.17 . 1 81 . 11 THR C C 175.31 . 1 82 . 12 GLY N N 106.28 . 1 83 . 12 GLY H H 9.27 . 1 84 . 12 GLY CA C 47.94 . 1 85 . 12 GLY HA2 H 3.57 . 1 86 . 12 GLY C C 174.95 . 1 87 . 13 ILE N N 115.31 . 1 88 . 13 ILE H H 8.05 . 1 89 . 13 ILE CA C 63.36 . 1 90 . 13 ILE HA H 4.45 . 1 91 . 13 ILE CB C 39.66 . 1 92 . 13 ILE HB H 1.89 . 1 93 . 13 ILE CG1 C 27.14 . 1 94 . 13 ILE HG12 H 1.40 . 1 95 . 13 ILE HG13 H 1.40 . 1 96 . 13 ILE CD1 C 15.35 . 1 97 . 13 ILE HD1 H 0.73 . 1 98 . 13 ILE CG2 C 18.23 . 1 99 . 13 ILE HG2 H 0.93 . 1 100 . 13 ILE C C 177.58 . 1 101 . 14 LEU N N 117.96 . 1 102 . 14 LEU H H 7.72 . 1 103 . 14 LEU CA C 57.31 . 1 104 . 14 LEU HA H 3.57 . 1 105 . 14 LEU CB C 42.09 . 1 106 . 14 LEU HB2 H 1.40 . 1 107 . 14 LEU HG H 1.60 . 1 108 . 14 LEU CD1 C 25.63 . 1 109 . 14 LEU HD1 H 0.73 . 1 110 . 14 LEU CD2 C 22.26 . 1 111 . 14 LEU HD2 H 0.54 . 1 112 . 14 LEU C C 177.03 . 1 113 . 15 PHE N N 112.58 . 1 114 . 15 PHE H H 7.54 . 1 115 . 15 PHE CA C 59.27 . 1 116 . 15 PHE HA H 4.27 . 1 117 . 15 PHE CB C 42.34 . 1 118 . 15 PHE HB3 H 3.12 . 1 119 . 15 PHE HB2 H 2.71 . 1 120 . 15 PHE HD1 H 6.99 . 1 121 . 15 PHE HE1 H 6.85 . 1 122 . 15 PHE HZ H 6.80 . 1 123 . 15 PHE HE2 H 6.85 . 1 124 . 15 PHE HD2 H 6.99 . 1 125 . 15 PHE C C 174.31 . 1 126 . 16 GLY N N 107.55 . 1 127 . 16 GLY H H 7.56 . 1 128 . 16 GLY CA C 46.08 . 1 129 . 16 GLY HA2 H 3.69 . 1 130 . 16 GLY HA3 H 4.21 . 1 131 . 17 ASN N N 112.83 . 1 132 . 17 ASN H H 8.16 . 1 133 . 17 ASN CA C 55.58 . 1 134 . 17 ASN HA H 4.20 . 1 135 . 17 ASN CB C 40.73 . 1 136 . 17 ASN HB2 H 2.52 . 1 137 . 17 ASN HB3 H 2.39 . 1 138 . 17 ASN ND2 N 113.68 . 1 139 . 17 ASN HD21 H 6.52 . 1 140 . 17 ASN HD22 H 7.90 . 1 141 . 18 ILE N N 107.98 . 1 142 . 18 ILE H H 6.20 . 1 143 . 18 ILE CA C 58.47 . 1 144 . 18 ILE HA H 5.50 . 1 145 . 18 ILE CB C 41.09 . 1 146 . 18 ILE CD1 C 14.19 . 1 147 . 18 ILE HD1 H 0.73 . 1 148 . 18 ILE CG2 C 16.79 . 1 149 . 18 ILE HG2 H 0.60 . 1 150 . 19 ASP N N 122.18 . 1 151 . 19 ASP H H 8.55 . 1 152 . 19 ASP CA C 52.56 . 1 153 . 19 ASP HA H 4.65 . 1 154 . 19 ASP CB C 42.38 . 1 155 . 19 ASP HB2 H 3.40 . 1 156 . 19 ASP HB3 H 2.61 . 1 157 . 20 SER N N 111.36 . 1 158 . 20 SER H H 8.30 . 1 159 . 20 SER CA C 61.12 . 1 160 . 20 SER HA H 4.18 . 1 161 . 20 SER CB C 63.95 . 1 162 . 20 SER HB3 H 3.96 . 1 163 . 21 GLU N N 118.04 . 1 164 . 21 GLU H H 8.09 . 1 165 . 21 GLU CA C 55.57 . 1 166 . 21 GLU HA H 4.41 . 1 167 . 21 GLU CB C 31.08 . 1 168 . 21 GLU HB3 H 2.30 . 1 169 . 21 GLU HB2 H 1.90 . 1 170 . 21 GLU CG C 36.78 . 1 171 . 21 GLU HG2 H 2.20 . 1 172 . 21 GLU HG3 H 2.09 . 1 173 . 22 GLY N N 108.05 . 1 174 . 22 GLY H H 8.16 . 1 175 . 22 GLY CA C 45.58 . 1 176 . 23 ARG N N 122.19 . 1 177 . 23 ARG H H 8.48 . 1 178 . 23 ARG CA C 56.28 . 1 179 . 23 ARG HA H 4.24 . 1 180 . 23 ARG CB C 31.04 . 1 181 . 23 ARG HB2 H 1.89 . 1 182 . 23 ARG CG C 28.24 . 1 183 . 23 ARG HG3 H 1.61 . 1 184 . 23 ARG HG2 H 1.46 . 1 185 . 23 ARG CD C 43.30 . 1 186 . 23 ARG HD3 H 3.23 . 1 187 . 23 ARG HD2 H 3.13 . 1 188 . 23 ARG NE N 86.37 . 1 189 . 23 ARG HE H 7.75 . 1 190 . 24 LEU N N 122.78 . 1 191 . 24 LEU H H 8.29 . 1 192 . 24 LEU CA C 54.50 . 1 193 . 24 LEU HA H 4.29 . 1 194 . 24 LEU CB C 44.04 . 1 195 . 24 LEU HB2 H 1.40 . 1 196 . 24 LEU CD1 C 25.62 . 1 197 . 24 LEU HD1 H 0.70 . 1 198 . 24 LEU CD2 C 23.90 . 1 199 . 24 LEU HD2 H 0.85 . 1 200 . 24 LEU C C 177.06 . 1 201 . 25 LEU N N 127.23 . 1 202 . 25 LEU H H 8.30 . 1 203 . 25 LEU CA C 54.79 . 1 204 . 25 LEU HA H 4.28 . 1 205 . 25 LEU CB C 43.66 . 1 206 . 25 LEU HB2 H 1.59 . 1 207 . 25 LEU CG C 27.62 . 1 208 . 25 LEU HG H 1.59 . 1 209 . 25 LEU CD1 C 25.63 . 1 210 . 25 LEU HD1 H 0.69 . 1 211 . 25 LEU CD2 C 23.05 . 1 212 . 25 LEU HD2 H 0.80 . 1 213 . 25 LEU C C 177.35 . 1 214 . 26 GLN N N 122.71 . 1 215 . 26 GLN H H 8.63 . 1 216 . 26 GLN CA C 55.66 . 1 217 . 26 GLN HA H 4.35 . 1 218 . 26 GLN CB C 30.14 . 1 219 . 26 GLN HB3 H 1.91 . 1 220 . 26 GLN HB2 H 2.05 . 1 221 . 26 GLN CG C 34.15 . 1 222 . 26 GLN HG2 H 2.30 . 1 223 . 26 GLN NE2 N 112.40 . 1 224 . 26 GLN HE21 H 7.68 . 1 225 . 26 GLN HE22 H 6.87 . 1 226 . 27 ASP N N 124.01 . 1 227 . 27 ASP H H 8.52 . 1 228 . 27 ASP CA C 54.38 . 1 229 . 27 ASP HA H 4.63 . 1 230 . 27 ASP CB C 41.68 . 1 231 . 27 ASP HB2 H 2.71 . 1 232 . 27 ASP HB3 H 2.59 . 1 233 . 27 ASP C C 175.81 . 1 234 . 28 ASP N N 121.46 . 1 235 . 28 ASP H H 8.40 . 1 236 . 28 ASP CA C 54.54 . 1 237 . 28 ASP HA H 4.60 . 1 238 . 28 ASP CB C 41.63 . 1 239 . 28 ASP HB3 H 2.71 . 1 240 . 29 ASP N N 121.25 . 1 241 . 29 ASP H H 8.38 . 1 242 . 29 ASP CA C 54.60 . 1 243 . 29 ASP HA H 4.59 . 1 244 . 29 ASP CB C 41.33 . 1 245 . 29 ASP HB3 H 2.71 . 1 246 . 29 ASP C C 177.08 . 1 247 . 30 GLY N N 109.53 . 1 248 . 30 GLY H H 8.44 . 1 249 . 30 GLY CA C 45.84 . 1 250 . 30 GLY HA3 H 3.96 . 1 251 . 30 GLY C C 174.81 . 1 252 . 31 GLU N N 120.74 . 1 253 . 31 GLU H H 8.37 . 1 254 . 31 GLU CA C 56.83 . 1 255 . 31 GLU HA H 4.27 . 1 256 . 31 GLU CB C 30.11 . 1 257 . 31 GLU HB3 H 2.09 . 1 258 . 31 GLU HB2 H 1.96 . 1 259 . 31 GLU CG C 36.31 . 1 260 . 31 GLU HG2 H 2.26 . 1 261 . 31 GLU HG3 H 2.23 . 1 262 . 31 GLU C C 177.40 . 1 263 . 32 GLY N N 110.00 . 1 264 . 32 GLY H H 8.49 . 1 265 . 32 GLY CA C 45.87 . 1 266 . 32 GLY HA2 H 3.97 . 1 267 . 32 GLY C C 174.90 . 1 268 . 33 ARG N N 120.63 . 1 269 . 33 ARG H H 8.25 . 1 270 . 33 ARG CA C 56.40 . 1 271 . 33 ARG HA H 4.36 . 1 272 . 33 ARG CB C 30.54 . 1 273 . 33 ARG HB2 H 1.93 . 1 274 . 33 ARG HB3 H 1.76 . 1 275 . 33 ARG CG C 27.31 . 1 276 . 33 ARG HG3 H 1.60 . 1 277 . 33 ARG CD C 43.15 . 1 278 . 33 ARG HD2 H 3.17 . 1 279 . 33 ARG C C 177.15 . 1 280 . 34 GLY N N 110.18 . 1 281 . 34 GLY H H 8.58 . 1 282 . 34 GLY CA C 45.62 . 1 283 . 34 GLY HA2 H 3.98 . 1 284 . 34 GLY C C 174.94 . 1 285 . 35 GLY N N 109.37 . 1 286 . 35 GLY H H 8.31 . 1 287 . 35 GLY CA C 45.53 . 1 288 . 35 GLY HA2 H 4.01 . 1 289 . 35 GLY C C 174.60 . 1 290 . 36 THR N N 112.75 . 1 291 . 36 THR H H 8.11 . 1 292 . 36 THR CA C 61.76 . 1 293 . 36 THR HA H 4.35 . 1 294 . 36 THR CB C 70.02 . 1 295 . 36 THR HB H 4.18 . 1 296 . 36 THR CG2 C 21.54 . 1 297 . 36 THR HG2 H 1.16 . 1 298 . 36 THR C C 175.04 . 1 299 . 37 GLY N N 111.20 . 1 300 . 37 GLY H H 8.33 . 1 301 . 37 GLY CA C 44.99 . 1 302 . 37 GLY HA2 H 3.78 . 1 303 . 37 GLY C C 173.99 . 1 304 . 38 PHE N N 119.80 . 1 305 . 38 PHE H H 8.35 . 1 306 . 38 PHE CA C 56.20 . 1 307 . 38 PHE HA H 4.64 . 1 308 . 38 PHE CB C 42.53 . 1 309 . 38 PHE HB3 H 3.09 . 1 310 . 38 PHE HB2 H 2.71 . 1 311 . 38 PHE HD1 H 7.24 . 1 312 . 38 PHE HE1 H 7.35 . 1 313 . 38 PHE HZ H 7.40 . 1 314 . 38 PHE HE2 H 7.35 . 1 315 . 38 PHE HD2 H 7.24 . 1 316 . 38 PHE C C 175.85 . 1 317 . 39 ASP N N 122.60 . 1 318 . 39 ASP H H 8.63 . 1 319 . 39 ASP CA C 53.73 . 1 320 . 39 ASP HA H 4.35 . 1 321 . 39 ASP CB C 42.24 . 1 322 . 39 ASP HB2 H 2.43 . 1 323 . 39 ASP HB3 H 2.20 . 1 324 . 39 ASP C C 177.03 . 1 325 . 40 ALA N N 127.05 . 1 326 . 40 ALA H H 8.61 . 1 327 . 40 ALA CA C 55.82 . 1 328 . 40 ALA HA H 3.83 . 1 329 . 40 ALA CB C 18.73 . 1 330 . 40 ALA HB H 1.37 . 1 331 . 40 ALA C C 178.52 . 1 332 . 41 GLU N N 115.51 . 1 333 . 41 GLU H H 8.72 . 1 334 . 41 GLU CA C 59.37 . 1 335 . 41 GLU HA H 3.82 . 1 336 . 41 GLU CB C 29.47 . 1 337 . 41 GLU HB3 H 1.69 . 1 338 . 41 GLU HB2 H 1.57 . 1 339 . 41 GLU CG C 37.09 . 1 340 . 41 GLU HG2 H 1.97 . 1 341 . 41 GLU HG3 H 2.10 . 1 342 . 41 GLU C C 178.27 . 1 343 . 42 LEU N N 117.32 . 1 344 . 42 LEU H H 7.08 . 1 345 . 42 LEU CA C 57.84 . 1 346 . 42 LEU HA H 4.18 . 1 347 . 42 LEU HB2 H 1.55 . 1 348 . 42 LEU HB3 H 1.32 . 1 349 . 42 LEU CG C 27.78 . 1 350 . 42 LEU HG H 1.06 . 1 351 . 42 LEU CD1 C 24.40 . 1 352 . 42 LEU HD1 H 0.40 . 1 353 . 42 LEU CD2 C 24.56 . 1 354 . 42 LEU HD2 H 0.11 . 1 355 . 42 LEU C C 177.84 . 1 356 . 43 ARG N N 115.87 . 1 357 . 43 ARG H H 7.71 . 1 358 . 43 ARG CA C 60.52 . 1 359 . 43 ARG HA H 3.60 . 1 360 . 43 ARG CB C 30.99 . 1 361 . 43 ARG HB2 H 1.77 . 1 362 . 43 ARG HB3 H 1.74 . 1 363 . 43 ARG CG C 28.55 . 1 364 . 43 ARG HG3 H 1.60 . 1 365 . 43 ARG HG2 H 1.45 . 1 366 . 43 ARG CD C 43.31 . 1 367 . 43 ARG HD2 H 3.13 . 1 368 . 43 ARG C C 178.47 . 1 369 . 44 GLU N N 114.65 . 1 370 . 44 GLU H H 8.50 . 1 371 . 44 GLU CA C 57.58 . 1 372 . 44 GLU HA H 4.19 . 1 373 . 44 GLU CB C 30.00 . 1 374 . 44 GLU HB3 H 2.12 . 1 375 . 44 GLU HB2 H 1.86 . 1 376 . 44 GLU CG C 36.63 . 1 377 . 44 GLU HG2 H 2.37 . 1 378 . 44 GLU HG3 H 2.27 . 1 379 . 44 GLU C C 177.38 . 1 380 . 45 ASN N N 114.87 . 1 381 . 45 ASN H H 7.46 . 1 382 . 45 ASN CA C 53.82 . 1 383 . 45 ASN HA H 5.32 . 1 384 . 45 ASN CB C 40.94 . 1 385 . 45 ASN HB2 H 3.29 . 1 386 . 45 ASN HB3 H 2.69 . 1 387 . 45 ASN ND2 N 118.53 . 1 388 . 45 ASN HD21 H 7.45 . 1 389 . 45 ASN HD22 H 8.39 . 1 390 . 45 ASN C C 175.60 . 1 391 . 46 ILE N N 120.68 . 1 392 . 46 ILE H H 7.26 . 1 393 . 46 ILE CA C 63.86 . 1 394 . 46 ILE HA H 3.72 . 1 395 . 46 ILE CB C 38.05 . 1 396 . 46 ILE HB H 1.88 . 1 397 . 46 ILE CG1 C 28.24 . 1 398 . 46 ILE HG12 H 1.13 . 1 399 . 46 ILE HG13 H 1.45 . 1 400 . 46 ILE CD1 C 13.63 . 1 401 . 46 ILE HD1 H 0.50 . 1 402 . 46 ILE CG2 C 17.91 . 1 403 . 46 ILE HG2 H 0.81 . 1 404 . 46 ILE C C 177.40 . 1 405 . 47 GLY N N 108.75 . 1 406 . 47 GLY H H 8.81 . 1 407 . 47 GLY CA C 46.77 . 1 408 . 47 GLY HA2 H 3.91 . 1 409 . 47 GLY HA3 H 4.05 . 1 410 . 47 GLY C C 175.99 . 1 411 . 48 SER N N 115.83 . 1 412 . 48 SER H H 7.85 . 1 413 . 48 SER CA C 59.89 . 1 414 . 48 SER HA H 4.51 . 1 415 . 48 SER CB C 64.24 . 1 416 . 48 SER HB2 H 4.18 . 1 417 . 49 LEU N N 120.22 . 1 418 . 49 LEU H H 7.69 . 1 419 . 49 LEU CA C 56.35 . 1 420 . 49 LEU HA H 3.76 . 1 421 . 49 LEU CB C 40.98 . 1 422 . 49 LEU HB2 H 1.89 . 1 423 . 49 LEU CG C 27.00 . 1 424 . 49 LEU HG H 1.38 . 1 425 . 49 LEU CD1 C 25.75 . 1 426 . 49 LEU HD1 H 0.56 . 1 427 . 49 LEU CD2 C 22.01 . 1 428 . 49 LEU HD2 H -0.07 . 1 429 . 49 LEU C C 179.33 . 1 430 . 50 SER N N 115.98 . 1 431 . 50 SER H H 8.57 . 1 432 . 50 SER CA C 62.56 . 1 433 . 50 SER HA H 4.04 . 1 434 . 50 SER CB C 62.56 . 1 435 . 50 SER HB3 H 4.00 . 1 436 . 50 SER C C 176.82 . 1 437 . 51 LYS N N 119.85 . 1 438 . 51 LYS H H 7.57 . 1 439 . 51 LYS CA C 57.38 . 1 440 . 51 LYS HA H 4.32 . 1 441 . 51 LYS CB C 32.34 . 1 442 . 51 LYS HB3 H 2.01 . 1 443 . 51 LYS HB2 H 1.96 . 1 444 . 51 LYS CG C 25.45 . 1 445 . 51 LYS HG2 H 1.52 . 1 446 . 51 LYS CD C 29.49 . 1 447 . 51 LYS HD2 H 1.74 . 1 448 . 51 LYS CE C 42.37 . 1 449 . 51 LYS HE2 H 3.01 . 1 450 . 51 LYS C C 177.47 . 1 451 . 52 LEU N N 119.03 . 1 452 . 52 LEU H H 7.35 . 1 453 . 52 LEU CA C 54.67 . 1 454 . 52 LEU HA H 4.43 . 1 455 . 52 LEU CB C 42.11 . 1 456 . 52 LEU HB2 H 1.56 . 1 457 . 52 LEU HB3 H 1.73 . 1 458 . 52 LEU HG H 1.61 . 1 459 . 52 LEU CD1 C 26.28 . 1 460 . 52 LEU HD1 H 0.72 . 1 461 . 52 LEU CD2 C 25.14 . 1 462 . 52 LEU HD2 H 0.86 . 1 463 . 52 LEU C C 176.87 . 1 464 . 53 GLY N N 105.87 . 1 465 . 53 GLY H H 7.84 . 1 466 . 53 GLY CA C 45.85 . 1 467 . 53 GLY HA2 H 4.31 . 1 468 . 53 GLY HA3 H 3.97 . 1 469 . 53 GLY C C 175.99 . 1 470 . 54 LEU N N 120.87 . 1 471 . 54 LEU H H 7.98 . 1 472 . 54 LEU CA C 56.30 . 1 473 . 54 LEU HA H 4.38 . 1 474 . 54 LEU CB C 40.45 . 1 475 . 54 LEU HB2 H 1.39 . 1 476 . 54 LEU HB3 H 1.69 . 1 477 . 54 LEU CG C 29.18 . 1 478 . 54 LEU HG H 1.68 . 1 479 . 54 LEU CD1 C 25.08 . 1 480 . 54 LEU HD1 H 0.85 . 1 481 . 54 LEU CD2 C 24.21 . 1 482 . 54 LEU HD2 H 0.81 . 1 483 . 54 LEU C C 177.04 . 1 484 . 55 ASP N N 120.01 . 1 485 . 55 ASP H H 8.90 . 1 486 . 55 ASP CA C 56.63 . 1 487 . 55 ASP HA H 4.20 . 1 488 . 55 ASP CB C 38.80 . 1 489 . 55 ASP HB2 H 2.76 . 1 490 . 55 ASP HB3 H 2.67 . 1 491 . 55 ASP C C 178.56 . 1 492 . 56 SER N N 116.41 . 1 493 . 56 SER H H 7.96 . 1 494 . 56 SER CA C 60.97 . 1 495 . 56 SER HA H 4.07 . 1 496 . 56 SER CB C 62.63 . 1 497 . 56 SER HB2 H 4.37 . 1 498 . 56 SER C C 176.34 . 1 499 . 57 MET N N 121.49 . 1 500 . 57 MET H H 7.43 . 1 501 . 57 MET CA C 58.58 . 1 502 . 57 MET HA H 4.15 . 1 503 . 57 MET CB C 32.96 . 1 504 . 57 MET HB2 H 2.00 . 1 505 . 57 MET HB3 H 1.99 . 1 506 . 57 MET CG C 32.44 . 1 507 . 57 MET HG2 H 2.65 . 1 508 . 57 MET HG3 H 2.37 . 1 509 . 57 MET CE C 17.22 . 1 510 . 57 MET HE H 2.08 . 1 511 . 57 MET C C 177.99 . 1 512 . 58 LEU N N 119.74 . 1 513 . 58 LEU H H 7.66 . 1 514 . 58 LEU CA C 57.06 . 1 515 . 58 LEU HA H 4.01 . 1 516 . 58 LEU CB C 41.74 . 1 517 . 58 LEU HB2 H 1.86 . 1 518 . 58 LEU HB3 H 1.50 . 1 519 . 58 LEU CG C 27.16 . 1 520 . 58 LEU HG H 1.56 . 1 521 . 58 LEU CD1 C 25.14 . 1 522 . 58 LEU HD1 H 0.80 . 1 523 . 58 LEU CD2 C 24.36 . 1 524 . 58 LEU HD2 H 0.78 . 1 525 . 58 LEU C C 178.34 . 1 526 . 59 LEU N N 118.63 . 1 527 . 59 LEU H H 7.83 . 1 528 . 59 LEU CA C 57.25 . 1 529 . 59 LEU HA H 4.10 . 1 530 . 59 LEU CB C 41.59 . 1 531 . 59 LEU HB2 H 1.72 . 1 532 . 59 LEU HB3 H 1.56 . 1 533 . 59 LEU CG C 27.62 . 1 534 . 59 LEU HG H 1.72 . 1 535 . 59 LEU CD1 C 24.92 . 1 536 . 59 LEU HD1 H 0.86 . 1 537 . 59 LEU CD2 C 23.43 . 1 538 . 59 LEU HD2 H 0.86 . 1 539 . 59 LEU C C 178.38 . 1 540 . 60 GLU N N 116.12 . 1 541 . 60 GLU H H 7.33 . 1 542 . 60 GLU CA C 58.20 . 1 543 . 60 GLU HA H 4.02 . 1 544 . 60 GLU CB C 29.99 . 1 545 . 60 GLU HB3 H 2.03 . 1 546 . 60 GLU HB2 H 2.03 . 1 547 . 60 GLU CG C 36.63 . 1 548 . 60 GLU HG2 H 2.41 . 1 549 . 60 GLU HG3 H 2.20 . 1 550 . 60 GLU C C 177.38 . 1 551 . 61 VAL N N 114.87 . 1 552 . 61 VAL H H 7.46 . 1 553 . 61 VAL CA C 63.75 . 1 554 . 61 VAL HA H 3.85 . 1 555 . 61 VAL CB C 32.75 . 1 556 . 61 VAL HB H 2.13 . 1 557 . 61 VAL CG2 C 21.46 . 1 558 . 61 VAL HG2 H 0.83 . 1 559 . 61 VAL CG1 C 22.47 . 1 560 . 61 VAL HG1 H 0.72 . 1 561 . 61 VAL C C 175.23 . 1 562 . 62 ILE N N 115.47 . 1 563 . 62 ILE H H 7.77 . 1 564 . 62 ILE CA C 60.72 . 1 565 . 62 ILE HA H 3.95 . 1 566 . 62 ILE CB C 39.32 . 1 567 . 62 ILE HB H 1.74 . 1 568 . 62 ILE CG1 C 27.31 . 1 569 . 62 ILE HG12 H 1.32 . 1 570 . 62 ILE HG13 H 1.08 . 1 571 . 62 ILE CD1 C 13.84 . 1 572 . 62 ILE HD1 H 0.73 . 1 573 . 62 ILE CG2 C 17.79 . 1 574 . 62 ILE HG2 H 0.74 . 1 575 . 62 ILE C C 173.75 . 1 576 . 63 ASP N N 122.16 . 1 577 . 63 ASP H H 7.49 . 1 578 . 63 ASP CA C 53.54 . 1 579 . 63 ASP HA H 4.50 . 1 580 . 63 ASP CB C 40.99 . 1 581 . 63 ASP HB2 H 2.63 . 1 582 . 63 ASP HB3 H 2.35 . 1 583 . 63 ASP C C 176.08 . 1 584 . 64 LEU N N 123.44 . 1 585 . 64 LEU H H 8.11 . 1 586 . 64 LEU CA C 55.44 . 1 587 . 64 LEU HA H 4.16 . 1 588 . 64 LEU CB C 42.28 . 1 589 . 64 LEU HB2 H 1.58 . 1 590 . 64 LEU HB3 H 1.56 . 1 591 . 64 LEU CG C 27.16 . 1 592 . 64 LEU HG H 1.55 . 1 593 . 64 LEU CD1 C 23.78 . 1 594 . 64 LEU HD1 H 0.78 . 1 595 . 64 LEU CD2 C 25.30 . 1 596 . 64 LEU HD2 H 0.86 . 1 597 . 64 LEU C C 177.46 . 1 598 . 65 LYS N N 121.09 . 1 599 . 65 LYS H H 8.21 . 1 600 . 65 LYS CA C 56.89 . 1 601 . 65 LYS HA H 4.23 . 1 602 . 65 LYS CB C 32.72 . 1 603 . 65 LYS HB2 H 1.80 . 1 604 . 65 LYS CG C 24.98 . 1 605 . 65 LYS HG2 H 1.40 . 1 606 . 65 LYS CD C 29.18 . 1 607 . 65 LYS HD3 H 1.66 . 1 608 . 65 LYS CE C 41.45 . 1 609 . 65 LYS HE2 H 2.98 . 1 610 . 65 LYS C C 176.73 . 1 611 . 66 GLU N N 121.48 . 1 612 . 66 GLU H H 8.11 . 1 613 . 66 GLU CA C 56.36 . 1 614 . 66 GLU HA H 4.27 . 1 615 . 66 GLU CB C 30.53 . 1 616 . 66 GLU HB3 H 1.88 . 1 617 . 66 GLU HB2 H 2.08 . 1 618 . 66 GLU CG C 36.63 . 1 619 . 66 GLU HG2 H 2.20 . 1 620 . 66 GLU C C 175.10 . 1 621 . 67 ALA N N 130.44 . 1 622 . 67 ALA H H 7.77 . 1 623 . 67 ALA CA C 53.86 . 1 624 . 67 ALA HA H 4.10 . 1 625 . 67 ALA CB C 20.47 . 1 626 . 67 ALA HB H 1.30 . 1 stop_ save_