data_4726 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of a Conserved Domain Common to the Transcription Factors TFIIS, elongin A, and CRSP70 ; _BMRB_accession_number 4726 _BMRB_flat_file_name bmr4726.str _Entry_type original _Submission_date 2000-04-27 _Accession_date 2000-04-27 _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 Booth Valerie . . 2 Koth Chris . . 3 Edwards Aled . . 4 Arrowsmith Cheryl . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 425 "13C chemical shifts" 245 "15N chemical shifts" 79 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-12-07 original author . stop_ _Original_release_date 2000-12-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Booth, V., Koth, C.M., Edwards, A.M., and Arrowsmith, C.H., "Structure of a Conserved Domain Common to the Transcription Factors TFIIS, elongin A, and CRSP70," J. Biol. Chem. 275, 31266-31268 (2000). ; _Citation_title ; Structure of a Conserved Domain Common to the Transcription Factors TFIIS, elongin A, and CRSP70 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20469488 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Booth Valerie . . 2 Koth Chris M. . 3 Edwards Aled M. . 4 Arrowsmith Cheryl H. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'Journal of Biological Chemistry' _Journal_volume 275 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 31266 _Page_last 31268 _Year 2000 _Details . save_ ################################## # Molecular system description # ################################## save_system_TFIIS_domain_I _Saveframe_category molecular_system _Mol_system_name 'TFIIS domain I' _Abbreviation_common 'TFIIS domain I' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'TFIIS domain I' $TFIIS_domain_I stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TFIIS_domain_I _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'TFIIS domain I' _Abbreviation_common 'TFIIS domain I' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 114 _Mol_residue_sequence ; GSHMDSKEVLVHVKNLEKNK SNDAAVLEILHVLDKEFVPT EKLLRETKVGVEVNKFKKST NVEISKLVKKMISSWKDAIN KNKRSRQAQQHHQDHAPGNA EDKTTVGESVNGVQ ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 HIS 4 MET 5 ASP 6 SER 7 LYS 8 GLU 9 VAL 10 LEU 11 VAL 12 HIS 13 VAL 14 LYS 15 ASN 16 LEU 17 GLU 18 LYS 19 ASN 20 LYS 21 SER 22 ASN 23 ASP 24 ALA 25 ALA 26 VAL 27 LEU 28 GLU 29 ILE 30 LEU 31 HIS 32 VAL 33 LEU 34 ASP 35 LYS 36 GLU 37 PHE 38 VAL 39 PRO 40 THR 41 GLU 42 LYS 43 LEU 44 LEU 45 ARG 46 GLU 47 THR 48 LYS 49 VAL 50 GLY 51 VAL 52 GLU 53 VAL 54 ASN 55 LYS 56 PHE 57 LYS 58 LYS 59 SER 60 THR 61 ASN 62 VAL 63 GLU 64 ILE 65 SER 66 LYS 67 LEU 68 VAL 69 LYS 70 LYS 71 MET 72 ILE 73 SER 74 SER 75 TRP 76 LYS 77 ASP 78 ALA 79 ILE 80 ASN 81 LYS 82 ASN 83 LYS 84 ARG 85 SER 86 ARG 87 GLN 88 ALA 89 GLN 90 GLN 91 HIS 92 HIS 93 GLN 94 ASP 95 HIS 96 ALA 97 PRO 98 GLY 99 ASN 100 ALA 101 GLU 102 ASP 103 LYS 104 THR 105 THR 106 VAL 107 GLY 108 GLU 109 SER 110 VAL 111 ASN 112 GLY 113 VAL 114 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-03-24 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 1EO0 "Conserved Domain Common To Transcription Factors Tfiis, Elongin A, Crsp70" 67.54 77 100.00 100.00 6.86e-44 PDB 1PQV "Rna Polymerase Ii-Tfiis Complex" 97.37 309 100.00 100.00 2.03e-70 DBJ BAA02046 "transcriptional elongation factor S-II [Saccharomyces cerevisiae]" 97.37 309 100.00 100.00 2.03e-70 DBJ GAA23345 "K7_Dst1p [Saccharomyces cerevisiae Kyokai no. 7]" 97.37 309 100.00 100.00 2.03e-70 EMBL CAA96744 "DST1 [Saccharomyces cerevisiae]" 97.37 309 100.00 100.00 2.03e-70 EMBL CAY79716 "Dst1p [Saccharomyces cerevisiae EC1118]" 97.37 309 100.00 100.00 1.91e-70 GB AHY79329 "Dst1p [Saccharomyces cerevisiae YJM993]" 97.37 309 100.00 100.00 2.03e-70 GB AJR76067 "Dst1p [Saccharomyces cerevisiae YJM189]" 97.37 309 100.00 100.00 2.03e-70 GB AJR76568 "Dst1p [Saccharomyces cerevisiae YJM193]" 97.37 309 100.00 100.00 2.03e-70 GB AJR77066 "Dst1p [Saccharomyces cerevisiae YJM195]" 97.37 309 100.00 100.00 2.47e-70 GB AJR77564 "Dst1p [Saccharomyces cerevisiae YJM244]" 97.37 309 100.00 100.00 2.03e-70 REF NP_011472 "Dst1p [Saccharomyces cerevisiae S288c]" 97.37 309 100.00 100.00 2.03e-70 SP P07273 "RecName: Full=Transcription elongation factor S-II; AltName: Full=DNA strand transfer protein alpha; Short=STP-alpha; AltName: " 97.37 309 100.00 100.00 2.03e-70 TPG DAA08057 "TPA: Dst1p [Saccharomyces cerevisiae S288c]" 97.37 309 100.00 100.00 2.03e-70 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TFIIS_domain_I 'baker's yeast' 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 $TFIIS_domain_I '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 $TFIIS_domain_I . mM . 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_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 0.1 n/a temperature 298 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_ref _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 . C 13 . . . . . . . . . H 1 . . . . . . . . . N 15 . . . . . . . . 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_cs_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chem_shift_ref _Mol_system_component_name 'TFIIS domain I' _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 MET N N 122.80 . . 2 . 4 MET H H 8.16 . . 3 . 4 MET CA C 56.70 . . 4 . 4 MET CB C 34.70 . . 5 . 4 MET HA H 4.43 . . 6 . 4 MET HB2 H 2.13 . . 7 . 4 MET HB3 H 2.13 . . 8 . 4 MET CG C 31.80 . . 9 . 4 MET HG2 H 2.69 . . 10 . 4 MET HG3 H 2.69 . . 11 . 5 ASP N N 126.30 . . 12 . 5 ASP H H 8.70 . . 13 . 5 ASP CA C 52.70 . . 14 . 5 ASP CB C 42.70 . . 15 . 5 ASP HA H 4.87 . . 16 . 5 ASP HB3 H 2.86 . . 17 . 5 ASP HB2 H 3.08 . . 18 . 6 SER N N 116.30 . . 19 . 6 SER H H 8.71 . . 20 . 6 SER CA C 62.60 . . 21 . 6 SER CB C 62.60 . . 22 . 6 SER HA H 3.84 . . 23 . 6 SER HB2 H 3.91 . . 24 . 6 SER HB3 H 3.91 . . 25 . 7 LYS N N 119.80 . . 26 . 7 LYS H H 8.06 . . 27 . 7 LYS CA C 59.60 . . 28 . 7 LYS CB C 31.70 . . 29 . 7 LYS HA H 4.00 . . 30 . 7 LYS HB3 H 1.86 . . 31 . 7 LYS HB2 H 1.99 . . 32 . 7 LYS CG C 25.00 . . 33 . 7 LYS HG3 H 1.53 . . 34 . 7 LYS HG2 H 1.66 . . 35 . 7 LYS CD C 29.10 . . 36 . 7 LYS CE C 42.00 . . 37 . 7 LYS HE3 H 2.99 . . 38 . 7 LYS HE2 H 3.04 . . 39 . 8 GLU N N 119.80 . . 40 . 8 GLU H H 7.78 . . 41 . 8 GLU CA C 59.10 . . 42 . 8 GLU CB C 29.50 . . 43 . 8 GLU HA H 4.06 . . 44 . 8 GLU HB3 H 2.11 . . 45 . 8 GLU HB2 H 2.29 . . 46 . 8 GLU CG C 36.60 . . 47 . 8 GLU HG3 H 2.30 . . 48 . 8 GLU HG2 H 2.41 . . 49 . 9 VAL N N 119.40 . . 50 . 9 VAL H H 8.16 . . 51 . 9 VAL CA C 67.00 . . 52 . 9 VAL CB C 31.50 . . 53 . 9 VAL HA H 3.57 . . 54 . 9 VAL HB H 2.26 . . 55 . 9 VAL CG1 C 21.30 . . 56 . 9 VAL CG2 C 23.40 . . 57 . 9 VAL HG1 H 0.75 . . 58 . 9 VAL HG2 H 1.06 . . 59 . 10 LEU N N 117.80 . . 60 . 10 LEU H H 8.13 . . 61 . 10 LEU CA C 58.30 . . 62 . 10 LEU CB C 41.70 . . 63 . 10 LEU HA H 3.99 . . 64 . 10 LEU HB3 H 1.56 . . 65 . 10 LEU HB2 H 1.99 . . 66 . 10 LEU CD1 C 25.10 . . 67 . 10 LEU HG H 1.86 . . 68 . 10 LEU CG C 24.30 . . 69 . 10 LEU HD1 H 0.95 . . 70 . 11 VAL N N 121.00 . . 71 . 11 VAL H H 7.31 . . 72 . 11 VAL CA C 66.60 . . 73 . 11 VAL CB C 31.40 . . 74 . 11 VAL HA H 3.59 . . 75 . 11 VAL HB H 2.08 . . 76 . 11 VAL CG1 C 21.00 . . 77 . 11 VAL HG1 H 0.76 . . 78 . 11 VAL CG2 C 22.50 . . 79 . 11 VAL HG2 H 1.06 . . 80 . 12 HIS N N 119.30 . . 81 . 12 HIS H H 7.46 . . 82 . 12 HIS CA C 59.90 . . 83 . 12 HIS CB C 30.80 . . 84 . 12 HIS HA H 4.63 . . 85 . 12 HIS HB3 H 2.86 . . 86 . 12 HIS HB2 H 3.27 . . 87 . 12 HIS HD2 H 6.91 . . 88 . 12 HIS HE1 H 7.72 . . 89 . 13 VAL N N 119.00 . . 90 . 13 VAL H H 8.66 . . 91 . 13 VAL CA C 67.40 . . 92 . 13 VAL CB C 31.60 . . 93 . 13 VAL HA H 3.59 . . 94 . 13 VAL HB H 2.30 . . 95 . 13 VAL CG1 C 21.60 . . 96 . 13 VAL HG1 H 1.04 . . 97 . 14 LYS N N 120.10 . . 98 . 14 LYS H H 8.11 . . 99 . 14 LYS CA C 59.10 . . 100 . 14 LYS CB C 31.70 . . 101 . 14 LYS HA H 4.24 . . 102 . 14 LYS HB3 H 1.98 . . 103 . 14 LYS HB2 H 2.03 . . 104 . 14 LYS HG3 H 1.74 . . 105 . 15 ASN N N 119.70 . . 106 . 15 ASN H H 8.45 . . 107 . 15 ASN CA C 55.00 . . 108 . 15 ASN CB C 37.60 . . 109 . 15 ASN HA H 4.74 . . 110 . 15 ASN HB3 H 2.75 . . 111 . 15 ASN HB2 H 3.14 . . 112 . 15 ASN HD21 H 6.89 . . 113 . 15 ASN HD22 H 7.54 . . 114 . 16 LEU N N 126.30 . . 115 . 16 LEU H H 8.73 . . 116 . 16 LEU CA C 58.50 . . 117 . 16 LEU CB C 41.80 . . 118 . 16 LEU HA H 3.96 . . 119 . 16 LEU HB3 H 1.80 . . 120 . 16 LEU HB2 H 2.28 . . 121 . 16 LEU CG C 26.10 . . 122 . 16 LEU HG H 1.99 . . 123 . 16 LEU CD1 C 25.20 . . 124 . 16 LEU HD1 H 0.75 . . 125 . 16 LEU CD2 C 25.80 . . 126 . 16 LEU HD2 H 0.68 . . 127 . 17 GLU N N 116.80 . . 128 . 17 GLU H H 7.31 . . 129 . 17 GLU CA C 58.80 . . 130 . 17 GLU CB C 29.50 . . 131 . 17 GLU HA H 4.24 . . 132 . 17 GLU HB3 H 2.16 . . 133 . 17 GLU HB2 H 2.36 . . 134 . 17 GLU CG C 35.60 . . 135 . 17 GLU HG2 H 2.38 . . 136 . 17 GLU HG3 H 2.38 . . 137 . 18 LYS N N 118.00 . . 138 . 18 LYS H H 8.09 . . 139 . 18 LYS CA C 58.90 . . 140 . 18 LYS CB C 38.90 . . 141 . 18 LYS HA H 4.18 . . 142 . 18 LYS HB3 H 1.95 . . 143 . 18 LYS HB2 H 2.01 . . 144 . 18 LYS CG C 24.90 . . 145 . 18 LYS HG3 H 1.57 . . 146 . 18 LYS HG2 H 1.65 . . 147 . 18 LYS HD3 H 3.04 . . 148 . 18 LYS CE C 42.10 . . 149 . 19 ASN N N 114.40 . . 150 . 19 ASN H H 7.80 . . 151 . 19 ASN CA C 53.30 . . 152 . 19 ASN CB C 39.50 . . 153 . 19 ASN HA H 5.07 . . 154 . 19 ASN HB3 H 2.58 . . 155 . 19 ASN HB2 H 3.15 . . 156 . 20 LYS N N 117.40 . . 157 . 20 LYS H H 6.97 . . 158 . 20 LYS CA C 59.90 . . 159 . 20 LYS CB C 32.20 . . 160 . 20 LYS HA H 4.28 . . 161 . 20 LYS HB3 H 2.15 . . 162 . 20 LYS HB2 H 2.38 . . 163 . 20 LYS CG C 22.80 . . 164 . 20 LYS HG3 H 1.42 . . 165 . 20 LYS HG2 H 1.69 . . 166 . 20 LYS CD C 29.70 . . 167 . 20 LYS CE C 42.10 . . 168 . 21 SER N N 115.10 . . 169 . 21 SER H H 8.38 . . 170 . 21 SER CA C 58.60 . . 171 . 21 SER CB C 63.40 . . 172 . 21 SER HA H 4.75 . . 173 . 21 SER HB2 H 4.04 . . 174 . 21 SER HB3 H 4.04 . . 175 . 22 ASN N N 123.60 . . 176 . 22 ASN H H 8.56 . . 177 . 22 ASN CA C 51.20 . . 178 . 22 ASN CB C 38.90 . . 179 . 22 ASN HA H 5.03 . . 180 . 22 ASN HB3 H 2.75 . . 181 . 22 ASN HB2 H 3.39 . . 182 . 22 ASN ND2 N 40.60 . . 183 . 22 ASN HD21 H 7.44 . . 184 . 22 ASN HD22 H 7.76 . . 185 . 23 ASP N N 125.00 . . 186 . 23 ASP H H 8.62 . . 187 . 23 ASP CA C 57.50 . . 188 . 23 ASP CB C 40.30 . . 189 . 23 ASP HA H 4.19 . . 190 . 23 ASP HB3 H 2.57 . . 191 . 23 ASP HB2 H 2.75 . . 192 . 24 ALA N N 119.40 . . 193 . 24 ALA H H 8.10 . . 194 . 24 ALA CA C 55.10 . . 195 . 24 ALA CB C 18.10 . . 196 . 24 ALA HA H 4.11 . . 197 . 24 ALA HB H 1.52 . . 198 . 25 ALA N N 121.80 . . 199 . 25 ALA H H 7.42 . . 200 . 25 ALA CA C 54.30 . . 201 . 25 ALA CB C 18.40 . . 202 . 25 ALA HA H 4.19 . . 203 . 25 ALA HB H 1.52 . . 204 . 26 VAL N N 120.10 . . 205 . 26 VAL H H 8.15 . . 206 . 26 VAL CA C 66.80 . . 207 . 26 VAL CB C 31.80 . . 208 . 26 VAL HA H 3.27 . . 209 . 26 VAL HB H 2.06 . . 210 . 26 VAL CG1 C 20.20 . . 211 . 26 VAL HG1 H 0.22 . . 212 . 26 VAL CG2 C 23.90 . . 213 . 26 VAL HG2 H 1.00 . . 214 . 27 LEU N N 119.60 . . 215 . 27 LEU H H 8.46 . . 216 . 27 LEU CA C 58.50 . . 217 . 27 LEU CB C 41.70 . . 218 . 27 LEU HA H 3.64 . . 219 . 27 LEU HB3 H 1.49 . . 220 . 27 LEU HB2 H 1.81 . . 221 . 27 LEU CG C 27.50 . . 222 . 27 LEU HG H 1.47 . . 223 . 27 LEU CD1 C 24.50 . . 224 . 27 LEU HD1 H 0.75 . . 225 . 27 LEU HD2 H 0.82 . . 226 . 28 GLU N N 117.30 . . 227 . 28 GLU H H 8.42 . . 228 . 28 GLU CA C 59.40 . . 229 . 28 GLU CB C 29.50 . . 230 . 28 GLU HA H 4.09 . . 231 . 28 GLU HB3 H 2.10 . . 232 . 28 GLU HB2 H 2.29 . . 233 . 28 GLU CG C 35.90 . . 234 . 28 GLU HG3 H 2.29 . . 235 . 28 GLU HG2 H 2.45 . . 236 . 29 ILE N N 120.20 . . 237 . 29 ILE H H 7.53 . . 238 . 29 ILE CA C 65.20 . . 239 . 29 ILE CB C 38.80 . . 240 . 29 ILE HA H 3.57 . . 241 . 29 ILE HB H 1.81 . . 242 . 29 ILE HG13 H 1.25 . . 243 . 29 ILE HG12 H 1.96 . . 244 . 29 ILE CG2 C 17.90 . . 245 . 29 ILE HG2 H 0.93 . . 246 . 29 ILE CD1 C 20.10 . . 247 . 29 ILE HD1 H 0.88 . . 248 . 30 LEU N N 118.50 . . 249 . 30 LEU H H 8.83 . . 250 . 30 LEU CA C 58.50 . . 251 . 30 LEU CB C 41.30 . . 252 . 30 LEU HA H 3.82 . . 253 . 30 LEU HB3 H 1.74 . . 254 . 30 LEU HB2 H 2.02 . . 255 . 30 LEU CD1 C 23.20 . . 256 . 30 LEU HG H 0.54 . . 257 . 30 LEU HD1 H 0.65 . . 258 . 31 HIS N N 115.70 . . 259 . 31 HIS H H 8.48 . . 260 . 31 HIS CA C 59.90 . . 261 . 31 HIS CB C 28.70 . . 262 . 31 HIS HA H 4.43 . . 263 . 31 HIS HB2 H 3.14 . . 264 . 31 HIS HB3 H 3.14 . . 265 . 31 HIS HD1 H 7.14 . . 266 . 31 HIS HE1 H 8.19 . . 267 . 32 VAL N N 121.30 . . 268 . 32 VAL H H 7.52 . . 269 . 32 VAL CA C 66.80 . . 270 . 32 VAL CB C 31.10 . . 271 . 32 VAL HA H 3.81 . . 272 . 32 VAL HB H 2.10 . . 273 . 32 VAL CG1 C 20.90 . . 274 . 32 VAL HG1 H 0.78 . . 275 . 32 VAL HG2 H 1.10 . . 276 . 33 LEU N N 120.10 . . 277 . 33 LEU H H 8.13 . . 278 . 33 LEU CA C 57.60 . . 279 . 33 LEU CB C 43.00 . . 280 . 33 LEU HA H 4.01 . . 281 . 33 LEU HB3 H 2.12 . . 282 . 33 LEU HB2 H 1.39 . . 283 . 33 LEU CG C 26.30 . . 284 . 33 LEU CD1 C 22.70 . . 285 . 33 LEU HD1 H 0.67 . . 286 . 34 ASP N N 118.70 . . 287 . 34 ASP H H 8.90 . . 288 . 34 ASP CA C 57.70 . . 289 . 34 ASP CB C 42.80 . . 290 . 34 ASP HA H 4.55 . . 291 . 34 ASP HB3 H 2.87 . . 292 . 34 ASP HB2 H 3.06 . . 293 . 35 LYS N N 114.60 . . 294 . 35 LYS H H 7.65 . . 295 . 35 LYS CA C 58.20 . . 296 . 35 LYS CB C 34.20 . . 297 . 35 LYS HA H 4.31 . . 298 . 35 LYS HB3 H 1.97 . . 299 . 35 LYS HB2 H 2.03 . . 300 . 35 LYS CG C 25.10 . . 301 . 35 LYS HG3 H 1.54 . . 302 . 35 LYS HG2 H 1.66 . . 303 . 35 LYS CD C 29.30 . . 304 . 35 LYS HD3 H 1.73 . . 305 . 35 LYS HD2 H 1.76 . . 306 . 35 LYS CE C 42.10 . . 307 . 35 LYS HE3 H 2.98 . . 308 . 35 LYS HE2 H 3.07 . . 309 . 36 GLU N N 114.50 . . 310 . 36 GLU H H 8.57 . . 311 . 36 GLU CA C 57.00 . . 312 . 36 GLU CB C 32.00 . . 313 . 36 GLU HA H 4.68 . . 314 . 36 GLU HB3 H 1.98 . . 315 . 36 GLU HB2 H 2.31 . . 316 . 36 GLU HG3 H 2.41 . . 317 . 37 PHE N N 120.30 . . 318 . 37 PHE H H 8.29 . . 319 . 37 PHE CA C 57.50 . . 320 . 37 PHE CB C 39.90 . . 321 . 37 PHE HA H 4.01 . . 322 . 37 PHE HB3 H 3.11 . . 323 . 37 PHE HB2 H 3.67 . . 324 . 37 PHE HD1 H 6.79 . . 325 . 37 PHE HD2 H 6.79 . . 326 . 37 PHE HE1 H 6.22 . . 327 . 37 PHE HE2 H 6.22 . . 328 . 37 PHE HZ H 6.38 . . 329 . 38 VAL N N 132.00 . . 330 . 38 VAL H H 7.91 . . 331 . 38 VAL CA C 58.10 . . 332 . 38 VAL CB C 32.50 . . 333 . 38 VAL HA H 4.21 . . 334 . 38 VAL HB H 1.68 . . 335 . 38 VAL CG1 C 20.20 . . 336 . 38 VAL CG2 C 20.20 . . 337 . 38 VAL HG2 H 0.71 . . 338 . 38 VAL HG1 H 0.39 . . 339 . 39 PRO CB C 62.60 . . 340 . 39 PRO CA C 31.60 . . 341 . 39 PRO HA H 3.37 . . 342 . 39 PRO HB3 H 1.31 . . 343 . 39 PRO HB2 H 1.51 . . 344 . 39 PRO CG C 27.20 . . 345 . 39 PRO HG2 H 1.92 . . 346 . 39 PRO CD C 48.50 . . 347 . 39 PRO HG3 H 3.07 . . 348 . 40 THR N N 107.00 . . 349 . 40 THR H H 6.39 . . 350 . 40 THR CA C 58.60 . . 351 . 40 THR CB C 72.60 . . 352 . 40 THR HA H 4.44 . . 353 . 40 THR HB H 4.61 . . 354 . 40 THR CG2 C 21.90 . . 355 . 40 THR HG2 H 1.17 . . 356 . 41 GLU N N 125.10 . . 357 . 41 GLU H H 9.51 . . 358 . 41 GLU CA C 60.80 . . 359 . 41 GLU CB C 29.50 . . 360 . 41 GLU HA H 4.69 . . 361 . 41 GLU CG C 36.90 . . 362 . 42 LYS N N 119.70 . . 363 . 42 LYS H H 8.43 . . 364 . 42 LYS CA C 59.90 . . 365 . 42 LYS CB C 33.10 . . 366 . 42 LYS HA H 4.02 . . 367 . 42 LYS HB3 H 1.73 . . 368 . 42 LYS HB2 H 1.83 . . 369 . 42 LYS CG C 24.80 . . 370 . 42 LYS HG2 H 1.65 . . 371 . 42 LYS HG3 H 1.65 . . 372 . 42 LYS CD C 29.80 . . 373 . 42 LYS CE C 42.00 . . 374 . 43 LEU N N 118.60 . . 375 . 43 LEU H H 7.99 . . 376 . 43 LEU CA C 58.10 . . 377 . 43 LEU CB C 43.60 . . 378 . 43 LEU HA H 4.30 . . 379 . 43 LEU HB3 H 1.45 . . 380 . 43 LEU HB2 H 1.94 . . 381 . 43 LEU CD1 C 25.60 . . 382 . 43 LEU HD1 H 1.02 . . 383 . 43 LEU HD2 H 1.09 . . 384 . 44 LEU N N 122.10 . . 385 . 44 LEU H H 8.50 . . 386 . 44 LEU CA C 59.00 . . 387 . 44 LEU CB C 41.20 . . 388 . 44 LEU CG C 26.90 . . 389 . 44 LEU HG H 1.76 . . 390 . 44 LEU HA H 4.01 . . 391 . 44 LEU HB3 H 1.71 . . 392 . 44 LEU HB2 H 2.03 . . 393 . 44 LEU HD1 H 0.96 . . 394 . 44 LEU HD2 H 0.86 . . 395 . 45 ARG N N 120.50 . . 396 . 45 ARG H H 8.18 . . 397 . 45 ARG CA C 59.10 . . 398 . 45 ARG CB C 30.40 . . 399 . 45 ARG HA H 4.24 . . 400 . 45 ARG HB3 H 2.06 . . 401 . 45 ARG HB2 H 2.21 . . 402 . 45 ARG CG C 27.20 . . 403 . 45 ARG HG3 H 1.71 . . 404 . 45 ARG HG2 H 1.80 . . 405 . 45 ARG CD C 43.30 . . 406 . 45 ARG HD2 H 3.31 . . 407 . 45 ARG HD3 H 3.31 . . 408 . 46 GLU N N 116.30 . . 409 . 46 GLU H H 8.66 . . 410 . 46 GLU CA C 59.00 . . 411 . 46 GLU CB C 30.30 . . 412 . 46 GLU HA H 4.23 . . 413 . 46 GLU HB3 H 2.08 . . 414 . 46 GLU HB2 H 2.21 . . 415 . 46 GLU CG C 36.90 . . 416 . 46 GLU HG3 H 2.36 . . 417 . 46 GLU HG2 H 2.61 . . 418 . 47 THR N N 105.30 . . 419 . 47 THR H H 7.78 . . 420 . 47 THR CA C 71.60 . . 421 . 47 THR CB C 62.20 . . 422 . 47 THR HA H 4.42 . . 423 . 47 THR HB H 4.08 . . 424 . 47 THR CG2 C 21.40 . . 425 . 47 THR HG2 H 1.38 . . 426 . 48 LYS N N 113.20 . . 427 . 48 LYS H H 7.48 . . 428 . 48 LYS CA C 57.70 . . 429 . 48 LYS CB C 29.50 . . 430 . 48 LYS HA H 4.24 . . 431 . 48 LYS HB3 H 2.11 . . 432 . 48 LYS HB2 H 2.30 . . 433 . 48 LYS CG C 25.10 . . 434 . 48 LYS HG2 H 1.46 . . 435 . 48 LYS HG3 H 1.46 . . 436 . 48 LYS CE C 42.10 . . 437 . 49 VAL N N 117.90 . . 438 . 49 VAL H H 7.71 . . 439 . 49 VAL CA C 64.90 . . 440 . 49 VAL CB C 30.70 . . 441 . 49 VAL HA H 3.97 . . 442 . 49 VAL HB H 2.16 . . 443 . 49 VAL CG1 C 22.00 . . 444 . 49 VAL CG2 C 22.00 . . 445 . 49 VAL HG1 H 1.11 . . 446 . 49 VAL HG2 H 1.08 . . 447 . 50 GLY N N 110.90 . . 448 . 50 GLY H H 8.59 . . 449 . 50 GLY CA C 46.80 . . 450 . 50 GLY HA2 H 4.08 . . 451 . 50 GLY HA3 H 4.08 . . 452 . 51 VAL N N 122.60 . . 453 . 51 VAL H H 7.15 . . 454 . 51 VAL CA C 65.60 . . 455 . 51 VAL CB C 32.00 . . 456 . 51 VAL HA H 3.72 . . 457 . 51 VAL HB H 2.31 . . 458 . 51 VAL CG1 C 21.50 . . 459 . 51 VAL HG1 H 1.05 . . 460 . 51 VAL HG2 H 1.11 . . 461 . 52 GLU N N 118.80 . . 462 . 52 GLU H H 8.07 . . 463 . 52 GLU CA C 58.70 . . 464 . 52 GLU CB C 28.90 . . 465 . 52 GLU HA H 4.15 . . 466 . 52 GLU HB3 H 2.01 . . 467 . 52 GLU CG C 34.80 . . 468 . 53 VAL N N 118.20 . . 469 . 53 VAL H H 8.65 . . 470 . 53 VAL CA C 67.00 . . 471 . 53 VAL CB C 31.90 . . 472 . 53 VAL HA H 3.83 . . 473 . 53 VAL HB H 2.35 . . 474 . 53 VAL CG1 C 22.20 . . 475 . 53 VAL CG2 C 22.20 . . 476 . 53 VAL HG1 H 1.07 . . 477 . 53 VAL HG2 H 1.11 . . 478 . 54 ASN N N 116.10 . . 479 . 54 ASN H H 7.92 . . 480 . 54 ASN CA C 55.60 . . 481 . 54 ASN CB C 39.00 . . 482 . 54 ASN HA H 4.44 . . 483 . 54 ASN HB3 H 2.83 . . 484 . 54 ASN HB2 H 2.97 . . 485 . 54 ASN ND2 N 112.20 . . 486 . 54 ASN HD21 H 6.68 . . 487 . 54 ASN HD22 H 7.45 . . 488 . 55 LYS N N 119.00 . . 489 . 55 LYS H H 7.54 . . 490 . 55 LYS CA C 59.30 . . 491 . 55 LYS CB C 32.10 . . 492 . 55 LYS HA H 4.04 . . 493 . 55 LYS HB3 H 1.66 . . 494 . 55 LYS HB2 H 1.85 . . 495 . 55 LYS HG3 H 1.34 . . 496 . 55 LYS HG2 H 1.41 . . 497 . 55 LYS CE C 45.00 . . 498 . 55 LYS HE3 H 3.04 . . 499 . 56 PHE N N 116.80 . . 500 . 56 PHE H H 7.98 . . 501 . 56 PHE CA C 57.80 . . 502 . 56 PHE CB C 43.60 . . 503 . 56 PHE HA H 4.43 . . 504 . 56 PHE HB3 H 3.08 . . 505 . 56 PHE HB2 H 3.36 . . 506 . 56 PHE HD1 H 7.57 . . 507 . 56 PHE HD2 H 7.57 . . 508 . 56 PHE HE1 H 7.26 . . 509 . 56 PHE HE2 H 7.26 . . 510 . 56 PHE HZ H 7.55 . . 511 . 57 LYS N N 120.50 . . 512 . 57 LYS H H 7.66 . . 513 . 57 LYS CA C 59.50 . . 514 . 57 LYS CB C 32.30 . . 515 . 57 LYS HA H 3.89 . . 516 . 57 LYS HB3 H 1.88 . . 517 . 57 LYS HB2 H 1.98 . . 518 . 57 LYS CG C 24.90 . . 519 . 57 LYS HG3 H 1.54 . . 520 . 57 LYS HG2 H 1.65 . . 521 . 57 LYS CD C 29.40 . . 522 . 57 LYS HD3 H 1.75 . . 523 . 57 LYS CE C 41.70 . . 524 . 57 LYS HE3 H 3.03 . . 525 . 58 LYS N N 116.30 . . 526 . 58 LYS H H 7.73 . . 527 . 58 LYS CA C 54.80 . . 528 . 58 LYS CB C 31.10 . . 529 . 58 LYS HA H 4.48 . . 530 . 58 LYS HB3 H 1.68 . . 531 . 58 LYS HB2 H 2.05 . . 532 . 58 LYS CG C 24.80 . . 533 . 58 LYS HG3 H 1.40 . . 534 . 58 LYS HG2 H 1.52 . . 535 . 58 LYS CD C 29.10 . . 536 . 58 LYS CE C 42.00 . . 537 . 58 LYS HE3 H 3.02 . . 538 . 59 SER N N 114.70 . . 539 . 59 SER H H 7.22 . . 540 . 59 SER CA C 59.20 . . 541 . 59 SER CB C 64.10 . . 542 . 59 SER HA H 4.22 . . 543 . 59 SER HB2 H 3.68 . . 544 . 59 SER HB3 H 3.68 . . 545 . 60 THR N N 117.80 . . 546 . 60 THR H H 8.54 . . 547 . 60 THR CA C 62.90 . . 548 . 60 THR CB C 68.50 . . 549 . 60 THR HA H 4.21 . . 550 . 60 THR HB H 4.31 . . 551 . 60 THR CG2 C 22.00 . . 552 . 60 THR HG2 H 1.39 . . 553 . 61 ASN N N 123.80 . . 554 . 61 ASN H H 8.66 . . 555 . 61 ASN CA C 52.90 . . 556 . 61 ASN CB C 38.40 . . 557 . 61 ASN HA H 4.80 . . 558 . 61 ASN HB3 H 2.73 . . 559 . 61 ASN HB2 H 3.17 . . 560 . 61 ASN ND2 N 114.30 . . 561 . 61 ASN HD21 H 7.25 . . 562 . 61 ASN HD22 H 8.16 . . 563 . 62 VAL N N 127.20 . . 564 . 62 VAL H H 8.60 . . 565 . 62 VAL CA C 64.70 . . 566 . 62 VAL CB C 31.60 . . 567 . 62 VAL HA H 3.97 . . 568 . 62 VAL HB H 2.16 . . 569 . 62 VAL CG1 C 21.10 . . 570 . 62 VAL HG1 H 1.10 . . 571 . 63 GLU N N 19.70 . . 572 . 63 GLU H H 7.97 . . 573 . 63 GLU CA C 58.90 . . 574 . 63 GLU CB C 29.20 . . 575 . 63 GLU HA H 4.04 . . 576 . 63 GLU HB3 H 2.14 . . 577 . 63 GLU CG C 36.50 . . 578 . 63 GLU HG3 H 2.29 . . 579 . 63 GLU HG2 H 2.44 . . 580 . 64 ILE N N 119.70 . . 581 . 64 ILE H H 7.75 . . 582 . 64 ILE CA C 65.90 . . 583 . 64 ILE CB C 37.70 . . 584 . 64 ILE HA H 3.44 . . 585 . 64 ILE HB H 2.18 . . 586 . 64 ILE CG1 C 31.40 . . 587 . 64 ILE HG13 H 0.61 . . 588 . 64 ILE HG12 H 1.56 . . 589 . 64 ILE CG2 C 17.80 . . 590 . 64 ILE HG2 H 0.97 . . 591 . 64 ILE CD1 C 12.50 . . 592 . 64 ILE HD1 H 0.76 . . 593 . 65 SER N N 113.50 . . 594 . 65 SER H H 8.35 . . 595 . 65 SER CA C 62.10 . . 596 . 65 SER HA H 4.75 . . 597 . 65 SER HB2 H 4.00 . . 598 . 65 SER HB3 H 4.00 . . 599 . 66 LYS N N 119.70 . . 600 . 66 LYS H H 8.27 . . 601 . 66 LYS CA C 59.90 . . 602 . 66 LYS CB C 32.80 . . 603 . 66 LYS HA H 4.00 . . 604 . 66 LYS HB3 H 2.01 . . 605 . 66 LYS HB2 H 2.83 . . 606 . 66 LYS CG C 25.50 . . 607 . 66 LYS HG3 H 1.48 . . 608 . 66 LYS HG2 H 1.69 . . 609 . 66 LYS CD C 29.50 . . 610 . 66 LYS HD3 H 1.75 . . 611 . 66 LYS HD2 H 1.81 . . 612 . 66 LYS CE C 41.80 . . 613 . 67 LEU N N 122.80 . . 614 . 67 LEU H H 7.50 . . 615 . 67 LEU CA C 57.60 . . 616 . 67 LEU CB C 41.80 . . 617 . 67 LEU HA H 4.14 . . 618 . 67 LEU HB3 H 1.55 . . 619 . 67 LEU HB2 H 1.77 . . 620 . 67 LEU CG C 26.90 . . 621 . 67 LEU HG H 0.45 . . 622 . 67 LEU CD1 C 22.90 . . 623 . 67 LEU HD1 H 0.76 . . 624 . 67 LEU CD2 C 26.90 . . 625 . 67 LEU HD2 H 1.56 . . 626 . 68 VAL N N 118.60 . . 627 . 68 VAL H H 8.55 . . 628 . 68 VAL CA C 66.60 . . 629 . 68 VAL CB C 31.50 . . 630 . 68 VAL HA H 3.35 . . 631 . 68 VAL HB H 2.05 . . 632 . 68 VAL CG1 C 23.20 . . 633 . 68 VAL HG1 H 0.85 . . 634 . 68 VAL HG2 H 0.99 . . 635 . 69 LYS N N 117.50 . . 636 . 69 LYS H H 7.65 . . 637 . 69 LYS CA C 59.90 . . 638 . 69 LYS CB C 32.00 . . 639 . 69 LYS HA H 3.86 . . 640 . 69 LYS HB3 H 1.89 . . 641 . 69 LYS HB2 H 1.98 . . 642 . 69 LYS CG C 42.00 . . 643 . 69 LYS CD C 29.40 . . 644 . 69 LYS HD3 H 1.79 . . 645 . 69 LYS CE C 25.90 . . 646 . 69 LYS HE3 H 1.42 . . 647 . 70 LYS N N 120.70 . . 648 . 70 LYS H H 7.65 . . 649 . 70 LYS CA C 59.40 . . 650 . 70 LYS CB C 32.50 . . 651 . 70 LYS HA H 3.97 . . 652 . 70 LYS HB3 H 1.88 . . 653 . 70 LYS HB2 H 2.01 . . 654 . 70 LYS CG C 24.30 . . 655 . 70 LYS HG3 H 1.26 . . 656 . 70 LYS HD3 H 1.58 . . 657 . 70 LYS CE C 41.60 . . 658 . 71 MET N N 121.30 . . 659 . 71 MET H H 8.55 . . 660 . 71 MET CA C 59.10 . . 661 . 71 MET CB C 34.10 . . 662 . 71 MET HA H 3.62 . . 663 . 71 MET HB3 H 0.99 . . 664 . 71 MET HB2 H 1.52 . . 665 . 71 MET CG C 31.20 . . 666 . 71 MET HG3 H 1.97 . . 667 . 72 ILE N N 116.50 . . 668 . 72 ILE H H 8.24 . . 669 . 72 ILE CA C 63.10 . . 670 . 72 ILE CB C 36.00 . . 671 . 72 ILE HA H 3.44 . . 672 . 72 ILE HB H 1.96 . . 673 . 72 ILE CG2 C 17.20 . . 674 . 72 ILE HG2 H 0.91 . . 675 . 72 ILE CG1 C 27.10 . . 676 . 72 ILE HG12 H 1.46 . . 677 . 72 ILE HG13 H 1.46 . . 678 . 72 ILE CD1 C 11.00 . . 679 . 72 ILE HD1 H 0.79 . . 680 . 73 SER N N 113.90 . . 681 . 73 SER H H 7.49 . . 682 . 73 SER CA C 61.40 . . 683 . 73 SER CB C 62.70 . . 684 . 73 SER HA H 4.26 . . 685 . 73 SER HB2 H 4.03 . . 686 . 73 SER HB3 H 4.03 . . 687 . 74 SER N N 119.00 . . 688 . 74 SER H H 8.13 . . 689 . 74 SER CA C 61.40 . . 690 . 74 SER CB C 63.00 . . 691 . 74 SER HA H 4.40 . . 692 . 74 SER HB2 H 4.13 . . 693 . 74 SER HB3 H 4.13 . . 694 . 75 TRP N N 124.80 . . 695 . 75 TRP H H 9.00 . . 696 . 75 TRP CA C 58.10 . . 697 . 75 TRP CB C 28.70 . . 698 . 75 TRP HA H 4.78 . . 699 . 75 TRP HB3 H 3.10 . . 700 . 75 TRP HB2 H 3.58 . . 701 . 75 TRP HD1 H 7.17 . . 702 . 75 TRP HH2 H 7.44 . . 703 . 75 TRP HZ3 H 6.67 . . 704 . 75 TRP HZ2 H 6.78 . . 705 . 75 TRP HE3 H 7.75 . . 706 . 76 LYS N N 119.70 . . 707 . 76 LYS H H 8.19 . . 708 . 76 LYS CA C 59.80 . . 709 . 76 LYS CB C 32.10 . . 710 . 76 LYS HA H 4.09 . . 711 . 76 LYS HB3 H 2.04 . . 712 . 76 LYS HB2 H 2.32 . . 713 . 76 LYS CG C 29.50 . . 714 . 76 LYS HG3 H 1.77 . . 715 . 76 LYS HG2 H 2.30 . . 716 . 76 LYS CD C 25.20 . . 717 . 76 LYS HD3 H 3.07 . . 718 . 76 LYS CE C 41.90 . . 719 . 77 ASP N N 119.40 . . 720 . 77 ASP H H 8.03 . . 721 . 77 ASP CA C 57.20 . . 722 . 77 ASP CB C 40.90 . . 723 . 77 ASP HA H 4.55 . . 724 . 77 ASP HB3 H 2.83 . . 725 . 77 ASP HB2 H 2.96 . . 726 . 78 ALA N N 122.00 . . 727 . 78 ALA H H 8.20 . . 728 . 78 ALA CA C 54.90 . . 729 . 78 ALA CB C 18.60 . . 730 . 78 ALA HA H 4.18 . . 731 . 78 ALA HB H 1.65 . . 732 . 79 ILE N N 116.70 . . 733 . 79 ILE H H 7.92 . . 734 . 79 ILE CA C 62.80 . . 735 . 79 ILE CB C 37.30 . . 736 . 79 ILE HA H 4.03 . . 737 . 79 ILE HB H 2.13 . . 738 . 79 ILE CG1 C 27.80 . . 739 . 79 ILE HG12 H 1.54 . . 740 . 79 ILE HG13 H 0.97 . . 741 . 79 ILE CG2 C 17.20 . . 742 . 79 ILE CD1 C 12.40 . . 743 . 80 ASN N N 120.40 . . 744 . 80 ASN H H 8.13 . . 745 . 80 ASN CA C 55.20 . . 746 . 80 ASN CB C 38.10 . . 747 . 80 ASN HA H 4.68 . . 748 . 80 ASN HB3 H 3.02 . . 749 . 80 ASN HB2 H 2.94 . . stop_ save_