data_5180 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution nmr structure of the dimerization domain of the yeast transcriptional activator Gal4 (residues 50-106) ; _BMRB_accession_number 5180 _BMRB_flat_file_name bmr5180.str _Entry_type original _Submission_date 2001-10-16 _Accession_date 2001-10-16 _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 Hidalgo P. . . 2 Ansari A. Z. . 3 Schmidt P. . . 4 Hare B. . . 5 Simkovic N. . . 6 Farrell S. . . 7 Shin E. J. . 8 Ptashne M. . . 9 Wagner G. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 138 "13C chemical shifts" 34 "15N chemical shifts" 39 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-11-12 original author . stop_ _Original_release_date 2001-11-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Recruitment of the transcriptional machinery through GAL11P:structure and interactions of the GAL4 dimerization domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11316794 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hidalgo Patricia . . 2 Ansari A. Z. . 3 Schmidt P. . . 4 Hare B. . . 5 Simkovic N. . . 6 Farrell S. . . 7 Shin E. J. . 8 Ptashne M. . . 9 Wagner G. . . stop_ _Journal_abbreviation 'Genes Dev.' _Journal_name_full 'Genes & Development' _Journal_volume 15 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1007 _Page_last 1020 _Year 2001 _Details . loop_ _Keyword 'coiled-coil homodimer' 'dimerization domain' 'galactose and melibiose metabolism' 'Transcriptional activator' stop_ save_ ################################## # Molecular system description # ################################## save_system_GAL4 _Saveframe_category molecular_system _Mol_system_name 'GAL4 dimerization domain' _Abbreviation_common GAL4 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Gal4 subunit A, monomer' $GAL4 'Gal4 subunit B, monomer' $GAL4 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'Gal4 subunit A, monomer' 1 'Gal4 subunit B, monomer' stop_ loop_ _Biological_function 'Transcriptional activation' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_GAL4 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'GAL4 dimerization domain' _Name_variant 'Q87R, K90E' _Abbreviation_common GAL4 _Molecular_mass 6812 _Mol_thiol_state 'not present' _Details 'The sequence contains heptad repeats common to coiled-coil dimerization domains' ############################## # Polymer residue sequence # ############################## _Residue_count 57 _Mol_residue_sequence ; TRAHLTEVESRLERLEQLFL LIFPREDLDMILKMDSLRDI EALLTGLFVQDNVNKDA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 50 THR 2 51 ARG 3 52 ALA 4 53 HIS 5 54 LEU 6 55 THR 7 56 GLU 8 57 VAL 9 58 GLU 10 59 SER 11 60 ARG 12 61 LEU 13 62 GLU 14 63 ARG 15 64 LEU 16 65 GLU 17 66 GLN 18 67 LEU 19 68 PHE 20 69 LEU 21 70 LEU 22 71 ILE 23 72 PHE 24 73 PRO 25 74 ARG 26 75 GLU 27 76 ASP 28 77 LEU 29 78 ASP 30 79 MET 31 80 ILE 32 81 LEU 33 82 LYS 34 83 MET 35 84 ASP 36 85 SER 37 86 LEU 38 87 ARG 39 88 ASP 40 89 ILE 41 90 GLU 42 91 ALA 43 92 LEU 44 93 LEU 45 94 THR 46 95 GLY 47 96 LEU 48 97 PHE 49 98 VAL 50 99 GLN 51 100 ASP 52 101 ASN 53 102 VAL 54 103 ASN 55 104 LYS 56 105 ASP 57 106 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2008-08-19 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 1HBW 'Solution Nmr Structure Of The Dimerization Domain Of The Yeast Transcriptional Activator Gal4 (Residues 50-106)' 100.00 57 100.00 100.00 1.56e-23 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $GAL4 '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 $GAL4 'recombinant technology' 'Escherichia coli' Escherichia coli 'BL-21 (DE3) pLysS' . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_gal4_sample1 _Saveframe_category sample _Sample_type solution _Details 'Dimer concentration is 0.5 - 1 mM' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $GAL4 . mM 1 2.0 . stop_ save_ save_gal4_sample2 _Saveframe_category sample _Sample_type solution _Details 'Dimer concentration is 0.5 - 1 mM' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $GAL4 . mM 1.0 2.0 '[U-15N; U-2H]' stop_ save_ save_gal4_sample3 _Saveframe_category sample _Sample_type solution _Details 'Dimer concentration is 0.5 - 1 mM' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $GAL4 . mM 1.0 2.0 [U-15N] stop_ save_ save_gal4_sample4 _Saveframe_category sample _Sample_type solution _Details 'Dimer concentration is 0.5 - 1 mM' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $GAL4 . mM 1.0 2.0 '[U-15N; U-13C]' stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name FELIX _Version . loop_ _Task 'Data processing' stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Task Assignments stop_ _Details . save_ save_MOLMOL _Saveframe_category software _Name Molmol _Version . loop_ _Task 'Visual inspection of structures' stop_ _Details . save_ save_InsightII _Saveframe_category software _Name InsightII _Version . loop_ _Task 'Visual inspection of structures' stop_ _Details . save_ save_PROCHECK _Saveframe_category software _Name Procheck _Version . loop_ _Task 'Assesment quality of structures' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 400 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 500 _Details . save_ save_NMR_spectrometer3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ save_NMR_spectrometer4 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 750 _Details . save_ save_NMR_spectrometer5 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label . save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label . save_ save_2D_1H-15N_HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label . save_ save_3D_1H-1H-15N_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _Sample_label . save_ save_3D_13C-1H-1H_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-1H-1H NOESY' _Sample_label . save_ save_3D_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label . save_ save_3D_HNHA_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label . save_ save_3D_HNHB_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _BMRB_pulse_sequence_accession_number . _Details . 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' 0.1 . M pH 7.4 0.2 n/a temperature 308 1 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 _Indirect_shift_ratio TMS H 1 'methyl protons' ppm 0.00 external direct cylindrical external_to_the_sample parallel_to_Bo 1 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 $gal4_sample1 $gal4_sample2 $gal4_sample3 $gal4_sample4 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chem_shift_ref _Mol_system_component_name 'Gal4 subunit A, monomer' _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 . 5 LEU CA C 51.43 . . 2 . 6 THR N N 113.89 . . 3 . 6 THR H H 8.21 . . 4 . 6 THR HA H 4.28 . . 5 . 6 THR CA C 58.49 . . 6 . 7 GLU CA C 54.74 . . 7 . 8 VAL N N 119.62 . . 8 . 8 VAL H H 7.89 . . 9 . 8 VAL HA H 3.67 . . 10 . 8 VAL HB H 2.02 . . 11 . 8 VAL CA C 61.48 . . 12 . 9 GLU N N 119.81 . . 13 . 9 GLU H H 8.00 . . 14 . 9 GLU HA H 3.83 . . 15 . 9 GLU HB2 H 2.13 . . 16 . 9 GLU HB3 H 2.01 . . 17 . 9 GLU CA C 55.51 . . 18 . 10 SER N N 116.11 . . 19 . 10 SER H H 8.19 . . 20 . 10 SER HA H 4.23 . . 21 . 10 SER HB2 H 3.90 . . 22 . 10 SER HB3 H 3.90 . . 23 . 10 SER CA C 56.78 . . 24 . 11 ARG N N 124.43 . . 25 . 11 ARG H H 7.99 . . 26 . 11 ARG HA H 3.95 . . 27 . 11 ARG HB2 H 1.85 . . 28 . 11 ARG HB3 H 1.85 . . 29 . 11 ARG CA C 55.47 . . 30 . 12 LEU N N 119.62 . . 31 . 12 LEU H H 8.20 . . 32 . 12 LEU HA H 3.99 . . 33 . 12 LEU HB2 H 1.96 . . 34 . 12 LEU HB3 H 1.50 . . 35 . 12 LEU CA C 54.12 . . 36 . 13 GLU N N 118.88 . . 37 . 13 GLU H H 7.97 . . 38 . 13 GLU HA H 4.06 . . 39 . 13 GLU HB2 H 2.12 . . 40 . 13 GLU HB3 H 2.12 . . 41 . 13 GLU CA C 55.27 . . 42 . 14 ARG N N 118.70 . . 43 . 14 ARG H H 7.70 . . 44 . 14 ARG HA H 4.10 . . 45 . 14 ARG HB2 H 1.97 . . 46 . 14 ARG HB3 H 1.85 . . 47 . 14 ARG CA C 54.09 . . 48 . 15 LEU N N 120.73 . . 49 . 15 LEU H H 8.25 . . 50 . 15 LEU HA H 4.04 . . 51 . 15 LEU HB2 H 2.02 . . 52 . 15 LEU HB3 H 1.60 . . 53 . 15 LEU CA C 53.54 . . 54 . 16 GLU N N 120.92 . . 55 . 16 GLU H H 8.90 . . 56 . 16 GLU HA H 3.92 . . 57 . 16 GLU HB2 H 2.25 . . 58 . 16 GLU HB3 H 1.98 . . 59 . 16 GLU CA C 56.70 . . 60 . 17 GLN N N 117.59 . . 61 . 17 GLN H H 8.02 . . 62 . 17 GLN HA H 3.95 . . 63 . 19 PHE N N 118.51 . . 64 . 19 PHE H H 8.42 . . 65 . 19 PHE HA H 4.31 . . 66 . 21 LEU N N 118.51 . . 67 . 21 LEU H H 7.58 . . 68 . 21 LEU HA H 4.20 . . 69 . 21 LEU HB2 H 1.99 . . 70 . 21 LEU HB3 H 1.52 . . 71 . 21 LEU HG H 1.75 . . 72 . 21 LEU CA C 52.46 . . 73 . 22 ILE N N 116.29 . . 74 . 22 ILE H H 7.47 . . 75 . 22 ILE HA H 3.83 . . 76 . 22 ILE HB H 1.44 . . 77 . 22 ILE CA C 58.39 . . 78 . 23 PHE N N 119.25 . . 79 . 23 PHE H H 8.44 . . 80 . 23 PHE HA H 5.09 . . 81 . 23 PHE HB2 H 2.77 . . 82 . 23 PHE HB3 H 2.77 . . 83 . 23 PHE CA C 50.19 . . 84 . 29 ASP N N 117.40 . . 85 . 29 ASP H H 8.10 . . 86 . 29 ASP HA H 4.18 . . 87 . 30 MET N N 118.70 . . 88 . 30 MET H H 7.36 . . 89 . 30 MET HA H 4.04 . . 90 . 30 MET HB2 H 2.15 . . 91 . 30 MET HB3 H 2.15 . . 92 . 31 ILE N N 121.84 . . 93 . 31 ILE H H 7.82 . . 94 . 31 ILE HA H 3.66 . . 95 . 31 ILE HB H 1.75 . . 96 . 32 LEU N N 117.96 . . 97 . 32 LEU H H 8.00 . . 98 . 32 LEU HA H 4.02 . . 99 . 32 LEU HB2 H 1.79 . . 100 . 32 LEU HB3 H 1.48 . . 101 . 33 LYS N N 117.77 . . 102 . 33 LYS H H 7.25 . . 103 . 33 LYS HA H 4.21 . . 104 . 33 LYS HB2 H 1.91 . . 105 . 33 LYS HB3 H 1.74 . . 106 . 33 LYS HG2 H 1.50 . . 107 . 33 LYS HG3 H 1.50 . . 108 . 34 MET N N 120.73 . . 109 . 34 MET H H 7.42 . . 110 . 34 MET HA H 4.21 . . 111 . 34 MET HB2 H 2.07 . . 112 . 34 MET HB3 H 2.07 . . 113 . 35 ASP CA C 51.29 . . 114 . 36 SER N N 112.59 . . 115 . 36 SER H H 7.74 . . 116 . 36 SER HA H 4.50 . . 117 . 36 SER HB2 H 3.86 . . 118 . 36 SER HB3 H 3.82 . . 119 . 36 SER CA C 51.94 . . 120 . 37 LEU N N 122.22 . . 121 . 37 LEU H H 8.24 . . 122 . 37 LEU CA C 50.06 . . 123 . 38 ARG N N 119.44 . . 124 . 38 ARG H H 8.00 . . 125 . 38 ARG CA C 54.12 . . 126 . 39 ASP N N 120.18 . . 127 . 39 ASP H H 7.65 . . 128 . 39 ASP HB2 H 2.74 . . 129 . 39 ASP HB3 H 2.74 . . 130 . 39 ASP CA C 52.06 . . 131 . 40 ILE N N 121.29 . . 132 . 40 ILE H H 7.62 . . 133 . 40 ILE HA H 3.67 . . 134 . 40 ILE HB H 1.91 . . 135 . 40 ILE CA C 59.76 . . 136 . 41 GLU N N 121.10 . . 137 . 41 GLU H H 8.39 . . 138 . 41 GLU HA H 3.73 . . 139 . 41 GLU HB2 H 2.07 . . 140 . 41 GLU HB3 H 2.07 . . 141 . 41 GLU CA C 55.78 . . 142 . 42 ALA N N 121.29 . . 143 . 42 ALA H H 7.76 . . 144 . 42 ALA HA H 4.10 . . 145 . 42 ALA HB H 1.46 . . 146 . 42 ALA CA C 50.28 . . 147 . 43 LEU N N 120.18 . . 148 . 43 LEU H H 7.57 . . 149 . 43 LEU HA H 4.10 . . 150 . 43 LEU HB2 H 1.71 . . 151 . 43 LEU HB3 H 1.71 . . 152 . 43 LEU CA C 52.87 . . 153 . 44 LEU N N 118.33 . . 154 . 44 LEU H H 7.99 . . 155 . 44 LEU HA H 4.03 . . 156 . 44 LEU HB2 H 1.81 . . 157 . 44 LEU HB3 H 1.50 . . 158 . 44 LEU CA C 52.40 . . 159 . 45 THR N N 112.78 . . 160 . 45 THR H H 7.89 . . 161 . 45 THR HA H 4.24 . . 162 . 45 THR HB H 4.05 . . 163 . 45 THR CA C 60.53 . . 164 . 46 GLY N N 109.82 . . 165 . 46 GLY H H 7.87 . . 166 . 46 GLY HA2 H 3.94 . . 167 . 46 GLY HA3 H 3.94 . . 168 . 46 GLY CA C 41.45 . . 169 . 47 LEU N N 121.10 . . 170 . 47 LEU H H 7.53 . . 171 . 47 LEU HA H 4.16 . . 172 . 47 LEU HB2 H 1.49 . . 173 . 47 LEU HB3 H 1.16 . . 174 . 47 LEU CA C 51.56 . . 175 . 48 PHE N N 118.14 . . 176 . 48 PHE H H 7.78 . . 177 . 48 PHE HA H 4.69 . . 178 . 48 PHE HB2 H 3.19 . . 179 . 48 PHE HB3 H 2.90 . . 180 . 48 PHE CA C 53.06 . . 181 . 49 VAL N N 120.92 . . 182 . 49 VAL H H 7.82 . . 183 . 49 VAL HA H 4.08 . . 184 . 49 VAL HB H 2.05 . . 185 . 49 VAL HG1 H 0.90 . . 186 . 49 VAL HG2 H 0.90 . . 187 . 49 VAL CA C 58.01 . . 188 . 50 GLN N N 124.62 . . 189 . 50 GLN H H 8.30 . . 190 . 50 GLN HA H 4.31 . . 191 . 50 GLN HB2 H 2.06 . . 192 . 50 GLN HB3 H 1.95 . . 193 . 50 GLN HG2 H 2.31 . . 194 . 50 GLN HG3 H 2.31 . . 195 . 50 GLN CA C 51.37 . . 196 . 51 ASP N N 122.21 . . 197 . 51 ASP H H 8.29 . . 198 . 51 ASP HA H 2.61 . . 199 . 51 ASP CA C 49.95 . . 200 . 52 ASN CA C 48.87 . . 201 . 53 VAL N N 120.55 . . 202 . 53 VAL H H 7.94 . . 203 . 53 VAL HA H 4.04 . . 204 . 53 VAL HB H 2.07 . . 205 . 53 VAL HG1 H 0.91 . . 206 . 53 VAL HG2 H 0.91 . . 207 . 53 VAL CA C 58.28 . . 208 . 57 ALA N N 129.98 . . 209 . 57 ALA H H 7.65 . . 210 . 57 ALA HA H 4.09 . . 211 . 57 ALA HB H 1.17 . . stop_ save_