data_4294 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Resonance Assignments, Secondary Structure and 15N Relaxation data of the Human Transcriptional Coactivator hMBF1(57-148) ; _BMRB_accession_number 4294 _BMRB_flat_file_name bmr4294.str _Entry_type original _Submission_date 1999-01-12 _Accession_date 1999-01-19 _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 Mishima Masaki . . 2 Ozaki J. . . 3 Ikegami T. . . 4 Kabe Y. . . 5 Goto M. . . 6 Ueda H. . . 7 Hirose S. . . 8 Handa H. . . 9 Shirakawa Masahiro . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 391 "13C chemical shifts" 340 "15N chemical shifts" 79 "coupling constants" 30 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-12-18 original author . stop_ _Original_release_date 2000-12-18 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Mishima, M., Ozaki, J., Ikegami, T., Kabe, Y., Goto, M., Ueda, H., Hirose, S., Handa, H., and Shirakawa, M., "Resonance Assignments, Secondary Structure and 15N Relaxation data of the Human Transcriptional Coactivator hMBF1(57-148)," J. Biomol. NMR 14, 373-376 (1999). ; _Citation_title ; Resonance Assignments, Secondary Structure and 15N Relaxation data of the Human Transcriptional Coactivator hMBF1(57-148) ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99455329 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mishima Masaki . . 2 Ozaki J. . . 3 Ikegami T. . . 4 Kabe Y. . . 5 Goto M. . . 6 Ueda H. . . 7 Hirose S. . . 8 Handa H. . . 9 Shirakawa Masahiro . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 14 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 373 _Page_last 376 _Year 1999 _Details . save_ ################################## # Molecular system description # ################################## save_system_hMBF1c _Saveframe_category molecular_system _Mol_system_name 'human MBF1(57-148) core domain' _Abbreviation_common hMBF1c _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label hMBF1c $hMBF1c stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'transciptional coactivator' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_hMBF1c _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'human Multi Protein Bridging Factor type1' _Abbreviation_common hMBF1c _Molecular_mass . _Mol_thiol_state . _Details 'EDF-1 protein is identical with human MBF1"' ############################## # Polymer residue sequence # ############################## _Residue_count 92 _Mol_residue_sequence ; NTAKLDRETEELHHDRVTLE VGKVIQQGRQSKGLTQKDLA TKINEKPQVIADYESGRAIP NNQVLGKIERAIGLKLRGKD IGKPIEKGPRAK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 57 ASN 2 58 THR 3 59 ALA 4 60 LYS 5 61 LEU 6 62 ASP 7 63 ARG 8 64 GLU 9 65 THR 10 66 GLU 11 67 GLU 12 68 LEU 13 69 HIS 14 70 HIS 15 71 ASP 16 72 ARG 17 73 VAL 18 74 THR 19 75 LEU 20 76 GLU 21 77 VAL 22 78 GLY 23 79 LYS 24 80 VAL 25 81 ILE 26 82 GLN 27 83 GLN 28 84 GLY 29 85 ARG 30 86 GLN 31 87 SER 32 88 LYS 33 89 GLY 34 90 LEU 35 91 THR 36 92 GLN 37 93 LYS 38 94 ASP 39 95 LEU 40 96 ALA 41 97 THR 42 98 LYS 43 99 ILE 44 100 ASN 45 101 GLU 46 102 LYS 47 103 PRO 48 104 GLN 49 105 VAL 50 106 ILE 51 107 ALA 52 108 ASP 53 109 TYR 54 110 GLU 55 111 SER 56 112 GLY 57 113 ARG 58 114 ALA 59 115 ILE 60 116 PRO 61 117 ASN 62 118 ASN 63 119 GLN 64 120 VAL 65 121 LEU 66 122 GLY 67 123 LYS 68 124 ILE 69 125 GLU 70 126 ARG 71 127 ALA 72 128 ILE 73 129 GLY 74 130 LEU 75 131 LYS 76 132 LEU 77 133 ARG 78 134 GLY 79 135 LYS 80 136 ASP 81 137 ILE 82 138 GLY 83 139 LYS 84 140 PRO 85 141 ILE 86 142 GLU 87 143 LYS 88 144 GLY 89 145 PRO 90 146 ARG 91 147 ALA 92 148 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-11 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 1X57 "Solution Structures Of The Hth Domain Of Human Edf-1 Protein" 84.78 91 100.00 100.00 9.13e-46 DBJ BAA88073 "hMBF1alpha [Homo sapiens]" 100.00 148 100.00 100.00 1.58e-57 DBJ BAA88074 "hMBF1beta [Homo sapiens]" 79.35 139 100.00 100.00 2.79e-43 DBJ BAA92749 "unnamed protein product [Mus musculus]" 100.00 148 97.83 100.00 3.16e-56 DBJ BAB22026 "unnamed protein product [Mus musculus]" 100.00 148 97.83 100.00 3.16e-56 DBJ BAB22854 "unnamed protein product [Mus musculus]" 100.00 148 97.83 100.00 3.16e-56 EMBL CAA06446 "EDF-1 [Homo sapiens]" 100.00 148 100.00 100.00 1.58e-57 EMBL CAC32040 "EDF-1 protein [Mus musculus]" 100.00 148 98.91 100.00 9.23e-57 EMBL CAG46712 "EDF1 [Homo sapiens]" 100.00 148 100.00 100.00 1.58e-57 GB AAH15500 "Endothelial differentiation-related factor 1 [Homo sapiens]" 100.00 148 100.00 100.00 1.58e-57 GB AAH23472 "Endothelial differentiation-related factor 1 [Mus musculus]" 100.00 148 97.83 100.00 3.16e-56 GB AAI02247 "Endothelial differentiation-related factor 1 [Bos taurus]" 100.00 148 100.00 100.00 1.58e-57 GB AAI58850 "Endothelial differentiation-related factor 1 [Rattus norvegicus]" 100.00 148 97.83 100.00 3.16e-56 GB AAP88865 "endothelial differentiation-related factor 1 [Homo sapiens]" 100.00 148 100.00 100.00 1.58e-57 REF NP_001030384 "endothelial differentiation-related factor 1 [Bos taurus]" 100.00 148 100.00 100.00 1.58e-57 REF NP_001100027 "endothelial differentiation-related factor 1 [Rattus norvegicus]" 100.00 148 97.83 100.00 3.16e-56 REF NP_001180526 "endothelial differentiation-related factor 1 [Macaca mulatta]" 100.00 148 100.00 100.00 1.58e-57 REF NP_003783 "endothelial differentiation-related factor 1 isoform alpha [Homo sapiens]" 100.00 148 100.00 100.00 1.58e-57 REF NP_067494 "endothelial differentiation-related factor 1 [Mus musculus]" 100.00 148 97.83 100.00 3.16e-56 SP O60869 "RecName: Full=Endothelial differentiation-related factor 1; Short=EDF-1; AltName: Full=Multiprotein-bridging factor 1; Short=MB" 100.00 148 100.00 100.00 1.58e-57 SP P69736 "RecName: Full=Endothelial differentiation-related factor 1; Short=EDF-1; AltName: Full=Calmodulin-associated peptide 19; Short=" 100.00 148 97.83 100.00 3.16e-56 SP Q3T0V7 "RecName: Full=Endothelial differentiation-related factor 1; Short=EDF-1" 100.00 148 100.00 100.00 1.58e-57 SP Q9JMG1 "RecName: Full=Endothelial differentiation-related factor 1; Short=EDF-1; AltName: Full=Multiprotein-bridging factor 1; Short=MB" 100.00 148 97.83 100.00 3.16e-56 TPG DAA24072 "TPA: endothelial differentiation-related factor 1 [Bos taurus]" 100.00 148 100.00 100.00 1.58e-57 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $hMBF1c Human 9606 Eukaryota Metazoa Homo sapiens 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 $hMBF1c recombinant_technology . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $hMBF1c . mM 0.50 2.0 . 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 $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.2 n/a temperature 310 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 0.00 external indirect cylindrical external_to_the_sample parallel_to_Bo 0.25144952 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.00 external indirect cylindrical external_to_the_sample parallel_to_Bo 1 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.00 external indirect cylindrical external_to_the_sample parallel_to_Bo 0.10132905 $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_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name hMBF1c _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 . 1 ASN HA H 4.84 . 1 2 . 1 ASN HB2 H 2.83 . 2 3 . 1 ASN CA C 53.35 . 1 4 . 1 ASN CB C 37.99 . 1 5 . 2 THR H H 8.23 . 1 6 . 2 THR HA H 4.33 . 1 7 . 2 THR HB H 4.10 . 1 8 . 2 THR HG2 H 1.40 . 1 9 . 2 THR CA C 61.86 . 1 10 . 2 THR CB C 69.10 . 1 11 . 2 THR CG2 C 21.88 . 1 12 . 2 THR N N 116.22 . 1 13 . 3 ALA H H 8.23 . 1 14 . 3 ALA HA H 4.32 . 1 15 . 3 ALA HB H 1.39 . 1 16 . 3 ALA C C 177.54 . 1 17 . 3 ALA CA C 52.72 . 1 18 . 3 ALA CB C 19.34 . 1 19 . 3 ALA N N 127.20 . 1 20 . 4 LYS H H 8.15 . 1 21 . 4 LYS HA H 4.28 . 1 22 . 4 LYS HB2 H 1.80 . 2 23 . 4 LYS HB3 H 1.70 . 2 24 . 4 LYS HG2 H 1.23 . 2 25 . 4 LYS HD2 H 1.40 . 2 26 . 4 LYS HE2 H 2.99 . 2 27 . 4 LYS C C 176.43 . 1 28 . 4 LYS CA C 56.30 . 1 29 . 4 LYS CB C 32.99 . 1 30 . 4 LYS CG C 24.76 . 1 31 . 4 LYS CD C 29.48 . 1 32 . 4 LYS CE C 42.14 . 1 33 . 4 LYS N N 121.52 . 1 34 . 5 LEU H H 8.21 . 1 35 . 5 LEU HA H 4.36 . 1 36 . 5 LEU HB2 H 1.62 . 2 37 . 5 LEU HG H 1.61 . 1 38 . 5 LEU HD1 H 0.86 . 1 39 . 5 LEU HD2 H 0.91 . 1 40 . 5 LEU C C 177.11 . 1 41 . 5 LEU CA C 55.34 . 1 42 . 5 LEU CB C 42.62 . 1 43 . 5 LEU CG C 27.17 . 1 44 . 5 LEU CD1 C 23.70 . 1 45 . 5 LEU CD2 C 24.86 . 1 46 . 5 LEU N N 124.66 . 1 47 . 6 ASP H H 8.28 . 1 48 . 6 ASP HA H 4.58 . 1 49 . 6 ASP HB2 H 2.65 . 2 50 . 6 ASP C C 176.21 . 1 51 . 6 ASP CA C 54.53 . 1 52 . 6 ASP CB C 40.33 . 1 53 . 6 ASP N N 122.27 . 1 54 . 7 ARG H H 8.15 . 1 55 . 7 ARG HA H 4.31 . 1 56 . 7 ARG HB2 H 1.86 . 2 57 . 7 ARG HG2 H 1.62 . 2 58 . 7 ARG HG3 H 1.78 . 2 59 . 7 ARG HD2 H 3.19 . 2 60 . 7 ARG C C 176.54 . 1 61 . 7 ARG CA C 56.30 . 1 62 . 7 ARG CB C 30.63 . 1 63 . 7 ARG CG C 27.18 . 1 64 . 7 ARG CD C 43.40 . 1 65 . 7 ARG N N 121.38 . 1 66 . 8 GLU H H 8.47 . 1 67 . 8 GLU HA H 4.28 . 1 68 . 8 GLU HB2 H 2.02 . 2 69 . 8 GLU HG2 H 2.28 . 2 70 . 8 GLU C C 177.06 . 1 71 . 8 GLU N N 122.23 . 1 72 . 9 THR H H 8.02 . 1 73 . 9 THR HA H 4.29 . 1 74 . 9 THR HG2 H 1.21 . 1 75 . 9 THR C C 174.79 . 1 76 . 9 THR CA C 62.28 . 1 77 . 9 THR CG2 C 21.83 . 1 78 . 9 THR N N 115.15 . 1 79 . 10 GLU H H 8.28 . 1 80 . 10 GLU HA H 4.24 . 1 81 . 10 GLU HB2 H 2.01 . 2 82 . 10 GLU HG2 H 2.25 . 2 83 . 10 GLU C C 176.62 . 1 84 . 10 GLU CA C 57.04 . 1 85 . 10 GLU CB C 30.52 . 1 86 . 10 GLU CG C 36.38 . 1 87 . 10 GLU N N 123.88 . 1 88 . 11 GLU H H 8.30 . 1 89 . 11 GLU HA H 4.19 . 1 90 . 11 GLU HB2 H 1.93 . 2 91 . 11 GLU HG2 H 2.22 . 2 92 . 11 GLU C C 176.38 . 1 93 . 11 GLU CA C 56.86 . 1 94 . 11 GLU CB C 30.41 . 1 95 . 11 GLU CG C 36.36 . 1 96 . 11 GLU N N 122.38 . 1 97 . 12 LEU H H 8.03 . 1 98 . 12 LEU HA H 4.25 . 1 99 . 12 LEU HB2 H 1.53 . 2 100 . 12 LEU HB3 H 1.40 . 2 101 . 12 LEU HG H 1.53 . 1 102 . 12 LEU HD1 H 0.82 . 1 103 . 12 LEU C C 177.12 . 1 104 . 12 LEU CA C 55.37 . 1 105 . 12 LEU CB C 42.53 . 1 106 . 12 LEU CG C 27.17 . 1 107 . 12 LEU CD1 C 23.67 . 1 108 . 12 LEU N N 123.36 . 1 109 . 13 HIS H H 8.24 . 1 110 . 13 HIS HA H 4.66 . 1 111 . 13 HIS HB2 H 3.10 . 2 112 . 13 HIS HB3 H 3.17 . 2 113 . 13 HIS C C 174.90 . 1 114 . 13 HIS CA C 55.66 . 1 115 . 13 HIS CB C 30.03 . 1 116 . 13 HIS N N 119.98 . 1 117 . 17 VAL H H 8.15 . 1 118 . 17 VAL HA H 4.09 . 1 119 . 17 VAL HB H 2.01 . 1 120 . 17 VAL HG1 H 0.94 . 1 121 . 17 VAL C C 176.24 . 1 122 . 17 VAL CA C 63.18 . 1 123 . 17 VAL CB C 32.61 . 1 124 . 17 VAL CG1 C 21.22 . 1 125 . 17 VAL N N 122.15 . 1 126 . 18 THR H H 8.07 . 1 127 . 18 THR HA H 4.26 . 1 128 . 18 THR HB H 1.21 . 1 129 . 18 THR HG2 H 0.88 . 1 130 . 18 THR C C 175.32 . 1 131 . 18 THR CA C 62.23 . 1 132 . 18 THR CB C 68.31 . 1 133 . 18 THR CG2 C 21.93 . 1 134 . 18 THR N N 117.90 . 1 135 . 19 LEU H H 8.21 . 1 136 . 19 LEU HA H 4.27 . 1 137 . 19 LEU HB2 H 1.64 . 2 138 . 19 LEU HD1 H 0.86 . 1 139 . 19 LEU HD2 H 0.91 . 1 140 . 19 LEU C C 177.72 . 1 141 . 19 LEU CA C 55.93 . 1 142 . 19 LEU CB C 42.49 . 1 143 . 19 LEU CG C 27.15 . 1 144 . 19 LEU CD1 C 23.74 . 1 145 . 19 LEU N N 124.83 . 1 146 . 20 GLU H H 8.28 . 1 147 . 20 GLU HA H 4.22 . 1 148 . 20 GLU HB2 H 2.03 . 2 149 . 20 GLU HG2 H 2.30 . 2 150 . 20 GLU C C 178.08 . 1 151 . 20 GLU N N 121.54 . 1 152 . 21 VAL H H 8.15 . 1 153 . 21 VAL HA H 3.62 . 1 154 . 21 VAL HB H 2.19 . 1 155 . 21 VAL HG1 H 1.00 . 1 156 . 21 VAL HG2 H 1.12 . 1 157 . 21 VAL C C 177.48 . 1 158 . 21 VAL CA C 66.38 . 1 159 . 21 VAL CB C 32.22 . 1 160 . 21 VAL CG1 C 21.20 . 1 161 . 21 VAL CG2 C 23.43 . 1 162 . 21 VAL N N 122.44 . 1 163 . 22 GLY H H 8.60 . 1 164 . 22 GLY HA2 H 3.72 . 2 165 . 22 GLY HA3 H 4.14 . 2 166 . 22 GLY C C 175.84 . 1 167 . 22 GLY CA C 48.90 . 1 168 . 22 GLY N N 127.30 . 1 169 . 23 LYS H H 7.54 . 1 170 . 23 LYS HA H 4.18 . 1 171 . 23 LYS HB2 H 1.96 . 2 172 . 23 LYS HG2 H 1.48 . 2 173 . 23 LYS HG3 H 1.59 . 2 174 . 23 LYS HD2 H 1.70 . 2 175 . 23 LYS HE2 H 2.97 . 2 176 . 23 LYS C C 179.21 . 1 177 . 23 LYS CA C 58.62 . 1 178 . 23 LYS CB C 32.30 . 1 179 . 23 LYS CG C 25.30 . 1 180 . 23 LYS CD C 29.31 . 1 181 . 23 LYS CE C 42.21 . 1 182 . 23 LYS N N 120.39 . 1 183 . 24 VAL H H 7.66 . 1 184 . 24 VAL HA H 3.67 . 1 185 . 24 VAL HB H 2.13 . 1 186 . 24 VAL HG1 H 0.87 . 1 187 . 24 VAL HG2 H 0.99 . 1 188 . 24 VAL C C 178.67 . 1 189 . 24 VAL CA C 66.29 . 1 190 . 24 VAL CB C 31.53 . 1 191 . 24 VAL CG1 C 23.43 . 1 192 . 24 VAL CG2 C 22.78 . 1 193 . 24 VAL N N 122.34 . 1 194 . 25 ILE H H 8.24 . 1 195 . 25 ILE HA H 3.43 . 1 196 . 25 ILE HB H 2.02 . 1 197 . 25 ILE HG12 H 2.08 . 2 198 . 25 ILE HG13 H 0.76 . 2 199 . 25 ILE HG2 H 0.99 . 1 200 . 25 ILE HD1 H 0.82 . 1 201 . 25 ILE C C 177.08 . 1 202 . 25 ILE CA C 66.48 . 1 203 . 25 ILE CB C 38.09 . 1 204 . 25 ILE CG1 C 30.17 . 1 205 . 25 ILE CG2 C 16.98 . 1 206 . 25 ILE CD1 C 14.44 . 1 207 . 25 ILE N N 120.93 . 1 208 . 26 GLN H H 7.89 . 1 209 . 26 GLN HA H 3.90 . 1 210 . 26 GLN HB2 H 2.14 . 2 211 . 26 GLN HB3 H 2.01 . 2 212 . 26 GLN HG2 H 2.43 . 2 213 . 26 GLN HG3 H 2.10 . 2 214 . 26 GLN C C 178.18 . 1 215 . 26 GLN CA C 60.05 . 1 216 . 26 GLN CB C 29.37 . 1 217 . 26 GLN CG C 34.12 . 1 218 . 26 GLN N N 119.36 . 1 219 . 27 GLN H H 8.34 . 1 220 . 27 GLN HA H 4.05 . 1 221 . 27 GLN HB2 H 2.16 . 2 222 . 27 GLN C C 179.91 . 1 223 . 27 GLN CA C 58.89 . 1 224 . 27 GLN CB C 28.50 . 1 225 . 27 GLN CG C 34.06 . 1 226 . 27 GLN N N 119.36 . 1 227 . 28 GLY H H 9.02 . 1 228 . 28 GLY HA2 H 3.92 . 2 229 . 28 GLY HA3 H 3.60 . 2 230 . 28 GLY C C 176.27 . 1 231 . 28 GLY CA C 47.22 . 1 232 . 28 GLY N N 128.56 . 1 233 . 29 ARG H H 9.10 . 1 234 . 29 ARG HA H 3.93 . 1 235 . 29 ARG HB2 H 1.55 . 2 236 . 29 ARG HB3 H 1.79 . 2 237 . 29 ARG HG2 H 1.80 . 2 238 . 29 ARG HG3 H 2.12 . 2 239 . 29 ARG HD2 H 2.72 . 2 240 . 29 ARG C C 178.89 . 1 241 . 29 ARG CA C 60.85 . 1 242 . 29 ARG CB C 28.89 . 1 243 . 29 ARG CG C 28.29 . 1 244 . 29 ARG CD C 42.10 . 1 245 . 29 ARG N N 123.15 . 1 246 . 30 GLN H H 8.38 . 1 247 . 30 GLN HA H 4.16 . 1 248 . 30 GLN HB2 H 2.14 . 2 249 . 30 GLN HB3 H 2.29 . 2 250 . 30 GLN HG2 H 2.41 . 2 251 . 30 GLN HG3 H 2.63 . 2 252 . 30 GLN C C 180.56 . 1 253 . 30 GLN CA C 59.30 . 1 254 . 30 GLN CB C 28.05 . 1 255 . 30 GLN CG C 34.70 . 1 256 . 30 GLN N N 120.38 . 1 257 . 31 SER H H 8.35 . 1 258 . 31 SER HA H 4.33 . 1 259 . 31 SER HB2 H 4.10 . 2 260 . 31 SER C C 175.66 . 1 261 . 31 SER CA C 61.62 . 1 262 . 31 SER CB C 63.99 . 1 263 . 31 SER N N 117.56 . 1 264 . 32 LYS H H 7.27 . 1 265 . 32 LYS HA H 4.48 . 1 266 . 32 LYS HB2 H 1.84 . 2 267 . 32 LYS HB3 H 2.10 . 2 268 . 32 LYS HG2 H 1.66 . 2 269 . 32 LYS HD2 H 1.66 . 2 270 . 32 LYS C C 176.61 . 1 271 . 32 LYS CA C 55.05 . 1 272 . 32 LYS CB C 33.43 . 1 273 . 32 LYS CG C 24.86 . 1 274 . 32 LYS CD C 28.72 . 1 275 . 32 LYS CE C 42.06 . 1 276 . 32 LYS N N 119.01 . 1 277 . 33 GLY H H 7.94 . 1 278 . 33 GLY HA2 H 3.85 . 2 279 . 33 GLY HA3 H 3.99 . 2 280 . 33 GLY C C 174.43 . 1 281 . 33 GLY CA C 46.47 . 1 282 . 33 GLY N N 128.50 . 1 283 . 34 LEU H H 7.65 . 1 284 . 34 LEU HA H 4.90 . 1 285 . 34 LEU HB2 H 1.65 . 2 286 . 34 LEU HB3 H 1.43 . 2 287 . 34 LEU HG H 1.46 . 1 288 . 34 LEU HD1 H 0.76 . 1 289 . 34 LEU HD2 H 0.80 . 1 290 . 34 LEU C C 178.41 . 1 291 . 34 LEU CA C 53.24 . 1 292 . 34 LEU CB C 44.35 . 1 293 . 34 LEU CG C 26.28 . 1 294 . 34 LEU CD1 C 26.15 . 1 295 . 34 LEU CD2 C 23.29 . 1 296 . 34 LEU N N 119.11 . 1 297 . 35 THR H H 9.27 . 1 298 . 35 THR HA H 4.41 . 1 299 . 35 THR HG2 H 1.40 . 1 300 . 35 THR C C 176.24 . 1 301 . 35 THR CA C 61.61 . 1 302 . 35 THR CG2 C 21.88 . 1 303 . 35 THR N N 116.34 . 1 304 . 36 GLN H H 9.22 . 1 305 . 36 GLN HA H 3.66 . 1 306 . 36 GLN HB2 H 2.12 . 2 307 . 36 GLN HB3 H 1.66 . 2 308 . 36 GLN HG2 H 2.61 . 2 309 . 36 GLN C C 178.29 . 1 310 . 36 GLN CA C 61.15 . 1 311 . 36 GLN CB C 28.08 . 1 312 . 36 GLN CG C 34.26 . 1 313 . 36 GLN N N 121.28 . 1 314 . 37 LYS H H 8.26 . 1 315 . 37 LYS HA H 3.83 . 1 316 . 37 LYS HB2 H 1.82 . 2 317 . 37 LYS HG2 H 1.42 . 2 318 . 37 LYS HD2 H 1.64 . 2 319 . 37 LYS HD3 H 2.15 . 2 320 . 37 LYS HE2 H 2.97 . 2 321 . 37 LYS C C 178.32 . 1 322 . 37 LYS CA C 59.97 . 1 323 . 37 LYS CB C 32.25 . 1 324 . 37 LYS CG C 25.43 . 1 325 . 37 LYS CD C 28.30 . 1 326 . 37 LYS CE C 42.13 . 1 327 . 37 LYS N N 119.01 . 1 328 . 38 ASP H H 8.08 . 1 329 . 38 ASP HA H 4.35 . 1 330 . 38 ASP HB2 H 2.88 . 2 331 . 38 ASP HB3 H 2.66 . 2 332 . 38 ASP C C 179.43 . 1 333 . 38 ASP CA C 57.38 . 1 334 . 38 ASP CB C 42.37 . 1 335 . 38 ASP N N 121.74 . 1 336 . 39 LEU H H 8.06 . 1 337 . 39 LEU HA H 3.98 . 1 338 . 39 LEU HB2 H 1.94 . 2 339 . 39 LEU HB3 H 1.15 . 2 340 . 39 LEU HG H 1.46 . 1 341 . 39 LEU HD1 H 0.85 . 1 342 . 39 LEU HD2 H 0.81 . 1 343 . 39 LEU C C 176.80 . 1 344 . 39 LEU CA C 57.76 . 1 345 . 39 LEU CB C 41.35 . 1 346 . 39 LEU CG C 27.44 . 1 347 . 39 LEU CD1 C 23.93 . 1 348 . 39 LEU CD2 C 26.58 . 1 349 . 39 LEU N N 120.66 . 1 350 . 40 ALA H H 8.22 . 1 351 . 40 ALA HA H 3.60 . 1 352 . 40 ALA HB H 1.45 . 1 353 . 40 ALA C C 179.35 . 1 354 . 40 ALA CA C 55.92 . 1 355 . 40 ALA CB C 17.90 . 1 356 . 40 ALA N N 121.82 . 1 357 . 41 THR H H 8.35 . 1 358 . 41 THR HA H 4.04 . 1 359 . 41 THR HB H 4.31 . 1 360 . 41 THR HG2 H 1.29 . 1 361 . 41 THR C C 177.49 . 1 362 . 41 THR CA C 66.35 . 1 363 . 41 THR CB C 69.70 . 1 364 . 41 THR CG2 C 21.77 . 1 365 . 41 THR N N 114.39 . 1 366 . 42 LYS H H 7.79 . 1 367 . 42 LYS HA H 4.11 . 1 368 . 42 LYS HB2 H 1.99 . 2 369 . 42 LYS HG2 H 1.57 . 2 370 . 42 LYS HD2 H 1.60 . 2 371 . 42 LYS C C 178.26 . 1 372 . 42 LYS CA C 59.18 . 1 373 . 42 LYS CB C 32.67 . 1 374 . 42 LYS CG C 25.31 . 1 375 . 42 LYS CD C 29.34 . 1 376 . 42 LYS CE C 41.90 . 1 377 . 42 LYS N N 121.97 . 1 378 . 43 ILE H H 7.47 . 1 379 . 43 ILE HA H 4.66 . 1 380 . 43 ILE HB H 2.14 . 1 381 . 43 ILE HG12 H 1.43 . 2 382 . 43 ILE HG13 H 1.14 . 2 383 . 43 ILE HG2 H 0.70 . 1 384 . 43 ILE HD1 H 0.64 . 1 385 . 43 ILE C C 174.47 . 1 386 . 43 ILE CA C 60.28 . 1 387 . 43 ILE CB C 39.01 . 1 388 . 43 ILE CG1 C 25.31 . 1 389 . 43 ILE CG2 C 17.36 . 1 390 . 43 ILE CD1 C 15.94 . 1 391 . 43 ILE N N 127.46 . 1 392 . 44 ASN H H 7.90 . 1 393 . 44 ASN HA H 4.37 . 1 394 . 44 ASN HB2 H 3.18 . 2 395 . 44 ASN HB3 H 2.71 . 2 396 . 44 ASN C C 173.87 . 1 397 . 44 ASN CA C 54.49 . 1 398 . 44 ASN CB C 37.40 . 1 399 . 44 ASN N N 120.81 . 1 400 . 45 GLU H H 8.18 . 1 401 . 45 GLU HA H 4.72 . 1 402 . 45 GLU HB2 H 1.19 . 2 403 . 45 GLU HG2 H 2.11 . 2 404 . 45 GLU C C 175.36 . 1 405 . 45 GLU CA C 53.68 . 1 406 . 45 GLU CB C 33.59 . 1 407 . 45 GLU CG C 35.54 . 1 408 . 45 GLU N N 117.18 . 1 409 . 46 LYS H H 8.89 . 1 410 . 46 LYS HA H 4.54 . 1 411 . 46 LYS HB2 H 2.05 . 2 412 . 46 LYS HB3 H 1.66 . 2 413 . 46 LYS HG2 H 1.57 . 2 414 . 46 LYS HD2 H 1.66 . 2 415 . 46 LYS C C 176.82 . 1 416 . 46 LYS CA C 54.86 . 1 417 . 46 LYS CB C 31.98 . 1 418 . 46 LYS CG C 25.46 . 1 419 . 46 LYS CD C 29.31 . 1 420 . 46 LYS N N 121.85 . 1 421 . 47 PRO HA H 3.88 . 1 422 . 47 PRO HB2 H 2.24 . 2 423 . 47 PRO HG2 H 1.99 . 2 424 . 47 PRO CA C 66.27 . 1 425 . 47 PRO CB C 31.35 . 1 426 . 47 PRO CG C 27.68 . 1 427 . 48 GLN H H 8.53 . 1 428 . 48 GLN HA H 3.85 . 1 429 . 48 GLN HB2 H 2.09 . 2 430 . 48 GLN HB3 H 1.84 . 2 431 . 48 GLN HG2 H 2.01 . 2 432 . 48 GLN C C 177.22 . 1 433 . 48 GLN CA C 58.53 . 1 434 . 48 GLN CB C 28.31 . 1 435 . 48 GLN CG C 31.68 . 1 436 . 48 GLN N N 116.91 . 1 437 . 49 VAL H H 7.30 . 1 438 . 49 VAL HA H 3.66 . 1 439 . 49 VAL HB H 2.09 . 1 440 . 49 VAL HG1 H 0.65 . 1 441 . 49 VAL HG2 H 1.06 . 1 442 . 49 VAL C C 177.58 . 1 443 . 49 VAL CA C 65.63 . 1 444 . 49 VAL CB C 31.39 . 1 445 . 49 VAL CG1 C 20.93 . 1 446 . 49 VAL CG2 C 22.93 . 1 447 . 49 VAL N N 118.95 . 1 448 . 50 ILE H H 6.70 . 1 449 . 50 ILE HA H 3.54 . 1 450 . 50 ILE HB H 2.13 . 1 451 . 50 ILE HG12 H 1.53 . 2 452 . 50 ILE HG13 H 1.26 . 2 453 . 50 ILE HG2 H 0.89 . 1 454 . 50 ILE HD1 H 0.58 . 1 455 . 50 ILE C C 177.94 . 1 456 . 50 ILE CA C 62.17 . 1 457 . 50 ILE CB C 35.38 . 1 458 . 50 ILE CG1 C 27.79 . 1 459 . 50 ILE CG2 C 19.08 . 1 460 . 50 ILE CD1 C 9.28 . 1 461 . 50 ILE N N 117.50 . 1 462 . 51 ALA H H 7.67 . 1 463 . 51 ALA HA H 4.01 . 1 464 . 51 ALA HB H 1.41 . 1 465 . 51 ALA C C 181.02 . 1 466 . 51 ALA CA C 55.60 . 1 467 . 51 ALA CB C 17.77 . 1 468 . 51 ALA N N 121.98 . 1 469 . 52 ASP H H 8.28 . 1 470 . 52 ASP HA H 4.36 . 1 471 . 52 ASP HB2 H 2.32 . 2 472 . 52 ASP HB3 H 2.88 . 2 473 . 52 ASP C C 179.14 . 1 474 . 52 ASP CA C 57.40 . 1 475 . 52 ASP CB C 39.35 . 1 476 . 52 ASP N N 121.14 . 1 477 . 53 TYR H H 8.50 . 1 478 . 53 TYR HA H 4.60 . 1 479 . 53 TYR HB2 H 2.81 . 2 480 . 53 TYR HB3 H 3.28 . 2 481 . 53 TYR C C 179.83 . 1 482 . 53 TYR CA C 59.46 . 1 483 . 53 TYR CB C 37.28 . 1 484 . 53 TYR N N 122.49 . 1 485 . 54 GLU H H 8.48 . 1 486 . 54 GLU HA H 4.13 . 1 487 . 54 GLU HB2 H 2.71 . 2 488 . 54 GLU HB3 H 2.24 . 2 489 . 54 GLU HG2 H 1.95 . 2 490 . 54 GLU C C 177.94 . 1 491 . 54 GLU CA C 59.82 . 1 492 . 54 GLU CB C 37.47 . 1 493 . 54 GLU CG C 29.71 . 1 494 . 54 GLU N N 118.57 . 1 495 . 55 SER H H 7.95 . 1 496 . 55 SER HA H 4.48 . 1 497 . 55 SER HB2 H 3.99 . 2 498 . 55 SER C C 175.56 . 1 499 . 55 SER CA C 58.62 . 1 500 . 55 SER CB C 64.56 . 1 501 . 55 SER N N 111.80 . 1 502 . 56 GLY H H 7.69 . 1 503 . 56 GLY HA2 H 3.95 . 2 504 . 56 GLY HA3 H 4.14 . 2 505 . 56 GLY C C 174.25 . 1 506 . 56 GLY CA C 46.12 . 1 507 . 56 GLY N N 110.73 . 1 508 . 57 ARG H H 8.14 . 1 509 . 57 ARG HA H 4.22 . 1 510 . 57 ARG HB2 H 1.58 . 2 511 . 57 ARG HB3 H 1.76 . 2 512 . 57 ARG HG2 H 1.60 . 2 513 . 57 ARG HD2 H 3.16 . 2 514 . 57 ARG C C 175.85 . 1 515 . 57 ARG CA C 57.38 . 1 516 . 57 ARG CB C 31.76 . 1 517 . 57 ARG CG C 27.96 . 1 518 . 57 ARG CD C 43.26 . 1 519 . 57 ARG N N 119.75 . 1 520 . 58 ALA H H 7.19 . 1 521 . 58 ALA HA H 4.42 . 1 522 . 58 ALA HB H 1.02 . 1 523 . 58 ALA C C 175.76 . 1 524 . 58 ALA CA C 50.98 . 1 525 . 58 ALA CB C 20.88 . 1 526 . 58 ALA N N 119.98 . 1 527 . 59 ILE H H 8.48 . 1 528 . 59 ILE HA H 4.43 . 1 529 . 59 ILE HB H 1.79 . 1 530 . 59 ILE HG12 H 1.48 . 2 531 . 59 ILE HG13 H 1.15 . 2 532 . 59 ILE HG2 H 0.88 . 1 533 . 59 ILE HD1 H 0.82 . 1 534 . 59 ILE C C 174.83 . 1 535 . 59 ILE CA C 57.80 . 1 536 . 59 ILE CB C 38.83 . 1 537 . 59 ILE CG1 C 27.46 . 1 538 . 59 ILE CG2 C 16.88 . 1 539 . 59 ILE CD1 C 12.30 . 1 540 . 59 ILE N N 123.74 . 1 541 . 62 ASN HA H 4.31 . 1 542 . 62 ASN HB2 H 2.79 . 2 543 . 62 ASN CA C 57.01 . 1 544 . 62 ASN CB C 38.72 . 1 545 . 63 GLN H H 8.29 . 1 546 . 63 GLN HA H 4.15 . 1 547 . 63 GLN HB2 H 2.22 . 2 548 . 63 GLN HG2 H 2.43 . 2 549 . 63 GLN C C 179.25 . 1 550 . 63 GLN CA C 59.26 . 1 551 . 63 GLN CB C 28.09 . 1 552 . 63 GLN CG C 34.43 . 1 553 . 63 GLN N N 121.49 . 1 554 . 64 VAL H H 8.10 . 1 555 . 64 VAL HA H 3.55 . 1 556 . 64 VAL HB H 2.14 . 1 557 . 64 VAL HG1 H 1.08 . 1 558 . 64 VAL HG2 H 0.74 . 1 559 . 64 VAL C C 178.49 . 1 560 . 64 VAL CA C 66.76 . 1 561 . 64 VAL CB C 31.59 . 1 562 . 64 VAL CG1 C 23.03 . 1 563 . 64 VAL CG2 C 21.95 . 1 564 . 64 VAL N N 122.49 . 1 565 . 65 LEU H H 8.50 . 1 566 . 65 LEU HA H 3.80 . 1 567 . 65 LEU HB2 H 1.80 . 2 568 . 65 LEU HB3 H 1.31 . 2 569 . 65 LEU HG H 1.68 . 1 570 . 65 LEU HD1 H 0.86 . 1 571 . 65 LEU HD2 H 0.81 . 1 572 . 65 LEU C C 179.12 . 1 573 . 65 LEU CA C 58.66 . 1 574 . 65 LEU CB C 42.14 . 1 575 . 65 LEU CG C 26.19 . 1 576 . 65 LEU CD1 C 25.54 . 1 577 . 65 LEU CD2 C 24.39 . 1 578 . 65 LEU N N 120.23 . 1 579 . 66 GLY H H 7.93 . 1 580 . 66 GLY HA2 H 3.91 . 2 581 . 66 GLY C C 176.38 . 1 582 . 66 GLY CA C 47.14 . 1 583 . 66 GLY N N 123.89 . 1 584 . 67 LYS H H 7.42 . 1 585 . 67 LYS HA H 4.10 . 1 586 . 67 LYS HB2 H 1.70 . 2 587 . 67 LYS HB3 H 2.08 . 2 588 . 67 LYS HG2 H 1.51 . 2 589 . 67 LYS HG3 H 1.80 . 2 590 . 67 LYS HD2 H 1.81 . 2 591 . 67 LYS C C 180.03 . 1 592 . 67 LYS CA C 60.07 . 1 593 . 67 LYS CB C 33.18 . 1 594 . 67 LYS CG C 25.90 . 1 595 . 67 LYS CD C 30.82 . 1 596 . 67 LYS N N 121.09 . 1 597 . 68 ILE H H 8.27 . 1 598 . 68 ILE HA H 3.44 . 1 599 . 68 ILE HB H 1.83 . 1 600 . 68 ILE HG12 H 0.54 . 2 601 . 68 ILE HG13 H 2.02 . 2 602 . 68 ILE HG2 H 0.92 . 1 603 . 68 ILE HD1 H 0.57 . 1 604 . 68 ILE C C 177.55 . 1 605 . 68 ILE CA C 66.67 . 1 606 . 68 ILE CB C 37.86 . 1 607 . 68 ILE CG1 C 30.78 . 1 608 . 68 ILE CG2 C 20.18 . 1 609 . 68 ILE CD1 C 13.94 . 1 610 . 68 ILE N N 121.04 . 1 611 . 69 GLU H H 8.78 . 1 612 . 69 GLU HA H 4.10 . 1 613 . 69 GLU HB2 H 2.38 . 2 614 . 69 GLU HG2 H 2.72 . 2 615 . 69 GLU C C 179.13 . 1 616 . 69 GLU CA C 59.77 . 1 617 . 69 GLU CB C 30.88 . 1 618 . 69 GLU CG C 36.82 . 1 619 . 69 GLU N N 121.24 . 1 620 . 70 ARG H H 7.22 . 1 621 . 70 ARG HA H 3.95 . 1 622 . 70 ARG HB2 H 1.89 . 2 623 . 70 ARG HG2 H 1.63 . 2 624 . 70 ARG HD2 H 3.22 . 2 625 . 70 ARG C C 178.07 . 1 626 . 70 ARG CA C 58.58 . 1 627 . 70 ARG CB C 30.25 . 1 628 . 70 ARG CG C 28.19 . 1 629 . 70 ARG CD C 43.35 . 1 630 . 70 ARG N N 114.95 . 1 631 . 71 ALA H H 7.61 . 1 632 . 71 ALA HA H 4.24 . 1 633 . 71 ALA HB H 1.31 . 1 634 . 71 ALA C C 179.32 . 1 635 . 71 ALA CA C 54.43 . 1 636 . 71 ALA CB C 19.49 . 1 637 . 71 ALA N N 121.32 . 1 638 . 72 ILE H H 8.19 . 1 639 . 72 ILE HA H 4.43 . 1 640 . 72 ILE HB H 1.93 . 1 641 . 72 ILE HG12 H 1.68 . 2 642 . 72 ILE HG13 H 1.25 . 2 643 . 72 ILE HG2 H 0.78 . 1 644 . 72 ILE HD1 H 0.91 . 1 645 . 72 ILE C C 175.54 . 1 646 . 72 ILE CA C 61.50 . 1 647 . 72 ILE CB C 39.15 . 1 648 . 72 ILE CG1 C 25.27 . 1 649 . 72 ILE CG2 C 16.91 . 1 650 . 72 ILE CD1 C 15.75 . 1 651 . 72 ILE N N 126.06 . 1 652 . 73 GLY H H 8.19 . 1 653 . 73 GLY HA2 H 3.76 . 2 654 . 73 GLY HA3 H 4.05 . 2 655 . 73 GLY C C 174.50 . 1 656 . 73 GLY CA C 46.69 . 1 657 . 73 GLY N N 111.67 . 1 658 . 74 LEU H H 7.09 . 1 659 . 74 LEU HA H 4.89 . 1 660 . 74 LEU HB2 H 1.21 . 2 661 . 74 LEU HB3 H 0.99 . 2 662 . 74 LEU HG H 1.40 . 1 663 . 74 LEU HD1 H 0.79 . 1 664 . 74 LEU HD2 H 0.76 . 1 665 . 74 LEU C C 174.32 . 1 666 . 74 LEU CA C 52.99 . 1 667 . 74 LEU CB C 46.86 . 1 668 . 74 LEU CG C 26.28 . 1 669 . 74 LEU CD1 C 26.31 . 1 670 . 74 LEU CD2 C 22.81 . 1 671 . 74 LEU N N 120.54 . 1 672 . 75 LYS H H 8.59 . 1 673 . 75 LYS HA H 3.93 . 1 674 . 75 LYS HB2 H 1.88 . 2 675 . 75 LYS HB3 H 1.69 . 2 676 . 75 LYS HG2 H 1.37 . 2 677 . 75 LYS HD2 H 1.59 . 2 678 . 75 LYS HE2 H 3.01 . 2 679 . 75 LYS C C 177.88 . 1 680 . 75 LYS CA C 57.08 . 1 681 . 75 LYS CB C 33.40 . 1 682 . 75 LYS CG C 26.42 . 1 683 . 75 LYS CD C 29.87 . 1 684 . 75 LYS CE C 42.22 . 1 685 . 75 LYS N N 119.23 . 1 686 . 76 LEU H H 10.02 . 1 687 . 76 LEU HA H 4.66 . 1 688 . 76 LEU HB2 H 1.82 . 2 689 . 76 LEU HB3 H 1.48 . 2 690 . 76 LEU HG H 1.79 . 1 691 . 76 LEU HD1 H 0.84 . 1 692 . 76 LEU HD2 H 0.79 . 1 693 . 76 LEU C C 174.20 . 1 694 . 76 LEU CA C 54.23 . 1 695 . 76 LEU CB C 44.49 . 1 696 . 76 LEU CG C 26.09 . 1 697 . 76 LEU CD1 C 26.75 . 1 698 . 76 LEU CD2 C 24.38 . 1 699 . 76 LEU N N 123.57 . 1 700 . 77 ARG H H 7.04 . 1 701 . 77 ARG HA H 4.66 . 1 702 . 77 ARG HB2 H 1.71 . 2 703 . 77 ARG HG2 H 1.37 . 2 704 . 77 ARG HG3 H 1.61 . 2 705 . 77 ARG HD2 H 3.08 . 2 706 . 77 ARG C C 175.91 . 1 707 . 77 ARG CA C 54.57 . 1 708 . 77 ARG CB C 33.72 . 1 709 . 77 ARG CG C 26.60 . 1 710 . 77 ARG CD C 43.72 . 1 711 . 77 ARG N N 115.57 . 1 712 . 78 GLY H H 8.51 . 1 713 . 78 GLY HA2 H 3.80 . 2 714 . 78 GLY HA3 H 4.17 . 2 715 . 78 GLY C C 174.64 . 1 716 . 78 GLY CA C 44.89 . 1 717 . 78 GLY N N 127.78 . 1 718 . 79 LYS H H 8.47 . 1 719 . 79 LYS HA H 4.15 . 1 720 . 79 LYS HB2 H 1.79 . 2 721 . 79 LYS HG2 H 1.42 . 2 722 . 79 LYS HE2 H 2.99 . 2 723 . 79 LYS C C 177.28 . 1 724 . 79 LYS CA C 57.69 . 1 725 . 79 LYS CB C 32.40 . 1 726 . 79 LYS CG C 24.38 . 1 727 . 79 LYS CD C 29.31 . 1 728 . 79 LYS CE C 42.05 . 1 729 . 79 LYS N N 120.90 . 1 730 . 80 ASP H H 8.42 . 1 731 . 80 ASP HA H 4.72 . 1 732 . 80 ASP C C 173.99 . 1 733 . 80 ASP CA C 53.82 . 1 734 . 80 ASP CB C 40.51 . 1 735 . 80 ASP N N 119.78 . 1 736 . 81 ILE H H 6.90 . 1 737 . 81 ILE HA H 3.45 . 1 738 . 81 ILE HB H 1.65 . 1 739 . 81 ILE HG12 H 1.50 . 2 740 . 81 ILE HG13 H 0.81 . 2 741 . 81 ILE HG2 H 0.87 . 1 742 . 81 ILE HD1 H 0.79 . 1 743 . 81 ILE C C 176.71 . 1 744 . 81 ILE CA C 62.74 . 1 745 . 81 ILE CB C 38.18 . 1 746 . 81 ILE CG1 C 28.93 . 1 747 . 81 ILE CG2 C 16.39 . 1 748 . 81 ILE CD1 C 14.03 . 1 749 . 81 ILE N N 118.17 . 1 750 . 82 GLY H H 9.28 . 1 751 . 82 GLY HA2 H 3.39 . 2 752 . 82 GLY HA3 H 4.32 . 2 753 . 82 GLY C C 173.35 . 1 754 . 82 GLY CA C 45.15 . 1 755 . 82 GLY N N 114.57 . 1 756 . 83 LYS H H 7.94 . 1 757 . 83 LYS HA H 4.64 . 1 758 . 83 LYS C C 173.93 . 1 759 . 83 LYS CA C 54.33 . 1 760 . 83 LYS N N 121.84 . 1 761 . 84 PRO HA H 4.80 . 1 762 . 84 PRO HB2 H 2.37 . 2 763 . 84 PRO HB3 H 2.10 . 2 764 . 84 PRO HG2 H 1.95 . 2 765 . 84 PRO HG3 H 1.86 . 2 766 . 84 PRO HD2 H 3.60 . 2 767 . 84 PRO CA C 62.92 . 1 768 . 84 PRO CB C 32.23 . 1 769 . 84 PRO CG C 27.81 . 1 770 . 84 PRO CD C 50.37 . 1 771 . 85 ILE H H 7.43 . 1 772 . 85 ILE HA H 3.94 . 1 773 . 85 ILE HB H 1.58 . 1 774 . 85 ILE HG12 H 1.31 . 2 775 . 85 ILE HG13 H 0.91 . 2 776 . 85 ILE HG2 H 0.78 . 1 777 . 85 ILE HD1 H 0.73 . 1 778 . 85 ILE C C 175.87 . 1 779 . 85 ILE CA C 61.70 . 1 780 . 85 ILE CB C 39.11 . 1 781 . 85 ILE CG1 C 27.69 . 1 782 . 85 ILE CG2 C 17.38 . 1 783 . 85 ILE CD1 C 13.87 . 1 784 . 85 ILE N N 120.40 . 1 785 . 86 GLU H H 8.38 . 1 786 . 86 GLU HA H 4.30 . 1 787 . 86 GLU HB2 H 2.02 . 2 788 . 86 GLU HB3 H 1.91 . 2 789 . 86 GLU HG2 H 2.24 . 2 790 . 86 GLU C C 176.19 . 1 791 . 86 GLU CA C 56.37 . 1 792 . 86 GLU CB C 30.54 . 1 793 . 86 GLU CG C 36.33 . 1 794 . 86 GLU N N 125.00 . 1 795 . 87 LYS H H 8.37 . 1 796 . 87 LYS HA H 4.30 . 1 797 . 87 LYS HB2 H 1.83 . 2 798 . 87 LYS HG2 H 1.44 . 2 799 . 87 LYS HD2 H 1.71 . 2 800 . 87 LYS HE2 H 2.99 . 2 801 . 87 LYS C C 176.70 . 1 802 . 87 LYS CA C 56.44 . 1 803 . 87 LYS CB C 33.28 . 1 804 . 87 LYS CG C 24.76 . 1 805 . 87 LYS CD C 29.44 . 1 806 . 87 LYS CE C 42.10 . 1 807 . 87 LYS N N 123.67 . 1 808 . 88 GLY H H 8.22 . 1 809 . 88 GLY C C 171.95 . 1 810 . 88 GLY N N 111.01 . 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Spectrometer_frequency_1H . _Mol_system_component_name hMBF1c _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 17 VAL H 17 VAL HA 6.9 . . . 2 3JHNHA 18 THR H 18 THR HA 6.1 . . . 3 3JHNHA 19 LEU H 19 LEU HA 4.9 . . . 4 3JHNHA 31 SER H 31 SER HA 2.1 . . . 5 3JHNHA 32 LYS H 32 LYS HA 9.0 . . . 6 3JHNHA 34 LEU H 34 LEU HA 9.4 . . . 7 3JHNHA 35 THR H 35 THR HA 7.8 . . . 8 3JHNHA 42 LYS H 42 LYS HA 3.1 . . . 9 3JHNHA 43 ILE H 43 ILE HA 10.6 . . . 10 3JHNHA 44 ASN H 44 ASN HA 8.0 . . . 11 3JHNHA 45 GLU H 45 GLU HA 9.7 . . . 12 3JHNHA 46 LYS H 46 LYS HA 4.0 . . . 13 3JHNHA 49 VAL H 49 VAL HA 5.6 . . . 14 3JHNHA 50 ILE H 50 ILE HA 4.4 . . . 15 3JHNHA 53 TYR H 53 TYR HA 3.6 . . . 16 3JHNHA 55 SER H 55 SER HA 8.1 . . . 17 3JHNHA 57 ARG H 57 ARG HA 8.0 . . . 18 3JHNHA 58 ALA H 58 ALA HA 7.4 . . . 19 3JHNHA 59 ILE H 59 ILE HA 9.1 . . . 20 3JHNHA 63 GLN H 63 GLN HA 5.2 . . . 21 3JHNHA 64 VAL H 64 VAL HA 5.3 . . . 22 3JHNHA 67 LYS H 67 LYS HA 4.0 . . . 23 3JHNHA 70 ARG H 70 ARG HA 2.3 . . . 24 3JHNHA 71 ALA H 71 ALA HA 6.1 . . . 25 3JHNHA 72 ILE H 72 ILE HA 10.2 . . . 26 3JHNHA 74 LEU H 74 LEU HA 10.2 . . . 27 3JHNHA 75 LYS H 75 LYS HA 3.4 . . . 28 3JHNHA 76 LEU H 76 LEU HA 9.6 . . . 29 3JHNHA 77 ARG H 77 ARG HA 9.4 . . . 30 3JHNHA 80 ASP H 80 ASP HA 9.0 . . . stop_ save_