data_4589 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Solution Structure of the Last Unknown Module of the Cellulosomal Scaffoldin Protein CIPC of Clostridum cellulolyticum ; _BMRB_accession_number 4589 _BMRB_flat_file_name bmr4589.str _Entry_type original _Submission_date 2000-05-05 _Accession_date 2000-09-07 _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 Mosbah A. . . 2 Belaich A. . . 3 Bornet O. . . 4 Belaich J. P. . 5 Henrissat B. . . 6 Darbon H. . . 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" 431 "15N chemical shifts" 86 "coupling constants" 77 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-03-08 original author . stop_ _Original_release_date 2001-03-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Solution Structure of the Last Unknown Module of the Cellulosomal Scaffoldin Protein CIPC of Clostridum cellulolyticum ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20534886 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mosbah A. . . 2 Belaich A. . . 3 Bornet O. . . 4 Belaich J. P. . 5 Henrissat B. . . 6 Darbon H. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 304 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 201 _Page_last 217 _Year 2000 _Details . loop_ _Keyword '3.10 helix' beta-beta-barrels stop_ save_ ################################## # Molecular system description # ################################## save_system_scaffoldin _Saveframe_category molecular_system _Mol_system_name 'scaffoldin protein' _Abbreviation_common scaffoldin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'scaffoldin protein' $scaffoldin 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_scaffoldin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'scaffoldin protein' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 94 _Mol_residue_sequence ; MQDPTINPTSISAKAGSFAD TKITLTPNGNTFNGISELQS SQYTKGTNEVTLLASYLNTL PENTTKTLTFDFGVGTKNPK LTITVLPKDIPGLE ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLN 3 ASP 4 PRO 5 THR 6 ILE 7 ASN 8 PRO 9 THR 10 SER 11 ILE 12 SER 13 ALA 14 LYS 15 ALA 16 GLY 17 SER 18 PHE 19 ALA 20 ASP 21 THR 22 LYS 23 ILE 24 THR 25 LEU 26 THR 27 PRO 28 ASN 29 GLY 30 ASN 31 THR 32 PHE 33 ASN 34 GLY 35 ILE 36 SER 37 GLU 38 LEU 39 GLN 40 SER 41 SER 42 GLN 43 TYR 44 THR 45 LYS 46 GLY 47 THR 48 ASN 49 GLU 50 VAL 51 THR 52 LEU 53 LEU 54 ALA 55 SER 56 TYR 57 LEU 58 ASN 59 THR 60 LEU 61 PRO 62 GLU 63 ASN 64 THR 65 THR 66 LYS 67 THR 68 LEU 69 THR 70 PHE 71 ASP 72 PHE 73 GLY 74 VAL 75 GLY 76 THR 77 LYS 78 ASN 79 PRO 80 LYS 81 LEU 82 THR 83 ILE 84 THR 85 VAL 86 LEU 87 PRO 88 LYS 89 ASP 90 ILE 91 PRO 92 GLY 93 LEU 94 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 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 1EHX "Nmr Solution Structure Of The Last Unknown Module Of The Cellulosomal Scaffoldin Protein Cipc Of Clostridum Cellulolyticum" 100.00 94 100.00 100.00 1.16e-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 $scaffoldin 'Clostridium cellulolyticum' 1521 Bacteria . Clostridium cellulolyticum 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 $scaffoldin . . . . . . 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 $scaffoldin 25 mM [U-15N] 'sodium acetate buffer' 20 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 2.1 loop_ _Task processing stop_ _Details . save_ save_Xeasy _Saveframe_category software _Name XEASY _Version 1.2 loop_ _Task 'data analysis' stop_ _Details . save_ save_DIANA _Saveframe_category software _Name DIANA _Version 2.8 loop_ _Task 'structure solution' stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version 1.0 loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ save_3D_15N-separated_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated_NOESY' _Sample_label $sample_1 save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $sample_1 save_ save_2D_15N_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 15N HSQC' _Sample_label $sample_1 save_ save_2D_15N_HSQC_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 15N HSQC_NOESY' _Sample_label $sample_1 save_ save_2D_15N_HSQC_TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 15N HSQC_TOCSY' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated_NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 15N HSQC_NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 15N HSQC_TOCSY' _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 pH 5.0 . n/a pressure 1 . atm temperature 300 . 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_citation_label _Correction_value_citation_label . H 1 . ppm . . . . . . $entry_citation $entry_citation . N 15 . ppm . . . . . . $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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'scaffoldin protein' _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 . 2 GLN N N 120.05 . . 2 . 2 GLN H H 8.04 . . 3 . 2 GLN HA H 4.39 . . 4 . 2 GLN HB2 H 1.59 . . 5 . 2 GLN HB3 H 1.53 . . 6 . 2 GLN HG2 H 1.65 . . 7 . 3 ASP N N 115.81 . . 8 . 3 ASP H H 7.19 . . 9 . 3 ASP HA H 4.69 . . 10 . 3 ASP HB2 H 3.76 . . 11 . 3 ASP HB3 H 3.57 . . 12 . 4 PRO HA H 4.57 . . 13 . 4 PRO HB2 H 1.93 . . 14 . 4 PRO HB3 H 1.81 . . 15 . 4 PRO HG2 H 1.58 . . 16 . 4 PRO HG3 H 0.86 . . 17 . 4 PRO HD2 H 3.98 . . 18 . 4 PRO HD3 H 3.81 . . 19 . 5 THR N N 110.17 . . 20 . 5 THR H H 8.05 . . 21 . 5 THR HA H 4.56 . . 22 . 5 THR HB H 4.22 . . 23 . 5 THR HG2 H 1.01 . . 24 . 6 ILE N N 112.11 . . 25 . 6 ILE H H 7.92 . . 26 . 6 ILE HA H 5.07 . . 27 . 6 ILE HB H 1.28 . . 28 . 6 ILE HG2 H 0.72 . . 29 . 6 ILE HD1 H 0.03 . . 30 . 7 ASN N N 117.64 . . 31 . 7 ASN H H 7.99 . . 32 . 7 ASN HA H 4.67 . . 33 . 7 ASN HB2 H 2.58 . . 34 . 7 ASN HD21 H 7.67 . . 35 . 7 ASN HD22 H 6.91 . . 36 . 8 PRO HA H 4.97 . . 37 . 8 PRO HB2 H 2.54 . . 38 . 8 PRO HB3 H 2.35 . . 39 . 8 PRO HG2 H 1.99 . . 40 . 8 PRO HG3 H 1.54 . . 41 . 8 PRO HD2 H 3.98 . . 42 . 8 PRO HD3 H 3.58 . . 43 . 9 THR N N 103.05 . . 44 . 9 THR H H 8.27 . . 45 . 9 THR HA H 4.96 . . 46 . 9 THR HB H 4.29 . . 47 . 9 THR HG2 H 1.28 . . 48 . 10 SER N N 118.11 . . 49 . 10 SER H H 7.52 . . 50 . 10 SER HA H 5.54 . . 51 . 10 SER HB2 H 3.85 . . 52 . 11 ILE N N 117.37 . . 53 . 11 ILE H H 8.63 . . 54 . 11 ILE HA H 4.85 . . 55 . 11 ILE HB H 2.15 . . 56 . 11 ILE HG2 H 0.97 . . 57 . 12 SER N N 117.14 . . 58 . 12 SER H H 8.50 . . 59 . 12 SER HA H 5.79 . . 60 . 12 SER HB2 H 3.77 . . 61 . 12 SER HB3 H 3.66 . . 62 . 13 ALA N N 122.98 . . 63 . 13 ALA H H 7.79 . . 64 . 13 ALA HA H 4.10 . . 65 . 13 ALA HB H 0.06 . . 66 . 14 LYS N N 132.72 . . 67 . 14 LYS H H 8.87 . . 68 . 14 LYS HA H 3.97 . . 69 . 14 LYS HB2 H 1.59 . . 70 . 14 LYS HB3 H 1.54 . . 71 . 14 LYS HG2 H 1.33 . . 72 . 14 LYS HD2 H 1.18 . . 73 . 14 LYS HE2 H 2.94 . . 74 . 15 ALA N N 125.49 . . 75 . 15 ALA H H 8.14 . . 76 . 15 ALA HA H 4.34 . . 77 . 15 ALA HB H 1.28 . . 78 . 16 GLY N N 111.31 . . 79 . 16 GLY H H 8.97 . . 80 . 16 GLY HA2 H 4.22 . . 81 . 16 GLY HA3 H 3.56 . . 82 . 17 SER N N 115.76 . . 83 . 17 SER H H 8.39 . . 84 . 17 SER HA H 4.72 . . 85 . 17 SER HB2 H 3.88 . . 86 . 17 SER HB3 H 3.80 . . 87 . 18 PHE N N 124.35 . . 88 . 18 PHE H H 9.62 . . 89 . 18 PHE HA H 4.16 . . 90 . 18 PHE HB2 H 2.89 . . 91 . 18 PHE HB3 H 2.71 . . 92 . 19 ALA N N 125.03 . . 93 . 19 ALA H H 8.52 . . 94 . 19 ALA HA H 4.67 . . 95 . 19 ALA HB H 1.44 . . 96 . 20 ASP N N 122.76 . . 97 . 20 ASP H H 8.61 . . 98 . 20 ASP HA H 4.90 . . 99 . 20 ASP HB2 H 2.60 . . 100 . 20 ASP HB3 H 2.35 . . 101 . 21 THR N N 123.00 . . 102 . 21 THR H H 9.05 . . 103 . 21 THR HA H 4.58 . . 104 . 21 THR HB H 3.86 . . 105 . 21 THR HG2 H 1.24 . . 106 . 22 LYS N N 131.16 . . 107 . 22 LYS H H 8.94 . . 108 . 22 LYS HA H 4.95 . . 109 . 22 LYS HB2 H 1.78 . . 110 . 22 LYS HB3 H 1.63 . . 111 . 22 LYS HG2 H 1.38 . . 112 . 22 LYS HD2 H 1.31 . . 113 . 22 LYS HE2 H 2.85 . . 114 . 23 ILE N N 128.30 . . 115 . 23 ILE H H 9.48 . . 116 . 23 ILE HA H 4.56 . . 117 . 23 ILE HB H 2.05 . . 118 . 23 ILE HG2 H 0.71 . . 119 . 23 ILE HD1 H 0.57 . . 120 . 24 THR N N 124.43 . . 121 . 24 THR H H 9.16 . . 122 . 24 THR HA H 4.38 . . 123 . 24 THR HB H 4.16 . . 124 . 24 THR HG2 H 1.29 . . 125 . 25 LEU N N 127.40 . . 126 . 25 LEU H H 8.37 . . 127 . 25 LEU HA H 4.66 . . 128 . 25 LEU HB2 H 1.33 . . 129 . 25 LEU HB3 H 1.29 . . 130 . 25 LEU HG H 1.47 . . 131 . 25 LEU HD1 H 0.38 . . 132 . 25 LEU HD2 H 0.34 . . 133 . 26 THR N N 120.65 . . 134 . 26 THR H H 8.73 . . 135 . 26 THR HA H 3.98 . . 136 . 26 THR HB H 4.23 . . 137 . 26 THR HG2 H 1.08 . . 138 . 27 PRO HA H 4.58 . . 139 . 27 PRO HB2 H 2.73 . . 140 . 27 PRO HB3 H 2.43 . . 141 . 27 PRO HG2 H 2.30 . . 142 . 27 PRO HG3 H 2.06 . . 143 . 27 PRO HD2 H 3.90 . . 144 . 27 PRO HD3 H 3.57 . . 145 . 28 ASN N N 116.44 . . 146 . 28 ASN H H 8.86 . . 147 . 28 ASN HA H 4.30 . . 148 . 28 ASN HB2 H 2.78 . . 149 . 28 ASN HB3 H 2.19 . . 150 . 29 GLY N N 102.66 . . 151 . 29 GLY H H 8.20 . . 152 . 29 GLY HA2 H 4.23 . . 153 . 29 GLY HA3 H 3.64 . . 154 . 30 ASN N N 119.28 . . 155 . 30 ASN H H 7.40 . . 156 . 30 ASN HA H 4.95 . . 157 . 30 ASN HB2 H 3.25 . . 158 . 30 ASN HB3 H 2.77 . . 159 . 31 THR N N 121.05 . . 160 . 31 THR H H 9.11 . . 161 . 31 THR HA H 4.27 . . 162 . 31 THR HB H 4.02 . . 163 . 31 THR HG2 H 1.13 . . 164 . 32 PHE N N 127.09 . . 165 . 32 PHE H H 8.88 . . 166 . 32 PHE HA H 4.03 . . 167 . 32 PHE HB2 H 2.77 . . 168 . 33 ASN N N 127.72 . . 169 . 33 ASN H H 8.92 . . 170 . 33 ASN HA H 4.49 . . 171 . 33 ASN HB2 H 2.48 . . 172 . 33 ASN HB3 H 2.25 . . 173 . 34 GLY N N 104.26 . . 174 . 34 GLY H H 5.37 . . 175 . 34 GLY HA2 H 4.01 . . 176 . 35 ILE N N 118.61 . . 177 . 35 ILE H H 6.73 . . 178 . 35 ILE HA H 4.54 . . 179 . 35 ILE HB H 0.61 . . 180 . 35 ILE HG2 H 0.45 . . 181 . 35 ILE HD1 H 0.85 . . 182 . 36 SER N N 123.77 . . 183 . 36 SER H H 8.25 . . 184 . 36 SER HA H 3.97 . . 185 . 36 SER HB2 H 3.53 . . 186 . 36 SER HB3 H 3.53 . . 187 . 37 GLU N N 117.40 . . 188 . 37 GLU H H 9.26 . . 189 . 37 GLU HA H 4.09 . . 190 . 37 GLU HB2 H 2.11 . . 191 . 37 GLU HB3 H 1.89 . . 192 . 37 GLU HG2 H 2.68 . . 193 . 38 LEU N N 116.98 . . 194 . 38 LEU H H 7.03 . . 195 . 38 LEU HA H 4.67 . . 196 . 38 LEU HB2 H 1.57 . . 197 . 38 LEU HG H 1.16 . . 198 . 38 LEU HD1 H 0.22 . . 199 . 38 LEU HD2 H 0.28 . . 200 . 39 GLN N N 119.54 . . 201 . 39 GLN H H 8.32 . . 202 . 39 GLN HA H 4.59 . . 203 . 39 GLN HB2 H 1.66 . . 204 . 39 GLN HB3 H 1.58 . . 205 . 39 GLN HG2 H 2.35 . . 206 . 40 SER N N 117.78 . . 207 . 40 SER H H 8.87 . . 208 . 40 SER HA H 3.83 . . 209 . 40 SER HB2 H 3.14 . . 210 . 40 SER HB3 H 3.14 . . 211 . 41 SER N N 111.39 . . 212 . 41 SER H H 7.33 . . 213 . 41 SER HA H 4.28 . . 214 . 41 SER HB2 H 3.99 . . 215 . 41 SER HB3 H 3.78 . . 216 . 42 GLN N N 121.05 . . 217 . 42 GLN H H 7.96 . . 218 . 42 GLN HA H 4.36 . . 219 . 42 GLN HB2 H 2.23 . . 220 . 42 GLN HB3 H 2.16 . . 221 . 43 TYR N N 114.01 . . 222 . 43 TYR H H 7.43 . . 223 . 43 TYR HA H 5.29 . . 224 . 43 TYR HB2 H 2.89 . . 225 . 43 TYR HB3 H 2.76 . . 226 . 44 THR N N 113.39 . . 227 . 44 THR H H 9.03 . . 228 . 44 THR HA H 4.28 . . 229 . 44 THR HB H 4.13 . . 230 . 44 THR HG2 H 1.14 . . 231 . 45 LYS N N 124.59 . . 232 . 45 LYS H H 8.86 . . 233 . 45 LYS HA H 4.81 . . 234 . 45 LYS HB2 H 2.09 . . 235 . 45 LYS HB3 H 1.83 . . 236 . 45 LYS HG2 H 1.58 . . 237 . 46 GLY N N 115.41 . . 238 . 46 GLY H H 8.36 . . 239 . 46 GLY HA2 H 4.62 . . 240 . 46 GLY HA3 H 3.69 . . 241 . 47 THR N N 120.93 . . 242 . 47 THR H H 8.99 . . 243 . 47 THR HA H 4.27 . . 244 . 47 THR HB H 4.09 . . 245 . 47 THR HG2 H 1.23 . . 246 . 48 ASN N N 123.70 . . 247 . 48 ASN H H 9.16 . . 248 . 48 ASN HA H 4.35 . . 249 . 48 ASN HB2 H 3.48 . . 250 . 48 ASN HB3 H 3.01 . . 251 . 49 GLU N N 115.29 . . 252 . 49 GLU H H 7.24 . . 253 . 49 GLU HA H 5.26 . . 254 . 49 GLU HB2 H 1.99 . . 255 . 49 GLU HB3 H 1.85 . . 256 . 49 GLU HG2 H 2.08 . . 257 . 50 VAL N N 119.44 . . 258 . 50 VAL H H 8.92 . . 259 . 50 VAL HA H 5.11 . . 260 . 50 VAL HB H 2.14 . . 261 . 51 THR N N 120.76 . . 262 . 51 THR H H 8.86 . . 263 . 51 THR HA H 4.91 . . 264 . 51 THR HB H 4.12 . . 265 . 51 THR HG2 H 0.90 . . 266 . 52 LEU N N 128.71 . . 267 . 52 LEU H H 9.31 . . 268 . 52 LEU HA H 4.44 . . 269 . 52 LEU HB2 H 1.87 . . 270 . 52 LEU HB3 H 1.68 . . 271 . 52 LEU HG H 1.31 . . 272 . 52 LEU HD1 H 0.63 . . 273 . 52 LEU HD2 H 0.82 . . 274 . 53 LEU N N 124.64 . . 275 . 53 LEU H H 7.54 . . 276 . 53 LEU HA H 4.43 . . 277 . 53 LEU HB2 H 1.72 . . 278 . 53 LEU HB3 H 1.55 . . 279 . 53 LEU HG H 1.49 . . 280 . 53 LEU HD1 H 0.76 . . 281 . 53 LEU HD2 H 1.10 . . 282 . 54 ALA N N 130.99 . . 283 . 54 ALA H H 10.35 . . 284 . 54 ALA HA H 3.65 . . 285 . 54 ALA HB H 1.37 . . 286 . 55 SER N N 110.91 . . 287 . 55 SER H H 8.41 . . 288 . 55 SER HA H 4.01 . . 289 . 55 SER HB2 H 4.08 . . 290 . 56 TYR N N 121.98 . . 291 . 56 TYR H H 7.26 . . 292 . 56 TYR HA H 4.65 . . 293 . 56 TYR HB2 H 3.27 . . 294 . 56 TYR HB3 H 3.15 . . 295 . 57 LEU N N 123.75 . . 296 . 57 LEU H H 8.40 . . 297 . 57 LEU HA H 3.65 . . 298 . 57 LEU HB2 H 1.47 . . 299 . 57 LEU HB3 H 1.18 . . 300 . 57 LEU HG H 1.36 . . 301 . 57 LEU HD1 H 0.67 . . 302 . 57 LEU HD2 H 0.36 . . 303 . 58 ASN N N 113.97 . . 304 . 58 ASN H H 8.79 . . 305 . 58 ASN HA H 5.26 . . 306 . 58 ASN HB2 H 2.94 . . 307 . 58 ASN HB3 H 2.80 . . 308 . 59 THR N N 111.59 . . 309 . 59 THR H H 7.82 . . 310 . 59 THR HA H 4.42 . . 311 . 59 THR HB H 4.32 . . 312 . 59 THR HG2 H 1.36 . . 313 . 60 LEU N N 124.95 . . 314 . 60 LEU H H 7.01 . . 315 . 60 LEU HA H 3.98 . . 316 . 60 LEU HB2 H 1.75 . . 317 . 60 LEU HB3 H 1.75 . . 318 . 60 LEU HG H 1.1 . . 319 . 61 PRO HA H 4.85 . . 320 . 61 PRO HB2 H 2.31 . . 321 . 61 PRO HB3 H 1.96 . . 322 . 61 PRO HG2 H 2.06 . . 323 . 61 PRO HD2 H 4.09 . . 324 . 61 PRO HD3 H 3.68 . . 325 . 62 GLU N N 118.49 . . 326 . 62 GLU H H 8.49 . . 327 . 62 GLU HA H 3.69 . . 328 . 62 GLU HB2 H 1.95 . . 329 . 62 GLU HB3 H 2.06 . . 330 . 62 GLU HG2 H 2.33 . . 331 . 62 GLU HG3 H 2.24 . . 332 . 63 ASN N N 114.19 . . 333 . 63 ASN H H 7.59 . . 334 . 63 ASN HA H 4.53 . . 335 . 63 ASN HB2 H 3.14 . . 336 . 63 ASN HB3 H 2.91 . . 337 . 64 THR N N 115.46 . . 338 . 64 THR H H 7.52 . . 339 . 64 THR HA H 4.69 . . 340 . 64 THR HB H 4.07 . . 341 . 64 THR HG2 H 1.14 . . 342 . 65 THR N N 117.54 . . 343 . 65 THR H H 8.34 . . 344 . 65 THR HA H 5.45 . . 345 . 65 THR HB H 3.96 . . 346 . 65 THR HG2 H 1.14 . . 347 . 66 LYS N N 129.05 . . 348 . 66 LYS H H 9.42 . . 349 . 66 LYS HA H 4.79 . . 350 . 66 LYS HB2 H 1.80 . . 351 . 66 LYS HB3 H 1.67 . . 352 . 66 LYS HG2 H 1.72 . . 353 . 66 LYS HD2 H 1.41 . . 354 . 66 LYS HD3 H 1.25 . . 355 . 67 THR N N 122.22 . . 356 . 67 THR H H 8.52 . . 357 . 67 THR HA H 5.34 . . 358 . 67 THR HB H 3.88 . . 359 . 67 THR HG2 H 1.13 . . 360 . 68 LEU N N 125.80 . . 361 . 68 LEU H H 9.15 . . 362 . 68 LEU HA H 4.74 . . 363 . 68 LEU HB2 H 1.78 . . 364 . 68 LEU HB3 H 1.52 . . 365 . 68 LEU HG H 1.23 . . 366 . 68 LEU HD1 H 0.83 . . 367 . 68 LEU HD2 H 0.76 . . 368 . 69 THR N N 124.95 . . 369 . 69 THR H H 11.31 . . 370 . 69 THR HA H 4.42 . . 371 . 69 THR HB H 4.18 . . 372 . 69 THR HG2 H 1.10 . . 373 . 70 PHE N N 130.94 . . 374 . 70 PHE H H 9.12 . . 375 . 70 PHE HA H 4.27 . . 376 . 70 PHE HB2 H 3.42 . . 377 . 70 PHE HB3 H 2.66 . . 378 . 71 ASP N N 124.35 . . 379 . 71 ASP H H 8.42 . . 380 . 71 ASP HA H 4.43 . . 381 . 71 ASP HB2 H 2.83 . . 382 . 71 ASP HB3 H 2.32 . . 383 . 72 PHE N N 129.08 . . 384 . 72 PHE H H 8.44 . . 385 . 72 PHE HA H 5.41 . . 386 . 72 PHE HB2 H 3.63 . . 387 . 72 PHE HB3 H 2.69 . . 388 . 73 GLY N N 109.55 . . 389 . 73 GLY H H 9.51 . . 390 . 73 GLY HA2 H 4.22 . . 391 . 73 GLY HA3 H 4.03 . . 392 . 74 VAL N N 109.33 . . 393 . 74 VAL H H 7.68 . . 394 . 74 VAL HA H 4.73 . . 395 . 74 VAL HB H 2.49 . . 396 . 75 GLY N N 113.92 . . 397 . 75 GLY H H 8.31 . . 398 . 75 GLY HA2 H 3.95 . . 399 . 75 GLY HA3 H 3.64 . . 400 . 76 THR N N 121.74 . . 401 . 76 THR H H 8.86 . . 402 . 76 THR HA H 4.75 . . 403 . 76 THR HB H 4.13 . . 404 . 76 THR HG2 H 1.33 . . 405 . 77 LYS N N 120.24 . . 406 . 77 LYS H H 7.75 . . 407 . 77 LYS HA H 4.34 . . 408 . 77 LYS HB2 H 1.90 . . 409 . 77 LYS HB3 H 1.72 . . 410 . 77 LYS HG2 H 1.50 . . 411 . 77 LYS HD2 H 1.38 . . 412 . 78 ASN N N 123.80 . . 413 . 78 ASN H H 8.07 . . 414 . 78 ASN HA H 4.84 . . 415 . 78 ASN HB2 H 3.07 . . 416 . 78 ASN HB3 H 2.74 . . 417 . 79 PRO HA H 4.54 . . 418 . 79 PRO HB2 H 2.28 . . 419 . 79 PRO HB3 H 1.90 . . 420 . 79 PRO HD2 H 3.15 . . 421 . 79 PRO HD3 H 2.92 . . 422 . 80 LYS N N 119.24 . . 423 . 80 LYS H H 7.93 . . 424 . 80 LYS HA H 5.56 . . 425 . 80 LYS HB2 H 1.68 . . 426 . 80 LYS HB3 H 1.56 . . 427 . 80 LYS HG2 H 1.50 . . 428 . 80 LYS HD2 H 1.45 . . 429 . 80 LYS HE2 H 3.00 . . 430 . 81 LEU N N 126.24 . . 431 . 81 LEU H H 9.32 . . 432 . 81 LEU HA H 4.91 . . 433 . 81 LEU HB2 H 1.77 . . 434 . 81 LEU HB3 H 1.32 . . 435 . 81 LEU HG H 0.82 . . 436 . 81 LEU HD1 H 0.69 . . 437 . 82 THR N N 123.01 . . 438 . 82 THR H H 8.28 . . 439 . 82 THR HA H 4.82 . . 440 . 82 THR HB H 4.01 . . 441 . 82 THR HG2 H 1.13 . . 442 . 83 ILE N N 129.95 . . 443 . 83 ILE H H 9.42 . . 444 . 83 ILE HA H 4.71 . . 445 . 83 ILE HB H 1.81 . . 446 . 83 ILE HD1 H 0.62 . . 447 . 84 THR N N 125.62 . . 448 . 84 THR H H 8.84 . . 449 . 84 THR HA H 4.78 . . 450 . 84 THR HB H 3.97 . . 451 . 84 THR HG2 H 1.13 . . 452 . 85 VAL N N 128.17 . . 453 . 85 VAL H H 8.81 . . 454 . 85 VAL HA H 4.74 . . 455 . 85 VAL HB H 2.34 . . 456 . 86 LEU N N 110.94 . . 457 . 86 LEU H H 7.51 . . 458 . 86 LEU HA H 4.02 . . 459 . 86 LEU HB2 H 3.07 . . 460 . 86 LEU HB3 H 3.07 . . 461 . 86 LEU HG H 2.91 . . 462 . 86 LEU HD1 H 0.82 . . 463 . 86 LEU HD2 H 0.73 . . 464 . 87 PRO HA H 4.58 . . 465 . 87 PRO HB2 H 2.33 . . 466 . 87 PRO HB3 H 1.89 . . 467 . 87 PRO HG2 H 2.06 . . 468 . 87 PRO HG3 H 1.96 . . 469 . 87 PRO HD2 H 3.96 . . 470 . 87 PRO HD3 H 3.78 . . 471 . 88 LYS N N 121.33 . . 472 . 88 LYS H H 8.65 . . 473 . 88 LYS HA H 4.08 . . 474 . 88 LYS HB2 H 1.78 . . 475 . 88 LYS HB3 H 1.74 . . 476 . 88 LYS HG2 H 1.65 . . 477 . 88 LYS HG3 H 1.52 . . 478 . 88 LYS HD2 H 1.47 . . 479 . 88 LYS HE2 H 2.93 . . 480 . 88 LYS HE3 H 3.62 . . 481 . 89 ASP N N 121.35 . . 482 . 89 ASP H H 8.35 . . 483 . 89 ASP HA H 4.57 . . 484 . 89 ASP HB2 H 2.58 . . 485 . 89 ASP HB3 H 2.44 . . 486 . 90 ILE N N 123.91 . . 487 . 90 ILE H H 8.19 . . 488 . 90 ILE HA H 3.98 . . 489 . 90 ILE HB H 1.82 . . 490 . 90 ILE HG12 H 1.50 . . 491 . 90 ILE HG2 H 1.15 . . 492 . 90 ILE HD1 H 0.91 . . 493 . 91 PRO HA H 4.38 . . 494 . 91 PRO HB2 H 2.28 . . 495 . 91 PRO HB3 H 1.91 . . 496 . 91 PRO HG2 H 2.04 . . 497 . 91 PRO HG3 H 1.97 . . 498 . 91 PRO HD2 H 3.10 . . 499 . 91 PRO HD3 H 3.84 . . 500 . 92 GLY N N 110.43 . . 501 . 92 GLY H H 8.49 . . 502 . 92 GLY HA2 H 4.75 . . 503 . 92 GLY HA3 H 3.93 . . 504 . 93 LEU N N 122.66 . . 505 . 93 LEU H H 7.98 . . 506 . 93 LEU HA H 4.25 . . 507 . 93 LEU HB2 H 1.55 . . 508 . 93 LEU HB3 H 1.55 . . 509 . 93 LEU HG H 0.87 . . 510 . 93 LEU HD1 H 0.81 . . 511 . 94 GLU N N 122.31 . . 512 . 94 GLU H H 8.47 . . 513 . 94 GLU HA H 4.14 . . 514 . 94 GLU HB2 H 1.85 . . 515 . 94 GLU HB3 H 1.85 . . 516 . 94 GLU HG2 H 2.19 . . 517 . 94 GLU HG3 H 2.10 . . stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 500 _Mol_system_component_name 'scaffoldin protein' _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 2 GLN H 2 GLN HA 8.00 . . . 2 3JHNHA 3 ASP H 3 ASP HA 7.98 . . . 3 3JHNHA 5 THR H 5 THR HA 8.98 . . . 4 3JHNHA 6 ILE H 6 ILE HA 9.14 . . . 5 3JHNHA 7 ASN H 7 ASN HA 5.25 . . . 6 3JHNHA 9 THR H 9 THR HA 8.19 . . . 7 3JHNHA 10 SER H 10 SER HA 8.04 . . . 8 3JHNHA 11 ILE H 11 ILE HA 9.16 . . . 9 3JHNHA 12 SER H 12 SER HA 9.05 . . . 10 3JHNHA 13 ALA H 13 ALA HA 7.93 . . . 11 3JHNHA 14 LYS H 14 LYS HA 5.25 . . . 12 3JHNHA 15 ALA H 15 ALA HA 5.80 . . . 13 3JHNHA 17 SER H 17 SER HA 9.93 . . . 14 3JHNHA 18 PHE H 18 PHE HA 5.24 . . . 15 3JHNHA 19 ALA H 19 ALA HA 9.20 . . . 16 3JHNHA 20 ASP H 20 ASP HA 4.74 . . . 17 3JHNHA 21 THR H 21 THR HA 10.13 . . . 18 3JHNHA 22 LYS H 22 LYS HA 8.47 . . . 19 3JHNHA 23 ILE H 23 ILE HA 8.40 . . . 20 3JHNHA 24 THR H 24 THR HA 11.17 . . . 21 3JHNHA 25 LEU H 25 LEU HA 9.90 . . . 22 3JHNHA 26 THR H 26 THR HA 9.85 . . . 23 3JHNHA 28 ASN H 28 ASN HA 6.45 . . . 24 3JHNHA 30 ASN H 30 ASN HA 9.66 . . . 25 3JHNHA 31 THR H 31 THR HA 9.23 . . . 26 3JHNHA 32 PHE H 32 PHE HA 11 . . . 27 3JHNHA 33 ASN H 33 ASN HA 10.33 . . . 28 3JHNHA 35 ILE H 35 ILE HA 8.64 . . . 29 3JHNHA 36 SER H 36 SER HA 6.74 . . . 30 3JHNHA 37 GLU H 37 GLU HA 4.65 . . . 31 3JHNHA 38 LEU H 38 LEU HA 8.83 . . . 32 3JHNHA 39 GLN H 39 GLN HA 4.97 . . . 33 3JHNHA 40 SER H 40 SER HA 6.7 . . . 34 3JHNHA 41 SER H 41 SER HA 4.97 . . . 35 3JHNHA 42 GLN H 42 GLN HA 4.24 . . . 36 3JHNHA 43 TYR H 43 TYR HA 5.83 . . . 37 3JHNHA 44 THR H 44 THR HA 9.70 . . . 38 3JHNHA 45 LYS H 45 LYS HA 7.50 . . . 39 3JHNHA 47 THR H 47 THR HA 6.95 . . . 40 3JHNHA 48 ASN H 48 ASN HA 7.71 . . . 41 3JHNHA 49 GLU H 49 GLU HA 7.24 . . . 42 3JHNHA 50 VAL H 50 VAL HA 8.20 . . . 43 3JHNHA 51 THR H 51 THR HA 8.91 . . . 44 3JHNHA 52 LEU H 52 LEU HA 7.63 . . . 45 3JHNHA 53 LEU H 53 LEU HA 10.71 . . . 46 3JHNHA 54 ALA H 54 ALA HA 7.69 . . . 47 3JHNHA 56 TYR H 56 TYR HA 7.95 . . . 48 3JHNHA 57 LEU H 57 LEU HA 4.07 . . . 49 3JHNHA 58 ASN H 58 ASN HA 6.43 . . . 50 3JHNHA 59 THR H 59 THR HA 9.18 . . . 51 3JHNHA 60 LEU H 60 LEU HA 5.52 . . . 52 3JHNHA 62 GLU H 62 GLU HA 4.39 . . . 53 3JHNHA 63 ASN H 63 ASN HA 5.39 . . . 54 3JHNHA 64 THR H 64 THR HA 8.31 . . . 55 3JHNHA 65 THR H 65 THR HA 8.77 . . . 56 3JHNHA 66 LYS H 66 LYS HA 5.79 . . . 57 3JHNHA 67 THR H 67 THR HA 9.00 . . . 58 3JHNHA 68 LEU H 68 LEU HA 8.27 . . . 59 3JHNHA 69 THR H 69 THR HA 11.11 . . . 60 3JHNHA 70 PHE H 70 PHE HA 9.04 . . . 61 3JHNHA 71 ASP H 71 ASP HA 8.00 . . . 62 3JHNHA 72 PHE H 72 PHE HA 12.00 . . . 63 3JHNHA 74 VAL H 74 VAL HA 10.00 . . . 64 3JHNHA 76 THR H 76 THR HA 5.39 . . . 65 3JHNHA 77 LYS H 77 LYS HA 8.14 . . . 66 3JHNHA 78 ASN H 78 ASN HA 3.86 . . . 67 3JHNHA 80 LYS H 80 LYS HA 9.98 . . . 68 3JHNHA 81 LEU H 81 LEU HA 9.91 . . . 69 3JHNHA 82 THR H 82 THR HA 9.20 . . . 70 3JHNHA 83 ILE H 83 ILE HA 9.61 . . . 71 3JHNHA 84 THR H 84 THR HA 9.32 . . . 72 3JHNHA 85 VAL H 85 VAL HA 8.98 . . . 73 3JHNHA 86 LEU H 86 LEU HA 7.12 . . . 74 3JHNHA 89 ASP H 89 ASP HA 7.57 . . . 75 3JHNHA 90 ILE H 90 ILE HA 7.62 . . . 76 3JHNHA 93 LEU H 93 LEU HA 6.63 . . . 77 3JHNHA 94 GLU H 94 GLU HA 5.72 . . . stop_ save_