data_5698 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and Side-chain 1H, and 15N Chemical Shift Assignments for TcPABC ; _BMRB_accession_number 5698 _BMRB_flat_file_name bmr5698.str _Entry_type original _Submission_date 2003-02-17 _Accession_date 2003-02-17 _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 Siddiqui Nadeem . . 2 Kozlov Guennadi . . 3 D'Orso Ivan . . 4 Trempe Jean-Francois . . 5 Gehring Kalle . . 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" 364 "15N chemical shifts" 80 "coupling constants" 74 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-09-12 original author . stop_ _Original_release_date 2003-09-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure of the C-terminal Domain from Poly(A)-binding Protein in Trypanosoma cruzi: A Vegetal PABC Domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22812265 _PubMed_ID 12930992 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Siddiqui Nadeem . . 2 Kozlov Guennadi . . 3 D'Orso Ivan . . 4 Trempe Jean-Francois . . 5 Gehring Kalle . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume 12 _Journal_issue 9 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1925 _Page_last 1933 _Year 2003 _Details . loop_ _Keyword 'Poly(A)-Binding Protein' PABC Trypanosomes stop_ save_ ################################## # Molecular system description # ################################## save_system_PABC _Saveframe_category molecular_system _Mol_system_name 'C-terminal domain of poly(A)-binding protein' _Abbreviation_common PABC _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'C-term domain of PABP' $TcPABC stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'peptide binding domain' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TcPABC _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'C-terminal domain of PABP' _Abbreviation_common PABC _Molecular_mass 9090 _Mol_thiol_state 'not present' _Details ; N-terminal helix is mobile. Last four helices fold into a right-handed supercoil which is characteristic in all PABC domains. ; ############################## # Polymer residue sequence # ############################## _Residue_count 85 _Mol_residue_sequence ; GSSLASQGQNLSTVLANLTP EQQKNVLGERLYNHIVAINP AAAAKVTGMLLEMDNGEILN LLDTPGLLDAKVQEALEVLN RHMNV ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 SER 4 LEU 5 ALA 6 SER 7 GLN 8 GLY 9 GLN 10 ASN 11 LEU 12 SER 13 THR 14 VAL 15 LEU 16 ALA 17 ASN 18 LEU 19 THR 20 PRO 21 GLU 22 GLN 23 GLN 24 LYS 25 ASN 26 VAL 27 LEU 28 GLY 29 GLU 30 ARG 31 LEU 32 TYR 33 ASN 34 HIS 35 ILE 36 VAL 37 ALA 38 ILE 39 ASN 40 PRO 41 ALA 42 ALA 43 ALA 44 ALA 45 LYS 46 VAL 47 THR 48 GLY 49 MET 50 LEU 51 LEU 52 GLU 53 MET 54 ASP 55 ASN 56 GLY 57 GLU 58 ILE 59 LEU 60 ASN 61 LEU 62 LEU 63 ASP 64 THR 65 PRO 66 GLY 67 LEU 68 LEU 69 ASP 70 ALA 71 LYS 72 VAL 73 GLN 74 GLU 75 ALA 76 LEU 77 GLU 78 VAL 79 LEU 80 ASN 81 ARG 82 HIS 83 MET 84 ASN 85 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 1NMR "Solution Structure Of C-Terminal Domain From Trypanosoma Cruzi Poly(A)-Binding Protein" 100.00 85 100.00 100.00 1.45e-51 GB AAC02537 "poly(A)-binding protein [Trypanosoma cruzi]" 97.65 550 100.00 100.00 1.34e-46 GB AAC02538 "poly(A)-binding protein [Trypanosoma cruzi]" 97.65 550 100.00 100.00 1.34e-46 GB AAC46487 "poly(A) binding protein [Trypanosoma cruzi]" 97.65 550 100.00 100.00 1.34e-46 GB AAC46489 "poly(A) binding protein [Trypanosoma cruzi]" 97.65 550 100.00 100.00 1.34e-46 GB EAN99758 "poly(A)-binding protein, putative [Trypanosoma cruzi]" 97.65 550 100.00 100.00 1.34e-46 REF XP_821609 "poly(A)-binding protein [Trypanosoma cruzi strain CL Brener]" 97.65 550 100.00 100.00 1.34e-46 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction _Plasmid _Gene_mnemonic $TcPABC 'Trypanosoma cruzi' 5693 Eukaryota . Trypanosoma cruzi cytpplasm PGEX-4T PABP1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $TcPABC 'recombinant technology' 'E. coli' Escherichia coli 'BL21 Gold' plasmid pGEX-4T ; TcPABC was expressed as an N-terminal GST tagged recombinant protein. The tag was cleaved with thrombin and overall yield was approx. 10mg/L in 1x Luria broth. ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $TcPABC 2 mM 1 2 [U-15N] 'sodium phosphate' 50 mM . . . 'sodium chloride' 100 mM . . . 'sodium azide' 1 mM . . . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.1 loop_ _Task Processing stop_ _Details . save_ save_GIFA _Saveframe_category software _Name GIFA _Version 4.31 loop_ _Task Processing stop_ _Details Delsuc. save_ save_CNS _Saveframe_category software _Name CNS _Version 1.1 loop_ _Task Refinement stop_ _Details Brunger. save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3 loop_ _Task 'data analysis' stop_ _Details Wutrich. save_ save_ARIA _Saveframe_category software _Name ARIA _Version 1.1 loop_ _Task 'structure solution' stop_ _Details Nilges. save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITYplus _Field_strength 800 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCACONH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label . save_ save_HNHA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_2D_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_3D-15N_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D-15N NOESY' _Sample_label . save_ save_IPAP-HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name IPAP-HSQC _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name IPAP-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.3 0.1 n/a temperature 303 1 K 'ionic strength' 0.20 0.02 M stop_ save_ save_Ex-cond_2 _Saveframe_category sample_conditions _Details '18mg/ml of Pf1 phage was added to sample for dipolar couplings experiment.' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.3 0.1 n/a temperature 303 1 K 'ionic strength' 0.20 0.02 M 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'C-term domain of PABP' _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 . 3 SER N N 117.7 0.25 1 2 . 3 SER H H 8.54 0.01 1 3 . 3 SER HA H 4.17 0.01 1 4 . 4 LEU N N 123.9 0.25 1 5 . 4 LEU H H 8.32 0.01 1 6 . 4 LEU HA H 4.29 0.01 1 7 . 4 LEU HB2 H 1.59 0.01 2 8 . 4 LEU HG H 0.85 0.01 1 9 . 5 ALA N N 123.9 0.25 1 10 . 5 ALA H H 8.22 0.01 1 11 . 5 ALA HA H 4.28 0.01 1 12 . 5 ALA HB H 1.35 0.01 1 13 . 6 SER N N 113.9 0.25 1 14 . 6 SER H H 8.11 0.01 1 15 . 6 SER HA H 4.28 0.01 1 16 . 6 SER HB2 H 3.83 0.01 2 17 . 7 GLN N N 121.3 0.25 1 18 . 7 GLN H H 8.28 0.01 1 19 . 7 GLN HA H 4.33 0.01 1 20 . 7 GLN HB3 H 2.11 0.01 2 21 . 7 GLN HB2 H 1.96 0.01 2 22 . 7 GLN HG2 H 2.33 0.01 2 23 . 8 GLY N N 109.0 0.25 1 24 . 8 GLY H H 8.40 0.01 1 25 . 8 GLY HA2 H 3.91 0.01 2 26 . 8 GLY HA3 H 3.81 0.01 2 27 . 9 GLN N N 119.3 0.25 1 28 . 9 GLN H H 8.14 0.01 1 29 . 9 GLN HA H 4.27 0.01 1 30 . 9 GLN HB3 H 2.02 0.01 2 31 . 9 GLN HB2 H 1.88 0.01 2 32 . 9 GLN HG2 H 2.25 0.01 2 33 . 10 ASN N N 119.5 0.25 1 34 . 10 ASN H H 8.46 0.01 1 35 . 10 ASN HA H 4.63 0.01 1 36 . 10 ASN HB2 H 2.84 0.01 2 37 . 11 LEU N N 123.4 0.25 1 38 . 11 LEU H H 8.58 0.01 1 39 . 11 LEU HA H 4.05 0.01 1 40 . 11 LEU HB2 H 1.62 0.01 2 41 . 11 LEU HG H 1.54 0.01 1 42 . 11 LEU HD1 H 0.80 0.01 2 43 . 12 SER N N 113.9 0.25 1 44 . 12 SER H H 8.45 0.01 1 45 . 12 SER HA H 4.08 0.01 1 46 . 12 SER HB2 H 3.87 0.01 2 47 . 13 THR N N 115.7 0.25 1 48 . 13 THR H H 7.71 0.01 1 49 . 13 THR HA H 4.09 0.01 1 50 . 13 THR HB H 4.21 0.01 1 51 . 13 THR HG2 H 1.19 0.01 1 52 . 14 VAL N N 121.3 0.25 1 53 . 14 VAL H H 7.65 0.01 1 54 . 14 VAL HA H 3.84 0.01 1 55 . 14 VAL HB H 2.15 0.01 1 56 . 14 VAL HG1 H 0.94 0.01 2 57 . 15 LEU N N 118.0 0.25 1 58 . 15 LEU H H 8.01 0.01 1 59 . 15 LEU HA H 4.04 0.01 1 60 . 15 LEU HB2 H 1.77 0.01 2 61 . 15 LEU HG H 1.43 0.01 1 62 . 15 LEU HD1 H 0.82 0.01 2 63 . 16 ALA N N 118.5 0.25 1 64 . 16 ALA H H 7.34 0.01 1 65 . 16 ALA HA H 4.03 0.01 1 66 . 16 ALA HB H 1.40 0.01 1 67 . 17 ASN N N 113.1 0.25 1 68 . 17 ASN H H 7.88 0.01 1 69 . 17 ASN HA H 4.71 0.01 1 70 . 17 ASN HB3 H 2.94 0.01 2 71 . 17 ASN HB2 H 2.72 0.01 2 72 . 18 LEU N N 119.8 0.25 1 73 . 18 LEU H H 7.48 0.01 1 74 . 18 LEU HA H 4.73 0.01 1 75 . 18 LEU HB2 H 1.80 0.01 2 76 . 18 LEU HG H 1.65 0.01 1 77 . 18 LEU HD1 H 0.78 0.01 2 78 . 19 THR N N 112.8 0.25 1 79 . 19 THR H H 8.54 0.01 1 80 . 19 THR HA H 4.55 0.01 1 81 . 19 THR HB H 4.71 0.01 1 82 . 19 THR HG2 H 1.33 0.01 1 83 . 21 GLU N N 116.7 0.25 1 84 . 21 GLU H H 8.67 0.01 1 85 . 21 GLU HA H 4.00 0.01 1 86 . 21 GLU HB3 H 2.02 0.01 2 87 . 21 GLU HB2 H 1.88 0.01 2 88 . 21 GLU HG2 H 2.28 0.01 2 89 . 22 GLN N N 119.5 0.25 1 90 . 22 GLN H H 7.61 0.01 1 91 . 22 GLN HA H 4.08 0.01 1 92 . 22 GLN HB2 H 1.98 0.01 2 93 . 22 GLN HG2 H 2.43 0.01 2 94 . 22 GLN HE21 H 7.45 0.01 1 95 . 22 GLN HE22 H 6.76 0.01 1 96 . 23 GLN N N 118.3 0.25 1 97 . 23 GLN H H 8.82 0.01 1 98 . 23 GLN HA H 3.75 0.01 1 99 . 23 GLN HB3 H 2.25 0.01 2 100 . 23 GLN HB2 H 1.84 0.01 2 101 . 23 GLN HG2 H 2.66 0.01 2 102 . 23 GLN HE21 H 7.06 0.01 1 103 . 24 LYS N N 115.9 0.25 1 104 . 24 LYS H H 7.65 0.01 1 105 . 24 LYS HA H 3.91 0.01 1 106 . 24 LYS HB2 H 2.07 0.01 2 107 . 24 LYS HG2 H 1.60 0.01 2 108 . 24 LYS HD2 H 1.85 0.01 2 109 . 24 LYS HE2 H 3.07 0.01 2 110 . 25 ASN N N 117.2 0.25 1 111 . 25 ASN H H 7.63 0.01 1 112 . 25 ASN HA H 4.45 0.01 1 113 . 25 ASN HB2 H 2.86 0.01 2 114 . 26 VAL N N 120.3 0.25 1 115 . 26 VAL H H 7.94 0.01 1 116 . 26 VAL HA H 3.79 0.01 1 117 . 26 VAL HB H 2.03 0.01 1 118 . 26 VAL HG1 H 0.99 0.01 2 119 . 26 VAL HG2 H 0.80 0.01 2 120 . 27 LEU N N 119.0 0.25 1 121 . 27 LEU H H 8.30 0.01 1 122 . 27 LEU HA H 3.86 0.01 1 123 . 27 LEU HB2 H 1.82 0.01 2 124 . 27 LEU HG H 1.21 0.01 1 125 . 27 LEU HD1 H 0.78 0.01 2 126 . 28 GLY N N 106.7 0.25 1 127 . 28 GLY H H 8.83 0.01 1 128 . 28 GLY HA2 H 4.01 0.01 2 129 . 28 GLY HA3 H 3.62 0.01 2 130 . 29 GLU N N 121.9 0.25 1 131 . 29 GLU H H 7.63 0.01 1 132 . 29 GLU HA H 4.07 0.01 1 133 . 29 GLU HB3 H 2.10 0.01 2 134 . 29 GLU HG3 H 2.38 0.01 2 135 . 30 ARG N N 119.5 0.25 1 136 . 30 ARG H H 7.57 0.01 1 137 . 30 ARG HA H 4.12 0.01 1 138 . 30 ARG HB3 H 1.93 0.01 2 139 . 30 ARG HB2 H 1.80 0.01 2 140 . 30 ARG HD2 H 3.14 0.01 2 141 . 31 LEU N N 119.5 0.25 1 142 . 31 LEU H H 8.72 0.01 1 143 . 31 LEU HA H 3.87 0.01 1 144 . 31 LEU HB3 H 2.05 0.01 2 145 . 31 LEU HB2 H 1.75 0.01 2 146 . 31 LEU HG H 1.45 0.01 1 147 . 31 LEU HD1 H 0.77 0.01 2 148 . 32 TYR N N 120.3 0.25 1 149 . 32 TYR H H 8.70 0.01 1 150 . 32 TYR HA H 3.84 0.01 1 151 . 32 TYR HB3 H 3.18 0.01 2 152 . 32 TYR HB2 H 2.98 0.01 2 153 . 32 TYR HD1 H 6.93 0.01 3 154 . 32 TYR HE1 H 6.64 0.01 3 155 . 33 ASN N N 114.7 0.25 1 156 . 33 ASN H H 8.11 0.01 1 157 . 33 ASN HA H 4.28 0.01 1 158 . 33 ASN HB3 H 2.92 0.01 2 159 . 33 ASN HB2 H 2.71 0.01 2 160 . 33 ASN HD21 H 7.04 0.01 2 161 . 34 HIS N N 116.7 0.25 1 162 . 34 HIS H H 7.66 0.01 1 163 . 34 HIS HA H 4.26 0.01 1 164 . 34 HIS HB3 H 3.18 0.01 2 165 . 34 HIS HB2 H 3.10 0.01 2 166 . 34 HIS HD2 H 6.69 0.01 1 167 . 34 HIS HE1 H 8.16 0.01 1 168 . 35 ILE N N 118.5 0.25 1 169 . 35 ILE H H 8.53 0.01 1 170 . 35 ILE HA H 3.51 0.01 1 171 . 35 ILE HB H 1.50 0.01 1 172 . 35 ILE HG2 H 0.78 0.01 1 173 . 36 VAL N N 121.9 0.25 1 174 . 36 VAL H H 8.87 0.01 1 175 . 36 VAL HA H 3.35 0.01 1 176 . 36 VAL HB H 1.36 0.01 1 177 . 36 VAL HG1 H 0.80 0.01 2 178 . 36 VAL HG2 H 0.73 0.01 2 179 . 37 ALA N N 118.3 0.25 1 180 . 37 ALA H H 6.39 0.01 1 181 . 37 ALA HA H 4.07 0.01 1 182 . 37 ALA HB H 1.34 0.01 1 183 . 38 ILE N N 116.2 0.25 1 184 . 38 ILE H H 7.33 0.01 1 185 . 38 ILE HA H 3.95 0.01 1 186 . 38 ILE HB H 1.76 0.01 1 187 . 38 ILE HG2 H 1.00 0.01 1 188 . 38 ILE HG12 H 1.53 0.01 2 189 . 38 ILE HD1 H 0.80 0.01 1 190 . 39 ASN N N 114.4 0.25 1 191 . 39 ASN H H 8.04 0.01 1 192 . 39 ASN HA H 4.84 0.01 1 193 . 39 ASN HB3 H 2.68 0.01 2 194 . 39 ASN HB2 H 2.50 0.01 2 195 . 39 ASN HD21 H 6.89 0.01 2 196 . 40 PRO HA H 4.23 0.01 1 197 . 40 PRO HB2 H 2.38 0.01 2 198 . 40 PRO HG3 H 2.17 0.01 2 199 . 40 PRO HG2 H 2.07 0.01 2 200 . 40 PRO HD3 H 3.84 0.01 2 201 . 40 PRO HD2 H 3.44 0.01 2 202 . 41 ALA N N 119.0 0.25 1 203 . 41 ALA H H 7.99 0.01 1 204 . 41 ALA HA H 4.20 0.01 1 205 . 41 ALA HB H 1.43 0.01 1 206 . 42 ALA N N 117.2 0.25 1 207 . 42 ALA H H 7.49 0.01 1 208 . 42 ALA HA H 4.49 0.01 1 209 . 42 ALA HB H 1.17 0.01 1 210 . 43 ALA N N 119.8 0.25 1 211 . 43 ALA H H 7.23 0.01 1 212 . 43 ALA HA H 3.73 0.01 1 213 . 43 ALA HB H 1.12 0.01 1 214 . 44 ALA N N 122.4 0.25 1 215 . 44 ALA H H 9.19 0.01 1 216 . 44 ALA HA H 4.24 0.01 1 217 . 44 ALA HB H 1.53 0.01 1 218 . 45 LYS N N 119.9 0.25 1 219 . 45 LYS H H 8.17 0.01 1 220 . 45 LYS HA H 4.10 0.01 1 221 . 45 LYS HB2 H 1.83 0.01 2 222 . 45 LYS HG2 H 1.52 0.01 2 223 . 45 LYS HE2 H 2.95 0.01 2 224 . 46 VAL N N 117.7 0.25 1 225 . 46 VAL H H 8.54 0.01 1 226 . 46 VAL HA H 3.74 0.01 1 227 . 46 VAL HB H 1.95 0.01 1 228 . 46 VAL HG1 H 0.95 0.01 2 229 . 47 THR N N 117.2 0.25 1 230 . 47 THR H H 8.21 0.01 1 231 . 47 THR HA H 3.52 0.01 1 232 . 47 THR HB H 4.32 0.01 1 233 . 47 THR HG2 H 1.28 0.01 1 234 . 48 GLY N N 104.4 0.25 1 235 . 48 GLY H H 7.70 0.01 1 236 . 48 GLY HA2 H 3.88 0.01 2 237 . 48 GLY HA3 H 3.69 0.01 2 238 . 49 MET N N 119.0 0.25 1 239 . 49 MET H H 7.49 0.01 1 240 . 49 MET HA H 4.10 0.01 1 241 . 49 MET HB2 H 2.49 0.01 2 242 . 49 MET HG2 H 2.68 0.01 2 243 . 49 MET HE H 2.19 0.01 1 244 . 50 LEU N N 120.1 0.25 1 245 . 50 LEU H H 8.13 0.01 1 246 . 50 LEU HA H 4.03 0.01 1 247 . 50 LEU HB2 H 1.82 0.01 2 248 . 50 LEU HG H 1.28 0.01 1 249 . 50 LEU HD1 H 0.70 0.01 2 250 . 51 LEU N N 116.0 0.25 1 251 . 51 LEU H H 7.97 0.01 1 252 . 51 LEU HA H 4.04 0.01 1 253 . 51 LEU HB2 H 1.81 0.01 2 254 . 51 LEU HG H 1.59 0.01 1 255 . 51 LEU HD1 H 0.82 0.01 2 256 . 52 GLU N N 115.9 0.25 1 257 . 52 GLU H H 7.09 0.01 1 258 . 52 GLU HA H 4.09 0.01 1 259 . 52 GLU HB3 H 2.17 0.01 2 260 . 52 GLU HB2 H 1.93 0.01 2 261 . 52 GLU HG2 H 2.52 0.01 2 262 . 53 MET N N 118.3 0.25 1 263 . 53 MET H H 7.61 0.01 1 264 . 53 MET HA H 4.12 0.01 1 265 . 53 MET HB2 H 2.50 0.01 2 266 . 53 MET HG2 H 2.74 0.01 2 267 . 53 MET HE H 2.15 0.01 1 268 . 54 ASP N N 116.7 0.25 1 269 . 54 ASP H H 8.28 0.01 1 270 . 54 ASP HA H 4.38 0.01 1 271 . 54 ASP HB3 H 2.71 0.01 2 272 . 54 ASP HB2 H 2.60 0.01 2 273 . 55 ASN N N 122.1 0.25 1 274 . 55 ASN H H 8.73 0.01 1 275 . 55 ASN HA H 4.14 0.01 1 276 . 55 ASN HB3 H 2.77 0.01 2 277 . 55 ASN HB2 H 2.48 0.01 2 278 . 55 ASN HD21 H 6.52 0.01 2 279 . 55 ASN HD22 H 7.32 0.01 2 280 . 56 GLY N N 106.4 0.25 1 281 . 56 GLY H H 8.66 0.01 1 282 . 56 GLY HA2 H 3.86 0.01 2 283 . 56 GLY HA3 H 3.73 0.01 2 284 . 57 GLU N N 121.4 0.25 1 285 . 57 GLU H H 7.41 0.01 1 286 . 57 GLU HA H 4.15 0.01 1 287 . 57 GLU HB3 H 2.25 0.01 2 288 . 57 GLU HB2 H 2.09 0.01 2 289 . 57 GLU HG3 H 2.39 0.01 2 290 . 58 ILE N N 120.3 0.25 1 291 . 58 ILE H H 7.99 0.01 1 292 . 58 ILE HA H 3.46 0.01 1 293 . 58 ILE HB H 1.92 0.01 1 294 . 58 ILE HG2 H 0.80 0.01 1 295 . 58 ILE HG12 H 1.23 0.01 2 296 . 59 LEU N N 119.0 0.25 1 297 . 59 LEU H H 8.27 0.01 1 298 . 59 LEU HA H 3.83 0.01 1 299 . 59 LEU HB2 H 1.72 0.01 2 300 . 59 LEU HG H 1.54 0.01 1 301 . 59 LEU HD1 H 0.80 0.01 2 302 . 59 LEU HD2 H 0.72 0.01 2 303 . 60 ASN N N 115.4 0.25 1 304 . 60 ASN H H 7.38 0.01 1 305 . 60 ASN HA H 4.41 0.01 1 306 . 60 ASN HB2 H 2.80 0.01 2 307 . 61 LEU N N 118.8 0.25 1 308 . 61 LEU H H 7.84 0.01 1 309 . 61 LEU HA H 3.93 0.01 1 310 . 61 LEU HB3 H 2.01 0.01 2 311 . 61 LEU HG H 1.26 0.01 1 312 . 61 LEU HD1 H 0.80 0.01 2 313 . 61 LEU HD2 H 0.72 0.01 2 314 . 62 LEU N N 115.7 0.25 1 315 . 62 LEU H H 7.76 0.01 1 316 . 62 LEU HA H 3.82 0.01 1 317 . 62 LEU HB3 H 1.83 0.01 2 318 . 62 LEU HB2 H 1.65 0.01 2 319 . 62 LEU HG H 1.31 0.01 1 320 . 62 LEU HD1 H 0.73 0.01 2 321 . 62 LEU HD2 H 0.59 0.01 2 322 . 63 ASP N N 116.5 0.25 1 323 . 63 ASP H H 7.79 0.01 1 324 . 63 ASP HA H 4.67 0.01 1 325 . 63 ASP HB2 H 2.66 0.01 2 326 . 64 THR N N 116.2 0.25 1 327 . 64 THR H H 7.32 0.01 1 328 . 64 THR HA H 4.64 0.01 1 329 . 64 THR HB H 4.16 0.01 1 330 . 64 THR HG2 H 1.33 0.01 1 331 . 66 GLY N N 109.3 0.25 1 332 . 66 GLY H H 8.81 0.01 1 333 . 66 GLY HA2 H 4.06 0.01 2 334 . 66 GLY HA3 H 3.86 0.01 2 335 . 67 LEU N N 122.1 0.25 1 336 . 67 LEU H H 7.62 0.01 1 337 . 67 LEU HA H 4.25 0.01 1 338 . 67 LEU HB3 H 1.72 0.01 2 339 . 67 LEU HB2 H 1.63 0.01 2 340 . 67 LEU HG H 1.21 0.01 1 341 . 67 LEU HD1 H 0.95 0.01 2 342 . 67 LEU HD2 H 0.83 0.01 2 343 . 68 LEU N N 120.3 0.25 1 344 . 68 LEU H H 7.97 0.01 1 345 . 68 LEU HA H 3.91 0.01 1 346 . 68 LEU HB3 H 1.72 0.01 2 347 . 68 LEU HB2 H 1.42 0.01 2 348 . 68 LEU HG H 1.22 0.01 1 349 . 68 LEU HD1 H 0.67 0.01 2 350 . 68 LEU HD2 H 0.44 0.01 2 351 . 69 ASP N N 117.7 0.25 1 352 . 69 ASP H H 8.54 0.01 1 353 . 69 ASP HA H 3.91 0.01 1 354 . 69 ASP HB2 H 2.61 0.01 2 355 . 70 ALA N N 120.6 0.25 1 356 . 70 ALA H H 7.41 0.01 1 357 . 70 ALA HA H 4.17 0.01 1 358 . 70 ALA HB H 1.51 0.01 1 359 . 71 LYS N N 119.3 0.25 1 360 . 71 LYS H H 8.07 0.01 1 361 . 71 LYS HA H 4.15 0.01 1 362 . 71 LYS HB3 H 1.85 0.01 2 363 . 71 LYS HG3 H 1.53 0.01 2 364 . 71 LYS HG2 H 1.43 0.01 2 365 . 72 VAL N N 120.8 0.25 1 366 . 72 VAL H H 8.77 0.01 1 367 . 72 VAL HA H 3.48 0.01 1 368 . 72 VAL HB H 2.34 0.01 1 369 . 72 VAL HG1 H 0.98 0.01 2 370 . 72 VAL HG2 H 0.91 0.01 2 371 . 73 GLN N N 117.5 0.25 1 372 . 73 GLN H H 7.86 0.01 1 373 . 73 GLN HA H 3.95 0.01 1 374 . 73 GLN HB3 H 2.16 0.01 2 375 . 73 GLN HG3 H 2.46 0.01 2 376 . 74 GLU N N 118.8 0.25 1 377 . 74 GLU H H 7.82 0.01 1 378 . 74 GLU HA H 3.98 0.01 1 379 . 74 GLU HB2 H 2.13 0.01 2 380 . 74 GLU HG2 H 2.40 0.01 2 381 . 75 ALA N N 122.1 0.25 1 382 . 75 ALA H H 8.10 0.01 1 383 . 75 ALA HA H 4.08 0.01 1 384 . 75 ALA HB H 1.55 0.01 1 385 . 76 LEU N N 117.0 0.25 1 386 . 76 LEU H H 8.45 0.01 1 387 . 76 LEU HA H 3.87 0.01 1 388 . 76 LEU HB3 H 1.89 0.01 2 389 . 76 LEU HB2 H 1.77 0.01 2 390 . 76 LEU HG H 1.37 0.01 1 391 . 76 LEU HD1 H 0.77 0.01 2 392 . 76 LEU HD2 H 0.68 0.01 2 393 . 77 GLU N N 118.8 0.25 1 394 . 77 GLU H H 7.73 0.01 1 395 . 77 GLU HA H 4.04 0.01 1 396 . 77 GLU HB3 H 2.15 0.01 2 397 . 77 GLU HB2 H 2.09 0.01 2 398 . 77 GLU HG3 H 2.40 0.01 2 399 . 78 VAL N N 119.0 0.25 1 400 . 78 VAL H H 7.58 0.01 1 401 . 78 VAL HA H 3.59 0.01 1 402 . 78 VAL HB H 2.23 0.01 1 403 . 78 VAL HG1 H 1.03 0.01 2 404 . 78 VAL HG2 H 0.87 0.01 2 405 . 79 LEU N N 119.8 0.25 1 406 . 79 LEU H H 8.12 0.01 1 407 . 79 LEU HA H 4.02 0.01 1 408 . 79 LEU HB2 H 1.77 0.01 2 409 . 79 LEU HD1 H 0.87 0.01 2 410 . 79 LEU HD2 H 0.79 0.01 2 411 . 80 ASN N N 116.0 0.25 1 412 . 80 ASN H H 8.05 0.01 1 413 . 80 ASN HA H 4.59 0.01 1 414 . 80 ASN HB3 H 2.80 0.01 2 415 . 81 ARG N N 119.0 0.25 1 416 . 81 ARG H H 7.63 0.01 1 417 . 81 ARG HA H 4.14 0.01 1 418 . 81 ARG HB3 H 1.84 0.01 2 419 . 81 ARG HB2 H 1.74 0.01 2 420 . 81 ARG HG3 H 1.59 0.01 2 421 . 81 ARG HD2 H 3.16 0.01 2 422 . 82 HIS N N 117.5 0.25 1 423 . 82 HIS H H 8.12 0.01 1 424 . 82 HIS HA H 4.59 0.01 1 425 . 82 HIS HB3 H 3.25 0.01 2 426 . 82 HIS HB2 H 3.14 0.01 2 427 . 82 HIS HD2 H 7.17 0.01 1 428 . 83 MET N N 119.3 0.25 1 429 . 83 MET H H 8.08 0.01 1 430 . 83 MET HA H 4.44 0.01 1 431 . 83 MET HB3 H 2.07 0.01 2 432 . 83 MET HB2 H 2.00 0.01 2 433 . 83 MET HG3 H 2.58 0.01 2 434 . 83 MET HG2 H 2.47 0.01 2 435 . 84 ASN N N 119.6 0.25 1 436 . 84 ASN H H 8.39 0.01 1 437 . 84 ASN HA H 4.71 0.01 1 438 . 84 ASN HB3 H 2.83 0.01 2 439 . 84 ASN HB2 H 2.71 0.01 2 440 . 85 VAL N N 123.2 0.25 1 441 . 85 VAL H H 7.59 0.01 1 442 . 85 VAL HA H 4.04 0.01 1 443 . 85 VAL HB H 2.05 0.01 1 444 . 85 VAL HG1 H 0.83 0.01 2 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constant_1 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Spectrometer_frequency_1H 500 _Mol_system_component_name 'C-term domain of PABP' _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 4 LEU H 4 LEU HA . 6.62 6.66 . 2 3JHNHA 5 ALA H 5 ALA HA . 5.71 5.77 . 3 3JHNHA 6 SER H 6 SER HA . 7.68 7.69 . 4 3JHNHA 7 GLN H 7 GLN HA . 6.7 6.7 . 5 3JHNHA 8 GLY H 8 GLY HA . 7.6 7.65 . 6 3JHNHA 9 GLN H 9 GLN HA . 7.15 7.15 . 7 3JHNHA 10 ASN H 10 ASN HA . 6.99 7.05 . 8 3JHNHA 11 LEU H 11 LEU HA . 4.98 5.05 . 9 3JHNHA 12 SER H 12 SER HA . 4.67 4.76 . 10 3JHNHA 13 THR H 13 THR HA . 6.72 6.79 . 11 3JHNHA 14 VAL H 14 VAL HA . 6.56 6.63 . 12 3JHNHA 15 LEU H 15 LEU HA . 5.04 5.16 . 13 3JHNHA 16 ALA H 16 ALA HA . 3.46 3.49 . 14 3JHNHA 17 ASN H 17 ASN HA . 8.98 9 . 15 3JHNHA 18 LEU H 18 LEU HA . 8.91 9.03 . 16 3JHNHA 19 THR H 19 THR HA . 6.05 6.07 . 17 3JHNHA 21 GLU H 21 GLU HA . 4.5 4.5 . 18 3JHNHA 22 GLN H 22 GLN HA . 6.36 6.38 . 19 3JHNHA 23 GLN H 23 GLN HA . 3.94 3.95 . 20 3JHNHA 24 LYS H 24 LYS HA . 4.64 4.85 . 21 3JHNHA 25 ASN H 25 ASN HA . 4.95 5.06 . 22 3JHNHA 26 VAL H 26 VAL HA . 4.78 5.15 . 23 3JHNHA 27 LEU H 27 LEU HA . 4.77 4.82 . 24 3JHNHA 28 GLY H 28 GLY HA . 6.54 6.86 . 25 3JHNHA 29 GLU H 29 GLU HA . 6.05 6.08 . 26 3JHNHA 30 ARG H 30 ARG HA . 5.12 5.12 . 27 3JHNHA 31 LEU H 31 LEU HA . 4.62 4.8 . 28 3JHNHA 32 TYR H 32 TYR HA . 2.7 2.75 . 29 3JHNHA 33 ASN H 33 ASN HA . 3.62 3.97 . 30 3JHNHA 34 HIS H 34 HIS HA . 6.8 6.91 . 31 3JHNHA 35 ILE H 35 ILE HA . 5.87 6 . 32 3JHNHA 37 ALA H 37 ALA HA . 5.76 5.81 . 33 3JHNHA 38 ILE H 38 ILE HA . 6.31 6.48 . 34 3JHNHA 39 ASN H 39 ASN HA . 8.35 8.49 . 35 3JHNHA 41 ALA H 41 ALA HA . 5.6 5.81 . 36 3JHNHA 42 ALA H 42 ALA HA . 8.99 9.09 . 37 3JHNHA 43 ALA H 43 ALA HA . 1.76 1.86 . 38 3JHNHA 45 LYS H 45 LYS HA . 4.95 5.14 . 39 3JHNHA 46 VAL H 46 VAL HA . 4.04 4.09 . 40 3JHNHA 47 THR H 47 THR HA . 3.74 3.85 . 41 3JHNHA 48 GLY H 48 GLY HA2 . 3.75 4.09 . 42 3JHNHA 49 MET H 49 MET HA . 5.37 5.42 . 43 3JHNHA 50 LEU H 50 LEU HA . 5.53 5.72 . 44 3JHNHA 51 LEU H 51 LEU HA . 4.39 4.47 . 45 3JHNHA 52 GLU H 52 GLU HA . 7 7.08 . 46 3JHNHA 53 MET H 53 MET HA . 6.57 6.64 . 47 3JHNHA 54 ASP H 54 ASP HA . 4.83 4.96 . 48 3JHNHA 55 ASN H 55 ASN HA . 2.03 2.06 . 49 3JHNHA 56 GLY H 56 GLY HA . 5.92 7.56 . 50 3JHNHA 57 GLU H 57 GLU HA . 6.98 7.04 . 51 3JHNHA 58 ILE H 58 ILE HA . 3.42 3.52 . 52 3JHNHA 59 LEU H 59 LEU HA . 3.62 3.71 . 53 3JHNHA 60 ASN H 60 ASN HA . 4.57 4.67 . 54 3JHNHA 62 LEU H 62 LEU HA . 2.7 2.96 . 55 3JHNHA 63 ASP H 63 ASP HA . 7.51 7.57 . 56 3JHNHA 64 THR H 64 THR HA . 8.01 8.22 . 57 3JHNHA 66 GLY H 66 GLY HA2 . 4.39 4.88 . 58 3JHNHA 67 LEU H 67 LEU HA . 3.43 3.7 . 59 3JHNHA 68 LEU H 68 LEU HA . 2.8 3.34 . 60 3JHNHA 70 ALA H 70 ALA HA . 4.67 4.72 . 61 3JHNHA 71 LYS H 71 LYS HA . 7.73 7.74 . 62 3JHNHA 72 VAL H 72 VAL HA . 4.9 4.9 . 63 3JHNHA 73 GLN H 73 GLN HA . 4.32 4.33 . 64 3JHNHA 74 GLU H 74 GLU HA . 4.11 4.73 . 65 3JHNHA 75 ALA H 75 ALA HA . 4.47 4.64 . 66 3JHNHA 76 LEU H 76 LEU HA . 4.3 4.33 . 67 3JHNHA 77 GLU H 77 GLU HA . 5.38 5.39 . 68 3JHNHA 78 VAL H 78 VAL HA . 5.61 5.62 . 69 3JHNHA 79 LEU H 79 LEU HA . 3.89 4.09 . 70 3JHNHA 80 ASN H 80 ASN HA . 6.33 6.36 . 71 3JHNHA 81 ARG H 81 ARG HA . 6.05 6.08 . 72 3JHNHA 82 HIS H 82 HIS HA . 7.96 8.05 . 73 3JHNHA 84 ASN H 84 ASN HA . 8.17 8.2 . 74 3JHNHA 85 VAL H 85 VAL HA . 9.5 9.57 . stop_ save_