data_5525 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of the first Zinc Binding domain of Nup475/TTP/TIS11 ; _BMRB_accession_number 5525 _BMRB_flat_file_name bmr5525.str _Entry_type original _Submission_date 2002-09-13 _Accession_date 2002-09-13 _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 Amann B. T. . 2 Guerrerio A. L. . 3 Pelo J. . . 4 Luo R. Q. . 5 Worthington M. T. . 6 Berg J. M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 198 "13C chemical shifts" 72 "coupling constants" 15 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-09-05 original author . stop_ _Original_release_date 2003-09-05 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; A Cys3His Zinc-binding Domain from Nup475/Tristetraprolin: A Novel Fold with a Disklike Structure ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22403688 _PubMed_ID 12515557 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Amann B. T. . 2 Worthington M. T. . 3 Berg J. M. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 42 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 217 _Page_last 221 _Year 2003 _Details . loop_ _Keyword 'Cys3His type zinc finger' stop_ save_ ################################## # Molecular system description # ################################## save_system_Tristetraproline _Saveframe_category molecular_system _Mol_system_name Tristetraproline _Abbreviation_common Tristetraproline _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Tristetraproline $Tristetraproline 'ZINC ION' $ZN stop_ _System_molecular_weight . _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'other bound and free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Tristetraproline _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Tristetraproline _Abbreviation_common Tristetraproline _Molecular_mass . _Mol_thiol_state 'other bound and free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 77 _Mol_residue_sequence ; GSHMTTSSRYKTELCRTYSE SGRCRYGAKCQFAHGLGELR QANRHPKYKTELCHKFKLQG RCPYGSRCHFIHNPTED ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 HIS 4 MET 5 THR 6 THR 7 SER 8 SER 9 ARG 10 TYR 11 LYS 12 THR 13 GLU 14 LEU 15 CYS 16 ARG 17 THR 18 TYR 19 SER 20 GLU 21 SER 22 GLY 23 ARG 24 CYS 25 ARG 26 TYR 27 GLY 28 ALA 29 LYS 30 CYS 31 GLN 32 PHE 33 ALA 34 HIS 35 GLY 36 LEU 37 GLY 38 GLU 39 LEU 40 ARG 41 GLN 42 ALA 43 ASN 44 ARG 45 HIS 46 PRO 47 LYS 48 TYR 49 LYS 50 THR 51 GLU 52 LEU 53 CYS 54 HIS 55 LYS 56 PHE 57 LYS 58 LEU 59 GLN 60 GLY 61 ARG 62 CYS 63 PRO 64 TYR 65 GLY 66 SER 67 ARG 68 CYS 69 HIS 70 PHE 71 ILE 72 HIS 73 ASN 74 PRO 75 THR 76 GLU 77 ASP stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value REF NP_035886 'zinc finger protein 36 [Mus musculus]' 94.81 319 98.63 98.63 3.55e-37 SWISS-PROT P22893 'Tristetraproline (TTP) (Zinc finger protein 36) (Zfp-36) (Protein TIS11A) (TIS11) (Growth factor-inducible nuclear protein NUP475) (TPA-induced sequence 11)' 94.81 319 98.63 98.63 3.55e-37 GenBank AAC37676 tristetraprolin 94.81 319 98.63 98.63 3.55e-37 GenBank AAH21391 'Zinc finger protein 36 [Mus musculus]' 94.81 319 98.63 98.63 3.55e-37 GenBank AAA40498 tristetraproline 94.81 319 98.63 98.63 3.55e-37 GenBank AAA72947 '[Mouse TIS11 primary response gene, complete cds.], gene product' 94.81 319 98.63 98.63 3.55e-37 EMBL CAA32807 'unnamed protein product [Mus musculus]' 94.81 183 98.63 98.63 3.35e-36 GenBank AAA39837 'nuclear protein' 94.81 319 98.63 98.63 3.55e-37 DBJ BAE32856 'unnamed protein product [Mus musculus]' 94.81 319 98.63 98.63 3.55e-37 DBJ BAE35432 'unnamed protein product [Mus musculus]' 94.81 262 98.63 98.63 5.67e-37 PDB 1M9O 'Nmr Structure Of The First Zinc Binding Domain Of Nup475TTPTIS11' 100.00 77 100.00 100.00 4.83e-38 DBJ BAB23739 'unnamed protein product [Mus musculus]' 94.81 307 98.63 98.63 4.49e-37 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jun 2 09:48:05 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Tristetraproline Mouse 10090 Eukaryota Metazoa Mus musculus 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 $Tristetraproline 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Tristetraproline 1.7 mM . ZnCl2 3.74 mM . Tris 50 mM [U-2H] H20 90 % . D20 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Tristetraproline 1.7 mM . ZnCl2 3.74 mM . Tris 50 mM [U-2H] D20 100 % . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 98 loop_ _Task processing stop_ _Details 'Biosym/Molecular Simulation' save_ save_CNS _Saveframe_category software _Name CNS _Version 1.0 loop_ _Task 'structure solution' refinement stop_ _Details Brunger save_ save_VNMR _Saveframe_category software _Name VNMR _Version 6.1b loop_ _Task collection stop_ _Details Varian save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITYplus _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_2D_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ save_3D_13C-separated_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _Sample_label . save_ save_3D_15N-separated_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_15N-HSQC-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC-TOCSY _Sample_label . save_ save_13C-HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-HCCH-TOCSY _Sample_label . save_ save_HSQCJ_WEX_9 _Saveframe_category NMR_applied_experiment _Experiment_name 'HSQCJ WEX' _Sample_label . 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 '2D TOCSY' _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 '3D 13C-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name 'HSQCJ WEX' _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 5.8 . pH temperature 293 . K pressure 1 . atm 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 Tristetraproline _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 5 THR CA C 61.63 . . 2 . 5 THR CB C 69.68 . . 3 . 6 THR H H 8.20 . . 4 . 6 THR HA H 4.39 . . 5 . 6 THR CA C 61.69 . . 6 . 6 THR CB C 69.70 . . 7 . 7 SER H H 8.39 . . 8 . 7 SER HA H 4.51 . . 9 . 7 SER HB2 H 4.65 . . 10 . 7 SER HB3 H 2.79 . . 11 . 7 SER CA C 58.42 . . 12 . 7 SER CB C 63.72 . . 13 . 8 SER H H 8.47 . . 14 . 8 SER HA H 4.42 . . 15 . 8 SER HB2 H 4.40 . . 16 . 8 SER HB3 H 3.89 . . 17 . 8 SER CA C 58.67 . . 18 . 8 SER CB C 63.49 . . 19 . 9 ARG H H 8.34 . . 20 . 9 ARG HA H 4.39 . . 21 . 9 ARG HB2 H 1.89 . . 22 . 9 ARG HB3 H 1.89 . . 23 . 9 ARG HG2 H 1.65 . . 24 . 9 ARG HD2 H 3.17 . . 25 . 9 ARG HE H 7.19 . . 26 . 9 ARG CA C 55.62 . . 27 . 9 ARG CB C 30.46 . . 28 . 10 TYR H H 7.90 . . 29 . 10 TYR HA H 4.40 . . 30 . 10 TYR HB2 H 2.84 . . 31 . 10 TYR HB3 H 3.02 . . 32 . 10 TYR HD1 H 7.02 . . 33 . 10 TYR HE1 H 6.73 . . 34 . 10 TYR CA C 58.80 . . 35 . 10 TYR CB C 39.13 . . 36 . 11 LYS H H 8.46 . . 37 . 11 LYS HA H 3.56 . . 38 . 11 LYS HB2 H 1.89 . . 39 . 11 LYS HB3 H 1.50 . . 40 . 11 LYS HG2 H 0.34 . . 41 . 11 LYS HG3 H 0.03 . . 42 . 11 LYS HD2 H 1.17 . . 43 . 11 LYS HD3 H 0.98 . . 44 . 11 LYS HE2 H 2.65 . . 45 . 11 LYS CA C 57.74 . . 46 . 11 LYS CB C 30.46 . . 47 . 12 THR H H 8.14 . . 48 . 12 THR HA H 4.60 . . 49 . 12 THR HB H 4.42 . . 50 . 12 THR HG2 H 1.12 . . 51 . 12 THR CA C 62.17 . . 52 . 12 THR CB C 69.99 . . 53 . 13 GLU H H 7.95 . . 54 . 13 GLU HA H 4.70 . . 55 . 13 GLU HB2 H 2.16 . . 56 . 13 GLU HB3 H 2.10 . . 57 . 13 GLU HG2 H 2.35 . . 58 . 13 GLU CA C 54.36 . . 59 . 13 GLU CB C 33.83 . . 60 . 14 LEU H H 9.05 . . 61 . 14 LEU HA H 4.40 . . 62 . 14 LEU HB2 H 1.73 . . 63 . 14 LEU HB3 H 1.73 . . 64 . 14 LEU HG H 1.41 . . 65 . 14 LEU HD1 H 0.74 . . 66 . 14 LEU HD2 H 0.76 . . 67 . 14 LEU CA C 55.43 . . 68 . 14 LEU CB C 42.99 . . 69 . 15 CYS H H 9.20 . . 70 . 15 CYS HA H 3.88 . . 71 . 15 CYS HB3 H 3.26 . . 72 . 15 CYS HB2 H 2.89 . . 73 . 15 CYS CA C 59.77 . . 74 . 15 CYS CB C 32.00 . . 75 . 16 ARG H H 8.94 . . 76 . 16 ARG HA H 4.06 . . 77 . 16 ARG HB2 H 1.68 . . 78 . 16 ARG HB3 H 1.87 . . 79 . 16 ARG HG2 H 1.59 . . 80 . 16 ARG HD2 H 3.19 . . 81 . 16 ARG HE H 7.34 . . 82 . 16 ARG CA C 59.76 . . 83 . 16 ARG CB C 29.78 . . 84 . 17 THR H H 8.26 . . 85 . 17 THR HA H 4.33 . . 86 . 17 THR HB H 4.18 . . 87 . 17 THR HG2 H 1.46 . . 88 . 17 THR CA C 65.94 . . 89 . 17 THR CB C 68.35 . . 90 . 18 TYR H H 8.86 . . 91 . 18 TYR HA H 3.80 . . 92 . 18 TYR HB3 H 2.87 . . 93 . 18 TYR HB2 H 3.08 . . 94 . 18 TYR HD1 H 6.61 . . 95 . 18 TYR HE1 H 6.60 . . 96 . 18 TYR CA C 62.37 . . 97 . 18 TYR CB C 37.78 . . 98 . 19 SER H H 8.49 . . 99 . 19 SER HA H 4.17 . . 100 . 19 SER HB2 H 4.02 . . 101 . 19 SER HB3 H 4.02 . . 102 . 19 SER CA C 62.08 . . 103 . 19 SER CB C 63.24 . . 104 . 20 GLU H H 8.02 . . 105 . 20 GLU HA H 4.23 . . 106 . 20 GLU HB2 H 2.05 . . 107 . 20 GLU HB3 H 2.11 . . 108 . 20 GLU HG2 H 2.31 . . 109 . 20 GLU HG3 H 2.49 . . 110 . 20 GLU CA C 58.22 . . 111 . 20 GLU CB C 30.74 . . 112 . 21 SER H H 8.30 . . 113 . 21 SER HA H 3.96 . . 114 . 21 SER HB2 H 3.89 . . 115 . 21 SER HB3 H 3.89 . . 116 . 21 SER CA C 58.61 . . 117 . 21 SER CB C 67.00 . . 118 . 22 GLY H H 8.25 . . 119 . 22 GLY HA3 H 3.83 . . 120 . 22 GLY HA2 H 2.87 . . 121 . 22 GLY CA C 45.31 . . 122 . 23 ARG H H 7.44 . . 123 . 23 ARG HA H 4.52 . . 124 . 23 ARG HB2 H 1.54 . . 125 . 23 ARG HB3 H 1.69 . . 126 . 23 ARG HG2 H 1.41 . . 127 . 23 ARG HD2 H 3.10 . . 128 . 23 ARG HE H 7.11 . . 129 . 23 ARG CA C 54.27 . . 130 . 23 ARG CB C 33.25 . . 131 . 24 CYS H H 8.36 . . 132 . 24 CYS HA H 4.42 . . 133 . 24 CYS HB2 H 2.93 . . 134 . 24 CYS HB3 H 2.64 . . 135 . 24 CYS CA C 59.38 . . 136 . 24 CYS CB C 32.29 . . 137 . 25 ARG H H 8.92 . . 138 . 25 ARG HA H 4.16 . . 139 . 25 ARG HB2 H 1.61 . . 140 . 25 ARG HB3 H 1.74 . . 141 . 25 ARG HG2 H 0.82 . . 142 . 25 ARG HG3 H 1.33 . . 143 . 25 ARG HD2 H 2.99 . . 144 . 25 ARG HE H 6.96 . . 145 . 25 ARG CA C 58.13 . . 146 . 25 ARG CB C 29.68 . . 147 . 26 TYR H H 8.78 . . 148 . 26 TYR HA H 4.55 . . 149 . 26 TYR HB2 H 2.98 . . 150 . 26 TYR HB3 H 3.06 . . 151 . 26 TYR HD1 H 7.39 . . 152 . 26 TYR HE1 H 6.95 . . 153 . 26 TYR CA C 59.26 . . 154 . 26 TYR CB C 37.97 . . 155 . 27 GLY H H 7.91 . . 156 . 27 GLY HA3 H 4.04 . . 157 . 27 GLY HA2 H 4.04 . . 158 . 27 GLY CA C 47.23 . . 159 . 28 ALA H H 9.10 . . 160 . 28 ALA HA H 4.28 . . 161 . 28 ALA HB H 1.53 . . 162 . 28 ALA CA C 55.88 . . 163 . 28 ALA CB C 18.79 . . 164 . 29 LYS H H 8.08 . . 165 . 29 LYS HA H 4.44 . . 166 . 29 LYS HB2 H 1.94 . . 167 . 29 LYS HB3 H 2.15 . . 168 . 29 LYS HG2 H 1.75 . . 169 . 29 LYS HG3 H 1.59 . . 170 . 29 LYS HD2 H 1.48 . . 171 . 29 LYS HE2 H 3.06 . . 172 . 29 LYS CA C 55.43 . . 173 . 29 LYS CB C 32.29 . . 174 . 30 CYS H H 7.44 . . 175 . 30 CYS HA H 3.81 . . 176 . 30 CYS HB2 H 3.06 . . 177 . 30 CYS HB3 H 2.59 . . 178 . 30 CYS CA C 61.89 . . 179 . 30 CYS CB C 31.13 . . 180 . 31 GLN H H 8.59 . . 181 . 31 GLN HA H 4.16 . . 182 . 31 GLN HB2 H 1.66 . . 183 . 31 GLN HB3 H 1.93 . . 184 . 31 GLN HG2 H 2.07 . . 185 . 31 GLN HG3 H 2.84 . . 186 . 31 GLN HE21 H 7.24 . . 187 . 31 GLN HE22 H 6.83 . . 188 . 31 GLN CA C 56.30 . . 189 . 31 GLN CB C 28.91 . . 190 . 32 PHE H H 9.27 . . 191 . 32 PHE HA H 4.90 . . 192 . 32 PHE HB2 H 3.12 . . 193 . 32 PHE HB3 H 3.24 . . 194 . 32 PHE HD1 H 7.38 . . 195 . 32 PHE HE1 H 7.32 . . 196 . 32 PHE HZ H 7.22 . . 197 . 32 PHE CA C 56.49 . . 198 . 32 PHE CB C 39.62 . . 199 . 33 ALA H H 9.22 . . 200 . 33 ALA HA H 3.94 . . 201 . 33 ALA HB H 1.18 . . 202 . 33 ALA CA C 52.34 . . 203 . 33 ALA CB C 19.37 . . 204 . 34 HIS H H 9.50 . . 205 . 34 HIS HA H 4.40 . . 206 . 34 HIS HB2 H 1.18 . . 207 . 34 HIS HB3 H 2.67 . . 208 . 34 HIS HD2 H 6.42 . . 209 . 34 HIS HE1 H 7.93 . . 210 . 34 HIS CA C 53.40 . . 211 . 34 HIS CB C 25.63 . . 212 . 35 GLY H H 7.66 . . 213 . 35 GLY HA2 H 4.43 . . 214 . 35 GLY HA3 H 3.93 . . 215 . 35 GLY CA C 43.57 . . 216 . 36 LEU H H 8.48 . . 217 . 36 LEU HA H 3.91 . . 218 . 36 LEU HB2 H 1.72 . . 219 . 36 LEU HB3 H 1.55 . . 220 . 36 LEU HG H 1.72 . . 221 . 36 LEU HD1 H 0.92 . . 222 . 36 LEU HD2 H 0.94 . . 223 . 36 LEU CA C 57.29 . . 224 . 36 LEU CB C 41.95 . . 225 . 37 GLY H H 8.68 . . 226 . 37 GLY HA2 H 3.84 . . 227 . 37 GLY HA3 H 3.89 . . 228 . 37 GLY CA C 46.37 . . 229 . 38 GLU H H 7.23 . . 230 . 38 GLU HA H 4.32 . . 231 . 38 GLU HB3 H 2.12 . . 232 . 38 GLU HB2 H 1.75 . . 233 . 38 GLU HG2 H 2.32 . . 234 . 38 GLU HG3 H 2.12 . . 235 . 38 GLU CA C 56.00 . . 236 . 38 GLU CB C 31.99 . . 237 . 39 LEU H H 7.19 . . 238 . 39 LEU HA H 4.16 . . 239 . 39 LEU HB2 H 1.74 . . 240 . 39 LEU HB3 H 1.74 . . 241 . 39 LEU HG H 1.38 . . 242 . 39 LEU HD1 H 0.75 . . 243 . 39 LEU HD2 H 0.75 . . 244 . 39 LEU CA C 55.81 . . 245 . 39 LEU CB C 42.99 . . 246 . 40 ARG H H 8.59 . . 247 . 40 ARG HA H 4.34 . . 248 . 40 ARG HB2 H 1.76 . . 249 . 40 ARG HB3 H 1.76 . . 250 . 40 ARG HG2 H 1.59 . . 251 . 40 ARG HD2 H 3.18 . . 252 . 40 ARG HE H 7.31 . . 253 . 40 ARG CA C 55.71 . . 254 . 40 ARG CB C 30.84 . . 255 . 41 GLN H H 8.38 . . 256 . 41 GLN HA H 4.28 . . 257 . 41 GLN HB2 H 2.11 . . 258 . 41 GLN HB3 H 1.96 . . 259 . 41 GLN HG2 H 2.35 . . 260 . 41 GLN CA C 55.62 . . 261 . 41 GLN CB C 29.68 . . 262 . 42 ALA H H 8.49 . . 263 . 42 ALA HA H 4.28 . . 264 . 42 ALA HB H 1.40 . . 265 . 42 ALA CA C 52.92 . . 266 . 42 ALA CB C 19.46 . . 267 . 43 ASN HA H 4.24 . . 268 . 43 ASN HB2 H 1.70 . . 269 . 43 ASN HB3 H 1.34 . . stop_ save_ save_chemical_shift_set_2 _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 Tristetraproline _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 . 8 SER HB3 H 3.94 . . 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 Tristetraproline _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 10 TYR H 10 TYR HA 4.8 . . . 2 3JHNHA 12 THR H 12 THR HA 8.9 . . . 3 3JHNHA 13 GLU H 13 GLU HA 8.9 . . . 4 3JHNHA 15 CYS H 15 CYS HA 4.7 . . . 5 3JHNHA 16 ARG H 16 ARG HA 3.7 . . . 6 3JHNHA 18 TYR H 18 TYR HA 3.3 . . . 7 3JHNHA 19 SER H 19 SER HA 4.0 . . . 8 3JHNHA 22 GLY H 22 GLY HA 4.0 . . . 9 3JHNHA 25 ARG H 25 ARG HA 5.1 . . . 10 3JHNHA 26 TYR H 26 TYR HA 9.2 . . . 11 3JHNHA 27 GLY H 27 GLY HA 3.8 . . . 12 3JHNHA 29 LYS H 29 LYS HA 10 . . . 13 3JHNHA 32 PHE H 32 PHE HA 10.8 . . . 14 3JHNHA 35 GLY H 35 GLY HA 4.6 . . . 15 3JHNHA 39 LEU H 39 LEU HA 4.8 . . . stop_ save_