data_16409 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N, and 13C assignments for beta phosphoglucomutase in a ternary complex with alpha-galactose 1-phosphate and MgF3- ; _BMRB_accession_number 16409 _BMRB_flat_file_name bmr16409.str _Entry_type original _Submission_date 2009-07-16 _Accession_date 2009-07-16 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Also included is the assignment of the three 19F resonances present in the ternary complex of beta phosphoglucomutase alpha-galactose 1-phosphate and MgF3-' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Baxter Nicola J. . 2 Waltho Jonathan P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 210 "13C chemical shifts" 415 "15N chemical shifts" 210 "19F chemical shifts" 3 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-11-16 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 7234 'Backbone 1H, 15N, and 13C assignments for beta phosphoglucomutase in a ternary complex with glucose-6-phosphate and MgF3-' stop_ _Original_release_date 2009-11-16 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'MgF(3)(-) and alpha-Galactose 1-Phosphate in the Active Site of beta-Phosphoglucomutase Form a Transition State Analogue of Phosphoryl Transfer.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19852484 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Baxter Nicola J. . 2 Hounslow Andrea M. . 3 Bowler Matthew W. . 4 Williams Nicholas H. . 5 Blackburn 'G. Michael' . . 6 Waltho Jonathan P. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full 'Journal of the American Chemical Society' _Journal_volume 131 _Journal_issue 45 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 16334 _Page_last 16335 _Year 2009 _Details . loop_ _Keyword 'active site' 'transition state analogue' trifluoromagnesate stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name beta-phosphoglucoutase _Enzyme_commission_number 5.4.2.6 loop_ _Mol_system_component_name _Mol_label 'beta phosphoglucomutase' $beta_phosphoglucomutase 'alpha-galactose 1-phosphate' $GL1 MgF3- $MGF Mg $MG stop_ _System_molecular_weight 25000 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function inhibitor 'transition state analogue' stop_ _Database_query_date . _Details ; A single catalytic magnesium ion is present in the protein. This is a ternary complex composed of beta phosphoglucomutase, alpha-galactose 1-phosphate and MgF3- forming a closed protein conformation and a transition state analogue. ; save_ ######################## # Monomeric polymers # ######################## save_beta_phosphoglucomutase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common beta_phosphoglucomutase _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'mutase reaction interconverting beta-glucose 1-phosphate and beta-glucose 6-phosphate' stop_ _Details ; A single catalytic magnesium ion is present in the protein. This is a ternary complex composed of beta phosphoglucomutase, alpha-galactose 1-phosphate and MgF3- forming a closed protein conformation and a transition state analogue. ; ############################## # Polymer residue sequence # ############################## _Residue_count 221 _Mol_residue_sequence ; MFKAVLFDLDGVITDTAEYH FRAWKALAEEIGINGVDRQF NEQLKGVSREDSLQKILDLA DKKVSAEEFKELAKRKNDNY VKMIQDVSPADVYPGILQLL KDLRSNKIKIALASASKNGP FLLERMNLTGYFDAIADPAE VAASKPAPDIFIAAAHAVGV APSESIGLEDSQAGIQAIKD SGALPIGVGRPEDLGDDIVI VPDTSHYTLEFLKEVWLQKQ K ; loop_ _Residue_seq_code _Residue_label 1 MET 2 PHE 3 LYS 4 ALA 5 VAL 6 LEU 7 PHE 8 ASP 9 LEU 10 ASP 11 GLY 12 VAL 13 ILE 14 THR 15 ASP 16 THR 17 ALA 18 GLU 19 TYR 20 HIS 21 PHE 22 ARG 23 ALA 24 TRP 25 LYS 26 ALA 27 LEU 28 ALA 29 GLU 30 GLU 31 ILE 32 GLY 33 ILE 34 ASN 35 GLY 36 VAL 37 ASP 38 ARG 39 GLN 40 PHE 41 ASN 42 GLU 43 GLN 44 LEU 45 LYS 46 GLY 47 VAL 48 SER 49 ARG 50 GLU 51 ASP 52 SER 53 LEU 54 GLN 55 LYS 56 ILE 57 LEU 58 ASP 59 LEU 60 ALA 61 ASP 62 LYS 63 LYS 64 VAL 65 SER 66 ALA 67 GLU 68 GLU 69 PHE 70 LYS 71 GLU 72 LEU 73 ALA 74 LYS 75 ARG 76 LYS 77 ASN 78 ASP 79 ASN 80 TYR 81 VAL 82 LYS 83 MET 84 ILE 85 GLN 86 ASP 87 VAL 88 SER 89 PRO 90 ALA 91 ASP 92 VAL 93 TYR 94 PRO 95 GLY 96 ILE 97 LEU 98 GLN 99 LEU 100 LEU 101 LYS 102 ASP 103 LEU 104 ARG 105 SER 106 ASN 107 LYS 108 ILE 109 LYS 110 ILE 111 ALA 112 LEU 113 ALA 114 SER 115 ALA 116 SER 117 LYS 118 ASN 119 GLY 120 PRO 121 PHE 122 LEU 123 LEU 124 GLU 125 ARG 126 MET 127 ASN 128 LEU 129 THR 130 GLY 131 TYR 132 PHE 133 ASP 134 ALA 135 ILE 136 ALA 137 ASP 138 PRO 139 ALA 140 GLU 141 VAL 142 ALA 143 ALA 144 SER 145 LYS 146 PRO 147 ALA 148 PRO 149 ASP 150 ILE 151 PHE 152 ILE 153 ALA 154 ALA 155 ALA 156 HIS 157 ALA 158 VAL 159 GLY 160 VAL 161 ALA 162 PRO 163 SER 164 GLU 165 SER 166 ILE 167 GLY 168 LEU 169 GLU 170 ASP 171 SER 172 GLN 173 ALA 174 GLY 175 ILE 176 GLN 177 ALA 178 ILE 179 LYS 180 ASP 181 SER 182 GLY 183 ALA 184 LEU 185 PRO 186 ILE 187 GLY 188 VAL 189 GLY 190 ARG 191 PRO 192 GLU 193 ASP 194 LEU 195 GLY 196 ASP 197 ASP 198 ILE 199 VAL 200 ILE 201 VAL 202 PRO 203 ASP 204 THR 205 SER 206 HIS 207 TYR 208 THR 209 LEU 210 GLU 211 PHE 212 LEU 213 LYS 214 GLU 215 VAL 216 TRP 217 LEU 218 GLN 219 LYS 220 GLN 221 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-12 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 BMRB 15467 beta_phosphoglucomutase 100.00 221 100.00 100.00 3.64e-156 BMRB 17851 beta_phosphoglucomutase 100.00 221 100.00 100.00 3.64e-156 BMRB 17852 beta_phosphoglucomutase 100.00 221 100.00 100.00 3.64e-156 PDB 1LVH "The Structure Of Phosphorylated Beta-phosphoglucomutase From Lactoccocus Lactis To 2.3 Angstrom Resolution" 100.00 221 99.55 99.55 3.10e-155 PDB 1O03 "Structure Of Pentavalent Phosphorous Intermediate Of An Enzyme Catalyzed Phosphoryl Transfer Reaction Observed On Cocrystalliza" 100.00 221 100.00 100.00 3.64e-156 PDB 1O08 "Structure Of Pentavalent Phosphorous Intermediate Of An Enzyme Catalyzed Phosphoryl Transfer Reaction Observed On Cocrystalliza" 100.00 221 100.00 100.00 3.64e-156 PDB 1Z4N "Structure Of Beta-phosphoglucomutase With Inhibitor Bound Alpha-galactose 1-phosphate Cocrystallized With Fluoride" 100.00 221 100.00 100.00 3.64e-156 PDB 1Z4O "Structure Of Beta-Phosphoglucomutase With Inhibitor Bound Alpha-Galactose 1-Phosphate" 100.00 221 100.00 100.00 3.64e-156 PDB 1ZOL "Native Beta-Pgm" 100.00 221 100.00 100.00 3.64e-156 PDB 2WF5 "Structure Of Beta-Phosphoglucomutase Inhibited With Glucose- 6-Phospahte And Trifluoromagnesate" 100.00 221 100.00 100.00 3.64e-156 PDB 2WF6 "Structure Of Beta-Phosphoglucomutase Inhibited With Glucose- 6-Phospahte And Aluminium Tetrafluoride" 100.00 221 100.00 100.00 3.64e-156 PDB 2WF7 "Structure Of Beta-phosphoglucomutase Inhibited With Glucose- 6-phosphonate And Aluminium Tetrafluoride" 100.00 221 100.00 100.00 3.64e-156 PDB 2WF8 "Structure Of Beta-Phosphoglucomutase Inhibited With Glucose- 6-Phosphate, Glucose-1-Phosphate And Beryllium Trifluoride" 100.00 221 100.00 100.00 3.64e-156 PDB 2WF9 "Structure Of Beta-Phosphoglucomutase Inhibited With Glucose- 6-Phosphate, And Beryllium Trifluoride, Crystal Form 2" 100.00 221 100.00 100.00 3.64e-156 PDB 2WFA "Structure Of Beta-Phosphoglucomutase Inhibited With Beryllium Trifluoride, In An Open Conformation." 100.00 221 100.00 100.00 3.64e-156 PDB 2WHE "Structure Of Native Beta-Phosphoglucomutase In An Open Conformation Without Bound Ligands." 100.00 221 100.00 100.00 3.64e-156 PDB 3FM9 "Analysis Of The Structural Determinants Underlying Discrimination Between Substrate And Solvent In Beta- Phosphoglucomutase Cat" 100.00 221 99.55 99.55 7.13e-155 PDB 3ZI4 "The Structure Of Beta-phosphoglucomutase Inhibited With Glucose-6-phospahte And Scandium Tetrafluoride" 100.00 221 100.00 100.00 3.64e-156 PDB 4C4R "Structure Of Beta-phosphoglucomutase In Complex With A Phosphonate Analogue Of Beta-glucose-1-phosphate And Magnesium Trifluori" 100.00 221 100.00 100.00 3.64e-156 PDB 4C4S "Structure Of Beta-phosphoglucomutase In Complex With An Alpha-fluorophosphonate Analogue Of Beta-glucose-1-phosphate And Magnes" 100.00 221 100.00 100.00 3.64e-156 PDB 4C4T "Structure Of Beta-phosphoglucomutase In Complex With A Phosphonate Analogue Of Beta-glucose-1-phosphate And Aluminium Tetrafluo" 100.00 221 100.00 100.00 3.64e-156 DBJ BAL50396 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis IO-1]" 100.00 221 100.00 100.00 3.64e-156 DBJ GAM81375 "predicted phosphatase/phosphohexomutase [Lactococcus lactis subsp. lactis]" 100.00 221 100.00 100.00 3.64e-156 EMBL CAA94734 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 100.00 100.00 3.64e-156 EMBL CDG03643 "Beta-phosphoglucomutase [Lactococcus lactis subsp. lactis A12]" 100.00 221 99.55 99.55 4.86e-155 EMBL CDI46177 "Beta-phosphoglucomutase [Lactococcus lactis subsp. lactis Dephy 1]" 100.00 221 100.00 100.00 3.64e-156 GB AAK04527 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis Il1403]" 100.00 221 99.10 100.00 1.71e-154 GB ADA64250 "Beta-phosphoglucomutase [Lactococcus lactis subsp. lactis KF147]" 100.00 221 100.00 100.00 3.64e-156 GB ADZ63078 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis CV56]" 100.00 221 99.55 100.00 4.26e-155 GB AEE43918 "beta-phosphoglucomutase [synthetic construct]" 100.00 221 99.10 100.00 1.71e-154 GB AGY43735 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis KLDS 4.0325]" 100.00 221 98.64 100.00 3.76e-154 REF NP_266585 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis Il1403]" 100.00 221 99.10 100.00 1.71e-154 REF WP_003131530 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 99.55 100.00 4.26e-155 REF WP_010905331 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 99.10 100.00 1.71e-154 REF WP_012897250 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 100.00 100.00 3.64e-156 REF WP_021469610 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 99.55 99.55 5.98e-155 SP P71447 "RecName: Full=Beta-phosphoglucomutase; Short=Beta-PGM" 100.00 221 99.10 100.00 1.71e-154 stop_ save_ ############# # Ligands # ############# save_GL1 _Saveframe_category ligand _Mol_type non-polymer _Name_common "GL1 (1-O-phosphono-alpha-D-galactopyranose)" _BMRB_code . _PDB_code GL1 _Molecular_mass 260.136 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Nov 1 15:45:01 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? O1 O1 O . 0 . ? O2 O2 O . 0 . ? O3 O3 O . 0 . ? O4 O4 O . 0 . ? O5 O5 O . 0 . ? O6 O6 O . 0 . ? P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? H4 H4 H . 0 . ? H5 H5 H . 0 . ? H61 H61 H . 0 . ? H62 H62 H . 0 . ? HO2 HO2 H . 0 . ? HO3 HO3 H . 0 . ? HO4 HO4 H . 0 . ? HO6 HO6 H . 0 . ? H1P H1P H . 0 . ? H2P H2P H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C1 C2 ? ? SING C1 O1 ? ? SING C1 O5 ? ? SING C1 H1 ? ? SING C2 C3 ? ? SING C2 O2 ? ? SING C2 H2 ? ? SING C3 C4 ? ? SING C3 O3 ? ? SING C3 H3 ? ? SING C4 C5 ? ? SING C4 O4 ? ? SING C4 H4 ? ? SING C5 C6 ? ? SING C5 O5 ? ? SING C5 H5 ? ? SING C6 O6 ? ? SING C6 H61 ? ? SING C6 H62 ? ? SING O1 P ? ? SING O2 HO2 ? ? SING O3 HO3 ? ? SING O4 HO4 ? ? SING O6 HO6 ? ? SING P O1P ? ? SING P O2P ? ? DOUB P O3P ? ? SING O1P H1P ? ? SING O2P H2P ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_MGF _Saveframe_category ligand _Mol_type non-polymer _Name_common "MGF (TRIFLUOROMAGNESATE)" _BMRB_code . _PDB_code MGF _Molecular_mass 81.300 _Mol_charge -1 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Nov 1 15:46:44 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons F1 F1 F . 0 . ? MG MG MG . -1 . ? F2 F2 F . 0 . ? F3 F3 F . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING F1 MG ? ? SING MG F2 ? ? SING MG F3 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_MG _Saveframe_category ligand _Mol_type non-polymer _Name_common "MG (MAGNESIUM ION)" _BMRB_code . _PDB_code MG _Molecular_mass 24.305 _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 Tue Nov 1 15:48:00 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons MG MG MG . 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 $beta_phosphoglucomutase 'Lactococcus lactis' 1358 Bacteria . Lactococcus lactis 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 $beta_phosphoglucomutase 'recombinant technology' . Escherichia coli BL21(DE3) pET-22b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; beta phosphoglucomutase closed conformation with alpha-galactose 1-phosphate and MgF3- forming a transition state analogue ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $beta_phosphoglucomutase 1 mM '[U-100% 13C; U-100% 15N; U-80% 2H]' $GL1 50 mM 'natural abundance' $MG 5 mM 'natural abundance' $MGF 10 mM 'natural abundance' 'sodium azide' 1 mM 'natural abundance' 'protease inhibitor' 1 times 'natural abundance' 'potassium HEPES' 50 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details ; beta phosphoglucomutase closed conformation with alpha-galactose 1-phosphate and MgF3- forming a transition state analogue ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $beta_phosphoglucomutase 0.5 mM 'natural abundance' $GL1 50 mM 'natural abundance' $MG 5 mM 'natural abundance' $MGF 10 mM 'natural abundance' 'sodium azide' 1 mM 'natural abundance' 'protease inhibitor' 1 times 'natural abundance' 'potassium HEPES' 50 mM 'natural abundance' H2O 100 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_Felix _Saveframe_category software _Name FELIX _Version . loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'Used for acquisition of 3D datasets for backbone assignment' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details 'Equipped with dual 1H/19F probe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-15N_TROSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $sample_1 save_ save_3D_TROSY_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCO' _Sample_label $sample_1 save_ save_3D_TROSY_HN(COCA)CB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(COCA)CB' _Sample_label $sample_1 save_ save_19F_1D_5 _Saveframe_category NMR_applied_experiment _Experiment_name '19F 1D' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.2 pH pressure 1 1 atm temperature 298 0.1 K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.2 pH pressure 1 1 atm temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details 19F 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 na indirect . . . 0.251449530 $citation_1 $citation_1 trichlorofluoromethane F 19 'methyl fluorine' ppm 0.0 na indirect . . . 0.94094008 $citation_1 $citation_1 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 $citation_1 $citation_1 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 $citation_1 $citation_1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $Felix stop_ loop_ _Experiment_label '2D 1H-15N TROSY' '3D TROSY HNCO' '3D TROSY HN(COCA)CB' '19F 1D' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'beta phosphoglucomutase' _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 2 PHE H H 5.258 0.005 1 2 2 2 PHE C C 173.947 0.050 1 3 2 2 PHE CB C 36.155 0.050 1 4 2 2 PHE N N 117.353 0.050 1 5 3 3 LYS H H 8.749 0.005 1 6 3 3 LYS C C 176.630 0.050 1 7 3 3 LYS CB C 35.692 0.050 1 8 3 3 LYS N N 116.413 0.050 1 9 4 4 ALA H H 7.657 0.005 1 10 4 4 ALA C C 175.305 0.050 1 11 4 4 ALA CB C 22.614 0.050 1 12 4 4 ALA N N 121.273 0.050 1 13 5 5 VAL H H 8.690 0.005 1 14 5 5 VAL C C 172.785 0.050 1 15 5 5 VAL CB C 32.822 0.050 1 16 5 5 VAL N N 120.181 0.050 1 17 6 6 LEU H H 9.299 0.005 1 18 6 6 LEU C C 175.546 0.050 1 19 6 6 LEU CB C 40.497 0.050 1 20 6 6 LEU N N 126.330 0.050 1 21 7 7 PHE H H 9.546 0.005 1 22 7 7 PHE C C 177.572 0.050 1 23 7 7 PHE CB C 40.614 0.050 1 24 7 7 PHE N N 122.988 0.050 1 25 8 8 ASP H H 7.406 0.005 1 26 8 8 ASP C C 172.835 0.050 1 27 8 8 ASP CB C 43.839 0.050 1 28 8 8 ASP N N 123.222 0.050 1 29 9 9 LEU H H 7.577 0.005 1 30 9 9 LEU C C 179.285 0.050 1 31 9 9 LEU CB C 44.001 0.050 1 32 9 9 LEU N N 119.888 0.050 1 33 10 10 ASP H H 9.769 0.005 1 34 10 10 ASP C C 176.289 0.050 1 35 10 10 ASP CB C 38.788 0.050 1 36 10 10 ASP N N 125.059 0.050 1 37 11 11 GLY H H 8.785 0.005 1 38 11 11 GLY C C 171.849 0.050 1 39 11 11 GLY N N 116.722 0.050 1 40 12 12 VAL H H 7.724 0.005 1 41 12 12 VAL C C 173.475 0.050 1 42 12 12 VAL CB C 33.066 0.050 1 43 12 12 VAL N N 119.242 0.050 1 44 13 13 ILE H H 8.593 0.005 1 45 13 13 ILE C C 175.351 0.050 1 46 13 13 ILE CB C 38.038 0.050 1 47 13 13 ILE N N 115.593 0.050 1 48 14 14 THR H H 7.194 0.005 1 49 14 14 THR C C 173.058 0.050 1 50 14 14 THR CB C 67.511 0.050 1 51 14 14 THR N N 110.327 0.050 1 52 15 15 ASP H H 7.924 0.005 1 53 15 15 ASP C C 177.171 0.050 1 54 15 15 ASP CB C 40.143 0.050 1 55 15 15 ASP N N 127.490 0.050 1 56 16 16 THR H H 7.713 0.005 1 57 16 16 THR C C 178.650 0.050 1 58 16 16 THR CB C 66.515 0.050 1 59 16 16 THR N N 108.536 0.050 1 60 17 17 ALA H H 7.417 0.005 1 61 17 17 ALA C C 181.313 0.050 1 62 17 17 ALA CB C 16.296 0.050 1 63 17 17 ALA N N 124.393 0.050 1 64 18 18 GLU H H 8.118 0.005 1 65 18 18 GLU C C 178.318 0.050 1 66 18 18 GLU CB C 28.312 0.050 1 67 18 18 GLU N N 122.221 0.050 1 68 19 19 TYR H H 6.594 0.005 1 69 19 19 TYR C C 178.161 0.050 1 70 19 19 TYR CB C 36.512 0.050 1 71 19 19 TYR N N 118.342 0.050 1 72 20 20 HIS H H 8.407 0.005 1 73 20 20 HIS C C 177.769 0.050 1 74 20 20 HIS CB C 30.599 0.050 1 75 20 20 HIS N N 119.178 0.050 1 76 21 21 PHE H H 8.139 0.005 1 77 21 21 PHE C C 176.490 0.050 1 78 21 21 PHE CB C 37.628 0.050 1 79 21 21 PHE N N 119.058 0.050 1 80 22 22 ARG H H 8.208 0.005 1 81 22 22 ARG C C 179.813 0.050 1 82 22 22 ARG CB C 29.541 0.050 1 83 22 22 ARG N N 117.387 0.050 1 84 23 23 ALA H H 8.404 0.005 1 85 23 23 ALA C C 180.308 0.050 1 86 23 23 ALA CB C 17.997 0.050 1 87 23 23 ALA N N 122.654 0.050 1 88 24 24 TRP H H 9.364 0.005 1 89 24 24 TRP C C 178.445 0.050 1 90 24 24 TRP CB C 29.302 0.050 1 91 24 24 TRP N N 122.789 0.050 1 92 25 25 LYS H H 8.852 0.005 1 93 25 25 LYS C C 178.005 0.050 1 94 25 25 LYS CB C 31.707 0.050 1 95 25 25 LYS N N 120.653 0.050 1 96 26 26 ALA H H 7.677 0.005 1 97 26 26 ALA C C 180.791 0.050 1 98 26 26 ALA CB C 17.179 0.050 1 99 26 26 ALA N N 119.903 0.050 1 100 27 27 LEU H H 7.623 0.005 1 101 27 27 LEU C C 178.443 0.050 1 102 27 27 LEU CB C 40.984 0.050 1 103 27 27 LEU N N 120.665 0.050 1 104 28 28 ALA H H 8.615 0.005 1 105 28 28 ALA C C 179.853 0.050 1 106 28 28 ALA CB C 17.643 0.050 1 107 28 28 ALA N N 120.976 0.050 1 108 29 29 GLU H H 8.386 0.005 1 109 29 29 GLU C C 180.616 0.050 1 110 29 29 GLU CB C 28.367 0.050 1 111 29 29 GLU N N 116.980 0.050 1 112 30 30 GLU H H 7.935 0.005 1 113 30 30 GLU C C 178.913 0.050 1 114 30 30 GLU CB C 29.014 0.050 1 115 30 30 GLU N N 121.711 0.050 1 116 31 31 ILE H H 7.612 0.005 1 117 31 31 ILE C C 175.933 0.050 1 118 31 31 ILE CB C 36.870 0.050 1 119 31 31 ILE N N 112.055 0.050 1 120 32 32 GLY H H 7.556 0.005 1 121 32 32 GLY C C 174.449 0.050 1 122 32 32 GLY N N 109.424 0.050 1 123 33 33 ILE H H 8.389 0.005 1 124 33 33 ILE C C 175.095 0.050 1 125 33 33 ILE CB C 38.442 0.050 1 126 33 33 ILE N N 123.223 0.050 1 127 34 34 ASN H H 8.505 0.005 1 128 34 34 ASN C C 175.326 0.050 1 129 34 34 ASN CB C 39.501 0.050 1 130 34 34 ASN N N 126.329 0.050 1 131 35 35 GLY H H 7.762 0.005 1 132 35 35 GLY C C 174.055 0.050 1 133 35 35 GLY N N 106.992 0.050 1 134 36 36 VAL H H 8.681 0.005 1 135 36 36 VAL C C 173.548 0.050 1 136 36 36 VAL CB C 27.956 0.050 1 137 36 36 VAL N N 123.406 0.050 1 138 37 37 ASP H H 7.495 0.005 1 139 37 37 ASP C C 176.475 0.050 1 140 37 37 ASP CB C 41.844 0.050 1 141 37 37 ASP N N 126.681 0.050 1 142 38 38 ARG H H 8.403 0.005 1 143 38 38 ARG C C 178.714 0.050 1 144 38 38 ARG CB C 28.428 0.050 1 145 38 38 ARG N N 118.460 0.050 1 146 39 39 GLN H H 7.992 0.005 1 147 39 39 GLN C C 179.725 0.050 1 148 39 39 GLN CB C 27.437 0.050 1 149 39 39 GLN N N 120.136 0.050 1 150 40 40 PHE H H 8.861 0.005 1 151 40 40 PHE C C 178.000 0.050 1 152 40 40 PHE CB C 39.208 0.050 1 153 40 40 PHE N N 125.288 0.050 1 154 41 41 ASN H H 8.626 0.005 1 155 41 41 ASN C C 177.242 0.050 1 156 41 41 ASN CB C 39.092 0.050 1 157 41 41 ASN N N 115.320 0.050 1 158 42 42 GLU H H 7.403 0.005 1 159 42 42 GLU C C 179.473 0.050 1 160 42 42 GLU CB C 28.367 0.050 1 161 42 42 GLU N N 117.253 0.050 1 162 43 43 GLN H H 7.904 0.005 1 163 43 43 GLN C C 174.880 0.050 1 164 43 43 GLN CB C 28.020 0.050 1 165 43 43 GLN N N 116.925 0.050 1 166 44 44 LEU H H 6.889 0.005 1 167 44 44 LEU C C 178.844 0.050 1 168 44 44 LEU CB C 40.440 0.050 1 169 44 44 LEU N N 116.800 0.050 1 170 45 45 LYS H H 7.181 0.005 1 171 45 45 LYS C C 176.981 0.050 1 172 45 45 LYS CB C 32.761 0.050 1 173 45 45 LYS N N 121.683 0.050 1 174 46 46 GLY H H 8.556 0.005 1 175 46 46 GLY C C 171.066 0.050 1 176 46 46 GLY N N 110.605 0.050 1 177 47 47 VAL H H 7.317 0.005 1 178 47 47 VAL C C 176.700 0.050 1 179 47 47 VAL CB C 30.941 0.050 1 180 47 47 VAL N N 118.129 0.050 1 181 48 48 SER H H 8.380 0.005 1 182 48 48 SER C C 175.470 0.050 1 183 48 48 SER CB C 64.817 0.050 1 184 48 48 SER N N 119.908 0.050 1 185 49 49 ARG H H 9.290 0.005 1 186 49 49 ARG C C 177.915 0.050 1 187 49 49 ARG CB C 30.659 0.050 1 188 49 49 ARG N N 125.657 0.050 1 189 50 50 GLU H H 9.055 0.005 1 190 50 50 GLU C C 178.526 0.050 1 191 50 50 GLU CB C 27.821 0.050 1 192 50 50 GLU N N 116.965 0.050 1 193 51 51 ASP H H 7.638 0.005 1 194 51 51 ASP C C 179.267 0.050 1 195 51 51 ASP CB C 39.212 0.050 1 196 51 51 ASP N N 119.912 0.050 1 197 52 52 SER H H 8.452 0.005 1 198 52 52 SER C C 174.002 0.050 1 199 52 52 SER N N 119.752 0.050 1 200 53 53 LEU H H 7.304 0.005 1 201 53 53 LEU C C 178.151 0.050 1 202 53 53 LEU CB C 38.836 0.050 1 203 53 53 LEU N N 121.612 0.050 1 204 54 54 GLN H H 8.020 0.005 1 205 54 54 GLN C C 177.224 0.050 1 206 54 54 GLN CB C 28.248 0.050 1 207 54 54 GLN N N 117.489 0.050 1 208 55 55 LYS H H 7.659 0.005 1 209 55 55 LYS C C 179.750 0.050 1 210 55 55 LYS CB C 31.876 0.050 1 211 55 55 LYS N N 118.364 0.050 1 212 56 56 ILE H H 7.583 0.005 1 213 56 56 ILE C C 177.218 0.050 1 214 56 56 ILE CB C 37.688 0.050 1 215 56 56 ILE N N 120.674 0.050 1 216 57 57 LEU H H 8.395 0.005 1 217 57 57 LEU C C 180.931 0.050 1 218 57 57 LEU CB C 39.033 0.050 1 219 57 57 LEU N N 119.370 0.050 1 220 58 58 ASP H H 8.671 0.005 1 221 58 58 ASP C C 179.443 0.050 1 222 58 58 ASP CB C 39.506 0.050 1 223 58 58 ASP N N 119.447 0.050 1 224 59 59 LEU H H 7.660 0.005 1 225 59 59 LEU C C 178.160 0.050 1 226 59 59 LEU CB C 40.789 0.050 1 227 59 59 LEU N N 123.350 0.050 1 228 60 60 ALA H H 7.016 0.005 1 229 60 60 ALA C C 176.052 0.050 1 230 60 60 ALA CB C 20.400 0.050 1 231 60 60 ALA N N 118.899 0.050 1 232 61 61 ASP H H 7.885 0.005 1 233 61 61 ASP C C 174.709 0.050 1 234 61 61 ASP CB C 39.501 0.050 1 235 61 61 ASP N N 120.775 0.050 1 236 62 62 LYS H H 7.827 0.005 1 237 62 62 LYS C C 175.486 0.050 1 238 62 62 LYS CB C 33.175 0.050 1 239 62 62 LYS N N 118.704 0.050 1 240 63 63 LYS H H 8.510 0.005 1 241 63 63 LYS C C 176.349 0.050 1 242 63 63 LYS CB C 32.122 0.050 1 243 63 63 LYS N N 127.003 0.050 1 244 64 64 VAL H H 8.405 0.005 1 245 64 64 VAL C C 175.806 0.050 1 246 64 64 VAL CB C 34.462 0.050 1 247 64 64 VAL N N 116.718 0.050 1 248 65 65 SER H H 9.018 0.005 1 249 65 65 SER C C 174.622 0.050 1 250 65 65 SER CB C 64.758 0.050 1 251 65 65 SER N N 119.637 0.050 1 252 66 66 ALA H H 8.911 0.005 1 253 66 66 ALA C C 181.015 0.050 1 254 66 66 ALA CB C 17.235 0.050 1 255 66 66 ALA N N 124.295 0.050 1 256 67 67 GLU H H 8.572 0.005 1 257 67 67 GLU C C 179.438 0.050 1 258 67 67 GLU CB C 28.489 0.050 1 259 67 67 GLU N N 117.986 0.050 1 260 68 68 GLU H H 7.887 0.005 1 261 68 68 GLU C C 178.558 0.050 1 262 68 68 GLU CB C 29.540 0.050 1 263 68 68 GLU N N 122.943 0.050 1 264 69 69 PHE H H 8.844 0.005 1 265 69 69 PHE C C 176.770 0.050 1 266 69 69 PHE CB C 38.917 0.050 1 267 69 69 PHE N N 121.623 0.050 1 268 70 70 LYS H H 7.664 0.005 1 269 70 70 LYS C C 179.956 0.050 1 270 70 70 LYS CB C 31.771 0.050 1 271 70 70 LYS N N 116.362 0.050 1 272 71 71 GLU H H 7.783 0.005 1 273 71 71 GLU C C 178.937 0.050 1 274 71 71 GLU CB C 28.487 0.050 1 275 71 71 GLU N N 121.197 0.050 1 276 72 72 LEU H H 8.399 0.005 1 277 72 72 LEU C C 178.157 0.050 1 278 72 72 LEU CB C 41.673 0.050 1 279 72 72 LEU N N 122.053 0.050 1 280 73 73 ALA H H 7.735 0.005 1 281 73 73 ALA C C 179.118 0.050 1 282 73 73 ALA CB C 16.072 0.050 1 283 73 73 ALA N N 120.567 0.050 1 284 74 74 LYS H H 7.702 0.005 1 285 74 74 LYS C C 178.116 0.050 1 286 74 74 LYS CB C 31.533 0.050 1 287 74 74 LYS N N 118.814 0.050 1 288 75 75 ARG H H 8.277 0.005 1 289 75 75 ARG C C 179.541 0.050 1 290 75 75 ARG CB C 29.484 0.050 1 291 75 75 ARG N N 121.424 0.050 1 292 76 76 LYS H H 7.749 0.005 1 293 76 76 LYS C C 179.024 0.050 1 294 76 76 LYS CB C 29.536 0.050 1 295 76 76 LYS N N 119.516 0.050 1 296 77 77 ASN H H 8.110 0.005 1 297 77 77 ASN C C 175.991 0.050 1 298 77 77 ASN CB C 37.864 0.050 1 299 77 77 ASN N N 118.864 0.050 1 300 78 78 ASP H H 9.072 0.005 1 301 78 78 ASP C C 179.233 0.050 1 302 78 78 ASP CB C 39.210 0.050 1 303 78 78 ASP N N 119.772 0.050 1 304 79 79 ASN H H 7.410 0.005 1 305 79 79 ASN C C 176.927 0.050 1 306 79 79 ASN CB C 37.743 0.050 1 307 79 79 ASN N N 118.654 0.050 1 308 80 80 TYR H H 8.413 0.005 1 309 80 80 TYR C C 176.726 0.050 1 310 80 80 TYR CB C 38.503 0.050 1 311 80 80 TYR N N 122.455 0.050 1 312 81 81 VAL H H 8.960 0.005 1 313 81 81 VAL C C 179.018 0.050 1 314 81 81 VAL CB C 30.476 0.050 1 315 81 81 VAL N N 118.416 0.050 1 316 82 82 LYS H H 7.016 0.005 1 317 82 82 LYS C C 179.461 0.050 1 318 82 82 LYS CB C 31.236 0.050 1 319 82 82 LYS N N 118.899 0.050 1 320 83 83 MET H H 7.562 0.005 1 321 83 83 MET C C 178.336 0.050 1 322 83 83 MET CB C 31.938 0.050 1 323 83 83 MET N N 118.394 0.050 1 324 84 84 ILE H H 6.969 0.005 1 325 84 84 ILE C C 176.666 0.050 1 326 84 84 ILE CB C 36.806 0.050 1 327 84 84 ILE N N 108.553 0.050 1 328 85 85 GLN H H 6.954 0.005 1 329 85 85 GLN C C 176.299 0.050 1 330 85 85 GLN CB C 28.073 0.050 1 331 85 85 GLN N N 118.511 0.050 1 332 86 86 ASP H H 7.880 0.005 1 333 86 86 ASP C C 176.563 0.050 1 334 86 86 ASP CB C 40.734 0.050 1 335 86 86 ASP N N 115.596 0.050 1 336 87 87 VAL H H 7.155 0.005 1 337 87 87 VAL C C 174.526 0.050 1 338 87 87 VAL CB C 30.595 0.050 1 339 87 87 VAL N N 124.006 0.050 1 340 88 88 SER H H 9.411 0.005 1 341 88 88 SER C C 173.844 0.050 1 342 88 88 SER N N 126.707 0.050 1 343 89 89 PRO C C 177.759 0.050 1 344 89 89 PRO CB C 30.859 0.050 1 345 90 90 ALA H H 7.704 0.005 1 346 90 90 ALA C C 178.029 0.050 1 347 90 90 ALA CB C 17.649 0.050 1 348 90 90 ALA N N 119.470 0.050 1 349 91 91 ASP H H 8.019 0.005 1 350 91 91 ASP C C 177.376 0.050 1 351 91 91 ASP CB C 41.318 0.050 1 352 91 91 ASP N N 114.992 0.050 1 353 92 92 VAL H H 7.183 0.005 1 354 92 92 VAL C C 176.690 0.050 1 355 92 92 VAL CB C 31.126 0.050 1 356 92 92 VAL N N 125.467 0.050 1 357 93 93 TYR H H 8.928 0.005 1 358 93 93 TYR C C 175.517 0.050 1 359 93 93 TYR N N 130.756 0.050 1 360 94 94 PRO C C 177.244 0.050 1 361 94 94 PRO CB C 31.416 0.050 1 362 95 95 GLY H H 8.372 0.005 1 363 95 95 GLY C C 176.108 0.050 1 364 95 95 GLY N N 111.566 0.050 1 365 96 96 ILE H H 7.138 0.005 1 366 96 96 ILE C C 176.979 0.050 1 367 96 96 ILE CB C 33.935 0.050 1 368 96 96 ILE N N 121.515 0.050 1 369 97 97 LEU H H 8.775 0.005 1 370 97 97 LEU C C 178.012 0.050 1 371 97 97 LEU CB C 40.377 0.050 1 372 97 97 LEU N N 121.222 0.050 1 373 98 98 GLN H H 8.688 0.005 1 374 98 98 GLN C C 177.403 0.050 1 375 98 98 GLN CB C 27.669 0.050 1 376 98 98 GLN N N 117.841 0.050 1 377 99 99 LEU H H 7.835 0.005 1 378 99 99 LEU C C 178.493 0.050 1 379 99 99 LEU CB C 39.908 0.050 1 380 99 99 LEU N N 119.829 0.050 1 381 100 100 LEU H H 8.266 0.005 1 382 100 100 LEU C C 179.092 0.050 1 383 100 100 LEU CB C 39.619 0.050 1 384 100 100 LEU N N 119.385 0.050 1 385 101 101 LYS H H 7.947 0.005 1 386 101 101 LYS C C 180.265 0.050 1 387 101 101 LYS CB C 32.003 0.050 1 388 101 101 LYS N N 117.840 0.050 1 389 102 102 ASP H H 8.831 0.005 1 390 102 102 ASP C C 179.812 0.050 1 391 102 102 ASP CB C 39.563 0.050 1 392 102 102 ASP N N 122.885 0.050 1 393 103 103 LEU H H 9.354 0.005 1 394 103 103 LEU C C 179.054 0.050 1 395 103 103 LEU CB C 39.855 0.050 1 396 103 103 LEU N N 123.875 0.050 1 397 104 104 ARG H H 8.261 0.005 1 398 104 104 ARG C C 181.895 0.050 1 399 104 104 ARG CB C 28.722 0.050 1 400 104 104 ARG N N 120.130 0.050 1 401 105 105 SER H H 8.718 0.005 1 402 105 105 SER C C 175.185 0.050 1 403 105 105 SER CB C 62.301 0.050 1 404 105 105 SER N N 117.393 0.050 1 405 106 106 ASN H H 7.424 0.005 1 406 106 106 ASN C C 172.378 0.050 1 407 106 106 ASN CB C 39.445 0.050 1 408 106 106 ASN N N 118.343 0.050 1 409 107 107 LYS H H 7.894 0.005 1 410 107 107 LYS C C 175.096 0.050 1 411 107 107 LYS CB C 27.432 0.050 1 412 107 107 LYS N N 115.000 0.050 1 413 108 108 ILE H H 7.999 0.005 1 414 108 108 ILE C C 175.757 0.050 1 415 108 108 ILE CB C 37.042 0.050 1 416 108 108 ILE N N 122.580 0.050 1 417 109 109 LYS H H 7.644 0.005 1 418 109 109 LYS C C 175.758 0.050 1 419 109 109 LYS CB C 32.652 0.050 1 420 109 109 LYS N N 125.135 0.050 1 421 110 110 ILE H H 9.275 0.005 1 422 110 110 ILE C C 175.855 0.050 1 423 110 110 ILE CB C 40.205 0.050 1 424 110 110 ILE N N 122.070 0.050 1 425 111 111 ALA H H 8.820 0.005 1 426 111 111 ALA C C 175.935 0.050 1 427 111 111 ALA CB C 23.736 0.050 1 428 111 111 ALA N N 128.080 0.050 1 429 112 112 LEU H H 8.533 0.005 1 430 112 112 LEU C C 173.948 0.050 1 431 112 112 LEU CB C 43.314 0.050 1 432 112 112 LEU N N 124.104 0.050 1 433 113 113 ALA H H 9.257 0.005 1 434 113 113 ALA C C 174.487 0.050 1 435 113 113 ALA CB C 19.054 0.050 1 436 113 113 ALA N N 133.694 0.050 1 437 114 114 SER H H 7.452 0.005 1 438 114 114 SER C C 175.779 0.050 1 439 114 114 SER CB C 64.521 0.050 1 440 114 114 SER N N 113.966 0.050 1 441 115 115 ALA H H 9.857 0.005 1 442 115 115 ALA C C 175.918 0.050 1 443 115 115 ALA CB C 17.772 0.050 1 444 115 115 ALA N N 129.896 0.050 1 445 116 116 SER H H 8.669 0.005 1 446 116 116 SER C C 178.905 0.050 1 447 116 116 SER CB C 63.813 0.050 1 448 116 116 SER N N 113.579 0.050 1 449 117 117 LYS H H 11.143 0.005 1 450 117 117 LYS C C 178.031 0.050 1 451 117 117 LYS CB C 31.256 0.050 1 452 117 117 LYS N N 135.668 0.050 1 453 118 118 ASN H H 8.228 0.005 1 454 118 118 ASN C C 174.329 0.050 1 455 118 118 ASN CB C 40.010 0.050 1 456 118 118 ASN N N 117.263 0.050 1 457 119 119 GLY H H 7.336 0.005 1 458 119 119 GLY C C 172.468 0.050 1 459 119 119 GLY N N 106.141 0.050 1 460 120 120 PRO C C 179.132 0.050 1 461 120 120 PRO CB C 30.715 0.050 1 462 121 121 PHE H H 7.664 0.005 1 463 121 121 PHE C C 177.315 0.050 1 464 121 121 PHE CB C 38.624 0.050 1 465 121 121 PHE N N 119.542 0.050 1 466 122 122 LEU H H 7.725 0.005 1 467 122 122 LEU C C 178.887 0.050 1 468 122 122 LEU CB C 41.259 0.050 1 469 122 122 LEU N N 121.068 0.050 1 470 123 123 LEU H H 8.298 0.005 1 471 123 123 LEU C C 179.154 0.050 1 472 123 123 LEU CB C 40.374 0.050 1 473 123 123 LEU N N 117.357 0.050 1 474 124 124 GLU H H 7.577 0.005 1 475 124 124 GLU C C 180.794 0.050 1 476 124 124 GLU CB C 28.311 0.050 1 477 124 124 GLU N N 119.888 0.050 1 478 125 125 ARG H H 8.046 0.005 1 479 125 125 ARG C C 178.469 0.050 1 480 125 125 ARG CB C 28.487 0.050 1 481 125 125 ARG N N 121.015 0.050 1 482 126 126 MET H H 7.412 0.005 1 483 126 126 MET C C 173.605 0.050 1 484 126 126 MET CB C 32.356 0.050 1 485 126 126 MET N N 113.398 0.050 1 486 127 127 ASN H H 7.979 0.005 1 487 127 127 ASN C C 175.773 0.050 1 488 127 127 ASN CB C 36.513 0.050 1 489 127 127 ASN N N 117.384 0.050 1 490 128 128 LEU H H 8.758 0.005 1 491 128 128 LEU C C 177.996 0.050 1 492 128 128 LEU CB C 44.659 0.050 1 493 128 128 LEU N N 114.279 0.050 1 494 129 129 THR H H 7.416 0.005 1 495 129 129 THR C C 176.344 0.050 1 496 129 129 THR CB C 68.456 0.050 1 497 129 129 THR N N 115.847 0.050 1 498 130 130 GLY H H 8.571 0.005 1 499 130 130 GLY C C 175.016 0.050 1 500 130 130 GLY N N 106.277 0.050 1 501 131 131 TYR H H 7.769 0.005 1 502 131 131 TYR C C 174.560 0.050 1 503 131 131 TYR CB C 38.628 0.050 1 504 131 131 TYR N N 116.493 0.050 1 505 132 132 PHE H H 7.363 0.005 1 506 132 132 PHE C C 175.878 0.050 1 507 132 132 PHE CB C 38.852 0.050 1 508 132 132 PHE N N 115.503 0.050 1 509 133 133 ASP H H 9.189 0.005 1 510 133 133 ASP C C 176.431 0.050 1 511 133 133 ASP CB C 42.142 0.050 1 512 133 133 ASP N N 125.289 0.050 1 513 134 134 ALA H H 7.644 0.005 1 514 134 134 ALA C C 175.438 0.050 1 515 134 134 ALA CB C 23.449 0.050 1 516 134 134 ALA N N 115.628 0.050 1 517 135 135 ILE H H 8.628 0.005 1 518 135 135 ILE C C 175.746 0.050 1 519 135 135 ILE CB C 40.089 0.050 1 520 135 135 ILE N N 122.111 0.050 1 521 136 136 ALA H H 8.498 0.005 1 522 136 136 ALA C C 175.613 0.050 1 523 136 136 ALA CB C 17.586 0.050 1 524 136 136 ALA N N 131.071 0.050 1 525 137 137 ASP H H 8.379 0.005 1 526 137 137 ASP C C 176.722 0.050 1 527 137 137 ASP N N 124.960 0.050 1 528 138 138 PRO C C 178.142 0.050 1 529 138 138 PRO CB C 31.539 0.050 1 530 139 139 ALA H H 8.595 0.005 1 531 139 139 ALA C C 178.919 0.050 1 532 139 139 ALA CB C 18.056 0.050 1 533 139 139 ALA N N 120.703 0.050 1 534 140 140 GLU H H 7.496 0.005 1 535 140 140 GLU C C 176.639 0.050 1 536 140 140 GLU CB C 29.775 0.050 1 537 140 140 GLU N N 116.094 0.050 1 538 141 141 VAL H H 6.964 0.005 1 539 141 141 VAL C C 175.798 0.050 1 540 141 141 VAL CB C 32.002 0.050 1 541 141 141 VAL N N 115.509 0.050 1 542 142 142 ALA H H 8.607 0.005 1 543 142 142 ALA C C 177.585 0.050 1 544 142 142 ALA CB C 18.174 0.050 1 545 142 142 ALA N N 125.730 0.050 1 546 143 143 ALA H H 7.209 0.005 1 547 143 143 ALA C C 176.062 0.050 1 548 143 143 ALA CB C 20.750 0.050 1 549 143 143 ALA N N 119.529 0.050 1 550 144 144 SER H H 8.557 0.005 1 551 144 144 SER C C 176.375 0.050 1 552 144 144 SER CB C 63.350 0.050 1 553 144 144 SER N N 117.903 0.050 1 554 145 145 LYS H H 8.820 0.005 1 555 145 145 LYS C C 175.203 0.050 1 556 145 145 LYS N N 128.080 0.050 1 557 146 146 PRO C C 176.353 0.050 1 558 146 146 PRO CB C 35.284 0.050 1 559 147 147 ALA H H 9.219 0.005 1 560 147 147 ALA C C 178.251 0.050 1 561 147 147 ALA N N 132.103 0.050 1 562 148 148 PRO C C 177.145 0.050 1 563 148 148 PRO CB C 32.062 0.050 1 564 149 149 ASP H H 9.326 0.005 1 565 149 149 ASP C C 178.051 0.050 1 566 149 149 ASP CB C 38.986 0.050 1 567 149 149 ASP N N 120.846 0.050 1 568 150 150 ILE H H 9.659 0.005 1 569 150 150 ILE C C 175.661 0.050 1 570 150 150 ILE CB C 37.335 0.050 1 571 150 150 ILE N N 120.214 0.050 1 572 151 151 PHE H H 7.236 0.005 1 573 151 151 PHE C C 177.666 0.050 1 574 151 151 PHE CB C 38.338 0.050 1 575 151 151 PHE N N 121.172 0.050 1 576 152 152 ILE H H 7.727 0.005 1 577 152 152 ILE C C 177.661 0.050 1 578 152 152 ILE CB C 37.404 0.050 1 579 152 152 ILE N N 120.382 0.050 1 580 153 153 ALA H H 8.400 0.005 1 581 153 153 ALA C C 180.948 0.050 1 582 153 153 ALA CB C 17.414 0.050 1 583 153 153 ALA N N 120.483 0.050 1 584 154 154 ALA H H 7.852 0.005 1 585 154 154 ALA C C 176.708 0.050 1 586 154 154 ALA CB C 17.887 0.050 1 587 154 154 ALA N N 122.363 0.050 1 588 155 155 ALA H H 7.601 0.005 1 589 155 155 ALA C C 179.750 0.050 1 590 155 155 ALA CB C 16.123 0.050 1 591 155 155 ALA N N 118.574 0.050 1 592 156 156 HIS H H 8.456 0.005 1 593 156 156 HIS C C 179.770 0.050 1 594 156 156 HIS CB C 29.123 0.050 1 595 156 156 HIS N N 117.087 0.050 1 596 157 157 ALA H H 8.234 0.005 1 597 157 157 ALA C C 179.314 0.050 1 598 157 157 ALA CB C 17.645 0.050 1 599 157 157 ALA N N 122.049 0.050 1 600 158 158 VAL H H 7.220 0.005 1 601 158 158 VAL C C 175.535 0.050 1 602 158 158 VAL CB C 30.527 0.050 1 603 158 158 VAL N N 107.591 0.050 1 604 159 159 GLY H H 7.777 0.005 1 605 159 159 GLY C C 174.615 0.050 1 606 159 159 GLY N N 110.346 0.050 1 607 160 160 VAL H H 7.674 0.005 1 608 160 160 VAL C C 174.233 0.050 1 609 160 160 VAL CB C 34.054 0.050 1 610 160 160 VAL N N 117.148 0.050 1 611 161 161 ALA H H 8.654 0.005 1 612 161 161 ALA C C 178.757 0.050 1 613 161 161 ALA N N 125.920 0.050 1 614 162 162 PRO C C 177.455 0.050 1 615 162 162 PRO CB C 30.821 0.050 1 616 163 163 SER H H 7.731 0.005 1 617 163 163 SER C C 175.937 0.050 1 618 163 163 SER CB C 61.830 0.050 1 619 163 163 SER N N 106.987 0.050 1 620 164 164 GLU H H 7.807 0.005 1 621 164 164 GLU C C 174.726 0.050 1 622 164 164 GLU CB C 29.307 0.050 1 623 164 164 GLU N N 121.935 0.050 1 624 165 165 SER H H 7.975 0.005 1 625 165 165 SER C C 172.137 0.050 1 626 165 165 SER CB C 65.227 0.050 1 627 165 165 SER N N 114.772 0.050 1 628 166 166 ILE H H 7.647 0.005 1 629 166 166 ILE C C 175.236 0.050 1 630 166 166 ILE CB C 40.789 0.050 1 631 166 166 ILE N N 121.888 0.050 1 632 167 167 GLY H H 8.752 0.005 1 633 167 167 GLY C C 170.387 0.050 1 634 167 167 GLY N N 112.847 0.050 1 635 168 168 LEU H H 7.877 0.005 1 636 168 168 LEU C C 175.395 0.050 1 637 168 168 LEU CB C 40.556 0.050 1 638 168 168 LEU N N 123.934 0.050 1 639 169 169 GLU H H 6.905 0.005 1 640 169 169 GLU C C 173.857 0.050 1 641 169 169 GLU CB C 39.677 0.050 1 642 169 169 GLU N N 124.389 0.050 1 643 170 170 ASP H H 8.498 0.005 1 644 170 170 ASP C C 174.129 0.050 1 645 170 170 ASP CB C 41.493 0.050 1 646 170 170 ASP N N 116.492 0.050 1 647 171 171 SER H H 8.078 0.005 1 648 171 171 SER C C 173.771 0.050 1 649 171 171 SER CB C 69.855 0.050 1 650 171 171 SER N N 114.219 0.050 1 651 172 172 GLN H H 9.728 0.005 1 652 172 172 GLN C C 179.397 0.050 1 653 172 172 GLN CB C 27.665 0.050 1 654 172 172 GLN N N 124.227 0.050 1 655 173 173 ALA H H 8.816 0.005 1 656 173 173 ALA C C 180.279 0.050 1 657 173 173 ALA CB C 16.820 0.050 1 658 173 173 ALA N N 121.583 0.050 1 659 174 174 GLY H H 8.339 0.005 1 660 174 174 GLY C C 175.722 0.050 1 661 174 174 GLY N N 106.450 0.050 1 662 175 175 ILE H H 8.436 0.005 1 663 175 175 ILE C C 177.818 0.050 1 664 175 175 ILE CB C 34.813 0.050 1 665 175 175 ILE N N 123.243 0.050 1 666 176 176 GLN H H 7.682 0.005 1 667 176 176 GLN C C 177.007 0.050 1 668 176 176 GLN CB C 27.251 0.050 1 669 176 176 GLN N N 120.293 0.050 1 670 177 177 ALA H H 7.743 0.005 1 671 177 177 ALA C C 179.807 0.050 1 672 177 177 ALA CB C 19.224 0.050 1 673 177 177 ALA N N 122.595 0.050 1 674 178 178 ILE H H 8.059 0.005 1 675 178 178 ILE C C 180.684 0.050 1 676 178 178 ILE CB C 36.335 0.050 1 677 178 178 ILE N N 117.807 0.050 1 678 179 179 LYS H H 8.488 0.005 1 679 179 179 LYS C C 180.985 0.050 1 680 179 179 LYS CB C 31.941 0.050 1 681 179 179 LYS N N 120.840 0.050 1 682 180 180 ASP H H 8.463 0.005 1 683 180 180 ASP C C 177.344 0.050 1 684 180 180 ASP CB C 38.842 0.050 1 685 180 180 ASP N N 118.782 0.050 1 686 181 181 SER H H 8.107 0.005 1 687 181 181 SER C C 173.867 0.050 1 688 181 181 SER CB C 64.344 0.050 1 689 181 181 SER N N 117.333 0.050 1 690 182 182 GLY H H 7.223 0.005 1 691 182 182 GLY C C 173.392 0.050 1 692 182 182 GLY N N 109.110 0.050 1 693 183 183 ALA H H 7.189 0.005 1 694 183 183 ALA C C 174.728 0.050 1 695 183 183 ALA CB C 19.516 0.050 1 696 183 183 ALA N N 124.351 0.050 1 697 184 184 LEU H H 8.074 0.005 1 698 184 184 LEU C C 174.817 0.050 1 699 184 184 LEU N N 122.691 0.050 1 700 185 185 PRO C C 176.404 0.050 1 701 185 185 PRO CB C 31.651 0.050 1 702 186 186 ILE H H 8.265 0.005 1 703 186 186 ILE C C 178.452 0.050 1 704 186 186 ILE CB C 38.098 0.050 1 705 186 186 ILE N N 119.515 0.050 1 706 187 187 GLY H H 8.940 0.005 1 707 187 187 GLY C C 171.352 0.050 1 708 187 187 GLY N N 116.305 0.050 1 709 188 188 VAL H H 8.107 0.005 1 710 188 188 VAL C C 173.969 0.050 1 711 188 188 VAL CB C 32.005 0.050 1 712 188 188 VAL N N 119.175 0.050 1 713 189 189 GLY H H 8.146 0.005 1 714 189 189 GLY C C 171.116 0.050 1 715 189 189 GLY N N 113.264 0.050 1 716 190 190 ARG H H 8.690 0.005 1 717 190 190 ARG C C 176.135 0.050 1 718 190 190 ARG N N 120.845 0.050 1 719 191 191 PRO C C 178.800 0.050 1 720 191 191 PRO CB C 30.949 0.050 1 721 192 192 GLU H H 9.637 0.005 1 722 192 192 GLU C C 176.824 0.050 1 723 192 192 GLU CB C 27.952 0.050 1 724 192 192 GLU N N 118.935 0.050 1 725 193 193 ASP H H 7.053 0.005 1 726 193 193 ASP C C 176.952 0.050 1 727 193 193 ASP CB C 41.616 0.050 1 728 193 193 ASP N N 114.943 0.050 1 729 194 194 LEU H H 7.658 0.005 1 730 194 194 LEU C C 176.462 0.050 1 731 194 194 LEU CB C 42.491 0.050 1 732 194 194 LEU N N 116.878 0.050 1 733 195 195 GLY H H 8.034 0.005 1 734 195 195 GLY C C 172.587 0.050 1 735 195 195 GLY N N 108.115 0.050 1 736 196 196 ASP H H 7.911 0.005 1 737 196 196 ASP C C 176.975 0.050 1 738 196 196 ASP CB C 41.142 0.050 1 739 196 196 ASP N N 116.600 0.050 1 740 197 197 ASP H H 8.908 0.005 1 741 197 197 ASP C C 175.379 0.050 1 742 197 197 ASP CB C 39.677 0.050 1 743 197 197 ASP N N 117.359 0.050 1 744 198 198 ILE H H 6.802 0.005 1 745 198 198 ILE C C 175.369 0.050 1 746 198 198 ILE CB C 40.559 0.050 1 747 198 198 ILE N N 113.493 0.050 1 748 199 199 VAL H H 8.936 0.005 1 749 199 199 VAL C C 174.256 0.050 1 750 199 199 VAL CB C 30.361 0.050 1 751 199 199 VAL N N 125.520 0.050 1 752 200 200 ILE H H 7.947 0.005 1 753 200 200 ILE C C 176.016 0.050 1 754 200 200 ILE CB C 40.975 0.050 1 755 200 200 ILE N N 126.661 0.050 1 756 201 201 VAL H H 8.779 0.005 1 757 201 201 VAL C C 174.290 0.050 1 758 201 201 VAL N N 120.767 0.050 1 759 202 202 PRO C C 177.235 0.050 1 760 202 202 PRO CB C 31.182 0.050 1 761 203 203 ASP H H 6.809 0.005 1 762 203 203 ASP C C 175.487 0.050 1 763 203 203 ASP CB C 41.320 0.050 1 764 203 203 ASP N N 110.324 0.050 1 765 204 204 THR H H 8.073 0.005 1 766 204 204 THR C C 176.546 0.050 1 767 204 204 THR CB C 68.745 0.050 1 768 204 204 THR N N 108.960 0.050 1 769 205 205 SER H H 8.882 0.005 1 770 205 205 SER C C 175.728 0.050 1 771 205 205 SER CB C 61.999 0.050 1 772 205 205 SER N N 120.042 0.050 1 773 206 206 HIS H H 7.064 0.005 1 774 206 206 HIS C C 176.847 0.050 1 775 206 206 HIS CB C 30.541 0.050 1 776 206 206 HIS N N 118.468 0.050 1 777 207 207 TYR H H 7.737 0.005 1 778 207 207 TYR C C 173.600 0.050 1 779 207 207 TYR CB C 35.281 0.050 1 780 207 207 TYR N N 119.899 0.050 1 781 208 208 THR H H 7.383 0.005 1 782 208 208 THR C C 174.774 0.050 1 783 208 208 THR CB C 71.147 0.050 1 784 208 208 THR N N 114.548 0.050 1 785 209 209 LEU H H 9.463 0.005 1 786 209 209 LEU C C 177.844 0.050 1 787 209 209 LEU CB C 39.851 0.050 1 788 209 209 LEU N N 125.201 0.050 1 789 210 210 GLU H H 8.548 0.005 1 790 210 210 GLU C C 178.818 0.050 1 791 210 210 GLU CB C 28.605 0.050 1 792 210 210 GLU N N 116.714 0.050 1 793 211 211 PHE H H 8.183 0.005 1 794 211 211 PHE C C 176.810 0.050 1 795 211 211 PHE CB C 39.460 0.050 1 796 211 211 PHE N N 122.528 0.050 1 797 212 212 LEU H H 8.370 0.005 1 798 212 212 LEU C C 179.074 0.050 1 799 212 212 LEU CB C 39.913 0.050 1 800 212 212 LEU N N 119.822 0.050 1 801 213 213 LYS H H 8.363 0.005 1 802 213 213 LYS C C 178.106 0.050 1 803 213 213 LYS CB C 31.997 0.050 1 804 213 213 LYS N N 116.339 0.050 1 805 214 214 GLU H H 7.788 0.005 1 806 214 214 GLU C C 179.578 0.050 1 807 214 214 GLU CB C 28.721 0.050 1 808 214 214 GLU N N 120.638 0.050 1 809 215 215 VAL H H 8.231 0.005 1 810 215 215 VAL C C 178.442 0.050 1 811 215 215 VAL CB C 30.715 0.050 1 812 215 215 VAL N N 120.513 0.050 1 813 216 216 TRP H H 8.437 0.005 1 814 216 216 TRP C C 178.649 0.050 1 815 216 216 TRP CB C 29.258 0.050 1 816 216 216 TRP N N 120.735 0.050 1 817 217 217 LEU H H 8.193 0.005 1 818 217 217 LEU C C 179.881 0.050 1 819 217 217 LEU CB C 40.966 0.050 1 820 217 217 LEU N N 117.219 0.050 1 821 218 218 GLN H H 7.822 0.005 1 822 218 218 GLN C C 177.709 0.050 1 823 218 218 GLN CB C 27.960 0.050 1 824 218 218 GLN N N 118.272 0.050 1 825 219 219 LYS H H 7.517 0.005 1 826 219 219 LYS C C 176.622 0.050 1 827 219 219 LYS CB C 31.403 0.050 1 828 219 219 LYS N N 118.081 0.050 1 829 220 220 GLN H H 7.627 0.005 1 830 220 220 GLN C C 175.124 0.050 1 831 220 220 GLN CB C 27.843 0.050 1 832 220 220 GLN N N 119.956 0.050 1 833 221 221 LYS H H 7.545 0.005 1 834 221 221 LYS C C 181.484 0.050 1 835 221 221 LYS N N 127.536 0.050 1 stop_ save_ save_assigned_chem_shift_list_1_3 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $Felix stop_ loop_ _Experiment_label '2D 1H-15N TROSY' '3D TROSY HNCO' '3D TROSY HN(COCA)CB' '19F 1D' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name MgF3- _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 MGF FA F -149.0 0.050 1 2 . 1 MGF FB F -153.5 0.050 1 3 . 1 MGF FC F -172.1 0.050 1 stop_ save_