data_15467 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N, and 13C assignments for beta phosphoglucomutase in a complex with glucose-6-phosphate and AlF4- ; _BMRB_accession_number 15467 _BMRB_flat_file_name bmr15467.str _Entry_type original _Submission_date 2007-09-12 _Accession_date 2007-09-12 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'This complex forms a stable transition state analogue of phosphoryl transfer' 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" 405 "15N chemical shifts" 210 "19F chemical shifts" 4 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-06-25 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 7234 'beta phosphoglucosmutase complex with glucose-6-phosphate and MgF3-' 7235 'beta phosphoglucomutase open form' stop_ _Original_release_date 2008-06-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Anionic charge is prioritized over geometry in aluminum and magnesium fluoride transition state analogs of phosphoryl transfer enzymes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18318536 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Baxter Nicola J. . 2 Blackburn G Michael . 3 Marston James P. . 4 Hounslow Andrea M. . 5 Cliff Matthew J. . 6 Bermel Wolfgang . . 7 Williams Nicholas H. . 8 Hollfelder Florian . . 9 Wemmer David E. . 10 Waltho Jonathan P. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_volume 130 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3952 _Page_last 3958 _Year 2008 _Details . loop_ _Keyword 'active site' 'AlF4- transition state analogue' 'enzyme mechanism' 'NOE directed docking of fluoride ions' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'beta phosphoglucomutase in complex with glucose-6-phosphate and AlF4-' _Enzyme_commission_number 5.4.2.6 loop_ _Mol_system_component_name _Mol_label beta_phosphoglucomutase $beta_phosphoglucomutase beta_phosphoglucomutase $BG6 beta_phosphoglucomutase $ALF beta_phosphoglucomutase $MG stop_ _System_molecular_weight 25000 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details ; This is a complex composed of beta phosphoglucomutase, glucose-6-phosphate and AlF4- forming a closed protein conformation and a transition state analogue. A single catalytic magnsium ion is bound to the protein. ; save_ ######################## # Monomeric polymers # ######################## save_beta_phosphoglucomutase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common beta_phosphoglucomutase _Molecular_mass 25000 _Mol_thiol_state 'not present' loop_ _Biological_function mutase stop_ _Details ; native monomer ; ############################## # 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 2015-08-05 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 16409 beta_phosphoglucomutase 100.00 221 100.00 100.00 3.59e-156 BMRB 17851 beta_phosphoglucomutase 100.00 221 100.00 100.00 3.59e-156 BMRB 17852 beta_phosphoglucomutase 100.00 221 100.00 100.00 3.59e-156 PDB 1LVH "The Structure Of Phosphorylated Beta-phosphoglucomutase From Lactoccocus Lactis To 2.3 Angstrom Resolution" 100.00 221 99.55 99.55 3.06e-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 3.59e-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 3.59e-156 PDB 1Z4N "Structure Of Beta-phosphoglucomutase With Inhibitor Bound Alpha-galactose 1-phosphate Cocrystallized With Fluoride" 100.00 221 100.00 100.00 3.59e-156 PDB 1Z4O "Structure Of Beta-Phosphoglucomutase With Inhibitor Bound Alpha-Galactose 1-Phosphate" 100.00 221 100.00 100.00 3.59e-156 PDB 1ZOL "Native Beta-Pgm" 100.00 221 100.00 100.00 3.59e-156 PDB 2WF5 "Structure Of Beta-Phosphoglucomutase Inhibited With Glucose- 6-Phospahte And Trifluoromagnesate" 100.00 221 100.00 100.00 3.59e-156 PDB 2WF6 "Structure Of Beta-Phosphoglucomutase Inhibited With Glucose- 6-Phospahte And Aluminium Tetrafluoride" 100.00 221 100.00 100.00 3.59e-156 PDB 2WF7 "Structure Of Beta-phosphoglucomutase Inhibited With Glucose- 6-phosphonate And Aluminium Tetrafluoride" 100.00 221 100.00 100.00 3.59e-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 3.59e-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 3.59e-156 PDB 2WFA "Structure Of Beta-Phosphoglucomutase Inhibited With Beryllium Trifluoride, In An Open Conformation." 100.00 221 100.00 100.00 3.59e-156 PDB 2WHE "Structure Of Native Beta-Phosphoglucomutase In An Open Conformation Without Bound Ligands." 100.00 221 100.00 100.00 3.59e-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 7.03e-155 PDB 3ZI4 "The Structure Of Beta-phosphoglucomutase Inhibited With Glucose-6-phospahte And Scandium Tetrafluoride" 100.00 221 100.00 100.00 3.59e-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 3.59e-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 3.59e-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 3.59e-156 DBJ BAL50396 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis IO-1]" 100.00 221 100.00 100.00 3.59e-156 DBJ GAM81375 "predicted phosphatase/phosphohexomutase [Lactococcus lactis subsp. lactis]" 100.00 221 100.00 100.00 3.59e-156 EMBL CAA94734 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 100.00 100.00 3.59e-156 EMBL CDG03643 "Beta-phosphoglucomutase [Lactococcus lactis subsp. lactis A12]" 100.00 221 99.55 99.55 4.80e-155 EMBL CDI46177 "Beta-phosphoglucomutase [Lactococcus lactis subsp. lactis Dephy 1]" 100.00 221 100.00 100.00 3.59e-156 GB AAK04527 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis Il1403]" 100.00 221 99.10 100.00 1.69e-154 GB ADA64250 "Beta-phosphoglucomutase [Lactococcus lactis subsp. lactis KF147]" 100.00 221 100.00 100.00 3.59e-156 GB ADZ63078 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis CV56]" 100.00 221 99.55 100.00 4.21e-155 GB AEE43918 "beta-phosphoglucomutase [synthetic construct]" 100.00 221 99.10 100.00 1.69e-154 GB AGY43735 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis KLDS 4.0325]" 100.00 221 98.64 100.00 3.71e-154 REF NP_266585 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis Il1403]" 100.00 221 99.10 100.00 1.69e-154 REF WP_003131530 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 99.55 100.00 4.21e-155 REF WP_010905331 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 99.10 100.00 1.69e-154 REF WP_012897250 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 100.00 100.00 3.59e-156 REF WP_021469610 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 99.55 99.55 5.90e-155 SP P71447 "RecName: Full=Beta-phosphoglucomutase; Short=Beta-PGM" 100.00 221 99.10 100.00 1.69e-154 stop_ save_ ############# # Ligands # ############# save_BG6 _Saveframe_category ligand _Mol_type non-polymer _Name_common "BG6 (BETA-D-GLUCOSE-6-PHOSPHATE)" _BMRB_code . _PDB_code BG6 _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 Mon Oct 17 12:06:32 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 . ? O1 O1 O . 0 . ? O5 O5 O . 0 . ? C3 C3 C . 0 . ? O2 O2 O . 0 . ? C4 C4 C . 0 . ? O3 O3 O . 0 . ? C5 C5 C . 0 . ? O4 O4 O . 0 . ? C6 C6 C . 0 . ? O6 O6 O . 0 . ? P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? HC1 HC1 H . 0 . ? HC2 HC2 H . 0 . ? HO1 HO1 H . 0 . ? HC3 HC3 H . 0 . ? HO2 HO2 H . 0 . ? HC4 HC4 H . 0 . ? HO3 HO3 H . 0 . ? HC5 HC5 H . 0 . ? HO4 HO4 H . 0 . ? HC61 HC61 H . 0 . ? HC62 HC62 H . 0 . ? H1O1 H1O1 H . 0 . ? H2O2 H2O2 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 HC1 ? ? SING C2 C3 ? ? SING C2 O2 ? ? SING C2 HC2 ? ? SING O1 HO1 ? ? SING O5 C5 ? ? SING C3 C4 ? ? SING C3 O3 ? ? SING C3 HC3 ? ? SING O2 HO2 ? ? SING C4 C5 ? ? SING C4 O4 ? ? SING C4 HC4 ? ? SING O3 HO3 ? ? SING C5 C6 ? ? SING C5 HC5 ? ? SING O4 HO4 ? ? SING C6 O6 ? ? SING C6 HC61 ? ? SING C6 HC62 ? ? SING O6 P ? ? SING P O1P ? ? SING P O2P ? ? DOUB P O3P ? ? SING O1P H1O1 ? ? SING O2P H2O2 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_ALF _Saveframe_category ligand _Mol_type non-polymer _Name_common "ALF (TETRAFLUOROALUMINATE ION)" _BMRB_code . _PDB_code ALF _Molecular_mass 102.975 _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 Mon Oct 17 12:07:17 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons AL AL AL . -1 . ? F1 F1 F . 0 . ? F2 F2 F . 0 . ? F3 F3 F . 0 . ? F4 F4 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 AL F1 ? ? SING AL F2 ? ? SING AL F3 ? ? SING AL F4 ? ? 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 Mon Oct 17 12:07:47 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 _Details $beta_phosphoglucomutase 'Lactococcus lactis' 1358 Bacteria . Lactococcus lactis '1360 Bacteria Metazoa Lactococcus lactis 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 _Details $beta_phosphoglucomutase 'recombinant technology' . Escherichia coli BL21(DE3) pET-22b Novagen stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_2H15N13C _Saveframe_category sample _Sample_type solution _Details ; beta phosphoglucomutase closed conformation with glucose-6-phosphate and AlF4- 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; 80% 2H]' $BG6 10 mM 'natural abundance' $ALF 10 mM 'natural abundance' $MG 5 mM 'natural abundance' 'sodium azide' 2 mM 'natural abundance' 'protease inhibitor' 1 X 'natural abundance' 'aluminum chloride' 2.5 mM 'natural abundance' 'potassium HEPES' 50 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % . stop_ save_ save_sample_2H15N _Saveframe_category sample _Sample_type solution _Details ; beta phosphoglucomutase closed conformation with glucose-6-phosphate and AlF4- forming a transition state analogue ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $beta_phosphoglucomutase 1 mM '[ U-100% 15N; 80% 2H]' $BG6 10 mM 'natural abundance' $ALF 10 mM 'natural abundance' $MG 5 mM 'natural abundance' 'sodium azide' 2 mM 'natural abundance' 'protease inhibitor' 1 X 'natural abundance' 'aluminum chloride' 2.5 mM 'natural abundance' 'potassium HEPES' 50 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' ; Banner Lane, Coventry, CV4 9GH ; . stop_ loop_ _Task collection stop_ _Details . save_ save_Felix _Saveframe_category software _Name FELIX _Version 2004 loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' 'San Diego, CA, USA' . 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 . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $sample_2H15N13C save_ save_3D_TROSY_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCO' _Sample_label $sample_2H15N13C save_ save_3D_TROSY_HN(COCA)CB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(COCA)CB' _Sample_label $sample_2H15N13C save_ save_2D_{19F}1H,15N-HSQC_NOE_difference_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D {19F}1H,15N-HSQC NOE difference' _Sample_label $sample_2H15N save_ save_1D_19F_observe_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1D 19F observe' _Sample_label $sample_2H15N 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 . 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 for aluminum tetrafluoride ion' 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 . indirect . . . 0.251449530 $entry_citation $entry_citation trichlorofluoromethane F 19 'methyl fluorine' ppm 0.0 n/a indirect . . . 0.940940080 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1_1 _Saveframe_category assigned_chemical_shifts _Details ; Backbone 1H, 15N, 13C chemical shifts for beta phosphoglucomutase in complex with glucose-6-phosphate and AlF4- in a closed conformation forming a transition state analogue ; loop_ _Software_label $Felix stop_ loop_ _Experiment_label '2D 1H-15N TROSY' '3D TROSY HNCO' '3D TROSY HN(COCA)CB' stop_ loop_ _Sample_label $sample_2H15N13C 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 5.292 0.005 1 2 2 2 PHE C C 173.830 0.050 1 3 2 2 PHE CB C 35.984 0.050 1 4 2 2 PHE N N 117.349 0.050 1 5 3 3 LYS H H 8.760 0.005 1 6 3 3 LYS C C 176.560 0.050 1 7 3 3 LYS CB C 35.634 0.050 1 8 3 3 LYS N N 116.633 0.050 1 9 4 4 ALA H H 7.648 0.005 1 10 4 4 ALA C C 175.315 0.050 1 11 4 4 ALA CB C 22.512 0.050 1 12 4 4 ALA N N 121.184 0.050 1 13 5 5 VAL H H 8.639 0.005 1 14 5 5 VAL C C 172.800 0.050 1 15 5 5 VAL CB C 32.765 0.050 1 16 5 5 VAL N N 120.082 0.050 1 17 6 6 LEU H H 9.329 0.005 1 18 6 6 LEU C C 175.630 0.050 1 19 6 6 LEU CB C 40.444 0.050 1 20 6 6 LEU N N 126.136 0.050 1 21 7 7 PHE H H 9.538 0.005 1 22 7 7 PHE C C 177.891 0.050 1 23 7 7 PHE CB C 40.426 0.050 1 24 7 7 PHE N N 122.848 0.050 1 25 8 8 ASP H H 7.437 0.005 1 26 8 8 ASP C C 172.175 0.050 1 27 8 8 ASP CB C 44.011 0.050 1 28 8 8 ASP N N 122.362 0.050 1 29 9 9 LEU H H 7.477 0.005 1 30 9 9 LEU C C 179.218 0.050 1 31 9 9 LEU CB C 44.187 0.050 1 32 9 9 LEU N N 119.114 0.050 1 33 10 10 ASP H H 9.283 0.005 1 34 10 10 ASP C C 176.972 0.050 1 35 10 10 ASP CB C 38.444 0.050 1 36 10 10 ASP N N 123.986 0.050 1 37 11 11 GLY H H 8.977 0.005 1 38 11 11 GLY C C 171.363 0.050 1 39 11 11 GLY N N 116.806 0.050 1 40 12 12 VAL H H 7.580 0.005 1 41 12 12 VAL C C 173.373 0.050 1 42 12 12 VAL CB C 33.181 0.050 1 43 12 12 VAL N N 118.878 0.050 1 44 13 13 ILE H H 8.480 0.005 1 45 13 13 ILE C C 175.245 0.050 1 46 13 13 ILE CB C 38.036 0.050 1 47 13 13 ILE N N 115.385 0.050 1 48 14 14 THR H H 7.196 0.005 1 49 14 14 THR C C 173.155 0.050 1 50 14 14 THR CB C 67.691 0.050 1 51 14 14 THR N N 110.280 0.050 1 52 15 15 ASP H H 8.017 0.005 1 53 15 15 ASP C C 177.093 0.050 1 54 15 15 ASP CB C 39.911 0.050 1 55 15 15 ASP N N 128.268 0.050 1 56 16 16 THR H H 7.747 0.005 1 57 16 16 THR C C 178.843 0.050 1 58 16 16 THR CB C 66.105 0.050 1 59 16 16 THR N N 108.688 0.050 1 60 17 17 ALA H H 7.292 0.005 1 61 17 17 ALA C C 181.585 0.050 1 62 17 17 ALA CB C 16.592 0.050 1 63 17 17 ALA N N 124.703 0.050 1 64 18 18 GLU H H 8.103 0.005 1 65 18 18 GLU C C 178.138 0.050 1 66 18 18 GLU CB C 28.308 0.050 1 67 18 18 GLU N N 122.461 0.050 1 68 19 19 TYR H H 6.544 0.005 1 69 19 19 TYR C C 177.939 0.050 1 70 19 19 TYR CB C 36.510 0.050 1 71 19 19 TYR N N 118.220 0.050 1 72 20 20 HIS H H 8.512 0.005 1 73 20 20 HIS C C 177.594 0.050 1 74 20 20 HIS CB C 31.124 0.050 1 75 20 20 HIS N N 121.047 0.050 1 76 21 21 PHE H H 7.791 0.005 1 77 21 21 PHE C C 176.614 0.050 1 78 21 21 PHE CB C 37.686 0.050 1 79 21 21 PHE N N 117.844 0.050 1 80 22 22 ARG H H 8.406 0.005 1 81 22 22 ARG C C 179.914 0.050 1 82 22 22 ARG CB C 29.773 0.050 1 83 22 22 ARG N N 117.858 0.050 1 84 23 23 ALA H H 8.581 0.005 1 85 23 23 ALA C C 180.390 0.050 1 86 23 23 ALA CB C 17.997 0.050 1 87 23 23 ALA N N 122.069 0.050 1 88 24 24 TRP H H 8.810 0.005 1 89 24 24 TRP C C 178.553 0.050 1 90 24 24 TRP CB C 29.191 0.050 1 91 24 24 TRP N N 121.899 0.050 1 92 25 25 LYS H H 8.922 0.005 1 93 25 25 LYS C C 178.036 0.050 1 94 25 25 LYS CB C 31.711 0.050 1 95 25 25 LYS N N 120.936 0.050 1 96 26 26 ALA H H 7.694 0.005 1 97 26 26 ALA C C 180.737 0.050 1 98 26 26 ALA CB C 17.181 0.050 1 99 26 26 ALA N N 119.735 0.050 1 100 27 27 LEU H H 7.568 0.005 1 101 27 27 LEU C C 178.697 0.050 1 102 27 27 LEU CB C 40.795 0.050 1 103 27 27 LEU N N 121.022 0.050 1 104 28 28 ALA H H 8.632 0.005 1 105 28 28 ALA C C 179.915 0.050 1 106 28 28 ALA CB C 17.589 0.050 1 107 28 28 ALA N N 121.120 0.050 1 108 29 29 GLU H H 8.316 0.005 1 109 29 29 GLU C C 180.644 0.050 1 110 29 29 GLU CB C 28.316 0.050 1 111 29 29 GLU N N 116.984 0.050 1 112 30 30 GLU H H 7.915 0.005 1 113 30 30 GLU C C 178.925 0.050 1 114 30 30 GLU CB C 28.964 0.050 1 115 30 30 GLU N N 121.773 0.050 1 116 31 31 ILE H H 7.600 0.005 1 117 31 31 ILE C C 175.928 0.050 1 118 31 31 ILE CB C 36.869 0.050 1 119 31 31 ILE N N 111.701 0.050 1 120 32 32 GLY H H 7.544 0.005 1 121 32 32 GLY C C 174.462 0.050 1 122 32 32 GLY N N 109.549 0.050 1 123 33 33 ILE H H 8.394 0.005 1 124 33 33 ILE C C 175.050 0.050 1 125 33 33 ILE CB C 38.388 0.050 1 126 33 33 ILE N N 123.219 0.050 1 127 34 34 ASN H H 8.473 0.005 1 128 34 34 ASN C C 175.368 0.050 1 129 34 34 ASN CB C 39.504 0.050 1 130 34 34 ASN N N 126.232 0.050 1 131 35 35 GLY H H 7.762 0.005 1 132 35 35 GLY C C 174.048 0.050 1 133 35 35 GLY N N 106.930 0.050 1 134 36 36 VAL H H 8.641 0.005 1 135 36 36 VAL C C 173.584 0.050 1 136 36 36 VAL CB C 27.961 0.050 1 137 36 36 VAL N N 123.290 0.050 1 138 37 37 ASP H H 7.491 0.005 1 139 37 37 ASP C C 176.379 0.050 1 140 37 37 ASP CB C 41.786 0.050 1 141 37 37 ASP N N 126.781 0.050 1 142 38 38 ARG H H 8.392 0.005 1 143 38 38 ARG C C 178.639 0.050 1 144 38 38 ARG CB C 28.484 0.050 1 145 38 38 ARG N N 118.883 0.050 1 146 39 39 GLN H H 7.988 0.005 1 147 39 39 GLN C C 179.960 0.050 1 148 39 39 GLN CB C 27.488 0.050 1 149 39 39 GLN N N 119.927 0.050 1 150 40 40 PHE H H 8.885 0.005 1 151 40 40 PHE C C 177.786 0.050 1 152 40 40 PHE CB C 39.044 0.050 1 153 40 40 PHE N N 125.370 0.050 1 154 41 41 ASN H H 8.619 0.005 1 155 41 41 ASN C C 177.178 0.050 1 156 41 41 ASN CB C 39.271 0.050 1 157 41 41 ASN N N 114.885 0.050 1 158 42 42 GLU H H 7.426 0.005 1 159 42 42 GLU C C 179.593 0.050 1 160 42 42 GLU CB C 28.366 0.050 1 161 42 42 GLU N N 118.386 0.050 1 162 43 43 GLN H H 8.089 0.005 1 163 43 43 GLN C C 174.771 0.050 1 164 43 43 GLN CB C 28.074 0.050 1 165 43 43 GLN N N 116.905 0.050 1 166 44 44 LEU H H 7.038 0.005 1 167 44 44 LEU C C 179.447 0.050 1 168 44 44 LEU CB C 40.210 0.050 1 169 44 44 LEU N N 115.851 0.050 1 170 45 45 LYS H H 7.207 0.005 1 171 45 45 LYS C C 176.618 0.050 1 172 45 45 LYS CB C 32.589 0.050 1 173 45 45 LYS N N 122.399 0.050 1 174 46 46 GLY H H 8.623 0.005 1 175 46 46 GLY C C 172.949 0.050 1 176 46 46 GLY N N 113.431 0.050 1 177 47 47 VAL H H 6.933 0.005 1 178 47 47 VAL C C 176.261 0.050 1 179 47 47 VAL CB C 30.779 0.050 1 180 47 47 VAL N N 116.736 0.050 1 181 48 48 SER H H 8.636 0.005 1 182 48 48 SER C C 174.154 0.050 1 183 48 48 SER CB C 64.872 0.050 1 184 48 48 SER N N 119.142 0.050 1 185 49 49 ARG H H 8.811 0.005 1 186 49 49 ARG C C 178.038 0.050 1 187 49 49 ARG CB C 31.366 0.050 1 188 49 49 ARG N N 126.505 0.050 1 189 50 50 GLU H H 9.029 0.005 1 190 50 50 GLU C C 178.451 0.050 1 191 50 50 GLU CB C 27.726 0.050 1 192 50 50 GLU N N 117.505 0.050 1 193 51 51 ASP H H 7.960 0.005 1 194 51 51 ASP C C 179.085 0.050 1 195 51 51 ASP CB C 39.617 0.050 1 196 51 51 ASP N N 120.054 0.050 1 197 52 52 SER H H 8.354 0.005 1 198 52 52 SER C C 173.842 0.050 1 199 52 52 SER CB C 63.173 0.050 1 200 52 52 SER N N 118.660 0.050 1 201 53 53 LEU H H 7.156 0.005 1 202 53 53 LEU C C 178.135 0.050 1 203 53 53 LEU CB C 38.683 0.050 1 204 53 53 LEU N N 121.404 0.050 1 205 54 54 GLN H H 8.203 0.005 1 206 54 54 GLN C C 177.404 0.050 1 207 54 54 GLN CB C 28.246 0.050 1 208 54 54 GLN N N 117.688 0.050 1 209 55 55 LYS H H 7.644 0.005 1 210 55 55 LYS C C 179.844 0.050 1 211 55 55 LYS CB C 31.886 0.050 1 212 55 55 LYS N N 117.947 0.050 1 213 56 56 ILE H H 7.504 0.005 1 214 56 56 ILE C C 177.199 0.050 1 215 56 56 ILE CB C 37.684 0.050 1 216 56 56 ILE N N 120.976 0.050 1 217 57 57 LEU H H 8.437 0.005 1 218 57 57 LEU C C 180.957 0.050 1 219 57 57 LEU CB C 38.917 0.050 1 220 57 57 LEU N N 119.331 0.050 1 221 58 58 ASP H H 8.641 0.005 1 222 58 58 ASP C C 179.445 0.050 1 223 58 58 ASP CB C 39.446 0.050 1 224 58 58 ASP N N 119.449 0.050 1 225 59 59 LEU H H 7.653 0.005 1 226 59 59 LEU C C 178.126 0.050 1 227 59 59 LEU CB C 40.731 0.050 1 228 59 59 LEU N N 123.571 0.050 1 229 60 60 ALA H H 6.990 0.005 1 230 60 60 ALA C C 176.089 0.050 1 231 60 60 ALA CB C 20.398 0.050 1 232 60 60 ALA N N 118.782 0.050 1 233 61 61 ASP H H 7.883 0.005 1 234 61 61 ASP C C 174.662 0.050 1 235 61 61 ASP CB C 39.389 0.050 1 236 61 61 ASP N N 120.897 0.050 1 237 62 62 LYS H H 7.875 0.005 1 238 62 62 LYS C C 175.407 0.050 1 239 62 62 LYS CB C 33.293 0.050 1 240 62 62 LYS N N 118.839 0.050 1 241 63 63 LYS H H 8.497 0.005 1 242 63 63 LYS C C 176.348 0.050 1 243 63 63 LYS CB C 32.235 0.050 1 244 63 63 LYS N N 126.817 0.050 1 245 64 64 VAL H H 8.410 0.005 1 246 64 64 VAL C C 175.825 0.050 1 247 64 64 VAL CB C 34.465 0.050 1 248 64 64 VAL N N 116.627 0.050 1 249 65 65 SER H H 9.000 0.005 1 250 65 65 SER C C 174.616 0.050 1 251 65 65 SER CB C 64.754 0.050 1 252 65 65 SER N N 119.569 0.050 1 253 66 66 ALA H H 8.903 0.005 1 254 66 66 ALA C C 181.021 0.050 1 255 66 66 ALA CB C 17.232 0.050 1 256 66 66 ALA N N 124.309 0.050 1 257 67 67 GLU H H 8.582 0.005 1 258 67 67 GLU C C 179.432 0.050 1 259 67 67 GLU CB C 28.486 0.050 1 260 67 67 GLU N N 118.045 0.050 1 261 68 68 GLU H H 7.883 0.005 1 262 68 68 GLU C C 178.500 0.050 1 263 68 68 GLU CB C 29.484 0.050 1 264 68 68 GLU N N 122.961 0.050 1 265 69 69 PHE H H 8.837 0.005 1 266 69 69 PHE C C 176.714 0.050 1 267 69 69 PHE CB C 38.917 0.050 1 268 69 69 PHE N N 121.576 0.050 1 269 70 70 LYS H H 7.659 0.005 1 270 70 70 LYS C C 180.059 0.050 1 271 70 70 LYS CB C 31.825 0.050 1 272 70 70 LYS N N 116.377 0.050 1 273 71 71 GLU H H 7.797 0.005 1 274 71 71 GLU C C 178.914 0.050 1 275 71 71 GLU CB C 28.428 0.050 1 276 71 71 GLU N N 121.183 0.050 1 277 72 72 LEU H H 8.413 0.005 1 278 72 72 LEU C C 178.240 0.050 1 279 72 72 LEU CB C 41.727 0.050 1 280 72 72 LEU N N 122.110 0.050 1 281 73 73 ALA H H 7.730 0.005 1 282 73 73 ALA C C 179.087 0.050 1 283 73 73 ALA CB C 16.008 0.050 1 284 73 73 ALA N N 120.701 0.050 1 285 74 74 LYS H H 7.676 0.005 1 286 74 74 LYS C C 178.198 0.050 1 287 74 74 LYS CB C 31.473 0.050 1 288 74 74 LYS N N 119.040 0.050 1 289 75 75 ARG H H 8.325 0.005 1 290 75 75 ARG C C 179.540 0.050 1 291 75 75 ARG CB C 29.488 0.050 1 292 75 75 ARG N N 121.493 0.050 1 293 76 76 LYS H H 7.805 0.005 1 294 76 76 LYS C C 179.131 0.050 1 295 76 76 LYS CB C 29.543 0.050 1 296 76 76 LYS N N 119.624 0.050 1 297 77 77 ASN H H 8.009 0.005 1 298 77 77 ASN C C 175.825 0.050 1 299 77 77 ASN CB C 38.154 0.050 1 300 77 77 ASN N N 118.744 0.050 1 301 78 78 ASP H H 8.999 0.005 1 302 78 78 ASP C C 179.235 0.050 1 303 78 78 ASP CB C 39.212 0.050 1 304 78 78 ASP N N 119.565 0.050 1 305 79 79 ASN H H 7.513 0.005 1 306 79 79 ASN C C 176.927 0.050 1 307 79 79 ASN CB C 37.689 0.050 1 308 79 79 ASN N N 119.051 0.050 1 309 80 80 TYR H H 8.590 0.005 1 310 80 80 TYR C C 176.721 0.050 1 311 80 80 TYR CB C 38.623 0.050 1 312 80 80 TYR N N 123.219 0.050 1 313 81 81 VAL H H 8.941 0.005 1 314 81 81 VAL C C 179.028 0.050 1 315 81 81 VAL CB C 30.479 0.050 1 316 81 81 VAL N N 118.553 0.050 1 317 82 82 LYS H H 7.014 0.005 1 318 82 82 LYS C C 179.488 0.050 1 319 82 82 LYS CB C 31.180 0.050 1 320 82 82 LYS N N 118.965 0.050 1 321 83 83 MET H H 7.525 0.005 1 322 83 83 MET C C 178.235 0.050 1 323 83 83 MET CB C 31.828 0.050 1 324 83 83 MET N N 118.411 0.050 1 325 84 84 ILE H H 7.051 0.005 1 326 84 84 ILE C C 176.661 0.050 1 327 84 84 ILE CB C 36.628 0.050 1 328 84 84 ILE N N 108.906 0.050 1 329 85 85 GLN H H 6.930 0.005 1 330 85 85 GLN C C 176.394 0.050 1 331 85 85 GLN CB C 28.074 0.050 1 332 85 85 GLN N N 118.036 0.050 1 333 86 86 ASP H H 7.746 0.005 1 334 86 86 ASP C C 176.511 0.050 1 335 86 86 ASP CB C 40.675 0.050 1 336 86 86 ASP N N 115.492 0.050 1 337 87 87 VAL H H 7.095 0.005 1 338 87 87 VAL C C 174.511 0.050 1 339 87 87 VAL CB C 30.657 0.050 1 340 87 87 VAL N N 123.808 0.050 1 341 88 88 SER H H 9.404 0.005 1 342 88 88 SER N N 126.678 0.050 1 343 89 89 PRO C C 177.767 0.050 1 344 89 89 PRO CB C 30.772 0.050 1 345 90 90 ALA H H 7.681 0.005 1 346 90 90 ALA C C 178.010 0.050 1 347 90 90 ALA CB C 17.645 0.050 1 348 90 90 ALA N N 119.334 0.050 1 349 91 91 ASP H H 8.018 0.005 1 350 91 91 ASP C C 177.503 0.050 1 351 91 91 ASP CB C 41.261 0.050 1 352 91 91 ASP N N 114.917 0.050 1 353 92 92 VAL H H 7.183 0.005 1 354 92 92 VAL C C 176.676 0.050 1 355 92 92 VAL CB C 31.120 0.050 1 356 92 92 VAL N N 125.685 0.050 1 357 93 93 TYR H H 8.856 0.005 1 358 93 93 TYR N N 130.900 0.050 1 359 94 94 PRO C C 177.242 0.050 1 360 94 94 PRO CB C 31.356 0.050 1 361 95 95 GLY H H 8.358 0.005 1 362 95 95 GLY C C 176.240 0.050 1 363 95 95 GLY N N 111.551 0.050 1 364 96 96 ILE H H 7.165 0.005 1 365 96 96 ILE C C 176.975 0.050 1 366 96 96 ILE CB C 33.815 0.050 1 367 96 96 ILE N N 121.636 0.050 1 368 97 97 LEU H H 8.725 0.005 1 369 97 97 LEU C C 178.084 0.050 1 370 97 97 LEU CB C 40.379 0.050 1 371 97 97 LEU N N 121.395 0.050 1 372 98 98 GLN H H 8.620 0.005 1 373 98 98 GLN C C 177.397 0.050 1 374 98 98 GLN CB C 27.666 0.050 1 375 98 98 GLN N N 117.763 0.050 1 376 99 99 LEU H H 7.846 0.005 1 377 99 99 LEU C C 178.495 0.050 1 378 99 99 LEU CB C 39.858 0.050 1 379 99 99 LEU N N 120.000 0.050 1 380 100 100 LEU H H 8.269 0.005 1 381 100 100 LEU C C 179.170 0.050 1 382 100 100 LEU CB C 39.621 0.050 1 383 100 100 LEU N N 119.247 0.050 1 384 101 101 LYS H H 7.930 0.005 1 385 101 101 LYS C C 180.230 0.050 1 386 101 101 LYS CB C 31.995 0.050 1 387 101 101 LYS N N 117.973 0.050 1 388 102 102 ASP H H 8.883 0.005 1 389 102 102 ASP C C 179.851 0.050 1 390 102 102 ASP CB C 39.559 0.050 1 391 102 102 ASP N N 122.912 0.050 1 392 103 103 LEU H H 9.324 0.005 1 393 103 103 LEU C C 179.029 0.050 1 394 103 103 LEU CB C 39.680 0.050 1 395 103 103 LEU N N 123.844 0.050 1 396 104 104 ARG H H 8.180 0.005 1 397 104 104 ARG C C 181.907 0.050 1 398 104 104 ARG CB C 28.722 0.050 1 399 104 104 ARG N N 119.941 0.050 1 400 105 105 SER H H 8.729 0.005 1 401 105 105 SER C C 175.211 0.050 1 402 105 105 SER CB C 62.286 0.050 1 403 105 105 SER N N 117.422 0.050 1 404 106 106 ASN H H 7.426 0.005 1 405 106 106 ASN C C 172.417 0.050 1 406 106 106 ASN CB C 39.444 0.050 1 407 106 106 ASN N N 118.383 0.050 1 408 107 107 LYS H H 7.889 0.005 1 409 107 107 LYS C C 175.098 0.050 1 410 107 107 LYS CB C 27.429 0.050 1 411 107 107 LYS N N 115.050 0.050 1 412 108 108 ILE H H 8.019 0.005 1 413 108 108 ILE C C 175.769 0.050 1 414 108 108 ILE CB C 37.098 0.050 1 415 108 108 ILE N N 122.583 0.050 1 416 109 109 LYS H H 7.648 0.005 1 417 109 109 LYS C C 175.741 0.050 1 418 109 109 LYS CB C 32.647 0.050 1 419 109 109 LYS N N 125.069 0.050 1 420 110 110 ILE H H 9.327 0.005 1 421 110 110 ILE C C 175.870 0.050 1 422 110 110 ILE CB C 40.083 0.050 1 423 110 110 ILE N N 122.042 0.050 1 424 111 111 ALA H H 8.869 0.005 1 425 111 111 ALA C C 175.987 0.050 1 426 111 111 ALA CB C 23.509 0.050 1 427 111 111 ALA N N 128.301 0.050 1 428 112 112 LEU H H 8.615 0.005 1 429 112 112 LEU C C 173.790 0.050 1 430 112 112 LEU CB C 42.727 0.050 1 431 112 112 LEU N N 124.372 0.050 1 432 113 113 ALA H H 9.115 0.005 1 433 113 113 ALA C C 174.155 0.050 1 434 113 113 ALA CB C 18.993 0.050 1 435 113 113 ALA N N 135.191 0.050 1 436 114 114 SER H H 7.391 0.005 1 437 114 114 SER C C 175.987 0.050 1 438 114 114 SER CB C 64.770 0.050 1 439 114 114 SER N N 111.900 0.050 1 440 115 115 ALA H H 9.880 0.005 1 441 115 115 ALA C C 176.775 0.050 1 442 115 115 ALA CB C 19.289 0.050 1 443 115 115 ALA N N 128.912 0.050 1 444 116 116 SER H H 8.368 0.005 1 445 116 116 SER C C 179.968 0.050 1 446 116 116 SER CB C 62.996 0.050 1 447 116 116 SER N N 112.053 0.050 1 448 117 117 LYS H H 11.040 0.005 1 449 117 117 LYS C C 177.872 0.050 1 450 117 117 LYS CB C 31.187 0.050 1 451 117 117 LYS N N 136.871 0.050 1 452 118 118 ASN H H 8.333 0.005 1 453 118 118 ASN C C 174.304 0.050 1 454 118 118 ASN CB C 39.914 0.050 1 455 118 118 ASN N N 118.238 0.050 1 456 119 119 GLY H H 7.559 0.005 1 457 119 119 GLY N N 106.849 0.050 1 458 120 120 PRO C C 179.228 0.050 1 459 120 120 PRO CB C 30.768 0.050 1 460 121 121 PHE H H 7.664 0.005 1 461 121 121 PHE C C 177.145 0.050 1 462 121 121 PHE CB C 38.564 0.050 1 463 121 121 PHE N N 119.331 0.050 1 464 122 122 LEU H H 7.680 0.005 1 465 122 122 LEU C C 178.813 0.050 1 466 122 122 LEU CB C 41.493 0.050 1 467 122 122 LEU N N 121.145 0.050 1 468 123 123 LEU H H 8.401 0.005 1 469 123 123 LEU C C 179.188 0.050 1 470 123 123 LEU CB C 40.557 0.050 1 471 123 123 LEU N N 117.593 0.050 1 472 124 124 GLU H H 7.580 0.005 1 473 124 124 GLU C C 180.797 0.050 1 474 124 124 GLU CB C 28.369 0.050 1 475 124 124 GLU N N 119.878 0.050 1 476 125 125 ARG H H 8.068 0.005 1 477 125 125 ARG C C 178.601 0.050 1 478 125 125 ARG CB C 28.427 0.050 1 479 125 125 ARG N N 121.117 0.050 1 480 126 126 MET H H 7.424 0.005 1 481 126 126 MET C C 173.636 0.050 1 482 126 126 MET CB C 32.469 0.050 1 483 126 126 MET N N 113.376 0.050 1 484 127 127 ASN H H 7.961 0.005 1 485 127 127 ASN C C 175.806 0.050 1 486 127 127 ASN CB C 36.391 0.050 1 487 127 127 ASN N N 117.271 0.050 1 488 128 128 LEU H H 8.680 0.005 1 489 128 128 LEU C C 178.064 0.050 1 490 128 128 LEU CB C 44.947 0.050 1 491 128 128 LEU N N 114.380 0.050 1 492 129 129 THR H H 7.433 0.005 1 493 129 129 THR C C 176.398 0.050 1 494 129 129 THR CB C 68.389 0.050 1 495 129 129 THR N N 115.711 0.050 1 496 130 130 GLY H H 8.574 0.005 1 497 130 130 GLY C C 175.052 0.050 1 498 130 130 GLY N N 106.236 0.050 1 499 131 131 TYR H H 7.768 0.005 1 500 131 131 TYR C C 174.579 0.050 1 501 131 131 TYR CB C 38.564 0.050 1 502 131 131 TYR N N 116.663 0.050 1 503 132 132 PHE H H 7.342 0.005 1 504 132 132 PHE C C 175.890 0.050 1 505 132 132 PHE CB C 38.799 0.050 1 506 132 132 PHE N N 115.370 0.050 1 507 133 133 ASP H H 9.200 0.005 1 508 133 133 ASP C C 176.413 0.050 1 509 133 133 ASP CB C 42.136 0.050 1 510 133 133 ASP N N 125.118 0.050 1 511 134 134 ALA H H 7.622 0.005 1 512 134 134 ALA C C 175.456 0.050 1 513 134 134 ALA CB C 23.503 0.050 1 514 134 134 ALA N N 115.597 0.050 1 515 135 135 ILE H H 8.630 0.005 1 516 135 135 ILE C C 175.822 0.050 1 517 135 135 ILE CB C 39.972 0.050 1 518 135 135 ILE N N 122.402 0.050 1 519 136 136 ALA H H 8.508 0.005 1 520 136 136 ALA C C 175.785 0.050 1 521 136 136 ALA CB C 17.703 0.050 1 522 136 136 ALA N N 130.787 0.050 1 523 137 137 ASP H H 8.500 0.005 1 524 137 137 ASP N N 123.622 0.050 1 525 138 138 PRO C C 178.167 0.050 1 526 138 138 PRO CB C 31.654 0.050 1 527 139 139 ALA H H 8.502 0.005 1 528 139 139 ALA C C 178.874 0.050 1 529 139 139 ALA CB C 17.998 0.050 1 530 139 139 ALA N N 121.175 0.050 1 531 140 140 GLU H H 7.414 0.005 1 532 140 140 GLU C C 176.718 0.050 1 533 140 140 GLU CB C 29.835 0.050 1 534 140 140 GLU N N 116.776 0.050 1 535 141 141 VAL H H 7.169 0.005 1 536 141 141 VAL C C 175.569 0.050 1 537 141 141 VAL CB C 31.533 0.050 1 538 141 141 VAL N N 117.204 0.050 1 539 142 142 ALA H H 8.313 0.005 1 540 142 142 ALA C C 177.761 0.050 1 541 142 142 ALA CB C 18.229 0.050 1 542 142 142 ALA N N 125.208 0.050 1 543 143 143 ALA H H 7.414 0.005 1 544 143 143 ALA C C 176.320 0.050 1 545 143 143 ALA CB C 20.221 0.050 1 546 143 143 ALA N N 120.316 0.050 1 547 144 144 SER H H 8.520 0.005 1 548 144 144 SER C C 176.779 0.050 1 549 144 144 SER CB C 63.525 0.050 1 550 144 144 SER N N 118.093 0.050 1 551 145 145 LYS H H 9.324 0.005 1 552 145 145 LYS N N 129.099 0.050 1 553 146 146 PRO C C 176.205 0.050 1 554 146 146 PRO CB C 35.288 0.050 1 555 147 147 ALA H H 9.197 0.005 1 556 147 147 ALA N N 131.922 0.050 1 557 148 148 PRO C C 177.209 0.050 1 558 148 148 PRO CB C 32.020 0.050 1 559 149 149 ASP H H 9.292 0.005 1 560 149 149 ASP C C 177.975 0.050 1 561 149 149 ASP CB C 38.976 0.050 1 562 149 149 ASP N N 121.027 0.050 1 563 150 150 ILE H H 9.685 0.005 1 564 150 150 ILE C C 175.824 0.050 1 565 150 150 ILE CB C 37.275 0.050 1 566 150 150 ILE N N 120.539 0.050 1 567 151 151 PHE H H 7.235 0.005 1 568 151 151 PHE C C 177.661 0.050 1 569 151 151 PHE CB C 38.215 0.050 1 570 151 151 PHE N N 120.889 0.050 1 571 152 152 ILE H H 7.726 0.005 1 572 152 152 ILE C C 177.826 0.050 1 573 152 152 ILE CB C 37.398 0.050 1 574 152 152 ILE N N 120.409 0.050 1 575 153 153 ALA H H 8.454 0.005 1 576 153 153 ALA C C 180.962 0.050 1 577 153 153 ALA CB C 17.472 0.050 1 578 153 153 ALA N N 120.827 0.050 1 579 154 154 ALA H H 7.830 0.005 1 580 154 154 ALA C C 176.776 0.050 1 581 154 154 ALA CB C 17.883 0.050 1 582 154 154 ALA N N 122.414 0.050 1 583 155 155 ALA H H 7.630 0.005 1 584 155 155 ALA C C 179.757 0.050 1 585 155 155 ALA CB C 16.122 0.050 1 586 155 155 ALA N N 118.451 0.050 1 587 156 156 HIS H H 8.441 0.005 1 588 156 156 HIS C C 179.275 0.050 1 589 156 156 HIS CB C 28.253 0.050 1 590 156 156 HIS N N 116.381 0.050 1 591 157 157 ALA H H 8.239 0.005 1 592 157 157 ALA C C 179.195 0.050 1 593 157 157 ALA CB C 17.642 0.050 1 594 157 157 ALA N N 122.315 0.050 1 595 158 158 VAL H H 7.185 0.005 1 596 158 158 VAL C C 175.516 0.050 1 597 158 158 VAL CB C 30.478 0.050 1 598 158 158 VAL N N 107.446 0.050 1 599 159 159 GLY H H 7.741 0.005 1 600 159 159 GLY C C 174.620 0.050 1 601 159 159 GLY N N 110.164 0.050 1 602 160 160 VAL H H 7.641 0.005 1 603 160 160 VAL C C 174.252 0.050 1 604 160 160 VAL CB C 34.108 0.050 1 605 160 160 VAL N N 117.116 0.050 1 606 161 161 ALA H H 8.655 0.005 1 607 161 161 ALA N N 126.116 0.050 1 608 162 162 PRO C C 177.398 0.050 1 609 162 162 PRO CB C 30.770 0.050 1 610 163 163 SER H H 7.732 0.005 1 611 163 163 SER C C 175.920 0.050 1 612 163 163 SER CB C 61.834 0.050 1 613 163 163 SER N N 107.065 0.050 1 614 164 164 GLU H H 7.780 0.005 1 615 164 164 GLU C C 174.733 0.050 1 616 164 164 GLU CB C 29.307 0.050 1 617 164 164 GLU N N 121.817 0.050 1 618 165 165 SER H H 7.980 0.005 1 619 165 165 SER C C 172.092 0.050 1 620 165 165 SER CB C 65.225 0.050 1 621 165 165 SER N N 114.805 0.050 1 622 166 166 ILE H H 7.601 0.005 1 623 166 166 ILE C C 175.247 0.050 1 624 166 166 ILE CB C 40.735 0.050 1 625 166 166 ILE N N 121.791 0.050 1 626 167 167 GLY H H 8.784 0.005 1 627 167 167 GLY C C 170.481 0.050 1 628 167 167 GLY N N 112.912 0.050 1 629 168 168 LEU H H 7.782 0.005 1 630 168 168 LEU C C 175.623 0.050 1 631 168 168 LEU CB C 40.851 0.050 1 632 168 168 LEU N N 123.593 0.050 1 633 169 169 GLU H H 6.921 0.005 1 634 169 169 GLU C C 173.688 0.050 1 635 169 169 GLU CB C 39.390 0.050 1 636 169 169 GLU N N 123.760 0.050 1 637 170 170 ASP H H 8.445 0.005 1 638 170 170 ASP C C 173.682 0.050 1 639 170 170 ASP CB C 41.358 0.050 1 640 170 170 ASP N N 115.857 0.050 1 641 171 171 SER H H 8.111 0.005 1 642 171 171 SER C C 174.046 0.050 1 643 171 171 SER CB C 69.215 0.050 1 644 171 171 SER N N 114.864 0.050 1 645 172 172 GLN H H 9.710 0.005 1 646 172 172 GLN C C 179.696 0.050 1 647 172 172 GLN CB C 27.429 0.050 1 648 172 172 GLN N N 124.982 0.050 1 649 173 173 ALA H H 8.471 0.005 1 650 173 173 ALA C C 179.963 0.050 1 651 173 173 ALA CB C 17.115 0.050 1 652 173 173 ALA N N 120.867 0.050 1 653 174 174 GLY H H 8.599 0.005 1 654 174 174 GLY C C 175.785 0.050 1 655 174 174 GLY N N 107.318 0.050 1 656 175 175 ILE H H 8.500 0.005 1 657 175 175 ILE C C 177.816 0.050 1 658 175 175 ILE CB C 34.638 0.050 1 659 175 175 ILE N N 123.617 0.050 1 660 176 176 GLN H H 7.644 0.005 1 661 176 176 GLN C C 177.036 0.050 1 662 176 176 GLN CB C 27.139 0.050 1 663 176 176 GLN N N 120.281 0.050 1 664 177 177 ALA H H 7.761 0.005 1 665 177 177 ALA C C 179.795 0.050 1 666 177 177 ALA CB C 19.169 0.050 1 667 177 177 ALA N N 122.632 0.050 1 668 178 178 ILE H H 8.116 0.005 1 669 178 178 ILE C C 180.684 0.050 1 670 178 178 ILE CB C 36.340 0.050 1 671 178 178 ILE N N 117.885 0.050 1 672 179 179 LYS H H 8.457 0.005 1 673 179 179 LYS C C 180.984 0.050 1 674 179 179 LYS CB C 31.880 0.050 1 675 179 179 LYS N N 120.821 0.050 1 676 180 180 ASP H H 8.460 0.005 1 677 180 180 ASP C C 177.355 0.050 1 678 180 180 ASP CB C 38.742 0.050 1 679 180 180 ASP N N 118.866 0.050 1 680 181 181 SER H H 8.116 0.005 1 681 181 181 SER C C 173.888 0.050 1 682 181 181 SER CB C 64.286 0.050 1 683 181 181 SER N N 117.324 0.050 1 684 182 182 GLY H H 7.220 0.005 1 685 182 182 GLY C C 173.470 0.050 1 686 182 182 GLY N N 109.142 0.050 1 687 183 183 ALA H H 7.177 0.005 1 688 183 183 ALA C C 174.729 0.050 1 689 183 183 ALA CB C 19.516 0.050 1 690 183 183 ALA N N 124.293 0.050 1 691 184 184 LEU H H 8.069 0.005 1 692 184 184 LEU N N 122.728 0.050 1 693 185 185 PRO C C 176.394 0.050 1 694 185 185 PRO CB C 31.642 0.050 1 695 186 186 ILE H H 8.267 0.005 1 696 186 186 ILE C C 178.500 0.050 1 697 186 186 ILE CB C 38.213 0.050 1 698 186 186 ILE N N 119.366 0.050 1 699 187 187 GLY H H 8.918 0.005 1 700 187 187 GLY C C 171.378 0.050 1 701 187 187 GLY N N 116.346 0.050 1 702 188 188 VAL H H 8.082 0.005 1 703 188 188 VAL C C 173.907 0.050 1 704 188 188 VAL CB C 31.998 0.050 1 705 188 188 VAL N N 119.148 0.050 1 706 189 189 GLY H H 8.091 0.005 1 707 189 189 GLY C C 171.162 0.050 1 708 189 189 GLY N N 113.272 0.050 1 709 190 190 ARG H H 8.744 0.005 1 710 190 190 ARG N N 120.988 0.050 1 711 191 191 PRO C C 178.773 0.050 1 712 191 191 PRO CB C 30.945 0.050 1 713 192 192 GLU H H 9.629 0.005 1 714 192 192 GLU C C 176.814 0.050 1 715 192 192 GLU CB C 27.901 0.050 1 716 192 192 GLU N N 118.948 0.050 1 717 193 193 ASP H H 7.037 0.005 1 718 193 193 ASP C C 176.986 0.050 1 719 193 193 ASP CB C 41.609 0.050 1 720 193 193 ASP N N 114.997 0.050 1 721 194 194 LEU H H 7.673 0.005 1 722 194 194 LEU C C 176.557 0.050 1 723 194 194 LEU CB C 42.432 0.050 1 724 194 194 LEU N N 116.665 0.050 1 725 195 195 GLY H H 8.027 0.005 1 726 195 195 GLY C C 172.586 0.050 1 727 195 195 GLY N N 108.248 0.050 1 728 196 196 ASP H H 7.924 0.005 1 729 196 196 ASP C C 176.932 0.050 1 730 196 196 ASP CB C 41.084 0.050 1 731 196 196 ASP N N 116.855 0.050 1 732 197 197 ASP H H 8.932 0.005 1 733 197 197 ASP C C 175.403 0.050 1 734 197 197 ASP CB C 39.621 0.050 1 735 197 197 ASP N N 117.321 0.050 1 736 198 198 ILE H H 6.771 0.005 1 737 198 198 ILE C C 175.399 0.050 1 738 198 198 ILE CB C 40.557 0.050 1 739 198 198 ILE N N 113.429 0.050 1 740 199 199 VAL H H 8.940 0.005 1 741 199 199 VAL C C 174.249 0.050 1 742 199 199 VAL CB C 30.300 0.050 1 743 199 199 VAL N N 125.441 0.050 1 744 200 200 ILE H H 7.960 0.005 1 745 200 200 ILE C C 176.044 0.050 1 746 200 200 ILE CB C 40.910 0.050 1 747 200 200 ILE N N 126.796 0.050 1 748 201 201 VAL H H 8.782 0.005 1 749 201 201 VAL N N 120.631 0.050 1 750 202 202 PRO C C 177.085 0.050 1 751 202 202 PRO CB C 31.063 0.050 1 752 203 203 ASP H H 6.797 0.005 1 753 203 203 ASP C C 175.568 0.050 1 754 203 203 ASP CB C 41.379 0.050 1 755 203 203 ASP N N 110.336 0.050 1 756 204 204 THR H H 8.164 0.005 1 757 204 204 THR C C 176.664 0.050 1 758 204 204 THR CB C 68.744 0.050 1 759 204 204 THR N N 109.219 0.050 1 760 205 205 SER H H 8.788 0.005 1 761 205 205 SER C C 175.678 0.050 1 762 205 205 SER CB C 61.888 0.050 1 763 205 205 SER N N 120.232 0.050 1 764 206 206 HIS H H 7.041 0.005 1 765 206 206 HIS C C 176.410 0.050 1 766 206 206 HIS CB C 29.664 0.050 1 767 206 206 HIS N N 117.439 0.050 1 768 207 207 TYR H H 7.748 0.005 1 769 207 207 TYR C C 173.576 0.050 1 770 207 207 TYR CB C 35.167 0.050 1 771 207 207 TYR N N 120.257 0.050 1 772 208 208 THR H H 7.342 0.005 1 773 208 208 THR C C 174.787 0.050 1 774 208 208 THR CB C 71.093 0.050 1 775 208 208 THR N N 114.278 0.050 1 776 209 209 LEU H H 9.480 0.005 1 777 209 209 LEU C C 177.865 0.050 1 778 209 209 LEU CB C 39.792 0.050 1 779 209 209 LEU N N 125.241 0.050 1 780 210 210 GLU H H 8.545 0.005 1 781 210 210 GLU C C 178.811 0.050 1 782 210 210 GLU CB C 28.549 0.050 1 783 210 210 GLU N N 116.727 0.050 1 784 211 211 PHE H H 8.163 0.005 1 785 211 211 PHE C C 176.782 0.050 1 786 211 211 PHE CB C 39.443 0.050 1 787 211 211 PHE N N 122.409 0.050 1 788 212 212 LEU H H 8.357 0.005 1 789 212 212 LEU C C 179.076 0.050 1 790 212 212 LEU CB C 39.860 0.050 1 791 212 212 LEU N N 119.743 0.050 1 792 213 213 LYS H H 8.353 0.005 1 793 213 213 LYS C C 178.172 0.050 1 794 213 213 LYS CB C 32.003 0.050 1 795 213 213 LYS N N 116.288 0.050 1 796 214 214 GLU H H 7.782 0.005 1 797 214 214 GLU C C 179.601 0.050 1 798 214 214 GLU CB C 28.721 0.050 1 799 214 214 GLU N N 120.545 0.050 1 800 215 215 VAL H H 8.242 0.005 1 801 215 215 VAL C C 178.441 0.050 1 802 215 215 VAL CB C 30.713 0.050 1 803 215 215 VAL N N 120.547 0.050 1 804 216 216 TRP H H 8.425 0.005 1 805 216 216 TRP C C 178.654 0.050 1 806 216 216 TRP CB C 28.893 0.050 1 807 216 216 TRP N N 120.773 0.050 1 808 217 217 LEU H H 8.172 0.005 1 809 217 217 LEU C C 179.916 0.050 1 810 217 217 LEU CB C 40.956 0.050 1 811 217 217 LEU N N 117.128 0.050 1 812 218 218 GLN H H 7.824 0.005 1 813 218 218 GLN C C 177.725 0.050 1 814 218 218 GLN CB C 27.959 0.050 1 815 218 218 GLN N N 118.363 0.050 1 816 219 219 LYS H H 7.524 0.005 1 817 219 219 LYS C C 176.584 0.050 1 818 219 219 LYS CB C 31.360 0.050 1 819 219 219 LYS N N 117.908 0.050 1 820 220 220 GLN H H 7.624 0.005 1 821 220 220 GLN C C 175.086 0.050 1 822 220 220 GLN CB C 27.785 0.050 1 823 220 220 GLN N N 119.913 0.050 1 824 221 221 LYS H H 7.533 0.005 1 825 221 221 LYS N N 127.436 0.050 1 stop_ save_ save_assigned_chem_shift_list_1_3 _Saveframe_category assigned_chemical_shifts _Details ; Backbone 1H, 15N, 13C chemical shifts for beta phosphoglucomutase in complex with glucose-6-phosphate and AlF4- in a closed conformation forming a transition state analogue ; loop_ _Software_label $Felix stop_ loop_ _Experiment_label '2D 1H-15N TROSY' '3D TROSY HNCO' '3D TROSY HN(COCA)CB' stop_ loop_ _Sample_label $sample_2H15N13C 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 1 1 ALF F1 F -137.030 0.005 1 2 1 1 ALF F2 F -130.660 0.005 1 3 1 1 ALF F3 F -144.000 0.005 1 4 1 1 ALF F4 F -140.670 0.005 1 stop_ save_