data_17852 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N, 13C assignments for beta phosphoglucomutase in a ternary complex with glucose-6-phosphate and BeF3- ; _BMRB_accession_number 17852 _BMRB_flat_file_name bmr17852.str _Entry_type original _Submission_date 2011-08-10 _Accession_date 2011-08-10 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Baxter Nicola J. . 2 Griffin Joanna L. . 3 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" 200 "13C chemical shifts" 634 "15N chemical shifts" 200 "19F chemical shifts" 2 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-06-01 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 17851 'Backbone 1H, 15N, 13C assignments for beta phosphoglucomutase in a binary complex with BeF3-' 7234 'Backbone 1H, 15N, 13C assignments for beta phosphoglucomutase in a ternary complex with glucose-6-phosphate and MgF3-' stop_ _Original_release_date 2012-06-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Near attack conformers dominate beta-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22505741 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Griffin Joanna L. . 2 Bowler Matthew W. . 3 Baxter Nicola J. . 4 Leigh Katherine N. . 5 Dannatt Hugh R.W. . 6 Hounslow Andrea M. . 7 Blackburn 'G. Michael' . . 8 Webster 'Charles Edwin' . . 9 Cliff Matthew J. . 10 Waltho Jonathan P. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U. S. A.' _Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Journal_volume 109 _Journal_issue 18 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6910 _Page_last 6915 _Year 2012 _Details . loop_ _Keyword 'beta phosphoglucomutase' 'ground state analogues' 'near attack conformers' 'phosphoryl transfer' trifluoroberyllate stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'beta phosphoglucomutase in a ternary complex with glucose-6-phosphate and trifluoroberyllate' _Enzyme_commission_number 5.4.2.6 loop_ _Mol_system_component_name _Mol_label 'phosphoglucomutase ground state analogue' $beta_phosphoglucomutase trifluoroberyllate_ion $BEF magnesium_ion $MG glucose-6-phosphate $BG6 stop_ _System_molecular_weight 25000 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'beta phosphoglucomutase in a ternary complex with glucose-6-phosphate and trifluoroberyllate forming a ground 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 . ############################## # 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 16409 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 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_BEF _Saveframe_category ligand _Mol_type non-polymer _Name_common "BEF (BERYLLIUM TRIFLUORIDE ION)" _BMRB_code . _PDB_code BEF _Molecular_mass 66.007 _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 Fri Aug 12 09:31:29 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons BE BE BE . -1 . ? F1 F1 F . 0 . ? 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 BE F1 ? ? SING BE F2 ? ? SING BE 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 Fri Aug 12 09:43:08 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_ 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 Fri Aug 12 09:45:10 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_ #################### # 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 'Sample used for backbone 1H, 15N, 13C assignment of beta phosphoglucomutase in a ternary complex with glucose-6-phosphate and trifluoroberyllate' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $beta_phosphoglucomutase 1 mM '[U-13C; U-15N; U-2H]' 'magnesium chloride' 5 mM 'natural abundance' 'ammonium fluoride' 10 mM 'natural abundance' 'beryllium chloride' 5 mM 'natural abundance' 'sodium azide' 2 mM 'natural abundance' D2O 10 % '[U-100% 2H]' 'potassium HEPES' 50 mM 'natural abundance' $BG6 10 mM 'natural abundance' H2O 90 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details 'Sample used for 19F assignment of beta phosphoglucomutase in a ternary complex with glucose-6-phosphate and trifluoroberyllate' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $beta_phosphoglucomutase 0.5 mM 'natural abundance' 'magnesium chloride' 5 mM 'natural abundance' 'ammonium fluoride' 10 mM 'natural abundance' 'beryllium chloride' 5 mM 'natural abundance' 'sodium azide' 2 mM 'natural abundance' D2O 10 % '[U-100% 2H]' 'potassium HEPES' 50 mM 'natural abundance' $BG6 10 mM 'natural abundance' H2O 90 % '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 collection 'data analysis' 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 'Equipped with a 1H/13C/15N/2H TXI cryoprobe' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details 'Equipped with a 1H/13C/15N/19F QXI probe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $sample_1 save_ save_3D_TROSY_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCA' _Sample_label $sample_1 save_ save_3D_TROSY_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(CO)CA' _Sample_label $sample_1 save_ save_3D_TROSY_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(CA)CO' _Sample_label $sample_1 save_ save_3D_TROSY_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCO' _Sample_label $sample_1 save_ save_3D_TROSY_HN(CA)CB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(CA)CB' _Sample_label $sample_1 save_ save_3D_TROSY_HN(COCA)CB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(COCA)CB' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_19F_1D_9 _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 'ionic strength' 70 . mM pH 6.1 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS F 19 'methyl protons' ppm 0.00 na indirect . . . 0.9409400 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N TROSY' '3D TROSY HNCA' '3D TROSY HN(CO)CA' '3D TROSY HN(CA)CO' '3D TROSY HNCO' '3D TROSY HN(CA)CB' '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 'phosphoglucomutase ground state analogue' _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 5.280 0.005 1 2 2 2 PHE C C 173.753 0.050 1 3 2 2 PHE CA C 56.118 0.050 1 4 2 2 PHE CB C 35.924 0.050 1 5 2 2 PHE N N 117.268 0.050 1 6 3 3 LYS H H 8.745 0.005 1 7 3 3 LYS C C 176.524 0.050 1 8 3 3 LYS CA C 55.566 0.050 1 9 3 3 LYS CB C 35.628 0.050 1 10 3 3 LYS N N 116.624 0.050 1 11 4 4 ALA H H 7.636 0.005 1 12 4 4 ALA C C 175.333 0.050 1 13 4 4 ALA CA C 50.712 0.050 1 14 4 4 ALA CB C 22.549 0.050 1 15 4 4 ALA N N 121.168 0.050 1 16 5 5 VAL H H 8.687 0.005 1 17 5 5 VAL C C 172.820 0.050 1 18 5 5 VAL CA C 61.014 0.050 1 19 5 5 VAL CB C 32.815 0.050 1 20 5 5 VAL N N 120.024 0.050 1 21 6 6 LEU H H 9.348 0.005 1 22 6 6 LEU C C 175.473 0.050 1 23 6 6 LEU CA C 51.474 0.050 1 24 6 6 LEU CB C 39.882 0.050 1 25 6 6 LEU N N 126.340 0.050 1 26 7 7 PHE H H 9.639 0.005 1 27 7 7 PHE C C 177.399 0.050 1 28 7 7 PHE CA C 59.151 0.050 1 29 7 7 PHE CB C 40.273 0.050 1 30 7 7 PHE N N 123.137 0.050 1 31 8 8 ASP H H 7.423 0.005 1 32 8 8 ASP C C 172.657 0.050 1 33 8 8 ASP CA C 53.764 0.050 1 34 8 8 ASP CB C 43.285 0.050 1 35 8 8 ASP N N 122.006 0.050 1 36 9 9 LEU H H 7.400 0.005 1 37 9 9 LEU C C 178.477 0.050 1 38 9 9 LEU CA C 56.105 0.050 1 39 9 9 LEU CB C 43.704 0.050 1 40 9 9 LEU N N 118.967 0.050 1 41 10 10 ASP H H 8.736 0.005 1 42 10 10 ASP C C 176.637 0.050 1 43 10 10 ASP CA C 56.357 0.050 1 44 10 10 ASP CB C 39.646 0.050 1 45 10 10 ASP N N 124.094 0.050 1 46 11 11 GLY C C 171.561 0.050 1 47 11 11 GLY CA C 45.238 0.050 1 48 12 12 VAL H H 7.555 0.005 1 49 12 12 VAL C C 172.986 0.050 1 50 12 12 VAL CA C 64.266 0.050 1 51 12 12 VAL CB C 33.220 0.050 1 52 12 12 VAL N N 118.521 0.050 1 53 13 13 ILE H H 8.368 0.005 1 54 13 13 ILE C C 175.310 0.050 1 55 13 13 ILE CA C 63.163 0.050 1 56 13 13 ILE CB C 38.146 0.050 1 57 13 13 ILE N N 115.490 0.050 1 58 14 14 THR H H 7.227 0.005 1 59 14 14 THR C C 172.694 0.050 1 60 14 14 THR CA C 59.298 0.050 1 61 14 14 THR CB C 67.580 0.050 1 62 14 14 THR N N 109.946 0.050 1 63 15 15 ASP H H 8.060 0.005 1 64 15 15 ASP C C 176.809 0.050 1 65 15 15 ASP CA C 53.670 0.050 1 66 15 15 ASP CB C 41.010 0.050 1 67 15 15 ASP N N 125.227 0.050 1 68 18 18 GLU C C 178.261 0.050 1 69 18 18 GLU CA C 58.331 0.050 1 70 18 18 GLU CB C 28.362 0.050 1 71 19 19 TYR H H 6.839 0.005 1 72 19 19 TYR C C 178.300 0.050 1 73 19 19 TYR CA C 59.706 0.050 1 74 19 19 TYR CB C 36.751 0.050 1 75 19 19 TYR N N 118.412 0.050 1 76 20 20 HIS H H 8.259 0.005 1 77 20 20 HIS C C 177.478 0.050 1 78 20 20 HIS CA C 61.337 0.050 1 79 20 20 HIS CB C 31.227 0.050 1 80 20 20 HIS N N 119.686 0.050 1 81 21 21 PHE H H 8.076 0.005 1 82 21 21 PHE C C 176.647 0.050 1 83 21 21 PHE CA C 59.802 0.050 1 84 21 21 PHE CB C 37.693 0.050 1 85 21 21 PHE N N 118.314 0.050 1 86 22 22 ARG H H 8.281 0.005 1 87 22 22 ARG C C 179.773 0.050 1 88 22 22 ARG CA C 59.137 0.050 1 89 22 22 ARG CB C 29.843 0.050 1 90 22 22 ARG N N 117.554 0.050 1 91 23 23 ALA H H 8.379 0.005 1 92 23 23 ALA C C 180.300 0.050 1 93 23 23 ALA CA C 54.636 0.050 1 94 23 23 ALA CB C 18.099 0.050 1 95 23 23 ALA N N 122.443 0.050 1 96 24 24 TRP H H 8.951 0.005 1 97 24 24 TRP C C 178.628 0.050 1 98 24 24 TRP CA C 59.467 0.050 1 99 24 24 TRP CB C 29.642 0.050 1 100 24 24 TRP N N 121.639 0.050 1 101 25 25 LYS H H 8.877 0.005 1 102 25 25 LYS C C 178.104 0.050 1 103 25 25 LYS CA C 59.611 0.050 1 104 25 25 LYS CB C 31.685 0.050 1 105 25 25 LYS N N 120.826 0.050 1 106 26 26 ALA H H 7.623 0.005 1 107 26 26 ALA C C 180.665 0.050 1 108 26 26 ALA CA C 54.234 0.050 1 109 26 26 ALA CB C 17.178 0.050 1 110 26 26 ALA N N 119.803 0.050 1 111 27 27 LEU H H 7.516 0.005 1 112 27 27 LEU C C 178.494 0.050 1 113 27 27 LEU CA C 57.006 0.050 1 114 27 27 LEU CB C 41.114 0.050 1 115 27 27 LEU N N 120.722 0.050 1 116 28 28 ALA H H 8.691 0.005 1 117 28 28 ALA C C 179.893 0.050 1 118 28 28 ALA CA C 55.057 0.050 1 119 28 28 ALA CB C 17.475 0.050 1 120 28 28 ALA N N 121.065 0.050 1 121 29 29 GLU H H 8.301 0.005 1 122 29 29 GLU C C 180.447 0.050 1 123 29 29 GLU CA C 58.764 0.050 1 124 29 29 GLU CB C 28.386 0.050 1 125 29 29 GLU N N 117.009 0.050 1 126 30 30 GLU H H 7.833 0.005 1 127 30 30 GLU C C 178.859 0.050 1 128 30 30 GLU CA C 58.932 0.050 1 129 30 30 GLU CB C 28.949 0.050 1 130 30 30 GLU N N 121.431 0.050 1 131 31 31 ILE H H 7.599 0.005 1 132 31 31 ILE C C 175.908 0.050 1 133 31 31 ILE CA C 60.745 0.050 1 134 31 31 ILE CB C 37.009 0.050 1 135 31 31 ILE N N 111.626 0.050 1 136 32 32 GLY H H 7.541 0.005 1 137 32 32 GLY C C 174.472 0.050 1 138 32 32 GLY CA C 45.980 0.050 1 139 32 32 GLY N N 109.746 0.050 1 140 33 33 ILE H H 8.332 0.005 1 141 33 33 ILE C C 175.045 0.050 1 142 33 33 ILE CA C 60.931 0.050 1 143 33 33 ILE CB C 38.547 0.050 1 144 33 33 ILE N N 122.881 0.050 1 145 34 34 ASN H H 8.504 0.005 1 146 34 34 ASN C C 175.169 0.050 1 147 34 34 ASN CA C 52.614 0.050 1 148 34 34 ASN CB C 39.594 0.050 1 149 34 34 ASN N N 126.440 0.050 1 150 35 35 GLY H H 7.803 0.005 1 151 35 35 GLY C C 174.042 0.050 1 152 35 35 GLY CA C 44.728 0.050 1 153 35 35 GLY N N 107.100 0.050 1 154 36 36 VAL H H 8.536 0.005 1 155 36 36 VAL C C 173.642 0.050 1 156 36 36 VAL CA C 62.273 0.050 1 157 36 36 VAL CB C 28.091 0.050 1 158 36 36 VAL N N 123.049 0.050 1 159 37 37 ASP H H 7.466 0.005 1 160 37 37 ASP C C 176.276 0.050 1 161 37 37 ASP CA C 50.923 0.050 1 162 37 37 ASP CB C 41.801 0.050 1 163 37 37 ASP N N 126.842 0.050 1 164 38 38 ARG H H 8.369 0.005 1 165 38 38 ARG C C 178.679 0.050 1 166 38 38 ARG CA C 59.588 0.050 1 167 38 38 ARG CB C 28.471 0.050 1 168 38 38 ARG N N 119.311 0.050 1 169 39 39 GLN H H 7.981 0.005 1 170 39 39 GLN C C 179.542 0.050 1 171 39 39 GLN CA C 58.690 0.050 1 172 39 39 GLN CB C 27.374 0.050 1 173 39 39 GLN N N 119.926 0.050 1 174 40 40 PHE H H 8.740 0.005 1 175 40 40 PHE C C 177.728 0.050 1 176 40 40 PHE CA C 61.376 0.050 1 177 40 40 PHE CB C 38.963 0.050 1 178 40 40 PHE N N 124.856 0.050 1 179 41 41 ASN H H 8.477 0.005 1 180 41 41 ASN C C 177.321 0.050 1 181 41 41 ASN CA C 55.919 0.050 1 182 41 41 ASN CB C 39.376 0.050 1 183 41 41 ASN N N 115.443 0.050 1 184 42 42 GLU H H 7.507 0.005 1 185 42 42 GLU C C 179.405 0.050 1 186 42 42 GLU CA C 58.946 0.050 1 187 42 42 GLU CB C 28.562 0.050 1 188 42 42 GLU N N 118.808 0.050 1 189 43 43 GLN H H 7.885 0.005 1 190 43 43 GLN C C 175.064 0.050 1 191 43 43 GLN CA C 56.229 0.050 1 192 43 43 GLN CB C 27.832 0.050 1 193 43 43 GLN N N 116.278 0.050 1 194 44 44 LEU H H 7.195 0.005 1 195 44 44 LEU C C 178.915 0.050 1 196 44 44 LEU CA C 53.576 0.050 1 197 44 44 LEU CB C 40.137 0.050 1 198 44 44 LEU N N 116.133 0.050 1 199 45 45 LYS H H 6.949 0.005 1 200 45 45 LYS C C 177.015 0.050 1 201 45 45 LYS CA C 58.533 0.050 1 202 45 45 LYS CB C 32.351 0.050 1 203 45 45 LYS N N 122.638 0.050 1 204 46 46 GLY H H 8.549 0.005 1 205 46 46 GLY C C 171.466 0.050 1 206 46 46 GLY CA C 45.652 0.050 1 207 46 46 GLY N N 112.905 0.050 1 208 48 48 SER C C 174.968 0.050 1 209 48 48 SER CA C 58.304 0.050 1 210 48 48 SER CB C 65.331 0.050 1 211 49 49 ARG H H 8.993 0.005 1 212 49 49 ARG C C 177.979 0.050 1 213 49 49 ARG CA C 59.913 0.050 1 214 49 49 ARG CB C 30.794 0.050 1 215 49 49 ARG N N 125.957 0.050 1 216 50 50 GLU H H 8.917 0.005 1 217 50 50 GLU C C 178.468 0.050 1 218 50 50 GLU CA C 61.075 0.050 1 219 50 50 GLU CB C 27.935 0.050 1 220 50 50 GLU N N 116.825 0.050 1 221 51 51 ASP H H 7.882 0.005 1 222 51 51 ASP C C 179.305 0.050 1 223 51 51 ASP CA C 56.746 0.050 1 224 51 51 ASP CB C 39.459 0.050 1 225 51 51 ASP N N 120.691 0.050 1 226 52 52 SER H H 8.540 0.005 1 227 52 52 SER C C 174.017 0.050 1 228 52 52 SER CA C 62.236 0.050 1 229 52 52 SER CB C 63.026 0.050 1 230 52 52 SER N N 119.567 0.050 1 231 53 53 LEU H H 7.447 0.005 1 232 53 53 LEU C C 178.237 0.050 1 233 53 53 LEU CA C 56.843 0.050 1 234 53 53 LEU CB C 38.791 0.050 1 235 53 53 LEU N N 121.592 0.050 1 236 54 54 GLN H H 8.116 0.005 1 237 54 54 GLN C C 177.280 0.050 1 238 54 54 GLN CA C 58.215 0.050 1 239 54 54 GLN CB C 28.194 0.050 1 240 54 54 GLN N N 117.694 0.050 1 241 55 55 LYS H H 7.599 0.005 1 242 55 55 LYS C C 179.719 0.050 1 243 55 55 LYS CA C 59.675 0.050 1 244 55 55 LYS CB C 31.721 0.050 1 245 55 55 LYS N N 118.035 0.050 1 246 56 56 ILE H H 7.468 0.005 1 247 56 56 ILE C C 177.276 0.050 1 248 56 56 ILE CA C 65.074 0.050 1 249 56 56 ILE CB C 37.465 0.050 1 250 56 56 ILE N N 120.836 0.050 1 251 57 57 LEU H H 8.352 0.005 1 252 57 57 LEU C C 180.909 0.050 1 253 57 57 LEU CA C 57.746 0.050 1 254 57 57 LEU CB C 38.959 0.050 1 255 57 57 LEU N N 119.316 0.050 1 256 58 58 ASP H H 8.639 0.005 1 257 58 58 ASP C C 179.358 0.050 1 258 58 58 ASP CA C 56.414 0.050 1 259 58 58 ASP CB C 39.488 0.050 1 260 58 58 ASP N N 119.422 0.050 1 261 59 59 LEU H H 7.650 0.005 1 262 59 59 LEU C C 178.193 0.050 1 263 59 59 LEU CA C 57.360 0.050 1 264 59 59 LEU CB C 40.785 0.050 1 265 59 59 LEU N N 123.279 0.050 1 266 60 60 ALA H H 7.013 0.005 1 267 60 60 ALA C C 176.050 0.050 1 268 60 60 ALA CA C 50.188 0.050 1 269 60 60 ALA CB C 20.386 0.050 1 270 60 60 ALA N N 118.791 0.050 1 271 61 61 ASP H H 7.854 0.005 1 272 61 61 ASP C C 174.653 0.050 1 273 61 61 ASP CA C 54.946 0.050 1 274 61 61 ASP CB C 39.319 0.050 1 275 61 61 ASP N N 120.722 0.050 1 276 62 62 LYS H H 7.820 0.005 1 277 62 62 LYS C C 175.433 0.050 1 278 62 62 LYS CA C 55.450 0.050 1 279 62 62 LYS CB C 33.187 0.050 1 280 62 62 LYS N N 118.686 0.050 1 281 63 63 LYS H H 8.488 0.005 1 282 63 63 LYS C C 176.303 0.050 1 283 63 63 LYS CA C 54.316 0.050 1 284 63 63 LYS CB C 32.120 0.050 1 285 63 63 LYS N N 126.967 0.050 1 286 64 64 VAL H H 8.391 0.005 1 287 64 64 VAL C C 175.784 0.050 1 288 64 64 VAL CA C 58.204 0.050 1 289 64 64 VAL CB C 34.467 0.050 1 290 64 64 VAL N N 116.674 0.050 1 291 65 65 SER H H 8.984 0.005 1 292 65 65 SER C C 174.576 0.050 1 293 65 65 SER CA C 57.066 0.050 1 294 65 65 SER CB C 64.740 0.050 1 295 65 65 SER N N 119.590 0.050 1 296 66 66 ALA H H 8.889 0.005 1 297 66 66 ALA C C 180.981 0.050 1 298 66 66 ALA CA C 55.036 0.050 1 299 66 66 ALA CB C 17.224 0.050 1 300 66 66 ALA N N 124.265 0.050 1 301 67 67 GLU H H 8.560 0.005 1 302 67 67 GLU C C 179.391 0.050 1 303 67 67 GLU CA C 59.387 0.050 1 304 67 67 GLU CB C 28.473 0.050 1 305 67 67 GLU N N 117.970 0.050 1 306 68 68 GLU H H 7.871 0.005 1 307 68 68 GLU C C 178.517 0.050 1 308 68 68 GLU CA C 58.638 0.050 1 309 68 68 GLU CB C 29.467 0.050 1 310 68 68 GLU N N 122.885 0.050 1 311 69 69 PHE H H 8.836 0.005 1 312 69 69 PHE C C 176.723 0.050 1 313 69 69 PHE CA C 61.907 0.050 1 314 69 69 PHE CB C 38.922 0.050 1 315 69 69 PHE N N 121.611 0.050 1 316 70 70 LYS H H 7.644 0.005 1 317 70 70 LYS C C 179.958 0.050 1 318 70 70 LYS CA C 59.065 0.050 1 319 70 70 LYS CB C 31.810 0.050 1 320 70 70 LYS N N 116.335 0.050 1 321 71 71 GLU H H 7.764 0.005 1 322 71 71 GLU C C 178.904 0.050 1 323 71 71 GLU CA C 58.755 0.050 1 324 71 71 GLU CB C 28.417 0.050 1 325 71 71 GLU N N 121.160 0.050 1 326 72 72 LEU H H 8.400 0.005 1 327 72 72 LEU C C 178.158 0.050 1 328 72 72 LEU CA C 57.563 0.050 1 329 72 72 LEU CB C 41.666 0.050 1 330 72 72 LEU N N 122.013 0.050 1 331 73 73 ALA H H 7.768 0.005 1 332 73 73 ALA C C 179.540 0.050 1 333 73 73 ALA CA C 55.050 0.050 1 334 73 73 ALA CB C 16.160 0.050 1 335 73 73 ALA N N 120.666 0.050 1 336 74 74 LYS H H 7.665 0.005 1 337 74 74 LYS C C 178.273 0.050 1 338 74 74 LYS CA C 58.985 0.050 1 339 74 74 LYS CB C 31.512 0.050 1 340 74 74 LYS N N 118.980 0.050 1 341 75 75 ARG H H 8.265 0.005 1 342 75 75 ARG C C 179.470 0.050 1 343 75 75 ARG CA C 59.066 0.050 1 344 75 75 ARG CB C 29.495 0.050 1 345 75 75 ARG N N 121.299 0.050 1 346 76 76 LYS H H 7.797 0.005 1 347 76 76 LYS C C 179.094 0.050 1 348 76 76 LYS CA C 59.376 0.050 1 349 76 76 LYS CB C 29.525 0.050 1 350 76 76 LYS N N 119.582 0.050 1 351 77 77 ASN H H 7.968 0.005 1 352 77 77 ASN C C 176.069 0.050 1 353 77 77 ASN CA C 56.870 0.050 1 354 77 77 ASN CB C 37.954 0.050 1 355 77 77 ASN N N 118.879 0.050 1 356 78 78 ASP H H 8.900 0.005 1 357 78 78 ASP C C 179.249 0.050 1 358 78 78 ASP CA C 56.860 0.050 1 359 78 78 ASP CB C 39.177 0.050 1 360 78 78 ASP N N 119.717 0.050 1 361 79 79 ASN H H 7.546 0.005 1 362 79 79 ASN C C 176.828 0.050 1 363 79 79 ASN CA C 55.005 0.050 1 364 79 79 ASN CB C 37.672 0.050 1 365 79 79 ASN N N 118.822 0.050 1 366 80 80 TYR H H 8.495 0.005 1 367 80 80 TYR C C 176.429 0.050 1 368 80 80 TYR CA C 61.594 0.050 1 369 80 80 TYR CB C 38.478 0.050 1 370 80 80 TYR N N 122.838 0.050 1 371 81 81 VAL H H 8.812 0.005 1 372 81 81 VAL C C 178.631 0.050 1 373 81 81 VAL CA C 65.600 0.050 1 374 81 81 VAL CB C 30.533 0.050 1 375 81 81 VAL N N 118.344 0.050 1 376 82 82 LYS H H 7.031 0.005 1 377 82 82 LYS C C 179.558 0.050 1 378 82 82 LYS CA C 58.770 0.050 1 379 82 82 LYS CB C 31.293 0.050 1 380 82 82 LYS N N 118.940 0.050 1 381 84 84 ILE C C 176.578 0.050 1 382 84 84 ILE CA C 62.222 0.050 1 383 84 84 ILE CB C 36.382 0.050 1 384 85 85 GLN H H 6.964 0.005 1 385 85 85 GLN C C 176.278 0.050 1 386 85 85 GLN CA C 57.691 0.050 1 387 85 85 GLN CB C 27.941 0.050 1 388 85 85 GLN N N 118.578 0.050 1 389 86 86 ASP H H 7.534 0.005 1 390 86 86 ASP C C 176.742 0.050 1 391 86 86 ASP CA C 53.572 0.050 1 392 86 86 ASP CB C 40.706 0.050 1 393 86 86 ASP N N 114.867 0.050 1 394 87 87 VAL H H 7.105 0.005 1 395 87 87 VAL C C 174.303 0.050 1 396 87 87 VAL CA C 63.565 0.050 1 397 87 87 VAL CB C 30.418 0.050 1 398 87 87 VAL N N 124.121 0.050 1 399 88 88 SER H H 9.294 0.005 1 400 88 88 SER C C 181.147 0.050 1 401 88 88 SER CA C 56.952 0.050 1 402 88 88 SER CB C 65.488 0.050 1 403 88 88 SER N N 126.179 0.050 1 404 89 89 PRO C C 177.718 0.050 1 405 89 89 PRO CA C 64.936 0.050 1 406 89 89 PRO CB C 30.823 0.050 1 407 90 90 ALA H H 7.692 0.005 1 408 90 90 ALA C C 177.971 0.050 1 409 90 90 ALA CA C 53.216 0.050 1 410 90 90 ALA CB C 17.640 0.050 1 411 90 90 ALA N N 119.499 0.050 1 412 91 91 ASP H H 8.024 0.005 1 413 91 91 ASP C C 177.182 0.050 1 414 91 91 ASP CA C 55.029 0.050 1 415 91 91 ASP CB C 41.129 0.050 1 416 91 91 ASP N N 115.296 0.050 1 417 92 92 VAL H H 7.145 0.005 1 418 92 92 VAL C C 176.722 0.050 1 419 92 92 VAL CA C 63.584 0.050 1 420 92 92 VAL CB C 31.112 0.050 1 421 92 92 VAL N N 124.772 0.050 1 422 93 93 TYR H H 8.945 0.005 1 423 93 93 TYR C C 175.434 0.050 1 424 93 93 TYR CA C 54.239 0.050 1 425 93 93 TYR CB C 35.381 0.050 1 426 93 93 TYR N N 130.939 0.050 1 427 94 94 PRO C C 177.257 0.050 1 428 94 94 PRO CA C 63.291 0.050 1 429 94 94 PRO CB C 31.409 0.050 1 430 95 95 GLY H H 8.369 0.005 1 431 95 95 GLY C C 176.103 0.050 1 432 95 95 GLY CA C 45.757 0.050 1 433 95 95 GLY N N 111.520 0.050 1 434 96 96 ILE H H 7.124 0.005 1 435 96 96 ILE C C 176.884 0.050 1 436 96 96 ILE CA C 61.070 0.050 1 437 96 96 ILE CB C 33.820 0.050 1 438 96 96 ILE N N 121.571 0.050 1 439 97 97 LEU H H 8.773 0.005 1 440 97 97 LEU C C 178.000 0.050 1 441 97 97 LEU CA C 58.106 0.050 1 442 97 97 LEU CB C 40.364 0.050 1 443 97 97 LEU N N 121.370 0.050 1 444 98 98 GLN H H 8.662 0.005 1 445 98 98 GLN C C 177.372 0.050 1 446 98 98 GLN CA C 57.572 0.050 1 447 98 98 GLN CB C 27.668 0.050 1 448 98 98 GLN N N 117.806 0.050 1 449 99 99 LEU H H 7.797 0.005 1 450 99 99 LEU C C 178.465 0.050 1 451 99 99 LEU CA C 57.787 0.050 1 452 99 99 LEU CB C 39.931 0.050 1 453 99 99 LEU N N 119.806 0.050 1 454 100 100 LEU H H 8.269 0.005 1 455 100 100 LEU C C 179.002 0.050 1 456 100 100 LEU CA C 58.026 0.050 1 457 100 100 LEU CB C 39.670 0.050 1 458 100 100 LEU N N 119.443 0.050 1 459 101 101 LYS H H 7.912 0.005 1 460 101 101 LYS C C 180.242 0.050 1 461 101 101 LYS CA C 59.968 0.050 1 462 101 101 LYS CB C 32.001 0.050 1 463 101 101 LYS N N 117.905 0.050 1 464 102 102 ASP H H 8.822 0.005 1 465 102 102 ASP C C 179.791 0.050 1 466 102 102 ASP CA C 57.055 0.050 1 467 102 102 ASP CB C 39.602 0.050 1 468 102 102 ASP N N 122.867 0.050 1 469 103 103 LEU H H 9.303 0.005 1 470 103 103 LEU C C 179.048 0.050 1 471 103 103 LEU CA C 58.219 0.050 1 472 103 103 LEU CB C 39.904 0.050 1 473 103 103 LEU N N 123.780 0.050 1 474 104 104 ARG H H 8.237 0.005 1 475 104 104 ARG C C 181.850 0.050 1 476 104 104 ARG CA C 59.246 0.050 1 477 104 104 ARG CB C 28.756 0.050 1 478 104 104 ARG N N 120.138 0.050 1 479 105 105 SER H H 8.693 0.005 1 480 105 105 SER C C 175.170 0.050 1 481 105 105 SER CA C 61.154 0.050 1 482 105 105 SER CB C 62.279 0.050 1 483 105 105 SER N N 117.407 0.050 1 484 106 106 ASN H H 7.403 0.005 1 485 106 106 ASN C C 172.383 0.050 1 486 106 106 ASN CA C 53.660 0.050 1 487 106 106 ASN CB C 39.454 0.050 1 488 106 106 ASN N N 118.312 0.050 1 489 107 107 LYS H H 7.880 0.005 1 490 107 107 LYS C C 175.089 0.050 1 491 107 107 LYS CA C 56.852 0.050 1 492 107 107 LYS CB C 27.426 0.050 1 493 107 107 LYS N N 115.025 0.050 1 494 108 108 ILE H H 7.952 0.005 1 495 108 108 ILE C C 175.743 0.050 1 496 108 108 ILE CA C 59.900 0.050 1 497 108 108 ILE CB C 37.026 0.050 1 498 108 108 ILE N N 122.482 0.050 1 499 109 109 LYS H H 7.617 0.005 1 500 109 109 LYS C C 175.750 0.050 1 501 109 109 LYS CA C 54.841 0.050 1 502 109 109 LYS CB C 32.679 0.050 1 503 109 109 LYS N N 125.100 0.050 1 504 110 110 ILE H H 9.254 0.005 1 505 110 110 ILE C C 175.825 0.050 1 506 110 110 ILE CA C 60.952 0.050 1 507 110 110 ILE CB C 40.198 0.050 1 508 110 110 ILE N N 121.945 0.050 1 509 111 111 ALA H H 8.748 0.005 1 510 111 111 ALA C C 175.896 0.050 1 511 111 111 ALA CA C 49.018 0.050 1 512 111 111 ALA CB C 23.783 0.050 1 513 111 111 ALA N N 128.062 0.050 1 514 112 112 LEU H H 8.497 0.005 1 515 112 112 LEU C C 174.124 0.050 1 516 112 112 LEU CA C 53.734 0.050 1 517 112 112 LEU CB C 43.588 0.050 1 518 112 112 LEU N N 123.754 0.050 1 519 113 113 ALA H H 9.065 0.005 1 520 113 113 ALA C C 175.163 0.050 1 521 113 113 ALA CA C 49.329 0.050 1 522 113 113 ALA CB C 18.924 0.050 1 523 113 113 ALA N N 133.142 0.050 1 524 114 114 SER H H 7.938 0.005 1 525 114 114 SER C C 174.868 0.050 1 526 114 114 SER CA C 56.014 0.050 1 527 114 114 SER CB C 64.299 0.050 1 528 114 114 SER N N 115.011 0.050 1 529 115 115 ALA H H 8.260 0.005 1 530 115 115 ALA C C 176.580 0.050 1 531 115 115 ALA CA C 52.178 0.050 1 532 115 115 ALA CB C 18.984 0.050 1 533 115 115 ALA N N 127.090 0.050 1 534 116 116 SER H H 8.502 0.005 1 535 116 116 SER C C 178.932 0.050 1 536 116 116 SER CA C 56.627 0.050 1 537 116 116 SER CB C 63.657 0.050 1 538 116 116 SER N N 113.036 0.050 1 539 117 117 LYS H H 10.762 0.005 1 540 117 117 LYS C C 177.681 0.050 1 541 117 117 LYS CA C 57.852 0.050 1 542 117 117 LYS CB C 31.114 0.050 1 543 117 117 LYS N N 134.757 0.050 1 544 118 118 ASN H H 8.561 0.005 1 545 118 118 ASN C C 174.395 0.050 1 546 118 118 ASN CA C 54.194 0.050 1 547 118 118 ASN CB C 39.542 0.050 1 548 118 118 ASN N N 117.695 0.050 1 549 119 119 GLY H H 7.266 0.005 1 550 119 119 GLY C C 172.389 0.050 1 551 119 119 GLY CA C 48.098 0.050 1 552 119 119 GLY N N 105.911 0.050 1 553 120 120 PRO C C 179.117 0.050 1 554 120 120 PRO CA C 65.729 0.050 1 555 120 120 PRO CB C 30.662 0.050 1 556 121 121 PHE H H 7.639 0.005 1 557 121 121 PHE C C 177.319 0.050 1 558 121 121 PHE CA C 60.226 0.050 1 559 121 121 PHE CB C 38.644 0.050 1 560 121 121 PHE N N 119.499 0.050 1 561 122 122 LEU C C 178.815 0.050 1 562 122 122 LEU CA C 57.573 0.050 1 563 122 122 LEU CB C 41.129 0.050 1 564 123 123 LEU H H 8.273 0.005 1 565 123 123 LEU C C 179.097 0.050 1 566 123 123 LEU CA C 58.029 0.050 1 567 123 123 LEU CB C 40.498 0.050 1 568 123 123 LEU N N 117.359 0.050 1 569 124 124 GLU H H 7.541 0.005 1 570 124 124 GLU C C 180.746 0.050 1 571 124 124 GLU CA C 58.627 0.050 1 572 124 124 GLU CB C 28.226 0.050 1 573 124 124 GLU N N 120.350 0.050 1 574 125 125 ARG H H 8.020 0.005 1 575 125 125 ARG C C 178.393 0.050 1 576 125 125 ARG CA C 56.727 0.050 1 577 125 125 ARG CB C 28.357 0.050 1 578 125 125 ARG N N 121.046 0.050 1 579 126 126 MET H H 7.324 0.005 1 580 126 126 MET C C 173.605 0.050 1 581 126 126 MET CA C 55.877 0.050 1 582 126 126 MET CB C 32.469 0.050 1 583 126 126 MET N N 113.300 0.050 1 584 127 127 ASN H H 7.960 0.005 1 585 127 127 ASN C C 175.849 0.050 1 586 127 127 ASN CA C 53.460 0.050 1 587 127 127 ASN CB C 36.514 0.050 1 588 127 127 ASN N N 117.242 0.050 1 589 128 128 LEU H H 8.653 0.005 1 590 128 128 LEU C C 177.912 0.050 1 591 128 128 LEU CA C 53.584 0.050 1 592 128 128 LEU CB C 44.642 0.050 1 593 128 128 LEU N N 114.313 0.050 1 594 129 129 THR H H 7.408 0.005 1 595 129 129 THR C C 176.360 0.050 1 596 129 129 THR CA C 67.062 0.050 1 597 129 129 THR CB C 68.440 0.050 1 598 129 129 THR N N 115.813 0.050 1 599 130 130 GLY H H 8.565 0.005 1 600 130 130 GLY C C 174.961 0.050 1 601 130 130 GLY CA C 45.655 0.050 1 602 130 130 GLY N N 106.315 0.050 1 603 131 131 TYR H H 7.716 0.005 1 604 131 131 TYR C C 174.414 0.050 1 605 131 131 TYR CA C 59.693 0.050 1 606 131 131 TYR CB C 38.675 0.050 1 607 131 131 TYR N N 116.369 0.050 1 608 132 132 PHE H H 7.325 0.005 1 609 132 132 PHE C C 175.791 0.050 1 610 132 132 PHE CA C 58.313 0.050 1 611 132 132 PHE CB C 38.969 0.050 1 612 132 132 PHE N N 115.304 0.050 1 613 133 133 ASP H H 9.154 0.005 1 614 133 133 ASP C C 176.372 0.050 1 615 133 133 ASP CA C 56.626 0.050 1 616 133 133 ASP CB C 42.184 0.050 1 617 133 133 ASP N N 124.941 0.050 1 618 134 134 ALA H H 7.606 0.005 1 619 134 134 ALA C C 175.485 0.050 1 620 134 134 ALA CA C 51.764 0.050 1 621 134 134 ALA CB C 23.492 0.050 1 622 134 134 ALA N N 115.588 0.050 1 623 135 135 ILE H H 8.632 0.005 1 624 135 135 ILE C C 175.588 0.050 1 625 135 135 ILE CA C 60.403 0.050 1 626 135 135 ILE CB C 40.071 0.050 1 627 135 135 ILE N N 121.922 0.050 1 628 136 136 ALA H H 8.454 0.005 1 629 136 136 ALA C C 175.380 0.050 1 630 136 136 ALA CA C 51.359 0.050 1 631 136 136 ALA CB C 17.820 0.050 1 632 136 136 ALA N N 130.907 0.050 1 633 137 137 ASP H H 8.448 0.005 1 634 137 137 ASP C C 176.687 0.050 1 635 137 137 ASP CA C 50.608 0.050 1 636 137 137 ASP CB C 41.356 0.050 1 637 137 137 ASP N N 125.581 0.050 1 638 138 138 PRO C C 178.000 0.050 1 639 138 138 PRO CA C 63.712 0.050 1 640 138 138 PRO CB C 31.409 0.050 1 641 139 139 ALA H H 8.643 0.005 1 642 139 139 ALA C C 178.792 0.050 1 643 139 139 ALA CA C 52.826 0.050 1 644 139 139 ALA CB C 18.167 0.050 1 645 139 139 ALA N N 120.572 0.050 1 646 140 140 GLU H H 7.498 0.005 1 647 140 140 GLU C C 176.691 0.050 1 648 140 140 GLU CA C 55.480 0.050 1 649 140 140 GLU CB C 29.816 0.050 1 650 140 140 GLU N N 116.302 0.050 1 651 141 141 VAL H H 6.888 0.005 1 652 141 141 VAL C C 175.846 0.050 1 653 141 141 VAL CA C 59.917 0.050 1 654 141 141 VAL CB C 32.206 0.050 1 655 141 141 VAL N N 113.912 0.050 1 656 142 142 ALA H H 8.552 0.005 1 657 142 142 ALA C C 177.633 0.050 1 658 142 142 ALA CA C 53.493 0.050 1 659 142 142 ALA CB C 18.046 0.050 1 660 142 142 ALA N N 124.763 0.050 1 661 143 143 ALA H H 7.230 0.005 1 662 143 143 ALA C C 176.112 0.050 1 663 143 143 ALA CA C 50.938 0.050 1 664 143 143 ALA CB C 20.797 0.050 1 665 143 143 ALA N N 119.289 0.050 1 666 144 144 SER H H 8.489 0.005 1 667 144 144 SER C C 175.961 0.050 1 668 144 144 SER CA C 56.829 0.050 1 669 144 144 SER CB C 63.352 0.050 1 670 144 144 SER N N 117.802 0.050 1 671 145 145 LYS H H 8.706 0.005 1 672 145 145 LYS C C 175.286 0.050 1 673 145 145 LYS CA C 57.268 0.050 1 674 145 145 LYS CB C 29.988 0.050 1 675 145 145 LYS N N 126.774 0.050 1 676 146 146 PRO C C 176.267 0.050 1 677 146 146 PRO CA C 62.864 0.050 1 678 146 146 PRO CB C 35.389 0.050 1 679 147 147 ALA H H 9.100 0.005 1 680 147 147 ALA C C 178.200 0.050 1 681 147 147 ALA CA C 51.572 0.050 1 682 147 147 ALA CB C 16.805 0.050 1 683 147 147 ALA N N 131.917 0.050 1 684 148 148 PRO C C 177.208 0.050 1 685 148 148 PRO CA C 63.457 0.050 1 686 148 148 PRO CB C 32.049 0.050 1 687 149 149 ASP H H 9.346 0.005 1 688 149 149 ASP C C 178.067 0.050 1 689 149 149 ASP CA C 57.998 0.050 1 690 149 149 ASP CB C 38.951 0.050 1 691 149 149 ASP N N 120.954 0.050 1 692 150 150 ILE H H 9.866 0.005 1 693 150 150 ILE C C 175.761 0.050 1 694 150 150 ILE CA C 63.072 0.050 1 695 150 150 ILE CB C 37.374 0.050 1 696 150 150 ILE N N 120.552 0.050 1 697 151 151 PHE H H 7.230 0.005 1 698 151 151 PHE C C 177.651 0.050 1 699 151 151 PHE CA C 63.170 0.050 1 700 151 151 PHE CB C 38.379 0.050 1 701 151 151 PHE N N 120.937 0.050 1 702 152 152 ILE H H 7.779 0.005 1 703 152 152 ILE C C 177.905 0.050 1 704 152 152 ILE CA C 65.609 0.050 1 705 152 152 ILE CB C 37.428 0.050 1 706 152 152 ILE N N 120.532 0.050 1 707 153 153 ALA H H 8.443 0.005 1 708 153 153 ALA C C 180.893 0.050 1 709 153 153 ALA CA C 54.318 0.050 1 710 153 153 ALA CB C 17.351 0.050 1 711 153 153 ALA N N 120.988 0.050 1 712 154 154 ALA H H 7.845 0.005 1 713 154 154 ALA C C 176.765 0.050 1 714 154 154 ALA CA C 55.027 0.050 1 715 154 154 ALA CB C 17.761 0.050 1 716 154 154 ALA N N 122.393 0.050 1 717 155 155 ALA H H 7.626 0.005 1 718 155 155 ALA C C 179.715 0.050 1 719 155 155 ALA CA C 54.209 0.050 1 720 155 155 ALA CB C 16.159 0.050 1 721 155 155 ALA N N 118.313 0.050 1 722 156 156 HIS H H 8.424 0.005 1 723 156 156 HIS C C 179.004 0.050 1 724 156 156 HIS CA C 57.672 0.050 1 725 156 156 HIS CB C 27.827 0.050 1 726 156 156 HIS N N 116.022 0.050 1 727 157 157 ALA H H 8.272 0.005 1 728 157 157 ALA C C 179.153 0.050 1 729 157 157 ALA CA C 54.095 0.050 1 730 157 157 ALA CB C 17.692 0.050 1 731 157 157 ALA N N 122.368 0.050 1 732 158 158 VAL H H 7.161 0.005 1 733 158 158 VAL C C 175.483 0.050 1 734 158 158 VAL CA C 59.367 0.050 1 735 158 158 VAL CB C 30.463 0.050 1 736 158 158 VAL N N 107.374 0.050 1 737 159 159 GLY H H 7.711 0.005 1 738 159 159 GLY C C 174.591 0.050 1 739 159 159 GLY CA C 46.038 0.050 1 740 159 159 GLY N N 110.053 0.050 1 741 160 160 VAL H H 7.625 0.005 1 742 160 160 VAL C C 174.264 0.050 1 743 160 160 VAL CA C 58.877 0.050 1 744 160 160 VAL CB C 34.108 0.050 1 745 160 160 VAL N N 116.893 0.050 1 746 161 161 ALA H H 8.652 0.005 1 747 161 161 ALA C C 178.727 0.050 1 748 161 161 ALA CA C 49.565 0.050 1 749 161 161 ALA CB C 17.276 0.050 1 750 161 161 ALA N N 126.076 0.050 1 751 162 162 PRO C C 177.414 0.050 1 752 162 162 PRO CA C 65.528 0.050 1 753 162 162 PRO CB C 30.883 0.050 1 754 163 163 SER H H 7.730 0.005 1 755 163 163 SER C C 175.898 0.050 1 756 163 163 SER CA C 59.790 0.050 1 757 163 163 SER CB C 61.863 0.050 1 758 163 163 SER N N 107.091 0.050 1 759 164 164 GLU H H 7.773 0.005 1 760 164 164 GLU C C 174.749 0.050 1 761 164 164 GLU CA C 55.512 0.050 1 762 164 164 GLU CB C 29.308 0.050 1 763 164 164 GLU N N 121.776 0.050 1 764 165 165 SER H H 7.988 0.005 1 765 165 165 SER C C 172.057 0.050 1 766 165 165 SER CA C 57.462 0.050 1 767 165 165 SER CB C 65.328 0.050 1 768 165 165 SER N N 114.832 0.050 1 769 166 166 ILE H H 7.582 0.005 1 770 166 166 ILE C C 175.235 0.050 1 771 166 166 ILE CA C 58.886 0.050 1 772 166 166 ILE CB C 40.788 0.050 1 773 166 166 ILE N N 121.727 0.050 1 774 167 167 GLY H H 8.785 0.005 1 775 167 167 GLY C C 170.414 0.050 1 776 167 167 GLY CA C 43.343 0.050 1 777 167 167 GLY N N 112.866 0.050 1 778 168 168 LEU H H 7.749 0.005 1 779 168 168 LEU C C 175.746 0.050 1 780 168 168 LEU CA C 53.253 0.050 1 781 168 168 LEU CB C 40.892 0.050 1 782 168 168 LEU N N 123.575 0.050 1 783 169 169 GLU H H 6.934 0.005 1 784 169 169 GLU C C 173.607 0.050 1 785 169 169 GLU CA C 56.378 0.050 1 786 169 169 GLU CB C 39.252 0.050 1 787 169 169 GLU N N 123.867 0.050 1 788 170 170 ASP H H 8.486 0.005 1 789 170 170 ASP C C 174.158 0.050 1 790 170 170 ASP CA C 52.148 0.050 1 791 170 170 ASP CB C 41.764 0.050 1 792 170 170 ASP N N 115.697 0.050 1 793 171 171 SER H H 8.077 0.005 1 794 171 171 SER C C 173.965 0.050 1 795 171 171 SER CA C 55.444 0.050 1 796 171 171 SER CB C 68.910 0.050 1 797 171 171 SER N N 114.776 0.050 1 798 172 172 GLN H H 9.589 0.005 1 799 172 172 GLN C C 179.199 0.050 1 800 172 172 GLN CA C 59.162 0.050 1 801 172 172 GLN CB C 27.473 0.050 1 802 172 172 GLN N N 125.279 0.050 1 803 173 173 ALA H H 8.655 0.005 1 804 173 173 ALA C C 180.143 0.050 1 805 173 173 ALA CA C 54.109 0.050 1 806 173 173 ALA CB C 17.127 0.050 1 807 173 173 ALA N N 121.086 0.050 1 808 174 174 GLY H H 8.199 0.005 1 809 174 174 GLY C C 175.544 0.050 1 810 174 174 GLY CA C 46.094 0.050 1 811 174 174 GLY N N 106.287 0.050 1 812 175 175 ILE H H 8.410 0.005 1 813 175 175 ILE C C 177.730 0.050 1 814 175 175 ILE CA C 62.340 0.050 1 815 175 175 ILE CB C 34.579 0.050 1 816 175 175 ILE N N 123.572 0.050 1 817 176 176 GLN H H 7.730 0.005 1 818 176 176 GLN C C 176.984 0.050 1 819 176 176 GLN CA C 58.219 0.050 1 820 176 176 GLN CB C 27.261 0.050 1 821 176 176 GLN N N 120.414 0.050 1 822 177 177 ALA H H 7.701 0.005 1 823 177 177 ALA C C 179.730 0.050 1 824 177 177 ALA CA C 54.770 0.050 1 825 177 177 ALA CB C 19.229 0.050 1 826 177 177 ALA N N 122.421 0.050 1 827 178 178 ILE H H 8.031 0.005 1 828 178 178 ILE C C 180.617 0.050 1 829 178 178 ILE CA C 64.773 0.050 1 830 178 178 ILE CB C 36.400 0.050 1 831 178 178 ILE N N 117.672 0.050 1 832 179 179 LYS H H 8.506 0.005 1 833 179 179 LYS C C 180.927 0.050 1 834 179 179 LYS CA C 59.790 0.050 1 835 179 179 LYS CB C 31.870 0.050 1 836 179 179 LYS N N 120.912 0.050 1 837 180 180 ASP H H 8.466 0.005 1 838 180 180 ASP C C 177.285 0.050 1 839 180 180 ASP CA C 56.210 0.050 1 840 180 180 ASP CB C 38.736 0.050 1 841 180 180 ASP N N 118.767 0.050 1 842 181 181 SER H H 8.079 0.005 1 843 181 181 SER C C 173.869 0.050 1 844 181 181 SER CA C 60.320 0.050 1 845 181 181 SER CB C 64.310 0.050 1 846 181 181 SER N N 117.239 0.050 1 847 182 182 GLY H H 7.217 0.005 1 848 182 182 GLY C C 173.479 0.050 1 849 182 182 GLY CA C 44.257 0.050 1 850 182 182 GLY N N 109.119 0.050 1 851 183 183 ALA H H 7.152 0.005 1 852 183 183 ALA C C 174.694 0.050 1 853 183 183 ALA CA C 50.871 0.050 1 854 183 183 ALA CB C 19.512 0.050 1 855 183 183 ALA N N 124.223 0.050 1 856 184 184 LEU H H 8.037 0.005 1 857 184 184 LEU C C 174.866 0.050 1 858 184 184 LEU CA C 51.863 0.050 1 859 184 184 LEU CB C 43.399 0.050 1 860 184 184 LEU N N 122.682 0.050 1 861 185 185 PRO C C 176.372 0.050 1 862 185 185 PRO CA C 61.389 0.050 1 863 185 185 PRO CB C 31.699 0.050 1 864 186 186 ILE H H 8.280 0.005 1 865 186 186 ILE C C 178.565 0.050 1 866 186 186 ILE CA C 61.488 0.050 1 867 186 186 ILE CB C 38.197 0.050 1 868 186 186 ILE N N 119.350 0.050 1 869 187 187 GLY H H 8.929 0.005 1 870 187 187 GLY C C 171.221 0.050 1 871 187 187 GLY CA C 44.797 0.050 1 872 187 187 GLY N N 116.426 0.050 1 873 188 188 VAL H H 8.071 0.005 1 874 188 188 VAL C C 173.807 0.050 1 875 188 188 VAL CA C 57.326 0.050 1 876 188 188 VAL CB C 32.032 0.050 1 877 188 188 VAL N N 119.232 0.050 1 878 189 189 GLY H H 8.081 0.005 1 879 189 189 GLY C C 171.145 0.050 1 880 189 189 GLY CA C 44.086 0.050 1 881 189 189 GLY N N 113.222 0.050 1 882 190 190 ARG H H 8.682 0.005 1 883 190 190 ARG C C 176.095 0.050 1 884 190 190 ARG CA C 52.525 0.050 1 885 190 190 ARG CB C 30.159 0.050 1 886 190 190 ARG N N 120.992 0.050 1 887 191 191 PRO C C 178.737 0.050 1 888 191 191 PRO CA C 64.231 0.050 1 889 191 191 PRO CB C 30.940 0.050 1 890 192 192 GLU H H 9.635 0.005 1 891 192 192 GLU C C 176.798 0.050 1 892 192 192 GLU CA C 59.483 0.050 1 893 192 192 GLU CB C 27.870 0.050 1 894 192 192 GLU N N 118.943 0.050 1 895 193 193 ASP H H 7.064 0.005 1 896 193 193 ASP C C 176.934 0.050 1 897 193 193 ASP CA C 55.053 0.050 1 898 193 193 ASP CB C 41.633 0.050 1 899 193 193 ASP N N 115.087 0.050 1 900 194 194 LEU H H 7.609 0.005 1 901 194 194 LEU C C 176.448 0.050 1 902 194 194 LEU CA C 55.414 0.050 1 903 194 194 LEU CB C 42.547 0.050 1 904 194 194 LEU N N 116.773 0.050 1 905 195 195 GLY H H 8.020 0.005 1 906 195 195 GLY C C 172.605 0.050 1 907 195 195 GLY CA C 43.652 0.050 1 908 195 195 GLY N N 108.066 0.050 1 909 196 196 ASP H H 7.923 0.005 1 910 196 196 ASP C C 176.898 0.050 1 911 196 196 ASP CA C 53.664 0.050 1 912 196 196 ASP CB C 41.060 0.050 1 913 196 196 ASP N N 116.853 0.050 1 914 197 197 ASP H H 8.906 0.005 1 915 197 197 ASP C C 175.373 0.050 1 916 197 197 ASP CA C 53.532 0.050 1 917 197 197 ASP CB C 39.603 0.050 1 918 197 197 ASP N N 117.298 0.050 1 919 198 198 ILE H H 6.775 0.005 1 920 198 198 ILE C C 175.396 0.050 1 921 198 198 ILE CA C 58.208 0.050 1 922 198 198 ILE CB C 40.596 0.050 1 923 198 198 ILE N N 113.450 0.050 1 924 199 199 VAL H H 8.931 0.005 1 925 199 199 VAL C C 174.285 0.050 1 926 199 199 VAL CA C 63.687 0.050 1 927 199 199 VAL CB C 30.302 0.050 1 928 199 199 VAL N N 125.529 0.050 1 929 200 200 ILE H H 7.973 0.005 1 930 200 200 ILE C C 176.064 0.050 1 931 200 200 ILE CA C 58.001 0.050 1 932 200 200 ILE CB C 41.069 0.050 1 933 200 200 ILE N N 126.604 0.050 1 934 201 201 VAL H H 8.766 0.005 1 935 201 201 VAL C C 174.277 0.050 1 936 201 201 VAL CA C 56.115 0.050 1 937 201 201 VAL CB C 31.800 0.050 1 938 201 201 VAL N N 120.286 0.050 1 939 202 202 PRO C C 176.996 0.050 1 940 202 202 PRO CA C 63.514 0.050 1 941 202 202 PRO CB C 31.002 0.050 1 942 203 203 ASP H H 6.781 0.005 1 943 203 203 ASP C C 175.723 0.050 1 944 203 203 ASP CA C 52.946 0.050 1 945 203 203 ASP CB C 41.482 0.050 1 946 203 203 ASP N N 110.284 0.050 1 947 204 204 THR H H 8.201 0.005 1 948 204 204 THR C C 176.639 0.050 1 949 204 204 THR CA C 65.054 0.050 1 950 204 204 THR CB C 68.713 0.050 1 951 204 204 THR N N 109.380 0.050 1 952 205 205 SER H H 8.709 0.005 1 953 205 205 SER C C 175.648 0.050 1 954 205 205 SER CA C 61.233 0.050 1 955 205 205 SER CB C 61.971 0.050 1 956 205 205 SER N N 119.895 0.050 1 957 206 206 HIS H H 7.073 0.005 1 958 206 206 HIS C C 176.052 0.050 1 959 206 206 HIS CA C 56.167 0.050 1 960 206 206 HIS CB C 28.936 0.050 1 961 206 206 HIS N N 116.841 0.050 1 962 207 207 TYR H H 7.776 0.005 1 963 207 207 TYR C C 173.459 0.050 1 964 207 207 TYR CA C 54.059 0.050 1 965 207 207 TYR CB C 35.268 0.050 1 966 207 207 TYR N N 120.557 0.050 1 967 208 208 THR H H 7.278 0.005 1 968 208 208 THR C C 174.707 0.050 1 969 208 208 THR CA C 57.905 0.050 1 970 208 208 THR CB C 71.122 0.050 1 971 208 208 THR N N 114.138 0.050 1 972 209 209 LEU H H 9.483 0.005 1 973 209 209 LEU C C 177.814 0.050 1 974 209 209 LEU CA C 58.303 0.050 1 975 209 209 LEU CB C 39.779 0.050 1 976 209 209 LEU N N 125.306 0.050 1 977 210 210 GLU H H 8.555 0.005 1 978 210 210 GLU C C 178.734 0.050 1 979 210 210 GLU CA C 59.437 0.050 1 980 210 210 GLU CB C 28.541 0.050 1 981 210 210 GLU N N 116.794 0.050 1 982 211 211 PHE H H 8.140 0.005 1 983 211 211 PHE C C 176.746 0.050 1 984 211 211 PHE CA C 60.746 0.050 1 985 211 211 PHE CB C 39.427 0.050 1 986 211 211 PHE N N 122.283 0.050 1 987 212 212 LEU H H 8.338 0.005 1 988 212 212 LEU C C 179.044 0.050 1 989 212 212 LEU CA C 58.939 0.050 1 990 212 212 LEU CB C 39.847 0.050 1 991 212 212 LEU N N 119.691 0.050 1 992 213 213 LYS H H 8.340 0.005 1 993 213 213 LYS C C 178.150 0.050 1 994 213 213 LYS CA C 60.508 0.050 1 995 213 213 LYS CB C 32.034 0.050 1 996 213 213 LYS N N 116.254 0.050 1 997 214 214 GLU C C 179.568 0.050 1 998 214 214 GLU CA C 59.058 0.050 1 999 214 214 GLU CB C 28.652 0.050 1 1000 215 215 VAL H H 8.226 0.005 1 1001 215 215 VAL C C 178.362 0.050 1 1002 215 215 VAL CA C 65.695 0.050 1 1003 215 215 VAL CB C 30.703 0.050 1 1004 215 215 VAL N N 120.539 0.050 1 1005 216 216 TRP H H 8.406 0.005 1 1006 216 216 TRP C C 178.619 0.050 1 1007 216 216 TRP CA C 60.552 0.050 1 1008 216 216 TRP CB C 29.039 0.050 1 1009 216 216 TRP N N 120.760 0.050 1 1010 217 217 LEU H H 8.152 0.005 1 1011 217 217 LEU C C 179.891 0.050 1 1012 217 217 LEU CA C 56.971 0.050 1 1013 217 217 LEU CB C 40.956 0.050 1 1014 217 217 LEU N N 117.087 0.050 1 1015 218 218 GLN H H 7.809 0.005 1 1016 218 218 GLN C C 177.726 0.050 1 1017 218 218 GLN CA C 57.172 0.050 1 1018 218 218 GLN CB C 28.008 0.050 1 1019 218 218 GLN N N 118.366 0.050 1 1020 219 219 LYS H H 7.513 0.005 1 1021 219 219 LYS C C 176.539 0.050 1 1022 219 219 LYS CA C 55.347 0.050 1 1023 219 219 LYS CB C 31.451 0.050 1 1024 219 219 LYS N N 117.830 0.050 1 1025 220 220 GLN H H 7.610 0.005 1 1026 220 220 GLN C C 175.016 0.050 1 1027 220 220 GLN CA C 55.148 0.050 1 1028 220 220 GLN CB C 27.771 0.050 1 1029 220 220 GLN N N 119.875 0.050 1 1030 221 221 LYS H H 7.520 0.005 1 1031 221 221 LYS C C 181.490 0.050 1 1032 221 221 LYS CA C 57.164 0.050 1 1033 221 221 LYS CB C 32.332 0.050 1 1034 221 221 LYS N N 127.373 0.050 1 stop_ save_ save_assigned_chem_shift_list_1_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N TROSY' '3D TROSY HNCA' '3D TROSY HN(CO)CA' '3D TROSY HN(CA)CO' '3D TROSY HNCO' '3D TROSY HN(CA)CB' '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 trifluoroberyllate_ion _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 BEF F1 F -150.2 0.050 1 2 . 1 BEF F2 F -150.6 0.050 1 stop_ save_