data_7234 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N, and 13C assignments for beta phosphoglucomutase in a ternary complex with glucose-6-phosphate and MgF3- ; _BMRB_accession_number 7234 _BMRB_flat_file_name bmr7234.str _Entry_type original _Submission_date 2006-07-13 _Accession_date 2006-07-14 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Also included is the assignment of the three 19F resonances present in the ternary complex of beta phosphoglucomutase glucose-6-phosphate and MgF3- ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Baxter Nicola J. . 2 Waltho Jonathan P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 210 "13C chemical shifts" 646 "15N chemical shifts" 210 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-09-20 update author 'complete entry citation' 2006-09-08 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'A trojan horse transition state analogue generated by MgF3- formation in an enzyme active site' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16990434 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Baxter Nicola J. . 2 Olguin Luis F. . 3 Golicnik Marko . . 4 Feng Guoqiang . . 5 Hounslow Andrea M. . 6 Bermel Wolfgang . . 7 Blackburn G. Michael . 8 Hollfelder Florian . . 9 Waltho Jonathan P. . 10 Williams Nicholas H. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 103 _Journal_issue 40 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 14732 _Page_last 14737 _Year 2006 _Details 'The first three authors contributed equally to this publication' loop_ _Keyword 'active site' 'MgF3- transition state analogue' 'NOE directed docking of fluoride ions' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'beta phosphoglucomutase' _Enzyme_commission_number 5.4.2.6 loop_ _Mol_system_component_name _Mol_label 'beta phosphoglucomutase' $beta_phosphoglucomutase glucose-6-phosphate $BG6 'magnesium trifluoride ion' $MGF stop_ _System_molecular_weight 25000 _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function mutase stop_ _Database_query_date . _Details . 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 'inhibited mutase' stop_ _Details ; A single catalytic magnsium ion is present in the protein. This is a ternary complex composed of beta phosphoglucomutase, glucose-6-phosphate and MgF3- forming a closed protein conformation and a transition state analogue. ; ############################## # Polymer residue sequence # ############################## _Residue_count 221 _Mol_residue_sequence ; MFKAVLFDLDGVITDTAEYH FRAWKALAEEIGINGVDRQF NEQLKGVSREDSLQKILDLA DKKVSAEEFKELAKRKNDNY VKMIQDVSPADVYPGILQLL KDLRSNKIKIALASASKNGP FLLERMNLTGYFDAIADPAE VAASKPAPDIFIAAAHAVGV APSESIGLEDSQAGIQAIKD SGALPIGVGRPEDLGDDIVI VPDTSHYTLEFLKEVWLQKQ K ; loop_ _Residue_seq_code _Residue_label 1 MET 2 PHE 3 LYS 4 ALA 5 VAL 6 LEU 7 PHE 8 ASP 9 LEU 10 ASP 11 GLY 12 VAL 13 ILE 14 THR 15 ASP 16 THR 17 ALA 18 GLU 19 TYR 20 HIS 21 PHE 22 ARG 23 ALA 24 TRP 25 LYS 26 ALA 27 LEU 28 ALA 29 GLU 30 GLU 31 ILE 32 GLY 33 ILE 34 ASN 35 GLY 36 VAL 37 ASP 38 ARG 39 GLN 40 PHE 41 ASN 42 GLU 43 GLN 44 LEU 45 LYS 46 GLY 47 VAL 48 SER 49 ARG 50 GLU 51 ASP 52 SER 53 LEU 54 GLN 55 LYS 56 ILE 57 LEU 58 ASP 59 LEU 60 ALA 61 ASP 62 LYS 63 LYS 64 VAL 65 SER 66 ALA 67 GLU 68 GLU 69 PHE 70 LYS 71 GLU 72 LEU 73 ALA 74 LYS 75 ARG 76 LYS 77 ASN 78 ASP 79 ASN 80 TYR 81 VAL 82 LYS 83 MET 84 ILE 85 GLN 86 ASP 87 VAL 88 SER 89 PRO 90 ALA 91 ASP 92 VAL 93 TYR 94 PRO 95 GLY 96 ILE 97 LEU 98 GLN 99 LEU 100 LEU 101 LYS 102 ASP 103 LEU 104 ARG 105 SER 106 ASN 107 LYS 108 ILE 109 LYS 110 ILE 111 ALA 112 LEU 113 ALA 114 SER 115 ALA 116 SER 117 LYS 118 ASN 119 GLY 120 PRO 121 PHE 122 LEU 123 LEU 124 GLU 125 ARG 126 MET 127 ASN 128 LEU 129 THR 130 GLY 131 TYR 132 PHE 133 ASP 134 ALA 135 ILE 136 ALA 137 ASP 138 PRO 139 ALA 140 GLU 141 VAL 142 ALA 143 ALA 144 SER 145 LYS 146 PRO 147 ALA 148 PRO 149 ASP 150 ILE 151 PHE 152 ILE 153 ALA 154 ALA 155 ALA 156 HIS 157 ALA 158 VAL 159 GLY 160 VAL 161 ALA 162 PRO 163 SER 164 GLU 165 SER 166 ILE 167 GLY 168 LEU 169 GLU 170 ASP 171 SER 172 GLN 173 ALA 174 GLY 175 ILE 176 GLN 177 ALA 178 ILE 179 LYS 180 ASP 181 SER 182 GLY 183 ALA 184 LEU 185 PRO 186 ILE 187 GLY 188 VAL 189 GLY 190 ARG 191 PRO 192 GLU 193 ASP 194 LEU 195 GLY 196 ASP 197 ASP 198 ILE 199 VAL 200 ILE 201 VAL 202 PRO 203 ASP 204 THR 205 SER 206 HIS 207 TYR 208 THR 209 LEU 210 GLU 211 PHE 212 LEU 213 LYS 214 GLU 215 VAL 216 TRP 217 LEU 218 GLN 219 LYS 220 GLN 221 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 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 2.50e-156 BMRB 16409 beta_phosphoglucomutase 100.00 221 100.00 100.00 2.50e-156 BMRB 17851 beta_phosphoglucomutase 100.00 221 100.00 100.00 2.50e-156 BMRB 17852 beta_phosphoglucomutase 100.00 221 100.00 100.00 2.50e-156 BMRB 7235 beta_phosphoglucomutase 100.00 221 100.00 100.00 2.50e-156 PDB 1LVH "The Structure Of Phosphorylated Beta-phosphoglucomutase From Lactoccocus Lactis To 2.3 Angstrom Resolution" 100.00 221 99.55 99.55 2.13e-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 2.50e-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 2.50e-156 PDB 1Z4N "Structure Of Beta-phosphoglucomutase With Inhibitor Bound Alpha-galactose 1-phosphate Cocrystallized With Fluoride" 100.00 221 100.00 100.00 2.50e-156 PDB 1Z4O "Structure Of Beta-Phosphoglucomutase With Inhibitor Bound Alpha-Galactose 1-Phosphate" 100.00 221 100.00 100.00 2.50e-156 PDB 1ZOL "Native Beta-Pgm" 100.00 221 100.00 100.00 2.50e-156 PDB 2WF5 "Structure Of Beta-Phosphoglucomutase Inhibited With Glucose- 6-Phospahte And Trifluoromagnesate" 100.00 221 100.00 100.00 2.50e-156 PDB 2WF6 "Structure Of Beta-Phosphoglucomutase Inhibited With Glucose- 6-Phospahte And Aluminium Tetrafluoride" 100.00 221 100.00 100.00 2.50e-156 PDB 2WF7 "Structure Of Beta-phosphoglucomutase Inhibited With Glucose- 6-phosphonate And Aluminium Tetrafluoride" 100.00 221 100.00 100.00 2.50e-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 2.50e-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 2.50e-156 PDB 2WFA "Structure Of Beta-Phosphoglucomutase Inhibited With Beryllium Trifluoride, In An Open Conformation." 100.00 221 100.00 100.00 2.50e-156 PDB 2WHE "Structure Of Native Beta-Phosphoglucomutase In An Open Conformation Without Bound Ligands." 100.00 221 100.00 100.00 2.50e-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 4.90e-155 PDB 3ZI4 "The Structure Of Beta-phosphoglucomutase Inhibited With Glucose-6-phospahte And Scandium Tetrafluoride" 100.00 221 100.00 100.00 2.50e-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 2.50e-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 2.50e-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 2.50e-156 DBJ BAL50396 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis IO-1]" 100.00 221 100.00 100.00 2.50e-156 EMBL CAA94734 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 100.00 100.00 2.50e-156 EMBL CDG03643 "Beta-phosphoglucomutase [Lactococcus lactis subsp. lactis A12]" 100.00 221 99.55 99.55 3.34e-155 EMBL CDI46177 "Beta-phosphoglucomutase [Lactococcus lactis subsp. lactis Dephy 1]" 100.00 221 100.00 100.00 2.50e-156 GB AAK04527 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis Il1403]" 100.00 221 99.10 100.00 1.17e-154 GB ADA64250 "Beta-phosphoglucomutase [Lactococcus lactis subsp. lactis KF147]" 100.00 221 100.00 100.00 2.50e-156 GB ADZ63078 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis CV56]" 100.00 221 99.55 100.00 2.93e-155 GB AEE43918 "beta-phosphoglucomutase [synthetic construct]" 100.00 221 99.10 100.00 1.17e-154 GB AGY43735 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis KLDS 4.0325]" 100.00 221 98.64 100.00 2.58e-154 REF NP_266585 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis Il1403]" 100.00 221 99.10 100.00 1.17e-154 REF WP_003131530 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 99.55 100.00 2.93e-155 REF WP_010905331 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 99.10 100.00 1.17e-154 REF WP_012897250 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 100.00 100.00 2.50e-156 REF WP_021469610 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 99.55 99.55 4.11e-155 SP P71447 "RecName: Full=Beta-phosphoglucomutase; Short=Beta-PGM [Lactococcus lactis subsp. lactis Il1403]" 100.00 221 99.10 100.00 1.17e-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 Tue Sep 20 17:56:00 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_MGF _Saveframe_category ligand _Mol_type non-polymer _Name_common "MGF (TRIFLUOROMAGNESATE)" _BMRB_code . _PDB_code MGF _Molecular_mass 81.300 _Mol_charge -1 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Sep 20 17:57:51 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons F1 F1 F . 0 . ? MG MG MG . -1 . ? F2 F2 F . 0 . ? F3 F3 F . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING F1 MG ? ? SING MG F2 ? ? SING MG F3 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $beta_phosphoglucomutase 'Lactococcus lactis' 1360 Eubacteria 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_type _Vector_name _Vendor_name $beta_phosphoglucomutase 'recombinant technology' 'E. coli' . . . plasmid . Novagen stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_closed_2H15N13C _Saveframe_category sample _Sample_type solution _Details ; beta phosphoglucomutase closed conformation with glucose-6-phosphate and MgF3- forming a transition state analogue ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $beta_phosphoglucomutase 1 mM '[U-2H; U-15N; U-13C]' 'magnesium chloride' 5 mM . 'ammonium fluoride' 10 mM . 'sodium azide' 2 mM . 'deuterium oxide' 15 % . 'protease inhibitor' 1 times . 'potassium HEPES' 50 mM . glucose-6-phosphate 20 mM . stop_ save_ save_sample_closed_2H15N _Saveframe_category sample _Sample_type solution _Details ; beta phosphoglucomutase closed conformation with glucose-6-phosphate and MgF3- forming a transition state analogue ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $beta_phosphoglucomutase 1 mM '[U-2H; U-15N]' 'magnesium chloride' 5 mM . 'ammonium fluoride' 10 mM . 'sodium azide' 2 mM . 'deuterium oxide' 15 % . 'protease inhibitor' 1 times . 'potassium HEPES' 50 mM . glucose-6-phosphate 20 mM . stop_ save_ ############################ # Computer software used # ############################ save_software_xwinnmr _Saveframe_category software _Name xwinnmr _Version . loop_ _Vendor _Address _Electronic_address 'Bruker BioSpin Ltd' ; Banner Lane Coventry CV4 9GH ; . stop_ loop_ _Task 'data acquisition' stop_ _Details 'software for data acquisition' save_ save_software_felix _Saveframe_category software _Name FELIX _Version 2004 loop_ _Vendor _Address _Electronic_address 'Accelrys Inc' ; San Diego CA USA ; . stop_ loop_ _Task 'data analysis' 'data processing' stop_ _Details 'software for data processing and analysis' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N TROSY' _Sample_label $sample_closed_2H15N13C save_ save_TROSY_ct-HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY ct-HNCA' _Sample_label $sample_closed_2H15N13C save_ save_TROSY_ct-HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY ct-HN(CO)CA' _Sample_label $sample_closed_2H15N13C save_ save_TROSY_HN(CA)CB_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY HN(CA)CB' _Sample_label $sample_closed_2H15N13C save_ save_TROSY_HN(COCA)CB_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY HN(COCA)CB' _Sample_label $sample_closed_2H15N13C save_ save_TROSY_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY HN(CA)CO' _Sample_label $sample_closed_2H15N13C save_ save_TROSY_HNCO_7 _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY HNCO' _Sample_label $sample_closed_2H15N13C save_ save_{19F}1H,15N-HSQC_NOE_difference_8 _Saveframe_category NMR_applied_experiment _Experiment_name '{19F}1H,15N-HSQC NOE difference' _Sample_label $sample_closed_2H15N save_ save_19F_1D_9 _Saveframe_category NMR_applied_experiment _Experiment_name '19F 1D' _Sample_label $sample_closed_2H15N save_ save_15N_TROSY _Saveframe_category NMR_applied_experiment _Experiment_name '15N TROSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY_ct-HNCA _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY ct-HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY_ct-HN(CO)CA _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY ct-HN(CO)CA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY_HN(CA)CB _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY HN(CA)CB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY_HN(COCA)CB _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY HN(COCA)CB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY_HN(CA)CO _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY HN(CA)CO' _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY_HNCO _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY HNCO' _BMRB_pulse_sequence_accession_number . _Details . save_ save_19F-1H-15N-HSQC_NOE_difference _Saveframe_category NMR_applied_experiment _Experiment_name '{19F}1H,15N-HSQC NOE difference' _BMRB_pulse_sequence_accession_number . _Details . save_ save_19F_1D _Saveframe_category NMR_applied_experiment _Experiment_name '19F 1D' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.2 pH temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $citation_1 $citation_1 trichlorofluoromethane F 19 'methyl fluorine' ppm 0 . indirect . . . 0.94094008 $citation_1 $citation_1 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $citation_1 $citation_1 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $citation_1 $citation_1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_list_closed _Saveframe_category assigned_chemical_shifts _Details ; beta phosphoglucomutase closed conformation with glucose-6-phosphate and MgF3- forming a transition state analogue ; loop_ _Software_label $software_xwinnmr $software_felix stop_ loop_ _Experiment_label '15N TROSY' 'TROSY ct-HNCA' 'TROSY ct-HN(CO)CA' 'TROSY HN(CA)CB' 'TROSY HN(COCA)CB' 'TROSY HN(CA)CO' 'TROSY HNCO' '{19F}1H,15N-HSQC NOE difference' '19F 1D' stop_ loop_ _Sample_label $sample_closed_2H15N13C $sample_closed_2H15N stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _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 5.266 0.005 1 2 2 2 PHE C C 173.943 0.050 1 3 2 2 PHE CA C 55.794 0.050 1 4 2 2 PHE CB C 36.046 0.050 1 5 2 2 PHE N N 117.375 0.050 1 6 3 3 LYS H H 8.746 0.005 1 7 3 3 LYS C C 176.589 0.050 1 8 3 3 LYS CA C 55.623 0.050 1 9 3 3 LYS CB C 35.723 0.050 1 10 3 3 LYS N N 116.464 0.050 1 11 4 4 ALA H H 7.658 0.005 1 12 4 4 ALA C C 175.332 0.050 1 13 4 4 ALA CA C 50.701 0.050 1 14 4 4 ALA CB C 22.598 0.050 1 15 4 4 ALA N N 121.179 0.050 1 16 5 5 VAL H H 8.674 0.005 1 17 5 5 VAL C C 172.820 0.050 1 18 5 5 VAL CA C 61.002 0.050 1 19 5 5 VAL CB C 32.823 0.050 1 20 5 5 VAL N N 120.110 0.050 1 21 6 6 LEU H H 9.353 0.005 1 22 6 6 LEU C C 175.592 0.050 1 23 6 6 LEU CA C 51.516 0.050 1 24 6 6 LEU CB C 40.269 0.050 1 25 6 6 LEU N N 126.299 0.050 1 26 7 7 PHE H H 9.580 0.005 1 27 7 7 PHE C C 177.690 0.050 1 28 7 7 PHE CA C 59.208 0.050 1 29 7 7 PHE CB C 40.510 0.050 1 30 7 7 PHE N N 123.104 0.050 1 31 8 8 ASP H H 7.397 0.005 1 32 8 8 ASP C C 172.792 0.050 1 33 8 8 ASP CA C 54.395 0.050 1 34 8 8 ASP CB C 43.811 0.050 1 35 8 8 ASP N N 122.909 0.050 1 36 9 9 LEU H H 7.840 0.005 1 37 9 9 LEU C C 179.921 0.050 1 38 9 9 LEU CA C 56.557 0.050 1 39 9 9 LEU CB C 44.119 0.050 1 40 9 9 LEU N N 120.370 0.050 1 41 10 10 ASP H H 9.708 0.005 1 42 10 10 ASP C C 176.342 0.050 1 43 10 10 ASP CA C 56.563 0.050 1 44 10 10 ASP CB C 38.331 0.050 1 45 10 10 ASP N N 124.727 0.050 1 46 11 11 GLY H H 8.852 0.005 1 47 11 11 GLY C C 171.566 0.050 1 48 11 11 GLY CA C 45.428 0.050 1 49 11 11 GLY N N 117.188 0.050 1 50 12 12 VAL H H 7.805 0.005 1 51 12 12 VAL C C 173.409 0.050 1 52 12 12 VAL CA C 64.481 0.050 1 53 12 12 VAL CB C 33.150 0.050 1 54 12 12 VAL N N 119.381 0.050 1 55 13 13 ILE H H 8.728 0.005 1 56 13 13 ILE C C 175.348 0.050 1 57 13 13 ILE CA C 63.078 0.050 1 58 13 13 ILE CB C 38.128 0.050 1 59 13 13 ILE N N 115.953 0.050 1 60 14 14 THR H H 7.233 0.005 1 61 14 14 THR C C 173.189 0.050 1 62 14 14 THR CA C 59.383 0.050 1 63 14 14 THR CB C 67.631 0.050 1 64 14 14 THR N N 110.373 0.050 1 65 15 15 ASP H H 8.010 0.005 1 66 15 15 ASP C C 177.166 0.050 1 67 15 15 ASP CA C 53.928 0.050 1 68 15 15 ASP CB C 39.855 0.050 1 69 15 15 ASP N N 127.718 0.050 1 70 16 16 THR H H 7.758 0.005 1 71 16 16 THR C C 178.815 0.050 1 72 16 16 THR CA C 63.498 0.050 1 73 16 16 THR CB C 65.899 0.050 1 74 16 16 THR N N 108.996 0.050 1 75 17 17 ALA H H 7.186 0.005 1 76 17 17 ALA C C 181.536 0.050 1 77 17 17 ALA CA C 55.185 0.050 1 78 17 17 ALA CB C 16.800 0.050 1 79 17 17 ALA N N 124.267 0.050 1 80 18 18 GLU H H 8.078 0.005 1 81 18 18 GLU C C 178.188 0.050 1 82 18 18 GLU CA C 58.358 0.050 1 83 18 18 GLU CB C 28.364 0.050 1 84 18 18 GLU N N 122.304 0.050 1 85 19 19 TYR H H 6.604 0.005 1 86 19 19 TYR C C 178.010 0.050 1 87 19 19 TYR CA C 59.601 0.050 1 88 19 19 TYR CB C 36.515 0.050 1 89 19 19 TYR N N 118.357 0.050 1 90 20 20 HIS H H 8.433 0.005 1 91 20 20 HIS C C 177.600 0.050 1 92 20 20 HIS CA C 61.245 0.050 1 93 20 20 HIS CB C 31.303 0.050 1 94 20 20 HIS N N 120.793 0.050 1 95 21 21 PHE H H 7.801 0.005 1 96 21 21 PHE C C 176.614 0.050 1 97 21 21 PHE CA C 59.712 0.050 1 98 21 21 PHE CB C 37.715 0.050 1 99 21 21 PHE N N 117.935 0.050 1 100 22 22 ARG H H 8.405 0.005 1 101 22 22 ARG C C 179.942 0.050 1 102 22 22 ARG CA C 59.105 0.050 1 103 22 22 ARG CB C 29.776 0.050 1 104 22 22 ARG N N 117.841 0.050 1 105 23 23 ALA H H 8.565 0.005 1 106 23 23 ALA C C 180.433 0.050 1 107 23 23 ALA CA C 54.540 0.050 1 108 23 23 ALA CB C 18.021 0.050 1 109 23 23 ALA N N 122.098 0.050 1 110 24 24 TRP H H 8.900 0.005 1 111 24 24 TRP C C 178.582 0.050 1 112 24 24 TRP CA C 59.594 0.050 1 113 24 24 TRP CB C 29.191 0.050 1 114 24 24 TRP N N 121.950 0.050 1 115 25 25 LYS H H 8.932 0.005 1 116 25 25 LYS C C 178.075 0.050 1 117 25 25 LYS CA C 59.704 0.050 1 118 25 25 LYS CB C 31.739 0.050 1 119 25 25 LYS N N 120.924 0.050 1 120 26 26 ALA H H 7.687 0.005 1 121 26 26 ALA C C 180.741 0.050 1 122 26 26 ALA CA C 54.252 0.050 1 123 26 26 ALA CB C 17.236 0.050 1 124 26 26 ALA N N 119.746 0.050 1 125 27 27 LEU H H 7.583 0.005 1 126 27 27 LEU C C 178.705 0.050 1 127 27 27 LEU CA C 56.865 0.050 1 128 27 27 LEU CB C 40.851 0.050 1 129 27 27 LEU N N 121.071 0.050 1 130 28 28 ALA H H 8.635 0.005 1 131 28 28 ALA C C 179.940 0.050 1 132 28 28 ALA CA C 55.082 0.050 1 133 28 28 ALA CB C 17.617 0.050 1 134 28 28 ALA N N 121.116 0.050 1 135 29 29 GLU H H 8.332 0.005 1 136 29 29 GLU C C 180.673 0.050 1 137 29 29 GLU CA C 58.892 0.050 1 138 29 29 GLU CB C 28.368 0.050 1 139 29 29 GLU N N 117.024 0.050 1 140 30 30 GLU H H 7.928 0.005 1 141 30 30 GLU C C 178.945 0.050 1 142 30 30 GLU CA C 58.996 0.050 1 143 30 30 GLU CB C 29.021 0.050 1 144 30 30 GLU N N 121.789 0.050 1 145 31 31 ILE H H 7.603 0.005 1 146 31 31 ILE C C 175.926 0.050 1 147 31 31 ILE CA C 60.684 0.050 1 148 31 31 ILE CB C 36.892 0.050 1 149 31 31 ILE N N 111.721 0.050 1 150 32 32 GLY H H 7.550 0.005 1 151 32 32 GLY C C 174.462 0.050 1 152 32 32 GLY CA C 45.912 0.050 1 153 32 32 GLY N N 109.531 0.050 1 154 33 33 ILE H H 8.404 0.005 1 155 33 33 ILE C C 175.070 0.050 1 156 33 33 ILE CA C 61.005 0.050 1 157 33 33 ILE CB C 38.389 0.050 1 158 33 33 ILE N N 123.236 0.050 1 159 34 34 ASN H H 8.483 0.005 1 160 34 34 ASN C C 175.386 0.050 1 161 34 34 ASN CA C 52.664 0.050 1 162 34 34 ASN CB C 39.523 0.050 1 163 34 34 ASN N N 126.218 0.050 1 164 35 35 GLY H H 7.758 0.005 1 165 35 35 GLY C C 174.040 0.050 1 166 35 35 GLY CA C 44.831 0.050 1 167 35 35 GLY N N 106.949 0.050 1 168 36 36 VAL H H 8.647 0.005 1 169 36 36 VAL C C 173.580 0.050 1 170 36 36 VAL CA C 62.267 0.050 1 171 36 36 VAL CB C 27.989 0.050 1 172 36 36 VAL N N 123.324 0.050 1 173 37 37 ASP H H 7.505 0.005 1 174 37 37 ASP C C 176.377 0.050 1 175 37 37 ASP CA C 50.746 0.050 1 176 37 37 ASP CB C 41.791 0.050 1 177 37 37 ASP N N 126.816 0.050 1 178 38 38 ARG H H 8.395 0.005 1 179 38 38 ARG C C 178.667 0.050 1 180 38 38 ARG CA C 59.624 0.050 1 181 38 38 ARG CB C 28.513 0.050 1 182 38 38 ARG N N 118.903 0.050 1 183 39 39 GLN H H 8.007 0.005 1 184 39 39 GLN C C 179.941 0.050 1 185 39 39 GLN CA C 58.756 0.050 1 186 39 39 GLN CB C 27.491 0.050 1 187 39 39 GLN N N 119.950 0.050 1 188 40 40 PHE H H 8.882 0.005 1 189 40 40 PHE C C 177.766 0.050 1 190 40 40 PHE CA C 61.391 0.050 1 191 40 40 PHE CB C 39.063 0.050 1 192 40 40 PHE N N 125.310 0.050 1 193 41 41 ASN H H 8.625 0.005 1 194 41 41 ASN C C 177.224 0.050 1 195 41 41 ASN CA C 55.810 0.050 1 196 41 41 ASN CB C 39.301 0.050 1 197 41 41 ASN N N 114.924 0.050 1 198 42 42 GLU H H 7.432 0.005 1 199 42 42 GLU C C 179.684 0.050 1 200 42 42 GLU CA C 59.078 0.050 1 201 42 42 GLU CB C 28.425 0.050 1 202 42 42 GLU N N 118.389 0.050 1 203 43 43 GLN H H 8.076 0.005 1 204 43 43 GLN C C 174.726 0.050 1 205 43 43 GLN CA C 56.397 0.050 1 206 43 43 GLN CB C 28.162 0.050 1 207 43 43 GLN N N 116.924 0.050 1 208 44 44 LEU H H 7.074 0.005 1 209 44 44 LEU C C 179.573 0.050 1 210 44 44 LEU CA C 53.759 0.050 1 211 44 44 LEU CB C 40.209 0.050 1 212 44 44 LEU N N 115.861 0.050 1 213 45 45 LYS H H 7.161 0.005 1 214 45 45 LYS C C 176.717 0.050 1 215 45 45 LYS CA C 59.177 0.050 1 216 45 45 LYS CB C 32.938 0.050 1 217 45 45 LYS N N 122.735 0.050 1 218 46 46 GLY H H 8.826 0.005 1 219 46 46 GLY C C 171.011 0.050 1 220 46 46 GLY CA C 45.468 0.050 1 221 46 46 GLY N N 111.356 0.050 1 222 47 47 VAL H H 6.954 0.005 1 223 47 47 VAL C C 176.248 0.050 1 224 47 47 VAL CA C 61.307 0.050 1 225 47 47 VAL CB C 30.948 0.050 1 226 47 47 VAL N N 116.818 0.050 1 227 48 48 SER H H 8.685 0.005 1 228 48 48 SER C C 174.366 0.050 1 229 48 48 SER CA C 58.572 0.050 1 230 48 48 SER CB C 65.343 0.050 1 231 48 48 SER N N 119.517 0.050 1 232 49 49 ARG H H 8.848 0.005 1 233 49 49 ARG C C 178.022 0.050 1 234 49 49 ARG CA C 60.032 0.050 1 235 49 49 ARG CB C 31.358 0.050 1 236 49 49 ARG N N 126.549 0.050 1 237 50 50 GLU H H 8.996 0.005 1 238 50 50 GLU C C 178.523 0.050 1 239 50 50 GLU CA C 61.301 0.050 1 240 50 50 GLU CB C 27.836 0.050 1 241 50 50 GLU N N 117.101 0.050 1 242 51 51 ASP H H 7.890 0.005 1 243 51 51 ASP C C 179.182 0.050 1 244 51 51 ASP CA C 56.782 0.050 1 245 51 51 ASP CB C 39.476 0.050 1 246 51 51 ASP N N 120.173 0.050 1 247 52 52 SER H H 8.407 0.005 1 248 52 52 SER C C 173.836 0.050 1 249 52 52 SER CA C 62.163 0.050 1 250 52 52 SER CB C 63.087 0.050 1 251 52 52 SER N N 118.837 0.050 1 252 53 53 LEU H H 7.173 0.005 1 253 53 53 LEU C C 178.129 0.050 1 254 53 53 LEU CA C 56.764 0.050 1 255 53 53 LEU CB C 38.741 0.050 1 256 53 53 LEU N N 121.381 0.050 1 257 54 54 GLN H H 8.196 0.005 1 258 54 54 GLN C C 177.426 0.050 1 259 54 54 GLN CA C 58.331 0.050 1 260 54 54 GLN CB C 28.253 0.050 1 261 54 54 GLN N N 117.640 0.050 1 262 55 55 LYS H H 7.666 0.005 1 263 55 55 LYS C C 179.835 0.050 1 264 55 55 LYS CA C 59.806 0.050 1 265 55 55 LYS CB C 31.914 0.050 1 266 55 55 LYS N N 118.034 0.050 1 267 56 56 ILE H H 7.535 0.005 1 268 56 56 ILE C C 177.219 0.050 1 269 56 56 ILE CA C 65.315 0.050 1 270 56 56 ILE CB C 37.686 0.050 1 271 56 56 ILE N N 121.009 0.050 1 272 57 57 LEU H H 8.454 0.005 1 273 57 57 LEU C C 180.962 0.050 1 274 57 57 LEU CA C 57.808 0.050 1 275 57 57 LEU CB C 38.974 0.050 1 276 57 57 LEU N N 119.366 0.050 1 277 58 58 ASP H H 8.647 0.005 1 278 58 58 ASP C C 179.465 0.050 1 279 58 58 ASP CA C 56.458 0.050 1 280 58 58 ASP CB C 39.502 0.050 1 281 58 58 ASP N N 119.450 0.050 1 282 59 59 LEU H H 7.664 0.005 1 283 59 59 LEU C C 178.130 0.050 1 284 59 59 LEU CA C 57.398 0.050 1 285 59 59 LEU CB C 40.734 0.050 1 286 59 59 LEU N N 123.589 0.050 1 287 60 60 ALA H H 6.997 0.005 1 288 60 60 ALA C C 176.090 0.050 1 289 60 60 ALA CA C 50.221 0.050 1 290 60 60 ALA CB C 20.401 0.050 1 291 60 60 ALA N N 118.834 0.050 1 292 61 61 ASP H H 7.894 0.005 1 293 61 61 ASP C C 174.674 0.050 1 294 61 61 ASP CA C 54.983 0.050 1 295 61 61 ASP CB C 39.444 0.050 1 296 61 61 ASP N N 120.927 0.050 1 297 62 62 LYS H H 7.878 0.005 1 298 62 62 LYS C C 175.408 0.050 1 299 62 62 LYS CA C 55.479 0.050 1 300 62 62 LYS CB C 33.319 0.050 1 301 62 62 LYS N N 118.800 0.050 1 302 63 63 LYS H H 8.508 0.005 1 303 63 63 LYS C C 176.348 0.050 1 304 63 63 LYS CA C 54.328 0.050 1 305 63 63 LYS CB C 32.236 0.050 1 306 63 63 LYS N N 126.855 0.050 1 307 64 64 VAL H H 8.417 0.005 1 308 64 64 VAL C C 175.805 0.050 1 309 64 64 VAL CA C 58.227 0.050 1 310 64 64 VAL CB C 34.477 0.050 1 311 64 64 VAL N N 116.665 0.050 1 312 65 65 SER H H 9.019 0.005 1 313 65 65 SER C C 174.602 0.050 1 314 65 65 SER CA C 57.102 0.050 1 315 65 65 SER CB C 64.755 0.050 1 316 65 65 SER N N 119.620 0.050 1 317 66 66 ALA H H 8.912 0.005 1 318 66 66 ALA C C 181.038 0.050 1 319 66 66 ALA CA C 55.062 0.050 1 320 66 66 ALA CB C 17.237 0.050 1 321 66 66 ALA N N 124.311 0.050 1 322 67 67 GLU H H 8.587 0.005 1 323 67 67 GLU C C 179.437 0.050 1 324 67 67 GLU CA C 59.490 0.050 1 325 67 67 GLU CB C 28.517 0.050 1 326 67 67 GLU N N 118.027 0.050 1 327 68 68 GLU H H 7.894 0.005 1 328 68 68 GLU C C 178.528 0.050 1 329 68 68 GLU CA C 58.684 0.050 1 330 68 68 GLU CB C 29.541 0.050 1 331 68 68 GLU N N 122.977 0.050 1 332 69 69 PHE H H 8.844 0.005 1 333 69 69 PHE C C 176.718 0.050 1 334 69 69 PHE CA C 61.837 0.050 1 335 69 69 PHE CB C 38.974 0.050 1 336 69 69 PHE N N 121.589 0.050 1 337 70 70 LYS H H 7.673 0.005 1 338 70 70 LYS C C 180.065 0.050 1 339 70 70 LYS CA C 59.105 0.050 1 340 70 70 LYS CB C 31.855 0.050 1 341 70 70 LYS N N 116.359 0.050 1 342 71 71 GLU H H 7.810 0.005 1 343 71 71 GLU C C 178.912 0.050 1 344 71 71 GLU CA C 58.777 0.050 1 345 71 71 GLU CB C 28.486 0.050 1 346 71 71 GLU N N 121.217 0.050 1 347 72 72 LEU H H 8.410 0.005 1 348 72 72 LEU C C 178.234 0.050 1 349 72 72 LEU CA C 57.613 0.050 1 350 72 72 LEU CB C 41.729 0.050 1 351 72 72 LEU N N 122.131 0.050 1 352 73 73 ALA H H 7.737 0.005 1 353 73 73 ALA C C 179.020 0.050 1 354 73 73 ALA CA C 55.074 0.050 1 355 73 73 ALA CB C 16.064 0.050 1 356 73 73 ALA N N 120.686 0.050 1 357 74 74 LYS H H 7.681 0.005 1 358 74 74 LYS C C 178.239 0.050 1 359 74 74 LYS CA C 59.070 0.050 1 360 74 74 LYS CB C 31.532 0.050 1 361 74 74 LYS N N 118.934 0.050 1 362 75 75 ARG H H 8.314 0.005 1 363 75 75 ARG C C 179.522 0.050 1 364 75 75 ARG CA C 59.179 0.050 1 365 75 75 ARG CB C 29.543 0.050 1 366 75 75 ARG N N 121.463 0.050 1 367 76 76 LYS H H 7.817 0.005 1 368 76 76 LYS C C 179.176 0.050 1 369 76 76 LYS CA C 59.509 0.050 1 370 76 76 LYS CB C 29.646 0.050 1 371 76 76 LYS N N 119.720 0.050 1 372 77 77 ASN H H 8.019 0.005 1 373 77 77 ASN C C 175.988 0.050 1 374 77 77 ASN CA C 57.062 0.050 1 375 77 77 ASN CB C 38.009 0.050 1 376 77 77 ASN N N 118.747 0.050 1 377 78 78 ASP H H 8.959 0.005 1 378 78 78 ASP C C 179.242 0.050 1 379 78 78 ASP CA C 56.890 0.050 1 380 78 78 ASP CB C 39.238 0.050 1 381 78 78 ASP N N 119.419 0.050 1 382 79 79 ASN H H 7.500 0.005 1 383 79 79 ASN C C 176.926 0.050 1 384 79 79 ASN CA C 55.065 0.050 1 385 79 79 ASN CB C 37.748 0.050 1 386 79 79 ASN N N 118.902 0.050 1 387 80 80 TYR H H 8.640 0.005 1 388 80 80 TYR C C 176.769 0.050 1 389 80 80 TYR CA C 61.603 0.050 1 390 80 80 TYR CB C 38.682 0.050 1 391 80 80 TYR N N 123.255 0.050 1 392 81 81 VAL H H 8.929 0.005 1 393 81 81 VAL C C 179.024 0.050 1 394 81 81 VAL CA C 65.623 0.050 1 395 81 81 VAL CB C 30.537 0.050 1 396 81 81 VAL N N 118.330 0.050 1 397 82 82 LYS H H 7.006 0.005 1 398 82 82 LYS C C 179.468 0.050 1 399 82 82 LYS CA C 58.894 0.050 1 400 82 82 LYS CB C 31.212 0.050 1 401 82 82 LYS N N 118.927 0.050 1 402 83 83 MET H H 7.554 0.005 1 403 83 83 MET C C 178.315 0.050 1 404 83 83 MET CA C 58.367 0.050 1 405 83 83 MET CB C 32.030 0.050 1 406 83 83 MET N N 118.476 0.050 1 407 84 84 ILE H H 7.074 0.005 1 408 84 84 ILE C C 176.663 0.050 1 409 84 84 ILE CA C 61.930 0.050 1 410 84 84 ILE CB C 36.601 0.050 1 411 84 84 ILE N N 108.940 0.050 1 412 85 85 GLN H H 6.938 0.005 1 413 85 85 GLN C C 176.350 0.050 1 414 85 85 GLN CA C 57.618 0.050 1 415 85 85 GLN CB C 28.105 0.050 1 416 85 85 GLN N N 117.961 0.050 1 417 86 86 ASP H H 7.725 0.005 1 418 86 86 ASP C C 176.559 0.050 1 419 86 86 ASP CA C 53.338 0.050 1 420 86 86 ASP CB C 40.733 0.050 1 421 86 86 ASP N N 115.267 0.050 1 422 87 87 VAL H H 7.086 0.005 1 423 87 87 VAL C C 174.525 0.050 1 424 87 87 VAL CA C 63.711 0.050 1 425 87 87 VAL CB C 30.683 0.050 1 426 87 87 VAL N N 124.044 0.050 1 427 88 88 SER H H 9.420 0.005 1 428 88 88 SER C C 173.845 0.050 1 429 88 88 SER CA C 56.958 0.050 1 430 88 88 SER CB C 65.466 0.050 1 431 88 88 SER N N 126.779 0.050 1 432 89 89 PRO C C 177.815 0.050 1 433 89 89 PRO CA C 65.075 0.050 1 434 89 89 PRO CB C 30.828 0.050 1 435 90 90 ALA H H 7.684 0.005 1 436 90 90 ALA C C 178.029 0.050 1 437 90 90 ALA CA C 53.179 0.050 1 438 90 90 ALA CB C 17.673 0.050 1 439 90 90 ALA N N 119.253 0.050 1 440 91 91 ASP H H 8.011 0.005 1 441 91 91 ASP C C 177.532 0.050 1 442 91 91 ASP CA C 54.889 0.050 1 443 91 91 ASP CB C 41.319 0.050 1 444 91 91 ASP N N 114.988 0.050 1 445 92 92 VAL H H 7.186 0.005 1 446 92 92 VAL C C 176.667 0.050 1 447 92 92 VAL CA C 63.839 0.050 1 448 92 92 VAL CB C 31.123 0.050 1 449 92 92 VAL N N 125.634 0.050 1 450 93 93 TYR H H 8.917 0.005 1 451 93 93 TYR C C 175.614 0.050 1 452 93 93 TYR CA C 54.010 0.050 1 453 93 93 TYR CB C 35.811 0.050 1 454 93 93 TYR N N 130.906 0.050 1 455 94 94 PRO C C 177.245 0.050 1 456 94 94 PRO CA C 63.392 0.050 1 457 94 94 PRO CB C 31.358 0.050 1 458 95 95 GLY H H 8.369 0.005 1 459 95 95 GLY C C 176.246 0.050 1 460 95 95 GLY CA C 45.793 0.050 1 461 95 95 GLY N N 111.518 0.050 1 462 96 96 ILE H H 7.150 0.005 1 463 96 96 ILE C C 176.955 0.050 1 464 96 96 ILE CA C 61.103 0.050 1 465 96 96 ILE CB C 33.848 0.050 1 466 96 96 ILE N N 121.607 0.050 1 467 97 97 LEU H H 8.736 0.005 1 468 97 97 LEU C C 178.063 0.050 1 469 97 97 LEU CA C 58.133 0.050 1 470 97 97 LEU CB C 40.382 0.050 1 471 97 97 LEU N N 121.292 0.050 1 472 98 98 GLN H H 8.650 0.005 1 473 98 98 GLN C C 177.395 0.050 1 474 98 98 GLN CA C 57.522 0.050 1 475 98 98 GLN CB C 27.696 0.050 1 476 98 98 GLN N N 117.802 0.050 1 477 99 99 LEU H H 7.856 0.005 1 478 99 99 LEU C C 178.497 0.050 1 479 99 99 LEU CA C 57.837 0.050 1 480 99 99 LEU CB C 39.885 0.050 1 481 99 99 LEU N N 119.939 0.050 1 482 100 100 LEU H H 8.265 0.005 1 483 100 100 LEU C C 179.077 0.050 1 484 100 100 LEU CA C 58.026 0.050 1 485 100 100 LEU CB C 39.639 0.050 1 486 100 100 LEU N N 119.339 0.050 1 487 101 101 LYS H H 7.929 0.005 1 488 101 101 LYS C C 180.252 0.050 1 489 101 101 LYS CA C 60.024 0.050 1 490 101 101 LYS CB C 32.002 0.050 1 491 101 101 LYS N N 117.860 0.050 1 492 102 102 ASP H H 8.877 0.005 1 493 102 102 ASP C C 179.833 0.050 1 494 102 102 ASP CA C 57.085 0.050 1 495 102 102 ASP CB C 39.561 0.050 1 496 102 102 ASP N N 122.943 0.050 1 497 103 103 LEU H H 9.338 0.005 1 498 103 103 LEU C C 179.070 0.050 1 499 103 103 LEU CA C 58.262 0.050 1 500 103 103 LEU CB C 39.808 0.050 1 501 103 103 LEU N N 123.869 0.050 1 502 104 104 ARG H H 8.215 0.005 1 503 104 104 ARG C C 181.926 0.050 1 504 104 104 ARG CA C 59.349 0.050 1 505 104 104 ARG CB C 28.752 0.050 1 506 104 104 ARG N N 119.986 0.050 1 507 105 105 SER H H 8.741 0.005 1 508 105 105 SER C C 175.203 0.050 1 509 105 105 SER CA C 61.181 0.050 1 510 105 105 SER CB C 62.294 0.050 1 511 105 105 SER N N 117.430 0.050 1 512 106 106 ASN H H 7.432 0.005 1 513 106 106 ASN C C 172.378 0.050 1 514 106 106 ASN CA C 53.691 0.050 1 515 106 106 ASN CB C 39.480 0.050 1 516 106 106 ASN N N 118.334 0.050 1 517 107 107 LYS H H 7.893 0.005 1 518 107 107 LYS C C 175.097 0.050 1 519 107 107 LYS CA C 56.875 0.050 1 520 107 107 LYS CB C 27.433 0.050 1 521 107 107 LYS N N 115.016 0.050 1 522 108 108 ILE H H 8.008 0.005 1 523 108 108 ILE C C 175.776 0.050 1 524 108 108 ILE CA C 59.939 0.050 1 525 108 108 ILE CB C 37.041 0.050 1 526 108 108 ILE N N 122.575 0.050 1 527 109 109 LYS H H 7.636 0.005 1 528 109 109 LYS C C 175.729 0.050 1 529 109 109 LYS CA C 54.854 0.050 1 530 109 109 LYS CB C 32.675 0.050 1 531 109 109 LYS N N 125.113 0.050 1 532 110 110 ILE H H 9.293 0.005 1 533 110 110 ILE C C 175.805 0.050 1 534 110 110 ILE CA C 60.902 0.050 1 535 110 110 ILE CB C 40.032 0.050 1 536 110 110 ILE N N 122.023 0.050 1 537 111 111 ALA H H 8.856 0.005 1 538 111 111 ALA C C 175.906 0.050 1 539 111 111 ALA CA C 48.977 0.050 1 540 111 111 ALA CB C 23.712 0.050 1 541 111 111 ALA N N 128.318 0.050 1 542 112 112 LEU H H 8.598 0.005 1 543 112 112 LEU C C 173.970 0.050 1 544 112 112 LEU CA C 53.927 0.050 1 545 112 112 LEU CB C 43.396 0.050 1 546 112 112 LEU N N 124.187 0.050 1 547 113 113 ALA H H 9.176 0.005 1 548 113 113 ALA C C 174.524 0.050 1 549 113 113 ALA CA C 49.088 0.050 1 550 113 113 ALA CB C 19.110 0.050 1 551 113 113 ALA N N 133.864 0.050 1 552 114 114 SER H H 7.564 0.005 1 553 114 114 SER C C 175.438 0.050 1 554 114 114 SER CA C 56.335 0.050 1 555 114 114 SER CB C 64.438 0.050 1 556 114 114 SER N N 114.479 0.050 1 557 115 115 ALA H H 9.672 0.005 1 558 115 115 ALA C C 176.141 0.050 1 559 115 115 ALA CA C 52.176 0.050 1 560 115 115 ALA CB C 18.381 0.050 1 561 115 115 ALA N N 129.419 0.050 1 562 116 116 SER H H 8.558 0.005 1 563 116 116 SER C C 179.939 0.050 1 564 116 116 SER CA C 56.345 0.050 1 565 116 116 SER CB C 63.383 0.050 1 566 116 116 SER N N 113.243 0.050 1 567 117 117 LYS H H 11.197 0.005 1 568 117 117 LYS C C 178.187 0.050 1 569 117 117 LYS CA C 58.037 0.050 1 570 117 117 LYS CB C 31.274 0.050 1 571 117 117 LYS N N 136.759 0.050 1 572 118 118 ASN H H 8.462 0.005 1 573 118 118 ASN C C 174.308 0.050 1 574 118 118 ASN CA C 54.566 0.050 1 575 118 118 ASN CB C 39.938 0.050 1 576 118 118 ASN N N 118.442 0.050 1 577 119 119 GLY H H 7.540 0.005 1 578 119 119 GLY C C 172.835 0.050 1 579 119 119 GLY CA C 47.886 0.050 1 580 119 119 GLY N N 106.824 0.050 1 581 120 120 PRO C C 179.179 0.050 1 582 120 120 PRO CA C 65.838 0.050 1 583 120 120 PRO CB C 30.655 0.050 1 584 121 121 PHE H H 7.639 0.005 1 585 121 121 PHE C C 177.267 0.050 1 586 121 121 PHE CA C 60.352 0.050 1 587 121 121 PHE CB C 38.505 0.050 1 588 121 121 PHE N N 119.543 0.050 1 589 122 122 LEU H H 7.637 0.005 1 590 122 122 LEU C C 178.964 0.050 1 591 122 122 LEU CA C 57.510 0.050 1 592 122 122 LEU CB C 41.582 0.050 1 593 122 122 LEU N N 121.154 0.050 1 594 123 123 LEU H H 8.320 0.005 1 595 123 123 LEU C C 179.182 0.050 1 596 123 123 LEU CA C 58.042 0.050 1 597 123 123 LEU CB C 40.645 0.050 1 598 123 123 LEU N N 117.487 0.050 1 599 124 124 GLU H H 7.564 0.005 1 600 124 124 GLU C C 180.750 0.050 1 601 124 124 GLU CA C 58.560 0.050 1 602 124 124 GLU CB C 28.340 0.050 1 603 124 124 GLU N N 119.934 0.050 1 604 125 125 ARG H H 8.048 0.005 1 605 125 125 ARG C C 178.552 0.050 1 606 125 125 ARG CA C 56.750 0.050 1 607 125 125 ARG CB C 28.497 0.050 1 608 125 125 ARG N N 121.203 0.050 1 609 126 126 MET H H 7.440 0.005 1 610 126 126 MET C C 173.632 0.050 1 611 126 126 MET CA C 55.937 0.050 1 612 126 126 MET CB C 32.418 0.050 1 613 126 126 MET N N 113.339 0.050 1 614 127 127 ASN H H 7.978 0.005 1 615 127 127 ASN C C 175.858 0.050 1 616 127 127 ASN CA C 53.486 0.050 1 617 127 127 ASN CB C 36.397 0.050 1 618 127 127 ASN N N 117.299 0.050 1 619 128 128 LEU H H 8.709 0.005 1 620 128 128 LEU C C 177.999 0.050 1 621 128 128 LEU CA C 53.726 0.050 1 622 128 128 LEU CB C 44.807 0.050 1 623 128 128 LEU N N 114.414 0.050 1 624 129 129 THR H H 7.441 0.005 1 625 129 129 THR C C 176.407 0.050 1 626 129 129 THR CA C 67.108 0.050 1 627 129 129 THR CB C 68.391 0.050 1 628 129 129 THR N N 115.792 0.050 1 629 130 130 GLY H H 8.584 0.005 1 630 130 130 GLY C C 175.041 0.050 1 631 130 130 GLY CA C 45.607 0.050 1 632 130 130 GLY N N 106.296 0.050 1 633 131 131 TYR H H 7.757 0.005 1 634 131 131 TYR C C 174.497 0.050 1 635 131 131 TYR CA C 59.916 0.050 1 636 131 131 TYR CB C 38.566 0.050 1 637 131 131 TYR N N 116.592 0.050 1 638 132 132 PHE H H 7.362 0.005 1 639 132 132 PHE C C 175.884 0.050 1 640 132 132 PHE CA C 58.365 0.050 1 641 132 132 PHE CB C 38.829 0.050 1 642 132 132 PHE N N 115.339 0.050 1 643 133 133 ASP H H 9.226 0.005 1 644 133 133 ASP C C 176.404 0.050 1 645 133 133 ASP CA C 56.678 0.050 1 646 133 133 ASP CB C 42.170 0.050 1 647 133 133 ASP N N 125.161 0.050 1 648 134 134 ALA H H 7.627 0.005 1 649 134 134 ALA C C 175.466 0.050 1 650 134 134 ALA CA C 51.721 0.050 1 651 134 134 ALA CB C 23.505 0.050 1 652 134 134 ALA N N 115.632 0.050 1 653 135 135 ILE H H 8.642 0.005 1 654 135 135 ILE C C 175.723 0.050 1 655 135 135 ILE CA C 60.361 0.050 1 656 135 135 ILE CB C 40.148 0.050 1 657 135 135 ILE N N 122.148 0.050 1 658 136 136 ALA H H 8.482 0.005 1 659 136 136 ALA C C 175.563 0.050 1 660 136 136 ALA CA C 51.577 0.050 1 661 136 136 ALA CB C 17.701 0.050 1 662 136 136 ALA N N 131.055 0.050 1 663 137 137 ASP H H 8.449 0.005 1 664 137 137 ASP C C 176.670 0.050 1 665 137 137 ASP CA C 50.567 0.050 1 666 137 137 ASP CB C 41.259 0.050 1 667 137 137 ASP N N 124.893 0.050 1 668 138 138 PRO C C 178.185 0.050 1 669 138 138 PRO CA C 63.723 0.050 1 670 138 138 PRO CB C 31.710 0.050 1 671 139 139 ALA H H 8.640 0.005 1 672 139 139 ALA C C 178.854 0.050 1 673 139 139 ALA CA C 52.970 0.050 1 674 139 139 ALA CB C 18.114 0.050 1 675 139 139 ALA N N 120.876 0.050 1 676 140 140 GLU H H 7.482 0.005 1 677 140 140 GLU C C 176.719 0.050 1 678 140 140 GLU CA C 55.602 0.050 1 679 140 140 GLU CB C 29.835 0.050 1 680 140 140 GLU N N 116.423 0.050 1 681 141 141 VAL H H 6.996 0.005 1 682 141 141 VAL C C 175.778 0.050 1 683 141 141 VAL CA C 60.343 0.050 1 684 141 141 VAL CB C 31.914 0.050 1 685 141 141 VAL N N 115.489 0.050 1 686 142 142 ALA H H 8.514 0.005 1 687 142 142 ALA C C 177.688 0.050 1 688 142 142 ALA CA C 53.505 0.050 1 689 142 142 ALA CB C 18.085 0.050 1 690 142 142 ALA N N 125.298 0.050 1 691 143 143 ALA H H 7.314 0.005 1 692 143 143 ALA C C 176.145 0.050 1 693 143 143 ALA CA C 51.069 0.050 1 694 143 143 ALA CB C 20.547 0.050 1 695 143 143 ALA N N 119.745 0.050 1 696 144 144 SER H H 8.528 0.005 1 697 144 144 SER C C 176.452 0.050 1 698 144 144 SER CA C 56.883 0.050 1 699 144 144 SER CB C 63.468 0.050 1 700 144 144 SER N N 118.012 0.050 1 701 145 145 LYS H H 8.994 0.005 1 702 145 145 LYS C C 175.205 0.050 1 703 145 145 LYS CA C 57.596 0.050 1 704 145 145 LYS CB C 29.776 0.050 1 705 145 145 LYS N N 128.026 0.050 1 706 146 146 PRO C C 176.251 0.050 1 707 146 146 PRO CA C 62.899 0.050 1 708 146 146 PRO CB C 35.343 0.050 1 709 147 147 ALA H H 9.185 0.005 1 710 147 147 ALA C C 178.238 0.050 1 711 147 147 ALA CA C 51.612 0.050 1 712 147 147 ALA CB C 16.709 0.050 1 713 147 147 ALA N N 132.018 0.050 1 714 148 148 PRO C C 177.193 0.050 1 715 148 148 PRO CA C 63.505 0.050 1 716 148 148 PRO CB C 32.060 0.050 1 717 149 149 ASP H H 9.342 0.005 1 718 149 149 ASP C C 178.024 0.050 1 719 149 149 ASP CA C 58.020 0.050 1 720 149 149 ASP CB C 38.976 0.050 1 721 149 149 ASP N N 120.841 0.050 1 722 150 150 ILE H H 9.723 0.005 1 723 150 150 ILE C C 175.724 0.050 1 724 150 150 ILE CA C 63.415 0.050 1 725 150 150 ILE CB C 37.218 0.050 1 726 150 150 ILE N N 120.358 0.050 1 727 151 151 PHE H H 7.242 0.005 1 728 151 151 PHE C C 177.612 0.050 1 729 151 151 PHE CA C 63.188 0.050 1 730 151 151 PHE CB C 38.272 0.050 1 731 151 151 PHE N N 120.897 0.050 1 732 152 152 ILE H H 7.717 0.005 1 733 152 152 ILE C C 177.658 0.050 1 734 152 152 ILE CA C 65.641 0.050 1 735 152 152 ILE CB C 37.452 0.050 1 736 152 152 ILE N N 120.329 0.050 1 737 153 153 ALA H H 8.412 0.005 1 738 153 153 ALA C C 180.934 0.050 1 739 153 153 ALA CA C 54.260 0.050 1 740 153 153 ALA CB C 17.443 0.050 1 741 153 153 ALA N N 120.448 0.050 1 742 154 154 ALA H H 7.841 0.005 1 743 154 154 ALA C C 176.692 0.050 1 744 154 154 ALA CA C 54.994 0.050 1 745 154 154 ALA CB C 17.854 0.050 1 746 154 154 ALA N N 122.286 0.050 1 747 155 155 ALA H H 7.578 0.005 1 748 155 155 ALA C C 179.753 0.050 1 749 155 155 ALA CA C 54.234 0.050 1 750 155 155 ALA CB C 16.181 0.050 1 751 155 155 ALA N N 118.492 0.050 1 752 156 156 HIS H H 8.469 0.005 1 753 156 156 HIS C C 179.749 0.050 1 754 156 156 HIS CA C 58.236 0.050 1 755 156 156 HIS CB C 28.956 0.050 1 756 156 156 HIS N N 117.038 0.050 1 757 157 157 ALA H H 8.244 0.005 1 758 157 157 ALA C C 179.327 0.050 1 759 157 157 ALA CA C 54.080 0.050 1 760 157 157 ALA CB C 17.704 0.050 1 761 157 157 ALA N N 122.087 0.050 1 762 158 158 VAL H H 7.223 0.005 1 763 158 158 VAL C C 175.541 0.050 1 764 158 158 VAL CA C 59.399 0.050 1 765 158 158 VAL CB C 30.450 0.050 1 766 158 158 VAL N N 107.560 0.050 1 767 159 159 GLY H H 7.783 0.005 1 768 159 159 GLY C C 174.625 0.050 1 769 159 159 GLY CA C 46.025 0.050 1 770 159 159 GLY N N 110.264 0.050 1 771 160 160 VAL H H 7.674 0.005 1 772 160 160 VAL C C 174.205 0.050 1 773 160 160 VAL CA C 58.889 0.050 1 774 160 160 VAL CB C 34.053 0.050 1 775 160 160 VAL N N 117.103 0.050 1 776 161 161 ALA H H 8.656 0.005 1 777 161 161 ALA C C 178.764 0.050 1 778 161 161 ALA CA C 49.514 0.050 1 779 161 161 ALA CB C 17.294 0.050 1 780 161 161 ALA N N 125.852 0.050 1 781 162 162 PRO C C 177.451 0.050 1 782 162 162 PRO CA C 65.627 0.050 1 783 162 162 PRO CB C 30.772 0.050 1 784 163 163 SER H H 7.735 0.005 1 785 163 163 SER C C 175.907 0.050 1 786 163 163 SER CA C 59.821 0.050 1 787 163 163 SER CB C 61.858 0.050 1 788 163 163 SER N N 107.000 0.050 1 789 164 164 GLU H H 7.810 0.005 1 790 164 164 GLU C C 174.730 0.050 1 791 164 164 GLU CA C 55.593 0.050 1 792 164 164 GLU CB C 29.334 0.050 1 793 164 164 GLU N N 121.902 0.050 1 794 165 165 SER H H 7.981 0.005 1 795 165 165 SER C C 172.113 0.050 1 796 165 165 SER CA C 57.495 0.050 1 797 165 165 SER CB C 65.284 0.050 1 798 165 165 SER N N 114.777 0.050 1 799 166 166 ILE H H 7.611 0.005 1 800 166 166 ILE C C 175.203 0.050 1 801 166 166 ILE CA C 58.962 0.050 1 802 166 166 ILE CB C 40.761 0.050 1 803 166 166 ILE N N 121.800 0.050 1 804 167 167 GLY H H 8.789 0.005 1 805 167 167 GLY C C 170.411 0.050 1 806 167 167 GLY CA C 43.369 0.050 1 807 167 167 GLY N N 112.916 0.050 1 808 168 168 LEU H H 7.828 0.005 1 809 168 168 LEU C C 175.617 0.050 1 810 168 168 LEU CA C 53.380 0.050 1 811 168 168 LEU CB C 40.820 0.050 1 812 168 168 LEU N N 123.779 0.050 1 813 169 169 GLU H H 6.987 0.005 1 814 169 169 GLU C C 173.577 0.050 1 815 169 169 GLU CA C 56.568 0.050 1 816 169 169 GLU CB C 39.617 0.050 1 817 169 169 GLU N N 124.536 0.050 1 818 170 170 ASP H H 8.372 0.005 1 819 170 170 ASP C C 173.865 0.050 1 820 170 170 ASP CA C 52.134 0.050 1 821 170 170 ASP CB C 41.405 0.050 1 822 170 170 ASP N N 116.574 0.050 1 823 171 171 SER H H 8.305 0.005 1 824 171 171 SER C C 173.628 0.050 1 825 171 171 SER CA C 55.306 0.050 1 826 171 171 SER CB C 70.352 0.050 1 827 171 171 SER N N 114.530 0.050 1 828 172 172 GLN H H 9.773 0.005 1 829 172 172 GLN C C 179.592 0.050 1 830 172 172 GLN CA C 58.993 0.050 1 831 172 172 GLN CB C 27.515 0.050 1 832 172 172 GLN N N 125.007 0.050 1 833 173 173 ALA H H 8.686 0.005 1 834 173 173 ALA C C 180.173 0.050 1 835 173 173 ALA CA C 54.129 0.050 1 836 173 173 ALA CB C 17.091 0.050 1 837 173 173 ALA N N 120.976 0.050 1 838 174 174 GLY H H 8.406 0.005 1 839 174 174 GLY C C 175.670 0.050 1 840 174 174 GLY CA C 45.922 0.050 1 841 174 174 GLY N N 106.274 0.050 1 842 175 175 ILE H H 8.475 0.005 1 843 175 175 ILE C C 177.770 0.050 1 844 175 175 ILE CA C 62.682 0.050 1 845 175 175 ILE CB C 34.727 0.050 1 846 175 175 ILE N N 123.725 0.050 1 847 176 176 GLN H H 7.693 0.005 1 848 176 176 GLN C C 177.035 0.050 1 849 176 176 GLN CA C 58.249 0.050 1 850 176 176 GLN CB C 27.195 0.050 1 851 176 176 GLN N N 120.480 0.050 1 852 177 177 ALA H H 7.712 0.005 1 853 177 177 ALA C C 179.755 0.050 1 854 177 177 ALA CA C 54.784 0.050 1 855 177 177 ALA CB C 19.198 0.050 1 856 177 177 ALA N N 122.454 0.050 1 857 178 178 ILE H H 8.069 0.005 1 858 178 178 ILE C C 180.642 0.050 1 859 178 178 ILE CA C 64.802 0.050 1 860 178 178 ILE CB C 36.339 0.050 1 861 178 178 ILE N N 117.948 0.050 1 862 179 179 LYS H H 8.503 0.005 1 863 179 179 LYS C C 180.962 0.050 1 864 179 179 LYS CA C 59.832 0.050 1 865 179 179 LYS CB C 31.886 0.050 1 866 179 179 LYS N N 120.875 0.050 1 867 180 180 ASP H H 8.458 0.005 1 868 180 180 ASP C C 177.346 0.050 1 869 180 180 ASP CA C 56.252 0.050 1 870 180 180 ASP CB C 38.771 0.050 1 871 180 180 ASP N N 118.818 0.050 1 872 181 181 SER H H 8.112 0.005 1 873 181 181 SER C C 173.885 0.050 1 874 181 181 SER CA C 60.406 0.050 1 875 181 181 SER CB C 64.260 0.050 1 876 181 181 SER N N 117.343 0.050 1 877 182 182 GLY H H 7.217 0.005 1 878 182 182 GLY C C 173.476 0.050 1 879 182 182 GLY CA C 44.231 0.050 1 880 182 182 GLY N N 109.111 0.050 1 881 183 183 ALA H H 7.193 0.005 1 882 183 183 ALA C C 174.703 0.050 1 883 183 183 ALA CA C 50.876 0.050 1 884 183 183 ALA CB C 19.521 0.050 1 885 183 183 ALA N N 124.317 0.050 1 886 184 184 LEU H H 8.069 0.005 1 887 184 184 LEU C C 174.881 0.050 1 888 184 184 LEU CA C 51.816 0.050 1 889 184 184 LEU CB C 43.374 0.050 1 890 184 184 LEU N N 122.728 0.050 1 891 185 185 PRO C C 176.357 0.050 1 892 185 185 PRO CA C 61.420 0.050 1 893 185 185 PRO CB C 31.650 0.050 1 894 186 186 ILE H H 8.273 0.005 1 895 186 186 ILE C C 178.485 0.050 1 896 186 186 ILE CA C 61.522 0.050 1 897 186 186 ILE CB C 38.184 0.050 1 898 186 186 ILE N N 119.421 0.050 1 899 187 187 GLY H H 8.927 0.005 1 900 187 187 GLY C C 171.352 0.050 1 901 187 187 GLY CA C 44.740 0.050 1 902 187 187 GLY N N 116.303 0.050 1 903 188 188 VAL H H 8.111 0.005 1 904 188 188 VAL C C 173.894 0.050 1 905 188 188 VAL CA C 57.312 0.050 1 906 188 188 VAL CB C 32.011 0.050 1 907 188 188 VAL N N 119.170 0.050 1 908 189 189 GLY H H 8.113 0.005 1 909 189 189 GLY C C 171.167 0.050 1 910 189 189 GLY CA C 44.111 0.050 1 911 189 189 GLY N N 113.258 0.050 1 912 190 190 ARG H H 8.743 0.005 1 913 190 190 ARG C C 176.192 0.050 1 914 190 190 ARG CA C 52.570 0.050 1 915 190 190 ARG CB C 30.127 0.050 1 916 190 190 ARG N N 120.924 0.050 1 917 191 191 PRO C C 178.809 0.050 1 918 191 191 PRO CA C 64.261 0.050 1 919 191 191 PRO CB C 30.948 0.050 1 920 192 192 GLU H H 9.634 0.005 1 921 192 192 GLU C C 176.824 0.050 1 922 192 192 GLU CA C 59.597 0.050 1 923 192 192 GLU CB C 27.902 0.050 1 924 192 192 GLU N N 118.922 0.050 1 925 193 193 ASP H H 7.052 0.005 1 926 193 193 ASP C C 177.002 0.050 1 927 193 193 ASP CA C 55.165 0.050 1 928 193 193 ASP CB C 41.611 0.050 1 929 193 193 ASP N N 115.022 0.050 1 930 194 194 LEU H H 7.692 0.005 1 931 194 194 LEU C C 176.562 0.050 1 932 194 194 LEU CA C 55.448 0.050 1 933 194 194 LEU CB C 42.431 0.050 1 934 194 194 LEU N N 116.782 0.050 1 935 195 195 GLY H H 8.036 0.005 1 936 195 195 GLY C C 172.576 0.050 1 937 195 195 GLY CA C 43.670 0.050 1 938 195 195 GLY N N 108.217 0.050 1 939 196 196 ASP H H 7.919 0.005 1 940 196 196 ASP C C 176.976 0.050 1 941 196 196 ASP CA C 53.606 0.050 1 942 196 196 ASP CB C 41.085 0.050 1 943 196 196 ASP N N 116.721 0.050 1 944 197 197 ASP H H 8.930 0.005 1 945 197 197 ASP C C 175.383 0.050 1 946 197 197 ASP CA C 53.590 0.050 1 947 197 197 ASP CB C 39.650 0.050 1 948 197 197 ASP N N 117.361 0.050 1 949 198 198 ILE H H 6.794 0.005 1 950 198 198 ILE C C 175.362 0.050 1 951 198 198 ILE CA C 58.245 0.050 1 952 198 198 ILE CB C 40.559 0.050 1 953 198 198 ILE N N 113.476 0.050 1 954 199 199 VAL H H 8.940 0.005 1 955 199 199 VAL C C 174.207 0.050 1 956 199 199 VAL CA C 63.809 0.050 1 957 199 199 VAL CB C 30.304 0.050 1 958 199 199 VAL N N 125.441 0.050 1 959 200 200 ILE H H 7.951 0.005 1 960 200 200 ILE C C 176.034 0.050 1 961 200 200 ILE CA C 57.833 0.050 1 962 200 200 ILE CB C 40.879 0.050 1 963 200 200 ILE N N 126.805 0.050 1 964 201 201 VAL H H 8.790 0.005 1 965 201 201 VAL C C 174.211 0.050 1 966 201 201 VAL CA C 56.130 0.050 1 967 201 201 VAL CB C 31.591 0.050 1 968 201 201 VAL N N 120.891 0.050 1 969 202 202 PRO C C 177.192 0.050 1 970 202 202 PRO CA C 63.704 0.050 1 971 202 202 PRO CB C 31.122 0.050 1 972 203 203 ASP H H 6.826 0.005 1 973 203 203 ASP C C 175.409 0.050 1 974 203 203 ASP CA C 53.056 0.050 1 975 203 203 ASP CB C 41.376 0.050 1 976 203 203 ASP N N 110.462 0.050 1 977 204 204 THR H H 8.125 0.005 1 978 204 204 THR C C 176.616 0.050 1 979 204 204 THR CA C 64.979 0.050 1 980 204 204 THR CB C 68.743 0.050 1 981 204 204 THR N N 108.991 0.050 1 982 205 205 SER H H 8.904 0.005 1 983 205 205 SER C C 175.762 0.050 1 984 205 205 SER CA C 61.206 0.050 1 985 205 205 SER CB C 61.829 0.050 1 986 205 205 SER N N 120.287 0.050 1 987 206 206 HIS H H 7.023 0.005 1 988 206 206 HIS C C 176.821 0.050 1 989 206 206 HIS CA C 56.750 0.050 1 990 206 206 HIS CB C 30.482 0.050 1 991 206 206 HIS N N 118.384 0.050 1 992 207 207 TYR H H 7.740 0.005 1 993 207 207 TYR C C 173.631 0.050 1 994 207 207 TYR CA C 53.920 0.050 1 995 207 207 TYR CB C 35.254 0.050 1 996 207 207 TYR N N 119.746 0.050 1 997 208 208 THR H H 7.407 0.005 1 998 208 208 THR C C 174.788 0.050 1 999 208 208 THR CA C 58.014 0.050 1 1000 208 208 THR CB C 71.174 0.050 1 1001 208 208 THR N N 114.610 0.050 1 1002 209 209 LEU H H 9.466 0.005 1 1003 209 209 LEU C C 177.870 0.050 1 1004 209 209 LEU CA C 58.334 0.050 1 1005 209 209 LEU CB C 39.825 0.050 1 1006 209 209 LEU N N 125.197 0.050 1 1007 210 210 GLU H H 8.543 0.005 1 1008 210 210 GLU C C 178.816 0.050 1 1009 210 210 GLU CA C 59.520 0.050 1 1010 210 210 GLU CB C 28.602 0.050 1 1011 210 210 GLU N N 116.710 0.050 1 1012 211 211 PHE H H 8.195 0.005 1 1013 211 211 PHE C C 176.823 0.050 1 1014 211 211 PHE CA C 60.778 0.050 1 1015 211 211 PHE CB C 39.471 0.050 1 1016 211 211 PHE N N 122.575 0.050 1 1017 212 212 LEU H H 8.370 0.005 1 1018 212 212 LEU C C 179.075 0.050 1 1019 212 212 LEU CA C 58.898 0.050 1 1020 212 212 LEU CB C 39.910 0.050 1 1021 212 212 LEU N N 119.723 0.050 1 1022 213 213 LYS H H 8.356 0.005 1 1023 213 213 LYS C C 178.130 0.050 1 1024 213 213 LYS CA C 60.550 0.050 1 1025 213 213 LYS CB C 32.003 0.050 1 1026 213 213 LYS N N 116.363 0.050 1 1027 214 214 GLU H H 7.798 0.005 1 1028 214 214 GLU C C 179.596 0.050 1 1029 214 214 GLU CA C 59.101 0.050 1 1030 214 214 GLU CB C 28.779 0.050 1 1031 214 214 GLU N N 120.645 0.050 1 1032 215 215 VAL H H 8.251 0.005 1 1033 215 215 VAL C C 178.445 0.050 1 1034 215 215 VAL CA C 65.743 0.050 1 1035 215 215 VAL CB C 30.742 0.050 1 1036 215 215 VAL N N 120.559 0.050 1 1037 216 216 TRP H H 8.437 0.005 1 1038 216 216 TRP C C 178.679 0.050 1 1039 216 216 TRP CA C 60.569 0.050 1 1040 216 216 TRP CB C 28.986 0.050 1 1041 216 216 TRP N N 120.720 0.050 1 1042 217 217 LEU H H 8.189 0.005 1 1043 217 217 LEU C C 179.909 0.050 1 1044 217 217 LEU CA C 57.071 0.050 1 1045 217 217 LEU CB C 40.966 0.050 1 1046 217 217 LEU N N 117.207 0.050 1 1047 218 218 GLN H H 7.835 0.005 1 1048 218 218 GLN C C 177.714 0.050 1 1049 218 218 GLN CA C 57.171 0.050 1 1050 218 218 GLN CB C 27.989 0.050 1 1051 218 218 GLN N N 118.304 0.050 1 1052 219 219 LYS H H 7.522 0.005 1 1053 219 219 LYS C C 176.614 0.050 1 1054 219 219 LYS CA C 55.410 0.050 1 1055 219 219 LYS CB C 31.358 0.050 1 1056 219 219 LYS N N 118.013 0.050 1 1057 220 220 GLN H H 7.623 0.005 1 1058 220 220 GLN C C 175.098 0.050 1 1059 220 220 GLN CA C 55.178 0.050 1 1060 220 220 GLN CB C 27.842 0.050 1 1061 220 220 GLN N N 119.971 0.050 1 1062 221 221 LYS H H 7.550 0.005 1 1063 221 221 LYS C C 181.486 0.050 1 1064 221 221 LYS CA C 57.271 0.050 1 1065 221 221 LYS CB C 32.412 0.050 1 1066 221 221 LYS N N 127.553 0.050 1 stop_ save_