data_28095 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C backbone resonance assignments of wild-type substrate-free beta-phosphoglucomutase from Lactococcus lactis with a cis K145-P146 peptide bond (conformer A) ; _BMRB_accession_number 28095 _BMRB_flat_file_name bmr28095.str _Entry_type original _Submission_date 2020-03-10 _Accession_date 2020-03-10 _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 Trevitt Clare R. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 193 "13C chemical shifts" 606 "15N chemical shifts" 193 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-12-04 update BMRB 'update entry citation' 2020-11-02 update BMRB 'update entry citation' 2020-09-03 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 28096 'binary complex; bPGM-Mg; with trans K145-P146 peptide bond' 28097 'transition state analogue complex; bPGM-P146A-Mg-MgF3-G6P TSA' 7235 'Backbone NMR assignments of wild-type substrate-free beta-phosphoglucomutase with a cis K145-P146 peptide bond' stop_ _Original_release_date 2020-03-10 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Allomorphy as a mechanism of post-translational control of enzyme activity ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 33139716 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wood Henry P. . 2 Cruz-Navarrete F Aaron . 3 Baxter Nicola J. . 4 Trevitt Clare R. . 5 Robertson Angus J. . 6 Dix Samuel R. . 7 Hounslow Andrea M. . 8 Cliff Matthew J. . 9 Waltho Jonathan P. . stop_ _Journal_abbreviation 'Nat. Commun.' _Journal_volume 11 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5538 _Page_last 5538 _Year 2020 _Details . loop_ _Keyword 'NMR spectroscopy' 'X-ray crystallography' allomorphy 'cis-trans proline isomerisation' 'enzyme regulation' 'phosphoryl transfer enzyme' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'bPGM-Mg complex' _Enzyme_commission_number 'EC 5.4.2.6' loop_ _Mol_system_component_name _Mol_label bPGM $beta-phosphoglucomutase Mg $entity_MG stop_ _System_molecular_weight 24233.95 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'The wild-type enzyme catalyses the reversible interconversion of beta-glucose 1-phosphate and beta-glucose 6-phosphate' stop_ _Database_query_date . _Details ; This is a binary complex involving wild-type substrate-free beta-phosphoglucomutase and a catalytic Mg ion with a cis K145-P146 peptide bond. ; save_ ######################## # Monomeric polymers # ######################## save_beta-phosphoglucomutase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common beta-phosphoglucomutase _Molecular_mass 24209.65 _Mol_thiol_state 'all free' loop_ _Biological_function 'The wild-type enzyme catalyses the reversible interconversion of beta-glucose 1-phosphate and beta-glucose 6-phosphate' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 221 _Mol_residue_sequence ; MFKAVLFDLNGVITDTAEYH 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 ASN 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 . save_ ############# # Ligands # ############# save_MG _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'MAGNESIUM ION' _BMRB_code MG _PDB_code MG _Molecular_mass 24.305 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons MG MG MG . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $beta-phosphoglucomutase 'Lactococcus lactis' 1358 Bacteria . Lactococcus lactis pgmB 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 . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $beta-phosphoglucomutase 1.0 mM '[U-100% 13C; U-100% 15N; U-80% 2H]' 'potassium HEPES buffer' 50 mM 'natural abundance' 'magnesium chloride' 5 mM 'natural abundance' 'sodium azide' 2 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % '[U-99% 2H]' TSP 2 mM [U-2H] TRIS 5 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.2 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing 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 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $sample_1 save_ save_3D_TROSY-HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCO' _Sample_label $sample_1 save_ save_3D_TROSY_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(CA)CO' _Sample_label $sample_1 save_ save_3D_TROSY_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCA' _Sample_label $sample_1 save_ save_3D_TROSY_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(CO)CA' _Sample_label $sample_1 save_ save_3D_TROSY_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCACB' _Sample_label $sample_1 save_ save_3D_TROSY_HN(CO)CACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_TROSY_(H)N(COCA)NNH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY (H)N(COCA)NNH' _Sample_label $sample_1 save_ save_3D_TROSY_H-(NCOCA)NNH_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY H-(NCOCA)NNH' _Sample_label $sample_1 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' 74 . mM pH 7.2 . 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 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $TOPSPIN $Felix stop_ loop_ _Experiment_label '2D 1H-15N TROSY' '3D TROSY-HNCO' '3D TROSY HN(CA)CO' '3D TROSY HNCA' '3D TROSY HN(CO)CA' '3D TROSY HNCACB' '3D TROSY HN(CO)CACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name bPGM _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 MET C C 174.643 0.050 1 2 2 2 PHE H H 5.292 0.005 1 3 2 2 PHE C C 173.881 0.050 1 4 2 2 PHE CA C 55.837 0.050 1 5 2 2 PHE CB C 35.903 0.050 1 6 2 2 PHE N N 117.168 0.050 1 7 3 3 LYS H H 8.812 0.005 1 8 3 3 LYS C C 176.665 0.050 1 9 3 3 LYS CA C 55.629 0.050 1 10 3 3 LYS CB C 35.645 0.050 1 11 3 3 LYS N N 116.280 0.050 1 12 4 4 ALA H H 7.680 0.005 1 13 4 4 ALA C C 175.365 0.050 1 14 4 4 ALA CA C 50.730 0.050 1 15 4 4 ALA CB C 22.578 0.050 1 16 4 4 ALA N N 121.034 0.050 1 17 5 5 VAL H H 8.699 0.005 1 18 5 5 VAL C C 172.768 0.050 1 19 5 5 VAL CA C 61.032 0.050 1 20 5 5 VAL CB C 32.691 0.050 1 21 5 5 VAL N N 119.864 0.050 1 22 6 6 LEU H H 9.318 0.005 1 23 6 6 LEU C C 175.576 0.050 1 24 6 6 LEU CA C 51.761 0.050 1 25 6 6 LEU CB C 40.642 0.050 1 26 6 6 LEU N N 125.887 0.050 1 27 7 7 PHE H H 9.425 0.005 1 28 7 7 PHE C C 177.315 0.050 1 29 7 7 PHE CA C 59.003 0.050 1 30 7 7 PHE CB C 40.715 0.050 1 31 7 7 PHE N N 122.408 0.050 1 32 8 8 ASP H H 7.203 0.005 1 33 8 8 ASP CA C 54.399 0.050 1 34 8 8 ASP N N 121.468 0.050 1 35 11 11 GLY C C 171.764 0.050 1 36 11 11 GLY CA C 44.804 0.050 1 37 12 12 VAL H H 7.452 0.005 1 38 12 12 VAL C C 172.726 0.050 1 39 12 12 VAL CA C 64.215 0.050 1 40 12 12 VAL CB C 33.269 0.050 1 41 12 12 VAL N N 118.211 0.050 1 42 13 13 ILE H H 8.067 0.005 1 43 13 13 ILE C C 175.378 0.050 1 44 13 13 ILE CA C 63.538 0.050 1 45 13 13 ILE CB C 38.410 0.050 1 46 13 13 ILE N N 114.485 0.050 1 47 14 14 THR H H 7.195 0.005 1 48 14 14 THR C C 175.798 0.050 1 49 14 14 THR CA C 59.078 0.050 1 50 14 14 THR CB C 67.115 0.050 1 51 14 14 THR N N 109.322 0.050 1 52 15 15 ASP H H 8.218 0.005 1 53 15 15 ASP C C 176.715 0.050 1 54 15 15 ASP CA C 53.678 0.050 1 55 15 15 ASP CB C 42.639 0.050 1 56 15 15 ASP N N 121.200 0.050 1 57 16 16 THR H H 9.257 0.005 1 58 16 16 THR C C 176.233 0.050 1 59 16 16 THR CA C 61.040 0.050 1 60 16 16 THR CB C 68.709 0.050 1 61 16 16 THR N N 115.201 0.050 1 62 17 17 ALA H H 9.002 0.005 1 63 17 17 ALA C C 180.990 0.050 1 64 17 17 ALA CA C 56.222 0.050 1 65 17 17 ALA CB C 18.223 0.050 1 66 17 17 ALA N N 128.848 0.050 1 67 18 18 GLU H H 9.209 0.005 1 68 18 18 GLU C C 178.238 0.050 1 69 18 18 GLU CA C 58.426 0.050 1 70 18 18 GLU CB C 28.378 0.050 1 71 18 18 GLU N N 119.792 0.050 1 72 19 19 TYR H H 7.330 0.005 1 73 19 19 TYR C C 178.712 0.050 1 74 19 19 TYR CA C 60.867 0.050 1 75 19 19 TYR CB C 37.187 0.050 1 76 19 19 TYR N N 118.094 0.050 1 77 20 20 HIS H H 8.015 0.005 1 78 20 20 HIS C C 177.338 0.050 1 79 20 20 HIS CA C 61.697 0.050 1 80 20 20 HIS CB C 30.767 0.050 1 81 20 20 HIS N N 119.096 0.050 1 82 21 21 PHE H H 8.394 0.005 1 83 21 21 PHE C C 176.988 0.050 1 84 21 21 PHE CA C 60.217 0.050 1 85 21 21 PHE CB C 37.457 0.050 1 86 21 21 PHE N N 119.080 0.050 1 87 22 22 ARG H H 8.409 0.005 1 88 22 22 ARG C C 179.560 0.050 1 89 22 22 ARG CA C 59.306 0.050 1 90 22 22 ARG CB C 29.857 0.050 1 91 22 22 ARG N N 117.815 0.050 1 92 23 23 ALA H H 8.188 0.005 1 93 23 23 ALA C C 179.781 0.050 1 94 23 23 ALA CA C 55.263 0.050 1 95 23 23 ALA CB C 17.857 0.050 1 96 23 23 ALA N N 123.241 0.050 1 97 24 24 TRP H H 8.526 0.005 1 98 24 24 TRP C C 178.644 0.050 1 99 24 24 TRP CA C 59.291 0.050 1 100 24 24 TRP CB C 29.815 0.050 1 101 24 24 TRP N N 120.042 0.050 1 102 25 25 LYS H H 8.837 0.005 1 103 25 25 LYS C C 178.208 0.050 1 104 25 25 LYS CA C 59.595 0.050 1 105 25 25 LYS CB C 31.453 0.050 1 106 25 25 LYS N N 120.879 0.050 1 107 26 26 ALA H H 7.825 0.005 1 108 26 26 ALA C C 180.692 0.050 1 109 26 26 ALA CA C 54.159 0.050 1 110 26 26 ALA CB C 17.145 0.050 1 111 26 26 ALA N N 119.553 0.050 1 112 27 27 LEU H H 7.473 0.005 1 113 27 27 LEU C C 178.106 0.050 1 114 27 27 LEU CA C 57.087 0.050 1 115 27 27 LEU CB C 41.484 0.050 1 116 27 27 LEU N N 120.310 0.050 1 117 28 28 ALA H H 8.673 0.005 1 118 28 28 ALA C C 179.743 0.050 1 119 28 28 ALA CA C 55.033 0.050 1 120 28 28 ALA CB C 17.343 0.050 1 121 28 28 ALA N N 120.867 0.050 1 122 29 29 GLU H H 8.288 0.005 1 123 29 29 GLU C C 180.242 0.050 1 124 29 29 GLU CA C 58.742 0.050 1 125 29 29 GLU CB C 28.305 0.050 1 126 29 29 GLU N N 116.949 0.050 1 127 30 30 GLU H H 7.854 0.005 1 128 30 30 GLU C C 178.794 0.050 1 129 30 30 GLU CA C 58.873 0.050 1 130 30 30 GLU CB C 28.794 0.050 1 131 30 30 GLU N N 121.329 0.050 1 132 31 31 ILE H H 7.670 0.005 1 133 31 31 ILE C C 175.972 0.050 1 134 31 31 ILE CA C 61.013 0.050 1 135 31 31 ILE CB C 36.931 0.050 1 136 31 31 ILE N N 111.716 0.050 1 137 32 32 GLY H H 7.605 0.005 1 138 32 32 GLY C C 174.563 0.050 1 139 32 32 GLY CA C 45.959 0.050 1 140 32 32 GLY N N 109.548 0.050 1 141 33 33 ILE H H 8.285 0.005 1 142 33 33 ILE C C 175.029 0.050 1 143 33 33 ILE CA C 60.908 0.050 1 144 33 33 ILE CB C 38.312 0.050 1 145 33 33 ILE N N 122.350 0.050 1 146 34 34 ASN H H 8.536 0.005 1 147 34 34 ASN C C 175.152 0.050 1 148 34 34 ASN CA C 52.587 0.050 1 149 34 34 ASN CB C 39.426 0.050 1 150 34 34 ASN N N 126.047 0.050 1 151 35 35 GLY H H 7.945 0.005 1 152 35 35 GLY C C 174.213 0.050 1 153 35 35 GLY CA C 44.847 0.050 1 154 35 35 GLY N N 107.471 0.050 1 155 36 36 VAL H H 8.454 0.005 1 156 36 36 VAL C C 174.088 0.050 1 157 36 36 VAL CA C 62.471 0.050 1 158 36 36 VAL CB C 28.620 0.050 1 159 36 36 VAL N N 122.107 0.050 1 160 37 37 ASP H H 7.555 0.005 1 161 37 37 ASP C C 181.485 0.050 1 162 37 37 ASP CA C 51.563 0.050 1 163 37 37 ASP CB C 41.619 0.050 1 164 37 37 ASP N N 126.142 0.050 1 165 38 38 ARG C C 178.634 0.050 1 166 38 38 ARG CA C 59.319 0.050 1 167 38 38 ARG CB C 28.332 0.050 1 168 39 39 GLN H H 8.048 0.005 1 169 39 39 GLN C C 178.803 0.050 1 170 39 39 GLN CA C 58.487 0.050 1 171 39 39 GLN CB C 27.249 0.050 1 172 39 39 GLN N N 119.685 0.050 1 173 40 40 PHE H H 8.583 0.005 1 174 40 40 PHE C C 177.605 0.050 1 175 40 40 PHE CA C 61.176 0.050 1 176 40 40 PHE CB C 38.812 0.050 1 177 40 40 PHE N N 123.805 0.050 1 178 41 41 ASN H H 8.348 0.005 1 179 41 41 ASN C C 177.503 0.050 1 180 41 41 ASN CA C 56.071 0.050 1 181 41 41 ASN CB C 39.226 0.050 1 182 41 41 ASN N N 116.002 0.050 1 183 42 42 GLU H H 7.716 0.005 1 184 42 42 GLU C C 179.108 0.050 1 185 42 42 GLU CA C 58.699 0.050 1 186 42 42 GLU CB C 28.395 0.050 1 187 42 42 GLU N N 119.049 0.050 1 188 43 43 GLN H H 7.673 0.005 1 189 43 43 GLN C C 176.265 0.050 1 190 43 43 GLN CA C 56.267 0.050 1 191 43 43 GLN CB C 27.421 0.050 1 192 43 43 GLN N N 115.930 0.050 1 193 46 46 GLY C C 174.337 0.050 1 194 46 46 GLY CA C 45.451 0.050 1 195 47 47 VAL H H 7.484 0.005 1 196 47 47 VAL C C 176.486 0.050 1 197 47 47 VAL CA C 61.347 0.050 1 198 47 47 VAL CB C 31.628 0.050 1 199 47 47 VAL N N 120.017 0.050 1 200 53 53 LEU C C 178.267 0.050 1 201 53 53 LEU CA C 57.044 0.050 1 202 53 53 LEU CB C 39.284 0.050 1 203 54 54 GLN H H 8.149 0.005 1 204 54 54 GLN C C 177.219 0.050 1 205 54 54 GLN CA C 58.199 0.050 1 206 54 54 GLN CB C 27.951 0.050 1 207 54 54 GLN N N 117.708 0.050 1 208 55 55 LYS H H 7.587 0.005 1 209 55 55 LYS C C 179.565 0.050 1 210 55 55 LYS CA C 59.183 0.050 1 211 55 55 LYS CB C 31.343 0.050 1 212 55 55 LYS N N 117.767 0.050 1 213 56 56 ILE H H 7.525 0.005 1 214 56 56 ILE C C 177.418 0.050 1 215 56 56 ILE CA C 64.892 0.050 1 216 56 56 ILE CB C 37.100 0.050 1 217 56 56 ILE N N 120.253 0.050 1 218 57 57 LEU H H 8.311 0.005 1 219 57 57 LEU C C 180.803 0.050 1 220 57 57 LEU CA C 57.782 0.050 1 221 57 57 LEU CB C 38.962 0.050 1 222 57 57 LEU N N 119.474 0.050 1 223 58 58 ASP H H 8.667 0.005 1 224 58 58 ASP C C 179.485 0.050 1 225 58 58 ASP CA C 56.407 0.050 1 226 58 58 ASP CB C 39.507 0.050 1 227 58 58 ASP N N 119.247 0.050 1 228 59 59 LEU H H 7.727 0.005 1 229 59 59 LEU C C 178.334 0.050 1 230 59 59 LEU CA C 57.310 0.050 1 231 59 59 LEU CB C 40.886 0.050 1 232 59 59 LEU N N 122.529 0.050 1 233 60 60 ALA H H 7.206 0.005 1 234 60 60 ALA C C 176.014 0.050 1 235 60 60 ALA CA C 50.374 0.050 1 236 60 60 ALA CB C 20.032 0.050 1 237 60 60 ALA N N 118.929 0.050 1 238 61 61 ASP H H 7.887 0.005 1 239 61 61 ASP C C 174.730 0.050 1 240 61 61 ASP CA C 54.992 0.050 1 241 61 61 ASP CB C 39.374 0.050 1 242 61 61 ASP N N 120.237 0.050 1 243 62 62 LYS H H 7.836 0.005 1 244 62 62 LYS C C 175.500 0.050 1 245 62 62 LYS CA C 55.352 0.050 1 246 62 62 LYS CB C 33.173 0.050 1 247 62 62 LYS N N 118.423 0.050 1 248 63 63 LYS H H 8.511 0.005 1 249 63 63 LYS C C 176.365 0.050 1 250 63 63 LYS CA C 54.445 0.050 1 251 63 63 LYS CB C 32.182 0.050 1 252 63 63 LYS N N 126.509 0.050 1 253 64 64 VAL H H 8.441 0.005 1 254 64 64 VAL C C 175.826 0.050 1 255 64 64 VAL CA C 58.270 0.050 1 256 64 64 VAL CB C 34.350 0.050 1 257 64 64 VAL N N 116.389 0.050 1 258 65 65 SER H H 9.033 0.005 1 259 65 65 SER C C 174.666 0.050 1 260 65 65 SER CA C 57.066 0.050 1 261 65 65 SER CB C 64.779 0.050 1 262 65 65 SER N N 119.417 0.050 1 263 66 66 ALA H H 8.932 0.005 1 264 66 66 ALA C C 181.069 0.050 1 265 66 66 ALA CA C 55.065 0.050 1 266 66 66 ALA CB C 17.195 0.050 1 267 66 66 ALA N N 124.046 0.050 1 268 67 67 GLU H H 8.602 0.005 1 269 67 67 GLU C C 179.491 0.050 1 270 67 67 GLU CA C 59.422 0.050 1 271 67 67 GLU CB C 28.349 0.050 1 272 67 67 GLU N N 117.938 0.050 1 273 68 68 GLU H H 7.900 0.005 1 274 68 68 GLU C C 178.740 0.050 1 275 68 68 GLU CA C 58.666 0.050 1 276 68 68 GLU CB C 29.376 0.050 1 277 68 68 GLU N N 122.551 0.050 1 278 69 69 PHE H H 8.899 0.005 1 279 69 69 PHE C C 176.849 0.050 1 280 69 69 PHE CA C 62.051 0.050 1 281 69 69 PHE CB C 38.780 0.050 1 282 69 69 PHE N N 121.637 0.050 1 283 70 70 LYS H H 7.647 0.005 1 284 70 70 LYS C C 179.928 0.050 1 285 70 70 LYS CA C 59.224 0.050 1 286 70 70 LYS CB C 31.662 0.050 1 287 70 70 LYS N N 116.466 0.050 1 288 71 71 GLU H H 7.740 0.005 1 289 71 71 GLU C C 179.176 0.050 1 290 71 71 GLU CA C 58.658 0.050 1 291 71 71 GLU CB C 28.284 0.050 1 292 71 71 GLU N N 121.020 0.050 1 293 72 72 LEU H H 8.477 0.005 1 294 72 72 LEU C C 178.300 0.050 1 295 72 72 LEU CA C 57.480 0.050 1 296 72 72 LEU CB C 41.560 0.050 1 297 72 72 LEU N N 121.889 0.050 1 298 73 73 ALA H H 7.996 0.005 1 299 73 73 ALA C C 180.260 0.050 1 300 73 73 ALA CA C 55.090 0.050 1 301 73 73 ALA CB C 16.239 0.050 1 302 73 73 ALA N N 121.109 0.050 1 303 74 74 LYS H H 7.665 0.005 1 304 74 74 LYS C C 178.636 0.050 1 305 74 74 LYS CA C 59.162 0.050 1 306 74 74 LYS CB C 31.169 0.050 1 307 74 74 LYS N N 120.115 0.050 1 308 75 75 ARG H H 8.279 0.005 1 309 75 75 ARG C C 179.161 0.050 1 310 75 75 ARG CA C 58.841 0.050 1 311 75 75 ARG CB C 28.904 0.050 1 312 75 75 ARG N N 121.227 0.050 1 313 76 76 LYS H H 7.908 0.005 1 314 76 76 LYS C C 178.830 0.050 1 315 76 76 LYS CA C 60.360 0.050 1 316 76 76 LYS CB C 28.790 0.050 1 317 76 76 LYS N N 119.503 0.050 1 318 77 77 ASN H H 7.531 0.005 1 319 77 77 ASN C C 176.558 0.050 1 320 77 77 ASN CA C 56.535 0.050 1 321 77 77 ASN CB C 37.882 0.050 1 322 77 77 ASN N N 118.892 0.050 1 323 78 78 ASP H H 8.680 0.005 1 324 78 78 ASP C C 179.425 0.050 1 325 78 78 ASP CA C 56.986 0.050 1 326 78 78 ASP CB C 39.127 0.050 1 327 78 78 ASP N N 121.036 0.050 1 328 79 79 ASN H H 8.327 0.005 1 329 79 79 ASN C C 176.750 0.050 1 330 79 79 ASN CA C 55.014 0.050 1 331 79 79 ASN CB C 37.175 0.050 1 332 79 79 ASN N N 119.495 0.050 1 333 80 80 TYR H H 8.292 0.005 1 334 80 80 TYR C C 175.694 0.050 1 335 80 80 TYR CA C 62.041 0.050 1 336 80 80 TYR CB C 37.889 0.050 1 337 80 80 TYR N N 122.587 0.050 1 338 81 81 VAL H H 8.288 0.005 1 339 81 81 VAL C C 177.808 0.050 1 340 81 81 VAL CA C 65.828 0.050 1 341 81 81 VAL CB C 30.557 0.050 1 342 81 81 VAL N N 118.069 0.050 1 343 82 82 LYS H H 7.281 0.005 1 344 82 82 LYS C C 179.905 0.050 1 345 82 82 LYS CA C 58.605 0.050 1 346 82 82 LYS CB C 31.222 0.050 1 347 82 82 LYS N N 118.869 0.050 1 348 83 83 MET H H 8.145 0.005 1 349 83 83 MET C C 179.352 0.050 1 350 83 83 MET CA C 58.156 0.050 1 351 83 83 MET CB C 31.595 0.050 1 352 83 83 MET N N 119.457 0.050 1 353 84 84 ILE H H 7.778 0.005 1 354 84 84 ILE C C 176.408 0.050 1 355 84 84 ILE CA C 63.419 0.050 1 356 84 84 ILE CB C 35.653 0.050 1 357 84 84 ILE N N 111.188 0.050 1 358 85 85 GLN H H 7.078 0.005 1 359 85 85 GLN C C 176.367 0.050 1 360 85 85 GLN CA C 57.731 0.050 1 361 85 85 GLN CB C 27.406 0.050 1 362 85 85 GLN N N 118.864 0.050 1 363 86 86 ASP H H 7.296 0.005 1 364 86 86 ASP C C 177.037 0.050 1 365 86 86 ASP CA C 54.227 0.050 1 366 86 86 ASP CB C 40.847 0.050 1 367 86 86 ASP N N 114.401 0.050 1 368 87 87 VAL H H 7.106 0.005 1 369 87 87 VAL C C 173.885 0.050 1 370 87 87 VAL CA C 63.678 0.050 1 371 87 87 VAL CB C 30.012 0.050 1 372 87 87 VAL N N 124.420 0.050 1 373 88 88 SER H H 9.183 0.005 1 374 88 88 SER CA C 57.232 0.050 1 375 88 88 SER CB C 65.409 0.050 1 376 88 88 SER N N 125.256 0.050 1 377 89 89 PRO C C 177.777 0.050 1 378 89 89 PRO CA C 64.951 0.050 1 379 89 89 PRO CB C 30.695 0.050 1 380 90 90 ALA H H 7.781 0.005 1 381 90 90 ALA C C 178.077 0.050 1 382 90 90 ALA CA C 53.303 0.050 1 383 90 90 ALA CB C 17.561 0.050 1 384 90 90 ALA N N 119.811 0.050 1 385 91 91 ASP H H 8.126 0.005 1 386 91 91 ASP C C 177.128 0.050 1 387 91 91 ASP CA C 55.331 0.050 1 388 91 91 ASP CB C 40.952 0.050 1 389 91 91 ASP N N 115.576 0.050 1 390 92 92 VAL H H 7.211 0.005 1 391 92 92 VAL C C 176.870 0.050 1 392 92 92 VAL CA C 63.640 0.050 1 393 92 92 VAL CB C 31.024 0.050 1 394 92 92 VAL N N 123.541 0.050 1 395 93 93 TYR H H 9.003 0.005 1 396 93 93 TYR C C 175.307 0.050 1 397 93 93 TYR CA C 54.447 0.050 1 398 93 93 TYR CB C 34.645 0.050 1 399 93 93 TYR N N 130.892 0.050 1 400 94 94 PRO C C 177.355 0.050 1 401 94 94 PRO CA C 63.280 0.050 1 402 94 94 PRO CB C 31.325 0.050 1 403 95 95 GLY H H 8.476 0.005 1 404 95 95 GLY C C 175.956 0.050 1 405 95 95 GLY CA C 45.827 0.050 1 406 95 95 GLY N N 111.397 0.050 1 407 96 96 ILE H H 7.179 0.005 1 408 96 96 ILE C C 176.921 0.050 1 409 96 96 ILE CA C 61.173 0.050 1 410 96 96 ILE CB C 33.752 0.050 1 411 96 96 ILE N N 121.479 0.050 1 412 97 97 LEU H H 8.872 0.005 1 413 97 97 LEU C C 177.932 0.050 1 414 97 97 LEU CA C 58.267 0.050 1 415 97 97 LEU CB C 40.229 0.050 1 416 97 97 LEU N N 121.195 0.050 1 417 98 98 GLN H H 8.711 0.005 1 418 98 98 GLN C C 177.437 0.050 1 419 98 98 GLN CA C 57.607 0.050 1 420 98 98 GLN CB C 27.463 0.050 1 421 98 98 GLN N N 117.654 0.050 1 422 99 99 LEU H H 7.828 0.005 1 423 99 99 LEU C C 178.518 0.050 1 424 99 99 LEU CA C 57.836 0.050 1 425 99 99 LEU CB C 39.831 0.050 1 426 99 99 LEU N N 119.564 0.050 1 427 100 100 LEU H H 8.343 0.005 1 428 100 100 LEU C C 179.020 0.050 1 429 100 100 LEU CA C 57.891 0.050 1 430 100 100 LEU CB C 39.401 0.050 1 431 100 100 LEU N N 119.078 0.050 1 432 101 101 LYS H H 7.946 0.005 1 433 101 101 LYS C C 180.301 0.050 1 434 101 101 LYS CA C 60.006 0.050 1 435 101 101 LYS CB C 31.930 0.050 1 436 101 101 LYS N N 117.730 0.050 1 437 102 102 ASP H H 8.741 0.005 1 438 102 102 ASP C C 179.793 0.050 1 439 102 102 ASP CA C 57.100 0.050 1 440 102 102 ASP CB C 39.496 0.050 1 441 102 102 ASP N N 122.513 0.050 1 442 103 103 LEU H H 9.393 0.005 1 443 103 103 LEU C C 179.065 0.050 1 444 103 103 LEU CA C 58.295 0.050 1 445 103 103 LEU CB C 39.947 0.050 1 446 103 103 LEU N N 123.648 0.050 1 447 104 104 ARG H H 8.373 0.005 1 448 104 104 ARG C C 181.875 0.050 1 449 104 104 ARG CA C 59.105 0.050 1 450 104 104 ARG CB C 28.454 0.050 1 451 104 104 ARG N N 120.140 0.050 1 452 105 105 SER H H 8.712 0.005 1 453 105 105 SER C C 175.178 0.050 1 454 105 105 SER CA C 61.194 0.050 1 455 105 105 SER CB C 62.273 0.050 1 456 105 105 SER N N 117.198 0.050 1 457 106 106 ASN H H 7.450 0.005 1 458 106 106 ASN C C 172.417 0.050 1 459 106 106 ASN CA C 53.628 0.050 1 460 106 106 ASN CB C 39.438 0.050 1 461 106 106 ASN N N 118.213 0.050 1 462 107 107 LYS H H 7.930 0.005 1 463 107 107 LYS C C 175.115 0.050 1 464 107 107 LYS CA C 56.879 0.050 1 465 107 107 LYS CB C 27.334 0.050 1 466 107 107 LYS N N 114.763 0.050 1 467 108 108 ILE H H 7.981 0.005 1 468 108 108 ILE C C 175.778 0.050 1 469 108 108 ILE CA C 60.017 0.050 1 470 108 108 ILE CB C 36.939 0.050 1 471 108 108 ILE N N 122.370 0.050 1 472 109 109 LYS H H 7.735 0.005 1 473 109 109 LYS C C 175.858 0.050 1 474 109 109 LYS CA C 55.020 0.050 1 475 109 109 LYS CB C 32.575 0.050 1 476 109 109 LYS N N 125.138 0.050 1 477 110 110 ILE H H 9.318 0.005 1 478 110 110 ILE C C 175.841 0.050 1 479 110 110 ILE CA C 61.078 0.050 1 480 110 110 ILE CB C 40.022 0.050 1 481 110 110 ILE N N 122.237 0.050 1 482 111 111 ALA H H 8.801 0.005 1 483 111 111 ALA C C 176.305 0.050 1 484 111 111 ALA CA C 49.027 0.050 1 485 111 111 ALA CB C 23.593 0.050 1 486 111 111 ALA N N 127.732 0.050 1 487 112 112 LEU H H 8.477 0.005 1 488 112 112 LEU C C 174.173 0.050 1 489 112 112 LEU CA C 53.868 0.050 1 490 112 112 LEU CB C 42.589 0.050 1 491 112 112 LEU N N 123.208 0.050 1 492 113 113 ALA H H 9.306 0.005 1 493 113 113 ALA C C 173.606 0.050 1 494 113 113 ALA CA C 49.171 0.050 1 495 113 113 ALA CB C 18.451 0.050 1 496 113 113 ALA N N 134.373 0.050 1 497 114 114 SER H H 7.312 0.005 1 498 114 114 SER C C 174.428 0.050 1 499 114 114 SER CA C 55.961 0.050 1 500 114 114 SER CB C 64.309 0.050 1 501 114 114 SER N N 111.887 0.050 1 502 115 115 ALA H H 8.946 0.005 1 503 115 115 ALA C C 176.645 0.050 1 504 115 115 ALA CA C 51.544 0.050 1 505 115 115 ALA CB C 18.398 0.050 1 506 115 115 ALA N N 129.265 0.050 1 507 116 116 SER H H 8.230 0.005 1 508 116 116 SER CA C 57.463 0.050 1 509 116 116 SER N N 113.152 0.050 1 510 118 118 ASN C C 174.767 0.050 1 511 118 118 ASN CA C 53.002 0.050 1 512 118 118 ASN CB C 38.638 0.050 1 513 119 119 GLY H H 7.477 0.005 1 514 119 119 GLY C C 172.131 0.050 1 515 119 119 GLY CA C 48.198 0.050 1 516 119 119 GLY N N 106.243 0.050 1 517 120 120 PRO C C 179.208 0.050 1 518 120 120 PRO CA C 65.627 0.050 1 519 120 120 PRO CB C 30.420 0.050 1 520 121 121 PHE H H 7.690 0.005 1 521 121 121 PHE C C 177.341 0.050 1 522 121 121 PHE CA C 60.411 0.050 1 523 121 121 PHE CB C 38.602 0.050 1 524 121 121 PHE N N 119.552 0.050 1 525 122 122 LEU H H 8.214 0.005 1 526 122 122 LEU C C 178.757 0.050 1 527 122 122 LEU CA C 57.739 0.050 1 528 122 122 LEU CB C 40.448 0.050 1 529 122 122 LEU N N 119.892 0.050 1 530 123 123 LEU H H 8.241 0.005 1 531 123 123 LEU C C 178.947 0.050 1 532 123 123 LEU CA C 58.145 0.050 1 533 123 123 LEU CB C 40.094 0.050 1 534 123 123 LEU N N 117.135 0.050 1 535 124 124 GLU H H 7.630 0.005 1 536 124 124 GLU C C 180.865 0.050 1 537 124 124 GLU CA C 58.739 0.050 1 538 124 124 GLU CB C 27.901 0.050 1 539 124 124 GLU N N 121.134 0.050 1 540 125 125 ARG H H 8.088 0.005 1 541 125 125 ARG C C 178.425 0.050 1 542 125 125 ARG CA C 56.725 0.050 1 543 125 125 ARG CB C 28.194 0.050 1 544 125 125 ARG N N 120.894 0.050 1 545 126 126 MET H H 7.322 0.005 1 546 126 126 MET C C 173.638 0.050 1 547 126 126 MET CA C 55.989 0.050 1 548 126 126 MET CB C 32.513 0.050 1 549 126 126 MET N N 113.323 0.050 1 550 127 127 ASN H H 8.012 0.005 1 551 127 127 ASN C C 175.849 0.050 1 552 127 127 ASN CA C 53.441 0.050 1 553 127 127 ASN CB C 36.480 0.050 1 554 127 127 ASN N N 116.870 0.050 1 555 128 128 LEU H H 8.749 0.005 1 556 128 128 LEU C C 177.868 0.050 1 557 128 128 LEU CA C 53.645 0.050 1 558 128 128 LEU CB C 44.084 0.050 1 559 128 128 LEU N N 113.988 0.050 1 560 129 129 THR H H 7.398 0.005 1 561 129 129 THR C C 176.310 0.050 1 562 129 129 THR CA C 67.154 0.050 1 563 129 129 THR CB C 68.555 0.050 1 564 129 129 THR N N 115.880 0.050 1 565 130 130 GLY H H 8.595 0.005 1 566 130 130 GLY C C 174.848 0.050 1 567 130 130 GLY CA C 45.626 0.050 1 568 130 130 GLY N N 106.106 0.050 1 569 131 131 TYR H H 7.756 0.005 1 570 131 131 TYR C C 174.541 0.050 1 571 131 131 TYR CA C 59.480 0.050 1 572 131 131 TYR CB C 38.870 0.050 1 573 131 131 TYR N N 116.007 0.050 1 574 132 132 PHE H H 7.282 0.005 1 575 132 132 PHE C C 175.802 0.050 1 576 132 132 PHE CA C 58.259 0.050 1 577 132 132 PHE CB C 39.054 0.050 1 578 132 132 PHE N N 115.203 0.050 1 579 133 133 ASP H H 9.137 0.005 1 580 133 133 ASP C C 176.431 0.050 1 581 133 133 ASP CA C 56.761 0.050 1 582 133 133 ASP CB C 42.291 0.050 1 583 133 133 ASP N N 124.909 0.050 1 584 134 134 ALA H H 7.688 0.005 1 585 134 134 ALA C C 175.228 0.050 1 586 134 134 ALA CA C 51.651 0.050 1 587 134 134 ALA CB C 23.410 0.050 1 588 134 134 ALA N N 115.338 0.050 1 589 135 135 ILE H H 8.567 0.005 1 590 135 135 ILE C C 175.444 0.050 1 591 135 135 ILE CA C 60.154 0.050 1 592 135 135 ILE CB C 39.659 0.050 1 593 135 135 ILE N N 121.169 0.050 1 594 136 136 ALA H H 8.247 0.005 1 595 136 136 ALA C C 175.716 0.050 1 596 136 136 ALA CA C 52.258 0.050 1 597 136 136 ALA CB C 17.866 0.050 1 598 136 136 ALA N N 128.888 0.050 1 599 137 137 ASP H H 8.497 0.005 1 600 137 137 ASP C C 176.252 0.050 1 601 137 137 ASP CA C 50.712 0.050 1 602 137 137 ASP CB C 41.096 0.050 1 603 137 137 ASP N N 123.672 0.050 1 604 138 138 PRO C C 178.088 0.050 1 605 138 138 PRO CA C 63.814 0.050 1 606 138 138 PRO CB C 31.226 0.050 1 607 139 139 ALA H H 8.479 0.005 1 608 139 139 ALA C C 179.046 0.050 1 609 139 139 ALA CA C 53.205 0.050 1 610 139 139 ALA CB C 17.873 0.050 1 611 139 139 ALA N N 120.862 0.050 1 612 140 140 GLU H H 7.661 0.005 1 613 140 140 GLU C C 176.142 0.050 1 614 140 140 GLU CA C 55.297 0.050 1 615 140 140 GLU CB C 29.450 0.050 1 616 140 140 GLU N N 116.078 0.050 1 617 141 141 VAL H H 7.208 0.005 1 618 141 141 VAL C C 175.381 0.050 1 619 141 141 VAL CA C 60.927 0.050 1 620 141 141 VAL CB C 31.398 0.050 1 621 141 141 VAL N N 118.184 0.050 1 622 142 142 ALA H H 8.576 0.005 1 623 142 142 ALA C C 177.516 0.050 1 624 142 142 ALA CA C 52.956 0.050 1 625 142 142 ALA CB C 18.514 0.050 1 626 142 142 ALA N N 127.927 0.050 1 627 143 143 ALA H H 7.517 0.005 1 628 143 143 ALA C C 176.556 0.050 1 629 143 143 ALA CA C 50.910 0.050 1 630 143 143 ALA CB C 20.582 0.050 1 631 143 143 ALA N N 120.674 0.050 1 632 144 144 SER H H 8.406 0.005 1 633 144 144 SER C C 175.236 0.050 1 634 144 144 SER CA C 57.026 0.050 1 635 144 144 SER CB C 63.840 0.050 1 636 144 144 SER N N 117.052 0.050 1 637 145 145 LYS H H 8.583 0.005 1 638 145 145 LYS CA C 56.540 0.050 1 639 145 145 LYS CB C 28.435 0.050 1 640 145 145 LYS N N 124.861 0.050 1 641 146 146 PRO C C 175.837 0.050 1 642 146 146 PRO CA C 63.074 0.050 1 643 146 146 PRO CB C 34.740 0.050 1 644 147 147 ALA H H 8.939 0.005 1 645 147 147 ALA C C 178.075 0.050 1 646 147 147 ALA CA C 51.576 0.050 1 647 147 147 ALA CB C 16.856 0.050 1 648 147 147 ALA N N 131.421 0.050 1 649 148 148 PRO C C 177.227 0.050 1 650 148 148 PRO CA C 63.587 0.050 1 651 148 148 PRO CB C 31.938 0.050 1 652 149 149 ASP H H 9.212 0.005 1 653 149 149 ASP C C 177.889 0.050 1 654 149 149 ASP CA C 57.884 0.050 1 655 149 149 ASP CB C 39.452 0.050 1 656 149 149 ASP N N 120.548 0.050 1 657 150 150 ILE H H 9.631 0.005 1 658 150 150 ILE C C 175.762 0.050 1 659 150 150 ILE CA C 62.528 0.050 1 660 150 150 ILE CB C 37.017 0.050 1 661 150 150 ILE N N 119.757 0.050 1 662 151 151 PHE H H 7.314 0.005 1 663 151 151 PHE C C 177.743 0.050 1 664 151 151 PHE CA C 63.158 0.050 1 665 151 151 PHE CB C 38.114 0.050 1 666 151 151 PHE N N 121.030 0.050 1 667 152 152 ILE H H 7.819 0.005 1 668 152 152 ILE C C 177.997 0.050 1 669 152 152 ILE CA C 65.719 0.050 1 670 152 152 ILE CB C 37.217 0.050 1 671 152 152 ILE N N 120.906 0.050 1 672 153 153 ALA H H 8.473 0.005 1 673 153 153 ALA C C 181.038 0.050 1 674 153 153 ALA CA C 54.253 0.050 1 675 153 153 ALA CB C 17.483 0.050 1 676 153 153 ALA N N 120.320 0.050 1 677 154 154 ALA H H 7.817 0.005 1 678 154 154 ALA C C 176.697 0.050 1 679 154 154 ALA CA C 55.001 0.050 1 680 154 154 ALA CB C 17.860 0.050 1 681 154 154 ALA N N 122.364 0.050 1 682 155 155 ALA H H 7.684 0.005 1 683 155 155 ALA C C 179.691 0.050 1 684 155 155 ALA CA C 54.349 0.050 1 685 155 155 ALA CB C 16.050 0.050 1 686 155 155 ALA N N 118.887 0.050 1 687 156 156 HIS H H 8.442 0.005 1 688 156 156 HIS C C 179.428 0.050 1 689 156 156 HIS CA C 58.045 0.050 1 690 156 156 HIS CB C 28.767 0.050 1 691 156 156 HIS N N 116.675 0.050 1 692 157 157 ALA H H 8.206 0.005 1 693 157 157 ALA C C 179.137 0.050 1 694 157 157 ALA CA C 54.106 0.050 1 695 157 157 ALA CB C 17.466 0.050 1 696 157 157 ALA N N 121.768 0.050 1 697 158 158 VAL H H 7.231 0.005 1 698 158 158 VAL C C 175.541 0.050 1 699 158 158 VAL CA C 59.549 0.050 1 700 158 158 VAL CB C 30.697 0.050 1 701 158 158 VAL N N 107.524 0.050 1 702 159 159 GLY H H 7.806 0.005 1 703 159 159 GLY C C 174.618 0.050 1 704 159 159 GLY CA C 46.140 0.050 1 705 159 159 GLY N N 110.466 0.050 1 706 160 160 VAL H H 7.656 0.005 1 707 160 160 VAL C C 174.317 0.050 1 708 160 160 VAL CA C 59.038 0.050 1 709 160 160 VAL CB C 33.982 0.050 1 710 160 160 VAL N N 117.068 0.050 1 711 161 161 ALA H H 8.711 0.005 1 712 161 161 ALA C C 178.733 0.050 1 713 161 161 ALA CA C 49.705 0.050 1 714 161 161 ALA CB C 17.098 0.050 1 715 161 161 ALA N N 126.397 0.050 1 716 162 162 PRO C C 177.521 0.050 1 717 162 162 PRO CA C 65.689 0.050 1 718 162 162 PRO CB C 30.658 0.050 1 719 163 163 SER H H 7.774 0.005 1 720 163 163 SER C C 175.931 0.050 1 721 163 163 SER CA C 59.849 0.050 1 722 163 163 SER CB C 61.870 0.050 1 723 163 163 SER N N 106.767 0.050 1 724 164 164 GLU H H 7.842 0.005 1 725 164 164 GLU C C 174.788 0.050 1 726 164 164 GLU CA C 55.547 0.050 1 727 164 164 GLU CB C 29.104 0.050 1 728 164 164 GLU N N 121.695 0.050 1 729 165 165 SER H H 8.046 0.005 1 730 165 165 SER C C 172.110 0.050 1 731 165 165 SER CA C 57.582 0.050 1 732 165 165 SER CB C 65.269 0.050 1 733 165 165 SER N N 114.768 0.050 1 734 166 166 ILE H H 7.706 0.005 1 735 166 166 ILE C C 175.358 0.050 1 736 166 166 ILE CA C 58.938 0.050 1 737 166 166 ILE CB C 40.545 0.050 1 738 166 166 ILE N N 121.681 0.050 1 739 167 167 GLY H H 8.724 0.005 1 740 167 167 GLY C C 170.408 0.050 1 741 167 167 GLY CA C 43.334 0.050 1 742 167 167 GLY N N 112.398 0.050 1 743 168 168 LEU H H 7.871 0.005 1 744 168 168 LEU C C 175.375 0.050 1 745 168 168 LEU CA C 53.412 0.050 1 746 168 168 LEU CB C 40.977 0.050 1 747 168 168 LEU N N 123.271 0.050 1 748 169 169 GLU H H 6.875 0.005 1 749 169 169 GLU C C 174.048 0.050 1 750 169 169 GLU CA C 56.443 0.050 1 751 169 169 GLU N N 123.352 0.050 1 752 171 171 SER C C 174.193 0.050 1 753 171 171 SER CA C 55.918 0.050 1 754 172 172 GLN H H 9.310 0.005 1 755 172 172 GLN C C 178.418 0.050 1 756 172 172 GLN CA C 59.946 0.050 1 757 172 172 GLN CB C 27.039 0.050 1 758 172 172 GLN N N 126.525 0.050 1 759 173 173 ALA H H 8.863 0.005 1 760 173 173 ALA C C 180.358 0.050 1 761 173 173 ALA CA C 54.150 0.050 1 762 173 173 ALA CB C 17.274 0.050 1 763 173 173 ALA N N 120.471 0.050 1 764 174 174 GLY H H 7.781 0.005 1 765 174 174 GLY C C 175.099 0.050 1 766 174 174 GLY CA C 46.194 0.050 1 767 174 174 GLY N N 105.715 0.050 1 768 175 175 ILE H H 8.269 0.005 1 769 175 175 ILE C C 177.845 0.050 1 770 175 175 ILE CA C 62.281 0.050 1 771 175 175 ILE CB C 34.398 0.050 1 772 175 175 ILE N N 123.186 0.050 1 773 176 176 GLN H H 8.090 0.005 1 774 176 176 GLN C C 177.045 0.050 1 775 176 176 GLN CA C 58.266 0.050 1 776 176 176 GLN CB C 27.209 0.050 1 777 176 176 GLN N N 120.406 0.050 1 778 177 177 ALA H H 7.658 0.005 1 779 177 177 ALA C C 179.655 0.050 1 780 177 177 ALA CA C 54.740 0.050 1 781 177 177 ALA CB C 19.075 0.050 1 782 177 177 ALA N N 122.201 0.050 1 783 178 178 ILE H H 7.956 0.005 1 784 178 178 ILE C C 180.431 0.050 1 785 178 178 ILE CA C 64.886 0.050 1 786 178 178 ILE CB C 36.513 0.050 1 787 178 178 ILE N N 117.775 0.050 1 788 179 179 LYS H H 8.663 0.005 1 789 179 179 LYS C C 181.060 0.050 1 790 179 179 LYS CA C 59.623 0.050 1 791 179 179 LYS CB C 31.773 0.050 1 792 179 179 LYS N N 120.997 0.050 1 793 180 180 ASP H H 8.671 0.005 1 794 180 180 ASP C C 177.541 0.050 1 795 180 180 ASP CA C 56.281 0.050 1 796 180 180 ASP CB C 38.627 0.050 1 797 180 180 ASP N N 119.253 0.050 1 798 181 181 SER H H 8.091 0.005 1 799 181 181 SER C C 173.835 0.050 1 800 181 181 SER CA C 60.412 0.050 1 801 181 181 SER CB C 64.249 0.050 1 802 181 181 SER N N 117.051 0.050 1 803 182 182 GLY H H 7.350 0.005 1 804 182 182 GLY C C 173.370 0.050 1 805 182 182 GLY CA C 44.137 0.050 1 806 182 182 GLY N N 109.007 0.050 1 807 183 183 ALA H H 7.180 0.005 1 808 183 183 ALA C C 174.931 0.050 1 809 183 183 ALA CA C 50.815 0.050 1 810 183 183 ALA CB C 19.617 0.050 1 811 183 183 ALA N N 124.293 0.050 1 812 184 184 LEU H H 8.168 0.005 1 813 184 184 LEU C C 174.926 0.050 1 814 184 184 LEU CA C 51.725 0.050 1 815 184 184 LEU CB C 43.241 0.050 1 816 184 184 LEU N N 122.675 0.050 1 817 185 185 PRO C C 176.510 0.050 1 818 185 185 PRO CA C 61.302 0.050 1 819 185 185 PRO CB C 31.794 0.050 1 820 186 186 ILE H H 8.262 0.005 1 821 186 186 ILE C C 178.518 0.050 1 822 186 186 ILE CA C 61.558 0.050 1 823 186 186 ILE CB C 38.114 0.050 1 824 186 186 ILE N N 119.319 0.050 1 825 187 187 GLY H H 8.925 0.005 1 826 187 187 GLY C C 171.079 0.050 1 827 187 187 GLY CA C 45.027 0.050 1 828 187 187 GLY N N 115.777 0.050 1 829 188 188 VAL H H 7.908 0.005 1 830 188 188 VAL C C 174.034 0.050 1 831 188 188 VAL CA C 57.173 0.050 1 832 188 188 VAL CB C 31.946 0.050 1 833 188 188 VAL N N 118.703 0.050 1 834 189 189 GLY H H 8.359 0.005 1 835 189 189 GLY C C 171.101 0.050 1 836 189 189 GLY CA C 44.175 0.050 1 837 189 189 GLY N N 113.644 0.050 1 838 190 190 ARG H H 8.652 0.005 1 839 190 190 ARG C C 176.009 0.050 1 840 190 190 ARG CA C 52.587 0.050 1 841 190 190 ARG CB C 29.930 0.050 1 842 190 190 ARG N N 120.755 0.050 1 843 191 191 PRO C C 178.812 0.050 1 844 191 191 PRO CA C 64.604 0.050 1 845 191 191 PRO CB C 30.775 0.050 1 846 192 192 GLU H H 9.691 0.005 1 847 192 192 GLU C C 176.859 0.050 1 848 192 192 GLU CA C 59.344 0.050 1 849 192 192 GLU CB C 27.600 0.050 1 850 192 192 GLU N N 118.599 0.050 1 851 193 193 ASP H H 7.181 0.005 1 852 193 193 ASP C C 176.851 0.050 1 853 193 193 ASP CA C 54.924 0.050 1 854 193 193 ASP CB C 41.776 0.050 1 855 193 193 ASP N N 115.393 0.050 1 856 194 194 LEU H H 7.593 0.005 1 857 194 194 LEU C C 176.170 0.050 1 858 194 194 LEU CA C 55.841 0.050 1 859 194 194 LEU CB C 42.831 0.050 1 860 194 194 LEU N N 117.260 0.050 1 861 195 195 GLY H H 8.024 0.005 1 862 195 195 GLY C C 172.752 0.050 1 863 195 195 GLY CA C 43.678 0.050 1 864 195 195 GLY N N 107.143 0.050 1 865 196 196 ASP H H 7.971 0.005 1 866 196 196 ASP C C 176.960 0.050 1 867 196 196 ASP CA C 53.792 0.050 1 868 196 196 ASP CB C 41.147 0.050 1 869 196 196 ASP N N 116.851 0.050 1 870 197 197 ASP H H 8.846 0.005 1 871 197 197 ASP C C 175.320 0.050 1 872 197 197 ASP CA C 53.528 0.050 1 873 197 197 ASP CB C 39.528 0.050 1 874 197 197 ASP N N 117.207 0.050 1 875 198 198 ILE H H 6.901 0.005 1 876 198 198 ILE C C 175.427 0.050 1 877 198 198 ILE CA C 58.140 0.050 1 878 198 198 ILE CB C 40.324 0.050 1 879 198 198 ILE N N 114.153 0.050 1 880 199 199 VAL H H 9.015 0.005 1 881 199 199 VAL C C 174.351 0.050 1 882 199 199 VAL CA C 63.753 0.050 1 883 199 199 VAL CB C 30.237 0.050 1 884 199 199 VAL N N 125.895 0.050 1 885 200 200 ILE H H 7.997 0.005 1 886 200 200 ILE C C 176.091 0.050 1 887 200 200 ILE CA C 58.227 0.050 1 888 200 200 ILE CB C 41.221 0.050 1 889 200 200 ILE N N 125.757 0.050 1 890 201 201 VAL H H 8.751 0.005 1 891 201 201 VAL C C 174.417 0.050 1 892 201 201 VAL CA C 56.273 0.050 1 893 201 201 VAL CB C 31.589 0.050 1 894 201 201 VAL N N 119.623 0.050 1 895 202 202 PRO C C 177.229 0.050 1 896 202 202 PRO CA C 63.979 0.050 1 897 202 202 PRO CB C 31.053 0.050 1 898 203 203 ASP H H 6.841 0.005 1 899 203 203 ASP C C 175.794 0.050 1 900 203 203 ASP CA C 53.086 0.050 1 901 203 203 ASP CB C 41.495 0.050 1 902 203 203 ASP N N 109.977 0.050 1 903 204 204 THR H H 8.222 0.005 1 904 204 204 THR C C 176.525 0.050 1 905 204 204 THR CA C 65.328 0.050 1 906 204 204 THR CB C 68.828 0.050 1 907 204 204 THR N N 109.141 0.050 1 908 205 205 SER H H 8.853 0.005 1 909 205 205 SER C C 175.629 0.050 1 910 205 205 SER CA C 61.282 0.050 1 911 205 205 SER CB C 61.989 0.050 1 912 205 205 SER N N 119.284 0.050 1 913 206 206 HIS H H 7.244 0.005 1 914 206 206 HIS C C 176.728 0.050 1 915 206 206 HIS CA C 56.758 0.050 1 916 206 206 HIS CB C 30.149 0.050 1 917 206 206 HIS N N 118.121 0.050 1 918 207 207 TYR H H 7.801 0.005 1 919 207 207 TYR C C 173.544 0.050 1 920 207 207 TYR CA C 54.306 0.050 1 921 207 207 TYR CB C 35.355 0.050 1 922 207 207 TYR N N 120.057 0.050 1 923 208 208 THR H H 7.345 0.005 1 924 208 208 THR C C 174.711 0.050 1 925 208 208 THR CA C 57.922 0.050 1 926 208 208 THR CB C 71.129 0.050 1 927 208 208 THR N N 114.317 0.050 1 928 209 209 LEU H H 9.523 0.005 1 929 209 209 LEU C C 177.850 0.050 1 930 209 209 LEU CA C 58.291 0.050 1 931 209 209 LEU CB C 39.764 0.050 1 932 209 209 LEU N N 125.014 0.050 1 933 210 210 GLU H H 8.606 0.005 1 934 210 210 GLU C C 178.839 0.050 1 935 210 210 GLU CA C 59.511 0.050 1 936 210 210 GLU CB C 28.424 0.050 1 937 210 210 GLU N N 116.644 0.050 1 938 211 211 PHE H H 8.187 0.005 1 939 211 211 PHE C C 176.794 0.050 1 940 211 211 PHE CA C 60.919 0.050 1 941 211 211 PHE CB C 39.380 0.050 1 942 211 211 PHE N N 122.077 0.050 1 943 212 212 LEU H H 8.391 0.005 1 944 212 212 LEU C C 179.075 0.050 1 945 212 212 LEU CA C 58.978 0.050 1 946 212 212 LEU CB C 39.875 0.050 1 947 212 212 LEU N N 119.595 0.050 1 948 213 213 LYS H H 8.436 0.005 1 949 213 213 LYS C C 178.114 0.050 1 950 213 213 LYS CA C 60.562 0.050 1 951 213 213 LYS CB C 31.949 0.050 1 952 213 213 LYS N N 116.133 0.050 1 953 214 214 GLU H H 7.792 0.005 1 954 214 214 GLU C C 179.635 0.050 1 955 214 214 GLU CA C 59.127 0.050 1 956 214 214 GLU CB C 28.561 0.050 1 957 214 214 GLU N N 120.287 0.050 1 958 215 215 VAL H H 8.236 0.005 1 959 215 215 VAL C C 178.437 0.050 1 960 215 215 VAL CA C 65.775 0.050 1 961 215 215 VAL CB C 30.602 0.050 1 962 215 215 VAL N N 120.146 0.050 1 963 216 216 TRP H H 8.469 0.005 1 964 216 216 TRP C C 178.656 0.050 1 965 216 216 TRP CA C 60.593 0.050 1 966 216 216 TRP CB C 28.941 0.050 1 967 216 216 TRP N N 120.615 0.050 1 968 217 217 LEU H H 8.227 0.005 1 969 217 217 LEU C C 179.911 0.050 1 970 217 217 LEU CA C 57.088 0.050 1 971 217 217 LEU CB C 40.931 0.050 1 972 217 217 LEU N N 116.949 0.050 1 973 218 218 GLN H H 7.848 0.005 1 974 218 218 GLN C C 177.749 0.050 1 975 218 218 GLN CA C 57.250 0.050 1 976 218 218 GLN CB C 27.828 0.050 1 977 218 218 GLN N N 118.108 0.050 1 978 219 219 LYS H H 7.567 0.005 1 979 219 219 LYS C C 176.651 0.050 1 980 219 219 LYS CA C 55.355 0.050 1 981 219 219 LYS CB C 31.243 0.050 1 982 219 219 LYS N N 117.817 0.050 1 983 220 220 GLN H H 7.656 0.005 1 984 220 220 GLN C C 175.105 0.050 1 985 220 220 GLN CA C 55.136 0.050 1 986 220 220 GLN CB C 27.648 0.050 1 987 220 220 GLN N N 119.793 0.050 1 988 221 221 LYS H H 7.573 0.005 1 989 221 221 LYS C C 181.504 0.050 1 990 221 221 LYS CA C 57.274 0.050 1 991 221 221 LYS CB C 32.299 0.050 1 992 221 221 LYS N N 127.355 0.050 1 stop_ save_