data_19244 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shifts of isolated Domain 2 from E. coli HisJ ; _BMRB_accession_number 19244 _BMRB_flat_file_name bmr19244.str _Entry_type original _Submission_date 2013-05-15 _Accession_date 2013-05-15 _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 Chu Byron 'C. H.' . 2 Vogel Hans J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 94 "13C chemical shifts" 290 "15N chemical shifts" 94 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-12-06 update BMRB 'update entry citation' 2013-09-30 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 19242 'E. coli apo-HisJ' 19243 'Backbone chemical shifts of isolated Domain 1 from E. coli HisJ' 19245 'Backbone chemical shifts from E. coli HisJ complexed with Histidine' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Role of the Two Structural Domains from the Periplasmic Escherichia coli Histidine-binding Protein HisJ.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24036119 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chu Byron C.H. . 2 Dewolf Timothy . . 3 Vogel Hans J. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 288 _Journal_issue 44 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 31409 _Page_last 31422 _Year 2013 _Details . loop_ _Keyword 'E. coli' HisJ histidine 'Periplasmic binding protein' 'structural domain' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Domain 2 from E. coli HisJ' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Domain 2 from E. coli HisJ' $D2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_D2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common D2 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 102 _Mol_residue_sequence ; GGMDSRLVVAKNSDIQPTVE SLKGKRVGVLQGTTQETFGN EHWAPKGIEIVSYQGQDNIY SDLTAGRIDAAFQDEVAASE GFLKQPVGKDYKFGGPSVKD EK ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 GLY 3 MET 4 ASP 5 SER 6 ARG 7 LEU 8 VAL 9 VAL 10 ALA 11 LYS 12 ASN 13 SER 14 ASP 15 ILE 16 GLN 17 PRO 18 THR 19 VAL 20 GLU 21 SER 22 LEU 23 LYS 24 GLY 25 LYS 26 ARG 27 VAL 28 GLY 29 VAL 30 LEU 31 GLN 32 GLY 33 THR 34 THR 35 GLN 36 GLU 37 THR 38 PHE 39 GLY 40 ASN 41 GLU 42 HIS 43 TRP 44 ALA 45 PRO 46 LYS 47 GLY 48 ILE 49 GLU 50 ILE 51 VAL 52 SER 53 TYR 54 GLN 55 GLY 56 GLN 57 ASP 58 ASN 59 ILE 60 TYR 61 SER 62 ASP 63 LEU 64 THR 65 ALA 66 GLY 67 ARG 68 ILE 69 ASP 70 ALA 71 ALA 72 PHE 73 GLN 74 ASP 75 GLU 76 VAL 77 ALA 78 ALA 79 SER 80 GLU 81 GLY 82 PHE 83 LEU 84 LYS 85 GLN 86 PRO 87 VAL 88 GLY 89 LYS 90 ASP 91 TYR 92 LYS 93 PHE 94 GLY 95 GLY 96 PRO 97 SER 98 VAL 99 LYS 100 ASP 101 GLU 102 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 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 16204 HisJ 97.06 238 100.00 100.00 3.68e-63 BMRB 16205 HisJ 97.06 238 100.00 100.00 3.68e-63 BMRB 19242 apo-HisJ 97.06 241 100.00 100.00 4.83e-63 BMRB 19245 Holo-HisJ 97.06 241 100.00 100.00 4.83e-63 PDB 1HPB "The Bacterial Periplasmic Histidine-Binding Protein: Structure(Slash)function Analysis Of The Ligand-Binding Site And Compariso" 97.06 238 97.98 98.99 7.33e-62 PDB 1HSL "Refined 1.89 Angstroms Structure Of The Histidine-Binding Protein Complexed With Histidine And Its Relationship With Many Other" 97.06 238 97.98 98.99 7.33e-62 PDB 2M8C "The Solution Nmr Structure Of E. Coli Apo-hisj" 97.06 241 100.00 100.00 4.83e-63 DBJ BAA16155 "histidine/lysine/arginine/ornithine transporter subunit [Escherichia coli str. K12 substr. W3110]" 97.06 260 100.00 100.00 1.82e-63 DBJ BAB36616 "histidine transport system histidine-binding periplasmic protein [Escherichia coli O157:H7 str. Sakai]" 97.06 260 100.00 100.00 1.82e-63 DBJ BAG66608 "histidine/lysine/arginine/ornithine transporter subunit [Escherichia coli O111:H-]" 97.06 260 100.00 100.00 1.82e-63 DBJ BAG78142 "histidine ABC transporter substrate binding component [Escherichia coli SE11]" 97.06 260 100.00 100.00 1.82e-63 DBJ BAI26504 "histidine/lysine/arginine/ornithine transporter subunit HisJ [Escherichia coli O26:H11 str. 11368]" 97.06 260 100.00 100.00 1.82e-63 EMBL CAA24658 "unnamed protein product [Salmonella enterica subsp. enterica serovar Typhimurium]" 97.06 260 97.98 98.99 3.45e-62 EMBL CAA24659 "unnamed protein product [Salmonella enterica subsp. enterica serovar Typhimurium]" 97.06 260 97.98 98.99 3.45e-62 EMBL CAD07586 "histidine-binding periplasmic protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 97.06 260 96.97 98.99 5.15e-62 EMBL CAJ55342 "periplasmic histidine-binding protein [Salmonella enterica subsp. enterica serovar Typhimurium]" 52.94 164 98.15 98.15 9.23e-29 EMBL CAJ55343 "periplasmic histidine-binding protein [Salmonella enterica subsp. enterica serovar Typhimurium]" 52.94 164 98.15 98.15 9.95e-29 GB AAA75578 "J protein [Salmonella enterica subsp. enterica serovar Typhimurium]" 97.06 260 97.98 98.99 3.45e-62 GB AAA85769 "histidine-binding periplasmic protein HisJ [Escherichia coli]" 97.06 260 98.99 98.99 1.36e-62 GB AAC75369 "histidine ABC transporter periplasmic binding protein [Escherichia coli str. K-12 substr. MG1655]" 97.06 260 100.00 100.00 1.82e-63 GB AAG57438 "histidine-binding periplasmic protein of high-affinity histidine transport system [Escherichia coli O157:H7 str. EDL933]" 97.06 260 100.00 100.00 1.82e-63 GB AAL21255 "histidine transport protein [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 97.06 260 97.98 98.99 3.45e-62 PIR AH0800 "histidine-binding periplasmic protein [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 97.06 260 96.97 98.99 5.15e-62 PRF 0809313B "protein hisJ" 97.06 260 97.98 98.99 3.45e-62 REF NP_311220 "histidine transport system histidine-binding periplasmic protein [Escherichia coli O157:H7 str. Sakai]" 97.06 260 100.00 100.00 1.82e-63 REF NP_416812 "histidine ABC transporter periplasmic binding protein [Escherichia coli str. K-12 substr. MG1655]" 97.06 260 100.00 100.00 1.82e-63 REF NP_456896 "histidine ABC transporter substrate-binding protein HisJ [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 97.06 260 96.97 98.99 5.15e-62 REF NP_461296 "histidine ABC transporter substrate-binding protein HisJ [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 97.06 260 97.98 98.99 3.45e-62 REF NP_708191 "histidine ABC transporter substrate-binding protein HisJ [Shigella flexneri 2a str. 301]" 97.06 264 100.00 100.00 5.33e-64 SP P02910 "RecName: Full=Histidine-binding periplasmic protein; Short=HBP; Flags: Precursor" 97.06 260 97.98 98.99 3.45e-62 SP P0AEU0 "RecName: Full=Histidine-binding periplasmic protein; Short=HBP; Flags: Precursor" 97.06 260 100.00 100.00 1.82e-63 SP P0AEU1 "RecName: Full=Histidine-binding periplasmic protein; Short=HBP; Flags: Precursor" 97.06 260 100.00 100.00 1.82e-63 SP P0AEU2 "RecName: Full=Histidine-binding periplasmic protein; Short=HBP; Flags: Precursor" 97.06 260 100.00 100.00 1.82e-63 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $D2 'E. coli' 562 Bacteria . Escherichia coli K12 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 $D2 'recombinant technology' . Escherichia coli BL21 pET-15 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 $D2 1 mM '[U-13C; U-15N]' 'sodium phosphate' 50 mM 'natural abundance' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' DSS 0.5 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . 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' 0 . M pH 7 . 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 '1H chemical shifts were referenced to the methyl signal of DSS, and 15N and 13C chemical shifts were indirectly referenced to DSS (0 ppm for 1H).' 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_ _Experiment_label '3D HNCACB' '3D CBCA(CO)NH' '3D HNCO' '2D 1H-15N HSQC' 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 'Domain 2 from E. coli HisJ' _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 GLY C C 173.9000 . 1 2 2 2 GLY CA C 45.5200 . 1 3 3 3 MET H H 8.5300 . 1 4 3 3 MET C C 175.8000 . 1 5 3 3 MET CA C 55.1100 . 1 6 3 3 MET CB C 33.0100 . 1 7 3 3 MET N N 119.9000 . 1 8 4 4 ASP H H 8.3360 . 1 9 4 4 ASP C C 175.8000 . 1 10 4 4 ASP CA C 54.5100 . 1 11 4 4 ASP CB C 41.7000 . 1 12 4 4 ASP N N 122.3000 . 1 13 5 5 SER H H 8.2930 . 1 14 5 5 SER C C 172.1000 . 1 15 5 5 SER CA C 57.8500 . 1 16 5 5 SER CB C 65.6300 . 1 17 5 5 SER N N 117.1000 . 1 18 6 6 ARG H H 9.1340 . 1 19 6 6 ARG C C 174.4000 . 1 20 6 6 ARG CA C 56.0200 . 1 21 6 6 ARG CB C 35.9700 . 1 22 6 6 ARG N N 123.6000 . 1 23 7 7 LEU H H 9.2530 . 1 24 7 7 LEU C C 177.1000 . 1 25 7 7 LEU CA C 54.4100 . 1 26 7 7 LEU CB C 43.7100 . 1 27 7 7 LEU N N 123.4000 . 1 28 8 8 VAL H H 9.7290 . 1 29 8 8 VAL C C 175.7000 . 1 30 8 8 VAL CA C 62.4500 . 1 31 8 8 VAL CB C 33.3400 . 1 32 8 8 VAL N N 125.7000 . 1 33 9 9 VAL H H 9.2470 . 1 34 9 9 VAL C C 174.6000 . 1 35 9 9 VAL CA C 58.6100 . 1 36 9 9 VAL CB C 37.5900 . 1 37 9 9 VAL N N 116.6000 . 1 38 10 10 ALA H H 9.0930 . 1 39 10 10 ALA C C 179.2000 . 1 40 10 10 ALA CA C 53.0900 . 1 41 10 10 ALA CB C 18.9900 . 1 42 10 10 ALA N N 123.2000 . 1 43 11 11 LYS H H 7.9970 . 1 44 11 11 LYS C C 176.8000 . 1 45 11 11 LYS CA C 59.9000 . 1 46 11 11 LYS CB C 32.3900 . 1 47 11 11 LYS N N 119.3000 . 1 48 12 12 ASN C C 175.4000 . 1 49 12 12 ASN CA C 52.6400 . 1 50 12 12 ASN CB C 37.5200 . 1 51 13 13 SER H H 7.7680 . 1 52 13 13 SER C C 175.8000 . 1 53 13 13 SER CA C 58.6800 . 1 54 13 13 SER CB C 64.8600 . 1 55 13 13 SER N N 114.3000 . 1 56 14 14 ASP H H 8.6430 . 1 57 14 14 ASP C C 176.6000 . 1 58 14 14 ASP CA C 53.4400 . 1 59 14 14 ASP CB C 40.9700 . 1 60 14 14 ASP N N 127.6000 . 1 61 15 15 ILE H H 7.8850 . 1 62 15 15 ILE C C 173.9000 . 1 63 15 15 ILE CA C 63.9700 . 1 64 15 15 ILE CB C 38.4600 . 1 65 15 15 ILE N N 122.1000 . 1 66 16 16 GLN H H 8.2920 . 1 67 16 16 GLN C C 174.6000 . 1 68 16 16 GLN CA C 52.0500 . 1 69 16 16 GLN CB C 31.8200 . 1 70 16 16 GLN N N 124.4000 . 1 71 17 17 PRO C C 175.0000 . 1 72 17 17 PRO CA C 62.2400 . 1 73 18 18 THR H H 8.5550 . 1 74 18 18 THR C C 173.9000 . 1 75 18 18 THR CA C 58.1500 . 1 76 18 18 THR CB C 71.5500 . 1 77 18 18 THR N N 114.1000 . 1 78 19 19 VAL H H 8.8460 . 1 79 19 19 VAL C C 177.3000 . 1 80 19 19 VAL CA C 66.1200 . 1 81 19 19 VAL CB C 31.4800 . 1 82 19 19 VAL N N 121.6000 . 1 83 20 20 GLU H H 8.4980 . 1 84 20 20 GLU C C 178.4000 . 1 85 20 20 GLU CA C 59.8700 . 1 86 20 20 GLU CB C 29.0500 . 1 87 20 20 GLU N N 116.6000 . 1 88 21 21 SER H H 7.4550 . 1 89 21 21 SER C C 176.4000 . 1 90 21 21 SER CA C 59.8400 . 1 91 21 21 SER CB C 64.0100 . 1 92 21 21 SER N N 112.6000 . 1 93 22 22 LEU H H 7.6510 . 1 94 22 22 LEU C C 176.5000 . 1 95 22 22 LEU CA C 54.9400 . 1 96 22 22 LEU CB C 43.6700 . 1 97 22 22 LEU N N 115.9000 . 1 98 23 23 LYS H H 7.4430 . 1 99 23 23 LYS C C 178.2000 . 1 100 23 23 LYS CA C 59.3000 . 1 101 23 23 LYS CB C 31.8800 . 1 102 23 23 LYS N N 120.5000 . 1 103 24 24 GLY H H 8.5470 . 1 104 24 24 GLY C C 174.2000 . 1 105 24 24 GLY CA C 45.7500 . 1 106 24 24 GLY N N 113.6000 . 1 107 25 25 LYS H H 8.5560 . 1 108 25 25 LYS C C 174.8000 . 1 109 25 25 LYS CA C 54.1600 . 1 110 25 25 LYS CB C 32.9500 . 1 111 25 25 LYS N N 120.0000 . 1 112 26 26 ARG H H 9.5300 . 1 113 26 26 ARG C C 175.9000 . 1 114 26 26 ARG CA C 55.2800 . 1 115 26 26 ARG CB C 33.2300 . 1 116 26 26 ARG N N 119.1000 . 1 117 27 27 VAL H H 9.2870 . 1 118 27 27 VAL C C 175.2000 . 1 119 27 27 VAL CA C 60.6200 . 1 120 27 27 VAL CB C 34.7300 . 1 121 27 27 VAL N N 125.7000 . 1 122 28 28 GLY H H 9.3820 . 1 123 28 28 GLY C C 172.3000 . 1 124 28 28 GLY CA C 45.5100 . 1 125 28 28 GLY N N 113.5000 . 1 126 29 29 VAL H H 9.2530 . 1 127 29 29 VAL C C 173.9000 . 1 128 29 29 VAL CA C 58.7500 . 1 129 29 29 VAL CB C 37.0900 . 1 130 29 29 VAL N N 115.8000 . 1 131 30 30 LEU H H 9.2210 . 1 132 30 30 LEU C C 176.8000 . 1 133 30 30 LEU CA C 53.9200 . 1 134 30 30 LEU CB C 42.4500 . 1 135 30 30 LEU N N 123.8000 . 1 136 31 31 GLN H H 9.2550 . 1 137 31 31 GLN C C 176.9000 . 1 138 31 31 GLN CA C 57.1700 . 1 139 31 31 GLN CB C 28.8100 . 1 140 31 31 GLN N N 127.3000 . 1 141 32 32 GLY H H 9.4580 . 1 142 32 32 GLY C C 175.1000 . 1 143 32 32 GLY CA C 45.7700 . 1 144 32 32 GLY N N 113.1000 . 1 145 33 33 THR H H 7.2630 . 1 146 33 33 THR C C 176.8000 . 1 147 33 33 THR CA C 60.5000 . 1 148 33 33 THR CB C 74.2500 . 1 149 33 33 THR N N 107.5000 . 1 150 34 34 THR C C 177.3000 . 1 151 34 34 THR CA C 64.7400 . 1 152 34 34 THR CB C 68.4200 . 1 153 35 35 GLN H H 7.2690 . 1 154 35 35 GLN C C 177.9000 . 1 155 35 35 GLN CA C 61.4500 . 1 156 35 35 GLN CB C 26.5400 . 1 157 35 35 GLN N N 119.8000 . 1 158 36 36 GLU H H 7.6110 . 1 159 36 36 GLU C C 177.6000 . 1 160 36 36 GLU CA C 60.2100 . 1 161 36 36 GLU CB C 29.6400 . 1 162 36 36 GLU N N 121.4000 . 1 163 37 37 THR H H 8.0110 . 1 164 37 37 THR C C 176.1000 . 1 165 37 37 THR CA C 66.6100 . 1 166 37 37 THR CB C 68.5000 . 1 167 37 37 THR N N 116.0000 . 1 168 38 38 PHE H H 8.6370 . 1 169 38 38 PHE C C 178.6000 . 1 170 38 38 PHE CA C 61.5100 . 1 171 38 38 PHE CB C 39.4400 . 1 172 38 38 PHE N N 122.1000 . 1 173 39 39 GLY H H 8.9570 . 1 174 39 39 GLY C C 176.3000 . 1 175 39 39 GLY CA C 47.0800 . 1 176 39 39 GLY N N 106.4000 . 1 177 40 40 ASN H H 8.8690 . 1 178 40 40 ASN C C 176.3000 . 1 179 40 40 ASN CA C 55.8400 . 1 180 40 40 ASN CB C 38.2000 . 1 181 40 40 ASN N N 122.3000 . 1 182 41 41 GLU H H 7.9620 . 1 183 41 41 GLU C C 177.8000 . 1 184 41 41 GLU CA C 58.4700 . 1 185 41 41 GLU CB C 30.3200 . 1 186 41 41 GLU N N 118.6000 . 1 187 42 42 HIS H H 7.9810 . 1 188 42 42 HIS C C 175.9000 . 1 189 42 42 HIS CA C 57.3400 . 1 190 42 42 HIS CB C 31.1600 . 1 191 42 42 HIS N N 112.1000 . 1 192 43 43 TRP H H 7.7680 . 1 193 43 43 TRP C C 176.9000 . 1 194 43 43 TRP CA C 55.9300 . 1 195 43 43 TRP CB C 30.5900 . 1 196 43 43 TRP N N 119.0000 . 1 197 44 44 ALA H H 8.6920 . 1 198 44 44 ALA C C 177.7000 . 1 199 44 44 ALA CA C 55.8400 . 1 200 44 44 ALA CB C 16.7400 . 1 201 44 44 ALA N N 125.1000 . 1 202 45 45 PRO C C 177.2000 . 1 203 45 45 PRO CA C 65.1400 . 1 204 45 45 PRO CB C 31.5500 . 1 205 46 46 LYS H H 7.7200 . 1 206 46 46 LYS C C 176.4000 . 1 207 46 46 LYS CA C 54.0600 . 1 208 46 46 LYS CB C 32.5000 . 1 209 46 46 LYS N N 115.4000 . 1 210 47 47 GLY H H 7.9560 . 1 211 47 47 GLY C C 174.3000 . 1 212 47 47 GLY CA C 46.2100 . 1 213 47 47 GLY N N 105.7000 . 1 214 48 48 ILE H H 6.9780 . 1 215 48 48 ILE C C 174.4000 . 1 216 48 48 ILE CA C 60.8300 . 1 217 48 48 ILE CB C 38.8800 . 1 218 48 48 ILE N N 123.8000 . 1 219 49 49 GLU H H 8.2930 . 1 220 49 49 GLU C C 174.0000 . 1 221 49 49 GLU CA C 56.5800 . 1 222 49 49 GLU CB C 30.4300 . 1 223 49 49 GLU N N 128.1000 . 1 224 50 50 ILE H H 8.6920 . 1 225 50 50 ILE C C 176.1000 . 1 226 50 50 ILE CA C 57.5500 . 1 227 50 50 ILE CB C 35.4600 . 1 228 50 50 ILE N N 129.0000 . 1 229 51 51 VAL H H 9.4380 . 1 230 51 51 VAL C C 174.4000 . 1 231 51 51 VAL CA C 61.5900 . 1 232 51 51 VAL CB C 33.3900 . 1 233 51 51 VAL N N 132.3000 . 1 234 52 52 SER H H 8.5850 . 1 235 52 52 SER C C 174.9000 . 1 236 52 52 SER CA C 58.0600 . 1 237 52 52 SER CB C 63.9600 . 1 238 52 52 SER N N 122.4000 . 1 239 53 53 TYR H H 9.0620 . 1 240 53 53 TYR C C 175.8000 . 1 241 53 53 TYR CA C 57.6300 . 1 242 53 53 TYR CB C 42.8500 . 1 243 53 53 TYR N N 123.1000 . 1 244 54 54 GLN H H 9.0160 . 1 245 54 54 GLN C C 176.0000 . 1 246 54 54 GLN CA C 57.0800 . 1 247 54 54 GLN CB C 29.3800 . 1 248 54 54 GLN N N 119.1000 . 1 249 55 55 GLY H H 7.6370 . 1 250 55 55 GLY C C 173.5000 . 1 251 55 55 GLY CA C 44.8000 . 1 252 55 55 GLY N N 106.3000 . 1 253 56 56 GLN H H 8.9420 . 1 254 56 56 GLN C C 177.1000 . 1 255 56 56 GLN CA C 58.5100 . 1 256 56 56 GLN CB C 29.1200 . 1 257 56 56 GLN N N 123.1000 . 1 258 57 57 ASP H H 8.7810 . 1 259 57 57 ASP C C 178.9000 . 1 260 57 57 ASP CA C 57.2000 . 1 261 57 57 ASP CB C 39.5600 . 1 262 57 57 ASP N N 117.6000 . 1 263 58 58 ASN H H 7.6200 . 1 264 58 58 ASN C C 176.6000 . 1 265 58 58 ASN CA C 55.6000 . 1 266 58 58 ASN CB C 39.3000 . 1 267 58 58 ASN N N 116.9000 . 1 268 59 59 ILE H H 6.8620 . 1 269 59 59 ILE C C 177.2000 . 1 270 59 59 ILE CA C 64.8900 . 1 271 59 59 ILE CB C 37.0200 . 1 272 59 59 ILE N N 119.3000 . 1 273 60 60 TYR H H 6.9280 . 1 274 60 60 TYR C C 178.7000 . 1 275 60 60 TYR CA C 60.6800 . 1 276 60 60 TYR CB C 36.8200 . 1 277 60 60 TYR N N 117.1000 . 1 278 61 61 SER H H 8.2070 . 1 279 61 61 SER C C 176.8000 . 1 280 61 61 SER CA C 61.6300 . 1 281 61 61 SER CB C 62.3800 . 1 282 61 61 SER N N 116.7000 . 1 283 62 62 ASP H H 7.5440 . 1 284 62 62 ASP C C 178.9000 . 1 285 62 62 ASP CA C 57.1400 . 1 286 62 62 ASP CB C 38.9500 . 1 287 62 62 ASP N N 121.5000 . 1 288 63 63 LEU H H 8.4410 . 1 289 63 63 LEU C C 180.2000 . 1 290 63 63 LEU CA C 58.6700 . 1 291 63 63 LEU CB C 42.8800 . 1 292 63 63 LEU N N 123.5000 . 1 293 64 64 THR H H 8.4670 . 1 294 64 64 THR C C 176.7000 . 1 295 64 64 THR CA C 64.4500 . 1 296 64 64 THR CB C 69.2300 . 1 297 64 64 THR N N 111.1000 . 1 298 65 65 ALA H H 7.4900 . 1 299 65 65 ALA C C 178.1000 . 1 300 65 65 ALA CA C 52.2000 . 1 301 65 65 ALA CB C 19.8000 . 1 302 65 65 ALA N N 121.4000 . 1 303 66 66 GLY H H 7.9840 . 1 304 66 66 GLY C C 175.2000 . 1 305 66 66 GLY CA C 45.9000 . 1 306 66 66 GLY N N 107.3000 . 1 307 67 67 ARG H H 8.5190 . 1 308 67 67 ARG C C 176.7000 . 1 309 67 67 ARG CA C 57.7400 . 1 310 67 67 ARG CB C 31.5000 . 1 311 67 67 ARG N N 118.6000 . 1 312 68 68 ILE H H 7.1880 . 1 313 68 68 ILE C C 173.7000 . 1 314 68 68 ILE CA C 60.3800 . 1 315 68 68 ILE CB C 41.0500 . 1 316 68 68 ILE N N 108.4000 . 1 317 69 69 ASP H H 8.8520 . 1 318 69 69 ASP C C 174.6000 . 1 319 69 69 ASP CA C 56.3000 . 1 320 69 69 ASP CB C 44.3400 . 1 321 69 69 ASP N N 118.6000 . 1 322 70 70 ALA H H 7.7410 . 1 323 70 70 ALA C C 175.0000 . 1 324 70 70 ALA CA C 50.6800 . 1 325 70 70 ALA CB C 23.8300 . 1 326 70 70 ALA N N 115.9000 . 1 327 71 71 ALA H H 8.9740 . 1 328 71 71 ALA C C 175.5000 . 1 329 71 71 ALA CA C 50.1000 . 1 330 71 71 ALA CB C 21.9800 . 1 331 71 71 ALA N N 123.0000 . 1 332 72 72 PHE H H 9.1950 . 1 333 72 72 PHE C C 173.5000 . 1 334 72 72 PHE CA C 54.8200 . 1 335 72 72 PHE CB C 39.8900 . 1 336 72 72 PHE N N 125.6000 . 1 337 73 73 GLN H H 8.2640 . 1 338 73 73 GLN C C 173.9000 . 1 339 73 73 GLN CA C 54.3500 . 1 340 73 73 GLN CB C 35.6300 . 1 341 73 73 GLN N N 124.4000 . 1 342 74 74 ASP H H 8.1950 . 1 343 74 74 ASP C C 176.3000 . 1 344 74 74 ASP CA C 55.5300 . 1 345 74 74 ASP CB C 42.5800 . 1 346 74 74 ASP N N 121.3000 . 1 347 75 75 GLU H H 8.5820 . 1 348 75 75 GLU C C 177.9000 . 1 349 75 75 GLU CA C 60.5100 . 1 350 75 75 GLU CB C 30.7300 . 1 351 75 75 GLU N N 127.4000 . 1 352 76 76 VAL H H 8.1680 . 1 353 76 76 VAL C C 178.2000 . 1 354 76 76 VAL CA C 66.4900 . 1 355 76 76 VAL CB C 31.3900 . 1 356 76 76 VAL N N 119.9000 . 1 357 77 77 ALA H H 8.3230 . 1 358 77 77 ALA C C 182.1000 . 1 359 77 77 ALA CA C 55.0600 . 1 360 77 77 ALA CB C 18.5700 . 1 361 77 77 ALA N N 122.4000 . 1 362 78 78 ALA H H 8.2050 . 1 363 78 78 ALA C C 179.5000 . 1 364 78 78 ALA CA C 54.9300 . 1 365 78 78 ALA CB C 19.5300 . 1 366 78 78 ALA N N 119.8000 . 1 367 79 79 SER H H 8.5210 . 1 368 79 79 SER C C 175.6000 . 1 369 79 79 SER CA C 61.8800 . 1 370 79 79 SER CB C 63.3800 . 1 371 79 79 SER N N 113.4000 . 1 372 80 80 GLU H H 8.4180 . 1 373 80 80 GLU C C 178.0000 . 1 374 80 80 GLU CA C 57.6000 . 1 375 80 80 GLU CB C 29.8500 . 1 376 80 80 GLU N N 115.4000 . 1 377 81 81 GLY H H 7.8320 . 1 378 81 81 GLY C C 173.7000 . 1 379 81 81 GLY CA C 45.4800 . 1 380 81 81 GLY N N 105.1000 . 1 381 82 82 PHE H H 7.6870 . 1 382 82 82 PHE C C 175.4000 . 1 383 82 82 PHE CA C 61.4500 . 1 384 82 82 PHE CB C 41.1800 . 1 385 82 82 PHE N N 122.6000 . 1 386 83 83 LEU H H 8.3520 . 1 387 83 83 LEU C C 178.6000 . 1 388 83 83 LEU CA C 57.8200 . 1 389 83 83 LEU CB C 41.0600 . 1 390 83 83 LEU N N 115.2000 . 1 391 84 84 LYS H H 7.9260 . 1 392 84 84 LYS C C 176.8000 . 1 393 84 84 LYS CA C 56.4300 . 1 394 84 84 LYS CB C 32.9200 . 1 395 84 84 LYS N N 115.2000 . 1 396 85 85 GLN H H 7.2390 . 1 397 85 85 GLN C C 176.1000 . 1 398 85 85 GLN CA C 53.2000 . 1 399 85 85 GLN CB C 27.8700 . 1 400 85 85 GLN N N 119.0000 . 1 401 86 86 PRO C C 179.3000 . 1 402 86 86 PRO CA C 66.5600 . 1 403 86 86 PRO CB C 31.4800 . 1 404 87 87 VAL H H 7.5620 . 1 405 87 87 VAL C C 175.9000 . 1 406 87 87 VAL CA C 63.4600 . 1 407 87 87 VAL CB C 31.5200 . 1 408 87 87 VAL N N 112.1000 . 1 409 88 88 GLY H H 7.2450 . 1 410 88 88 GLY C C 175.0000 . 1 411 88 88 GLY CA C 44.7400 . 1 412 88 88 GLY N N 109.1000 . 1 413 89 89 LYS H H 7.1010 . 1 414 89 89 LYS C C 177.1000 . 1 415 89 89 LYS CA C 58.7600 . 1 416 89 89 LYS CB C 32.2700 . 1 417 89 89 LYS N N 120.2000 . 1 418 90 90 ASP H H 8.0040 . 1 419 90 90 ASP C C 174.0000 . 1 420 90 90 ASP CA C 54.3400 . 1 421 90 90 ASP CB C 40.4300 . 1 422 90 90 ASP N N 116.8000 . 1 423 91 91 TYR H H 7.8230 . 1 424 91 91 TYR C C 172.4000 . 1 425 91 91 TYR CA C 58.3000 . 1 426 91 91 TYR CB C 42.6300 . 1 427 91 91 TYR N N 120.0000 . 1 428 92 92 LYS H H 9.5690 . 1 429 92 92 LYS C C 174.8000 . 1 430 92 92 LYS CA C 54.6500 . 1 431 92 92 LYS CB C 36.4700 . 1 432 92 92 LYS N N 116.5000 . 1 433 93 93 PHE H H 8.5030 . 1 434 93 93 PHE C C 177.7000 . 1 435 93 93 PHE CA C 56.7700 . 1 436 93 93 PHE CB C 39.1800 . 1 437 93 93 PHE N N 116.9000 . 1 438 94 94 GLY H H 9.3510 . 1 439 94 94 GLY C C 173.4000 . 1 440 94 94 GLY CA C 46.9000 . 1 441 94 94 GLY N N 113.4000 . 1 442 95 95 GLY H H 8.0010 . 1 443 95 95 GLY C C 171.2000 . 1 444 95 95 GLY CA C 45.0100 . 1 445 95 95 GLY N N 110.6000 . 1 446 96 96 PRO C C 175.7000 . 1 447 96 96 PRO CA C 62.2900 . 1 448 96 96 PRO CB C 33.4900 . 1 449 97 97 SER H H 8.2750 . 1 450 97 97 SER C C 174.2000 . 1 451 97 97 SER CA C 59.0100 . 1 452 97 97 SER CB C 63.6800 . 1 453 97 97 SER N N 112.8000 . 1 454 98 98 VAL H H 8.9030 . 1 455 98 98 VAL C C 175.4000 . 1 456 98 98 VAL CA C 62.0700 . 1 457 98 98 VAL CB C 33.5600 . 1 458 98 98 VAL N N 123.2000 . 1 459 99 99 LYS H H 8.4510 . 1 460 99 99 LYS C C 175.6000 . 1 461 99 99 LYS CA C 55.4900 . 1 462 99 99 LYS CB C 34.0100 . 1 463 99 99 LYS N N 126.3000 . 1 464 100 100 ASP H H 8.5770 . 1 465 100 100 ASP C C 175.8000 . 1 466 100 100 ASP CA C 54.0500 . 1 467 100 100 ASP CB C 41.3300 . 1 468 100 100 ASP N N 122.3000 . 1 469 101 101 GLU H H 8.3340 . 1 470 101 101 GLU C C 175.4000 . 1 471 101 101 GLU CA C 56.2300 . 1 472 101 101 GLU CB C 30.9500 . 1 473 101 101 GLU N N 122.4000 . 1 474 102 102 LYS H H 8.0330 . 1 475 102 102 LYS C C 181.4000 . 1 476 102 102 LYS CA C 57.7800 . 1 477 102 102 LYS CB C 33.6200 . 1 478 102 102 LYS N N 127.6000 . 1 stop_ save_