data_5604 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the N-terminal domain of ZntA in the apo- and Zn(II) forms ; _BMRB_accession_number 5604 _BMRB_flat_file_name bmr5604.str _Entry_type original _Submission_date 2002-11-28 _Accession_date 2002-12-02 _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 Banci L. . . 2 Bertini I. . . 3 Ciofi-Baffoni S. . . 4 Finney L. A. . 5 Outten C. E. . 6 O'Halloran T. V. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 328 "15N chemical shifts" 72 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-03-24 original author . stop_ _Original_release_date 2003-03-24 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; A new-zinc protein coordination site in intracellular metal trafficking: solution structure of the apo and Zn(II) forms of ZntA (46-118) ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22305097 _PubMed_ID 12417201 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Banci L. . . 2 Bertini I. . . 3 Ciofi-Baffoni S. . . 4 Finney L. A. . 5 Outten C. E. . 6 O'Halloran T. V. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 323 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 883 _Page_last 897 _Year 2002 _Details . loop_ _Keyword 'open-faced beta-sandwich fold' beta-alpha-beta-beta-alpha-beta stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; A New Zinc-protein Coordination Site in Intracellular Metal Trafficking: Solution Structure of the Apo and Zn(II) forms of ZntA(46-118) Lucia Banci, Ivano Bertini, Simone Ciofi-Baffoni, Lydia A. Finney, Caryn E. Outten, Thomas V. O'Halloran Journal of Molecular Biology, Vol. 323, No. 5, Nov 2002, pp. 883-897 (doi: 10.1016/S0022-2836(02)01007-0) ; _Citation_title 'A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118).' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12417201 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Banci Lucia . . 2 Bertini Ivano . . 3 Ciofi-Baffoni Simone . . 4 Finney 'Lydia A' A. . 5 Outten 'Caryn E' E. . 6 O'Halloran 'Thomas V' V. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 323 _Journal_issue 5 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 883 _Page_last 897 _Year 2002 _Details ; Zinc, a metal ion that functions in a wide variety of catalytic and structural sites in metalloproteins, is shown here to adopt a novel coordination environment in the Escherichia coli transport protein ZntA. The ZntA protein is a P-type ATPase that pumps zinc out of the cytoplasm and into the periplasm. It is physiologically selective for Zn(II) and functions with metalloregulatory proteins in the cell to keep the zinc quota within strict limits. Yet, the N-terminal cytoplasmic domain contains a region that is highly homologous to the yeast Cu(I) metallochaperone Atx1. To investigate how the structure of this region may influence its function, this fragment, containing residues 46-118, has been cloned out of the gene and overexpressed. We report here the solution structure of this fragment as determined by NMR. Both the apo and Zn(II)-ZntA(46-118) structures have been determined. It contains a previously unknown protein coordination site for zinc that includes two cysteine residues, Cys59 and Cys62, and a carboxylate residue, Asp58. The solvent accessibility of this site is also remarkably high, a feature that increasingly appears to be a characteristic of domains of heavy metal ion transport proteins. The participation of Asp58 in this ZntA metal ion binding site may play an important role in modulating the relative affinities and metal exchange rates for Zn(II)/Pb(II)/Cd(II) as compared with other P-type ATPases, which are selective for Cu(I) or Ag(I). ; save_ ################################## # Molecular system description # ################################## save_system_ZntA _Saveframe_category molecular_system _Mol_system_name 'ZNTA (E.C.3.6.3.3/E.C.3.6.3.5)' _Abbreviation_common ZntA _Enzyme_commission_number E.C.3.6.3.3 loop_ _Mol_system_component_name _Mol_label 'P-type zinc atpase' $ZntA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'zinc, cadmium transport ATPase' stop_ _Database_query_date . _Details 'Additional enzyme commission number E.C.3.6.3.5' save_ ######################## # Monomeric polymers # ######################## save_ZntA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'p-type ATPase' _Abbreviation_common ZntA _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 73 _Mol_residue_sequence ; SGTRYSWKVSGMDCAACARK VENAVRQLAGVNQVQVLFAT EKLVVDADNDIRAQVESALQ KAGYSLRDEQAAE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 46 SER 2 47 GLY 3 48 THR 4 49 ARG 5 50 TYR 6 51 SER 7 52 TRP 8 53 LYS 9 54 VAL 10 55 SER 11 56 GLY 12 57 MET 13 58 ASP 14 59 CYS 15 60 ALA 16 61 ALA 17 62 CYS 18 63 ALA 19 64 ARG 20 65 LYS 21 66 VAL 22 67 GLU 23 68 ASN 24 69 ALA 25 70 VAL 26 71 ARG 27 72 GLN 28 73 LEU 29 74 ALA 30 75 GLY 31 76 VAL 32 77 ASN 33 78 GLN 34 79 VAL 35 80 GLN 36 81 VAL 37 82 LEU 38 83 PHE 39 84 ALA 40 85 THR 41 86 GLU 42 87 LYS 43 88 LEU 44 89 VAL 45 90 VAL 46 91 ASP 47 92 ALA 48 93 ASP 49 94 ASN 50 95 ASP 51 96 ILE 52 97 ARG 53 98 ALA 54 99 GLN 55 100 VAL 56 101 GLU 57 102 SER 58 103 ALA 59 104 LEU 60 105 GLN 61 106 LYS 62 107 ALA 63 108 GLY 64 109 TYR 65 110 SER 66 111 LEU 67 112 ARG 68 113 ASP 69 114 GLU 70 115 GLN 71 116 ALA 72 117 ALA 73 118 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 PDB 1MWY "Solution Structure Of The N-Terminal Domain Of Znta In The Apo-Form" 98.63 73 100.00 100.00 5.82e-43 PDB 1MWZ "Solution Structure Of The N-Terminal Domain Of Znta In The Zn(Ii)-Form" 98.63 73 100.00 100.00 5.82e-43 PDB 4UMV "Crystal Structure Of A Zinc-transporting Pib-type Atpase In The E2p State" 100.00 732 97.26 100.00 1.03e-39 PDB 4UMW "Crystal Structure Of A Zinc-transporting Pib-type Atpase In E2.pi State" 100.00 732 97.26 100.00 1.03e-39 DBJ BAB37741 "zinc-transporting ATPase [Escherichia coli O157:H7 str. Sakai]" 100.00 732 97.26 100.00 9.86e-40 DBJ BAE77824 "zinc, cobalt and lead efflux system [Escherichia coli str. K-12 substr. W3110]" 100.00 732 100.00 100.00 7.15e-41 DBJ BAG79261 "zinc-transporting ATPase [Escherichia coli SE11]" 100.00 732 97.26 100.00 1.03e-39 DBJ BAI32897 "zinc, cobalt and lead efflux system protein ZntA [Escherichia coli O103:H2 str. 12009]" 100.00 732 97.26 100.00 1.03e-39 DBJ BAJ45202 "zinc/cadmium/mercury/lead-transporting ATPase [Escherichia coli DH1]" 100.00 732 100.00 100.00 7.15e-41 EMBL CAQ90919 "zinc, cobalt and lead efflux system [Escherichia fergusonii ATCC 35469]" 98.63 733 98.61 100.00 1.19e-39 EMBL CAR00414 "zinc, cobalt and lead efflux system [Escherichia coli IAI1]" 100.00 732 97.26 100.00 1.03e-39 EMBL CAR15077 "zinc, cobalt and lead efflux system [Escherichia coli UMN026]" 100.00 732 97.26 100.00 9.09e-40 EMBL CAV00282 "zinc, cobalt and lead efflux system [Escherichia coli 55989]" 100.00 732 97.26 100.00 1.03e-39 EMBL CBG36554 "lead, cadmium, zinc and mercury-transporting ATPase [Escherichia coli 042]" 100.00 732 97.26 100.00 9.09e-40 GB AAB18444 "unnamed protein product [Escherichia coli str. K-12 substr. MG1655]" 100.00 732 100.00 100.00 7.15e-41 GB AAC76494 "zinc, cobalt and lead efflux system [Escherichia coli str. K-12 substr. MG1655]" 100.00 732 100.00 100.00 7.15e-41 GB AAG58578 "zinc-transporting ATPase [Escherichia coli O157:H7 str. EDL933]" 100.00 732 97.26 100.00 9.86e-40 GB AAN44946 "zinc-transporting ATPase [Shigella flexneri 2a str. 301]" 100.00 732 97.26 100.00 1.03e-39 GB AAP19236 "zinc-transporting ATPase [Shigella flexneri 2a str. 2457T]" 100.00 732 97.26 100.00 1.03e-39 REF NP_290017 "zinc/cadmium/mercury/lead-transporting ATPase [Escherichia coli O157:H7 str. EDL933]" 100.00 732 97.26 100.00 9.86e-40 REF NP_312345 "zinc/cadmium/mercury/lead-transporting ATPase [Escherichia coli O157:H7 str. Sakai]" 100.00 732 97.26 100.00 9.86e-40 REF NP_417926 "zinc, cobalt and lead efflux system [Escherichia coli str. K-12 substr. MG1655]" 100.00 732 100.00 100.00 7.15e-41 REF NP_709239 "zinc/cadmium/mercury/lead-transporting ATPase [Shigella flexneri 2a str. 301]" 100.00 732 97.26 100.00 1.03e-39 REF NP_839425 "zinc/cadmium/mercury/lead-transporting ATPase [Shigella flexneri 2a str. 2457T]" 100.00 732 97.26 100.00 1.03e-39 SP P37617 "RecName: Full=Lead, cadmium, zinc and mercury-transporting ATPase [Escherichia coli K-12]" 100.00 732 100.00 100.00 7.15e-41 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $ZntA 'E. coli' 562 Eubacteria . Escherichia coli 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 $ZntA 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) PET11C 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 $ZntA 1.5 mM [U-15N] 'phosphate buffer' 100 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ZntA 2 mM . 'phosphate buffer' 100 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 1.3 loop_ _Task collection processing stop_ _Details 'Bruker software' save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'structure solution' stop_ _Details 'Guentert P., Wuthrich K. et al.' save_ save_CORMA _Saveframe_category software _Name CORMA _Version . loop_ _Task 'iterative matrix relaxation' stop_ _Details 'Borgias B., Thomas P.D., James T.L.' save_ save_AMBER _Saveframe_category software _Name AMBER _Version 5.0 loop_ _Task refinement stop_ _Details 'Case D.A., Pearlman D.A. et al.' save_ save_xeasy _Saveframe_category software _Name xeasy _Version 3.2 loop_ _Task 'data analysis' stop_ _Details 'Bartels C., Billiter M., Guentert P., Wuthrich K.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_HNHA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_2D_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_2D_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7 0.1 n/a temperature 298 0.1 K 'ionic strength' 100 . mM pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'P-type zinc atpase' _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 GLY HA2 H 3.93 0.02 1 2 . 3 THR H H 8.44 0.02 1 3 . 3 THR N N 118.2 0.1 1 4 . 3 THR HA H 4.14 0.02 1 5 . 3 THR HB H 3.71 0.02 1 6 . 3 THR HG2 H 0.57 0.02 1 7 . 4 ARG H H 7.82 0.02 1 8 . 4 ARG N N 124.7 0.1 1 9 . 4 ARG HA H 4.94 0.02 1 10 . 4 ARG HB2 H 1.42 0.02 1 11 . 4 ARG HG2 H 1.17 0.02 1 12 . 4 ARG HG3 H 1.22 0.02 1 13 . 4 ARG HD2 H 2.83 0.02 1 14 . 4 ARG HD3 H 2.89 0.02 1 15 . 5 TYR H H 9.19 0.02 1 16 . 5 TYR N N 127.6 0.1 1 17 . 5 TYR HA H 4.4 0.02 1 18 . 5 TYR HB2 H 1.99 0.02 1 19 . 5 TYR HE1 H 6.64 0.02 3 20 . 5 TYR HD1 H 6.82 0.02 3 21 . 6 SER H H 7.94 0.02 1 22 . 6 SER N N 113.9 0.1 1 23 . 6 SER HA H 5.66 0.02 1 24 . 6 SER HB2 H 3.54 0.02 1 25 . 7 TRP H H 9.12 0.02 1 26 . 7 TRP N N 120.9 0.1 1 27 . 7 TRP HA H 5.1 0.02 1 28 . 7 TRP HB2 H 3.24 0.02 1 29 . 7 TRP HE1 H 10.95 0.02 1 30 . 7 TRP HD1 H 6.96 0.02 1 31 . 7 TRP HZ2 H 7.07 0.02 1 32 . 7 TRP HH2 H 6.42 0.02 1 33 . 7 TRP HZ3 H 6.59 0.02 1 34 . 7 TRP HE3 H 7.29 0.02 1 35 . 7 TRP NE1 N 130.8 0.1 1 36 . 8 LYS H H 8.77 0.02 1 37 . 8 LYS N N 120.1 0.1 1 38 . 8 LYS HA H 5.17 0.02 1 39 . 8 LYS HB2 H 1.66 0.02 1 40 . 8 LYS HD2 H 1.46 0.02 2 41 . 8 LYS HG2 H 1.31 0.02 2 42 . 8 LYS HE2 H 2.91 0.02 2 43 . 9 VAL H H 8.81 0.02 1 44 . 9 VAL N N 124.9 0.1 1 45 . 9 VAL HA H 4.54 0.02 1 46 . 9 VAL HB H 1.66 0.02 1 47 . 9 VAL HG1 H 0.66 0.02 1 48 . 9 VAL HG2 H 0.65 0.02 1 49 . 10 SER H H 8.91 0.02 1 50 . 10 SER N N 122.8 0.1 1 51 . 10 SER HA H 4.53 0.02 1 52 . 10 SER HB2 H 3.66 0.02 1 53 . 11 GLY H H 8.71 0.02 1 54 . 11 GLY N N 111.2 0.1 1 55 . 11 GLY HA2 H 4.49 0.02 1 56 . 12 MET H H 8.78 0.02 1 57 . 12 MET N N 120.6 0.1 1 58 . 12 MET HA H 4.63 0.02 1 59 . 12 MET HB2 H 1.88 0.02 1 60 . 12 MET HG2 H 2.17 0.02 1 61 . 12 MET HG3 H 2.26 0.02 1 62 . 13 ASP H H 9.1 0.02 1 63 . 13 ASP N N 124.3 0.1 1 64 . 13 ASP HA H 4.83 0.02 1 65 . 13 ASP HB2 H 2.81 0.02 1 66 . 14 CYS H H 7.89 0.02 1 67 . 14 CYS N N 112.6 0.1 1 68 . 14 CYS HA H 4.5 0.02 1 69 . 14 CYS HB2 H 3.22 0.02 1 70 . 15 ALA H H 8.41 0.02 1 71 . 15 ALA N N 123.8 0.1 1 72 . 15 ALA HA H 3.09 0.02 1 73 . 15 ALA HB H 1.09 0.02 1 74 . 16 ALA H H 8.33 0.02 1 75 . 16 ALA N N 120.4 0.1 1 76 . 16 ALA HA H 3.99 0.02 1 77 . 16 ALA HB H 1.39 0.02 1 78 . 17 CYS H H 7.71 0.02 1 79 . 17 CYS N N 118.7 0.1 1 80 . 17 CYS HA H 3.98 0.02 1 81 . 17 CYS HB2 H 3.14 0.02 1 82 . 18 ALA H H 7.4 0.02 1 83 . 18 ALA N N 120.4 0.1 1 84 . 18 ALA HA H 3.91 0.02 1 85 . 18 ALA HB H 1.41 0.02 1 86 . 19 ARG H H 7.47 0.02 1 87 . 19 ARG N N 115.8 0.1 1 88 . 19 ARG HA H 4.06 0.02 1 89 . 19 ARG HB2 H 1.8 0.02 1 90 . 19 ARG HG2 H 1.63 0.02 2 91 . 19 ARG HD2 H 3.15 0.02 2 92 . 20 LYS H H 7.28 0.02 1 93 . 20 LYS N N 119.3 0.1 1 94 . 20 LYS HA H 3.94 0.02 1 95 . 20 LYS HB2 H 1.89 0.02 1 96 . 20 LYS HD2 H 1.57 0.02 2 97 . 20 LYS HG2 H 1.38 0.02 2 98 . 20 LYS HE2 H 2.91 0.02 2 99 . 21 VAL H H 7.89 0.02 1 100 . 21 VAL N N 120.9 0.1 1 101 . 21 VAL HA H 3.13 0.02 1 102 . 21 VAL HB H 1.93 0.02 1 103 . 21 VAL HG1 H 0.55 0.02 1 104 . 21 VAL HG2 H 0.20 0.02 1 105 . 22 GLU H H 8.11 0.02 1 106 . 22 GLU N N 118.1 0.1 1 107 . 22 GLU HA H 3.42 0.02 1 108 . 22 GLU HB2 H 1.91 0.02 1 109 . 22 GLU HG2 H 2.19 0.02 1 110 . 22 GLU HG3 H 2.09 0.02 1 111 . 23 ASN H H 8.2 0.02 1 112 . 23 ASN N N 114.8 0.1 1 113 . 23 ASN HA H 4.2 0.02 1 114 . 23 ASN HB2 H 2.67 0.02 1 115 . 23 ASN HD21 H 6.78 0.02 1 116 . 23 ASN HD22 H 7.55 0.02 1 117 . 24 ALA H H 7.58 0.02 1 118 . 24 ALA N N 120.4 0.1 1 119 . 24 ALA HA H 4.02 0.02 1 120 . 24 ALA HB H 1.3 0.02 1 121 . 25 VAL H H 7.65 0.02 1 122 . 25 VAL N N 115.5 0.1 1 123 . 25 VAL HA H 3.56 0.02 1 124 . 25 VAL HB H 1.95 0.02 1 125 . 25 VAL HG1 H 0.83 0.02 2 126 . 26 ARG H H 8.25 0.02 1 127 . 26 ARG N N 116.8 0.1 1 128 . 26 ARG HA H 3.75 0.02 1 129 . 26 ARG HB2 H 1.82 0.02 1 130 . 26 ARG HG2 H 1.62 0.02 1 131 . 26 ARG HG3 H 1.57 0.02 1 132 . 26 ARG HD2 H 3.14 0.02 1 133 . 26 ARG HD3 H 3.08 0.02 1 134 . 27 GLN H H 6.86 0.02 1 135 . 27 GLN N N 112.3 0.1 1 136 . 27 GLN HA H 4.15 0.02 1 137 . 27 GLN HB2 H 1.84 0.02 1 138 . 27 GLN HG2 H 2.37 0.02 1 139 . 27 GLN HG3 H 2.17 0.02 1 140 . 27 GLN HE21 H 7.33 0.02 1 141 . 27 GLN HE22 H 6.74 0.02 1 142 . 28 LEU H H 7.46 0.02 1 143 . 28 LEU N N 120.4 0.1 1 144 . 28 LEU HA H 4.13 0.02 1 145 . 28 LEU HB2 H 1.92 0.02 1 146 . 28 LEU HG H 1.79 0.02 1 147 . 28 LEU HD1 H 1.20 0.02 2 148 . 29 ALA H H 8.25 0.02 1 149 . 29 ALA N N 125.3 0.1 1 150 . 29 ALA HA H 4.07 0.02 1 151 . 29 ALA HB H 1.27 0.02 1 152 . 30 GLY H H 8.49 0.02 1 153 . 30 GLY N N 108.5 0.1 1 154 . 30 GLY HA2 H 3.65 0.02 1 155 . 31 VAL H H 7.21 0.02 1 156 . 31 VAL N N 118.5 0.1 1 157 . 31 VAL HA H 3.74 0.02 1 158 . 31 VAL HB H 2.04 0.02 1 159 . 31 VAL HG1 H 0.78 0.02 1 160 . 31 VAL HG2 H 0.69 0.02 1 161 . 32 ASN H H 9.24 0.02 1 162 . 32 ASN N N 126.2 0.1 1 163 . 32 ASN HA H 4.8 0.02 1 164 . 32 ASN HB2 H 2.68 0.02 1 165 . 32 ASN HD22 H 7.29 0.02 1 166 . 32 ASN HD21 H 6.95 0.02 1 167 . 33 GLN H H 7.79 0.02 1 168 . 33 GLN N N 117.3 0.1 1 169 . 33 GLN HA H 4.53 0.02 1 170 . 33 GLN HB2 H 2.04 0.02 1 171 . 33 GLN HG2 H 2.2 0.02 2 172 . 33 GLN HE21 H 6.68 0.02 1 173 . 33 GLN HE22 H 7.40 0.02 1 174 . 34 VAL H H 8.5 0.02 1 175 . 34 VAL N N 122.0 0.1 1 176 . 34 VAL HA H 4.97 0.02 1 177 . 34 VAL HB H 1.84 0.02 1 178 . 34 VAL HG2 H 0.80 0.02 2 179 . 35 GLN H H 8.93 0.02 1 180 . 35 GLN N N 124.9 0.1 1 181 . 35 GLN HA H 4.6 0.02 1 182 . 35 GLN HB2 H 1.87 0.02 1 183 . 35 GLN HG2 H 2.18 0.02 1 184 . 35 GLN HG3 H 2.03 0.02 1 185 . 35 GLN HE21 H 6.61 0.02 1 186 . 35 GLN HE22 H 7.44 0.02 1 187 . 36 VAL H H 9.12 0.02 1 188 . 36 VAL N N 123.1 0.1 1 189 . 36 VAL HA H 4.83 0.02 1 190 . 36 VAL HB H 1.89 0.02 1 191 . 36 VAL HG1 H 0.71 0.02 1 192 . 36 VAL HG2 H 0.81 0.02 1 193 . 37 LEU H H 9.08 0.02 1 194 . 37 LEU N N 129.8 0.1 1 195 . 37 LEU HA H 4.58 0.02 1 196 . 37 LEU HB2 H 1.73 0.02 1 197 . 37 LEU HG H 1.41 0.02 1 198 . 37 LEU HD1 H 0.71 0.02 2 199 . 38 PHE H H 8.42 0.02 1 200 . 38 PHE N N 123.4 0.1 1 201 . 38 PHE HA H 3.94 0.02 1 202 . 38 PHE HB2 H 2.79 0.02 1 203 . 38 PHE HD1 H 6.99 0.02 3 204 . 38 PHE HE1 H 7.14 0.02 3 205 . 38 PHE HZ H 7.05 0.02 1 206 . 39 ALA H H 8.62 0.02 1 207 . 39 ALA N N 119.7 0.1 1 208 . 39 ALA HA H 3.81 0.02 1 209 . 39 ALA HB H 1.31 0.02 1 210 . 40 THR H H 6.79 0.02 1 211 . 40 THR N N 102.2 0.1 1 212 . 40 THR HA H 4.33 0.02 1 213 . 40 THR HB H 3.8 0.02 1 214 . 40 THR HG2 H 0.99 0.02 1 215 . 41 GLU H H 7.58 0.02 1 216 . 41 GLU N N 117.4 0.1 1 217 . 41 GLU HA H 3.37 0.02 1 218 . 41 GLU HB2 H 1.92 0.02 1 219 . 41 GLU HG2 H 2.12 0.02 1 220 . 41 GLU HG3 H 2.45 0.02 1 221 . 42 LYS H H 7.58 0.02 1 222 . 42 LYS N N 117.2 0.1 1 223 . 42 LYS HA H 5.04 0.02 1 224 . 42 LYS HB2 H 1.58 0.02 1 225 . 42 LYS HG2 H 1.18 0.02 2 226 . 42 LYS HD2 H 1.46 0.02 1 227 . 42 LYS HD3 H 1.37 0.02 1 228 . 42 LYS HE2 H 2.74 0.02 1 229 . 42 LYS HE3 H 2.74 0.02 1 230 . 43 LEU H H 8.93 0.02 1 231 . 43 LEU N N 126.5 0.1 1 232 . 43 LEU HA H 4.95 0.02 1 233 . 43 LEU HB2 H 1.53 0.02 1 234 . 43 LEU HG H 1.06 0.02 1 235 . 43 LEU HD1 H 0.35 0.02 1 236 . 43 LEU HD2 H 0.62 0.02 1 237 . 44 VAL H H 9.07 0.02 1 238 . 44 VAL N N 126.2 0.1 1 239 . 44 VAL HA H 4.91 0.02 1 240 . 44 VAL HB H 1.88 0.02 1 241 . 44 VAL HG1 H 0.73 0.02 1 242 . 44 VAL HG2 H 0.76 0.02 1 243 . 45 VAL H H 9.46 0.02 1 244 . 45 VAL N N 127.2 0.1 1 245 . 45 VAL HA H 4.82 0.02 1 246 . 45 VAL HB H 2.2 0.02 1 247 . 45 VAL HG1 H 1.03 0.02 1 248 . 45 VAL HG2 H 1.05 0.02 1 249 . 46 ASP H H 8.71 0.02 1 250 . 46 ASP N N 127.1 0.1 1 251 . 46 ASP HA H 5.52 0.02 1 252 . 46 ASP HB2 H 2.66 0.02 1 253 . 47 ALA H H 9.15 0.02 1 254 . 47 ALA N N 126.7 0.1 1 255 . 47 ALA HA H 5.25 0.02 1 256 . 47 ALA HB H 1.62 0.02 1 257 . 48 ASP H H 8.89 0.02 1 258 . 48 ASP N N 119.6 0.1 1 259 . 48 ASP HA H 4.61 0.02 1 260 . 48 ASP HB2 H 2.67 0.02 1 261 . 49 ASN H H 7.65 0.02 1 262 . 49 ASN N N 114.5 0.1 1 263 . 49 ASN HA H 4.75 0.02 1 264 . 49 ASN HB2 H 2.71 0.02 1 265 . 49 ASN HD21 H 7.40 0.02 1 266 . 49 ASN HD22 H 6.66 0.02 1 267 . 50 ASP H H 8.35 0.02 1 268 . 50 ASP N N 116.1 0.1 1 269 . 50 ASP HA H 4.66 0.02 1 270 . 50 ASP HB2 H 2.9 0.02 1 271 . 51 ILE H H 7.06 0.02 1 272 . 51 ILE N N 121.0 0.1 1 273 . 51 ILE HA H 4.53 0.02 1 274 . 51 ILE HB H 2.13 0.02 1 275 . 51 ILE HG12 H 1.20 0.02 1 276 . 51 ILE HG13 H 1.06 0.02 1 277 . 51 ILE HG2 H 0.79 0.02 1 278 . 52 ARG H H 7.75 0.02 1 279 . 52 ARG N N 121.1 0.1 1 280 . 52 ARG HA H 3.5 0.02 1 281 . 52 ARG HB2 H 1.86 0.02 1 282 . 52 ARG HG2 H 1.23 0.02 1 283 . 52 ARG HG3 H 0.84 0.02 1 284 . 52 ARG HD2 H 3.00 0.02 1 285 . 52 ARG HD3 H 2.93 0.02 1 286 . 53 ALA H H 8.66 0.02 1 287 . 53 ALA N N 118.7 0.1 1 288 . 53 ALA HA H 4.01 0.02 1 289 . 53 ALA HB H 1.28 0.02 1 290 . 54 GLN H H 7.78 0.02 1 291 . 54 GLN N N 117.6 0.1 1 292 . 54 GLN HA H 3.96 0.02 1 293 . 54 GLN HB2 H 2.01 0.02 1 294 . 54 GLN HE21 H 6.84 0.02 1 295 . 54 GLN HG2 H 2.38 0.02 2 296 . 54 GLN HE22 H 7.41 0.02 1 297 . 55 VAL H H 8.12 0.02 1 298 . 55 VAL N N 121.6 0.1 1 299 . 55 VAL HA H 3.15 0.02 1 300 . 55 VAL HB H 1.71 0.02 1 301 . 55 VAL HG1 H 0.77 0.02 1 302 . 55 VAL HG2 H -0.08 0.02 1 303 . 56 GLU H H 8.21 0.02 1 304 . 56 GLU N N 117.8 0.1 1 305 . 56 GLU HA H 3.43 0.02 1 306 . 56 GLU HB2 H 1.95 0.02 1 307 . 56 GLU HG2 H 2.29 0.02 2 308 . 57 SER H H 7.81 0.02 1 309 . 57 SER N N 112.3 0.1 1 310 . 57 SER HA H 4.11 0.02 1 311 . 57 SER HB2 H 3.86 0.02 1 312 . 58 ALA H H 7.87 0.02 1 313 . 58 ALA N N 122.6 0.1 1 314 . 58 ALA HA H 3.98 0.02 1 315 . 58 ALA HB H 1.32 0.02 1 316 . 59 LEU H H 8.23 0.02 1 317 . 59 LEU N N 117.1 0.1 1 318 . 59 LEU HA H 4.0 0.02 1 319 . 59 LEU HB2 H 1.62 0.02 1 320 . 59 LEU HG H 1.20 0.02 1 321 . 59 LEU HD1 H 0.56 0.02 1 322 . 59 LEU HD2 H 0.39 0.02 1 323 . 60 GLN H H 8.16 0.02 1 324 . 60 GLN N N 120.8 0.1 1 325 . 60 GLN HA H 4.29 0.02 1 326 . 60 GLN HB2 H 2.16 0.02 1 327 . 60 GLN HG2 H 2.45 0.02 1 328 . 60 GLN HG3 H 2.30 0.02 1 329 . 60 GLN HE21 H 7.24 0.02 1 330 . 60 GLN HE22 H 6.72 0.02 1 331 . 61 LYS H H 7.75 0.02 1 332 . 61 LYS N N 119.7 0.1 1 333 . 61 LYS HA H 3.91 0.02 1 334 . 61 LYS HB2 H 1.81 0.02 1 335 . 61 LYS HG2 H 1.38 0.02 2 336 . 61 LYS HD2 H 1.51 0.02 1 337 . 61 LYS HD3 H 1.56 0.02 1 338 . 61 LYS HE2 H 2.85 0.02 2 339 . 62 ALA H H 7.16 0.02 1 340 . 62 ALA N N 118.5 0.1 1 341 . 62 ALA HA H 4.27 0.02 1 342 . 62 ALA HB H 1.47 0.02 1 343 . 63 GLY H H 7.43 0.02 1 344 . 63 GLY N N 104.4 0.1 1 345 . 63 GLY HA2 H 3.84 0.02 1 346 . 64 TYR H H 7.89 0.02 1 347 . 64 TYR N N 119.9 0.1 1 348 . 64 TYR HA H 4.72 0.02 1 349 . 64 TYR HB2 H 2.94 0.02 1 350 . 64 TYR HD1 H 6.75 0.02 3 351 . 64 TYR HE1 H 6.48 0.02 3 352 . 65 SER H H 8.03 0.02 1 353 . 65 SER N N 113.4 0.1 1 354 . 65 SER HA H 4.61 0.02 1 355 . 65 SER HB2 H 3.66 0.02 1 356 . 66 LEU H H 8.56 0.02 1 357 . 66 LEU N N 123.2 0.1 1 358 . 66 LEU HA H 5.09 0.02 1 359 . 66 LEU HB2 H 1.36 0.02 1 360 . 66 LEU HG H 1.26 0.02 1 361 . 66 LEU HD1 H 0.20 0.02 1 362 . 66 LEU HD2 H -0.03 0.02 1 363 . 67 ARG H H 8.7 0.02 1 364 . 67 ARG N N 120.4 0.1 1 365 . 67 ARG HA H 4.64 0.02 1 366 . 67 ARG HB2 H 1.76 0.02 1 367 . 67 ARG HG2 H 1.46 0.02 1 368 . 67 ARG HG3 H 1.52 0.02 1 369 . 67 ARG HD2 H 3.07 0.02 2 370 . 68 ASP H H 8.72 0.02 1 371 . 68 ASP N N 123.0 0.1 1 372 . 68 ASP HA H 4.48 0.02 1 373 . 68 ASP HB2 H 2.67 0.02 1 374 . 69 GLU H H 8.44 0.02 1 375 . 69 GLU N N 122.5 0.1 1 376 . 69 GLU HA H 4.13 0.02 1 377 . 69 GLU HB2 H 1.85 0.02 1 378 . 69 GLU HG2 H 2.02 0.02 1 379 . 69 GLU HG3 H 1.96 0.02 1 380 . 70 GLN H H 8.54 0.02 1 381 . 70 GLN N N 121.2 0.1 1 382 . 70 GLN HA H 4.22 0.02 1 383 . 70 GLN HB2 H 1.86 0.02 1 384 . 70 GLN HG2 H 2.22 0.02 1 385 . 70 GLN HG3 H 1.47 0.02 1 386 . 70 GLN HE21 H 6.72 0.02 1 387 . 70 GLN HE22 H 7.49 0.02 1 388 . 71 ALA H H 8.11 0.02 1 389 . 71 ALA N N 124.9 0.1 1 390 . 71 ALA HA H 4.23 0.02 1 391 . 71 ALA HB H 1.27 0.02 1 392 . 72 ALA H H 8.18 0.02 1 393 . 72 ALA N N 124.2 0.1 1 394 . 72 ALA HA H 4.21 0.02 1 395 . 72 ALA HB H 1.26 0.02 1 396 . 73 GLU H H 7.82 0.02 1 397 . 73 GLU N N 124.8 0.1 1 398 . 73 GLU HA H 3.98 0.02 1 399 . 73 GLU HB2 H 1.91 0.02 1 400 . 73 GLU HG2 H 2.06 0.02 2 stop_ save_