data_4324 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Characterization of Monomeric and Dimeric B-domain of Staphyococcal Protein A: Sources of Stabilization of a 3-helix Bundle Protein. ; _BMRB_accession_number 4324 _BMRB_flat_file_name bmr4324.str _Entry_type original _Submission_date 1999-03-22 _Accession_date 1999-03-23 _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 Karimi Afshin . . 2 Matsumura Masazumi . . 3 Wright Peter E. . 4 Dyson H. Jane . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 361 "15N chemical shifts" 69 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-07-12 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4325 'dimeric form of B-domain of Staphyococcal Protein A' stop_ _Original_release_date 1999-07-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Karimi, A., Matsumura, M., Wright, P. E., and Dyson, H. J., "Characterization of Monomeric and Dimeric B-domain of Staphyococcal Protein A: Sources of Stabilization of a 3-helix Bundle Protein," J. Pept. Res., Submitted. ; _Citation_title ; Characterization of Monomeric and Dimeric B-domain of Staphyococcal Protein A: Sources of Stabilization of a 3-helix Bundle Protein. ; _Citation_status submitted _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Karimi Afshin . . 2 Matsumura Masazumi . . 3 Wright Peter E. . 4 Dyson H. Jane . stop_ _Journal_abbreviation 'J. Pept. Res.' _Journal_name_full 'Journal of Peptide Research' _Journal_volume . _Journal_issue na _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword NMR 'protein A' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full 'Wishart et al., 1995 (J.Biomol.NMR 6, 135-140)"' _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _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 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_protein_A_(B_domain) _Saveframe_category molecular_system _Mol_system_name 'B domain of protein A' _Abbreviation_common 'protein A (B domain)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'B domain of protein A' $protein_A_(B_domain) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_protein_A_(B_domain) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'B domain of protein A' _Abbreviation_common 'protein A (B domain)' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 58 _Mol_residue_sequence ; ADNKFNKEQQNAFYEILHLP NLNEEQRNGFIQSLKDDPSQ SANLLAEAKKLNDAQAPK ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ASP 3 ASN 4 LYS 5 PHE 6 ASN 7 LYS 8 GLU 9 GLN 10 GLN 11 ASN 12 ALA 13 PHE 14 TYR 15 GLU 16 ILE 17 LEU 18 HIS 19 LEU 20 PRO 21 ASN 22 LEU 23 ASN 24 GLU 25 GLU 26 GLN 27 ARG 28 ASN 29 GLY 30 PHE 31 ILE 32 GLN 33 SER 34 LEU 35 LYS 36 ASP 37 ASP 38 PRO 39 SER 40 GLN 41 SER 42 ALA 43 ASN 44 LEU 45 LEU 46 ALA 47 GLU 48 ALA 49 LYS 50 LYS 51 LEU 52 ASN 53 ASP 54 ALA 55 GLN 56 ALA 57 PRO 58 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-15 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 1120 "IgG Fc region-binding protein" 100.00 60 100.00 100.00 1.96e-31 BMRB 1136 "IgG Fc region-binding protein" 100.00 60 100.00 100.00 1.96e-31 BMRB 2353 "IgG Fc region-binding protein" 100.00 60 100.00 100.00 1.96e-31 BMRB 4325 "dimer of B domain of protein A" 100.00 123 100.00 100.00 1.57e-30 PDB 1BDC "Staphylococcus Aureus Protein A, Immunoglobulin-Binding B Domain, Nmr, 10 Structures" 100.00 60 100.00 100.00 1.96e-31 PDB 1BDD "Staphylococcus Aureus Protein A, Immunoglobulin-Binding B Domain, Nmr, Minimized Average Structure" 100.00 60 100.00 100.00 1.96e-31 PDB 1SS1 "Staphylococcal Protein A, B-Domain, Y15w Mutant, Nmr, 25 Structures" 100.00 62 98.28 100.00 4.69e-31 PDB 4NPF "High-resolution Structure Of Two Tandem B Domains Of Staphylococcal Protein A Connected By The Conserved Linker" 100.00 116 98.28 100.00 4.51e-30 EMBL CAA49867 "staphylococcal protein A [synthetic construct]" 100.00 88 100.00 100.00 1.92e-31 GB AAA72944 "bifunctional fusion protein, partial [synthetic construct]" 100.00 308 100.00 100.00 1.52e-30 GB ABX88876 "single chain surrogate light chain variable domain [synthetic construct]" 100.00 190 100.00 100.00 7.77e-31 GB ABX88877 "single chain surrogate light chain variable domain [synthetic construct]" 100.00 214 100.00 100.00 7.98e-31 GB ACX42323 "4xProteinA tag [Recombineering donor plasmid pDOC-P]" 63.79 230 97.30 97.30 7.98e-15 GB EEV74738 "immunoglobulin G-binding protein A [Staphylococcus aureus A8115]" 75.86 296 100.00 100.00 1.44e-19 REF WP_031789382 "hypothetical protein, partial [Staphylococcus aureus]" 58.62 303 97.06 97.06 1.35e-12 REF WP_052996913 "hypothetical protein, partial [Staphylococcus aureus]" 60.34 242 100.00 100.00 8.44e-13 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $protein_A_(B_domain) 'golden staph.' 1280 Eubacteria . Staphylococcus aureus 'commercial vector pRIT5 (Pharmacia) containing entire protein A gene' 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 _Details $protein_A_(B_domain) 'recombinant technology' . . . . . ; fusion with the gene for the N-terminal 78 residues of T4 lysozyme produced an unusual folded, soluble chimeric protein. ; 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $protein_A_(B_domain) . mM 1.0 4.0 '[U-95% 15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_1H-15N_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond-1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 0.2 na temperature 303 1 K 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 _Indirect_shift_ratio_citation_label dioxan H 1 H ppm 3.75 internal direct cylindrical internal parallel_to_Bo 1.00 . dioxan N 15 H ppm 3.75 internal indirect cylindrical internal parallel_to_Bo .1013291444 $ref_1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond-1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'B domain of protein A' _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 ALA HA H 4.02 0.02 1 2 . 1 ALA HB H 1.55 0.02 1 3 . 2 ASP H H 8.67 0.02 1 4 . 2 ASP HA H 4.64 0.02 1 5 . 2 ASP HB2 H 2.59 0.02 2 6 . 2 ASP HB3 H 2.69 0.02 2 7 . 2 ASP N N 120.3 0.1 1 8 . 3 ASN H H 8.43 0.02 1 9 . 3 ASN HA H 4.62 0.02 1 10 . 3 ASN HB2 H 2.60 0.02 1 11 . 3 ASN HB3 H 2.60 0.02 1 12 . 3 ASN HD21 H 6.88 0.02 2 13 . 3 ASN HD22 H 7.54 0.02 2 14 . 3 ASN N N 119.4 0.1 1 15 . 3 ASN ND2 N 112.7 0.1 1 16 . 4 LYS H H 8.28 0.02 1 17 . 4 LYS HA H 4.20 0.02 1 18 . 4 LYS HB2 H 1.70 0.02 1 19 . 4 LYS HB3 H 1.70 0.02 1 20 . 4 LYS HG2 H 1.28 0.02 1 21 . 4 LYS HG3 H 1.28 0.02 1 22 . 4 LYS HE2 H 2.97 0.02 1 23 . 4 LYS HE3 H 2.97 0.02 1 24 . 4 LYS N N 121.4 0.1 1 25 . 5 PHE H H 8.18 0.02 1 26 . 5 PHE HA H 5.04 0.02 1 27 . 5 PHE HB2 H 3.04 0.02 2 28 . 5 PHE HB3 H 3.37 0.02 2 29 . 5 PHE HD1 H 7.10 0.02 1 30 . 5 PHE HD2 H 7.10 0.02 1 31 . 5 PHE HE1 H 7.16 0.02 1 32 . 5 PHE HE2 H 7.16 0.02 1 33 . 5 PHE N N 119.9 0.1 1 34 . 6 ASN H H 8.48 0.02 1 35 . 6 ASN HA H 4.75 0.02 1 36 . 6 ASN HB2 H 2.95 0.02 2 37 . 6 ASN HB3 H 3.31 0.02 2 38 . 6 ASN HD21 H 6.94 0.02 2 39 . 6 ASN HD22 H 7.52 0.02 2 40 . 6 ASN N N 120.9 0.1 1 41 . 6 ASN ND2 N 110.2 0.1 1 42 . 7 LYS H H 8.37 0.02 1 43 . 7 LYS HA H 4.01 0.02 1 44 . 7 LYS HB2 H 1.83 0.02 2 45 . 7 LYS HB3 H 1.88 0.02 2 46 . 7 LYS HG2 H 1.46 0.02 2 47 . 7 LYS HG3 H 1.54 0.02 2 48 . 7 LYS HD2 H 1.72 0.02 1 49 . 7 LYS HD3 H 1.72 0.02 1 50 . 7 LYS N N 119.0 0.1 1 51 . 8 GLU H H 8.29 0.02 1 52 . 8 GLU HA H 4.13 0.02 1 53 . 8 GLU HB2 H 2.09 0.02 2 54 . 8 GLU HB3 H 2.14 0.02 2 55 . 8 GLU HG2 H 2.38 0.02 1 56 . 8 GLU HG3 H 2.38 0.02 1 57 . 8 GLU N N 119.7 0.1 1 58 . 9 GLN H H 8.52 0.02 1 59 . 9 GLN HA H 3.91 0.02 1 60 . 9 GLN HB2 H 2.22 0.02 1 61 . 9 GLN HB3 H 2.22 0.02 1 62 . 9 GLN HG2 H 2.49 0.02 1 63 . 9 GLN HG3 H 2.49 0.02 1 64 . 9 GLN HE21 H 7.01 0.02 2 65 . 9 GLN HE22 H 7.31 0.02 2 66 . 9 GLN N N 121.2 0.1 1 67 . 9 GLN NE2 N 110.8 0.1 1 68 . 10 GLN H H 8.68 0.02 1 69 . 10 GLN HA H 3.99 0.02 1 70 . 10 GLN HB2 H 2.22 0.02 1 71 . 10 GLN HB3 H 2.22 0.02 1 72 . 10 GLN HG2 H 2.49 0.02 1 73 . 10 GLN HG3 H 2.49 0.02 1 74 . 10 GLN HE21 H 6.86 0.02 2 75 . 10 GLN HE22 H 7.22 0.02 2 76 . 10 GLN N N 118.9 0.1 1 77 . 10 GLN NE2 N 111.3 0.1 1 78 . 11 ASN H H 8.32 0.02 1 79 . 11 ASN HA H 4.63 0.02 1 80 . 11 ASN HB2 H 2.93 0.02 1 81 . 11 ASN HB3 H 2.93 0.02 1 82 . 11 ASN HD21 H 7.01 0.02 2 83 . 11 ASN HD22 H 7.74 0.02 2 84 . 11 ASN N N 117.9 0.1 1 85 . 11 ASN ND2 N 112.1 0.1 1 86 . 12 ALA H H 7.98 0.02 1 87 . 12 ALA HA H 4.10 0.02 1 88 . 12 ALA HB H 1.47 0.02 1 89 . 12 ALA N N 122.6 0.1 1 90 . 13 PHE H H 8.19 0.02 1 91 . 13 PHE HA H 3.86 0.02 1 92 . 13 PHE HB2 H 3.04 0.02 2 93 . 13 PHE HB3 H 3.37 0.02 2 94 . 13 PHE HD1 H 7.07 0.02 1 95 . 13 PHE HD2 H 7.07 0.02 1 96 . 13 PHE HE1 H 7.30 0.02 1 97 . 13 PHE HE2 H 7.30 0.02 1 98 . 13 PHE N N 117.8 0.1 1 99 . 14 TYR H H 8.16 0.02 1 100 . 14 TYR HA H 3.97 0.02 1 101 . 14 TYR HB2 H 3.22 0.02 1 102 . 14 TYR HB3 H 3.22 0.02 1 103 . 14 TYR HD1 H 7.16 0.02 1 104 . 14 TYR HD2 H 7.16 0.02 1 105 . 14 TYR HE1 H 6.75 0.02 1 106 . 14 TYR HE2 H 6.75 0.02 1 107 . 14 TYR N N 117.0 0.1 1 108 . 15 GLU H H 8.60 0.02 1 109 . 15 GLU HA H 4.02 0.02 1 110 . 15 GLU HB2 H 2.02 0.02 2 111 . 15 GLU HB3 H 2.18 0.02 2 112 . 15 GLU HG2 H 2.29 0.02 2 113 . 15 GLU HG3 H 2.51 0.02 2 114 . 15 GLU N N 119.2 0.1 1 115 . 16 ILE H H 8.48 0.02 1 116 . 16 ILE HA H 3.43 0.02 1 117 . 16 ILE HB H 1.82 0.02 1 118 . 16 ILE HG12 H 1.84 0.02 1 119 . 16 ILE HG13 H 1.84 0.02 1 120 . 16 ILE HG2 H 0.81 0.02 1 121 . 16 ILE HD1 H 0.54 0.02 1 122 . 16 ILE N N 119.5 0.1 1 123 . 17 LEU H H 7.91 0.02 1 124 . 17 LEU HA H 3.72 0.02 1 125 . 17 LEU HB2 H 1.15 0.02 2 126 . 17 LEU HB3 H 1.50 0.02 2 127 . 17 LEU HG H 1.39 0.02 1 128 . 17 LEU HD1 H 0.59 0.02 2 129 . 17 LEU HD2 H 0.68 0.02 2 130 . 17 LEU N N 117.4 0.1 1 131 . 18 HIS H H 7.29 0.02 1 132 . 18 HIS HA H 4.50 0.02 1 133 . 18 HIS HB2 H 2.80 0.02 2 134 . 18 HIS HB3 H 3.48 0.02 2 135 . 18 HIS HD2 H 7.10 0.02 1 136 . 18 HIS HE1 H 8.29 0.02 1 137 . 18 HIS N N 111.8 0.1 1 138 . 19 LEU H H 7.24 0.02 1 139 . 19 LEU HA H 4.51 0.02 1 140 . 19 LEU HB2 H 1.38 0.02 2 141 . 19 LEU HB3 H 1.75 0.02 2 142 . 19 LEU HG H 2.21 0.02 1 143 . 19 LEU HD1 H 0.70 0.02 2 144 . 19 LEU HD2 H 0.88 0.02 2 145 . 19 LEU N N 124.3 0.1 1 146 . 20 PRO HA H 4.43 0.02 1 147 . 20 PRO HB2 H 2.08 0.02 2 148 . 20 PRO HB3 H 2.09 0.02 2 149 . 20 PRO HG2 H 2.02 0.02 1 150 . 20 PRO HG3 H 2.02 0.02 1 151 . 20 PRO HD2 H 3.84 0.02 2 152 . 20 PRO HD3 H 4.08 0.02 2 153 . 21 ASN H H 8.90 0.02 1 154 . 21 ASN HA H 5.03 0.02 1 155 . 21 ASN HB2 H 2.92 0.02 1 156 . 21 ASN HB3 H 2.92 0.02 1 157 . 21 ASN HD21 H 7.00 0.02 2 158 . 21 ASN HD22 H 7.44 0.02 2 159 . 21 ASN N N 113.8 0.1 1 160 . 21 ASN ND2 N 114.4 0.1 1 161 . 22 LEU H H 6.55 0.02 1 162 . 22 LEU HA H 4.46 0.02 1 163 . 22 LEU HB2 H 1.64 0.02 2 164 . 22 LEU HB3 H 1.73 0.02 2 165 . 22 LEU HG H 1.73 0.02 1 166 . 22 LEU HD1 H 0.92 0.02 2 167 . 22 LEU HD2 H 1.01 0.02 2 168 . 22 LEU N N 117.0 0.1 1 169 . 23 ASN H H 8.57 0.02 1 170 . 23 ASN HA H 4.93 0.02 1 171 . 23 ASN HB2 H 2.84 0.02 2 172 . 23 ASN HB3 H 2.31 0.02 2 173 . 23 ASN HD21 H 7.04 0.02 2 174 . 23 ASN HD22 H 7.53 0.02 2 175 . 23 ASN N N 119.2 0.1 1 176 . 23 ASN ND2 N 111.6 0.1 1 177 . 24 GLU H H 8.62 0.02 1 178 . 24 GLU HA H 3.97 0.02 1 179 . 24 GLU HB2 H 2.04 0.02 1 180 . 24 GLU HB3 H 2.04 0.02 1 181 . 24 GLU HG2 H 2.38 0.02 1 182 . 24 GLU HG3 H 2.38 0.02 1 183 . 24 GLU N N 118.2 0.1 1 184 . 25 GLU H H 8.26 0.02 1 185 . 25 GLU HA H 4.08 0.02 1 186 . 25 GLU HB2 H 2.07 0.02 1 187 . 25 GLU HB3 H 2.07 0.02 1 188 . 25 GLU HG2 H 2.33 0.02 2 189 . 25 GLU HG3 H 2.35 0.02 2 190 . 25 GLU N N 119.7 0.1 1 191 . 26 GLN H H 8.63 0.02 1 192 . 26 GLN HA H 3.89 0.02 1 193 . 26 GLN HB2 H 2.49 0.02 1 194 . 26 GLN HB3 H 2.49 0.02 1 195 . 26 GLN HG2 H 2.38 0.02 2 196 . 26 GLN HG3 H 2.81 0.02 2 197 . 26 GLN HE21 H 7.65 0.02 2 198 . 26 GLN HE22 H 8.28 0.02 2 199 . 26 GLN N N 119.8 0.1 1 200 . 26 GLN NE2 N 112.4 0.1 1 201 . 27 ARG H H 8.67 0.02 1 202 . 27 ARG HA H 3.81 0.02 1 203 . 27 ARG HB2 H 1.77 0.02 2 204 . 27 ARG HB3 H 1.89 0.02 2 205 . 27 ARG HG2 H 1.50 0.02 1 206 . 27 ARG HG3 H 1.50 0.02 1 207 . 27 ARG HD2 H 3.26 0.02 2 208 . 27 ARG HD3 H 3.41 0.02 2 209 . 27 ARG HE H 7.58 0.02 1 210 . 27 ARG N N 119.5 0.1 1 211 . 27 ARG NE N 128.8 0.1 1 212 . 28 ASN H H 8.65 0.02 1 213 . 28 ASN HA H 4.43 0.02 1 214 . 28 ASN HB2 H 2.82 0.02 2 215 . 28 ASN HB3 H 2.92 0.02 2 216 . 28 ASN HD21 H 7.01 0.02 2 217 . 28 ASN HD22 H 7.64 0.02 2 218 . 28 ASN N N 115.6 0.1 1 219 . 28 ASN ND2 N 111.9 0.1 1 220 . 29 GLY H H 8.08 0.02 1 221 . 29 GLY HA2 H 3.82 0.02 1 222 . 29 GLY HA3 H 3.82 0.02 1 223 . 29 GLY N N 108.2 0.1 1 224 . 30 PHE H H 7.86 0.02 1 225 . 30 PHE HA H 4.48 0.02 1 226 . 30 PHE HB2 H 3.05 0.02 1 227 . 30 PHE HB3 H 3.05 0.02 1 228 . 30 PHE HD1 H 7.27 0.02 1 229 . 30 PHE HD2 H 7.27 0.02 1 230 . 30 PHE HE1 H 7.30 0.02 1 231 . 30 PHE HE2 H 7.30 0.02 1 232 . 30 PHE HZ H 7.17 0.02 1 233 . 30 PHE N N 120.2 0.1 1 234 . 31 ILE H H 8.29 0.02 1 235 . 31 ILE HA H 3.76 0.02 1 236 . 31 ILE HB H 2.12 0.02 1 237 . 31 ILE HG12 H 1.39 0.02 2 238 . 31 ILE HG13 H 1.63 0.02 2 239 . 31 ILE HG2 H 0.68 0.02 1 240 . 31 ILE HD1 H 0.99 0.02 1 241 . 31 ILE N N 118.7 0.1 1 242 . 32 GLN H H 8.44 0.02 1 243 . 32 GLN HA H 3.97 0.02 1 244 . 32 GLN HB2 H 2.22 0.02 1 245 . 32 GLN HB3 H 2.22 0.02 1 246 . 32 GLN HG2 H 2.44 0.02 1 247 . 32 GLN HG3 H 2.44 0.02 1 248 . 32 GLN HE21 H 6.94 0.02 2 249 . 32 GLN HE22 H 7.82 0.02 2 250 . 32 GLN N N 119.2 0.1 1 251 . 32 GLN NE2 N 115.5 0.1 1 252 . 33 SER H H 8.02 0.02 1 253 . 33 SER HA H 4.30 0.02 1 254 . 33 SER HB2 H 4.00 0.02 2 255 . 33 SER HB3 H 4.43 0.02 2 256 . 33 SER N N 114.9 0.1 1 257 . 34 LEU H H 8.19 0.02 1 258 . 34 LEU HA H 3.78 0.02 1 259 . 34 LEU HB2 H 1.69 0.02 2 260 . 34 LEU HB3 H 1.87 0.02 2 261 . 34 LEU HG H 1.69 0.02 1 262 . 34 LEU HD1 H 0.74 0.02 2 263 . 34 LEU HD2 H 0.81 0.02 2 264 . 34 LEU N N 124.0 0.1 1 265 . 35 LYS H H 8.02 0.02 1 266 . 35 LYS HA H 4.02 0.02 1 267 . 35 LYS HB2 H 1.98 0.02 1 268 . 35 LYS HB3 H 1.98 0.02 1 269 . 35 LYS HG2 H 1.47 0.02 1 270 . 35 LYS HG3 H 1.47 0.02 1 271 . 35 LYS HD2 H 1.69 0.02 1 272 . 35 LYS HD3 H 1.69 0.02 1 273 . 35 LYS HE2 H 3.03 0.02 1 274 . 35 LYS HE3 H 3.03 0.02 1 275 . 35 LYS N N 115.8 0.1 1 276 . 36 ASP H H 8.11 0.02 1 277 . 36 ASP HA H 4.47 0.02 1 278 . 36 ASP HB2 H 2.75 0.02 2 279 . 36 ASP HB3 H 2.82 0.02 2 280 . 36 ASP N N 117.7 0.1 1 281 . 37 ASP H H 7.68 0.02 1 282 . 37 ASP HA H 4.96 0.02 1 283 . 37 ASP HB2 H 2.61 0.02 2 284 . 37 ASP HB3 H 3.01 0.02 2 285 . 37 ASP N N 114.0 0.1 1 286 . 38 PRO HA H 4.53 0.02 1 287 . 38 PRO HB2 H 2.00 0.02 1 288 . 38 PRO HB3 H 2.00 0.02 1 289 . 38 PRO HG2 H 2.15 0.02 2 290 . 38 PRO HG3 H 2.29 0.02 2 291 . 38 PRO HD2 H 3.70 0.02 2 292 . 38 PRO HD3 H 3.89 0.02 2 293 . 39 SER H H 8.11 0.02 1 294 . 39 SER HA H 4.33 0.02 1 295 . 39 SER HB2 H 4.00 0.02 2 296 . 39 SER HB3 H 4.07 0.02 2 297 . 39 SER N N 113.0 0.1 1 298 . 40 GLN H H 7.89 0.02 1 299 . 40 GLN HA H 4.64 0.02 1 300 . 40 GLN HB2 H 2.01 0.02 2 301 . 40 GLN HB3 H 2.67 0.02 2 302 . 40 GLN HG2 H 2.34 0.02 2 303 . 40 GLN HG3 H 2.48 0.02 2 304 . 40 GLN HE21 H 6.89 0.02 2 305 . 40 GLN HE22 H 7.60 0.02 2 306 . 40 GLN N N 120.1 0.1 1 307 . 40 GLN NE2 N 113.8 0.1 1 308 . 41 SER H H 7.79 0.02 1 309 . 41 SER HA H 3.75 0.02 1 310 . 41 SER HB2 H 3.98 0.02 1 311 . 41 SER HB3 H 3.98 0.02 1 312 . 41 SER N N 115.4 0.1 1 313 . 42 ALA H H 8.51 0.02 1 314 . 42 ALA HA H 4.14 0.02 1 315 . 42 ALA HB H 1.45 0.02 1 316 . 42 ALA N N 122.8 0.1 1 317 . 43 ASN H H 7.93 0.02 1 318 . 43 ASN HA H 4.54 0.02 1 319 . 43 ASN HB2 H 2.91 0.02 1 320 . 43 ASN HB3 H 2.91 0.02 1 321 . 43 ASN HD21 H 6.99 0.02 2 322 . 43 ASN HD22 H 7.77 0.02 2 323 . 43 ASN N N 118.3 0.1 1 324 . 43 ASN ND2 N 112.6 0.1 1 325 . 44 LEU H H 8.60 0.02 1 326 . 44 LEU HA H 4.17 0.02 1 327 . 44 LEU HB2 H 1.27 0.02 2 328 . 44 LEU HB3 H 1.82 0.02 2 329 . 44 LEU HG H 1.88 0.02 1 330 . 44 LEU HD1 H 1.13 0.02 2 331 . 44 LEU HD2 H 0.81 0.02 2 332 . 44 LEU N N 121.2 0.1 1 333 . 45 LEU H H 8.43 0.02 1 334 . 45 LEU HA H 3.82 0.02 1 335 . 45 LEU HB2 H 1.48 0.02 2 336 . 45 LEU HB3 H 1.89 0.02 2 337 . 45 LEU HG H 1.57 0.02 1 338 . 45 LEU HD1 H 0.92 0.02 1 339 . 45 LEU HD2 H 0.92 0.02 1 340 . 45 LEU N N 118.7 0.1 1 341 . 46 ALA H H 7.62 0.02 1 342 . 46 ALA HA H 4.07 0.02 1 343 . 46 ALA HB H 1.57 0.02 1 344 . 46 ALA N N 119.5 0.1 1 345 . 47 GLU H H 8.08 0.02 1 346 . 47 GLU HA H 4.03 0.02 1 347 . 47 GLU HB2 H 2.25 0.02 2 348 . 47 GLU HB3 H 2.33 0.02 2 349 . 47 GLU HG2 H 2.52 0.02 2 350 . 47 GLU HG3 H 2.62 0.02 2 351 . 47 GLU N N 119.0 0.1 1 352 . 48 ALA H H 8.42 0.02 1 353 . 48 ALA HA H 3.49 0.02 1 354 . 48 ALA HB H 0.50 0.02 1 355 . 48 ALA N N 123.7 0.1 1 356 . 49 LYS H H 8.52 0.02 1 357 . 49 LYS HA H 3.78 0.02 1 358 . 49 LYS HB2 H 1.80 0.02 2 359 . 49 LYS HB3 H 1.96 0.02 2 360 . 49 LYS HG2 H 1.37 0.02 1 361 . 49 LYS HG3 H 1.37 0.02 1 362 . 49 LYS HE2 H 2.98 0.02 1 363 . 49 LYS HE3 H 2.98 0.02 1 364 . 49 LYS N N 118.0 0.1 1 365 . 50 LYS H H 7.73 0.02 1 366 . 50 LYS HA H 4.13 0.02 1 367 . 50 LYS HB2 H 1.96 0.02 1 368 . 50 LYS HB3 H 1.96 0.02 1 369 . 50 LYS HG2 H 1.47 0.02 1 370 . 50 LYS HG3 H 1.47 0.02 1 371 . 50 LYS HD2 H 1.63 0.02 1 372 . 50 LYS HD3 H 1.63 0.02 1 373 . 50 LYS HE2 H 2.99 0.02 1 374 . 50 LYS HE3 H 2.99 0.02 1 375 . 50 LYS N N 119.9 0.1 1 376 . 51 LEU H H 7.94 0.02 1 377 . 51 LEU HA H 4.18 0.02 1 378 . 51 LEU HB2 H 1.74 0.02 1 379 . 51 LEU HB3 H 1.74 0.02 1 380 . 51 LEU HG H 1.51 0.02 1 381 . 51 LEU HD1 H 1.02 0.02 1 382 . 51 LEU HD2 H 1.02 0.02 1 383 . 51 LEU N N 121.8 0.1 1 384 . 52 ASN H H 8.59 0.02 1 385 . 52 ASN HA H 3.89 0.02 1 386 . 52 ASN HB2 H 2.42 0.02 2 387 . 52 ASN HB3 H 3.13 0.02 2 388 . 52 ASN HD21 H 6.88 0.02 2 389 . 52 ASN HD22 H 7.95 0.02 2 390 . 52 ASN N N 116.8 0.1 1 391 . 52 ASN ND2 N 115.9 0.1 1 392 . 53 ASP H H 8.28 0.02 1 393 . 53 ASP HA H 4.48 0.02 1 394 . 53 ASP HB2 H 2.74 0.02 2 395 . 53 ASP HB3 H 2.80 0.02 2 396 . 53 ASP N N 118.6 0.1 1 397 . 54 ALA H H 8.05 0.02 1 398 . 54 ALA HA H 4.28 0.02 1 399 . 54 ALA HB H 1.62 0.02 1 400 . 54 ALA N N 122.8 0.1 1 401 . 55 GLN H H 7.56 0.02 1 402 . 55 GLN HA H 4.41 0.02 1 403 . 55 GLN HB2 H 1.83 0.02 2 404 . 55 GLN HB3 H 2.32 0.02 2 405 . 55 GLN HG2 H 2.50 0.02 2 406 . 55 GLN HG3 H 2.66 0.02 2 407 . 55 GLN HE21 H 7.29 0.02 2 408 . 55 GLN HE22 H 8.72 0.02 2 409 . 55 GLN N N 114.9 0.1 1 410 . 55 GLN NE2 N 110.8 0.1 1 411 . 56 ALA H H 7.15 0.02 1 412 . 56 ALA HA H 4.38 0.02 1 413 . 56 ALA HB H 1.47 0.02 1 414 . 56 ALA N N 124.2 0.1 1 415 . 57 PRO HA H 4.45 0.02 1 416 . 57 PRO HB2 H 1.99 0.02 2 417 . 57 PRO HB3 H 2.12 0.02 2 418 . 57 PRO HD2 H 3.66 0.02 2 419 . 57 PRO HD3 H 3.81 0.02 2 420 . 58 LYS H H 8.06 0.02 1 421 . 58 LYS HA H 4.22 0.02 1 422 . 58 LYS HB2 H 1.88 0.02 1 423 . 58 LYS HB3 H 1.88 0.02 1 424 . 58 LYS HG2 H 1.48 0.02 1 425 . 58 LYS HG3 H 1.48 0.02 1 426 . 58 LYS HD2 H 1.73 0.02 1 427 . 58 LYS HD3 H 1.73 0.02 1 428 . 58 LYS HE2 H 3.07 0.02 1 429 . 58 LYS HE3 H 3.07 0.02 1 430 . 58 LYS N N 127.0 0.1 1 stop_ save_