data_4850 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Glutaredoxin 3 from Escherichia coli in the fully oxidized form ; _BMRB_accession_number 4850 _BMRB_flat_file_name bmr4850.str _Entry_type original _Submission_date 2000-10-06 _Accession_date 2000-10-06 _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 Nordstrand K. . . 2 Sandstrom A. . . 3 Aslund F. . . 4 Holmgren A. . . 5 Otting G. . . 6 Berndt K. D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 486 "15N chemical shifts" 81 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-03-12 original author . stop_ _Original_release_date 2001-03-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR Structure of Oxidized Glutaredoxin 3 from Escherichia coli' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11031118 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nordstrand K. . . 2 Sandstrom A. . . 3 Aslund F. . . 4 Holmgren A. . . 5 Otting G. . . 6 Berndt K. D. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume 303 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 423 _Page_last 432 _Year 2000 _Details . save_ ################################## # Molecular system description # ################################## save_system_Grx3 _Saveframe_category molecular_system _Mol_system_name 'GLUTAREDOXIN 3' _Abbreviation_common Grx3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'GLUTAREDOXIN 3' $Grx3 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Grx3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'GLUTAREDOXIN 3' _Name_variant C65Y _Abbreviation_common Grx3 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 82 _Mol_residue_sequence ; ANVEIYTKETCPYCHRAKAL LSSKGVSFQELPIDGNAAKR EEMIKRSGRTTVPQIFIDAQ HIGGYDDLYALDARGGLDPL LK ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ASN 3 VAL 4 GLU 5 ILE 6 TYR 7 THR 8 LYS 9 GLU 10 THR 11 CYS 12 PRO 13 TYR 14 CYS 15 HIS 16 ARG 17 ALA 18 LYS 19 ALA 20 LEU 21 LEU 22 SER 23 SER 24 LYS 25 GLY 26 VAL 27 SER 28 PHE 29 GLN 30 GLU 31 LEU 32 PRO 33 ILE 34 ASP 35 GLY 36 ASN 37 ALA 38 ALA 39 LYS 40 ARG 41 GLU 42 GLU 43 MET 44 ILE 45 LYS 46 ARG 47 SER 48 GLY 49 ARG 50 THR 51 THR 52 VAL 53 PRO 54 GLN 55 ILE 56 PHE 57 ILE 58 ASP 59 ALA 60 GLN 61 HIS 62 ILE 63 GLY 64 GLY 65 TYR 66 ASP 67 ASP 68 LEU 69 TYR 70 ALA 71 LEU 72 ASP 73 ALA 74 ARG 75 GLY 76 GLY 77 LEU 78 ASP 79 PRO 80 LEU 81 LEU 82 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 4225 Glutaredoxin_3 100.00 83 98.78 98.78 6.38e-52 PDB 1FOV "Glutaredoxin 3 From Escherichia Coli In The Fully Oxidized Form" 100.00 82 100.00 100.00 4.21e-53 PDB 3GRX "Nmr Structure Of Escherichia Coli Glutaredoxin 3-Glutathione Mixed Disulfide Complex, 20 Structures" 100.00 82 98.78 98.78 6.21e-52 DBJ BAB37911 "glutaredoxin 3 [Escherichia coli O157:H7 str. Sakai]" 100.00 83 98.78 98.78 9.25e-52 DBJ BAE77682 "glutaredoxin 3 [Escherichia coli str. K-12 substr. W3110]" 100.00 83 98.78 98.78 9.25e-52 DBJ BAG79416 "glutaredoxin [Escherichia coli SE11]" 100.00 83 98.78 98.78 9.25e-52 DBJ BAI28143 "glutaredoxin 3 [Escherichia coli O26:H11 str. 11368]" 100.00 83 98.78 98.78 9.25e-52 DBJ BAI33266 "glutaredoxin 3 [Escherichia coli O103:H2 str. 12009]" 100.00 83 98.78 98.78 9.25e-52 EMBL CAP78066 "glutaredoxin-3 [Escherichia coli LF82]" 100.00 83 98.78 98.78 9.25e-52 EMBL CAQ33936 "reduced glutaredoxin 3 [Escherichia coli BL21(DE3)]" 100.00 83 98.78 98.78 9.25e-52 EMBL CAR00580 "glutaredoxin 3 [Escherichia coli IAI1]" 100.00 83 98.78 98.78 9.25e-52 EMBL CAR05236 "glutaredoxin 3 [Escherichia coli S88]" 100.00 83 98.78 98.78 9.25e-52 EMBL CAR10284 "glutaredoxin 3 [Escherichia coli ED1a]" 100.00 83 98.78 98.78 9.25e-52 GB AAB18587 "unnamed protein product [Escherichia coli str. K-12 substr. MG1655]" 100.00 83 98.78 98.78 9.25e-52 GB AAC76634 "glutaredoxin 3 [Escherichia coli str. K-12 substr. MG1655]" 100.00 83 98.78 98.78 9.25e-52 GB AAG58757 "glutaredoxin 3 [Escherichia coli O157:H7 str. EDL933]" 100.00 83 98.78 98.78 9.25e-52 GB AAN45096 "glutaredoxin 3 [Shigella flexneri 2a str. 301]" 100.00 83 97.56 97.56 1.89e-50 GB AAN82869 "Glutaredoxin 3 [Escherichia coli CFT073]" 100.00 83 98.78 98.78 9.25e-52 REF NP_290193 "glutaredoxin 3 [Escherichia coli O157:H7 str. EDL933]" 100.00 83 98.78 98.78 9.25e-52 REF NP_312515 "glutaredoxin 3 [Escherichia coli O157:H7 str. Sakai]" 100.00 83 98.78 98.78 9.25e-52 REF NP_418067 "glutaredoxin 3 [Escherichia coli str. K-12 substr. MG1655]" 100.00 83 98.78 98.78 9.25e-52 REF NP_709389 "glutaredoxin [Shigella flexneri 2a str. 301]" 100.00 83 97.56 97.56 1.89e-50 REF NP_756295 "glutaredoxin 3 [Escherichia coli CFT073]" 100.00 83 98.78 98.78 9.25e-52 SP P0AC62 "RecName: Full=Glutaredoxin-3; Short=Grx3 [Escherichia coli K-12]" 100.00 83 98.78 98.78 9.25e-52 SP P0AC63 "RecName: Full=Glutaredoxin-3; Short=Grx3 [Escherichia coli CFT073]" 100.00 83 98.78 98.78 9.25e-52 SP P0AC64 "RecName: Full=Glutaredoxin-3; Short=Grx3 [Escherichia coli O157:H7]" 100.00 83 98.78 98.78 9.25e-52 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Grx3 . 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 $Grx3 'recombinant technology' 'E. coli' Escherichia coli 'HMS-174 DE3' PET-3 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 $Grx3 . mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Grx3 . mM [U-15N] stop_ save_ ############################ # Computer software used # ############################ save_PROSA _Saveframe_category software _Name PROSA _Version 3.6 loop_ _Task processing stop_ _Details 'Guntert, Billeter, Ohlenschlager, Brown, & Wuthrich' save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.4 loop_ _Task 'data analysis' stop_ _Details 'Bartels, Xia, Billeter, Guntert, & Wuthrich' save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task refinement stop_ _Details 'Guntert, Mumenthaler, & Wuthrich' save_ save_OPAL _Saveframe_category software _Name OPAL _Version 2.6 loop_ _Task refinement stop_ _Details 'Luginbuhl, Guntert, Billeter, & Wuthrich' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _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 5.5 0.05 n/a temperature 301 0.2 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 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 $sample_2 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'GLUTAREDOXIN 3' _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 4.47 . 1 2 . 1 ALA HB H 1.52 . 1 3 . 2 ASN N N 121.0 . 1 4 . 2 ASN H H 9.38 . 1 5 . 2 ASN HA H 5.02 . 1 6 . 2 ASN HB2 H 3.01 . 1 7 . 2 ASN HB3 H 2.86 . 1 8 . 2 ASN ND2 N 111.9 . 1 9 . 2 ASN HD21 H 7.66 . 1 10 . 2 ASN HD22 H 6.86 . 1 11 . 3 VAL N N 129.1 . 1 12 . 3 VAL H H 9.26 . 1 13 . 3 VAL HA H 5.04 . 1 14 . 3 VAL HB H 2.31 . 1 15 . 3 VAL HG1 H 0.92 . 1 16 . 3 VAL HG2 H 0.97 . 1 17 . 4 GLU N N 127.0 . 1 18 . 4 GLU H H 9.30 . 1 19 . 4 GLU HA H 5.34 . 1 20 . 4 GLU HB2 H 2.07 . 2 21 . 4 GLU HB3 H 1.95 . 2 22 . 4 GLU HG2 H 1.96 . 1 23 . 4 GLU HG3 H 1.96 . 1 24 . 5 ILE N N 118.3 . 1 25 . 5 ILE H H 8.74 . 1 26 . 5 ILE HA H 5.47 . 1 27 . 5 ILE HB H 1.48 . 1 28 . 5 ILE HG2 H 0.72 . 1 29 . 5 ILE HG12 H 1.48 . 2 30 . 5 ILE HG13 H 0.91 . 2 31 . 5 ILE HD1 H 0.42 . 1 32 . 6 TYR N N 129.0 . 1 33 . 6 TYR H H 9.21 . 1 34 . 6 TYR HA H 5.51 . 1 35 . 6 TYR HB2 H 3.01 . 1 36 . 6 TYR HB3 H 3.18 . 1 37 . 6 TYR HD1 H 7.26 . 1 38 . 6 TYR HD2 H 7.26 . 1 39 . 6 TYR HE1 H 6.56 . 1 40 . 6 TYR HE2 H 6.56 . 1 41 . 7 THR N N 109.4 . 1 42 . 7 THR H H 8.08 . 1 43 . 7 THR HA H 4.84 . 1 44 . 7 THR HB H 4.33 . 1 45 . 7 THR HG2 H 1.05 . 1 46 . 8 LYS N N 114.6 . 1 47 . 8 LYS H H 7.22 . 1 48 . 8 LYS HA H 5.04 . 1 49 . 8 LYS HB2 H 2.09 . 1 50 . 8 LYS HB3 H 1.71 . 1 51 . 8 LYS HG2 H 1.57 . 2 52 . 8 LYS HG3 H 1.46 . 2 53 . 8 LYS HD2 H 1.07 . 1 54 . 8 LYS HD3 H 1.07 . 1 55 . 8 LYS HE2 H 3.11 . 1 56 . 8 LYS HE3 H 3.11 . 1 57 . 9 GLU N N 121.7 . 1 58 . 9 GLU H H 9.96 . 1 59 . 9 GLU HA H 4.17 . 1 60 . 9 GLU HB2 H 2.11 . 1 61 . 9 GLU HB3 H 2.11 . 1 62 . 9 GLU HG2 H 2.43 . 2 63 . 9 GLU HG3 H 2.35 . 2 64 . 10 THR N N 114.1 . 1 65 . 10 THR H H 8.52 . 1 66 . 10 THR HA H 4.30 . 1 67 . 10 THR HB H 4.78 . 1 68 . 10 THR HG2 H 1.28 . 1 69 . 11 CYS HA H 4.83 . 1 70 . 11 CYS HB2 H 3.61 . 1 71 . 11 CYS HB3 H 3.28 . 1 72 . 12 PRO HA H 4.45 . 1 73 . 12 PRO HB2 H 1.68 . 1 74 . 12 PRO HB3 H 2.35 . 1 75 . 12 PRO HG2 H 2.03 . 2 76 . 12 PRO HG3 H 2.02 . 2 77 . 12 PRO HD2 H 3.96 . 2 78 . 12 PRO HD3 H 3.66 . 2 79 . 13 TYR H H 9.41 . 1 80 . 13 TYR HA H 4.12 . 1 81 . 13 TYR HB2 H 3.18 . 1 82 . 13 TYR HB3 H 3.02 . 1 83 . 13 TYR HD1 H 7.02 . 1 84 . 13 TYR HD2 H 7.02 . 1 85 . 13 TYR HE1 H 6.92 . 1 86 . 13 TYR HE2 H 6.92 . 1 87 . 14 CYS N N 118.8 . 1 88 . 14 CYS H H 8.81 . 1 89 . 14 CYS HA H 4.30 . 1 90 . 14 CYS HB2 H 2.72 . 1 91 . 14 CYS HB3 H 2.72 . 1 92 . 15 HIS H H 7.82 . 1 93 . 15 HIS HA H 4.28 . 1 94 . 15 HIS HB2 H 3.32 . 2 95 . 15 HIS HB3 H 3.28 . 2 96 . 15 HIS HD2 H 7.19 . 1 97 . 15 HIS HE1 H 7.92 . 1 98 . 16 ARG N N 118.1 . 1 99 . 16 ARG H H 8.01 . 1 100 . 16 ARG HA H 4.02 . 1 101 . 16 ARG HB2 H 1.21 . 1 102 . 16 ARG HB3 H 1.44 . 1 103 . 16 ARG HG2 H 1.68 . 2 104 . 16 ARG HG3 H 1.57 . 2 105 . 16 ARG HD2 H 2.76 . 1 106 . 16 ARG HD3 H 2.76 . 1 107 . 17 ALA N N 121.3 . 1 108 . 17 ALA H H 8.06 . 1 109 . 17 ALA HA H 4.15 . 1 110 . 17 ALA HB H 1.52 . 1 111 . 18 LYS N N 116.4 . 1 112 . 18 LYS H H 7.81 . 1 113 . 18 LYS HA H 3.30 . 1 114 . 18 LYS HB2 H 1.91 . 2 115 . 18 LYS HB3 H 1.89 . 2 116 . 18 LYS HG2 H 1.53 . 2 117 . 18 LYS HG3 H 0.84 . 2 118 . 18 LYS HD2 H 1.70 . 2 119 . 18 LYS HD3 H 1.67 . 2 120 . 18 LYS HE2 H 2.98 . 2 121 . 18 LYS HE3 H 2.71 . 2 122 . 19 ALA N N 121.0 . 1 123 . 19 ALA H H 8.25 . 1 124 . 19 ALA HA H 4.20 . 1 125 . 19 ALA HB H 1.48 . 1 126 . 20 LEU N N 121.3 . 1 127 . 20 LEU H H 7.88 . 1 128 . 20 LEU HA H 4.26 . 1 129 . 20 LEU HB2 H 2.05 . 2 130 . 20 LEU HB3 H 1.99 . 2 131 . 20 LEU HG H 1.63 . 1 132 . 20 LEU HD1 H 1.03 . 1 133 . 20 LEU HD2 H 0.76 . 1 134 . 21 LEU N N 119.1 . 1 135 . 21 LEU H H 7.92 . 1 136 . 21 LEU HA H 3.88 . 1 137 . 21 LEU HB2 H 1.93 . 1 138 . 21 LEU HB3 H 1.38 . 1 139 . 21 LEU HG H 1.80 . 1 140 . 21 LEU HD1 H 0.44 . 1 141 . 21 LEU HD2 H 0.78 . 1 142 . 22 SER N N 115.6 . 1 143 . 22 SER H H 9.25 . 1 144 . 22 SER HA H 4.55 . 1 145 . 22 SER HB2 H 4.15 . 1 146 . 22 SER HB3 H 4.15 . 1 147 . 23 SER N N 119.5 . 1 148 . 23 SER H H 8.45 . 1 149 . 23 SER HA H 4.43 . 1 150 . 23 SER HB2 H 4.20 . 2 151 . 23 SER HB3 H 4.17 . 2 152 . 24 LYS N N 119.5 . 1 153 . 24 LYS H H 7.47 . 1 154 . 24 LYS HA H 4.48 . 1 155 . 24 LYS HB2 H 2.03 . 1 156 . 24 LYS HB3 H 2.14 . 1 157 . 24 LYS HG2 H 1.38 . 1 158 . 24 LYS HG3 H 1.73 . 1 159 . 24 LYS HD2 H 1.62 . 1 160 . 24 LYS HD3 H 1.62 . 1 161 . 24 LYS HE2 H 2.74 . 1 162 . 24 LYS HE3 H 2.74 . 1 163 . 25 GLY N N 107.1 . 1 164 . 25 GLY H H 8.15 . 1 165 . 25 GLY HA3 H 4.15 . 2 166 . 25 GLY HA2 H 3.91 . 2 167 . 26 VAL N N 116.7 . 1 168 . 26 VAL H H 7.38 . 1 169 . 26 VAL HA H 4.34 . 1 170 . 26 VAL HB H 2.23 . 1 171 . 26 VAL HG1 H 1.03 . 1 172 . 26 VAL HG2 H 1.08 . 1 173 . 27 SER N N 121.1 . 1 174 . 27 SER H H 8.57 . 1 175 . 27 SER HA H 4.46 . 1 176 . 27 SER HB2 H 3.84 . 1 177 . 27 SER HB3 H 3.84 . 1 178 . 28 PHE N N 117.4 . 1 179 . 28 PHE H H 7.53 . 1 180 . 28 PHE HA H 5.19 . 1 181 . 28 PHE HB2 H 2.75 . 1 182 . 28 PHE HB3 H 2.78 . 1 183 . 28 PHE HD1 H 6.87 . 1 184 . 28 PHE HD2 H 6.87 . 1 185 . 28 PHE HE1 H 7.39 . 1 186 . 28 PHE HE2 H 7.39 . 1 187 . 28 PHE HZ H 7.38 . 1 188 . 29 GLN N N 120.5 . 1 189 . 29 GLN H H 9.13 . 1 190 . 29 GLN HA H 4.66 . 1 191 . 29 GLN HB2 H 2.13 . 1 192 . 29 GLN HB3 H 2.06 . 1 193 . 29 GLN HG2 H 2.33 . 1 194 . 29 GLN HG3 H 2.33 . 1 195 . 29 GLN NE2 N 111.9 . 1 196 . 29 GLN HE21 H 7.49 . 1 197 . 29 GLN HE22 H 6.94 . 1 198 . 30 GLU N N 127.9 . 1 199 . 30 GLU H H 9.09 . 1 200 . 30 GLU HA H 4.96 . 1 201 . 30 GLU HB2 H 1.95 . 1 202 . 30 GLU HB3 H 1.95 . 1 203 . 30 GLU HG2 H 2.16 . 1 204 . 30 GLU HG3 H 2.16 . 1 205 . 31 LEU N N 129.3 . 1 206 . 31 LEU H H 9.08 . 1 207 . 31 LEU HA H 4.91 . 1 208 . 31 LEU HB2 H 1.20 . 1 209 . 31 LEU HB3 H 0.87 . 1 210 . 31 LEU HG H 1.25 . 1 211 . 31 LEU HD1 H 0.29 . 1 212 . 31 LEU HD2 H 0.70 . 1 213 . 32 PRO HA H 4.88 . 1 214 . 32 PRO HB2 H 2.11 . 1 215 . 32 PRO HB3 H 2.38 . 1 216 . 32 PRO HG2 H 2.20 . 2 217 . 32 PRO HG3 H 1.86 . 2 218 . 32 PRO HD2 H 3.82 . 2 219 . 32 PRO HD3 H 3.67 . 2 220 . 33 ILE N N 113.0 . 1 221 . 33 ILE H H 8.91 . 1 222 . 33 ILE HA H 4.79 . 1 223 . 33 ILE HB H 2.19 . 1 224 . 33 ILE HG2 H 1.20 . 1 225 . 33 ILE HG12 H 1.38 . 2 226 . 33 ILE HG13 H 1.25 . 2 227 . 33 ILE HD1 H 0.89 . 1 228 . 34 ASP N N 122.3 . 1 229 . 34 ASP H H 8.64 . 1 230 . 34 ASP HA H 4.41 . 1 231 . 34 ASP HB2 H 2.66 . 2 232 . 34 ASP HB3 H 2.59 . 2 233 . 35 GLY N N 110.4 . 1 234 . 35 GLY H H 9.05 . 1 235 . 35 GLY HA3 H 4.01 . 1 236 . 35 GLY HA2 H 4.01 . 1 237 . 36 ASN N N 118.1 . 1 238 . 36 ASN H H 7.63 . 1 239 . 36 ASN HA H 5.02 . 1 240 . 36 ASN HB2 H 3.04 . 2 241 . 36 ASN HB3 H 2.50 . 2 242 . 36 ASN ND2 N 112.4 . 1 243 . 36 ASN HD21 H 7.94 . 1 244 . 36 ASN HD22 H 7.08 . 1 245 . 37 ALA N N 127.2 . 1 246 . 37 ALA H H 8.85 . 1 247 . 37 ALA HA H 4.15 . 1 248 . 37 ALA HB H 1.55 . 1 249 . 38 ALA N N 119.8 . 1 250 . 38 ALA H H 8.44 . 1 251 . 38 ALA HA H 4.26 . 1 252 . 38 ALA HB H 1.56 . 1 253 . 39 LYS N N 120.1 . 1 254 . 39 LYS H H 7.85 . 1 255 . 39 LYS HA H 4.25 . 1 256 . 39 LYS HB2 H 1.92 . 1 257 . 39 LYS HB3 H 1.92 . 1 258 . 39 LYS HG2 H 1.73 . 2 259 . 39 LYS HG3 H 1.59 . 2 260 . 39 LYS HD2 H 1.75 . 1 261 . 39 LYS HD3 H 1.75 . 1 262 . 39 LYS HE2 H 3.04 . 1 263 . 39 LYS HE3 H 3.04 . 1 264 . 40 ARG N N 119.7 . 1 265 . 40 ARG H H 8.06 . 1 266 . 40 ARG HA H 3.92 . 1 267 . 40 ARG HB2 H 2.03 . 1 268 . 40 ARG HB3 H 2.13 . 1 269 . 40 ARG HG2 H 1.55 . 1 270 . 40 ARG HG3 H 1.55 . 1 271 . 40 ARG HD2 H 3.30 . 1 272 . 40 ARG HD3 H 3.30 . 1 273 . 41 GLU N N 117.4 . 1 274 . 41 GLU H H 8.34 . 1 275 . 41 GLU HA H 3.96 . 1 276 . 41 GLU HB2 H 2.15 . 1 277 . 41 GLU HB3 H 2.15 . 1 278 . 41 GLU HG2 H 2.43 . 2 279 . 41 GLU HG3 H 2.34 . 2 280 . 42 GLU N N 120.8 . 1 281 . 42 GLU H H 8.00 . 1 282 . 42 GLU HA H 3.99 . 1 283 . 42 GLU HB2 H 2.31 . 1 284 . 42 GLU HB3 H 2.40 . 1 285 . 42 GLU HG2 H 2.28 . 2 286 . 42 GLU HG3 H 2.03 . 2 287 . 43 MET N N 119.4 . 1 288 . 43 MET H H 8.07 . 1 289 . 43 MET HA H 2.93 . 1 290 . 43 MET HB2 H 1.40 . 1 291 . 43 MET HB3 H 2.25 . 1 292 . 43 MET HG2 H 1.68 . 2 293 . 43 MET HG3 H 1.51 . 2 294 . 43 MET HE H 1.74 . 1 295 . 44 ILE N N 123.8 . 1 296 . 44 ILE H H 8.38 . 1 297 . 44 ILE HA H 3.95 . 1 298 . 44 ILE HB H 1.78 . 1 299 . 44 ILE HG2 H 0.75 . 1 300 . 44 ILE HG12 H 1.53 . 2 301 . 44 ILE HG13 H 1.02 . 2 302 . 44 ILE HD1 H 0.80 . 1 303 . 45 LYS N N 122.1 . 1 304 . 45 LYS H H 8.50 . 1 305 . 45 LYS HA H 3.99 . 1 306 . 45 LYS HB2 H 1.95 . 1 307 . 45 LYS HB3 H 1.95 . 1 308 . 45 LYS HG2 H 1.56 . 2 309 . 45 LYS HG3 H 1.43 . 2 310 . 45 LYS HD2 H 1.71 . 1 311 . 45 LYS HD3 H 1.71 . 1 312 . 45 LYS HE2 H 2.99 . 1 313 . 45 LYS HE3 H 2.99 . 1 314 . 46 ARG N N 114.7 . 1 315 . 46 ARG H H 8.30 . 1 316 . 46 ARG HA H 4.14 . 1 317 . 46 ARG HB2 H 1.98 . 2 318 . 46 ARG HB3 H 1.49 . 2 319 . 46 ARG HG2 H 2.01 . 2 320 . 46 ARG HG3 H 1.46 . 2 321 . 46 ARG HD2 H 3.03 . 2 322 . 46 ARG HD3 H 2.60 . 2 323 . 46 ARG NE N 82.4 . 1 324 . 46 ARG HE H 6.28 . 1 325 . 47 SER N N 110.3 . 1 326 . 47 SER H H 8.38 . 1 327 . 47 SER HA H 3.76 . 1 328 . 47 SER HB2 H 3.41 . 1 329 . 47 SER HB3 H 3.48 . 1 330 . 47 SER HG H 4.72 . 1 331 . 48 GLY N N 112.4 . 1 332 . 48 GLY H H 8.64 . 1 333 . 48 GLY HA3 H 3.89 . 1 334 . 48 GLY HA2 H 4.17 . 1 335 . 49 ARG N N 119.7 . 1 336 . 49 ARG H H 8.43 . 1 337 . 49 ARG HA H 4.83 . 1 338 . 49 ARG HB2 H 1.59 . 1 339 . 49 ARG HB3 H 1.99 . 1 340 . 49 ARG HG2 H 1.68 . 1 341 . 49 ARG HG3 H 1.75 . 1 342 . 49 ARG HD2 H 3.35 . 2 343 . 49 ARG HD3 H 3.26 . 2 344 . 50 THR N N 101.7 . 1 345 . 50 THR H H 8.15 . 1 346 . 50 THR HA H 4.30 . 1 347 . 50 THR HB H 4.42 . 1 348 . 50 THR HG2 H 1.12 . 1 349 . 51 THR N N 111.3 . 1 350 . 51 THR H H 7.11 . 1 351 . 51 THR HA H 4.61 . 1 352 . 51 THR HB H 4.34 . 1 353 . 51 THR HG2 H 1.27 . 1 354 . 52 VAL N N 111.3 . 1 355 . 52 VAL H H 8.06 . 1 356 . 52 VAL HA H 4.54 . 1 357 . 52 VAL HB H 2.11 . 1 358 . 52 VAL HG1 H 0.96 . 1 359 . 52 VAL HG2 H 1.10 . 1 360 . 53 PRO HA H 5.46 . 1 361 . 53 PRO HB2 H 2.53 . 2 362 . 53 PRO HB3 H 1.93 . 2 363 . 53 PRO HG2 H 1.94 . 1 364 . 53 PRO HG3 H 1.94 . 1 365 . 53 PRO HD2 H 4.21 . 2 366 . 53 PRO HD3 H 3.38 . 2 367 . 54 GLN N N 113.0 . 1 368 . 54 GLN H H 7.38 . 1 369 . 54 GLN HA H 4.97 . 1 370 . 54 GLN HB2 H 1.95 . 1 371 . 54 GLN HB3 H 2.16 . 1 372 . 54 GLN HG2 H 3.12 . 2 373 . 54 GLN HG3 H 2.25 . 2 374 . 54 GLN NE2 N 114.1 . 1 375 . 54 GLN HE21 H 7.75 . 1 376 . 54 GLN HE22 H 6.45 . 1 377 . 55 ILE N N 123.3 . 1 378 . 55 ILE H H 9.13 . 1 379 . 55 ILE HA H 5.22 . 1 380 . 55 ILE HB H 1.54 . 1 381 . 55 ILE HG2 H 0.81 . 1 382 . 55 ILE HG12 H 1.53 . 2 383 . 55 ILE HG13 H 0.99 . 2 384 . 55 ILE HD1 H 0.79 . 1 385 . 56 PHE N N 126.9 . 1 386 . 56 PHE H H 9.51 . 1 387 . 56 PHE HA H 5.47 . 1 388 . 56 PHE HB2 H 3.15 . 1 389 . 56 PHE HB3 H 2.74 . 1 390 . 56 PHE HD1 H 7.17 . 1 391 . 56 PHE HD2 H 7.17 . 1 392 . 56 PHE HE1 H 7.27 . 1 393 . 56 PHE HE2 H 7.27 . 1 394 . 56 PHE HZ H 6.59 . 1 395 . 57 ILE N N 119.6 . 1 396 . 57 ILE H H 8.91 . 1 397 . 57 ILE HA H 4.79 . 1 398 . 57 ILE HB H 1.66 . 1 399 . 57 ILE HG2 H 0.82 . 1 400 . 57 ILE HG12 H 1.53 . 2 401 . 57 ILE HG13 H 1.00 . 2 402 . 57 ILE HD1 H 0.67 . 1 403 . 58 ASP N N 131.3 . 1 404 . 58 ASP H H 9.98 . 1 405 . 58 ASP HA H 4.59 . 1 406 . 58 ASP HB2 H 2.79 . 1 407 . 58 ASP HB3 H 3.07 . 1 408 . 59 ALA N N 113.8 . 1 409 . 59 ALA H H 9.42 . 1 410 . 59 ALA HA H 3.78 . 1 411 . 59 ALA HB H 1.69 . 1 412 . 60 GLN N N 120.8 . 1 413 . 60 GLN H H 8.40 . 1 414 . 60 GLN HA H 4.66 . 1 415 . 60 GLN HB2 H 2.24 . 1 416 . 60 GLN HB3 H 2.24 . 1 417 . 60 GLN HG2 H 2.46 . 2 418 . 60 GLN HG3 H 2.40 . 2 419 . 60 GLN NE2 N 111.9 . 1 420 . 60 GLN HE21 H 7.60 . 1 421 . 60 GLN HE22 H 6.91 . 1 422 . 61 HIS N N 126.0 . 1 423 . 61 HIS H H 9.33 . 1 424 . 61 HIS HA H 3.86 . 1 425 . 61 HIS HB2 H 3.02 . 1 426 . 61 HIS HB3 H 3.16 . 1 427 . 61 HIS HD2 H 5.82 . 1 428 . 61 HIS HE1 H 7.56 . 1 429 . 62 ILE N N 128.4 . 1 430 . 62 ILE H H 8.45 . 1 431 . 62 ILE HA H 3.98 . 1 432 . 62 ILE HB H 1.64 . 1 433 . 62 ILE HG2 H 0.60 . 1 434 . 62 ILE HG12 H 1.53 . 2 435 . 62 ILE HG13 H 1.00 . 2 436 . 62 ILE HD1 H 0.56 . 1 437 . 63 GLY N N 102.7 . 1 438 . 63 GLY H H 6.30 . 1 439 . 63 GLY HA3 H 4.72 . 2 440 . 63 GLY HA2 H 3.19 . 2 441 . 64 GLY N N 108.7 . 1 442 . 64 GLY H H 8.98 . 1 443 . 64 GLY HA3 H 4.74 . 1 444 . 64 GLY HA2 H 3.87 . 1 445 . 65 TYR N N 119.2 . 1 446 . 65 TYR H H 8.87 . 1 447 . 65 TYR HA H 3.87 . 1 448 . 65 TYR HB2 H 3.13 . 1 449 . 65 TYR HB3 H 2.77 . 1 450 . 65 TYR HD1 H 6.74 . 1 451 . 65 TYR HD2 H 6.74 . 1 452 . 65 TYR HE1 H 6.60 . 1 453 . 65 TYR HE2 H 6.60 . 1 454 . 66 ASP N N 116.0 . 1 455 . 66 ASP H H 8.44 . 1 456 . 66 ASP HA H 3.97 . 1 457 . 66 ASP HB2 H 2.63 . 1 458 . 66 ASP HB3 H 2.52 . 1 459 . 67 ASP N N 117.4 . 1 460 . 67 ASP H H 7.05 . 1 461 . 67 ASP HA H 4.33 . 1 462 . 67 ASP HB2 H 2.54 . 1 463 . 67 ASP HB3 H 2.66 . 1 464 . 68 LEU N N 122.1 . 1 465 . 68 LEU H H 7.92 . 1 466 . 68 LEU HA H 3.70 . 1 467 . 68 LEU HB2 H 1.25 . 1 468 . 68 LEU HB3 H 1.95 . 1 469 . 68 LEU HG H 1.58 . 1 470 . 68 LEU HD1 H 0.93 . 1 471 . 68 LEU HD2 H 0.86 . 1 472 . 69 TYR N N 118.4 . 1 473 . 69 TYR H H 8.69 . 1 474 . 69 TYR HA H 3.65 . 1 475 . 69 TYR HB2 H 2.29 . 1 476 . 69 TYR HB3 H 2.63 . 1 477 . 69 TYR HD1 H 7.01 . 1 478 . 69 TYR HD2 H 7.01 . 1 479 . 69 TYR HE1 H 6.83 . 1 480 . 69 TYR HE2 H 6.83 . 1 481 . 70 ALA N N 120.3 . 1 482 . 70 ALA H H 7.96 . 1 483 . 70 ALA HA H 3.97 . 1 484 . 70 ALA HB H 1.50 . 1 485 . 71 LEU N N 118.7 . 1 486 . 71 LEU H H 7.69 . 1 487 . 71 LEU HA H 3.98 . 1 488 . 71 LEU HB2 H 1.62 . 1 489 . 71 LEU HB3 H 1.78 . 1 490 . 71 LEU HG H 1.21 . 1 491 . 71 LEU HD1 H 0.87 . 1 492 . 71 LEU HD2 H 0.81 . 1 493 . 72 ASP N N 118.3 . 1 494 . 72 ASP H H 8.00 . 1 495 . 72 ASP HA H 4.41 . 1 496 . 72 ASP HB2 H 2.50 . 1 497 . 72 ASP HB3 H 2.50 . 1 498 . 73 ALA N N 122.1 . 1 499 . 73 ALA H H 8.57 . 1 500 . 73 ALA HA H 3.98 . 1 501 . 73 ALA HB H 1.25 . 1 502 . 74 ARG N N 112.4 . 1 503 . 74 ARG H H 7.29 . 1 504 . 74 ARG HA H 4.67 . 1 505 . 74 ARG HB2 H 2.06 . 2 506 . 74 ARG HB3 H 1.85 . 2 507 . 74 ARG HG2 H 2.02 . 2 508 . 74 ARG HG3 H 1.58 . 2 509 . 74 ARG HD2 H 3.18 . 1 510 . 74 ARG HD3 H 3.18 . 1 511 . 74 ARG NE N 84.7 . 1 512 . 74 ARG HE H 7.38 . 1 513 . 75 GLY N N 110.4 . 1 514 . 75 GLY H H 8.21 . 1 515 . 75 GLY HA3 H 4.16 . 2 516 . 75 GLY HA2 H 4.07 . 2 517 . 76 GLY N N 104.0 . 1 518 . 76 GLY H H 8.43 . 1 519 . 76 GLY HA3 H 4.27 . 2 520 . 76 GLY HA2 H 3.47 . 2 521 . 77 LEU N N 121.7 . 1 522 . 77 LEU H H 8.01 . 1 523 . 77 LEU HA H 4.47 . 1 524 . 77 LEU HB2 H 1.05 . 1 525 . 77 LEU HB3 H 2.10 . 1 526 . 77 LEU HG H 1.48 . 1 527 . 77 LEU HD1 H 0.84 . 2 528 . 77 LEU HD2 H 0.79 . 2 529 . 78 ASP N N 119.6 . 1 530 . 78 ASP H H 8.57 . 1 531 . 78 ASP HA H 4.40 . 1 532 . 78 ASP HB2 H 2.64 . 1 533 . 78 ASP HB3 H 2.64 . 1 534 . 79 PRO HA H 4.37 . 1 535 . 79 PRO HB2 H 2.41 . 2 536 . 79 PRO HB3 H 1.77 . 2 537 . 79 PRO HG2 H 2.04 . 1 538 . 79 PRO HG3 H 2.04 . 1 539 . 79 PRO HD2 H 3.36 . 1 540 . 79 PRO HD3 H 3.59 . 1 541 . 80 LEU N N 113.6 . 1 542 . 80 LEU H H 7.49 . 1 543 . 80 LEU HA H 4.29 . 1 544 . 80 LEU HB2 H 2.02 . 1 545 . 80 LEU HB3 H 1.56 . 1 546 . 80 LEU HG H 1.92 . 1 547 . 80 LEU HD1 H 0.95 . 2 548 . 80 LEU HD2 H 0.88 . 2 549 . 81 LEU N N 116.1 . 1 550 . 81 LEU H H 7.46 . 1 551 . 81 LEU HA H 4.29 . 1 552 . 81 LEU HB2 H 1.87 . 1 553 . 81 LEU HB3 H 1.69 . 1 554 . 81 LEU HG H 1.84 . 1 555 . 81 LEU HD1 H 0.85 . 2 556 . 81 LEU HD2 H 0.74 . 2 557 . 82 LYS N N 124.6 . 1 558 . 82 LYS H H 7.14 . 1 559 . 82 LYS HA H 4.11 . 1 560 . 82 LYS HB2 H 1.87 . 2 561 . 82 LYS HB3 H 1.79 . 2 562 . 82 LYS HG2 H 1.47 . 1 563 . 82 LYS HG3 H 1.47 . 1 564 . 82 LYS HD2 H 1.70 . 1 565 . 82 LYS HD3 H 1.70 . 1 566 . 82 LYS HE2 H 3.03 . 1 567 . 82 LYS HE3 H 3.03 . 1 stop_ save_