data_6335 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Near complete chemical shift assignments for the zinc-bound redox switch domain of the E. coli Hsp33 ; _BMRB_accession_number 6335 _BMRB_flat_file_name bmr6335.str _Entry_type original _Submission_date 2004-10-04 _Accession_date 2004-10-04 _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 Won Hyung-Sik . . 2 Low Lieh Y. . 3 Guzman Roberto . . 4 Martinez-Yamout Maria . . 5 Jakob Ursula . . 6 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" 336 "13C chemical shifts" 242 "15N chemical shifts" 63 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-10-12 original author . stop_ _Original_release_date 2004-10-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The zinc-dependent redox switch domain of the chaperone Hsp33 has a novel fold' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15328602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Won Hyung-Sik . . 2 Low Lieh Y. . 3 'De Guzman' Roberto . . 4 Martinez-Yamout Maria . . 5 Jakob Ursula . . 6 Dyson H. Jane . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 341 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 893 _Page_last 899 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_system_Hsp33 _Saveframe_category molecular_system _Mol_system_name 'redox-switch domain of Hsp33' _Abbreviation_common Hsp33 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Hsp33-RSD $Hsp33-RSD 'ZINC (II) ION' $ZN stop_ _System_molecular_weight . _System_physical_state reduced _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'other bound and free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Hsp33-RSD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'E. coli heat shock protein 33 redox-switch domain' _Abbreviation_common Hsp33-RSD _Molecular_mass . _Mol_thiol_state 'other bound and free' _Details ; The first Met is a cloning artifact. Residues from D2 to S62 correspond to the residues D227 to S287 of the intact E. coli Hsp33. ; ############################## # Polymer residue sequence # ############################## _Residue_count 62 _Mol_residue_sequence ; MDVEFKCTCSRERCADALKT LPDEEVDSILAEDGEIDMHC DYCGNHYLFNAMDIAEIRNN AS ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 VAL 4 GLU 5 PHE 6 LYS 7 CYS 8 THR 9 CYS 10 SER 11 ARG 12 GLU 13 ARG 14 CYS 15 ALA 16 ASP 17 ALA 18 LEU 19 LYS 20 THR 21 LEU 22 PRO 23 ASP 24 GLU 25 GLU 26 VAL 27 ASP 28 SER 29 ILE 30 LEU 31 ALA 32 GLU 33 ASP 34 GLY 35 GLU 36 ILE 37 ASP 38 MET 39 HIS 40 CYS 41 ASP 42 TYR 43 CYS 44 GLY 45 ASN 46 HIS 47 TYR 48 LEU 49 PHE 50 ASN 51 ALA 52 MET 53 ASP 54 ILE 55 ALA 56 GLU 57 ILE 58 ARG 59 ASN 60 ASN 61 ALA 62 SER stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 SWISS-PROT Q31VN3 '33 kDa chaperonin (Heat shock protein 33 homolog) (HSP33)' 98.39 292 98.36 98.36 7.39e-29 SWISS-PROT Q0SZR7 '33 kDa chaperonin (Heat shock protein 33 homolog) (HSP33)' 98.39 289 100.00 100.00 1.51e-29 SWISS-PROT P0A6Y7 '33 kDa chaperonin (Heat shock protein 33) (HSP33)' 98.39 292 100.00 100.00 1.24e-29 SWISS-PROT P0A6Y6 '33 kDa chaperonin (Heat shock protein 33) (HSP33)' 98.39 292 100.00 100.00 1.24e-29 SWISS-PROT P0A6Y5 '33 kDa chaperonin (Heat shock protein 33) (HSP33)' 98.39 292 100.00 100.00 1.24e-29 REF NP_709173 'Hsp33-like chaperonin [Shigella flexneri 2a str. 301]' 98.39 289 100.00 100.00 1.51e-29 REF NP_417860 'heat shock protein Hsp33 [Escherichia coli str. K-12 substr. MG1655]' 98.39 292 100.00 100.00 1.24e-29 REF NP_312270 'Hsp33-like chaperonin [Escherichia coli O157:H7 str. Sakai]' 98.39 292 100.00 100.00 1.24e-29 REF NP_289940 'Hsp33-like chaperonin [Escherichia coli O157:H7 EDL933]' 98.39 292 100.00 100.00 1.24e-29 REF AP_004389 'heat shock protein Hsp33 [Escherichia coli W3110]' 98.39 292 100.00 100.00 1.24e-29 PIR A86005 'hypothetical protein yrfI [imported] - Escherichia coli (strain O157:H7, substrain EDL933)' 98.39 294 100.00 100.00 1.20e-29 GenBank AAN82610 'Heat shock protein 33 [Escherichia coli CFT073]' 98.39 294 100.00 100.00 1.20e-29 GenBank AAN44880 'orf, conserved hypothetical protein [Shigella flexneri 2a str. 301]' 98.39 289 100.00 100.00 1.51e-29 GenBank AAG58501 'orf, hypothetical protein [Escherichia coli O157:H7 EDL933]' 98.39 294 100.00 100.00 1.20e-29 GenBank AAC76426 'heat shock protein Hsp33 [Escherichia coli str. K-12 substr. MG1655]' 98.39 292 100.00 100.00 1.24e-29 GenBank AAA58198 'ORF_o294 [Escherichia coli]' 98.39 294 100.00 100.00 1.20e-29 DBJ BAE77890 'heat shock protein Hsp33 [Escherichia coli W3110]' 98.39 292 100.00 100.00 1.24e-29 DBJ BAB37666 'redox-responsive chaperonin Hsp33 [Escherichia coli O157:H7 str. Sakai]' 98.39 292 100.00 100.00 1.24e-29 PDB 1XJH 'Nmr Structure Of The Redox Switch Domain Of The E. Coli Hsp33' 100.00 62 100.00 100.00 1.61e-28 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Jun 10 14:23:33 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Hsp33-RSD 'E. coli' 562 Bacteria . 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 $Hsp33-RSD 'recombinant technology' . . . . . 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 $Hsp33-RSD . mM 1.0 2.0 '[U-99% 13C; U-99% 15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Hsp33-RSD . mM 1.0 2.0 '[U-99% 15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 601 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.2 n/a temperature 298 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 _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation 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 $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Hsp33-RSD _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 ASP HA H 4.86 . 1 2 . 2 ASP HB2 H 2.72 . 2 3 . 2 ASP HB3 H 2.56 . 2 4 . 2 ASP C C 175.81 . 1 5 . 2 ASP CA C 54.38 . 1 6 . 2 ASP CB C 41.43 . 1 7 . 3 VAL H H 8.27 . 1 8 . 3 VAL HA H 4.15 . 1 9 . 3 VAL HB H 1.91 . 1 10 . 3 VAL HG1 H 0.81 . 2 11 . 3 VAL HG2 H 0.82 . 2 12 . 3 VAL C C 175.60 . 1 13 . 3 VAL CA C 61.93 . 1 14 . 3 VAL CB C 33.04 . 1 15 . 3 VAL CG1 C 21.54 . 2 16 . 3 VAL CG2 C 20.65 . 2 17 . 3 VAL N N 120.05 . 1 18 . 4 GLU H H 8.38 . 1 19 . 4 GLU HA H 4.23 . 1 20 . 4 GLU HB2 H 1.90 . 2 21 . 4 GLU HB3 H 1.83 . 2 22 . 4 GLU HG2 H 2.16 . 2 23 . 4 GLU HG3 H 2.05 . 2 24 . 4 GLU C C 175.75 . 1 25 . 4 GLU CA C 56.22 . 1 26 . 4 GLU CB C 30.50 . 1 27 . 4 GLU CG C 36.14 . 1 28 . 4 GLU N N 124.08 . 1 29 . 5 PHE H H 8.31 . 1 30 . 5 PHE HA H 4.56 . 1 31 . 5 PHE HB2 H 2.99 . 1 32 . 5 PHE HB3 H 2.99 . 1 33 . 5 PHE HD1 H 7.19 . 1 34 . 5 PHE HD2 H 7.19 . 1 35 . 5 PHE HE1 H 7.27 . 1 36 . 5 PHE HE2 H 7.27 . 1 37 . 5 PHE HZ H 7.09 . 1 38 . 5 PHE C C 174.83 . 1 39 . 5 PHE CA C 57.77 . 1 40 . 5 PHE CB C 39.76 . 1 41 . 5 PHE CD1 C 130.76 . 3 42 . 5 PHE N N 122.85 . 1 43 . 6 LYS H H 8.04 . 1 44 . 6 LYS HA H 4.25 . 1 45 . 6 LYS HB2 H 1.73 . 2 46 . 6 LYS HB3 H 1.62 . 2 47 . 6 LYS HG2 H 1.36 . 1 48 . 6 LYS HG3 H 1.36 . 1 49 . 6 LYS HD2 H 1.62 . 1 50 . 6 LYS HD3 H 1.62 . 1 51 . 6 LYS HE2 H 2.93 . 1 52 . 6 LYS HE3 H 2.93 . 1 53 . 6 LYS C C 174.55 . 1 54 . 6 LYS CA C 55.37 . 1 55 . 6 LYS CB C 33.44 . 1 56 . 6 LYS CG C 24.71 . 1 57 . 6 LYS CD C 28.82 . 1 58 . 6 LYS CE C 41.91 . 1 59 . 6 LYS N N 125.69 . 1 60 . 7 CYS H H 8.38 . 1 61 . 7 CYS HA H 4.18 . 1 62 . 7 CYS HB2 H 3.05 . 2 63 . 7 CYS HB3 H 2.89 . 2 64 . 7 CYS C C 175.75 . 1 65 . 7 CYS CA C 59.15 . 1 66 . 7 CYS CB C 30.75 . 1 67 . 7 CYS N N 125.60 . 1 68 . 8 THR H H 8.74 . 1 69 . 8 THR HA H 4.38 . 1 70 . 8 THR HB H 4.38 . 1 71 . 8 THR HG2 H 1.15 . 1 72 . 8 THR C C 175.30 . 1 73 . 8 THR CA C 61.45 . 1 74 . 8 THR CB C 69.45 . 1 75 . 8 THR CG2 C 22.18 . 1 76 . 8 THR N N 114.74 . 1 77 . 9 CYS H H 8.08 . 1 78 . 9 CYS HA H 4.39 . 1 79 . 9 CYS HB2 H 3.23 . 2 80 . 9 CYS HB3 H 2.97 . 2 81 . 9 CYS C C 173.85 . 1 82 . 9 CYS CA C 57.49 . 1 83 . 9 CYS CB C 31.45 . 1 84 . 9 CYS N N 123.52 . 1 85 . 10 SER H H 7.39 . 1 86 . 10 SER HA H 4.46 . 1 87 . 10 SER HB2 H 4.17 . 2 88 . 10 SER HB3 H 4.06 . 2 89 . 10 SER C C 173.89 . 1 90 . 10 SER CA C 57.17 . 1 91 . 10 SER CB C 65.68 . 1 92 . 10 SER N N 107.92 . 1 93 . 11 ARG H H 9.19 . 1 94 . 11 ARG HA H 3.21 . 1 95 . 11 ARG HB2 H 1.81 . 2 96 . 11 ARG HB3 H 1.73 . 2 97 . 11 ARG HG2 H 1.62 . 2 98 . 11 ARG HG3 H 1.60 . 2 99 . 11 ARG HD2 H 3.24 . 2 100 . 11 ARG HD3 H 3.15 . 2 101 . 11 ARG C C 178.04 . 1 102 . 11 ARG CA C 60.40 . 1 103 . 11 ARG CB C 29.51 . 1 104 . 11 ARG CG C 28.58 . 1 105 . 11 ARG CD C 42.85 . 1 106 . 11 ARG N N 123.66 . 1 107 . 12 GLU H H 8.69 . 1 108 . 12 GLU HA H 3.94 . 1 109 . 12 GLU HB2 H 1.98 . 2 110 . 12 GLU HB3 H 1.89 . 2 111 . 12 GLU HG2 H 2.37 . 2 112 . 12 GLU HG3 H 2.21 . 2 113 . 12 GLU C C 178.78 . 1 114 . 12 GLU CA C 60.19 . 1 115 . 12 GLU CB C 28.65 . 1 116 . 12 GLU CG C 37.08 . 1 117 . 12 GLU N N 118.07 . 1 118 . 13 ARG H H 7.90 . 1 119 . 13 ARG HA H 4.07 . 1 120 . 13 ARG HB2 H 1.75 . 2 121 . 13 ARG HB3 H 1.73 . 2 122 . 13 ARG HG2 H 1.65 . 2 123 . 13 ARG HG3 H 1.56 . 2 124 . 13 ARG HD2 H 3.16 . 2 125 . 13 ARG HD3 H 3.11 . 2 126 . 13 ARG C C 180.51 . 1 127 . 13 ARG CA C 59.01 . 1 128 . 13 ARG CB C 29.87 . 1 129 . 13 ARG CG C 27.96 . 1 130 . 13 ARG CD C 43.33 . 1 131 . 13 ARG N N 120.12 . 1 132 . 14 CYS H H 7.68 . 1 133 . 14 CYS HA H 3.97 . 1 134 . 14 CYS HB2 H 3.09 . 1 135 . 14 CYS HB3 H 3.09 . 1 136 . 14 CYS C C 175.80 . 1 137 . 14 CYS CA C 63.72 . 1 138 . 14 CYS CB C 26.64 . 1 139 . 14 CYS N N 119.05 . 1 140 . 15 ALA H H 8.50 . 1 141 . 15 ALA HA H 3.48 . 1 142 . 15 ALA HB H 1.48 . 1 143 . 15 ALA C C 179.13 . 1 144 . 15 ALA CA C 55.06 . 1 145 . 15 ALA CB C 17.83 . 1 146 . 15 ALA N N 122.99 . 1 147 . 16 ASP H H 7.69 . 1 148 . 16 ASP HA H 4.23 . 1 149 . 16 ASP HB2 H 2.71 . 2 150 . 16 ASP HB3 H 2.56 . 2 151 . 16 ASP C C 178.92 . 1 152 . 16 ASP CA C 57.10 . 1 153 . 16 ASP CB C 40.41 . 1 154 . 16 ASP N N 116.79 . 1 155 . 17 ALA H H 7.41 . 1 156 . 17 ALA HA H 4.10 . 1 157 . 17 ALA HB H 1.45 . 1 158 . 17 ALA C C 180.81 . 1 159 . 17 ALA CA C 54.46 . 1 160 . 17 ALA CB C 17.64 . 1 161 . 17 ALA N N 122.15 . 1 162 . 18 LEU H H 8.01 . 1 163 . 18 LEU HA H 3.81 . 1 164 . 18 LEU HB2 H 1.66 . 2 165 . 18 LEU HB3 H 1.19 . 2 166 . 18 LEU HG H 1.42 . 1 167 . 18 LEU HD1 H 0.09 . 2 168 . 18 LEU HD2 H 0.55 . 2 169 . 18 LEU C C 179.06 . 1 170 . 18 LEU CA C 57.62 . 1 171 . 18 LEU CB C 41.94 . 1 172 . 18 LEU CG C 27.10 . 1 173 . 18 LEU CD1 C 24.94 . 2 174 . 18 LEU CD2 C 24.28 . 2 175 . 18 LEU N N 120.28 . 1 176 . 19 LYS H H 7.67 . 1 177 . 19 LYS HA H 3.86 . 1 178 . 19 LYS HB2 H 1.93 . 2 179 . 19 LYS HB3 H 1.86 . 2 180 . 19 LYS HG2 H 1.55 . 2 181 . 19 LYS HG3 H 1.41 . 2 182 . 19 LYS HD2 H 1.69 . 1 183 . 19 LYS HD3 H 1.69 . 1 184 . 19 LYS HE2 H 2.97 . 2 185 . 19 LYS HE3 H 2.92 . 2 186 . 19 LYS C C 176.96 . 1 187 . 19 LYS CA C 58.88 . 1 188 . 19 LYS CB C 32.71 . 1 189 . 19 LYS CG C 25.74 . 1 190 . 19 LYS CD C 29.56 . 1 191 . 19 LYS CE C 41.93 . 1 192 . 19 LYS N N 116.98 . 1 193 . 20 THR H H 7.31 . 1 194 . 20 THR HA H 4.29 . 1 195 . 20 THR HB H 4.36 . 1 196 . 20 THR HG2 H 1.22 . 1 197 . 20 THR C C 175.12 . 1 198 . 20 THR CA C 61.85 . 1 199 . 20 THR CB C 69.41 . 1 200 . 20 THR CG2 C 21.79 . 1 201 . 20 THR N N 106.39 . 1 202 . 21 LEU H H 7.02 . 1 203 . 21 LEU HA H 4.47 . 1 204 . 21 LEU HB2 H 1.62 . 2 205 . 21 LEU HB3 H 1.24 . 2 206 . 21 LEU HG H 1.82 . 1 207 . 21 LEU HD1 H 0.79 . 2 208 . 21 LEU HD2 H 0.82 . 2 209 . 21 LEU CA C 53.47 . 1 210 . 21 LEU CB C 41.72 . 1 211 . 21 LEU CG C 26.66 . 1 212 . 21 LEU CD1 C 25.62 . 2 213 . 21 LEU CD2 C 22.94 . 2 214 . 21 LEU N N 123.57 . 1 215 . 22 PRO HA H 4.48 . 1 216 . 22 PRO HB2 H 2.48 . 2 217 . 22 PRO HB3 H 1.89 . 2 218 . 22 PRO HG2 H 2.14 . 2 219 . 22 PRO HG3 H 2.08 . 2 220 . 22 PRO HD2 H 3.94 . 2 221 . 22 PRO HD3 H 3.60 . 2 222 . 22 PRO C C 177.94 . 1 223 . 22 PRO CA C 62.68 . 1 224 . 22 PRO CB C 32.42 . 1 225 . 22 PRO CG C 28.04 . 1 226 . 22 PRO CD C 50.54 . 1 227 . 23 ASP H H 8.73 . 1 228 . 23 ASP HA H 4.07 . 1 229 . 23 ASP HB2 H 2.63 . 2 230 . 23 ASP HB3 H 2.49 . 2 231 . 23 ASP C C 177.77 . 1 232 . 23 ASP CA C 57.88 . 1 233 . 23 ASP CB C 40.19 . 1 234 . 23 ASP N N 124.83 . 1 235 . 24 GLU H H 9.30 . 1 236 . 24 GLU HA H 4.08 . 1 237 . 24 GLU HB2 H 2.00 . 1 238 . 24 GLU HB3 H 2.00 . 1 239 . 24 GLU HG2 H 2.32 . 1 240 . 24 GLU HG3 H 2.32 . 1 241 . 24 GLU C C 179.07 . 1 242 . 24 GLU CA C 59.42 . 1 243 . 24 GLU CB C 28.70 . 1 244 . 24 GLU CG C 36.21 . 1 245 . 24 GLU N N 115.92 . 1 246 . 25 GLU H H 7.20 . 1 247 . 25 GLU HA H 4.17 . 1 248 . 25 GLU HB2 H 2.09 . 2 249 . 25 GLU HB3 H 2.04 . 2 250 . 25 GLU HG2 H 2.27 . 2 251 . 25 GLU HG3 H 2.20 . 2 252 . 25 GLU C C 178.40 . 1 253 . 25 GLU CA C 58.49 . 1 254 . 25 GLU CB C 29.92 . 1 255 . 25 GLU CG C 36.12 . 1 256 . 25 GLU N N 119.59 . 1 257 . 26 VAL H H 7.37 . 1 258 . 26 VAL HA H 3.46 . 1 259 . 26 VAL HB H 1.96 . 1 260 . 26 VAL HG1 H 0.81 . 2 261 . 26 VAL HG2 H 0.85 . 2 262 . 26 VAL C C 177.41 . 1 263 . 26 VAL CA C 66.17 . 1 264 . 26 VAL CB C 32.04 . 1 265 . 26 VAL CG1 C 21.99 . 2 266 . 26 VAL CG2 C 23.98 . 2 267 . 26 VAL N N 119.27 . 1 268 . 27 ASP H H 8.61 . 1 269 . 27 ASP HA H 4.28 . 1 270 . 27 ASP HB2 H 2.61 . 2 271 . 27 ASP HB3 H 2.57 . 2 272 . 27 ASP C C 179.45 . 1 273 . 27 ASP CA C 57.61 . 1 274 . 27 ASP CB C 39.91 . 1 275 . 27 ASP N N 118.71 . 1 276 . 28 SER H H 7.64 . 1 277 . 28 SER HA H 4.24 . 1 278 . 28 SER HB2 H 3.98 . 1 279 . 28 SER HB3 H 3.98 . 1 280 . 28 SER C C 176.49 . 1 281 . 28 SER CA C 61.64 . 1 282 . 28 SER CB C 62.92 . 1 283 . 28 SER N N 115.09 . 1 284 . 29 ILE H H 7.68 . 1 285 . 29 ILE HA H 3.91 . 1 286 . 29 ILE HB H 1.83 . 1 287 . 29 ILE HG12 H 1.78 . 2 288 . 29 ILE HG13 H 1.13 . 2 289 . 29 ILE HG2 H 0.93 . 1 290 . 29 ILE HD1 H 0.82 . 1 291 . 29 ILE C C 178.96 . 1 292 . 29 ILE CA C 64.46 . 1 293 . 29 ILE CB C 38.21 . 1 294 . 29 ILE CG1 C 28.29 . 1 295 . 29 ILE CG2 C 18.64 . 1 296 . 29 ILE CD1 C 13.77 . 1 297 . 29 ILE N N 122.68 . 1 298 . 30 LEU H H 8.19 . 1 299 . 30 LEU HA H 3.83 . 1 300 . 30 LEU HB2 H 1.87 . 2 301 . 30 LEU HB3 H 1.45 . 2 302 . 30 LEU HG H 1.74 . 1 303 . 30 LEU HD1 H 0.72 . 2 304 . 30 LEU HD2 H 0.82 . 2 305 . 30 LEU C C 179.68 . 1 306 . 30 LEU CA C 57.73 . 1 307 . 30 LEU CB C 41.72 . 1 308 . 30 LEU CG C 26.68 . 1 309 . 30 LEU CD1 C 23.08 . 2 310 . 30 LEU CD2 C 25.65 . 2 311 . 30 LEU N N 119.45 . 1 312 . 31 ALA H H 7.96 . 1 313 . 31 ALA HA H 4.10 . 1 314 . 31 ALA HB H 1.49 . 1 315 . 31 ALA C C 178.83 . 1 316 . 31 ALA CA C 54.40 . 1 317 . 31 ALA CB C 18.52 . 1 318 . 31 ALA N N 120.94 . 1 319 . 32 GLU H H 7.62 . 1 320 . 32 GLU HA H 4.27 . 1 321 . 32 GLU HB2 H 2.05 . 2 322 . 32 GLU HB3 H 2.01 . 2 323 . 32 GLU HG2 H 2.32 . 1 324 . 32 GLU HG3 H 2.32 . 1 325 . 32 GLU C C 176.97 . 1 326 . 32 GLU CA C 57.43 . 1 327 . 32 GLU CB C 30.26 . 1 328 . 32 GLU CG C 35.84 . 1 329 . 32 GLU N N 116.38 . 1 330 . 33 ASP H H 8.44 . 1 331 . 33 ASP HA H 4.71 . 1 332 . 33 ASP HB2 H 2.90 . 2 333 . 33 ASP HB3 H 2.75 . 2 334 . 33 ASP C C 177.62 . 1 335 . 33 ASP CA C 55.02 . 1 336 . 33 ASP CB C 42.00 . 1 337 . 33 ASP N N 117.25 . 1 338 . 34 GLY H H 8.21 . 1 339 . 34 GLY HA2 H 4.13 . 2 340 . 34 GLY HA3 H 3.95 . 2 341 . 34 GLY C C 172.21 . 1 342 . 34 GLY CA C 45.92 . 1 343 . 34 GLY N N 108.07 . 1 344 . 35 GLU H H 7.46 . 1 345 . 35 GLU HA H 4.83 . 1 346 . 35 GLU HB2 H 2.05 . 2 347 . 35 GLU HB3 H 1.74 . 2 348 . 35 GLU HG2 H 2.04 . 2 349 . 35 GLU HG3 H 1.93 . 2 350 . 35 GLU C C 174.33 . 1 351 . 35 GLU CA C 54.34 . 1 352 . 35 GLU CB C 32.42 . 1 353 . 35 GLU CG C 34.95 . 1 354 . 35 GLU N N 114.58 . 1 355 . 36 ILE H H 9.08 . 1 356 . 36 ILE HA H 4.28 . 1 357 . 36 ILE HB H 1.75 . 1 358 . 36 ILE HG12 H 1.53 . 2 359 . 36 ILE HG13 H 1.08 . 2 360 . 36 ILE HG2 H 0.92 . 1 361 . 36 ILE HD1 H 0.82 . 1 362 . 36 ILE C C 173.22 . 1 363 . 36 ILE CA C 60.76 . 1 364 . 36 ILE CB C 40.86 . 1 365 . 36 ILE CG1 C 28.41 . 1 366 . 36 ILE CG2 C 17.67 . 1 367 . 36 ILE CD1 C 14.47 . 1 368 . 36 ILE N N 120.84 . 1 369 . 37 ASP H H 8.76 . 1 370 . 37 ASP HA H 5.17 . 1 371 . 37 ASP HB2 H 2.96 . 2 372 . 37 ASP HB3 H 2.36 . 2 373 . 37 ASP C C 176.27 . 1 374 . 37 ASP CA C 52.34 . 1 375 . 37 ASP CB C 42.12 . 1 376 . 37 ASP N N 128.59 . 1 377 . 38 MET H H 9.02 . 1 378 . 38 MET HA H 4.92 . 1 379 . 38 MET HB2 H 2.44 . 2 380 . 38 MET HB3 H 2.19 . 2 381 . 38 MET HG2 H 2.54 . 1 382 . 38 MET HG3 H 2.54 . 1 383 . 38 MET C C 174.43 . 1 384 . 38 MET CA C 54.66 . 1 385 . 38 MET CB C 34.27 . 1 386 . 38 MET CG C 33.16 . 1 387 . 38 MET N N 125.41 . 1 388 . 39 HIS H H 8.68 . 1 389 . 39 HIS HA H 5.16 . 1 390 . 39 HIS HB2 H 2.64 . 1 391 . 39 HIS HB3 H 2.64 . 1 392 . 39 HIS HD2 H 6.41 . 1 393 . 39 HIS HE1 H 8.13 . 1 394 . 39 HIS C C 173.51 . 1 395 . 39 HIS CA C 53.66 . 1 396 . 39 HIS CB C 31.27 . 1 397 . 39 HIS CD2 C 118.60 . 1 398 . 39 HIS CE1 C 133.63 . 1 399 . 39 HIS N N 120.91 . 1 400 . 40 CYS H H 8.64 . 1 401 . 40 CYS HA H 4.47 . 1 402 . 40 CYS HB2 H 3.13 . 2 403 . 40 CYS HB3 H 2.68 . 2 404 . 40 CYS C C 176.71 . 1 405 . 40 CYS CA C 58.24 . 1 406 . 40 CYS CB C 31.79 . 1 407 . 40 CYS N N 126.78 . 1 408 . 41 ASP H H 8.82 . 1 409 . 41 ASP HA H 4.32 . 1 410 . 41 ASP HB2 H 2.45 . 2 411 . 41 ASP HB3 H 2.28 . 2 412 . 41 ASP C C 176.17 . 1 413 . 41 ASP CA C 56.03 . 1 414 . 41 ASP CB C 40.90 . 1 415 . 41 ASP N N 129.17 . 1 416 . 42 TYR H H 9.01 . 1 417 . 42 TYR HA H 4.52 . 1 418 . 42 TYR HB2 H 3.18 . 2 419 . 42 TYR HB3 H 3.06 . 2 420 . 42 TYR HD1 H 7.22 . 1 421 . 42 TYR HD2 H 7.22 . 1 422 . 42 TYR HE1 H 6.80 . 1 423 . 42 TYR HE2 H 6.80 . 1 424 . 42 TYR C C 176.93 . 1 425 . 42 TYR CA C 59.91 . 1 426 . 42 TYR CB C 38.82 . 1 427 . 42 TYR CD1 C 132.12 . 3 428 . 42 TYR CE1 C 117.35 . 3 429 . 42 TYR N N 121.61 . 1 430 . 43 CYS H H 8.37 . 1 431 . 43 CYS HA H 4.91 . 1 432 . 43 CYS HB2 H 3.24 . 2 433 . 43 CYS HB3 H 2.92 . 2 434 . 43 CYS C C 176.87 . 1 435 . 43 CYS CA C 58.17 . 1 436 . 43 CYS CB C 32.81 . 1 437 . 43 CYS N N 116.88 . 1 438 . 44 GLY H H 7.74 . 1 439 . 44 GLY HA2 H 4.24 . 2 440 . 44 GLY HA3 H 3.84 . 2 441 . 44 GLY C C 174.29 . 1 442 . 44 GLY CA C 46.06 . 1 443 . 44 GLY N N 112.83 . 1 444 . 45 ASN H H 8.78 . 1 445 . 45 ASN HA H 4.50 . 1 446 . 45 ASN HB2 H 2.89 . 2 447 . 45 ASN HB3 H 2.16 . 2 448 . 45 ASN HD21 H 6.74 . 2 449 . 45 ASN HD22 H 6.81 . 2 450 . 45 ASN C C 174.26 . 1 451 . 45 ASN CA C 53.86 . 1 452 . 45 ASN CB C 38.99 . 1 453 . 45 ASN N N 122.52 . 1 454 . 45 ASN ND2 N 110.89 . 1 455 . 46 HIS H H 8.16 . 1 456 . 46 HIS HA H 5.09 . 1 457 . 46 HIS HB2 H 2.92 . 2 458 . 46 HIS HB3 H 2.80 . 2 459 . 46 HIS HD2 H 7.35 . 1 460 . 46 HIS HE1 H 8.31 . 1 461 . 46 HIS C C 173.38 . 1 462 . 46 HIS CA C 54.44 . 1 463 . 46 HIS CB C 31.03 . 1 464 . 46 HIS CD2 C 118.85 . 1 465 . 46 HIS CE1 C 135.49 . 1 466 . 46 HIS N N 116.25 . 1 467 . 47 TYR H H 9.08 . 1 468 . 47 TYR HA H 4.36 . 1 469 . 47 TYR HB2 H 3.08 . 2 470 . 47 TYR HB3 H 2.62 . 2 471 . 47 TYR HD1 H 6.98 . 1 472 . 47 TYR HD2 H 6.98 . 1 473 . 47 TYR HE1 H 6.68 . 1 474 . 47 TYR HE2 H 6.68 . 1 475 . 47 TYR C C 172.91 . 1 476 . 47 TYR CA C 57.14 . 1 477 . 47 TYR CB C 41.00 . 1 478 . 47 TYR CD1 C 133.21 . 3 479 . 47 TYR CE1 C 115.94 . 3 480 . 47 TYR N N 121.88 . 1 481 . 48 LEU H H 8.41 . 1 482 . 48 LEU HA H 5.20 . 1 483 . 48 LEU HB2 H 1.51 . 2 484 . 48 LEU HB3 H 1.42 . 2 485 . 48 LEU HG H 1.43 . 1 486 . 48 LEU HD1 H 0.78 . 1 487 . 48 LEU HD2 H 0.78 . 1 488 . 48 LEU C C 177.36 . 1 489 . 48 LEU CA C 54.08 . 1 490 . 48 LEU CB C 43.41 . 1 491 . 48 LEU CG C 27.74 . 1 492 . 48 LEU CD1 C 24.46 . 1 493 . 48 LEU CD2 C 24.46 . 1 494 . 48 LEU N N 124.59 . 1 495 . 49 PHE H H 9.31 . 1 496 . 49 PHE HA H 5.08 . 1 497 . 49 PHE HB2 H 2.90 . 2 498 . 49 PHE HB3 H 2.77 . 2 499 . 49 PHE HD1 H 7.05 . 1 500 . 49 PHE HD2 H 7.05 . 1 501 . 49 PHE HE1 H 7.16 . 1 502 . 49 PHE HE2 H 7.16 . 1 503 . 49 PHE HZ H 6.97 . 1 504 . 49 PHE C C 174.54 . 1 505 . 49 PHE CA C 56.35 . 1 506 . 49 PHE CB C 41.83 . 1 507 . 49 PHE CD1 C 131.40 . 3 508 . 49 PHE N N 124.10 . 1 509 . 50 ASN H H 9.40 . 1 510 . 50 ASN HA H 5.01 . 1 511 . 50 ASN HB2 H 3.41 . 2 512 . 50 ASN HB3 H 2.91 . 2 513 . 50 ASN HD21 H 6.82 . 2 514 . 50 ASN HD22 H 7.50 . 2 515 . 50 ASN C C 175.39 . 1 516 . 50 ASN CA C 50.73 . 1 517 . 50 ASN CB C 39.38 . 1 518 . 50 ASN N N 121.76 . 1 519 . 50 ASN ND2 N 112.21 . 1 520 . 51 ALA H H 8.61 . 1 521 . 51 ALA HA H 3.91 . 1 522 . 51 ALA HB H 1.47 . 1 523 . 51 ALA C C 180.49 . 1 524 . 51 ALA CA C 56.12 . 1 525 . 51 ALA CB C 18.45 . 1 526 . 51 ALA N N 118.90 . 1 527 . 52 MET H H 8.08 . 1 528 . 52 MET HA H 4.25 . 1 529 . 52 MET HB2 H 2.17 . 2 530 . 52 MET HB3 H 2.14 . 2 531 . 52 MET HG2 H 2.65 . 2 532 . 52 MET HG3 H 2.58 . 2 533 . 52 MET C C 178.88 . 1 534 . 52 MET CA C 58.36 . 1 535 . 52 MET CB C 31.47 . 1 536 . 52 MET CG C 32.44 . 1 537 . 52 MET N N 118.97 . 1 538 . 53 ASP H H 8.44 . 1 539 . 53 ASP HA H 4.41 . 1 540 . 53 ASP HB2 H 3.23 . 2 541 . 53 ASP HB3 H 2.84 . 2 542 . 53 ASP C C 179.45 . 1 543 . 53 ASP CA C 57.19 . 1 544 . 53 ASP CB C 41.75 . 1 545 . 53 ASP N N 121.57 . 1 546 . 54 ILE H H 8.36 . 1 547 . 54 ILE HA H 3.58 . 1 548 . 54 ILE HB H 1.89 . 1 549 . 54 ILE HG12 H 1.60 . 2 550 . 54 ILE HG13 H 1.18 . 2 551 . 54 ILE HG2 H 0.76 . 1 552 . 54 ILE HD1 H 0.68 . 1 553 . 54 ILE C C 177.03 . 1 554 . 54 ILE CA C 63.91 . 1 555 . 54 ILE CB C 37.04 . 1 556 . 54 ILE CG1 C 29.59 . 1 557 . 54 ILE CG2 C 17.80 . 1 558 . 54 ILE CD1 C 13.29 . 1 559 . 54 ILE N N 119.29 . 1 560 . 55 ALA H H 7.94 . 1 561 . 55 ALA HA H 4.03 . 1 562 . 55 ALA HB H 1.49 . 1 563 . 55 ALA C C 179.95 . 1 564 . 55 ALA CA C 55.09 . 1 565 . 55 ALA CB C 17.61 . 1 566 . 55 ALA N N 122.45 . 1 567 . 56 GLU H H 7.72 . 1 568 . 56 GLU HA H 4.06 . 1 569 . 56 GLU HB2 H 2.18 . 1 570 . 56 GLU HB3 H 2.18 . 1 571 . 56 GLU HG2 H 2.38 . 2 572 . 56 GLU HG3 H 2.26 . 2 573 . 56 GLU C C 179.16 . 1 574 . 56 GLU CA C 59.00 . 1 575 . 56 GLU CB C 29.59 . 1 576 . 56 GLU CG C 36.15 . 1 577 . 56 GLU N N 117.05 . 1 578 . 57 ILE H H 7.88 . 1 579 . 57 ILE HA H 3.75 . 1 580 . 57 ILE HB H 1.85 . 1 581 . 57 ILE HG12 H 1.83 . 2 582 . 57 ILE HG13 H 1.14 . 2 583 . 57 ILE HG2 H 0.81 . 1 584 . 57 ILE HD1 H 0.74 . 1 585 . 57 ILE C C 178.29 . 1 586 . 57 ILE CA C 64.46 . 1 587 . 57 ILE CB C 38.77 . 1 588 . 57 ILE CG1 C 29.51 . 1 589 . 57 ILE CG2 C 17.77 . 1 590 . 57 ILE CD1 C 15.18 . 1 591 . 57 ILE N N 119.56 . 1 592 . 58 ARG H H 8.14 . 1 593 . 58 ARG HA H 4.07 . 1 594 . 58 ARG HB2 H 1.99 . 2 595 . 58 ARG HB3 H 1.71 . 2 596 . 58 ARG HG2 H 1.69 . 2 597 . 58 ARG HG3 H 1.64 . 2 598 . 58 ARG HD2 H 2.98 . 1 599 . 58 ARG HD3 H 2.98 . 1 600 . 58 ARG C C 177.21 . 1 601 . 58 ARG CA C 57.84 . 1 602 . 58 ARG CB C 30.22 . 1 603 . 58 ARG CG C 28.19 . 1 604 . 58 ARG CD C 43.17 . 1 605 . 58 ARG N N 117.25 . 1 606 . 59 ASN H H 7.91 . 1 607 . 59 ASN HA H 4.63 . 1 608 . 59 ASN HB2 H 2.87 . 2 609 . 59 ASN HB3 H 2.84 . 2 610 . 59 ASN HD21 H 6.86 . 2 611 . 59 ASN HD22 H 7.60 . 2 612 . 59 ASN C C 175.44 . 1 613 . 59 ASN CA C 53.91 . 1 614 . 59 ASN CB C 38.63 . 1 615 . 59 ASN N N 117.16 . 1 616 . 59 ASN ND2 N 112.29 . 1 617 . 60 ASN H H 7.99 . 1 618 . 60 ASN HA H 4.72 . 1 619 . 60 ASN HB2 H 2.85 . 2 620 . 60 ASN HB3 H 2.77 . 2 621 . 60 ASN HD21 H 6.90 . 2 622 . 60 ASN HD22 H 7.62 . 2 623 . 60 ASN C C 174.77 . 1 624 . 60 ASN CA C 53.26 . 1 625 . 60 ASN CB C 38.99 . 1 626 . 60 ASN N N 118.87 . 1 627 . 60 ASN ND2 N 112.92 . 1 628 . 61 ALA H H 8.07 . 1 629 . 61 ALA HA H 4.37 . 1 630 . 61 ALA HB H 1.40 . 1 631 . 61 ALA C C 176.86 . 1 632 . 61 ALA CA C 52.49 . 1 633 . 61 ALA CB C 19.28 . 1 634 . 61 ALA N N 124.65 . 1 635 . 62 SER H H 7.88 . 1 636 . 62 SER HA H 4.22 . 1 637 . 62 SER HB2 H 3.82 . 1 638 . 62 SER HB3 H 3.82 . 1 639 . 62 SER CA C 59.94 . 1 640 . 62 SER CB C 64.55 . 1 641 . 62 SER N N 120.92 . 1 stop_ save_