data_16787 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR assignments for Thermus thermophilus Rieske protein at pH 5.2 at the reduced state ; _BMRB_accession_number 16787 _BMRB_flat_file_name bmr16787.str _Entry_type original _Submission_date 2010-03-23 _Accession_date 2010-03-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'same as title' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hsueh Kuang-Lung . . 2 Markley John . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 131 "13C chemical shifts" 335 "15N chemical shifts" 131 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-08-12 update BMRB 'Complete entry citation' 2010-06-15 original author 'Original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16804 'oxidized Rieske Protein' stop_ save_ ############################# # Citation for this entry # ############################# save_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR investigations of the Rieske protein from Thermus thermophilus support a coupled proton and electron transfer mechanism.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20496909 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hsueh Kuang-Lung . . 2 Westler William M. . 3 Markley John L. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full 'Journal of the American Chemical Society' _Journal_volume 132 _Journal_issue 23 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7908 _Page_last 7918 _Year 2010 _Details . loop_ _Keyword 'iron sulfur cluster' paramagnetic 'Rieske protein' 'thermus thermophilus' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Thermus thermophilus Rieske protein (cofactor bound)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Rieske protein' $Rieske_protein '[2Fe-2S] cofactor' $(2Fe-2S) stop_ _System_molecular_weight 16508 _System_physical_state native _System_oligomer_state ? _System_paramagnetic yes _System_thiol_state . _Database_query_date . _Details 'cluster bound to Cys151, Cys132, His134, His154. The molecular weight is apo-protein not for holoprotein.' save_ ######################## # Monomeric polymers # ######################## save_Rieske_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Rieske_protein _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 157 _Mol_residue_sequence ; MTPEKEPLKPGDILVYAQGG GEPKPIRLEELKPGDPFVLA YPMDPKTKVVKSGEAKNTLL VARFDPEELAPEVAQHAAEG VVAYSAVCTHLGPIVSQFVA DEEAALCPCPGPVYDLRHGA QVIAGPPPRPVPQLPVRVED GVLVAAGEFLGPVGVQA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 45 MET 2 46 THR 3 47 PRO 4 48 GLU 5 49 LYS 6 50 GLU 7 51 PRO 8 52 LEU 9 53 LYS 10 54 PRO 11 55 GLY 12 56 ASP 13 57 ILE 14 58 LEU 15 59 VAL 16 60 TYR 17 61 ALA 18 62 GLN 19 63 GLY 20 64 GLY 21 65 GLY 22 66 GLU 23 67 PRO 24 68 LYS 25 69 PRO 26 70 ILE 27 71 ARG 28 72 LEU 29 73 GLU 30 74 GLU 31 75 LEU 32 76 LYS 33 77 PRO 34 78 GLY 35 79 ASP 36 80 PRO 37 81 PHE 38 82 VAL 39 83 LEU 40 84 ALA 41 85 TYR 42 86 PRO 43 87 MET 44 88 ASP 45 89 PRO 46 90 LYS 47 91 THR 48 92 LYS 49 93 VAL 50 94 VAL 51 95 LYS 52 96 SER 53 97 GLY 54 98 GLU 55 99 ALA 56 100 LYS 57 101 ASN 58 102 THR 59 103 LEU 60 104 LEU 61 105 VAL 62 106 ALA 63 107 ARG 64 108 PHE 65 109 ASP 66 110 PRO 67 111 GLU 68 112 GLU 69 113 LEU 70 114 ALA 71 115 PRO 72 116 GLU 73 117 VAL 74 118 ALA 75 119 GLN 76 120 HIS 77 121 ALA 78 122 ALA 79 123 GLU 80 124 GLY 81 125 VAL 82 126 VAL 83 127 ALA 84 128 TYR 85 129 SER 86 130 ALA 87 131 VAL 88 132 CYS 89 133 THR 90 134 HIS 91 135 LEU 92 136 GLY 93 137 PRO 94 138 ILE 95 139 VAL 96 140 SER 97 141 GLN 98 142 PHE 99 143 VAL 100 144 ALA 101 145 ASP 102 146 GLU 103 147 GLU 104 148 ALA 105 149 ALA 106 150 LEU 107 151 CYS 108 152 PRO 109 153 CYS 110 154 PRO 111 155 GLY 112 156 PRO 113 157 VAL 114 158 TYR 115 159 ASP 116 160 LEU 117 161 ARG 118 162 HIS 119 163 GLY 120 164 ALA 121 165 GLN 122 166 VAL 123 167 ILE 124 168 ALA 125 169 GLY 126 170 PRO 127 171 PRO 128 172 PRO 129 173 ARG 130 174 PRO 131 175 VAL 132 176 PRO 133 177 GLN 134 178 LEU 135 179 PRO 136 180 VAL 137 181 ARG 138 182 VAL 139 183 GLU 140 184 ASP 141 185 GLY 142 186 VAL 143 187 LEU 144 188 VAL 145 189 ALA 146 190 ALA 147 191 GLY 148 192 GLU 149 193 PHE 150 194 LEU 151 195 GLY 152 196 PRO 153 197 VAL 154 198 GLY 155 199 VAL 156 200 GLN 157 201 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-05 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 16804 Rieske_protein 100.00 157 98.73 98.73 3.24e-101 PDB 1NYK "Crystal Structure Of The Rieske Protein From Thermus Thermophilus" 99.36 165 97.44 98.08 1.72e-99 PDB 3FOU "Low Ph Structure Of The Rieske Protein From Thermus Thermophilus At 2.1 A" 99.36 156 97.44 98.08 5.32e-99 stop_ save_ ############# # Ligands # ############# save_(2Fe-2S) _Saveframe_category ligand _Mol_type non-polymer _Name_common "[2Fe-2S] (cofactor, two iron two sulfur cluster [2Fe-2S])" _BMRB_code . _PDB_code . _Molecular_mass . _Mol_charge . _Mol_paramagnetic yes _Mol_aromatic no _Details . _Mol_thiol_state 'not present' _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 _Strain $Rieske_protein 'Thermus thermophilus' 274 Bacteria . Thermus thermophilus BL21(DE3)pLysS 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 $Rieske_protein 'recombinant technology' . Escherichia coli BL21(DE3)pLysS pET17b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_2_reduced _Saveframe_category sample _Sample_type solution _Details 'reduced by dithionite' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Rieske_protein 5 mM 'natural abundance' TRIS 20 mM 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' 'boric acid' 20 mM 'natural abundance' dithionite 30 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.114 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2_reduced save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_2_reduced save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_2_reduced save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.4 0.1 M pH 5.2 0.02 pH pressure 1 . atm temperature 298 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 $1 $1 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 $1 $1 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 $1 $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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $SPARKY stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' stop_ loop_ _Sample_label $sample_2_reduced stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Rieske protein' _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 45 2 THR H H 8.213 . 1 2 45 2 THR N N 117.933 . 1 3 46 3 PRO CA C 65.814 . 1 4 46 3 PRO CB C 32.373 . 1 5 46 3 PRO CG C 27.828 . 1 6 47 4 GLU H H 9.362 . 1 7 47 4 GLU CA C 53.283 . 1 8 47 4 GLU CB C 28.376 . 1 9 47 4 GLU CG C 36.408 . 1 10 47 4 GLU N N 116.087 . 1 11 48 5 LYS H H 7.726 . 1 12 48 5 LYS CA C 55.416 . 1 13 48 5 LYS CB C 33.391 . 1 14 48 5 LYS CD C 29.476 . 1 15 48 5 LYS CG C 26.316 . 1 16 48 5 LYS N N 117.823 . 1 17 49 6 GLU H H 6.958 . 1 18 49 6 GLU CB C 29.635 . 1 19 49 6 GLU N N 120.535 . 1 20 50 7 PRO CA C 61.200 . 1 21 50 7 PRO CB C 32.603 . 1 22 50 7 PRO CG C 26.371 . 1 23 51 8 LEU H H 7.712 . 1 24 51 8 LEU CA C 57.222 . 1 25 51 8 LEU CB C 43.303 . 1 26 51 8 LEU CD1 C 27.601 . 2 27 51 8 LEU CG C 28.217 . 1 28 51 8 LEU N N 122.563 . 1 29 52 9 LYS H H 8.998 . 1 30 52 9 LYS CA C 52.702 . 1 31 52 9 LYS CB C 35.006 . 1 32 52 9 LYS N N 128.283 . 1 33 53 10 PRO CA C 63.572 . 1 34 53 10 PRO CB C 31.352 . 1 35 53 10 PRO CG C 28.042 . 1 36 54 11 GLY H H 9.174 . 1 37 54 11 GLY CA C 44.557 . 1 38 54 11 GLY N N 115.096 . 1 39 55 12 ASP H H 7.800 . 1 40 55 12 ASP CA C 55.328 . 1 41 55 12 ASP CB C 40.380 . 1 42 55 12 ASP N N 120.089 . 1 43 56 13 ILE H H 8.396 . 1 44 56 13 ILE CA C 62.211 . 1 45 56 13 ILE CB C 29.448 . 1 46 56 13 ILE CD1 C 13.222 . 1 47 56 13 ILE CG1 C 30.251 . 1 48 56 13 ILE CG2 C 21.018 . 1 49 56 13 ILE N N 122.441 . 1 50 57 14 LEU H H 8.500 . 1 51 57 14 LEU CA C 54.449 . 1 52 57 14 LEU CB C 40.859 . 1 53 57 14 LEU N N 126.320 . 1 54 58 15 VAL H H 8.947 . 1 55 58 15 VAL CA C 57.748 . 1 56 58 15 VAL CB C 34.330 . 1 57 58 15 VAL N N 114.874 . 1 58 59 16 TYR H H 7.781 . 1 59 59 16 TYR CA C 61.109 . 1 60 59 16 TYR CB C 38.678 . 1 61 59 16 TYR N N 118.944 . 1 62 60 17 ALA H H 8.547 . 1 63 60 17 ALA CA C 53.187 . 1 64 60 17 ALA CB C 18.714 . 1 65 60 17 ALA N N 125.063 . 1 66 61 18 GLN H H 8.379 . 1 67 61 18 GLN CA C 55.356 . 1 68 61 18 GLN CB C 30.003 . 1 69 61 18 GLN CG C 33.870 . 1 70 61 18 GLN N N 118.453 . 1 71 62 19 GLY H H 8.461 . 1 72 62 19 GLY CA C 45.770 . 1 73 62 19 GLY N N 110.268 . 1 74 63 20 GLY H H 7.710 . 1 75 63 20 GLY CA C 44.538 . 1 76 63 20 GLY N N 108.699 . 1 77 64 21 GLY H H 8.211 . 1 78 64 21 GLY CA C 43.342 . 1 79 64 21 GLY N N 106.044 . 1 80 65 22 GLU H H 8.648 . 1 81 65 22 GLU CB C 30.574 . 1 82 65 22 GLU N N 120.546 . 1 83 66 23 PRO CA C 58.248 . 1 84 67 24 LYS H H 9.747 . 1 85 67 24 LYS N N 127.071 . 1 86 68 25 PRO CA C 63.066 . 1 87 68 25 PRO CB C 33.667 . 1 88 69 26 ILE H H 9.750 . 1 89 69 26 ILE CA C 62.694 . 1 90 69 26 ILE CB C 37.598 . 1 91 69 26 ILE CD1 C 14.677 . 1 92 69 26 ILE CG1 C 26.086 . 1 93 69 26 ILE CG2 C 17.453 . 1 94 69 26 ILE N N 126.946 . 1 95 70 27 ARG H H 7.573 . 1 96 70 27 ARG CA C 54.047 . 1 97 70 27 ARG CB C 31.415 . 1 98 70 27 ARG CD C 45.244 . 1 99 70 27 ARG N N 126.149 . 1 100 71 28 LEU H H 7.830 . 1 101 71 28 LEU CA C 58.774 . 1 102 71 28 LEU CB C 42.473 . 1 103 71 28 LEU CG C 29.134 . 1 104 71 28 LEU N N 123.522 . 1 105 72 29 GLU H H 8.606 . 1 106 72 29 GLU CA C 57.450 . 1 107 72 29 GLU CB C 28.620 . 1 108 72 29 GLU CG C 35.428 . 1 109 72 29 GLU N N 110.768 . 1 110 73 30 GLU H H 7.614 . 1 111 73 30 GLU CA C 57.540 . 1 112 73 30 GLU CB C 31.370 . 1 113 73 30 GLU N N 118.456 . 1 114 74 31 LEU H H 7.407 . 1 115 74 31 LEU CA C 53.235 . 1 116 74 31 LEU CB C 32.861 . 1 117 74 31 LEU N N 118.486 . 1 118 75 32 LYS H H 8.789 . 1 119 75 32 LYS N N 125.090 . 1 120 77 34 GLY H H 8.076 . 1 121 77 34 GLY CA C 45.483 . 1 122 77 34 GLY N N 101.724 . 1 123 78 35 ASP H H 7.307 . 1 124 78 35 ASP N N 121.385 . 1 125 79 36 PRO CA C 52.721 . 1 126 79 36 PRO CB C 33.236 . 1 127 79 36 PRO CD C 55.286 . 1 128 79 36 PRO CG C 29.044 . 1 129 80 37 PHE H H 8.354 . 1 130 80 37 PHE CA C 55.484 . 1 131 80 37 PHE CB C 40.215 . 1 132 80 37 PHE N N 123.518 . 1 133 81 38 VAL H H 9.300 . 1 134 81 38 VAL CA C 59.860 . 1 135 81 38 VAL CB C 34.262 . 1 136 81 38 VAL N N 117.002 . 1 137 82 39 LEU H H 8.913 . 1 138 82 39 LEU CA C 53.832 . 1 139 82 39 LEU CB C 43.528 . 1 140 82 39 LEU CD1 C 25.763 . 2 141 82 39 LEU N N 124.546 . 1 142 83 40 ALA H H 8.905 . 1 143 83 40 ALA CA C 50.286 . 1 144 83 40 ALA CB C 26.088 . 1 145 83 40 ALA N N 125.304 . 1 146 84 41 TYR H H 8.463 . 1 147 84 41 TYR N N 113.400 . 1 148 85 42 PRO CA C 61.656 . 1 149 85 42 PRO CB C 32.353 . 1 150 85 42 PRO CG C 26.842 . 1 151 86 43 MET H H 9.862 . 1 152 86 43 MET CA C 53.021 . 1 153 86 43 MET CB C 37.471 . 1 154 86 43 MET CG C 30.508 . 1 155 86 43 MET N N 123.536 . 1 156 87 44 ASP H H 8.124 . 1 157 87 44 ASP N N 127.789 . 1 158 88 45 PRO CA C 64.665 . 1 159 88 45 PRO CB C 32.397 . 1 160 88 45 PRO CD C 45.383 . 1 161 88 45 PRO CG C 27.688 . 1 162 89 46 LYS H H 8.554 . 1 163 89 46 LYS CA C 57.958 . 1 164 89 46 LYS CB C 33.230 . 1 165 89 46 LYS CD C 28.793 . 1 166 89 46 LYS CE C 42.203 . 1 167 89 46 LYS CG C 25.164 . 1 168 89 46 LYS N N 118.096 . 1 169 90 47 THR H H 8.419 . 1 170 90 47 THR CA C 62.157 . 1 171 90 47 THR CB C 70.176 . 1 172 90 47 THR N N 109.226 . 1 173 91 48 LYS H H 7.960 . 1 174 91 48 LYS CA C 57.254 . 1 175 91 48 LYS CB C 28.429 . 1 176 91 48 LYS CG C 25.010 . 1 177 91 48 LYS N N 114.602 . 1 178 92 49 VAL H H 7.268 . 1 179 92 49 VAL CA C 58.624 . 1 180 92 49 VAL CB C 32.784 . 1 181 92 49 VAL CG1 C 20.908 . 2 182 92 49 VAL CG2 C 21.988 . 2 183 92 49 VAL N N 117.908 . 1 184 93 50 VAL H H 8.666 . 1 185 93 50 VAL CA C 63.065 . 1 186 93 50 VAL CB C 31.682 . 1 187 93 50 VAL N N 130.078 . 1 188 94 51 LYS H H 8.890 . 1 189 94 51 LYS CA C 56.007 . 1 190 94 51 LYS CB C 30.192 . 1 191 94 51 LYS N N 132.810 . 1 192 95 52 SER H H 8.034 . 1 193 95 52 SER CA C 57.543 . 1 194 95 52 SER CB C 62.657 . 1 195 95 52 SER N N 110.792 . 1 196 96 53 GLY H H 8.570 . 1 197 96 53 GLY CA C 45.922 . 1 198 96 53 GLY N N 109.860 . 1 199 97 54 GLU H H 6.526 . 1 200 97 54 GLU CA C 52.889 . 1 201 97 54 GLU CB C 31.183 . 1 202 97 54 GLU N N 120.886 . 1 203 98 55 ALA H H 9.108 . 1 204 98 55 ALA CA C 54.968 . 1 205 98 55 ALA CB C 19.083 . 1 206 98 55 ALA N N 131.299 . 1 207 99 56 LYS H H 10.146 . 1 208 99 56 LYS CA C 59.255 . 1 209 99 56 LYS CB C 30.834 . 1 210 99 56 LYS CD C 27.186 . 1 211 99 56 LYS CE C 43.273 . 1 212 99 56 LYS N N 117.811 . 1 213 100 57 ASN H H 8.522 . 1 214 100 57 ASN CA C 52.631 . 1 215 100 57 ASN CB C 38.842 . 1 216 100 57 ASN N N 119.159 . 1 217 101 58 THR H H 7.613 . 1 218 101 58 THR CA C 65.640 . 1 219 101 58 THR CB C 68.689 . 1 220 101 58 THR N N 113.200 . 1 221 102 59 LEU H H 9.250 . 1 222 102 59 LEU CA C 53.644 . 1 223 102 59 LEU CB C 46.190 . 1 224 102 59 LEU N N 131.135 . 1 225 103 60 LEU H H 9.181 . 1 226 103 60 LEU CA C 53.761 . 1 227 103 60 LEU CB C 44.986 . 1 228 103 60 LEU N N 118.629 . 1 229 104 61 VAL H H 8.909 . 1 230 104 61 VAL CA C 61.252 . 1 231 104 61 VAL CB C 34.320 . 1 232 104 61 VAL CG1 C 19.314 . 2 233 104 61 VAL CG2 C 21.847 . 2 234 104 61 VAL N N 122.441 . 1 235 105 62 ALA H H 8.920 . 1 236 105 62 ALA CA C 50.266 . 1 237 105 62 ALA CB C 24.569 . 1 238 105 62 ALA N N 128.181 . 1 239 106 63 ARG H H 8.631 . 1 240 106 63 ARG CA C 54.230 . 1 241 106 63 ARG CB C 31.368 . 1 242 106 63 ARG CD C 45.269 . 1 243 106 63 ARG CG C 31.433 . 1 244 106 63 ARG N N 119.495 . 1 245 107 64 PHE H H 7.943 . 1 246 107 64 PHE CA C 56.577 . 1 247 107 64 PHE CB C 43.139 . 1 248 107 64 PHE N N 124.062 . 1 249 108 65 ASP H H 9.258 . 1 250 108 65 ASP CA C 57.603 . 1 251 108 65 ASP N N 123.152 . 1 252 109 66 PRO CA C 65.744 . 1 253 109 66 PRO CB C 32.084 . 1 254 109 66 PRO CG C 27.752 . 1 255 110 67 GLU H H 8.738 . 1 256 110 67 GLU CA C 57.933 . 1 257 110 67 GLU CB C 28.909 . 1 258 110 67 GLU CG C 36.051 . 1 259 110 67 GLU N N 114.705 . 1 260 111 68 GLU H H 8.145 . 1 261 111 68 GLU CA C 56.250 . 1 262 111 68 GLU CB C 30.816 . 1 263 111 68 GLU CG C 36.697 . 1 264 111 68 GLU N N 116.430 . 1 265 112 69 LEU H H 7.002 . 1 266 112 69 LEU CA C 53.280 . 1 267 112 69 LEU CB C 43.411 . 1 268 112 69 LEU N N 116.888 . 1 269 113 70 ALA H H 7.981 . 1 270 113 70 ALA N N 125.495 . 1 271 114 71 PRO CA C 66.251 . 1 272 114 71 PRO CB C 31.888 . 1 273 114 71 PRO CG C 27.794 . 1 274 115 72 GLU H H 9.545 . 1 275 115 72 GLU CA C 59.346 . 1 276 115 72 GLU CB C 28.386 . 1 277 115 72 GLU CG C 36.153 . 1 278 115 72 GLU N N 116.481 . 1 279 116 73 VAL H H 7.175 . 1 280 116 73 VAL CA C 63.495 . 1 281 116 73 VAL CB C 32.863 . 1 282 116 73 VAL CG1 C 22.474 . 2 283 116 73 VAL N N 119.810 . 1 284 117 74 ALA H H 8.530 . 1 285 117 74 ALA CA C 54.441 . 1 286 117 74 ALA CB C 18.369 . 1 287 117 74 ALA N N 122.527 . 1 288 118 75 GLN H H 7.425 . 1 289 118 75 GLN CA C 57.773 . 1 290 118 75 GLN CB C 28.458 . 1 291 118 75 GLN CG C 33.234 . 1 292 118 75 GLN N N 114.276 . 1 293 119 76 HIS H H 7.204 . 1 294 119 76 HIS CA C 53.467 . 1 295 119 76 HIS CB C 28.975 . 1 296 119 76 HIS N N 113.177 . 1 297 120 77 ALA H H 7.493 . 1 298 120 77 ALA CA C 50.562 . 1 299 120 77 ALA CB C 22.953 . 1 300 120 77 ALA N N 125.712 . 1 301 121 78 ALA H H 8.285 . 1 302 121 78 ALA CA C 50.873 . 1 303 121 78 ALA CB C 20.760 . 1 304 121 78 ALA N N 122.340 . 1 305 122 79 GLU H H 9.082 . 1 306 122 79 GLU CA C 56.672 . 1 307 122 79 GLU CB C 26.996 . 1 308 122 79 GLU CG C 35.203 . 1 309 122 79 GLU N N 120.950 . 1 310 123 80 GLY H H 8.455 . 1 311 123 80 GLY CA C 45.079 . 1 312 123 80 GLY N N 103.287 . 1 313 124 81 VAL H H 8.236 . 1 314 124 81 VAL CA C 62.665 . 1 315 124 81 VAL CB C 30.832 . 1 316 124 81 VAL CG1 C 22.906 . 2 317 124 81 VAL N N 121.621 . 1 318 125 82 VAL H H 8.921 . 1 319 125 82 VAL CA C 58.048 . 1 320 125 82 VAL CB C 34.931 . 1 321 125 82 VAL CG2 C 19.710 . 2 322 125 82 VAL N N 119.029 . 1 323 126 83 ALA H H 7.522 . 1 324 126 83 ALA CA C 49.221 . 1 325 126 83 ALA CB C 23.240 . 1 326 126 83 ALA N N 121.456 . 1 327 127 84 TYR H H 8.964 . 1 328 127 84 TYR CA C 55.740 . 1 329 127 84 TYR CB C 43.902 . 1 330 127 84 TYR N N 116.690 . 1 331 128 85 SER H H 8.434 . 1 332 128 85 SER CB C 63.012 . 1 333 128 85 SER N N 112.225 . 1 334 129 86 ALA H H 7.740 . 1 335 129 86 ALA CA C 49.832 . 1 336 129 86 ALA CB C 19.747 . 1 337 129 86 ALA N N 122.514 . 1 338 130 87 VAL H H 7.497 . 1 339 130 87 VAL CA C 62.982 . 1 340 130 87 VAL CB C 31.939 . 1 341 130 87 VAL N N 119.852 . 1 342 131 88 CYS H H 8.513 . 1 343 131 88 CYS N N 109.320 . 1 344 132 89 THR H H 8.156 . 1 345 132 89 THR N N 123.702 . 1 346 135 92 GLY H H 9.277 . 1 347 135 92 GLY N N 110.179 . 1 348 136 93 PRO CA C 63.158 . 1 349 136 93 PRO CB C 31.916 . 1 350 136 93 PRO CD C 51.662 . 1 351 136 93 PRO CG C 27.819 . 1 352 137 94 ILE H H 8.682 . 1 353 137 94 ILE CA C 61.103 . 1 354 137 94 ILE CB C 38.874 . 1 355 137 94 ILE CD1 C 13.039 . 1 356 137 94 ILE CG1 C 27.169 . 1 357 137 94 ILE CG2 C 17.616 . 1 358 137 94 ILE N N 123.362 . 1 359 138 95 VAL H H 8.248 . 1 360 138 95 VAL CA C 62.545 . 1 361 138 95 VAL CB C 32.434 . 1 362 138 95 VAL CG1 C 19.204 . 2 363 138 95 VAL N N 126.587 . 1 364 139 96 SER H H 8.151 . 1 365 139 96 SER CA C 58.188 . 1 366 139 96 SER CB C 65.889 . 1 367 139 96 SER N N 123.702 . 1 368 140 97 GLN H H 8.663 . 1 369 140 97 GLN CA C 54.859 . 1 370 140 97 GLN CB C 31.219 . 1 371 140 97 GLN CG C 34.228 . 1 372 140 97 GLN N N 121.613 . 1 373 141 98 PHE H H 8.992 . 1 374 141 98 PHE CA C 63.092 . 1 375 141 98 PHE CB C 45.407 . 1 376 141 98 PHE N N 124.463 . 1 377 142 99 VAL H H 8.495 . 1 378 142 99 VAL CA C 60.806 . 1 379 142 99 VAL CB C 31.939 . 1 380 142 99 VAL CG1 C 21.789 . 2 381 142 99 VAL N N 121.023 . 1 382 143 100 ALA H H 8.611 . 1 383 143 100 ALA CA C 55.874 . 1 384 143 100 ALA CB C 18.653 . 1 385 143 100 ALA N N 130.551 . 1 386 144 101 ASP H H 8.803 . 1 387 144 101 ASP CA C 56.732 . 1 388 144 101 ASP CB C 39.961 . 1 389 144 101 ASP N N 115.393 . 1 390 145 102 GLU H H 6.825 . 1 391 145 102 GLU CA C 54.924 . 1 392 145 102 GLU CB C 30.625 . 1 393 145 102 GLU CG C 34.171 . 1 394 145 102 GLU N N 114.332 . 1 395 146 103 GLU H H 7.783 . 1 396 146 103 GLU CA C 57.261 . 1 397 146 103 GLU CB C 26.169 . 1 398 146 103 GLU N N 117.858 . 1 399 147 104 ALA H H 7.487 . 1 400 147 104 ALA CA C 50.269 . 1 401 147 104 ALA CB C 23.909 . 1 402 147 104 ALA N N 119.089 . 1 403 148 105 ALA H H 8.579 . 1 404 148 105 ALA CA C 50.509 . 1 405 148 105 ALA CB C 22.982 . 1 406 148 105 ALA N N 122.899 . 1 407 149 106 LEU H H 9.328 . 1 408 149 106 LEU CA C 53.685 . 1 409 149 106 LEU CB C 46.223 . 1 410 149 106 LEU N N 129.995 . 1 411 150 107 CYS H H 9.184 . 1 412 150 107 CYS N N 118.671 . 1 413 153 110 PRO CA C 63.781 . 1 414 153 110 PRO CB C 31.995 . 1 415 153 110 PRO CD C 50.660 . 1 416 153 110 PRO CG C 27.528 . 1 417 154 111 GLY H H 8.149 . 1 418 154 111 GLY N N 106.574 . 1 419 155 112 PRO CA C 62.715 . 1 420 155 112 PRO CB C 34.533 . 1 421 155 112 PRO CD C 54.119 . 1 422 155 112 PRO CG C 24.856 . 1 423 156 113 VAL H H 8.021 . 1 424 156 113 VAL CA C 61.427 . 1 425 156 113 VAL CB C 34.669 . 1 426 156 113 VAL CG1 C 23.988 . 2 427 156 113 VAL N N 124.221 . 1 428 157 114 TYR H H 9.352 . 1 429 157 114 TYR CA C 55.892 . 1 430 157 114 TYR CB C 40.699 . 1 431 157 114 TYR N N 123.852 . 1 432 158 115 ASP H H 9.648 . 1 433 158 115 ASP CA C 53.557 . 1 434 158 115 ASP CB C 41.141 . 1 435 158 115 ASP N N 122.511 . 1 436 159 116 LEU H H 7.361 . 1 437 159 116 LEU CA C 58.858 . 1 438 159 116 LEU CB C 42.249 . 1 439 159 116 LEU N N 125.642 . 1 440 160 117 ARG H H 8.866 . 1 441 160 117 ARG CA C 58.670 . 1 442 160 117 ARG CB C 29.664 . 1 443 160 117 ARG N N 118.058 . 1 444 161 118 HIS H H 7.149 . 1 445 161 118 HIS CA C 53.763 . 1 446 161 118 HIS CB C 27.544 . 1 447 161 118 HIS N N 114.159 . 1 448 162 119 GLY H H 6.552 . 1 449 162 119 GLY CA C 47.891 . 1 450 162 119 GLY N N 105.763 . 1 451 163 120 ALA H H 8.046 . 1 452 163 120 ALA CA C 52.787 . 1 453 163 120 ALA CB C 17.314 . 1 454 163 120 ALA N N 118.617 . 1 455 164 121 GLN H H 6.668 . 1 456 164 121 GLN CA C 57.043 . 1 457 164 121 GLN CB C 29.471 . 1 458 164 121 GLN CG C 33.670 . 1 459 164 121 GLN N N 113.366 . 1 460 165 122 VAL H H 8.784 . 1 461 165 122 VAL CA C 56.533 . 1 462 165 122 VAL CB C 35.799 . 1 463 165 122 VAL CG1 C 24.694 . 2 464 165 122 VAL CG2 C 27.339 . 2 465 165 122 VAL N N 126.754 . 1 466 166 123 ILE H H 8.593 . 1 467 166 123 ILE CA C 54.797 . 1 468 166 123 ILE CB C 34.408 . 1 469 166 123 ILE CG1 C 26.830 . 1 470 166 123 ILE N N 119.546 . 1 471 167 124 ALA H H 8.648 . 1 472 167 124 ALA CA C 52.508 . 1 473 167 124 ALA CB C 21.961 . 1 474 167 124 ALA N N 124.977 . 1 475 168 125 GLY H H 8.300 . 1 476 168 125 GLY CA C 44.870 . 1 477 168 125 GLY N N 103.805 . 1 478 171 128 PRO CA C 63.145 . 1 479 171 128 PRO CB C 32.065 . 1 480 172 129 ARG H H 7.220 . 1 481 172 129 ARG N N 115.068 . 1 482 173 130 PRO CA C 63.271 . 1 483 173 130 PRO CB C 32.083 . 1 484 174 131 VAL H H 7.792 . 1 485 174 131 VAL N N 125.482 . 1 486 175 132 PRO CA C 63.420 . 1 487 175 132 PRO CB C 32.093 . 1 488 175 132 PRO CD C 50.525 . 1 489 175 132 PRO CG C 27.431 . 1 490 176 133 GLN H H 8.579 . 1 491 176 133 GLN CA C 55.406 . 1 492 176 133 GLN CB C 29.045 . 1 493 176 133 GLN CG C 32.912 . 1 494 176 133 GLN N N 120.287 . 1 495 177 134 LEU H H 8.614 . 1 496 177 134 LEU N N 128.312 . 1 497 178 135 PRO CA C 62.710 . 1 498 178 135 PRO CB C 31.929 . 1 499 178 135 PRO CD C 55.131 . 1 500 178 135 PRO CG C 31.525 . 1 501 179 136 VAL H H 8.508 . 1 502 179 136 VAL CA C 62.067 . 1 503 179 136 VAL CB C 32.035 . 1 504 179 136 VAL CG1 C 21.936 . 2 505 179 136 VAL CG2 C 27.433 . 2 506 179 136 VAL N N 124.325 . 1 507 180 137 ARG H H 9.865 . 1 508 180 137 ARG CA C 54.187 . 1 509 180 137 ARG CB C 32.234 . 1 510 180 137 ARG N N 115.984 . 1 511 181 138 VAL H H 8.480 . 1 512 181 138 VAL CA C 60.702 . 1 513 181 138 VAL CB C 32.900 . 1 514 181 138 VAL CG1 C 21.697 . 2 515 181 138 VAL N N 119.344 . 1 516 182 139 GLU H H 9.276 . 1 517 182 139 GLU CA C 55.045 . 1 518 182 139 GLU CB C 31.949 . 1 519 182 139 GLU CG C 35.583 . 1 520 182 139 GLU N N 128.306 . 1 521 183 140 ASP H H 9.447 . 1 522 183 140 ASP CA C 55.263 . 1 523 183 140 ASP CB C 39.828 . 1 524 183 140 ASP N N 128.301 . 1 525 184 141 GLY H H 8.110 . 1 526 184 141 GLY CA C 45.639 . 1 527 184 141 GLY N N 101.711 . 1 528 185 142 VAL H H 7.801 . 1 529 185 142 VAL CA C 60.734 . 1 530 185 142 VAL CB C 34.371 . 1 531 185 142 VAL CG1 C 22.844 . 2 532 185 142 VAL N N 120.735 . 1 533 186 143 LEU H H 8.189 . 1 534 186 143 LEU CA C 54.550 . 1 535 186 143 LEU CB C 43.147 . 1 536 186 143 LEU CD1 C 25.819 . 2 537 186 143 LEU CG C 32.256 . 1 538 186 143 LEU N N 124.768 . 1 539 187 144 VAL H H 8.686 . 1 540 187 144 VAL CA C 59.369 . 1 541 187 144 VAL CB C 36.307 . 1 542 187 144 VAL CG1 C 19.588 . 2 543 187 144 VAL CG2 C 21.360 . 2 544 187 144 VAL N N 119.202 . 1 545 188 145 ALA H H 8.986 . 1 546 188 145 ALA CA C 52.327 . 1 547 188 145 ALA CB C 18.982 . 1 548 188 145 ALA N N 124.845 . 1 549 189 146 ALA H H 9.067 . 1 550 189 146 ALA CA C 50.899 . 1 551 189 146 ALA CB C 19.392 . 1 552 189 146 ALA N N 128.670 . 1 553 190 147 GLY H H 7.276 . 1 554 190 147 GLY CA C 44.385 . 1 555 190 147 GLY N N 104.605 . 1 556 191 148 GLU H H 7.698 . 1 557 191 148 GLU CA C 55.227 . 1 558 191 148 GLU CB C 30.706 . 1 559 191 148 GLU CG C 35.762 . 1 560 191 148 GLU N N 115.109 . 1 561 192 149 PHE H H 7.787 . 1 562 192 149 PHE CA C 60.823 . 1 563 192 149 PHE CB C 40.936 . 1 564 192 149 PHE N N 115.270 . 1 565 193 150 LEU H H 8.648 . 1 566 193 150 LEU CA C 55.542 . 1 567 193 150 LEU CB C 40.448 . 1 568 193 150 LEU CD1 C 22.603 . 2 569 193 150 LEU N N 120.243 . 1 570 194 151 GLY H H 7.389 . 1 571 194 151 GLY N N 107.788 . 1 572 195 152 PRO CA C 63.025 . 1 573 195 152 PRO CB C 32.006 . 1 574 195 152 PRO CD C 50.678 . 1 575 195 152 PRO CG C 27.433 . 1 576 196 153 VAL H H 8.382 . 1 577 196 153 VAL CA C 62.933 . 1 578 196 153 VAL CB C 31.476 . 1 579 196 153 VAL CG1 C 23.834 . 2 580 196 153 VAL CG2 C 27.528 . 2 581 196 153 VAL N N 123.219 . 1 582 197 154 GLY H H 8.892 . 1 583 197 154 GLY CA C 45.243 . 1 584 197 154 GLY N N 113.923 . 1 585 198 155 VAL H H 7.741 . 1 586 198 155 VAL CA C 61.234 . 1 587 198 155 VAL CB C 32.776 . 1 588 198 155 VAL CG1 C 19.624 . 2 589 198 155 VAL CG2 C 20.415 . 2 590 198 155 VAL N N 122.051 . 1 591 199 156 GLN H H 8.662 . 1 592 199 156 GLN CA C 55.633 . 1 593 199 156 GLN CB C 31.212 . 1 594 199 156 GLN CG C 33.807 . 1 595 199 156 GLN N N 128.597 . 1 596 200 157 ALA H H 8.348 . 1 597 200 157 ALA N N 123.272 . 1 stop_ save_