data_4776 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Letter to the Editor: Backbone resonance assignment and secondary structure of the 30 kDa Sud dimer from Wolinella succinogenes ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lin Yi-Jan . . 2 Pfeiffer Stefania . . 3 Loehr Frank . . 4 Klimmek Oliver . . 5 Rueterjans Heinz . . stop_ _BMRB_accession_number 4776 _BMRB_flat_file_name bmr4776.str _Entry_type new _Submission_date 2000-07-04 _Accession_date 2000-07-05 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 chemical_shift_isotope_effect 2 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 250 '13C chemical shifts' 368 '15N chemical shifts' 117 'chemical shift isotope effect' 224 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Letter to the Editor: Backbone resonance assignment and secondary structure of the 30 kDa Sud dimer from Wolinella succinogenes ; _Citation_status published _Citation_type journal _MEDLINE_UI_code ? _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lin Yi-Jan . . 2 Pfeiffer Stefania . . 3 Loehr Frank . . 4 Klimmek Oliver . . 5 Rueterjans Heinz . . stop_ _Journal_abbreviation "J. Biomol. NMR" _Journal_name_full ? _Journal_volume 18 _Journal_issue 3 _Page_first 285 _Page_last 286 _Year 2000 loop_ _Keyword NMR Sud "sulfur transferase" dimer perdeuteration "chemical shifts" stop_ save_ ################################## # Molecular system description # ################################## save_system_Sud _Saveframe_category molecular_system _Mol_system_name "Sud dimer" _Abbreviation_common Sud loop_ _Mol_system_component_name _Mol_label "Sud subunit 1" $Sud "Sud subunit 2" $Sud polysulfide $polysulfide stop_ _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'all other bound' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 "Sud subunit 1" 1 "Sud subunit 2" stop_ loop_ _Biological_function "polysulfide-sulfur transferase" stop_ save_ ######################## # Monomeric polymers # ######################## save_Sud _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "Sulfide Dehydrogenase" _Abbreviation_common Sud _Molecular_mass 30662 _Mol_thiol_state 'all other bound' _Details ; Each monomer has bound a chain of polysulfide sulfur atoms to the single cystein under the used solvent conditions. The given molecular mass does not include the additional sulfur atoms. ; ############################## # Polymer residue sequence # ############################## _Residue_count 137 _Mol_residue_sequence ; ADMGEKFDATFKAQVKAAKA DMVMLSPKDAYKLLQENPDI TLIDVRDPDELKAMGKPDVK NYKHMSRGKLEPLLAKSGLD PEKPVVVFCKTAARAALAGK TLREYGFKTIYNSEGGMDKW LEEGLPSLDRSHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ASP 3 MET 4 GLY 5 GLU 6 LYS 7 PHE 8 ASP 9 ALA 10 THR 11 PHE 12 LYS 13 ALA 14 GLN 15 VAL 16 LYS 17 ALA 18 ALA 19 LYS 20 ALA 21 ASP 22 MET 23 VAL 24 MET 25 LEU 26 SER 27 PRO 28 LYS 29 ASP 30 ALA 31 TYR 32 LYS 33 LEU 34 LEU 35 GLN 36 GLU 37 ASN 38 PRO 39 ASP 40 ILE 41 THR 42 LEU 43 ILE 44 ASP 45 VAL 46 ARG 47 ASP 48 PRO 49 ASP 50 GLU 51 LEU 52 LYS 53 ALA 54 MET 55 GLY 56 LYS 57 PRO 58 ASP 59 VAL 60 LYS 61 ASN 62 TYR 63 LYS 64 HIS 65 MET 66 SER 67 ARG 68 GLY 69 LYS 70 LEU 71 GLU 72 PRO 73 LEU 74 LEU 75 ALA 76 LYS 77 SER 78 GLY 79 LEU 80 ASP 81 PRO 82 GLU 83 LYS 84 PRO 85 VAL 86 VAL 87 VAL 88 PHE 89 CYS 90 LYS 91 THR 92 ALA 93 ALA 94 ARG 95 ALA 96 ALA 97 LEU 98 ALA 99 GLY 100 LYS 101 THR 102 LEU 103 ARG 104 GLU 105 TYR 106 GLY 107 PHE 108 LYS 109 THR 110 ILE 111 TYR 112 ASN 113 SER 114 GLU 115 GLY 116 GLY 117 MET 118 ASP 119 LYS 120 TRP 121 LEU 122 GLU 123 GLU 124 GLY 125 LEU 126 PRO 127 SER 128 LEU 129 ASP 130 ARG 131 SER 132 HIS 133 HIS 134 HIS 135 HIS 136 HIS 137 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-03-03 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1QXN "Solution Structure Of The 30 Kda Polysulfide-Sulfur Transferase Homodimer From Wolinella Succinogenes" 100.00 137 100.00 100.00 4.74e-95 EMBL CAA57300 "sulfide dehydrogenase [Wolinella succinogenes]" 94.16 149 100.00 100.00 4.92e-88 EMBL CAE10660 "SULFIDE DEHYDROGENASE PRECURSOR [Wolinella succinogenes]" 94.16 149 100.00 100.00 4.92e-88 PRF 2104202A "sulfide dehydrogenase" 94.16 149 100.00 100.00 4.92e-88 REF NP_907760 "sulfide dehydrogenase precursor [Wolinella succinogenes DSM 1740]" 94.16 149 100.00 100.00 4.92e-88 REF WP_011139444 "sulfide dehydrogenase precursor [Wolinella succinogenes]" 94.16 149 100.00 100.00 4.92e-88 stop_ save_ ############# # Ligands # ############# save_polysulfide _Saveframe_category ligand _Mol_type non-polymer _Name_common polysulfide _Abbreviation_common polysulfide _Mol_paramagnetic no _Mol_aromatic no _Details ; The protein was loaded with sulfur before dissolved in the buffer. That means, a polysulfide with up to 10 sulfur atoms is bound to the single cysteine of each monomer. ; save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction $Sud "Wolinella succinogenes" 844 Eubacteria . Wolinella succinogenes periplasm 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 $Sud 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; The protein was loaded with sulfur before dissolved in the buffer. That means, a polysulfide with up to 10 sulfur atoms is bound to the single cysteine of each monomer. The buffer actually contains 14 mM Na2S and 2 mM Na2S4O6-- which results in 12 mM Na2S, 2mM Na2[S] ( [S] denotes polysulfide), 4mM S2O3--, 2mM Na+ ,and 2mM H+. Here, Na2S and Na2S4O6-- are used to produce polysulfide solutions with a defined concentration. The pH has to be > 7. And the solution has to be anaerob. For example: 5 HS- + 4 S4O6-- -> S5-- + 8 S2O3-- + 5 H+ The protein is than dissolved in the polysulfide solution and would built up a polysulfide sulfur chain at the cysteine residue. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Sud 1.2 mM "[U-13C; U-15N; U-2H]" "phosphate buffer" 50.0 mM . H2O 95 % . D2O 5 % . $polysulfide 1.0 mM . Na2S 14.0 mM . Na2S4O6 2.0 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Sud . mM 1.2 2.0 "[U-13C; U-15N]" "phosphate buffer" 50 mM . . . H2O 95 % . . . D2O 5 % . . . $polysulfide 1.0 mM . . . Na2S 14.0 mM . . . Na2S4O6 2.0 mM . . . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Sud 2.0 mM [U-15N] "phosphate buffer" 50.0 mM . H2O 95 % . D2O 5 % . $polysulfide 1.0 mM . Na2S 14.0 mM . Na2S4O6 2.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR loop_ _Task "recording experiments and processing spectra" stop_ _Citation_label $ref_1 save_ save_AURELIA _Saveframe_category software _Name AURELIA loop_ _Task "analysis of 2D and 3D NMR spectra" stop_ _Citation_label $ref_2 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Details ; 1H-15N HSQC (sample3) HNCO (sample 1, sample 2) HN(CA)CO (sample 1) HNCACB (sample 1) NHCA (sample 2) HN(CA)N (sample 1) CC(CO)NH (sample 1) CC(CA)NH (sample 1) H(C)CH-COSY (sample 2) HCC-COSY (sample 2) ; save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details ; The sample tube was filled under nitrogen gass and sealed in order to obtain rather anaerob than aerob athmosphere for the protein. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.6 0.2 n/a temperature 300 2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference 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 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_Sud_backbone_shift_1 _Saveframe_category assigned_chemical_shifts _Details ; After a certain time, we have observed a second set of signals which can be also combined to a sequential backbone assignment. Perhaps, this indicates aggregation of the Sud dimer to higher oligomers or changes due to the exposure of the solution to oxygen. The CB chemical shifts marked with an ambiguity code 9 are the expected CB shifts of the protonated protein derived by correcting the CB shifts of the deuterated protein by the isotope shift. See also the paper which describes the assignment. ; loop_ _Sample_label $sample_1 $sample_2 $sample_3 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "Sud subunit 1" loop_ _Atom_shift_assign_ID _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 4.66 0.03 1 2 2 ASP C C 176.8 0.2 1 3 2 ASP CA C 54.0 0.2 1 4 2 ASP CB C 41.3 0.2 1 5 3 MET H H 8.75 0.03 1 6 3 MET HA H 4.60 0.03 1 7 3 MET C C 177.1 0.2 1 8 3 MET CA C 55.4 0.2 1 9 3 MET CB C 31.2 0.2 9 10 3 MET N N 123.3 0.1 1 11 4 GLY H H 8.62 0.03 1 12 4 GLY HA2 H 3.96 0.03 2 13 4 GLY HA3 H 4.25 0.03 2 14 4 GLY C C 175.8 0.2 1 15 4 GLY CA C 48.4 0.2 1 16 4 GLY N N 108.8 0.1 1 17 5 GLU H H 8.20 0.03 1 18 5 GLU HA H 4.18 0.03 1 19 5 GLU C C 179.3 0.2 1 20 5 GLU CA C 59.2 0.2 1 21 5 GLU CB C 29.1 0.2 1 22 5 GLU N N 120.0 0.1 1 23 6 LYS H H 7.79 0.03 1 24 6 LYS HA H 4.20 0.03 1 25 6 LYS C C 180.1 0.2 1 26 6 LYS CA C 59.1 0.2 1 27 6 LYS CB C 31.6 0.2 1 28 6 LYS N N 121.0 0.1 1 29 7 PHE H H 8.38 0.03 1 30 7 PHE HA H 4.98 0.03 1 31 7 PHE C C 179.1 0.2 1 32 7 PHE CA C 58.3 0.2 1 33 7 PHE CB C 37.8 0.2 1 34 7 PHE N N 120.0 0.1 1 35 8 ASP H H 8.60 0.03 1 36 8 ASP HA H 4.80 0.03 1 37 8 ASP C C 177.6 0.2 1 38 8 ASP CA C 57.9 0.2 1 39 8 ASP CB C 41.3 0.2 1 40 8 ASP N N 120.0 0.1 1 41 9 ALA H H 8.35 0.03 1 42 9 ALA HA H 4.12 0.03 1 43 9 ALA C C 181.6 0.2 1 44 9 ALA CA C 55.4 0.2 1 45 9 ALA CB C 17.8 0.2 9 46 9 ALA N N 120.0 0.1 1 47 10 THR H H 8.40 0.03 1 48 10 THR HA H 3.88 0.03 1 49 10 THR C C 175.6 0.2 1 50 10 THR CA C 67.0 0.2 1 51 10 THR CB C 68.8 0.2 1 52 10 THR N N 117.7 0.1 1 53 11 PHE H H 8.43 0.03 1 54 11 PHE HA H 4.90 0.03 1 55 11 PHE C C 177.2 0.2 1 56 11 PHE CA C 60.3 0.2 1 57 11 PHE CB C 38.8 0.2 1 58 11 PHE N N 124.1 0.1 1 59 12 LYS H H 8.79 0.03 1 60 12 LYS HA H 3.41 0.03 1 61 12 LYS C C 180.1 0.2 1 62 12 LYS CA C 60.0 0.2 1 63 12 LYS CB C 32.2 0.2 1 64 12 LYS N N 118.1 0.1 1 65 13 ALA H H 8.02 0.03 1 66 13 ALA HA H 4.11 0.03 1 67 13 ALA C C 181.0 0.2 1 68 13 ALA CA C 55.0 0.2 1 69 13 ALA CB C 17.8 0.2 9 70 13 ALA N N 121.4 0.1 1 71 14 GLN H H 8.56 0.03 1 72 14 GLN HA H 4.02 0.03 1 73 14 GLN C C 180.1 0.2 1 74 14 GLN CA C 59.5 0.2 1 75 14 GLN CB C 27.5 0.2 1 76 14 GLN N N 120.6 0.1 1 77 15 VAL H H 8.43 0.03 1 78 15 VAL HA H 3.26 0.03 1 79 15 VAL C C 177.1 0.2 1 80 15 VAL CA C 67.1 0.2 1 81 15 VAL CB C 31.9 0.2 1 82 15 VAL N N 121.6 0.1 1 83 16 LYS H H 7.85 0.03 1 84 16 LYS HA H 3.78 0.03 1 85 16 LYS C C 179.4 0.2 1 86 16 LYS CA C 60.1 0.2 1 87 16 LYS CB C 32.4 0.2 9 88 16 LYS N N 119.6 0.1 1 89 17 ALA H H 7.92 0.03 1 90 17 ALA HA H 4.08 0.03 1 91 17 ALA C C 180.1 0.2 1 92 17 ALA CA C 54.6 0.2 1 93 17 ALA CB C 17.8 0.2 9 94 17 ALA N N 119.8 0.1 1 95 18 ALA H H 7.94 0.03 1 96 18 ALA HA H 4.11 0.03 1 97 18 ALA C C 180.9 0.2 1 98 18 ALA CA C 54.6 0.2 1 99 18 ALA CB C 17.8 0.2 1 100 18 ALA N N 120.4 0.1 1 101 19 LYS H H 8.47 0.03 1 102 19 LYS HA H 3.80 0.03 1 103 19 LYS C C 177.6 0.2 1 104 19 LYS CA C 60.3 0.2 1 105 19 LYS CB C 33.3 0.2 9 106 19 LYS N N 117.1 0.1 1 107 20 ALA H H 7.13 0.03 1 108 20 ALA HA H 4.18 0.03 1 109 20 ALA C C 177.9 0.2 1 110 20 ALA CA C 53.9 0.2 1 111 20 ALA CB C 18.1 0.2 1 112 20 ALA N N 116.9 0.1 1 113 21 ASP H H 7.27 0.03 1 114 21 ASP HA H 4.98 0.03 1 115 21 ASP C C 174.4 0.2 1 116 21 ASP CA C 53.5 0.2 1 117 21 ASP CB C 41.9 0.2 1 118 21 ASP N N 116.0 0.1 1 119 22 MET H H 7.70 0.03 1 120 22 MET HA H 4.82 0.03 1 121 22 MET C C 172.6 0.2 1 122 22 MET CA C 53.8 0.2 1 123 22 MET CB C 33.7 0.2 1 124 22 MET N N 116.7 0.1 1 125 23 VAL H H 7.68 0.03 1 126 23 VAL HA H 4.28 0.03 1 127 23 VAL C C 175.8 0.2 1 128 23 VAL CA C 62.3 0.2 1 129 23 VAL CB C 32.2 0.2 9 130 23 VAL N N 118.7 0.1 1 131 24 MET H H 8.86 0.03 1 132 24 MET HA H 5.21 0.03 1 133 24 MET C C 176.4 0.2 1 134 24 MET CA C 52.3 0.2 1 135 24 MET CB C 29.0 0.2 9 136 24 MET N N 125.8 0.1 1 137 25 LEU H H 8.93 0.03 1 138 25 LEU HA H 5.06 0.03 1 139 25 LEU C C 176.2 0.2 1 140 25 LEU CA C 52.4 0.2 1 141 25 LEU CB C 46.3 0.2 1 142 25 LEU N N 123.9 0.1 1 143 26 SER H H 9.28 0.03 1 144 26 SER HA H 4.78 0.03 1 145 26 SER C C 172.8 0.2 1 146 26 SER CA C 57.0 0.2 1 147 26 SER CB C 62.2 0.2 9 148 26 SER N N 119.2 0.1 1 149 27 PRO HA H 4.55 0.03 1 150 27 PRO C C 178.3 0.2 1 151 27 PRO CA C 65.5 0.2 1 152 27 PRO CB C 30.3 0.2 1 153 28 LYS H H 8.27 0.03 1 154 28 LYS HA H 3.73 0.03 1 155 28 LYS C C 179.6 0.2 1 156 28 LYS CA C 60.4 0.2 1 157 28 LYS CB C 31.9 0.2 1 158 28 LYS N N 113.6 0.1 1 159 29 ASP H H 7.65 0.03 1 160 29 ASP HA H 4.48 0.03 1 161 29 ASP C C 179.1 0.2 1 162 29 ASP CA C 57.0 0.2 1 163 29 ASP CB C 39.9 0.2 9 164 29 ASP N N 120.8 0.1 1 165 30 ALA H H 9.07 0.03 1 166 30 ALA HA H 3.94 0.03 1 167 30 ALA C C 178.2 0.2 1 168 30 ALA CA C 55.4 0.2 1 169 30 ALA CB C 16.9 0.2 1 170 30 ALA N N 125.8 0.1 1 171 31 TYR H H 8.77 0.03 1 172 31 TYR HA H 4.12 0.03 1 173 31 TYR C C 177.1 0.2 1 174 31 TYR CA C 62.5 0.2 1 175 31 TYR CB C 38.1 0.2 1 176 31 TYR N N 117.5 0.1 1 177 32 LYS H H 7.70 0.03 1 178 32 LYS HA H 3.83 0.03 1 179 32 LYS C C 177.6 0.2 1 180 32 LYS CA C 59.5 0.2 1 181 32 LYS CB C 32.5 0.2 1 182 32 LYS N N 118.1 0.1 1 183 33 LEU H H 7.87 0.03 1 184 33 LEU HA H 3.86 0.03 1 185 33 LEU C C 179.8 0.2 1 186 33 LEU CA C 58.1 0.2 1 187 33 LEU CB C 42.1 0.2 9 188 33 LEU N N 119.4 0.1 1 189 34 LEU H H 7.99 0.03 1 190 34 LEU HA H 3.86 0.03 1 191 34 LEU C C 179.3 0.2 1 192 34 LEU CA C 57.6 0.2 1 193 34 LEU CB C 40.9 0.2 1 194 34 LEU N N 117.7 0.1 1 195 35 GLN H H 8.04 0.03 1 196 35 GLN HA H 3.86 0.03 1 197 35 GLN C C 178.6 0.2 1 198 35 GLN CA C 58.0 0.2 1 199 35 GLN CB C 29.6 0.2 9 200 35 GLN N N 116.9 0.1 1 201 36 GLU H H 7.85 0.03 1 202 36 GLU HA H 4.13 0.03 1 203 36 GLU C C 176.3 0.2 1 204 36 GLU CA C 56.9 0.2 1 205 36 GLU CB C 30.3 0.2 1 206 36 GLU N N 115.0 0.1 1 207 37 ASN H H 7.44 0.03 1 208 37 ASN HA H 5.25 0.03 1 209 37 ASN C C 172.2 0.2 1 210 37 ASN CA C 50.5 0.2 1 211 37 ASN CB C 40.0 0.2 1 212 37 ASN N N 116.2 0.1 1 213 38 PRO HA H 4.63 0.03 1 214 38 PRO C C 176.4 0.2 1 215 38 PRO CA C 63.9 0.2 1 216 38 PRO CB C 31.9 0.2 1 217 39 ASP H H 8.51 0.03 1 218 39 ASP HA H 4.48 0.03 1 219 39 ASP C C 175.7 0.2 1 220 39 ASP CA C 54.5 0.2 1 221 39 ASP CB C 40.0 0.2 1 222 39 ASP N N 115.4 0.1 1 223 40 ILE H H 7.75 0.03 1 224 40 ILE HA H 4.23 0.03 1 225 40 ILE C C 174.7 0.2 1 226 40 ILE CA C 61.8 0.2 1 227 40 ILE CB C 37.8 0.2 1 228 40 ILE N N 120.8 0.1 1 229 41 THR H H 7.15 0.03 1 230 41 THR HA H 4.22 0.03 1 231 41 THR C C 173.0 0.2 1 232 41 THR CA C 62.3 0.2 1 233 41 THR CB C 70.3 0.2 1 234 41 THR N N 123.1 0.1 1 235 42 LEU H H 8.49 0.03 1 236 42 LEU HA H 5.05 0.03 1 237 42 LEU C C 173.4 0.2 1 238 42 LEU CA C 54.6 0.2 1 239 42 LEU CB C 42.1 0.2 9 240 42 LEU N N 129.1 0.1 1 241 43 ILE H H 9.18 0.03 1 242 43 ILE HA H 4.36 0.03 1 243 43 ILE C C 172.7 0.2 1 244 43 ILE CA C 59.5 0.2 1 245 43 ILE CB C 37.8 0.2 1 246 43 ILE N N 127.9 0.1 1 247 44 ASP H H 8.42 0.03 1 248 44 ASP HA H 4.76 0.03 1 249 44 ASP C C 177.0 0.2 1 250 44 ASP CA C 51.5 0.2 1 251 44 ASP CB C 41.3 0.2 9 252 44 ASP N N 128.1 0.1 1 253 45 VAL H H 8.76 0.03 1 254 45 VAL HA H 5.60 0.03 1 255 45 VAL C C 178.4 0.2 1 256 45 VAL CA C 59.1 0.2 1 257 45 VAL CB C 30.3 0.2 1 258 45 VAL N N 115.4 0.1 1 259 46 ARG H H 7.64 0.03 1 260 46 ARG HA H 4.13 0.03 1 261 46 ARG C C 174.3 0.2 1 262 46 ARG CA C 57.2 0.2 1 263 46 ARG CB C 31.5 0.2 9 264 46 ARG N N 121.4 0.1 1 265 47 ASP H H 9.34 0.03 1 266 47 ASP HA H 4.98 0.03 1 267 47 ASP C C 177.0 0.2 1 268 47 ASP CA C 53.4 0.2 1 269 47 ASP CB C 40.3 0.2 1 270 47 ASP N N 122.3 0.1 1 271 48 PRO HA H 4.11 0.03 1 272 48 PRO C C 178.2 0.2 1 273 48 PRO CA C 65.3 0.2 1 274 48 PRO CB C 31.3 0.2 1 275 49 ASP H H 8.98 0.03 1 276 49 ASP HA H 4.29 0.03 1 277 49 ASP C C 178.7 0.2 1 278 49 ASP CA C 56.2 0.2 1 279 49 ASP CB C 38.1 0.2 1 280 49 ASP N N 115.4 0.1 1 281 50 GLU H H 7.44 0.03 1 282 50 GLU HA H 4.14 0.03 5 283 50 GLU C C 177.8 0.2 1 284 50 GLU CA C 59.0 0.2 1 285 50 GLU CB C 30.9 0.2 9 286 50 GLU N N 123.1 0.1 1 287 51 LEU H H 6.86 0.03 1 288 51 LEU HA H 3.96 0.03 1 289 51 LEU C C 180.1 0.2 1 290 51 LEU CA C 58.7 0.2 1 291 51 LEU CB C 41.6 0.2 1 292 51 LEU N N 119.8 0.1 1 293 52 LYS H H 6.92 0.03 1 294 52 LYS HA H 4.00 0.03 1 295 52 LYS C C 177.5 0.2 1 296 52 LYS CA C 58.4 0.2 1 297 52 LYS CB C 32.2 0.2 1 298 52 LYS N N 116.9 0.1 1 299 53 ALA H H 7.58 0.03 1 300 53 ALA HA H 4.22 0.03 1 301 53 ALA C C 179.5 0.2 1 302 53 ALA CA C 54.5 0.2 1 303 53 ALA CB C 19.7 0.2 1 304 53 ALA N N 118.5 0.1 1 305 54 MET H H 8.33 0.03 1 306 54 MET HA H 4.70 0.03 1 307 54 MET C C 176.5 0.2 1 308 54 MET CA C 54.6 0.2 1 309 54 MET CB C 34.4 0.2 1 310 54 MET N N 112.1 0.1 1 311 55 GLY H H 7.54 0.03 1 312 55 GLY HA2 H 3.78 0.03 2 313 55 GLY HA3 H 4.34 0.03 2 314 55 GLY C C 173.3 0.2 1 315 55 GLY CA C 44.1 0.2 1 316 55 GLY N N 106.3 0.1 1 317 56 LYS H H 8.33 0.03 1 318 56 LYS HA H 4.53 0.03 1 319 56 LYS C C 172.4 0.2 1 320 56 LYS CA C 53.3 0.2 1 321 56 LYS CB C 32.8 0.2 1 322 56 LYS N N 114.8 0.1 1 323 57 PRO HA H 3.84 0.03 1 324 57 PRO C C 174.1 0.2 1 325 57 PRO CA C 62.5 0.2 1 326 57 PRO CB C 31.0 0.2 9 327 58 ASP H H 8.02 0.03 1 328 58 ASP HA H 4.40 0.03 1 329 58 ASP C C 174.3 0.2 1 330 58 ASP CA C 52.5 0.2 1 331 58 ASP CB C 39.7 0.2 1 332 58 ASP N N 122.5 0.1 1 333 59 VAL H H 6.89 0.03 1 334 59 VAL HA H 4.65 0.03 1 335 59 VAL C C 175.8 0.2 1 336 59 VAL CA C 58.4 0.2 1 337 59 VAL CB C 34.4 0.2 1 338 59 VAL N N 114.0 0.1 1 339 60 LYS H H 8.57 0.03 1 340 60 LYS HA H 4.05 0.03 1 341 60 LYS C C 177.6 0.2 1 342 60 LYS CA C 59.1 0.2 1 343 60 LYS CB C 32.5 0.2 1 344 60 LYS N N 121.6 0.1 1 345 61 ASN H H 9.30 0.03 1 346 61 ASN HA H 4.93 0.03 1 347 61 ASN C C 172.5 0.2 1 348 61 ASN CA C 51.9 0.2 1 349 61 ASN CB C 36.9 0.2 1 350 61 ASN N N 119.6 0.1 1 351 62 TYR H H 7.98 0.03 1 352 62 TYR HA H 4.92 0.03 1 353 62 TYR C C 174.7 0.2 1 354 62 TYR CA C 57.3 0.2 1 355 62 TYR CB C 42.5 0.2 1 356 62 TYR N N 124.8 0.1 1 357 63 LYS H H 8.48 0.03 1 358 63 LYS HA H 4.25 0.03 1 359 63 LYS C C 172.8 0.2 1 360 63 LYS CA C 55.0 0.2 1 361 63 LYS CB C 36.5 0.2 9 362 63 LYS N N 128.5 0.1 1 363 64 HIS H H 8.66 0.03 1 364 64 HIS HA H 5.23 0.03 1 365 64 HIS C C 175.2 0.2 1 366 64 HIS CA C 54.7 0.2 1 367 64 HIS CB C 31.3 0.2 1 368 64 HIS N N 123.5 0.1 1 369 65 MET H H 7.99 0.03 1 370 65 MET HA H 3.79 0.03 1 371 65 MET C C 171.4 0.2 1 372 65 MET CA C 53.8 0.2 1 373 65 MET CB C 35.9 0.2 9 374 65 MET N N 130.2 0.1 1 375 66 SER H H 7.65 0.03 1 376 66 SER HA H 3.73 0.03 1 377 66 SER C C 176.6 0.2 1 378 66 SER CA C 57.9 0.2 1 379 66 SER CB C 63.4 0.2 1 380 66 SER N N 117.3 0.1 1 381 67 ARG H H 8.34 0.03 1 382 67 ARG HA H 4.81 0.03 1 383 67 ARG C C 177.9 0.2 1 384 67 ARG CA C 60.6 0.2 1 385 67 ARG CB C 28.0 0.2 9 386 67 ARG N N 118.9 0.1 1 387 68 GLY H H 8.73 0.03 1 388 68 GLY HA2 H 3.65 0.03 9 389 68 GLY HA3 H 4.12 0.03 9 390 68 GLY C C 173.8 0.2 1 391 68 GLY CA C 47.3 0.2 1 392 68 GLY N N 105.2 0.1 1 393 69 LYS H H 7.27 0.03 1 394 69 LYS HA H 4.09 0.03 9 395 69 LYS C C 175.1 0.2 1 396 69 LYS CA C 54.9 0.2 1 397 69 LYS CB C 33.3 0.2 9 398 69 LYS N N 115.6 0.1 1 399 70 LEU H H 7.28 0.03 1 400 70 LEU HA H 3.28 0.03 1 401 70 LEU C C 176.2 0.2 1 402 70 LEU CA C 59.8 0.2 1 403 70 LEU CB C 43.4 0.2 9 404 70 LEU N N 122.7 0.1 1 405 71 GLU H H 10.22 0.03 1 406 71 GLU HA H 3.34 0.03 1 407 71 GLU C C 176.3 0.2 1 408 71 GLU CA C 62.2 0.2 1 409 71 GLU CB C 25.2 0.2 9 410 71 GLU N N 112.9 0.1 1 411 72 PRO HA H 3.27 0.03 1 412 72 PRO C C 179.0 0.2 1 413 72 PRO CA C 64.2 0.2 1 414 72 PRO CB C 29.6 0.2 9 415 73 LEU H H 7.61 0.03 1 416 73 LEU HA H 4.04 0.03 1 417 73 LEU C C 180.3 0.2 1 418 73 LEU CA C 56.2 0.2 1 419 73 LEU CB C 42.2 0.2 1 420 73 LEU N N 115.8 0.1 1 421 74 LEU H H 7.75 0.03 1 422 74 LEU HA H 3.51 0.03 9 423 74 LEU C C 180.8 0.2 1 424 74 LEU CA C 58.8 0.2 1 425 74 LEU CB C 40.1 0.2 9 426 74 LEU N N 122.1 0.1 1 427 75 ALA H H 8.29 0.03 1 428 75 ALA HA H 4.20 0.03 1 429 75 ALA C C 178.7 0.2 1 430 75 ALA CA C 56.3 0.2 1 431 75 ALA CB C 18.7 0.2 9 432 75 ALA N N 120.4 0.1 1 433 76 LYS H H 7.50 0.03 1 434 76 LYS HA H 4.68 0.03 1 435 76 LYS C C 177.4 0.2 1 436 76 LYS CA C 55.0 0.2 1 437 76 LYS CB C 31.9 0.2 1 438 76 LYS N N 114.6 0.1 1 439 77 SER H H 7.88 0.03 1 440 77 SER HA H 4.08 0.03 1 441 77 SER C C 175.5 0.2 1 442 77 SER CA C 61.3 0.2 1 443 77 SER CB C 64.4 0.2 1 444 77 SER N N 116.0 0.1 1 445 78 GLY H H 8.95 0.03 1 446 78 GLY HA2 H 3.81 0.03 2 447 78 GLY HA3 H 4.12 0.03 2 448 78 GLY C C 174.8 0.2 1 449 78 GLY CA C 45.7 0.2 1 450 78 GLY N N 111.3 0.1 1 451 79 LEU H H 7.84 0.03 1 452 79 LEU HA H 4.26 0.03 1 453 79 LEU C C 175.5 0.2 1 454 79 LEU CA C 55.2 0.2 1 455 79 LEU CB C 43.2 0.2 9 456 79 LEU N N 120.0 0.1 1 457 80 ASP H H 8.60 0.03 1 458 80 ASP HA H 4.99 0.03 1 459 80 ASP C C 176.8 0.2 1 460 80 ASP CA C 49.6 0.2 1 461 80 ASP CB C 42.2 0.2 1 462 80 ASP N N 120.8 0.1 1 463 81 PRO HA H 3.56 0.03 1 464 81 PRO C C 176.4 0.2 1 465 81 PRO CA C 64.1 0.2 1 466 81 PRO CB C 30.2 0.2 9 467 82 GLU H H 8.32 0.03 1 468 82 GLU HA H 4.12 0.03 1 469 82 GLU C C 177.7 0.2 1 470 82 GLU CA C 56.7 0.2 1 471 82 GLU CB C 29.4 0.2 1 472 82 GLU N N 117.3 0.1 1 473 83 LYS H H 8.00 0.03 1 474 83 LYS HA H 4.88 0.03 1 475 83 LYS C C 174.5 0.2 1 476 83 LYS CA C 53.1 0.2 1 477 83 LYS CB C 32.2 0.2 1 478 83 LYS N N 120.6 0.1 1 479 84 PRO HA H 5.08 0.03 1 480 84 PRO C C 174.7 0.2 1 481 84 PRO CA C 62.3 0.2 1 482 84 PRO CB C 31.9 0.2 1 483 85 VAL H H 7.79 0.03 1 484 85 VAL HA H 5.24 0.03 1 485 85 VAL C C 174.5 0.2 1 486 85 VAL CA C 58.3 0.2 1 487 85 VAL CB C 35.9 0.2 1 488 85 VAL N N 109.0 0.1 1 489 86 VAL H H 8.77 0.03 1 490 86 VAL HA H 4.84 0.03 1 491 86 VAL C C 176.0 0.2 1 492 86 VAL CA C 59.7 0.2 1 493 86 VAL CB C 33.3 0.2 9 494 86 VAL N N 121.4 0.1 1 495 87 VAL H H 9.13 0.03 1 496 87 VAL HA H 4.91 0.03 1 497 87 VAL C C 175.5 0.2 1 498 87 VAL CA C 61.1 0.2 1 499 87 VAL CB C 32.5 0.2 1 500 87 VAL N N 121.4 0.1 1 501 88 PHE H H 8.17 0.03 1 502 88 PHE HA H 5.50 0.03 1 503 88 PHE C C 174.3 0.2 1 504 88 PHE CA C 57.3 0.2 1 505 88 PHE N N 121.4 0.1 1 506 89 CYS H H 7.20 0.03 1 507 89 CYS HA H 3.65 0.03 1 508 89 CYS C C 180.7 0.2 1 509 89 CYS CA C 58.1 0.2 1 510 89 CYS N N 122.9 0.1 1 511 90 LYS H H 7.76 0.03 1 512 90 LYS HA H 4.53 0.03 1 513 90 LYS C C 175.1 0.2 1 514 90 LYS CA C 55.1 0.2 1 515 90 LYS N N 120.4 0.1 1 516 91 THR H H 8.37 0.03 1 517 91 THR HA H 4.07 0.03 9 518 91 THR C C 175.5 0.2 1 519 91 THR CA C 62.5 0.2 1 520 91 THR N N 125.2 0.1 1 521 92 ALA CA C 55.3 0.2 1 522 95 ALA HA H 3.78 0.03 1 523 95 ALA C C 177.8 0.2 1 524 95 ALA CA C 54.6 0.2 1 525 96 ALA H H 7.60 0.03 1 526 96 ALA HA H 3.83 0.03 1 527 96 ALA C C 178.7 0.2 1 528 96 ALA CA C 54.6 0.2 1 529 96 ALA CB C 18.3 0.2 9 530 96 ALA N N 120.2 0.1 1 531 97 LEU H H 7.21 0.03 1 532 97 LEU HA H 3.91 0.03 1 533 97 LEU C C 180.0 0.2 1 534 97 LEU CA C 57.8 0.2 1 535 97 LEU CB C 38.6 0.2 9 536 97 LEU N N 115.8 0.1 1 537 98 ALA H H 8.89 0.03 1 538 98 ALA HA H 4.44 0.03 1 539 98 ALA C C 179.3 0.2 1 540 98 ALA CA C 54.1 0.2 1 541 98 ALA CB C 18.7 0.2 9 542 98 ALA N N 122.3 0.1 1 543 99 GLY H H 8.87 0.03 1 544 99 GLY HA2 H 3.54 0.03 4 545 99 GLY HA3 H 3.54 0.03 4 546 99 GLY C C 174.9 0.2 1 547 99 GLY CA C 47.1 0.2 1 548 99 GLY N N 106.3 0.1 1 549 100 LYS H H 7.71 0.03 1 550 100 LYS HA H 4.07 0.03 1 551 100 LYS C C 179.0 0.2 1 552 100 LYS CA C 60.0 0.2 1 553 100 LYS CB C 31.9 0.2 1 554 100 LYS N N 124.8 0.1 1 555 101 THR H H 7.82 0.03 1 556 101 THR HA H 4.07 0.03 1 557 101 THR C C 176.7 0.2 1 558 101 THR CA C 67.3 0.2 1 559 101 THR CB C 68.4 0.2 1 560 101 THR N N 119.2 0.1 1 561 102 LEU H H 8.75 0.03 1 562 102 LEU HA H 3.80 0.03 1 563 102 LEU C C 180.1 0.2 1 564 102 LEU CA C 58.4 0.2 1 565 102 LEU CB C 39.4 0.2 1 566 102 LEU N N 119.2 0.1 1 567 103 ARG H H 8.18 0.03 1 568 103 ARG HA H 4.54 0.03 1 569 103 ARG C C 181.1 0.2 1 570 103 ARG CA C 59.6 0.2 1 571 103 ARG CB C 29.1 0.2 1 572 103 ARG N N 121.9 0.1 1 573 104 GLU H H 8.07 0.03 1 574 104 GLU HA H 4.13 0.03 5 575 104 GLU C C 178.0 0.2 1 576 104 GLU CA C 59.1 0.2 1 577 104 GLU CB C 29.3 0.2 9 578 104 GLU N N 121.4 0.1 1 579 105 TYR H H 8.12 0.03 1 580 105 TYR HA H 4.32 0.03 1 581 105 TYR C C 175.1 0.2 1 582 105 TYR CA C 60.0 0.2 1 583 105 TYR CB C 38.8 0.2 1 584 105 TYR N N 118.9 0.1 1 585 106 GLY H H 7.82 0.03 1 586 106 GLY HA2 H 3.71 0.03 2 587 106 GLY HA3 H 4.37 0.03 2 588 106 GLY C C 174.8 0.2 1 589 106 GLY CA C 45.2 0.2 1 590 106 GLY N N 105.0 0.1 1 591 107 PHE H H 8.36 0.03 1 592 107 PHE HA H 4.65 0.03 1 593 107 PHE C C 176.6 0.2 1 594 107 PHE CA C 59.2 0.2 1 595 107 PHE CB C 37.5 0.2 9 596 107 PHE N N 120.8 0.1 1 597 108 LYS H H 7.62 0.03 1 598 108 LYS HA H 4.26 0.03 1 599 108 LYS C C 177.9 0.2 1 600 108 LYS CA C 57.6 0.2 1 601 108 LYS CB C 34.4 0.2 1 602 108 LYS N N 121.4 0.1 1 603 109 THR H H 9.14 0.03 1 604 109 THR HA H 4.30 0.03 1 605 109 THR C C 172.1 0.2 1 606 109 THR CA C 62.7 0.2 1 607 109 THR CB C 69.4 0.2 1 608 109 THR N N 118.7 0.1 1 609 110 ILE H H 8.07 0.03 1 610 110 ILE HA H 4.60 0.03 1 611 110 ILE C C 174.4 0.2 1 612 110 ILE CA C 60.1 0.2 1 613 110 ILE CB C 40.3 0.2 1 614 110 ILE N N 126.4 0.1 1 615 111 TYR H H 9.10 0.03 1 616 111 TYR HA H 5.75 0.03 1 617 111 TYR C C 174.4 0.2 1 618 111 TYR CA C 55.5 0.2 1 619 111 TYR CB C 41.6 0.2 1 620 111 TYR N N 126.8 0.1 1 621 112 ASN H H 8.81 0.03 1 622 112 ASN HA H 5.39 0.03 1 623 112 ASN C C 174.8 0.2 1 624 112 ASN CA C 51.4 0.2 1 625 112 ASN CB C 41.3 0.2 1 626 112 ASN N N 118.9 0.1 1 627 113 SER H H 7.26 0.03 1 628 113 SER HA H 4.74 0.03 9 629 113 SER C C 174.6 0.2 1 630 113 SER CA C 58.3 0.2 1 631 113 SER CB C 64.0 0.2 9 632 113 SER N N 120.2 0.1 1 633 114 GLU H H 9.97 0.03 1 634 114 GLU HA H 3.85 0.03 1 635 114 GLU C C 177.8 0.2 1 636 114 GLU CA C 58.2 0.2 1 637 114 GLU CB C 29.7 0.2 1 638 114 GLU N N 134.4 0.1 1 639 115 GLY H H 8.54 0.03 1 640 115 GLY HA2 H 3.85 0.03 9 641 115 GLY HA3 H 4.05 0.03 9 642 115 GLY C C 174.4 0.2 1 643 115 GLY CA C 46.0 0.2 1 644 115 GLY N N 116.7 0.1 1 645 116 GLY H H 8.02 0.03 1 646 116 GLY C C 174.0 0.2 1 647 116 GLY CA C 45.5 0.2 1 648 116 GLY N N 105.7 0.1 1 649 117 MET H H 8.92 0.03 1 650 117 MET HA H 4.35 0.03 1 651 117 MET C C 176.8 0.2 1 652 117 MET CA C 56.5 0.2 1 653 117 MET CB C 32.2 0.2 9 654 117 MET N N 126.4 0.1 1 655 118 ASP H H 9.09 0.03 1 656 118 ASP HA H 4.40 0.03 1 657 118 ASP C C 179.5 0.2 1 658 118 ASP CA C 58.0 0.2 1 659 118 ASP CB C 39.1 0.2 1 660 118 ASP N N 118.9 0.1 1 661 119 LYS H H 7.45 0.03 1 662 119 LYS HA H 4.28 0.03 1 663 119 LYS C C 177.3 0.2 1 664 119 LYS CA C 57.5 0.2 1 665 119 LYS CB C 32.8 0.2 9 666 119 LYS N N 120.2 0.1 1 667 120 TRP H H 8.51 0.03 1 668 120 TRP HA H 3.78 0.03 1 669 120 TRP C C 178.0 0.2 1 670 120 TRP CA C 61.6 0.2 1 671 120 TRP CB C 29.4 0.2 1 672 120 TRP N N 123.3 0.1 1 673 121 LEU H H 8.57 0.03 1 674 121 LEU HA H 4.24 0.03 1 675 121 LEU C C 182.1 0.2 1 676 121 LEU CA C 57.1 0.2 1 677 121 LEU CB C 42.1 0.2 9 678 121 LEU N N 114.4 0.1 1 679 122 GLU H H 7.84 0.03 1 680 122 GLU HA H 3.98 0.03 1 681 122 GLU C C 178.7 0.2 1 682 122 GLU CA C 59.9 0.2 1 683 122 GLU CB C 30.0 0.2 1 684 122 GLU N N 122.9 0.1 1 685 123 GLU H H 8.18 0.03 1 686 123 GLU HA H 4.24 0.03 1 687 123 GLU C C 176.6 0.2 1 688 123 GLU CA C 56.5 0.2 1 689 123 GLU CB C 29.1 0.2 1 690 123 GLU N N 115.0 0.1 1 691 124 GLY H H 7.78 0.03 1 692 124 GLY HA2 H 3.73 0.03 2 693 124 GLY HA3 H 3.87 0.03 2 694 124 GLY C C 174.9 0.2 1 695 124 GLY CA C 45.9 0.2 1 696 124 GLY N N 107.5 0.1 1 697 125 LEU H H 7.33 0.03 1 698 125 LEU HA H 3.88 0.03 1 699 125 LEU C C 174.4 0.2 1 700 125 LEU CA C 53.1 0.2 1 701 125 LEU CB C 36.2 0.2 9 702 125 LEU N N 122.1 0.1 1 703 126 PRO HA H 4.39 0.03 1 704 126 PRO C C 177.7 0.2 1 705 126 PRO CA C 64.5 0.2 1 706 126 PRO CB C 32.2 0.2 9 707 127 SER H H 8.92 0.03 1 708 127 SER HA H 5.09 0.03 1 709 127 SER C C 172.2 0.2 1 710 127 SER CA C 57.6 0.2 1 711 127 SER CB C 66.9 0.2 1 712 127 SER N N 120.2 0.1 1 713 128 LEU H H 9.06 0.03 1 714 128 LEU HA H 4.64 0.03 1 715 128 LEU C C 176.1 0.2 1 716 128 LEU CA C 53.6 0.2 1 717 128 LEU CB C 44.7 0.2 9 718 128 LEU N N 121.4 0.1 1 719 129 ASP H H 8.64 0.03 1 720 129 ASP HA H 4.39 0.03 1 721 129 ASP C C 175.8 0.2 1 722 129 ASP CA C 54.6 0.2 1 723 129 ASP CB C 39.9 0.2 9 724 129 ASP N N 118.5 0.1 1 725 130 ARG H H 8.26 0.03 1 726 130 ARG HA H 4.17 0.03 1 727 130 ARG C C 176.3 0.2 1 728 130 ARG CA C 56.1 0.2 1 729 130 ARG CB C 30.0 0.2 1 730 130 ARG N N 118.1 0.1 1 731 131 SER H H 8.39 0.03 1 732 131 SER C C 174.5 0.2 1 733 131 SER CA C 58.7 0.2 1 734 131 SER CB C 64.0 0.2 9 735 131 SER N N 116.6 0.1 1 stop_ save_ save_chemical_shift_isotope_effects_CA _Saveframe_category chemical_shift_isotope_effect loop_ _Isotope_label_ID _Sample_label _Sample_conditions_label 1 $sample_1 $condition_1 2 $sample_2 $condition_1 stop_ _Isotope_effect_type "uniformly 2H labeled molecule" _Isotope_effect_value_units ppm _Isotope_effect_bond_number 1 loop_ _Isotope_effect_ID _Mol_system_component_name _Residue_seq_code _Residue_label _Atom_name _Atom_type _Atom_isotope_number _Isotope_label_one_ID _Isotope_label_one_chem_shift_value _Isotope_label_one_chem_shift_value_error _Isotope_label_two_ID _Isotope_label_two_chem_shift_value _Isotope_label_two_chem_shift_value_error _Isotope_chem_shift_effect_value _Isotope_chem_shift_effect_value_error 1 "Sud subunit 1" 3 MET CA C 13 . . . . . . -0.6 . 2 "Sud subunit 1" 4 GLY CA C 13 . . . . . . -0.6 . 3 "Sud subunit 1" 5 GLU CA C 13 . . . . . . -0.7 . 4 "Sud subunit 1" 6 LYS CA C 13 . . . . . . -0.6 . 5 "Sud subunit 1" 7 PHE CA C 13 . . . . . . -0.7 . 6 "Sud subunit 1" 8 ASP CA C 13 . . . . . . -0.7 . 7 "Sud subunit 1" 9 ALA CA C 13 . . . . . . -0.6 . 8 "Sud subunit 1" 10 THR CA C 13 . . . . . . -0.6 . 9 "Sud subunit 1" 11 PHE CA C 13 . . . . . . -0.7 . 10 "Sud subunit 1" 12 LYS CA C 13 . . . . . . -0.6 . 11 "Sud subunit 1" 13 ALA CA C 13 . . . . . . -0.7 . 12 "Sud subunit 1" 14 GLN CA C 13 . . . . . . -0.8 . 13 "Sud subunit 1" 15 VAL CA C 13 . . . . . . -0.7 . 14 "Sud subunit 1" 16 LYS CA C 13 . . . . . . -0.7 . 15 "Sud subunit 1" 17 ALA CA C 13 . . . . . . -0.7 . 16 "Sud subunit 1" 18 ALA CA C 13 . . . . . . -0.7 . 17 "Sud subunit 1" 19 LYS CA C 13 . . . . . . -0.7 . 18 "Sud subunit 1" 20 ALA CA C 13 . . . . . . -0.7 . 19 "Sud subunit 1" 21 ASP CA C 13 . . . . . . -0.7 . 20 "Sud subunit 1" 22 MET CA C 13 . . . . . . -0.6 . 21 "Sud subunit 1" 23 VAL CA C 13 . . . . . . -0.8 . 22 "Sud subunit 1" 24 MET CA C 13 . . . . . . -0.6 . 23 "Sud subunit 1" 25 LEU CA C 13 . . . . . . -0.7 . 24 "Sud subunit 1" 26 SER CA C 13 . . . . . . -0.7 . 25 "Sud subunit 1" 27 PRO CA C 13 . . . . . . -0.7 . 26 "Sud subunit 1" 28 LYS CA C 13 . . . . . . -0.8 . 27 "Sud subunit 1" 29 ASP CA C 13 . . . . . . -0.7 . 28 "Sud subunit 1" 30 ALA CA C 13 . . . . . . -0.8 . 29 "Sud subunit 1" 31 TYR CA C 13 . . . . . . -0.7 . 30 "Sud subunit 1" 32 LYS CA C 13 . . . . . . -0.8 . 31 "Sud subunit 1" 33 LEU CA C 13 . . . . . . -0.7 . 32 "Sud subunit 1" 34 LEU CA C 13 . . . . . . -0.6 . 33 "Sud subunit 1" 35 GLN CA C 13 . . . . . . -0.6 . 34 "Sud subunit 1" 36 GLU CA C 13 . . . . . . -0.6 . 35 "Sud subunit 1" 37 ASN CA C 13 . . . . . . -0.5 . 36 "Sud subunit 1" 38 PRO CA C 13 . . . . . . -0.6 . 37 "Sud subunit 1" 39 ASP CA C 13 . . . . . . -0.6 . 38 "Sud subunit 1" 40 ILE CA C 13 . . . . . . -0.7 . 39 "Sud subunit 1" 41 THR CA C 13 . . . . . . -0.8 . 40 "Sud subunit 1" 42 LEU CA C 13 . . . . . . -0.7 . 41 "Sud subunit 1" 43 ILE CA C 13 . . . . . . -0.8 . 42 "Sud subunit 1" 44 ASP CA C 13 . . . . . . -0.7 . 43 "Sud subunit 1" 46 ARG CA C 13 . . . . . . -0.7 . 44 "Sud subunit 1" 47 ASP CA C 13 . . . . . . -0.6 . 45 "Sud subunit 1" 48 PRO CA C 13 . . . . . . -0.5 . 46 "Sud subunit 1" 49 ASP CA C 13 . . . . . . -0.6 . 47 "Sud subunit 1" 50 GLU CA C 13 . . . . . . -0.7 . 48 "Sud subunit 1" 51 LEU CA C 13 . . . . . . -0.6 . 49 "Sud subunit 1" 52 LYS CA C 13 . . . . . . -0.8 . 50 "Sud subunit 1" 53 ALA CA C 13 . . . . . . -0.8 . 51 "Sud subunit 1" 54 MET CA C 13 . . . . . . -0.5 . 52 "Sud subunit 1" 55 GLY CA C 13 . . . . . . -0.7 . 53 "Sud subunit 1" 56 LYS CA C 13 . . . . . . -0.5 . 54 "Sud subunit 1" 57 PRO CA C 13 . . . . . . -0.7 . 55 "Sud subunit 1" 58 ASP CA C 13 . . . . . . -0.8 . 56 "Sud subunit 1" 59 VAL CA C 13 . . . . . . -0.6 . 57 "Sud subunit 1" 60 LYS CA C 13 . . . . . . -0.6 . 58 "Sud subunit 1" 61 ASN CA C 13 . . . . . . -0.6 . 59 "Sud subunit 1" 62 TYR CA C 13 . . . . . . -0.6 . 60 "Sud subunit 1" 63 LYS CA C 13 . . . . . . -0.7 . 61 "Sud subunit 1" 64 HIS CA C 13 . . . . . . -0.6 . 62 "Sud subunit 1" 65 MET CA C 13 . . . . . . -0.8 . 63 "Sud subunit 1" 66 SER CA C 13 . . . . . . -0.7 . 64 "Sud subunit 1" 67 ARG CA C 13 . . . . . . -0.6 . 65 "Sud subunit 1" 68 GLY CA C 13 . . . . . . -0.8 . 66 "Sud subunit 1" 69 LYS CA C 13 . . . . . . -0.8 . 67 "Sud subunit 1" 70 LEU CA C 13 . . . . . . -0.7 . 68 "Sud subunit 1" 71 GLU CA C 13 . . . . . . -0.9 . 69 "Sud subunit 1" 72 PRO CA C 13 . . . . . . -0.7 . 70 "Sud subunit 1" 73 LEU CA C 13 . . . . . . -0.8 . 71 "Sud subunit 1" 74 LEU CA C 13 . . . . . . -0.7 . 72 "Sud subunit 1" 75 ALA CA C 13 . . . . . . -0.7 . 73 "Sud subunit 1" 76 LYS CA C 13 . . . . . . -0.9 . 74 "Sud subunit 1" 77 SER CA C 13 . . . . . . -0.6 . 75 "Sud subunit 1" 78 GLY CA C 13 . . . . . . -0.8 . 76 "Sud subunit 1" 79 LEU CA C 13 . . . . . . -0.6 . 77 "Sud subunit 1" 80 ASP CA C 13 . . . . . . -0.5 . 78 "Sud subunit 1" 81 PRO CA C 13 . . . . . . -0.6 . 79 "Sud subunit 1" 82 GLU CA C 13 . . . . . . -0.6 . 80 "Sud subunit 1" 83 LYS CA C 13 . . . . . . -0.7 . 81 "Sud subunit 1" 84 PRO CA C 13 . . . . . . -0.5 . 82 "Sud subunit 1" 85 VAL CA C 13 . . . . . . -0.7 . 83 "Sud subunit 1" 86 VAL CA C 13 . . . . . . -0.8 . 84 "Sud subunit 1" 97 LEU CA C 13 . . . . . . -0.6 . 85 "Sud subunit 1" 99 GLY CA C 13 . . . . . . -0.6 . 86 "Sud subunit 1" 100 LYS CA C 13 . . . . . . -0.6 . 87 "Sud subunit 1" 101 THR CA C 13 . . . . . . -0.7 . 88 "Sud subunit 1" 102 LEU CA C 13 . . . . . . -0.8 . 89 "Sud subunit 1" 103 ARG CA C 13 . . . . . . -0.7 . 90 "Sud subunit 1" 104 GLU CA C 13 . . . . . . -0.8 . 91 "Sud subunit 1" 105 TYR CA C 13 . . . . . . -0.6 . 92 "Sud subunit 1" 106 GLY CA C 13 . . . . . . -0.7 . 93 "Sud subunit 1" 107 PHE CA C 13 . . . . . . -0.7 . 94 "Sud subunit 1" 108 LYS CA C 13 . . . . . . -0.6 . 95 "Sud subunit 1" 109 THR CA C 13 . . . . . . -0.7 . 96 "Sud subunit 1" 110 ILE CA C 13 . . . . . . -0.7 . 97 "Sud subunit 1" 111 TYR CA C 13 . . . . . . -0.5 . 98 "Sud subunit 1" 112 ASN CA C 13 . . . . . . -0.6 . 99 "Sud subunit 1" 113 SER CA C 13 . . . . . . -0.7 . 100 "Sud subunit 1" 114 GLU CA C 13 . . . . . . -0.8 . 101 "Sud subunit 1" 115 GLY CA C 13 . . . . . . -1 . 102 "Sud subunit 1" 116 GLY CA C 13 . . . . . . -0.8 . 103 "Sud subunit 1" 117 MET CA C 13 . . . . . . -0.8 . 104 "Sud subunit 1" 118 ASP CA C 13 . . . . . . -0.6 . 105 "Sud subunit 1" 119 LYS CA C 13 . . . . . . -0.8 . 106 "Sud subunit 1" 120 TRP CA C 13 . . . . . . -0.7 . 107 "Sud subunit 1" 121 LEU CA C 13 . . . . . . -0.6 . 108 "Sud subunit 1" 122 GLU CA C 13 . . . . . . -0.8 . 109 "Sud subunit 1" 123 GLU CA C 13 . . . . . . -0.9 . 110 "Sud subunit 1" 124 GLY CA C 13 . . . . . . -0.7 . 111 "Sud subunit 1" 125 LEU CA C 13 . . . . . . -0.7 . 112 "Sud subunit 1" 126 PRO CA C 13 . . . . . . -0.8 . 113 "Sud subunit 1" 127 SER CA C 13 . . . . . . -0.6 . 114 "Sud subunit 1" 128 LEU CA C 13 . . . . . . -0.6 . 115 "Sud subunit 1" 129 ASP CA C 13 . . . . . . -0.7 . 116 "Sud subunit 1" 130 ARG CA C 13 . . . . . . -0.7 . stop_ save_ save_chemical_shift_isotope_effects_CB _Saveframe_category chemical_shift_isotope_effect loop_ _Isotope_label_ID _Sample_label _Sample_conditions_label 1 $sample_1 $condition_1 2 $sample_2 $condition_1 stop_ _Isotope_effect_type "uniformly 2H labeled molecule" _Isotope_effect_value_units ppm _Isotope_effect_bond_number 1 loop_ _Isotope_effect_ID _Mol_system_component_name _Residue_seq_code _Residue_label _Atom_name _Atom_type _Atom_isotope_number _Isotope_label_one_ID _Isotope_label_one_chem_shift_value _Isotope_label_one_chem_shift_value_error _Isotope_label_two_ID _Isotope_label_two_chem_shift_value _Isotope_label_two_chem_shift_value_error _Isotope_chem_shift_effect_value _Isotope_chem_shift_effect_value_error 1 "Sud subunit 1" 2 ASP CB C 13 . . . . . . -0.5 . 2 "Sud subunit 1" 3 MET CB C 13 . . . . . . -0.9 . 3 "Sud subunit 1" 5 GLU CB C 13 . . . . . . -0.8 . 4 "Sud subunit 1" 6 LYS CB C 13 . . . . . . -1.1 . 5 "Sud subunit 1" 7 PHE CB C 13 . . . . . . -1 . 6 "Sud subunit 1" 8 ASP CB C 13 . . . . . . 0.1 . 7 "Sud subunit 1" 9 ALA CB C 13 . . . . . . -0.9 . 8 "Sud subunit 1" 10 THR CB C 13 . . . . . . -0.7 . 9 "Sud subunit 1" 11 PHE CB C 13 . . . . . . -0.9 . 10 "Sud subunit 1" 12 LYS CB C 13 . . . . . . -1 . 11 "Sud subunit 1" 13 ALA CB C 13 . . . . . . -0.9 . 12 "Sud subunit 1" 14 GLN CB C 13 . . . . . . -0.3 . 13 "Sud subunit 1" 15 VAL CB C 13 . . . . . . -1.2 . 14 "Sud subunit 1" 16 LYS CB C 13 . . . . . . -1 . 15 "Sud subunit 1" 17 ALA CB C 13 . . . . . . -0.9 . 16 "Sud subunit 1" 18 ALA CB C 13 . . . . . . -0.6 . 17 "Sud subunit 1" 19 LYS CB C 13 . . . . . . -1 . 18 "Sud subunit 1" 20 ALA CB C 13 . . . . . . -0.9 . 19 "Sud subunit 1" 21 ASP CB C 13 . . . . . . -0.7 . 20 "Sud subunit 1" 22 MET CB C 13 . . . . . . -0.8 . 21 "Sud subunit 1" 23 VAL CB C 13 . . . . . . -0.8 . 22 "Sud subunit 1" 24 MET CB C 13 . . . . . . -0.9 . 23 "Sud subunit 1" 25 LEU CB C 13 . . . . . . -0.9 . 24 "Sud subunit 1" 26 SER CB C 13 . . . . . . -0.7 . 25 "Sud subunit 1" 27 PRO CB C 13 . . . . . . -0.7 . 26 "Sud subunit 1" 28 LYS CB C 13 . . . . . . -1 . 27 "Sud subunit 1" 29 ASP CB C 13 . . . . . . -0.7 . 28 "Sud subunit 1" 30 ALA CB C 13 . . . . . . -1 . 29 "Sud subunit 1" 31 TYR CB C 13 . . . . . . -0.8 . 30 "Sud subunit 1" 32 LYS CB C 13 . . . . . . -0.9 . 31 "Sud subunit 1" 33 LEU CB C 13 . . . . . . -1.1 . 32 "Sud subunit 1" 34 LEU CB C 13 . . . . . . -1 . 33 "Sud subunit 1" 35 GLN CB C 13 . . . . . . -0.8 . 34 "Sud subunit 1" 36 GLU CB C 13 . . . . . . -0.7 . 35 "Sud subunit 1" 37 ASN CB C 13 . . . . . . -0.8 . 36 "Sud subunit 1" 38 PRO CB C 13 . . . . . . -0.7 . 37 "Sud subunit 1" 39 ASP CB C 13 . . . . . . -0.3 . 38 "Sud subunit 1" 40 ILE CB C 13 . . . . . . -1.2 . 39 "Sud subunit 1" 41 THR CB C 13 . . . . . . -0.7 . 40 "Sud subunit 1" 42 LEU CB C 13 . . . . . . -1.1 . 41 "Sud subunit 1" 43 ILE CB C 13 . . . . . . -0.5 . 42 "Sud subunit 1" 44 ASP CB C 13 . . . . . . -0.7 . 43 "Sud subunit 1" 46 ARG CB C 13 . . . . . . -1 . 44 "Sud subunit 1" 47 ASP CB C 13 . . . . . . -1.3 . 45 "Sud subunit 1" 48 PRO CB C 13 . . . . . . -0.6 . 46 "Sud subunit 1" 49 ASP CB C 13 . . . . . . -0.6 . 47 "Sud subunit 1" 50 GLU CB C 13 . . . . . . -0.8 . 48 "Sud subunit 1" 51 LEU CB C 13 . . . . . . -0.8 . 49 "Sud subunit 1" 52 LYS CB C 13 . . . . . . -1 . 50 "Sud subunit 1" 53 ALA CB C 13 . . . . . . -1 . 51 "Sud subunit 1" 54 MET CB C 13 . . . . . . -0.8 . 52 "Sud subunit 1" 56 LYS CB C 13 . . . . . . 0.1 . 53 "Sud subunit 1" 57 PRO CB C 13 . . . . . . -0.9 . 54 "Sud subunit 1" 58 ASP CB C 13 . . . . . . -0.7 . 55 "Sud subunit 1" 59 VAL CB C 13 . . . . . . -1.1 . 56 "Sud subunit 1" 60 LYS CB C 13 . . . . . . -0.7 . 57 "Sud subunit 1" 61 ASN CB C 13 . . . . . . -0.5 . 58 "Sud subunit 1" 62 TYR CB C 13 . . . . . . -1.1 . 59 "Sud subunit 1" 63 LYS CB C 13 . . . . . . -1 . 60 "Sud subunit 1" 64 HIS CB C 13 . . . . . . -1 . 61 "Sud subunit 1" 65 MET CB C 13 . . . . . . -1 . 62 "Sud subunit 1" 66 SER CB C 13 . . . . . . -0.8 . 63 "Sud subunit 1" 67 ARG CB C 13 . . . . . . -1 . 64 "Sud subunit 1" 69 LYS CB C 13 . . . . . . -1 . 65 "Sud subunit 1" 70 LEU CB C 13 . . . . . . -1.1 . 66 "Sud subunit 1" 71 GLU CB C 13 . . . . . . -0.8 . 67 "Sud subunit 1" 72 PRO CB C 13 . . . . . . -0.8 . 68 "Sud subunit 1" 73 LEU CB C 13 . . . . . . -1 . 69 "Sud subunit 1" 74 LEU CB C 13 . . . . . . -1.1 . 70 "Sud subunit 1" 75 ALA CB C 13 . . . . . . -0.9 . 71 "Sud subunit 1" 76 LYS CB C 13 . . . . . . -1 . 72 "Sud subunit 1" 77 SER CB C 13 . . . . . . -0.7 . 73 "Sud subunit 1" 79 LEU CB C 13 . . . . . . -1.1 . 74 "Sud subunit 1" 80 ASP CB C 13 . . . . . . -0.5 . 75 "Sud subunit 1" 81 PRO CB C 13 . . . . . . -0.8 . 76 "Sud subunit 1" 82 GLU CB C 13 . . . . . . -0.9 . 77 "Sud subunit 1" 83 LYS CB C 13 . . . . . . -1.3 . 78 "Sud subunit 1" 84 PRO CB C 13 . . . . . . -1 . 79 "Sud subunit 1" 85 VAL CB C 13 . . . . . . -1 . 80 "Sud subunit 1" 86 VAL CB C 13 . . . . . . -0.8 . 81 "Sud subunit 1" 97 LEU CB C 13 . . . . . . -1.1 . 82 "Sud subunit 1" 100 LYS CB C 13 . . . . . . -1 . 83 "Sud subunit 1" 101 THR CB C 13 . . . . . . -0.7 . 84 "Sud subunit 1" 102 LEU CB C 13 . . . . . . -1.2 . 85 "Sud subunit 1" 103 ARG CB C 13 . . . . . . -1 . 86 "Sud subunit 1" 104 GLU CB C 13 . . . . . . -0.8 . 87 "Sud subunit 1" 105 TYR CB C 13 . . . . . . -1.5 . 88 "Sud subunit 1" 107 PHE CB C 13 . . . . . . -0.9 . 89 "Sud subunit 1" 108 LYS CB C 13 . . . . . . -0.8 . 90 "Sud subunit 1" 109 THR CB C 13 . . . . . . -0.6 . 91 "Sud subunit 1" 110 ILE CB C 13 . . . . . . -1.1 . 92 "Sud subunit 1" 111 TYR CB C 13 . . . . . . -0.8 . 93 "Sud subunit 1" 112 ASN CB C 13 . . . . . . -0.5 . 94 "Sud subunit 1" 113 SER CB C 13 . . . . . . -0.7 . 95 "Sud subunit 1" 114 GLU CB C 13 . . . . . . -0.9 . 96 "Sud subunit 1" 117 MET CB C 13 . . . . . . -0.9 . 97 "Sud subunit 1" 118 ASP CB C 13 . . . . . . -0.5 . 98 "Sud subunit 1" 119 LYS CB C 13 . . . . . . -1 . 99 "Sud subunit 1" 120 TRP CB C 13 . . . . . . -0.6 . 100 "Sud subunit 1" 121 LEU CB C 13 . . . . . . -1.1 . 101 "Sud subunit 1" 122 GLU CB C 13 . . . . . . -0.8 . 102 "Sud subunit 1" 123 GLU CB C 13 . . . . . . -0.3 . 103 "Sud subunit 1" 126 PRO CB C 13 . . . . . . -0.8 . 104 "Sud subunit 1" 127 SER CB C 13 . . . . . . -1 . 105 "Sud subunit 1" 128 LEU CB C 13 . . . . . . -1.1 . 106 "Sud subunit 1" 129 ASP CB C 13 . . . . . . -0.7 . 107 "Sud subunit 1" 130 ARG CB C 13 . . . . . . -0.8 . 108 "Sud subunit 1" 131 SER CB C 13 . . . . . . -1.1 . stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Details "Bruker Analytische Messtechnik GmbH" save_ save_ref_2 _Saveframe_category citation _Details ; Peter Neidig, Bruker Analythische Messtechnik GmbH ; save_