data_27013 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignments (HN,N,CA,CB) of reduced n-NmDsbD ; _BMRB_accession_number 27013 _BMRB_flat_file_name bmr27013.str _Entry_type original _Submission_date 2017-01-26 _Accession_date 2017-01-26 _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 Smith Roxanne P. . 2 Mohanty Biswaranjan . . 3 Williams Martin L. . 4 Heras Begona . . 5 Scanlon Martin J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 128 "13C chemical shifts" 261 "15N chemical shifts" 128 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-02-06 update BMRB 'update entry citation' 2017-06-30 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27012 'oxidised n-NmDsbD' 27014 'oxidised c-NmDsbD' 27015 'reduced c-NmDsbD' stop_ _Original_release_date 2017-01-30 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; H(N), N, C(alpha) and C(beta) assignments of the two periplasmic domains of Neisseria meningitidis DsbD ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28589218 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Smith Roxanne P. . 2 Mohanty Biswaranjan . . 3 Williams Martin L. . 4 Scanlon Martin J. . 5 Heras Begona . . stop_ _Journal_abbreviation 'Biomol. NMR Assign.' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 11 _Journal_issue 2 _Journal_ISSN 1874-270X _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 181 _Page_last 186 _Year 2017 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'n-NmDsbD monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'N-terminal periplasmic domain NmDsbD' $Reduced_n-NmDsbD stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Reduced_n-NmDsbD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Reduced_n-NmDsbD _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 147 _Mol_residue_sequence ; MHHHHHHSSGVDLGTENLYF QSNANDLLPPEKAFVPELAV ADDGVNVRFRIADGYYMYQA KIVGKTDPADLLGQPSFSKG EEKEDEFFGRQTVYHHEAQV AFPYAKAVGEPYKLVLTYQG CAEVGVCYPPVDTEFDISGN GTYHPQT ; loop_ _Residue_seq_code _Residue_label 1 MET 2 HIS 3 HIS 4 HIS 5 HIS 6 HIS 7 HIS 8 SER 9 SER 10 GLY 11 VAL 12 ASP 13 LEU 14 GLY 15 THR 16 GLU 17 ASN 18 LEU 19 TYR 20 PHE 21 GLN 22 SER 23 ASN 24 ALA 25 ASN 26 ASP 27 LEU 28 LEU 29 PRO 30 PRO 31 GLU 32 LYS 33 ALA 34 PHE 35 VAL 36 PRO 37 GLU 38 LEU 39 ALA 40 VAL 41 ALA 42 ASP 43 ASP 44 GLY 45 VAL 46 ASN 47 VAL 48 ARG 49 PHE 50 ARG 51 ILE 52 ALA 53 ASP 54 GLY 55 TYR 56 TYR 57 MET 58 TYR 59 GLN 60 ALA 61 LYS 62 ILE 63 VAL 64 GLY 65 LYS 66 THR 67 ASP 68 PRO 69 ALA 70 ASP 71 LEU 72 LEU 73 GLY 74 GLN 75 PRO 76 SER 77 PHE 78 SER 79 LYS 80 GLY 81 GLU 82 GLU 83 LYS 84 GLU 85 ASP 86 GLU 87 PHE 88 PHE 89 GLY 90 ARG 91 GLN 92 THR 93 VAL 94 TYR 95 HIS 96 HIS 97 GLU 98 ALA 99 GLN 100 VAL 101 ALA 102 PHE 103 PRO 104 TYR 105 ALA 106 LYS 107 ALA 108 VAL 109 GLY 110 GLU 111 PRO 112 TYR 113 LYS 114 LEU 115 VAL 116 LEU 117 THR 118 TYR 119 GLN 120 GLY 121 CYS 122 ALA 123 GLU 124 VAL 125 GLY 126 VAL 127 CYS 128 TYR 129 PRO 130 PRO 131 VAL 132 ASP 133 THR 134 GLU 135 PHE 136 ASP 137 ILE 138 SER 139 GLY 140 ASN 141 GLY 142 THR 143 TYR 144 HIS 145 PRO 146 GLN 147 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Reduced_n-NmDsbD 'Neisseria meningitidis' 487 Bacteria . Neisseria meningitidis 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 $Reduced_n-NmDsbD 'recombinant technology' . Escherichia coli . pMCSG7 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1 mM protein; 10 mM Sodium Phosphate; 50 mM NaCl; pH 6.5; 40 mM DTT' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Reduced_n-NmDsbD 1 mM '[U-98% 13C; U-98% 15N]' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' 'sodium phosphate' 10 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' DTT 40 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_Topspin _Saveframe_category software _Name Topspin _Version 3.2 loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task Acquisition processing stop_ _Details Topspin3.2(pl6) save_ save_UNIO-MATCH _Saveframe_category software _Name UNIO-MATCH _Version 2.0.2 loop_ _Vendor _Address _Electronic_address 'Volk,J., Herrmann,T.,Wuthrich,K.' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Keller, K. and Wuthrich, K.' . . stop_ loop_ _Task 'chemical shift calculation' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_[15N,1H]-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D [15N,1H]-HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . pH pressure 1 . atm temperature 298 . 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 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D [15N,1H]-HSQC' '3D HNCA' '3D CBCA(CO)NH' '3D HNCACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'N-terminal periplasmic domain NmDsbD' _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 9 9 SER CA C 58.549 0.3 1 2 9 9 SER CB C 63.832 0.3 1 3 10 10 GLY H H 8.437 0.02 1 4 10 10 GLY CA C 45.249 0.3 1 5 10 10 GLY N N 111.163 0.25 1 6 11 11 VAL H H 7.892 0.02 1 7 11 11 VAL CA C 61.994 0.3 1 8 11 11 VAL CB C 32.736 0.3 1 9 11 11 VAL N N 119.126 0.25 1 10 12 12 ASP H H 8.401 0.02 1 11 12 12 ASP CA C 53.960 0.3 1 12 12 12 ASP CB C 41.070 0.3 1 13 12 12 ASP N N 124.223 0.25 1 14 13 13 LEU H H 8.349 0.02 1 15 13 13 LEU CA C 55.342 0.3 1 16 13 13 LEU CB C 42.087 0.3 1 17 13 13 LEU N N 124.095 0.25 1 18 14 14 GLY H H 8.550 0.02 1 19 14 14 GLY CA C 45.522 0.3 1 20 14 14 GLY N N 109.663 0.25 1 21 15 15 THR H H 7.985 0.02 1 22 15 15 THR CA C 62.154 0.3 1 23 15 15 THR CB C 69.428 0.3 1 24 15 15 THR N N 113.228 0.25 1 25 16 16 GLU H H 8.560 0.02 1 26 16 16 GLU CA C 57.190 0.3 1 27 16 16 GLU CB C 29.793 0.3 1 28 16 16 GLU N N 123.062 0.25 1 29 17 17 ASN H H 8.375 0.02 1 30 17 17 ASN CA C 53.381 0.3 1 31 17 17 ASN CB C 38.631 0.3 1 32 17 17 ASN N N 119.190 0.25 1 33 18 18 LEU H H 8.013 0.02 1 34 18 18 LEU CA C 55.344 0.3 1 35 18 18 LEU CB C 42.337 0.3 1 36 18 18 LEU N N 122.205 0.25 1 37 19 19 TYR H H 8.003 0.02 1 38 19 19 TYR CA C 58.002 0.3 1 39 19 19 TYR CB C 38.535 0.3 1 40 19 19 TYR N N 119.928 0.25 1 41 20 20 PHE H H 7.908 0.02 1 42 20 20 PHE CA C 57.868 0.3 1 43 20 20 PHE CB C 39.529 0.3 1 44 20 20 PHE N N 121.468 0.25 1 45 21 21 GLN H H 8.125 0.02 1 46 21 21 GLN CA C 55.772 0.3 1 47 21 21 GLN CB C 29.396 0.3 1 48 21 21 GLN N N 122.168 0.25 1 49 22 22 SER H H 8.200 0.02 1 50 22 22 SER CA C 58.608 0.3 1 51 22 22 SER CB C 63.713 0.3 1 52 22 22 SER N N 116.854 0.25 1 53 23 23 ASN H H 8.408 0.02 1 54 23 23 ASN CA C 53.182 0.3 1 55 23 23 ASN CB C 38.822 0.3 1 56 23 23 ASN N N 120.784 0.25 1 57 24 24 ALA H H 8.227 0.02 1 58 24 24 ALA CA C 52.908 0.3 1 59 24 24 ALA CB C 18.934 0.3 1 60 24 24 ALA N N 124.135 0.25 1 61 25 25 ASN H H 8.297 0.02 1 62 25 25 ASN CA C 53.512 0.3 1 63 25 25 ASN CB C 38.949 0.3 1 64 25 25 ASN N N 116.967 0.25 1 65 26 26 ASP H H 8.270 0.02 1 66 26 26 ASP CA C 54.294 0.3 1 67 26 26 ASP CB C 40.709 0.3 1 68 26 26 ASP N N 119.881 0.25 1 69 27 27 LEU H H 7.943 0.02 1 70 27 27 LEU CA C 54.322 0.3 1 71 27 27 LEU CB C 42.654 0.3 1 72 27 27 LEU N N 121.721 0.25 1 73 28 28 LEU H H 8.197 0.02 1 74 28 28 LEU CA C 52.528 0.3 1 75 28 28 LEU CB C 42.314 0.3 1 76 28 28 LEU N N 122.442 0.25 1 77 30 30 PRO CA C 65.420 0.3 1 78 30 30 PRO CB C 31.103 0.3 1 79 31 31 GLU H H 9.483 0.02 1 80 31 31 GLU CA C 58.617 0.3 1 81 31 31 GLU CB C 27.942 0.3 1 82 31 31 GLU N N 114.531 0.25 1 83 32 32 LYS H H 7.447 0.02 1 84 32 32 LYS CA C 55.671 0.3 1 85 32 32 LYS CB C 34.135 0.3 1 86 32 32 LYS N N 115.708 0.25 1 87 33 33 ALA H H 7.252 0.02 1 88 33 33 ALA CA C 53.645 0.3 1 89 33 33 ALA CB C 16.884 0.3 1 90 33 33 ALA N N 123.029 0.25 1 91 34 34 PHE H H 7.390 0.02 1 92 34 34 PHE CA C 53.876 0.3 1 93 34 34 PHE CB C 39.805 0.3 1 94 34 34 PHE N N 114.853 0.25 1 95 35 35 VAL H H 8.402 0.02 1 96 35 35 VAL CA C 59.484 0.3 1 97 35 35 VAL CB C 34.901 0.3 1 98 35 35 VAL N N 121.478 0.25 1 99 36 36 PRO CA C 61.274 0.3 1 100 36 36 PRO CB C 32.042 0.3 1 101 37 37 GLU H H 8.445 0.02 1 102 37 37 GLU CA C 55.648 0.3 1 103 37 37 GLU CB C 33.345 0.3 1 104 37 37 GLU N N 119.835 0.25 1 105 38 38 LEU H H 8.575 0.02 1 106 38 38 LEU CA C 53.488 0.3 1 107 38 38 LEU CB C 45.308 0.3 1 108 38 38 LEU N N 124.828 0.25 1 109 39 39 ALA H H 9.138 0.02 1 110 39 39 ALA CA C 51.416 0.3 1 111 39 39 ALA CB C 20.376 0.3 1 112 39 39 ALA N N 127.004 0.25 1 113 40 40 VAL H H 9.387 0.02 1 114 40 40 VAL CA C 62.941 0.3 1 115 40 40 VAL CB C 33.275 0.3 1 116 40 40 VAL N N 126.960 0.25 1 117 41 41 ALA H H 8.988 0.02 1 118 41 41 ALA CA C 50.486 0.3 1 119 41 41 ALA CB C 22.460 0.3 1 120 41 41 ALA N N 134.524 0.25 1 121 42 42 ASP H H 8.466 0.02 1 122 42 42 ASP CA C 57.270 0.3 1 123 42 42 ASP CB C 40.709 0.3 1 124 42 42 ASP N N 116.425 0.25 1 125 43 43 ASP H H 8.359 0.02 1 126 43 43 ASP CA C 53.370 0.3 1 127 43 43 ASP CB C 40.388 0.3 1 128 43 43 ASP N N 111.899 0.25 1 129 44 44 GLY H H 7.385 0.02 1 130 44 44 GLY CA C 44.197 0.3 1 131 44 44 GLY N N 112.052 0.25 1 132 45 45 VAL H H 8.304 0.02 1 133 45 45 VAL CA C 60.705 0.3 1 134 45 45 VAL CB C 34.910 0.3 1 135 45 45 VAL N N 117.653 0.25 1 136 46 46 ASN H H 9.099 0.02 1 137 46 46 ASN CA C 52.446 0.3 1 138 46 46 ASN CB C 41.352 0.3 1 139 46 46 ASN N N 127.018 0.25 1 140 47 47 VAL H H 9.598 0.02 1 141 47 47 VAL CA C 60.689 0.3 1 142 47 47 VAL CB C 33.190 0.3 1 143 47 47 VAL N N 126.090 0.25 1 144 48 48 ARG H H 8.631 0.02 1 145 48 48 ARG CA C 54.074 0.3 1 146 48 48 ARG CB C 32.725 0.3 1 147 48 48 ARG N N 127.745 0.25 1 148 49 49 PHE H H 9.133 0.02 1 149 49 49 PHE CA C 57.056 0.3 1 150 49 49 PHE CB C 41.662 0.3 1 151 49 49 PHE N N 122.149 0.25 1 152 50 50 ARG H H 8.706 0.02 1 153 50 50 ARG CA C 55.758 0.3 1 154 50 50 ARG CB C 30.784 0.3 1 155 50 50 ARG N N 123.493 0.25 1 156 51 51 ILE H H 8.014 0.02 1 157 51 51 ILE CA C 59.908 0.3 1 158 51 51 ILE CB C 39.748 0.3 1 159 51 51 ILE N N 127.996 0.25 1 160 52 52 ALA H H 8.558 0.02 1 161 52 52 ALA CA C 52.569 0.3 1 162 52 52 ALA CB C 19.574 0.3 1 163 52 52 ALA N N 131.865 0.25 1 164 53 53 ASP H H 8.857 0.02 1 165 53 53 ASP CA C 56.209 0.3 1 166 53 53 ASP CB C 40.377 0.3 1 167 53 53 ASP N N 123.424 0.25 1 168 54 54 GLY H H 9.373 0.02 1 169 54 54 GLY CA C 44.931 0.3 1 170 54 54 GLY N N 111.157 0.25 1 171 55 55 TYR H H 8.021 0.02 1 172 55 55 TYR CA C 56.833 0.3 1 173 55 55 TYR CB C 41.190 0.3 1 174 55 55 TYR N N 120.707 0.25 1 175 56 56 TYR H H 8.933 0.02 1 176 56 56 TYR CA C 55.530 0.3 1 177 56 56 TYR CB C 39.720 0.3 1 178 56 56 TYR N N 113.913 0.25 1 179 57 57 MET H H 8.525 0.02 1 180 57 57 MET CA C 54.166 0.3 1 181 57 57 MET CB C 38.102 0.3 1 182 57 57 MET N N 115.738 0.25 1 183 58 58 TYR H H 7.448 0.02 1 184 58 58 TYR CA C 58.063 0.3 1 185 58 58 TYR CB C 38.407 0.3 1 186 58 58 TYR N N 119.562 0.25 1 187 59 59 GLN H H 8.434 0.02 1 188 59 59 GLN CA C 59.986 0.3 1 189 59 59 GLN CB C 30.821 0.3 1 190 59 59 GLN N N 129.203 0.25 1 191 60 60 ALA H H 9.411 0.02 1 192 60 60 ALA CA C 53.351 0.3 1 193 60 60 ALA CB C 18.585 0.3 1 194 60 60 ALA N N 116.261 0.25 1 195 61 61 LYS H H 6.797 0.02 1 196 61 61 LYS CA C 53.104 0.3 1 197 61 61 LYS CB C 32.822 0.3 1 198 61 61 LYS N N 113.551 0.25 1 199 62 62 ILE H H 7.085 0.02 1 200 62 62 ILE CA C 62.104 0.3 1 201 62 62 ILE CB C 38.407 0.3 1 202 62 62 ILE N N 120.075 0.25 1 203 63 63 VAL H H 9.095 0.02 1 204 63 63 VAL CA C 60.951 0.3 1 205 63 63 VAL CB C 36.949 0.3 1 206 63 63 VAL N N 128.051 0.25 1 207 64 64 GLY H H 9.026 0.02 1 208 64 64 GLY CA C 43.911 0.3 1 209 64 64 GLY N N 111.457 0.25 1 210 65 65 LYS H H 8.694 0.02 1 211 65 65 LYS CA C 54.921 0.3 1 212 65 65 LYS CB C 36.169 0.3 1 213 65 65 LYS N N 123.453 0.25 1 214 66 66 THR H H 8.761 0.02 1 215 66 66 THR CA C 59.334 0.3 1 216 66 66 THR CB C 73.631 0.3 1 217 66 66 THR N N 111.532 0.25 1 218 67 67 ASP H H 8.529 0.02 1 219 67 67 ASP CA C 51.706 0.3 1 220 67 67 ASP CB C 43.620 0.3 1 221 67 67 ASP N N 119.943 0.25 1 222 68 68 PRO CA C 63.322 0.3 1 223 68 68 PRO CB C 34.622 0.3 1 224 69 69 ALA H H 8.502 0.02 1 225 69 69 ALA CA C 52.653 0.3 1 226 69 69 ALA CB C 19.957 0.3 1 227 69 69 ALA N N 122.927 0.25 1 228 70 70 ASP H H 8.532 0.02 1 229 70 70 ASP CA C 55.740 0.3 1 230 70 70 ASP CB C 37.921 0.3 1 231 70 70 ASP N N 113.307 0.25 1 232 71 71 LEU H H 7.067 0.02 1 233 71 71 LEU CA C 56.686 0.3 1 234 71 71 LEU CB C 42.419 0.3 1 235 71 71 LEU N N 115.414 0.25 1 236 72 72 LEU H H 8.725 0.02 1 237 72 72 LEU CA C 53.256 0.3 1 238 72 72 LEU CB C 42.632 0.3 1 239 72 72 LEU N N 117.310 0.25 1 240 73 73 GLY H H 8.920 0.02 1 241 73 73 GLY CA C 42.796 0.3 1 242 73 73 GLY N N 108.827 0.25 1 243 74 74 GLN H H 8.315 0.02 1 244 74 74 GLN CA C 53.722 0.3 1 245 74 74 GLN CB C 28.402 0.3 1 246 74 74 GLN N N 120.286 0.25 1 247 75 75 PRO CA C 61.647 0.3 1 248 75 75 PRO CB C 31.872 0.3 1 249 76 76 SER H H 8.436 0.02 1 250 76 76 SER CA C 56.692 0.3 1 251 76 76 SER CB C 64.624 0.3 1 252 76 76 SER N N 114.175 0.25 1 253 77 77 PHE H H 8.884 0.02 1 254 77 77 PHE CA C 58.153 0.3 1 255 77 77 PHE CB C 42.223 0.3 1 256 77 77 PHE N N 123.878 0.25 1 257 78 78 SER H H 8.659 0.02 1 258 78 78 SER CA C 58.417 0.3 1 259 78 78 SER CB C 63.516 0.3 1 260 78 78 SER N N 117.722 0.25 1 261 79 79 LYS H H 9.025 0.02 1 262 79 79 LYS CA C 58.383 0.3 1 263 79 79 LYS CB C 32.586 0.3 1 264 79 79 LYS N N 124.559 0.25 1 265 80 80 GLY H H 8.874 0.02 1 266 80 80 GLY CA C 44.113 0.3 1 267 80 80 GLY N N 116.292 0.25 1 268 81 81 GLU H H 8.854 0.02 1 269 81 81 GLU CA C 54.208 0.3 1 270 81 81 GLU CB C 33.428 0.3 1 271 81 81 GLU N N 120.237 0.25 1 272 82 82 GLU H H 8.704 0.02 1 273 82 82 GLU CA C 56.562 0.3 1 274 82 82 GLU CB C 30.814 0.3 1 275 82 82 GLU N N 122.636 0.25 1 276 83 83 LYS H H 8.964 0.02 1 277 83 83 LYS CA C 54.947 0.3 1 278 83 83 LYS CB C 37.770 0.3 1 279 83 83 LYS N N 127.422 0.25 1 280 84 84 GLU H H 8.452 0.02 1 281 84 84 GLU CA C 54.742 0.3 1 282 84 84 GLU CB C 30.948 0.3 1 283 84 84 GLU N N 125.541 0.25 1 284 85 85 ASP H H 8.147 0.02 1 285 85 85 ASP CA C 52.471 0.3 1 286 85 85 ASP CB C 43.793 0.3 1 287 85 85 ASP N N 124.307 0.25 1 288 86 86 GLU H H 8.875 0.02 1 289 86 86 GLU CA C 56.933 0.3 1 290 86 86 GLU CB C 29.111 0.3 1 291 86 86 GLU N N 117.883 0.25 1 292 87 87 PHE H H 8.085 0.02 1 293 87 87 PHE CA C 59.185 0.3 1 294 87 87 PHE CB C 39.498 0.3 1 295 87 87 PHE N N 122.049 0.25 1 296 88 88 PHE H H 8.772 0.02 1 297 88 88 PHE CA C 56.968 0.3 1 298 88 88 PHE CB C 40.629 0.3 1 299 88 88 PHE N N 114.909 0.25 1 300 89 89 GLY H H 7.656 0.02 1 301 89 89 GLY CA C 46.109 0.3 1 302 89 89 GLY N N 111.926 0.25 1 303 90 90 ARG H H 8.633 0.02 1 304 90 90 ARG CA C 56.864 0.3 1 305 90 90 ARG CB C 29.486 0.3 1 306 90 90 ARG N N 126.206 0.25 1 307 91 91 GLN H H 9.058 0.02 1 308 91 91 GLN CA C 53.420 0.3 1 309 91 91 GLN CB C 33.779 0.3 1 310 91 91 GLN N N 126.642 0.25 1 311 92 92 THR H H 8.495 0.02 1 312 92 92 THR CA C 62.910 0.3 1 313 92 92 THR CB C 67.991 0.3 1 314 92 92 THR N N 117.590 0.25 1 315 93 93 VAL H H 9.766 0.02 1 316 93 93 VAL CA C 57.884 0.3 1 317 93 93 VAL CB C 36.069 0.3 1 318 93 93 VAL N N 124.121 0.25 1 319 94 94 TYR H H 8.549 0.02 1 320 94 94 TYR CA C 56.275 0.3 1 321 94 94 TYR CB C 42.693 0.3 1 322 94 94 TYR N N 115.225 0.25 1 323 95 95 HIS H H 9.139 0.02 1 324 95 95 HIS CA C 55.879 0.3 1 325 95 95 HIS CB C 31.025 0.3 1 326 95 95 HIS N N 118.590 0.25 1 327 96 96 HIS H H 9.472 0.02 1 328 96 96 HIS CA C 61.253 0.3 1 329 96 96 HIS CB C 28.104 0.3 1 330 96 96 HIS N N 116.218 0.25 1 331 97 97 GLU H H 9.923 0.02 1 332 97 97 GLU CA C 55.395 0.3 1 333 97 97 GLU CB C 33.825 0.3 1 334 97 97 GLU N N 125.646 0.25 1 335 98 98 ALA H H 7.889 0.02 1 336 98 98 ALA CA C 51.639 0.3 1 337 98 98 ALA CB C 22.014 0.3 1 338 98 98 ALA N N 121.725 0.25 1 339 99 99 GLN H H 8.029 0.02 1 340 99 99 GLN CA C 54.904 0.3 1 341 99 99 GLN CB C 31.744 0.3 1 342 99 99 GLN N N 120.667 0.25 1 343 100 100 VAL H H 9.016 0.02 1 344 100 100 VAL CA C 60.215 0.3 1 345 100 100 VAL CB C 34.892 0.3 1 346 100 100 VAL N N 124.143 0.25 1 347 101 101 ALA H H 8.472 0.02 1 348 101 101 ALA CA C 50.300 0.3 1 349 101 101 ALA CB C 20.705 0.3 1 350 101 101 ALA N N 130.456 0.25 1 351 102 102 PHE H H 9.186 0.02 1 352 102 102 PHE CA C 54.004 0.3 1 353 102 102 PHE CB C 41.470 0.3 1 354 102 102 PHE N N 121.249 0.25 1 355 103 103 PRO CA C 61.681 0.3 1 356 103 103 PRO CB C 31.634 0.3 1 357 104 104 TYR H H 8.130 0.02 1 358 104 104 TYR CA C 57.250 0.3 1 359 104 104 TYR CB C 37.883 0.3 1 360 104 104 TYR N N 120.126 0.25 1 361 105 105 ALA H H 9.262 0.02 1 362 105 105 ALA CA C 52.474 0.3 1 363 105 105 ALA CB C 19.442 0.3 1 364 105 105 ALA N N 126.429 0.25 1 365 106 106 LYS H H 7.627 0.02 1 366 106 106 LYS CA C 53.961 0.3 1 367 106 106 LYS CB C 34.796 0.3 1 368 106 106 LYS N N 115.393 0.25 1 369 107 107 ALA H H 8.074 0.02 1 370 107 107 ALA CA C 52.545 0.3 1 371 107 107 ALA CB C 18.152 0.3 1 372 107 107 ALA N N 121.937 0.25 1 373 108 108 VAL H H 8.055 0.02 1 374 108 108 VAL CA C 62.220 0.3 1 375 108 108 VAL CB C 33.235 0.3 1 376 108 108 VAL N N 123.728 0.25 1 377 109 109 GLY H H 8.627 0.02 1 378 109 109 GLY CA C 45.001 0.3 1 379 109 109 GLY N N 115.089 0.25 1 380 110 110 GLU H H 7.311 0.02 1 381 110 110 GLU CA C 53.697 0.3 1 382 110 110 GLU CB C 30.896 0.3 1 383 110 110 GLU N N 119.596 0.25 1 384 111 111 PRO CA C 63.142 0.3 1 385 111 111 PRO CB C 32.680 0.3 1 386 112 112 TYR H H 8.273 0.02 1 387 112 112 TYR CA C 55.999 0.3 1 388 112 112 TYR CB C 41.520 0.3 1 389 112 112 TYR N N 116.623 0.25 1 390 113 113 LYS H H 8.435 0.02 1 391 113 113 LYS CA C 54.194 0.3 1 392 113 113 LYS CB C 35.197 0.3 1 393 113 113 LYS N N 119.920 0.25 1 394 114 114 LEU H H 9.054 0.02 1 395 114 114 LEU CA C 53.723 0.3 1 396 114 114 LEU CB C 46.263 0.3 1 397 114 114 LEU N N 127.742 0.25 1 398 115 115 VAL H H 9.410 0.02 1 399 115 115 VAL CA C 61.676 0.3 1 400 115 115 VAL CB C 33.004 0.3 1 401 115 115 VAL N N 127.207 0.25 1 402 116 116 LEU H H 9.322 0.02 1 403 116 116 LEU CA C 52.792 0.3 1 404 116 116 LEU CB C 46.142 0.3 1 405 116 116 LEU N N 132.214 0.25 1 406 117 117 THR H H 9.524 0.02 1 407 117 117 THR CA C 61.295 0.3 1 408 117 117 THR CB C 71.071 0.3 1 409 117 117 THR N N 124.522 0.25 1 410 118 118 TYR H H 8.242 0.02 1 411 118 118 TYR CA C 55.658 0.3 1 412 118 118 TYR CB C 38.754 0.3 1 413 118 118 TYR N N 118.714 0.25 1 414 119 119 GLN H H 7.956 0.02 1 415 119 119 GLN CA C 54.809 0.3 1 416 119 119 GLN CB C 32.769 0.3 1 417 119 119 GLN N N 117.867 0.25 1 418 120 120 GLY H H 7.904 0.02 1 419 120 120 GLY CA C 45.683 0.3 1 420 120 120 GLY N N 114.760 0.25 1 421 121 121 CYS H H 8.536 0.02 1 422 121 121 CYS CA C 57.028 0.3 1 423 121 121 CYS CB C 31.759 0.3 1 424 121 121 CYS N N 116.910 0.25 1 425 122 122 ALA H H 9.122 0.02 1 426 122 122 ALA CA C 50.971 0.3 1 427 122 122 ALA CB C 21.376 0.3 1 428 122 122 ALA N N 125.436 0.25 1 429 123 123 GLU H H 8.924 0.02 1 430 123 123 GLU CA C 59.467 0.3 1 431 123 123 GLU CB C 29.414 0.3 1 432 123 123 GLU N N 125.825 0.25 1 433 124 124 VAL H H 7.504 0.02 1 434 124 124 VAL CA C 63.033 0.3 1 435 124 124 VAL CB C 31.333 0.3 1 436 124 124 VAL N N 110.837 0.25 1 437 125 125 GLY H H 8.324 0.02 1 438 125 125 GLY CA C 45.844 0.3 1 439 125 125 GLY N N 108.966 0.25 1 440 126 126 VAL H H 6.869 0.02 1 441 126 126 VAL CA C 61.482 0.3 1 442 126 126 VAL CB C 35.348 0.3 1 443 126 126 VAL N N 119.734 0.25 1 444 127 127 CYS H H 8.265 0.02 1 445 127 127 CYS CA C 58.551 0.3 1 446 127 127 CYS CB C 25.653 0.3 1 447 127 127 CYS N N 129.927 0.25 1 448 128 128 TYR H H 8.616 0.02 1 449 128 128 TYR CA C 56.974 0.3 1 450 128 128 TYR CB C 37.621 0.3 1 451 128 128 TYR N N 131.064 0.25 1 452 130 130 PRO CA C 62.727 0.3 1 453 130 130 PRO CB C 31.255 0.3 1 454 131 131 VAL H H 8.572 0.02 1 455 131 131 VAL CA C 60.511 0.3 1 456 131 131 VAL CB C 34.892 0.3 1 457 131 131 VAL N N 123.498 0.25 1 458 132 132 ASP H H 7.859 0.02 1 459 132 132 ASP CA C 51.961 0.3 1 460 132 132 ASP CB C 43.069 0.3 1 461 132 132 ASP N N 121.621 0.25 1 462 133 133 THR H H 9.462 0.02 1 463 133 133 THR CA C 61.955 0.3 1 464 133 133 THR CB C 71.117 0.3 1 465 133 133 THR N N 120.664 0.25 1 466 134 134 GLU H H 8.567 0.02 1 467 134 134 GLU CA C 54.896 0.3 1 468 134 134 GLU CB C 32.178 0.3 1 469 134 134 GLU N N 127.157 0.25 1 470 135 135 PHE H H 9.425 0.02 1 471 135 135 PHE CA C 56.440 0.3 1 472 135 135 PHE CB C 42.712 0.3 1 473 135 135 PHE N N 121.333 0.25 1 474 136 136 ASP H H 8.687 0.02 1 475 136 136 ASP CA C 53.705 0.3 1 476 136 136 ASP CB C 40.674 0.3 1 477 136 136 ASP N N 124.645 0.25 1 478 137 137 ILE H H 8.399 0.02 1 479 137 137 ILE CA C 60.448 0.3 1 480 137 137 ILE CB C 36.827 0.3 1 481 137 137 ILE N N 126.666 0.25 1 482 138 138 SER H H 7.834 0.02 1 483 138 138 SER CA C 57.039 0.3 1 484 138 138 SER CB C 62.968 0.3 1 485 138 138 SER N N 120.756 0.25 1 486 139 139 GLY H H 7.503 0.02 1 487 139 139 GLY CA C 43.840 0.3 1 488 139 139 GLY N N 110.570 0.25 1 489 140 140 ASN H H 8.609 0.02 1 490 140 140 ASN CA C 53.627 0.3 1 491 140 140 ASN CB C 38.084 0.3 1 492 140 140 ASN N N 120.515 0.25 1 493 141 141 GLY H H 8.672 0.02 1 494 141 141 GLY CA C 44.446 0.3 1 495 141 141 GLY N N 108.519 0.25 1 496 142 142 THR H H 8.255 0.02 1 497 142 142 THR CA C 61.451 0.3 1 498 142 142 THR CB C 70.105 0.3 1 499 142 142 THR N N 116.631 0.25 1 500 143 143 TYR H H 9.103 0.02 1 501 143 143 TYR CA C 57.250 0.3 1 502 143 143 TYR CB C 41.737 0.3 1 503 143 143 TYR N N 124.644 0.25 1 504 144 144 HIS H H 8.836 0.02 1 505 144 144 HIS CA C 53.228 0.3 1 506 144 144 HIS CB C 30.820 0.3 1 507 144 144 HIS N N 120.325 0.25 1 508 145 145 PRO CA C 63.065 0.3 1 509 145 145 PRO CB C 32.113 0.3 1 510 146 146 GLN H H 8.813 0.02 1 511 146 146 GLN CA C 55.949 0.3 1 512 146 146 GLN CB C 29.421 0.3 1 513 146 146 GLN N N 122.897 0.25 1 514 147 147 THR H H 7.841 0.02 1 515 147 147 THR CA C 62.977 0.3 1 516 147 147 THR CB C 70.639 0.3 1 517 147 147 THR N N 121.149 0.25 1 stop_ save_