data_18567 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Overexpression, purification and structural characterization of S114A mutant of UVI31+ from chlamydomonas reinhardtii ; _BMRB_accession_number 18567 _BMRB_flat_file_name bmr18567.str _Entry_type original _Submission_date 2012-07-05 _Accession_date 2012-07-05 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Overexpression, purification and structural characterization of S114A mutant of UVI31+ from chlamydomonas reinhardtii' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Singh Himanshu . . 2 Chary Kandala V. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 107 "13C chemical shifts" 314 "15N chemical shifts" 107 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-05-13 update BMRB 'update entry citation' 2013-02-28 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16864 'Sequence Specific 1H, 13C and 15N backbone resonance assignments of uvi31+ from Chlamydomonas reinhardtii' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'H, 13C and 15N resonance assignments of S114A mutant of UVI31+ from Chlamydomonas reinhardtii.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23266947 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Singh Himanshu . . 2 Raghavan Vandana . . 3 Shukla Manish . . 4 Rao Basuthkar J. . 5 Chary Kandala V.R. . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 8 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 71 _Page_last 74 _Year 2014 _Details . loop_ _Keyword 'S114A mutant of UVI31+' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'S114A mutant of UVI31+' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'S114A mutant of UVI31+' $S114A_mutant_of_UVI31+ stop_ _System_molecular_weight 13360 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_S114A_mutant_of_UVI31+ _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common S114A_mutant_of_UVI31+ _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 123 _Mol_residue_sequence ; MRGSHHHHHHGSHVISSIAS RGSMAEHQLGPIAGAIKSKV EAALSPTHFKLINDSHKHAG HYARDGSTASDAGETHFRLE VTSDAFKGLTLVKRHQLIYG LLSDEFKAGLHALAMTTKTP AEQ ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ARG 3 3 GLY 4 4 SER 5 5 HIS 6 6 HIS 7 7 HIS 8 8 HIS 9 9 HIS 10 10 HIS 11 11 GLY 12 12 SER 13 13 HIS 14 14 VAL 15 15 ILE 16 16 SER 17 17 SER 18 18 ILE 19 19 ALA 20 20 SER 21 21 ARG 22 22 GLY 23 23 SER 24 24 MET 25 25 ALA 26 26 GLU 27 27 HIS 28 28 GLN 29 29 LEU 30 30 GLY 31 31 PRO 32 32 ILE 33 33 ALA 34 34 GLY 35 35 ALA 36 36 ILE 37 37 LYS 38 38 SER 39 39 LYS 40 40 VAL 41 41 GLU 42 42 ALA 43 43 ALA 44 44 LEU 45 45 SER 46 46 PRO 47 47 THR 48 48 HIS 49 49 PHE 50 50 LYS 51 51 LEU 52 52 ILE 53 53 ASN 54 54 ASP 55 55 SER 56 56 HIS 57 57 LYS 58 58 HIS 59 59 ALA 60 60 GLY 61 61 HIS 62 62 TYR 63 63 ALA 64 64 ARG 65 65 ASP 66 66 GLY 67 67 SER 68 68 THR 69 69 ALA 70 70 SER 71 71 ASP 72 72 ALA 73 73 GLY 74 74 GLU 75 75 THR 76 76 HIS 77 77 PHE 78 78 ARG 79 79 LEU 80 80 GLU 81 81 VAL 82 82 THR 83 83 SER 84 84 ASP 85 85 ALA 86 86 PHE 87 87 LYS 88 88 GLY 89 89 LEU 90 90 THR 91 91 LEU 92 92 VAL 93 93 LYS 94 94 ARG 95 95 HIS 96 96 GLN 97 97 LEU 98 98 ILE 99 99 TYR 100 100 GLY 101 101 LEU 102 102 LEU 103 103 SER 104 104 ASP 105 105 GLU 106 106 PHE 107 107 LYS 108 108 ALA 109 109 GLY 110 110 LEU 111 111 HIS 112 112 ALA 113 113 LEU 114 114 ALA 115 115 MET 116 116 THR 117 117 THR 118 118 LYS 119 119 THR 120 120 PRO 121 121 ALA 122 122 GLU 123 123 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 18969 S55A_of_UVI31+ 100.00 123 100.00 100.00 8.20e-81 BMRB 19307 UVI31+Mg 100.00 123 99.19 100.00 2.17e-80 BMRB 19308 Phophorylated_UVI31+ 100.00 123 99.19 100.00 2.17e-80 PDB 2MA0 "Nmr Structural Of Uvi31+" 100.00 123 99.19 100.00 2.17e-80 GB EDO96758 "predicted protein [Chlamydomonas reinhardtii]" 81.30 100 99.00 100.00 6.62e-64 REF XP_001702905 "predicted protein [Chlamydomonas reinhardtii]" 81.30 100 99.00 100.00 6.62e-64 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $S114A_mutant_of_UVI31+ 'Green algae' 3055 Eukaryota . Chlamydomonas reinhardtii cc125 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 $S114A_mutant_of_UVI31+ 'cell free synthesis' . chlamydomonas reinhardtii cc125 'pET and pQE-30' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; Uniformly 15N-labelled (u-15N UVI31+) and uniformly 13C/15N doubly-labelled (u-13C/15N UVI31+) samples were produced in minimal (M9) media. E. coli strain BL21 (DE3) harboring the vector pET was grown in the appropriate minimal (M9) medium containing ampicillin (100 mg/ml) to an absorbance A600 of 0.5 at 33 C. The cells were harvested and resuspended in fresh minimal (M9) medium without ampicillin, followed by induction with 1 mM IPTG at 25 C for overnight. Cells were collected by centrifugation, resuspended in lysis buffer [50 mM sodium phosphate (pH 7.6), 50 mM NaCl, 1 mM PMSF, 5 mM Imidazole, 2% Tween 20, and 1 mg/ml lysozyme] and incubated on ice for 30 min. Cells were disrupted by ultrasonication. The cell debris was removed by centrifugation (15,000 rpm for 20 min at 4 C). The UVI31+ protein was purified from the resulting supernatant using Ni NTA (Ni2+-nitrilotriacetate) agarose (Qiagen, Hilden, Germany). His6-tagged UVI31+ was eluted with 250 mM imidazole in 50 mM sodium phosphate (pH 7.6), 50 mM NaCl. The eluted fractions were dialyzed overnight against 50 mM sodium phosphate (pH 6.4), 50 mM NaCl at 4 C. The protein was further purified by gel filtration using a Sephadex G75 column (GE healthcare, USA) equilibrated with 50 mM sodium phosphate (pH 6.4), 50 mM NaCl. The recombinant protein eluted at a volume corresponding to a monomer of approximately 13 kDa. N-terminal amino acid sequence analysis was performed by the Proteomics International Pty Ltd, Australia. The UVI31+ was quantitated by Bradfords with bovine serum albumin as a standard, and by measuring absorbance at 280 nm (Bradford 1976). Typical yields were 25 30 mg/l of culture. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $S114A_mutant_of_UVI31+ 0.8 mM '[U-100% 13C; U-100% 15N]' H2O 90 % 'natural abundance' D2O 10 % [U-2H] stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name FELIX _Version 2002 loop_ _Vendor _Address _Electronic_address 'accelrys Inc.' 'San diego' . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _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_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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 'ionic strength' 0.1 . M pH 6.4 . 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 cylindrical 'insert at center of experimental sample tube' . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct cylindrical 'insert at center of experimental sample tube' . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect cylindrical 'insert at center of experimental sample tube' . 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 'experiments performed, 15N-H HSQC, HNCO,HNCACO, CBCANH, CBCACONH.' loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCA' '3D HNCACB' '3D CBCA(CO)NH' 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 'S114A mutant of UVI31+' _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 11 11 GLY H H 8.416 0.02 1 2 11 11 GLY C C 173.642 0.3 1 3 11 11 GLY CA C 44.663 0.3 1 4 11 11 GLY N N 109.392 0.3 1 5 12 12 SER H H 8.29 0.02 1 6 12 12 SER C C 174.247 0.3 1 7 12 12 SER CA C 57.67 0.3 1 8 12 12 SER CB C 63.081 0.3 1 9 12 12 SER N N 115.599 0.3 1 10 13 13 HIS H H 8.34 0.02 1 11 13 13 HIS C C 176.327 0.3 1 12 13 13 HIS CA C 55.867 0.3 1 13 13 13 HIS CB C 29.856 0.3 1 14 13 13 HIS N N 122.786 0.3 1 15 14 14 VAL H H 7.51 0.02 1 16 14 14 VAL C C 173.982 0.3 1 17 14 14 VAL CA C 57.67 0.3 1 18 14 14 VAL CB C 31.73 0.3 1 19 14 14 VAL N N 115.416 0.3 1 20 15 15 ILE H H 8.112 0.02 1 21 15 15 ILE C C 175.344 0.3 1 22 15 15 ILE CA C 60.898 0.3 1 23 15 15 ILE CB C 37.735 0.3 1 24 15 15 ILE N N 122.061 0.3 1 25 16 16 SER H H 8.322 0.02 1 26 16 16 SER C C 175.571 0.3 1 27 16 16 SER CA C 60.225 0.3 1 28 16 16 SER CB C 64.889 0.3 1 29 16 16 SER N N 125.407 0.3 1 30 17 17 SER H H 8.426 0.02 1 31 17 17 SER C C 173.869 0.3 1 32 17 17 SER CA C 55.006 0.3 1 33 17 17 SER CB C 65.356 0.3 1 34 17 17 SER N N 120.273 0.3 1 35 18 18 ILE H H 8.149 0.02 1 36 18 18 ILE C C 175.684 0.3 1 37 18 18 ILE CA C 61.562 0.3 1 38 18 18 ILE CB C 39.948 0.3 1 39 18 18 ILE N N 122.116 0.3 1 40 19 19 ALA H H 8.285 0.02 1 41 19 19 ALA C C 177.424 0.3 1 42 19 19 ALA CA C 51.969 0.3 1 43 19 19 ALA CB C 18.285 0.3 1 44 19 19 ALA N N 127.023 0.3 1 45 20 20 SER H H 8.211 0.02 1 46 20 20 SER C C 174.323 0.3 1 47 20 20 SER CA C 57.758 0.3 1 48 20 20 SER CB C 63.071 0.3 1 49 20 20 SER N N 114.737 0.3 1 50 24 24 MET H H 8.429 0.02 1 51 24 24 MET C C 175.571 0.3 1 52 24 24 MET CA C 55.012 0.3 1 53 24 24 MET CB C 31.66 0.3 1 54 24 24 MET N N 121.879 0.3 1 55 25 25 ALA H H 8.203 0.02 1 56 25 25 ALA C C 177.235 0.3 1 57 25 25 ALA CA C 52.159 0.3 1 58 25 25 ALA CB C 18.38 0.3 1 59 25 25 ALA N N 124.418 0.3 1 60 26 26 GLU H H 8.302 0.02 1 61 26 26 GLU C C 173.415 0.3 1 62 26 26 GLU CA C 58.308 0.3 1 63 26 26 GLU CB C 29.387 0.3 1 64 26 26 GLU N N 119.327 0.3 1 65 27 27 HIS H H 8.122 0.02 1 66 27 27 HIS C C 173.869 0.3 1 67 27 27 HIS CA C 54.911 0.3 1 68 27 27 HIS CB C 28.628 0.3 1 69 27 27 HIS N N 118.213 0.3 1 70 28 28 GLN H H 8.371 0.02 1 71 28 28 GLN C C 175.079 0.3 1 72 28 28 GLN CA C 54.911 0.3 1 73 28 28 GLN CB C 28.628 0.3 1 74 28 28 GLN N N 121.309 0.3 1 75 29 29 LEU H H 8.417 0.02 1 76 29 29 LEU C C 177.921 0.3 1 77 29 29 LEU CA C 54.911 0.3 1 78 29 29 LEU CB C 42.007 0.3 1 79 29 29 LEU N N 123.827 0.3 1 80 30 30 GLY H H 8.519 0.02 1 81 30 30 GLY C C 172.452 0.3 1 82 30 30 GLY CA C 44.568 0.3 1 83 30 30 GLY N N 110.871 0.3 1 84 31 31 PRO C C 180.224 0.3 1 85 32 32 ILE H H 10.329 0.02 1 86 32 32 ILE C C 176.857 0.3 1 87 32 32 ILE CA C 63.556 0.3 1 88 32 32 ILE CB C 37.033 0.3 1 89 32 32 ILE N N 124.287 0.3 1 90 33 33 ALA H H 9.347 0.02 1 91 33 33 ALA C C 179.316 0.3 1 92 33 33 ALA CA C 54.443 0.3 1 93 33 33 ALA CB C 18.844 0.3 1 94 33 33 ALA N N 124.412 0.3 1 95 34 34 GLY H H 8.67 0.02 1 96 34 34 GLY C C 175.684 0.3 1 97 34 34 GLY CA C 46.181 0.3 1 98 34 34 GLY N N 132.175 0.3 1 99 35 35 ALA H H 7.397 0.02 1 100 35 35 ALA C C 178.635 0.3 1 101 35 35 ALA CA C 54.152 0.3 1 102 35 35 ALA CB C 18.19 0.3 1 103 35 35 ALA N N 126.174 0.3 1 104 36 36 ILE H H 8.425 0.02 1 105 36 36 ILE C C 176.706 0.3 1 106 36 36 ILE CA C 65.075 0.3 1 107 36 36 ILE CB C 36.786 0.3 1 108 36 36 ILE N N 117.159 0.3 1 109 37 37 LYS H H 7.908 0.02 1 110 37 37 LYS C C 176.895 0.3 1 111 37 37 LYS CA C 58.991 0.3 1 112 37 37 LYS CB C 32.328 0.3 1 113 37 37 LYS N N 116.596 0.3 1 114 38 38 SER H H 8.048 0.02 1 115 38 38 SER C C 177.76 0.3 1 116 38 38 SER CA C 55.101 0.3 1 117 38 38 SER CB C 62.122 0.3 1 118 38 38 SER N N 111.668 0.3 1 119 39 39 LYS H H 8.624 0.02 1 120 39 39 LYS C C 179.694 0.3 1 121 39 39 LYS CA C 55.101 0.3 1 122 39 39 LYS CB C 34.395 0.3 1 123 39 39 LYS N N 120.626 0.3 1 124 40 40 VAL H H 8.475 0.02 1 125 40 40 VAL C C 180.715 0.3 1 126 40 40 VAL CA C 56.239 0.3 1 127 40 40 VAL CB C 30.046 0.3 1 128 40 40 VAL N N 118.92 0.3 1 129 41 41 GLU H H 8.341 0.02 1 130 41 41 GLU C C 178.786 0.3 1 131 41 41 GLU CA C 54.816 0.3 1 132 41 41 GLU CB C 28.628 0.3 1 133 41 41 GLU N N 118.628 0.3 1 134 42 42 ALA H H 7.618 0.02 1 135 42 42 ALA C C 178.786 0.3 1 136 42 42 ALA CA C 53.393 0.3 1 137 42 42 ALA CB C 17.906 0.3 1 138 42 42 ALA N N 118.67 0.3 1 139 43 43 ALA H H 7.523 0.02 1 140 43 43 ALA C C 179.127 0.3 1 141 43 43 ALA CA C 53.772 0.3 1 142 43 43 ALA CB C 19.793 0.3 1 143 43 43 ALA N N 115.576 0.3 1 144 44 44 LEU H H 8.052 0.02 1 145 44 44 LEU C C 176.214 0.3 1 146 44 44 LEU CA C 53.298 0.3 1 147 44 44 LEU CB C 41.342 0.3 1 148 44 44 LEU N N 112.134 0.3 1 149 45 45 SER H H 7.73 0.02 1 150 45 45 SER C C 177.144 0.3 1 151 45 45 SER CA C 57.093 0.3 1 152 45 45 SER CB C 61.553 0.3 1 153 45 45 SER N N 113.571 0.3 1 154 46 46 PRO C C 177.198 0.3 1 155 47 47 THR H H 8.415 0.02 1 156 47 47 THR C C 175.563 0.3 1 157 47 47 THR CA C 61.648 0.3 1 158 47 47 THR CB C 67.436 0.3 1 159 47 47 THR N N 111.443 0.3 1 160 48 48 HIS H H 7.33 0.02 1 161 48 48 HIS C C 171.864 0.3 1 162 48 48 HIS CA C 55.772 0.3 1 163 48 48 HIS CB C 31.565 0.3 1 164 48 48 HIS N N 119.441 0.3 1 165 49 49 PHE H H 8.155 0.02 1 166 49 49 PHE C C 172.129 0.3 1 167 49 49 PHE CA C 55.772 0.3 1 168 49 49 PHE CB C 41.912 0.3 1 169 49 49 PHE N N 127.577 0.3 1 170 50 50 LYS H H 8.19 0.02 1 171 50 50 LYS C C 172.598 0.3 1 172 50 50 LYS CA C 55.101 0.3 1 173 50 50 LYS CB C 35.934 0.3 1 174 50 50 LYS N N 128.69 0.3 1 175 51 51 LEU H H 8.582 0.02 1 176 51 51 LEU C C 174.587 0.3 1 177 51 51 LEU CA C 52.639 0.3 1 178 51 51 LEU CB C 44.853 0.3 1 179 51 51 LEU N N 128.371 0.3 1 180 52 52 ILE H H 9.281 0.02 1 181 52 52 ILE C C 174.133 0.3 1 182 52 52 ILE CA C 60.035 0.3 1 183 52 52 ILE CB C 41.058 0.3 1 184 52 52 ILE N N 126.939 0.3 1 185 53 53 ASN H H 9.288 0.02 1 186 53 53 ASN C C 174.096 0.3 1 187 53 53 ASN CA C 51.969 0.3 1 188 53 53 ASN CB C 37.25 0.3 1 189 53 53 ASN N N 126.146 0.3 1 190 54 54 ASP H H 8.641 0.02 1 191 54 54 ASP C C 177.273 0.3 1 192 54 54 ASP CA C 52.634 0.3 1 193 54 54 ASP CB C 41.722 0.3 1 194 54 54 ASP N N 128.565 0.3 1 195 55 55 SER H H 8.814 0.02 1 196 55 55 SER C C 175.824 0.3 1 197 55 55 SER CA C 62.702 0.3 1 198 55 55 SER CB C 62.132 0.3 1 199 55 55 SER N N 118.945 0.3 1 200 56 56 HIS H H 8.406 0.02 1 201 56 56 HIS C C 175.495 0.3 1 202 56 56 HIS CA C 57.101 0.3 1 203 56 56 HIS CB C 30.529 0.3 1 204 56 56 HIS N N 118.328 0.3 1 205 57 57 LYS H H 7.291 0.02 1 206 57 57 LYS C C 175.42 0.3 1 207 57 57 LYS CA C 55.86 0.3 1 208 57 57 LYS CB C 31.095 0.3 1 209 57 57 LYS N N 118.721 0.3 1 210 58 58 HIS H H 7.457 0.02 1 211 58 58 HIS CA C 54.158 0.3 1 212 58 58 HIS CB C 29.191 0.3 1 213 58 58 HIS N N 116.837 0.3 1 214 59 59 ALA H H 7.713 0.02 1 215 59 59 ALA C C 177.5 0.3 1 216 59 59 ALA CA C 52.444 0.3 1 217 59 59 ALA CB C 18.464 0.3 1 218 59 59 ALA N N 123.866 0.3 1 219 60 60 GLY H H 8.447 0.02 1 220 60 60 GLY C C 173.415 0.3 1 221 60 60 GLY CA C 44.76 0.3 1 222 60 60 GLY N N 107.641 0.3 1 223 61 61 HIS H H 8.117 0.02 1 224 61 61 HIS C C 173.679 0.3 1 225 61 61 HIS CA C 54.917 0.3 1 226 61 61 HIS CB C 28.717 0.3 1 227 61 61 HIS N N 117.993 0.3 1 228 62 62 TYR H H 8.045 0.02 1 229 62 62 TYR C C 174.625 0.3 1 230 62 62 TYR CA C 56.816 0.3 1 231 62 62 TYR CB C 38.305 0.3 1 232 62 62 TYR N N 120.61 0.3 1 233 63 63 ALA H H 8.219 0.02 1 234 63 63 ALA C C 177.084 0.3 1 235 63 63 ALA CA C 51.4 0.3 1 236 63 63 ALA CB C 18.665 0.3 1 237 63 63 ALA N N 125.883 0.3 1 238 64 64 ARG H H 8.339 0.02 1 239 64 64 ARG C C 175.722 0.3 1 240 64 64 ARG CA C 55.962 0.3 1 241 64 64 ARG CB C 29.476 0.3 1 242 64 64 ARG N N 120.435 0.3 1 243 65 65 ASP H H 8.189 0.02 1 244 65 65 ASP C C 176.327 0.3 1 245 65 65 ASP CA C 53.298 0.3 1 246 65 65 ASP CB C 40.299 0.3 1 247 65 65 ASP N N 120.014 0.3 1 248 66 66 GLY H H 8.368 0.02 1 249 66 66 GLY C C 173.831 0.3 1 250 66 66 GLY CA C 44.663 0.3 1 251 66 66 GLY N N 109.2 0.3 1 252 67 67 SER H H 8.245 0.02 1 253 67 67 SER C C 175.1 0.3 1 254 67 67 SER CA C 57.947 0.3 1 255 67 67 SER CB C 63.356 0.3 1 256 67 67 SER N N 115.739 0.3 1 257 68 68 THR H H 8.417 0.02 1 258 68 68 THR C C 174.285 0.3 1 259 68 68 THR CA C 61.932 0.3 1 260 68 68 THR CB C 68.859 0.3 1 261 68 68 THR N N 115.837 0.3 1 262 69 69 ALA H H 8.368 0.02 1 263 69 69 ALA C C 177.387 0.3 1 264 69 69 ALA CA C 52.444 0.3 1 265 69 69 ALA CB C 18.38 0.3 1 266 69 69 ALA N N 125.438 0.3 1 267 70 70 SER H H 8.24 0.02 1 268 70 70 SER C C 174.323 0.3 1 269 70 70 SER CA C 58.422 0.3 1 270 70 70 SER CB C 62.976 0.3 1 271 70 70 SER N N 114.469 0.3 1 272 71 71 ASP H H 8.314 0.02 1 273 71 71 ASP C C 175.457 0.3 1 274 71 71 ASP CA C 54.152 0.3 1 275 71 71 ASP CB C 40.393 0.3 1 276 71 71 ASP N N 121.882 0.3 1 277 72 72 ALA H H 8.123 0.02 1 278 72 72 ALA C C 177.198 0.3 1 279 72 72 ALA CA C 51.685 0.3 1 280 72 72 ALA CB C 18.475 0.3 1 281 72 72 ALA N N 122.98 0.3 1 282 73 73 GLY H H 8.266 0.02 1 283 73 73 GLY C C 173.188 0.3 1 284 73 73 GLY CA C 44.948 0.3 1 285 73 73 GLY N N 107.044 0.3 1 286 74 74 GLU H H 8.517 0.02 1 287 74 74 GLU C C 173.519 0.3 1 288 74 74 GLU CA C 54.816 0.3 1 289 74 74 GLU CB C 31.379 0.3 1 290 74 74 GLU N N 121.975 0.3 1 291 75 75 THR H H 8.22 0.02 1 292 75 75 THR C C 175.306 0.3 1 293 75 75 THR CA C 62.217 0.3 1 294 75 75 THR CB C 68.574 0.3 1 295 75 75 THR N N 107.572 0.3 1 296 76 76 HIS H H 7.832 0.02 1 297 76 76 HIS C C 172.847 0.3 1 298 76 76 HIS CA C 55.67 0.3 1 299 76 76 HIS CB C 32.613 0.3 1 300 76 76 HIS N N 122.562 0.3 1 301 77 77 PHE H H 7.972 0.02 1 302 77 77 PHE C C 175.722 0.3 1 303 77 77 PHE CA C 57.663 0.3 1 304 77 77 PHE CB C 43.525 0.3 1 305 77 77 PHE N N 116.13 0.3 1 306 78 78 ARG H H 9.393 0.02 1 307 78 78 ARG C C 174.854 0.3 1 308 78 78 ARG CA C 54.531 0.3 1 309 78 78 ARG CB C 32.613 0.3 1 310 78 78 ARG N N 121.854 0.3 1 311 79 79 LEU H H 8.614 0.02 1 312 79 79 LEU C C 173.566 0.3 1 313 79 79 LEU CA C 52.444 0.3 1 314 79 79 LEU CB C 44.758 0.3 1 315 79 79 LEU N N 123.859 0.3 1 316 80 80 GLU H H 9.234 0.02 1 317 80 80 GLU C C 174.02 0.3 1 318 80 80 GLU CA C 59.75 0.3 1 319 80 80 GLU CB C 30.146 0.3 1 320 80 80 GLU N N 126.84 0.3 1 321 81 81 VAL H H 8.583 0.02 1 322 81 81 VAL C C 173.301 0.3 1 323 81 81 VAL CA C 59.94 0.3 1 324 81 81 VAL CB C 34.795 0.3 1 325 81 81 VAL N N 119.171 0.3 1 326 82 82 THR H H 8.823 0.02 1 327 82 82 THR C C 173.642 0.3 1 328 82 82 THR CA C 59.181 0.3 1 329 82 82 THR CB C 68.669 0.3 1 330 82 82 THR N N 127.148 0.3 1 331 83 83 SER H H 8.939 0.02 1 332 83 83 SER C C 174.55 0.3 1 333 83 83 SER CA C 56.05 0.3 1 334 83 83 SER CB C 63.356 0.3 1 335 83 83 SER N N 117.236 0.3 1 336 84 84 ASP H H 9.19 0.02 1 337 84 84 ASP C C 177.16 0.3 1 338 84 84 ASP CA C 56.334 0.3 1 339 84 84 ASP CB C 40.204 0.3 1 340 84 84 ASP N N 130.628 0.3 1 341 85 85 ALA H H 8.665 0.02 1 342 85 85 ALA C C 177.424 0.3 1 343 85 85 ALA CA C 53.013 0.3 1 344 85 85 ALA CB C 17.716 0.3 1 345 85 85 ALA N N 122.589 0.3 1 346 86 86 PHE H H 6.71 0.02 1 347 86 86 PHE C C 174.474 0.3 1 348 86 86 PHE CA C 53.962 0.3 1 349 86 86 PHE CB C 37.167 0.3 1 350 86 86 PHE N N 111.325 0.3 1 351 87 87 LYS H H 7.515 0.02 1 352 87 87 LYS C C 176.857 0.3 1 353 87 87 LYS CA C 58.232 0.3 1 354 87 87 LYS CB C 31.379 0.3 1 355 87 87 LYS N N 120.471 0.3 1 356 88 88 GLY H H 9.09 0.02 1 357 88 88 GLY C C 173.339 0.3 1 358 88 88 GLY CA C 44.758 0.3 1 359 88 88 GLY N N 113.642 0.3 1 360 89 89 LEU H H 7.958 0.02 1 361 89 89 LEU C C 178.105 0.3 1 362 89 89 LEU CA C 53.108 0.3 1 363 89 89 LEU CB C 44.815 0.3 1 364 89 89 LEU N N 120.043 0.3 1 365 90 90 THR H H 7.851 0.02 1 366 90 90 THR C C 174.285 0.3 1 367 90 90 THR CA C 60.225 0.3 1 368 90 90 THR CB C 69.334 0.3 1 369 90 90 THR N N 114.99 0.3 1 370 91 91 LEU H H 8.651 0.02 1 371 91 91 LEU C C 178.03 0.3 1 372 91 91 LEU CA C 59.181 0.3 1 373 91 91 LEU CB C 40.393 0.3 1 374 91 91 LEU N N 122.821 0.3 1 375 92 92 VAL H H 7.99 0.02 1 376 92 92 VAL C C 177.765 0.3 1 377 92 92 VAL CA C 65.253 0.3 1 378 92 92 VAL CB C 30.715 0.3 1 379 92 92 VAL N N 114.283 0.3 1 380 93 93 LYS H H 7.14 0.02 1 381 93 93 LYS C C 179.429 0.3 1 382 93 93 LYS CA C 58.232 0.3 1 383 93 93 LYS CB C 32.044 0.3 1 384 93 93 LYS N N 119.841 0.3 1 385 94 94 ARG H H 8.528 0.02 1 386 94 94 ARG C C 176.857 0.3 1 387 94 94 ARG CA C 59.276 0.3 1 388 94 94 ARG CB C 28.912 0.3 1 389 94 94 ARG N N 121.222 0.3 1 390 95 95 HIS H H 8.145 0.02 1 391 95 95 HIS C C 176.819 0.3 1 392 95 95 HIS CA C 57.188 0.3 1 393 95 95 HIS CB C 28.817 0.3 1 394 95 95 HIS N N 116.41 0.3 1 395 96 96 GLN H H 8.451 0.02 1 396 96 96 GLN C C 178.068 0.3 1 397 96 96 GLN CA C 58.327 0.3 1 398 96 96 GLN CB C 27.584 0.3 1 399 96 96 GLN N N 117.748 0.3 1 400 97 97 LEU H H 7.892 0.02 1 401 97 97 LEU C C 179.013 0.3 1 402 97 97 LEU CA C 57.947 0.3 1 403 97 97 LEU CB C 41.627 0.3 1 404 97 97 LEU N N 121.924 0.3 1 405 98 98 ILE H H 7.17 0.02 1 406 98 98 ILE C C 177.198 0.3 1 407 98 98 ILE CA C 63.071 0.3 1 408 98 98 ILE CB C 34.89 0.3 1 409 98 98 ILE N N 117.792 0.3 1 410 99 99 TYR H H 8.678 0.02 1 411 99 99 TYR C C 179.278 0.3 1 412 99 99 TYR CA C 63.128 0.3 1 413 99 99 TYR CB C 36.503 0.3 1 414 99 99 TYR N N 118.375 0.3 1 415 100 100 GLY H H 8.414 0.02 1 416 100 100 GLY C C 175.722 0.3 1 417 100 100 GLY CA C 46.276 0.3 1 418 100 100 GLY N N 104.597 0.3 1 419 101 101 LEU H H 7.76 0.02 1 420 101 101 LEU C C 178.37 0.3 1 421 101 101 LEU CA C 56.05 0.3 1 422 101 101 LEU CB C 42.481 0.3 1 423 101 101 LEU N N 121.169 0.3 1 424 102 102 LEU H H 7.472 0.02 1 425 102 102 LEU C C 176.025 0.3 1 426 102 102 LEU CA C 55.082 0.3 1 427 102 102 LEU CB C 43.313 0.3 1 428 102 102 LEU N N 115.881 0.3 1 429 103 103 SER H H 7.962 0.02 1 430 103 103 SER C C 177.16 0.3 1 431 103 103 SER CA C 61.265 0.3 1 432 103 103 SER CB C 64.34 0.3 1 433 103 103 SER N N 126.115 0.3 1 434 104 104 ASP H H 8.988 0.02 1 435 104 104 ASP C C 177.689 0.3 1 436 104 104 ASP CA C 56.809 0.3 1 437 104 104 ASP CB C 38.686 0.3 1 438 104 104 ASP N N 119.77 0.3 1 439 105 105 GLU H H 7.964 0.02 1 440 105 105 GLU C C 178.257 0.3 1 441 105 105 GLU CA C 60.889 0.3 1 442 105 105 GLU CB C 27.204 0.3 1 443 105 105 GLU N N 123.658 0.3 1 444 106 106 PHE H H 7.906 0.02 1 445 106 106 PHE C C 178.597 0.3 1 446 106 106 PHE CA C 61.268 0.3 1 447 106 106 PHE CB C 37.737 0.3 1 448 106 106 PHE N N 118.409 0.3 1 449 107 107 LYS H H 7.694 0.02 1 450 107 107 LYS C C 176.933 0.3 1 451 107 107 LYS CA C 58.042 0.3 1 452 107 107 LYS CB C 31.379 0.3 1 453 107 107 LYS N N 119.416 0.3 1 454 108 108 ALA H H 7.477 0.02 1 455 108 108 ALA C C 176.214 0.3 1 456 108 108 ALA CA C 51.59 0.3 1 457 108 108 ALA CB C 18.475 0.3 1 458 108 108 ALA N N 120.329 0.3 1 459 109 109 GLY H H 7.488 0.02 1 460 109 109 GLY C C 173.642 0.3 1 461 109 109 GLY CA C 44.758 0.3 1 462 109 109 GLY N N 104.704 0.3 1 463 110 110 LEU H H 7.805 0.02 1 464 110 110 LEU C C 174.323 0.3 1 465 110 110 LEU CA C 55.575 0.3 1 466 110 110 LEU CB C 41.437 0.3 1 467 110 110 LEU N N 123.173 0.3 1 468 111 111 HIS H H 9.452 0.02 1 469 111 111 HIS C C 174.474 0.3 1 470 111 111 HIS CA C 55.575 0.3 1 471 111 111 HIS CB C 30.051 0.3 1 472 111 111 HIS N N 124.289 0.3 1 473 112 112 ALA H H 7.9 0.02 1 474 112 112 ALA C C 173.831 0.3 1 475 112 112 ALA CA C 51.495 0.3 1 476 112 112 ALA CB C 22.27 0.3 1 477 112 112 ALA N N 119.264 0.3 1 478 113 113 LEU H H 8.694 0.02 1 479 113 113 LEU C C 175.586 0.3 1 480 113 113 LEU CA C 51.88 0.3 1 481 113 113 LEU CB C 48.399 0.3 1 482 113 113 LEU N N 120.243 0.3 1 483 114 114 ALA H H 8.302 0.02 1 484 114 114 ALA C C 176.857 0.3 1 485 114 114 ALA CA C 56.151 0.3 1 486 114 114 ALA CB C 18.369 0.3 1 487 114 114 ALA N N 118.869 0.3 1 488 115 115 MET H H 8.941 0.02 1 489 115 115 MET C C 174.777 0.3 1 490 115 115 MET CA C 54.531 0.3 1 491 115 115 MET CB C 36.883 0.3 1 492 115 115 MET N N 122.739 0.3 1 493 116 116 THR H H 8.725 0.02 1 494 116 116 THR C C 173.642 0.3 1 495 116 116 THR CA C 61.363 0.3 1 496 116 116 THR CB C 69.808 0.3 1 497 116 116 THR N N 119.563 0.3 1 498 117 117 THR H H 9.045 0.02 1 499 117 117 THR C C 174.814 0.3 1 500 117 117 THR CA C 58 0.3 1 501 117 117 THR CB C 69.144 0.3 1 502 117 117 THR N N 117.42 0.3 1 503 118 118 LYS H H 8.604 0.02 1 504 118 118 LYS C C 175.117 0.3 1 505 118 118 LYS CA C 54.247 0.3 1 506 118 118 LYS CB C 36.313 0.3 1 507 118 118 LYS N N 125.33 0.3 1 508 119 119 THR H H 8.604 0.02 1 509 119 119 THR C C 175.811 0.3 1 510 119 119 THR CA C 58.801 0.3 1 511 119 119 THR CB C 67.056 0.3 1 512 119 119 THR N N 111.934 0.3 1 513 120 120 PRO C C 176.29 0.3 1 514 121 121 ALA H H 7.703 0.02 1 515 121 121 ALA C C 177.803 0.3 1 516 121 121 ALA CA C 52.064 0.3 1 517 121 121 ALA CB C 18.475 0.3 1 518 121 121 ALA N N 116.789 0.3 1 519 122 122 GLU H H 7.518 0.02 1 520 122 122 GLU C C 175.344 0.3 1 521 122 122 GLU CA C 55.385 0.3 1 522 122 122 GLU CB C 29.766 0.3 1 523 122 122 GLU N N 119.118 0.3 1 524 123 123 GLN H H 7.825 0.02 1 525 123 123 GLN C C 181.273 0.3 1 526 123 123 GLN CA C 57.188 0.3 1 527 123 123 GLN CB C 29.197 0.3 1 528 123 123 GLN N N 125.396 0.3 1 stop_ save_