data_18969 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N resonance assignments of S55A mutant of UVI31+ from Chlamydomonas reinhardtii ; _BMRB_accession_number 18969 _BMRB_flat_file_name bmr18969.str _Entry_type original _Submission_date 2013-01-22 _Accession_date 2013-01-22 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Overexpression, purification and structural' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Singh Himanshu . . 2 Chary Kandala . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 94 "13C chemical shifts" 288 "15N chemical shifts" 94 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-02-14 original author . stop_ _Original_release_date 2014-02-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title '(1)H, (13)C and (15)N NMR assignments of a mutant of UV inducible transcript (S55A-UVI31+) from Chlamydomonas reinhardtii.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23979961 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Singh Himanshu . . 2 Rao B. J. . 3 Chary Kandala V.R. . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'S55A mutant of UVI31+' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'S55A mutant of UVI31+' $S55A_of_UVI31+ stop_ _System_molecular_weight 13360 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'gain in endonuclease activity' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_S55A_of_UVI31+ _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common S55A_of_UVI31+ _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'gain in endonuclease activity' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 123 _Mol_residue_sequence ; MRGSHHHHHHGSHVISSIAS RGSMAEHQLGPIAGAIKSKV EAALSPTHFKLINDSHKHAG HYARDGSTASDAGETHFRLE VTSDAFKGLTLVKRHQLIYG LLSDEFKAGLHALAMTTKTP AEQ ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ARG 3 GLY 4 SER 5 HIS 6 HIS 7 HIS 8 HIS 9 HIS 10 HIS 11 GLY 12 SER 13 HIS 14 VAL 15 ILE 16 SER 17 SER 18 ILE 19 ALA 20 SER 21 ARG 22 GLY 23 SER 24 MET 25 ALA 26 GLU 27 HIS 28 GLN 29 LEU 30 GLY 31 PRO 32 ILE 33 ALA 34 GLY 35 ALA 36 ILE 37 LYS 38 SER 39 LYS 40 VAL 41 GLU 42 ALA 43 ALA 44 LEU 45 SER 46 PRO 47 THR 48 HIS 49 PHE 50 LYS 51 LEU 52 ILE 53 ASN 54 ASP 55 SER 56 HIS 57 LYS 58 HIS 59 ALA 60 GLY 61 HIS 62 TYR 63 ALA 64 ARG 65 ASP 66 GLY 67 SER 68 THR 69 ALA 70 SER 71 ASP 72 ALA 73 GLY 74 GLU 75 THR 76 HIS 77 PHE 78 ARG 79 LEU 80 GLU 81 VAL 82 THR 83 SER 84 ASP 85 ALA 86 PHE 87 LYS 88 GLY 89 LEU 90 THR 91 LEU 92 VAL 93 LYS 94 ARG 95 HIS 96 GLN 97 LEU 98 ILE 99 TYR 100 GLY 101 LEU 102 LEU 103 SER 104 ASP 105 GLU 106 PHE 107 LYS 108 ALA 109 GLY 110 LEU 111 HIS 112 ALA 113 LEU 114 ALA 115 MET 116 THR 117 THR 118 LYS 119 THR 120 PRO 121 ALA 122 GLU 123 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-05 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 18567 S114A_mutant_of_UVI31+ 100.00 123 100.00 100.00 8.27e-81 BMRB 19307 UVI31+Mg 100.00 123 99.19 100.00 2.18e-80 BMRB 19308 Phophorylated_UVI31+ 100.00 123 99.19 100.00 2.18e-80 PDB 2MA0 "Nmr Structural Of Uvi31+" 100.00 123 99.19 100.00 2.18e-80 GB EDO96758 "predicted protein [Chlamydomonas reinhardtii]" 81.30 100 99.00 100.00 6.67e-64 REF XP_001702905 "predicted protein [Chlamydomonas reinhardtii]" 81.30 100 99.00 100.00 6.67e-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 $S55A_of_UVI31+ 'Chlamydomonas reinhardtii' 3055 Eukaryota Viridiplantae 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 $S55A_of_UVI31+ 'recombinant technology' . 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 S55A mutant of 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 $S55A_of_UVI31+ 0.8 mM '[U-100% 13C; U-100% 15N]' 'sodium phosphate' 50 mM 'natural abundance' NaCl 50 mM 'natural abundance' 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_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . 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' parallel 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct cylindrical 'insert at center of experimental sample tube' parallel 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect cylindrical 'insert at center of experimental sample tube' parallel 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 '15N-H HSQC, HNCO,HNCACO, CBCANH, CBCACONH' loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D CBCA(CO)NH' '3D HN(CO)CA' '3D H(CCO)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 'S55A 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 8.342 0.020 1 2 11 11 GLY C C 172.428 0.3 1 3 11 11 GLY CA C 42.463 0.3 1 4 11 11 GLY N N 109.538 0.3 1 5 12 12 SER H H 8.248 0.020 1 6 12 12 SER C C 172.364 0.3 1 7 12 12 SER CA C 55.470 0.3 1 8 12 12 SER CB C 60.881 0.3 1 9 12 12 SER N N 115.588 0.3 1 10 13 13 HIS H H 8.261 0.020 1 11 13 13 HIS C C 175.151 0.3 1 12 13 13 HIS CA C 53.762 0.3 1 13 13 13 HIS CB C 27.656 0.3 1 14 13 13 HIS N N 122.795 0.3 1 15 14 14 VAL H H 7.451 0.020 1 16 14 14 VAL C C 177.861 0.3 1 17 14 14 VAL CA C 55.490 0.3 1 18 14 14 VAL CB C 17.793 0.3 1 19 14 14 VAL N N 115.503 0.3 1 20 15 15 ILE H H 8.001 0.020 1 21 15 15 ILE C C 174.084 0.3 1 22 15 15 ILE CA C 58.758 0.3 1 23 15 15 ILE CB C 35.601 0.3 1 24 15 15 ILE N N 121.942 0.3 1 25 16 16 SER H H 8.145 0.020 1 26 16 16 SER C C 174.303 0.3 1 27 16 16 SER CA C 58.025 0.3 1 28 16 16 SER CB C 35.442 0.3 1 29 16 16 SER N N 125.526 0.3 1 30 17 17 SER H H 8.326 0.020 1 31 17 17 SER C C 172.745 0.3 1 32 17 17 SER CA C 53.806 0.3 1 33 17 17 SER CB C 26.683 0.3 1 34 17 17 SER N N 120.273 0.3 1 35 18 18 ILE H H 8.049 0.020 1 36 18 18 ILE C C 174.446 0.3 1 37 18 18 ILE CA C 59.362 0.3 1 38 18 18 ILE CB C 29.901 0.3 1 39 18 18 ILE N N 122.116 0.3 1 40 19 19 ALA H H 8.185 0.020 1 41 19 19 ALA C C 176.030 0.3 1 42 19 19 ALA CA C 49.769 0.3 1 43 19 19 ALA CB C 16.085 0.3 1 44 19 19 ALA N N 127.023 0.3 1 45 20 20 SER H H 8.111 0.020 1 46 20 20 SER C C 173.036 0.3 1 47 20 20 SER CA C 55.628 0.3 1 48 20 20 SER CB C 61.071 0.3 1 49 20 20 SER N N 114.737 0.3 1 50 24 24 MET H H 8.256 0.020 1 51 24 24 MET C C 174.376 0.3 1 52 24 24 MET CA C 52.812 0.3 1 53 24 24 MET CB C 29.460 0.3 1 54 24 24 MET N N 121.626 0.3 1 55 25 25 ALA H H 8.150 0.020 1 56 25 25 ALA C C 176.031 0.3 1 57 25 25 ALA CA C 49.959 0.3 1 58 25 25 ALA CB C 16.180 0.3 1 59 25 25 ALA N N 124.516 0.3 1 60 26 26 GLU H H 8.260 0.020 1 61 26 26 GLU C C 174.600 0.3 1 62 26 26 GLU CA C 53.850 0.3 1 63 26 26 GLU CB C 27.187 0.3 1 64 26 26 GLU N N 119.449 0.3 1 65 28 28 GLN H H 7.996 0.020 1 66 28 28 GLN C C 173.695 0.3 1 67 28 28 GLN CA C 52.721 0.3 1 68 28 28 GLN CB C 26.458 0.3 1 69 28 28 GLN N N 120.906 0.3 1 70 29 29 LEU H H 8.224 0.020 1 71 29 29 LEU C C 175.721 0.3 1 72 29 29 LEU CA C 52.711 0.3 1 73 29 29 LEU CB C 39.807 0.3 1 74 29 29 LEU N N 123.604 0.3 1 75 30 30 GLY H H 8.307 0.020 1 76 30 30 GLY C C 170.252 0.3 1 77 30 30 GLY CA C 42.368 0.3 1 78 30 30 GLY N N 110.158 0.3 1 79 31 31 PRO C C 179.073 0.3 1 80 33 33 ALA H H 9.018 0.020 1 81 33 33 ALA C C 178.057 0.3 1 82 33 33 ALA CA C 52.243 0.3 1 83 33 33 ALA CB C 16.644 0.3 1 84 33 33 ALA N N 124.190 0.3 1 85 34 34 GLY H H 8.488 0.020 1 86 34 34 GLY C C 174.460 0.3 1 87 34 34 GLY CA C 43.981 0.3 1 88 34 34 GLY N N 132.542 0.3 1 89 35 35 ALA H H 7.405 0.020 1 90 35 35 ALA C C 177.280 0.3 1 91 35 35 ALA CA C 51.952 0.3 1 92 35 35 ALA CB C 15.990 0.3 1 93 35 35 ALA N N 126.339 0.3 1 94 36 36 ILE H H 8.274 0.020 1 95 36 36 ILE C C 175.551 0.3 1 96 36 36 ILE CA C 62.875 0.3 1 97 36 36 ILE CB C 34.586 0.3 1 98 36 36 ILE N N 117.217 0.3 1 99 37 37 LYS H H 7.838 0.020 1 100 37 37 LYS C C 175.620 0.3 1 101 37 37 LYS CA C 56.791 0.3 1 102 37 37 LYS CB C 30.128 0.3 1 103 37 37 LYS N N 117.064 0.3 1 104 38 38 SER H H 7.939 0.020 1 105 38 38 SER C C 175.560 0.3 1 106 38 38 SER CA C 51.199 0.3 1 107 38 38 SER CB C 60.022 0.3 1 108 38 38 SER N N 111.795 0.3 1 109 39 39 LYS H H 8.373 0.020 1 110 39 39 LYS C C 178.379 0.3 1 111 39 39 LYS CA C 52.811 0.3 1 112 39 39 LYS CB C 26.652 0.3 1 113 39 39 LYS N N 120.831 0.3 1 114 40 40 VAL H H 8.437 0.020 1 115 40 40 VAL C C 178.515 0.3 1 116 40 40 VAL CA C 64.014 0.3 1 117 40 40 VAL CB C 27.846 0.3 1 118 40 40 VAL N N 118.957 0.3 1 119 41 41 GLU H H 8.310 0.020 1 120 41 41 GLU C C 177.456 0.3 1 121 41 41 GLU CA C 52.586 0.3 1 122 41 41 GLU CB C 26.528 0.3 1 123 41 41 GLU N N 118.825 0.3 1 124 42 42 ALA H H 7.540 0.020 1 125 42 42 ALA C C 177.523 0.3 1 126 42 42 ALA CA C 51.193 0.3 1 127 42 42 ALA CB C 15.706 0.3 1 128 42 42 ALA N N 118.796 0.3 1 129 43 43 ALA H H 7.447 0.020 1 130 43 43 ALA C C 177.831 0.3 1 131 43 43 ALA CA C 51.622 0.3 1 132 43 43 ALA CB C 17.593 0.3 1 133 43 43 ALA N N 115.666 0.3 1 134 44 44 LEU H H 7.999 0.020 1 135 44 44 LEU C C 175.011 0.3 1 136 44 44 LEU CA C 51.108 0.3 1 137 44 44 LEU CB C 39.142 0.3 1 138 44 44 LEU N N 112.225 0.3 1 139 45 45 SER H H 7.682 0.020 1 140 45 45 SER C C 174.944 0.3 1 141 45 45 SER CA C 54.893 0.3 1 142 45 45 SER CB C 59.353 0.3 1 143 45 45 SER N N 113.751 0.3 1 144 46 46 PRO C C 175.933 0.3 1 145 47 47 THR H H 8.334 0.020 1 146 47 47 THR C C 173.363 0.3 1 147 47 47 THR CA C 59.548 0.3 1 148 47 47 THR CB C 65.436 0.3 1 149 47 47 THR N N 111.716 0.3 1 150 48 48 HIS C C 169.664 0.3 1 151 49 49 PHE H H 7.980 0.020 1 152 49 49 PHE C C 170.977 0.3 1 153 49 49 PHE CA C 53.572 0.3 1 154 49 49 PHE CB C 39.712 0.3 1 155 49 49 PHE N N 127.431 0.3 1 156 50 50 LYS H H 8.202 0.020 1 157 50 50 LYS C C 170.398 0.3 1 158 50 50 LYS CA C 52.901 0.3 1 159 50 50 LYS CB C 33.734 0.3 1 160 50 50 LYS N N 128.732 0.3 1 161 51 51 LEU H H 8.455 0.020 1 162 51 51 LEU C C 173.441 0.3 1 163 51 51 LEU CA C 50.439 0.3 1 164 51 51 LEU CB C 42.653 0.3 1 165 51 51 LEU N N 128.212 0.3 1 166 52 52 ILE H H 9.104 0.020 1 167 52 52 ILE C C 172.789 0.3 1 168 52 52 ILE CA C 57.835 0.3 1 169 52 52 ILE CB C 38.858 0.3 1 170 52 52 ILE N N 126.526 0.3 1 171 53 53 ASN H H 9.104 0.020 1 172 53 53 ASN C C 172.917 0.3 1 173 53 53 ASN CA C 50.339 0.3 1 174 53 53 ASN CB C 34.872 0.3 1 175 53 53 ASN N N 126.205 0.3 1 176 54 54 ASP H H 8.447 0.020 1 177 54 54 ASP C C 176.236 0.3 1 178 54 54 ASP CA C 50.454 0.3 1 179 54 54 ASP CB C 39.542 0.3 1 180 54 54 ASP N N 128.129 0.3 1 181 56 56 HIS H H 8.306 0.020 1 182 56 56 HIS C C 174.616 0.3 1 183 56 56 HIS CA C 54.911 0.3 1 184 56 56 HIS CB C 60.986 0.3 1 185 56 56 HIS N N 118.328 0.3 1 186 57 57 LYS C C 174.450 0.3 1 187 57 57 LYS CA C 53.660 0.3 1 188 57 57 LYS CB C 28.895 0.3 1 189 60 60 GLY H H 8.342 0.020 1 190 60 60 GLY C C 172.351 0.3 1 191 60 60 GLY CA C 42.560 0.3 1 192 60 60 GLY N N 107.964 0.3 1 193 62 62 TYR H H 8.001 0.020 1 194 62 62 TYR C C 172.425 0.3 1 195 62 62 TYR CA C 54.616 0.3 1 196 62 62 TYR CB C 36.105 0.3 1 197 62 62 TYR N N 120.689 0.3 1 198 63 63 ALA H H 8.266 0.020 1 199 63 63 ALA C C 175.714 0.3 1 200 63 63 ALA CA C 49.200 0.3 1 201 63 63 ALA CB C 16.465 0.3 1 202 63 63 ALA N N 125.885 0.3 1 203 64 64 ARG H H 8.239 0.020 1 204 64 64 ARG C C 174.605 0.3 1 205 64 64 ARG CA C 53.762 0.3 1 206 64 64 ARG CB C 27.276 0.3 1 207 64 64 ARG N N 120.435 0.3 1 208 65 65 ASP H H 8.169 0.020 1 209 65 65 ASP C C 176.735 0.3 1 210 65 65 ASP CA C 51.098 0.3 1 211 65 65 ASP CB C 38.099 0.3 1 212 65 65 ASP N N 120.040 0.3 1 213 66 66 GLY H H 8.293 0.020 1 214 66 66 GLY C C 172.591 0.3 1 215 66 66 GLY CA C 42.463 0.3 1 216 66 66 GLY N N 109.268 0.3 1 217 67 67 SER H H 8.174 0.020 1 218 67 67 SER C C 172.900 0.3 1 219 67 67 SER CA C 55.757 0.3 1 220 67 67 SER CB C 61.166 0.3 1 221 67 67 SER N N 115.713 0.3 1 222 68 68 THR H H 8.174 0.020 1 223 68 68 THR C C 173.053 0.3 1 224 68 68 THR CA C 59.802 0.3 1 225 68 68 THR CB C 66.659 0.3 1 226 68 68 THR N N 115.848 0.3 1 227 69 69 ALA H H 8.210 0.020 1 228 69 69 ALA C C 176.339 0.3 1 229 69 69 ALA CA C 50.244 0.3 1 230 69 69 ALA CB C 16.180 0.3 1 231 69 69 ALA N N 125.262 0.3 1 232 70 70 SER H H 8.210 0.020 1 233 70 70 SER C C 173.306 0.3 1 234 70 70 SER CA C 56.222 0.3 1 235 70 70 SER CB C 60.776 0.3 1 236 70 70 SER N N 114.798 0.3 1 237 71 71 ASP H H 8.234 0.020 1 238 71 71 ASP C C 174.375 0.3 1 239 71 71 ASP CA C 51.952 0.3 1 240 71 71 ASP CB C 38.193 0.3 1 241 71 71 ASP N N 122.226 0.3 1 242 73 73 GLY H H 8.223 0.020 1 243 73 73 GLY C C 171.959 0.3 1 244 73 73 GLY CA C 42.748 0.3 1 245 73 73 GLY N N 107.503 0.3 1 246 74 74 GLU H H 8.363 0.020 1 247 74 74 GLU C C 171.319 0.3 1 248 74 74 GLU CA C 52.616 0.3 1 249 74 74 GLU CB C 29.179 0.3 1 250 74 74 GLU N N 122.000 0.3 1 251 75 75 THR H H 8.150 0.020 1 252 75 75 THR C C 173.964 0.3 1 253 75 75 THR CA C 60.017 0.3 1 254 75 75 THR CB C 66.374 0.3 1 255 75 75 THR N N 107.503 0.3 1 256 76 76 HIS C C 171.887 0.3 1 257 76 76 HIS CA C 53.470 0.3 1 258 76 76 HIS CB C 30.413 0.3 1 259 77 77 PHE C C 174.622 0.3 1 260 77 77 PHE CB C 41.325 0.3 1 261 78 78 ARG C C 172.654 0.3 1 262 78 78 ARG CA C 52.331 0.3 1 263 78 78 ARG CB C 30.413 0.3 1 264 79 79 LEU H H 8.522 0.020 1 265 79 79 LEU C C 172.660 0.3 1 266 79 79 LEU CA C 50.244 0.3 1 267 79 79 LEU CB C 27.756 0.3 1 268 79 79 LEU N N 123.748 0.3 1 269 80 80 GLU H H 9.112 0.020 1 270 80 80 GLU C C 172.682 0.3 1 271 80 80 GLU CA C 57.620 0.3 1 272 80 80 GLU CB C 27.946 0.3 1 273 80 80 GLU N N 126.620 0.3 1 274 81 81 VAL H H 8.564 0.020 1 275 81 81 VAL C C 172.198 0.3 1 276 81 81 VAL CA C 57.740 0.3 1 277 81 81 VAL CB C 32.595 0.3 1 278 81 81 VAL N N 119.407 0.3 1 279 82 82 THR H H 8.766 0.020 1 280 82 82 THR C C 172.426 0.3 1 281 82 82 THR CA C 56.981 0.3 1 282 82 82 THR CB C 50.054 0.3 1 283 82 82 THR N N 127.167 0.3 1 284 83 83 SER H H 8.886 0.020 1 285 83 83 SER C C 173.220 0.3 1 286 83 83 SER CA C 53.910 0.3 1 287 83 83 SER CB C 61.156 0.3 1 288 83 83 SER N N 117.305 0.3 1 289 84 84 ASP H H 9.144 0.020 1 290 84 84 ASP C C 175.944 0.3 1 291 84 84 ASP CA C 54.134 0.3 1 292 84 84 ASP CB C 38.004 0.3 1 293 84 84 ASP N N 130.769 0.3 1 294 85 85 ALA H H 8.600 0.020 1 295 85 85 ALA C C 176.256 0.3 1 296 85 85 ALA CA C 50.813 0.3 1 297 85 85 ALA CB C 15.516 0.3 1 298 85 85 ALA N N 122.747 0.3 1 299 86 86 PHE H H 6.653 0.020 1 300 86 86 PHE C C 173.141 0.3 1 301 86 86 PHE CA C 51.762 0.3 1 302 86 86 PHE CB C 34.967 0.3 1 303 86 86 PHE N N 111.350 0.3 1 304 87 87 LYS H H 7.467 0.020 1 305 87 87 LYS C C 175.636 0.3 1 306 87 87 LYS CA C 56.032 0.3 1 307 87 87 LYS CB C 29.179 0.3 1 308 87 87 LYS N N 120.573 0.3 1 309 88 88 GLY H H 8.990 0.020 1 310 88 88 GLY C C 172.110 0.3 1 311 88 88 GLY CA C 42.558 0.3 1 312 88 88 GLY N N 113.642 0.3 1 313 89 89 LEU H H 7.915 0.020 1 314 89 89 LEU C C 176.881 0.3 1 315 89 89 LEU CA C 50.908 0.3 1 316 89 89 LEU CB C 36.106 0.3 1 317 89 89 LEU N N 120.149 0.3 1 318 90 90 THR H H 7.783 0.020 1 319 90 90 THR C C 173.061 0.3 1 320 90 90 THR CA C 58.025 0.3 1 321 90 90 THR CB C 67.134 0.3 1 322 90 90 THR N N 115.144 0.3 1 323 91 91 LEU H H 8.581 0.020 1 324 91 91 LEU C C 176.236 0.3 1 325 91 91 LEU CA C 56.981 0.3 1 326 91 91 LEU CB C 38.193 0.3 1 327 91 91 LEU N N 122.843 0.3 1 328 92 92 VAL H H 7.890 0.020 1 329 92 92 VAL C C 176.536 0.3 1 330 92 92 VAL CA C 63.053 0.3 1 331 92 92 VAL CB C 28.515 0.3 1 332 92 92 VAL N N 114.283 0.3 1 333 93 93 LYS H H 7.040 0.020 1 334 93 93 LYS C C 178.142 0.3 1 335 93 93 LYS CA C 56.032 0.3 1 336 93 93 LYS CB C 29.749 0.3 1 337 93 93 LYS N N 119.841 0.3 1 338 94 94 ARG H H 8.439 0.020 1 339 94 94 ARG C C 175.553 0.3 1 340 94 94 ARG CA C 57.126 0.3 1 341 94 94 ARG CB C 26.722 0.3 1 342 94 94 ARG N N 121.566 0.3 1 343 95 95 HIS H H 8.087 0.020 1 344 95 95 HIS C C 175.873 0.3 1 345 95 95 HIS CA C 54.988 0.3 1 346 95 95 HIS CB C 26.617 0.3 1 347 95 95 HIS N N 117.042 0.3 1 348 96 96 GLN H H 8.328 0.020 1 349 96 96 GLN C C 176.886 0.3 1 350 96 96 GLN CA C 56.217 0.3 1 351 96 96 GLN CB C 25.414 0.3 1 352 96 96 GLN N N 117.808 0.3 1 353 97 97 LEU H H 7.831 0.020 1 354 97 97 LEU C C 177.747 0.3 1 355 97 97 LEU CA C 55.747 0.3 1 356 97 97 LEU CB C 39.427 0.3 1 357 97 97 LEU N N 122.151 0.3 1 358 98 98 ILE H H 7.197 0.020 1 359 98 98 ILE C C 175.942 0.3 1 360 98 98 ILE CA C 60.871 0.3 1 361 98 98 ILE CB C 32.690 0.3 1 362 98 98 ILE N N 118.007 0.3 1 363 99 99 TYR H H 8.637 0.020 1 364 99 99 TYR C C 177.981 0.3 1 365 99 99 TYR CA C 60.928 0.3 1 366 99 99 TYR CB C 34.303 0.3 1 367 99 99 TYR N N 118.618 0.3 1 368 100 100 GLY H H 8.345 0.020 1 369 100 100 GLY C C 174.542 0.3 1 370 100 100 GLY CA C 44.076 0.3 1 371 100 100 GLY N N 104.854 0.3 1 372 101 101 LEU H H 7.718 0.020 1 373 101 101 LEU C C 177.036 0.3 1 374 101 101 LEU CA C 53.850 0.3 1 375 101 101 LEU CB C 40.281 0.3 1 376 101 101 LEU N N 121.434 0.3 1 377 102 102 LEU H H 7.427 0.020 1 378 102 102 LEU C C 173.594 0.3 1 379 102 102 LEU CA C 50.813 0.3 1 380 102 102 LEU CB C 38.763 0.3 1 381 102 102 LEU N N 116.114 0.3 1 382 103 103 SER H H 7.847 0.020 1 383 103 103 SER C C 175.995 0.3 1 384 103 103 SER CA C 39.241 0.3 1 385 103 103 SER CB C 68.427 0.3 1 386 103 103 SER N N 125.854 0.3 1 387 104 104 ASP H H 8.886 0.020 1 388 104 104 ASP C C 176.418 0.3 1 389 104 104 ASP CA C 54.609 0.3 1 390 104 104 ASP CB C 36.486 0.3 1 391 104 104 ASP N N 119.908 0.3 1 392 105 105 GLU H H 7.966 0.020 1 393 105 105 GLU C C 176.987 0.3 1 394 105 105 GLU CA C 58.689 0.3 1 395 105 105 GLU CB C 25.004 0.3 1 396 105 105 GLU N N 123.508 0.3 1 397 106 106 PHE H H 7.938 0.020 1 398 106 106 PHE C C 177.445 0.3 1 399 106 106 PHE CA C 59.068 0.3 1 400 106 106 PHE CB C 35.537 0.3 1 401 106 106 PHE N N 118.694 0.3 1 402 107 107 LYS H H 7.643 0.020 1 403 107 107 LYS C C 175.623 0.3 1 404 107 107 LYS CA C 55.842 0.3 1 405 107 107 LYS CB C 29.179 0.3 1 406 107 107 LYS N N 119.471 0.3 1 407 108 108 ALA H H 7.283 0.020 1 408 108 108 ALA C C 174.928 0.3 1 409 108 108 ALA CA C 49.390 0.3 1 410 108 108 ALA CB C 16.275 0.3 1 411 108 108 ALA N N 119.904 0.3 1 412 109 109 GLY H H 7.501 0.020 1 413 109 109 GLY C C 172.276 0.3 1 414 109 109 GLY CA C 42.558 0.3 1 415 109 109 GLY N N 104.978 0.3 1 416 110 110 LEU H H 7.754 0.020 1 417 110 110 LEU C C 172.972 0.3 1 418 110 110 LEU CA C 53.375 0.3 1 419 110 110 LEU CB C 39.237 0.3 1 420 110 110 LEU N N 122.999 0.3 1 421 111 111 HIS H H 9.003 0.020 1 422 111 111 HIS C C 173.762 0.3 1 423 111 111 HIS CA C 53.381 0.3 1 424 111 111 HIS CB C 27.921 0.3 1 425 111 111 HIS N N 124.122 0.3 1 426 113 113 LEU H H 8.358 0.020 1 427 113 113 LEU C C 173.386 0.3 1 428 113 113 LEU CA C 49.680 0.3 1 429 113 113 LEU CB C 26.707 0.3 1 430 113 113 LEU N N 120.130 0.3 1 431 114 114 ALA H H 8.187 0.020 1 432 114 114 ALA C C 173.379 0.3 1 433 114 114 ALA CA C 53.951 0.3 1 434 114 114 ALA CB C 16.169 0.3 1 435 114 114 ALA N N 119.296 0.3 1 436 115 115 MET H H 8.841 0.020 1 437 115 115 MET C C 173.368 0.3 1 438 115 115 MET CA C 52.331 0.3 1 439 115 115 MET CB C 34.683 0.3 1 440 115 115 MET N N 122.739 0.3 1 441 116 116 THR H H 8.511 0.020 1 442 116 116 THR C C 172.454 0.3 1 443 116 116 THR CA C 59.163 0.3 1 444 116 116 THR CB C 67.608 0.3 1 445 116 116 THR N N 119.525 0.3 1 446 117 117 THR H H 8.973 0.020 1 447 117 117 THR C C 173.469 0.3 1 448 117 117 THR CA C 53.660 0.3 1 449 117 117 THR CB C 67.014 0.3 1 450 117 117 THR N N 117.447 0.3 1 451 118 118 LYS H H 8.568 0.020 1 452 118 118 LYS C C 173.836 0.3 1 453 118 118 LYS CA C 52.047 0.3 1 454 118 118 LYS CB C 34.113 0.3 1 455 118 118 LYS N N 125.413 0.3 1 456 119 119 THR H H 8.531 0.020 1 457 119 119 THR C C 173.611 0.3 1 458 119 119 THR CA C 56.601 0.3 1 459 119 119 THR CB C 64.856 0.3 1 460 119 119 THR N N 112.102 0.3 1 461 120 120 PRO C C 175.086 0.3 1 462 121 121 ALA H H 7.629 0.020 1 463 121 121 ALA C C 176.495 0.3 1 464 121 121 ALA CA C 49.864 0.3 1 465 121 121 ALA CB C 16.275 0.3 1 466 121 121 ALA N N 117.042 0.3 1 467 122 122 GLU H H 7.461 0.020 1 468 122 122 GLU C C 174.064 0.3 1 469 122 122 GLU CA C 53.185 0.3 1 470 122 122 GLU CB C 27.566 0.3 1 471 122 122 GLU N N 119.274 0.3 1 472 123 123 GLN H H 7.763 0.020 1 473 123 123 GLN C C 179.073 0.3 1 474 123 123 GLN CA C 54.988 0.3 1 475 123 123 GLN CB C 26.997 0.3 1 476 123 123 GLN N N 125.511 0.3 1 stop_ save_