data_5825 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific 1H, 13C and 15N resonance assignments of the C-terminal domain of KaiA, a circadian clock protein (reduced form) ; _BMRB_accession_number 5825 _BMRB_flat_file_name bmr5825.str _Entry_type original _Submission_date 2003-06-08 _Accession_date 2003-06-09 _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 Vakonakis Ioannis . . 2 LiWang Andy C. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 95 "13C chemical shifts" 177 "15N chemical shifts" 95 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-02-13 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5824 'oxidized form' stop_ _Original_release_date 2004-02-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Sequence-specific 1H, 13C and 15N resonance assignments of the C-terminal domain of KaiA, a circadian clock protein ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14872133 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vakonakis Ioannis . . 2 LiWang Andy C. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 28 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 403 _Page_last 404 _Year 2004 _Details . loop_ _Keyword assignment 'circadian clock' KaiA 'Thermosynechococcus elongatus' stop_ save_ ################################## # Molecular system description # ################################## save_system_ThKaiA180C _Saveframe_category molecular_system _Mol_system_name 'KaiA C-terminal domain' _Abbreviation_common ThKaiA180C _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ThKaiA180C subunit 1' $ThKaiA180C_monomer 'ThKaiA180C subunit 2' $ThKaiA180C_monomer stop_ _System_molecular_weight . _System_physical_state reduced _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'ThKaiA180C subunit 1' 1 'ThKaiA180C subunit 2' stop_ loop_ _Biological_function 'KaiC autophosphorylation enhancer' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ThKaiA180C_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Thermosynechococcus KaiA' _Name_variant ThKaiA180C _Abbreviation_common ThKaiA180C _Molecular_mass 12583 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 107 _Mol_residue_sequence ; AMARMSPADKRKLLDELRSI YRTIVLEYFNTDAKVNERID EFVSKAFFADISVSQVLEIH VELMDTFSKQLKLEGRSEDI LLDYRLTLIDVIAHLCEMYR RSIPREV ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 MET 3 ALA 4 ARG 5 MET 6 SER 7 PRO 8 ALA 9 ASP 10 LYS 11 ARG 12 LYS 13 LEU 14 LEU 15 ASP 16 GLU 17 LEU 18 ARG 19 SER 20 ILE 21 TYR 22 ARG 23 THR 24 ILE 25 VAL 26 LEU 27 GLU 28 TYR 29 PHE 30 ASN 31 THR 32 ASP 33 ALA 34 LYS 35 VAL 36 ASN 37 GLU 38 ARG 39 ILE 40 ASP 41 GLU 42 PHE 43 VAL 44 SER 45 LYS 46 ALA 47 PHE 48 PHE 49 ALA 50 ASP 51 ILE 52 SER 53 VAL 54 SER 55 GLN 56 VAL 57 LEU 58 GLU 59 ILE 60 HIS 61 VAL 62 GLU 63 LEU 64 MET 65 ASP 66 THR 67 PHE 68 SER 69 LYS 70 GLN 71 LEU 72 LYS 73 LEU 74 GLU 75 GLY 76 ARG 77 SER 78 GLU 79 ASP 80 ILE 81 LEU 82 LEU 83 ASP 84 TYR 85 ARG 86 LEU 87 THR 88 LEU 89 ILE 90 ASP 91 VAL 92 ILE 93 ALA 94 HIS 95 LEU 96 CYS 97 GLU 98 MET 99 TYR 100 ARG 101 ARG 102 SER 103 ILE 104 PRO 105 ARG 106 GLU 107 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-07-28 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 5824 ThKaiA180C_monomer 100.00 107 100.00 100.00 1.98e-69 PDB 1Q6A "Solution Structure Of The C-Terminal Domain Of Thermosynechococcus Elongatus Kaia (Thkaia180c); Averaged Minimized Structure" 100.00 107 100.00 100.00 1.98e-69 PDB 1Q6B "Solution Structure Of The C-Terminal Domain Of Thermosynechococcus Elongatus Kaia (Thkaia180c); Ensemble Of 25 Structures" 100.00 107 100.00 100.00 1.98e-69 PDB 1SUY "Nmr Structure Of The Thkaia180c-Ciiabd Complex (Average Minimized Structure)" 100.00 107 100.00 100.00 1.98e-69 PDB 1SV1 "Nmr Structure Of The Thkaia180c-Ciiabd Complex (25-Structure Ensemble)" 100.00 107 100.00 100.00 1.98e-69 PDB 1V2Z "Crystal Structure Of The C-terminal Domain Of Thermosynechococcus Elongatus Bp-1 Kaia" 97.20 111 100.00 100.00 5.24e-67 DBJ BAB85983 "circadian clock protein KaiA [Synechococcus elongatus]" 97.20 283 100.00 100.00 3.96e-65 DBJ BAC08033 "kaiA [Thermosynechococcus elongatus BP-1]" 97.20 283 100.00 100.00 3.96e-65 DBJ BAD21221 "circadian clock protein KaiA [Thermosynechococcus vulcanus]" 97.20 283 100.00 100.00 3.96e-65 REF NP_681271 "circadian clock protein KaiA [Thermosynechococcus elongatus BP-1]" 97.20 283 100.00 100.00 3.96e-65 REF WP_011056332 "circadian clock protein KaiA [Thermosynechococcus elongatus]" 97.20 283 100.00 100.00 3.96e-65 SP Q6L8K1 "RecName: Full=Circadian clock protein KaiA [Thermosynechococcus vulcanus]" 97.20 283 100.00 100.00 3.96e-65 SP Q79V62 "RecName: Full=Circadian clock protein KaiA [Thermosynechococcus elongatus BP-1]" 97.20 283 100.00 100.00 3.96e-65 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 $ThKaiA180C_monomer 'Thermosynechococcus elongatus' 146786 Eubacteria . Thermosynechococcus elongatus BP-1 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 _Details $ThKaiA180C_monomer 'recombinant technology' 'E. coli' Escherichia coli . BL21(DE3) 'Escherichia coli BL21(DE3) was used for overexpression.' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ThKaiA180C_monomer 1.2 mM '[U-99% 13C; U-99% 15N]' Na2HPO4 20.0 mM . NaCl 20.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version '2.1 Rev 2002.044.17.08' loop_ _Task 'data processing' stop_ _Details ; Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J. and Bax, A. (1995) J. Biomol. NMR., 6, 277-293. ; save_ save_PIPP _Saveframe_category software _Name PIPP _Version 4.2.6 loop_ _Task 'data analysis' stop_ _Details ; Garrett, D.S., Powers, R., Gronenborn, A.M. and Clore, G.M. (1991) J. Magn. Reson., 95, 214-220. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC' _Sample_label . save_ save_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details ; Phosphate buffer was used and the pH was adjusted to 7.07 at 23 C in order to be 7.0 at 50C. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 na temperature 323 0.5 K 'ionic strength' 0.15 0.01 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '15N HSQC' CBCA(CO)NH stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'ThKaiA180C subunit 1' _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 . 8 ALA CA C 54.78 0.2 1 2 . 8 ALA CB C 18.7 0.2 1 3 . 9 ASP H H 7.81 0.02 1 4 . 9 ASP N N 119.78 0.08 1 5 . 9 ASP CB C 40.64 0.2 1 6 . 10 LYS H H 8.31 0.02 1 7 . 10 LYS N N 122.02 0.08 1 8 . 10 LYS CA C 59.61 0.2 1 9 . 10 LYS CB C 32.34 0.2 1 10 . 11 ARG H H 7.96 0.02 1 11 . 11 ARG N N 119.01 0.08 1 12 . 11 ARG CA C 59.53 0.2 1 13 . 11 ARG CB C 29.92 0.2 1 14 . 12 LYS H H 7.66 0.02 1 15 . 12 LYS N N 119.22 0.08 1 16 . 12 LYS CA C 59.34 0.2 1 17 . 12 LYS CB C 32.43 0.2 1 18 . 13 LEU H H 7.84 0.02 1 19 . 13 LEU N N 121.14 0.08 1 20 . 13 LEU CA C 57.49 0.2 1 21 . 13 LEU CB C 41.43 0.2 1 22 . 14 LEU H H 8.36 0.02 1 23 . 14 LEU N N 120.53 0.08 1 24 . 14 LEU CA C 58.5 0.2 1 25 . 14 LEU CB C 41.38 0.2 1 26 . 15 ASP H H 7.99 0.02 1 27 . 15 ASP N N 119.54 0.08 1 28 . 15 ASP CA C 57.96 0.2 1 29 . 15 ASP CB C 40.72 0.2 1 30 . 16 GLU H H 7.69 0.02 1 31 . 16 GLU N N 121.59 0.08 1 32 . 16 GLU CA C 59.77 0.2 1 33 . 16 GLU CB C 29.55 0.2 1 34 . 17 LEU H H 8.77 0.02 1 35 . 17 LEU N N 119.41 0.08 1 36 . 17 LEU CA C 58.53 0.2 1 37 . 17 LEU CB C 40.86 0.2 1 38 . 18 ARG H H 8.55 0.02 1 39 . 18 ARG N N 119.51 0.08 1 40 . 18 ARG CA C 60.75 0.2 1 41 . 18 ARG CB C 30.56 0.2 1 42 . 19 SER H H 7.76 0.02 1 43 . 19 SER N N 115.43 0.08 1 44 . 19 SER CA C 62.08 0.2 1 45 . 19 SER CB C 63.09 0.2 1 46 . 20 ILE H H 8.63 0.02 1 47 . 20 ILE N N 122.49 0.08 1 48 . 20 ILE CA C 65.58 0.2 1 49 . 20 ILE CB C 39.25 0.2 1 50 . 21 TYR H H 9.08 0.02 1 51 . 21 TYR N N 121.57 0.08 1 52 . 21 TYR CA C 63.06 0.2 1 53 . 21 TYR CB C 38.68 0.2 1 54 . 22 ARG H H 7.86 0.02 1 55 . 22 ARG N N 116.47 0.08 1 56 . 22 ARG CA C 60.17 0.2 1 57 . 22 ARG CB C 29.62 0.2 1 58 . 23 THR H H 7.53 0.02 1 59 . 23 THR N N 113.94 0.08 1 60 . 23 THR CA C 67.16 0.2 1 61 . 23 THR CB C 68.77 0.2 1 62 . 24 ILE H H 8.05 0.02 1 63 . 24 ILE N N 121.35 0.08 1 64 . 24 ILE CA C 66.16 0.2 1 65 . 24 ILE CB C 37.37 0.2 1 66 . 25 VAL H H 7.86 0.02 1 67 . 25 VAL N N 117.54 0.08 1 68 . 25 VAL CA C 66.91 0.2 1 69 . 25 VAL CB C 31.61 0.2 1 70 . 26 LEU H H 8.08 0.02 1 71 . 26 LEU N N 117.28 0.08 1 72 . 26 LEU CA C 57.74 0.2 1 73 . 26 LEU CB C 42.14 0.2 1 74 . 27 GLU H H 7.86 0.02 1 75 . 27 GLU N N 116.09 0.08 1 76 . 27 GLU CA C 56.58 0.2 1 77 . 27 GLU CB C 30.88 0.2 1 78 . 28 TYR H H 7.94 0.02 1 79 . 28 TYR N N 120.98 0.08 1 80 . 28 TYR CA C 63.92 0.2 1 81 . 28 TYR CB C 38.95 0.2 1 82 . 29 PHE H H 8.34 0.02 1 83 . 29 PHE N N 111.52 0.08 1 84 . 29 PHE CA C 57.82 0.2 1 85 . 29 PHE CB C 38.4 0.2 1 86 . 30 ASN H H 7.81 0.02 1 87 . 30 ASN N N 120.05 0.08 1 88 . 31 THR CA C 64.03 0.2 1 89 . 31 THR CB C 69.01 0.2 1 90 . 32 ASP H H 8.29 0.02 1 91 . 32 ASP N N 120.39 0.08 1 92 . 32 ASP CA C 54.64 0.2 1 93 . 32 ASP CB C 41.11 0.2 1 94 . 33 ALA H H 7.59 0.02 1 95 . 33 ALA N N 122.22 0.08 1 96 . 33 ALA CA C 52.42 0.2 1 97 . 33 ALA CB C 20.36 0.2 1 98 . 34 LYS H H 8.43 0.02 1 99 . 34 LYS N N 121.44 0.08 1 100 . 34 LYS CA C 55.51 0.2 1 101 . 34 LYS CB C 30.9 0.2 1 102 . 35 VAL H H 7.81 0.02 1 103 . 35 VAL N N 120.06 0.08 1 104 . 35 VAL CA C 64.94 0.2 1 105 . 35 VAL CB C 32.51 0.2 1 106 . 36 ASN H H 8.52 0.02 1 107 . 36 ASN N N 120.19 0.08 1 108 . 36 ASN CA C 57.04 0.2 1 109 . 36 ASN CB C 37.22 0.2 1 110 . 37 GLU H H 7.95 0.02 1 111 . 37 GLU N N 119.34 0.08 1 112 . 37 GLU CA C 59.49 0.2 1 113 . 37 GLU CB C 29.56 0.2 1 114 . 38 ARG H H 7.39 0.02 1 115 . 38 ARG N N 119.74 0.08 1 116 . 38 ARG CA C 57.94 0.2 1 117 . 38 ARG CB C 31.03 0.2 1 118 . 39 ILE H H 8.27 0.02 1 119 . 39 ILE N N 120.16 0.08 1 120 . 39 ILE CA C 66.85 0.2 1 121 . 39 ILE CB C 37.7 0.2 1 122 . 40 ASP H H 7.99 0.02 1 123 . 40 ASP N N 119.54 0.08 1 124 . 40 ASP CA C 57.94 0.2 1 125 . 40 ASP CB C 40.29 0.2 1 126 . 41 GLU H H 8.01 0.02 1 127 . 41 GLU N N 122.96 0.08 1 128 . 41 GLU CA C 59.9 0.2 1 129 . 41 GLU CB C 29.83 0.2 1 130 . 42 PHE H H 8.49 0.02 1 131 . 42 PHE N N 119.16 0.08 1 132 . 42 PHE CA C 62.45 0.2 1 133 . 42 PHE CB C 40.18 0.2 1 134 . 43 VAL H H 9.19 0.02 1 135 . 43 VAL N N 115.76 0.08 1 136 . 43 VAL CA C 66.76 0.2 1 137 . 43 VAL CB C 31.71 0.2 1 138 . 44 SER H H 8.33 0.02 1 139 . 44 SER N N 115.81 0.08 1 140 . 44 SER CA C 62.84 0.2 1 141 . 45 LYS H H 7.84 0.02 1 142 . 45 LYS N N 121.28 0.08 1 143 . 45 LYS CA C 60.17 0.2 1 144 . 45 LYS CB C 32.98 0.2 1 145 . 46 ALA H H 8.69 0.02 1 146 . 46 ALA N N 121.4 0.08 1 147 . 46 ALA CA C 55.07 0.2 1 148 . 46 ALA CB C 17.69 0.2 1 149 . 47 PHE H H 8.75 0.02 1 150 . 47 PHE N N 120.3 0.08 1 151 . 47 PHE CA C 61.42 0.2 1 152 . 47 PHE CB C 39.86 0.2 1 153 . 48 PHE H H 8.28 0.02 1 154 . 48 PHE N N 120.23 0.08 1 155 . 48 PHE CA C 61.31 0.2 1 156 . 48 PHE CB C 38.83 0.2 1 157 . 49 ALA H H 7.62 0.02 1 158 . 49 ALA N N 117.98 0.08 1 159 . 49 ALA CA C 51.94 0.2 1 160 . 49 ALA CB C 20.23 0.2 1 161 . 50 ASP H H 7.8 0.02 1 162 . 50 ASP N N 117.62 0.08 1 163 . 50 ASP CA C 55.1 0.2 1 164 . 50 ASP CB C 40.14 0.2 1 165 . 51 ILE H H 7.39 0.02 1 166 . 51 ILE N N 114.35 0.08 1 167 . 51 ILE CA C 59.65 0.2 1 168 . 51 ILE CB C 37.52 0.2 1 169 . 52 SER H H 8.51 0.02 1 170 . 52 SER N N 119.69 0.08 1 171 . 52 SER CA C 57.14 0.2 1 172 . 52 SER CB C 65.42 0.2 1 173 . 53 VAL H H 8.77 0.02 1 174 . 53 VAL N N 123.02 0.08 1 175 . 54 SER CA C 62.23 0.2 1 176 . 55 GLN H H 7.6 0.02 1 177 . 55 GLN N N 121.15 0.08 1 178 . 55 GLN CA C 58.88 0.2 1 179 . 55 GLN CB C 29.46 0.2 1 180 . 56 VAL H H 7.53 0.02 1 181 . 56 VAL N N 121.06 0.08 1 182 . 56 VAL CA C 67.13 0.2 1 183 . 56 VAL CB C 31.11 0.2 1 184 . 57 LEU H H 8.06 0.02 1 185 . 57 LEU N N 119.31 0.08 1 186 . 57 LEU CA C 58.92 0.2 1 187 . 57 LEU CB C 41.04 0.2 1 188 . 58 GLU H H 7.71 0.02 1 189 . 58 GLU N N 117.52 0.08 1 190 . 58 GLU CA C 59.92 0.2 1 191 . 58 GLU CB C 30.04 0.2 1 192 . 59 ILE H H 7.56 0.02 1 193 . 59 ILE N N 120.21 0.08 1 194 . 59 ILE CA C 65.62 0.2 1 195 . 59 ILE CB C 38.42 0.2 1 196 . 60 HIS H H 7.84 0.02 1 197 . 60 HIS N N 120.01 0.08 1 198 . 60 HIS CA C 61.39 0.2 1 199 . 60 HIS CB C 31.6 0.2 1 200 . 61 VAL H H 8.69 0.02 1 201 . 61 VAL N N 118.54 0.08 1 202 . 61 VAL CA C 67.07 0.2 1 203 . 61 VAL CB C 32.03 0.2 1 204 . 62 GLU H H 8.21 0.02 1 205 . 62 GLU N N 120.1 0.08 1 206 . 62 GLU CA C 59.44 0.2 1 207 . 62 GLU CB C 29.94 0.2 1 208 . 63 LEU H H 7.89 0.02 1 209 . 63 LEU N N 121.26 0.08 1 210 . 63 LEU CA C 57.51 0.2 1 211 . 63 LEU CB C 40.97 0.2 1 212 . 64 MET H H 8.67 0.02 1 213 . 64 MET N N 118.39 0.08 1 214 . 64 MET CA C 57.04 0.2 1 215 . 64 MET CB C 32.86 0.2 1 216 . 65 ASP H H 8.3 0.02 1 217 . 65 ASP N N 121.35 0.08 1 218 . 65 ASP CA C 57.8 0.2 1 219 . 65 ASP CB C 41.37 0.2 1 220 . 66 THR H H 7.88 0.02 1 221 . 66 THR N N 115.89 0.08 1 222 . 66 THR CA C 66.56 0.2 1 223 . 66 THR CB C 68.99 0.2 1 224 . 67 PHE H H 8.69 0.02 1 225 . 67 PHE N N 122.4 0.08 1 226 . 67 PHE CA C 58.94 0.2 1 227 . 67 PHE CB C 38.55 0.2 1 228 . 68 SER H H 8.85 0.02 1 229 . 68 SER N N 115.79 0.08 1 230 . 68 SER CA C 62.98 0.2 1 231 . 69 LYS H H 7.72 0.02 1 232 . 69 LYS N N 119.87 0.08 1 233 . 69 LYS CA C 59.52 0.2 1 234 . 69 LYS CB C 32.61 0.2 1 235 . 70 GLN H H 7.67 0.02 1 236 . 70 GLN N N 119.02 0.08 1 237 . 70 GLN CA C 58.44 0.2 1 238 . 70 GLN CB C 28.6 0.2 1 239 . 71 LEU H H 8.38 0.02 1 240 . 71 LEU N N 119.97 0.08 1 241 . 71 LEU CA C 57.99 0.2 1 242 . 71 LEU CB C 41.22 0.2 1 243 . 72 LYS H H 8.02 0.02 1 244 . 72 LYS N N 118.7 0.08 1 245 . 72 LYS CA C 58.96 0.2 1 246 . 72 LYS CB C 32.48 0.2 1 247 . 73 LEU H H 7.78 0.02 1 248 . 73 LEU N N 121.31 0.08 1 249 . 73 LEU CA C 57.4 0.2 1 250 . 73 LEU CB C 42.15 0.2 1 251 . 74 GLU H H 7.81 0.02 1 252 . 74 GLU N N 117.1 0.08 1 253 . 74 GLU CA C 56.66 0.2 1 254 . 74 GLU CB C 30.89 0.2 1 255 . 75 GLY H H 8.02 0.02 1 256 . 75 GLY N N 108.91 0.08 1 257 . 75 GLY CA C 46.22 0.2 1 258 . 76 ARG H H 8.06 0.02 1 259 . 76 ARG N N 119.65 0.08 1 260 . 76 ARG CA C 55.2 0.2 1 261 . 77 SER H H 8.28 0.02 1 262 . 77 SER N N 115.15 0.08 1 263 . 77 SER CA C 58.59 0.2 1 264 . 77 SER CB C 63.97 0.2 1 265 . 78 GLU H H 8.78 0.02 1 266 . 78 GLU N N 122.12 0.08 1 267 . 78 GLU CA C 57.38 0.2 1 268 . 78 GLU CB C 29.96 0.2 1 269 . 79 ASP H H 8.35 0.02 1 270 . 79 ASP N N 122.09 0.08 1 271 . 79 ASP CA C 56.44 0.2 1 272 . 79 ASP CB C 40.21 0.2 1 273 . 80 ILE H H 7.52 0.02 1 274 . 80 ILE N N 118.1 0.08 1 275 . 80 ILE CA C 62.45 0.2 1 276 . 80 ILE CB C 38.5 0.2 1 277 . 81 LEU H H 7.77 0.02 1 278 . 81 LEU N N 119.62 0.08 1 279 . 82 LEU H H 7.63 0.02 1 280 . 82 LEU N N 120.09 0.08 1 281 . 83 ASP H H 7.63 0.02 1 282 . 83 ASP N N 119.77 0.08 1 283 . 84 TYR CA C 60.34 0.2 1 284 . 85 ARG H H 8.27 0.02 1 285 . 85 ARG N N 120 0.08 1 286 . 85 ARG CA C 60.57 0.2 1 287 . 85 ARG CB C 30.5 0.2 1 288 . 86 LEU H H 7.9 0.02 1 289 . 86 LEU N N 116.71 0.08 1 290 . 86 LEU CA C 58.18 0.2 1 291 . 86 LEU CB C 41.45 0.2 1 292 . 87 THR H H 6.6 0.02 1 293 . 87 THR N N 115.95 0.08 1 294 . 87 THR CA C 66.09 0.2 1 295 . 88 LEU H H 7.05 0.02 1 296 . 88 LEU N N 120.72 0.08 1 297 . 88 LEU CA C 57.78 0.2 1 298 . 88 LEU CB C 41.32 0.2 1 299 . 89 ILE H H 7.84 0.02 1 300 . 89 ILE N N 117.78 0.08 1 301 . 89 ILE CA C 66.33 0.2 1 302 . 89 ILE CB C 38.14 0.2 1 303 . 90 ASP H H 7.65 0.02 1 304 . 90 ASP N N 119.02 0.08 1 305 . 90 ASP CA C 57.26 0.2 1 306 . 90 ASP CB C 41.29 0.2 1 307 . 91 VAL H H 8.36 0.02 1 308 . 91 VAL N N 119.28 0.08 1 309 . 91 VAL CA C 68.12 0.2 1 310 . 91 VAL CB C 31.82 0.2 1 311 . 92 ILE H H 8.88 0.02 1 312 . 92 ILE N N 116.64 0.08 1 313 . 92 ILE CA C 65.9 0.2 1 314 . 92 ILE CB C 37.55 0.2 1 315 . 93 ALA H H 9.33 0.02 1 316 . 93 ALA N N 124.91 0.08 1 317 . 93 ALA CA C 56.24 0.2 1 318 . 93 ALA CB C 18.26 0.2 1 319 . 94 HIS H H 8.08 0.02 1 320 . 94 HIS N N 116.15 0.08 1 321 . 94 HIS CA C 60.95 0.2 1 322 . 94 HIS CB C 29.86 0.2 1 323 . 95 LEU H H 8.71 0.02 1 324 . 95 LEU N N 123.72 0.08 1 325 . 95 LEU CA C 58.27 0.2 1 326 . 95 LEU CB C 42.86 0.2 1 327 . 96 CYS H H 9.05 0.02 1 328 . 96 CYS N N 118.97 0.08 1 329 . 96 CYS CA C 62.72 0.2 1 330 . 96 CYS CB C 38.8 0.2 1 331 . 97 GLU H H 8.43 0.02 1 332 . 97 GLU N N 119.9 0.08 1 333 . 97 GLU CA C 58.41 0.2 1 334 . 97 GLU CB C 29.72 0.2 1 335 . 98 MET H H 7.7 0.02 1 336 . 98 MET N N 119.78 0.08 1 337 . 98 MET CA C 58.55 0.2 1 338 . 98 MET CB C 31.36 0.2 1 339 . 99 TYR H H 7.92 0.02 1 340 . 99 TYR N N 117.43 0.08 1 341 . 99 TYR CA C 60.33 0.2 1 342 . 100 ARG H H 8.16 0.02 1 343 . 100 ARG N N 119.07 0.08 1 344 . 100 ARG CA C 60.18 0.2 1 345 . 100 ARG CB C 30.65 0.2 1 346 . 101 ARG H H 7.98 0.02 1 347 . 101 ARG N N 115.54 0.08 1 348 . 101 ARG CA C 57.94 0.2 1 349 . 101 ARG CB C 30.3 0.2 1 350 . 102 SER H H 7.6 0.02 1 351 . 102 SER N N 114.15 0.08 1 352 . 102 SER CA C 59.64 0.2 1 353 . 102 SER CB C 64.44 0.2 1 354 . 103 ILE H H 7.23 0.02 1 355 . 103 ILE N N 121.68 0.08 1 356 . 104 PRO CA C 63.22 0.2 1 357 . 104 PRO CB C 31.51 0.2 1 358 . 105 ARG H H 8.27 0.02 1 359 . 105 ARG N N 122.48 0.08 1 360 . 105 ARG CA C 55.21 0.2 1 361 . 105 ARG CB C 32.24 0.2 1 362 . 106 GLU H H 8.38 0.02 1 363 . 106 GLU N N 122.26 0.08 1 364 . 106 GLU CA C 56.7 0.2 1 365 . 106 GLU CB C 30.53 0.2 1 366 . 107 VAL H H 7.72 0.02 1 367 . 107 VAL N N 125.23 0.08 1 stop_ save_