data_6232 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; TM1442-PO4 ; _BMRB_accession_number 6232 _BMRB_flat_file_name bmr6232.str _Entry_type original _Submission_date 2004-06-10 _Accession_date 2004-06-11 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'TM1442 in phosphorylated state' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Etezady-Esfarjani Touraj . . 2 Placzek William . . 3 Herrmann Torsten . . 4 Wuthrich Kurt . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 164 "13C chemical shifts" 199 "15N chemical shifts" 103 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-03-22 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5921 'the same protein but unphosphorylated' stop_ _Original_release_date 2007-03-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution structures of the putative anti-sigma-factor antagonist TM1442 from Thermotoga maritima in the free and phosphorylated states.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16826544 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Etezady-Esfarjani Touraj . . 2 Placzek William . . 3 Herrmann Torsten . . 4 Wuthrich Kurt . . stop_ _Journal_abbreviation 'Magn Reson Chem.' _Journal_volume 44 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first S61 _Page_last S70 _Year 2006 _Details . loop_ _Keyword JCSG 'sigma factor' stop_ save_ ################################## # Molecular system description # ################################## save_system_TM1442-PO4 _Saveframe_category molecular_system _Mol_system_name TM1442-PO4 _Abbreviation_common TM1442-PO4 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Tm1442 monomer' $TM1442 stop_ _System_molecular_weight 12300 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details 'TM1442 in phosphorylated state' save_ ######################## # Monomeric polymers # ######################## save_TM1442 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'anti-sigma-factor antagonist' _Abbreviation_common TM1442 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 110 _Mol_residue_sequence ; MNNLKLDIVEQDDKAIVRVQ GDIDAYNSSELKEQLRNFIS TTSKKKIVLDLSSVSYMDXA GLGTLVVILKDAKINGKEFI LSSLKESISRILKLTHLDKI FKITDTVEEA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASN 3 ASN 4 LEU 5 LYS 6 LEU 7 ASP 8 ILE 9 VAL 10 GLU 11 GLN 12 ASP 13 ASP 14 LYS 15 ALA 16 ILE 17 VAL 18 ARG 19 VAL 20 GLN 21 GLY 22 ASP 23 ILE 24 ASP 25 ALA 26 TYR 27 ASN 28 SER 29 SER 30 GLU 31 LEU 32 LYS 33 GLU 34 GLN 35 LEU 36 ARG 37 ASN 38 PHE 39 ILE 40 SER 41 THR 42 THR 43 SER 44 LYS 45 LYS 46 LYS 47 ILE 48 VAL 49 LEU 50 ASP 51 LEU 52 SER 53 SER 54 VAL 55 SER 56 TYR 57 MET 58 ASP 59 SEP 60 ALA 61 GLY 62 LEU 63 GLY 64 THR 65 LEU 66 VAL 67 VAL 68 ILE 69 LEU 70 LYS 71 ASP 72 ALA 73 LYS 74 ILE 75 ASN 76 GLY 77 LYS 78 GLU 79 PHE 80 ILE 81 LEU 82 SER 83 SER 84 LEU 85 LYS 86 GLU 87 SER 88 ILE 89 SER 90 ARG 91 ILE 92 LEU 93 LYS 94 LEU 95 THR 96 HIS 97 LEU 98 ASP 99 LYS 100 ILE 101 PHE 102 LYS 103 ILE 104 THR 105 ASP 106 THR 107 VAL 108 GLU 109 GLU 110 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-06-11 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 5921 TM1442 100.00 110 99.09 99.09 6.78e-68 PDB 1SBO "Solution Structure Of Putative Anti Sigma Factor Antagonist From Thermotoga Maritima (Tm1442)" 100.00 110 99.09 99.09 6.78e-68 PDB 1T6R "Solution Structure Of Tm1442, A Putative Anti Sigma Factor Antagonist In Phosphorylated State" 100.00 110 100.00 100.00 9.94e-68 PDB 1VC1 "Crystal Structure Of The Tm1442 Protein From Thermotoga Maritima, A Homolog Of The Bacillus Subtilis General Stress Response An" 100.00 110 99.09 99.09 6.78e-68 GB AAD36511 "anti-sigma factor antagonist, putative [Thermotoga maritima MSB8]" 100.00 110 99.09 99.09 6.78e-68 GB ACB09678 "anti-sigma-factor antagonist [Thermotoga sp. RQ2]" 100.00 110 99.09 99.09 6.78e-68 GB ADA67453 "anti-sigma-factor antagonist [Thermotoga naphthophila RKU-10]" 100.00 110 99.09 99.09 6.78e-68 GB AGL50372 "anti-sigma F factor antagonist (spoIIAA-2); anti sigma b factor antagonist RsbV [Thermotoga maritima MSB8]" 100.00 110 99.09 99.09 6.78e-68 GB AHD18665 "anti-sigma factor antagonist [Thermotoga maritima MSB8]" 100.00 110 99.09 99.09 6.78e-68 REF NP_229241 "anti-sigma factor antagonist [Thermotoga maritima MSB8]" 100.00 110 99.09 99.09 6.78e-68 REF WP_004081714 "MULTISPECIES: anti-sigma factor antagonist [Thermotoga]" 100.00 110 99.09 99.09 6.78e-68 REF YP_001739361 "anti-sigma-factor antagonist [Thermotoga sp. RQ2]" 100.00 110 99.09 99.09 6.78e-68 REF YP_003346867 "anti-sigma-factor antagonist [Thermotoga naphthophila RKU-10]" 100.00 110 99.09 99.09 6.78e-68 REF YP_007977797 "anti-sigma F factor antagonist (spoIIAA-2); anti sigma b factor antagonist RsbV [Thermotoga maritima MSB8]" 100.00 110 99.09 99.09 6.78e-68 SP Q9X1F5 "RecName: Full=Putative anti-sigma factor antagonist TM_1442 [Thermotoga maritima MSB8]" 100.00 110 99.09 99.09 6.78e-68 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_SEP _Saveframe_category polymer_residue _Mol_type 'L-peptide linking' _Name_common PHOSPHOSERINE _BMRB_code . _PDB_code SEP _Standard_residue_derivative . _Molecular_mass 185.072 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Jun 21 11:37:22 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? OG OG O . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HXT HXT H . 0 . ? HOP2 HOP2 H . 0 . ? HOP3 HOP3 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H ? ? SING N H2 ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB OG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING OG P ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HOP2 ? ? SING O3P HOP3 ? ? stop_ save_ ############# # Ligands # ############# save_SEP _Saveframe_category ligand _Mol_type non-polymer _Name_common SEP _Molecular_mass . _Details . _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TM1442 'Thermotoga maritima' 2336 Bacteria . Thermotoga maritima 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 $TM1442 'recombinant technology' 'E. coli' Escherichia coli pET25b(+) pET 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 $TM1442 1.5 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TM1442 2 mM [U-15N] stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TM1442 1.2 mM '[U-13C; U-15N]' stop_ 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_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HCCH-TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_CBCA(CO)NH_3 _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 HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 pH temperature 313 . K 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation 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 HNCACB HCCH-TOCSY CBCA(CO)NH stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Tm1442 monomer' _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 . 4 LEU N N 122.005 0.1 1 2 . 4 LEU H H 7.980 0.01 1 3 . 4 LEU CA C 57.751 0.1 1 4 . 4 LEU CB C 46.081 0.1 1 5 . 5 LYS N N 126.460 0.1 1 6 . 5 LYS H H 8.467 0.01 1 7 . 5 LYS CA C 58.045 0.1 1 8 . 5 LYS CB C 37.647 0.1 1 9 . 6 LEU N N 123.606 0.1 1 10 . 6 LEU H H 8.434 0.01 1 11 . 6 LEU CA C 56.182 0.1 1 12 . 6 LEU CB C 46.669 0.1 1 13 . 7 ASP N N 123.014 0.1 1 14 . 7 ASP H H 8.218 0.01 1 15 . 7 ASP CA C 56.378 0.1 1 16 . 7 ASP HA H 4.874 0.01 1 17 . 7 ASP CB C 46.669 0.1 1 18 . 7 ASP HB2 H 2.570 0.01 1 19 . 7 ASP HB3 H 2.417 0.01 1 20 . 8 ILE N N 124.580 0.1 1 21 . 8 ILE H H 8.364 0.01 1 22 . 8 ILE CA C 63.733 0.1 1 23 . 8 ILE CB C 42.256 0.1 1 24 . 9 VAL N N 127.851 0.1 1 25 . 9 VAL H H 9.066 0.01 1 26 . 9 VAL CA C 63.505 0.1 1 27 . 9 VAL CB C 37.670 0.1 1 28 . 10 GLU N N 124.522 0.1 1 29 . 10 GLU H H 8.714 0.01 1 30 . 10 GLU CA C 58.378 0.1 1 31 . 10 GLU CB C 34.252 0.1 1 32 . 11 GLN N N 123.033 0.1 1 33 . 11 GLN H H 8.648 0.01 1 34 . 11 GLN CA C 57.163 0.1 1 35 . 13 ASP N N 117.804 0.1 1 36 . 13 ASP H H 8.720 0.01 1 37 . 13 ASP CA C 56.374 0.1 1 38 . 13 ASP HA H 4.588 0.01 1 39 . 13 ASP CB C 43.426 0.1 1 40 . 13 ASP HB2 H 2.740 0.01 1 41 . 14 LYS N N 116.456 0.1 1 42 . 14 LYS H H 7.867 0.01 1 43 . 14 LYS CA C 57.261 0.1 1 44 . 14 LYS CB C 38.235 0.1 1 45 . 15 ALA N N 123.033 0.1 1 46 . 15 ALA H H 8.664 0.01 1 47 . 15 ALA CA C 52.848 0.1 1 48 . 15 ALA HA H 5.095 0.01 1 49 . 15 ALA HB H 1.459 0.01 1 50 . 15 ALA CB C 24.015 0.1 1 51 . 16 ILE N N 123.282 0.1 1 52 . 16 ILE H H 9.245 0.01 1 53 . 16 ILE CA C 62.949 0.1 1 54 . 16 ILE CB C 42.256 0.1 1 55 . 17 VAL N N 127.883 0.1 1 56 . 17 VAL H H 9.418 0.01 1 57 . 17 VAL CA C 63.103 0.1 1 58 . 17 VAL CB C 34.855 0.1 1 59 . 18 ARG N N 127.529 0.1 1 60 . 18 ARG H H 9.240 0.01 1 61 . 18 ARG CA C 58.278 0.1 1 62 . 18 ARG CB C 33.146 0.1 1 63 . 19 VAL N N 123.882 0.1 1 64 . 19 VAL H H 7.202 0.01 1 65 . 19 VAL CA C 63.807 0.1 1 66 . 19 VAL CB C 35.559 0.1 1 67 . 20 GLN N N 126.894 0.1 1 68 . 20 GLN H H 8.633 0.01 1 69 . 20 GLN CA C 57.373 0.1 1 70 . 20 GLN CB C 32.744 0.1 1 71 . 21 GLY N N 111.799 0.1 1 72 . 21 GLY H H 7.557 0.01 1 73 . 21 GLY CA C 46.571 0.1 1 74 . 22 ASP N N 116.718 0.1 1 75 . 22 ASP H H 7.794 0.01 1 76 . 22 ASP CA C 56.574 0.1 1 77 . 22 ASP HA H 4.999 0.01 1 78 . 22 ASP CB C 44.806 0.1 1 79 . 22 ASP HB2 H 2.585 0.01 1 80 . 22 ASP HB3 H 2.473 0.01 1 81 . 23 ILE N N 120.226 0.1 1 82 . 23 ILE H H 7.734 0.01 1 83 . 23 ILE CA C 62.949 0.1 1 84 . 23 ILE CB C 39.804 0.1 1 85 . 24 ASP N N 124.928 0.1 1 86 . 24 ASP H H 8.139 0.01 1 87 . 24 ASP CA C 54.515 0.1 1 88 . 24 ASP HA H 5.381 0.01 1 89 . 24 ASP CB C 47.160 0.1 1 90 . 24 ASP HB2 H 3.095 0.01 1 91 . 24 ASP HB3 H 2.384 0.01 1 92 . 25 ALA N N 122.550 0.1 1 93 . 25 ALA H H 9.484 0.01 1 94 . 25 ALA CA C 57.457 0.1 1 95 . 25 ALA HA H 3.751 0.01 1 96 . 25 ALA HB H 1.149 0.01 1 97 . 25 ALA CB C 20.877 0.1 1 98 . 26 TYR N N 116.527 0.1 1 99 . 26 TYR H H 7.887 0.01 1 100 . 26 TYR CA C 62.164 0.1 1 101 . 26 TYR HA H 4.324 0.01 1 102 . 26 TYR CB C 40.491 0.1 1 103 . 26 TYR HB2 H 3.106 0.01 1 104 . 27 ASN N N 116.231 0.1 1 105 . 27 ASN H H 8.265 0.01 1 106 . 27 ASN CA C 56.378 0.1 1 107 . 27 ASN HA H 4.968 0.01 1 108 . 27 ASN CB C 42.747 0.1 1 109 . 27 ASN HB2 H 3.089 0.01 1 110 . 27 ASN HB3 H 2.831 0.01 1 111 . 28 SER N N 117.070 0.1 1 112 . 28 SER H H 8.276 0.01 1 113 . 28 SER CA C 67.362 0.1 1 114 . 28 SER CB C 65.793 0.1 1 115 . 29 SER CA C 64.433 0.1 1 116 . 30 GLU N N 123.053 0.1 1 117 . 30 GLU H H 7.838 0.01 1 118 . 30 GLU CA C 61.870 0.1 1 119 . 30 GLU CB C 32.057 0.1 1 120 . 31 LEU N N 119.494 0.1 1 121 . 31 LEU H H 7.768 0.01 1 122 . 31 LEU CA C 61.083 0.1 1 123 . 31 LEU CB C 44.331 0.1 1 124 . 32 LYS N N 117.199 0.1 1 125 . 32 LYS H H 8.165 0.01 1 126 . 32 LYS CA C 62.441 0.1 1 127 . 32 LYS CB C 34.733 0.1 1 128 . 33 GLU N N 117.558 0.1 1 129 . 33 GLU H H 8.020 0.01 1 130 . 33 GLU CA C 61.988 0.1 1 131 . 33 GLU CB C 32.379 0.1 1 132 . 34 GLN N N 116.493 0.1 1 133 . 34 GLN H H 8.379 0.01 1 134 . 34 GLN CA C 61.968 0.1 1 135 . 34 GLN CB C 31.468 0.1 1 136 . 35 LEU N N 119.565 0.1 1 137 . 35 LEU H H 8.461 0.01 1 138 . 35 LEU CA C 59.944 0.1 1 139 . 35 LEU CB C 42.795 0.1 1 140 . 36 ARG N N 121.228 0.1 1 141 . 36 ARG H H 8.691 0.01 1 142 . 36 ARG CA C 63.439 0.1 1 143 . 36 ARG CB C 32.645 0.1 1 144 . 37 ASN N N 117.470 0.1 1 145 . 37 ASN H H 7.867 0.01 1 146 . 37 ASN CA C 58.536 0.1 1 147 . 37 ASN HA H 4.375 0.01 1 148 . 37 ASN CB C 40.883 0.1 1 149 . 37 ASN HB2 H 2.839 0.01 1 150 . 38 PHE N N 120.944 0.1 1 151 . 38 PHE H H 8.001 0.01 1 152 . 38 PHE CA C 63.832 0.1 1 153 . 38 PHE HA H 4.214 0.01 1 154 . 38 PHE CB C 42.060 0.1 1 155 . 38 PHE HB2 H 3.327 0.01 1 156 . 38 PHE HB3 H 2.943 0.01 1 157 . 39 ILE N N 119.711 0.1 1 158 . 39 ILE H H 9.067 0.01 1 159 . 39 ILE CA C 68.147 0.1 1 160 . 39 ILE CB C 40.393 0.1 1 161 . 40 SER N N 109.867 0.1 1 162 . 40 SER H H 7.400 0.01 1 163 . 40 SER CA C 63.047 0.1 1 164 . 40 SER CB C 66.185 0.1 1 165 . 41 THR N N 110.550 0.1 1 166 . 41 THR H H 7.356 0.01 1 167 . 41 THR CA C 65.303 0.1 1 168 . 41 THR CB C 70.81 0.1 1 169 . 42 THR N N 117.712 0.1 1 170 . 42 THR H H 7.583 0.01 1 171 . 42 THR CA C 64.252 0.1 1 172 . 43 SER CA C 61.083 0.1 1 173 . 43 SER CB C 66.063 0.1 1 174 . 44 LYS N N 122.314 0.1 1 175 . 44 LYS H H 8.248 0.01 1 176 . 44 LYS CA C 56.967 0.1 1 177 . 44 LYS CB C 34.312 0.1 1 178 . 45 LYS N N 120.485 0.1 1 179 . 45 LYS H H 8.398 0.01 1 180 . 45 LYS CA C 60.105 0.1 1 181 . 45 LYS CB C 36.274 0.1 1 182 . 46 LYS N N 117.394 0.1 1 183 . 46 LYS H H 7.308 0.01 1 184 . 46 LYS CA C 58.045 0.1 1 185 . 46 LYS CB C 37.647 0.1 1 186 . 47 ILE N N 125.671 0.1 1 187 . 47 ILE H H 8.918 0.01 1 188 . 47 ILE CA C 61.902 0.1 1 189 . 47 ILE CB C 41.993 0.1 1 190 . 48 VAL N N 126.833 0.1 1 191 . 48 VAL H H 9.022 0.01 1 192 . 48 VAL CA C 62.006 0.1 1 193 . 48 VAL CB C 36.263 0.1 1 194 . 49 LEU N N 128.879 0.1 1 195 . 49 LEU H H 9.168 0.01 1 196 . 49 LEU CA C 55.966 0.1 1 197 . 49 LEU CB C 45.209 0.1 1 198 . 50 ASP N N 125.462 0.1 1 199 . 50 ASP H H 8.810 0.01 1 200 . 50 ASP CA C 55.765 0.1 1 201 . 50 ASP HA H 4.497 0.01 1 202 . 50 ASP CB C 43.903 0.1 1 203 . 50 ASP HB2 H 2.804 0.01 1 204 . 50 ASP HB3 H 2.113 0.01 1 205 . 51 LEU N N 126.878 0.1 1 206 . 51 LEU H H 8.411 0.01 1 207 . 51 LEU CA C 56.267 0.1 1 208 . 51 LEU CB C 43.199 0.1 1 209 . 52 SER N N 119.677 0.1 1 210 . 52 SER H H 8.836 0.01 1 211 . 52 SER CA C 65.725 0.1 1 212 . 53 SER N N 114.768 0.1 1 213 . 53 SER H H 8.967 0.01 1 214 . 53 SER CA C 59.944 0.1 1 215 . 54 VAL N N 123.765 0.1 1 216 . 54 VAL H H 7.705 0.01 1 217 . 54 VAL CA C 64.954 0.1 1 218 . 54 VAL CB C 34.702 0.1 1 219 . 55 SER N N 121.877 0.1 1 220 . 55 SER H H 8.714 0.01 1 221 . 55 SER CA C 61.967 0.1 1 222 . 55 SER CB C 67.073 0.1 1 223 . 56 TYR N N 122.457 0.1 1 224 . 56 TYR H H 7.781 0.01 1 225 . 56 TYR CA C 60.137 0.1 1 226 . 56 TYR HA H 4.532 0.01 1 227 . 56 TYR CB C 44.047 0.1 1 228 . 56 TYR HB2 H 2.859 0.01 1 229 . 56 TYR HB3 H 2.623 0.01 1 230 . 57 MET N N 124.776 0.1 1 231 . 57 MET H H 7.159 0.01 1 232 . 57 MET CA C 56.476 0.1 1 233 . 57 MET CB C 40.193 0.1 1 234 . 58 ASP N N 124.698 0.1 1 235 . 58 ASP H H 7.501 0.01 1 236 . 58 ASP CA C 54.549 0.1 1 237 . 58 ASP HA H 4.667 0.01 1 238 . 58 ASP CB C 44.625 0.1 1 239 . 58 ASP HB2 H 3.313 0.01 1 240 . 58 ASP HB3 H 2.715 0.01 1 241 . 59 SEP N N 116.146 0.1 1 242 . 59 SEP H H 10.049 0.01 1 243 . 59 SEP CA C 63.701 0.1 1 244 . 59 SEP CB C 67.073 0.1 1 245 . 60 ALA N N 125.644 0.1 1 246 . 60 ALA H H 7.794 0.01 1 247 . 60 ALA CA C 57.054 0.1 1 248 . 60 ALA HA H 4.031 0.01 1 249 . 60 ALA HB H 1.360 0.01 1 250 . 60 ALA CB C 20.057 0.1 1 251 . 61 GLY N N 110.645 0.1 1 252 . 61 GLY H H 8.714 0.01 1 253 . 61 GLY CA C 50.406 0.1 1 254 . 62 LEU N N 122.376 0.1 1 255 . 62 LEU H H 8.137 0.01 1 256 . 62 LEU CA C 60.522 0.1 1 257 . 62 LEU CB C 44.625 0.1 1 258 . 63 GLY N N 102.558 0.1 1 259 . 63 GLY H H 7.995 0.01 1 260 . 63 GLY CA C 49.924 0.1 1 261 . 64 THR N N 117.469 0.1 1 262 . 64 THR H H 7.862 0.01 1 263 . 64 THR CA C 70.156 0.1 1 264 . 64 THR CB C 70.44 0.1 1 265 . 65 LEU N N 120.992 0.1 1 266 . 65 LEU H H 8.048 0.01 1 267 . 65 LEU CA C 61.196 0.1 1 268 . 65 LEU CB C 44.143 0.1 1 269 . 66 VAL N N 116.306 0.1 1 270 . 66 VAL H H 7.398 0.01 1 271 . 66 VAL CA C 69.289 0.1 1 272 . 66 VAL CB C 33.835 0.1 1 273 . 67 VAL N N 120.695 0.1 1 274 . 67 VAL H H 7.644 0.01 1 275 . 67 VAL CA C 69.289 0.1 1 276 . 67 VAL CB C 33.738 0.1 1 277 . 68 ILE N N 119.262 0.1 1 278 . 68 ILE H H 8.125 0.01 1 279 . 68 ILE CA C 65.917 0.1 1 280 . 68 ILE CB C 39.230 0.1 1 281 . 69 LEU N N 121.145 0.1 1 282 . 69 LEU H H 7.829 0.01 1 283 . 69 LEU CA C 60.715 0.1 1 284 . 69 LEU CB C 43.854 0.1 1 285 . 70 LYS N N 119.194 0.1 1 286 . 70 LYS H H 7.825 0.01 1 287 . 70 LYS CA C 63.316 0.1 1 288 . 70 LYS CB C 32.486 0.1 1 289 . 71 ASP N N 120.014 0.1 1 290 . 71 ASP H H 8.074 0.01 1 291 . 71 ASP CA C 60.087 0.1 1 292 . 71 ASP HA H 4.281 0.01 1 293 . 71 ASP CB C 42.882 0.1 1 294 . 71 ASP HB2 H 2.751 0.01 1 295 . 71 ASP HB3 H 2.331 0.01 1 296 . 72 ALA N N 123.443 0.1 1 297 . 72 ALA H H 8.870 0.01 1 298 . 72 ALA CA C 58.306 0.1 1 299 . 72 ALA HA H 3.752 0.01 1 300 . 72 ALA HB H 1.351 0.01 1 301 . 72 ALA CB C 20.057 0.1 1 302 . 73 LYS N N 117.692 0.1 1 303 . 73 LYS H H 8.566 0.01 1 304 . 73 LYS CA C 61.100 0.1 1 305 . 73 LYS CB C 34.316 0.1 1 306 . 74 ILE N N 120.350 0.1 1 307 . 74 ILE H H 8.668 0.01 1 308 . 74 ILE CA C 67.073 0.1 1 309 . 74 ILE CB C 40.097 0.1 1 310 . 75 ASN N N 115.987 0.1 1 311 . 75 ASN H H 7.353 0.01 1 312 . 75 ASN CA C 56.476 0.1 1 313 . 75 ASN HA H 4.728 0.01 1 314 . 75 ASN CB C 42.891 0.1 1 315 . 75 ASN HB2 H 2.790 0.01 1 316 . 75 ASN HB3 H 2.452 0.01 1 317 . 76 GLY N N 108.313 0.1 1 318 . 76 GLY H H 7.801 0.01 1 319 . 76 GLY CA C 49.539 0.1 1 320 . 77 LYS N N 117.120 0.1 1 321 . 77 LYS H H 8.427 0.01 1 322 . 77 LYS CA C 55.994 0.1 1 323 . 77 LYS CB C 36.629 0.1 1 324 . 78 GLU N N 122.063 0.1 1 325 . 78 GLU H H 8.577 0.01 1 326 . 78 GLU CA C 58.306 0.1 1 327 . 78 GLU CB C 34.124 0.1 1 328 . 79 PHE N N 127.346 0.1 1 329 . 79 PHE H H 8.542 0.01 1 330 . 79 PHE CA C 58.499 0.1 1 331 . 79 PHE HA H 5.547 0.01 1 332 . 79 PHE CB C 44.625 0.1 1 333 . 79 PHE HB2 H 3.126 0.01 1 334 . 79 PHE HB3 H 2.599 0.01 1 335 . 80 ILE N N 129.965 0.1 1 336 . 80 ILE H H 8.701 0.01 1 337 . 80 ILE CA C 62.256 0.1 1 338 . 80 ILE CB C 45.011 0.1 1 339 . 81 LEU N N 123.873 0.1 1 340 . 81 LEU H H 8.514 0.01 1 341 . 81 LEU CA C 55.416 0.1 1 342 . 81 LEU CB C 46.648 0.1 1 343 . 82 SER N N 114.168 0.1 1 344 . 82 SER H H 8.403 0.01 1 345 . 82 SER CA C 58.884 0.1 1 346 . 82 SER CB C 69.675 0.1 1 347 . 83 SER N N 115.312 0.1 1 348 . 83 SER H H 7.592 0.01 1 349 . 83 SER CA C 60.040 0.1 1 350 . 83 SER CB C 63.701 0.1 1 351 . 84 LEU N N 118.601 0.1 1 352 . 84 LEU H H 8.199 0.01 1 353 . 84 LEU CA C 58.402 0.1 1 354 . 84 LEU CB C 45.107 0.1 1 355 . 85 LYS N N 123.397 0.1 1 356 . 85 LYS H H 9.328 0.01 1 357 . 85 LYS CA C 58.276 0.1 1 358 . 85 LYS CB C 36.182 0.1 1 359 . 87 SER N N 117.535 0.1 1 360 . 87 SER H H 8.343 0.01 1 361 . 87 SER CA C 64.524 0.1 1 362 . 88 ILE N N 121.032 0.1 1 363 . 88 ILE H H 7.132 0.01 1 364 . 88 ILE CA C 65.067 0.1 1 365 . 88 ILE CB C 39.623 0.1 1 366 . 89 SER N N 115.743 0.1 1 367 . 89 SER H H 8.398 0.01 1 368 . 89 SER CA C 64.433 0.1 1 369 . 90 ARG N N 118.533 0.1 1 370 . 90 ARG H H 8.437 0.01 1 371 . 90 ARG CA C 62.079 0.1 1 372 . 90 ARG CB C 32.741 0.1 1 373 . 91 ILE N N 118.181 0.1 1 374 . 91 ILE H H 7.080 0.01 1 375 . 91 ILE CA C 65.731 0.1 1 376 . 91 ILE CB C 40.372 0.1 1 377 . 92 LEU N N 121.239 0.1 1 378 . 92 LEU H H 7.587 0.01 1 379 . 92 LEU CA C 60.697 0.1 1 380 . 92 LEU CB C 43.031 0.1 1 381 . 93 LYS N N 117.894 0.1 1 382 . 93 LYS H H 8.154 0.01 1 383 . 93 LYS CA C 61.742 0.1 1 384 . 93 LYS CB C 34.863 0.1 1 385 . 94 LEU N N 120.951 0.1 1 386 . 94 LEU H H 8.024 0.01 1 387 . 94 LEU CA C 60.317 0.1 1 388 . 94 LEU CB C 45.501 0.1 1 389 . 95 THR N N 102.954 0.1 1 390 . 95 THR H H 7.114 0.01 1 391 . 95 THR CA C 64.211 0.1 1 392 . 95 THR CB C 70.43 0.1 1 393 . 96 HIS N N 109.742 0.1 1 394 . 96 HIS H H 7.285 0.01 1 395 . 96 HIS CA C 60.032 0.1 1 396 . 96 HIS HA H 4.508 0.01 1 397 . 96 HIS CB C 29.640 0.1 1 398 . 96 HIS HB2 H 3.791 0.01 1 399 . 96 HIS HB3 H 3.367 0.01 1 400 . 97 LEU N N 119.397 0.1 1 401 . 97 LEU H H 8.199 0.01 1 402 . 97 LEU CA C 60.032 0.1 1 403 . 97 LEU CB C 44.836 0.1 1 404 . 98 ASP N N 117.961 0.1 1 405 . 98 ASP H H 8.599 0.01 1 406 . 98 ASP CA C 58.228 0.1 1 407 . 98 ASP HA H 4.209 0.01 1 408 . 98 ASP CB C 41.350 0.1 1 409 . 98 ASP HB2 H 2.748 0.01 1 410 . 98 ASP HB3 H 2.132 0.01 1 411 . 99 LYS N N 116.287 0.1 1 412 . 99 LYS H H 7.649 0.01 1 413 . 99 LYS CA C 59.944 0.1 1 414 . 99 LYS CB C 35.183 0.1 1 415 . 100 ILE N N 112.930 0.1 1 416 . 100 ILE H H 7.412 0.01 1 417 . 100 ILE CA C 63.799 0.1 1 418 . 100 ILE CB C 41.252 0.1 1 419 . 101 PHE N N 118.669 0.1 1 420 . 101 PHE H H 7.478 0.01 1 421 . 101 PHE CA C 60.177 0.1 1 422 . 101 PHE HA H 4.778 0.01 1 423 . 101 PHE CB C 43.788 0.1 1 424 . 101 PHE HB2 H 2.887 0.01 1 425 . 101 PHE HB3 H 2.625 0.01 1 426 . 102 LYS N N 123.067 0.1 1 427 . 102 LYS H H 8.648 0.01 1 428 . 102 LYS CA C 58.728 0.1 1 429 . 102 LYS CB C 35.097 0.1 1 430 . 103 ILE N N 126.796 0.1 1 431 . 103 ILE H H 8.117 0.01 1 432 . 103 ILE CA C 61.870 0.1 1 433 . 103 ILE CB C 43.433 0.1 1 434 . 104 THR N N 117.244 0.1 1 435 . 104 THR H H 8.999 0.01 1 436 . 104 THR CA C 61.968 0.1 1 437 . 104 THR CB C 70.92 0.1 1 438 . 105 ASP N N 122.840 0.1 1 439 . 105 ASP H H 8.997 0.01 1 440 . 105 ASP CA C 59.909 0.1 1 441 . 105 ASP HA H 4.584 0.01 1 442 . 105 ASP CB C 43.923 0.1 1 443 . 105 ASP HB2 H 2.871 0.01 1 444 . 105 ASP HB3 H 2.697 0.01 1 445 . 106 THR N N 106.730 0.1 1 446 . 106 THR H H 7.553 0.01 1 447 . 106 THR CA C 61.870 0.1 1 448 . 106 THR CB C 72.41 0.1 1 449 . 107 VAL N N 121.228 0.1 1 450 . 107 VAL H H 8.705 0.01 1 451 . 107 VAL CA C 67.512 0.1 1 452 . 107 VAL CB C 34.190 0.1 1 453 . 108 GLU N N 119.980 0.1 1 454 . 108 GLU H H 8.587 0.01 1 455 . 108 GLU CA C 61.967 0.1 1 456 . 108 GLU CB C 31.426 0.1 1 457 . 109 GLU N N 115.799 0.1 1 458 . 109 GLU H H 7.099 0.01 1 459 . 109 GLU CA C 58.438 0.1 1 460 . 109 GLU CB C 33.724 0.1 1 461 . 110 ALA N N 127.082 0.1 1 462 . 110 ALA H H 7.108 0.01 1 463 . 110 ALA CA C 56.672 0.1 1 464 . 110 ALA HA H 3.819 0.01 1 465 . 110 ALA HB H 1.246 0.01 1 466 . 110 ALA CB C 23.231 0.1 1 stop_ save_