data_19286 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Structure of BeF3 Activated Sma0114 ; _BMRB_accession_number 19286 _BMRB_flat_file_name bmr19286.str _Entry_type original _Submission_date 2013-06-04 _Accession_date 2013-06-04 _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 Sheftic Sarah R. . 2 Gage Daniel J. . 3 Alexandrescu Andrei T. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 206 "13C chemical shifts" 71 "15N chemical shifts" 103 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-01-27 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 16905 Sma0114 stop_ _Original_release_date 2014-01-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR Structure of the HWE Kinase Associated Response Regulator Sma0114 in Its Activated State' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24364624 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sheftic Sarah R. . 2 Gage Daniel J. . 3 Alexandrescu Andrei T. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 53 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 311 _Page_last 322 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'BeF3 Activated Sma0114' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Two-component response regulator' $entity_1 'CALCIUM ION' $entity_CA 'BERYLLIUM TRIFLUORIDE ION' $entity_BEF stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 13606.619 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 123 _Mol_residue_sequence ; GSHMTERRLRVLVVEDESMI AMLIEDTLCELGHEVAATAS RMQEALDIARKGQFDIAIID VNLDGEPSYPVADILAERNV PFIFATGYGSKGLDTRYSNI PLLTKPFLDSELEAVLVQIS KEV ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 HIS 4 MET 5 THR 6 GLU 7 ARG 8 ARG 9 LEU 10 ARG 11 VAL 12 LEU 13 VAL 14 VAL 15 GLU 16 ASP 17 GLU 18 SER 19 MET 20 ILE 21 ALA 22 MET 23 LEU 24 ILE 25 GLU 26 ASP 27 THR 28 LEU 29 CYS 30 GLU 31 LEU 32 GLY 33 HIS 34 GLU 35 VAL 36 ALA 37 ALA 38 THR 39 ALA 40 SER 41 ARG 42 MET 43 GLN 44 GLU 45 ALA 46 LEU 47 ASP 48 ILE 49 ALA 50 ARG 51 LYS 52 GLY 53 GLN 54 PHE 55 ASP 56 ILE 57 ALA 58 ILE 59 ILE 60 ASP 61 VAL 62 ASN 63 LEU 64 ASP 65 GLY 66 GLU 67 PRO 68 SER 69 TYR 70 PRO 71 VAL 72 ALA 73 ASP 74 ILE 75 LEU 76 ALA 77 GLU 78 ARG 79 ASN 80 VAL 81 PRO 82 PHE 83 ILE 84 PHE 85 ALA 86 THR 87 GLY 88 TYR 89 GLY 90 SER 91 LYS 92 GLY 93 LEU 94 ASP 95 THR 96 ARG 97 TYR 98 SER 99 ASN 100 ILE 101 PRO 102 LEU 103 LEU 104 THR 105 LYS 106 PRO 107 PHE 108 LEU 109 ASP 110 SER 111 GLU 112 LEU 113 GLU 114 ALA 115 VAL 116 LEU 117 VAL 118 GLN 119 ILE 120 SER 121 LYS 122 GLU 123 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 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 16905 Sma0114 100.00 123 100.00 100.00 1.18e-82 PDB 2LPM "Chemical Shift And Structure Assignments For Sma0114" 100.00 123 100.00 100.00 1.18e-82 PDB 2M98 "Nmr Structure Of Bef3 Activated Sma0114" 100.00 123 100.00 100.00 1.18e-82 EMBL CCM71308 "two-component response regulator [Sinorhizobium meliloti Rm41]" 97.56 120 100.00 100.00 9.26e-80 EMBL CDH82688 "two-component response regulator [Sinorhizobium meliloti RU11/001]" 97.56 120 100.00 100.00 9.26e-80 GB AAK64716 "two-component response regulator [Sinorhizobium meliloti 1021]" 97.56 120 100.00 100.00 9.26e-80 GB AEG06710 "response regulator receiver protein [Sinorhizobium meliloti BL225C]" 97.56 120 100.00 100.00 9.26e-80 GB AEG57042 "response regulator receiver protein [Sinorhizobium meliloti AK83]" 97.56 120 100.00 100.00 9.26e-80 GB AEH82764 "two-component response regulator [Sinorhizobium meliloti SM11]" 97.56 120 100.00 100.00 9.26e-80 GB AGG69741 "two-component response regulator [Sinorhizobium meliloti 2011]" 97.56 120 100.00 100.00 9.26e-80 REF NP_435304 "two-component response regulator [Sinorhizobium meliloti 1021]" 97.56 120 100.00 100.00 9.26e-80 REF WP_010967059 "hypothetical protein [Sinorhizobium meliloti]" 97.56 120 100.00 100.00 9.26e-80 REF WP_033048070 "chemotaxis protein CheY [Sinorhizobium meliloti]" 97.56 120 98.33 98.33 4.87e-78 REF WP_046066705 "chemotaxis protein CheY [Sinorhizobium meliloti]" 97.56 120 99.17 99.17 7.05e-79 stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_CA (CALCIUM ION)" _BMRB_code CA _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_BEF _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_BEF (BERYLLIUM TRIFLUORIDE ION)" _BMRB_code BEF _PDB_code BEF _Molecular_mass 66.007 _Mol_charge -1 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons BE BE BE . -1 . ? F1 F1 F . 0 . ? F2 F2 F . 0 . ? F3 F3 F . 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 BE F1 ? ? SING BE F2 ? ? SING BE F3 ? ? stop_ _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 $entity_1 'Sinorhizobium meliloti' 382 Bacteria . Sinorhizobium meliloti 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 $entity_1 'recombinant technology' . Escherichia coli . pet-28+ 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 'CALCIUM ION' 1.5 mM 'natural abundance' 'BERYLLIUM TRIFLUORIDE ION' 36 mM 'natural abundance' $entity_1 0.5 mM '[U-100% 15N]' DTT 1 mM 'natural abundance' 'sodium azide' 0.02 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling 'CALCIUM ION' 1.5 mM 'natural abundance' 'BERYLLIUM TRIFLUORIDE ION' 36 mM 'natural abundance' $entity_1 0.5 mM '[U-100% 13C; U-100% 15N]' DTT 1 mM 'natural abundance' 'sodium azide' 0.02 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name Felix _Version . loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' . . stop_ loop_ _Task processing stop_ _Details . save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version . loop_ _Vendor _Address _Electronic_address Brunger . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _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_2D_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_2 save_ save_3D_1H-15N_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_2 save_ save_2D_1H-1H_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_2 save_ save_2D_DQF-COSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _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' 38 . mM pH 6.0 . pH pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-1H NOESY' '3D HNCACB' '3D 1H-15N NOESY' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Two-component response regulator' _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 4 MET H H 8.45 . 1 2 4 4 MET N N 121.52 . 1 3 5 5 THR H H 8.09 . 1 4 5 5 THR N N 115.27 . 1 5 6 6 GLU H H 8.43 . 1 6 6 6 GLU N N 123.58 . 1 7 7 7 ARG H H 8.03 . 1 8 7 7 ARG N N 120.85 . 1 9 8 8 ARG H H 8.31 . 1 10 8 8 ARG HA H 4.37 . 1 11 8 8 ARG N N 125.41 . 1 12 9 9 LEU H H 11.10 . 1 13 9 9 LEU HA H 4.61 . 1 14 9 9 LEU N N 130.33 . 1 15 10 10 ARG H H 9.62 . 1 16 10 10 ARG HA H 5.01 . 1 17 10 10 ARG CA C 55.94 . 1 18 10 10 ARG N N 121.42 . 1 19 11 11 VAL H H 9.21 . 1 20 11 11 VAL HA H 4.97 . 1 21 11 11 VAL N N 125.11 . 1 22 12 12 LEU H H 8.26 . 1 23 12 12 LEU HA H 4.78 . 1 24 12 12 LEU N N 130.05 . 1 25 13 13 VAL H H 8.33 . 1 26 13 13 VAL HA H 4.61 . 1 27 13 13 VAL N N 128.06 . 1 28 14 14 VAL H H 8.84 . 1 29 14 14 VAL HA H 4.70 . 1 30 14 14 VAL HG1 H 0.79 . 2 31 14 14 VAL N N 128.47 . 1 32 15 15 GLU H H 7.95 . 1 33 15 15 GLU HA H 4.62 . 1 34 15 15 GLU N N 124.84 . 1 35 16 16 ASP H H 9.36 . 1 36 16 16 ASP HA H 4.54 . 1 37 16 16 ASP N N 125.84 . 1 38 17 17 GLU HA H 4.29 . 1 39 17 17 GLU CA C 55.54 . 1 40 18 18 SER H H 8.82 . 1 41 18 18 SER HA H 4.61 . 1 42 18 18 SER N N 124.99 . 1 43 19 19 MET H H 9.03 . 1 44 19 19 MET N N 119.94 . 1 45 20 20 ILE H H 7.20 . 1 46 20 20 ILE HG12 H 1.71 . . 47 20 20 ILE HG2 H 0.65 . 1 48 20 20 ILE HD1 H 0.23 . 1 49 20 20 ILE CG1 C 27.61 . 1 50 20 20 ILE CG2 C 14.07 . 1 51 20 20 ILE CD1 C 14.07 . 1 52 20 20 ILE N N 118.70 . 1 53 21 21 ALA H H 8.37 . 1 54 21 21 ALA HB H 1.34 . 1 55 21 21 ALA CB C 18.86 . 1 56 21 21 ALA N N 123.50 . 1 57 22 22 MET H H 8.09 . 1 58 22 22 MET HA H 4.16 . 1 59 22 22 MET CA C 58.44 . 1 60 22 22 MET N N 115.79 . 1 61 23 23 LEU H H 7.49 . 1 62 23 23 LEU N N 120.40 . 1 63 24 24 ILE H H 8.63 . 1 64 24 24 ILE HA H 3.52 . 1 65 24 24 ILE HB H 1.94 . 1 66 24 24 ILE HG2 H 0.68 . 1 67 24 24 ILE CA C 67.19 . 1 68 24 24 ILE CB C 38.44 . 1 69 24 24 ILE CG2 C 14.07 . 1 70 24 24 ILE N N 120.84 . 1 71 25 25 GLU H H 8.55 . 1 72 25 25 GLU N N 119.38 . 1 73 26 26 ASP H H 8.89 . 1 74 26 26 ASP N N 119.70 . 1 75 27 27 THR H H 8.10 . 1 76 27 27 THR HA H 4.27 . 1 77 27 27 THR CA C 68.89 . 1 78 27 27 THR N N 117.46 . 1 79 28 28 LEU H H 8.61 . 1 80 28 28 LEU HA H 3.92 . 1 81 28 28 LEU CA C 58.44 . 1 82 28 28 LEU N N 120.44 . 1 83 29 29 CYS H H 8.18 . 1 84 29 29 CYS N N 116.92 . 1 85 30 30 GLU H H 8.06 . 1 86 30 30 GLU HA H 4.16 . 1 87 30 30 GLU CA C 59.69 . 1 88 30 30 GLU N N 122.82 . 1 89 31 31 LEU H H 7.66 . 1 90 31 31 LEU N N 116.98 . 1 91 32 32 GLY H H 7.60 . 1 92 32 32 GLY N N 105.41 . 1 93 33 33 HIS H H 7.78 . 1 94 33 33 HIS HA H 5.13 . 1 95 33 33 HIS HB2 H 3.37 . 2 96 33 33 HIS CA C 56.35 . 1 97 33 33 HIS CB C 33.47 . 1 98 33 33 HIS N N 119.38 . 1 99 34 34 GLU H H 8.87 . 1 100 34 34 GLU N N 117.93 . 1 101 35 35 VAL H H 8.87 . 1 102 35 35 VAL HA H 4.71 . 1 103 35 35 VAL N N 125.86 . 1 104 36 36 ALA H H 9.11 . 1 105 36 36 ALA HA H 4.20 . 1 106 36 36 ALA HB H 1.37 . 1 107 36 36 ALA CB C 23.86 . 1 108 36 36 ALA N N 132.95 . 1 109 37 37 ALA H H 7.48 . 1 110 37 37 ALA N N 115.42 . 1 111 38 38 THR H H 8.17 . 1 112 38 38 THR N N 112.98 . 1 113 39 39 ALA HB H 1.37 . 1 114 39 39 ALA CB C 22.61 . 1 115 40 40 SER H H 8.98 . 1 116 40 40 SER HA H 4.45 . 1 117 40 40 SER CA C 57.48 . 1 118 40 40 SER N N 113.63 . 1 119 41 41 ARG H H 7.34 . 1 120 41 41 ARG HB2 H 2.05 . 2 121 41 41 ARG CB C 34.11 . 1 122 41 41 ARG N N 117.89 . 1 123 42 42 MET H H 9.34 . 1 124 42 42 MET HA H 4.04 . 1 125 42 42 MET N N 123.46 . 1 126 43 43 GLN H H 8.94 . 1 127 43 43 GLN N N 117.01 . 1 128 44 44 GLU H H 7.16 . 1 129 44 44 GLU HB2 H 2.28 . 2 130 44 44 GLU CB C 26.69 . 1 131 44 44 GLU N N 117.43 . 1 132 45 45 ALA H H 8.22 . 1 133 45 45 ALA HA H 3.68 . 1 134 45 45 ALA HB H 1.28 . 1 135 45 45 ALA CA C 55.94 . 1 136 45 45 ALA CB C 20.94 . 1 137 45 45 ALA N N 121.06 . 1 138 46 46 LEU H H 8.35 . 1 139 46 46 LEU N N 116.75 . 1 140 47 47 ASP H H 7.40 . 1 141 47 47 ASP N N 117.76 . 1 142 48 48 ILE H H 8.22 . 1 143 48 48 ILE HG12 H 1.07 . 2 144 48 48 ILE HG2 H 0.88 . 1 145 48 48 ILE HD1 H 0.39 . 1 146 48 48 ILE CG1 C 26.57 . 1 147 48 48 ILE CG2 C 20.32 . 1 148 48 48 ILE CD1 C 16.57 . 1 149 48 48 ILE N N 118.66 . 1 150 49 49 ALA H H 8.61 . 1 151 49 49 ALA HA H 4.04 . 1 152 49 49 ALA HB H 1.33 . 1 153 49 49 ALA CA C 55.94 . 1 154 49 49 ALA CB C 18.12 . 1 155 49 49 ALA N N 123.15 . 1 156 50 50 ARG H H 7.44 . 1 157 50 50 ARG HB2 H 1.70 . 2 158 50 50 ARG CB C 26.57 . 1 159 50 50 ARG N N 113.11 . 1 160 51 51 LYS H H 7.55 . 1 161 51 51 LYS N N 114.91 . 1 162 52 52 GLY H H 8.92 . 1 163 52 52 GLY N N 108.15 . 1 164 53 53 GLN H H 8.32 . 1 165 53 53 GLN N N 120.45 . 1 166 54 54 PHE H H 7.18 . 1 167 54 54 PHE HD1 H 7.14 . 3 168 54 54 PHE HE1 H 7.00 . 3 169 54 54 PHE HZ H 6.92 . 1 170 54 54 PHE N N 119.09 . 1 171 55 55 ASP H H 9.33 . 1 172 55 55 ASP N N 117.29 . 1 173 56 56 ILE H H 7.69 . 1 174 56 56 ILE HA H 5.22 . 1 175 56 56 ILE HG2 H 0.78 . 1 176 56 56 ILE HD1 H 0.60 . 1 177 56 56 ILE CA C 59.69 . 1 178 56 56 ILE CG2 C 19.77 . 1 179 56 56 ILE CD1 C 16.20 . 1 180 56 56 ILE N N 109.55 . 1 181 57 57 ALA H H 8.00 . 1 182 57 57 ALA HA H 5.48 . 1 183 57 57 ALA CA C 50.94 . 1 184 57 57 ALA N N 122.39 . 1 185 58 58 ILE HD1 H 0.40 . 1 186 58 58 ILE CD1 C 11.36 . 1 187 59 59 ILE H H 8.93 . 1 188 59 59 ILE HA H 4.99 . 1 189 59 59 ILE CA C 57.19 . 1 190 59 59 ILE N N 122.95 . 1 191 60 60 ASP H H 8.36 . 1 192 60 60 ASP HA H 5.10 . 1 193 60 60 ASP CA C 55.10 . 1 194 60 60 ASP N N 127.32 . 1 195 61 61 VAL H H 8.54 . 1 196 61 61 VAL HA H 3.70 . 1 197 61 61 VAL HB H 1.96 . 1 198 61 61 VAL CA C 64.63 . 1 199 61 61 VAL CB C 31.59 . 1 200 61 61 VAL N N 121.04 . 1 201 63 63 LEU H H 8.96 . 1 202 63 63 LEU HA H 4.40 . 1 203 63 63 LEU CA C 52.81 . 1 204 63 63 LEU N N 121.83 . 1 205 64 64 ASP H H 9.84 . 1 206 64 64 ASP HA H 4.29 . 1 207 64 64 ASP HB2 H 3.19 . . 208 64 64 ASP CA C 55.94 . 1 209 64 64 ASP CB C 40.39 . 1 210 64 64 ASP N N 128.45 . 1 211 65 65 GLY H H 8.40 . 1 212 65 65 GLY HA2 H 4.21 . 2 213 65 65 GLY HA3 H 3.56 . 2 214 65 65 GLY N N 133.58 . 1 215 66 66 GLU H H 7.79 . 1 216 66 66 GLU HA H 4.92 . 1 217 66 66 GLU CA C 53.10 . 1 218 66 66 GLU N N 121.11 . 1 219 69 69 TYR H H 6.48 . 1 220 69 69 TYR HA H 4.41 . 1 221 69 69 TYR HD1 H 6.98 . 3 222 69 69 TYR HE1 H 6.70 . 3 223 69 69 TYR CA C 60.97 . 1 224 69 69 TYR N N 120.02 . 1 225 71 71 VAL H H 7.64 . 1 226 71 71 VAL HG1 H 0.68 . 4 227 71 71 VAL CG1 C 22.61 . 4 228 71 71 VAL N N 115.00 . 1 229 72 72 ALA H H 6.89 . 1 230 72 72 ALA HB H 1.11 . 1 231 72 72 ALA CB C 20.11 . 1 232 72 72 ALA N N 122.00 . 1 233 73 73 ASP H H 8.61 . 1 234 73 73 ASP N N 116.02 . 1 235 74 74 ILE H H 7.06 . 1 236 74 74 ILE N N 120.95 . 1 237 75 75 LEU H H 7.46 . 1 238 75 75 LEU HD1 H 0.39 . 4 239 75 75 LEU CD1 C 20.11 . 4 240 75 75 LEU N N 119.76 . 1 241 76 76 ALA H H 8.91 . 1 242 76 76 ALA N N 121.16 . 1 243 77 77 GLU H H 7.80 . 1 244 77 77 GLU N N 120.34 . 1 245 78 78 ARG H H 7.74 . 1 246 78 78 ARG N N 116.21 . 1 247 79 79 ASN H H 8.03 . 1 248 79 79 ASN N N 116.23 . 1 249 80 80 VAL H H 8.20 . 1 250 80 80 VAL N N 121.20 . 1 251 82 82 PHE H H 7.31 . 1 252 82 82 PHE HA H 5.69 . 1 253 82 82 PHE HB2 H 2.57 . . 254 82 82 PHE HB3 H 2.86 . . 255 82 82 PHE HD2 H 6.68 . 3 256 82 82 PHE HE2 H 7.06 . 3 257 82 82 PHE HZ H 7.19 . 1 258 82 82 PHE CA C 55.48 . 1 259 82 82 PHE CB C 43.61 . 1 260 82 82 PHE N N 113.44 . 1 261 83 83 ILE H H 7.88 . 1 262 83 83 ILE HA H 4.26 . 1 263 83 83 ILE HG2 H 0.72 . 1 264 83 83 ILE CA C 59.69 . 1 265 83 83 ILE CG2 C 17.82 . 1 266 83 83 ILE N N 115.23 . 1 267 84 84 PHE H H 8.36 . 1 268 84 84 PHE HA H 6.19 . 1 269 84 84 PHE HD2 H 7.33 . 3 270 84 84 PHE HE2 H 7.19 . 3 271 84 84 PHE HZ H 6.67 . 1 272 84 84 PHE CA C 55.47 . 1 273 84 84 PHE N N 122.68 . 1 274 85 85 ALA H H 8.57 . 1 275 85 85 ALA HA H 5.54 . 1 276 85 85 ALA CA C 50.94 . 1 277 85 85 ALA N N 123.76 . 1 278 86 86 THR H H 8.64 . 1 279 86 86 THR HA H 4.29 . 1 280 86 86 THR HB H 3.94 . 1 281 86 86 THR CA C 56.72 . 1 282 86 86 THR CB C 69.61 . 1 283 86 86 THR N N 114.26 . 1 284 87 87 GLY H H 8.59 . 1 285 87 87 GLY N N 112.83 . 1 286 88 88 TYR HD1 H 7.12 . 3 287 88 88 TYR HE1 H 6.82 . 3 288 89 89 GLY H H 8.30 . 1 289 89 89 GLY N N 111.75 . 1 290 90 90 SER H H 4.99 . 1 291 90 90 SER CA C 57.97 . 1 292 91 91 LYS H H 8.18 . 1 293 91 91 LYS N N 122.95 . 1 294 92 92 GLY H H 8.32 . 1 295 92 92 GLY N N 109.39 . 1 296 93 93 LEU H H 7.91 . 1 297 93 93 LEU HB2 H 1.55 . 2 298 93 93 LEU CB C 42.97 . 1 299 93 93 LEU N N 121.76 . 1 300 94 94 ASP H H 7.65 . 1 301 94 94 ASP N N 122.71 . 1 302 95 95 THR H H 8.21 . 1 303 95 95 THR N N 117.65 . 1 304 96 96 ARG H H 8.70 . 1 305 96 96 ARG N N 122.36 . 1 306 97 97 TYR H H 8.00 . 1 307 97 97 TYR HB2 H 3.86 . 2 308 97 97 TYR HD2 H 7.01 . 3 309 97 97 TYR HE2 H 6.56 . 3 310 97 97 TYR CB C 39.22 . 1 311 97 97 TYR N N 117.08 . 1 312 98 98 SER H H 7.58 . 1 313 98 98 SER N N 114.73 . 1 314 99 99 ASN H H 8.60 . 1 315 99 99 ASN N N 117.23 . 1 316 100 100 ILE H H 7.52 . 1 317 100 100 ILE HG2 H 0.77 . 4 318 100 100 ILE HD1 H 0.90 . 4 319 100 100 ILE CG2 C 19.07 . 4 320 100 100 ILE CD1 C 16.57 . 4 321 100 100 ILE N N 124.25 . 1 322 102 102 LEU H H 7.87 . 1 323 102 102 LEU N N 121.06 . 1 324 103 103 LEU H H 9.08 . 1 325 103 103 LEU HA H 4.62 . 1 326 103 103 LEU CA C 54.69 . 1 327 103 103 LEU N N 126.97 . 1 328 104 104 THR H H 8.43 . 1 329 104 104 THR HA H 4.76 . 1 330 104 104 THR CA C 63.44 . 1 331 104 104 THR N N 118.43 . 1 332 105 105 LYS H H 8.17 . 1 333 105 105 LYS HA H 4.29 . 1 334 105 105 LYS HD2 H 2.17 . 2 335 105 105 LYS CA C 54.69 . 1 336 105 105 LYS CD C 30.25 . 1 337 105 105 LYS N N 122.03 . 1 338 107 107 PHE H H 7.47 . 1 339 107 107 PHE N N 118.49 . 1 340 109 109 ASP H H 9.13 . 1 341 109 109 ASP HA H 4.71 . 1 342 109 109 ASP N N 124.81 . 1 343 110 110 SER HA H 4.27 . 1 344 110 110 SER CA C 59.69 . 1 345 111 111 GLU H H 7.41 . 1 346 111 111 GLU HA H 4.06 . 1 347 111 111 GLU CA C 58.44 . 1 348 111 111 GLU N N 123.78 . 1 349 112 112 LEU H H 7.67 . 1 350 112 112 LEU HA H 3.90 . 1 351 112 112 LEU HD1 H 0.94 . 4 352 112 112 LEU CA C 58.44 . 1 353 112 112 LEU CD1 C 15.32 . . 354 112 112 LEU N N 120.18 . 1 355 113 113 GLU H H 8.53 . 1 356 113 113 GLU HA H 3.73 . 1 357 113 113 GLU CA C 60.94 . 1 358 113 113 GLU N N 118.38 . 1 359 114 114 ALA H H 7.48 . 1 360 114 114 ALA HA H 4.14 . 1 361 114 114 ALA HB H 1.55 . 1 362 114 114 ALA CA C 55.54 . 1 363 114 114 ALA CB C 18.44 . 1 364 114 114 ALA N N 117.79 . 1 365 115 115 VAL H H 7.54 . 1 366 115 115 VAL HA H 4.03 . 1 367 115 115 VAL CA C 65.94 . 1 368 115 115 VAL N N 116.00 . 1 369 116 116 LEU HA H 4.28 . 1 370 116 116 LEU CA C 57.57 . 1 371 117 117 VAL H H 8.20 . 1 372 117 117 VAL N N 119.14 . 1 373 120 120 SER H H 7.78 . 1 374 120 120 SER N N 115.73 . 1 375 121 121 LYS H H 7.54 . 1 376 121 121 LYS N N 120.87 . 1 377 122 122 GLU H H 8.14 . 1 378 122 122 GLU N N 120.16 . 1 379 123 123 VAL H H 7.41 . 1 380 123 123 VAL N N 123.54 . 1 stop_ save_