data_5954 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequential Resonance Assignments of the Extracellular Domain of the Human TGFB type II Receptor in Complex woth Monomeric TGFB3 ; _BMRB_accession_number 5954 _BMRB_flat_file_name bmr5954.str _Entry_type original _Submission_date 2003-09-18 _Accession_date 2003-09-18 _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 Ilangovan Udayar . . 2 Deep Shashank . . 3 Hinck Cynthia . . 4 Hinck Andrew . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 119 "13C chemical shifts" 331 "15N chemical shifts" 93 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-03-18 update BMRB 'Updated Citation' 2003-12-05 original author 'Original Release' stop_ loop_ _Related_BMRB_accession_number _Relationship 5953 'TGFB type II Receptor in complex with Monomeric TGFB3' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Sequential Resonance Assignments of the Extracellular Domain of the Human TGFbeta type II Receptor in Complex with Monomeric TGFbeta3 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15017149 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ilangovan Udayar . . 2 Deep Shashank . . 3 Hinck Cynthia S. . 4 Hinck Andrew P. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 29 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 103 _Page_last 104 _Year 2004 _Details . loop_ _Keyword 'Transforming growth factor-beta' TGF 'type II receptor' 'Ligand-Receptor Complex' NMR Deutration TROSY stop_ save_ ################################## # Molecular system description # ################################## save_system_TGFB_type_II_Receptor _Saveframe_category molecular_system _Mol_system_name 'Human TGFB type II Receptor' _Abbreviation_common 'TGFB type II Receptor' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'tgfb type II receptor' $TGFB_type_II_Receptor stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TGFB_type_II_Receptor _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Transforming Growth Factor type II Receptor' _Abbreviation_common 'TGFB type II Receptor' _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 116 _Mol_residue_sequence ; AVKFPQLCKFCDVRFSTCDN QKSCMSNCSITSICEKPQEV CVAVWRKNDENITLETVCHD PKLPYHDFILEDAASPKCIM KEKKKPGETFFMCSCSSDEC NDNIIFSEEYNTSNPE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 21 ALA 2 22 VAL 3 23 LYS 4 24 PHE 5 25 PRO 6 26 GLN 7 27 LEU 8 28 CYS 9 29 LYS 10 30 PHE 11 31 CYS 12 32 ASP 13 33 VAL 14 34 ARG 15 35 PHE 16 36 SER 17 37 THR 18 38 CYS 19 39 ASP 20 40 ASN 21 41 GLN 22 42 LYS 23 43 SER 24 44 CYS 25 45 MET 26 46 SER 27 47 ASN 28 48 CYS 29 49 SER 30 50 ILE 31 51 THR 32 52 SER 33 53 ILE 34 54 CYS 35 55 GLU 36 56 LYS 37 57 PRO 38 58 GLN 39 59 GLU 40 60 VAL 41 61 CYS 42 62 VAL 43 63 ALA 44 64 VAL 45 65 TRP 46 66 ARG 47 67 LYS 48 68 ASN 49 69 ASP 50 70 GLU 51 71 ASN 52 72 ILE 53 73 THR 54 74 LEU 55 75 GLU 56 76 THR 57 77 VAL 58 78 CYS 59 79 HIS 60 80 ASP 61 81 PRO 62 82 LYS 63 83 LEU 64 84 PRO 65 85 TYR 66 86 HIS 67 87 ASP 68 88 PHE 69 89 ILE 70 90 LEU 71 91 GLU 72 92 ASP 73 93 ALA 74 94 ALA 75 95 SER 76 96 PRO 77 97 LYS 78 98 CYS 79 99 ILE 80 100 MET 81 101 LYS 82 102 GLU 83 103 LYS 84 104 LYS 85 105 LYS 86 106 PRO 87 107 GLY 88 108 GLU 89 109 THR 90 110 PHE 91 111 PHE 92 112 MET 93 113 CYS 94 114 SER 95 115 CYS 96 116 SER 97 117 SER 98 118 ASP 99 119 GLU 100 120 CYS 101 121 ASN 102 122 ASP 103 123 ASN 104 124 ILE 105 125 ILE 106 126 PHE 107 127 SER 108 128 GLU 109 129 GLU 110 130 TYR 111 131 ASN 112 132 THR 113 133 SER 114 134 ASN 115 135 PRO 116 136 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 4779 TbR2 100.00 122 99.14 100.00 4.01e-77 PDB 1KTZ "Crystal Structure Of The Human Tgf-Beta Type Ii Receptor Extracellular Domain In Complex With Tgf-Beta3" 100.00 122 99.14 100.00 4.88e-77 PDB 1M9Z "Crystal Structure Of Human Tgf-beta Type Ii Receptor Ligand Binding Domain" 94.83 111 98.18 99.09 1.58e-71 PDB 1PLO "Transforming Growth Factor-Beta Type Ii Receptor Extracellular Domain" 100.00 122 99.14 100.00 4.01e-77 PDB 2PJY "Structural Basis For Cooperative Assembly Of The Tgf-Beta Signaling Complex" 91.38 108 100.00 100.00 4.48e-70 PDB 3KFD "Ternary Complex Of Tgf-B1 Reveals Isoform-Specific Ligand Re And Receptor Recruitment In The Superfamily" 94.83 116 100.00 100.00 4.85e-73 DBJ BAA05673 "TGF-beta receptor type IIB [Homo sapiens]" 100.00 283 99.14 100.00 4.51e-77 DBJ BAA09332 "TGF-betaIIR alpha [Homo sapiens]" 100.00 567 99.14 100.00 7.46e-75 DBJ BAG10803 "TGF-beta receptor type-2 precursor [synthetic construct]" 100.00 567 99.14 100.00 6.86e-75 DBJ BAG36796 "unnamed protein product [Homo sapiens]" 100.00 567 99.14 100.00 6.86e-75 DBJ BAG62117 "unnamed protein product [Homo sapiens]" 100.00 592 99.14 100.00 1.32e-74 GB AAA61164 "TGF-beta type II receptor [Homo sapiens]" 100.00 567 99.14 100.00 6.86e-75 GB AAB17553 "transforming growth factor-beta type II receptor [Homo sapiens]" 100.00 567 99.14 100.00 6.86e-75 GB AAB40916 "transforming growth factor-beta type II receptor [Homo sapiens]" 100.00 567 99.14 100.00 6.86e-75 GB AAI52841 "Transforming growth factor, beta receptor II (70/80kDa), partial [synthetic construct]" 100.00 592 99.14 100.00 1.32e-74 GB AAQ02596 "transforming growth factor, beta receptor II [synthetic construct]" 100.00 568 99.14 100.00 6.23e-75 REF NP_001020018 "TGF-beta receptor type-2 isoform A precursor [Homo sapiens]" 100.00 592 99.14 100.00 1.32e-74 REF NP_001248080 "TGF-beta receptor type-2 precursor [Macaca mulatta]" 100.00 567 98.28 100.00 2.30e-74 REF NP_003233 "TGF-beta receptor type-2 isoform B precursor [Homo sapiens]" 100.00 567 99.14 100.00 6.86e-75 REF XP_001166647 "PREDICTED: TGF-beta receptor type-2 isoform X2 [Pan troglodytes]" 100.00 567 99.14 100.00 6.86e-75 REF XP_002814024 "PREDICTED: TGF-beta receptor type-2 isoform X1 [Pongo abelii]" 100.00 592 99.14 100.00 1.55e-74 SP P37173 "RecName: Full=TGF-beta receptor type-2; Short=TGFR-2; AltName: Full=TGF-beta type II receptor; AltName: Full=Transforming growt" 100.00 567 99.14 100.00 6.86e-75 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TGFB_type_II_Receptor Human 9606 Eukaryota Metazoa Homo sapiens 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 $TGFB_type_II_Receptor 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_free_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $TGFB_type_II_Receptor . mM 0.1 0.1 . stop_ save_ ############################ # Computer software used # ############################ save_NMRPIPeE _Saveframe_category software _Name NMRPIPeE _Version . loop_ _Task processing stop_ _Details . save_ save_NMRVIEW _Saveframe_category software _Name NMRVIEW _Version 4.1.3 loop_ _Task analyzing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 700 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HN(CO)CACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _Sample_label . save_ save_C(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _Sample_label . save_ save_HC(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name HC(CO)NH _Sample_label . save_ save_HNCO_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CA)CO_8 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_CT-13C-HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name CT-13C-HSQC _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details 'All the experiments are TROSY versions.' save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details 'All the experiments are TROSY versions.' save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details 'All the experiments are TROSY versions.' save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details 'All the experiments are TROSY versions.' save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _BMRB_pulse_sequence_accession_number . _Details 'All the experiments are TROSY versions.' save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HC(CO)NH _BMRB_pulse_sequence_accession_number . _Details 'All the experiments are TROSY versions.' save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details 'All the experiments are TROSY versions.' save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details 'All the experiments are TROSY versions.' save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name CT-13C-HSQC _BMRB_pulse_sequence_accession_number . _Details 'All the experiments are TROSY versions.' save_ ####################### # Sample conditions # ####################### save_Expt_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.6 0.05 pH temperature 312 0.3 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 DSS H 1 'methyl protons' ppm 0.0 . direct . . . 1.0 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_chemical_shift_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $free_sample_1 stop_ _Sample_conditions_label $Expt_condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'tgfb type II receptor' _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 . 2 VAL C C 175.04 . 1 2 . 2 VAL CG1 C 20.98 . 2 3 . 2 VAL HG1 H 0.74 . 2 4 . 2 VAL CG2 C 20.54 . 2 5 . 2 VAL HG2 H 0.85 . 2 6 . 3 LYS H H 8.00 . 1 7 . 3 LYS N N 125.19 . 1 8 . 3 LYS CA C 55.09 . 1 9 . 3 LYS C C 175.12 . 1 10 . 3 LYS CB C 32.67 . 1 11 . 4 PHE H H 8.35 . 1 12 . 4 PHE N N 124.79 . 1 13 . 4 PHE CA C 55.36 . 1 14 . 4 PHE C C 173.62 . 1 15 . 4 PHE CB C 38.21 . 1 16 . 5 PRO CA C 62.25 . 1 17 . 5 PRO C C 175.26 . 1 18 . 5 PRO CB C 31.47 . 1 19 . 6 GLN H H 8.77 . 1 20 . 6 GLN N N 121.54 . 1 21 . 6 GLN CA C 54.54 . 1 22 . 6 GLN C C 173.69 . 1 23 . 6 GLN CB C 31.45 . 1 24 . 7 LEU H H 7.96 . 1 25 . 7 LEU N N 119.62 . 1 26 . 7 LEU CA C 53.65 . 1 27 . 7 LEU C C 178.65 . 1 28 . 7 LEU CB C 43.11 . 1 29 . 7 LEU CD1 C 25.20 . 2 30 . 7 LEU HD1 H 0.80 . 2 31 . 7 LEU CD2 C 24.69 . 2 32 . 7 LEU HD2 H 0.71 . 2 33 . 8 CYS H H 8.98 . 1 34 . 8 CYS N N 118.67 . 1 35 . 8 CYS CA C 52.29 . 1 36 . 8 CYS C C 175.71 . 1 37 . 8 CYS CB C 42.49 . 1 38 . 9 LYS H H 9.09 . 1 39 . 9 LYS N N 119.80 . 1 40 . 9 LYS CA C 54.52 . 1 41 . 9 LYS C C 177.61 . 1 42 . 9 LYS CB C 28.71 . 1 43 . 10 PHE H H 8.33 . 1 44 . 10 PHE N N 126.55 . 1 45 . 10 PHE CA C 53.89 . 1 46 . 10 PHE C C 174.68 . 1 47 . 10 PHE CB C 38.68 . 1 48 . 11 CYS H H 8.57 . 1 49 . 11 CYS N N 119.34 . 1 50 . 11 CYS CA C 60.63 . 1 51 . 11 CYS C C 175.04 . 1 52 . 11 CYS CB C 39.66 . 1 53 . 12 ASP H H 9.32 . 1 54 . 12 ASP N N 118.46 . 1 55 . 12 ASP CA C 57.10 . 1 56 . 12 ASP C C 175.19 . 1 57 . 12 ASP CB C 39.95 . 1 58 . 13 VAL H H 8.17 . 1 59 . 13 VAL N N 121.79 . 1 60 . 13 VAL CA C 63.88 . 1 61 . 13 VAL C C 176.07 . 1 62 . 13 VAL CB C 31.16 . 1 63 . 13 VAL CG1 C 21.25 . 2 64 . 13 VAL HG1 H 0.96 . 2 65 . 13 VAL CG2 C 21.10 . 2 66 . 13 VAL HG2 H 0.77 . 2 67 . 14 ARG H H 8.56 . 1 68 . 14 ARG N N 126.80 . 1 69 . 14 ARG CA C 52.17 . 1 70 . 14 ARG C C 176.00 . 1 71 . 14 ARG CB C 33.46 . 1 72 . 15 PHE H H 8.45 . 1 73 . 15 PHE N N 119.89 . 1 74 . 15 PHE CA C 58.69 . 1 75 . 15 PHE C C 176.22 . 1 76 . 15 PHE CB C 38.26 . 1 77 . 16 SER H H 8.10 . 1 78 . 16 SER N N 116.95 . 1 79 . 16 SER CA C 55.90 . 1 80 . 16 SER C C 173.37 . 1 81 . 16 SER CB C 65.90 . 1 82 . 17 THR H H 8.16 . 1 83 . 17 THR N N 113.14 . 1 84 . 17 THR CA C 60.45 . 1 85 . 17 THR C C 175.05 . 1 86 . 17 THR CB C 68.49 . 1 87 . 18 CYS H H 8.48 . 1 88 . 18 CYS N N 122.80 . 1 89 . 18 CYS CA C 56.41 . 1 90 . 18 CYS C C 173.28 . 1 91 . 18 CYS CB C 40.59 . 1 92 . 19 ASP H H 8.02 . 1 93 . 19 ASP N N 125.94 . 1 94 . 19 ASP CA C 53.10 . 1 95 . 19 ASP C C 175.12 . 1 96 . 19 ASP CB C 41.88 . 1 97 . 20 ASN H H 7.84 . 1 98 . 20 ASN N N 118.16 . 1 99 . 20 ASN CA C 52.41 . 1 100 . 20 ASN C C 173.80 . 1 101 . 20 ASN CB C 36.22 . 1 102 . 21 GLN H H 7.33 . 1 103 . 21 GLN N N 114.73 . 1 104 . 21 GLN CA C 54.41 . 1 105 . 21 GLN C C 175.34 . 1 106 . 21 GLN CB C 30.92 . 1 107 . 22 LYS H H 8.37 . 1 108 . 22 LYS N N 118.35 . 1 109 . 22 LYS CA C 57.59 . 1 110 . 22 LYS C C 175.71 . 1 111 . 22 LYS CB C 31.00 . 1 112 . 23 SER H H 7.69 . 1 113 . 23 SER N N 112.58 . 1 114 . 23 SER CA C 57.08 . 1 115 . 23 SER C C 172.84 . 1 116 . 23 SER CB C 64.65 . 1 117 . 24 CYS H H 9.16 . 1 118 . 24 CYS N N 119.03 . 1 119 . 24 CYS CA C 53.44 . 1 120 . 24 CYS C C 172.70 . 1 121 . 24 CYS CB C 46.28 . 1 122 . 25 MET H H 8.36 . 1 123 . 25 MET N N 121.02 . 1 124 . 25 MET CA C 52.85 . 1 125 . 25 MET C C 178.79 . 1 126 . 25 MET CB C 46.46 . 1 127 . 26 SER H H 9.14 . 1 128 . 26 SER N N 116.50 . 1 129 . 26 SER CA C 61.55 . 1 130 . 26 SER C C 176.37 . 1 131 . 26 SER CB C 63.38 . 1 132 . 27 ASN H H 8.90 . 1 133 . 27 ASN N N 118.27 . 1 134 . 27 ASN CA C 54.18 . 1 135 . 27 ASN C C 174.17 . 1 136 . 27 ASN CB C 36.95 . 1 137 . 28 CYS H H 8.09 . 1 138 . 28 CYS N N 116.37 . 1 139 . 28 CYS CA C 53.69 . 1 140 . 28 CYS C C 176.19 . 1 141 . 28 CYS CB C 37.49 . 1 142 . 29 SER H H 8.76 . 1 143 . 29 SER N N 125.33 . 1 144 . 29 SER CA C 58.62 . 1 145 . 29 SER C C 173.13 . 1 146 . 29 SER CB C 63.06 . 1 147 . 30 ILE H H 7.44 . 1 148 . 30 ILE N N 123.26 . 1 149 . 30 ILE CA C 61.09 . 1 150 . 30 ILE C C 174.68 . 1 151 . 30 ILE CB C 37.70 . 1 152 . 30 ILE CD1 C 12.65 . 1 153 . 30 ILE HD1 H 0.86 . 1 154 . 31 THR H H 8.39 . 1 155 . 31 THR N N 125.56 . 1 156 . 31 THR CA C 61.66 . 1 157 . 31 THR C C 174.10 . 1 158 . 31 THR CB C 69.05 . 1 159 . 32 SER H H 9.02 . 1 160 . 32 SER N N 122.34 . 1 161 . 32 SER CA C 56.27 . 1 162 . 32 SER C C 173.21 . 1 163 . 32 SER CB C 66.25 . 1 164 . 33 ILE H H 8.19 . 1 165 . 33 ILE N N 124.12 . 1 166 . 33 ILE CA C 60.42 . 1 167 . 33 ILE C C 177.10 . 1 168 . 33 ILE CB C 37.94 . 1 169 . 33 ILE CD1 C 13.92 . 1 170 . 33 ILE HD1 H 0.82 . 1 171 . 34 CYS H H 8.77 . 1 172 . 34 CYS N N 127.35 . 1 173 . 34 CYS CA C 53.29 . 1 174 . 34 CYS C C 174.97 . 1 175 . 34 CYS CB C 36.31 . 1 176 . 35 GLU H H 8.81 . 1 177 . 35 GLU N N 120.34 . 1 178 . 35 GLU CA C 58.85 . 1 179 . 35 GLU C C 177.25 . 1 180 . 35 GLU CB C 29.99 . 1 181 . 36 LYS H H 7.84 . 1 182 . 36 LYS N N 114.79 . 1 183 . 36 LYS CA C 52.09 . 1 184 . 36 LYS C C 176.32 . 1 185 . 36 LYS CB C 32.44 . 1 186 . 37 PRO CA C 64.77 . 1 187 . 37 PRO C C 175.71 . 1 188 . 37 PRO CB C 31.16 . 1 189 . 38 GLN H H 8.50 . 1 190 . 38 GLN N N 112.85 . 1 191 . 38 GLN CA C 56.15 . 1 192 . 38 GLN C C 176.44 . 1 193 . 38 GLN CB C 26.95 . 1 194 . 39 GLU H H 7.06 . 1 195 . 39 GLU N N 116.62 . 1 196 . 39 GLU CA C 57.45 . 1 197 . 39 GLU C C 176.15 . 1 198 . 39 GLU CB C 29.80 . 1 199 . 40 VAL H H 8.58 . 1 200 . 40 VAL N N 113.35 . 1 201 . 40 VAL CA C 58.27 . 1 202 . 40 VAL C C 174.67 . 1 203 . 40 VAL CB C 32.21 . 1 204 . 40 VAL CG1 C 17.71 . 2 205 . 40 VAL HG1 H 0.87 . 2 206 . 40 VAL CG2 C 21.48 . 2 207 . 40 VAL HG2 H 0.97 . 2 208 . 41 CYS H H 8.05 . 1 209 . 41 CYS N N 114.42 . 1 210 . 41 CYS CA C 52.58 . 1 211 . 41 CYS C C 174.97 . 1 212 . 41 CYS CB C 35.18 . 1 213 . 42 VAL H H 8.52 . 1 214 . 42 VAL N N 118.67 . 1 215 . 42 VAL CA C 60.20 . 1 216 . 42 VAL CB C 35.58 . 1 217 . 42 VAL CG1 C 21.67 . 2 218 . 42 VAL HG1 H 0.62 . 2 219 . 42 VAL CG2 C 23.90 . 2 220 . 42 VAL HG2 H 0.64 . 2 221 . 43 ALA CA C 50.59 . 1 222 . 43 ALA C C 175.87 . 1 223 . 43 ALA CB C 21.98 . 1 224 . 44 VAL H H 8.90 . 1 225 . 44 VAL N N 119.85 . 1 226 . 44 VAL CA C 60.58 . 1 227 . 44 VAL C C 175.24 . 1 228 . 44 VAL CG1 C 22.24 . 2 229 . 44 VAL HG1 H 0.60 . 2 230 . 44 VAL CG2 C 20.58 . 2 231 . 44 VAL HG2 H 0.85 . 2 232 . 45 TRP H H 9.75 . 1 233 . 45 TRP N N 133.96 . 1 234 . 45 TRP CA C 56.47 . 1 235 . 45 TRP C C 174.17 . 1 236 . 45 TRP CB C 33.25 . 1 237 . 46 ARG H H 8.28 . 1 238 . 46 ARG N N 125.14 . 1 239 . 46 ARG CA C 54.19 . 1 240 . 46 ARG C C 173.22 . 1 241 . 46 ARG CB C 34.00 . 1 242 . 47 LYS H H 8.41 . 1 243 . 47 LYS N N 121.95 . 1 244 . 47 LYS CA C 54.52 . 1 245 . 47 LYS C C 175.26 . 1 246 . 47 LYS CB C 35.03 . 1 247 . 48 ASN H H 8.32 . 1 248 . 48 ASN N N 125.52 . 1 249 . 48 ASN CA C 51.72 . 1 250 . 48 ASN C C 174.39 . 1 251 . 48 ASN CB C 39.37 . 1 252 . 49 ASP H H 8.70 . 1 253 . 49 ASP N N 120.89 . 1 254 . 49 ASP CA C 56.39 . 1 255 . 49 ASP C C 175.78 . 1 256 . 49 ASP CB C 39.27 . 1 257 . 50 GLU H H 8.39 . 1 258 . 50 GLU N N 117.19 . 1 259 . 50 GLU CA C 56.83 . 1 260 . 50 GLU C C 176.00 . 1 261 . 50 GLU CB C 29.95 . 1 262 . 51 ASN H H 8.17 . 1 263 . 51 ASN N N 117.19 . 1 264 . 51 ASN CA C 52.80 . 1 265 . 51 ASN C C 172.70 . 1 266 . 51 ASN CB C 40.61 . 1 267 . 52 ILE H H 8.18 . 1 268 . 52 ILE N N 123.93 . 1 269 . 52 ILE CA C 60.34 . 1 270 . 52 ILE C C 176.52 . 1 271 . 52 ILE CB C 38.51 . 1 272 . 52 ILE CD1 C 13.85 . 1 273 . 52 ILE HD1 H 0.85 . 1 274 . 53 THR H H 8.66 . 1 275 . 53 THR N N 115.72 . 1 276 . 53 THR CA C 58.22 . 1 277 . 53 THR C C 172.18 . 1 278 . 53 THR CB C 72.38 . 1 279 . 54 LEU H H 9.04 . 1 280 . 54 LEU N N 120.44 . 1 281 . 54 LEU CA C 52.84 . 1 282 . 54 LEU C C 174.84 . 1 283 . 54 LEU CB C 45.70 . 1 284 . 54 LEU CD1 C 24.27 . 2 285 . 54 LEU HD1 H 1.03 . 2 286 . 54 LEU CD2 C 26.88 . 2 287 . 54 LEU HD2 H 0.97 . 2 288 . 55 GLU H H 9.60 . 1 289 . 55 GLU N N 130.91 . 1 290 . 55 GLU CA C 52.64 . 1 291 . 55 GLU C C 176.07 . 1 292 . 55 GLU CB C 31.95 . 1 293 . 56 THR H H 7.96 . 1 294 . 56 THR N N 115.57 . 1 295 . 56 THR CA C 57.79 . 1 296 . 56 THR C C 174.09 . 1 297 . 56 THR CB C 70.36 . 1 298 . 57 VAL H H 7.42 . 1 299 . 57 VAL N N 112.58 . 1 300 . 57 VAL CA C 58.88 . 1 301 . 57 VAL CB C 37.13 . 1 302 . 57 VAL CG1 C 18.12 . 2 303 . 57 VAL HG1 H 0.18 . 2 304 . 57 VAL CG2 C 22.88 . 2 305 . 57 VAL HG2 H 0.97 . 2 306 . 58 CYS CA C 57.07 . 1 307 . 58 CYS C C 175.11 . 1 308 . 58 CYS CB C 46.90 . 1 309 . 59 HIS H H 9.24 . 1 310 . 59 HIS N N 118.46 . 1 311 . 59 HIS CA C 56.39 . 1 312 . 59 HIS C C 173.21 . 1 313 . 59 HIS CB C 34.13 . 1 314 . 60 ASP H H 7.55 . 1 315 . 60 ASP N N 128.37 . 1 316 . 60 ASP CA C 50.71 . 1 317 . 60 ASP CB C 40.75 . 1 318 . 61 PRO CA C 63.81 . 1 319 . 61 PRO C C 177.53 . 1 320 . 61 PRO CB C 31.04 . 1 321 . 62 LYS H H 8.39 . 1 322 . 62 LYS N N 122.01 . 1 323 . 62 LYS CA C 57.36 . 1 324 . 62 LYS C C 176.59 . 1 325 . 62 LYS CB C 31.07 . 1 326 . 63 LEU H H 8.11 . 1 327 . 63 LEU N N 120.23 . 1 328 . 63 LEU CA C 51.25 . 1 329 . 63 LEU C C 176.18 . 1 330 . 63 LEU CB C 41.39 . 1 331 . 63 LEU CD1 C 22.83 . 2 332 . 63 LEU HD1 H 0.88 . 2 333 . 63 LEU CD2 C 25.18 . 2 334 . 63 LEU HD2 H 0.94 . 2 335 . 64 PRO CA C 62.61 . 1 336 . 64 PRO C C 175.41 . 1 337 . 64 PRO CB C 31.34 . 1 338 . 65 TYR H H 9.33 . 1 339 . 65 TYR N N 123.28 . 1 340 . 65 TYR CA C 58.27 . 1 341 . 65 TYR C C 175.41 . 1 342 . 65 TYR CB C 40.46 . 1 343 . 66 HIS H H 8.33 . 1 344 . 66 HIS N N 123.13 . 1 345 . 66 HIS CA C 57.35 . 1 346 . 66 HIS C C 173.94 . 1 347 . 66 HIS CB C 27.34 . 1 348 . 67 ASP H H 8.09 . 1 349 . 67 ASP N N 105.33 . 1 350 . 67 ASP CA C 56.12 . 1 351 . 67 ASP C C 174.83 . 1 352 . 67 ASP CB C 39.22 . 1 353 . 68 PHE H H 7.85 . 1 354 . 68 PHE N N 118.62 . 1 355 . 68 PHE CA C 56.96 . 1 356 . 68 PHE C C 174.82 . 1 357 . 68 PHE CB C 41.13 . 1 358 . 69 ILE H H 8.41 . 1 359 . 69 ILE N N 120.72 . 1 360 . 69 ILE CA C 58.87 . 1 361 . 69 ILE C C 177.60 . 1 362 . 69 ILE CB C 36.86 . 1 363 . 69 ILE CD1 C 10.88 . 1 364 . 69 ILE HD1 H 0.75 . 1 365 . 70 LEU H H 9.51 . 1 366 . 70 LEU N N 129.55 . 1 367 . 70 LEU CA C 53.96 . 1 368 . 70 LEU C C 176.99 . 1 369 . 70 LEU CB C 38.43 . 1 370 . 70 LEU CD1 C 23.38 . 2 371 . 70 LEU HD1 H 0.95 . 2 372 . 70 LEU CD2 C 26.11 . 2 373 . 70 LEU HD2 H 0.94 . 2 374 . 71 GLU H H 8.39 . 1 375 . 71 GLU N N 123.30 . 1 376 . 71 GLU CA C 56.82 . 1 377 . 71 GLU C C 176.51 . 1 378 . 71 GLU CB C 29.70 . 1 379 . 72 ASP H H 9.23 . 1 380 . 72 ASP N N 117.93 . 1 381 . 72 ASP CA C 52.65 . 1 382 . 72 ASP C C 175.27 . 1 383 . 72 ASP CB C 39.35 . 1 384 . 73 ALA H H 7.00 . 1 385 . 73 ALA N N 119.80 . 1 386 . 73 ALA CA C 54.70 . 1 387 . 73 ALA C C 177.54 . 1 388 . 73 ALA CB C 18.75 . 1 389 . 74 ALA H H 8.05 . 1 390 . 74 ALA N N 116.40 . 1 391 . 74 ALA CA C 52.11 . 1 392 . 74 ALA C C 178.42 . 1 393 . 74 ALA CB C 17.84 . 1 394 . 75 SER H H 8.35 . 1 395 . 75 SER N N 116.56 . 1 396 . 75 SER CA C 56.23 . 1 397 . 75 SER C C 174.53 . 1 398 . 75 SER CB C 64.70 . 1 399 . 76 PRO CA C 64.22 . 1 400 . 76 PRO C C 176.81 . 1 401 . 76 PRO CB C 31.13 . 1 402 . 77 LYS H H 7.34 . 1 403 . 77 LYS N N 114.57 . 1 404 . 77 LYS CA C 53.60 . 1 405 . 77 LYS C C 174.18 . 1 406 . 77 LYS CB C 35.02 . 1 407 . 81 LYS CA C 53.99 . 1 408 . 81 LYS C C 175.49 . 1 409 . 81 LYS CB C 34.01 . 1 410 . 82 GLU H H 8.54 . 1 411 . 82 GLU N N 124.86 . 1 412 . 82 GLU CA C 56.41 . 1 413 . 82 GLU C C 175.99 . 1 414 . 82 GLU CB C 29.27 . 1 415 . 83 LYS H H 8.57 . 1 416 . 83 LYS N N 126.01 . 1 417 . 83 LYS CA C 51.93 . 1 418 . 83 LYS C C 174.90 . 1 419 . 83 LYS CB C 31.46 . 1 420 . 84 LYS H H 8.07 . 1 421 . 84 LYS N N 120.86 . 1 422 . 84 LYS CA C 55.52 . 1 423 . 84 LYS C C 175.42 . 1 424 . 84 LYS CB C 32.35 . 1 425 . 85 LYS H H 8.85 . 1 426 . 85 LYS N N 126.14 . 1 427 . 85 LYS CA C 52.91 . 1 428 . 85 LYS C C 173.44 . 1 429 . 85 LYS CB C 33.71 . 1 430 . 86 PRO CA C 63.98 . 1 431 . 86 PRO C C 176.15 . 1 432 . 86 PRO CB C 31.30 . 1 433 . 87 GLY H H 8.64 . 1 434 . 87 GLY N N 111.29 . 1 435 . 87 GLY CA C 45.36 . 1 436 . 87 GLY C C 173.80 . 1 437 . 88 GLU H H 7.93 . 1 438 . 88 GLU N N 117.98 . 1 439 . 88 GLU CA C 55.42 . 1 440 . 88 GLU C C 174.31 . 1 441 . 88 GLU CB C 32.58 . 1 442 . 89 THR H H 8.55 . 1 443 . 89 THR N N 118.20 . 1 444 . 89 THR CA C 62.07 . 1 445 . 89 THR C C 173.21 . 1 446 . 89 THR CB C 69.75 . 1 447 . 90 PHE H H 9.16 . 1 448 . 90 PHE N N 127.62 . 1 449 . 90 PHE CA C 56.49 . 1 450 . 90 PHE C C 172.56 . 1 451 . 90 PHE CB C 41.56 . 1 452 . 91 PHE H H 9.61 . 1 453 . 91 PHE N N 124.12 . 1 454 . 91 PHE CA C 55.98 . 1 455 . 91 PHE CB C 43.25 . 1 456 . 94 SER CA C 57.16 . 1 457 . 94 SER C C 171.60 . 1 458 . 95 CYS H H 8.71 . 1 459 . 95 CYS N N 110.21 . 1 460 . 95 CYS CA C 54.40 . 1 461 . 95 CYS C C 174.83 . 1 462 . 95 CYS CB C 45.85 . 1 463 . 96 SER H H 8.68 . 1 464 . 96 SER N N 113.10 . 1 465 . 96 SER CA C 56.67 . 1 466 . 96 SER C C 174.38 . 1 467 . 96 SER CB C 63.27 . 1 468 . 97 SER H H 7.42 . 1 469 . 97 SER N N 114.74 . 1 470 . 97 SER CA C 57.55 . 1 471 . 97 SER C C 174.37 . 1 472 . 97 SER CB C 66.10 . 1 473 . 98 ASP H H 8.71 . 1 474 . 98 ASP N N 123.38 . 1 475 . 98 ASP CA C 56.34 . 1 476 . 98 ASP C C 177.69 . 1 477 . 98 ASP CB C 40.22 . 1 478 . 99 GLU H H 9.63 . 1 479 . 99 GLU N N 113.98 . 1 480 . 99 GLU CA C 58.08 . 1 481 . 99 GLU C C 177.32 . 1 482 . 99 GLU CB C 27.54 . 1 483 . 100 CYS H H 8.10 . 1 484 . 100 CYS N N 116.46 . 1 485 . 100 CYS CA C 58.69 . 1 486 . 100 CYS C C 174.23 . 1 487 . 100 CYS CB C 46.37 . 1 488 . 101 ASN H H 8.00 . 1 489 . 101 ASN N N 116.40 . 1 490 . 101 ASN CA C 52.11 . 1 491 . 101 ASN C C 170.94 . 1 492 . 101 ASN CB C 35.56 . 1 493 . 102 ASP H H 7.40 . 1 494 . 102 ASP N N 111.23 . 1 495 . 102 ASP CA C 54.61 . 1 496 . 102 ASP C C 175.04 . 1 497 . 102 ASP CB C 43.19 . 1 498 . 103 ASN H H 7.11 . 1 499 . 103 ASN N N 114.81 . 1 500 . 103 ASN CA C 51.54 . 1 501 . 103 ASN CB C 38.93 . 1 502 . 104 ILE CD1 C 14.01 . 1 503 . 104 ILE HD1 H 0.57 . 1 504 . 105 ILE CA C 60.60 . 1 505 . 105 ILE C C 175.05 . 1 506 . 105 ILE CB C 38.84 . 1 507 . 105 ILE CD1 C 13.38 . 1 508 . 105 ILE HD1 H 0.68 . 1 509 . 106 PHE H H 8.57 . 1 510 . 106 PHE N N 124.28 . 1 511 . 106 PHE CA C 58.41 . 1 512 . 106 PHE C C 176.15 . 1 513 . 106 PHE CB C 38.94 . 1 514 . 107 SER H H 8.11 . 1 515 . 107 SER N N 114.14 . 1 516 . 107 SER CA C 57.43 . 1 517 . 107 SER C C 173.73 . 1 518 . 107 SER CB C 64.22 . 1 519 . 108 GLU H H 8.59 . 1 520 . 108 GLU N N 123.75 . 1 521 . 108 GLU CA C 56.45 . 1 522 . 108 GLU C C 176.22 . 1 523 . 108 GLU CB C 29.90 . 1 524 . 109 GLU H H 8.29 . 1 525 . 109 GLU N N 121.10 . 1 526 . 109 GLU CA C 56.32 . 1 527 . 109 GLU C C 176.07 . 1 528 . 109 GLU CB C 29.72 . 1 529 . 110 TYR H H 8.01 . 1 530 . 110 TYR N N 120.42 . 1 531 . 110 TYR CA C 57.45 . 1 532 . 110 TYR C C 175.84 . 1 533 . 110 TYR CB C 37.99 . 1 534 . 111 ASN H H 8.15 . 1 535 . 111 ASN N N 120.32 . 1 536 . 111 ASN CA C 51.28 . 1 537 . 115 PRO CA C 63.34 . 1 538 . 115 PRO C C 176.77 . 1 539 . 115 PRO CB C 31.08 . 1 540 . 116 GLU H H 8.15 . 1 541 . 116 GLU N N 118.81 . 1 542 . 116 GLU CA C 54.08 . 1 543 . 116 GLU CB C 40.42 . 1 stop_ save_