data_19480 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase ; _BMRB_accession_number 19480 _BMRB_flat_file_name bmr19480.str _Entry_type original _Submission_date 2013-09-06 _Accession_date 2013-09-06 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'TROSY-based triple-resonance experiments, including 3D HNCACB, HN(CO)CACB, HNCA and HN(CO)CA' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 zhang shengnan . . 2 Huang Tao . . 3 Hinck Andrew . . 4 Fitzpatrick Paul . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 123 "13C chemical shifts" 217 "15N chemical shifts" 123 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-04-28 update BMRB 'update entry citation' 2014-02-12 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 19481 'Ser40 phosphorylated RDTH' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24361276 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhang Shengnan . . 2 Huang Tao . . 3 Ilangovan Udayar . . 4 Hinck Andrew P. . 5 Fitzpatrick Paul F. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 426 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1483 _Page_last 1497 _Year 2013 _Details . loop_ _Keyword 'ACT domain' 'NMR spectroscopy' regulation 'Tyrosine hydroxylase' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'RDTH dimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'RDTH, chain 1' $regulatory_domain_of_tyrosine_hydroxylase 'RDTH, chain 2' $regulatory_domain_of_tyrosine_hydroxylase stop_ _System_molecular_weight 17174.3 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details homodimer save_ ######################## # Monomeric polymers # ######################## save_regulatory_domain_of_tyrosine_hydroxylase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common regulatory_domain_of_tyrosine_hydroxylase _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 159 _Mol_residue_sequence ; MPTPSAPSPQPKGFRRAVSE QDAKQAEAVTSPRFIGRRQS LIEDARKEREAAAAAAAAAV ASSEPGNPLEAVVFEERDGN AVLNLLFSLRGTKPSSLSRA VKVFETFEAKIHHLETRPAQ RPLAGSPHLEYFVRFEVPSG DLAALLSSVRRVSDDVRSA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 PRO 3 THR 4 PRO 5 SER 6 ALA 7 PRO 8 SER 9 PRO 10 GLN 11 PRO 12 LYS 13 GLY 14 PHE 15 ARG 16 ARG 17 ALA 18 VAL 19 SER 20 GLU 21 GLN 22 ASP 23 ALA 24 LYS 25 GLN 26 ALA 27 GLU 28 ALA 29 VAL 30 THR 31 SER 32 PRO 33 ARG 34 PHE 35 ILE 36 GLY 37 ARG 38 ARG 39 GLN 40 SER 41 LEU 42 ILE 43 GLU 44 ASP 45 ALA 46 ARG 47 LYS 48 GLU 49 ARG 50 GLU 51 ALA 52 ALA 53 ALA 54 ALA 55 ALA 56 ALA 57 ALA 58 ALA 59 ALA 60 VAL 61 ALA 62 SER 63 SER 64 GLU 65 PRO 66 GLY 67 ASN 68 PRO 69 LEU 70 GLU 71 ALA 72 VAL 73 VAL 74 PHE 75 GLU 76 GLU 77 ARG 78 ASP 79 GLY 80 ASN 81 ALA 82 VAL 83 LEU 84 ASN 85 LEU 86 LEU 87 PHE 88 SER 89 LEU 90 ARG 91 GLY 92 THR 93 LYS 94 PRO 95 SER 96 SER 97 LEU 98 SER 99 ARG 100 ALA 101 VAL 102 LYS 103 VAL 104 PHE 105 GLU 106 THR 107 PHE 108 GLU 109 ALA 110 LYS 111 ILE 112 HIS 113 HIS 114 LEU 115 GLU 116 THR 117 ARG 118 PRO 119 ALA 120 GLN 121 ARG 122 PRO 123 LEU 124 ALA 125 GLY 126 SER 127 PRO 128 HIS 129 LEU 130 GLU 131 TYR 132 PHE 133 VAL 134 ARG 135 PHE 136 GLU 137 VAL 138 PRO 139 SER 140 GLY 141 ASP 142 LEU 143 ALA 144 ALA 145 LEU 146 LEU 147 SER 148 SER 149 VAL 150 ARG 151 ARG 152 VAL 153 SER 154 ASP 155 ASP 156 VAL 157 ARG 158 SER 159 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 19481 Ser40_phosphorylated_regulatory_domain_of_tyrosine_hydroxylase 100.00 159 100.00 100.00 9.88e-106 BMRB 19482 RDTyrH65-159 58.49 93 100.00 100.00 1.46e-57 PDB 2MDA "The Solution Structure Of The Regulatory Domain Of Tyrosine Hydroxylase" 59.75 95 100.00 100.00 2.65e-59 GB AAA40434 "tyrosine hydroxylase [Mus musculus]" 100.00 498 97.48 98.74 4.92e-99 GB AAA42257 "tyrosine hydroxylase (EC 1.14.16.2) [Rattus norvegicus]" 100.00 498 100.00 100.00 1.61e-101 GB AAA42258 "tyrosine hydroxylase [Rattus norvegicus]" 100.00 498 100.00 100.00 1.61e-101 GB AAB59722 "tyrosine hydroxylase [Rattus norvegicus]" 66.04 105 100.00 100.00 9.25e-64 GB AAI56669 "Tyrosine hydroxylase [synthetic construct]" 100.00 498 97.48 98.74 4.92e-99 REF NP_033403 "tyrosine 3-monooxygenase [Mus musculus]" 100.00 498 97.48 98.74 4.92e-99 REF NP_036872 "tyrosine 3-monooxygenase [Rattus norvegicus]" 100.00 498 100.00 100.00 1.61e-101 SP P04177 "RecName: Full=Tyrosine 3-monooxygenase; AltName: Full=Tyrosine 3-hydroxylase; Short=TH" 100.00 498 100.00 100.00 1.61e-101 SP P24529 "RecName: Full=Tyrosine 3-monooxygenase; AltName: Full=Tyrosine 3-hydroxylase; Short=TH" 100.00 498 97.48 98.74 4.92e-99 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $regulatory_domain_of_tyrosine_hydroxylase Rat 10116 Eukaryota Metazoa Rattus norvegicus 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 $regulatory_domain_of_tyrosine_hydroxylase 'recombinant technology' . Escherichia coli . pETNTERM stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1 M leupeptin and 1 M pepstatin A were added as protease inhibitor' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $regulatory_domain_of_tyrosine_hydroxylase . mM 0.8 1.2 '[U-95% 13C; U-95% 15N]' D2O 5 % . . 'natural abundance' H2O 95 % . . 'natural abundance' 'sodium phosphate' 50 mM . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignments' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HCACO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.11 . M pH 7 . pH pressure 1 . atm temperature 300 . 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 DSS P 31 'methyl protons' ppm 0.00 na indirect . . . 0.404808636 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' '3D CBCA(CO)NH' '3D HNCA' '3D HNCACB' '3D HCACO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'RDTH, chain 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 2 2 PRO CA C 61.651 0.30 1 2 2 2 PRO CB C 32.595 0.30 1 3 3 3 THR N N 116.761 0.30 1 4 3 3 THR H H 8.071 0.02 1 5 3 3 THR CA C 62.361 0.30 1 6 3 3 THR CB C 69.786 0.30 1 7 4 4 PRO CA C 62.424 0.30 1 8 4 4 PRO CB C 32.975 0.30 1 9 5 5 SER N N 119.117 0.30 1 10 5 5 SER H H 8.387 0.02 1 11 5 5 SER CA C 58.340 0.30 1 12 5 5 SER CB C 63.833 0.30 1 13 6 6 ALA N N 127.058 0.30 1 14 6 6 ALA H H 8.241 0.02 1 15 6 6 ALA CA C 50.453 0.30 1 16 6 6 ALA CB C 18.202 0.30 1 17 7 7 PRO CA C 63.250 0.30 1 18 7 7 PRO CB C 31.850 0.30 1 19 8 8 SER N N 116.560 0.30 1 20 8 8 SER H H 8.370 0.02 1 21 8 8 SER CA C 58.530 0.30 1 22 8 8 SER CB C 63.970 0.30 1 23 9 9 PRO CA C 62.800 0.30 1 24 9 9 PRO CB C 32.130 0.30 1 25 10 10 GLN N N 121.820 0.30 1 26 10 10 GLN H H 8.440 0.02 1 27 10 10 GLN CA C 56.760 0.30 1 28 10 10 GLN CB C 32.800 0.30 1 29 12 13 GLY N N 109.790 0.30 1 30 12 13 GLY H H 8.377 0.02 1 31 13 13 GLY CA C 45.665 0.30 1 32 13 14 PHE N N 120.230 0.30 1 33 13 14 PHE H H 8.000 0.02 1 34 14 14 PHE CA C 57.490 0.30 1 35 14 14 PHE CB C 39.600 0.30 1 36 14 15 ARG N N 122.620 0.30 1 37 14 15 ARG H H 8.278 0.02 1 38 15 15 ARG CA C 56.567 0.30 1 39 15 15 ARG CB C 30.457 0.30 1 40 15 16 ARG N N 122.813 0.30 1 41 15 16 ARG H H 8.387 0.02 1 42 16 16 ARG CA C 56.650 0.30 1 43 16 16 ARG CB C 30.450 0.30 1 44 16 17 ALA N N 126.080 0.30 1 45 16 17 ALA H H 8.380 0.02 1 46 17 17 ALA CA C 52.988 0.30 1 47 17 17 ALA CB C 19.047 0.30 1 48 17 18 VAL N N 118.866 0.30 1 49 17 18 VAL H H 8.039 0.02 1 50 18 18 VAL CA C 62.400 0.30 1 51 18 18 VAL CB C 32.600 0.30 1 52 18 19 SER N N 117.800 0.30 1 53 18 19 SER H H 8.400 0.02 1 54 19 19 SER CA C 56.500 0.30 1 55 19 19 SER CB C 63.300 0.30 1 56 19 20 GLU N N 123.149 0.30 1 57 19 20 GLU H H 8.534 0.02 1 58 20 20 GLU CA C 57.370 0.30 1 59 20 20 GLU CB C 29.730 0.30 1 60 20 21 GLN N N 119.790 0.30 1 61 20 21 GLN H H 8.270 0.02 1 62 21 21 GLN CA C 56.560 0.30 1 63 21 21 GLN CB C 28.890 0.30 1 64 21 22 ASP N N 121.140 0.30 1 65 21 22 ASP H H 8.130 0.02 1 66 22 22 ASP CA C 54.910 0.30 1 67 22 22 ASP CB C 41.140 0.30 1 68 22 23 ALA N N 124.346 0.30 1 69 22 23 ALA H H 8.126 0.02 1 70 23 23 ALA CA C 53.160 0.30 1 71 23 23 ALA CB C 19.050 0.30 1 72 23 24 LYS N N 119.560 0.30 1 73 23 24 LYS H H 8.140 0.02 1 74 24 24 LYS CA C 56.800 0.30 1 75 24 24 LYS CB C 32.800 0.30 1 76 24 25 GLN N N 120.900 0.30 1 77 24 25 GLN H H 8.170 0.02 1 78 25 25 GLN CA C 56.300 0.30 1 79 25 25 GLN CB C 30.200 0.30 1 80 25 26 ALA N N 124.700 0.30 1 81 25 26 ALA H H 8.190 0.02 1 82 26 26 ALA CA C 52.500 0.30 1 83 26 26 ALA CB C 18.900 0.30 1 84 26 27 GLU N N 119.800 0.30 1 85 26 27 GLU H H 8.200 0.02 1 86 27 27 GLU CA C 56.600 0.30 1 87 27 27 GLU CB C 30.300 0.30 1 88 27 28 ALA N N 124.700 0.30 1 89 27 28 ALA H H 8.170 0.02 1 90 28 28 ALA CA C 52.600 0.30 1 91 28 28 ALA CB C 19.200 0.30 1 92 28 29 VAL CA C 56.354 0.30 1 93 28 29 VAL CB C 30.581 0.30 1 94 29 30 THR N N 115.844 0.30 1 95 29 30 THR H H 8.125 0.02 1 96 30 30 THR CA C 61.598 0.30 1 97 30 30 THR CB C 70.015 0.30 1 98 30 31 SER N N 117.619 0.30 1 99 30 31 SER H H 8.028 0.02 1 100 31 31 SER CA C 55.664 0.30 1 101 31 31 SER CB C 64.114 0.30 1 102 31 32 PRO CA C 63.500 0.30 1 103 31 32 PRO CB C 31.800 0.30 1 104 32 33 ARG N N 120.360 0.30 1 105 32 33 ARG H H 8.210 0.02 1 106 33 33 ARG CA C 56.275 0.30 1 107 33 33 ARG CB C 30.159 0.30 1 108 33 34 PHE N N 120.150 0.30 1 109 33 34 PHE H H 7.887 0.02 1 110 34 34 PHE CA C 57.617 0.30 1 111 34 34 PHE CB C 39.454 0.30 1 112 34 35 ILE N N 123.323 0.30 1 113 34 35 ILE H H 7.990 0.02 1 114 35 35 ILE CA C 61.160 0.30 1 115 35 35 ILE CB C 38.240 0.30 1 116 35 36 GLY N N 112.274 0.30 1 117 35 36 GLY H H 8.040 0.02 1 118 36 36 GLY CA C 45.370 0.30 1 119 36 37 ARG N N 120.664 0.30 1 120 36 37 ARG H H 8.128 0.02 1 121 37 37 ARG CA C 55.686 0.30 1 122 37 37 ARG CB C 30.946 0.30 1 123 37 38 ARG N N 123.509 0.30 1 124 37 38 ARG H H 8.440 0.02 1 125 38 38 ARG CA C 56.153 0.30 1 126 38 38 ARG CB C 30.561 0.30 1 127 38 42 ILE CA C 62.430 0.30 1 128 38 42 ILE CB C 38.430 0.30 1 129 42 43 GLU N N 123.530 0.30 1 130 42 43 GLU H H 8.310 0.02 1 131 43 43 GLU CA C 57.636 0.30 1 132 43 43 GLU CB C 29.891 0.30 1 133 43 44 ASP N N 121.349 0.30 1 134 43 44 ASP H H 8.291 0.02 1 135 44 44 ASP CA C 55.726 0.30 1 136 44 44 ASP CB C 40.876 0.30 1 137 44 45 ALA N N 123.896 0.30 1 138 44 45 ALA H H 8.135 0.02 1 139 45 45 ALA CA C 54.079 0.30 1 140 45 45 ALA CB C 18.343 0.30 1 141 45 46 ARG N N 119.505 0.30 1 142 45 46 ARG H H 8.049 0.02 1 143 46 46 ARG CA C 58.622 0.30 1 144 46 46 ARG CB C 29.750 0.30 1 145 46 47 LYS N N 120.193 0.30 1 146 46 47 LYS H H 8.093 0.02 1 147 47 47 LYS CA C 58.715 0.30 1 148 47 47 LYS CB C 32.285 0.30 1 149 47 48 GLU N N 120.917 0.30 1 150 47 48 GLU H H 8.170 0.02 1 151 48 48 GLU CA C 58.654 0.30 1 152 48 48 GLU CB C 29.469 0.30 1 153 48 49 ARG CA C 58.370 0.30 1 154 48 49 ARG CB C 30.010 0.30 1 155 49 50 GLU N N 120.986 0.30 1 156 49 50 GLU H H 8.366 0.02 1 157 50 50 GLU CA C 58.519 0.30 1 158 50 50 GLU CB C 29.450 0.30 1 159 50 51 ALA N N 123.780 0.30 1 160 50 51 ALA H H 8.160 0.02 1 161 51 51 ALA CA C 54.200 0.30 1 162 51 51 ALA CB C 18.000 0.30 1 163 51 52 ALA N N 122.300 0.30 1 164 51 52 ALA H H 8.080 0.02 1 165 52 52 ALA CA C 54.100 0.30 1 166 52 52 ALA CB C 18.000 0.30 1 167 52 53 ALA N N 122.200 0.30 1 168 52 53 ALA H H 8.000 0.02 1 169 53 53 ALA CA C 54.000 0.30 1 170 53 53 ALA CB C 18.200 0.30 1 171 53 54 ALA N N 122.230 0.30 1 172 53 54 ALA H H 8.000 0.02 1 173 54 54 ALA CA C 53.900 0.30 1 174 54 54 ALA CB C 18.200 0.30 1 175 54 55 ALA N N 121.970 0.30 1 176 54 55 ALA H H 7.960 0.02 1 177 55 55 ALA CA C 53.800 0.30 1 178 55 55 ALA CB C 18.200 0.30 1 179 55 56 ALA N N 121.870 0.30 1 180 55 56 ALA H H 7.930 0.02 1 181 56 56 ALA CA C 53.600 0.30 1 182 56 56 ALA CB C 18.600 0.30 1 183 56 57 ALA N N 121.440 0.30 1 184 56 57 ALA H H 7.870 0.02 1 185 57 57 ALA CA C 53.400 0.30 1 186 57 57 ALA CB C 18.300 0.30 1 187 57 58 ALA N N 121.400 0.30 1 188 57 58 ALA H H 7.850 0.02 1 189 58 58 ALA CA C 52.900 0.30 1 190 58 58 ALA CB C 18.500 0.30 1 191 58 59 ALA N N 122.050 0.30 1 192 58 59 ALA H H 7.820 0.02 1 193 59 59 ALA CA C 52.800 0.30 1 194 59 59 ALA CB C 18.800 0.30 1 195 59 60 VAL N N 118.141 0.30 1 196 59 60 VAL H H 7.776 0.02 1 197 60 60 VAL CA C 62.680 0.30 1 198 60 60 VAL CB C 32.271 0.30 1 199 60 61 ALA N N 126.578 0.30 1 200 60 61 ALA H H 8.140 0.02 1 201 61 61 ALA CA C 52.787 0.30 1 202 61 61 ALA CB C 18.884 0.30 1 203 61 62 SER N N 114.536 0.30 1 204 61 62 SER H H 8.148 0.02 1 205 62 62 SER CA C 58.379 0.30 1 206 62 62 SER CB C 63.918 0.30 1 207 62 63 SER N N 117.627 0.30 1 208 62 63 SER H H 8.217 0.02 1 209 63 63 SER CA C 58.481 0.30 1 210 63 63 SER CB C 63.833 0.30 1 211 63 64 GLU N N 123.720 0.30 1 212 63 64 GLU H H 8.250 0.02 1 213 64 64 GLU CA C 54.320 0.30 1 214 64 64 GLU CB C 29.891 0.30 1 215 64 65 PRO CA C 63.612 0.30 1 216 64 65 PRO CB C 32.004 0.30 1 217 65 66 GLY N N 109.119 0.30 1 218 65 66 GLY H H 8.434 0.02 1 219 66 66 GLY CA C 45.051 0.30 1 220 66 67 ASN N N 119.429 0.30 1 221 66 67 ASN H H 8.227 0.02 1 222 67 67 ASN CA C 51.017 0.30 1 223 67 67 ASN CB C 38.764 0.30 1 224 67 69 LEU CA C 56.085 0.30 1 225 67 69 LEU CB C 42.285 0.30 1 226 69 70 GLU N N 121.670 0.30 1 227 69 70 GLU H H 7.610 0.02 1 228 70 70 GLU CA C 57.900 0.30 1 229 70 70 GLU CB C 29.800 0.30 1 230 70 71 ALA CA C 52.800 0.30 1 231 70 72 VAL N N 120.062 0.30 1 232 71 72 VAL H H 7.858 0.02 1 233 72 72 VAL CA C 62.009 0.30 1 234 72 73 VAL N N 126.000 0.30 1 235 72 73 VAL H H 8.230 0.02 1 236 73 73 VAL CA C 61.600 0.30 1 237 73 74 PHE CA C 55.238 0.30 1 238 73 75 GLU N N 120.315 0.30 1 239 74 75 GLU H H 8.503 0.02 1 240 75 75 GLU CA C 54.384 0.30 1 241 75 76 GLU N N 124.046 0.30 1 242 75 76 GLU H H 8.788 0.02 1 243 76 76 GLU CA C 55.416 0.30 1 244 76 77 ARG N N 125.467 0.30 1 245 76 77 ARG H H 9.088 0.02 1 246 77 77 ARG CA C 55.570 0.30 1 247 77 78 ASP N N 126.486 0.30 1 248 77 78 ASP H H 9.238 0.02 1 249 78 78 ASP CA C 55.613 0.30 1 250 78 79 GLY N N 104.639 0.30 1 251 78 79 GLY H H 8.674 0.02 1 252 79 79 GLY CA C 45.295 0.30 1 253 79 80 ASN CA C 51.680 0.30 1 254 79 81 ALA N N 124.245 0.30 1 255 80 81 ALA H H 9.257 0.02 1 256 81 81 ALA CA C 50.358 0.30 1 257 81 82 VAL N N 121.247 0.30 1 258 81 82 VAL H H 8.920 0.02 1 259 82 82 VAL CA C 60.720 0.30 1 260 82 83 LEU N N 125.900 0.30 1 261 82 83 LEU H H 8.340 0.02 1 262 83 83 LEU CA C 55.900 0.30 1 263 83 84 ASN N N 115.643 0.30 1 264 83 84 ASN H H 8.289 0.02 1 265 84 84 ASN CA C 50.724 0.30 1 266 84 85 LEU N N 123.352 0.30 1 267 84 85 LEU H H 9.215 0.02 1 268 85 85 LEU CA C 53.652 0.30 1 269 85 86 LEU N N 122.400 0.30 1 270 85 86 LEU H H 8.990 0.02 1 271 86 86 LEU CA C 53.500 0.30 1 272 86 87 PHE N N 113.880 0.30 1 273 86 87 PHE H H 8.550 0.02 1 274 87 87 PHE CA C 56.200 0.30 1 275 87 88 SER N N 115.400 0.30 1 276 87 88 SER H H 9.420 0.02 1 277 88 88 SER CA C 56.600 0.30 1 278 88 89 LEU N N 122.300 0.30 1 279 88 89 LEU H H 9.165 0.02 1 280 89 89 LEU CA C 53.000 0.30 1 281 89 91 GLY N N 108.940 0.30 1 282 89 91 GLY H H 8.410 0.02 1 283 91 91 GLY CA C 45.300 0.30 1 284 91 92 THR N N 113.800 0.30 1 285 91 92 THR H H 7.540 0.02 1 286 92 92 THR CA C 61.090 0.30 1 287 92 92 THR CB C 70.030 0.30 1 288 92 95 SER CA C 58.100 0.30 1 289 92 96 SER N N 117.100 0.30 1 290 95 96 SER H H 7.880 0.02 1 291 96 96 SER CA C 56.900 0.30 1 292 96 97 LEU N N 125.300 0.30 1 293 96 97 LEU H H 8.680 0.02 1 294 97 97 LEU CA C 58.220 0.30 1 295 97 97 LEU C C 178.800 0.30 1 296 97 98 SER N N 117.030 0.30 1 297 97 98 SER H H 9.910 0.02 1 298 98 98 SER CA C 62.430 0.30 1 299 98 99 ARG N N 121.900 0.30 1 300 98 99 ARG H H 7.420 0.02 1 301 99 99 ARG CA C 59.500 0.30 1 302 99 100 ALA N N 121.380 0.30 1 303 99 100 ALA H H 7.470 0.02 1 304 100 100 ALA CA C 55.100 0.30 1 305 100 101 VAL N N 113.870 0.30 1 306 100 101 VAL H H 8.900 0.02 1 307 101 101 VAL CA C 65.480 0.30 1 308 101 102 LYS CA C 58.400 0.30 1 309 101 103 VAL N N 119.435 0.30 1 310 102 103 VAL H H 7.290 0.02 1 311 103 103 VAL CA C 66.820 0.30 1 312 103 104 PHE N N 115.570 0.30 1 313 103 104 PHE H H 6.890 0.02 1 314 104 104 PHE CA C 62.400 0.30 1 315 104 106 THR C C 175.100 0.30 1 316 104 107 PHE N N 116.760 0.30 1 317 106 107 PHE H H 7.230 0.02 1 318 107 107 PHE CA C 60.420 0.30 1 319 107 108 GLU N N 114.974 0.30 1 320 107 108 GLU H H 7.912 0.02 1 321 108 108 GLU CA C 57.070 0.30 1 322 108 109 ALA CA C 51.949 0.30 1 323 108 110 LYS N N 122.595 0.30 1 324 109 110 LYS H H 8.777 0.02 1 325 110 110 LYS CA C 55.480 0.30 1 326 110 111 ILE N N 126.340 0.30 1 327 110 111 ILE H H 8.699 0.02 1 328 111 111 ILE CA C 62.620 0.30 1 329 111 112 HIS N N 127.760 0.30 1 330 111 112 HIS H H 9.336 0.02 1 331 112 112 HIS CA C 57.200 0.30 1 332 112 113 HIS N N 116.940 0.30 1 333 112 113 HIS H H 8.010 0.02 1 334 113 113 HIS CA C 56.820 0.30 1 335 113 115 GLU N N 119.810 0.30 1 336 113 115 GLU H H 9.300 0.02 1 337 115 115 GLU CA C 54.890 0.30 1 338 115 116 THR N N 111.200 0.30 1 339 115 116 THR H H 8.165 0.02 1 340 116 116 THR CA C 59.200 0.30 1 341 116 116 THR C C 175.100 0.30 1 342 116 117 ARG N N 120.260 0.30 1 343 116 117 ARG H H 8.875 0.02 1 344 117 117 ARG CA C 53.800 0.30 1 345 117 118 PRO CA C 63.046 0.30 1 346 117 119 ALA N N 126.020 0.30 1 347 118 119 ALA H H 8.298 0.02 1 348 119 119 ALA CA C 51.883 0.30 1 349 119 119 ALA CB C 19.200 0.30 1 350 119 120 GLN N N 120.559 0.30 1 351 119 120 GLN H H 8.340 0.02 1 352 120 120 GLN CA C 56.824 0.30 1 353 120 120 GLN CB C 29.751 0.30 1 354 120 121 ARG N N 121.000 0.30 1 355 120 121 ARG H H 8.400 0.02 1 356 121 121 ARG CA C 53.591 0.30 1 357 121 121 ARG CB C 29.750 0.30 1 358 121 122 PRO CA C 63.275 0.30 1 359 121 122 PRO CB C 31.860 0.30 1 360 122 123 LEU N N 122.025 0.30 1 361 122 123 LEU H H 8.483 0.02 1 362 123 123 LEU CA C 54.872 0.30 1 363 123 123 LEU CB C 42.270 0.30 1 364 123 124 ALA N N 124.624 0.30 1 365 123 124 ALA H H 8.306 0.02 1 366 124 124 ALA CA C 52.981 0.30 1 367 124 124 ALA CB C 19.100 0.30 1 368 124 125 GLY N N 108.562 0.30 1 369 124 125 GLY H H 8.485 0.02 1 370 125 125 GLY CA C 45.295 0.30 1 371 125 126 SER N N 116.207 0.30 1 372 125 126 SER H H 7.926 0.02 1 373 126 126 SER CA C 56.636 0.30 1 374 126 126 SER CB C 63.410 0.30 1 375 126 130 GLU N N 120.065 0.30 1 376 126 130 GLU H H 8.757 0.02 1 377 130 130 GLU CA C 54.300 0.30 1 378 130 131 TYR N N 118.967 0.30 1 379 130 131 TYR H H 8.725 0.02 1 380 131 131 TYR CA C 57.310 0.30 1 381 131 132 PHE N N 122.541 0.30 1 382 131 132 PHE H H 8.947 0.02 1 383 132 132 PHE CA C 55.716 0.30 1 384 132 133 VAL N N 125.792 0.30 1 385 132 133 VAL H H 8.950 0.02 1 386 133 133 VAL CA C 58.715 0.30 1 387 133 134 ARG N N 127.972 0.30 1 388 133 134 ARG H H 9.073 0.02 1 389 134 134 ARG CA C 54.262 0.30 1 390 134 135 PHE N N 124.425 0.30 1 391 134 135 PHE H H 9.058 0.02 1 392 135 135 PHE CA C 55.423 0.30 1 393 135 135 PHE C C 170.200 0.30 1 394 135 136 GLU N N 116.577 0.30 1 395 135 136 GLU H H 8.572 0.02 1 396 136 136 GLU CA C 52.900 0.30 1 397 136 137 VAL N N 121.912 0.30 1 398 136 137 VAL H H 8.858 0.02 1 399 137 137 VAL CA C 57.900 0.30 1 400 137 137 VAL CB C 37.000 0.30 1 401 137 139 SER N N 120.486 0.30 1 402 137 139 SER H H 8.916 0.02 1 403 139 139 SER CA C 62.802 0.30 1 404 139 140 GLY N N 108.932 0.30 1 405 139 140 GLY H H 9.039 0.02 1 406 140 140 GLY CA C 46.127 0.30 1 407 140 141 ASP N N 118.207 0.30 1 408 140 141 ASP H H 7.854 0.02 1 409 141 141 ASP CA C 54.384 0.30 1 410 141 142 LEU N N 120.885 0.30 1 411 141 142 LEU H H 7.089 0.02 1 412 142 142 LEU CA C 58.776 0.30 1 413 142 143 ALA N N 119.946 0.30 1 414 142 143 ALA H H 8.685 0.02 1 415 143 143 ALA CA C 55.888 0.30 1 416 143 144 ALA N N 122.096 0.30 1 417 143 144 ALA H H 8.083 0.02 1 418 144 144 ALA CA C 54.628 0.30 1 419 144 145 LEU N N 122.990 0.30 1 420 144 145 LEU H H 7.746 0.02 1 421 145 145 LEU CA C 58.837 0.30 1 422 145 146 LEU N N 120.370 0.30 1 423 145 146 LEU H H 8.530 0.02 1 424 146 146 LEU CA C 57.617 0.30 1 425 146 147 SER N N 113.711 0.30 1 426 146 147 SER H H 8.147 0.02 1 427 147 147 SER CA C 61.948 0.30 1 428 147 148 SER N N 116.833 0.30 1 429 147 148 SER H H 7.668 0.02 1 430 148 148 SER CA C 62.424 0.30 1 431 148 149 VAL N N 123.357 0.30 1 432 148 149 VAL H H 8.673 0.02 1 433 149 149 VAL CA C 66.401 0.30 1 434 149 150 ARG CA C 58.959 0.30 1 435 149 151 ARG N N 115.343 0.30 1 436 150 151 ARG H H 7.156 0.02 1 437 151 151 ARG CA C 58.166 0.30 1 438 151 152 VAL N N 111.155 0.30 1 439 151 152 VAL H H 7.278 0.02 1 440 152 152 VAL CA C 60.171 0.30 1 441 152 153 SER N N 116.152 0.30 1 442 152 153 SER H H 7.536 0.02 1 443 153 153 SER CA C 58.227 0.30 1 444 153 154 ASP N N 120.290 0.30 1 445 153 154 ASP H H 8.857 0.02 1 446 154 154 ASP CA C 55.292 0.30 1 447 154 155 ASP N N 118.354 0.30 1 448 154 155 ASP H H 8.543 0.02 1 449 155 155 ASP CA C 54.323 0.30 1 450 155 156 VAL N N 120.567 0.30 1 451 155 156 VAL H H 7.974 0.02 1 452 156 156 VAL CA C 62.558 0.30 1 453 156 156 VAL CB C 32.080 0.30 1 454 156 157 ARG N N 126.396 0.30 1 455 156 157 ARG H H 9.150 0.02 1 456 157 157 ARG CA C 54.914 0.30 1 457 157 158 SER N N 115.697 0.30 1 458 157 158 SER H H 8.770 0.02 1 459 158 158 SER CA C 59.691 0.30 1 460 158 159 ALA N N 130.748 0.30 1 461 158 159 ALA H H 7.810 0.02 1 462 159 159 ALA CA C 53.286 0.30 1 463 159 159 ALA CB C 21.864 0.30 1 stop_ save_