data_19481 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase ; _BMRB_accession_number 19481 _BMRB_flat_file_name bmr19481.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 . 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" 127 "13C chemical shifts" 223 "15N chemical shifts" 127 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 19480 'RDTH dimer' 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 Hinck Andrew . . 4 Fitzpatrick Paul . . 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 17252.3 _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 Ser40_phosphorylated_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 19480 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 'BL21 DE3' 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 114.795 0.30 1 95 29 30 THR H H 8.042 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 7.976 0.02 1 114 35 35 ILE CA C 61.072 0.30 1 115 35 35 ILE CB C 38.468 0.30 1 116 35 36 GLY N N 112.274 0.30 1 117 35 36 GLY H H 8.003 0.02 1 118 36 36 GLY CA C 45.112 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 8.478 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 39 GLN N N 123.255 0.30 1 128 38 39 GLN H H 8.625 0.02 1 129 39 39 GLN CA C 57.032 0.30 1 130 39 39 GLN CB C 28.915 0.30 1 131 39 40 SER N N 117.626 0.30 1 132 39 40 SER H H 9.030 0.02 1 133 40 40 SER CA C 58.853 0.30 1 134 40 40 SER CB C 65.213 0.30 1 135 40 41 LEU N N 122.997 0.30 1 136 40 41 LEU H H 7.875 0.02 1 137 41 41 LEU CA C 56.087 0.30 1 138 41 41 LEU CB C 42.426 0.30 1 139 41 42 ILE N N 121.860 0.30 1 140 41 42 ILE H H 7.912 0.02 1 141 42 42 ILE CA C 62.269 0.30 1 142 42 42 ILE CB C 38.341 0.30 1 143 42 43 GLU N N 123.930 0.30 1 144 42 43 GLU H H 8.372 0.02 1 145 43 43 GLU CA C 57.636 0.30 1 146 43 43 GLU CB C 29.891 0.30 1 147 43 44 ASP N N 121.349 0.30 1 148 43 44 ASP H H 8.291 0.02 1 149 44 44 ASP CA C 55.726 0.30 1 150 44 44 ASP CB C 40.876 0.30 1 151 44 45 ALA N N 123.896 0.30 1 152 44 45 ALA H H 8.135 0.02 1 153 45 45 ALA CA C 54.079 0.30 1 154 45 45 ALA CB C 18.343 0.30 1 155 45 46 ARG N N 119.505 0.30 1 156 45 46 ARG H H 8.049 0.02 1 157 46 46 ARG CA C 58.622 0.30 1 158 46 46 ARG CB C 29.750 0.30 1 159 46 47 LYS N N 120.193 0.30 1 160 46 47 LYS H H 8.093 0.02 1 161 47 47 LYS CA C 58.715 0.30 1 162 47 47 LYS CB C 32.285 0.30 1 163 47 48 GLU N N 120.917 0.30 1 164 47 48 GLU H H 8.170 0.02 1 165 48 48 GLU CA C 58.654 0.30 1 166 48 48 GLU CB C 29.469 0.30 1 167 48 49 ARG CA C 58.370 0.30 1 168 48 49 ARG CB C 30.010 0.30 1 169 49 50 GLU N N 120.986 0.30 1 170 49 50 GLU H H 8.366 0.02 1 171 50 50 GLU CA C 58.519 0.30 1 172 50 50 GLU CB C 29.450 0.30 1 173 50 51 ALA N N 123.780 0.30 1 174 50 51 ALA H H 8.160 0.02 1 175 51 51 ALA CA C 54.200 0.30 1 176 51 51 ALA CB C 18.000 0.30 1 177 51 52 ALA N N 122.300 0.30 1 178 51 52 ALA H H 8.080 0.02 1 179 52 52 ALA CA C 54.100 0.30 1 180 52 52 ALA CB C 18.000 0.30 1 181 52 53 ALA N N 122.200 0.30 1 182 52 53 ALA H H 8.000 0.02 1 183 53 53 ALA CA C 54.000 0.30 1 184 53 53 ALA CB C 18.200 0.30 1 185 53 54 ALA N N 122.230 0.30 1 186 53 54 ALA H H 8.000 0.02 1 187 54 54 ALA CA C 53.900 0.30 1 188 54 54 ALA CB C 18.200 0.30 1 189 54 55 ALA N N 121.970 0.30 1 190 54 55 ALA H H 7.960 0.02 1 191 55 55 ALA CA C 53.800 0.30 1 192 55 55 ALA CB C 18.200 0.30 1 193 55 56 ALA N N 121.870 0.30 1 194 55 56 ALA H H 7.930 0.02 1 195 56 56 ALA CA C 53.600 0.30 1 196 56 56 ALA CB C 18.600 0.30 1 197 56 57 ALA N N 121.440 0.30 1 198 56 57 ALA H H 7.870 0.02 1 199 57 57 ALA CA C 53.400 0.30 1 200 57 57 ALA CB C 18.300 0.30 1 201 57 58 ALA N N 121.400 0.30 1 202 57 58 ALA H H 7.850 0.02 1 203 58 58 ALA CA C 52.900 0.30 1 204 58 58 ALA CB C 18.500 0.30 1 205 58 59 ALA N N 122.050 0.30 1 206 58 59 ALA H H 7.820 0.02 1 207 59 59 ALA CA C 52.800 0.30 1 208 59 59 ALA CB C 18.800 0.30 1 209 59 60 VAL N N 118.141 0.30 1 210 59 60 VAL H H 7.776 0.02 1 211 60 60 VAL CA C 62.680 0.30 1 212 60 60 VAL CB C 32.271 0.30 1 213 60 61 ALA N N 126.578 0.30 1 214 60 61 ALA H H 8.140 0.02 1 215 61 61 ALA CA C 52.787 0.30 1 216 61 61 ALA CB C 18.884 0.30 1 217 61 62 SER N N 114.536 0.30 1 218 61 62 SER H H 8.148 0.02 1 219 62 62 SER CA C 58.379 0.30 1 220 62 62 SER CB C 63.918 0.30 1 221 62 63 SER N N 117.627 0.30 1 222 62 63 SER H H 8.217 0.02 1 223 63 63 SER CA C 58.481 0.30 1 224 63 63 SER CB C 63.833 0.30 1 225 63 64 GLU N N 123.720 0.30 1 226 63 64 GLU H H 8.250 0.02 1 227 64 64 GLU CA C 54.320 0.30 1 228 64 64 GLU CB C 29.891 0.30 1 229 64 65 PRO CA C 63.612 0.30 1 230 64 65 PRO CB C 32.004 0.30 1 231 65 66 GLY N N 109.119 0.30 1 232 65 66 GLY H H 8.434 0.02 1 233 66 66 GLY CA C 45.051 0.30 1 234 66 67 ASN N N 119.429 0.30 1 235 66 67 ASN H H 8.227 0.02 1 236 67 67 ASN CA C 51.017 0.30 1 237 67 67 ASN CB C 38.764 0.30 1 238 67 69 LEU CA C 56.085 0.30 1 239 67 69 LEU CB C 42.285 0.30 1 240 69 70 GLU N N 121.670 0.30 1 241 69 70 GLU H H 7.610 0.02 1 242 70 70 GLU CA C 57.900 0.30 1 243 70 70 GLU CB C 29.800 0.30 1 244 70 71 ALA CA C 52.800 0.30 1 245 70 72 VAL N N 120.062 0.30 1 246 71 72 VAL H H 7.858 0.02 1 247 72 72 VAL CA C 62.009 0.30 1 248 72 73 VAL N N 126.000 0.30 1 249 72 73 VAL H H 8.230 0.02 1 250 73 73 VAL CA C 61.600 0.30 1 251 73 74 PHE CA C 55.238 0.30 1 252 73 75 GLU N N 120.315 0.30 1 253 74 75 GLU H H 8.503 0.02 1 254 75 75 GLU CA C 54.384 0.30 1 255 75 76 GLU N N 124.046 0.30 1 256 75 76 GLU H H 8.788 0.02 1 257 76 76 GLU CA C 55.416 0.30 1 258 76 77 ARG N N 125.467 0.30 1 259 76 77 ARG H H 9.088 0.02 1 260 77 77 ARG CA C 55.570 0.30 1 261 77 78 ASP N N 126.486 0.30 1 262 77 78 ASP H H 9.238 0.02 1 263 78 78 ASP CA C 55.613 0.30 1 264 78 79 GLY N N 104.639 0.30 1 265 78 79 GLY H H 8.674 0.02 1 266 79 79 GLY CA C 45.295 0.30 1 267 79 80 ASN CA C 51.680 0.30 1 268 79 81 ALA N N 124.245 0.30 1 269 80 81 ALA H H 9.257 0.02 1 270 81 81 ALA CA C 50.358 0.30 1 271 81 82 VAL N N 121.247 0.30 1 272 81 82 VAL H H 8.920 0.02 1 273 82 82 VAL CA C 60.720 0.30 1 274 82 83 LEU N N 125.900 0.30 1 275 82 83 LEU H H 8.340 0.02 1 276 83 83 LEU CA C 55.900 0.30 1 277 83 84 ASN N N 115.643 0.30 1 278 83 84 ASN H H 8.289 0.02 1 279 84 84 ASN CA C 50.724 0.30 1 280 84 85 LEU N N 123.352 0.30 1 281 84 85 LEU H H 9.215 0.02 1 282 85 85 LEU CA C 53.652 0.30 1 283 85 86 LEU N N 122.400 0.30 1 284 85 86 LEU H H 8.990 0.02 1 285 86 86 LEU CA C 53.500 0.30 1 286 86 87 PHE N N 113.880 0.30 1 287 86 87 PHE H H 8.550 0.02 1 288 87 87 PHE CA C 56.200 0.30 1 289 87 88 SER N N 115.400 0.30 1 290 87 88 SER H H 9.420 0.02 1 291 88 88 SER CA C 56.600 0.30 1 292 88 89 LEU N N 122.300 0.30 1 293 88 89 LEU H H 9.165 0.02 1 294 89 89 LEU CA C 53.000 0.30 1 295 89 91 GLY N N 108.940 0.30 1 296 89 91 GLY H H 8.410 0.02 1 297 91 91 GLY CA C 45.300 0.30 1 298 91 92 THR N N 113.800 0.30 1 299 91 92 THR H H 7.540 0.02 1 300 92 92 THR CA C 61.090 0.30 1 301 92 92 THR CB C 70.030 0.30 1 302 92 95 SER CA C 58.100 0.30 1 303 92 96 SER N N 117.100 0.30 1 304 95 96 SER H H 7.880 0.02 1 305 96 96 SER CA C 56.900 0.30 1 306 96 97 LEU N N 125.300 0.30 1 307 96 97 LEU H H 8.680 0.02 1 308 97 97 LEU CA C 58.220 0.30 1 309 97 97 LEU C C 178.800 0.30 1 310 97 98 SER N N 117.030 0.30 1 311 97 98 SER H H 9.910 0.02 1 312 98 98 SER CA C 62.430 0.30 1 313 98 99 ARG N N 121.900 0.30 1 314 98 99 ARG H H 7.420 0.02 1 315 99 99 ARG CA C 59.500 0.30 1 316 99 100 ALA N N 121.380 0.30 1 317 99 100 ALA H H 7.470 0.02 1 318 100 100 ALA CA C 55.100 0.30 1 319 100 101 VAL N N 113.870 0.30 1 320 100 101 VAL H H 8.900 0.02 1 321 101 101 VAL CA C 65.480 0.30 1 322 101 102 LYS CA C 58.400 0.30 1 323 101 103 VAL N N 119.435 0.30 1 324 102 103 VAL H H 7.290 0.02 1 325 103 103 VAL CA C 66.820 0.30 1 326 103 104 PHE N N 115.570 0.30 1 327 103 104 PHE H H 6.890 0.02 1 328 104 104 PHE CA C 62.400 0.30 1 329 104 106 THR C C 175.100 0.30 1 330 104 107 PHE N N 116.760 0.30 1 331 106 107 PHE H H 7.230 0.02 1 332 107 107 PHE CA C 60.420 0.30 1 333 107 108 GLU N N 114.974 0.30 1 334 107 108 GLU H H 7.912 0.02 1 335 108 108 GLU CA C 57.070 0.30 1 336 108 109 ALA CA C 51.949 0.30 1 337 108 110 LYS N N 122.595 0.30 1 338 109 110 LYS H H 8.777 0.02 1 339 110 110 LYS CA C 55.480 0.30 1 340 110 111 ILE N N 126.340 0.30 1 341 110 111 ILE H H 8.699 0.02 1 342 111 111 ILE CA C 62.620 0.30 1 343 111 112 HIS N N 127.760 0.30 1 344 111 112 HIS H H 9.336 0.02 1 345 112 112 HIS CA C 57.200 0.30 1 346 112 113 HIS N N 116.940 0.30 1 347 112 113 HIS H H 8.010 0.02 1 348 113 113 HIS CA C 56.820 0.30 1 349 113 115 GLU N N 119.810 0.30 1 350 113 115 GLU H H 9.300 0.02 1 351 115 115 GLU CA C 54.890 0.30 1 352 115 116 THR N N 111.200 0.30 1 353 115 116 THR H H 8.165 0.02 1 354 116 116 THR CA C 59.200 0.30 1 355 116 116 THR C C 175.100 0.30 1 356 116 117 ARG N N 120.260 0.30 1 357 116 117 ARG H H 8.875 0.02 1 358 117 117 ARG CA C 53.800 0.30 1 359 117 118 PRO CA C 63.046 0.30 1 360 117 119 ALA N N 126.020 0.30 1 361 118 119 ALA H H 8.298 0.02 1 362 119 119 ALA CA C 51.883 0.30 1 363 119 119 ALA CB C 19.200 0.30 1 364 119 120 GLN N N 120.559 0.30 1 365 119 120 GLN H H 8.340 0.02 1 366 120 120 GLN CA C 56.824 0.30 1 367 120 120 GLN CB C 29.751 0.30 1 368 120 121 ARG N N 121.000 0.30 1 369 120 121 ARG H H 8.400 0.02 1 370 121 121 ARG CA C 53.591 0.30 1 371 121 121 ARG CB C 29.750 0.30 1 372 121 122 PRO CA C 63.275 0.30 1 373 121 122 PRO CB C 31.860 0.30 1 374 122 123 LEU N N 122.025 0.30 1 375 122 123 LEU H H 8.483 0.02 1 376 123 123 LEU CA C 54.872 0.30 1 377 123 123 LEU CB C 42.270 0.30 1 378 123 124 ALA N N 124.624 0.30 1 379 123 124 ALA H H 8.306 0.02 1 380 124 124 ALA CA C 52.981 0.30 1 381 124 124 ALA CB C 19.100 0.30 1 382 124 125 GLY N N 108.562 0.30 1 383 124 125 GLY H H 8.485 0.02 1 384 125 125 GLY CA C 45.295 0.30 1 385 125 126 SER N N 116.207 0.30 1 386 125 126 SER H H 7.926 0.02 1 387 126 126 SER CA C 56.636 0.30 1 388 126 126 SER CB C 63.410 0.30 1 389 126 130 GLU N N 120.065 0.30 1 390 126 130 GLU H H 8.757 0.02 1 391 130 130 GLU CA C 54.300 0.30 1 392 130 131 TYR N N 118.967 0.30 1 393 130 131 TYR H H 8.725 0.02 1 394 131 131 TYR CA C 57.310 0.30 1 395 131 132 PHE N N 122.541 0.30 1 396 131 132 PHE H H 8.947 0.02 1 397 132 132 PHE CA C 55.716 0.30 1 398 132 133 VAL N N 125.792 0.30 1 399 132 133 VAL H H 8.950 0.02 1 400 133 133 VAL CA C 58.715 0.30 1 401 133 134 ARG N N 127.972 0.30 1 402 133 134 ARG H H 9.073 0.02 1 403 134 134 ARG CA C 54.262 0.30 1 404 134 135 PHE N N 124.425 0.30 1 405 134 135 PHE H H 9.058 0.02 1 406 135 135 PHE CA C 55.423 0.30 1 407 135 135 PHE C C 170.200 0.30 1 408 135 136 GLU N N 116.577 0.30 1 409 135 136 GLU H H 8.572 0.02 1 410 136 136 GLU CA C 52.900 0.30 1 411 136 137 VAL N N 121.912 0.30 1 412 136 137 VAL H H 8.858 0.02 1 413 137 137 VAL CA C 57.900 0.30 1 414 137 137 VAL CB C 37.000 0.30 1 415 137 139 SER N N 120.486 0.30 1 416 137 139 SER H H 8.916 0.02 1 417 139 139 SER CA C 62.802 0.30 1 418 139 140 GLY N N 108.932 0.30 1 419 139 140 GLY H H 9.039 0.02 1 420 140 140 GLY CA C 46.127 0.30 1 421 140 141 ASP N N 118.207 0.30 1 422 140 141 ASP H H 7.854 0.02 1 423 141 141 ASP CA C 54.384 0.30 1 424 141 142 LEU N N 120.885 0.30 1 425 141 142 LEU H H 7.089 0.02 1 426 142 142 LEU CA C 58.776 0.30 1 427 142 143 ALA N N 119.946 0.30 1 428 142 143 ALA H H 8.685 0.02 1 429 143 143 ALA CA C 55.888 0.30 1 430 143 144 ALA N N 122.096 0.30 1 431 143 144 ALA H H 8.083 0.02 1 432 144 144 ALA CA C 54.628 0.30 1 433 144 145 LEU N N 122.990 0.30 1 434 144 145 LEU H H 7.746 0.02 1 435 145 145 LEU CA C 58.837 0.30 1 436 145 146 LEU N N 120.370 0.30 1 437 145 146 LEU H H 8.530 0.02 1 438 146 146 LEU CA C 57.617 0.30 1 439 146 147 SER N N 113.711 0.30 1 440 146 147 SER H H 8.147 0.02 1 441 147 147 SER CA C 61.948 0.30 1 442 147 148 SER N N 116.833 0.30 1 443 147 148 SER H H 7.668 0.02 1 444 148 148 SER CA C 62.424 0.30 1 445 148 149 VAL N N 123.357 0.30 1 446 148 149 VAL H H 8.673 0.02 1 447 149 149 VAL CA C 66.401 0.30 1 448 149 150 ARG CA C 58.959 0.30 1 449 149 151 ARG N N 115.343 0.30 1 450 150 151 ARG H H 7.156 0.02 1 451 151 151 ARG CA C 58.166 0.30 1 452 151 152 VAL N N 111.155 0.30 1 453 151 152 VAL H H 7.278 0.02 1 454 152 152 VAL CA C 60.171 0.30 1 455 152 153 SER N N 116.152 0.30 1 456 152 153 SER H H 7.536 0.02 1 457 153 153 SER CA C 58.227 0.30 1 458 153 154 ASP N N 120.290 0.30 1 459 153 154 ASP H H 8.857 0.02 1 460 154 154 ASP CA C 55.292 0.30 1 461 154 155 ASP N N 118.354 0.30 1 462 154 155 ASP H H 8.543 0.02 1 463 155 155 ASP CA C 54.323 0.30 1 464 155 156 VAL N N 120.567 0.30 1 465 155 156 VAL H H 7.974 0.02 1 466 156 156 VAL CA C 62.558 0.30 1 467 156 156 VAL CB C 32.080 0.30 1 468 156 157 ARG N N 126.396 0.30 1 469 156 157 ARG H H 9.150 0.02 1 470 157 157 ARG CA C 54.914 0.30 1 471 157 158 SER N N 115.697 0.30 1 472 157 158 SER H H 8.770 0.02 1 473 158 158 SER CA C 59.691 0.30 1 474 158 159 ALA N N 130.748 0.30 1 475 158 159 ALA H H 7.810 0.02 1 476 159 159 ALA CA C 53.286 0.30 1 477 159 159 ALA CB C 21.864 0.30 1 stop_ save_