data_25467 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone H, N and C assignments for PLAT domain of human polycystin-1, W3128A mutant ; _BMRB_accession_number 25467 _BMRB_flat_file_name bmr25467.str _Entry_type original _Submission_date 2015-02-05 _Accession_date 2015-02-05 _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 Williamson Mike P. . 2 Ong Albert CM . 3 Xu Yaoxian . . 4 Hounslow Andrea M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 109 "13C chemical shifts" 325 "15N chemical shifts" 109 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-06-30 original BMRB . stop_ _Original_release_date 2016-06-30 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone assignment and secondary structure of the PLAT domain of human polycystin-1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25943267 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Xu Yaoxian . . 2 Ong Albert CM . 3 Williamson Mike P. . 4 Hounslow Andrea M. . stop_ _Journal_abbreviation 'Biomol. NMR Assign.' _Journal_volume 9 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 369 _Page_last 373 _Year 2015 _Details . loop_ _Keyword ADPKD LH2 PLAT polycystin stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'GB1-PLAT (PKD1_PLAT)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label PKD1_PLAT $PKD1_PLAT stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 PKD1_PLAT stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PKD1_PLAT _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PKD1_PLAT _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'Unknown, though presumed to regulate the PKD2 channel' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 210 _Mol_residue_sequence ; AAAAAAAAMQYKLALNGKTL KGETTTEAVDAATAEKVFKQ YANDNGVDGEWTYDDATKTF TVTELVPRGSCGQRGRFKYE ILVKTGAGRGSGTTAHVGIM LYGVDSRSGHRHLDGDRAFH RNSLDIFRIATPHSLGSVWK IRVWHDNKGLSPAWFLQHVI VRDLQTARSAFFLVNDWLSV ETEANGGLVEKEVLAASDAA LLRFHHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -75 ALA 2 -74 ALA 3 -73 ALA 4 -72 ALA 5 -71 ALA 6 -70 ALA 7 -69 ALA 8 -68 ALA 9 -67 MET 10 -66 GLN 11 -65 TYR 12 -64 LYS 13 -63 LEU 14 -62 ALA 15 -61 LEU 16 -60 ASN 17 -59 GLY 18 -58 LYS 19 -57 THR 20 -56 LEU 21 -55 LYS 22 -54 GLY 23 -53 GLU 24 -52 THR 25 -51 THR 26 -50 THR 27 -49 GLU 28 -48 ALA 29 -47 VAL 30 -46 ASP 31 -45 ALA 32 -44 ALA 33 -43 THR 34 -42 ALA 35 -41 GLU 36 -40 LYS 37 -39 VAL 38 -38 PHE 39 -37 LYS 40 -36 GLN 41 -35 TYR 42 -34 ALA 43 -33 ASN 44 -32 ASP 45 -31 ASN 46 -30 GLY 47 -29 VAL 48 -28 ASP 49 -27 GLY 50 -26 GLU 51 -25 TRP 52 -24 THR 53 -23 TYR 54 -22 ASP 55 -21 ASP 56 -20 ALA 57 -19 THR 58 -18 LYS 59 -17 THR 60 -16 PHE 61 -15 THR 62 -14 VAL 63 -13 THR 64 -12 GLU 65 -11 LEU 66 -10 VAL 67 -9 PRO 68 -8 ARG 69 -7 GLY 70 -6 SER 71 -5 CYS 72 -4 GLY 73 -3 GLN 74 -2 ARG 75 -1 GLY 76 0 ARG 77 1 PHE 78 2 LYS 79 3 TYR 80 4 GLU 81 5 ILE 82 6 LEU 83 7 VAL 84 8 LYS 85 9 THR 86 10 GLY 87 11 ALA 88 12 GLY 89 13 ARG 90 14 GLY 91 15 SER 92 16 GLY 93 17 THR 94 18 THR 95 19 ALA 96 20 HIS 97 21 VAL 98 22 GLY 99 23 ILE 100 24 MET 101 25 LEU 102 26 TYR 103 27 GLY 104 28 VAL 105 29 ASP 106 30 SER 107 31 ARG 108 32 SER 109 33 GLY 110 34 HIS 111 35 ARG 112 36 HIS 113 37 LEU 114 38 ASP 115 39 GLY 116 40 ASP 117 41 ARG 118 42 ALA 119 43 PHE 120 44 HIS 121 45 ARG 122 46 ASN 123 47 SER 124 48 LEU 125 49 ASP 126 50 ILE 127 51 PHE 128 52 ARG 129 53 ILE 130 54 ALA 131 55 THR 132 56 PRO 133 57 HIS 134 58 SER 135 59 LEU 136 60 GLY 137 61 SER 138 62 VAL 139 63 TRP 140 64 LYS 141 65 ILE 142 66 ARG 143 67 VAL 144 68 TRP 145 69 HIS 146 70 ASP 147 71 ASN 148 72 LYS 149 73 GLY 150 74 LEU 151 75 SER 152 76 PRO 153 77 ALA 154 78 TRP 155 79 PHE 156 80 LEU 157 81 GLN 158 82 HIS 159 83 VAL 160 84 ILE 161 85 VAL 162 86 ARG 163 87 ASP 164 88 LEU 165 89 GLN 166 90 THR 167 91 ALA 168 92 ARG 169 93 SER 170 94 ALA 171 95 PHE 172 96 PHE 173 97 LEU 174 98 VAL 175 99 ASN 176 100 ASP 177 101 TRP 178 102 LEU 179 103 SER 180 104 VAL 181 105 GLU 182 106 THR 183 107 GLU 184 108 ALA 185 109 ASN 186 110 GLY 187 111 GLY 188 112 LEU 189 113 VAL 190 114 GLU 191 115 LYS 192 116 GLU 193 117 VAL 194 118 LEU 195 119 ALA 196 120 ALA 197 121 SER 198 122 ASP 199 123 ALA 200 124 ALA 201 125 LEU 202 126 LEU 203 127 ARG 204 128 PHE 205 129 HIS 206 130 HIS 207 131 HIS 208 132 HIS 209 133 HIS 210 134 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 Uniprot P98161 . . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PKD1_PLAT 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 $PKD1_PLAT 'recombinant technology' . Escherichia coli BL21(DE3) GEVS2 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 $PKD1_PLAT 200 uM '[U-13C; U-15N; U-2H]' DTT 10 mM 'natural abundance' 'sodium chloride' 500 mM 'natural abundance' TRIS 50 mM '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 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _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_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _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_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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' 550 . mM pH 6.5 . pH pressure 1 . atm temperature 298 . 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_ _Software_label $Felix stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCA' '3D HN(CO)CA' '3D HNCACB' '3D CBCA(CO)NH' 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 PKD1_PLAT _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 1 77 PHE H H 8.190 0.005 1 2 1 77 PHE C C 173.920 0.050 1 3 1 77 PHE CA C 57.780 0.050 1 4 1 77 PHE CB C 38.470 0.050 1 5 1 77 PHE N N 121.480 0.050 1 6 2 78 LYS H H 9.090 0.005 1 7 2 78 LYS C C 175.655 0.050 1 8 2 78 LYS CA C 54.960 0.050 1 9 2 78 LYS CB C 35.220 0.050 1 10 2 78 LYS N N 122.280 0.050 1 11 3 79 TYR H H 8.710 0.005 1 12 3 79 TYR C C 174.340 0.050 1 13 3 79 TYR CA C 56.970 0.050 1 14 3 79 TYR CB C 41.290 0.050 1 15 3 79 TYR N N 119.080 0.050 1 16 4 80 GLU H H 9.200 0.005 1 17 4 80 GLU C C 174.230 0.050 1 18 4 80 GLU CA C 54.250 0.050 1 19 4 80 GLU CB C 33.260 0.050 1 20 4 80 GLU N N 123.600 0.050 1 21 5 81 ILE H H 9.560 0.005 1 22 5 81 ILE C C 174.140 0.050 1 23 5 81 ILE CA C 59.260 0.050 1 24 5 81 ILE CB C 39.320 0.050 1 25 5 81 ILE N N 127.170 0.050 1 26 6 82 LEU H H 9.660 0.005 1 27 6 82 LEU C C 175.990 0.050 1 28 6 82 LEU CA C 54.650 0.050 1 29 6 82 LEU CB C 42.030 0.050 1 30 6 82 LEU N N 129.720 0.050 1 31 7 83 VAL H H 9.550 0.005 1 32 7 83 VAL C C 174.800 0.050 1 33 7 83 VAL CA C 61.370 0.050 1 34 7 83 VAL CB C 33.620 0.050 1 35 7 83 VAL N N 123.240 0.050 1 36 8 84 LYS H H 8.750 0.005 1 37 8 84 LYS C C 174.790 0.050 1 38 8 84 LYS CA C 52.780 0.050 1 39 8 84 LYS CB C 33.090 0.050 1 40 8 84 LYS N N 132.140 0.050 1 41 9 85 THR H H 9.230 0.005 1 42 9 85 THR C C 174.920 0.050 1 43 9 85 THR CA C 64.490 0.050 1 44 9 85 THR CB C 69.580 0.050 1 45 9 85 THR N N 129.870 0.050 1 46 10 86 GLY H H 8.840 0.005 1 47 10 86 GLY C C 172.560 0.050 1 48 10 86 GLY CA C 45.760 0.050 1 49 10 86 GLY N N 110.560 0.050 1 50 11 87 ALA H H 8.150 0.005 1 51 11 87 ALA C C 179.250 0.050 1 52 11 87 ALA CA C 52.360 0.050 1 53 11 87 ALA CB C 19.430 0.050 1 54 11 87 ALA N N 120.520 0.050 1 55 12 88 GLY H H 8.140 0.005 1 56 12 88 GLY C C 175.020 0.050 1 57 12 88 GLY CA C 44.330 0.050 1 58 12 88 GLY N N 107.030 0.050 1 59 13 89 ARG H H 8.810 0.005 1 60 13 89 ARG C C 177.560 0.050 1 61 13 89 ARG CA C 58.200 0.050 1 62 13 89 ARG CB C 29.020 0.050 1 63 13 89 ARG N N 124.710 0.050 1 64 14 90 GLY H H 9.140 0.005 1 65 14 90 GLY C C 175.140 0.050 1 66 14 90 GLY CA C 45.240 0.050 1 67 14 90 GLY N N 115.870 0.050 1 68 15 91 SER H H 7.750 0.005 1 69 15 91 SER C C 175.160 0.050 1 70 15 91 SER CA C 62.330 0.050 1 71 15 91 SER CB C 65.370 0.050 1 72 15 91 SER N N 114.120 0.050 1 73 16 92 GLY H H 8.290 0.005 1 74 16 92 GLY C C 172.890 0.050 1 75 16 92 GLY CA C 45.190 0.050 1 76 16 92 GLY N N 104.480 0.050 1 77 17 93 THR H H 7.890 0.005 1 78 17 93 THR C C 174.380 0.050 1 79 17 93 THR CA C 57.990 0.050 1 80 17 93 THR CB C 70.160 0.050 1 81 17 93 THR N N 114.490 0.050 1 82 18 94 THR H H 7.180 0.005 1 83 18 94 THR C C 173.570 0.050 1 84 18 94 THR CA C 60.790 0.050 1 85 18 94 THR CB C 70.100 0.050 1 86 18 94 THR N N 118.200 0.050 1 87 19 95 ALA H H 8.730 0.005 1 88 19 95 ALA C C 175.200 0.050 1 89 19 95 ALA CA C 51.240 0.050 1 90 19 95 ALA CB C 21.550 0.050 1 91 19 95 ALA N N 130.220 0.050 1 92 20 96 HIS H H 8.760 0.005 1 93 20 96 HIS C C 175.760 0.050 1 94 20 96 HIS CA C 55.200 0.050 1 95 20 96 HIS CB C 27.520 0.050 1 96 20 96 HIS N N 117.130 0.050 1 97 21 97 VAL H H 8.500 0.005 1 98 21 97 VAL C C 175.680 0.050 1 99 21 97 VAL CA C 61.410 0.050 1 100 21 97 VAL CB C 33.210 0.050 1 101 21 97 VAL N N 129.050 0.050 1 102 26 102 TYR C C 173.610 0.050 1 103 27 103 GLY H H 7.840 0.005 1 104 27 103 GLY C C 176.680 0.050 1 105 27 103 GLY CA C 43.430 0.050 1 106 27 103 GLY N N 110.830 0.050 1 107 28 104 VAL H H 8.430 0.005 1 108 28 104 VAL C C 175.070 0.050 1 109 28 104 VAL CA C 64.730 0.050 1 110 28 104 VAL CB C 31.700 0.050 1 111 28 104 VAL N N 119.530 0.050 1 112 37 113 LEU C C 173.480 0.050 1 113 38 114 ASP H H 7.960 0.005 1 114 38 114 ASP C C 175.470 0.050 1 115 38 114 ASP CA C 53.010 0.050 1 116 38 114 ASP CB C 42.820 0.050 1 117 38 114 ASP N N 122.630 0.050 1 118 39 115 GLY H H 8.250 0.005 1 119 39 115 GLY C C 173.330 0.050 1 120 39 115 GLY CA C 45.200 0.050 1 121 39 115 GLY N N 110.020 0.050 1 122 40 116 ASP H H 8.530 0.005 1 123 40 116 ASP C C 176.690 0.050 1 124 40 116 ASP CA C 55.770 0.050 1 125 40 116 ASP CB C 40.330 0.050 1 126 40 116 ASP N N 124.090 0.050 1 127 41 117 ARG H H 8.760 0.005 1 128 41 117 ARG C C 174.970 0.050 1 129 41 117 ARG CA C 55.450 0.050 1 130 41 117 ARG CB C 28.000 0.050 1 131 41 117 ARG N N 120.820 0.050 1 132 42 118 ALA H H 7.010 0.005 1 133 42 118 ALA C C 178.130 0.050 1 134 42 118 ALA CA C 51.480 0.050 1 135 42 118 ALA CB C 18.430 0.050 1 136 42 118 ALA N N 122.420 0.050 1 137 43 119 PHE H H 9.360 0.005 1 138 43 119 PHE C C 175.830 0.050 1 139 43 119 PHE CA C 57.120 0.050 1 140 43 119 PHE CB C 35.900 0.050 1 141 43 119 PHE N N 115.990 0.050 1 142 44 120 HIS H H 7.690 0.005 1 143 44 120 HIS C C 174.410 0.050 1 144 44 120 HIS CA C 54.030 0.050 1 145 44 120 HIS CB C 29.570 0.050 1 146 44 120 HIS N N 114.080 0.050 1 147 45 121 ARG H H 8.530 0.005 1 148 45 121 ARG C C 177.300 0.050 1 149 45 121 ARG CA C 58.330 0.050 1 150 45 121 ARG CB C 29.820 0.050 1 151 45 121 ARG N N 121.030 0.050 1 152 46 122 ASN H H 8.590 0.005 1 153 46 122 ASN C C 175.210 0.050 1 154 46 122 ASN CA C 53.460 0.050 1 155 46 122 ASN CB C 39.660 0.050 1 156 46 122 ASN N N 123.750 0.050 1 157 47 123 SER H H 8.170 0.005 1 158 47 123 SER C C 172.860 0.050 1 159 47 123 SER CA C 61.280 0.050 1 160 47 123 SER CB C 63.830 0.050 1 161 47 123 SER N N 118.090 0.050 1 162 48 124 LEU H H 8.180 0.005 1 163 48 124 LEU C C 174.980 0.050 1 164 48 124 LEU CA C 53.750 0.050 1 165 48 124 LEU CB C 42.100 0.050 1 166 48 124 LEU N N 126.540 0.050 1 167 49 125 ASP H H 8.860 0.005 1 168 49 125 ASP C C 174.980 0.050 1 169 49 125 ASP CA C 53.690 0.050 1 170 49 125 ASP CB C 45.870 0.050 1 171 49 125 ASP N N 126.880 0.050 1 172 50 126 ILE H H 8.000 0.005 1 173 50 126 ILE C C 174.800 0.050 1 174 50 126 ILE CA C 60.030 0.050 1 175 50 126 ILE CB C 39.040 0.050 1 176 50 126 ILE N N 121.410 0.050 1 177 51 127 PHE H H 9.380 0.005 1 178 51 127 PHE C C 174.580 0.050 1 179 51 127 PHE CA C 55.760 0.050 1 180 51 127 PHE CB C 42.040 0.050 1 181 51 127 PHE N N 126.670 0.050 1 182 52 128 ARG H H 8.910 0.005 1 183 52 128 ARG C C 175.920 0.050 1 184 52 128 ARG CA C 55.040 0.050 1 185 52 128 ARG CB C 31.500 0.050 1 186 52 128 ARG N N 123.160 0.050 1 187 53 129 ILE H H 8.820 0.005 1 188 53 129 ILE C C 173.460 0.050 1 189 53 129 ILE CA C 58.690 0.050 1 190 53 129 ILE CB C 42.040 0.050 1 191 53 129 ILE N N 118.850 0.050 1 192 54 130 ALA H H 8.640 0.005 1 193 54 130 ALA C C 177.230 0.050 1 194 54 130 ALA CA C 49.680 0.050 1 195 54 130 ALA CB C 21.740 0.050 1 196 54 130 ALA N N 125.660 0.050 1 197 55 131 THR H H 9.760 0.005 1 198 55 131 THR C C 174.100 0.050 1 199 55 131 THR CA C 58.710 0.050 1 200 55 131 THR CB C 68.680 0.050 1 201 55 131 THR N N 114.710 0.050 1 202 56 132 PRO CB C 31.360 0.050 1 203 57 133 HIS H H 7.290 0.005 1 204 57 133 HIS C C 173.220 0.050 1 205 57 133 HIS CA C 52.910 0.050 1 206 57 133 HIS CB C 31.470 0.050 1 207 57 133 HIS N N 113.610 0.050 1 208 58 134 SER C C 177.460 0.050 1 209 58 134 SER CA C 57.790 0.050 1 210 58 134 SER CB C 61.870 0.050 1 211 59 135 LEU H H 8.240 0.005 1 212 59 135 LEU C C 179.430 0.050 1 213 59 135 LEU CA C 56.150 0.050 1 214 59 135 LEU CB C 40.380 0.050 1 215 59 135 LEU N N 126.930 0.050 1 216 60 136 GLY H H 7.610 0.005 1 217 60 136 GLY C C 173.770 0.050 1 218 60 136 GLY CA C 44.380 0.050 1 219 60 136 GLY N N 105.950 0.050 1 220 61 137 SER H H 8.300 0.005 1 221 61 137 SER C C 173.800 0.050 1 222 61 137 SER CA C 59.560 0.050 1 223 61 137 SER CB C 62.730 0.050 1 224 61 137 SER N N 116.890 0.050 1 225 62 138 VAL H H 8.450 0.005 1 226 62 138 VAL C C 175.450 0.050 1 227 62 138 VAL CA C 62.820 0.050 1 228 62 138 VAL CB C 30.640 0.050 1 229 62 138 VAL N N 127.320 0.050 1 230 63 139 TRP H H 8.440 0.005 1 231 63 139 TRP C C 175.750 0.050 1 232 63 139 TRP CA C 55.780 0.050 1 233 63 139 TRP N N 126.570 0.050 1 234 64 140 LYS H H 7.330 0.005 1 235 64 140 LYS C C 172.870 0.050 1 236 64 140 LYS CB C 33.160 0.050 1 237 64 140 LYS N N 124.080 0.050 1 238 65 141 ILE H H 8.220 0.005 1 239 65 141 ILE C C 173.950 0.050 1 240 65 141 ILE CA C 58.620 0.050 1 241 65 141 ILE CB C 40.420 0.050 1 242 65 141 ILE N N 115.880 0.050 1 243 66 142 ARG H H 8.510 0.005 1 244 66 142 ARG C C 173.220 0.050 1 245 66 142 ARG CA C 54.990 0.050 1 246 66 142 ARG N N 122.240 0.050 1 247 67 143 VAL H H 8.990 0.005 1 248 67 143 VAL C C 172.870 0.050 1 249 67 143 VAL CA C 58.440 0.050 1 250 67 143 VAL CB C 34.630 0.050 1 251 67 143 VAL N N 125.040 0.050 1 252 68 144 TRP H H 8.330 0.005 1 253 68 144 TRP C C 173.690 0.050 1 254 68 144 TRP CA C 55.940 0.050 1 255 68 144 TRP CB C 32.880 0.050 1 256 68 144 TRP N N 123.190 0.050 1 257 69 145 HIS H H 8.510 0.005 1 258 69 145 HIS C C 174.540 0.050 1 259 69 145 HIS CA C 54.600 0.050 1 260 69 145 HIS CB C 33.960 0.050 1 261 69 145 HIS N N 112.560 0.050 1 262 70 146 ASP H H 8.070 0.005 1 263 70 146 ASP C C 177.640 0.050 1 264 70 146 ASP CA C 52.710 0.050 1 265 70 146 ASP CB C 40.500 0.050 1 266 70 146 ASP N N 117.750 0.050 1 267 71 147 ASN C C 175.620 0.050 1 268 71 147 ASN CB C 40.750 0.050 1 269 72 148 LYS H H 6.870 0.005 1 270 72 148 LYS C C 177.220 0.050 1 271 72 148 LYS CA C 55.780 0.050 1 272 72 148 LYS CB C 33.990 0.050 1 273 72 148 LYS N N 116.910 0.050 1 274 73 149 GLY H H 8.210 0.005 1 275 73 149 GLY C C 174.860 0.050 1 276 73 149 GLY CA C 43.955 0.050 1 277 73 149 GLY N N 105.930 0.050 1 278 74 150 LEU H H 8.330 0.005 1 279 74 150 LEU C C 178.460 0.050 1 280 74 150 LEU CA C 56.210 0.050 1 281 74 150 LEU CB C 43.190 0.050 1 282 74 150 LEU N N 116.630 0.050 1 283 75 151 SER H H 8.010 0.005 1 284 75 151 SER C C 179.000 0.050 1 285 75 151 SER CA C 54.430 0.050 1 286 75 151 SER CB C 61.890 0.050 1 287 75 151 SER N N 113.350 0.050 1 288 76 152 PRO C C 177.900 0.050 1 289 76 152 PRO CB C 31.250 0.050 1 290 77 153 ALA H H 7.690 0.005 1 291 77 153 ALA C C 176.360 0.050 1 292 77 153 ALA CA C 54.150 0.050 1 293 77 153 ALA CB C 18.180 0.050 1 294 77 153 ALA N N 121.030 0.050 1 295 78 154 TRP H H 7.730 0.005 1 296 78 154 TRP C C 175.030 0.050 1 297 78 154 TRP CA C 51.860 0.050 1 298 78 154 TRP CB C 34.090 0.050 1 299 78 154 TRP N N 121.520 0.050 1 300 79 155 PHE H H 9.220 0.005 1 301 79 155 PHE C C 172.420 0.050 1 302 79 155 PHE CA C 56.750 0.050 1 303 79 155 PHE CB C 36.240 0.050 1 304 79 155 PHE N N 131.910 0.050 1 305 80 156 LEU H H 7.000 0.005 1 306 80 156 LEU C C 175.740 0.050 1 307 80 156 LEU CA C 55.220 0.050 1 308 80 156 LEU CB C 41.600 0.050 1 309 80 156 LEU N N 132.350 0.050 1 310 81 157 GLN C C 176.310 0.050 1 311 81 157 GLN CB C 28.770 0.050 1 312 82 158 HIS H H 7.180 0.005 1 313 82 158 HIS C C 171.780 0.050 1 314 82 158 HIS CA C 55.260 0.050 1 315 82 158 HIS CB C 33.420 0.050 1 316 82 158 HIS N N 110.950 0.050 1 317 83 159 VAL H H 8.810 0.005 1 318 83 159 VAL C C 172.500 0.050 1 319 83 159 VAL CA C 59.630 0.050 1 320 83 159 VAL CB C 35.600 0.050 1 321 83 159 VAL N N 119.200 0.050 1 322 84 160 ILE H H 9.570 0.005 1 323 84 160 ILE C C 175.400 0.050 1 324 84 160 ILE CA C 59.630 0.050 1 325 84 160 ILE CB C 40.820 0.050 1 326 84 160 ILE N N 127.850 0.050 1 327 85 161 VAL H H 9.160 0.005 1 328 85 161 VAL C C 175.410 0.050 1 329 85 161 VAL CA C 60.530 0.050 1 330 85 161 VAL CB C 34.560 0.050 1 331 85 161 VAL N N 125.990 0.050 1 332 86 162 ARG H H 10.040 0.005 1 333 86 162 ARG C C 174.500 0.050 1 334 86 162 ARG CA C 54.840 0.050 1 335 86 162 ARG CB C 31.650 0.050 1 336 86 162 ARG N N 130.180 0.050 1 337 87 163 ASP H H 8.540 0.005 1 338 87 163 ASP C C 177.270 0.050 1 339 87 163 ASP CA C 53.020 0.050 1 340 87 163 ASP CB C 41.990 0.050 1 341 87 163 ASP N N 126.520 0.050 1 342 88 164 LEU H H 7.300 0.005 1 343 88 164 LEU C C 177.720 0.050 1 344 88 164 LEU CA C 56.160 0.050 1 345 88 164 LEU CB C 38.490 0.050 1 346 88 164 LEU N N 125.580 0.050 1 347 89 165 GLN H H 9.070 0.005 1 348 89 165 GLN C C 177.620 0.050 1 349 89 165 GLN CA C 59.210 0.050 1 350 89 165 GLN CB C 28.270 0.050 1 351 89 165 GLN N N 118.770 0.050 1 352 90 166 THR H H 7.600 0.005 1 353 90 166 THR C C 175.320 0.050 1 354 90 166 THR CA C 61.220 0.050 1 355 90 166 THR CB C 70.490 0.050 1 356 90 166 THR N N 109.010 0.050 1 357 91 167 ALA H H 8.210 0.005 1 358 91 167 ALA C C 176.370 0.050 1 359 91 167 ALA CA C 53.430 0.050 1 360 91 167 ALA CB C 16.430 0.050 1 361 91 167 ALA N N 121.500 0.050 1 362 92 168 ARG H H 7.580 0.005 1 363 92 168 ARG C C 176.570 0.050 1 364 92 168 ARG CA C 55.900 0.050 1 365 92 168 ARG CB C 31.120 0.050 1 366 92 168 ARG N N 119.730 0.050 1 367 93 169 SER H H 8.820 0.005 1 368 93 169 SER C C 172.140 0.050 1 369 93 169 SER CA C 57.370 0.050 1 370 93 169 SER CB C 65.590 0.050 1 371 93 169 SER N N 119.960 0.050 1 372 94 170 ALA H H 8.780 0.005 1 373 94 170 ALA C C 173.900 0.050 1 374 94 170 ALA CA C 50.570 0.050 1 375 94 170 ALA CB C 22.280 0.050 1 376 94 170 ALA N N 127.110 0.050 1 377 95 171 PHE H H 8.650 0.005 1 378 95 171 PHE C C 172.880 0.050 1 379 95 171 PHE CA C 56.630 0.050 1 380 95 171 PHE CB C 41.880 0.050 1 381 95 171 PHE N N 123.180 0.050 1 382 96 172 PHE H H 8.840 0.005 1 383 96 172 PHE C C 173.740 0.050 1 384 96 172 PHE CA C 56.270 0.050 1 385 96 172 PHE CB C 38.310 0.050 1 386 96 172 PHE N N 123.470 0.050 1 387 97 173 LEU H H 8.960 0.005 1 388 97 173 LEU C C 175.250 0.050 1 389 97 173 LEU CA C 54.630 0.050 1 390 97 173 LEU CB C 40.270 0.050 1 391 97 173 LEU N N 127.500 0.050 1 392 98 174 VAL H H 7.650 0.005 1 393 98 174 VAL C C 174.180 0.050 1 394 98 174 VAL CA C 63.780 0.050 1 395 98 174 VAL N N 125.620 0.050 1 396 99 175 ASN H H 8.690 0.005 1 397 99 175 ASN C C 172.960 0.050 1 398 99 175 ASN CA C 53.360 0.050 1 399 99 175 ASN CB C 37.410 0.050 1 400 99 175 ASN N N 121.450 0.050 1 401 100 176 ASP H H 6.960 0.005 1 402 100 176 ASP C C 173.220 0.050 1 403 100 176 ASP CA C 51.930 0.050 1 404 100 176 ASP CB C 43.710 0.050 1 405 100 176 ASP N N 115.670 0.050 1 406 101 177 TRP H H 8.380 0.005 1 407 101 177 TRP C C 177.300 0.050 1 408 101 177 TRP CA C 55.960 0.050 1 409 101 177 TRP CB C 30.450 0.050 1 410 101 177 TRP N N 118.780 0.050 1 411 102 178 LEU H H 9.990 0.005 1 412 102 178 LEU C C 176.790 0.050 1 413 102 178 LEU CA C 56.170 0.050 1 414 102 178 LEU CB C 40.810 0.050 1 415 102 178 LEU N N 126.550 0.050 1 416 103 179 SER H H 8.630 0.005 1 417 103 179 SER C C 172.720 0.050 1 418 103 179 SER CA C 56.630 0.050 1 419 103 179 SER CB C 65.520 0.050 1 420 103 179 SER N N 121.320 0.050 1 421 104 180 VAL H H 8.920 0.005 1 422 104 180 VAL C C 175.510 0.050 1 423 104 180 VAL CA C 61.760 0.050 1 424 104 180 VAL CB C 32.780 0.050 1 425 104 180 VAL N N 123.020 0.050 1 426 105 181 GLU H H 8.620 0.005 1 427 105 181 GLU C C 176.810 0.050 1 428 105 181 GLU CA C 56.770 0.050 1 429 105 181 GLU CB C 29.720 0.050 1 430 105 181 GLU N N 125.760 0.050 1 431 106 182 THR H H 8.000 0.005 1 432 106 182 THR C C 174.420 0.050 1 433 106 182 THR CA C 61.730 0.050 1 434 106 182 THR CB C 69.200 0.050 1 435 106 182 THR N N 114.700 0.050 1 436 107 183 GLU H H 8.280 0.005 1 437 107 183 GLU C C 176.160 0.050 1 438 107 183 GLU CA C 56.220 0.050 1 439 107 183 GLU CB C 29.455 0.050 1 440 107 183 GLU N N 122.550 0.050 1 441 108 184 ALA H H 8.210 0.005 1 442 108 184 ALA C C 177.900 0.050 1 443 108 184 ALA CA C 52.530 0.050 1 444 108 184 ALA CB C 18.350 0.050 1 445 108 184 ALA N N 125.040 0.050 1 446 109 185 ASN H H 8.440 0.005 1 447 109 185 ASN C C 175.800 0.050 1 448 109 185 ASN CA C 53.250 0.050 1 449 109 185 ASN CB C 38.090 0.050 1 450 109 185 ASN N N 118.570 0.050 1 451 110 186 GLY H H 8.370 0.005 1 452 110 186 GLY C C 174.670 0.050 1 453 110 186 GLY CA C 45.220 0.050 1 454 110 186 GLY N N 110.270 0.050 1 455 111 187 GLY H H 8.100 0.005 1 456 111 187 GLY C C 173.005 0.050 1 457 111 187 GLY CA C 44.920 0.050 1 458 111 187 GLY N N 109.650 0.050 1 459 112 188 LEU H H 7.570 0.005 1 460 112 188 LEU C C 176.450 0.050 1 461 112 188 LEU CA C 53.890 0.050 1 462 112 188 LEU CB C 42.640 0.050 1 463 112 188 LEU N N 119.090 0.050 1 464 113 189 VAL H H 8.420 0.005 1 465 113 189 VAL C C 174.060 0.050 1 466 113 189 VAL CA C 61.330 0.050 1 467 113 189 VAL CB C 30.650 0.050 1 468 113 189 VAL N N 125.150 0.050 1 469 114 190 GLU H H 8.160 0.005 1 470 114 190 GLU C C 176.055 0.050 1 471 114 190 GLU CA C 53.970 0.050 1 472 114 190 GLU CB C 34.310 0.050 1 473 114 190 GLU N N 122.620 0.050 1 474 115 191 LYS H H 9.210 0.005 1 475 115 191 LYS C C 174.200 0.050 1 476 115 191 LYS CA C 55.270 0.050 1 477 115 191 LYS CB C 36.110 0.050 1 478 115 191 LYS N N 122.830 0.050 1 479 116 192 GLU H H 8.670 0.005 1 480 116 192 GLU C C 176.030 0.050 1 481 116 192 GLU CA C 54.760 0.050 1 482 116 192 GLU CB C 31.210 0.050 1 483 116 192 GLU N N 125.690 0.050 1 484 117 193 VAL H H 8.660 0.005 1 485 117 193 VAL C C 174.140 0.050 1 486 117 193 VAL CA C 60.560 0.050 1 487 117 193 VAL CB C 34.060 0.050 1 488 117 193 VAL N N 123.530 0.050 1 489 118 194 LEU H H 8.720 0.005 1 490 118 194 LEU C C 176.970 0.050 1 491 118 194 LEU CA C 53.900 0.050 1 492 118 194 LEU CB C 42.110 0.050 1 493 118 194 LEU N N 127.990 0.050 1 494 119 195 ALA H H 7.560 0.005 1 495 119 195 ALA C C 178.010 0.050 1 496 119 195 ALA CA C 51.900 0.050 1 497 119 195 ALA CB C 17.740 0.050 1 498 119 195 ALA N N 123.850 0.050 1 499 120 196 ALA H H 8.690 0.005 1 500 120 196 ALA C C 178.030 0.050 1 501 120 196 ALA CA C 51.770 0.050 1 502 120 196 ALA CB C 18.680 0.050 1 503 120 196 ALA N N 125.750 0.050 1 504 121 197 SER H H 8.440 0.005 1 505 121 197 SER C C 174.170 0.050 1 506 121 197 SER CA C 57.120 0.050 1 507 121 197 SER CB C 64.340 0.050 1 508 121 197 SER N N 117.560 0.050 1 509 122 198 ASP H H 8.480 0.005 1 510 122 198 ASP C C 177.990 0.050 1 511 122 198 ASP CA C 56.120 0.050 1 512 122 198 ASP CB C 39.880 0.050 1 513 122 198 ASP N N 121.660 0.050 1 514 123 199 ALA H H 8.320 0.005 1 515 123 199 ALA C C 179.700 0.050 1 516 123 199 ALA CA C 54.170 0.050 1 517 123 199 ALA CB C 17.690 0.050 1 518 123 199 ALA N N 123.660 0.050 1 519 124 200 ALA H H 7.930 0.005 1 520 124 200 ALA C C 180.020 0.050 1 521 124 200 ALA CA C 53.950 0.050 1 522 124 200 ALA CB C 17.840 0.050 1 523 124 200 ALA N N 122.100 0.050 1 524 125 201 LEU H H 7.820 0.005 1 525 125 201 LEU C C 178.310 0.050 1 526 125 201 LEU CA C 56.260 0.050 1 527 125 201 LEU CB C 40.650 0.050 1 528 125 201 LEU N N 119.570 0.050 1 529 126 202 LEU H H 7.610 0.005 1 530 126 202 LEU C C 178.850 0.050 1 531 126 202 LEU CA C 56.830 0.050 1 532 126 202 LEU CB C 40.700 0.050 1 533 126 202 LEU N N 120.400 0.050 1 534 127 203 ARG H H 7.500 0.005 1 535 127 203 ARG C C 177.410 0.050 1 536 127 203 ARG CA C 57.340 0.050 1 537 127 203 ARG CB C 29.290 0.050 1 538 127 203 ARG N N 118.280 0.050 1 539 128 204 PHE H H 7.750 0.005 1 540 128 204 PHE C C 176.570 0.050 1 541 128 204 PHE CA C 58.860 0.050 1 542 128 204 PHE CB C 38.640 0.050 1 543 128 204 PHE N N 120.420 0.050 1 stop_ save_