data_16167 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR data for FXYD4 in micelles ; _BMRB_accession_number 16167 _BMRB_flat_file_name bmr16167.str _Entry_type original _Submission_date 2009-02-11 _Accession_date 2009-02-11 _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 Marassi Francesca M. . 2 Franzin Carla M. . 3 Teriete Peter . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 136 "13C chemical shifts" 123 "15N chemical shifts" 60 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-10-30 update BMRB 'update entry, etc.' 2009-03-12 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16168 'STRUCTURE OF THE NA,K-ATPASE REGULATORY PROTEIN FXYD1 IN MICELLES' stop_ _Original_release_date 2009-02-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural similarity of a membrane protein in micelles and membranes. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17567018 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Franzin Carla M. . 2 Teriete Peter . . 3 Marassi Francesca M. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_volume 129 _Journal_issue 26 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 8078 _Page_last 8079 _Year 2007 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'FXYD4 monomer in micelles' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'FXYD4 subunit' $FXYD4 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_FXYD4 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FXYD4 _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'regulatory subunit of the Na,K-ATPase in kidney' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 67 _Mol_residue_sequence ; NGPVDKGSPFYYDWESLQLG GLIFGGLLCIAGIALALSGK CKCRRNHTPSSLPEKVTPLI TPGSAST ; loop_ _Residue_seq_code _Residue_label 1 ASN 2 GLY 3 PRO 4 VAL 5 ASP 6 LYS 7 GLY 8 SER 9 PRO 10 PHE 11 TYR 12 TYR 13 ASP 14 TRP 15 GLU 16 SER 17 LEU 18 GLN 19 LEU 20 GLY 21 GLY 22 LEU 23 ILE 24 PHE 25 GLY 26 GLY 27 LEU 28 LEU 29 CYS 30 ILE 31 ALA 32 GLY 33 ILE 34 ALA 35 LEU 36 ALA 37 LEU 38 SER 39 GLY 40 LYS 41 CYS 42 LYS 43 CYS 44 ARG 45 ARG 46 ASN 47 HIS 48 THR 49 PRO 50 SER 51 SER 52 LEU 53 PRO 54 GLU 55 LYS 56 VAL 57 THR 58 PRO 59 LEU 60 ILE 61 THR 62 PRO 63 GLY 64 SER 65 ALA 66 SER 67 THR 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 GB NP_071783 'FXYD4, CHIF' . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Variant $FXYD4 Rat 10116 Eukaryota Metazoa Rattus norvegicus 'ML mutant' 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 $FXYD4 'recombinant technology' . Escherichia coli C41(DE3) pET stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type 'micelle, lipid bilayers' _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $FXYD4 0.75 mM 0.5 1.0 '[U-100% 13C; U-100% 15N]' $FXYD4 0.75 mM 0.5 1.0 '[U-100% 15N]' H2O 95 % . . 'natural abundance' D2O 5 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'solution NMR spectrometer' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details 'solid-state NMR spectrometer' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 20 . mM pH 5 . pH pressure 1 . atm temperature 313 . 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 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' '3D HNCA' '3D HNCACB' 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 'FXYD4 subunit' _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 1 ASN HA H 4.547 . . 2 1 1 ASN CA C 53.185 . . 3 1 1 ASN CB C 38.020 . . 4 2 2 GLY H H 8.525 . 1 5 2 2 GLY HA2 H 4.295 . . 6 2 2 GLY HA3 H 4.295 . . 7 2 2 GLY CA C 45.194 . . 8 2 2 GLY N N 109.434 . . 9 3 3 PRO HA H 4.549 . . 10 3 3 PRO CA C 64.249 . . 11 3 3 PRO CB C 32.230 . . 12 4 4 VAL H H 7.854 . 1 13 4 4 VAL HA H 4.183 . . 14 4 4 VAL CA C 62.934 . . 15 4 4 VAL CB C 32.660 . . 16 4 4 VAL N N 117.083 . . 17 5 5 ASP H H 8.160 . 1 18 5 5 ASP HA H 4.734 . . 19 5 5 ASP CA C 54.120 . . 20 5 5 ASP CB C 40.560 . . 21 5 5 ASP N N 122.006 . . 22 6 6 LYS H H 8.101 . 1 23 6 6 LYS HA H 4.256 . . 24 6 6 LYS CA C 57.127 . . 25 6 6 LYS CB C 32.990 . . 26 6 6 LYS N N 120.893 . . 27 7 7 GLY H H 8.268 . 1 28 7 7 GLY HA2 H 4.059 . . 29 7 7 GLY HA3 H 4.059 . . 30 7 7 GLY CA C 45.593 . . 31 7 7 GLY N N 108.006 . . 32 8 8 SER H H 7.885 . 1 33 8 8 SER HA H 4.783 . . 34 8 8 SER CA C 57.002 . . 35 8 8 SER CB C 64.180 . . 36 8 8 SER N N 115.797 . . 37 9 9 PRO HA H 4.470 . . 38 9 9 PRO CA C 64.184 . . 39 9 9 PRO CB C 32.130 . . 40 10 10 PHE H H 7.876 . 1 41 10 10 PHE HA H 4.617 . . 42 10 10 PHE CA C 59.080 . . 43 10 10 PHE CB C 39.360 . . 44 10 10 PHE N N 117.498 . . 45 11 11 TYR H H 7.397 . 1 46 11 11 TYR HA H 4.293 . . 47 11 11 TYR CA C 58.921 . . 48 11 11 TYR CB C 38.460 . . 49 11 11 TYR N N 118.430 . . 50 12 12 TYR H H 7.426 . 1 51 12 12 TYR HA H 4.343 . . 52 12 12 TYR CA C 58.921 . . 53 12 12 TYR CB C 38.810 . . 54 12 12 TYR N N 119.816 . . 55 13 13 ASP H H 7.946 . 1 56 13 13 ASP HA H 4.714 . . 57 13 13 ASP CA C 53.888 . . 58 13 13 ASP CB C 38.720 . . 59 13 13 ASP N N 119.791 . . 60 14 14 TRP H H 7.898 . 1 61 14 14 TRP HA H 4.412 . . 62 14 14 TRP CA C 58.926 . . 63 14 14 TRP CB C 29.560 . . 64 14 14 TRP N N 122.157 . . 65 15 15 GLU H H 8.068 . 1 66 15 15 GLU HA H 4.170 . . 67 15 15 GLU CA C 57.790 . . 68 15 15 GLU CB C 28.560 . . 69 15 15 GLU N N 117.706 . . 70 16 16 SER H H 7.839 . 1 71 16 16 SER HA H 4.476 . . 72 16 16 SER CA C 59.602 . . 73 16 16 SER CB C 64.270 . . 74 16 16 SER N N 114.103 . . 75 17 17 LEU H H 7.767 . 1 76 17 17 LEU HA H 4.092 . . 77 17 17 LEU CA C 56.227 . . 78 17 17 LEU CB C 42.740 . . 79 17 17 LEU N N 122.451 . . 80 18 18 GLN H H 8.116 . 1 81 18 18 GLN HA H 4.301 . . 82 18 18 GLN CA C 57.390 . . 83 18 18 GLN CB C 28.940 . . 84 18 18 GLN N N 119.059 . . 85 19 19 LEU H H 7.981 . 1 86 19 19 LEU HA H 4.343 . . 87 19 19 LEU CA C 56.891 . . 88 19 19 LEU CB C 42.490 . . 89 19 19 LEU N N 120.130 . . 90 20 20 GLY H H 8.229 . 1 91 20 20 GLY HA2 H 3.917 . . 92 20 20 GLY HA3 H 3.917 . . 93 20 20 GLY CA C 47.422 . . 94 20 20 GLY N N 105.581 . . 95 21 21 GLY H H 8.257 . 1 96 21 21 GLY HA2 H 3.984 . . 97 21 21 GLY HA3 H 3.984 . . 98 21 21 GLY CA C 47.644 . . 99 21 21 GLY N N 107.420 . . 100 22 22 LEU H H 7.931 . 1 101 22 22 LEU HA H 4.245 . . 102 22 22 LEU CA C 58.433 . . 103 22 22 LEU CB C 42.370 . . 104 22 22 LEU N N 120.980 . . 105 23 23 ILE H H 8.119 . 1 106 23 23 ILE HA H 3.794 . . 107 23 23 ILE CA C 65.285 . . 108 23 23 ILE N N 117.257 . . 109 24 24 PHE H H 8.251 . 1 110 24 24 PHE HA H 4.317 . . 111 24 24 PHE CA C 61.466 . . 112 24 24 PHE CB C 39.630 . . 113 24 24 PHE N N 118.423 . . 114 25 25 GLY H H 8.731 . 1 115 25 25 GLY HA2 H 3.712 . . 116 25 25 GLY HA3 H 3.712 . . 117 25 25 GLY CA C 47.650 . . 118 25 25 GLY N N 104.808 . . 119 26 26 GLY H H 8.676 . 1 120 26 26 GLY HA2 H 3.740 . . 121 26 26 GLY HA3 H 3.740 . . 122 26 26 GLY CA C 47.847 . . 123 26 26 GLY N N 109.323 . . 124 27 27 LEU H H 8.405 . 1 125 27 27 LEU HA H 3.699 . . 126 27 27 LEU CA C 58.500 . . 127 27 27 LEU CB C 41.930 . . 128 27 27 LEU N N 121.344 . . 129 28 28 LEU H H 8.073 . 1 130 28 28 LEU HA H 3.948 . . 131 28 28 LEU CA C 58.425 . . 132 28 28 LEU CB C 41.690 . . 133 28 28 LEU N N 118.260 . . 134 29 29 CYS H H 8.008 . 1 135 29 29 CYS HA H 4.103 . . 136 29 29 CYS CA C 64.411 . . 137 29 29 CYS N N 116.229 . . 138 30 30 ILE H H 8.217 . 1 139 30 30 ILE HA H 3.653 . . 140 30 30 ILE CA C 65.665 . . 141 30 30 ILE CB C 37.490 . . 142 30 30 ILE N N 118.426 . . 143 31 31 ALA H H 8.586 . 1 144 31 31 ALA HA H 3.994 . . 145 31 31 ALA CA C 55.685 . . 146 31 31 ALA CB C 17.870 . . 147 31 31 ALA N N 121.322 . . 148 32 32 GLY H H 8.674 . 1 149 32 32 GLY HA2 H 3.700 . . 150 32 32 GLY HA3 H 3.700 . . 151 32 32 GLY CA C 47.932 . . 152 32 32 GLY N N 104.616 . . 153 33 33 ILE H H 8.449 . 1 154 33 33 ILE HA H 3.719 . . 155 33 33 ILE CA C 66.057 . . 156 33 33 ILE CB C 38.060 . . 157 33 33 ILE N N 121.743 . . 158 34 34 ALA H H 8.657 . 1 159 34 34 ALA HA H 4.031 . . 160 34 34 ALA CA C 55.914 . . 161 34 34 ALA CB C 18.490 . . 162 34 34 ALA N N 121.516 . . 163 35 35 LEU H H 8.741 . 1 164 35 35 LEU HA H 4.028 . . 165 35 35 LEU CA C 58.299 . . 166 35 35 LEU CB C 42.180 . . 167 35 35 LEU N N 118.557 . . 168 36 36 ALA H H 8.533 . 1 169 36 36 ALA HA H 4.284 . . 170 36 36 ALA CA C 55.480 . . 171 36 36 ALA CB C 18.720 . . 172 36 36 ALA N N 123.154 . . 173 37 37 LEU H H 8.754 . 1 174 37 37 LEU HA H 4.246 . . 175 37 37 LEU CA C 57.347 . . 176 37 37 LEU CB C 42.370 . . 177 37 37 LEU N N 117.400 . . 178 38 38 SER H H 8.086 . 1 179 38 38 SER HA H 4.416 . . 180 38 38 SER CA C 60.698 . . 181 38 38 SER CB C 64.400 . . 182 38 38 SER N N 112.848 . . 183 39 39 GLY H H 7.966 . 1 184 39 39 GLY HA2 H 4.171 . . 185 39 39 GLY HA3 H 4.171 . . 186 39 39 GLY CA C 46.592 . . 187 39 39 GLY N N 109.679 . . 188 40 40 LYS H H 8.084 . 1 189 40 40 LYS HA H 4.369 . . 190 40 40 LYS CA C 57.421 . . 191 40 40 LYS CB C 33.400 . . 192 40 40 LYS N N 119.316 . . 193 41 41 CYS H H 8.175 . 1 194 41 41 CYS HA H 4.553 . . 195 41 41 CYS CA C 59.606 . . 196 41 41 CYS CB C 28.320 . . 197 41 41 CYS N N 115.777 . . 198 42 42 LYS H H 8.038 . 1 199 42 42 LYS HA H 4.089 . . 200 42 42 LYS CA C 57.218 . . 201 42 42 LYS CB C 32.990 . . 202 42 42 LYS N N 121.228 . . 203 43 43 CYS H H 8.101 . 1 204 43 43 CYS HA H 4.542 . . 205 43 43 CYS CA C 59.627 . . 206 43 43 CYS CB C 27.890 . . 207 43 43 CYS N N 117.640 . . 208 44 44 ARG H H 8.101 . 1 209 44 44 ARG HA H 4.420 . . 210 44 44 ARG CA C 57.127 . . 211 44 44 ARG CB C 30.900 . . 212 44 44 ARG N N 120.893 . . 213 45 45 ARG H H 8.021 . 1 214 45 45 ARG HA H 4.389 . . 215 45 45 ARG CA C 56.652 . . 216 45 45 ARG CB C 30.730 . . 217 45 45 ARG N N 118.963 . . 218 46 46 ASN H H 8.203 . 1 219 46 46 ASN HA H 4.767 . . 220 46 46 ASN CA C 53.723 . . 221 46 46 ASN CB C 39.270 . . 222 46 46 ASN N N 117.580 . . 223 47 47 HIS H H 8.218 . 1 224 47 47 HIS HA H 4.874 . . 225 47 47 HIS CA C 55.485 . . 226 47 47 HIS CB C 29.250 . . 227 47 47 HIS N N 117.820 . . 228 48 48 THR H H 8.136 . 1 229 48 48 THR HA H 4.278 . . 230 48 48 THR CA C 60.038 . . 231 48 48 THR CB C 70.070 . . 232 48 48 THR N N 116.184 . . 233 49 49 PRO HA H 4.621 . . 234 49 49 PRO CA C 63.826 . . 235 49 49 PRO CB C 32.080 . . 236 50 50 SER H H 8.323 . 1 237 50 50 SER HA H 4.535 . . 238 50 50 SER CA C 59.133 . . 239 50 50 SER CB C 64.290 . . 240 50 50 SER N N 115.177 . . 241 51 51 SER H H 8.136 . 1 242 51 51 SER HA H 4.689 . . 243 51 51 SER CA C 58.434 . . 244 51 51 SER CB C 64.500 . . 245 51 51 SER N N 116.184 . . 246 52 52 LEU H H 8.198 . 1 247 52 52 LEU HA H 4.515 . . 248 52 52 LEU CA C 56.647 . . 249 52 52 LEU CB C 41.130 . . 250 52 52 LEU N N 122.316 . . 251 53 53 PRO HA H 4.409 . . 252 53 53 PRO CA C 65.350 . . 253 53 53 PRO CB C 31.600 . . 254 54 54 GLU H H 7.995 . 1 255 54 54 GLU HA H 4.277 . . 256 54 54 GLU CA C 58.200 . . 257 54 54 GLU CB C 28.970 . . 258 54 54 GLU N N 117.669 . . 259 55 55 LYS H H 8.047 . 1 260 55 55 LYS HA H 4.353 . . 261 55 55 LYS CA C 57.687 . . 262 55 55 LYS CB C 33.410 . . 263 55 55 LYS N N 117.513 . . 264 56 56 VAL H H 7.722 . 1 265 56 56 VAL HA H 4.301 . . 266 56 56 VAL CA C 63.111 . . 267 56 56 VAL CB C 33.410 . . 268 56 56 VAL N N 113.389 . . 269 57 57 THR H H 7.885 . 1 270 57 57 THR HA H 4.288 . . 271 57 57 THR CA C 65.930 . . 272 57 57 THR CB C 70.230 . . 273 57 57 THR N N 115.797 . . 274 58 58 PRO HA H 4.526 . . 275 58 58 PRO CA C 65.111 . . 276 58 58 PRO CB C 31.600 . . 277 59 59 LEU H H 7.744 . 1 278 59 59 LEU HA H 4.367 . . 279 59 59 LEU CA C 56.267 . . 280 59 59 LEU CB C 42.760 . . 281 59 59 LEU N N 116.041 . . 282 60 60 ILE H H 7.450 . 1 283 60 60 ILE HA H 4.411 . . 284 60 60 ILE CA C 61.040 . . 285 60 60 ILE CB C 39.310 . . 286 60 60 ILE N N 114.245 . . 287 61 61 THR H H 7.861 . 1 288 61 61 THR HA H 4.215 . . 289 61 61 THR CA C 59.556 . . 290 61 61 THR CB C 70.240 . . 291 61 61 THR N N 116.433 . . 292 62 62 PRO HA H 4.564 . . 293 62 62 PRO CA C 63.858 . . 294 62 62 PRO CB C 32.170 . . 295 63 63 GLY H H 8.445 . 1 296 63 63 GLY HA2 H 4.095 . . 297 63 63 GLY HA3 H 4.095 . . 298 63 63 GLY CA C 45.746 . . 299 63 63 GLY N N 109.077 . . 300 64 64 SER H H 8.097 . 1 301 64 64 SER HA H 4.547 . . 302 64 64 SER CA C 58.689 . . 303 64 64 SER CB C 64.320 . . 304 64 64 SER N N 115.238 . . 305 65 65 ALA H H 8.271 . 1 306 65 65 ALA HA H 4.516 . . 307 65 65 ALA CA C 52.738 . . 308 65 65 ALA CB C 19.580 . . 309 65 65 ALA N N 125.566 . . 310 66 66 SER H H 8.224 . 1 311 66 66 SER HA H 4.633 . . 312 66 66 SER CA C 58.527 . . 313 66 66 SER CB C 64.320 . . 314 66 66 SER N N 115.270 . . 315 67 67 THR H H 7.808 . 1 316 67 67 THR HA H 4.305 . . 317 67 67 THR CA C 63.208 . . 318 67 67 THR CB C 71.100 . . 319 67 67 THR N N 120.218 . . stop_ save_