data_30437 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of SH3 domain from Shank2 ; _BMRB_accession_number 30437 _BMRB_flat_file_name bmr30437.str _Entry_type original _Submission_date 2018-03-13 _Accession_date 2018-03-13 _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 Ishida H. . . 2 Vogel H. J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 55 "13C chemical shifts" 173 "15N chemical shifts" 55 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-05-03 update BMRB 'update entry citation' 2018-08-07 original author 'original release' stop_ _Original_release_date 2018-04-16 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structures of the SH3 domains from Shank scaffold proteins and their interactions with Cav1.3 calcium channels ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30058071 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ishida Hiroaki . . 2 Skorobogatov Anton . . 3 Yamniuk Aaron P. . 4 Vogel Hans J. . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_name_full 'FEBS letters' _Journal_volume 592 _Journal_issue 16 _Journal_ISSN 1873-3468 _Journal_CSD 0353 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2786 _Page_last 2797 _Year 2018 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'SH3 and multiple ankyrin repeat domains protein 2' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $entity_1 stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 6741.667 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 61 _Mol_residue_sequence ; MVPGRLFVAIKPYQPQVDGE IPLHRGDRVKVLSIGEGGFW EGSARGHIGWFPAECVEEVQ S ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 525 MET 2 526 VAL 3 527 PRO 4 528 GLY 5 529 ARG 6 530 LEU 7 531 PHE 8 532 VAL 9 533 ALA 10 534 ILE 11 535 LYS 12 536 PRO 13 537 TYR 14 538 GLN 15 539 PRO 16 540 GLN 17 541 VAL 18 542 ASP 19 543 GLY 20 544 GLU 21 545 ILE 22 546 PRO 23 547 LEU 24 548 HIS 25 549 ARG 26 550 GLY 27 551 ASP 28 552 ARG 29 553 VAL 30 554 LYS 31 555 VAL 32 556 LEU 33 557 SER 34 558 ILE 35 559 GLY 36 560 GLU 37 561 GLY 38 562 GLY 39 563 PHE 40 564 TRP 41 565 GLU 42 566 GLY 43 567 SER 44 568 ALA 45 569 ARG 46 570 GLY 47 571 HIS 48 572 ILE 49 573 GLY 50 574 TRP 51 575 PHE 52 576 PRO 53 577 ALA 54 578 GLU 55 579 CYS 56 580 VAL 57 581 GLU 58 582 GLU 59 583 VAL 60 584 GLN 61 585 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $entity_1 Rat 10116 Eukaryota Metazoa Rattus norvegicus 'Shank2, Cortbp1' 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 $entity_1 'recombinant technology' . Escherichia coli . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1 mM [U-99% 13C; U-99% 15N] Shank2 SH3, 20 mM Bis-Tris, 100 mM KCl, 90% H2O/10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1 mM '[U-99% 13C; U-99% 15N]' Bis-Tris 20 mM 'natural abundance' KCl 100 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details '1 mM [U-99% 13C; U-99% 15N] Shank2 SH3, 20 mM Bis-Tris, 100 mM KCl, 100% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1 mM '[U-99% 13C; U-99% 15N]' Bis-Tris 20 mM 'natural abundance' KCl 100 mM 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details '1 mM [U-99% 13C; U-99% 15N] Shank2 SH3, 20 mM Bis-Tris, 100 mM KCl, 90% H2O/10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1 mM '[U-99% 13C; U-99% 15N]' Bis-Tris 20 mM 'natural abundance' KCl 100 mM 'natural abundance' stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details '1 mM Shank2 SH3, 20 mM Bis-Tris, 100 mM KCl, 100% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1 mM 'natural abundance' Bis-Tris 20 mM 'natural abundance' KCl 100 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_software_2 _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name CYANA _Version 2.0 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure calculation' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _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_3 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_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_2 save_ save_2D_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_4 save_ save_3D_1H-15N_NOESY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_3 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' 100 . mM pH 6.8 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 internal indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0 internal 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D HNCO' '3D HN(CA)CO' '3D H(CCO)NH' '3D C(CO)NH' '3D HBHA(CO)NH' '3D 1H-13C NOESY' '2D NOESY' '3D 1H-15N NOESY' stop_ loop_ _Sample_label $sample_3 $sample_1 $sample_2 $sample_4 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name entity_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 1 525 1 MET C C 175.459 . . 2 525 1 MET CA C 55.210 . . 3 525 1 MET CB C 32.942 . . 4 526 2 VAL H H 8.371 . . 5 526 2 VAL C C 174.253 . . 6 526 2 VAL CA C 60.796 . . 7 526 2 VAL CB C 32.652 . . 8 526 2 VAL N N 124.451 . . 9 527 3 PRO C C 177.357 . . 10 527 3 PRO CA C 63.706 . . 11 527 3 PRO CB C 32.038 . . 12 528 4 GLY H H 8.590 . . 13 528 4 GLY C C 174.084 . . 14 528 4 GLY CA C 45.261 . . 15 528 4 GLY N N 109.391 . . 16 529 5 ARG H H 7.928 . . 17 529 5 ARG C C 175.125 . . 18 529 5 ARG CA C 55.935 . . 19 529 5 ARG CB C 31.782 . . 20 529 5 ARG N N 120.277 . . 21 530 6 LEU H H 8.491 . . 22 530 6 LEU C C 174.948 . . 23 530 6 LEU CA C 54.633 . . 24 530 6 LEU CB C 43.805 . . 25 530 6 LEU N N 124.162 . . 26 531 7 PHE H H 8.673 . . 27 531 7 PHE C C 174.583 . . 28 531 7 PHE CA C 56.667 . . 29 531 7 PHE CB C 43.156 . . 30 531 7 PHE N N 121.679 . . 31 532 8 VAL H H 9.427 . . 32 532 8 VAL C C 174.481 . . 33 532 8 VAL CA C 58.463 . . 34 532 8 VAL CB C 35.586 . . 35 532 8 VAL N N 119.675 . . 36 533 9 ALA H H 8.961 . . 37 533 9 ALA C C 178.447 . . 38 533 9 ALA CA C 51.979 . . 39 533 9 ALA CB C 18.578 . . 40 533 9 ALA N N 127.121 . . 41 534 10 ILE H H 9.132 . . 42 534 10 ILE C C 175.248 . . 43 534 10 ILE CA C 60.789 . . 44 534 10 ILE CB C 39.106 . . 45 534 10 ILE N N 121.129 . . 46 535 11 LYS H H 7.921 . . 47 535 11 LYS C C 171.404 . . 48 535 11 LYS CA C 53.712 . . 49 535 11 LYS CB C 35.019 . . 50 535 11 LYS N N 122.366 . . 51 536 12 PRO C C 175.286 . . 52 536 12 PRO CA C 61.650 . . 53 536 12 PRO CB C 32.957 . . 54 537 13 TYR H H 8.527 . . 55 537 13 TYR C C 174.173 . . 56 537 13 TYR CA C 59.321 . . 57 537 13 TYR CB C 42.913 . . 58 537 13 TYR N N 117.694 . . 59 538 14 GLN H H 7.273 . . 60 538 14 GLN C C 171.840 . . 61 538 14 GLN CA C 51.124 . . 62 538 14 GLN CB C 29.538 . . 63 538 14 GLN N N 128.042 . . 64 539 15 PRO C C 176.837 . . 65 539 15 PRO CA C 63.108 . . 66 539 15 PRO CB C 33.537 . . 67 540 16 GLN H H 9.342 . . 68 540 16 GLN C C 175.633 . . 69 540 16 GLN CA C 55.770 . . 70 540 16 GLN CB C 31.724 . . 71 540 16 GLN N N 120.713 . . 72 541 17 VAL H H 7.124 . . 73 541 17 VAL C C 175.138 . . 74 541 17 VAL CA C 59.316 . . 75 541 17 VAL CB C 36.156 . . 76 541 17 VAL N N 113.579 . . 77 542 18 ASP H H 8.409 . . 78 542 18 ASP C C 176.840 . . 79 542 18 ASP CA C 56.294 . . 80 542 18 ASP CB C 40.862 . . 81 542 18 ASP N N 122.896 . . 82 543 19 GLY H H 8.891 . . 83 543 19 GLY C C 175.445 . . 84 543 19 GLY CA C 45.215 . . 85 543 19 GLY N N 112.676 . . 86 544 20 GLU H H 7.730 . . 87 544 20 GLU C C 177.198 . . 88 544 20 GLU CA C 55.259 . . 89 544 20 GLU CB C 32.496 . . 90 544 20 GLU N N 119.437 . . 91 545 21 ILE H H 8.506 . . 92 545 21 ILE C C 171.572 . . 93 545 21 ILE CA C 57.563 . . 94 545 21 ILE CB C 39.407 . . 95 545 21 ILE N N 114.113 . . 96 546 22 PRO C C 177.188 . . 97 546 22 PRO CA C 61.079 . . 98 546 22 PRO CB C 32.360 . . 99 547 23 LEU H H 8.423 . . 100 547 23 LEU C C 176.372 . . 101 547 23 LEU CA C 53.588 . . 102 547 23 LEU CB C 46.117 . . 103 547 23 LEU N N 116.819 . . 104 548 24 HIS H H 8.850 . . 105 548 24 HIS C C 174.575 . . 106 548 24 HIS CA C 53.761 . . 107 548 24 HIS CB C 30.608 . . 108 548 24 HIS N N 122.347 . . 109 549 25 ARG H H 8.920 . . 110 549 25 ARG C C 177.352 . . 111 549 25 ARG CA C 58.746 . . 112 549 25 ARG CB C 29.449 . . 113 549 25 ARG N N 122.633 . . 114 550 26 GLY H H 9.123 . . 115 550 26 GLY C C 174.600 . . 116 550 26 GLY CA C 44.678 . . 117 550 26 GLY N N 114.690 . . 118 551 27 ASP H H 8.289 . . 119 551 27 ASP C C 173.381 . . 120 551 27 ASP CA C 55.506 . . 121 551 27 ASP CB C 41.156 . . 122 551 27 ASP N N 121.870 . . 123 552 28 ARG H H 8.546 . . 124 552 28 ARG C C 176.325 . . 125 552 28 ARG CA C 55.804 . . 126 552 28 ARG CB C 30.019 . . 127 552 28 ARG N N 121.682 . . 128 553 29 VAL H H 8.862 . . 129 553 29 VAL C C 174.943 . . 130 553 29 VAL CA C 60.765 . . 131 553 29 VAL CB C 35.294 . . 132 553 29 VAL N N 126.563 . . 133 554 30 LYS H H 8.366 . . 134 554 30 LYS C C 175.856 . . 135 554 30 LYS CA C 54.642 . . 136 554 30 LYS CB C 33.522 . . 137 554 30 LYS N N 128.087 . . 138 555 31 VAL H H 8.898 . . 139 555 31 VAL C C 175.192 . . 140 555 31 VAL CA C 64.292 . . 141 555 31 VAL CB C 32.080 . . 142 555 31 VAL N N 127.323 . . 143 556 32 LEU H H 9.588 . . 144 556 32 LEU C C 177.350 . . 145 556 32 LEU CA C 55.520 . . 146 556 32 LEU CB C 43.798 . . 147 556 32 LEU N N 128.948 . . 148 557 33 SER H H 7.809 . . 149 557 33 SER C C 171.075 . . 150 557 33 SER CA C 57.879 . . 151 557 33 SER CB C 64.864 . . 152 557 33 SER N N 112.294 . . 153 558 34 ILE H H 8.323 . . 154 558 34 ILE C C 176.503 . . 155 558 34 ILE CA C 60.217 . . 156 558 34 ILE CB C 38.518 . . 157 558 34 ILE N N 121.482 . . 158 559 35 GLY H H 8.071 . . 159 559 35 GLY C C 173.737 . . 160 559 35 GLY CA C 44.660 . . 161 559 35 GLY N N 114.785 . . 162 560 36 GLU H H 8.494 . . 163 560 36 GLU C C 178.393 . . 164 560 36 GLU CA C 55.793 . . 165 560 36 GLU CB C 30.895 . . 166 560 36 GLU N N 119.672 . . 167 561 37 GLY H H 8.944 . . 168 561 37 GLY C C 175.304 . . 169 561 37 GLY CA C 46.429 . . 170 561 37 GLY N N 108.919 . . 171 562 38 GLY H H 8.683 . . 172 562 38 GLY C C 173.795 . . 173 562 38 GLY CA C 45.254 . . 174 562 38 GLY N N 106.604 . . 175 563 39 PHE H H 7.577 . . 176 563 39 PHE C C 174.426 . . 177 563 39 PHE CA C 57.558 . . 178 563 39 PHE CB C 41.664 . . 179 563 39 PHE N N 120.041 . . 180 564 40 TRP H H 9.042 . . 181 564 40 TRP C C 171.833 . . 182 564 40 TRP CA C 52.881 . . 183 564 40 TRP CB C 33.530 . . 184 564 40 TRP N N 123.469 . . 185 565 41 GLU H H 8.334 . . 186 565 41 GLU C C 177.217 . . 187 565 41 GLU CA C 41.955 . . 188 565 41 GLU CB C 30.900 . . 189 565 41 GLU N N 121.955 . . 190 566 42 GLY H H 9.477 . . 191 566 42 GLY C C 169.328 . . 192 566 42 GLY CA C 46.673 . . 193 566 42 GLY N N 114.532 . . 194 567 43 SER H H 8.968 . . 195 567 43 SER C C 173.922 . . 196 567 43 SER CA C 54.886 . . 197 567 43 SER CB C 65.770 . . 198 567 43 SER N N 111.836 . . 199 568 44 ALA H H 8.686 . . 200 568 44 ALA C C 177.270 . . 201 568 44 ALA CA C 52.278 . . 202 568 44 ALA CB C 22.436 . . 203 568 44 ALA N N 126.557 . . 204 569 45 ARG H H 9.793 . . 205 569 45 ARG C C 175.819 . . 206 569 45 ARG CA C 57.244 . . 207 569 45 ARG CB C 27.964 . . 208 569 45 ARG N N 122.153 . . 209 570 46 GLY H H 8.678 . . 210 570 46 GLY C C 173.904 . . 211 570 46 GLY CA C 45.529 . . 212 570 46 GLY N N 104.351 . . 213 571 47 HIS H H 8.029 . . 214 571 47 HIS C C 175.934 . . 215 571 47 HIS CA C 54.642 . . 216 571 47 HIS CB C 31.483 . . 217 571 47 HIS N N 120.146 . . 218 572 48 ILE H H 8.535 . . 219 572 48 ILE C C 176.152 . . 220 572 48 ILE CA C 59.891 . . 221 572 48 ILE CB C 40.482 . . 222 572 48 ILE N N 121.682 . . 223 573 49 GLY H H 9.043 . . 224 573 49 GLY C C 170.978 . . 225 573 49 GLY CA C 45.915 . . 226 573 49 GLY N N 115.046 . . 227 574 50 TRP H H 8.627 . . 228 574 50 TRP C C 176.325 . . 229 574 50 TRP CA C 56.985 . . 230 574 50 TRP CB C 32.230 . . 231 574 50 TRP N N 121.204 . . 232 575 51 PHE H H 8.945 . . 233 575 51 PHE C C 170.820 . . 234 575 51 PHE CA C 55.677 . . 235 575 51 PHE CB C 37.789 . . 236 575 51 PHE N N 115.500 . . 237 576 52 PRO C C 177.520 . . 238 576 52 PRO CA C 61.967 . . 239 576 52 PRO CB C 31.440 . . 240 577 53 ALA H H 8.118 . . 241 577 53 ALA C C 178.912 . . 242 577 53 ALA CA C 54.649 . . 243 577 53 ALA CB C 15.658 . . 244 577 53 ALA N N 129.873 . . 245 578 54 GLU H H 8.002 . . 246 578 54 GLU C C 176.844 . . 247 578 54 GLU CA C 57.267 . . 248 578 54 GLU CB C 28.572 . . 249 578 54 GLU N N 111.241 . . 250 579 55 CYS H H 7.703 . . 251 579 55 CYS C C 174.604 . . 252 579 55 CYS CA C 61.672 . . 253 579 55 CYS CB C 28.284 . . 254 579 55 CYS N N 115.075 . . 255 580 56 VAL H H 7.676 . . 256 580 56 VAL C C 173.739 . . 257 580 56 VAL CA C 58.450 . . 258 580 56 VAL CB C 36.457 . . 259 580 56 VAL N N 110.062 . . 260 581 57 GLU H H 8.931 . . 261 581 57 GLU C C 174.589 . . 262 581 57 GLU CA C 54.578 . . 263 581 57 GLU CB C 34.510 . . 264 581 57 GLU N N 118.523 . . 265 582 58 GLU H H 8.966 . . 266 582 58 GLU C C 176.654 . . 267 582 58 GLU CA C 57.184 . . 268 582 58 GLU CB C 30.020 . . 269 582 58 GLU N N 125.911 . . 270 583 59 VAL H H 8.209 . . 271 583 59 VAL C C 175.635 . . 272 583 59 VAL CA C 61.959 . . 273 583 59 VAL CB C 32.805 . . 274 583 59 VAL N N 124.613 . . 275 584 60 GLN H H 8.581 . . 276 584 60 GLN C C 175.288 . . 277 584 60 GLN CA C 55.809 . . 278 584 60 GLN CB C 29.603 . . 279 584 60 GLN N N 125.340 . . 280 585 61 SER H H 7.990 . . 281 585 61 SER CA C 60.086 . . 282 585 61 SER CB C 64.944 . . 283 585 61 SER N N 122.882 . . stop_ save_