data_30438 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of SH3 domain from Shank3 ; _BMRB_accession_number 30438 _BMRB_flat_file_name bmr30438.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" 56 "13C chemical shifts" 173 "15N chemical shifts" 56 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 3' _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 6616.582 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 61 _Mol_residue_sequence ; MVPGRKFIAVKAHSPQGEGE IPLHRGEAVKVLSIGEGGFW EGTVKGRTGWFPADCVEEVQ M ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 470 MET 2 471 VAL 3 472 PRO 4 473 GLY 5 474 ARG 6 475 LYS 7 476 PHE 8 477 ILE 9 478 ALA 10 479 VAL 11 480 LYS 12 481 ALA 13 482 HIS 14 483 SER 15 484 PRO 16 485 GLN 17 486 GLY 18 487 GLU 19 488 GLY 20 489 GLU 21 490 ILE 22 491 PRO 23 492 LEU 24 493 HIS 25 494 ARG 26 495 GLY 27 496 GLU 28 497 ALA 29 498 VAL 30 499 LYS 31 500 VAL 32 501 LEU 33 502 SER 34 503 ILE 35 504 GLY 36 505 GLU 37 506 GLY 38 507 GLY 39 508 PHE 40 509 TRP 41 510 GLU 42 511 GLY 43 512 THR 44 513 VAL 45 514 LYS 46 515 GLY 47 516 ARG 48 517 THR 49 518 GLY 50 519 TRP 51 520 PHE 52 521 PRO 53 522 ALA 54 523 ASP 55 524 CYS 56 525 VAL 57 526 GLU 58 527 GLU 59 528 VAL 60 529 GLN 61 530 MET 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 Human 9606 Eukaryota Metazoa Homo sapiens 'SHANK3, KIAA1650, PROSAP2, PSAP2' 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] Shank3 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] Shank3 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% 15N] Shank3 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% 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 Shank3 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_HBHA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(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 HBHA(CO)NH' '3D H(CCO)NH' '3D C(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 1 470 1 MET C C 175.412 . . 2 470 1 MET CA C 55.168 . . 3 470 1 MET CB C 32.902 . . 4 471 2 VAL H H 8.393 . . 5 471 2 VAL C C 174.290 . . 6 471 2 VAL CA C 60.758 . . 7 471 2 VAL CB C 32.424 . . 8 471 2 VAL N N 124.454 . . 9 472 3 PRO C C 177.364 . . 10 472 3 PRO CA C 63.614 . . 11 472 3 PRO CB C 32.162 . . 12 473 4 GLY H H 8.517 . . 13 473 4 GLY C C 174.162 . . 14 473 4 GLY CA C 45.528 . . 15 473 4 GLY N N 108.842 . . 16 474 5 ARG H H 7.933 . . 17 474 5 ARG C C 175.394 . . 18 474 5 ARG CA C 55.800 . . 19 474 5 ARG CB C 32.108 . . 20 474 5 ARG N N 120.231 . . 21 475 6 LYS H H 8.660 . . 22 475 6 LYS C C 174.408 . . 23 475 6 LYS CA C 55.554 . . 24 475 6 LYS CB C 34.560 . . 25 475 6 LYS N N 123.494 . . 26 476 7 PHE H H 8.340 . . 27 476 7 PHE C C 175.030 . . 28 476 7 PHE CA C 57.100 . . 29 476 7 PHE CB C 43.462 . . 30 476 7 PHE N N 119.528 . . 31 477 8 ILE H H 9.156 . . 32 477 8 ILE C C 174.207 . . 33 477 8 ILE CA C 58.313 . . 34 477 8 ILE CB C 42.804 . . 35 477 8 ILE N N 120.669 . . 36 478 9 ALA H H 8.900 . . 37 478 9 ALA C C 178.487 . . 38 478 9 ALA CA C 52.008 . . 39 478 9 ALA CB C 18.314 . . 40 478 9 ALA N N 126.208 . . 41 479 10 VAL H H 9.187 . . 42 479 10 VAL C C 174.923 . . 43 479 10 VAL CA C 61.090 . . 44 479 10 VAL CB C 32.352 . . 45 479 10 VAL N N 120.243 . . 46 480 11 LYS H H 7.837 . . 47 480 11 LYS C C 172.919 . . 48 480 11 LYS CA C 55.118 . . 49 480 11 LYS CB C 36.581 . . 50 480 11 LYS N N 122.001 . . 51 481 12 ALA H H 8.146 . . 52 481 12 ALA C C 177.290 . . 53 481 12 ALA CA C 51.214 . . 54 481 12 ALA CB C 19.977 . . 55 481 12 ALA N N 120.572 . . 56 482 13 HIS H H 8.479 . . 57 482 13 HIS C C 174.609 . . 58 482 13 HIS CA C 57.087 . . 59 482 13 HIS CB C 35.198 . . 60 482 13 HIS N N 117.581 . . 61 483 14 SER H H 7.765 . . 62 483 14 SER C C 171.253 . . 63 483 14 SER CA C 56.952 . . 64 483 14 SER CB C 63.919 . . 65 483 14 SER N N 124.617 . . 66 484 15 PRO C C 176.888 . . 67 484 15 PRO CA C 63.560 . . 68 484 15 PRO CB C 33.059 . . 69 485 16 GLN H H 9.109 . . 70 485 16 GLN C C 175.217 . . 71 485 16 GLN CA C 55.143 . . 72 485 16 GLN CB C 30.041 . . 73 485 16 GLN N N 124.155 . . 74 486 17 GLY H H 7.350 . . 75 486 17 GLY C C 173.276 . . 76 486 17 GLY CA C 44.518 . . 77 486 17 GLY N N 106.750 . . 78 487 18 GLU H H 8.629 . . 79 487 18 GLU C C 177.692 . . 80 487 18 GLU CA C 57.761 . . 81 487 18 GLU CB C 29.860 . . 82 487 18 GLU N N 120.624 . . 83 488 19 GLY H H 9.049 . . 84 488 19 GLY C C 174.771 . . 85 488 19 GLY CA C 45.522 . . 86 488 19 GLY N N 111.474 . . 87 489 20 GLU H H 7.443 . . 88 489 20 GLU C C 177.017 . . 89 489 20 GLU CA C 55.358 . . 90 489 20 GLU CB C 33.435 . . 91 489 20 GLU N N 118.753 . . 92 490 21 ILE H H 8.350 . . 93 490 21 ILE C C 171.930 . . 94 490 21 ILE CA C 57.427 . . 95 490 21 ILE CB C 39.528 . . 96 490 21 ILE N N 113.441 . . 97 491 22 PRO C C 176.724 . . 98 491 22 PRO CA C 61.316 . . 99 491 22 PRO CB C 32.263 . . 100 492 23 LEU H H 8.231 . . 101 492 23 LEU C C 176.288 . . 102 492 23 LEU CA C 54.094 . . 103 492 23 LEU CB C 46.842 . . 104 492 23 LEU N N 117.427 . . 105 493 24 HIS H H 8.509 . . 106 493 24 HIS C C 173.596 . . 107 493 24 HIS CA C 53.952 . . 108 493 24 HIS CB C 30.520 . . 109 493 24 HIS N N 120.111 . . 110 494 25 ARG H H 8.731 . . 111 494 25 ARG C C 177.143 . . 112 494 25 ARG CA C 58.803 . . 113 494 25 ARG CB C 29.810 . . 114 494 25 ARG N N 121.608 . . 115 495 26 GLY H H 9.140 . . 116 495 26 GLY C C 174.026 . . 117 495 26 GLY CA C 45.251 . . 118 495 26 GLY N N 113.217 . . 119 496 27 GLU H H 7.671 . . 120 496 27 GLU C C 175.237 . . 121 496 27 GLU CA C 56.940 . . 122 496 27 GLU CB C 30.379 . . 123 496 27 GLU N N 119.986 . . 124 497 28 ALA H H 8.454 . . 125 497 28 ALA C C 177.126 . . 126 497 28 ALA CA C 52.376 . . 127 497 28 ALA CB C 19.323 . . 128 497 28 ALA N N 124.677 . . 129 498 29 VAL H H 8.062 . . 130 498 29 VAL C C 175.158 . . 131 498 29 VAL CA C 61.054 . . 132 498 29 VAL CB C 35.206 . . 133 498 29 VAL N N 121.272 . . 134 499 30 LYS H H 8.077 . . 135 499 30 LYS C C 175.349 . . 136 499 30 LYS CA C 54.978 . . 137 499 30 LYS CB C 33.202 . . 138 499 30 LYS N N 128.945 . . 139 500 31 VAL H H 8.733 . . 140 500 31 VAL C C 175.207 . . 141 500 31 VAL CA C 64.147 . . 142 500 31 VAL CB C 32.200 . . 143 500 31 VAL N N 128.257 . . 144 501 32 LEU H H 9.535 . . 145 501 32 LEU C C 177.361 . . 146 501 32 LEU CA C 55.354 . . 147 501 32 LEU CB C 44.059 . . 148 501 32 LEU N N 128.345 . . 149 502 33 SER H H 7.613 . . 150 502 33 SER C C 171.165 . . 151 502 33 SER CA C 57.690 . . 152 502 33 SER CB C 64.823 . . 153 502 33 SER N N 111.714 . . 154 503 34 ILE H H 8.232 . . 155 503 34 ILE C C 176.343 . . 156 503 34 ILE CA C 60.379 . . 157 503 34 ILE CB C 38.480 . . 158 503 34 ILE N N 121.975 . . 159 504 35 GLY H H 7.881 . . 160 504 35 GLY C C 173.780 . . 161 504 35 GLY CA C 44.762 . . 162 504 35 GLY N N 114.028 . . 163 505 36 GLU H H 8.566 . . 164 505 36 GLU C C 178.047 . . 165 505 36 GLU CA C 56.024 . . 166 505 36 GLU CB C 30.702 . . 167 505 36 GLU N N 119.570 . . 168 506 37 GLY H H 8.885 . . 169 506 37 GLY C C 175.221 . . 170 506 37 GLY CA C 46.268 . . 171 506 37 GLY N N 109.023 . . 172 507 38 GLY H H 8.612 . . 173 507 38 GLY C C 173.841 . . 174 507 38 GLY CA C 45.251 . . 175 507 38 GLY N N 106.869 . . 176 508 39 PHE H H 7.675 . . 177 508 39 PHE C C 174.502 . . 178 508 39 PHE CA C 57.367 . . 179 508 39 PHE CB C 41.790 . . 180 508 39 PHE N N 119.700 . . 181 509 40 TRP H H 9.074 . . 182 509 40 TRP C C 171.740 . . 183 509 40 TRP CA C 53.222 . . 184 509 40 TRP CB C 33.495 . . 185 509 40 TRP N N 123.405 . . 186 510 41 GLU H H 8.230 . . 187 510 41 GLU C C 177.111 . . 188 510 41 GLU CA C 52.837 . . 189 510 41 GLU CB C 31.585 . . 190 510 41 GLU N N 121.513 . . 191 511 42 GLY H H 9.381 . . 192 511 42 GLY C C 169.797 . . 193 511 42 GLY CA C 46.493 . . 194 511 42 GLY N N 114.274 . . 195 512 43 THR H H 9.048 . . 196 512 43 THR C C 174.541 . . 197 512 43 THR CA C 61.032 . . 198 512 43 THR CB C 71.230 . . 199 512 43 THR N N 114.546 . . 200 513 44 VAL H H 9.109 . . 201 513 44 VAL C C 175.295 . . 202 513 44 VAL CA C 61.569 . . 203 513 44 VAL CB C 35.043 . . 204 513 44 VAL N N 128.196 . . 205 514 45 LYS H H 9.530 . . 206 514 45 LYS C C 176.538 . . 207 514 45 LYS CA C 57.340 . . 208 514 45 LYS CB C 30.310 . . 209 514 45 LYS N N 127.790 . . 210 515 46 GLY H H 8.520 . . 211 515 46 GLY C C 173.883 . . 212 515 46 GLY CA C 45.756 . . 213 515 46 GLY N N 104.790 . . 214 516 47 ARG H H 8.178 . . 215 516 47 ARG C C 174.425 . . 216 516 47 ARG CA C 54.938 . . 217 516 47 ARG CB C 32.214 . . 218 516 47 ARG N N 122.278 . . 219 517 48 THR H H 8.665 . . 220 517 48 THR C C 173.883 . . 221 517 48 THR CA C 61.229 . . 222 517 48 THR CB C 70.974 . . 223 517 48 THR N N 120.143 . . 224 518 49 GLY H H 9.063 . . 225 518 49 GLY C C 170.500 . . 226 518 49 GLY CA C 46.142 . . 227 518 49 GLY N N 114.756 . . 228 519 50 TRP H H 8.692 . . 229 519 50 TRP C C 176.309 . . 230 519 50 TRP CA C 56.842 . . 231 519 50 TRP CB C 32.055 . . 232 519 50 TRP N N 120.647 . . 233 520 51 PHE H H 8.865 . . 234 520 51 PHE C C 170.823 . . 235 520 51 PHE CA C 55.001 . . 236 520 51 PHE CB C 38.045 . . 237 520 51 PHE N N 115.089 . . 238 521 52 PRO C C 177.642 . . 239 521 52 PRO CA C 62.194 . . 240 521 52 PRO CB C 31.322 . . 241 522 53 ALA H H 8.161 . . 242 522 53 ALA C C 178.027 . . 243 522 53 ALA CA C 54.805 . . 244 522 53 ALA CB C 16.384 . . 245 522 53 ALA N N 127.876 . . 246 523 54 ASP H H 7.795 . . 247 523 54 ASP C C 177.019 . . 248 523 54 ASP CA C 54.606 . . 249 523 54 ASP CB C 39.516 . . 250 523 54 ASP N N 111.403 . . 251 524 55 CYS H H 7.766 . . 252 524 55 CYS C C 175.065 . . 253 524 55 CYS CA C 61.562 . . 254 524 55 CYS CB C 28.738 . . 255 524 55 CYS N N 113.940 . . 256 525 56 VAL H H 7.540 . . 257 525 56 VAL C C 173.687 . . 258 525 56 VAL CA C 58.746 . . 259 525 56 VAL CB C 36.160 . . 260 525 56 VAL N N 110.406 . . 261 526 57 GLU H H 8.887 . . 262 526 57 GLU C C 174.509 . . 263 526 57 GLU CA C 54.695 . . 264 526 57 GLU CB C 34.688 . . 265 526 57 GLU N N 119.184 . . 266 527 58 GLU H H 8.904 . . 267 527 58 GLU C C 176.438 . . 268 527 58 GLU CA C 56.328 . . 269 527 58 GLU CB C 30.050 . . 270 527 58 GLU N N 125.321 . . 271 528 59 VAL H H 8.379 . . 272 528 59 VAL C C 175.379 . . 273 528 59 VAL CA C 61.718 . . 274 528 59 VAL CB C 33.143 . . 275 528 59 VAL N N 125.408 . . 276 529 60 GLN H H 8.578 . . 277 529 60 GLN C C 175.027 . . 278 529 60 GLN CA C 55.720 . . 279 529 60 GLN CB C 29.400 . . 280 529 60 GLN N N 125.370 . . 281 530 61 MET H H 8.050 . . 282 530 61 MET C C 180.760 . . 283 530 61 MET CA C 56.960 . . 284 530 61 MET CB C 33.826 . . 285 530 61 MET N N 127.328 . . stop_ save_