data_25023 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 15N HSQC assignment of Drosophila ELF domain from FANCL ; _BMRB_accession_number 25023 _BMRB_flat_file_name bmr25023.str _Entry_type original _Submission_date 2014-06-16 _Accession_date 2014-06-16 _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 Miles Jennifer A. . 2 Carroll Ellis . . 3 Rowe Michelle L. . 4 Howard Mark J. . 5 Sihu Ateesh . . 6 Frost Mark G. . 7 Williamson Richard . . 8 Alpi Arno F. . 9 Walden Helen . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 81 "15N chemical shifts" 74 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-07-01 original BMRB . stop_ _Original_release_date 2016-07-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The Fanconi Anemia DNA Repair Pathway Is Regulated by an Interaction between Ubiquitin and the E2-like Fold Domain of FANCL ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26149689 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Miles Jennifer A. . 2 Carroll Ellis . . 3 Rowe Michelle L. . 4 Howard Mark J. . 5 Sidhu Ateesh . . 6 Frost Mark G. . 7 Williamson Richard . . 8 Alpi Arno F. . 9 Walden Helen . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 290 _Journal_issue 34 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 20995 _Page_last 21006 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Drosophila ELF domain from FANCL' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label ELF $ELF 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_ELF _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ELF _Molecular_mass . _Mol_thiol_state unknown _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 104 _Mol_residue_sequence ; MESNEDVERLLCQKYPGLAA ELQPSGACIIRGVLGSEDTW RRLKLYLPHHPALHGFQLYV QESLEYKLYTSANLKLQDDW LLEDFLDHLPKILPAQKAPT VPKE ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLU 3 SER 4 ASN 5 GLU 6 ASP 7 VAL 8 GLU 9 ARG 10 LEU 11 LEU 12 CYS 13 GLN 14 LYS 15 TYR 16 PRO 17 GLY 18 LEU 19 ALA 20 ALA 21 GLU 22 LEU 23 GLN 24 PRO 25 SER 26 GLY 27 ALA 28 CYS 29 ILE 30 ILE 31 ARG 32 GLY 33 VAL 34 LEU 35 GLY 36 SER 37 GLU 38 ASP 39 THR 40 TRP 41 ARG 42 ARG 43 LEU 44 LYS 45 LEU 46 TYR 47 LEU 48 PRO 49 HIS 50 HIS 51 PRO 52 ALA 53 LEU 54 HIS 55 GLY 56 PHE 57 GLN 58 LEU 59 TYR 60 VAL 61 GLN 62 GLU 63 SER 64 LEU 65 GLU 66 TYR 67 LYS 68 LEU 69 TYR 70 THR 71 SER 72 ALA 73 ASN 74 LEU 75 LYS 76 LEU 77 GLN 78 ASP 79 ASP 80 TRP 81 LEU 82 LEU 83 GLU 84 ASP 85 PHE 86 LEU 87 ASP 88 HIS 89 LEU 90 PRO 91 LYS 92 ILE 93 LEU 94 PRO 95 ALA 96 GLN 97 LYS 98 ALA 99 PRO 100 THR 101 VAL 102 PRO 103 LYS 104 GLU 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 $ELF 'fruit fly' 7227 Eukaryota Metazoa Drosophila melanogaster 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 $ELF 'recombinant technology' . Escherichia coli . 'pet28a SUMO' 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 $ELF 0.6 mM '[U-99% 15N]' 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 processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.05 . M pH 6.5 . pH pressure 1 . atm temperature 273 . 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 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_ _Experiment_label '2D 1H-15N HSQC' 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 ELF _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 3 3 SER H H 8.6243 . 1 2 3 3 SER HA H 4.5101 . 1 3 3 3 SER HB2 H 4.0057 . 2 4 3 3 SER HB3 H 3.9083 . 2 5 3 3 SER N N 116.7072 . 1 6 4 4 ASN H H 8.7600 . 1 7 4 4 ASN N N 121.2234 . 1 8 5 5 GLU H H 8.3998 . 1 9 5 5 GLU N N 120.3710 . 1 10 6 6 ASP H H 8.2838 . 1 11 6 6 ASP N N 120.8716 . 1 12 7 7 VAL H H 8.2039 . 1 13 7 7 VAL N N 122.5982 . 1 14 8 8 GLU H H 8.1680 . 1 15 8 8 GLU N N 119.9597 . 1 16 9 9 ARG H H 7.9757 . 1 17 9 9 ARG N N 119.4286 . 1 18 10 10 LEU H H 7.7201 . 1 19 10 10 LEU N N 120.4876 . 1 20 11 11 LEU H H 8.2610 . 1 21 11 11 LEU N N 117.4404 . 1 22 12 12 CYS H H 8.0259 . 1 23 12 12 CYS N N 114.8286 . 1 24 13 13 GLN H H 7.7875 . 1 25 13 13 GLN N N 115.9983 . 1 26 17 17 GLY H H 8.8294 . 1 27 17 17 GLY HA2 H 4.1625 . 2 28 17 17 GLY HA3 H 3.9409 . 2 29 17 17 GLY N N 107.7873 . 1 30 19 19 ALA H H 8.5284 . 1 31 19 19 ALA N N 121.5781 . 1 32 20 20 ALA H H 9.0988 . 1 33 20 20 ALA N N 123.6984 . 1 34 21 21 GLU H H 9.0722 . 1 35 21 21 GLU N N 122.9007 . 1 36 22 22 LEU H H 9.0025 . 1 37 22 22 LEU N N 130.0489 . 1 38 23 23 GLN H H 8.7238 . 1 39 23 23 GLN N N 122.2125 . 1 40 25 25 SER H H 7.6875 . 1 41 25 25 SER N N 109.2497 . 1 42 26 26 GLY H H 8.3482 . 1 43 26 26 GLY N N 111.4144 . 1 44 27 27 ALA H H 7.3152 . 1 45 27 27 ALA N N 120.1839 . 1 46 28 28 CYS H H 7.8025 . 1 47 28 28 CYS N N 118.2426 . 1 48 29 29 ILE H H 8.7023 . 1 49 29 29 ILE N N 125.0980 . 1 50 32 32 GLY H H 8.1927 . 1 51 32 32 GLY N N 108.3848 . 1 52 33 33 VAL H H 7.7425 . 1 53 33 33 VAL N N 118.0673 . 1 54 34 34 LEU H H 8.7460 . 1 55 34 34 LEU N N 124.6163 . 1 56 35 35 GLY H H 8.5968 . 1 57 35 35 GLY HA2 H 4.0174 . 2 58 35 35 GLY HA3 H 3.8343 . 2 59 35 35 GLY N N 114.1415 . 1 60 36 36 SER H H 7.7654 . 1 61 36 36 SER N N 113.9360 . 1 62 37 37 GLU H H 8.9805 . 1 63 37 37 GLU N N 120.3998 . 1 64 38 38 ASP H H 8.4479 . 1 65 38 38 ASP N N 118.2392 . 1 66 39 39 THR H H 7.9410 . 1 67 39 39 THR N N 113.5651 . 1 68 40 40 TRP H H 8.0191 . 1 69 40 40 TRP N N 123.5091 . 1 70 41 41 ARG H H 8.6429 . 1 71 41 41 ARG N N 127.7941 . 1 72 42 42 ARG H H 9.5292 . 1 73 42 42 ARG N N 129.3446 . 1 74 43 43 LEU H H 8.9080 . 1 75 43 43 LEU N N 123.8753 . 1 76 52 52 ALA H H 8.3917 . 1 77 52 52 ALA N N 128.3591 . 1 78 53 53 LEU H H 8.5561 . 1 79 53 53 LEU N N 117.3777 . 1 80 54 54 HIS H H 7.1077 . 1 81 54 54 HIS N N 115.6167 . 1 82 55 55 GLY H H 9.4243 . 1 83 55 55 GLY N N 112.6231 . 1 84 56 56 PHE N N 116.3871 . 1 85 57 57 GLN H H 8.7260 . 1 86 57 57 GLN N N 117.4346 . 1 87 58 58 LEU H H 9.3310 . 1 88 58 58 LEU N N 126.8923 . 1 89 59 59 TYR H H 9.9369 . 1 90 59 59 TYR N N 127.4224 . 1 91 60 60 VAL H H 9.4336 . 1 92 60 60 VAL N N 122.6276 . 1 93 61 61 GLN H H 8.9017 . 1 94 61 61 GLN N N 129.5142 . 1 95 62 62 GLU H H 8.7261 . 1 96 62 62 GLU N N 130.0167 . 1 97 63 63 SER H H 8.8288 . 1 98 63 63 SER N N 118.7002 . 1 99 64 64 LEU H H 8.3068 . 1 100 64 64 LEU N N 119.6291 . 1 101 65 65 GLU H H 7.8845 . 1 102 65 65 GLU N N 118.6953 . 1 103 66 66 TYR H H 8.8954 . 1 104 66 66 TYR N N 120.4057 . 1 105 67 67 LYS H H 8.2930 . 1 106 67 67 LYS N N 114.3009 . 1 107 71 71 SER H H 8.8223 . 1 108 71 71 SER N N 115.2197 . 1 109 72 72 ALA H H 7.9005 . 1 110 72 72 ALA N N 121.9788 . 1 111 73 73 ASN H H 8.0321 . 1 112 73 73 ASN N N 113.6658 . 1 113 74 74 LEU H H 7.9644 . 1 114 74 74 LEU N N 122.3536 . 1 115 75 75 LYS H H 8.2658 . 1 116 75 75 LYS N N 124.7409 . 1 117 76 76 LEU H H 8.1885 . 1 118 76 76 LEU N N 125.3478 . 1 119 78 78 ASP H H 9.7372 . 1 120 78 78 ASP N N 128.2946 . 1 121 79 79 ASP H H 8.2548 . 1 122 79 79 ASP N N 121.8088 . 1 123 81 81 LEU H H 9.3337 . 1 124 81 81 LEU N N 123.0743 . 1 125 82 82 LEU H H 8.9703 . 1 126 82 82 LEU N N 123.0312 . 1 127 83 83 GLU H H 9.1270 . 1 128 83 83 GLU N N 116.4681 . 1 129 84 84 ASP H H 6.7435 . 1 130 84 84 ASP N N 114.2350 . 1 131 85 85 PHE H H 8.0459 . 1 132 85 85 PHE N N 120.0896 . 1 133 91 91 LYS H H 7.5504 . 1 134 91 91 LYS N N 112.6414 . 1 135 92 92 ILE H H 7.6173 . 1 136 92 92 ILE N N 112.3149 . 1 137 93 93 LEU H H 7.3540 . 1 138 93 93 LEU N N 123.1941 . 1 139 95 95 ALA H H 8.4397 . 1 140 95 95 ALA HA H 4.2380 . 1 141 95 95 ALA N N 125.1595 . 1 142 96 96 GLN H H 8.5236 . 1 143 96 96 GLN N N 120.7652 . 1 144 97 97 LYS H H 8.4331 . 1 145 97 97 LYS N N 123.5538 . 1 146 98 98 ALA H H 8.3921 . 1 147 98 98 ALA N N 127.2371 . 1 148 100 100 THR H H 8.2736 . 1 149 100 100 THR N N 115.3861 . 1 150 101 101 VAL H H 8.1680 . 1 151 101 101 VAL N N 124.1955 . 1 152 103 103 LYS H H 8.3846 . 1 153 103 103 LYS N N 122.3772 . 1 154 104 104 GLU H H 7.9767 . 1 155 104 104 GLU N N 127.3056 . 1 stop_ save_