data_25505 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; CCR5-ECL2 helical structure, residues Q186-T195. ; _BMRB_accession_number 25505 _BMRB_flat_file_name bmr25505.str _Entry_type original _Submission_date 2015-02-26 _Accession_date 2015-02-26 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; CCR5 ECL2 peptides inhibit HIV-1 infection. The structure of an elongated ECL2 peptide was determined using triple resonance approach by NMR. A helical structure was found at the C-terminal segment of this peptide, residues Q186-T195. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Abayev Meital . . 2 Anglister Jacob . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 20 "13C chemical shifts" 30 "15N chemical shifts" 10 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-08-30 update BMRB 'update entry citation' 2015-04-20 original author 'original release' stop_ _Original_release_date 2015-04-20 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; An extended CCR5 ECL2 peptide forms a helix that binds HIV-1 gp120 through non-specific hydrophobic interactions ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25703038 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Anglister Jacob . . 2 Abayev Meital . . 3 Moseri Adi . . 4 Tchaicheeyan Oren . . 5 Kessler Naama . . 6 Arshava Boris . . 7 Naider Fred . . 8 Scherf Tali . . stop_ _Journal_abbreviation 'FEBS J.' _Journal_volume 282 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1906 _Page_last 1921 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'CCR5-ECL2 helical structure, residues Q186-T195' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity $entity 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_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 1390.537 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 10 _Mol_residue_sequence ; QYQFWKNFQT ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 186 GLN 2 187 TYR 3 188 GLN 4 189 PHE 5 190 TRP 6 191 LYS 7 192 ASN 8 193 PHE 9 194 GLN 10 195 THR 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 $entity E.coli 562 Bacteria . Escherichia coli 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 'recombinant technology' . Escherichia coli . Pet24a 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 $entity 20 mM '[U-99% 2H]' Thiomersal 0.005 '% v/v' 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Saveframe_category software _Name X-PLOR_NIH _Version 2.31 loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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_2D_1H-15N_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_3D_HNCO_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '1mM ECL2s:GSGS-RSQ KEGLHYTSSSHFPYSQYQFWKNFQTLK-GSGS' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0 . mM pH 4.8 . pH pressure 1 . atm temperature 277 . 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 TSP C 1 'methyl protons' ppm 0.00 na indirect . . . 0.1932576 TSP H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 TSP N 1 'methyl protons' ppm 0.00 na indirect . . . 0.07684768 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 '3D CBCA(CO)NH' '3D HNCACB' '2D 1H-15N HSQC' '3D HNCO' 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 entity _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 1 186 1 GLN HA H 4.24 0.01 1 2 186 1 GLN H H 8.41 0.01 1 3 186 1 GLN C C 174.909 0.001 1 4 186 1 GLN CA C 56.746 0.001 1 5 186 1 GLN CB C 28.993 0.001 1 6 186 1 GLN N N 120.690 0.001 1 7 187 2 TYR H H 8.10 0.01 1 8 187 2 TYR HA H 4.34 0.01 1 9 187 2 TYR C C 176.2183 0.001 1 10 187 2 TYR CA C 58.970 0.001 1 11 187 2 TYR CB C 38.401 0.001 1 12 187 2 TYR N N 120.720 0.001 1 13 188 3 GLN H H 8.17 0.01 1 14 188 3 GLN HA H 3.91 0.01 1 15 188 3 GLN C C 176.288 0.001 1 16 188 3 GLN CA C 56.7819 0.001 1 17 188 3 GLN CB C 28.607 0.001 1 18 188 3 GLN N N 120.417 0.001 1 19 189 4 PHE H H 7.96 0.01 1 20 189 4 PHE HA H 4.38 0.01 1 21 189 4 PHE C C 176.196 0.001 1 22 189 4 PHE CA C 59.003 0.001 1 23 189 4 PHE CB C 39.11 0.001 1 24 189 4 PHE N N 120.153 0.001 1 25 190 5 TRP H H 7.88 0.01 1 26 190 5 TRP HA H 4.50 0.01 1 27 190 5 TRP C C 176.298 0.001 1 28 190 5 TRP CA C 58.125 0.001 1 29 190 5 TRP CB C 29.268 0.001 1 30 190 5 TRP N N 121.072 0.001 1 31 191 6 LYS H H 7.97 0.01 1 32 191 6 LYS HA H 3.95 0.01 1 33 191 6 LYS C C 176.686 0.001 1 34 191 6 LYS CA C 57.206 0.001 1 35 191 6 LYS CB C 32.499 0.001 1 36 191 6 LYS N N 121.958 0.001 1 37 192 7 ASN H H 8.07 0.01 1 38 192 7 ASN HA H 4.52 0.01 1 39 192 7 ASN C C 176.762 0.001 1 40 192 7 ASN CA C 53.752 0.001 1 41 192 7 ASN CB C 38.448 0.001 1 42 192 7 ASN N N 117.983 0.001 1 43 193 8 PHE H H 8.03 0.01 1 44 193 8 PHE HA H 4.50 0.01 1 45 193 8 PHE C C 175.348 0.001 1 46 193 8 PHE CA C 58.480 0.001 1 47 193 8 PHE CB C 39.240 0.001 1 48 193 8 PHE N N 120.529 0.001 1 49 194 9 GLN H H 8.19 0.01 1 50 194 9 GLN HA H 4.25 0.01 1 51 194 9 GLN C C 175.890 0.001 1 52 194 9 GLN CA C 56.257 0.001 1 53 194 9 GLN CB C 29.571 0.001 1 54 194 9 GLN N N 120.689 0.001 1 55 195 10 THR H H 8.13 0.01 1 56 195 10 THR HA H 4.24 0.01 1 57 195 10 THR C C 176.130 0.001 1 58 195 10 THR CA C 62.586 0.001 1 59 195 10 THR CB C 69.795 0.001 1 60 195 10 THR N N 115.265 0.001 1 stop_ save_