data_4595 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation -- P25 ; _BMRB_accession_number 4595 _BMRB_flat_file_name bmr4595.str _Entry_type original _Submission_date 2000-05-05 _Accession_date 2000-09-07 _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 Massiah M. A. . 2 Ko Y. H. . 3 Pedersen P. L. . 4 Mildvan A. S. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 127 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-12-04 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4596 'P26 in Trifluroethanol' 4597 'P26 in H2O' 4598 'P25 in H2O' stop_ _Original_release_date 2000-12-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99303984 _PubMed_ID 10360942 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Massiah M. A. . 2 Ko Y. H. . 3 Pedersen P. L. . 4 Mildvan A. S. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 38 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7453 _Page_last 7461 _Year 1999 _Details . loop_ _Keyword 'P25 TFE' 'cystic fibrosis' peptides NMR stop_ save_ ################################## # Molecular system description # ################################## save_system_cftr-p25 _Saveframe_category molecular_system _Mol_system_name 'cystic fibrosis transmembrane conductance regulator (CFTR)' _Abbreviation_common cftr-p25 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'cystic fibrosis transmembrane conductance regulator (CFTR)' $cftr-p25 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cftr-p25 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'protein (cystic fibrosis transmembrane conductance regulator (CFTR))' _Abbreviation_common cftr _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 25 _Mol_residue_sequence ; MPGTIKENIIGVSYDEYRYR SVIKA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 PRO 3 GLY 4 THR 5 ILE 6 LYS 7 GLU 8 ASN 9 ILE 10 ILE 11 GLY 12 VAL 13 SER 14 TYR 15 ASP 16 GLU 17 TYR 18 ARG 19 TYR 20 ARG 21 SER 22 VAL 23 ILE 24 LYS 25 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-24 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 BMRB 25698 hCFTR_NBD1_delta_RI_F508del 100.00 228 100.00 100.00 1.20e-07 BMRB 4598 "PROTEIN (CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR (CFTR))" 100.00 25 100.00 100.00 1.04e-07 PDB 1CKW "Cystic Fibrosis Transmembrane Conductance Regulator: Solution Structures Of Peptides Based On The Phe508 Region, The Most Commo" 100.00 25 100.00 100.00 1.04e-07 PDB 1CKZ "Cystic Fibrosis Transmembrane Conductance Regulator: Solution Structures Of Peptides Based On The Phe508 Region, The Most Commo" 100.00 25 100.00 100.00 1.04e-07 PDB 1XMJ "Crystal Structure Of Human Deltaf508 Human Nbd1 Domain With Atp" 100.00 290 100.00 100.00 8.88e-08 PDB 2BBS "Human Deltaf508 Nbd1 With Three Solubilizing Mutations" 100.00 290 100.00 100.00 1.00e-07 PDB 2BBT "Human Deltaf508 Nbd1 With Two Solublizing Mutations" 100.00 290 100.00 100.00 9.73e-08 PDB 2PZF "Minimal Human Cftr First Nucleotide Binding Domain As A Head-To-Tail Dimer With Delta F508" 100.00 228 100.00 100.00 1.20e-07 PDB 4WZ6 "Human Cftr Aa389-678 (nbd1), Deltaf508 With Three Solubilizing Mutations, Bound Atp" 100.00 290 100.00 100.00 1.00e-07 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $cftr-p25 Human 9606 Eucaryota Metazoa Homo sapiens 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 $cftr-p25 'chemical synthesis' . . . . . 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 $cftr-p25 1.4 mM . Trifluroethanol 43 % . stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.8 loop_ _Task 'structure refinement' stop_ _Details BRUNGER save_ save_NMRVIEW2.1 _Saveframe_category software _Name NMRVIEW2.1 _Version . loop_ _Task 'Structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_1 save_ save_COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _Sample_label $sample_1 save_ save_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.0 0.1 n/a temperature 298 0.5 K pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label H2O H 1 'water protons' ppm 4.773 internal direct spherical internal parallel_to_Bo 1 $entry_citation $entry_citation 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'cystic fibrosis transmembrane conductance regulator (CFTR)' _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 MET HA H 4.42 . 1 2 . 1 MET HB2 H 2.66 . 4 3 . 1 MET HB3 H 2.64 . 4 4 . 1 MET HG2 H 2.20 . 4 5 . 2 PRO HA H 4.52 . 1 6 . 2 PRO HB2 H 2.40 . 4 7 . 2 PRO HG2 H 2.04 . 4 8 . 2 PRO HG3 H 2.10 . 4 9 . 2 PRO HD2 H 3.97 . 2 10 . 2 PRO HD3 H 3.63 . 2 11 . 3 GLY H H 8.47 . 1 12 . 3 GLY HA2 H 3.99 . 2 13 . 4 THR H H 7.78 . 1 14 . 4 THR HA H 4.00 . 1 15 . 4 THR HB H 4.30 . 1 16 . 4 THR HG2 H 1.56 . 1 17 . 5 ILE H H 7.78 . 1 18 . 5 ILE HA H 4.30 . 1 19 . 5 ILE HB H 1.90 . 4 20 . 5 ILE HG12 H 1.24 . 4 21 . 5 ILE HG2 H 0.96 . 1 22 . 5 ILE HD1 H 0.89 . 1 23 . 6 LYS H H 7.85 . 1 24 . 6 LYS HA H 4.31 . 1 25 . 6 LYS HB2 H 1.82 . 4 26 . 6 LYS HG2 H 1.39 . 4 27 . 7 GLU H H 7.97 . 1 28 . 7 GLU HA H 4.07 . 1 29 . 7 GLU HB2 H 2.47 . 4 30 . 7 GLU HG2 H 2.10 . 4 31 . 8 ASN H H 8.03 . 1 32 . 8 ASN HA H 4.59 . 1 33 . 8 ASN HB2 H 2.93 . 2 34 . 8 ASN HB3 H 2.81 . 2 35 . 8 ASN HD21 H 7.19 . 2 36 . 8 ASN HD22 H 6.68 . 2 37 . 9 ILE H H 8.09 . 1 38 . 9 ILE HA H 3.87 . 1 39 . 9 ILE HB H 1.96 . 1 40 . 9 ILE HG12 H 1.17 . 2 41 . 9 ILE HG13 H 1.66 . 2 42 . 9 ILE HG2 H 0.90 . 1 43 . 9 ILE HD1 H 0.83 . 1 44 . 10 ILE H H 8.12 . 1 45 . 10 ILE HA H 4.05 . 1 46 . 10 ILE HB H 1.90 . 1 47 . 10 ILE HG12 H 1.15 . 2 48 . 10 ILE HG2 H 0.94 . 1 49 . 10 ILE HD1 H 0.87 . 1 50 . 11 GLY H H 8.08 . 1 51 . 11 GLY HA2 H 3.87 . 2 52 . 11 GLY HA3 H 3.93 . 2 53 . 12 VAL H H 8.17 . 1 54 . 12 VAL HA H 3.90 . 1 55 . 12 VAL HB H 2.15 . 1 56 . 12 VAL HG1 H 1.17 . 2 57 . 12 VAL HG2 H 0.97 . 2 58 . 13 SER H H 8.12 . 1 59 . 13 SER HA H 4.26 . 4 60 . 13 SER HB2 H 4.11 . 4 61 . 13 SER HB3 H 3.93 . 4 62 . 14 TYR H H 8.50 . 1 63 . 14 TYR HA H 4.35 . 1 64 . 14 TYR HB2 H 3.16 . 2 65 . 14 TYR HD1 H 7.15 . 1 66 . 14 TYR HD2 H 7.15 . 1 67 . 14 TYR HE1 H 6.79 . 1 68 . 14 TYR HE2 H 6.79 . 1 69 . 15 ASP H H 8.34 . 1 70 . 15 ASP HA H 4.36 . 1 71 . 15 ASP HB2 H 2.86 . 2 72 . 15 ASP HB3 H 2.83 . 2 73 . 16 GLU H H 8.44 . 1 74 . 16 GLU HA H 4.08 . 1 75 . 16 GLU HB2 H 2.24 . 4 76 . 16 GLU HB3 H 2.09 . 4 77 . 16 GLU HG2 H 2.61 . 4 78 . 16 GLU HG3 H 2.40 . 4 79 . 17 TYR H H 8.13 . 1 80 . 17 TYR HA H 4.20 . 1 81 . 17 TYR HB2 H 3.13 . 2 82 . 17 TYR HD1 H 7.00 . 1 83 . 17 TYR HD2 H 7.00 . 1 84 . 17 TYR HE1 H 6.78 . 1 85 . 17 TYR HE2 H 6.78 . 1 86 . 18 ARG HA H 3.77 . 1 87 . 18 ARG HB2 H 1.66 . 4 88 . 18 ARG HG2 H 1.42 . 4 89 . 18 ARG HG3 H 1.35 . 4 90 . 18 ARG H H 8.30 . 1 91 . 19 TYR H H 8.07 . 1 92 . 19 TYR HA H 4.33 . 1 93 . 19 TYR HB2 H 3.13 . 2 94 . 19 TYR HB3 H 3.04 . 2 95 . 19 TYR HD1 H 7.06 . 1 96 . 19 TYR HD2 H 7.06 . 1 97 . 19 TYR HE1 H 6.76 . 1 98 . 19 TYR HE2 H 6.76 . 1 99 . 20 ARG H H 7.99 . 1 100 . 20 ARG HA H 4.04 . 1 101 . 20 ARG HB2 H 1.87 . 4 102 . 20 ARG HG2 H 1.67 . 4 103 . 21 SER H H 7.85 . 1 104 . 21 SER HA H 4.25 . 1 105 . 21 SER HB2 H 3.86 . 2 106 . 21 SER HB3 H 3.73 . 2 107 . 22 VAL H H 7.60 . 1 108 . 22 VAL HA H 4.05 . 1 109 . 22 VAL HB H 2.14 . 1 110 . 22 VAL HG1 H 0.96 . 2 111 . 22 VAL HG2 H 0.90 . 2 112 . 23 ILE H H 7.65 . 1 113 . 23 ILE HA H 4.04 . 1 114 . 23 ILE HB H 1.81 . 1 115 . 23 ILE HG12 H 1.15 . 2 116 . 23 ILE HG13 H 1.40 . 2 117 . 23 ILE HG2 H 0.82 . 1 118 . 23 ILE HD1 H 0.78 . 1 119 . 24 LYS H H 7.84 . 1 120 . 24 LYS HA H 4.04 . 1 121 . 24 LYS HB2 H 1.83 . 4 122 . 24 LYS HG2 H 1.67 . 4 123 . 24 LYS HG3 H 1.47 . 4 124 . 24 LYS HE2 H 2.96 . 3 125 . 25 ALA H H 7.85 . 1 126 . 25 ALA HA H 4.28 . 1 127 . 25 ALA HB H 1.39 . 1 stop_ save_