data_4598 #Corrected using PDB structure: 1CKWA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 18 R HA 3.94 3.12 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.12 N/A N/A N/A N/A -0.30 # #bmr4598.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4598.str file): #HA CA CB CO N HN #N/A N/A N/A N/A N/A N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.06 N/A N/A N/A N/A +/-0.12 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.646 N/A N/A N/A N/A 0.422 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.145 N/A N/A N/A N/A 0.297 # ####################### # 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 ; 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_ _BMRB_accession_number 4598 _BMRB_flat_file_name bmr4598.str _Entry_type new _Submission_date 2000-05-05 _Accession_date 2000-09-07 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR 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_ _Related_BMRB_accession_number _Relationship 4595 "P25 in Trifluroethanol" 4596 "P26 in Trifluroethanol" 4597 "P26 in H2O" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _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 _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_name_full . _Journal_volume 38 _Page_first 7453 _Page_last 7461 _Year 1999 loop_ _Keyword "Cystic fibrosis" peptides NMR stop_ save_ ################################## # Molecular system description # ################################## save_system_cftr-p25 _Saveframe_category molecular_system _Mol_system_name "CYSTIC FIBROSIS TRANSMEMBRANE CONDUNTANCE REGULATOR (CFTR)" _Abbreviation_common cftr-p25 loop_ _Mol_system_component_name _Mol_label "cystic fibrosis transmembrane conductance regulator (CFTR)" $cftr-p25 stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1CKW "A Chain A, Cystic Fibrosis Transmembrane Conductance Regulator: Solution Structures Of Peptides Based On The Phe508 Region, The Most Common Site Of Disease-Causing Delta-F508 Mutation" . PDB 1CKZ "A Chain A, Cystic Fibrosis Transmembrane Conductance Regulator: Solution Structures Of Peptides Based On The Phe508 Region, The Most Common Site Of Disease-Causing Delta-F508 Mutation" . stop_ 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))" _Name_variant . _Abbreviation_common cftr-p25 _Mol_thiol_state 'not present' ############################## # 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 2004-07-29 _Sequence_homology_query_revised_last_date 2004-05-28 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 PDB 1CKW "A Chain A, Cystic Fibrosis TransmembraneConductance Regulator: Solution Structures Of PeptidesBased On The Phe508 Region, The Most Common Site OfDisease-Causing Delta-F508 Mutation" 100.00 25 100 100 9e-07 PDB 1CKZ "A Chain A, Cystic Fibrosis TransmembraneConductance Regulator: Solution Structures Of PeptidesBased On The Phe508 Region, The Most Common Site OfDisease-Causing Delta-F508 Mutation" 100.00 25 100 100 9e-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 loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $cftr-p25 . mM . H2O 90 % . DMSO 10 % [U-2H] stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.8 loop_ _Task REFINEMENT stop_ _Details BRUNGER save_ save_NMRVIEW2.1 _Saveframe_category software _Name NMRVIEW2.1 loop_ _Task "STRUCTURE SOLUTION" stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Details ; NOESY COSY TOCSY ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions 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 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 H2O H 1 'water protons' ppm 4.773 internal direct spherical internal parallel_to_Bo 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts 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)" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 PRO HA H 4.48 . 1 2 2 PRO HB2 H 2.13 . 4 3 2 PRO HB3 H 2.29 . 4 4 2 PRO HG2 H 2.04 . 4 5 2 PRO HG3 H 1.97 . 4 6 2 PRO HD2 H 3.64 . 1 7 3 GLY H H 8.50 . 1 8 3 GLY HA2 H 3.99 . 2 9 3 GLY HA3 H 3.93 . 2 10 4 THR H H 7.99 . 1 11 4 THR HA H 4.30 . 1 12 4 THR HB H 4.12 . 1 13 4 THR HG2 H 1.14 . 1 14 5 ILE H H 8.18 . 1 15 5 ILE HA H 4.14 . 1 16 5 ILE HB H 1.80 . 1 17 5 ILE HG12 H 1.14 . 2 18 5 ILE HG13 H 1.44 . 2 19 5 ILE HG2 H 0.84 . 1 20 5 ILE HD1 H 0.80 . 1 21 6 LYS H H 8.36 . 1 22 6 LYS HA H 4.26 . 1 23 6 LYS HB2 H 1.75 . 4 24 6 LYS HB3 H 1.68 . 4 25 6 LYS HG2 H 1.63 . 4 26 6 LYS HG3 H 1.39 . 4 27 6 LYS HD2 H 1.34 . 4 28 6 LYS HE2 H 2.94 . 3 29 7 GLU H H 8.29 . 1 30 7 GLU HA H 4.30 . 1 31 7 GLU HB2 H 1.89 . 4 32 7 GLU HG2 H 2.02 . 4 33 7 GLU HG3 H 2.37 . 4 34 8 ASN H H 8.49 . 1 35 8 ASN HA H 4.65 . 1 36 8 ASN HB2 H 2.74 . 2 37 8 ASN HB3 H 2.67 . 2 38 9 ILE H H 8.06 . 1 39 9 ILE HA H 4.13 . 1 40 9 ILE HB H 1.81 . 1 41 9 ILE HG12 H 1.11 . 2 42 9 ILE HG13 H 1.38 . 2 43 9 ILE HG2 H 0.81 . 1 44 10 ILE H H 8.17 . 1 45 10 ILE HA H 4.09 . 1 46 10 ILE HB H 1.81 . 4 47 10 ILE HG12 H 1.15 . 4 48 10 ILE HG2 H 0.86 . 1 49 10 ILE HD1 H 0.80 . 1 50 11 GLY H H 8.35 . 1 51 11 GLY HA2 H 3.91 . 2 52 12 VAL H H 7.91 . 1 53 12 VAL HA H 4.10 . 1 54 12 VAL HB H 1.99 . 1 55 12 VAL HG1 H 0.83 . 2 56 12 VAL HG2 H 0.81 . 2 57 13 SER H H 8.27 . 1 58 13 SER HA H 4.39 . 1 59 13 SER HB2 H 3.76 . 2 60 13 SER HB3 H 3.79 . 2 61 14 TYR H H 8.20 . 1 62 14 TYR HA H 4.45 . 1 63 14 TYR HB2 H 2.99 . 2 64 14 TYR HB3 H 2.93 . 2 65 14 TYR HD1 H 7.05 . 1 66 14 TYR HD2 H 7.05 . 1 67 14 TYR HE1 H 6.74 . 1 68 14 TYR HE2 H 6.74 . 1 69 15 ASP H H 8.28 . 1 70 15 ASP HA H 4.51 . 1 71 15 ASP HB2 H 2.74 . 2 72 15 ASP HB3 H 2.68 . 2 73 16 GLU H H 8.11 . 1 74 16 GLU HA H 4.11 . 1 75 16 GLU HB2 H 2.21 . 4 76 16 GLU HG2 H 1.90 . 4 77 17 TYR H H 8.01 . 1 78 17 TYR HA H 4.40 . 1 79 17 TYR HB2 H 2.98 . 2 80 17 TYR HB3 H 2.88 . 2 81 17 TYR HD1 H 7.04 . 1 82 17 TYR HD2 H 7.04 . 1 83 17 TYR HE1 H 6.75 . 1 84 17 TYR HE2 H 6.75 . 1 85 18 ARG HA H 4.06 . 1 86 18 ARG HB2 H 1.54 . 4 87 18 ARG HG2 H 1.29 . 4 88 18 ARG HD2 H 3.02 . 2 89 18 ARG H H 7.82 . 1 90 19 TYR H H 7.90 . 1 91 19 TYR HA H 4.49 . 1 92 19 TYR HB2 H 3.04 . 2 93 19 TYR HB3 H 2.87 . 2 94 19 TYR HD1 H 7.08 . 1 95 19 TYR HD2 H 7.08 . 1 96 19 TYR HE1 H 6.76 . 1 97 19 TYR HE2 H 6.76 . 1 98 20 ARG H H 7.93 . 1 99 20 ARG HA H 4.25 . 1 100 20 ARG HB2 H 1.78 . 4 101 20 ARG HG2 H 1.68 . 4 102 20 ARG HG3 H 1.53 . 4 103 20 ARG HD2 H 3.10 . 2 104 21 SER H H 8.17 . 1 105 21 SER HA H 4.39 . 1 106 21 SER HB2 H 3.78 . 2 107 22 VAL H H 8.07 . 1 108 22 VAL HA H 4.11 . 1 109 22 VAL HB H 2.03 . 1 110 22 VAL HG1 H 0.87 . 2 111 23 ILE H H 8.13 . 1 112 23 ILE HA H 4.10 . 1 113 23 ILE HB H 1.78 . 1 114 23 ILE HG12 H 1.43 . 2 115 23 ILE HG13 H 1.13 . 2 116 23 ILE HG2 H 0.86 . 1 117 23 ILE HD1 H 0.79 . 1 118 24 LYS H H 8.31 . 1 119 24 LYS HA H 4.27 . 1 120 24 LYS HB2 H 1.77 . 4 121 24 LYS HG2 H 1.69 . 4 122 24 LYS HG3 H 1.62 . 4 123 24 LYS HD2 H 1.38 . 4 124 24 LYS HE2 H 2.94 . 3 125 25 ALA H H 8.23 . 1 126 25 ALA HA H 4.21 . 1 127 25 ALA HB H 1.33 . 1 stop_ save_