data_5025 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The Solution Structure of the Complex Formed between alpha-Bungarotoxin and an 18mer Cognate Peptide Derived from the alpha1 Subunit of the Nicotinic Acetylcholine Receptor from Torpedo californica ; _BMRB_accession_number 5025 _BMRB_flat_file_name bmr5025.str _Entry_type original _Submission_date 2001-05-21 _Accession_date 2001-05-21 _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 Zeng Haoyu . . 2 Moise Leonard . . 3 Grant Marianne A. . 4 Hawrot Edward . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 309 "15N chemical shifts" 15 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-07-16 original author . stop_ _Original_release_date 2001-07-16 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The Solution Structure of the Complex Formed between alpha-Bungarotoxin and an 18mer Cognate Peptide Derived from the alpha1 Subunit of the Nicotinic Acetylcholine Receptor from Torpedo californica ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11312275 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zeng Haoyu . . 2 Moise Leonard . . 3 Grant Marianne A. . 4 Hawrot Edward . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 276 _Journal_issue 25 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 22930 _Page_last 22940 _Year 2001 _Details . loop_ _Keyword alpha-bungarotoxin 'nicotinic acetylcholine receptor' 'alpha 1 subunit' NMR 'protein-protein interaction' 'cation-pi interaction' stop_ save_ ################################## # Molecular system description # ################################## save_system_Bgtx_18mer _Saveframe_category molecular_system _Mol_system_name 'ALPHA-BUNGAROTOXIN/ACETYLCHOLINE RECEPTOR PROTEIN (ALPHA CHAIN) COMPLEX' _Abbreviation_common Bgtx/18mer _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label ALPHA-BUNGAROTOXIN $Bgtx 18mer $18mer stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Bgtx _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common alpha-neurotoxin _Abbreviation_common alpha-Ntx _Molecular_mass 7977 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 74 _Mol_residue_sequence ; IVCHTTATSPISAVTCPPGE NLCYRKMWCDAFCSSRGKVV ELGCAATCPSKKPYEEVTCC STDKCNPHPKQRPG ; loop_ _Residue_seq_code _Residue_label 1 ILE 2 VAL 3 CYS 4 HIS 5 THR 6 THR 7 ALA 8 THR 9 SER 10 PRO 11 ILE 12 SER 13 ALA 14 VAL 15 THR 16 CYS 17 PRO 18 PRO 19 GLY 20 GLU 21 ASN 22 LEU 23 CYS 24 TYR 25 ARG 26 LYS 27 MET 28 TRP 29 CYS 30 ASP 31 ALA 32 PHE 33 CYS 34 SER 35 SER 36 ARG 37 GLY 38 LYS 39 VAL 40 VAL 41 GLU 42 LEU 43 GLY 44 CYS 45 ALA 46 ALA 47 THR 48 CYS 49 PRO 50 SER 51 LYS 52 LYS 53 PRO 54 TYR 55 GLU 56 GLU 57 VAL 58 THR 59 CYS 60 CYS 61 SER 62 THR 63 ASP 64 LYS 65 CYS 66 ASN 67 PRO 68 HIS 69 PRO 70 LYS 71 GLN 72 ARG 73 PRO 74 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_18mer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 18mer _Abbreviation_common 18mer _Molecular_mass 2338 _Mol_thiol_state 'all disulfide bound' _Details ; The first 18 amino acids in the '18mer' sequence are from the Torpedo nAChR alpha 1 subunit (positions 181-198). The C-terminal amino acid is a homoserine lactone produced from Met by CNBr cleavage. The theoretical mass of the 18 amino acid sequence is 2338. The peptide used in this study was isolated by RP-HPLC and contains 19 residues in total. ; _Residue_count 19 _Mol_residue_sequence YRGWKHWVYYTCCPDTPYX loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 181 TYR 2 182 ARG 3 183 GLY 4 184 TRP 5 185 LYS 6 186 HIS 7 187 TRP 8 188 VAL 9 189 TYR 10 190 TYR 11 191 THR 12 192 CYS 13 193 CYS 14 194 PRO 15 195 ASP 16 196 THR 17 197 PRO 18 198 TYR 19 . HSL stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 SWISS-PROT P02711 'Acetylcholine receptor subunit alpha precursor' 94.74 461 100.00 100.00 1.95e-05 SWISS-PROT P02710 'Acetylcholine receptor subunit alpha precursor' 94.74 461 100.00 100.00 1.98e-05 PRF 0811252A 'acetylcholine receptor alpha' 84.21 466 100.00 100.00 1.13e-03 PIR A39718 'nicotinic acetylcholine receptor alpha chain - marbled electric ray (fragments)' 84.21 51 100.00 100.00 8.69e-02 GenBank ABS70800 'cholinergic receptor nicotinic alpha polypeptide 1 [Astatotilapia burtoni]' 94.74 459 100.00 100.00 1.05e-05 GenBank AAR29368 'acetylcholine receptor alpha subunit [Narcine tasmaniensis]' 94.74 461 100.00 100.00 2.36e-05 GenBank AAR29364 'acetylcholine receptor alpha subunit [Hypnos monopterygium]' 94.74 461 100.00 100.00 1.75e-05 GenBank AAA96705 'acetylcholine receptor alpha subunit' 94.74 461 100.00 100.00 1.98e-05 GenBank AAA96704 'acetylcholine receptor alpha-subunit' 94.74 461 100.00 100.00 2.19e-05 PDB 2BG9 'Refined Structure Of The Nicotinic Acetylcholine Receptor At 4a Resolution' 94.74 370 100.00 100.00 3.19e-05 PDB 1LXH 'Solution Structure Of Alpha-Cobratoxin Complexed With A Cognate Peptide (Minimized Average Structure)' 94.74 19 100.00 100.00 1.86e-02 PDB 1LXG 'Solution Structure Of Alpha-Cobratoxin Complexed With A Cognate Peptide (Structure Ensemble)' 94.74 19 100.00 100.00 1.86e-02 PDB 1LJZ 'Nmr Structure Of An Achr-Peptide (Torpedo Californica, Alpha-Subunit Residues 182-202) In Complex With Alpha- Bungarotoxin' 89.47 25 100.00 100.00 2.49e-02 PDB 1L4W 'Nmr Structure Of An Achr-Peptide (Torpedo Californica, Alpha-Subunit Residues 182-202) In Complex With Alpha- Bungarotoxin' 89.47 25 100.00 100.00 2.49e-02 PDB 1IDH 'The Nmr Solution Structure Of The Complex Formed Between Alpha-Bungarotoxin And An 18mer Cognate Peptide' 94.74 19 100.00 100.00 1.86e-02 PDB 1IDG 'The Nmr Solution Structure Of The Complex Formed Between Alpha-Bungarotoxin And An 18mer Cognate Peptide' 94.74 19 100.00 100.00 1.86e-02 BMRB 4838 'acetylcholine receptor peptide' 89.47 25 100.00 100.00 2.49e-02 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_HSL _Saveframe_category polymer_residue _Mol_type 'L-peptide linking' _Name_common 'HOMOSERINE LACTONE' _BMRB_code . _PDB_code HSL _Standard_residue_derivative . _Molecular_mass 101.104 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jun 8 16:53:18 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? C C C . 0 . ? O O O . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? OD OD O . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG2 HG2 H . 0 . ? HG3 HG3 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H ? ? SING N H2 ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OD ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG OD ? ? SING CG HG2 ? ? SING CG HG3 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Bgtx 'Many-banded krait' 8616 Eukaryota Metazoa Bungarus multicinctus $18mer 'Pacific electric ray' 7787 Eukaryota Metazoa Torpedo californica stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Vendor_name $Bgtx vendor . . . . . . Sigma $18mer 'recombinant technology' 'E. coli' . . 'BL21 (DE3)' plasmid 'pET 31b+' . 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 $Bgtx 2.1 mM . $18mer 2.1 mM '[U-99% 15N]' 'potassium acetate buffer' 50 mM [U-2H] H2O 95 % . D2O 5 % . 'sodium azide' 0.05 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.1 loop_ _Task collection stop_ _Details Bruker save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.8 loop_ _Task processing stop_ _Details 'Delaglio, F. et al.' save_ save_Sparky _Saveframe_category software _Name Sparky _Version 3.95 loop_ _Task 'data analysis' stop_ _Details 'Goddard, T.D. and Kneller, D.G.' save_ save_CNSsolve _Saveframe_category software _Name CNSsolve _Version 1.0 loop_ _Task refinement stop_ _Details 'Brunger, A.T. et al.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-separated_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated TOCSY' _Sample_label $sample_1 save_ save_3D_HNHA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label $sample_1 save_ save_3D_15N-separated_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label $sample_1 save_ save_2D_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label $sample_1 save_ save_2D_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _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 0.2 n/a temperature 308 1 K 'ionic strength' 29 1 mM pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_ref_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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label TSP H 1 'methyl protons' ppm 0.00 internal direct cylindrical internal perpendicular 1.0 $entry_citation $entry_citation TSP N 15 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $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_ _Experiment_label '3D 15N-separated TOCSY' '3D HNHA' '3D 15N-separated NOESY' '2D TOCSY' '2D NOESY' '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_ref_1 _Mol_system_component_name ALPHA-BUNGAROTOXIN _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 ILE HA H 4.25 0.01 1 2 . 1 ILE HG2 H 1.24 0.01 1 3 . 2 VAL HA H 5.03 0.01 1 4 . 2 VAL HB H 1.64 0.01 1 5 . 2 VAL HG1 H 0.93 0.01 2 6 . 2 VAL HG2 H 0.65 0.01 2 7 . 2 VAL H H 8.19 0.01 1 8 . 3 CYS HA H 5.15 0.01 1 9 . 3 CYS HB2 H 3.08 0.01 2 10 . 3 CYS HB3 H 2.50 0.01 2 11 . 3 CYS H H 8.83 0.01 1 12 . 4 HIS HA H 5.24 0.01 1 13 . 4 HIS HB2 H 3.05 0.01 2 14 . 4 HIS HB3 H 2.61 0.01 2 15 . 4 HIS HD2 H 6.46 0.01 2 16 . 4 HIS H H 9.41 0.01 1 17 . 5 THR HA H 5.28 0.01 1 18 . 5 THR HB H 4.08 0.01 1 19 . 5 THR HG2 H 1.41 0.01 1 20 . 5 THR H H 8.99 0.01 1 21 . 6 THR HA H 4.61 0.01 1 22 . 6 THR HB H 5.28 0.01 1 23 . 6 THR H H 8.21 0.01 1 24 . 7 ALA HA H 4.75 0.01 1 25 . 7 ALA HB H 1.65 0.01 1 26 . 7 ALA H H 9.28 0.01 1 27 . 8 THR HA H 4.58 0.01 1 28 . 8 THR HB H 4.34 0.01 1 29 . 8 THR H H 7.15 0.01 1 30 . 9 SER HA H 4.43 0.01 1 31 . 9 SER HB2 H 2.89 0.01 2 32 . 9 SER H H 8.15 0.01 1 33 . 10 PRO HA H 4.95 0.01 1 34 . 10 PRO HB2 H 2.23 0.01 2 35 . 10 PRO HD2 H 3.40 0.01 2 36 . 10 PRO HG2 H 1.89 0.01 2 37 . 10 PRO HG3 H 1.64 0.01 2 38 . 11 ILE HA H 3.89 0.01 1 39 . 11 ILE HB H 0.93 0.01 1 40 . 11 ILE HG2 H 0.41 0.01 1 41 . 11 ILE H H 8.72 0.01 1 42 . 12 SER HA H 5.03 0.01 1 43 . 12 SER HB2 H 3.84 0.01 2 44 . 12 SER HB3 H 3.92 0.01 2 45 . 12 SER H H 7.66 0.01 1 46 . 13 ALA HA H 5.14 0.01 1 47 . 13 ALA HB H 0.95 0.01 1 48 . 13 ALA H H 8.31 0.01 1 49 . 14 VAL HA H 4.64 0.01 1 50 . 14 VAL HG1 H 0.94 0.01 2 51 . 14 VAL H H 8.93 0.01 1 52 . 15 THR HA H 4.51 0.01 1 53 . 15 THR HB H 4.09 0.01 1 54 . 15 THR HG2 H 1.32 0.01 1 55 . 15 THR H H 8.56 0.01 1 56 . 16 CYS HA H 4.95 0.01 1 57 . 16 CYS HB2 H 3.35 0.01 2 58 . 16 CYS HB3 H 3.11 0.01 2 59 . 16 CYS H H 8.93 0.01 1 60 . 19 GLY HA2 H 4.38 0.01 2 61 . 19 GLY HA3 H 3.75 0.01 2 62 . 19 GLY H H 8.85 0.01 1 63 . 20 GLU HA H 4.40 0.01 1 64 . 20 GLU HB2 H 2.34 0.01 2 65 . 20 GLU HB3 H 2.30 0.01 2 66 . 20 GLU H H 7.94 0.01 1 67 . 21 ASN HA H 5.05 0.01 1 68 . 21 ASN HB2 H 3.10 0.01 2 69 . 21 ASN HB3 H 2.74 0.01 2 70 . 21 ASN H H 8.07 0.01 1 71 . 22 LEU HA H 5.05 0.01 1 72 . 22 LEU HB2 H 1.78 0.01 2 73 . 22 LEU HB3 H 1.56 0.01 2 74 . 22 LEU HD1 H 0.82 0.01 2 75 . 22 LEU HG H 1.66 0.01 1 76 . 22 LEU H H 8.33 0.01 1 77 . 23 CYS HA H 6.01 0.01 1 78 . 23 CYS HB2 H 3.31 0.01 2 79 . 23 CYS HB3 H 2.95 0.01 2 80 . 23 CYS H H 8.83 0.01 1 81 . 24 TYR HA H 6.08 0.01 1 82 . 24 TYR HB2 H 3.10 0.01 2 83 . 24 TYR HB3 H 2.76 0.01 2 84 . 24 TYR HD1 H 6.75 0.01 2 85 . 24 TYR H H 9.06 0.01 1 86 . 25 ARG HA H 5.37 0.01 1 87 . 25 ARG HB2 H 2.01 0.01 2 88 . 25 ARG H H 9.11 0.01 1 89 . 26 LYS HA H 5.93 0.01 1 90 . 26 LYS HB2 H 2.24 0.01 2 91 . 26 LYS HB3 H 2.00 0.01 2 92 . 26 LYS HG2 H 1.72 0.01 2 93 . 26 LYS H H 9.94 0.01 1 94 . 27 MET HA H 6.28 0.01 1 95 . 27 MET HB2 H 2.08 0.01 2 96 . 27 MET H H 9.30 0.01 1 97 . 28 TRP HA H 5.26 0.01 1 98 . 28 TRP HB2 H 3.87 0.01 2 99 . 28 TRP H H 8.15 0.01 1 100 . 29 CYS HA H 5.48 0.01 1 101 . 29 CYS HB2 H 3.54 0.01 2 102 . 29 CYS HB3 H 3.15 0.01 2 103 . 29 CYS H H 9.64 0.01 1 104 . 30 ASP HA H 5.08 0.01 1 105 . 30 ASP H H 9.41 0.01 1 106 . 31 ALA HA H 4.15 0.01 1 107 . 31 ALA HB H 1.14 0.01 1 108 . 31 ALA H H 8.17 0.01 1 109 . 32 PHE HA H 4.80 0.01 1 110 . 32 PHE HB2 H 2.82 0.01 2 111 . 32 PHE H H 8.88 0.01 1 112 . 33 CYS HA H 4.79 0.01 1 113 . 33 CYS HB2 H 3.94 0.01 2 114 . 33 CYS H H 7.75 0.01 1 115 . 34 SER HA H 4.35 0.01 1 116 . 34 SER HB2 H 4.05 0.01 2 117 . 34 SER H H 9.05 0.01 1 118 . 35 SER HA H 4.78 0.01 1 119 . 35 SER HB2 H 3.94 0.01 2 120 . 35 SER H H 7.68 0.01 1 121 . 36 ARG HA H 4.55 0.01 1 122 . 36 ARG HB2 H 1.93 0.01 2 123 . 36 ARG HG2 H 1.75 0.01 2 124 . 36 ARG H H 8.17 0.01 1 125 . 37 GLY HA2 H 4.90 0.01 2 126 . 37 GLY HA3 H 3.89 0.01 2 127 . 37 GLY H H 7.33 0.01 1 128 . 38 LYS HA H 4.38 0.01 1 129 . 38 LYS HB2 H 2.12 0.01 2 130 . 38 LYS HD2 H 1.73 0.01 2 131 . 38 LYS HG2 H 1.51 0.01 2 132 . 38 LYS H H 7.95 0.01 1 133 . 39 VAL HA H 3.66 0.01 1 134 . 39 VAL HB H 0.22 0.01 1 135 . 39 VAL HG1 H 0.48 0.01 2 136 . 39 VAL HG2 H 0.37 0.01 2 137 . 39 VAL H H 8.75 0.01 1 138 . 40 VAL HA H 4.62 0.01 1 139 . 40 VAL HB H 0.61 0.01 1 140 . 40 VAL HG1 H 0.54 0.01 2 141 . 40 VAL H H 8.36 0.01 1 142 . 41 GLU HA H 5.10 0.01 1 143 . 41 GLU HB2 H 2.42 0.01 2 144 . 41 GLU H H 9.32 0.01 1 145 . 42 LEU HA H 5.19 0.01 1 146 . 42 LEU HG H 1.60 0.01 1 147 . 42 LEU H H 8.79 0.01 1 148 . 43 GLY HA2 H 4.42 0.01 2 149 . 43 GLY HA3 H 4.10 0.01 2 150 . 43 GLY H H 6.80 0.01 1 151 . 44 CYS HA H 5.67 0.01 1 152 . 44 CYS HB2 H 3.36 0.01 2 153 . 44 CYS HB3 H 3.15 0.01 2 154 . 44 CYS H H 8.48 0.01 1 155 . 45 ALA HA H 4.67 0.01 1 156 . 45 ALA HB H 1.48 0.01 1 157 . 45 ALA H H 9.45 0.01 1 158 . 46 ALA HA H 4.93 0.01 1 159 . 46 ALA HB H 1.62 0.01 1 160 . 46 ALA H H 8.83 0.01 1 161 . 47 THR HA H 4.42 0.01 1 162 . 47 THR HB H 4.06 0.01 1 163 . 47 THR HG2 H 1.22 0.01 1 164 . 47 THR H H 7.47 0.01 1 165 . 48 CYS HA H 4.64 0.01 1 166 . 48 CYS HB2 H 3.00 0.01 2 167 . 48 CYS H H 9.08 0.01 1 168 . 49 PRO HA H 4.19 0.01 1 169 . 49 PRO HB2 H 2.18 0.01 2 170 . 50 SER HA H 4.27 0.01 1 171 . 50 SER HB2 H 3.91 0.01 2 172 . 50 SER HB3 H 3.84 0.01 2 173 . 50 SER H H 8.08 0.01 1 174 . 51 LYS HA H 4.49 0.01 1 175 . 51 LYS HB2 H 1.95 0.01 2 176 . 51 LYS HG2 H 1.38 0.01 2 177 . 51 LYS H H 8.35 0.01 1 178 . 52 LYS HA H 4.59 0.01 1 179 . 52 LYS HB2 H 1.97 0.01 2 180 . 52 LYS HD2 H 1.57 0.01 2 181 . 52 LYS HG2 H 1.45 0.01 2 182 . 52 LYS H H 8.61 0.01 1 183 . 54 TYR HA H 4.62 0.01 1 184 . 54 TYR HB2 H 3.26 0.01 2 185 . 54 TYR HE1 H 6.90 0.01 3 186 . 54 TYR H H 7.32 0.01 1 187 . 55 GLU HA H 5.19 0.01 1 188 . 55 GLU HB2 H 2.21 0.01 2 189 . 55 GLU HG2 H 2.04 0.01 2 190 . 55 GLU HG3 H 1.94 0.01 2 191 . 55 GLU H H 7.77 0.01 1 192 . 56 GLU HA H 4.87 0.01 1 193 . 56 GLU HB2 H 2.39 0.01 2 194 . 56 GLU HG2 H 2.20 0.01 2 195 . 56 GLU HG3 H 2.11 0.01 2 196 . 56 GLU H H 8.99 0.01 1 197 . 57 VAL HA H 5.38 0.01 1 198 . 57 VAL HB H 0.98 0.01 1 199 . 57 VAL HG1 H 1.04 0.01 2 200 . 57 VAL HG2 H 0.93 0.01 2 201 . 57 VAL H H 8.61 0.01 1 202 . 58 THR HA H 4.84 0.01 1 203 . 58 THR HB H 4.09 0.01 1 204 . 58 THR HG2 H 1.31 0.01 1 205 . 58 THR H H 9.17 0.01 1 206 . 59 CYS HA H 5.70 0.01 1 207 . 59 CYS HB2 H 3.81 0.01 2 208 . 59 CYS HB3 H 3.09 0.01 2 209 . 59 CYS H H 9.21 0.01 1 210 . 60 CYS HA H 5.21 0.01 1 211 . 60 CYS HB2 H 3.70 0.01 2 212 . 60 CYS H H 9.28 0.01 1 213 . 61 SER HA H 5.02 0.01 1 214 . 61 SER HB2 H 4.27 0.01 2 215 . 61 SER HB3 H 3.89 0.01 2 216 . 61 SER H H 8.94 0.01 1 217 . 62 THR HA H 4.82 0.01 1 218 . 62 THR HB H 4.35 0.01 1 219 . 62 THR H H 7.56 0.01 1 220 . 63 ASP HA H 4.87 0.01 1 221 . 63 ASP HB2 H 2.39 0.01 2 222 . 63 ASP H H 8.39 0.01 1 223 . 64 LYS HA H 3.20 0.01 1 224 . 64 LYS HB2 H 1.06 0.01 2 225 . 64 LYS HB3 H 0.40 0.01 2 226 . 64 LYS HG2 H 1.63 0.01 2 227 . 64 LYS H H 10.01 0.01 1 228 . 65 CYS HA H 4.63 0.01 1 229 . 65 CYS HB2 H 3.85 0.01 2 230 . 65 CYS HB3 H 3.61 0.01 2 231 . 65 CYS H H 7.72 0.01 1 232 . 66 ASN HA H 5.03 0.01 1 233 . 66 ASN HB2 H 2.11 0.01 2 234 . 66 ASN H H 9.02 0.01 1 235 . 67 PRO HA H 3.69 0.01 1 236 . 68 HIS HA H 4.03 0.01 1 237 . 68 HIS HB2 H 2.83 0.01 2 238 . 68 HIS HB3 H 2.75 0.01 2 239 . 68 HIS H H 8.51 0.01 1 240 . 69 PRO HA H 4.53 0.01 1 241 . 69 PRO HG2 H 2.04 0.01 2 242 . 69 PRO HG3 H 1.56 0.01 2 243 . 70 LYS HA H 4.65 0.01 1 244 . 70 LYS HB2 H 1.84 0.01 2 245 . 70 LYS HE2 H 2.22 0.01 3 246 . 70 LYS HG2 H 1.63 0.01 2 247 . 70 LYS H H 10.37 0.01 1 248 . 71 GLN HA H 4.40 0.01 1 249 . 71 GLN HB2 H 1.83 0.01 2 250 . 71 GLN H H 8.37 0.01 1 251 . 72 ARG HA H 4.38 0.01 1 252 . 72 ARG HB2 H 2.21 0.01 2 253 . 72 ARG HG2 H 2.10 0.01 2 254 . 72 ARG HG3 H 2.04 0.01 2 255 . 72 ARG H H 8.14 0.01 1 256 . 74 GLY HA2 H 3.89 0.01 2 257 . 74 GLY HA3 H 3.77 0.01 2 258 . 74 GLY H H 7.95 0.01 1 stop_ save_ save_chemical_shift_set_2 _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_ref_1 _Mol_system_component_name 18mer _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 . 2 ARG HA H 4.38 0.01 1 2 . 2 ARG H H 8.55 0.01 1 3 . 2 ARG N N 124.71 0.01 1 4 . 3 GLY HA2 H 4.01 0.01 2 5 . 3 GLY H H 8.11 0.01 1 6 . 3 GLY N N 110.18 0.01 1 7 . 4 TRP HA H 4.83 0.01 1 8 . 4 TRP HB2 H 3.29 0.01 2 9 . 4 TRP H H 8.05 0.01 1 10 . 4 TRP N N 120.73 0.01 1 11 . 5 LYS HA H 4.17 0.01 1 12 . 5 LYS HB2 H 1.16 0.01 2 13 . 5 LYS H H 8.10 0.01 1 14 . 5 LYS N N 122.84 0.01 1 15 . 6 HIS HA H 4.56 0.01 1 16 . 6 HIS HB2 H 3.18 0.01 2 17 . 6 HIS HB3 H 3.01 0.01 2 18 . 6 HIS H H 7.98 0.01 1 19 . 6 HIS N N 118.85 0.01 1 20 . 7 TRP HA H 4.97 0.01 1 21 . 7 TRP HB2 H 3.23 0.01 2 22 . 7 TRP HB3 H 3.13 0.01 2 23 . 7 TRP H H 7.56 0.01 1 24 . 7 TRP N N 121.43 0.01 1 25 . 8 VAL HA H 4.52 0.01 1 26 . 8 VAL HB H 2.04 0.01 1 27 . 8 VAL HG1 H 1.03 0.01 2 28 . 8 VAL HG2 H 0.78 0.01 2 29 . 8 VAL H H 8.96 0.01 1 30 . 8 VAL N N 122.84 0.01 1 31 . 9 TYR HA H 5.44 0.01 1 32 . 9 TYR HB2 H 3.26 0.01 2 33 . 9 TYR HB3 H 2.84 0.01 2 34 . 9 TYR H H 8.79 0.01 1 35 . 9 TYR N N 124.01 0.01 1 36 . 10 TYR HA H 5.43 0.01 1 37 . 10 TYR HB2 H 3.32 0.01 2 38 . 10 TYR HB3 H 2.95 0.01 2 39 . 10 TYR H H 9.57 0.01 1 40 . 10 TYR N N 116.51 0.01 1 41 . 11 THR HA H 3.70 0.01 1 42 . 11 THR H H 9.48 0.01 1 43 . 11 THR N N 119.32 0.01 1 44 . 12 CYS HA H 4.70 0.01 1 45 . 12 CYS HB2 H 3.15 0.01 2 46 . 12 CYS H H 9.40 0.01 1 47 . 12 CYS N N 120.49 0.01 1 48 . 13 CYS HA H 4.79 0.01 1 49 . 13 CYS HB2 H 2.40 0.01 2 50 . 13 CYS H H 8.94 0.01 1 51 . 13 CYS N N 114.63 0.01 1 52 . 15 ASP HA H 4.94 0.01 1 53 . 15 ASP HB2 H 2.92 0.01 2 54 . 15 ASP HB3 H 2.65 0.01 2 55 . 15 ASP H H 8.22 0.01 1 56 . 15 ASP N N 112.52 0.01 1 57 . 16 THR HA H 4.77 0.01 1 58 . 16 THR HB H 4.01 0.01 1 59 . 16 THR HG2 H 0.96 0.01 1 60 . 16 THR H H 7.08 0.01 1 61 . 16 THR N N 111.82 0.01 1 62 . 18 TYR HA H 5.52 0.01 1 63 . 18 TYR HB2 H 4.04 0.01 2 64 . 18 TYR HB3 H 3.57 0.01 2 65 . 18 TYR H H 7.37 0.01 1 66 . 18 TYR N N 111.59 0.01 1 stop_ save_