data_5601 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Complete 1H,13C,15N assignments of zinc Pyrococcus furiosus rubredoxin ; _BMRB_accession_number 5601 _BMRB_flat_file_name bmr5601.str _Entry_type original _Submission_date 2002-11-26 _Accession_date 2002-11-26 _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 Bougault Catherine M. . 2 Eidsness Marly K. . 3 Prestegard James H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 3 coupling_constants 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 478 "13C chemical shifts" 550 "15N chemical shifts" 159 "coupling constants" 96 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-30 update BMRB 'Updating non-standard residue' 2003-05-14 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4051 'CpRdFe(III) 1H,13C,15N data' 4050 'CpRdFe(II) 1H,13C,15N data' 4182 'CpRdFe(II) 1H data' 4137 'CpRdFe(II) and CpRdFe(III) 1H/2H isotopic shifts' 4066 'CpRdFe(II) and CpRdFe(III) 15N hyperfine shifts' 4319 'CpRdFe(III) 1H-15N and 1H-13C dipolar shifts' 4320 'CpRdFe(II) 1H-15N and 1H-13C dipolar shifts' 5600 'CpRdZn(II) 1H,13C,15N data' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Hydrogen Bonds in Rubredoxins from Mesophilic and Hyperthermophilic Organisms' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22580601 _PubMed_ID 12693931 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bougault Catherine M. . 2 Eidsness Marly K. . 3 Prestegard James H. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 42 _Journal_issue 15 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4357 _Page_last 4372 _Year 2003 _Details . loop_ _Keyword rubredoxin 'pyrococcus furiosus' assignment 'scalar couplings' stop_ save_ ################################## # Molecular system description # ################################## save_PfRdZn _Saveframe_category molecular_system _Mol_system_name rubredoxin _Abbreviation_common PfRdZn _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label fMetPfRdZn $fMetPfRd Zn1 $ZN MetPfRdZn $MetPfRd Zn2 $ZN WT-PfRdZn $WT-PfRdZn Zn3 $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' loop_ _Biological_function 'electron transfer' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_fMetPfRd _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'pyrococcus furiosus rubredoxin' _Name_variant fMetPfRd _Abbreviation_common fMetPfRd _Molecular_mass 6443.68 _Mol_thiol_state 'all other bound' _Details ; X=FME The given mass takes into account the uniform 13C, 15N labeling. ; ############################## # Polymer residue sequence # ############################## _Residue_count 54 _Mol_residue_sequence ; XAKWVCKICGYIYDEDAGDP DNGISPGTKFEELPDDWVCP ICGAPKSEFEKLED ; loop_ _Residue_seq_code _Residue_label 1 FME 2 ALA 3 LYS 4 TRP 5 VAL 6 CYS 7 LYS 8 ILE 9 CYS 10 GLY 11 TYR 12 ILE 13 TYR 14 ASP 15 GLU 16 ASP 17 ALA 18 GLY 19 ASP 20 PRO 21 ASP 22 ASN 23 GLY 24 ILE 25 SER 26 PRO 27 GLY 28 THR 29 LYS 30 PHE 31 GLU 32 GLU 33 LEU 34 PRO 35 ASP 36 ASP 37 TRP 38 VAL 39 CYS 40 PRO 41 ILE 42 CYS 43 GLY 44 ALA 45 PRO 46 LYS 47 SER 48 GLU 49 PHE 50 GLU 51 LYS 52 LEU 53 GLU 54 ASP stop_ _Sequence_homology_query_date 2008-03-24 _Sequence_homology_query_revised_last_date 2008-01-16 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 P24297 'RUBR_PYRFU Rubredoxin (Rd)' 100.00 54 100 100 3e-27 REF NP_579011.1 'rubredoxin [Pyrococcus furiosus DSM3638]' 100.00 54 100 100 3e-27 GenBank AAL81406.1 'rubredoxin [Pyrococcus furiosus DSM3638]' 100.00 54 100 100 3e-27 GenBank AAF03228.1 'AF156097_8 rubredoxin [Pyrococcusfuriosus]' 100.00 54 100 100 3e-27 GenBank AAB20233.1 'rubredoxin, Rd [Pyrococcus furiosus,DSM 3638, Peptide, 53 aa]' 101.89 53 100 100 3e-27 PDB 1BQ9 'A Chain A, Rubredoxin (Formyl MethionineMutant) From Pyrococcus Furiosus' 100.00 54 100 100 3e-27 PDB 1BQ8 'A Chain A, Rubredoxin (Methionine Mutant)From Pyrococcus Furiosus' 100.00 54 100 100 3e-27 PDB 1ZRP 'A Chain A, Solution-State Structure By NmrOf Zinc-Substituted Rubredoxin From The MarineHyperthermophilic Archaebacteriu' 101.89 53 100 100 3e-27 PDB 1VCX 'A Chain A, Neutron Crystal Structure Of TheWild Type Rubredoxin From Pyrococcus Furiosus At 1.5aResolution' 101.89 53 100 100 8e-27 PDB 1CAD 'A Chain A, X-Ray Crystal Structures Of TheOxidized And Reduced Forms Of The Rubredoxin From TheMarine Hyperthermophilic' 101.89 53 100 100 3e-27 PDB 1CAA 'A Chain A, X-Ray Crystal Structures Of TheOxidized And Reduced Forms Of The Rubredoxin From TheMarine Hyperthermophilic' 101.89 53 100 100 3e-27 PDB 1BRF 'A Chain A, Rubredoxin (Wild Type) FromPyrococcus Furiosus' 101.89 53 100 100 3e-27 BMRB 5601 'pyrococcus furiosus rubredoxin' 100.00 54 100 100 3e-27 BMRB 5601 'pyrococcus furiosus rubredoxin' 100.00 54 100 100 3e-27 BMRB 1991 rubredoxin 101.89 53 100 100 3e-27 stop_ save_ save_MetPfRd _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'pyrococcus furiosus rubredoxin' _Name_variant MetPfRd _Abbreviation_common MetPfRd _Molecular_mass 6414.67 _Mol_thiol_state 'all other bound' _Details 'The given mass takes into account the uniform 13C, 15N labeling.' _Residue_count 54 _Mol_residue_sequence ; MAKWVCKICGYIYDEDAGDP DNGISPGTKFEELPDDWVCP ICGAPKSEFEKLED ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 LYS 4 TRP 5 VAL 6 CYS 7 LYS 8 ILE 9 CYS 10 GLY 11 TYR 12 ILE 13 TYR 14 ASP 15 GLU 16 ASP 17 ALA 18 GLY 19 ASP 20 PRO 21 ASP 22 ASN 23 GLY 24 ILE 25 SER 26 PRO 27 GLY 28 THR 29 LYS 30 PHE 31 GLU 32 GLU 33 LEU 34 PRO 35 ASP 36 ASP 37 TRP 38 VAL 39 CYS 40 PRO 41 ILE 42 CYS 43 GLY 44 ALA 45 PRO 46 LYS 47 SER 48 GLU 49 PHE 50 GLU 51 LYS 52 LEU 53 GLU 54 ASP stop_ _Sequence_homology_query_date 2008-03-24 _Sequence_homology_query_revised_last_date 2008-01-16 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 P24297 'RUBR_PYRFU Rubredoxin (Rd)' 100.00 54 100 100 7e-28 REF NP_579011.1 'rubredoxin [Pyrococcus furiosus DSM3638]' 100.00 54 100 100 7e-28 GenBank AAL81406.1 'rubredoxin [Pyrococcus furiosus DSM3638]' 100.00 54 100 100 7e-28 GenBank AAF03228.1 'AF156097_8 rubredoxin [Pyrococcusfuriosus]' 100.00 54 100 100 7e-28 GenBank AAB20233.1 'rubredoxin, Rd [Pyrococcus furiosus,DSM 3638, Peptide, 53 aa]' 101.89 53 100 100 3e-27 PDB 1BQ9 'A Chain A, Rubredoxin (Formyl MethionineMutant) From Pyrococcus Furiosus' 100.00 54 100 100 3e-27 PDB 1BQ8 'A Chain A, Rubredoxin (Methionine Mutant)From Pyrococcus Furiosus' 100.00 54 100 100 7e-28 PDB 1ZRP 'A Chain A, Solution-State Structure By NmrOf Zinc-Substituted Rubredoxin From The MarineHyperthermophilic Archaebacteriu' 101.89 53 100 100 3e-27 PDB 1VCX 'A Chain A, Neutron Crystal Structure Of TheWild Type Rubredoxin From Pyrococcus Furiosus At 1.5aResolution' 101.89 53 100 100 8e-27 PDB 1CAD 'A Chain A, X-Ray Crystal Structures Of TheOxidized And Reduced Forms Of The Rubredoxin From TheMarine Hyperthermophilic' 101.89 53 100 100 3e-27 PDB 1CAA 'A Chain A, X-Ray Crystal Structures Of TheOxidized And Reduced Forms Of The Rubredoxin From TheMarine Hyperthermophilic' 101.89 53 100 100 3e-27 PDB 1BRF 'A Chain A, Rubredoxin (Wild Type) FromPyrococcus Furiosus' 101.89 53 100 100 3e-27 BMRB 5601 'pyrococcus furiosus rubredoxin' 100.00 54 100 100 3e-27 BMRB 5601 'pyrococcus furiosus rubredoxin' 101.89 53 100 100 3e-27 BMRB 1991 rubredoxin 101.89 53 100 100 3e-27 stop_ save_ save_WT-PfRdZn _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'pyrococcus furiosus rubredoxin' _Abbreviation_common WT-PfRdZn _Molecular_mass 6277.52 _Mol_thiol_state 'all other bound' _Details 'The given mass takes into account the uniform 13C, 15N labeling. Wild type form of the protein.' _Residue_count 53 _Mol_residue_sequence ; AKWVCKICGYIYDEDAGDPD NGISPGTKFEELPDDWVCPI CGAPKSEFEKLED ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 ALA 2 3 LYS 3 4 TRP 4 5 VAL 5 6 CYS 6 7 LYS 7 8 ILE 8 9 CYS 9 10 GLY 10 11 TYR 11 12 ILE 12 13 TYR 13 14 ASP 14 15 GLU 15 16 ASP 16 17 ALA 17 18 GLY 18 19 ASP 19 20 PRO 20 21 ASP 21 22 ASN 22 23 GLY 23 24 ILE 24 25 SER 25 26 PRO 26 27 GLY 27 28 THR 28 29 LYS 29 30 PHE 30 31 GLU 31 32 GLU 32 33 LEU 33 34 PRO 34 35 ASP 35 36 ASP 36 37 TRP 37 38 VAL 38 39 CYS 39 40 PRO 40 41 ILE 41 42 CYS 42 43 GLY 43 44 ALA 44 45 PRO 45 46 LYS 46 47 SER 47 48 GLU 48 49 PHE 49 50 GLU 50 51 LYS 51 52 LEU 52 53 GLU 53 54 ASP stop_ _Sequence_homology_query_date 2008-03-24 _Sequence_homology_query_revised_last_date 2007-11-12 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 P24297 'RUBR_PYRFU Rubredoxin (Rd)' 98.15 54 100 100 3e-27 REF NP_579011.1 'rubredoxin [Pyrococcus furiosus DSM3638]' 98.15 54 100 100 3e-27 GenBank AAL81406.1 'rubredoxin [Pyrococcus furiosus DSM3638]' 98.15 54 100 100 3e-27 GenBank AAF03228.1 'AF156097_8 rubredoxin [Pyrococcusfuriosus]' 98.15 54 100 100 3e-27 GenBank AAB20233.1 'rubredoxin, Rd [Pyrococcus furiosus,DSM 3638, Peptide, 53 aa]' 100.00 53 100 100 3e-27 PDB 1BQ9 'A Chain A, Rubredoxin (Formyl MethionineMutant) From Pyrococcus Furiosus' 98.15 54 100 100 3e-27 PDB 1BQ8 'A Chain A, Rubredoxin (Methionine Mutant)From Pyrococcus Furiosus' 98.15 54 100 100 3e-27 PDB 1ZRP 'A Chain A, Solution-State Structure By NmrOf Zinc-Substituted Rubredoxin From The MarineHyperthermophilic Archaebacteriu' 100.00 53 100 100 3e-27 PDB 1VCX 'A Chain A, Neutron Crystal Structure Of TheWild Type Rubredoxin From Pyrococcus Furiosus At 1.5aResolution' 100.00 53 100 100 8e-27 PDB 1CAD 'A Chain A, X-Ray Crystal Structures Of TheOxidized And Reduced Forms Of The Rubredoxin From TheMarine Hyperthermophilic' 100.00 53 100 100 3e-27 PDB 1CAA 'A Chain A, X-Ray Crystal Structures Of TheOxidized And Reduced Forms Of The Rubredoxin From TheMarine Hyperthermophilic' 100.00 53 100 100 3e-27 PDB 1BRF 'A Chain A, Rubredoxin (Wild Type) FromPyrococcus Furiosus' 100.00 53 100 100 3e-27 BMRB 5601 'pyrococcus furiosus rubredoxin' 98.15 54 100 100 3e-27 BMRB 5601 'pyrococcus furiosus rubredoxin' 98.15 54 100 100 3e-27 BMRB 1991 rubredoxin 100.00 53 100 100 3e-27 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_FME _Saveframe_category polymer_residue _Mol_type 'L-peptide linking' _Name_common N-FORMYLMETHIONINE _BMRB_code . _PDB_code FME _Standard_residue_derivative . _Molecular_mass 177.221 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jul 25 14:49:33 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CN CN C . 0 . ? O1 O1 O . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? SD SD S . 0 . ? CE CE C . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? HCN HCN H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG2 HG2 H . 0 . ? HG3 HG3 H . 0 . ? HE1 HE1 H . 0 . ? HE2 HE2 H . 0 . ? HE3 HE3 H . 0 . ? HXT HXT 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 CN ? ? SING N CA ? ? SING N H ? ? DOUB CN O1 ? ? SING CN HCN ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG SD ? ? SING CG HG2 ? ? SING CG HG3 ? ? SING SD CE ? ? SING CE HE1 ? ? SING CE HE2 ? ? SING CE HE3 ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jul 25 12:24:02 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $WT-PfRdZn 'Pyrococcus furiosus' 2261 Archaea . Pyrococcus furiosus 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 $WT-PfRdZn 'recombinant technology' 'E. coli' Escherichia coli 'BL21 DE3' plasmid 'pEt T7' $fMetPfRd 'recombinant technology' 'E. coli' Escherichia coli 'BL21 DE3' plasmid 'pEt T7' $MetPfRd 'recombinant technology' 'E. coli' Escherichia coli 'BL21 DE3' plasmid 'pEt T7' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; This sample contains three forms of Pyrococcus furiosus rubredoxin a Met-form, a N-formylmethionine form, and the wild-type form missing the first methionine residue ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $fMetPfRd 3.29 mM 2.84 3.27 '[U-100% 13C; U-100% 15N]' $MetPfRd 0.65 mM 0.22 0.87 '[U-100% 13C; U-100% 15N]' $WT-PfRdZn 0.65 mM 0.22 0.87 '[U-100% 13C; U-100% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 2000 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _Sample_label $sample_1 save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_HCACO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCACO _Sample_label $sample_1 save_ save_1H-13C_HSQC-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC-TOCSY' _Sample_label $sample_1 save_ save_1H-13C_HSQC-NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC-NOESY' _Sample_label $sample_1 save_ save_(HB)CB(CGCD)HD_8 _Saveframe_category NMR_applied_experiment _Experiment_name (HB)CB(CGCD)HD _Sample_label $sample_1 save_ save_(HB)CB(CGCDCE)HE_9 _Saveframe_category NMR_applied_experiment _Experiment_name (HB)CB(CGCDCE)HE _Sample_label $sample_1 save_ save_HCCH-TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_1 save_ save_HCCO2_11 _Saveframe_category NMR_applied_experiment _Experiment_name HCCO2 _Sample_label $sample_1 save_ save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCACO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC-NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name (HB)CB(CGCD)HD _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name (HB)CB(CGCDCE)HE _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name HCCO2 _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.44 0.05 na temperature 298 0.5 K 'ionic strength' 0.29 0.01 M 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 '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_fMetPfRdZn_shift _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N HSQC' '1H-13C HSQC' HNCO HNCACB HCACO '1H-13C HSQC-TOCSY' '1H-13C HSQC-NOESY' (HB)CB(CGCD)HD (HB)CB(CGCDCE)HE HCCH-TOCSY HCCO2 stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name fMetPfRdZn _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 FME HCN H 8.19 0.01 1 2 . 1 FME H H 8.59 0.01 1 3 . 1 FME HA H 4.70 0.01 1 4 . 1 FME HB2 H 2.46 0.01 2 5 . 1 FME HB3 H 2.00 0.01 2 6 . 1 FME HG2 H 2.77 0.01 2 7 . 1 FME HG3 H 2.48 0.01 2 8 . 1 FME HE1 H 2.07 0.01 1 9 . 1 FME HE2 H 2.07 0.01 1 10 . 1 FME HE3 H 2.07 0.01 1 11 . 1 FME C C 174.97 0.05 1 12 . 1 FME CA C 53.33 0.1 1 13 . 1 FME CB C 33.10 0.1 1 14 . 1 FME CG C 33.26 0.1 1 15 . 1 FME CE C 17.18 0.1 1 16 . 1 FME CN C 167.25 0.1 1 17 . 1 FME N N 129.20 0.05 1 18 . 2 ALA H H 8.83 0.01 1 19 . 2 ALA HA H 4.63 0.01 1 20 . 2 ALA HB H 1.46 0.01 1 21 . 2 ALA C C 175.84 0.05 1 22 . 2 ALA CA C 50.93 0.1 1 23 . 2 ALA CB C 21.80 0.1 1 24 . 2 ALA N N 125.87 0.05 1 25 . 3 LYS H H 8.29 0.01 1 26 . 3 LYS HA H 5.41 0.01 1 27 . 3 LYS HB2 H 1.59 0.01 1 28 . 3 LYS HB3 H 1.59 0.01 1 29 . 3 LYS HG2 H 1.53 0.01 2 30 . 3 LYS HG3 H 1.24 0.01 2 31 . 3 LYS HD2 H 1.59 0.01 1 32 . 3 LYS HD3 H 1.59 0.01 1 33 . 3 LYS HE2 H 2.92 0.01 2 34 . 3 LYS HE3 H 2.88 0.01 2 35 . 3 LYS C C 174.54 0.05 1 36 . 3 LYS CA C 54.61 0.1 1 37 . 3 LYS CB C 35.94 0.1 1 38 . 3 LYS CG C 25.63 0.1 1 39 . 3 LYS CD C 28.75 0.1 1 40 . 3 LYS CE C 41.25 0.1 1 41 . 3 LYS N N 118.42 0.05 1 42 . 4 TRP H H 9.35 0.01 1 43 . 4 TRP HA H 4.97 0.01 1 44 . 4 TRP HB2 H 2.96 0.01 2 45 . 4 TRP HB3 H 2.82 0.01 2 46 . 4 TRP HD1 H 6.94 0.01 1 47 . 4 TRP HE1 H 9.92 0.01 1 48 . 4 TRP HZ2 H 7.56 0.01 1 49 . 4 TRP HH2 H 7.15 0.01 1 50 . 4 TRP HZ3 H 6.84 0.01 1 51 . 4 TRP HE3 H 6.45 0.01 1 52 . 4 TRP C C 174.07 0.05 1 53 . 4 TRP CA C 55.04 0.1 1 54 . 4 TRP CB C 31.57 0.1 1 55 . 4 TRP CG C 102.53 0.1 1 56 . 4 TRP CD1 C 124.50 0.1 1 57 . 4 TRP CD2 C 129.27 0.1 9 58 . 4 TRP CE2 C 128.93 0.1 9 59 . 4 TRP CZ2 C 114.38 0.1 1 60 . 4 TRP CH2 C 124.20 0.1 1 61 . 4 TRP CZ3 C 121.88 0.1 1 62 . 4 TRP CE3 C 119.87 0.1 1 63 . 4 TRP N N 123.16 0.05 1 64 . 4 TRP NE1 N 130.42 0.05 1 65 . 5 VAL H H 9.70 0.01 1 66 . 5 VAL HA H 5.27 0.01 1 67 . 5 VAL HB H 1.77 0.01 1 68 . 5 VAL HG1 H 0.89 0.01 2 69 . 5 VAL HG2 H 0.87 0.01 2 70 . 5 VAL C C 173.10 0.05 1 71 . 5 VAL CA C 58.09 0.1 1 72 . 5 VAL CB C 35.22 0.1 1 73 . 5 VAL CG1 C 19.38 0.1 1 74 . 5 VAL CG2 C 21.26 0.1 1 75 . 5 VAL N N 123.16 0.05 1 76 . 6 CYS H H 9.26 0.01 1 77 . 6 CYS HA H 2.81 0.01 1 78 . 6 CYS HB2 H 3.05 0.01 2 79 . 6 CYS HB3 H 2.67 0.01 2 80 . 6 CYS C C 178.85 0.05 1 81 . 6 CYS CA C 59.11 0.1 1 82 . 6 CYS CB C 30.47 0.1 1 83 . 6 CYS N N 131.23 0.05 1 84 . 7 LYS H H 9.07 0.01 1 85 . 7 LYS HA H 3.94 0.01 1 86 . 7 LYS HB2 H 2.00 0.01 2 87 . 7 LYS HB3 H 1.87 0.01 2 88 . 7 LYS HG2 H 1.62 0.01 2 89 . 7 LYS HG3 H 1.49 0.01 2 90 . 7 LYS HD2 H 1.67 0.01 1 91 . 7 LYS HD3 H 1.67 0.01 1 92 . 7 LYS HE2 H 2.98 0.01 2 93 . 7 LYS HE3 H 2.84 0.01 2 94 . 7 LYS C C 176.43 0.05 1 95 . 7 LYS CA C 58.43 0.1 1 96 . 7 LYS CB C 31.53 0.1 1 97 . 7 LYS CG C 25.63 0.1 1 98 . 7 LYS CD C 28.75 0.1 1 99 . 7 LYS CE C 41.25 0.1 1 100 . 7 LYS N N 131.28 0.05 1 101 . 8 ILE H H 9.08 0.01 1 102 . 8 ILE HA H 4.03 0.01 1 103 . 8 ILE HB H 2.53 0.01 1 104 . 8 ILE HG12 H 1.36 0.01 2 105 . 8 ILE HG13 H 1.35 0.01 2 106 . 8 ILE HG2 H 0.83 0.01 1 107 . 8 ILE HD1 H 0.71 0.01 1 108 . 8 ILE C C 178.36 0.05 1 109 . 8 ILE CA C 61.75 0.1 1 110 . 8 ILE CB C 34.84 0.1 1 111 . 8 ILE CG1 C 26.88 0.1 1 112 . 8 ILE CG2 C 17.51 0.1 1 113 . 8 ILE CD1 C 9.38 0.1 1 114 . 8 ILE N N 122.14 0.05 1 115 . 9 CYS H H 9.32 0.01 1 116 . 9 CYS HA H 5.02 0.01 1 117 . 9 CYS HB2 H 3.28 0.01 2 118 . 9 CYS HB3 H 2.51 0.01 2 119 . 9 CYS C C 177.64 0.05 1 120 . 9 CYS CA C 58.40 0.1 1 121 . 9 CYS CB C 33.17 0.1 1 122 . 9 CYS N N 122.15 0.05 1 123 . 10 GLY H H 7.99 0.01 1 124 . 10 GLY HA2 H 4.23 0.01 2 125 . 10 GLY HA3 H 3.65 0.01 2 126 . 10 GLY C C 173.99 0.05 1 127 . 10 GLY CA C 45.33 0.1 1 128 . 10 GLY N N 113.29 0.05 1 129 . 11 TYR H H 9.38 0.01 1 130 . 11 TYR HA H 4.21 0.01 1 131 . 11 TYR HB2 H 3.15 0.01 2 132 . 11 TYR HB3 H 3.10 0.01 2 133 . 11 TYR HD1 H 7.36 0.01 1 134 . 11 TYR HD2 H 7.36 0.01 1 135 . 11 TYR HE1 H 7.08 0.01 1 136 . 11 TYR HE2 H 7.08 0.01 1 137 . 11 TYR C C 173.05 0.05 1 138 . 11 TYR CA C 59.85 0.1 1 139 . 11 TYR CB C 39.64 0.1 1 140 . 11 TYR CG C 122.43 0.1 1 141 . 11 TYR CD1 C 134.01 0.1 1 142 . 11 TYR CE1 C 118.46 0.1 1 143 . 11 TYR CZ C 157.74 0.1 1 144 . 11 TYR N N 128.36 0.05 1 145 . 12 ILE H H 6.98 0.01 1 146 . 12 ILE HA H 4.80 0.01 1 147 . 12 ILE HB H 1.47 0.01 1 148 . 12 ILE HG12 H 1.80 0.01 1 149 . 12 ILE HG13 H 1.80 0.01 1 150 . 12 ILE HG2 H 0.65 0.01 1 151 . 12 ILE HD1 H 0.79 0.01 1 152 . 12 ILE C C 175.26 0.05 1 153 . 12 ILE CA C 58.54 0.1 1 154 . 12 ILE CB C 38.79 0.1 1 155 . 12 ILE CG1 C 26.88 0.1 1 156 . 12 ILE CG2 C 16.88 0.1 1 157 . 12 ILE CD1 C 12.51 0.1 1 158 . 12 ILE N N 126.30 0.05 1 159 . 13 TYR H H 9.72 0.01 1 160 . 13 TYR HA H 4.58 0.01 1 161 . 13 TYR HB2 H 3.30 0.01 2 162 . 13 TYR HB3 H 3.11 0.01 2 163 . 13 TYR HD1 H 7.14 0.01 1 164 . 13 TYR HD2 H 7.14 0.01 1 165 . 13 TYR HE1 H 6.38 0.01 1 166 . 13 TYR HE2 H 6.38 0.01 1 167 . 13 TYR C C 173.03 0.05 1 168 . 13 TYR CA C 57.34 0.1 1 169 . 13 TYR CB C 38.67 0.1 1 170 . 13 TYR CG C 120.94 0.1 1 171 . 13 TYR CD1 C 133.20 0.1 1 172 . 13 TYR CE1 C 116.54 0.1 1 173 . 13 TYR N N 127.50 0.05 1 174 . 14 ASP H H 8.58 0.01 1 175 . 14 ASP HA H 4.75 0.01 1 176 . 14 ASP HB2 H 2.88 0.01 2 177 . 14 ASP HB3 H 2.24 0.01 2 178 . 14 ASP C C 176.69 0.05 1 179 . 14 ASP CA C 51.02 0.1 1 180 . 14 ASP CB C 41.85 0.1 1 181 . 14 ASP CG C 179.20 0.1 1 182 . 14 ASP N N 129.92 0.05 1 183 . 15 GLU H H 8.32 0.01 1 184 . 15 GLU HA H 3.73 0.01 1 185 . 15 GLU HB2 H 2.30 0.01 2 186 . 15 GLU HB3 H 1.91 0.01 2 187 . 15 GLU HG2 H 2.94 0.01 2 188 . 15 GLU HG3 H 2.86 0.01 2 189 . 15 GLU C C 177.73 0.05 1 190 . 15 GLU CA C 58.38 0.1 1 191 . 15 GLU CB C 30.86 0.1 1 192 . 15 GLU CG C 37.50 0.1 1 193 . 15 GLU N N 124.41 0.05 1 194 . 16 ASP H H 8.05 0.01 1 195 . 16 ASP HA H 4.27 0.01 1 196 . 16 ASP HB2 H 2.59 0.01 2 197 . 16 ASP HB3 H 2.53 0.01 2 198 . 16 ASP C C 177.60 0.05 1 199 . 16 ASP CA C 56.38 0.1 1 200 . 16 ASP CB C 41.33 0.1 1 201 . 16 ASP CG C 179.50 0.1 1 202 . 16 ASP N N 114.13 0.05 1 203 . 17 ALA H H 7.13 0.01 1 204 . 17 ALA HA H 4.27 0.01 1 205 . 17 ALA HB H 1.47 0.01 1 206 . 17 ALA C C 179.98 0.05 1 207 . 17 ALA CA C 52.07 0.1 1 208 . 17 ALA CB C 19.71 0.1 1 209 . 17 ALA N N 119.42 0.05 1 210 . 18 GLY H H 8.28 0.01 1 211 . 18 GLY HA2 H 3.93 0.01 2 212 . 18 GLY HA3 H 3.58 0.01 2 213 . 18 GLY C C 173.47 0.05 1 214 . 18 GLY CA C 44.39 0.1 1 215 . 18 GLY N N 104.06 0.05 1 216 . 19 ASP H H 8.19 0.01 1 217 . 19 ASP HA H 5.15 0.01 1 218 . 19 ASP HB2 H 3.02 0.01 2 219 . 19 ASP HB3 H 2.95 0.01 2 220 . 19 ASP C C 174.78 0.05 1 221 . 19 ASP CA C 52.33 0.1 1 222 . 19 ASP CB C 40.16 0.1 1 223 . 19 ASP CG C 179.85 0.1 1 224 . 19 ASP N N 117.04 0.05 1 225 . 20 PRO HA H 4.16 0.01 1 226 . 20 PRO HB2 H 2.36 0.01 2 227 . 20 PRO HB3 H 2.14 0.01 2 228 . 20 PRO HG2 H 2.20 0.01 2 229 . 20 PRO HG3 H 2.10 0.01 2 230 . 20 PRO HD2 H 4.01 0.01 2 231 . 20 PRO HD3 H 3.90 0.01 2 232 . 20 PRO C C 180.06 0.05 1 233 . 20 PRO CA C 65.03 0.1 1 234 . 20 PRO CB C 31.53 0.1 1 235 . 20 PRO CG C 27.33 0.1 1 236 . 20 PRO CD C 50.21 0.1 1 237 . 20 PRO N N 142.27 0.05 1 238 . 21 ASP H H 9.21 0.01 1 239 . 21 ASP HA H 4.45 0.01 1 240 . 21 ASP HB2 H 2.71 0.01 2 241 . 21 ASP HB3 H 1.50 0.01 2 242 . 21 ASP C C 177.04 0.05 1 243 . 21 ASP CA C 56.48 0.1 1 244 . 21 ASP CB C 39.60 0.1 1 245 . 21 ASP CG C 179.94 0.1 1 246 . 21 ASP N N 120.46 0.05 1 247 . 22 ASN H H 7.67 0.01 1 248 . 22 ASN HA H 5.09 0.01 1 249 . 22 ASN HB2 H 3.04 0.01 2 250 . 22 ASN HB3 H 2.70 0.01 2 251 . 22 ASN HD21 H 9.36 0.01 2 252 . 22 ASN HD22 H 6.98 0.01 2 253 . 22 ASN C C 175.19 0.05 1 254 . 22 ASN CA C 52.03 0.1 1 255 . 22 ASN CB C 38.87 0.1 1 256 . 22 ASN CG C 178.82 0.1 1 257 . 22 ASN N N 114.94 0.05 1 258 . 22 ASN ND2 N 119.63 0.05 1 259 . 23 GLY H H 7.76 0.01 1 260 . 23 GLY HA2 H 4.11 0.01 2 261 . 23 GLY HA3 H 3.81 0.01 2 262 . 23 GLY C C 173.80 0.05 1 263 . 23 GLY CA C 45.57 0.1 1 264 . 23 GLY N N 106.03 0.05 1 265 . 24 ILE H H 7.60 0.01 1 266 . 24 ILE HA H 4.38 0.01 1 267 . 24 ILE HB H 1.99 0.01 1 268 . 24 ILE HG12 H 1.40 0.01 2 269 . 24 ILE HG13 H 1.39 0.01 2 270 . 24 ILE HG2 H 0.88 0.01 1 271 . 24 ILE HD1 H 0.78 0.01 1 272 . 24 ILE C C 176.41 0.05 1 273 . 24 ILE CA C 57.37 0.1 1 274 . 24 ILE CB C 35.46 0.1 1 275 . 24 ILE CG1 C 25.01 0.1 1 276 . 24 ILE CG2 C 17.88 0.1 1 277 . 24 ILE CD1 C 10.01 0.1 1 278 . 24 ILE N N 121.84 0.05 1 279 . 25 SER H H 8.62 0.01 1 280 . 25 SER HA H 4.59 0.01 1 281 . 25 SER HB2 H 3.87 0.01 2 282 . 25 SER HB3 H 3.70 0.01 2 283 . 25 SER C C 175.81 0.05 1 284 . 25 SER CA C 57.27 0.1 1 285 . 25 SER CB C 61.71 0.1 1 286 . 25 SER N N 124.99 0.05 1 287 . 26 PRO HA H 3.72 0.01 1 288 . 26 PRO HB2 H 2.52 0.01 2 289 . 26 PRO HB3 H 1.80 0.01 2 290 . 26 PRO HG2 H 2.12 0.01 2 291 . 26 PRO HG3 H 2.02 0.01 2 292 . 26 PRO HD2 H 3.89 0.01 2 293 . 26 PRO HD3 H 3.68 0.01 2 294 . 26 PRO C C 176.69 0.05 1 295 . 26 PRO CA C 63.85 0.1 1 296 . 26 PRO CB C 31.20 0.1 1 297 . 26 PRO CG C 27.21 0.1 1 298 . 26 PRO CD C 50.81 0.1 1 299 . 26 PRO N N 138.38 0.05 1 300 . 27 GLY H H 8.20 0.01 1 301 . 27 GLY HA2 H 4.02 0.01 2 302 . 27 GLY HA3 H 3.70 0.01 2 303 . 27 GLY C C 174.41 0.05 1 304 . 27 GLY CA C 44.99 0.1 1 305 . 27 GLY N N 114.08 0.05 1 306 . 28 THR H H 7.15 0.01 1 307 . 28 THR HA H 4.03 0.01 1 308 . 28 THR HB H 3.86 0.01 1 309 . 28 THR HG2 H 0.99 0.01 1 310 . 28 THR HG1 H 6.36 0.01 1 311 . 28 THR C C 174.46 0.05 1 312 . 28 THR CA C 62.72 0.1 1 313 . 28 THR CB C 67.92 0.1 1 314 . 28 THR CG2 C 20.07 0.1 1 315 . 28 THR N N 117.07 0.05 1 316 . 29 LYS H H 8.81 0.01 1 317 . 29 LYS HA H 3.95 0.01 1 318 . 29 LYS HB2 H 2.08 0.01 2 319 . 29 LYS HB3 H 1.42 0.01 2 320 . 29 LYS HG2 H 1.60 0.01 2 321 . 29 LYS HG3 H 1.53 0.01 2 322 . 29 LYS HD2 H 1.60 0.01 1 323 . 29 LYS HD3 H 1.60 0.01 1 324 . 29 LYS HE2 H 3.12 0.01 2 325 . 29 LYS HE3 H 3.05 0.01 2 326 . 29 LYS C C 177.33 0.05 1 327 . 29 LYS CA C 55.71 0.1 1 328 . 29 LYS CB C 31.61 0.1 1 329 . 29 LYS CG C 25.00 0.1 1 330 . 29 LYS CD C 28.13 0.1 1 331 . 29 LYS CE C 41.25 0.1 1 332 . 29 LYS N N 129.81 0.05 1 333 . 30 PHE H H 9.92 0.01 1 334 . 30 PHE HA H 3.11 0.01 1 335 . 30 PHE HB2 H 2.09 0.01 2 336 . 30 PHE HB3 H 1.85 0.01 2 337 . 30 PHE HD1 H 5.66 0.01 1 338 . 30 PHE HD2 H 5.66 0.01 1 339 . 30 PHE HE1 H 6.22 0.01 1 340 . 30 PHE HE2 H 6.22 0.01 1 341 . 30 PHE HZ H 6.76 0.01 1 342 . 30 PHE C C 178.82 0.05 1 343 . 30 PHE CA C 60.71 0.1 1 344 . 30 PHE CB C 37.90 0.1 1 345 . 30 PHE CG C 127.84 0.1 1 346 . 30 PHE CD1 C 130.66 0.1 1 347 . 30 PHE CE1 C 129.34 0.1 1 348 . 30 PHE CZ C 129.28 0.1 1 349 . 30 PHE N N 125.95 0.05 1 350 . 31 GLU H H 9.48 0.01 1 351 . 31 GLU HA H 3.71 0.01 1 352 . 31 GLU HB2 H 2.00 0.01 2 353 . 31 GLU HB3 H 1.91 0.01 2 354 . 31 GLU HG2 H 2.37 0.01 2 355 . 31 GLU HG3 H 2.24 0.01 2 356 . 31 GLU C C 176.86 0.05 1 357 . 31 GLU CA C 58.30 0.1 1 358 . 31 GLU CB C 28.20 0.1 1 359 . 31 GLU CG C 36.38 0.1 1 360 . 31 GLU CD C 184.07 0.1 1 361 . 31 GLU N N 114.83 0.05 1 362 . 32 GLU H H 7.45 0.01 1 363 . 32 GLU HA H 4.05 0.01 1 364 . 32 GLU HB2 H 2.02 0.01 1 365 . 32 GLU HB3 H 2.02 0.01 1 366 . 32 GLU HG2 H 2.16 0.01 2 367 . 32 GLU HG3 H 2.05 0.01 2 368 . 32 GLU C C 176.76 0.05 1 369 . 32 GLU CA C 54.70 0.1 1 370 . 32 GLU CB C 29.36 0.1 1 371 . 32 GLU CG C 36.25 0.1 1 372 . 32 GLU CD C 183.61 0.1 1 373 . 32 GLU N N 116.43 0.05 1 374 . 33 LEU H H 6.85 0.01 1 375 . 33 LEU HA H 3.81 0.01 1 376 . 33 LEU HB2 H 0.52 0.01 2 377 . 33 LEU HB3 H 0.22 0.01 2 378 . 33 LEU HG H 0.74 0.01 1 379 . 33 LEU HD1 H -1.76 0.01 1 380 . 33 LEU HD2 H -0.22 0.01 2 381 . 33 LEU C C 175.09 0.05 2 382 . 33 LEU CA C 52.85 0.1 1 383 . 33 LEU CB C 39.29 0.1 1 384 . 33 LEU CG C 25.01 0.1 1 385 . 33 LEU CD1 C 22.51 0.1 2 386 . 33 LEU CD2 C 21.88 0.1 2 387 . 33 LEU N N 122.78 0.05 1 388 . 34 PRO HA H 4.30 0.01 1 389 . 34 PRO HB2 H 2.40 0.01 2 390 . 34 PRO HB3 H 2.07 0.01 2 391 . 34 PRO HG2 H 2.15 0.01 2 392 . 34 PRO HG3 H 2.07 0.01 2 393 . 34 PRO HD2 H 3.72 0.01 2 394 . 34 PRO HD3 H 3.22 0.01 2 395 . 34 PRO C C 177.03 0.05 1 396 . 34 PRO CA C 62.12 0.1 1 397 . 34 PRO CB C 32.02 0.1 1 398 . 34 PRO CG C 27.25 0.1 1 399 . 34 PRO CD C 49.38 0.1 1 400 . 34 PRO N N 135.12 0.05 1 401 . 35 ASP H H 8.71 0.01 1 402 . 35 ASP HA H 4.17 0.01 1 403 . 35 ASP HB2 H 2.66 0.01 2 404 . 35 ASP HB3 H 2.56 0.01 2 405 . 35 ASP C C 176.47 0.05 1 406 . 35 ASP CA C 56.42 0.1 1 407 . 35 ASP CB C 39.93 0.1 1 408 . 35 ASP CG C 179.68 0.1 1 409 . 35 ASP N N 120.66 0.05 1 410 . 36 ASP H H 8.18 0.01 1 411 . 36 ASP HA H 4.51 0.01 1 412 . 36 ASP HB2 H 2.82 0.01 2 413 . 36 ASP HB3 H 2.53 0.01 2 414 . 36 ASP C C 175.57 0.05 1 415 . 36 ASP CA C 51.96 0.1 1 416 . 36 ASP CB C 39.09 0.1 1 417 . 36 ASP CG C 181.07 0.1 1 418 . 36 ASP N N 114.26 0.05 1 419 . 37 TRP H H 7.61 0.01 1 420 . 37 TRP HA H 4.05 0.01 1 421 . 37 TRP HB2 H 2.87 0.01 2 422 . 37 TRP HB3 H 2.81 0.01 2 423 . 37 TRP HD1 H 7.12 0.01 1 424 . 37 TRP HE1 H 10.54 0.01 1 425 . 37 TRP HZ2 H 7.22 0.01 1 426 . 37 TRP HH2 H 6.78 0.01 1 427 . 37 TRP HZ3 H 5.74 0.01 1 428 . 37 TRP HE3 H 6.56 0.01 1 429 . 37 TRP C C 174.90 0.05 1 430 . 37 TRP CA C 59.71 0.1 1 431 . 37 TRP CB C 29.22 0.1 1 432 . 37 TRP CG C 104.69 0.1 1 433 . 37 TRP CD1 C 126.08 0.1 1 434 . 37 TRP CD2 C 130.70 0.1 1 435 . 37 TRP CZ2 C 113.70 0.1 1 436 . 37 TRP CH2 C 123.12 0.1 1 437 . 37 TRP CZ3 C 121.50 0.1 1 438 . 37 TRP CE3 C 119.06 0.1 1 439 . 37 TRP N N 123.42 0.05 1 440 . 37 TRP NE1 N 129.66 0.05 1 441 . 38 VAL H H 6.17 0.01 1 442 . 38 VAL HA H 4.38 0.01 1 443 . 38 VAL HB H 1.55 0.01 1 444 . 38 VAL HG1 H 0.60 0.01 2 445 . 38 VAL HG2 H 0.30 0.01 2 446 . 38 VAL C C 172.11 0.05 1 447 . 38 VAL CA C 56.60 0.1 1 448 . 38 VAL CB C 34.74 0.1 1 449 . 38 VAL CG1 C 21.22 0.1 2 450 . 38 VAL CG2 C 16.69 0.1 2 451 . 38 VAL N N 117.29 0.05 1 452 . 39 CYS H H 8.97 0.01 1 453 . 39 CYS HA H 3.82 0.01 1 454 . 39 CYS HB2 H 3.22 0.01 2 455 . 39 CYS HB3 H 3.09 0.01 2 456 . 39 CYS C C 177.15 0.05 1 457 . 39 CYS CA C 56.69 0.1 1 458 . 39 CYS CB C 30.75 0.1 1 459 . 39 CYS N N 121.69 0.05 1 460 . 40 PRO HA H 4.00 0.01 1 461 . 40 PRO HB2 H 2.17 0.01 2 462 . 40 PRO HB3 H 1.66 0.01 2 463 . 40 PRO HG2 H 1.85 0.01 2 464 . 40 PRO HG3 H 1.25 0.01 2 465 . 40 PRO HD2 H 3.45 0.01 2 466 . 40 PRO HD3 H 3.20 0.01 2 467 . 40 PRO C C 176.18 0.05 1 468 . 40 PRO CA C 63.19 0.1 1 469 . 40 PRO CB C 31.66 0.1 1 470 . 40 PRO CG C 26.05 0.1 1 471 . 40 PRO CD C 51.30 0.1 1 472 . 40 PRO N N 141.30 0.05 1 473 . 41 ILE H H 8.72 0.01 1 474 . 41 ILE HA H 4.08 0.01 1 475 . 41 ILE HB H 2.75 0.01 1 476 . 41 ILE HG12 H 1.47 0.01 2 477 . 41 ILE HG13 H 1.23 0.01 2 478 . 41 ILE HG2 H 0.83 0.01 1 479 . 41 ILE HD1 H 0.73 0.01 1 480 . 41 ILE C C 178.12 0.05 1 481 . 41 ILE CA C 60.47 0.1 1 482 . 41 ILE CB C 34.89 0.1 1 483 . 41 ILE CG1 C 26.88 0.1 1 484 . 41 ILE CG2 C 16.88 0.1 1 485 . 41 ILE CD1 C 8.13 0.1 1 486 . 41 ILE N N 122.03 0.05 1 487 . 42 CYS H H 8.83 0.01 1 488 . 42 CYS HA H 4.88 0.01 1 489 . 42 CYS HB2 H 3.22 0.01 2 490 . 42 CYS HB3 H 2.52 0.01 2 491 . 42 CYS C C 177.64 0.05 1 492 . 42 CYS CA C 58.42 0.1 1 493 . 42 CYS CB C 32.53 0.1 1 494 . 42 CYS N N 121.29 0.05 1 495 . 43 GLY H H 7.89 0.01 1 496 . 43 GLY HA2 H 4.05 0.01 2 497 . 43 GLY HA3 H 3.53 0.01 2 498 . 43 GLY C C 173.26 0.05 1 499 . 43 GLY CA C 45.38 0.1 1 500 . 43 GLY N N 112.97 0.05 1 501 . 44 ALA H H 9.14 0.01 1 502 . 44 ALA HA H 4.38 0.01 1 503 . 44 ALA HB H 1.48 0.01 1 504 . 44 ALA C C 174.34 0.05 1 505 . 44 ALA CA C 50.75 0.1 1 506 . 44 ALA CB C 19.03 0.1 1 507 . 44 ALA N N 128.76 0.05 1 508 . 45 PRO HA H 4.76 0.01 1 509 . 45 PRO HB2 H 2.40 0.01 2 510 . 45 PRO HB3 H 2.39 0.01 2 511 . 45 PRO HG2 H 2.14 0.01 2 512 . 45 PRO HG3 H 2.10 0.01 2 513 . 45 PRO HD2 H 3.84 0.01 2 514 . 45 PRO HD3 H 3.60 0.01 2 515 . 45 PRO C C 177.15 0.05 1 516 . 45 PRO CA C 61.17 0.1 1 517 . 45 PRO CB C 32.25 0.1 1 518 . 45 PRO CG C 26.46 0.1 1 519 . 45 PRO CD C 49.36 0.1 1 520 . 45 PRO N N 142.27 0.05 1 521 . 46 LYS H H 8.49 0.01 1 522 . 46 LYS HA H 4.15 0.01 1 523 . 46 LYS HB2 H 1.87 0.01 1 524 . 46 LYS HB3 H 1.87 0.01 1 525 . 46 LYS HG2 H 1.71 0.01 2 526 . 46 LYS HG3 H 1.06 0.01 2 527 . 46 LYS HD2 H 1.25 0.01 1 528 . 46 LYS HD3 H 1.25 0.01 1 529 . 46 LYS HE2 H 2.31 0.01 2 530 . 46 LYS HE3 H 2.06 0.01 2 531 . 46 LYS C C 178.27 0.05 1 532 . 46 LYS CA C 60.04 0.1 1 533 . 46 LYS CB C 32.21 0.1 1 534 . 46 LYS CG C 25.63 0.1 1 535 . 46 LYS CD C 28.75 0.1 1 536 . 46 LYS CE C 41.25 0.1 1 537 . 46 LYS N N 117.64 0.05 1 538 . 47 SER H H 7.91 0.01 1 539 . 47 SER HA H 4.42 0.01 1 540 . 47 SER HB2 H 4.21 0.01 2 541 . 47 SER HB3 H 3.97 0.01 2 542 . 47 SER C C 175.85 0.05 1 543 . 47 SER CA C 59.66 0.1 1 544 . 47 SER CB C 61.81 0.1 1 545 . 47 SER N N 110.13 0.05 1 546 . 48 GLU H H 8.42 0.01 1 547 . 48 GLU HA H 4.76 0.01 1 548 . 48 GLU HB2 H 2.58 0.01 2 549 . 48 GLU HB3 H 2.00 0.01 2 550 . 48 GLU HG2 H 2.40 0.01 2 551 . 48 GLU HG3 H 2.22 0.01 2 552 . 48 GLU C C 173.75 0.05 1 553 . 48 GLU CA C 54.73 0.1 1 554 . 48 GLU CB C 27.67 0.1 1 555 . 48 GLU CG C 34.38 0.1 1 556 . 48 GLU CD C 182.90 0.1 1 557 . 48 GLU N N 121.31 0.05 1 558 . 49 PHE H H 7.75 0.01 1 559 . 49 PHE HA H 5.68 0.01 1 560 . 49 PHE HB2 H 3.64 0.01 2 561 . 49 PHE HB3 H 2.59 0.01 2 562 . 49 PHE HD1 H 7.55 0.01 1 563 . 49 PHE HD2 H 7.55 0.01 1 564 . 49 PHE HE1 H 7.37 0.01 1 565 . 49 PHE HE2 H 7.37 0.01 1 566 . 49 PHE HZ H 7.65 0.01 1 567 . 49 PHE C C 177.09 0.05 1 568 . 49 PHE CA C 56.21 0.1 1 569 . 49 PHE CB C 42.34 0.1 1 570 . 49 PHE CG C 132.75 0.1 1 571 . 49 PHE CD1 C 131.67 0.1 1 572 . 49 PHE CE1 C 131.71 0.1 1 573 . 49 PHE CZ C 130.49 0.1 1 574 . 49 PHE N N 118.80 0.05 1 575 . 50 GLU H H 9.09 0.01 1 576 . 50 GLU HA H 4.85 0.01 1 577 . 50 GLU HB2 H 1.92 0.01 2 578 . 50 GLU HB3 H 1.88 0.01 2 579 . 50 GLU HG2 H 2.15 0.01 2 580 . 50 GLU HG3 H 2.13 0.01 2 581 . 50 GLU C C 174.06 0.05 1 582 . 50 GLU CA C 53.36 0.1 1 583 . 50 GLU CB C 33.27 0.1 1 584 . 50 GLU CG C 35.63 0.1 1 585 . 50 GLU CD C 183.61 0.1 1 586 . 50 GLU N N 120.12 0.05 1 587 . 51 LYS H H 8.28 0.01 1 588 . 51 LYS HA H 3.19 0.01 1 589 . 51 LYS HB2 H 0.99 0.01 2 590 . 51 LYS HB3 H 0.01 0.01 2 591 . 51 LYS HG2 H 0.68 0.01 2 592 . 51 LYS HG3 H 0.06 0.01 2 593 . 51 LYS HD2 H 1.28 0.01 2 594 . 51 LYS HD3 H 1.24 0.01 2 595 . 51 LYS HE2 H 2.71 0.01 1 596 . 51 LYS HE3 H 2.71 0.01 1 597 . 51 LYS C C 176.81 0.05 1 598 . 51 LYS CA C 56.67 0.1 1 599 . 51 LYS CB C 31.12 0.1 1 600 . 51 LYS CG C 23.76 0.1 1 601 . 51 LYS CD C 28.13 0.1 1 602 . 51 LYS CE C 41.25 0.1 1 603 . 51 LYS N N 127.50 0.05 1 604 . 52 LEU H H 8.65 0.01 1 605 . 52 LEU HA H 4.22 0.01 1 606 . 52 LEU HB2 H 1.45 0.01 2 607 . 52 LEU HB3 H 1.33 0.01 2 608 . 52 LEU HG H 1.43 0.01 1 609 . 52 LEU HD1 H 0.80 0.01 1 610 . 52 LEU HD2 H 0.80 0.01 1 611 . 52 LEU C C 176.36 0.05 1 612 . 52 LEU CA C 54.29 0.1 1 613 . 52 LEU CB C 41.94 0.1 1 614 . 52 LEU CG C 26.88 0.1 1 615 . 52 LEU CD1 C 24.38 0.1 1 616 . 52 LEU N N 129.21 0.05 1 617 . 53 GLU H H 8.33 0.01 1 618 . 53 GLU HA H 4.27 0.01 1 619 . 53 GLU HB2 H 2.02 0.01 2 620 . 53 GLU HB3 H 1.80 0.01 2 621 . 53 GLU HG2 H 2.17 0.01 2 622 . 53 GLU HG3 H 2.10 0.01 2 623 . 53 GLU C C 175.02 0.05 1 624 . 53 GLU CA C 55.30 0.1 1 625 . 53 GLU CB C 30.32 0.1 1 626 . 53 GLU CG C 35.75 0.1 1 627 . 53 GLU CD C 184.12 0.1 1 628 . 53 GLU N N 123.98 0.05 1 629 . 54 ASP H H 7.91 0.01 1 630 . 54 ASP HA H 4.29 0.01 1 631 . 54 ASP HB2 H 2.59 0.01 2 632 . 54 ASP HB3 H 2.49 0.01 2 633 . 54 ASP C C 180.85 0.05 1 634 . 54 ASP CA C 55.30 0.1 1 635 . 54 ASP CB C 41.71 0.1 1 636 . 54 ASP CG C 181.38 0.1 1 637 . 54 ASP N N 127.20 0.05 1 stop_ save_ save_MetPfRdZn_cs _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name MetPfRdZn _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 ALA H H 8.92 . 1 2 . 2 ALA HA H 4.64 . 1 3 . 2 ALA HB H 1.46 . 1 4 . 2 ALA C C 175.84 . 1 5 . 2 ALA CA C 51.38 . 5 6 . 2 ALA CB C 21.74 . 5 7 . 2 ALA N N 125.82 . 1 8 . 3 LYS H H 8.3 . 5 9 . 3 LYS HA H 5.47 . 5 10 . 3 LYS HB2 H 1.63 . 5 11 . 3 LYS C C 174.69 . 5 12 . 3 LYS CA C 54.61 . 5 13 . 3 LYS CB C 35.93 . 5 14 . 3 LYS N N 118.71 . 5 15 . 4 TRP H H 9.51 . 5 16 . 4 TRP HA H 4.98 . 5 17 . 4 TRP HE1 H 9.95 . 5 18 . 4 TRP C C 173.90 . 1 19 . 4 TRP CA C 55.16 . 1 20 . 4 TRP CB C 31.55 . 1 21 . 4 TRP N N 124.22 . 5 22 . 4 TRP NE1 N 129.2 . 5 23 . 5 VAL H H 9.74 . 1 24 . 5 VAL C C 172.81 . 1 25 . 5 VAL CA C 58.12 . 1 26 . 5 VAL CB C 35.48 . 1 27 . 5 VAL N N 123.28 . 1 28 . 6 CYS H H 9.23 . 1 29 . 6 CYS C C 178.85 . 1 30 . 6 CYS CA C 59.24 . 1 31 . 6 CYS CB C 30.39 . 1 32 . 6 CYS N N 131.23 . 1 33 . 7 LYS H H 9.07 . 1 34 . 7 LYS C C 176.43 . 1 35 . 7 LYS CA C 58.43 . 1 36 . 7 LYS CB C 31.53 . 1 37 . 7 LYS N N 131.28 . 1 38 . 8 ILE H H 9.08 . 1 39 . 8 ILE C C 178.36 . 1 40 . 8 ILE CA C 61.75 . 1 41 . 8 ILE CB C 34.84 . 1 42 . 8 ILE N N 122.14 . 1 43 . 9 CYS H H 9.32 . 1 44 . 9 CYS C C 177.64 . 1 45 . 9 CYS CA C 58.44 . 1 46 . 9 CYS CB C 33.17 . 1 47 . 9 CYS N N 122.15 . 1 48 . 10 GLY H H 8.04 . 1 49 . 10 GLY C C 173.99 . 1 50 . 10 GLY CA C 45.33 . 1 51 . 10 GLY N N 113.6 . 1 52 . 11 TYR H H 9.38 . 1 53 . 11 TYR C C 173.08 . 1 54 . 11 TYR CA C 59.81 . 1 55 . 11 TYR CB C 39.64 . 1 56 . 11 TYR N N 128.36 . 1 57 . 12 ILE H H 7.03 . 1 58 . 12 ILE HA H 4.76 . 1 59 . 12 ILE HB H 1.46 . 1 60 . 12 ILE HG2 H 0.65 . 1 61 . 12 ILE C C 175.11 . 1 62 . 12 ILE CA C 58.63 . 1 63 . 12 ILE CB C 38.78 . 1 64 . 12 ILE N N 126.19 . 1 65 . 13 TYR H H 9.71 . 5 66 . 13 TYR CA C 57.34 . 1 67 . 13 TYR CB C 38.67 . 1 68 . 13 TYR N N 127.85 . 5 69 . 14 ASP H H 8.58 . 1 70 . 14 ASP C C 176.79 . 5 71 . 14 ASP CA C 51.05 . 5 72 . 14 ASP CB C 41.96 . 5 73 . 14 ASP N N 129.92 . 1 74 . 15 GLU H H 8.24 . 5 75 . 15 GLU C C 177.73 . 1 76 . 15 GLU CA C 58.13 . 5 77 . 15 GLU CB C 30.38 . 5 78 . 15 GLU N N 124.68 . 5 79 . 16 ASP H H 8 . 1 80 . 16 ASP C C 177.23 . 5 81 . 16 ASP CA C 56.33 . 5 82 . 16 ASP CB C 40.02 . 5 83 . 16 ASP N N 114.14 . 1 84 . 17 ALA H H 7.29 . 5 85 . 17 ALA HA H 4.34 . 5 86 . 17 ALA HB H 1.48 . 5 87 . 17 ALA C C 179.93 . 5 88 . 17 ALA CA C 52.01 . 5 89 . 17 ALA CB C 19.76 . 5 90 . 17 ALA N N 120.46 . 5 91 . 18 GLY H H 8.12 . 5 92 . 18 GLY HA2 H 3.98 . 2 93 . 18 GLY HA3 H 3.58 . 2 94 . 18 GLY C C 173.27 . 1 95 . 18 GLY CA C 44.36 . 1 96 . 18 GLY N N 103.8 . 5 97 . 19 ASP H H 8.26 . 1 98 . 19 ASP HA H 5.16 . 1 99 . 19 ASP HB3 H 2.98 . 2 100 . 19 ASP CA C 52.24 . 1 101 . 19 ASP CB C 40.14 . 1 102 . 19 ASP N N 116.85 . 1 103 . 20 PRO C C 180.06 . 1 104 . 20 PRO CA C 64.99 . 1 105 . 20 PRO CB C 31.53 . 1 106 . 21 ASP H H 9.21 . 1 107 . 21 ASP C C 177.04 . 1 108 . 21 ASP CA C 56.48 . 1 109 . 21 ASP CB C 39.60 . 1 110 . 21 ASP N N 120.46 . 1 111 . 22 ASN H H 7.67 . 1 112 . 22 ASN HD21 H 9.36 . 2 113 . 22 ASN HD22 H 6.98 . 2 114 . 22 ASN C C 175.19 . 1 115 . 22 ASN CA C 52.03 . 1 116 . 22 ASN CB C 38.87 . 1 117 . 22 ASN N N 114.94 . 1 118 . 22 ASN ND2 N 119.63 . 1 119 . 23 GLY H H 7.76 . 1 120 . 23 GLY C C 173.80 . 1 121 . 23 GLY CA C 45.57 . 1 122 . 23 GLY N N 106.03 . 1 123 . 24 ILE H H 7.60 . 1 124 . 24 ILE C C 176.47 . 1 125 . 24 ILE CA C 57.37 . 1 126 . 24 ILE CB C 35.46 . 1 127 . 24 ILE N N 121.84 . 1 128 . 25 SER H H 8.65 . 1 129 . 25 SER CA C 57.27 . 1 130 . 25 SER CB C 61.71 . 1 131 . 25 SER N N 125.04 . 1 132 . 26 PRO C C 176.69 . 1 133 . 26 PRO CA C 63.79 . 1 134 . 26 PRO CB C 31.20 . 1 135 . 27 GLY H H 8.22 . 1 136 . 27 GLY C C 175 . 5 137 . 27 GLY CA C 44.8 . 5 138 . 27 GLY N N 113.79 . 1 139 . 28 THR H H 7.25 . 5 140 . 28 THR HB H 3.93 . 5 141 . 28 THR C C 174.48 . 1 142 . 28 THR CA C 63.21 . 5 143 . 28 THR CB C 67.81 . 5 144 . 28 THR N N 117.54 . 5 145 . 29 LYS H H 8.65 . 5 146 . 29 LYS HA H 4.22 . 5 147 . 29 LYS HG2 H 1.41 . 2 148 . 29 LYS C C 177.2 . 5 149 . 29 LYS CA C 55.53 . 5 150 . 29 LYS CB C 31.61 . 5 151 . 29 LYS N N 130.03 . 1 152 . 30 PHE H H 10.01 . 5 153 . 30 PHE C C 178.78 . 5 154 . 30 PHE CA C 60.74 . 5 155 . 30 PHE CB C 37.91 . 5 156 . 30 PHE N N 126.02 . 5 157 . 31 GLU H H 9.59 . 5 158 . 31 GLU C C 176.82 . 1 159 . 31 GLU CA C 58.44 . 5 160 . 31 GLU CB C 28.23 . 5 161 . 31 GLU N N 114.98 . 5 162 . 32 GLU H H 7.41 . 1 163 . 32 GLU C C 176.76 . 1 164 . 32 GLU CA C 54.69 . 1 165 . 32 GLU CB C 29.40 . 1 166 . 32 GLU N N 116.37 . 1 167 . 33 LEU H H 6.82 . 1 168 . 33 LEU CA C 52.85 . 1 169 . 33 LEU CB C 39.29 . 1 170 . 33 LEU N N 122.86 . 1 171 . 34 PRO C C 177.03 . 1 172 . 34 PRO CA C 62.12 . 1 173 . 34 PRO CB C 32.02 . 1 174 . 35 ASP H H 8.71 . 1 175 . 35 ASP C C 176.47 . 1 176 . 35 ASP CA C 56.42 . 1 177 . 35 ASP CB C 39.93 . 1 178 . 35 ASP N N 120.66 . 1 179 . 36 ASP H H 8.18 . 1 180 . 36 ASP C C 175.57 . 1 181 . 36 ASP CA C 51.96 . 1 182 . 36 ASP CB C 39.09 . 1 183 . 36 ASP N N 114.26 . 1 184 . 37 TRP H H 7.61 . 1 185 . 37 TRP HE1 H 10.6 . 1 186 . 37 TRP C C 174.90 . 1 187 . 37 TRP CA C 59.71 . 1 188 . 37 TRP CB C 29.22 . 1 189 . 37 TRP N N 123.42 . 1 190 . 37 TRP NE1 N 129.74 . 1 191 . 38 VAL H H 6.17 . 1 192 . 38 VAL C C 172.11 . 1 193 . 38 VAL CA C 56.60 . 1 194 . 38 VAL CB C 34.74 . 1 195 . 38 VAL N N 117.29 . 1 196 . 39 CYS H H 8.97 . 1 197 . 39 CYS CA C 56.69 . 1 198 . 39 CYS CB C 30.75 . 1 199 . 39 CYS N N 121.69 . 1 200 . 40 PRO C C 176.18 . 1 201 . 40 PRO CA C 63.07 . 1 202 . 40 PRO CB C 31.66 . 1 203 . 41 ILE H H 8.72 . 1 204 . 41 ILE C C 178.12 . 1 205 . 41 ILE CA C 60.47 . 1 206 . 41 ILE CB C 34.89 . 1 207 . 41 ILE N N 122.03 . 1 208 . 42 CYS H H 8.83 . 1 209 . 42 CYS C C 177.64 . 1 210 . 42 CYS CA C 58.42 . 1 211 . 42 CYS CB C 32.53 . 1 212 . 42 CYS N N 121.29 . 1 213 . 43 GLY H H 7.89 . 1 214 . 43 GLY C C 173.26 . 1 215 . 43 GLY CA C 45.38 . 1 216 . 43 GLY N N 112.97 . 1 217 . 44 ALA H H 9.14 . 1 218 . 44 ALA CA C 50.75 . 1 219 . 44 ALA CB C 19.03 . 1 220 . 44 ALA N N 128.76 . 1 221 . 45 PRO C C 177.12 . 5 222 . 45 PRO CA C 61.48 . 1 223 . 45 PRO CB C 32.31 . 1 224 . 46 LYS H H 8.45 . 5 225 . 46 LYS C C 178.27 . 1 226 . 46 LYS CA C 60.01 . 5 227 . 46 LYS CB C 32.31 . 5 228 . 46 LYS N N 117.88 . 5 229 . 47 SER H H 7.91 . 1 230 . 47 SER C C 175.85 . 1 231 . 47 SER CA C 59.66 . 1 232 . 47 SER CB C 61.81 . 1 233 . 47 SER N N 110.12 . 1 234 . 48 GLU H H 8.42 . 1 235 . 48 GLU HA H 4.76 . 1 236 . 48 GLU HB2 H 2.58 . 2 237 . 48 GLU HB3 H 2.00 . 2 238 . 48 GLU C C 173.75 . 1 239 . 48 GLU CA C 54.73 . 1 240 . 48 GLU CB C 27.67 . 1 241 . 48 GLU N N 121.31 . 1 242 . 49 PHE H H 7.75 . 1 243 . 49 PHE C C 177.09 . 1 244 . 49 PHE CA C 56.21 . 1 245 . 49 PHE CB C 42.34 . 1 246 . 49 PHE N N 118.80 . 1 247 . 50 GLU H H 9.09 . 1 248 . 50 GLU C C 174.10 . 1 249 . 50 GLU CA C 53.36 . 1 250 . 50 GLU CB C 33.27 . 1 251 . 50 GLU N N 120.12 . 1 252 . 51 LYS H H 8.3 . 5 253 . 51 LYS C C 176.65 . 1 254 . 51 LYS CA C 56.8 . 1 255 . 51 LYS CB C 30.87 . 1 256 . 51 LYS N N 127.34 . 5 257 . 52 LEU H H 8.636 . 5 258 . 52 LEU C C 176.71 . 5 259 . 52 LEU CA C 54.55 . 5 260 . 52 LEU CB C 42.41 . 5 261 . 52 LEU N N 128.92 . 5 262 . 53 GLU H H 8.15 . 5 263 . 53 GLU HA H 4.29 . 1 264 . 53 GLU HB2 H 2.12 . 2 265 . 53 GLU HB3 H 1.82 . 5 266 . 53 GLU C C 174.78 . 5 267 . 53 GLU CA C 55.57 . 5 268 . 53 GLU CB C 30.72 . 5 269 . 53 GLU N N 121.99 . 5 270 . 54 ASP H H 7.92 . 5 271 . 54 ASP HA H 4.29 . 5 272 . 54 ASP HB2 H 2.627 . 5 273 . 54 ASP CA C 55.62 . 5 274 . 54 ASP CB C 42.01 . 5 275 . 54 ASP N N 126.99 . 5 stop_ save_ save_WT-PfRdZn_shift _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name WT-PfRdZn _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 1 ALA H H 8.92 . 1 2 2 1 ALA HA H 4.64 . 1 3 2 1 ALA HB H 1.46 . 1 4 2 1 ALA C C 175.84 . 1 5 2 1 ALA CA C 51.13 . 5 6 2 1 ALA CB C 19.94 . 5 7 2 1 ALA N N 125.82 . 1 8 3 2 LYS H H 8.67 . 5 9 3 2 LYS HA H 5.58 . 5 10 3 2 LYS HB2 H 1.54 . 5 11 3 2 LYS C C 174.46 . 5 12 3 2 LYS CA C 54.46 . 5 13 3 2 LYS CB C 35.81 . 5 14 3 2 LYS N N 117.83 . 5 15 4 3 TRP H H 9.42 . 5 16 4 3 TRP HA H 4.98 . 5 17 4 3 TRP HE1 H 9.74 . 5 18 4 3 TRP C C 173.90 . 1 19 4 3 TRP CA C 55.16 . 1 20 4 3 TRP CB C 31.55 . 1 21 4 3 TRP N N 123.55 . 5 22 4 3 TRP NE1 N 130.68 . 5 23 5 4 VAL H H 9.74 . 1 24 5 4 VAL C C 172.81 . 1 25 5 4 VAL CA C 58.12 . 1 26 5 4 VAL CB C 35.48 . 1 27 5 4 VAL N N 123.28 . 1 28 6 5 CYS H H 9.23 . 1 29 6 5 CYS C C 178.85 . 1 30 6 5 CYS CA C 59.24 . 1 31 6 5 CYS CB C 30.39 . 1 32 6 5 CYS N N 131.23 . 1 33 7 6 LYS H H 9.07 . 1 34 7 6 LYS C C 176.43 . 1 35 7 6 LYS CA C 58.43 . 1 36 7 6 LYS CB C 31.53 . 1 37 7 6 LYS N N 131.28 . 1 38 8 7 ILE H H 9.08 . 1 39 8 7 ILE C C 178.36 . 1 40 8 7 ILE CA C 61.75 . 1 41 8 7 ILE CB C 34.84 . 1 42 8 7 ILE N N 122.14 . 1 43 9 8 CYS H H 9.32 . 1 44 9 8 CYS C C 178.011 . 1 45 9 8 CYS CA C 58.44 . 1 46 9 8 CYS CB C 33.17 . 1 47 9 8 CYS N N 122.15 . 1 48 10 9 GLY H H 8.04 . 1 49 10 9 GLY C C 173.99 . 1 50 10 9 GLY CA C 45.33 . 1 51 10 9 GLY N N 113.47 . 1 52 11 10 TYR H H 9.38 . 1 53 11 10 TYR C C 173.08 . 1 54 11 10 TYR CA C 59.81 . 1 55 11 10 TYR CB C 39.64 . 1 56 11 10 TYR N N 128.36 . 1 57 12 11 ILE H H 7.03 . 1 58 12 11 ILE HA H 4.76 . 1 59 12 11 ILE HB H 1.46 . 1 60 12 11 ILE HG2 H 0.65 . 1 61 12 11 ILE C C 175.33 . 1 62 12 11 ILE CA C 58.63 . 1 63 12 11 ILE CB C 38.78 . 1 64 12 11 ILE N N 126.19 . 1 65 13 12 TYR H H 9.7 . 5 66 13 12 TYR CA C 57.34 . 1 67 13 12 TYR CB C 38.67 . 1 68 13 12 TYR N N 127.38 . 5 69 14 13 ASP H H 8.58 . 1 70 14 13 ASP C C 176.47 . 5 71 14 13 ASP CA C 50.97 . 5 72 14 13 ASP CB C 41.75 . 5 73 14 13 ASP N N 129.92 . 1 74 15 14 GLU H H 8.42 . 5 75 15 14 GLU C C 177.73 . 1 76 15 14 GLU CA C 58.37 . 5 77 15 14 GLU CB C 30.1 . 5 78 15 14 GLU N N 124.46 . 5 79 16 15 ASP H H 8 . 1 80 16 15 ASP C C 177.59 . 5 81 16 15 ASP CA C 56.80 . 5 82 16 15 ASP CB C 40.55 . 5 83 16 15 ASP N N 114.14 . 1 84 17 16 ALA H H 7.22 . 5 85 17 16 ALA HA H 4.29 . 5 86 17 16 ALA HB H 1.47 . 5 87 17 16 ALA C C 179.79 . 5 88 17 16 ALA CA C 52.02 . 5 89 17 16 ALA CB C 19.70 . 5 90 17 16 ALA N N 120.14 . 5 91 18 17 GLY H H 8.3 . 5 92 18 17 GLY HA2 H 3.98 . 2 93 18 17 GLY HA3 H 3.58 . 2 94 18 17 GLY C C 173.27 . 1 95 18 17 GLY CA C 44.36 . 1 96 18 17 GLY N N 104.26 . 5 97 19 18 ASP H H 8.26 . 1 98 19 18 ASP HA H 5.16 . 1 99 19 18 ASP HB3 H 2.98 . 2 100 19 18 ASP CA C 52.24 . 1 101 19 18 ASP CB C 40.14 . 1 102 19 18 ASP N N 116.85 . 1 103 20 19 PRO C C 180.06 . 1 104 20 19 PRO CA C 64.99 . 1 105 20 19 PRO CB C 31.53 . 1 106 21 20 ASP H H 9.21 . 1 107 21 20 ASP C C 177.04 . 1 108 21 20 ASP CA C 56.48 . 1 109 21 20 ASP CB C 39.60 . 1 110 21 20 ASP N N 120.46 . 1 111 22 21 ASN H H 7.67 . 1 112 22 21 ASN HD21 H 9.36 . 2 113 22 21 ASN HD22 H 6.98 . 2 114 22 21 ASN C C 175.19 . 1 115 22 21 ASN CA C 52.03 . 1 116 22 21 ASN CB C 38.87 . 1 117 22 21 ASN N N 114.94 . 1 118 22 21 ASN ND2 N 119.63 . 1 119 23 22 GLY H H 7.76 . 1 120 23 22 GLY C C 173.80 . 1 121 23 22 GLY CA C 45.57 . 1 122 23 22 GLY N N 106.03 . 1 123 24 23 ILE H H 7.60 . 1 124 24 23 ILE C C 176.47 . 1 125 24 23 ILE CA C 57.37 . 1 126 24 23 ILE CB C 35.46 . 1 127 24 23 ILE N N 121.84 . 1 128 25 24 SER H H 8.65 . 1 129 25 24 SER CA C 57.27 . 1 130 25 24 SER CB C 61.71 . 1 131 25 24 SER N N 125.04 . 1 132 26 25 PRO C C 176.69 . 1 133 26 25 PRO CA C 63.79 . 1 134 26 25 PRO CB C 31.20 . 1 135 27 26 GLY H H 8.22 . 1 136 27 26 GLY C C 174.36 . 5 137 27 26 GLY CA C 45.14 . 5 138 27 26 GLY N N 113.79 . 1 139 28 27 THR H H 7.1 . 5 140 28 27 THR HB H 4.04 . 5 141 28 27 THR C C 174.48 . 1 142 28 27 THR CA C 62.52 . 5 143 28 27 THR CB C 68.01 . 5 144 28 27 THR N N 117.1 . 5 145 29 28 LYS H H 8.76 . 5 146 29 28 LYS HA H 4.27 . 5 147 29 28 LYS HG2 H 1.41 . 2 148 29 28 LYS C C 177.40 . 5 149 29 28 LYS CA C 55.81 . 5 150 29 28 LYS CB C 31.77 . 5 151 29 28 LYS N N 130.03 . 1 152 30 29 PHE H H 9.85 . 5 153 30 29 PHE C C 178.77 . 5 154 30 29 PHE CA C 60.65 . 5 155 30 29 PHE CB C 37.95 . 5 156 30 29 PHE N N 125.97 . 5 157 31 30 GLU H H 9.39 . 5 158 31 30 GLU C C 176.82 . 1 159 31 30 GLU CA C 58.27 . 5 160 31 30 GLU CB C 28.13 . 5 161 31 30 GLU N N 114.68 . 5 162 32 31 GLU H H 7.41 . 1 163 32 31 GLU C C 176.76 . 1 164 32 31 GLU CA C 54.69 . 1 165 32 31 GLU CB C 29.40 . 1 166 32 31 GLU N N 116.37 . 1 167 33 32 LEU H H 6.82 . 1 168 33 32 LEU CA C 52.85 . 1 169 33 32 LEU CB C 39.29 . 1 170 33 32 LEU N N 122.86 . 1 171 34 33 PRO C C 177.03 . 1 172 34 33 PRO CA C 62.12 . 1 173 34 33 PRO CB C 32.02 . 1 174 35 34 ASP H H 8.71 . 1 175 35 34 ASP C C 176.47 . 1 176 35 34 ASP CA C 56.42 . 1 177 35 34 ASP CB C 39.93 . 1 178 35 34 ASP N N 120.66 . 1 179 36 35 ASP H H 8.18 . 1 180 36 35 ASP C C 175.57 . 1 181 36 35 ASP CA C 51.96 . 1 182 36 35 ASP CB C 39.09 . 1 183 36 35 ASP N N 114.26 . 1 184 37 36 TRP H H 7.61 . 1 185 37 36 TRP HE1 H 10.46 . 1 186 37 36 TRP C C 174.90 . 1 187 37 36 TRP CA C 59.71 . 1 188 37 36 TRP CB C 29.22 . 1 189 37 36 TRP N N 123.42 . 1 190 37 36 TRP NE1 N 129.59 . 1 191 38 37 VAL H H 6.17 . 1 192 38 37 VAL C C 172.11 . 1 193 38 37 VAL CA C 56.60 . 1 194 38 37 VAL CB C 34.74 . 1 195 38 37 VAL N N 117.29 . 1 196 39 38 CYS H H 8.97 . 1 197 39 38 CYS CA C 56.69 . 1 198 39 38 CYS CB C 30.75 . 1 199 39 38 CYS N N 121.69 . 1 200 40 39 PRO C C 176.18 . 1 201 40 39 PRO CA C 63.07 . 1 202 40 39 PRO CB C 31.66 . 1 203 41 40 ILE H H 8.72 . 1 204 41 40 ILE C C 178.12 . 1 205 41 40 ILE CA C 60.47 . 1 206 41 40 ILE CB C 34.89 . 1 207 41 40 ILE N N 122.03 . 1 208 42 41 CYS H H 8.83 . 1 209 42 41 CYS C C 177.64 . 1 210 42 41 CYS CA C 58.42 . 1 211 42 41 CYS CB C 32.53 . 1 212 42 41 CYS N N 121.29 . 1 213 43 42 GLY H H 7.89 . 1 214 43 42 GLY C C 173.26 . 1 215 43 42 GLY CA C 45.38 . 1 216 43 42 GLY N N 112.97 . 1 217 44 43 ALA H H 9.14 . 1 218 44 43 ALA CA C 50.75 . 1 219 44 43 ALA CB C 19.03 . 1 220 44 43 ALA N N 128.76 . 1 221 45 44 PRO C C 177.16 . 5 222 45 44 PRO CA C 61.48 . 1 223 45 44 PRO CB C 32.31 . 1 224 46 45 LYS H H 8.51 . 5 225 46 45 LYS C C 178.27 . 1 226 46 45 LYS CA C 60.03 . 5 227 46 45 LYS CB C 32.21 . 5 228 46 45 LYS N N 117.57 . 5 229 47 46 SER H H 7.91 . 1 230 47 46 SER C C 175.85 . 1 231 47 46 SER CA C 59.66 . 1 232 47 46 SER CB C 61.81 . 1 233 47 46 SER N N 110.12 . 1 234 48 47 GLU H H 8.42 . 1 235 48 47 GLU HA H 4.76 . 1 236 48 47 GLU HB2 H 2.58 . 2 237 48 47 GLU HB3 H 2.00 . 2 238 48 47 GLU C C 173.75 . 1 239 48 47 GLU CA C 54.73 . 1 240 48 47 GLU CB C 27.67 . 1 241 48 47 GLU N N 121.31 . 1 242 49 48 PHE H H 7.75 . 1 243 49 48 PHE C C 177.09 . 1 244 49 48 PHE CA C 56.21 . 1 245 49 48 PHE CB C 42.34 . 1 246 49 48 PHE N N 118.80 . 1 247 50 49 GLU H H 9.09 . 1 248 50 49 GLU C C 174.10 . 1 249 50 49 GLU CA C 53.34 . 1 250 50 49 GLU CB C 33.22 . 1 251 50 49 GLU N N 120.12 . 1 252 51 50 LYS H H 8.31 . 5 253 51 50 LYS C C 176.65 . 1 254 51 50 LYS CA C 56.8 . 1 255 51 50 LYS CB C 30.87 . 1 256 51 50 LYS N N 127.52 . 5 257 52 51 LEU H H 8.76 . 5 258 52 51 LEU C C 176.65 . 5 259 52 51 LEU CA C 54.41 . 5 260 52 51 LEU CB C 42.54 . 5 261 52 51 LEU N N 129.56 . 5 262 53 52 GLU H H 8.05 . 5 263 53 52 GLU HA H 4.29 . 1 264 53 52 GLU HB2 H 2.12 . 2 265 53 52 GLU HB3 H 1.88 . 5 266 53 52 GLU C C 174.82 . 5 267 53 52 GLU CA C 55.47 . 5 268 53 52 GLU CB C 30.84 . 5 269 53 52 GLU N N 120.8 . 5 270 54 53 ASP H H 8.01 . 5 271 54 53 ASP HA H 4.33 . 5 272 54 53 ASP HB2 H 2.47 . 5 273 54 53 ASP CA C 55.47 . 5 274 54 53 ASP CB C 41.7 . 5 275 54 53 ASP N N 127.23 . 5 stop_ save_ ######################## # Coupling constants # ######################## save_fMetPfRdZn_jnh_coupling _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Condition_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name fMetPfRdZn _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 1JNH 2 ALA N 2 ALA H 93.22 . . 0.05 2 1JNH 3 LYS N 3 LYS H 92.88 . . 0.09 3 1JNH 4 TRP N 4 TRP H 93.33 . . 0.31 4 1JNH 5 VAL N 5 VAL H 92.88 . . 0.17 5 1JNH 6 CYS N 6 CYS H 94.53 . . 0.63 6 1JNH 7 LYS N 7 LYS H 95.46 . . 0.06 7 1JNH 8 ILE N 8 ILE H 92.71 . . 0.02 8 1JNH 9 CYS N 9 CYS H 90.31 . . 0.15 9 1JNH 10 GLY N 10 GLY H 95.27 . . 0.36 10 1JNH 11 TYR N 11 TYR H 93.56 . . 0.41 11 1JNH 12 ILE N 12 ILE H 92.82 . . 0.17 12 1JNH 13 TYR N 13 TYR H 92.40 . . 0.01 13 1JNH 14 ASP N 14 ASP H 94.45 . . 0.41 14 1JNH 15 GLU N 15 GLU H 93.52 . . 0.56 15 1JNH 16 ASP N 16 ASP H 93.54 . . 0.18 16 1JNH 17 ALA N 17 ALA H 92.82 . . 0.05 17 1JNH 18 GLY N 18 GLY H 94.85 . . 0.44 18 1JNH 19 ASP N 19 ASP H 92.19 . . 0.42 19 1JNH 21 ASP N 21 ASP H 95.22 . . 0.26 20 1JNH 22 ASN N 22 ASN H 92.92 . . 0.07 21 1JNH 23 GLY N 23 GLY H 93.84 . . 0.19 22 1JNH 24 ILE N 24 ILE H 94.72 . . 0.58 23 1JNH 25 SER N 25 SER H 95.52 . . 0.61 24 1JNH 27 GLY N 27 GLY H 94.56 . . 0.15 25 1JNH 28 THR N 28 THR H 93.53 . . 0.42 26 1JNH 29 LYS N 29 LYS H 95.25 . . 0.00 27 1JNH 30 PHE N 30 PHE H 92.73 . . 0.22 28 1JNH 31 GLU N 31 GLU H 92.82 . . 0.17 29 1JNH 32 GLU N 32 GLU H 92.07 . . 0.59 30 1JNH 33 LEU N 33 LEU H 95.49 . . 0.08 31 1JNH 35 ASP N 35 ASP H 92.80 . . 0.42 32 1JNH 36 ASP N 36 ASP H 96.83 . . 0.05 33 1JNH 37 TRP N 37 TRP H 95.07 . . 0.18 34 1JNH 38 VAL N 38 VAL H 92.97 . . 0.04 35 1JNH 39 CYS N 39 CYS H 93.96 . . 0.15 36 1JNH 41 ILE N 41 ILE H 91.76 . . 0.09 37 1JNH 42 CYS N 42 CYS H 90.89 . . 0.45 38 1JNH 43 GLY N 43 GLY H 95.12 . . 0.19 39 1JNH 44 ALA N 44 ALA H 93.97 . . 0.17 40 1JNH 46 LYS N 46 LYS H 93.41 . . 0.49 41 1JNH 47 SER N 47 SER H 94.36 . . 0.53 42 1JNH 48 GLU N 48 GLU H 92.95 . . 0.26 43 1JNH 49 PHE N 49 PHE H 93.79 . . 0.22 44 1JNH 50 GLU N 50 GLU H 93.62 . . 0.20 45 1JNH 51 LYS N 51 LYS H 94.39 . . 0.57 46 1JNH 52 LEU N 52 LEU H 94.17 . . 0.06 47 1JNH 53 GLU N 53 GLU H 95.20 . . 0.11 48 1JNH 54 ASP N 54 ASP H 93.04 . . 0.10 stop_ save_ save_fMetPfRdZn_jnc_coupling _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Condition_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name fMetPfRdZn _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 1JNC 2 ALA N 1 FME C 15.74 . . 0.43 2 1JNC 3 LYS N 2 ALA C 15.53 . . 0.04 3 1JNC 4 TRP N 3 LYS C 14.92 . . 0.39 4 1JNC 5 VAL N 4 TRP C 14.65 . . 0.17 5 1JNC 6 CYS N 5 VAL C 14.35 . . 0.17 6 1JNC 7 LYS N 6 CYS C 14.28 . . 0.09 7 1JNC 8 ILE N 7 LYS C 15.71 . . 0.21 8 1JNC 9 CYS N 8 ILE C 13.46 . . 0.30 9 1JNC 10 GLY N 9 CYS C 16.29 . . 0.26 10 1JNC 11 TYR N 10 GLY C 16.20 . . 0.39 11 1JNC 12 ILE N 11 TYR C 16.38 . . 0.39 12 1JNC 13 TYR N 12 ILE C 13.22 . . 0.47 13 1JNC 14 ASP N 13 TYR C 14.16 . . 0.17 14 1JNC 15 GLU N 14 ASP C 14.74 . . 0.30 15 1JNC 16 ASP N 15 GLU C 13.68 . . 0.34 16 1JNC 17 ALA N 16 ASP C 15.32 . . 0.26 17 1JNC 18 GLY N 17 ALA C 14.68 . . 0.39 18 1JNC 19 ASP N 18 GLY C 14.41 . . 0.01 19 1JNC 21 ASP N 19 ASP C 14.86 . . 0.04 20 1JNC 22 ASN N 21 ASP C 15.44 . . 0.34 21 1JNC 23 GLY N 22 ASN C 16.32 . . 0.21 22 1JNC 24 ILE N 23 GLY C 16.59 . . 0.43 23 1JNC 25 SER N 24 ILE C 14.44 . . 0.21 24 1JNC 27 GLY N 25 SER C 16.02 . . 0.30 25 1JNC 28 THR N 27 GLY C 16.53 . . 0.43 26 1JNC 29 LYS N 28 THR C 15.41 . . 0.47 27 1JNC 30 PHE N 29 LYS C 13.77 . . 0.13 28 1JNC 31 GLU N 30 PHE C 13.83 . . 0.21 29 1JNC 32 GLU N 31 GLU C 15.68 . . 0.01 30 1JNC 33 LEU N 32 GLU C 16.20 . . 0.39 31 1JNC 35 ASP N 33 LEU C 17.02 . . 0.09 32 1JNC 36 ASP N 35 ASP C 15.50 . . 0.09 33 1JNC 37 TRP N 36 ASP C 16.56 . . 0.47 34 1JNC 38 VAL N 37 TRP C 16.47 . . 0.34 35 1JNC 39 CYS N 38 VAL C 14.92 . . 0.21 36 1JNC 41 ILE N 39 CYS C 15.50 . . 0.34 37 1JNC 42 CYS N 41 ILE C 13.49 . . 0.26 38 1JNC 43 GLY N 42 CYS C 16.32 . . 0.13 39 1JNC 44 ALA N 43 GLY C 16.17 . . 0.34 40 1JNC 46 LYS N 44 ALA C 13.25 . . 0.17 41 1JNC 47 SER N 46 LYS C 15.14 . . 0.26 42 1JNC 48 GLU N 47 SER C 15.74 . . 0.17 43 1JNC 49 PHE N 48 GLU C 16.02 . . 0.39 44 1JNC 50 GLU N 49 PHE C 14.53 . . 0.09 45 1JNC 51 LYS N 50 GLU C 15.17 . . 0.30 46 1JNC 52 LEU N 51 LYS C 14.89 . . 0.09 47 1JNC 53 GLU N 52 LEU C 14.83 . . 0.52 48 1JNC 54 ASP N 53 GLU C 15.87 . . 0.26 stop_ save_