data_10010 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; bovine beta-lactoglobulin A34C mutant ; _BMRB_accession_number 10010 _BMRB_flat_file_name bmr10010.str _Entry_type original _Submission_date 2005-10-31 _Accession_date 2005-11-01 _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 Sakurai Kazumasa . . 2 Goto Yuji . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 147 "13C chemical shifts" 463 "15N chemical shifts" 147 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-06-13 original author . stop_ _Original_release_date 2007-06-13 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Dynamics and Mechanism of the Tanford Transition of Bovine beta-Lactoglobulin Studied using Heteronuclear NMR Spectroscopy ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16368109 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sakurai Kazumasa . . 2 Goto Yuji . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 356 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 483 _Page_last 496 _Year 2006 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_citation_2 _Saveframe_category citation _Citation_full ; Kim, T.-R., Goto, Y., Hirota, N., Kuwata, K., Denton, H., Wu, S.-Y., Sawyer, L., and Batt, C.A. (1997) High-level expression of bovine beta-lactoglobulin in Pichia pastoris and characterization of its physical properties. Protein Eng. 10:1339-1345. ; _Citation_title ; High-level expression of bovine beta-lactoglobulin in Pichia pastoris and characterization of its physical properties. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9514124 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kim Tae-Rak . . 2 Goto Yuji . . 3 Hirota Nami . . 4 Kuwata Kazuo . . 5 Denton Helen . . 6 Wu Su-Ying . . 7 Sawyer Lindsay . . 8 Batt Carl A. . stop_ _Journal_abbreviation 'Protein Eng.' _Journal_name_full . _Journal_volume 10 _Journal_issue 11 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1339 _Page_last 1345 _Year 1997 _Details . save_ save_citation_3 _Saveframe_category citation _Citation_full ; Kuwata, K., Hoshino, M., Era, S., Batt, C.A., and Goto, Y. (1998) alpha to beta Transition of beta-lactoglobulin as evidenced by heteronuclear NMR. J. Mol. Biol. 283: 731-739. ; _Citation_title 'alpha to beta Transition of beta-lactoglobulin as evidenced by heteronuclear NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9790836 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kuwata Kazuo . . 2 Hoshino Masaru . . 3 Era Seiichi . . 4 Batt Carl A. . 5 Goto Yuji . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full . _Journal_volume 283 _Journal_issue 4 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 731 _Page_last 739 _Year 1998 _Details . save_ save_citation_4 _Saveframe_category citation _Citation_full ; Uhrinova, S., Uhrin, D., Denton, H., Smith, M., Sawyer, L., and Barlow, P.N. (1998) Complete assignment of 1H, 13C and 15N chemical shifts for bovine beta-lactoglobulin: Secondary structure and topology of the native state is retained in a partially unfolded form. J. Biomol. NMR 12: 89-107. ; _Citation_title ; Complete assignment of 1H, 13C and 15N chemical shifts for bovine beta-lactoglobulin: Secondary structure and topology of the native state is retained in a partially unfolded form. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9729790 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Uhrinova Stanislava . . 2 Uhrin Dusan . . 3 Denton Helen . . 4 Smith Mark . . 5 Sawyer Lindsay . . 6 Barlow Paul N. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full . _Journal_volume 12 _Journal_issue 1 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 89 _Page_last 107 _Year 1998 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'bovine beta-lactoglobulin A34C; disulfide linked dimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'BLG A34C, 1' $BLG_A34C 'BLG A34C, 2' $BLG_A34C stop_ _System_molecular_weight 37000 _System_physical_state native _System_oligomer_state 'protein-protein complex' _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'BLG A34C, 1' 1 'BLG A34C, 2' stop_ _Database_query_date . _Details ; This sample is a symmetric homodimer, in which the same residues in each monomer generate the same signals, thus the spectrum seems of the monomer. ; save_ ######################## # Monomeric polymers # ######################## save_BLG_A34C _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common BLG_A34C _Molecular_mass 18400 _Mol_thiol_state 'free and bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 165 _Mol_residue_sequence ; EAEAYVTQTMKGLDIQKVAG TWYSLAMAASDISLLDCQSA PLRVYVEELKPTPEGDLEIL LQKWENDECAQKKIIAEKTK IPAVFKIDALNENKVLVLDT DYKKYLLFCMENSAEPEQSL VCQCLVRTPEVDDEALEKFD KALKALPMHIRLSFNPTQLE EQCHI ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 GLU 2 -2 ALA 3 -1 GLU 4 1 ALA 5 2 TYR 6 3 VAL 7 4 THR 8 5 GLN 9 6 THR 10 7 MET 11 8 LYS 12 9 GLY 13 10 LEU 14 11 ASP 15 12 ILE 16 13 GLN 17 14 LYS 18 15 VAL 19 16 ALA 20 17 GLY 21 18 THR 22 19 TRP 23 20 TYR 24 21 SER 25 22 LEU 26 23 ALA 27 24 MET 28 25 ALA 29 26 ALA 30 27 SER 31 28 ASP 32 29 ILE 33 30 SER 34 31 LEU 35 32 LEU 36 33 ASP 37 34 CYS 38 35 GLN 39 36 SER 40 37 ALA 41 38 PRO 42 39 LEU 43 40 ARG 44 41 VAL 45 42 TYR 46 43 VAL 47 44 GLU 48 45 GLU 49 46 LEU 50 47 LYS 51 48 PRO 52 49 THR 53 50 PRO 54 51 GLU 55 52 GLY 56 53 ASP 57 54 LEU 58 55 GLU 59 56 ILE 60 57 LEU 61 58 LEU 62 59 GLN 63 60 LYS 64 61 TRP 65 62 GLU 66 63 ASN 67 64 ASP 68 65 GLU 69 66 CYS 70 67 ALA 71 68 GLN 72 69 LYS 73 70 LYS 74 71 ILE 75 72 ILE 76 73 ALA 77 74 GLU 78 75 LYS 79 76 THR 80 77 LYS 81 78 ILE 82 79 PRO 83 80 ALA 84 81 VAL 85 82 PHE 86 83 LYS 87 84 ILE 88 85 ASP 89 86 ALA 90 87 LEU 91 88 ASN 92 89 GLU 93 90 ASN 94 91 LYS 95 92 VAL 96 93 LEU 97 94 VAL 98 95 LEU 99 96 ASP 100 97 THR 101 98 ASP 102 99 TYR 103 100 LYS 104 101 LYS 105 102 TYR 106 103 LEU 107 104 LEU 108 105 PHE 109 106 CYS 110 107 MET 111 108 GLU 112 109 ASN 113 110 SER 114 111 ALA 115 112 GLU 116 113 PRO 117 114 GLU 118 115 GLN 119 116 SER 120 117 LEU 121 118 VAL 122 119 CYS 123 120 GLN 124 121 CYS 125 122 LEU 126 123 VAL 127 124 ARG 128 125 THR 129 126 PRO 130 127 GLU 131 128 VAL 132 129 ASP 133 130 ASP 134 131 GLU 135 132 ALA 136 133 LEU 137 134 GLU 138 135 LYS 139 136 PHE 140 137 ASP 141 138 LYS 142 139 ALA 143 140 LEU 144 141 LYS 145 142 ALA 146 143 LEU 147 144 PRO 148 145 MET 149 146 HIS 150 147 ILE 151 148 ARG 152 149 LEU 153 150 SER 154 151 PHE 155 152 ASN 156 153 PRO 157 154 THR 158 155 GLN 159 156 LEU 160 157 GLU 161 158 GLU 162 159 GLN 163 160 CYS 164 161 HIS 165 162 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-05 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 1B0O "Bovine Beta-Lactoglobulin Complexed With Palmitate, Lattice Z" 96.97 162 98.13 98.13 4.87e-109 PDB 1B8E "High Resolution Crystal Structure Of The Bovine Beta- Lactoglobulin (Isoforms A And B) In Orthorombic Space Group" 96.97 162 98.13 98.13 4.87e-109 PDB 1BEB "Bovine Beta-Lactoglobulin, Lattice X" 96.97 162 98.75 98.75 1.01e-109 PDB 1BSO "12-Bromododecanoic Acid Binds Inside The Calyx Of Bovine Beta-Lactoglobulin" 96.97 162 99.38 99.38 1.35e-110 PDB 1BSQ "Structural And Functional Consequences Of Point Mutations Of Variants A And B Of Bovine Beta-Lactoglobulin" 96.97 162 98.13 98.13 4.87e-109 PDB 1BSY "Structural Basis Of The Tanford Transition Of Bovine Beta- Lactoglobulin From Crystal Structures At Three Ph Values; Ph 7.1" 96.97 162 99.38 99.38 1.35e-110 PDB 1CJ5 "Bovine Beta-Lactoglobulin A" 98.18 162 99.38 99.38 1.84e-112 PDB 1DV9 "Structural Changes Accompanying Ph-Induced Dissociation Of The B-Lactoglobulin Dimer" 98.18 162 99.38 99.38 1.84e-112 PDB 1GX8 "Bovine Beta-Lactoglobulin Complexed With Retinol, Trigonal Lattice Z" 96.97 162 98.13 98.13 4.87e-109 PDB 1GX9 "Bovine Beta-Lactoglobulin Complexed With Retinoic Acid, Trigonal Lattice Z" 96.97 162 98.13 98.13 4.87e-109 PDB 1GXA "Bovine Beta-Lactoglobulin Complexed With Retinol And Palmitic Acid, Trigonal Lattice Z" 96.97 162 98.13 98.13 4.87e-109 PDB 1QG5 "High Resolution Crystal Structure Of The Bovine Beta- Lactoglobulin (Isoform A)" 96.97 162 99.38 99.38 1.35e-110 PDB 1UZ2 "The Cys121ser Mutant Of Beta-lactoglobulin" 96.97 162 98.75 98.75 7.51e-110 PDB 2AKQ "The Structure Of Bovine B-Lactoglobulin A In Crystals Grown At Very Low Ionic Strength" 96.97 162 99.38 99.38 1.35e-110 PDB 2BLG "Structural Basis Of The Tanford Transition Of Bovine Beta- Lactoglobulin From Crystal Structures At Three Ph Values; Ph 8.2" 96.97 162 99.38 99.38 1.35e-110 PDB 2GJ5 "Crystal Structure Of A Secondary Vitamin D3 Binding Site Of Milk Beta-Lactoglobulin" 96.97 162 98.13 98.13 4.87e-109 PDB 2Q2M "Beta-Lactoglobulin (Native)" 96.97 162 99.38 99.38 1.35e-110 PDB 2Q2P "Beta-Lactoglobulin (Reverse Native)" 96.97 162 99.38 99.38 1.35e-110 PDB 2Q39 "Beta-Lactoglobulin (Low Humidity)" 96.97 162 99.38 99.38 1.35e-110 PDB 2R56 "Crystal Structure Of A Recombinant Ige Fab Fragment In Complex With Bovine Beta-Lactoglobulin Allergen" 96.97 162 98.13 98.13 4.87e-109 PDB 3BLG "Structural Basis Of The Tanford Transition Of Bovine Beta- Lactoglobulin From Crystal Structures At Three Ph Values; Ph 6.2" 96.97 162 99.38 99.38 1.35e-110 PDB 3NPO "Bovine Beta Lactoglobulin Unliganded Form" 96.97 162 98.13 98.13 4.87e-109 PDB 3NQ3 "Bovine Beta-Lactoglobulin Complex With Capric Acid" 96.97 162 98.13 98.13 4.87e-109 PDB 3NQ9 "Bovine Beta-Lactoglobulin Complex With Caprylic Acid" 96.97 162 98.13 98.13 4.87e-109 PDB 3PH5 "Bovine Beta Lactoglobulin Crystallized Through Ligandation Of Yttrium Cations" 96.97 161 98.13 98.13 3.62e-109 PDB 3PH6 "Bovine Beta Lactoglobulin Crytsallized Through Ligandation Of Yttrium" 96.97 161 98.13 98.13 3.62e-109 PDB 3UEU "Bovine Beta-Lactoglobulin Complex With Lauric Acid" 96.97 162 98.13 98.13 4.87e-109 PDB 3UEV "Bovine Beta-Lactoglobulin Complex With Myristic Acid" 96.97 162 98.13 98.13 4.87e-109 PDB 3UEW "Bovine Beta-Lactoglobulin Complex With Palmitic Acid" 96.97 162 98.13 98.13 4.87e-109 PDB 3UEX "Bovine Beta-Lactoglobulin Complex With Stearic Acid" 96.97 162 98.13 98.13 4.87e-109 PDB 4DQ3 "Bovine Beta-lactoglobulin Complex With Oleic Acid" 96.97 162 98.13 98.13 4.87e-109 PDB 4DQ4 "Bovine Beta-lactoglobulin Complex With Linoleic Acid" 96.97 162 98.13 98.13 4.87e-109 PDB 4GNY "Bovine Beta-lactoglobulin Complex With Dodecyl Sulfate" 96.97 162 98.13 98.13 4.87e-109 PDB 4IB6 "Bovine Beta-lactoglobulin (isoform A) In Complex With Lauric Acid (c12)" 96.97 162 99.38 99.38 1.35e-110 PDB 4IB7 "Bovine Beta-lactoglobulin (isoform A) In Complex With Dodecyltrimethylammonium (dtac)" 96.97 162 99.38 99.38 1.35e-110 PDB 4IB8 "Bovine Beta-lactoglobulin (isoform A) In Complex With Dodecyl Sulphate (sds)" 96.97 162 99.38 99.38 1.35e-110 PDB 4IB9 "Bovine Beta-lactoglobulin (isoform B) In Complex With Dodecyltrimethylammonium (dtac)" 96.97 162 98.13 98.13 4.87e-109 PDB 4IBA "Bovine Beta-lactoglobulin (isoform B) In Complex With Dodecyl Sulphate (sds)" 96.97 162 98.13 98.13 4.87e-109 PDB 4KII "Beta-lactoglobulin In Complex With Cp*rh(iii)cl N,n-di(pyridin-2-yl) Dodecanamide" 96.97 162 99.38 99.38 1.35e-110 PDB 4LZU "Bovine Beta-lactoglobulin Crystallized In The Presence Of 2 Mm Zinc Chloride" 96.97 162 98.13 98.13 4.87e-109 PDB 4LZV "Bovine Beta-lactoglobulin Crystallized In The Presence Of 20 Mm Zinc Chloride" 96.97 162 98.13 98.13 4.87e-109 PDB 4Y0P "Bovine Beta-lactoglobulin Complex With Tetracaine (blg-tet)" 96.97 162 98.13 98.13 4.87e-109 PDB 4Y0Q "Bovine Beta-lactoglobulin Complex With Pramocaine Crystallized From Sodium Citrate (blg-prm1)" 96.97 162 98.13 98.13 4.87e-109 PDB 4Y0R "Bovine Beta-lactoglobulin Complex With Pramocaine Crystallized From Ammonium Sulphate (blg-prm2)" 96.97 162 98.13 98.13 4.87e-109 EMBL CAA06532 "beta-lactoglobulin [Bubalus bubalis]" 96.97 180 97.50 98.13 8.15e-109 EMBL CAA32835 "beta-lactoglobulin [Bos taurus]" 96.97 178 98.75 98.75 2.31e-109 EMBL CAA88303 "beta-lactoglobulin variant B precursor [Bos taurus]" 96.97 178 98.13 98.13 4.87e-109 EMBL CAY39357 "beta-lactoglobulin [Bubalus bubalis]" 96.97 180 97.50 98.13 9.40e-109 GB AAA30411 "beta-lactoglobulin, partial [Bos taurus]" 91.52 151 99.34 99.34 2.08e-103 GB AAI08214 "Lactoglobulin, beta [Bos taurus]" 96.97 178 98.13 98.13 4.87e-109 GB ABF48380 "beta-lactoglobulin variant B precursor [Bos taurus]" 96.97 178 98.13 98.13 4.87e-109 GB ACG59280 "major allergen beta-lactoglobulin [Bos taurus]" 96.97 178 99.38 99.38 2.16e-110 GB AFB74990 "beta-lactoglobulin, partial [Bos grunniens]" 65.45 108 97.22 97.22 1.01e-67 PRF 0601265A "lactoglobulin beta" 96.97 162 97.50 98.13 7.96e-109 REF NP_001277893 "beta-lactoglobulin precursor [Bubalus bubalis]" 96.97 180 97.50 98.13 9.40e-109 REF NP_776354 "beta-lactoglobulin precursor [Bos taurus]" 96.97 178 98.13 98.13 4.87e-109 REF XP_005888577 "PREDICTED: beta-lactoglobulin isoform X1 [Bos mutus]" 96.97 178 97.50 97.50 2.86e-108 REF XP_006062245 "PREDICTED: beta-lactoglobulin-like isoform X2 [Bubalus bubalis]" 96.97 180 97.50 98.13 9.40e-109 SP P02754 "RecName: Full=Beta-lactoglobulin; Short=Beta-LG; AltName: Allergen=Bos d 5; Flags: Precursor" 96.97 178 98.13 98.13 4.87e-109 SP P02755 "RecName: Full=Beta-lactoglobulin; Short=Beta-LG; Flags: Precursor" 96.97 180 97.50 98.13 8.15e-109 TPG DAA24277 "TPA: beta-lactoglobulin precursor [Bos taurus]" 96.97 178 98.75 98.75 1.40e-109 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Secretion $BLG_A34C Cow 9913 Eukaryota Metazoa Bos taurus milk 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 $BLG_A34C 'recombinant technology' 'Methylotrophic yeast' Pichia pastoris GS115 plasmid pPIC9 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; Protein dissolved into water. (No buffer is added.) pH is adjusted by adding HCl. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $assembly 2 mM . . '[U-99% 13C; U-99.3% 15N]' 'Hydrochloric acid' . mM 7 9 . stop_ save_ ############################ # Computer software used # ############################ save_pipp.com _Saveframe_category software _Name pipp.com _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_Bruker_DRX800 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H15N HSQC' _Sample_label $sample_1 save_ save_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HNCACO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACO _Sample_label $sample_1 save_ save_1H15N_HSQC _Saveframe_category NMR_applied_experiment _Experiment_name '1H15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_CBCA(CO)NH _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_HNCACB _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_HNCO _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_HNCACO _Saveframe_category NMR_applied_experiment _Experiment_name HNCACO _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_for_BLG_A34C_at_pH_6.5 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.000 0.000 M pH 6.5 0.1 pH temperature 313 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_default_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 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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_assignment_for_bLG_A34C_at_pH_6.5 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $pipp.com stop_ loop_ _Experiment_label '1H15N HSQC' CBCA(CO)NH HNCACB HNCO HNCACO stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_for_BLG_A34C_at_pH_6.5 _Chem_shift_reference_set_label $default_reference _Mol_system_component_name 'BLG A34C, 1' _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 2 ALA CA C 52.68 0.2 1 2 -2 2 ALA CB C 19.32 0.2 1 3 -1 3 GLU H H 8.51 0.02 1 4 -1 3 GLU C C 176.02 0.2 1 5 -1 3 GLU CA C 56.71 0.2 1 6 -1 3 GLU CB C 30.26 0.2 1 7 -1 3 GLU N N 120.73 0.1 1 8 1 4 ALA H H 8.22 0.02 1 9 1 4 ALA C C 177.22 0.2 1 10 1 4 ALA CA C 52.56 0.2 1 11 1 4 ALA CB C 19.49 0.2 1 12 1 4 ALA N N 124.3 0.1 1 13 2 5 TYR H H 8.58 0.02 1 14 2 5 TYR C C 176.14 0.2 1 15 2 5 TYR CA C 58.91 0.2 1 16 2 5 TYR CB C 38.88 0.2 1 17 2 5 TYR N N 118.51 0.1 1 18 3 6 VAL H H 8.2 0.02 1 19 3 6 VAL C C 175.86 0.2 1 20 3 6 VAL CA C 63.2 0.2 1 21 3 6 VAL CB C 32.01 0.2 1 22 3 6 VAL N N 120.44 0.1 1 23 4 7 THR H H 7.91 0.02 1 24 4 7 THR C C 174.91 0.2 1 25 4 7 THR CA C 62.03 0.2 1 26 4 7 THR CB C 69.59 0.2 1 27 4 7 THR N N 115.29 0.1 1 28 5 8 GLN H H 8.11 0.02 1 29 5 8 GLN C C 175.03 0.2 1 30 5 8 GLN CA C 55.67 0.2 1 31 5 8 GLN CB C 29.14 0.2 1 32 5 8 GLN N N 123.1 0.1 1 33 6 9 THR H H 7.65 0.02 1 34 6 9 THR C C 174.89 0.2 1 35 6 9 THR CA C 60.59 0.2 1 36 6 9 THR CB C 70.7 0.2 1 37 6 9 THR N N 110.49 0.1 1 38 7 10 MET H H 7.87 0.02 1 39 7 10 MET C C 175.8 0.2 1 40 7 10 MET CA C 56.87 0.2 1 41 7 10 MET CB C 33.18 0.2 1 42 7 10 MET N N 120.44 0.1 1 43 8 11 LYS H H 8.61 0.02 1 44 8 11 LYS C C 177.45 0.2 1 45 8 11 LYS CA C 56.94 0.2 1 46 8 11 LYS CB C 32.71 0.2 1 47 8 11 LYS N N 127.15 0.1 1 48 9 12 GLY H H 8.53 0.02 1 49 9 12 GLY C C 174.26 0.2 1 50 9 12 GLY CA C 45.84 0.2 1 51 9 12 GLY N N 109.16 0.1 1 52 10 13 LEU H H 7.51 0.02 1 53 10 13 LEU C C 175.42 0.2 1 54 10 13 LEU CA C 56.29 0.2 1 55 10 13 LEU CB C 43.02 0.2 1 56 10 13 LEU N N 120.55 0.1 1 57 11 14 ASP H H 8.59 0.02 1 58 11 14 ASP C C 177.07 0.2 1 59 11 14 ASP CA C 52.06 0.2 1 60 11 14 ASP CB C 40.53 0.2 1 61 11 14 ASP N N 127.98 0.1 1 62 12 15 ILE H H 8.74 0.02 1 63 12 15 ILE C C 176.57 0.2 1 64 12 15 ILE CA C 61.77 0.2 1 65 12 15 ILE CB C 39.14 0.2 1 66 12 15 ILE N N 122.66 0.1 1 67 13 16 GLN H H 8.11 0.02 1 68 13 16 GLN C C 179.55 0.2 1 69 13 16 GLN CA C 57.9 0.2 1 70 13 16 GLN CB C 27.35 0.2 1 71 13 16 GLN N N 116.85 0.1 1 72 14 17 LYS H H 7.34 0.02 1 73 14 17 LYS C C 177.76 0.2 1 74 14 17 LYS CA C 57.56 0.2 1 75 14 17 LYS CB C 33.39 0.2 1 76 14 17 LYS N N 114.22 0.1 1 77 15 18 VAL H H 7.39 0.02 1 78 15 18 VAL C C 173.95 0.2 1 79 15 18 VAL CA C 60.99 0.2 1 80 15 18 VAL CB C 31.25 0.2 1 81 15 18 VAL N N 110.18 0.1 1 82 16 19 ALA H H 6.81 0.02 1 83 16 19 ALA C C 178.56 0.2 1 84 16 19 ALA CA C 52.77 0.2 1 85 16 19 ALA CB C 20.28 0.2 1 86 16 19 ALA N N 120.67 0.1 1 87 17 20 GLY H H 9.18 0.02 1 88 17 20 GLY C C 172.72 0.2 1 89 17 20 GLY CA C 44.42 0.2 1 90 17 20 GLY N N 110.78 0.1 1 91 18 21 THR H H 8.28 0.02 1 92 18 21 THR C C 173.9 0.2 1 93 18 21 THR CA C 64 0.2 1 94 18 21 THR CB C 70.07 0.2 1 95 18 21 THR N N 117.41 0.1 1 96 19 22 TRP H H 7.49 0.02 1 97 19 22 TRP C C 172.12 0.2 1 98 19 22 TRP CA C 55.73 0.2 1 99 19 22 TRP CB C 36.97 0.2 1 100 19 22 TRP N N 123.57 0.1 1 101 20 23 TYR H H 9.22 0.02 1 102 20 23 TYR C C 177.52 0.2 1 103 20 23 TYR CA C 56.86 0.2 1 104 20 23 TYR CB C 42.01 0.2 1 105 20 23 TYR N N 112.6 0.1 1 106 21 24 SER H H 9.93 0.02 1 107 21 24 SER C C 172.82 0.2 1 108 21 24 SER CA C 60.06 0.2 1 109 21 24 SER CB C 62.97 0.2 1 110 21 24 SER N N 119.91 0.1 1 111 22 25 LEU C C 174.61 0.2 1 112 22 25 LEU CA C 56.71 0.2 1 113 22 25 LEU CB C 44.02 0.2 1 114 23 26 ALA H H 7.81 0.02 1 115 23 26 ALA C C 175.58 0.2 1 116 23 26 ALA CA C 50.86 0.2 1 117 23 26 ALA CB C 23.34 0.2 1 118 23 26 ALA N N 115.14 0.1 1 119 24 27 MET H H 9.24 0.02 1 120 24 27 MET C C 173 0.2 1 121 24 27 MET CA C 54.32 0.2 1 122 24 27 MET CB C 37 0.2 1 123 24 27 MET N N 114.58 0.1 1 124 25 28 ALA H H 9.39 0.02 1 125 25 28 ALA C C 174.49 0.2 1 126 25 28 ALA CA C 51.26 0.2 1 127 25 28 ALA CB C 24.85 0.2 1 128 25 28 ALA N N 123.72 0.1 1 129 26 29 ALA H H 8.64 0.02 1 130 26 29 ALA C C 178.13 0.2 1 131 26 29 ALA CA C 51.07 0.2 1 132 26 29 ALA CB C 25.27 0.2 1 133 26 29 ALA N N 119.86 0.1 1 134 27 30 SER H H 8.96 0.02 1 135 27 30 SER C C 173.65 0.2 1 136 27 30 SER CA C 60.24 0.2 1 137 27 30 SER CB C 63.8 0.2 1 138 27 30 SER N N 116.44 0.1 1 139 28 31 ASP H H 7.2 0.02 1 140 28 31 ASP C C 176.66 0.2 1 141 28 31 ASP CA C 52.68 0.2 1 142 28 31 ASP CB C 44.4 0.2 1 143 28 31 ASP N N 121.59 0.1 1 144 29 32 ILE H H 9.14 0.02 1 145 29 32 ILE C C 177.46 0.2 1 146 29 32 ILE CA C 65.78 0.2 1 147 29 32 ILE CB C 39.42 0.2 1 148 29 32 ILE N N 126.43 0.1 1 149 30 33 SER H H 8.55 0.02 1 150 30 33 SER C C 175.79 0.2 1 151 30 33 SER CA C 61.02 0.2 1 152 30 33 SER CB C 63.42 0.2 1 153 30 33 SER N N 113.18 0.1 1 154 31 34 LEU H H 7.72 0.02 1 155 31 34 LEU C C 176.88 0.2 1 156 31 34 LEU CA C 57.56 0.2 1 157 31 34 LEU CB C 41.76 0.2 1 158 31 34 LEU N N 119.57 0.1 1 159 32 35 LEU H H 6.91 0.02 1 160 32 35 LEU C C 173.87 0.2 1 161 32 35 LEU CA C 53.98 0.2 1 162 32 35 LEU CB C 46.89 0.2 1 163 32 35 LEU N N 110.64 0.1 1 164 33 36 ASP H H 7.55 0.02 1 165 33 36 ASP C C 175.81 0.2 1 166 33 36 ASP CA C 56.24 0.2 1 167 33 36 ASP CB C 42.14 0.2 1 168 33 36 ASP N N 119.58 0.1 1 169 34 37 CYS H H 8.56 0.02 1 170 34 37 CYS C C 175.07 0.2 1 171 34 37 CYS CA C 58.16 0.2 1 172 34 37 CYS CB C 45.24 0.2 1 173 34 37 CYS N N 121.41 0.1 1 174 35 38 GLN H H 8.29 0.02 1 175 35 38 GLN C C 175.82 0.2 1 176 35 38 GLN CA C 59.25 0.2 1 177 35 38 GLN CB C 28.86 0.2 1 178 35 38 GLN N N 121.17 0.1 1 179 36 39 SER H H 7.34 0.02 1 180 36 39 SER C C 174.24 0.2 1 181 36 39 SER CA C 57.25 0.2 1 182 36 39 SER CB C 63.64 0.2 1 183 36 39 SER N N 106.73 0.1 1 184 37 40 ALA H H 7.74 0.02 1 185 37 40 ALA C C 178.03 0.2 1 186 37 40 ALA CA C 51.69 0.2 1 187 37 40 ALA CB C 17.98 0.2 1 188 37 40 ALA N N 127.73 0.1 1 189 38 41 PRO C C 176.69 0.2 1 190 38 41 PRO CA C 65.15 0.2 1 191 38 41 PRO CB C 32.01 0.2 1 192 39 42 LEU H H 7.56 0.02 1 193 39 42 LEU C C 175.72 0.2 1 194 39 42 LEU CA C 52.08 0.2 1 195 39 42 LEU CB C 41.02 0.2 1 196 39 42 LEU N N 114.38 0.1 1 197 40 43 ARG H H 7.08 0.02 1 198 40 43 ARG C C 172.43 0.2 1 199 40 43 ARG CA C 55.29 0.2 1 200 40 43 ARG CB C 29.62 0.2 1 201 40 43 ARG N N 122.41 0.1 1 202 41 44 VAL H H 7.03 0.02 1 203 41 44 VAL C C 172.89 0.2 1 204 41 44 VAL CA C 57.36 0.2 1 205 41 44 VAL CB C 34.62 0.2 1 206 41 44 VAL N N 115.77 0.1 1 207 42 45 TYR H H 8.66 0.02 1 208 42 45 TYR C C 176.17 0.2 1 209 42 45 TYR CA C 55.33 0.2 1 210 42 45 TYR CB C 38.85 0.2 1 211 42 45 TYR N N 120.63 0.1 1 212 43 46 VAL H H 8.65 0.02 1 213 43 46 VAL C C 174.11 0.2 1 214 43 46 VAL CA C 64.51 0.2 1 215 43 46 VAL CB C 31.92 0.2 1 216 43 46 VAL N N 125.34 0.1 1 217 44 47 GLU H H 8.97 0.02 1 218 44 47 GLU C C 176.58 0.2 1 219 44 47 GLU CA C 55.83 0.2 1 220 44 47 GLU CB C 32.86 0.2 1 221 44 47 GLU N N 122.9 0.1 1 222 45 48 GLU H H 7.66 0.02 1 223 45 48 GLU C C 174.01 0.2 1 224 45 48 GLU CA C 55.48 0.2 1 225 45 48 GLU CB C 34.68 0.2 1 226 45 48 GLU N N 117.2 0.1 1 227 46 49 LEU H H 8.66 0.02 1 228 46 49 LEU C C 176.5 0.2 1 229 46 49 LEU CA C 53.71 0.2 1 230 46 49 LEU CB C 43.8 0.2 1 231 46 49 LEU N N 121.98 0.1 1 232 47 50 LYS H H 9.26 0.02 1 233 47 50 LYS C C 173.27 0.2 1 234 47 50 LYS CA C 53.01 0.2 1 235 47 50 LYS CB C 34.64 0.2 1 236 47 50 LYS N N 123.12 0.1 1 237 48 51 PRO C C 176.86 0.2 1 238 48 51 PRO CA C 62.25 0.2 1 239 48 51 PRO CB C 32.44 0.2 1 240 49 52 THR H H 8.8 0.02 1 241 49 52 THR C C 175.83 0.2 1 242 49 52 THR CA C 59.25 0.2 1 243 49 52 THR CB C 68.64 0.2 1 244 49 52 THR N N 115.66 0.1 1 245 50 53 PRO C C 177.79 0.2 1 246 50 53 PRO CA C 65.36 0.2 1 247 50 53 PRO CB C 31.74 0.2 1 248 51 54 GLU H H 7.71 0.02 1 249 51 54 GLU C C 176.86 0.2 1 250 51 54 GLU CA C 56.83 0.2 1 251 51 54 GLU CB C 29.44 0.2 1 252 51 54 GLU N N 112.72 0.1 1 253 52 55 GLY H H 8.3 0.02 1 254 52 55 GLY C C 174.31 0.2 1 255 52 55 GLY CA C 45.76 0.2 1 256 52 55 GLY N N 108.08 0.1 1 257 53 56 ASP H H 7.22 0.02 1 258 53 56 ASP C C 174.17 0.2 1 259 53 56 ASP CA C 54.09 0.2 1 260 53 56 ASP CB C 41.63 0.2 1 261 53 56 ASP N N 117.23 0.1 1 262 54 57 LEU H H 8.94 0.02 1 263 54 57 LEU C C 174.09 0.2 1 264 54 57 LEU CA C 54.19 0.2 1 265 54 57 LEU CB C 46.38 0.2 1 266 54 57 LEU N N 119.44 0.1 1 267 55 58 GLU H H 8.38 0.02 1 268 55 58 GLU C C 175.39 0.2 1 269 55 58 GLU CA C 55.42 0.2 1 270 55 58 GLU CB C 30.8 0.2 1 271 55 58 GLU N N 126 0.1 1 272 56 59 ILE H H 9.19 0.02 1 273 56 59 ILE C C 173.99 0.2 1 274 56 59 ILE CA C 60.96 0.2 1 275 56 59 ILE CB C 39.95 0.2 1 276 56 59 ILE N N 125.31 0.1 1 277 57 60 LEU H H 8.58 0.02 1 278 57 60 LEU C C 175.71 0.2 1 279 57 60 LEU CA C 54.78 0.2 1 280 57 60 LEU CB C 42.46 0.2 1 281 57 60 LEU N N 128.99 0.1 1 282 58 61 LEU H H 9.09 0.02 1 283 58 61 LEU C C 175.11 0.2 1 284 58 61 LEU CA C 53.2 0.2 1 285 58 61 LEU CB C 46.25 0.2 1 286 58 61 LEU N N 122.94 0.1 1 287 59 62 GLN H H 9.31 0.02 1 288 59 62 GLN C C 175.4 0.2 1 289 59 62 GLN CA C 53.84 0.2 1 290 59 62 GLN CB C 31.93 0.2 1 291 59 62 GLN N N 118.48 0.1 1 292 60 63 LYS H H 8.95 0.02 1 293 60 63 LYS C C 173.72 0.2 1 294 60 63 LYS CA C 55.34 0.2 1 295 60 63 LYS CB C 37.54 0.2 1 296 60 63 LYS N N 121.55 0.1 1 297 61 64 TRP H H 9.67 0.02 1 298 61 64 TRP C C 175.85 0.2 1 299 61 64 TRP CA C 57.97 0.2 1 300 61 64 TRP CB C 29.84 0.2 1 301 61 64 TRP N N 129.37 0.1 1 302 62 65 GLU H H 8.78 0.02 1 303 62 65 GLU C C 175.23 0.2 1 304 62 65 GLU CA C 55.71 0.2 1 305 62 65 GLU CB C 32.66 0.2 1 306 62 65 GLU N N 128.12 0.1 1 307 63 66 ASN H H 8.95 0.02 1 308 63 66 ASN C C 173.89 0.2 1 309 63 66 ASN CA C 54.92 0.2 1 310 63 66 ASN CB C 37.23 0.2 1 311 63 66 ASN N N 122.08 0.1 1 312 64 67 ASP H H 7.9 0.02 1 313 64 67 ASP C C 173.38 0.2 1 314 64 67 ASP CA C 55.38 0.2 1 315 64 67 ASP CB C 39.8 0.2 1 316 64 67 ASP N N 110.86 0.1 1 317 65 68 GLU H H 6.84 0.02 1 318 65 68 GLU C C 172.5 0.2 1 319 65 68 GLU CA C 54.27 0.2 1 320 65 68 GLU CB C 32.8 0.2 1 321 65 68 GLU N N 115.52 0.1 1 322 66 69 CYS H H 8.53 0.02 1 323 66 69 CYS C C 173.54 0.2 1 324 66 69 CYS CA C 55.23 0.2 1 325 66 69 CYS CB C 39.75 0.2 1 326 66 69 CYS N N 119.67 0.1 1 327 67 70 ALA H H 9.05 0.02 1 328 67 70 ALA C C 176.14 0.2 1 329 67 70 ALA CA C 51.33 0.2 1 330 67 70 ALA CB C 21.5 0.2 1 331 67 70 ALA N N 132.85 0.1 1 332 68 71 GLN H H 8.38 0.02 1 333 68 71 GLN C C 176.38 0.2 1 334 68 71 GLN CA C 55.05 0.2 1 335 68 71 GLN CB C 31.14 0.2 1 336 68 71 GLN N N 119.55 0.1 1 337 69 72 LYS H H 9.2 0.02 1 338 69 72 LYS C C 173.91 0.2 1 339 69 72 LYS CA C 54.08 0.2 1 340 69 72 LYS CB C 35.61 0.2 1 341 69 72 LYS N N 124.04 0.1 1 342 70 73 LYS H H 8.41 0.02 1 343 70 73 LYS C C 175.82 0.2 1 344 70 73 LYS CA C 55.19 0.2 1 345 70 73 LYS CB C 34.67 0.2 1 346 70 73 LYS N N 122.76 0.1 1 347 71 74 ILE H H 9.07 0.02 1 348 71 74 ILE C C 174.13 0.2 1 349 71 74 ILE CA C 59.6 0.2 1 350 71 74 ILE CB C 41.51 0.2 1 351 71 74 ILE N N 125 0.1 1 352 72 75 ILE H H 8.42 0.02 1 353 72 75 ILE C C 173.74 0.2 1 354 72 75 ILE CA C 60.24 0.2 1 355 72 75 ILE CB C 37.96 0.2 1 356 72 75 ILE N N 125.28 0.1 1 357 73 76 ALA H H 9.36 0.02 1 358 73 76 ALA C C 175.52 0.2 1 359 73 76 ALA CA C 49.65 0.2 1 360 73 76 ALA CB C 19.61 0.2 1 361 73 76 ALA N N 134 0.1 1 362 74 77 GLU H H 9.37 0.02 1 363 74 77 GLU C C 176.82 0.2 1 364 74 77 GLU CA C 55.36 0.2 1 365 74 77 GLU CB C 32.45 0.2 1 366 74 77 GLU N N 125.29 0.1 1 367 75 78 LYS H H 9.23 0.02 1 368 75 78 LYS C C 175.91 0.2 1 369 75 78 LYS CA C 57.32 0.2 1 370 75 78 LYS CB C 32.17 0.2 1 371 75 78 LYS N N 124.05 0.1 1 372 76 79 THR H H 8.36 0.02 1 373 76 79 THR C C 174.56 0.2 1 374 76 79 THR CA C 60.15 0.2 1 375 76 79 THR CB C 72.2 0.2 1 376 76 79 THR N N 112.06 0.1 1 377 77 80 LYS H H 8.24 0.02 1 378 77 80 LYS C C 176.17 0.2 1 379 77 80 LYS CA C 57.54 0.2 1 380 77 80 LYS CB C 32.18 0.2 1 381 77 80 LYS N N 116.17 0.1 1 382 78 81 ILE H H 8.05 0.02 1 383 78 81 ILE C C 174.81 0.2 1 384 78 81 ILE CB C 39.1 0.2 1 385 78 81 ILE N N 122.55 0.1 1 386 79 82 PRO C C 175.86 0.2 1 387 79 82 PRO CA C 64.74 0.2 1 388 80 83 ALA H H 7.9 0.02 1 389 80 83 ALA C C 174.31 0.2 1 390 80 83 ALA CA C 52.82 0.2 1 391 80 83 ALA CB C 19.82 0.2 1 392 80 83 ALA N N 115.43 0.1 1 393 81 84 VAL H H 7.29 0.02 1 394 81 84 VAL C C 175.08 0.2 1 395 81 84 VAL CA C 61.99 0.2 1 396 81 84 VAL CB C 33.58 0.2 1 397 81 84 VAL N N 117.26 0.1 1 398 82 85 PHE H H 9.61 0.02 1 399 82 85 PHE C C 174.77 0.2 1 400 82 85 PHE CA C 55.94 0.2 1 401 82 85 PHE CB C 43.66 0.2 1 402 82 85 PHE N N 126.89 0.1 1 403 83 86 LYS H H 9.64 0.02 1 404 83 86 LYS C C 176.36 0.2 1 405 83 86 LYS CA C 55.67 0.2 1 406 83 86 LYS CB C 34.81 0.2 1 407 83 86 LYS N N 124.08 0.1 1 408 84 87 ILE H H 7.72 0.02 1 409 84 87 ILE C C 174.6 0.2 1 410 84 87 ILE CA C 59.43 0.2 1 411 84 87 ILE CB C 43.88 0.2 1 412 84 87 ILE N N 116.93 0.1 1 413 85 88 ASP H H 8.75 0.02 1 414 85 88 ASP C C 174.04 0.2 1 415 85 88 ASP CA C 53.6 0.2 1 416 85 88 ASP CB C 40.87 0.2 1 417 85 88 ASP N N 120.56 0.1 1 418 86 89 ALA H H 7.2 0.02 1 419 86 89 ALA C C 175.91 0.2 1 420 86 89 ALA CA C 51.88 0.2 1 421 86 89 ALA CB C 22.72 0.2 1 422 86 89 ALA N N 121.96 0.1 1 423 87 90 LEU H H 8.99 0.02 1 424 87 90 LEU C C 175.89 0.2 1 425 87 90 LEU CA C 55.66 0.2 1 426 87 90 LEU CB C 38.52 0.2 1 427 87 90 LEU N N 114.61 0.1 1 428 88 91 ASN H H 8.71 0.02 1 429 88 91 ASN C C 174.45 0.2 1 430 88 91 ASN CA C 55.2 0.2 1 431 88 91 ASN CB C 38.23 0.2 1 432 88 91 ASN N N 111.07 0.1 1 433 89 92 GLU H H 8.28 0.02 1 434 89 92 GLU C C 176.3 0.2 1 435 89 92 GLU CA C 53.97 0.2 1 436 89 92 GLU CB C 32.43 0.2 1 437 89 92 GLU N N 117.17 0.1 1 438 90 93 ASN H H 9.16 0.02 1 439 90 93 ASN C C 176.71 0.2 1 440 90 93 ASN CA C 52.99 0.2 1 441 90 93 ASN CB C 40.25 0.2 1 442 90 93 ASN N N 115.34 0.1 1 443 91 94 LYS H H 8.51 0.02 1 444 91 94 LYS C C 175.32 0.2 1 445 91 94 LYS CA C 55.52 0.2 1 446 91 94 LYS CB C 37.95 0.2 1 447 91 94 LYS N N 121.56 0.1 1 448 92 95 VAL H H 9.02 0.02 1 449 92 95 VAL C C 173.95 0.2 1 450 92 95 VAL CA C 61.31 0.2 1 451 92 95 VAL CB C 35.09 0.2 1 452 92 95 VAL N N 121.25 0.1 1 453 93 96 LEU H H 9.51 0.02 1 454 93 96 LEU C C 176.22 0.2 1 455 93 96 LEU CA C 53.88 0.2 1 456 93 96 LEU CB C 44.51 0.2 1 457 93 96 LEU N N 126.01 0.1 1 458 94 97 VAL H H 9.3 0.02 1 459 94 97 VAL C C 175.04 0.2 1 460 94 97 VAL CA C 63.57 0.2 1 461 94 97 VAL CB C 31.66 0.2 1 462 94 97 VAL N N 123.74 0.1 1 463 95 98 LEU H H 8.55 0.02 1 464 95 98 LEU C C 176.75 0.2 1 465 95 98 LEU CA C 57.82 0.2 1 466 95 98 LEU CB C 42.73 0.2 1 467 95 98 LEU N N 128.08 0.1 1 468 96 99 ASP H H 7.25 0.02 1 469 96 99 ASP C C 174.18 0.2 1 470 96 99 ASP CA C 54.85 0.2 1 471 96 99 ASP CB C 44.33 0.2 1 472 96 99 ASP N N 110.55 0.1 1 473 97 100 THR H H 7.76 0.02 1 474 97 100 THR C C 169.55 0.2 1 475 97 100 THR CA C 60.38 0.2 1 476 97 100 THR CB C 69.22 0.2 1 477 97 100 THR N N 119.07 0.1 1 478 98 101 ASP H H 6.87 0.02 1 479 98 101 ASP C C 179.46 0.2 1 480 98 101 ASP CA C 52.66 0.2 1 481 98 101 ASP CB C 42.29 0.2 1 482 98 101 ASP N N 123.8 0.1 1 483 99 102 TYR H H 9.03 0.02 1 484 99 102 TYR C C 176.59 0.2 1 485 99 102 TYR CA C 65.05 0.2 1 486 99 102 TYR CB C 36.77 0.2 1 487 99 102 TYR N N 117.51 0.1 1 488 100 103 LYS H H 9.05 0.02 1 489 100 103 LYS C C 176.25 0.2 1 490 100 103 LYS CA C 56.84 0.2 1 491 100 103 LYS CB C 34.53 0.2 1 492 100 103 LYS N N 119.95 0.1 1 493 101 104 LYS H H 9.75 0.02 1 494 101 104 LYS C C 175.88 0.2 1 495 101 104 LYS CA C 59.47 0.2 1 496 101 104 LYS CB C 35.59 0.2 1 497 101 104 LYS N N 121.68 0.1 1 498 102 105 TYR H H 9.19 0.02 1 499 102 105 TYR C C 174.38 0.2 1 500 102 105 TYR CA C 56.72 0.2 1 501 102 105 TYR CB C 44.16 0.2 1 502 102 105 TYR N N 116.6 0.1 1 503 103 106 LEU H H 9.21 0.02 1 504 103 106 LEU C C 173.66 0.2 1 505 103 106 LEU CA C 56.82 0.2 1 506 103 106 LEU CB C 44.31 0.2 1 507 103 106 LEU N N 124.97 0.1 1 508 104 107 LEU H H 9.41 0.02 1 509 104 107 LEU C C 176.35 0.2 1 510 104 107 LEU CA C 52.65 0.2 1 511 104 107 LEU CB C 44.04 0.2 1 512 104 107 LEU N N 124.82 0.1 1 513 105 108 PHE H H 8.92 0.02 1 514 105 108 PHE C C 172.27 0.2 1 515 105 108 PHE CA C 55.95 0.2 1 516 105 108 PHE CB C 42.33 0.2 1 517 105 108 PHE N N 121.51 0.1 1 518 106 109 CYS H H 9.63 0.02 1 519 106 109 CYS C C 172.8 0.2 1 520 106 109 CYS CA C 55.74 0.2 1 521 106 109 CYS CB C 49.56 0.2 1 522 106 109 CYS N N 117.1 0.1 1 523 107 110 MET H H 9.97 0.02 1 524 107 110 MET C C 173.22 0.2 1 525 107 110 MET CA C 54.58 0.2 1 526 107 110 MET CB C 37.54 0.2 1 527 107 110 MET N N 120.86 0.1 1 528 108 111 GLU H H 8.29 0.02 1 529 108 111 GLU C C 174.61 0.2 1 530 108 111 GLU CA C 55.21 0.2 1 531 108 111 GLU CB C 33.62 0.2 1 532 108 111 GLU N N 113.83 0.1 1 533 109 112 ASN H H 9.13 0.02 1 534 109 112 ASN C C 177.29 0.2 1 535 109 112 ASN CA C 52.08 0.2 1 536 109 112 ASN CB C 38.89 0.2 1 537 109 112 ASN N N 119.8 0.1 1 538 110 113 SER H H 9.67 0.02 1 539 110 113 SER C C 174.66 0.2 1 540 110 113 SER CA C 61 0.2 1 541 110 113 SER CB C 63.18 0.2 1 542 110 113 SER N N 121.2 0.1 1 543 111 114 ALA H H 8.24 0.02 1 544 111 114 ALA C C 178.43 0.2 1 545 111 114 ALA CA C 53.82 0.2 1 546 111 114 ALA CB C 19.44 0.2 1 547 111 114 ALA N N 122.92 0.1 1 548 112 115 GLU H H 7.66 0.02 1 549 112 115 GLU C C 175.11 0.2 1 550 112 115 GLU CB C 29.89 0.2 1 551 112 115 GLU N N 114.44 0.1 1 552 113 116 PRO C C 178.43 0.2 1 553 113 116 PRO CA C 66.36 0.2 1 554 113 116 PRO CB C 31.9 0.2 1 555 114 117 GLU H H 8.69 0.02 1 556 114 117 GLU C C 178.68 0.2 1 557 114 117 GLU CA C 59.62 0.2 1 558 114 117 GLU CB C 29 0.2 1 559 114 117 GLU N N 114.5 0.1 1 560 115 118 GLN H H 7.63 0.02 1 561 115 118 GLN C C 175.84 0.2 1 562 115 118 GLN CA C 56.42 0.2 1 563 115 118 GLN CB C 29.42 0.2 1 564 115 118 GLN N N 116.61 0.1 1 565 116 119 SER H H 7.68 0.02 1 566 116 119 SER C C 173.2 0.2 1 567 116 119 SER CA C 58.69 0.2 1 568 116 119 SER CB C 65.73 0.2 1 569 116 119 SER N N 110.49 0.1 1 570 117 120 LEU H H 7.36 0.02 1 571 117 120 LEU C C 175.75 0.2 1 572 117 120 LEU CA C 56.66 0.2 1 573 117 120 LEU CB C 42.99 0.2 1 574 117 120 LEU N N 127.26 0.1 1 575 118 121 VAL H H 8.8 0.02 1 576 118 121 VAL C C 174.68 0.2 1 577 118 121 VAL CA C 60.05 0.2 1 578 118 121 VAL CB C 35.74 0.2 1 579 118 121 VAL N N 125.66 0.1 1 580 119 122 CYS H H 9.53 0.02 1 581 119 122 CYS C C 173.26 0.2 1 582 119 122 CYS CA C 55.35 0.2 1 583 119 122 CYS CB C 50.23 0.2 1 584 119 122 CYS N N 122 0.1 1 585 120 123 GLN H H 9.31 0.02 1 586 120 123 GLN C C 173.63 0.2 1 587 120 123 GLN CA C 55.57 0.2 1 588 120 123 GLN CB C 32.77 0.2 1 589 120 123 GLN N N 118.48 0.1 1 590 121 124 CYS H H 7.84 0.02 1 591 121 124 CYS C C 173 0.2 1 592 121 124 CYS CA C 56.76 0.2 1 593 121 124 CYS CB C 27.62 0.2 1 594 121 124 CYS N N 120.03 0.1 1 595 122 125 LEU H H 9.78 0.02 1 596 122 125 LEU C C 177.26 0.2 1 597 122 125 LEU CA C 52.64 0.2 1 598 122 125 LEU CB C 44.96 0.2 1 599 122 125 LEU N N 128.55 0.1 1 600 123 126 VAL H H 9.47 0.02 1 601 123 126 VAL C C 178.2 0.2 1 602 123 126 VAL CA C 59.26 0.2 1 603 123 126 VAL CB C 37.29 0.2 1 604 123 126 VAL N N 111.65 0.1 1 605 124 127 ARG H H 8.05 0.02 1 606 124 127 ARG C C 176.06 0.2 1 607 124 127 ARG CA C 57.03 0.2 1 608 124 127 ARG CB C 33.72 0.2 1 609 124 127 ARG N N 119.59 0.1 1 610 125 128 THR H H 7.59 0.02 1 611 125 128 THR C C 172.88 0.2 1 612 125 128 THR CA C 57.56 0.2 1 613 125 128 THR CB C 69.8 0.2 1 614 125 128 THR N N 108.1 0.1 1 615 126 129 PRO C C 173.45 0.2 1 616 126 129 PRO CA C 62.21 0.2 1 617 126 129 PRO CB C 26.72 0.2 1 618 127 130 GLU H H 8.45 0.02 1 619 127 130 GLU C C 175.23 0.2 1 620 127 130 GLU CA C 54.34 0.2 1 621 127 130 GLU CB C 33.49 0.2 1 622 127 130 GLU N N 121.73 0.1 1 623 128 131 VAL H H 8.64 0.02 1 624 128 131 VAL C C 174.95 0.2 1 625 128 131 VAL CA C 64.01 0.2 1 626 128 131 VAL CB C 31.44 0.2 1 627 128 131 VAL N N 121.26 0.1 1 628 129 132 ASP H H 6.14 0.02 1 629 129 132 ASP C C 175.31 0.2 1 630 129 132 ASP CA C 52.93 0.2 1 631 129 132 ASP CB C 43.11 0.2 1 632 129 132 ASP N N 126.93 0.1 1 633 130 133 ASP H H 8.8 0.02 1 634 130 133 ASP C C 178.65 0.2 1 635 130 133 ASP CA C 57.77 0.2 1 636 130 133 ASP CB C 40.88 0.2 1 637 130 133 ASP N N 125.66 0.1 1 638 131 134 GLU H H 8.19 0.02 1 639 131 134 GLU C C 178.72 0.2 1 640 131 134 GLU CA C 59.45 0.2 1 641 131 134 GLU CB C 29.12 0.2 1 642 131 134 GLU N N 121.84 0.1 1 643 132 135 ALA H H 8.27 0.02 1 644 132 135 ALA C C 179.3 0.2 1 645 132 135 ALA CA C 55.2 0.2 1 646 132 135 ALA CB C 18.67 0.2 1 647 132 135 ALA N N 123.3 0.1 1 648 133 136 LEU H H 7.71 0.02 1 649 133 136 LEU C C 179.27 0.2 1 650 133 136 LEU CA C 57.93 0.2 1 651 133 136 LEU CB C 41.51 0.2 1 652 133 136 LEU N N 115.54 0.1 1 653 134 137 GLU H H 8.03 0.02 1 654 134 137 GLU C C 179.48 0.2 1 655 134 137 GLU CA C 59.56 0.2 1 656 134 137 GLU CB C 29.14 0.2 1 657 134 137 GLU N N 121.78 0.1 1 658 135 138 LYS H H 8.07 0.02 1 659 135 138 LYS C C 179.72 0.2 1 660 135 138 LYS CA C 59.6 0.2 1 661 135 138 LYS CB C 32.27 0.2 1 662 135 138 LYS N N 119.51 0.1 1 663 136 139 PHE H H 8.49 0.02 1 664 136 139 PHE C C 175.56 0.2 1 665 136 139 PHE CA C 60.47 0.2 1 666 136 139 PHE CB C 39.11 0.2 1 667 136 139 PHE N N 121.48 0.1 1 668 137 140 ASP H H 8.44 0.02 1 669 137 140 ASP C C 179.61 0.2 1 670 137 140 ASP CA C 57.8 0.2 1 671 137 140 ASP CB C 40.91 0.2 1 672 137 140 ASP N N 118.42 0.1 1 673 138 141 LYS H H 8.11 0.02 1 674 138 141 LYS C C 179.3 0.2 1 675 138 141 LYS CA C 59.59 0.2 1 676 138 141 LYS CB C 32.42 0.2 1 677 138 141 LYS N N 118.5 0.1 1 678 139 142 ALA H H 7.88 0.02 1 679 139 142 ALA C C 179.25 0.2 1 680 139 142 ALA CA C 54.26 0.2 1 681 139 142 ALA CB C 17.79 0.2 1 682 139 142 ALA N N 121.74 0.1 1 683 140 143 LEU H H 7.46 0.02 1 684 140 143 LEU C C 178.73 0.2 1 685 140 143 LEU CA C 55.34 0.2 1 686 140 143 LEU CB C 41.44 0.2 1 687 140 143 LEU N N 114.71 0.1 1 688 141 144 LYS H H 7.17 0.02 1 689 141 144 LYS C C 177 0.2 1 690 141 144 LYS CA C 59.23 0.2 1 691 141 144 LYS CB C 32.46 0.2 1 692 141 144 LYS N N 120.19 0.1 1 693 142 145 ALA H H 7.82 0.02 1 694 142 145 ALA C C 176.7 0.2 1 695 142 145 ALA CA C 51.72 0.2 1 696 142 145 ALA CB C 19.32 0.2 1 697 142 145 ALA N N 117.97 0.1 1 698 143 146 LEU H H 7.78 0.02 1 699 143 146 LEU C C 175.92 0.2 1 700 143 146 LEU CB C 42.71 0.2 1 701 143 146 LEU N N 120.02 0.1 1 702 144 147 PRO C C 174.89 0.2 1 703 144 147 PRO CA C 62.3 0.2 1 704 144 147 PRO CB C 28.25 0.2 1 705 145 148 MET H H 7.66 0.02 1 706 145 148 MET C C 177.41 0.2 1 707 145 148 MET CA C 54.3 0.2 1 708 145 148 MET CB C 32.77 0.2 1 709 145 148 MET N N 117.94 0.1 1 710 146 149 HIS H H 8.87 0.02 1 711 146 149 HIS C C 171.66 0.2 1 712 146 149 HIS CA C 57.19 0.2 1 713 146 149 HIS CB C 31.38 0.2 1 714 146 149 HIS N N 118.8 0.1 1 715 147 150 ILE H H 7.68 0.02 1 716 147 150 ILE C C 172.73 0.2 1 717 147 150 ILE CA C 59.44 0.2 1 718 147 150 ILE CB C 40.58 0.2 1 719 147 150 ILE N N 116.3 0.1 1 720 148 151 ARG H H 8.55 0.02 1 721 148 151 ARG C C 174.09 0.2 1 722 148 151 ARG CA C 55.14 0.2 1 723 148 151 ARG CB C 34.33 0.2 1 724 148 151 ARG N N 125.75 0.1 1 725 149 152 LEU H H 9.21 0.02 1 726 149 152 LEU C C 175.67 0.2 1 727 149 152 LEU CA C 54.42 0.2 1 728 149 152 LEU CB C 46.72 0.2 1 729 149 152 LEU N N 124.39 0.1 1 730 150 153 SER H H 8.84 0.02 1 731 150 153 SER C C 173.35 0.2 1 732 150 153 SER CA C 57.21 0.2 1 733 150 153 SER CB C 65.65 0.2 1 734 150 153 SER N N 116.5 0.1 1 735 151 154 PHE H H 8.46 0.02 1 736 151 154 PHE C C 174.13 0.2 1 737 151 154 PHE CA C 58.41 0.2 1 738 151 154 PHE CB C 41.49 0.2 1 739 151 154 PHE N N 121.29 0.1 1 740 152 155 ASN H H 8.66 0.02 1 741 152 155 ASN C C 174.34 0.2 1 742 152 155 ASN CA C 50.9 0.2 1 743 152 155 ASN CB C 38.11 0.2 1 744 152 155 ASN N N 118.63 0.1 1 745 153 156 PRO C C 177.96 0.2 1 746 153 156 PRO CA C 66.45 0.2 1 747 153 156 PRO CB C 32.18 0.2 1 748 154 157 THR H H 7.7 0.02 1 749 154 157 THR C C 176.71 0.2 1 750 154 157 THR CA C 65.43 0.2 1 751 154 157 THR CB C 68.72 0.2 1 752 154 157 THR N N 110.84 0.1 1 753 155 158 GLN H H 7.85 0.02 1 754 155 158 GLN C C 177.74 0.2 1 755 155 158 GLN CA C 57.87 0.2 1 756 155 158 GLN CB C 28.67 0.2 1 757 155 158 GLN N N 119.91 0.1 1 stop_ save_