data_4980 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N sequential assignment and secondary structure of the monomeric N67D mutant of bovine seminal ribonuclease ; _BMRB_accession_number 4980 _BMRB_flat_file_name bmr4980.str _Entry_type original _Submission_date 2001-03-25 _Accession_date 2001-03-25 _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 Crescenzi Orlando . . 2 Carotenuto Alfonso . . 3 D'Ursi Anna M. . 4 Tancredi Teodorico . . 5 D'Alessio Giuseppe . . 6 Avitabile Francesca . . 7 Picone Delia . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 614 "15N chemical shifts" 129 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-02-04 update BMRB 'update entry release, etc.' 2001-07-30 original author 'original release' stop_ _Original_release_date 2001-03-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H and 15N sequential assignment and secondary structure of the monomeric N67D mutant of bovine seminal ribonuclease ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Crescenzi Orlando . . 2 Carotenuto Alfonso . . 3 D'Ursi Anna M. . 4 Tancredi Teodorico . . 5 D'Alessio Giuseppe . . 6 Avitabile Francesca . . 7 Picone Delia . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 20 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 289 _Page_last 290 _Year 2001 _Details . loop_ _Keyword 'antitumor activity' 'domain swapping' ribonuclease stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., Bax, A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR (1995) 6, 277-93 ; _Citation_title ; NMRPipe: a multidimensional spectral processing system based on UNIX pipes. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F. . . 2 Grzesiek S. . . 3 Vuister G.W. W. . 4 Zhu G. . . 5 Pfeifer J. . . 6 Bax A. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 3 _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 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Johnson, B.A., Blevins, R.A. NMR View: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR (1994) 4, 603-614 ; _Citation_title . _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 . . . . stop_ _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _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 . _Page_last . _Year . _Details . save_ save_ref_3 _Saveframe_category citation _Citation_full ; Guntert, P., Mumenthaler, C., Wuthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. (1997) 273, 283-98 ; _Citation_title ; Torsion angle dynamics for NMR structure calculation with the new program DYANA. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9367762 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Guntert P. . . 2 Mumenthaler C. . . 3 Wuthrich K. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 273 _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 283 _Page_last 298 _Year 1997 _Details ; The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the "bundle" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures. ; save_ save_ref_4 _Saveframe_category citation _Citation_full ; Pearlman, D.A., Case, D.A., Caldwell, J.W., Ross, W.S., Cheatham III, T.E., DeBolt, S., Ferguson, D., Seibel, G & Kollman, P.A. AMBER, a computer program for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to elucidate the structures and energies of molecules. Comp. Phys. Commun. (1995) 91, 1-41 ; _Citation_title . _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 . . . . stop_ _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _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 . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_mBS-RNAse _Saveframe_category molecular_system _Mol_system_name 'bovine seminal ribonuclease monomer (N67D mutant)' _Abbreviation_common mBS-RNAse _Enzyme_commission_number 3.1.27.5 loop_ _Mol_system_component_name _Mol_label ribonuclease $mBS-RNAse glutathione_1 $entity_GSH glutathione_2 $entity_GSH stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function ribonuclease stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_mBS-RNAse _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'bovine seminal ribonuclease monomer' _Name_variant N67D _Abbreviation_common mBS-RNAse _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details ; The N-terminal Met-0 is introduced by expression in E. coli. The N67D mutation has been engeneered to prevent deamidation, which occurs spontaneously at the Asn-67 site. ; ############################## # Polymer residue sequence # ############################## _Residue_count 125 _Mol_residue_sequence ; MKESAAAKFERQHMDSGNSP SSSSNYCNLMMCCRKMTQGK CKPVNTFVHESLADVKAVCS QKKVTCKDGQTNCYQSKSTM RITDCRETGSSKYPNCAYKT TQVEKHIIVACGGKPSVPVH FDASV ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 MET 2 1 LYS 3 2 GLU 4 3 SER 5 4 ALA 6 5 ALA 7 6 ALA 8 7 LYS 9 8 PHE 10 9 GLU 11 10 ARG 12 11 GLN 13 12 HIS 14 13 MET 15 14 ASP 16 15 SER 17 16 GLY 18 17 ASN 19 18 SER 20 19 PRO 21 20 SER 22 21 SER 23 22 SER 24 23 SER 25 24 ASN 26 25 TYR 27 26 CYS 28 27 ASN 29 28 LEU 30 29 MET 31 30 MET 32 31 CYS 33 32 CYS 34 33 ARG 35 34 LYS 36 35 MET 37 36 THR 38 37 GLN 39 38 GLY 40 39 LYS 41 40 CYS 42 41 LYS 43 42 PRO 44 43 VAL 45 44 ASN 46 45 THR 47 46 PHE 48 47 VAL 49 48 HIS 50 49 GLU 51 50 SER 52 51 LEU 53 52 ALA 54 53 ASP 55 54 VAL 56 55 LYS 57 56 ALA 58 57 VAL 59 58 CYS 60 59 SER 61 60 GLN 62 61 LYS 63 62 LYS 64 63 VAL 65 64 THR 66 65 CYS 67 66 LYS 68 67 ASP 69 68 GLY 70 69 GLN 71 70 THR 72 71 ASN 73 72 CYS 74 73 TYR 75 74 GLN 76 75 SER 77 76 LYS 78 77 SER 79 78 THR 80 79 MET 81 80 ARG 82 81 ILE 83 82 THR 84 83 ASP 85 84 CYS 86 85 ARG 87 86 GLU 88 87 THR 89 88 GLY 90 89 SER 91 90 SER 92 91 LYS 93 92 TYR 94 93 PRO 95 94 ASN 96 95 CYS 97 96 ALA 98 97 TYR 99 98 LYS 100 99 THR 101 100 THR 102 101 GLN 103 102 VAL 104 103 GLU 105 104 LYS 106 105 HIS 107 106 ILE 108 107 ILE 109 108 VAL 110 109 ALA 111 110 CYS 112 111 GLY 113 112 GLY 114 113 LYS 115 114 PRO 116 115 SER 117 116 VAL 118 117 PRO 119 118 VAL 120 119 HIS 121 120 PHE 122 121 ASP 123 122 ALA 124 123 SER 125 124 VAL stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 11BA ; Binding Of A Substrate Analogue To A Domain Swapping Protein In The Complex Of Bovine Seminal Ribonuclease With Uridylyl-2',5'-Adenosine ; 99.20 124 99.19 100.00 1.09e-66 PDB 11BG 'A Potential Allosteric Subsite Generated By Domain Swapping In Bovine Seminal Ribonuclease' 99.20 124 99.19 100.00 1.09e-66 PDB 1BSR 'Bovine Seminal Ribonuclease Structure At 1.9 Angstroms Resolution' 99.20 124 99.19 100.00 1.09e-66 PDB 1QWQ 'Solution Structure Of The Monomeric N67d Mutant Of Bovine Seminal Ribonuclease' 99.20 124 100.00 100.00 3.14e-67 PDB 1R3M 'Crystal Structure Of The Dimeric Unswapped Form Of Bovine Seminal Ribonuclease' 99.20 124 99.19 100.00 1.09e-66 PDB 1R5C 'X-Ray Structure Of The Complex Of Bovine Seminal Ribonuclease Swapping Dimer With D(Cpa)' 99.20 124 99.19 100.00 1.09e-66 PDB 1R5D 'X-Ray Structure Of Bovine Seminal Ribonuclease Swapping Dimer From A New Crystal Form' 99.20 124 99.19 100.00 1.09e-66 PDB 1Y92 'Crystal Structure Of The P19aN67D VARIANT OF BOVINE Seminal Ribonuclease' 99.20 124 99.19 99.19 1.57e-66 PDB 3BCM 'Crystal Structure Of The Unswapped Form Of P19aL28QN67D Bs-Rnase' 99.20 124 98.39 98.39 1.34e-65 PDB 3BCO 'Crystal Structure Of The Swapped Form Of P19aL28QN67D BS- Rnase' 99.20 124 98.39 98.39 1.34e-65 EMBL CAA04155 'seminal ribonuclease [Bos taurus]' 99.20 150 99.19 100.00 1.45e-67 EMBL CAA35716 'seminal ribonuclease [Bos taurus]' 99.20 150 99.19 100.00 1.45e-67 GenBank AAB27820 'bovine seminal ribonuclease; BS-RNase [synthetic construct]' 100.00 125 99.20 100.00 2.33e-67 GenBank AAB36140 'seminal ribonuclease [Bos taurus]' 99.20 124 99.19 100.00 1.09e-66 REF NP_861526 'pancreatic ribonuclease [Bos taurus]' 99.20 150 99.19 100.00 1.45e-67 SWISS-PROT P00669 'Seminal ribonuclease precursor (Seminal RNase) (S-RNase) (Ribonuclease BS-1)' 99.20 150 99.19 100.00 1.45e-67 stop_ save_ ############# # Ligands # ############# save_GSH _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common GLUTATHIONE _BMRB_code GSH _PDB_code GSH _Molecular_mass 307.323 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N1 N1 N . 0 . ? CA1 CA1 C . 0 . ? C1 C1 C . 0 . ? O11 O11 O . 0 . ? O12 O12 O . 0 . ? CB1 CB1 C . 0 . ? CG1 CG1 C . 0 . ? CD1 CD1 C . 0 . ? OE1 OE1 O . 0 . ? N2 N2 N . 0 . ? CA2 CA2 C . 0 . ? C2 C2 C . 0 . ? O2 O2 O . 0 . ? CB2 CB2 C . 0 . ? SG2 SG2 S . 0 . ? N3 N3 N . 0 . ? CA3 CA3 C . 0 . ? C3 C3 C . 0 . ? O31 O31 O . 0 . ? O32 O32 O . 0 . ? HN11 HN11 H . 0 . ? HN12 HN12 H . 0 . ? HA1 HA1 H . 0 . ? H12 H12 H . 0 . ? HB12 HB12 H . 0 . ? HB13 HB13 H . 0 . ? HG12 HG12 H . 0 . ? HG13 HG13 H . 0 . ? HN2 HN2 H . 0 . ? HA2 HA2 H . 0 . ? HB22 HB22 H . 0 . ? HB23 HB23 H . 0 . ? HSG HSG H . 0 . ? HN3 HN3 H . 0 . ? HA31 HA31 H . 0 . ? HA32 HA32 H . 0 . ? H32 H32 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 N1 CA1 ? ? SING N1 HN11 ? ? SING N1 HN12 ? ? SING CA1 C1 ? ? SING CA1 CB1 ? ? SING CA1 HA1 ? ? DOUB C1 O11 ? ? SING C1 O12 ? ? SING O12 H12 ? ? SING CB1 CG1 ? ? SING CB1 HB12 ? ? SING CB1 HB13 ? ? SING CG1 CD1 ? ? SING CG1 HG12 ? ? SING CG1 HG13 ? ? DOUB CD1 OE1 ? ? SING CD1 N2 ? ? SING N2 CA2 ? ? SING N2 HN2 ? ? SING CA2 C2 ? ? SING CA2 CB2 ? ? SING CA2 HA2 ? ? DOUB C2 O2 ? ? SING C2 N3 ? ? SING CB2 SG2 ? ? SING CB2 HB22 ? ? SING CB2 HB23 ? ? SING SG2 HSG ? ? SING N3 CA3 ? ? SING N3 HN3 ? ? SING CA3 C3 ? ? SING CA3 HA31 ? ? SING CA3 HA32 ? ? DOUB C3 O31 ? ? SING C3 O32 ? ? SING O32 H32 ? ? 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 _Organ _Secretion $mBS-RNAse bull 9913 Eukaryota Metazoa Bos taurus 'seminal vesicles' 'seminal plasma' 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 $mBS-RNAse 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET-22b+ stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_15N-labelled _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $mBS-RNAse 2.0 mM '[U-97% 15N]' $entity_GSH 4.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_nmrPipe _Saveframe_category software _Name nmrPipe _Version . loop_ _Task 'data processing' stop_ _Details . _Citation_label $ref_1 save_ save_nmrView _Saveframe_category software _Name nmrView _Version 4.0.3 loop_ _Task 'spectra visualization' stop_ _Details . _Citation_label $ref_2 save_ save_dyana _Saveframe_category software _Name dyana _Version 1.5 loop_ _Task 'simulated annealing' stop_ _Details . _Citation_label $ref_3 save_ save_amber _Saveframe_category software _Name amber _Version 5.0 loop_ _Task 'restrained minimization' stop_ _Details . _Citation_label $ref_4 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H COSY' _Sample_label $15N-labelled save_ save_2D_1H-1H_DQ-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H DQ-COSY' _Sample_label $15N-labelled save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $15N-labelled save_ save_2D_1H-1H_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $15N-labelled save_ save_2D_1H-1H_CLEAN-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H CLEAN-TOCSY' _Sample_label $15N-labelled save_ save_2D_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $15N-labelled save_ save_3D_1H-1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _Sample_label $15N-labelled save_ save_3D_1H-1H-15N_TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N TOCSY' _Sample_label $15N-labelled save_ save_3D_HNHA_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label $15N-labelled save_ save_3D_HNHB_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _Sample_label $15N-labelled save_ ####################### # Sample conditions # ####################### save_standard _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.65 0.02 n/a temperature 300 0.2 K 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 H2O H 1 . ppm 4.70 internal direct . . . . DSS N 15 . ppm . internal 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H COSY' stop_ loop_ _Sample_label $15N-labelled stop_ _Sample_conditions_label $standard _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name ribonuclease _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 . 3 GLU N N 125.4 . 1 2 . 3 GLU H H 8.45 . 1 3 . 3 GLU HA H 4.34 . 1 4 . 3 GLU HB2 H 2.06 . 2 5 . 3 GLU HB3 H 1.88 . 2 6 . 3 GLU HG2 H 2.41 . 2 7 . 3 GLU HG3 H 2.17 . 2 8 . 4 SER N N 123.9 . 1 9 . 4 SER H H 8.76 . 1 10 . 4 SER HA H 4.47 . 1 11 . 4 SER HB2 H 4.34 . 2 12 . 4 SER HB3 H 4.09 . 2 13 . 5 ALA N N 124.7 . 1 14 . 5 ALA H H 8.96 . 1 15 . 5 ALA HA H 4.18 . 1 16 . 5 ALA HB H 1.57 . 1 17 . 6 ALA N N 121.2 . 1 18 . 6 ALA H H 8.66 . 1 19 . 6 ALA HA H 4.35 . 1 20 . 6 ALA HB H 1.45 . 1 21 . 7 ALA N N 123.1 . 1 22 . 7 ALA H H 8.01 . 1 23 . 7 ALA HA H 4.18 . 1 24 . 7 ALA HB H 1.57 . 1 25 . 8 LYS N N 122.4 . 1 26 . 8 LYS H H 8.74 . 1 27 . 8 LYS HA H 3.98 . 1 28 . 8 LYS HB2 H 1.97 . 2 29 . 8 LYS HB3 H 1.80 . 2 30 . 8 LYS HG2 H 1.57 . 2 31 . 8 LYS HG3 H 1.43 . 2 32 . 9 PHE N N 119.9 . 1 33 . 9 PHE H H 8.06 . 1 34 . 9 PHE HA H 4.35 . 1 35 . 9 PHE HB2 H 3.46 . 2 36 . 9 PHE HB3 H 2.93 . 2 37 . 9 PHE HD1 H 6.98 . 1 38 . 9 PHE HD2 H 6.98 . 1 39 . 9 PHE HE1 H 6.83 . 1 40 . 9 PHE HE2 H 6.83 . 1 41 . 9 PHE HZ H 7.00 . 1 42 . 10 GLU N N 119.3 . 1 43 . 10 GLU H H 7.92 . 1 44 . 10 GLU HA H 3.72 . 1 45 . 10 GLU HB2 H 2.72 . 2 46 . 10 GLU HB3 H 2.22 . 2 47 . 11 ARG N N 120.2 . 1 48 . 11 ARG H H 8.32 . 1 49 . 11 ARG HA H 4.17 . 1 50 . 11 ARG HB2 H 1.97 . 2 51 . 11 ARG HB3 H 1.86 . 2 52 . 11 ARG HG2 H 1.57 . 2 53 . 11 ARG HD2 H 3.19 . 2 54 . 11 ARG HD3 H 3.08 . 2 55 . 11 ARG NE N 83.3 . 1 56 . 11 ARG HE H 9.68 . 1 57 . 12 GLN N N 111.5 . 1 58 . 12 GLN H H 8.43 . 1 59 . 12 GLN HA H 3.76 . 1 60 . 12 GLN HB2 H 1.34 . 2 61 . 12 GLN HB3 H 0.97 . 2 62 . 12 GLN HG2 H 2.60 . 2 63 . 12 GLN HG3 H 2.02 . 2 64 . 13 HIS N N 105.9 . 1 65 . 13 HIS H H 7.71 . 1 66 . 13 HIS HA H 4.90 . 1 67 . 13 HIS HB2 H 2.50 . 2 68 . 13 HIS HB3 H 1.75 . 2 69 . 13 HIS HD2 H 6.56 . 1 70 . 13 HIS HE1 H 7.38 . 1 71 . 14 MET N N 116.5 . 1 72 . 14 MET H H 8.04 . 1 73 . 14 MET HA H 5.42 . 1 74 . 14 MET HB2 H 2.76 . 2 75 . 14 MET HB3 H 2.22 . 2 76 . 14 MET HG2 H 2.32 . 2 77 . 14 MET HE H 1.94 . 1 78 . 15 ASP N N 123.2 . 1 79 . 15 ASP H H 8.80 . 1 80 . 15 ASP HA H 4.99 . 1 81 . 15 ASP HB2 H 2.35 . 2 82 . 15 ASP HB3 H 2.30 . 2 83 . 16 SER N N 121.2 . 1 84 . 16 SER H H 8.95 . 1 85 . 16 SER HA H 4.18 . 1 86 . 16 SER HB2 H 3.81 . 2 87 . 16 SER HB3 H 3.67 . 2 88 . 17 GLY N N 111.0 . 1 89 . 17 GLY H H 8.59 . 1 90 . 17 GLY HA2 H 4.09 . 2 91 . 17 GLY HA3 H 3.87 . 2 92 . 18 ASN N N 118.7 . 1 93 . 18 ASN H H 7.98 . 1 94 . 18 ASN HA H 4.63 . 1 95 . 18 ASN HB2 H 2.64 . 2 96 . 18 ASN HB3 H 2.58 . 2 97 . 18 ASN ND2 N 113.9 . 1 98 . 18 ASN HD21 H 7.80 . 2 99 . 18 ASN HD22 H 6.78 . 2 100 . 19 SER N N 116.9 . 1 101 . 19 SER H H 8.29 . 1 102 . 19 SER HA H 4.17 . 1 103 . 19 SER HB2 H 3.63 . 2 104 . 19 SER HB3 H 3.58 . 2 105 . 20 PRO HA H 4.18 . 1 106 . 21 SER N N 114.9 . 1 107 . 21 SER H H 8.12 . 1 108 . 21 SER HA H 4.32 . 1 109 . 21 SER HB2 H 3.78 . 2 110 . 21 SER HB3 H 3.62 . 2 111 . 22 SER N N 118.1 . 1 112 . 22 SER H H 8.41 . 1 113 . 22 SER HA H 4.36 . 1 114 . 22 SER HB2 H 3.90 . 1 115 . 22 SER HB3 H 3.90 . 1 116 . 23 SER N N 116.3 . 1 117 . 23 SER H H 8.28 . 1 118 . 23 SER HA H 4.55 . 1 119 . 23 SER HB2 H 3.98 . 2 120 . 23 SER HB3 H 3.88 . 2 121 . 24 SER N N 118.5 . 1 122 . 24 SER H H 8.38 . 1 123 . 24 SER HA H 4.50 . 1 124 . 24 SER HB2 H 4.06 . 2 125 . 24 SER HB3 H 3.94 . 2 126 . 25 ASN N N 119.8 . 1 127 . 25 ASN H H 8.48 . 1 128 . 25 ASN HA H 4.90 . 1 129 . 25 ASN HB2 H 2.93 . 2 130 . 25 ASN HB3 H 2.75 . 2 131 . 25 ASN ND2 N 113.9 . 1 132 . 25 ASN HD21 H 7.66 . 2 133 . 25 ASN HD22 H 7.18 . 2 134 . 26 TYR N N 120.9 . 1 135 . 26 TYR H H 7.76 . 1 136 . 26 TYR HA H 3.91 . 1 137 . 26 TYR HB2 H 3.25 . 2 138 . 26 TYR HB3 H 2.74 . 2 139 . 26 TYR HD1 H 6.96 . 1 140 . 26 TYR HD2 H 6.96 . 1 141 . 26 TYR HE1 H 6.38 . 1 142 . 26 TYR HE2 H 6.38 . 1 143 . 27 CYS N N 114.6 . 1 144 . 27 CYS H H 7.80 . 1 145 . 27 CYS HA H 3.76 . 1 146 . 27 CYS HB2 H 3.06 . 2 147 . 27 CYS HB3 H 2.10 . 2 148 . 28 ASN N N 119.7 . 1 149 . 28 ASN H H 7.77 . 1 150 . 28 ASN HA H 4.37 . 1 151 . 28 ASN HB2 H 2.85 . 2 152 . 28 ASN ND2 N 109.5 . 1 153 . 28 ASN HD21 H 7.63 . 2 154 . 28 ASN HD22 H 6.95 . 2 155 . 29 LEU N N 119.4 . 1 156 . 29 LEU H H 7.43 . 1 157 . 29 LEU HA H 4.05 . 1 158 . 29 LEU HB2 H 1.52 . 2 159 . 29 LEU HG H 1.35 . 1 160 . 29 LEU HD1 H 0.74 . 1 161 . 29 LEU HD2 H 0.74 . 1 162 . 30 MET N N 117.4 . 1 163 . 30 MET H H 8.47 . 1 164 . 30 MET HA H 4.14 . 1 165 . 30 MET HB2 H 0.81 . 1 166 . 30 MET HB3 H 0.81 . 1 167 . 30 MET HG2 H 2.31 . 2 168 . 30 MET HG3 H 1.33 . 2 169 . 31 MET N N 116.3 . 1 170 . 31 MET H H 8.67 . 1 171 . 31 MET HA H 4.27 . 1 172 . 31 MET HB2 H 1.64 . 2 173 . 31 MET HB3 H 1.35 . 2 174 . 31 MET HG2 H 2.30 . 2 175 . 31 MET HG3 H 0.46 . 2 176 . 32 CYS N N 115.5 . 1 177 . 32 CYS H H 6.59 . 1 178 . 32 CYS HA H 4.70 . 1 179 . 32 CYS HB2 H 3.35 . 2 180 . 32 CYS HB3 H 3.12 . 2 181 . 33 CYS N N 123.4 . 1 182 . 33 CYS H H 9.45 . 1 183 . 33 CYS HA H 4.39 . 1 184 . 33 CYS HB2 H 3.16 . 2 185 . 33 CYS HB3 H 3.10 . 2 186 . 34 ARG N N 116.2 . 1 187 . 34 ARG H H 8.10 . 1 188 . 34 ARG HA H 4.45 . 1 189 . 34 ARG HB2 H 2.38 . 2 190 . 34 ARG HB3 H 1.89 . 2 191 . 34 ARG HG2 H 1.84 . 2 192 . 34 ARG HG3 H 1.72 . 2 193 . 34 ARG HD2 H 3.43 . 2 194 . 34 ARG HD3 H 3.09 . 2 195 . 34 ARG NE N 83.8 . 1 196 . 34 ARG HE H 7.29 . 1 197 . 35 LYS N N 110.4 . 1 198 . 35 LYS H H 7.69 . 1 199 . 35 LYS HA H 4.34 . 1 200 . 35 LYS HB2 H 2.18 . 2 201 . 35 LYS HB3 H 1.94 . 2 202 . 35 LYS HG2 H 1.41 . 2 203 . 35 LYS HG3 H 1.26 . 2 204 . 35 LYS HD2 H 1.68 . 2 205 . 35 LYS HD3 H 1.58 . 2 206 . 36 MET N N 116.0 . 1 207 . 36 MET H H 8.20 . 1 208 . 36 MET HA H 4.72 . 1 209 . 36 MET HB2 H 2.33 . 2 210 . 36 MET HB3 H 1.99 . 2 211 . 36 MET HG2 H 2.57 . 2 212 . 36 MET HG3 H 2.18 . 2 213 . 37 THR N N 107.0 . 1 214 . 37 THR H H 7.56 . 1 215 . 37 THR HA H 5.23 . 1 216 . 37 THR HB H 4.79 . 1 217 . 37 THR HG2 H 1.15 . 1 218 . 38 GLN N N 120.4 . 1 219 . 38 GLN H H 7.33 . 1 220 . 38 GLN HA H 4.51 . 1 221 . 38 GLN HB2 H 2.04 . 1 222 . 38 GLN HB3 H 2.04 . 1 223 . 38 GLN HG2 H 2.35 . 1 224 . 38 GLN HG3 H 2.35 . 1 225 . 38 GLN NE2 N 111.8 . 1 226 . 38 GLN HE21 H 7.39 . 2 227 . 38 GLN HE22 H 6.47 . 2 228 . 39 GLY N N 117.7 . 1 229 . 39 GLY H H 8.35 . 1 230 . 39 GLY HA2 H 4.16 . 2 231 . 39 GLY HA3 H 3.20 . 2 232 . 40 LYS N N 116.3 . 1 233 . 40 LYS H H 7.22 . 1 234 . 40 LYS HA H 3.53 . 1 235 . 40 LYS HB2 H 1.59 . 2 236 . 40 LYS HB3 H 1.48 . 2 237 . 40 LYS HG2 H 1.11 . 2 238 . 40 LYS HG3 H 0.93 . 2 239 . 40 LYS HD2 H 1.49 . 2 240 . 40 LYS HE2 H 2.82 . 2 241 . 41 CYS N N 118.8 . 1 242 . 41 CYS H H 8.89 . 1 243 . 41 CYS HA H 4.67 . 1 244 . 41 CYS HB2 H 2.98 . 2 245 . 41 CYS HB3 H 2.76 . 2 246 . 42 LYS N N 129.6 . 1 247 . 42 LYS H H 7.90 . 1 248 . 42 LYS HA H 4.53 . 1 249 . 42 LYS HB2 H 1.66 . 2 250 . 43 PRO HA H 4.56 . 1 251 . 43 PRO HB2 H 2.47 . 2 252 . 43 PRO HB3 H 2.07 . 2 253 . 43 PRO HG2 H 2.17 . 2 254 . 43 PRO HD2 H 4.02 . 2 255 . 43 PRO HD3 H 3.89 . 2 256 . 44 VAL N N 111.1 . 1 257 . 44 VAL H H 6.97 . 1 258 . 44 VAL HA H 5.29 . 1 259 . 44 VAL HB H 2.12 . 1 260 . 44 VAL HG1 H 0.95 . 1 261 . 44 VAL HG2 H 0.95 . 1 262 . 45 ASN N N 119.9 . 1 263 . 45 ASN H H 8.74 . 1 264 . 45 ASN HA H 4.76 . 1 265 . 45 ASN HB2 H 2.35 . 2 266 . 45 ASN HB3 H 2.10 . 2 267 . 45 ASN ND2 N 115.1 . 1 268 . 45 ASN HD21 H 6.76 . 2 269 . 45 ASN HD22 H 4.19 . 2 270 . 46 THR N N 120.0 . 1 271 . 46 THR H H 6.94 . 1 272 . 46 THR HA H 5.13 . 1 273 . 46 THR HB H 2.25 . 1 274 . 46 THR HG2 H 0.73 . 1 275 . 47 PHE N N 124.5 . 1 276 . 47 PHE H H 9.32 . 1 277 . 47 PHE HA H 4.90 . 1 278 . 47 PHE HB2 H 2.70 . 2 279 . 47 PHE HB3 H 2.58 . 2 280 . 47 PHE HD1 H 6.81 . 1 281 . 47 PHE HD2 H 6.81 . 1 282 . 47 PHE HE1 H 6.87 . 1 283 . 47 PHE HE2 H 6.87 . 1 284 . 47 PHE HZ H 6.48 . 1 285 . 48 VAL N N 120.8 . 1 286 . 48 VAL H H 9.33 . 1 287 . 48 VAL HA H 4.19 . 1 288 . 48 VAL HB H 2.47 . 1 289 . 48 VAL HG1 H 0.99 . 2 290 . 48 VAL HG2 H 0.87 . 2 291 . 49 HIS N N 124.6 . 1 292 . 49 HIS H H 8.77 . 1 293 . 49 HIS HA H 5.30 . 1 294 . 49 HIS HB2 H 3.43 . 2 295 . 49 HIS HB3 H 2.79 . 2 296 . 49 HIS HD2 H 6.54 . 1 297 . 49 HIS HE1 H 7.94 . 1 298 . 50 GLU N N 116.4 . 1 299 . 50 GLU H H 6.56 . 1 300 . 50 GLU HA H 4.72 . 1 301 . 50 GLU HB2 H 1.45 . 1 302 . 50 GLU HB3 H 1.45 . 1 303 . 50 GLU HG2 H 2.55 . 1 304 . 50 GLU HG3 H 2.55 . 1 305 . 51 SER N N 116.8 . 1 306 . 51 SER H H 9.59 . 1 307 . 51 SER HA H 4.19 . 1 308 . 51 SER HB2 H 4.25 . 2 309 . 51 SER HB3 H 4.05 . 2 310 . 52 LEU N N 123.4 . 1 311 . 52 LEU H H 8.78 . 1 312 . 52 LEU HA H 4.05 . 1 313 . 52 LEU HB2 H 1.74 . 1 314 . 52 LEU HB3 H 1.74 . 1 315 . 52 LEU HG H 1.58 . 1 316 . 52 LEU HD1 H 1.06 . 2 317 . 52 LEU HD2 H 0.98 . 2 318 . 53 ALA N N 119.8 . 1 319 . 53 ALA H H 8.46 . 1 320 . 53 ALA HA H 3.93 . 1 321 . 53 ALA HB H 1.36 . 1 322 . 54 ASP N N 119.6 . 1 323 . 54 ASP H H 7.83 . 1 324 . 54 ASP HA H 4.35 . 1 325 . 54 ASP HB2 H 2.91 . 2 326 . 54 ASP HB3 H 2.44 . 2 327 . 55 VAL N N 121.1 . 1 328 . 55 VAL H H 7.88 . 1 329 . 55 VAL HA H 3.68 . 1 330 . 55 VAL HB H 2.14 . 1 331 . 55 VAL HG1 H 1.03 . 1 332 . 55 VAL HG2 H 1.03 . 1 333 . 56 LYS N N 119.3 . 1 334 . 56 LYS H H 9.00 . 1 335 . 56 LYS HA H 3.62 . 1 336 . 56 LYS HB2 H 1.82 . 2 337 . 56 LYS HB3 H 1.81 . 2 338 . 56 LYS HG2 H 1.66 . 2 339 . 56 LYS HG3 H 1.14 . 2 340 . 57 ALA N N 119.5 . 1 341 . 57 ALA H H 7.53 . 1 342 . 57 ALA HA H 3.97 . 1 343 . 57 ALA HB H 1.44 . 1 344 . 58 VAL N N 120.3 . 1 345 . 58 VAL H H 7.58 . 1 346 . 58 VAL HA H 3.18 . 1 347 . 58 VAL HB H 2.16 . 1 348 . 58 VAL HG1 H 1.09 . 2 349 . 58 VAL HG2 H 0.72 . 2 350 . 59 CYS N N 112.4 . 1 351 . 59 CYS H H 6.81 . 1 352 . 59 CYS HA H 3.49 . 1 353 . 59 CYS HB2 H 2.65 . 2 354 . 59 CYS HB3 H 2.52 . 2 355 . 60 SER N N 112.5 . 1 356 . 60 SER H H 7.48 . 1 357 . 60 SER HA H 4.55 . 1 358 . 60 SER HB2 H 3.91 . 2 359 . 60 SER HB3 H 3.87 . 2 360 . 61 GLN N N 123.7 . 1 361 . 61 GLN H H 7.70 . 1 362 . 61 GLN HA H 4.56 . 1 363 . 61 GLN HB2 H 2.33 . 2 364 . 61 GLN HG2 H 2.68 . 2 365 . 62 LYS N N 121.7 . 1 366 . 62 LYS H H 7.54 . 1 367 . 62 LYS HA H 4.22 . 1 368 . 62 LYS HB2 H 1.91 . 2 369 . 62 LYS HB3 H 1.80 . 2 370 . 62 LYS HG2 H 1.38 . 2 371 . 62 LYS HG3 H 1.19 . 2 372 . 63 LYS N N 129.2 . 1 373 . 63 LYS H H 8.41 . 1 374 . 63 LYS HA H 4.06 . 1 375 . 63 LYS HB2 H 1.60 . 2 376 . 63 LYS HB3 H 1.52 . 2 377 . 63 LYS HG2 H 1.19 . 2 378 . 63 LYS HG3 H 1.12 . 2 379 . 64 VAL N N 121.0 . 1 380 . 64 VAL H H 8.32 . 1 381 . 64 VAL HA H 4.48 . 1 382 . 64 VAL HB H 2.10 . 1 383 . 64 VAL HG1 H 0.67 . 2 384 . 64 VAL HG2 H 0.38 . 2 385 . 65 THR N N 116.2 . 1 386 . 65 THR H H 7.96 . 1 387 . 65 THR HA H 4.26 . 1 388 . 65 THR HB H 3.85 . 1 389 . 65 THR HG2 H 1.26 . 1 390 . 66 CYS N N 124.1 . 1 391 . 66 CYS H H 8.79 . 1 392 . 66 CYS HA H 4.43 . 1 393 . 66 CYS HB2 H 3.39 . 2 394 . 66 CYS HB3 H 2.87 . 2 395 . 67 LYS N N 127.4 . 1 396 . 67 LYS H H 10.96 . 1 397 . 67 LYS HA H 3.97 . 1 398 . 67 LYS HB2 H 1.89 . 2 399 . 67 LYS HB3 H 1.76 . 2 400 . 67 LYS HG2 H 1.49 . 2 401 . 68 ASP N N 116.3 . 1 402 . 68 ASP H H 8.02 . 1 403 . 68 ASP HA H 4.43 . 1 404 . 68 ASP HB2 H 2.96 . 2 405 . 68 ASP HB3 H 2.56 . 2 406 . 69 GLY N N 108.2 . 1 407 . 69 GLY H H 8.03 . 1 408 . 69 GLY HA2 H 4.22 . 2 409 . 69 GLY HA3 H 3.47 . 2 410 . 70 GLN N N 119.4 . 1 411 . 70 GLN H H 8.12 . 1 412 . 70 GLN HA H 4.32 . 1 413 . 70 GLN HB2 H 2.12 . 2 414 . 70 GLN HB3 H 1.89 . 2 415 . 70 GLN HG2 H 2.30 . 2 416 . 71 THR N N 111.9 . 1 417 . 71 THR H H 8.55 . 1 418 . 71 THR HA H 4.46 . 1 419 . 71 THR HB H 4.34 . 1 420 . 71 THR HG2 H 1.14 . 1 421 . 72 ASN N N 118.9 . 1 422 . 72 ASN H H 8.22 . 1 423 . 72 ASN HA H 4.82 . 1 424 . 72 ASN HB2 H 3.01 . 2 425 . 72 ASN HB3 H 2.80 . 2 426 . 72 ASN ND2 N 111.4 . 1 427 . 72 ASN HD21 H 7.40 . 2 428 . 72 ASN HD22 H 6.68 . 2 429 . 73 CYS N N 117.4 . 1 430 . 73 CYS H H 7.48 . 1 431 . 73 CYS HA H 5.38 . 1 432 . 73 CYS HB2 H 2.61 . 2 433 . 73 CYS HB3 H 2.56 . 2 434 . 74 TYR N N 119.2 . 1 435 . 74 TYR H H 8.98 . 1 436 . 74 TYR HA H 5.09 . 1 437 . 74 TYR HB2 H 2.91 . 2 438 . 74 TYR HB3 H 2.15 . 2 439 . 74 TYR HD1 H 6.69 . 1 440 . 74 TYR HD2 H 6.69 . 1 441 . 74 TYR HE1 H 6.54 . 1 442 . 74 TYR HE2 H 6.54 . 1 443 . 75 GLN N N 122.5 . 1 444 . 75 GLN H H 9.48 . 1 445 . 75 GLN HA H 5.38 . 1 446 . 75 GLN HB2 H 1.86 . 2 447 . 75 GLN HB3 H 1.66 . 2 448 . 75 GLN HG2 H 2.43 . 2 449 . 75 GLN NE2 N 108.6 . 1 450 . 75 GLN HE21 H 6.49 . 2 451 . 75 GLN HE22 H 6.41 . 2 452 . 76 SER N N 122.1 . 1 453 . 76 SER H H 9.29 . 1 454 . 76 SER HA H 4.68 . 1 455 . 76 SER HB2 H 4.80 . 2 456 . 77 LYS N N 126.6 . 1 457 . 77 LYS H H 8.94 . 1 458 . 77 LYS HA H 4.18 . 1 459 . 77 LYS HB2 H 1.84 . 1 460 . 77 LYS HB3 H 1.84 . 1 461 . 77 LYS HG2 H 1.47 . 2 462 . 77 LYS HD2 H 1.70 . 2 463 . 77 LYS HE2 H 2.93 . 2 464 . 78 SER N N 113.6 . 1 465 . 78 SER H H 8.59 . 1 466 . 78 SER HA H 4.84 . 1 467 . 78 SER HB2 H 3.90 . 2 468 . 78 SER HB3 H 3.72 . 2 469 . 78 SER HG H 5.55 . 1 470 . 79 THR N N 113.2 . 1 471 . 79 THR H H 8.13 . 1 472 . 79 THR HA H 3.22 . 1 473 . 79 THR HB H 3.66 . 1 474 . 79 THR HG2 H 0.69 . 1 475 . 80 MET N N 120.6 . 1 476 . 80 MET H H 8.51 . 1 477 . 80 MET HA H 4.62 . 1 478 . 80 MET HB2 H 1.83 . 2 479 . 81 ARG N N 122.1 . 1 480 . 81 ARG H H 9.51 . 1 481 . 81 ARG HA H 4.34 . 1 482 . 81 ARG HB2 H 1.84 . 2 483 . 81 ARG HG2 H 1.70 . 2 484 . 81 ARG HD2 H 3.27 . 2 485 . 81 ARG HD3 H 3.10 . 2 486 . 81 ARG NE N 85.3 . 1 487 . 81 ARG HE H 7.34 . 1 488 . 82 ILE N N 119.9 . 1 489 . 82 ILE H H 8.64 . 1 490 . 82 ILE HA H 5.26 . 1 491 . 82 ILE HB H 1.81 . 1 492 . 82 ILE HG2 H 0.77 . 1 493 . 82 ILE HG12 H 1.23 . 2 494 . 82 ILE HG13 H 0.96 . 2 495 . 82 ILE HD1 H 0.70 . 1 496 . 83 THR N N 118.5 . 1 497 . 83 THR H H 9.26 . 1 498 . 83 THR HA H 5.01 . 1 499 . 83 THR HB H 3.90 . 1 500 . 83 THR HG2 H 1.22 . 1 501 . 84 ASP N N 127.2 . 1 502 . 84 ASP H H 9.24 . 1 503 . 84 ASP HA H 5.01 . 1 504 . 84 ASP HB2 H 2.58 . 2 505 . 84 ASP HB3 H 2.46 . 2 506 . 85 CYS N N 121.5 . 1 507 . 85 CYS H H 8.81 . 1 508 . 85 CYS HA H 5.91 . 1 509 . 85 CYS HB2 H 2.82 . 2 510 . 85 CYS HB3 H 2.53 . 2 511 . 86 ARG N N 121.5 . 1 512 . 86 ARG H H 8.20 . 1 513 . 86 ARG HA H 5.39 . 1 514 . 86 ARG HB2 H 1.94 . 2 515 . 86 ARG HB3 H 1.84 . 2 516 . 86 ARG HG2 H 1.73 . 2 517 . 86 ARG HD2 H 3.25 . 2 518 . 86 ARG NE N 85.4 . 1 519 . 86 ARG HE H 7.79 . 1 520 . 87 GLU N N 128.0 . 1 521 . 87 GLU H H 8.76 . 1 522 . 87 GLU HA H 4.26 . 1 523 . 87 GLU HB2 H 2.02 . 2 524 . 88 THR N N 115.0 . 1 525 . 88 THR H H 8.12 . 1 526 . 88 THR HA H 4.49 . 1 527 . 88 THR HB H 4.50 . 1 528 . 88 THR HG2 H 1.06 . 1 529 . 89 GLY N N 107.1 . 1 530 . 89 GLY H H 8.77 . 1 531 . 89 GLY HA2 H 3.90 . 1 532 . 89 GLY HA3 H 3.90 . 1 533 . 90 SER N N 112.3 . 1 534 . 90 SER H H 7.60 . 1 535 . 90 SER HA H 4.47 . 1 536 . 90 SER HB2 H 3.78 . 2 537 . 90 SER HB3 H 3.73 . 2 538 . 91 SER N N 117.6 . 1 539 . 91 SER H H 6.99 . 1 540 . 91 SER HA H 3.91 . 1 541 . 91 SER HB2 H 4.07 . 2 542 . 91 SER HB3 H 3.82 . 2 543 . 92 LYS N N 129.1 . 1 544 . 92 LYS H H 7.53 . 1 545 . 92 LYS HA H 4.41 . 1 546 . 92 LYS HB2 H 1.69 . 2 547 . 92 LYS HG2 H 1.33 . 2 548 . 92 LYS HE2 H 3.00 . 2 549 . 93 TYR N N 131.2 . 1 550 . 93 TYR H H 9.29 . 1 551 . 93 TYR HA H 3.68 . 1 552 . 93 TYR HB2 H 3.38 . 2 553 . 93 TYR HB3 H 2.75 . 2 554 . 93 TYR HD1 H 6.90 . 1 555 . 93 TYR HD2 H 6.90 . 1 556 . 93 TYR HE1 H 6.96 . 1 557 . 93 TYR HE2 H 6.96 . 1 558 . 94 PRO HA H 3.01 . 1 559 . 94 PRO HB2 H 1.16 . 2 560 . 94 PRO HG2 H 1.38 . 2 561 . 94 PRO HD2 H 3.33 . 2 562 . 94 PRO HD3 H 3.24 . 2 563 . 95 ASN N N 130.3 . 1 564 . 95 ASN H H 8.82 . 1 565 . 95 ASN HA H 4.91 . 1 566 . 95 ASN HB2 H 2.68 . 2 567 . 95 ASN ND2 N 114.0 . 1 568 . 95 ASN HD21 H 7.68 . 2 569 . 95 ASN HD22 H 6.92 . 2 570 . 96 CYS N N 121.7 . 1 571 . 96 CYS H H 7.69 . 1 572 . 96 CYS HA H 4.76 . 1 573 . 96 CYS HB2 H 2.94 . 2 574 . 96 CYS HB3 H 2.80 . 2 575 . 97 ALA N N 128.7 . 1 576 . 97 ALA H H 8.63 . 1 577 . 97 ALA HA H 4.71 . 1 578 . 97 ALA HB H 1.14 . 1 579 . 98 TYR N N 117.7 . 1 580 . 98 TYR H H 9.37 . 1 581 . 98 TYR HA H 4.88 . 1 582 . 98 TYR HB2 H 2.48 . 2 583 . 98 TYR HB3 H 2.36 . 2 584 . 98 TYR HD1 H 6.96 . 1 585 . 98 TYR HD2 H 6.96 . 1 586 . 98 TYR HE1 H 6.43 . 1 587 . 98 TYR HE2 H 6.43 . 1 588 . 98 TYR HH H 9.13 . 1 589 . 99 LYS N N 124.9 . 1 590 . 99 LYS H H 9.43 . 1 591 . 99 LYS HA H 4.72 . 1 592 . 99 LYS HB2 H 1.89 . 2 593 . 99 LYS HB3 H 1.73 . 2 594 . 99 LYS HG2 H 1.44 . 2 595 . 99 LYS HG3 H 1.39 . 2 596 . 100 THR N N 126.0 . 1 597 . 100 THR H H 9.05 . 1 598 . 100 THR HA H 5.21 . 1 599 . 100 THR HB H 4.22 . 1 600 . 100 THR HG2 H 1.31 . 1 601 . 101 THR N N 123.8 . 1 602 . 101 THR H H 8.86 . 1 603 . 101 THR HA H 4.61 . 1 604 . 101 THR HB H 4.07 . 1 605 . 101 THR HG2 H 1.21 . 1 606 . 102 GLN N N 127.9 . 1 607 . 102 GLN H H 8.82 . 1 608 . 102 GLN HA H 5.16 . 1 609 . 102 GLN HB2 H 2.06 . 2 610 . 102 GLN HB3 H 1.93 . 2 611 . 102 GLN HG2 H 2.32 . 2 612 . 103 VAL N N 120.8 . 1 613 . 103 VAL H H 8.64 . 1 614 . 103 VAL HA H 4.59 . 1 615 . 103 VAL HB H 2.05 . 1 616 . 103 VAL HG1 H 0.89 . 2 617 . 103 VAL HG2 H 0.78 . 2 618 . 104 GLU N N 121.4 . 1 619 . 104 GLU H H 8.07 . 1 620 . 104 GLU HA H 5.39 . 1 621 . 104 GLU HB2 H 1.81 . 2 622 . 104 GLU HB3 H 1.64 . 2 623 . 104 GLU HG2 H 2.13 . 2 624 . 104 GLU HG3 H 2.00 . 2 625 . 105 LYS N N 121.6 . 1 626 . 105 LYS H H 8.34 . 1 627 . 105 LYS HA H 4.76 . 1 628 . 105 LYS HB2 H 2.25 . 2 629 . 105 LYS HB3 H 1.40 . 2 630 . 105 LYS HG2 H 1.56 . 2 631 . 106 HIS N N 118.7 . 1 632 . 106 HIS H H 9.20 . 1 633 . 106 HIS HA H 4.38 . 1 634 . 106 HIS HB2 H 3.17 . 2 635 . 106 HIS HB3 H 3.11 . 2 636 . 106 HIS HD2 H 7.34 . 1 637 . 106 HIS HE1 H 8.45 . 1 638 . 107 ILE N N 113.5 . 1 639 . 107 ILE H H 8.45 . 1 640 . 107 ILE HA H 4.99 . 1 641 . 107 ILE HB H 1.77 . 1 642 . 107 ILE HG2 H 1.00 . 1 643 . 107 ILE HG12 H 1.52 . 2 644 . 107 ILE HG13 H 1.43 . 2 645 . 107 ILE HD1 H 0.98 . 1 646 . 108 ILE N N 121.7 . 1 647 . 108 ILE H H 8.31 . 1 648 . 108 ILE HA H 5.26 . 1 649 . 108 ILE HB H 1.43 . 1 650 . 108 ILE HG2 H 0.63 . 1 651 . 108 ILE HG12 H 1.31 . 2 652 . 108 ILE HG13 H 0.96 . 2 653 . 108 ILE HD1 H 0.72 . 1 654 . 109 VAL N N 117.5 . 1 655 . 109 VAL H H 8.91 . 1 656 . 109 VAL HA H 4.88 . 1 657 . 109 VAL HB H 2.13 . 1 658 . 109 VAL HG1 H 0.77 . 2 659 . 109 VAL HG2 H 0.61 . 2 660 . 110 ALA N N 122.0 . 1 661 . 110 ALA H H 8.71 . 1 662 . 110 ALA HA H 5.26 . 1 663 . 110 ALA HB H 1.43 . 1 664 . 111 CYS N N 119.7 . 1 665 . 111 CYS H H 8.80 . 1 666 . 111 CYS HA H 5.65 . 1 667 . 111 CYS HB2 H 3.29 . 2 668 . 111 CYS HB3 H 2.72 . 2 669 . 112 GLY N N 110.5 . 1 670 . 112 GLY H H 9.11 . 1 671 . 112 GLY HA2 H 4.47 . 2 672 . 112 GLY HA3 H 3.89 . 2 673 . 113 GLY N N 106.9 . 1 674 . 113 GLY H H 8.21 . 1 675 . 113 GLY HA2 H 4.42 . 2 676 . 113 GLY HA3 H 3.65 . 2 677 . 114 LYS N N 117.9 . 1 678 . 114 LYS H H 7.77 . 1 679 . 114 LYS HA H 4.37 . 1 680 . 114 LYS HB2 H 1.63 . 2 681 . 114 LYS HE2 H 2.93 . 2 682 . 115 PRO HA H 4.59 . 1 683 . 115 PRO HB2 H 2.30 . 2 684 . 115 PRO HB3 H 1.85 . 2 685 . 115 PRO HG2 H 1.83 . 2 686 . 115 PRO HG3 H 1.72 . 2 687 . 115 PRO HD2 H 3.56 . 2 688 . 115 PRO HD3 H 3.41 . 2 689 . 116 SER N N 115.5 . 1 690 . 116 SER H H 8.20 . 1 691 . 116 SER HA H 3.92 . 1 692 . 116 SER HB2 H 3.57 . 2 693 . 116 SER HB3 H 3.54 . 2 694 . 117 VAL N N 119.9 . 1 695 . 117 VAL H H 8.51 . 1 696 . 117 VAL HA H 4.84 . 1 697 . 117 VAL HB H 2.06 . 1 698 . 117 VAL HG1 H 0.81 . 1 699 . 117 VAL HG2 H 0.81 . 1 700 . 118 PRO HA H 4.49 . 1 701 . 118 PRO HB2 H 0.94 . 2 702 . 118 PRO HB3 H 0.15 . 2 703 . 118 PRO HG2 H 1.51 . 2 704 . 118 PRO HD2 H 3.58 . 2 705 . 118 PRO HD3 H 3.32 . 2 706 . 119 VAL N N 111.3 . 1 707 . 119 VAL H H 8.93 . 1 708 . 119 VAL HA H 4.49 . 1 709 . 119 VAL HB H 2.27 . 1 710 . 119 VAL HG1 H 0.78 . 2 711 . 119 VAL HG2 H 0.56 . 2 712 . 120 HIS N N 120.6 . 1 713 . 120 HIS H H 7.62 . 1 714 . 120 HIS HA H 5.25 . 1 715 . 120 HIS HB2 H 3.49 . 2 716 . 120 HIS HB3 H 2.92 . 2 717 . 121 PHE HA H 4.26 . 1 718 . 121 PHE HB2 H 2.45 . 2 719 . 121 PHE HD1 H 6.61 . 1 720 . 121 PHE HD2 H 6.61 . 1 721 . 121 PHE HE1 H 6.96 . 1 722 . 121 PHE HE2 H 6.96 . 1 723 . 121 PHE HZ H 6.58 . 1 724 . 122 ASP N N 130.7 . 1 725 . 122 ASP H H 8.64 . 1 726 . 122 ASP HA H 4.64 . 1 727 . 122 ASP HB2 H 2.25 . 2 728 . 122 ASP HB3 H 2.08 . 2 729 . 123 ALA N N 116.3 . 1 730 . 123 ALA H H 7.42 . 1 731 . 123 ALA HA H 4.45 . 1 732 . 123 ALA HB H 1.31 . 1 733 . 124 SER N N 111.9 . 1 734 . 124 SER H H 8.09 . 1 735 . 124 SER HA H 5.30 . 1 736 . 124 SER HB2 H 3.82 . 2 737 . 124 SER HB3 H 3.76 . 2 738 . 125 VAL N N 123.8 . 1 739 . 125 VAL H H 8.68 . 1 740 . 125 VAL HA H 4.29 . 1 741 . 125 VAL HB H 1.98 . 1 742 . 125 VAL HG1 H 0.77 . 2 743 . 125 VAL HG2 H 0.73 . 2 stop_ save_