data_4982 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N NMR sequence-specific resonance assignments for bovine apo-S100A1(aa) in oxidized form ; _BMRB_accession_number 4982 _BMRB_flat_file_name bmr4982.str _Entry_type original _Submission_date 2001-03-29 _Accession_date 2001-04-03 _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 Zhukov Igor . . 2 Ejchart Andrzej . . 3 Bierzynski Andrzej . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 3 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 522 "13C chemical shifts" 404 "15N chemical shifts" 103 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-01 update BMRB 'update entry citation' 2003-05-23 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural and motional changes induced in apo-S100A1 protein by the disulfide formation between its Cys 85 residue and beta-mercaptoethanol ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18088104 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhukov Igor . . 2 Ejchart Andrzej . . 3 Bierzynski Andrzej . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 47 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 640 _Page_last 650 _Year 2008 _Details . loop_ _Keyword 'heteronuclear NMR' 'S100 proteins' S100A1 'sequence-specific assignments' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):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 ; Bartels C., Xia T., Billeter M., Guntert P., and Wuthrich K. (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR, 6, 1-10 ; _Citation_title . _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _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 ; Cornilescu G, Delaglio F, Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR. 1999 Mar;13(3):289-302. ; _Citation_title 'Protein backbone angle restraints from searching a database for chemical shift and sequence homology.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10212987 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cornilescu G. . . 2 Delaglio F. . . 3 Bax A. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 13 _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 289 _Page_last 302 _Year 1999 _Details ; Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local conformation, and homologous proteins show quite similar patterns of secondary chemical shifts. The inverse of this relation is used to search a database for triplets of adjacent residues with secondary chemical shifts and sequence similarity which provide the best match to the query triplet of interest. The database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached to the secondary chemical shifts of the five types of resonances relative to that of sequence similarity was optimized empirically. TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence. If the central residues in these 10 triplets exhibit similar phi and psi backbone angles, their averages can reliably be used as angular restraints for the protein whose structure is being studied. Tests carried out for proteins of known structure indicate that the root-mean-square difference (rmsd) between the output of TALOS and the X-ray derived backbone angles is about 15 degrees. Approximately 3% of the predictions made by TALOS are found to be in error. ; save_ save_ref_4 _Saveframe_category citation _Citation_full ; Hoffman R.E., and Davies D.B. (1988) Temperature dependence of NMR secondary references for D2O and (CD3)2SO solutions. Magn. Reson. in Chemistry, 26, 523-525 ; _Citation_title . _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _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_5 _Saveframe_category citation _Citation_full ; Wishart DS, Bigam CG, Yao J, Abildgaard F, Dyson HJ, Oldfield E, Markley JL, Sykes BD. 1H, 13C and 15N chemical shift referencing in biomolecular NMR. J Biomol NMR. 1995 Sep;6(2):135-40. ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart D.S. S. . 2 Bigam C.G. G. . 3 Yao J. . . 4 Abildgaard F. . . 5 Dyson H.J. J. . 6 Oldfield E. . . 7 Markley J.L. L. . 8 Sykes B.D. D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _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 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_S100A1 _Saveframe_category molecular_system _Mol_system_name 'Apo-S100A1(aa) dimer' _Abbreviation_common S100A1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'S100A1 subunit 1' $S100A1_monomer 'S100A1 subunit 2' $S100A1_monomer MERCAPTOETHANOL $BME stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'S100A1 subunit 1' 1 'S100A1 subunit 2' stop_ loop_ _Biological_function 'Ca-binding protein' stop_ _Database_query_date . _Details 'Reidue CYS are all disulfide bound with mercaptoethanol' save_ ######################## # Monomeric polymers # ######################## save_S100A1_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'bovine S100A1(aa)' _Name_variant 'bovine S100A1(aa) oxidized' _Abbreviation_common S100A1 _Molecular_mass 10594.9 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 94 _Mol_residue_sequence ; MGSELETAMETLINVFHAHS GKEGDKYKLSKKELKELLQT ELSGFLDAQKDADAVDKVMK ELDEDGDGEVDFQEYVVLVA ALTVACNNFFWENS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 MET 2 1 GLY 3 2 SER 4 3 GLU 5 4 LEU 6 5 GLU 7 6 THR 8 7 ALA 9 8 MET 10 9 GLU 11 10 THR 12 11 LEU 13 12 ILE 14 13 ASN 15 14 VAL 16 15 PHE 17 16 HIS 18 17 ALA 19 18 HIS 20 19 SER 21 20 GLY 22 21 LYS 23 22 GLU 24 23 GLY 25 24 ASP 26 25 LYS 27 26 TYR 28 27 LYS 29 28 LEU 30 29 SER 31 30 LYS 32 31 LYS 33 32 GLU 34 33 LEU 35 34 LYS 36 35 GLU 37 36 LEU 38 37 LEU 39 38 GLN 40 39 THR 41 40 GLU 42 41 LEU 43 42 SER 44 43 GLY 45 44 PHE 46 45 LEU 47 46 ASP 48 47 ALA 49 48 GLN 50 49 LYS 51 50 ASP 52 51 ALA 53 52 ASP 54 53 ALA 55 54 VAL 56 55 ASP 57 56 LYS 58 57 VAL 59 58 MET 60 59 LYS 61 60 GLU 62 61 LEU 63 62 ASP 64 63 GLU 65 64 ASP 66 65 GLY 67 66 ASP 68 67 GLY 69 68 GLU 70 69 VAL 71 70 ASP 72 71 PHE 73 72 GLN 74 73 GLU 75 74 TYR 76 75 VAL 77 76 VAL 78 77 LEU 79 78 VAL 80 79 ALA 81 80 ALA 82 81 LEU 83 82 THR 84 83 VAL 85 84 ALA 86 85 CYS 87 86 ASN 88 87 ASN 89 88 PHE 90 89 PHE 91 90 TRP 92 91 GLU 93 92 ASN 94 93 SER stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value SWISS-PROT P02639 'Protein S100-A1 (S100 calcium-binding protein A1) (S-100 protein alpha subunit) (S-100 protein alpha chain)' 100.00 94 98.94 100.00 2.72e-46 REF XP_001253745 'PREDICTED: S100 calcium binding protein A1-like isoform 2 [Bos taurus]' 100.00 94 98.94 100.00 2.72e-46 REF XP_001253725 'PREDICTED: S100 calcium binding protein A1-like isoform 1 [Bos taurus]' 100.00 94 98.94 100.00 2.72e-46 REF NP_001092512 'S100 calcium binding protein A1 [Bos taurus]' 100.00 94 98.94 100.00 2.72e-46 GenBank AAI48020 'S100A1 protein [Bos taurus]' 100.00 94 98.94 100.00 2.72e-46 GenBank AAI41992 'S100A1 protein [Bos taurus]' 100.00 94 98.94 100.00 2.72e-46 PDB 2JPT 'Structural Changes Induced In Apo-S100a1 Protein By The Disulphide Formation Between Its Cys85 Residue And B- Mercaptoethanol' 98.94 93 100.00 100.00 6.02e-46 stop_ save_ ############# # Ligands # ############# save_BME _Saveframe_category ligand _Mol_type non-polymer _Name_common "BME (BETA-MERCAPTOETHANOL)" _BMRB_code . _PDB_code BME _Molecular_mass 78.133 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jul 21 11:30:25 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C2 C2 C . 0 . ? O1 O1 O . 0 . ? S2 S2 S . 0 . ? H11 H11 H . 0 . ? H12 H12 H . 0 . ? H21 H21 H . 0 . ? H22 H22 H . 0 . ? HO1 HO1 H . 0 . ? HS2 HS2 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 C1 C2 ? ? SING C1 O1 ? ? SING C1 H11 ? ? SING C1 H12 ? ? SING C2 S2 ? ? SING C2 H21 ? ? SING C2 H22 ? ? SING O1 HO1 ? ? SING S2 HS2 ? ? 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 $S100A1_monomer Bovine 9913 Eukaryota Metazoa Bos taurus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name $S100A1_monomer 'recombinant technology' 'E. coli' Escherichia coli K12 HMS174(DE3) plasmid pAED4 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $S100A1_monomer 1.2 mM 1.0 1.5 '[U-98% 13C; U-98% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task 'processing heteronuclear NMR spectra' stop_ _Details . _Citation_label $ref_1 save_ save_XEASY _Saveframe_category software _Name XEASY _Version 3.11 loop_ _Task 'analysis 3D heteronuclear spectra' stop_ _Details . _Citation_label $ref_2 save_ save_TALOS _Saveframe_category software _Name TALOS _Version . loop_ _Task 'analysis 1H, 13C, and 15N chemical shifts' stop_ _Details . _Citation_label $ref_3 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 500 _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_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_(HCA)CO(CA)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name (HCA)CO(CA)NH _Sample_label $sample_1 save_ save_HNHA_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label $sample_1 save_ save_HA(CO)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name HA(CO)NH _Sample_label $sample_1 save_ save_HBHA(CO)NH_10 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label $sample_1 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 HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name (HCA)CO(CA)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name HA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.3 0.2 n/a temperature 308 1.0 K 'ionic strength' 0.09 0.005 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 _Reference_correction_type _Correction_value _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.00 external direct cylindrical external parallel . . temperature -0.010167 $ref_4 DSS C 13 'methyl protons' ppm 0.00 external indirect cylindrical external parallel 0.251449530 $ref_5 . . . DSS N 15 'methyl protons' ppm 0.00 external indirect cylindrical external parallel 0.101329118 $ref_5 . . . 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_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'S100A1 subunit 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 . 1 MET CA C 54.1 0.05 1 2 . 1 MET HA H 4.70 0.02 1 3 . 1 MET HB2 H 2.98 0.02 1 4 . 1 MET HB3 H 2.98 0.02 1 5 . 1 MET CG C 27.3 0.05 1 6 . 2 GLY N N 111.1 0.05 1 7 . 2 GLY H H 8.63 0.02 1 8 . 2 GLY CA C 45.2 0.05 1 9 . 2 GLY HA2 H 4.07 0.02 1 10 . 2 GLY HA3 H 4.07 0.02 1 11 . 2 GLY C C 173.9 0.05 1 12 . 3 SER N N 116.9 0.05 1 13 . 3 SER H H 8.68 0.02 1 14 . 3 SER CA C 57.9 0.05 1 15 . 3 SER HA H 4.73 0.02 1 16 . 3 SER CB C 64.9 0.05 1 17 . 3 SER HB2 H 4.46 0.02 2 18 . 3 SER HB3 H 4.15 0.02 2 19 . 3 SER C C 175.6 0.05 1 20 . 4 GLU N N 124.5 0.05 1 21 . 4 GLU H H 9.27 0.02 1 22 . 4 GLU CA C 60.7 0.05 1 23 . 4 GLU HA H 4.14 0.02 1 24 . 4 GLU CB C 29.9 0.05 1 25 . 4 GLU HB2 H 2.07 0.02 1 26 . 4 GLU HB3 H 2.07 0.02 1 27 . 4 GLU CG C 37.3 0.05 1 28 . 4 GLU HG2 H 2.38 0.02 1 29 . 4 GLU HG3 H 2.38 0.02 1 30 . 4 GLU C C 178.9 0.05 1 31 . 5 LEU N N 119.6 0.05 1 32 . 5 LEU H H 8.98 0.02 1 33 . 5 LEU CA C 58.4 0.05 1 34 . 5 LEU HA H 4.04 0.02 1 35 . 5 LEU CB C 42.3 0.05 1 36 . 5 LEU HB2 H 1.61 0.02 1 37 . 5 LEU HB3 H 1.61 0.02 1 38 . 5 LEU CG C 24.4 0.05 1 39 . 5 LEU HG H 1.58 0.02 1 40 . 5 LEU CD1 C 23.9 0.05 1 41 . 5 LEU HD1 H 0.83 0.02 1 42 . 5 LEU HD2 H 0.83 0.02 1 43 . 5 LEU C C 178.3 0.05 1 44 . 6 GLU N N 118.5 0.05 1 45 . 6 GLU H H 8.03 0.02 1 46 . 6 GLU CA C 60.2 0.05 1 47 . 6 GLU HA H 3.78 0.02 1 48 . 6 GLU CB C 30.3 0.05 1 49 . 6 GLU CG C 37.3 0.05 1 50 . 6 GLU HG2 H 2.27 0.02 1 51 . 6 GLU HG3 H 2.27 0.02 1 52 . 6 GLU C C 178.4 0.05 1 53 . 7 THR N N 114.5 0.05 1 54 . 7 THR H H 8.20 0.02 1 55 . 7 THR CA C 66.6 0.05 1 56 . 7 THR HA H 4.00 0.02 1 57 . 7 THR CB C 69.0 0.05 1 58 . 7 THR HB H 4.35 0.02 1 59 . 7 THR HG2 H 1.26 0.02 1 60 . 7 THR CG2 C 21.4 0.05 1 61 . 7 THR C C 177.0 0.05 1 62 . 8 ALA N N 126.5 0.05 1 63 . 8 ALA H H 8.24 0.02 1 64 . 8 ALA CA C 56.2 0.05 1 65 . 8 ALA HA H 4.16 0.02 1 66 . 8 ALA HB H 1.59 0.02 1 67 . 8 ALA CB C 18.1 0.05 1 68 . 8 ALA C C 179.3 0.05 1 69 . 9 MET N N 116.9 0.05 1 70 . 9 MET H H 8.14 0.02 1 71 . 9 MET CA C 60.3 0.05 1 72 . 9 MET HA H 3.76 0.02 1 73 . 9 MET CB C 35.2 0.05 1 74 . 9 MET HB2 H 2.28 0.02 1 75 . 9 MET HB3 H 2.28 0.02 1 76 . 9 MET CG C 30.5 0.05 1 77 . 9 MET HG2 H 2.55 0.02 1 78 . 9 MET HG3 H 2.55 0.02 1 79 . 9 MET C C 178.0 0.05 1 80 . 10 GLU N N 117.1 0.05 1 81 . 10 GLU H H 8.53 0.02 1 82 . 10 GLU CA C 60.2 0.05 1 83 . 10 GLU HA H 3.90 0.02 1 84 . 10 GLU CB C 29.7 0.05 1 85 . 10 GLU HB2 H 2.05 0.02 1 86 . 10 GLU HB3 H 2.05 0.02 1 87 . 10 GLU CG C 37.4 0.05 1 88 . 10 GLU HG2 H 2.54 0.02 1 89 . 10 GLU HG3 H 2.54 0.02 1 90 . 10 GLU C C 179.1 0.05 1 91 . 11 THR N N 117.5 0.05 1 92 . 11 THR H H 8.53 0.02 1 93 . 11 THR CA C 67.6 0.05 1 94 . 11 THR HA H 4.09 0.02 1 95 . 11 THR HB H 4.47 0.02 1 96 . 11 THR HG2 H 1.22 0.02 1 97 . 11 THR CG2 C 22.4 0.05 1 98 . 11 THR C C 175.7 0.05 1 99 . 12 LEU N N 119.5 0.05 1 100 . 12 LEU H H 8.02 0.02 1 101 . 12 LEU CA C 59.5 0.05 1 102 . 12 LEU HA H 3.95 0.02 1 103 . 12 LEU CB C 42.1 0.05 1 104 . 12 LEU HB2 H 1.42 0.02 1 105 . 12 LEU HB3 H 1.42 0.02 1 106 . 12 LEU CG C 24.3 0.05 1 107 . 12 LEU CD1 C 23.7 0.05 1 108 . 12 LEU HD1 H 0.75 0.02 1 109 . 12 LEU HD2 H 0.75 0.02 1 110 . 12 LEU C C 181.0 0.05 1 111 . 13 ILE N N 120.0 0.05 1 112 . 13 ILE H H 7.76 0.02 1 113 . 13 ILE CA C 66.0 0.05 1 114 . 13 ILE HA H 3.90 0.02 1 115 . 13 ILE CB C 39.4 0.05 1 116 . 13 ILE HB H 1.98 0.02 1 117 . 13 ILE HG2 H 0.81 0.02 1 118 . 13 ILE CG2 C 17.5 0.05 1 119 . 13 ILE CG1 C 30.6 0.05 1 120 . 13 ILE HD1 H 0.74 0.02 1 121 . 13 ILE CD1 C 14.8 0.05 1 122 . 13 ILE C C 177.6 0.05 1 123 . 14 ASN N N 121.2 0.05 1 124 . 14 ASN H H 9.11 0.02 1 125 . 14 ASN CA C 56.5 0.05 1 126 . 14 ASN HA H 4.50 0.02 1 127 . 14 ASN CB C 38.3 0.05 1 128 . 14 ASN HB2 H 2.99 0.02 1 129 . 14 ASN HB3 H 2.99 0.02 1 130 . 14 ASN C C 178.9 0.05 1 131 . 15 VAL N N 120.8 0.05 1 132 . 15 VAL H H 8.94 0.02 1 133 . 15 VAL CA C 67.0 0.05 1 134 . 15 VAL HA H 3.86 0.02 1 135 . 15 VAL CB C 31.9 0.05 1 136 . 15 VAL HB H 2.14 0.02 1 137 . 15 VAL CG1 C 23.2 0.05 1 138 . 15 VAL CG2 C 22.2 0.05 1 139 . 15 VAL HG1 H 1.07 0.02 1 140 . 15 VAL HG2 H 1.07 0.02 1 141 . 15 VAL C C 177.9 0.05 1 142 . 16 PHE N N 117.7 0.05 1 143 . 16 PHE H H 6.97 0.02 1 144 . 16 PHE CA C 62.7 0.05 1 145 . 16 PHE HA H 3.44 0.02 1 146 . 16 PHE CB C 39.3 0.05 1 147 . 16 PHE HB2 H 2.92 0.02 2 148 . 16 PHE HB3 H 2.30 0.02 2 149 . 16 PHE C C 177.8 0.05 1 150 . 17 HIS N N 115.2 0.05 1 151 . 17 HIS H H 8.12 0.02 1 152 . 17 HIS CA C 59.4 0.05 1 153 . 17 HIS HA H 4.23 0.02 1 154 . 17 HIS CB C 28.2 0.05 1 155 . 17 HIS HB2 H 2.85 0.02 1 156 . 17 HIS HB3 H 2.85 0.02 1 157 . 17 HIS C C 176.6 0.05 1 158 . 18 ALA N N 122.2 0.05 1 159 . 18 ALA H H 8.34 0.02 1 160 . 18 ALA CA C 54.4 0.05 1 161 . 18 ALA HA H 4.16 0.02 1 162 . 18 ALA HB H 1.38 0.02 1 163 . 18 ALA CB C 18.0 0.05 1 164 . 18 ALA C C 178.5 0.05 1 165 . 19 HIS N N 112.6 0.05 1 166 . 19 HIS H H 7.17 0.02 1 167 . 19 HIS CA C 57.4 0.05 1 168 . 19 HIS HA H 4.51 0.02 1 169 . 19 HIS CB C 30.7 0.05 1 170 . 19 HIS HB2 H 3.25 0.02 2 171 . 19 HIS HB3 H 2.56 0.02 2 172 . 19 HIS C C 174.4 0.05 1 173 . 20 SER N N 116.6 0.05 1 174 . 20 SER H H 7.95 0.02 1 175 . 20 SER CA C 59.2 0.05 1 176 . 20 SER HA H 4.11 0.02 1 177 . 20 SER CB C 63.8 0.05 1 178 . 20 SER HB2 H 3.39 0.02 2 179 . 20 SER HB3 H 2.64 0.02 2 180 . 20 SER C C 174.6 0.05 1 181 . 21 GLY N N 107.8 0.05 1 182 . 21 GLY H H 8.16 0.02 1 183 . 21 GLY CA C 45.1 0.05 1 184 . 21 GLY HA2 H 4.27 0.02 2 185 . 21 GLY HA3 H 3.88 0.02 2 186 . 21 GLY C C 173.7 0.05 1 187 . 22 LYS N N 121.2 0.05 1 188 . 22 LYS H H 8.05 0.02 1 189 . 22 LYS CA C 57.3 0.05 1 190 . 22 LYS HA H 4.24 0.02 1 191 . 22 LYS CB C 33.6 0.05 1 192 . 22 LYS HB2 H 1.51 0.02 1 193 . 22 LYS HB3 H 1.51 0.02 1 194 . 22 LYS CG C 24.9 0.05 1 195 . 22 LYS HG2 H 1.04 0.02 1 196 . 22 LYS HG3 H 1.04 0.02 1 197 . 22 LYS CD C 29.1 0.05 1 198 . 22 LYS HD2 H 1.76 0.02 1 199 . 22 LYS HD3 H 1.76 0.02 1 200 . 22 LYS CE C 42.3 0.05 1 201 . 22 LYS HE2 H 2.85 0.02 1 202 . 22 LYS HE3 H 2.85 0.02 1 203 . 22 LYS C C 176.3 0.05 1 204 . 23 GLU N N 122.6 0.05 1 205 . 23 GLU H H 8.29 0.02 1 206 . 23 GLU CA C 56.0 0.05 1 207 . 23 GLU HA H 4.45 0.02 1 208 . 23 GLU CB C 31.3 0.05 1 209 . 23 GLU HB2 H 1.39 0.02 1 210 . 23 GLU HB3 H 1.39 0.02 1 211 . 23 GLU CG C 35.9 0.05 1 212 . 23 GLU HG2 H 2.19 0.02 1 213 . 23 GLU HG3 H 2.19 0.02 1 214 . 23 GLU C C 176.1 0.05 1 215 . 24 GLY N N 112.1 0.05 1 216 . 24 GLY H H 8.49 0.02 1 217 . 24 GLY CA C 46.4 0.05 1 218 . 24 GLY HA2 H 3.98 0.02 2 219 . 24 GLY HA3 H 3.75 0.02 2 220 . 24 GLY C C 174.1 0.05 1 221 . 25 ASP N N 123.3 0.05 1 222 . 25 ASP H H 8.51 0.02 1 223 . 25 ASP CA C 54.5 0.05 1 224 . 25 ASP HA H 4.55 0.02 1 225 . 25 ASP CB C 41.5 0.05 1 226 . 25 ASP HB2 H 3.11 0.02 1 227 . 25 ASP HB3 H 3.11 0.02 1 228 . 25 ASP C C 176.2 0.05 1 229 . 26 LYS N N 120.4 0.05 1 230 . 26 LYS H H 7.93 0.02 1 231 . 26 LYS CA C 56.2 0.05 1 232 . 26 LYS HA H 4.56 0.02 1 233 . 26 LYS CB C 34.2 0.05 1 234 . 26 LYS HB2 H 1.74 0.02 1 235 . 26 LYS HB3 H 1.74 0.02 1 236 . 26 LYS HG2 H 1.34 0.02 1 237 . 26 LYS HG3 H 1.34 0.02 1 238 . 26 LYS HE2 H 3.01 0.02 1 239 . 26 LYS HE3 H 3.01 0.02 1 240 . 26 LYS C C 176.1 0.05 1 241 . 27 TYR N N 120.0 0.05 1 242 . 27 TYR H H 8.64 0.02 1 243 . 27 TYR CA C 58.5 0.05 1 244 . 27 TYR HA H 4.51 0.02 1 245 . 27 TYR CB C 38.9 0.05 1 246 . 27 TYR HB2 H 3.15 0.02 1 247 . 27 TYR HB3 H 3.15 0.02 1 248 . 27 TYR C C 175.7 0.05 1 249 . 28 LYS N N 119.0 0.05 1 250 . 28 LYS H H 8.20 0.02 1 251 . 28 LYS CA C 54.7 0.05 1 252 . 28 LYS HA H 5.29 0.02 1 253 . 28 LYS CB C 37.2 0.05 1 254 . 28 LYS HB2 H 1.48 0.02 1 255 . 28 LYS HB3 H 1.48 0.02 1 256 . 28 LYS CG C 24.5 0.05 1 257 . 28 LYS HG2 H 1.65 0.02 1 258 . 28 LYS HG3 H 1.65 0.02 1 259 . 28 LYS CD C 29.1 0.05 1 260 . 28 LYS CE C 42.2 0.05 1 261 . 28 LYS HE2 H 2.96 0.02 1 262 . 28 LYS HE3 H 2.96 0.02 1 263 . 28 LYS C C 174.4 0.05 1 264 . 29 LEU N N 121.9 0.05 1 265 . 29 LEU H H 8.77 0.02 1 266 . 29 LEU CA C 53.4 0.05 1 267 . 29 LEU HA H 4.70 0.02 1 268 . 29 LEU CB C 46.1 0.05 1 269 . 29 LEU HB2 H 1.00 0.02 1 270 . 29 LEU HB3 H 1.00 0.02 1 271 . 29 LEU CG C 26.1 0.05 1 272 . 29 LEU HG H 1.61 0.02 1 273 . 29 LEU CD1 C 25.8 0.05 1 274 . 29 LEU HD1 H 0.54 0.02 1 275 . 29 LEU HD2 H 0.54 0.02 1 276 . 29 LEU C C 175.7 0.05 1 277 . 30 SER N N 120.3 0.05 1 278 . 30 SER H H 8.87 0.02 1 279 . 30 SER CA C 58.2 0.05 1 280 . 30 SER HA H 4.93 0.02 1 281 . 30 SER CB C 64.7 0.05 1 282 . 30 SER HB2 H 4.46 0.02 2 283 . 30 SER HB3 H 4.06 0.02 2 284 . 30 SER C C 175.7 0.05 1 285 . 31 LYS N N 124.8 0.05 1 286 . 31 LYS H H 8.90 0.02 1 287 . 31 LYS CA C 61.8 0.05 1 288 . 31 LYS HA H 3.83 0.02 1 289 . 31 LYS CB C 32.1 0.05 1 290 . 31 LYS HB2 H 2.08 0.02 1 291 . 31 LYS HB3 H 2.08 0.02 1 292 . 31 LYS HG2 H 1.36 0.02 1 293 . 31 LYS HG3 H 1.36 0.02 1 294 . 31 LYS CD C 29.6 0.05 1 295 . 31 LYS HD2 H 1.93 0.02 1 296 . 31 LYS HD3 H 1.93 0.02 1 297 . 31 LYS CE C 42.6 0.05 1 298 . 31 LYS HE2 H 2.80 0.02 1 299 . 31 LYS HE3 H 2.80 0.02 1 300 . 31 LYS C C 178.6 0.05 1 301 . 32 LYS N N 119.6 0.05 1 302 . 32 LYS H H 8.73 0.02 1 303 . 32 LYS CA C 59.7 0.05 1 304 . 32 LYS HA H 4.14 0.02 1 305 . 32 LYS CB C 32.4 0.05 1 306 . 32 LYS HB2 H 1.90 0.02 2 307 . 32 LYS HB3 H 1.70 0.02 2 308 . 32 LYS CG C 24.5 0.05 1 309 . 32 LYS HG2 H 1.46 0.02 1 310 . 32 LYS HG3 H 1.46 0.02 1 311 . 32 LYS CD C 29.5 0.05 1 312 . 32 LYS CE C 42.1 0.05 1 313 . 32 LYS HE2 H 2.99 0.02 1 314 . 32 LYS HE3 H 2.99 0.02 1 315 . 32 LYS C C 179.0 0.05 1 316 . 33 GLU N N 120.4 0.05 1 317 . 33 GLU H H 7.72 0.02 1 318 . 33 GLU CA C 58.9 0.05 1 319 . 33 GLU HA H 4.09 0.02 1 320 . 33 GLU CB C 30.2 0.05 1 321 . 33 GLU CG C 37.2 0.05 1 322 . 33 GLU HG2 H 2.31 0.02 1 323 . 33 GLU HG3 H 2.31 0.02 1 324 . 33 GLU C C 179.6 0.05 1 325 . 34 LEU N N 121.8 0.05 1 326 . 34 LEU H H 8.62 0.02 1 327 . 34 LEU CA C 57.7 0.05 1 328 . 34 LEU HA H 4.07 0.02 1 329 . 34 LEU CB C 40.7 0.05 1 330 . 34 LEU HB2 H 2.16 0.02 2 331 . 34 LEU HB3 H 1.39 0.02 2 332 . 34 LEU CG C 27.5 0.05 1 333 . 34 LEU HG H 1.66 0.02 1 334 . 34 LEU CD1 C 23.5 0.05 1 335 . 34 LEU CD2 C 22.9 0.05 1 336 . 34 LEU HD1 H 1.09 0.02 1 337 . 34 LEU HD2 H 1.09 0.02 1 338 . 34 LEU C C 177.3 0.05 1 339 . 35 LYS N N 120.6 0.05 1 340 . 35 LYS H H 8.68 0.02 1 341 . 35 LYS CA C 60.8 0.05 1 342 . 35 LYS HA H 3.64 0.02 1 343 . 35 LYS CB C 32.2 0.05 1 344 . 35 LYS HB2 H 1.84 0.02 2 345 . 35 LYS HB3 H 1.65 0.02 2 346 . 35 LYS CG C 25.2 0.05 1 347 . 35 LYS HG2 H 1.33 0.02 1 348 . 35 LYS HG3 H 1.33 0.02 1 349 . 35 LYS CD C 29.5 0.05 1 350 . 35 LYS HD2 H 2.08 0.02 1 351 . 35 LYS HD3 H 2.08 0.02 1 352 . 35 LYS CE C 42.0 0.05 1 353 . 35 LYS HE2 H 2.89 0.02 1 354 . 35 LYS HE3 H 2.89 0.02 1 355 . 35 LYS C C 177.8 0.05 1 356 . 36 GLU N N 117.5 0.05 1 357 . 36 GLU H H 7.71 0.02 1 358 . 36 GLU CA C 59.6 0.05 1 359 . 36 GLU HA H 4.04 0.02 1 360 . 36 GLU CB C 29.7 0.05 1 361 . 36 GLU HB2 H 2.26 0.02 1 362 . 36 GLU HB3 H 2.26 0.02 1 363 . 36 GLU CG C 36.4 0.05 1 364 . 36 GLU HG2 H 2.44 0.02 1 365 . 36 GLU HG3 H 2.44 0.02 1 366 . 36 GLU C C 179.0 0.05 1 367 . 37 LEU N N 122.7 0.05 1 368 . 37 LEU H H 8.20 0.02 1 369 . 37 LEU CA C 58.3 0.05 1 370 . 37 LEU HA H 4.23 0.02 1 371 . 37 LEU CB C 42.1 0.05 1 372 . 37 LEU HB2 H 1.95 0.02 1 373 . 37 LEU HB3 H 1.95 0.02 1 374 . 37 LEU CG C 26.9 0.05 1 375 . 37 LEU HG H 1.37 0.02 1 376 . 37 LEU CD1 C 24.6 0.05 1 377 . 37 LEU HD1 H 0.49 0.02 1 378 . 37 LEU HD2 H 0.49 0.02 1 379 . 37 LEU C C 178.7 0.05 1 380 . 38 LEU N N 119.0 0.05 1 381 . 38 LEU H H 8.56 0.02 1 382 . 38 LEU CA C 58.7 0.05 1 383 . 38 LEU HA H 3.76 0.02 1 384 . 38 LEU CB C 41.5 0.05 1 385 . 38 LEU HB2 H 1.93 0.02 1 386 . 38 LEU HB3 H 1.93 0.02 1 387 . 38 LEU CG C 26.3 0.05 1 388 . 38 LEU HG H 1.13 0.02 1 389 . 38 LEU CD1 C 21.6 0.05 1 390 . 38 LEU CD2 C 21.2 0.05 1 391 . 38 LEU HD1 H 0.64 0.02 1 392 . 38 LEU HD2 H 0.64 0.02 1 393 . 38 LEU C C 178.5 0.05 1 394 . 39 GLN N N 115.5 0.05 1 395 . 39 GLN H H 8.36 0.02 1 396 . 39 GLN CA C 59.1 0.05 1 397 . 39 GLN HA H 3.81 0.02 1 398 . 39 GLN CB C 28.3 0.05 1 399 . 39 GLN HB2 H 2.23 0.02 1 400 . 39 GLN HB3 H 2.23 0.02 1 401 . 39 GLN CG C 34.9 0.05 1 402 . 39 GLN HG2 H 2.51 0.02 1 403 . 39 GLN HG3 H 2.51 0.02 1 404 . 39 GLN C C 177.8 0.05 1 405 . 40 THR N N 112.2 0.05 1 406 . 40 THR H H 7.92 0.02 1 407 . 40 THR CA C 65.5 0.05 1 408 . 40 THR HA H 4.30 0.02 1 409 . 40 THR CB C 69.4 0.05 1 410 . 40 THR HB H 4.24 0.02 1 411 . 40 THR HG2 H 1.35 0.02 1 412 . 40 THR CG2 C 21.4 0.05 1 413 . 40 THR C C 177.1 0.05 1 414 . 41 GLU N N 119.6 0.05 1 415 . 41 GLU H H 8.69 0.02 1 416 . 41 GLU CA C 58.7 0.05 1 417 . 41 GLU HA H 4.37 0.02 1 418 . 41 GLU CB C 31.2 0.05 1 419 . 41 GLU HB2 H 2.27 0.02 1 420 . 41 GLU HB3 H 2.27 0.02 1 421 . 41 GLU CG C 36.7 0.05 1 422 . 41 GLU HG2 H 2.54 0.02 1 423 . 41 GLU HG3 H 2.54 0.02 1 424 . 41 GLU C C 178.2 0.05 1 425 . 42 LEU N N 118.3 0.05 1 426 . 42 LEU H H 8.27 0.02 1 427 . 42 LEU CA C 53.1 0.05 1 428 . 42 LEU HA H 5.12 0.02 1 429 . 42 LEU CB C 42.1 0.05 1 430 . 42 LEU HB2 H 1.98 0.02 1 431 . 42 LEU HB3 H 1.98 0.02 1 432 . 42 LEU CG C 26.7 0.05 1 433 . 42 LEU HG H 1.62 0.02 1 434 . 42 LEU CD1 C 23.9 0.05 1 435 . 42 LEU CD2 C 23.4 0.05 1 436 . 42 LEU HD1 H 0.86 0.02 1 437 . 42 LEU HD2 H 0.86 0.02 1 438 . 42 LEU C C 177.0 0.05 1 439 . 43 SER N N 114.6 0.05 1 440 . 43 SER H H 7.13 0.02 1 441 . 43 SER CA C 62.7 0.05 1 442 . 43 SER HA H 3.99 0.02 1 443 . 43 SER CB C 65.4 0.05 1 444 . 43 SER HB2 H 4.16 0.02 1 445 . 43 SER HB3 H 4.16 0.02 1 446 . 43 SER C C 176.8 0.05 1 447 . 44 GLY N N 109.5 0.05 1 448 . 44 GLY H H 8.73 0.02 1 449 . 44 GLY CA C 47.3 0.05 1 450 . 44 GLY HA2 H 3.95 0.02 1 451 . 44 GLY HA3 H 3.95 0.02 1 452 . 44 GLY C C 176.5 0.05 1 453 . 45 PHE N N 124.4 0.05 1 454 . 45 PHE H H 8.23 0.02 1 455 . 45 PHE CA C 60.3 0.05 1 456 . 45 PHE HA H 4.40 0.02 1 457 . 45 PHE CB C 39.8 0.05 1 458 . 45 PHE HB2 H 3.48 0.02 2 459 . 45 PHE HB3 H 2.89 0.02 2 460 . 45 PHE C C 176.6 0.05 1 461 . 46 LEU N N 117.4 0.05 1 462 . 46 LEU H H 8.58 0.02 1 463 . 46 LEU CA C 57.7 0.05 1 464 . 46 LEU HA H 3.52 0.02 1 465 . 46 LEU CB C 40.8 0.05 1 466 . 46 LEU HB2 H 1.76 0.02 1 467 . 46 LEU HB3 H 1.76 0.02 1 468 . 46 LEU CG C 26.6 0.05 1 469 . 46 LEU HG H 1.38 0.02 1 470 . 46 LEU CD1 C 22.8 0.05 1 471 . 46 LEU CD2 C 22.5 0.05 1 472 . 46 LEU HD1 H 0.76 0.02 1 473 . 46 LEU HD2 H 0.76 0.02 1 474 . 46 LEU C C 179.1 0.05 1 475 . 47 ASP N N 117.2 0.05 1 476 . 47 ASP H H 7.92 0.02 1 477 . 47 ASP CA C 57.0 0.05 1 478 . 47 ASP HA H 4.40 0.02 1 479 . 47 ASP CB C 41.4 0.05 1 480 . 47 ASP HB2 H 2.78 0.02 2 481 . 47 ASP HB3 H 2.64 0.02 2 482 . 47 ASP C C 177.9 0.05 1 483 . 48 ALA N N 120.1 0.05 1 484 . 48 ALA H H 7.51 0.02 1 485 . 48 ALA CA C 54.3 0.05 1 486 . 48 ALA HA H 4.17 0.02 1 487 . 48 ALA HB H 1.42 0.02 1 488 . 48 ALA CB C 19.1 0.05 1 489 . 48 ALA C C 179.5 0.05 1 490 . 49 GLN N N 115.1 0.05 1 491 . 49 GLN H H 7.63 0.02 1 492 . 49 GLN CA C 54.3 0.05 1 493 . 49 GLN HA H 4.32 0.02 1 494 . 49 GLN CB C 27.9 0.05 1 495 . 49 GLN CG C 33.5 0.05 1 496 . 49 GLN HG2 H 1.41 0.02 1 497 . 49 GLN HG3 H 1.41 0.02 1 498 . 49 GLN C C 175.7 0.05 1 499 . 50 LYS N N 119.1 0.05 1 500 . 50 LYS H H 7.21 0.02 1 501 . 50 LYS CA C 58.7 0.05 1 502 . 50 LYS HA H 3.95 0.02 1 503 . 50 LYS CB C 32.0 0.05 1 504 . 50 LYS HB2 H 1.65 0.02 1 505 . 50 LYS HB3 H 1.65 0.02 1 506 . 50 LYS CG C 23.4 0.05 1 507 . 50 LYS HG2 H 1.35 0.02 1 508 . 50 LYS HG3 H 1.35 0.02 1 509 . 50 LYS CD C 29.3 0.05 1 510 . 50 LYS HD2 H 1.76 0.02 1 511 . 50 LYS HD3 H 1.76 0.02 1 512 . 50 LYS CE C 42.1 0.05 1 513 . 50 LYS HE2 H 2.99 0.02 1 514 . 50 LYS HE3 H 2.99 0.02 1 515 . 50 LYS C C 176.1 0.05 1 516 . 51 ASP N N 116.2 0.05 1 517 . 51 ASP H H 8.12 0.02 1 518 . 51 ASP CA C 53.9 0.05 1 519 . 51 ASP HA H 4.65 0.02 1 520 . 51 ASP CB C 40.9 0.05 1 521 . 51 ASP HB2 H 2.74 0.02 2 522 . 51 ASP HB3 H 2.53 0.02 2 523 . 51 ASP C C 176.2 0.05 1 524 . 52 ALA N N 125.0 0.05 1 525 . 52 ALA H H 7.85 0.02 1 526 . 52 ALA CA C 52.1 0.05 1 527 . 52 ALA HA H 4.34 0.02 1 528 . 52 ALA HB H 1.43 0.02 1 529 . 52 ALA CB C 18.5 0.05 1 530 . 52 ALA C C 178.4 0.05 1 531 . 53 ASP N N 124.6 0.05 1 532 . 53 ASP H H 8.66 0.02 1 533 . 53 ASP CA C 58.0 0.05 1 534 . 53 ASP HA H 4.31 0.02 1 535 . 53 ASP CB C 41.3 0.05 1 536 . 53 ASP HB2 H 2.69 0.02 1 537 . 53 ASP HB3 H 2.69 0.02 1 538 . 53 ASP C C 177.8 0.05 1 539 . 54 ALA N N 118.2 0.05 1 540 . 54 ALA H H 8.66 0.02 1 541 . 54 ALA CA C 55.4 0.05 1 542 . 54 ALA HA H 4.09 0.02 1 543 . 54 ALA HB H 1.45 0.02 1 544 . 54 ALA CB C 19.3 0.05 1 545 . 54 ALA C C 179.6 0.05 1 546 . 55 VAL N N 115.3 0.05 1 547 . 55 VAL H H 6.97 0.02 1 548 . 55 VAL CA C 65.6 0.05 1 549 . 55 VAL HA H 3.52 0.02 1 550 . 55 VAL CB C 32.0 0.05 1 551 . 55 VAL HB H 2.17 0.02 1 552 . 55 VAL CG1 C 22.7 0.05 1 553 . 55 VAL CG2 C 22.1 0.05 1 554 . 55 VAL HG1 H 0.78 0.02 1 555 . 55 VAL HG2 H 0.78 0.02 1 556 . 55 VAL C C 177.1 0.05 1 557 . 56 ASP N N 120.5 0.05 1 558 . 56 ASP H H 8.27 0.02 1 559 . 56 ASP CA C 57.7 0.05 1 560 . 56 ASP HA H 4.32 0.02 1 561 . 56 ASP CB C 42.1 0.05 1 562 . 56 ASP HB2 H 2.62 0.02 1 563 . 56 ASP HB3 H 2.62 0.02 1 564 . 56 ASP C C 178.0 0.05 1 565 . 57 LYS N N 115.7 0.05 1 566 . 57 LYS H H 8.07 0.02 1 567 . 57 LYS CA C 59.9 0.05 1 568 . 57 LYS HA H 3.90 0.02 1 569 . 57 LYS CB C 32.5 0.05 1 570 . 57 LYS HB2 H 1.89 0.02 2 571 . 57 LYS HB3 H 1.65 0.02 2 572 . 57 LYS CG C 25.2 0.05 1 573 . 57 LYS HG2 H 1.47 0.02 1 574 . 57 LYS HG3 H 1.47 0.02 1 575 . 57 LYS CD C 29.4 0.05 1 576 . 57 LYS CE C 42.3 0.05 1 577 . 57 LYS HE2 H 2.97 0.02 1 578 . 57 LYS HE3 H 2.97 0.02 1 579 . 57 LYS C C 179.2 0.05 1 580 . 58 VAL N N 118.2 0.05 1 581 . 58 VAL H H 7.13 0.02 1 582 . 58 VAL CA C 66.1 0.05 1 583 . 58 VAL HA H 3.73 0.02 1 584 . 58 VAL CB C 32.2 0.05 1 585 . 58 VAL HB H 2.17 0.02 1 586 . 58 VAL HG1 H 1.09 0.02 2 587 . 58 VAL HG2 H 0.90 0.02 2 588 . 58 VAL CG1 C 22.0 0.05 1 589 . 58 VAL CG2 C 21.4 0.05 1 590 . 58 VAL C C 177.5 0.05 1 591 . 59 MET N N 116.0 0.05 1 592 . 59 MET H H 8.03 0.02 1 593 . 59 MET CA C 57.1 0.05 1 594 . 59 MET HA H 4.28 0.02 1 595 . 59 MET CB C 30.8 0.05 1 596 . 59 MET HB2 H 2.62 0.02 1 597 . 59 MET HB3 H 2.62 0.02 1 598 . 59 MET CG C 32.7 0.05 1 599 . 59 MET HG2 H 2.80 0.02 1 600 . 59 MET HG3 H 2.80 0.02 1 601 . 59 MET C C 179.8 0.05 1 602 . 60 LYS N N 119.6 0.05 1 603 . 60 LYS H H 8.60 0.02 1 604 . 60 LYS CA C 59.4 0.05 1 605 . 60 LYS HA H 4.05 0.02 1 606 . 60 LYS CB C 32.3 0.05 1 607 . 60 LYS HB2 H 1.84 0.02 1 608 . 60 LYS HB3 H 1.84 0.02 1 609 . 60 LYS CG C 25.4 0.05 1 610 . 60 LYS HG2 H 1.60 0.02 1 611 . 60 LYS HG3 H 1.60 0.02 1 612 . 60 LYS CD C 29.0 0.05 1 613 . 60 LYS CE C 42.1 0.05 1 614 . 60 LYS HE2 H 2.97 0.02 1 615 . 60 LYS HE3 H 2.97 0.02 1 616 . 60 LYS C C 179.4 0.05 1 617 . 61 GLU N N 119.0 0.05 1 618 . 61 GLU H H 7.55 0.02 1 619 . 61 GLU CA C 59.3 0.05 1 620 . 61 GLU HA H 4.05 0.02 1 621 . 61 GLU CB C 29.4 0.05 1 622 . 61 GLU HB2 H 2.26 0.02 1 623 . 61 GLU HB3 H 2.26 0.02 1 624 . 61 GLU CG C 36.3 0.05 1 625 . 61 GLU HG2 H 2.43 0.02 1 626 . 61 GLU HG3 H 2.43 0.02 1 627 . 61 GLU C C 179.1 0.05 1 628 . 62 LEU N N 116.8 0.05 1 629 . 62 LEU H H 7.56 0.02 1 630 . 62 LEU CA C 56.8 0.05 1 631 . 62 LEU HA H 4.05 0.02 1 632 . 62 LEU CB C 41.2 0.05 1 633 . 62 LEU HB2 H 1.92 0.02 1 634 . 62 LEU HB3 H 1.92 0.02 1 635 . 62 LEU CG C 25.9 0.05 1 636 . 62 LEU HG H 1.48 0.02 1 637 . 62 LEU CD1 C 22.6 0.05 1 638 . 62 LEU CD2 C 22.2 0.05 1 639 . 62 LEU HD1 H 0.83 0.02 1 640 . 62 LEU HD2 H 0.83 0.02 1 641 . 62 LEU C C 177.4 0.05 1 642 . 63 ASP N N 116.7 0.05 1 643 . 63 ASP H H 7.59 0.02 1 644 . 63 ASP CA C 55.7 0.05 1 645 . 63 ASP HA H 4.51 0.02 1 646 . 63 ASP CB C 41.9 0.05 1 647 . 63 ASP HB2 H 2.69 0.02 1 648 . 63 ASP HB3 H 2.69 0.02 1 649 . 63 ASP C C 178.0 0.05 1 650 . 64 GLU N N 119.0 0.05 1 651 . 64 GLU H H 7.82 0.02 1 652 . 64 GLU CA C 57.6 0.05 1 653 . 64 GLU HA H 4.16 0.02 1 654 . 64 GLU CB C 30.3 0.05 1 655 . 64 GLU HB2 H 1.80 0.02 1 656 . 64 GLU HB3 H 1.80 0.02 1 657 . 64 GLU CG C 36.4 0.05 1 658 . 64 GLU HG2 H 2.35 0.02 1 659 . 64 GLU HG3 H 2.35 0.02 1 660 . 64 GLU C C 176.4 0.05 1 661 . 65 ASP N N 119.9 0.05 1 662 . 65 ASP H H 7.73 0.02 1 663 . 65 ASP CA C 53.3 0.05 1 664 . 65 ASP HA H 4.91 0.02 1 665 . 65 ASP CB C 41.0 0.05 1 666 . 65 ASP HB2 H 2.59 0.02 1 667 . 65 ASP HB3 H 2.59 0.02 1 668 . 65 ASP C C 177.1 0.05 1 669 . 66 GLY N N 107.5 0.05 1 670 . 66 GLY H H 8.00 0.02 1 671 . 66 GLY CA C 47.6 0.05 1 672 . 66 GLY HA2 H 3.91 0.02 1 673 . 66 GLY HA3 H 3.91 0.02 1 674 . 66 GLY C C 174.5 0.05 1 675 . 67 ASP N N 117.2 0.05 1 676 . 67 ASP H H 8.23 0.02 1 677 . 67 ASP CA C 54.4 0.05 1 678 . 67 ASP HA H 4.89 0.02 1 679 . 67 ASP CB C 41.1 0.05 1 680 . 67 ASP HB2 H 2.86 0.02 2 681 . 67 ASP HB3 H 2.63 0.02 2 682 . 67 ASP C C 177.3 0.05 1 683 . 68 GLY N N 109.1 0.05 1 684 . 68 GLY H H 8.21 0.02 1 685 . 68 GLY CA C 45.3 0.05 1 686 . 68 GLY HA2 H 4.20 0.02 2 687 . 68 GLY HA3 H 3.92 0.02 2 688 . 68 GLY C C 173.0 0.05 1 689 . 69 GLU N N 118.4 0.05 1 690 . 69 GLU H H 8.53 0.02 1 691 . 69 GLU CA C 55.5 0.05 1 692 . 69 GLU HA H 5.03 0.02 1 693 . 69 GLU CB C 34.1 0.05 1 694 . 69 GLU HB2 H 1.91 0.02 1 695 . 69 GLU HB3 H 1.91 0.02 1 696 . 69 GLU CG C 36.0 0.05 1 697 . 69 GLU HG2 H 2.17 0.02 1 698 . 69 GLU HG3 H 2.17 0.02 1 699 . 69 GLU C C 175.6 0.05 1 700 . 70 VAL N N 116.2 0.05 1 701 . 70 VAL H H 9.15 0.02 1 702 . 70 VAL CA C 59.8 0.05 1 703 . 70 VAL HA H 4.86 0.02 1 704 . 70 VAL CB C 34.6 0.05 1 705 . 70 VAL HB H 2.38 0.02 1 706 . 70 VAL CG1 C 22.5 0.05 1 707 . 70 VAL CG2 C 20.1 0.05 1 708 . 70 VAL HG1 H 0.93 0.02 1 709 . 70 VAL HG2 H 0.93 0.02 1 710 . 70 VAL C C 174.9 0.05 1 711 . 71 ASP N N 122.3 0.05 1 712 . 71 ASP H H 8.36 0.02 1 713 . 71 ASP CA C 51.8 0.05 1 714 . 71 ASP HA H 5.26 0.02 1 715 . 71 ASP CB C 42.1 0.05 1 716 . 71 ASP HB2 H 3.39 0.02 2 717 . 71 ASP HB3 H 2.73 0.02 2 718 . 71 ASP C C 175.9 0.05 1 719 . 72 PHE N N 119.2 0.05 1 720 . 72 PHE H H 8.96 0.02 1 721 . 72 PHE CA C 63.4 0.05 1 722 . 72 PHE HA H 2.81 0.02 1 723 . 72 PHE CB C 39.3 0.05 1 724 . 72 PHE HB2 H 2.66 0.02 2 725 . 72 PHE HB3 H 2.41 0.02 2 726 . 72 PHE C C 176.4 0.05 1 727 . 73 GLN N N 117.0 0.05 1 728 . 73 GLN H H 8.06 0.02 1 729 . 73 GLN CA C 59.4 0.05 1 730 . 73 GLN HA H 3.71 0.02 1 731 . 73 GLN CB C 28.4 0.05 1 732 . 73 GLN HB2 H 2.16 0.02 1 733 . 73 GLN HB3 H 2.16 0.02 1 734 . 73 GLN CG C 34.4 0.05 1 735 . 73 GLN HG2 H 2.37 0.02 1 736 . 73 GLN HG3 H 2.37 0.02 1 737 . 73 GLN C C 177.2 0.05 1 738 . 74 GLU N N 119.2 0.05 1 739 . 74 GLU H H 8.17 0.02 1 740 . 74 GLU CA C 59.4 0.05 1 741 . 74 GLU HA H 3.94 0.02 1 742 . 74 GLU CB C 30.6 0.05 1 743 . 74 GLU HB2 H 2.32 0.02 2 744 . 74 GLU HB3 H 1.96 0.02 2 745 . 74 GLU CG C 36.7 0.05 1 746 . 74 GLU HG2 H 2.54 0.02 1 747 . 74 GLU HG3 H 2.54 0.02 1 748 . 74 GLU C C 179.2 0.05 1 749 . 75 TYR N N 120.8 0.05 1 750 . 75 TYR H H 8.10 0.02 1 751 . 75 TYR CA C 60.7 0.05 1 752 . 75 TYR HA H 4.10 0.02 1 753 . 75 TYR CB C 37.6 0.05 1 754 . 75 TYR HB2 H 2.94 0.02 1 755 . 75 TYR HB3 H 2.94 0.02 1 756 . 75 TYR C C 175.8 0.05 1 757 . 76 VAL N N 120.3 0.05 1 758 . 76 VAL H H 8.31 0.02 1 759 . 76 VAL CA C 66.1 0.05 1 760 . 76 VAL HA H 2.95 0.02 1 761 . 76 VAL CB C 30.8 0.05 1 762 . 76 VAL HB H 1.52 0.02 1 763 . 76 VAL HG1 H 0.72 0.02 2 764 . 76 VAL HG2 H 0.58 0.02 2 765 . 76 VAL CG1 C 24.0 0.05 1 766 . 76 VAL CG2 C 21.4 0.05 1 767 . 76 VAL C C 177.3 0.05 1 768 . 77 VAL N N 121.2 0.05 1 769 . 77 VAL H H 7.65 0.02 1 770 . 77 VAL CA C 66.8 0.05 1 771 . 77 VAL HA H 3.52 0.02 1 772 . 77 VAL CB C 31.4 0.05 1 773 . 77 VAL HB H 2.15 0.02 1 774 . 77 VAL HG1 H 1.00 0.02 2 775 . 77 VAL HG2 H 0.91 0.02 2 776 . 77 VAL CG1 C 22.5 0.05 1 777 . 77 VAL CG2 C 21.0 0.05 1 778 . 77 VAL C C 178.8 0.05 1 779 . 78 LEU N N 122.8 0.05 1 780 . 78 LEU H H 7.42 0.02 1 781 . 78 LEU CA C 58.9 0.05 1 782 . 78 LEU HA H 4.13 0.02 1 783 . 78 LEU CB C 41.4 0.05 1 784 . 78 LEU HB2 H 1.92 0.02 1 785 . 78 LEU HB3 H 1.92 0.02 1 786 . 78 LEU CG C 26.7 0.05 1 787 . 78 LEU HG H 1.38 0.02 1 788 . 78 LEU CD1 C 24.0 0.05 1 789 . 78 LEU CD2 C 23.6 0.05 1 790 . 78 LEU HD1 H 0.87 0.02 1 791 . 78 LEU HD2 H 0.87 0.02 1 792 . 78 LEU C C 179.0 0.05 1 793 . 79 VAL N N 119.0 0.05 1 794 . 79 VAL H H 8.18 0.02 1 795 . 79 VAL CA C 67.4 0.05 1 796 . 79 VAL HA H 3.29 0.02 1 797 . 79 VAL CB C 31.2 0.05 1 798 . 79 VAL HB H 1.61 0.02 1 799 . 79 VAL HG1 H 0.67 0.02 2 800 . 79 VAL HG2 H 0.38 0.02 2 801 . 79 VAL CG1 C 22.0 0.05 1 802 . 79 VAL CG2 C 21.0 0.05 1 803 . 79 VAL C C 180.3 0.05 1 804 . 80 ALA N N 126.1 0.05 1 805 . 80 ALA H H 9.17 0.02 1 806 . 80 ALA CA C 56.2 0.05 1 807 . 80 ALA HA H 3.81 0.02 1 808 . 80 ALA HB H 1.33 0.02 1 809 . 80 ALA CB C 17.3 0.05 1 810 . 80 ALA C C 178.7 0.05 1 811 . 81 ALA N N 121.3 0.05 1 812 . 81 ALA H H 7.86 0.02 1 813 . 81 ALA CA C 55.7 0.05 1 814 . 81 ALA HA H 4.07 0.02 1 815 . 81 ALA HB H 1.58 0.02 1 816 . 81 ALA CB C 17.6 0.05 1 817 . 81 ALA C C 182.1 0.05 1 818 . 82 LEU N N 118.4 0.05 1 819 . 82 LEU H H 8.06 0.02 1 820 . 82 LEU CA C 57.5 0.05 1 821 . 82 LEU HA H 4.09 0.02 1 822 . 82 LEU CB C 42.1 0.05 1 823 . 82 LEU HB2 H 1.34 0.02 1 824 . 82 LEU HB3 H 1.34 0.02 1 825 . 82 LEU CG C 26.4 0.05 1 826 . 82 LEU HG H 2.00 0.02 1 827 . 82 LEU CD1 C 23.6 0.05 1 828 . 82 LEU CD2 C 23.1 0.05 1 829 . 82 LEU HD1 H 0.87 0.02 1 830 . 82 LEU HD2 H 0.87 0.02 1 831 . 82 LEU C C 177.9 0.05 1 832 . 83 THR N N 119.6 0.05 1 833 . 83 THR H H 8.56 0.02 1 834 . 83 THR CA C 68.3 0.05 1 835 . 83 THR HA H 3.76 0.02 1 836 . 83 THR CB C 69.9 0.05 1 837 . 83 THR HB H 4.53 0.02 1 838 . 83 THR HG2 H 1.42 0.02 1 839 . 83 THR CG2 C 22.2 0.05 1 840 . 83 THR C C 176.9 0.05 1 841 . 84 VAL N N 123.8 0.05 1 842 . 84 VAL H H 8.42 0.02 1 843 . 84 VAL CA C 67.5 0.05 1 844 . 84 VAL HA H 3.73 0.02 1 845 . 84 VAL CB C 31.4 0.05 1 846 . 84 VAL HB H 2.35 0.02 1 847 . 84 VAL CG1 C 24.0 0.05 1 848 . 84 VAL CG2 C 21.3 0.05 1 849 . 84 VAL HG1 H 1.16 0.02 1 850 . 84 VAL HG2 H 1.16 0.02 1 851 . 84 VAL C C 177.7 0.05 1 852 . 85 ALA N N 121.5 0.05 1 853 . 85 ALA H H 7.63 0.02 1 854 . 85 ALA CA C 55.6 0.05 1 855 . 85 ALA HA H 4.09 0.02 1 856 . 85 ALA HB H 1.61 0.02 1 857 . 85 ALA CB C 17.4 0.05 1 858 . 85 ALA C C 180.0 0.05 1 859 . 86 CYS N N 119.1 0.05 1 860 . 86 CYS H H 8.56 0.02 1 861 . 86 CYS CA C 58.9 0.05 1 862 . 86 CYS HA H 4.07 0.02 1 863 . 86 CYS CB C 40.9 0.05 1 864 . 86 CYS HB2 H 3.16 0.02 2 865 . 86 CYS HB3 H 2.83 0.02 2 866 . 86 CYS C C 175.7 0.05 1 867 . 87 ASN N N 119.1 0.05 1 868 . 87 ASN H H 8.68 0.02 1 869 . 87 ASN CA C 57.7 0.05 1 870 . 87 ASN HA H 4.24 0.02 1 871 . 87 ASN CB C 40.4 0.05 1 872 . 87 ASN HB2 H 2.54 0.02 2 873 . 87 ASN HB3 H 1.75 0.02 2 874 . 87 ASN C C 176.9 0.05 1 875 . 88 ASN N N 117.3 0.05 1 876 . 88 ASN H H 8.50 0.02 1 877 . 88 ASN CA C 55.9 0.05 1 878 . 88 ASN HA H 4.42 0.02 1 879 . 88 ASN CB C 37.8 0.05 1 880 . 88 ASN HB2 H 2.92 0.02 1 881 . 88 ASN HB3 H 2.92 0.02 1 882 . 88 ASN C C 176.8 0.05 1 883 . 89 PHE N N 118.9 0.05 1 884 . 89 PHE H H 7.96 0.02 1 885 . 89 PHE CA C 60.0 0.05 1 886 . 89 PHE HA H 4.44 0.02 1 887 . 89 PHE CB C 39.8 0.05 1 888 . 89 PHE HB2 H 3.09 0.02 1 889 . 89 PHE HB3 H 3.09 0.02 1 890 . 89 PHE C C 177.0 0.05 1 891 . 90 PHE N N 115.2 0.05 1 892 . 90 PHE H H 7.99 0.02 1 893 . 90 PHE CA C 59.9 0.05 1 894 . 90 PHE HA H 4.29 0.02 1 895 . 90 PHE CB C 40.5 0.05 1 896 . 90 PHE HB2 H 2.89 0.02 2 897 . 90 PHE HB3 H 2.69 0.02 2 898 . 90 PHE C C 177.2 0.05 1 899 . 91 TRP N N 117.9 0.05 1 900 . 91 TRP H H 8.34 0.02 1 901 . 91 TRP CA C 58.5 0.05 1 902 . 91 TRP HA H 4.56 0.02 1 903 . 91 TRP CB C 30.1 0.05 1 904 . 91 TRP HB2 H 2.73 0.02 1 905 . 91 TRP HB3 H 2.73 0.02 1 906 . 91 TRP C C 176.6 0.05 1 907 . 92 GLU N N 120.2 0.05 1 908 . 92 GLU H H 7.93 0.02 1 909 . 92 GLU CA C 57.1 0.05 1 910 . 92 GLU HA H 4.52 0.02 1 911 . 92 GLU CB C 30.3 0.05 1 912 . 92 GLU HB2 H 2.26 0.02 1 913 . 92 GLU HB3 H 2.26 0.02 1 914 . 92 GLU CG C 36.4 0.05 1 915 . 92 GLU HG2 H 2.29 0.02 1 916 . 92 GLU HG3 H 2.29 0.02 1 917 . 92 GLU C C 176.2 0.05 1 918 . 93 ASN N N 119.0 0.05 1 919 . 93 ASN H H 8.24 0.02 1 920 . 93 ASN CA C 53.4 0.05 1 921 . 93 ASN HA H 4.79 0.02 1 922 . 93 ASN CB C 39.4 0.05 1 923 . 93 ASN HB2 H 2.83 0.02 2 924 . 93 ASN HB3 H 2.68 0.02 2 925 . 93 ASN C C 174.4 0.05 1 926 . 94 SER N N 121.2 0.05 1 927 . 94 SER H H 7.81 0.02 1 928 . 94 SER C C 178.7 0.05 1 stop_ save_ save_shift_set_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'S100A1 subunit 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 . 3 SER N N 117.6 0.05 1 2 . 3 SER H H 8.80 0.02 1 3 . 3 SER CA C 57.9 0.05 1 4 . 3 SER HA H 4.73 0.02 1 5 . 3 SER CB C 64.9 0.05 1 6 . 3 SER HB2 H 4.46 0.02 2 7 . 3 SER HB3 H 4.15 0.02 2 8 . 3 SER C C 175.6 0.05 1 9 . 4 GLU N N 125.0 0.05 1 10 . 4 GLU H H 9.20 0.02 1 11 . 4 GLU CA C 60.7 0.05 1 12 . 4 GLU HA H 4.14 0.02 1 13 . 4 GLU CB C 29.9 0.05 1 14 . 4 GLU HB2 H 2.07 0.02 1 15 . 4 GLU HB3 H 2.07 0.02 1 16 . 4 GLU CG C 37.3 0.05 1 17 . 4 GLU HG2 H 2.38 0.02 1 18 . 4 GLU HG3 H 2.38 0.02 1 19 . 4 GLU C C 178.9 0.05 1 20 . 5 LEU N N 119.6 0.05 1 21 . 5 LEU H H 8.95 0.02 1 22 . 5 LEU CA C 58.4 0.05 1 23 . 5 LEU HA H 4.04 0.02 1 24 . 5 LEU CB C 42.3 0.05 1 25 . 5 LEU HB2 H 1.61 0.02 1 26 . 5 LEU HB3 H 1.61 0.02 1 27 . 5 LEU CG C 24.4 0.05 1 28 . 5 LEU HG H 1.58 0.02 1 29 . 5 LEU CD1 C 23.9 0.05 1 30 . 5 LEU HD1 H 0.83 0.02 1 31 . 5 LEU HD2 H 0.83 0.02 1 32 . 5 LEU C C 178.3 0.05 1 33 . 6 GLU N N 118.5 0.05 1 34 . 6 GLU H H 8.08 0.02 1 35 . 6 GLU CA C 60.2 0.05 1 36 . 6 GLU HA H 3.78 0.02 1 37 . 6 GLU CB C 30.3 0.05 1 38 . 6 GLU CG C 37.3 0.05 1 39 . 6 GLU HG2 H 2.27 0.02 1 40 . 6 GLU HG3 H 2.27 0.02 1 41 . 6 GLU C C 178.4 0.05 1 42 . 7 THR N N 114.2 0.05 1 43 . 7 THR H H 8.15 0.02 1 44 . 7 THR CA C 66.6 0.05 1 45 . 7 THR HA H 4.00 0.02 1 46 . 7 THR CB C 69.0 0.05 1 47 . 7 THR HB H 4.35 0.02 1 48 . 7 THR HG2 H 1.26 0.02 1 49 . 7 THR CG2 C 21.4 0.05 1 50 . 7 THR C C 177.0 0.05 1 51 . 41 GLU N N 119.7 0.05 1 52 . 41 GLU H H 8.65 0.02 1 53 . 41 GLU CA C 58.7 0.05 1 54 . 41 GLU HA H 4.37 0.02 1 55 . 41 GLU CB C 31.2 0.05 1 56 . 41 GLU HB2 H 2.27 0.02 1 57 . 41 GLU HB3 H 2.27 0.02 1 58 . 41 GLU CG C 36.7 0.05 1 59 . 41 GLU HG2 H 2.54 0.02 1 60 . 41 GLU HG3 H 2.54 0.02 1 61 . 41 GLU C C 178.2 0.05 1 62 . 42 LEU N N 118.1 0.05 1 63 . 42 LEU H H 8.25 0.02 1 64 . 42 LEU CA C 53.1 0.05 1 65 . 42 LEU HA H 5.12 0.02 1 66 . 42 LEU CB C 42.1 0.05 1 67 . 42 LEU HB2 H 1.98 0.02 1 68 . 42 LEU HB3 H 1.98 0.02 1 69 . 42 LEU CG C 26.7 0.05 1 70 . 42 LEU HG H 1.62 0.02 1 71 . 42 LEU CD1 C 23.9 0.05 1 72 . 42 LEU CD2 C 23.4 0.05 1 73 . 42 LEU HD1 H 0.86 0.02 1 74 . 42 LEU HD2 H 0.86 0.02 1 75 . 42 LEU C C 177.0 0.05 1 76 . 44 GLY N N 109.5 0.05 1 77 . 44 GLY H H 8.69 0.02 1 78 . 44 GLY CA C 47.3 0.05 1 79 . 44 GLY HA2 H 3.95 0.02 1 80 . 44 GLY HA3 H 3.95 0.02 1 81 . 44 GLY C C 176.5 0.05 1 stop_ save_ save_shift_set_3 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'S100A1 subunit 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 . 4 GLU N N 124.9 0.05 1 2 . 4 GLU H H 9.18 0.02 1 3 . 4 GLU CA C 60.7 0.05 1 4 . 4 GLU HA H 4.14 0.02 1 5 . 4 GLU CB C 29.9 0.05 1 6 . 4 GLU HB2 H 2.07 0.02 1 7 . 4 GLU HB3 H 2.07 0.02 1 8 . 4 GLU CG C 37.3 0.05 1 9 . 4 GLU HG2 H 2.38 0.02 1 10 . 4 GLU HG3 H 2.38 0.02 1 11 . 4 GLU C C 178.9 0.05 1 12 . 7 THR N N 114.0 0.05 1 13 . 7 THR H H 8.12 0.02 1 14 . 7 THR CA C 66.6 0.05 1 15 . 7 THR HA H 4.00 0.02 1 16 . 7 THR CB C 69.0 0.05 1 17 . 7 THR HB H 4.35 0.02 1 18 . 7 THR HG2 H 1.26 0.02 1 19 . 7 THR CG2 C 21.4 0.05 1 20 . 7 THR C C 177.0 0.05 1 stop_ save_