data_5377 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignments of 1H, 13C and 15N resonances of human Ca2+-S100B in complex with the TRTK-12 peptide ; _BMRB_accession_number 5377 _BMRB_flat_file_name bmr5377.str _Entry_type original _Submission_date 2002-05-15 _Accession_date 2002-05-15 _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 McClintock Kimberly A. . 2 Shaw Gary S. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 584 "13C chemical shifts" 400 "15N chemical shifts" 95 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-17 update BMRB 'Updating non-standard residue' stop_ loop_ _Related_BMRB_accession_number _Relationship 5206 'human S100B in the calcium-bound form' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Assignments of 1H, 13C and 15N resonances of human Ca2+-S100B in complex with the TRTK-12 peptide ; _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 McClintock Kimberly A. . 2 Shaw Gary S. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 23 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 255 _Page_last 256 _Year 2002 _Details . loop_ _Keyword S100B TRTK-12 'calcium-binding protein' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_reference_1 _Saveframe_category citation _Citation_full ; Smith SP, Shaw GS. A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form. Structure. 1998 Feb 15;6(2):211-22. ; _Citation_title 'A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9519411 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Smith 'S. P.' P. . 2 Shaw 'G. S.' S. . stop_ _Journal_abbreviation Structure _Journal_name_full 'Structure (London, England : 1993)' _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 211 _Page_last 222 _Year 1998 _Details ; BACKGROUND: S100B is a homodimeric member of the EF-hand calcium-binding protein superfamily. The protein has been implicated in cellular processes such as cell differentiation and growth, plays a role in cytoskeletal structure and function, and may have a role in neuropathological diseases, such as Alzheimers. The effects of S100B are mediated via its interaction with target proteins. While several studies have suggested that this interaction is propagated through a calcium-induced conformational change, leading to the exposure of a hydrophobic region of S100B, the molecular details behind this structural alteration remain unclear. RESULTS: The solution structure of calcium-saturated human S100B (Ca(2+)-S100B) has been determined by heteronuclear NMR spectroscopy. Ca(2+)-S100B forms a well defined globular structure comprising four EF-hand calcium-binding sites and an extensive hydrophobic dimer interface. A comparison of Ca(2+)-S100B with apo S100B and Ca(2+)-calbindin D9k indicates that while calcium-binding to S100B results in little change in the site I EF-hand, it induces a backbone reorientation of the N terminus of the site II EF-hand. This reorientation leads to a dramatic change in the position of helix III relative to the other helices. CONCLUSIONS: The calcium-induced reorientation of calcium-binding site II results in the increased exposure of several hydrophobic residues in helix IV and the linker region. While following the general mechanism of calcium modulatory proteins, whereby a hydrophobic target site is exposed, the 'calcium switch' observed in S100B appears to be unique from that of other EF-hand proteins and may provide insights into target specificity among calcium modulatory proteins. ; save_ save_reference_2 _Saveframe_category citation _Citation_full ; Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. 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_reference_3 _Saveframe_category citation _Citation_full ; Garrett, D.S., Powers, R., Gronenborn, A.M., Clore, G.M. (1991) J. Mag. Res. 95:214-220" ; _Citation_title . _Citation_status . _Citation_type . _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_ ################################## # Molecular system description # ################################## save_system_S100B-TRTK-12_complex _Saveframe_category molecular_system _Mol_system_name 'Ca(2+)S100B-TRTK-12 peptide complex' _Abbreviation_common 'S100B-TRTK-12 complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'S100B subunit 1' $S100B 'S100B subunit 2' $S100B 'TRTK-12 molecule 1' $TRTK-12 'TRTK-12 molecule 2' $TRTK-12 'CALCIUM (II) ION 1' $CA 'CALCIUM (II) ION 2' $CA 'CALCIUM (II) ION 3' $CA 'CALCIUM (II) ION 4' $CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'S100B subunit 1' 1 'S100B subunit 2' 2 'TRTK-12 molecule 1' 2 'TRTK-12 molecule 2' stop_ _Database_query_date . _Details 'Entry 1UWO is the solution structure of human calcium-bound S100B.' save_ ######################## # Monomeric polymers # ######################## save_S100B _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common S100B _Abbreviation_common S100B _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 91 _Mol_residue_sequence ; SELEKAMVALIDVFHQYSGR EGDKHKLKKSELKELINNEL SHFLEEIKEQEVVDKVMETL DNDGDGECDFQEFMAFVAMV TTACHEFFEHE ; loop_ _Residue_seq_code _Residue_label 1 SER 2 GLU 3 LEU 4 GLU 5 LYS 6 ALA 7 MET 8 VAL 9 ALA 10 LEU 11 ILE 12 ASP 13 VAL 14 PHE 15 HIS 16 GLN 17 TYR 18 SER 19 GLY 20 ARG 21 GLU 22 GLY 23 ASP 24 LYS 25 HIS 26 LYS 27 LEU 28 LYS 29 LYS 30 SER 31 GLU 32 LEU 33 LYS 34 GLU 35 LEU 36 ILE 37 ASN 38 ASN 39 GLU 40 LEU 41 SER 42 HIS 43 PHE 44 LEU 45 GLU 46 GLU 47 ILE 48 LYS 49 GLU 50 GLN 51 GLU 52 VAL 53 VAL 54 ASP 55 LYS 56 VAL 57 MET 58 GLU 59 THR 60 LEU 61 ASP 62 ASN 63 ASP 64 GLY 65 ASP 66 GLY 67 GLU 68 CYS 69 ASP 70 PHE 71 GLN 72 GLU 73 PHE 74 MET 75 ALA 76 PHE 77 VAL 78 ALA 79 MET 80 VAL 81 THR 82 THR 83 ALA 84 CYS 85 HIS 86 GLU 87 PHE 88 PHE 89 GLU 90 HIS 91 GLU stop_ _Sequence_homology_query_date 2008-03-24 _Sequence_homology_query_revised_last_date 2008-01-23 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 P04631 'S100B_RAT Protein S100-B (S100calcium-binding protein B) (S-100 protein subunit beta)(S-100 protein beta chain)' 98.91 92 98 99 2e-45 SWISS-PROT P50114 'S100B_MOUSE Protein S100-B (S100calcium-binding protein B) (S-100 protein subunit beta)(S-100 protein beta chain)' 98.91 92 99 99 9e-46 SWISS-PROT Q6YNR6 'S100B_RABIT Protein S100-B (S100calcium-binding protein B) (S-100 protein subunit beta)(S-100 protein beta chain)' 98.91 92 100 100 2e-46 SWISS-PROT P04271 'S100B_HUMAN Protein S100-B (S100calcium-binding protein B) (S-100 protein subunit beta)(S-100 protein beta chain)' 98.91 92 100 100 2e-46 REF XP_001487942.1 'PREDICTED: similar to ProteinS100-B (S100 calcium-binding protein B) (S-100 proteinbeta subunit) (S-100 protein beta cha' 97.85 93 100 100 2e-46 REF XP_531586.1 'PREDICTED: S100 calcium-bindingprotein, beta isoform 3 [Pan troglodytes]' 98.91 92 100 100 2e-46 REF XP_001160520.1 'PREDICTED: S100 calcium-bindingprotein, beta isoform 1 [Pan troglodytes]' 98.91 92 100 100 2e-46 REF NP_006263.1 'S100 calcium-binding protein, beta[Homo sapiens]' 98.91 92 100 100 2e-46 REF NP_001076199.1 'S100 calcium-binding protein,beta [Oryctolagus cuniculus]' 98.91 92 100 100 2e-46 PRF 2003367B 'S-100 protein:SUBUNIT=beta' 98.91 92 100 100 2e-46 GenBank AAX43954.1 'S100 calcium binding protein beta[synthetic construct]' 97.85 93 100 100 2e-46 GenBank AAX43953.1 'S100 calcium binding protein beta[synthetic construct]' 97.85 93 100 100 2e-46 GenBank AAP36596.1 'Homo sapiens S100 calcium bindingprotein, beta (neural) [synthetic construct]' 97.85 93 100 100 2e-46 GenBank AAH01766.1 'S100 calcium binding protein B [Homosapiens]' 98.91 92 100 100 2e-46 GenBank AAA60367.1 'S100 protein beta subunit' 98.91 92 100 100 2e-46 EMBL CAA25567.1 'unnamed protein product [Rattusnorvegicus]' 98.91 92 98 99 2e-45 EMBL CAG46920.1 'S100B [Homo sapiens]' 98.91 92 100 100 2e-46 DBJ BAE88979.1 'unnamed protein product [Macacafascicularis]' 98.91 92 99 100 7e-46 DBJ BAE36647.1 'unnamed protein product [Musmusculus]' 98.91 92 99 99 9e-46 DBJ BAE22413.1 'unnamed protein product [Musmusculus]' 98.91 92 99 99 9e-46 DBJ BAE22214.1 'unnamed protein product [Musmusculus]' 98.91 92 99 99 9e-46 PDB 1XYD 'A Chain A, Nmr Solution Structure Of RatZinc-Calcium-S100b, 20 Structures' 98.91 92 98 99 2e-45 PDB 1SYM 'A Chain A, 3-D Solution Structure Of ReducedApo-S100b From Rat, Nmr, 20 Structures' 98.91 92 98 99 2e-45 PDB 1QLK 'A Chain A, Solution Structure OfCa(2+)-Loaded Rat S100b (Betabeta) Nmr, 20 Structures' 98.91 92 98 99 2e-45 PDB 1MWN 'A Chain A, Solution Nmr Structure Of S100bBound To The High-Affinity Target Peptide Trtk-12' 98.91 92 98 99 2e-45 PDB 1DT7 'A Chain A, Solution Structure Of TheC-Terminal Negative Regulatory Domain Of P53 In AComplex With Ca2+-Bound S100b(Bb)' 98.91 92 98 99 2e-45 PDB 1B4C 'A Chain A, Solution Structure Of RatApo-S100b Using Dipolar Couplings' 98.91 92 98 99 2e-45 PDB 2H61 'A Chain A, X-Ray Structure Of HumanCa2+-Loaded S100b' 98.91 92 100 100 2e-46 PDB 1UWO 'A Chain A, Calcium Form Of Human S100b,Nmr, 20 Structures' 100.00 91 100 100 2e-46 PDB 1MQ1 'A Chain A, Ca2+-S100b-Trtk-12 Complex' 100.00 91 100 100 2e-46 BMRB 5895 S100B 98.91 92 98 99 2e-45 BMRB 5544 S100B 98.91 92 98 99 2e-45 BMRB 4105 S100B 98.91 92 98 99 2e-45 BMRB 5206 S100B 98.91 92 100 100 2e-46 BMRB 4702 'S100B beta' 100.00 91 98 99 2e-45 stop_ save_ save_TRTK-12 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TRTK-12 _Abbreviation_common TRTK-12 _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 14 _Mol_residue_sequence XTRTKIDWNKILSX loop_ _Residue_seq_code _Residue_label 1 ACE 2 THR 3 ARG 4 THR 5 LYS 6 ILE 7 ASP 8 TRP 9 ASN 10 LYS 11 ILE 12 LEU 13 SER 14 NH2 stop_ _Sequence_homology_query_date 2005-11-24 _Sequence_homology_query_revised_last_date 2002-08-25 save_ ###################### # Polymer residues # ###################### save_chem_comp_ACE _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'ACETYL GROUP' _BMRB_code . _PDB_code ACE _Standard_residue_derivative . _Molecular_mass 44.053 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jul 14 16:15:33 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . 0 . ? O O O . 0 . ? CH3 CH3 C . 0 . ? H H H . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 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 DOUB C O ? ? SING C CH3 ? ? SING C H ? ? SING CH3 H1 ? ? SING CH3 H2 ? ? SING CH3 H3 ? ? stop_ save_ save_chem_comp_NH2 _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'AMINO GROUP' _BMRB_code . _PDB_code NH2 _Standard_residue_derivative . _Molecular_mass 16.023 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jul 14 16:09:34 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? HN1 HN1 H . 0 . ? HN2 HN2 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N HN1 ? ? SING N HN2 ? ? stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type non-polymer _Name_common "CA (CALCIUM ION)" _BMRB_code . _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jul 13 17:18:35 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $S100B Human 9606 Eukaryota Metazoa Homo sapiens 'The TRTK-12 peptide has no natural source.' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $S100B 'recombinant technology' 'E. coli' . . N99 . $TRTK-12 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $S100B 1.0 mM '[U-13C; U-15N]' $TRTK-12 1.2 mM . $CA 3 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $S100B 0.350 mM '[U-2H; U-15N]' $TRTK-12 0.8 mM . $CA 1.0 mM . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $S100B 1.0 mM '[U-15N; U-13C]' $TRTK-12 1.2 mM '[U-13C]-acetyl; [U-13C]-Ile' $CA 3 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task 'data processing' stop_ _Details . _Citation_label $reference_2 save_ save_Pipp _Saveframe_category software _Name Pipp _Version . loop_ _Task 'peak assignment' stop_ _Details . _Citation_label $reference_3 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_C(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _Sample_label . save_ save_HC(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name HC(CO)NH _Sample_label . save_ save_1H-15N_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1H-13N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13N HSQC' _Sample_label . save_ save_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_1H-15N_TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_1H-13C_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C NOESY' _Sample_label . save_ save_HCCH-TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_HNHA_11 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_HNCO_12 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_1H-1H_NOESY_13 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label . save_ save_1H-1H_TOCSY_14 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_experimental_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.05 0.05 n/a temperature 308 0.10 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 DSS H 1 'methyl protons' ppm 0.00 external direct cylindrical external . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 external indirect cylindrical external . 0.101329118 DSS C 13 'methyl protons' ppm 0.00 external indirect cylindrical external . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shifts_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 $sample_3 stop_ _Sample_conditions_label $experimental_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'S100B 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 SER H H 9.99 0.01 1 2 . 1 SER HA H 4.74 0.01 1 3 . 1 SER HB2 H 4.22 0.01 1 4 . 1 SER HB3 H 4.22 0.01 1 5 . 1 SER C C 174.68 0.20 1 6 . 1 SER CA C 57.11 0.20 1 7 . 1 SER CB C 65.68 0.20 1 8 . 1 SER N N 121.76 0.20 1 9 . 2 GLU H H 9.27 0.01 1 10 . 2 GLU HA H 4.12 0.01 1 11 . 2 GLU HB2 H 2.22 0.01 2 12 . 2 GLU HB3 H 2.26 0.01 2 13 . 2 GLU HG2 H 2.51 0.01 1 14 . 2 GLU HG3 H 2.51 0.01 1 15 . 2 GLU C C 179.66 0.20 1 16 . 2 GLU CA C 59.88 0.20 1 17 . 2 GLU CB C 29.31 0.20 1 18 . 2 GLU CG C 36.30 0.20 1 19 . 2 GLU N N 120.18 0.20 1 20 . 3 LEU H H 8.75 0.01 1 21 . 3 LEU HA H 4.22 0.01 1 22 . 3 LEU HB2 H 1.80 0.01 2 23 . 3 LEU HB3 H 1.93 0.01 2 24 . 3 LEU HG H 1.44 0.01 1 25 . 3 LEU HD1 H 0.69 0.01 2 26 . 3 LEU HD2 H 1.11 0.01 2 27 . 3 LEU C C 177.75 0.20 1 28 . 3 LEU CA C 58.10 0.20 1 29 . 3 LEU CB C 42.61 0.20 1 30 . 3 LEU CG C 27.75 0.20 1 31 . 3 LEU CD1 C 26.77 0.20 2 32 . 3 LEU CD2 C 24.92 0.20 2 33 . 3 LEU N N 121.84 0.20 1 34 . 4 GLU H H 8.24 0.01 1 35 . 4 GLU HA H 3.91 0.01 1 36 . 4 GLU HB2 H 2.37 0.01 1 37 . 4 GLU HB3 H 2.37 0.01 1 38 . 4 GLU HG2 H 2.53 0.01 1 39 . 4 GLU HG3 H 2.53 0.01 1 40 . 4 GLU C C 178.90 0.20 1 41 . 4 GLU CA C 59.34 0.20 1 42 . 4 GLU CB C 29.56 0.20 1 43 . 4 GLU CG C 38.18 0.20 1 44 . 4 GLU N N 120.03 0.20 1 45 . 5 LYS H H 8.73 0.01 1 46 . 5 LYS HA H 3.97 0.01 1 47 . 5 LYS HB2 H 1.93 0.01 1 48 . 5 LYS HB3 H 1.93 0.01 1 49 . 5 LYS HG2 H 1.42 0.01 1 50 . 5 LYS HG3 H 1.42 0.01 1 51 . 5 LYS HD2 H 1.72 0.01 2 52 . 5 LYS HD3 H 1.79 0.01 2 53 . 5 LYS HE2 H 2.91 0.01 1 54 . 5 LYS HE3 H 2.91 0.01 1 55 . 5 LYS C C 179.78 0.20 1 56 . 5 LYS CA C 60.01 0.20 1 57 . 5 LYS CB C 32.90 0.20 1 58 . 5 LYS CG C 26.69 0.20 1 59 . 5 LYS CD C 29.82 0.20 1 60 . 5 LYS CE C 42.01 0.20 1 61 . 5 LYS N N 117.67 0.20 1 62 . 6 ALA H H 8.08 0.01 1 63 . 6 ALA HA H 4.29 0.01 1 64 . 6 ALA HB H 1.79 0.01 1 65 . 6 ALA CA C 55.21 0.20 1 66 . 6 ALA CB C 18.20 0.20 1 67 . 6 ALA N N 124.14 0.20 1 68 . 7 MET H H 7.95 0.01 1 69 . 7 MET HA H 3.81 0.01 1 70 . 7 MET HB2 H 1.69 0.01 2 71 . 7 MET HB3 H 1.71 0.01 2 72 . 7 MET CA C 62.96 0.20 1 73 . 7 MET CB C 39.20 0.20 1 74 . 7 MET N N 116.75 0.20 1 75 . 8 VAL H H 8.08 0.01 1 76 . 8 VAL HA H 3.64 0.01 1 77 . 8 VAL HB H 2.27 0.01 1 78 . 8 VAL HG1 H 1.21 0.01 2 79 . 8 VAL HG2 H 1.05 0.01 2 80 . 8 VAL C C 177.77 0.20 1 81 . 8 VAL CA C 66.86 0.20 1 82 . 8 VAL CB C 31.83 0.20 1 83 . 8 VAL CG1 C 23.33 0.20 2 84 . 8 VAL CG2 C 21.73 0.20 2 85 . 8 VAL N N 117.22 0.20 1 86 . 9 ALA H H 8.22 0.01 1 87 . 9 ALA HA H 4.37 0.01 1 88 . 9 ALA HB H 1.67 0.01 1 89 . 9 ALA CA C 55.58 0.20 1 90 . 9 ALA CB C 18.38 0.20 1 91 . 9 ALA N N 123.37 0.20 1 92 . 10 LEU H H 8.07 0.01 1 93 . 10 LEU HA H 4.18 0.01 1 94 . 10 LEU HB2 H 1.63 0.01 2 95 . 10 LEU HB3 H 2.64 0.01 2 96 . 10 LEU HG H 2.44 0.01 1 97 . 10 LEU HD1 H 0.92 0.01 1 98 . 10 LEU HD2 H 0.92 0.01 1 99 . 10 LEU C C 178.62 0.20 1 100 . 10 LEU CA C 58.96 0.20 1 101 . 10 LEU CB C 42.06 0.20 1 102 . 10 LEU CG C 26.18 0.20 1 103 . 10 LEU CD1 C 23.99 0.20 2 104 . 10 LEU CD2 C 26.03 0.20 2 105 . 10 LEU N N 117.54 0.20 1 106 . 11 ILE H H 7.47 0.01 1 107 . 11 ILE HA H 3.70 0.01 1 108 . 11 ILE HB H 2.00 0.01 1 109 . 11 ILE HG2 H 0.83 0.01 1 110 . 11 ILE HD1 H 0.72 0.01 1 111 . 11 ILE C C 178.13 0.20 1 112 . 11 ILE CA C 65.72 0.20 1 113 . 11 ILE CB C 38.61 0.20 1 114 . 11 ILE CG2 C 18.02 0.20 1 115 . 11 ILE CD1 C 13.12 0.20 1 116 . 11 ILE N N 118.71 0.20 1 117 . 12 ASP H H 8.85 0.01 1 118 . 12 ASP HA H 4.59 0.01 1 119 . 12 ASP HB2 H 2.82 0.01 2 120 . 12 ASP HB3 H 2.95 0.01 2 121 . 12 ASP C C 179.97 0.20 1 122 . 12 ASP CA C 57.84 0.20 1 123 . 12 ASP CB C 40.90 0.20 1 124 . 12 ASP N N 120.39 0.20 1 125 . 13 VAL H H 9.01 0.01 1 126 . 13 VAL HA H 4.06 0.01 1 127 . 13 VAL HB H 2.42 0.01 1 128 . 13 VAL HG1 H 1.36 0.01 2 129 . 13 VAL HG2 H 1.37 0.01 2 130 . 13 VAL C C 178.19 0.20 1 131 . 13 VAL CA C 66.15 0.20 1 132 . 13 VAL CB C 31.14 0.20 1 133 . 13 VAL CG1 C 23.28 0.20 2 134 . 13 VAL CG2 C 22.11 0.20 2 135 . 13 VAL N N 120.64 0.20 1 136 . 14 PHE H H 7.75 0.01 1 137 . 14 PHE HA H 3.56 0.01 1 138 . 14 PHE HB2 H 2.83 0.01 2 139 . 14 PHE HB3 H 3.22 0.01 2 140 . 14 PHE HD1 H 6.08 0.01 1 141 . 14 PHE HD2 H 6.08 0.01 1 142 . 14 PHE HE1 H 6.98 0.01 1 143 . 14 PHE HE2 H 6.98 0.01 1 144 . 14 PHE HZ H 7.39 0.01 1 145 . 14 PHE C C 177.27 0.20 1 146 . 14 PHE CA C 62.88 0.20 1 147 . 14 PHE CB C 38.72 0.20 1 148 . 14 PHE CD1 C 131.47 0.20 1 149 . 14 PHE CD2 C 131.47 0.20 1 150 . 14 PHE CE1 C 129.78 0.20 1 151 . 14 PHE CE2 C 129.78 0.20 1 152 . 14 PHE CZ C 131.25 0.20 1 153 . 14 PHE N N 120.01 0.20 1 154 . 15 HIS H H 8.24 0.01 1 155 . 15 HIS HA H 4.87 0.01 1 156 . 15 HIS HB2 H 3.20 0.01 2 157 . 15 HIS HB3 H 3.76 0.01 2 158 . 15 HIS HD2 H 7.39 0.01 1 159 . 15 HIS C C 177.98 0.20 1 160 . 15 HIS CA C 58.94 0.20 1 161 . 15 HIS CB C 29.06 0.20 1 162 . 15 HIS CD2 C 123.34 0.20 1 163 . 15 HIS N N 117.45 0.20 1 164 . 16 GLN H H 8.39 0.01 1 165 . 16 GLN HA H 4.02 0.01 1 166 . 16 GLN HB2 H 2.17 0.01 2 167 . 16 GLN HB3 H 2.40 0.01 2 168 . 16 GLN HG2 H 2.20 0.01 2 169 . 16 GLN HG3 H 2.76 0.01 2 170 . 16 GLN HE21 H 6.86 0.01 2 171 . 16 GLN HE22 H 7.21 0.01 2 172 . 16 GLN C C 177.65 0.20 1 173 . 16 GLN CA C 58.38 0.20 1 174 . 16 GLN CB C 28.36 0.20 1 175 . 16 GLN CG C 33.76 0.20 1 176 . 16 GLN CD C 179.72 0.20 1 177 . 16 GLN N N 122.23 0.20 1 178 . 16 GLN NE2 N 111.20 0.20 1 179 . 17 TYR H H 7.29 0.01 1 180 . 17 TYR HA H 4.14 0.01 1 181 . 17 TYR HB2 H 2.51 0.01 2 182 . 17 TYR HB3 H 2.70 0.01 2 183 . 17 TYR HD1 H 7.37 0.01 1 184 . 17 TYR HD2 H 7.37 0.01 1 185 . 17 TYR HE1 H 6.71 0.01 1 186 . 17 TYR HE2 H 6.71 0.01 1 187 . 17 TYR C C 176.30 0.20 1 188 . 17 TYR CA C 60.77 0.20 1 189 . 17 TYR CB C 40.66 0.20 1 190 . 17 TYR CD1 C 133.12 0.20 1 191 . 17 TYR CD2 C 133.12 0.20 1 192 . 17 TYR CE1 C 117.13 0.20 1 193 . 17 TYR CE2 C 117.13 0.20 1 194 . 17 TYR N N 115.89 0.20 1 195 . 18 SER H H 9.03 0.01 1 196 . 18 SER HA H 3.64 0.01 1 197 . 18 SER HB2 H 2.21 0.01 2 198 . 18 SER HB3 H 3.14 0.01 2 199 . 18 SER C C 177.42 0.20 1 200 . 18 SER CA C 61.65 0.20 1 201 . 18 SER CB C 61.08 0.20 1 202 . 18 SER N N 115.90 0.20 1 203 . 19 GLY H H 7.71 0.01 1 204 . 19 GLY HA2 H 3.96 0.01 2 205 . 19 GLY HA3 H 4.14 0.01 2 206 . 19 GLY C C 173.78 0.20 1 207 . 19 GLY CA C 45.24 0.20 1 208 . 19 GLY N N 110.42 0.20 1 209 . 20 ARG H H 7.20 0.01 1 210 . 20 ARG HA H 3.99 0.01 1 211 . 20 ARG HB2 H 2.06 0.01 2 212 . 20 ARG HB3 H 2.23 0.01 2 213 . 20 ARG HG2 H 1.68 0.01 2 214 . 20 ARG HG3 H 1.90 0.01 2 215 . 20 ARG HD2 H 3.22 0.01 1 216 . 20 ARG HD3 H 3.22 0.01 1 217 . 20 ARG C C 177.38 0.20 1 218 . 20 ARG CA C 59.74 0.20 1 219 . 20 ARG CB C 30.75 0.20 1 220 . 20 ARG CG C 30.10 0.20 1 221 . 20 ARG CD C 43.68 0.20 1 222 . 20 ARG N N 121.73 0.20 1 223 . 21 GLU H H 9.48 0.01 1 224 . 21 GLU HA H 4.67 0.01 1 225 . 21 GLU HB2 H 1.75 0.01 2 226 . 21 GLU HB3 H 1.99 0.01 2 227 . 21 GLU HG2 H 2.11 0.01 2 228 . 21 GLU HG3 H 2.22 0.01 2 229 . 21 GLU CA C 54.69 0.20 1 230 . 21 GLU CB C 35.09 0.20 1 231 . 21 GLU N N 116.26 0.20 1 232 . 22 GLY HA2 H 3.83 0.01 2 233 . 22 GLY HA3 H 3.92 0.01 2 234 . 22 GLY CA C 45.96 0.20 1 235 . 23 ASP HA H 4.17 0.01 1 236 . 23 ASP HB2 H 2.85 0.01 2 237 . 23 ASP HB3 H 2.93 0.01 2 238 . 23 ASP C C 176.39 0.20 1 239 . 23 ASP CA C 58.74 0.20 1 240 . 23 ASP CB C 39.65 0.20 1 241 . 24 LYS H H 7.82 0.01 1 242 . 24 LYS HA H 4.43 0.01 1 243 . 24 LYS HB2 H 1.68 0.01 2 244 . 24 LYS HB3 H 1.81 0.01 2 245 . 24 LYS HG2 H 1.38 0.01 1 246 . 24 LYS HG3 H 1.38 0.01 1 247 . 24 LYS HE2 H 3.01 0.01 1 248 . 24 LYS HE3 H 3.01 0.01 1 249 . 24 LYS C C 176.67 0.20 1 250 . 24 LYS CA C 58.24 0.20 1 251 . 24 LYS CB C 31.24 0.20 1 252 . 24 LYS CG C 24.95 0.20 1 253 . 24 LYS CE C 42.41 0.20 1 254 . 24 LYS N N 118.47 0.20 1 255 . 25 HIS H H 9.55 0.01 1 256 . 25 HIS HA H 4.98 0.01 1 257 . 25 HIS HB2 H 3.27 0.01 2 258 . 25 HIS HB3 H 3.62 0.01 2 259 . 25 HIS HD2 H 7.26 0.01 1 260 . 25 HIS C C 173.30 0.20 1 261 . 25 HIS CA C 55.30 0.20 1 262 . 25 HIS CB C 31.13 0.20 1 263 . 25 HIS CD2 C 119.19 0.20 1 264 . 25 HIS N N 118.90 0.20 1 265 . 26 LYS H H 7.16 0.01 1 266 . 26 LYS HA H 5.15 0.01 1 267 . 26 LYS HB2 H 1.62 0.01 1 268 . 26 LYS HB3 H 1.62 0.01 1 269 . 26 LYS HG2 H 1.47 0.01 1 270 . 26 LYS HG3 H 1.47 0.01 1 271 . 26 LYS HE2 H 2.96 0.01 1 272 . 26 LYS HE3 H 2.96 0.01 1 273 . 26 LYS CA C 55.26 0.20 1 274 . 26 LYS CB C 38.91 0.20 1 275 . 26 LYS CD C 31.24 0.20 1 276 . 26 LYS CE C 40.26 0.20 1 277 . 26 LYS N N 115.41 0.20 1 278 . 27 LEU H H 9.64 0.01 1 279 . 27 LEU HA H 5.27 0.01 1 280 . 27 LEU HB2 H 1.18 0.01 2 281 . 27 LEU HB3 H 2.16 0.01 2 282 . 27 LEU HG H 1.26 0.01 1 283 . 27 LEU HD1 H 0.78 0.01 2 284 . 27 LEU HD2 H 0.32 0.01 2 285 . 27 LEU C C 175.96 0.20 1 286 . 27 LEU CA C 52.45 0.20 1 287 . 27 LEU CB C 43.73 0.20 1 288 . 27 LEU CG C 25.14 0.20 1 289 . 27 LEU CD1 C 29.03 0.20 2 290 . 27 LEU CD2 C 24.79 0.20 2 291 . 27 LEU N N 126.39 0.20 1 292 . 28 LYS H H 9.76 0.01 1 293 . 28 LYS HA H 4.61 0.01 1 294 . 28 LYS HB2 H 2.17 0.01 1 295 . 28 LYS HB3 H 2.17 0.01 1 296 . 28 LYS HD2 H 1.68 0.01 1 297 . 28 LYS HD3 H 1.68 0.01 1 298 . 28 LYS HE2 H 2.96 0.01 1 299 . 28 LYS HE3 H 2.96 0.01 1 300 . 28 LYS C C 177.73 0.20 1 301 . 28 LYS CA C 55.09 0.20 1 302 . 28 LYS CB C 33.14 0.20 1 303 . 28 LYS CG C 24.13 0.20 1 304 . 28 LYS CE C 39.95 0.20 1 305 . 28 LYS N N 124.63 0.20 1 306 . 29 LYS H H 9.09 0.01 1 307 . 29 LYS HA H 4.72 0.01 1 308 . 29 LYS HB2 H 1.82 0.01 2 309 . 29 LYS HB3 H 1.98 0.01 2 310 . 29 LYS HD2 H 1.87 0.01 1 311 . 29 LYS HD3 H 1.87 0.01 1 312 . 29 LYS HE2 H 3.60 0.01 1 313 . 29 LYS HE3 H 3.60 0.01 1 314 . 29 LYS C C 177.70 0.20 1 315 . 29 LYS CA C 62.23 0.20 1 316 . 29 LYS CB C 32.81 0.20 1 317 . 29 LYS CG C 29.23 0.20 1 318 . 29 LYS CD C 31.00 0.20 1 319 . 29 LYS N N 121.44 0.20 1 320 . 30 SER H H 8.14 0.01 1 321 . 30 SER HA H 4.72 0.01 1 322 . 30 SER HB2 H 3.98 0.01 1 323 . 30 SER HB3 H 3.98 0.01 1 324 . 30 SER C C 177.23 0.20 1 325 . 30 SER CA C 61.35 0.20 1 326 . 30 SER CB C 61.35 0.20 1 327 . 30 SER N N 110.41 0.20 1 328 . 31 GLU H H 6.61 0.01 1 329 . 31 GLU HA H 4.25 0.01 1 330 . 31 GLU HB2 H 2.37 0.01 1 331 . 31 GLU HB3 H 2.37 0.01 1 332 . 31 GLU C C 177.72 0.20 1 333 . 31 GLU CA C 58.68 0.20 1 334 . 31 GLU CB C 31.42 0.20 1 335 . 31 GLU CG C 37.14 0.20 1 336 . 31 GLU N N 123.71 0.20 1 337 . 32 LEU H H 8.51 0.01 1 338 . 32 LEU HA H 3.97 0.01 1 339 . 32 LEU HB2 H 1.17 0.01 2 340 . 32 LEU HB3 H 1.94 0.01 2 341 . 32 LEU HG H 1.33 0.01 1 342 . 32 LEU HD1 H 0.86 0.01 2 343 . 32 LEU HD2 H 0.66 0.01 2 344 . 32 LEU C C 177.39 0.20 1 345 . 32 LEU CA C 57.87 0.20 1 346 . 32 LEU CB C 42.06 0.20 1 347 . 32 LEU CG C 26.56 0.20 1 348 . 32 LEU CD1 C 22.35 0.20 2 349 . 32 LEU N N 120.14 0.20 1 350 . 33 LYS H H 8.36 0.01 1 351 . 33 LYS HA H 3.63 0.01 1 352 . 33 LYS HB2 H 2.35 0.01 1 353 . 33 LYS HB3 H 2.35 0.01 1 354 . 33 LYS HG2 H 1.31 0.01 1 355 . 33 LYS HG3 H 1.31 0.01 1 356 . 33 LYS HD2 H 1.66 0.01 1 357 . 33 LYS HD3 H 1.66 0.01 1 358 . 33 LYS HE2 H 2.78 0.01 1 359 . 33 LYS HE3 H 2.78 0.01 1 360 . 33 LYS C C 177.08 0.20 1 361 . 33 LYS CA C 60.33 0.20 1 362 . 33 LYS CB C 32.38 0.20 1 363 . 33 LYS CG C 25.19 0.20 1 364 . 33 LYS CD C 30.30 0.20 1 365 . 33 LYS CE C 41.70 0.20 1 366 . 33 LYS N N 118.58 0.20 1 367 . 34 GLU H H 7.40 0.01 1 368 . 34 GLU HA H 4.06 0.01 1 369 . 34 GLU HB3 H 2.34 0.01 2 370 . 34 GLU HG2 H 2.47 0.01 2 371 . 34 GLU HG3 H 2.61 0.01 2 372 . 34 GLU C C 177.97 0.20 1 373 . 34 GLU CA C 59.50 0.20 1 374 . 34 GLU CB C 29.37 0.20 1 375 . 34 GLU CG C 36.58 0.20 1 376 . 34 GLU N N 116.70 0.20 1 377 . 35 LEU H H 7.96 0.01 1 378 . 35 LEU HA H 2.65 0.01 1 379 . 35 LEU HB2 H 1.00 0.01 2 380 . 35 LEU HB3 H 1.54 0.01 2 381 . 35 LEU HG H 1.12 0.01 1 382 . 35 LEU HD1 H 0.77 0.01 2 383 . 35 LEU HD2 H 0.64 0.01 2 384 . 35 LEU C C 179.17 0.20 1 385 . 35 LEU CA C 59.39 0.20 1 386 . 35 LEU CB C 41.97 0.20 1 387 . 35 LEU CG C 27.95 0.20 1 388 . 35 LEU CD1 C 24.23 0.20 2 389 . 35 LEU CD2 C 28.15 0.20 2 390 . 35 LEU N N 123.68 0.20 1 391 . 36 ILE H H 8.39 0.01 1 392 . 36 ILE HA H 3.45 0.01 1 393 . 36 ILE HB H 1.87 0.01 1 394 . 36 ILE HG12 H 1.92 0.01 1 395 . 36 ILE HG13 H 1.92 0.01 1 396 . 36 ILE HG2 H 1.23 0.01 1 397 . 36 ILE HD1 H 0.74 0.01 1 398 . 36 ILE C C 178.35 0.20 1 399 . 36 ILE CA C 66.10 0.20 1 400 . 36 ILE CB C 38.48 0.20 1 401 . 36 ILE CG1 C 30.30 0.20 1 402 . 36 ILE CG2 C 17.76 0.20 1 403 . 36 ILE CD1 C 11.85 0.20 1 404 . 36 ILE N N 120.90 0.20 1 405 . 37 ASN H H 8.46 0.01 1 406 . 37 ASN HA H 4.72 0.01 1 407 . 37 ASN HB2 H 2.87 0.01 1 408 . 37 ASN HB3 H 2.87 0.01 1 409 . 37 ASN HD21 H 7.15 0.01 2 410 . 37 ASN HD22 H 7.53 0.01 2 411 . 37 ASN C C 177.51 0.20 1 412 . 37 ASN CA C 54.68 0.20 1 413 . 37 ASN CB C 37.31 0.20 1 414 . 37 ASN CG C 175.34 0.20 1 415 . 37 ASN N N 117.60 0.20 1 416 . 37 ASN ND2 N 107.05 0.20 1 417 . 38 ASN H H 8.28 0.01 1 418 . 38 ASN HA H 4.92 0.01 1 419 . 38 ASN HB2 H 2.84 0.01 2 420 . 38 ASN HB3 H 3.34 0.01 2 421 . 38 ASN HD21 H 7.18 0.01 2 422 . 38 ASN HD22 H 8.09 0.01 2 423 . 38 ASN C C 177.12 0.20 1 424 . 38 ASN CA C 54.97 0.20 1 425 . 38 ASN CB C 40.37 0.20 1 426 . 38 ASN CG C 177.51 0.20 1 427 . 38 ASN N N 115.05 0.20 1 428 . 38 ASN ND2 N 113.97 0.20 1 429 . 39 GLU H H 8.56 0.01 1 430 . 39 GLU HA H 5.12 0.01 1 431 . 39 GLU HB2 H 1.96 0.01 1 432 . 39 GLU HB3 H 1.96 0.01 1 433 . 39 GLU HG2 H 2.54 0.01 2 434 . 39 GLU HG3 H 2.63 0.01 2 435 . 39 GLU C C 177.263 0.20 1 436 . 39 GLU CA C 55.20 0.20 1 437 . 39 GLU CB C 30.74 0.20 1 438 . 39 GLU CG C 35.14 0.20 1 439 . 39 GLU N N 114.02 0.20 1 440 . 40 LEU H H 7.74 0.01 1 441 . 40 LEU HA H 5.40 0.01 1 442 . 40 LEU HB2 H 2.14 0.01 1 443 . 40 LEU HB3 H 2.14 0.01 1 444 . 40 LEU HG H 1.65 0.01 1 445 . 40 LEU HD1 H 1.04 0.01 2 446 . 40 LEU HD2 H 0.94 0.01 2 447 . 40 LEU C C 177.41 0.20 1 448 . 40 LEU CA C 54.22 0.20 1 449 . 40 LEU CB C 42.09 0.20 1 450 . 40 LEU CG C 26.72 0.20 1 451 . 40 LEU CD1 C 25.22 0.20 2 452 . 40 LEU N N 120.49 0.20 1 453 . 41 SER H H 7.33 0.01 1 454 . 41 SER HA H 4.59 0.01 1 455 . 41 SER HB2 H 3.90 0.01 1 456 . 41 SER HB3 H 3.90 0.01 1 457 . 41 SER C C 175.75 0.20 1 458 . 41 SER CA C 60.10 0.20 1 459 . 41 SER CB C 63.96 0.20 1 460 . 41 SER N N 113.44 0.20 1 461 . 42 HIS H H 9.94 0.01 1 462 . 42 HIS HA H 4.45 0.01 1 463 . 42 HIS HB2 H 2.88 0.01 2 464 . 42 HIS HB3 H 3.22 0.01 2 465 . 42 HIS HD2 H 7.14 0.01 1 466 . 42 HIS C C 175.78 0.20 1 467 . 42 HIS CA C 58.58 0.20 1 468 . 42 HIS CB C 27.42 0.20 1 469 . 42 HIS CD2 C 119.58 0.20 1 470 . 42 HIS N N 119.45 0.20 1 471 . 43 PHE H H 7.87 0.01 1 472 . 43 PHE HB2 H 2.88 0.01 2 473 . 43 PHE HB3 H 3.27 0.01 2 474 . 43 PHE C C 174.70 0.20 1 475 . 43 PHE CA C 57.62 0.20 1 476 . 43 PHE CB C 39.34 0.20 1 477 . 43 PHE N N 118.38 0.20 1 478 . 44 LEU H H 8.34 0.01 1 479 . 44 LEU HA H 5.08 0.01 1 480 . 44 LEU HB2 H 1.57 0.01 1 481 . 44 LEU HB3 H 1.57 0.01 1 482 . 44 LEU HG H 1.72 0.01 1 483 . 44 LEU HD1 H 0.93 0.01 2 484 . 44 LEU HD2 H 0.99 0.01 2 485 . 44 LEU C C 176.31 0.20 1 486 . 44 LEU CA C 52.97 0.20 1 487 . 44 LEU CB C 44.54 0.20 1 488 . 44 LEU CG C 27.51 0.20 1 489 . 44 LEU CD1 C 23.73 0.20 2 490 . 44 LEU CD2 C 17.98 0.20 2 491 . 44 LEU N N 119.00 0.20 1 492 . 45 GLU H H 8.27 0.01 1 493 . 45 GLU HA H 4.07 0.01 1 494 . 45 GLU HB2 H 1.84 0.01 2 495 . 45 GLU HB3 H 2.00 0.01 2 496 . 45 GLU HG2 H 2.01 0.01 2 497 . 45 GLU HG3 H 2.38 0.01 2 498 . 45 GLU C C 175.56 0.20 1 499 . 45 GLU CA C 56.45 0.20 1 500 . 45 GLU CB C 30.57 0.20 1 501 . 45 GLU CG C 36.62 0.20 1 502 . 45 GLU N N 121.03 0.20 1 503 . 46 GLU H H 8.26 0.01 1 504 . 46 GLU HA H 4.27 0.01 1 505 . 46 GLU HB2 H 2.12 0.01 1 506 . 46 GLU HB3 H 2.12 0.01 1 507 . 46 GLU C C 177.26 0.20 1 508 . 46 GLU CA C 56.61 0.20 1 509 . 46 GLU CB C 30.85 0.20 1 510 . 46 GLU N N 123.21 0.20 1 511 . 47 ILE H H 9.84 0.01 1 512 . 47 ILE HA H 4.08 0.01 1 513 . 47 ILE HB H 1.74 0.01 1 514 . 47 ILE HG2 H 0.74 0.01 1 515 . 47 ILE C C 176.36 0.20 1 516 . 47 ILE CA C 62.24 0.20 1 517 . 47 ILE CB C 38.22 0.20 1 518 . 47 ILE CG1 C 27.78 0.20 1 519 . 47 ILE CG2 C 18.77 0.20 1 520 . 47 ILE N N 126.11 0.20 1 521 . 48 LYS H H 8.95 0.01 1 522 . 48 LYS HA H 4.55 0.01 1 523 . 48 LYS HB2 H 1.83 0.01 1 524 . 48 LYS HB3 H 1.83 0.01 1 525 . 48 LYS HG2 H 1.45 0.01 1 526 . 48 LYS HG3 H 1.45 0.01 1 527 . 48 LYS HE2 H 3.00 0.01 2 528 . 48 LYS HE3 H 3.71 0.01 2 529 . 48 LYS C C 176.12 0.20 1 530 . 48 LYS CA C 56.37 0.20 1 531 . 48 LYS CB C 34.36 0.20 1 532 . 48 LYS CG C 25.06 0.20 1 533 . 48 LYS CD C 29.32 0.20 1 534 . 48 LYS CE C 42.11 0.20 1 535 . 48 LYS N N 127.40 0.20 1 536 . 49 GLU H H 7.62 0.01 1 537 . 49 GLU HA H 4.65 0.01 1 538 . 49 GLU HB2 H 1.99 0.01 2 539 . 49 GLU HB3 H 2.33 0.01 2 540 . 49 GLU HG2 H 2.32 0.01 1 541 . 49 GLU HG3 H 2.32 0.01 1 542 . 49 GLU C C 176.73 0.20 1 543 . 49 GLU CA C 55.45 0.20 1 544 . 49 GLU CB C 31.25 0.20 1 545 . 49 GLU CG C 34.63 0.20 1 546 . 49 GLU N N 119.19 0.20 1 547 . 50 GLN H H 8.91 0.01 1 548 . 50 GLN HA H 3.77 0.01 1 549 . 50 GLN HB2 H 2.31 0.01 2 550 . 50 GLN HB3 H 2.49 0.01 2 551 . 50 GLN HG2 H 1.99 0.01 2 552 . 50 GLN HG3 H 2.24 0.01 2 553 . 50 GLN HE21 H 6.52 0.01 2 554 . 50 GLN HE22 H 8.04 0.01 2 555 . 50 GLN C C 177.05 0.20 1 556 . 50 GLN CA C 58.24 0.20 1 557 . 50 GLN CB C 28.23 0.20 1 558 . 50 GLN CG C 28.50 0.20 1 559 . 50 GLN CD C 180.44 0.20 1 560 . 50 GLN N N 125.45 0.20 1 561 . 50 GLN NE2 N 113.90 0.20 1 562 . 51 GLU H H 9.31 0.01 1 563 . 51 GLU HA H 4.17 0.01 1 564 . 51 GLU HB2 H 2.02 0.01 2 565 . 51 GLU HB3 H 2.11 0.01 2 566 . 51 GLU HG2 H 2.37 0.01 1 567 . 51 GLU HG3 H 2.37 0.01 1 568 . 51 GLU C C 178.68 0.20 1 569 . 51 GLU CA C 59.51 0.20 1 570 . 51 GLU CB C 28.94 0.20 1 571 . 51 GLU CG C 36.57 0.20 1 572 . 51 GLU N N 116.77 0.20 1 573 . 52 VAL H H 7.18 0.01 1 574 . 52 VAL HA H 3.59 0.01 1 575 . 52 VAL HB H 1.98 0.01 1 576 . 52 VAL HG1 H 0.97 0.01 2 577 . 52 VAL HG2 H 0.35 0.01 2 578 . 52 VAL C C 177.28 0.20 1 579 . 52 VAL CA C 66.14 0.20 1 580 . 52 VAL CB C 31.35 0.20 1 581 . 52 VAL CG1 C 22.46 0.20 2 582 . 52 VAL CG2 C 20.27 0.20 2 583 . 52 VAL N N 118.62 0.20 1 584 . 53 VAL H H 7.00 0.01 1 585 . 53 VAL HA H 3.37 0.01 1 586 . 53 VAL HB H 2.11 0.01 1 587 . 53 VAL HG1 H 0.91 0.01 2 588 . 53 VAL HG2 H 0.95 0.01 2 589 . 53 VAL C C 177.28 0.20 1 590 . 53 VAL CA C 66.20 0.20 1 591 . 53 VAL CB C 31.30 0.20 1 592 . 53 VAL CG1 C 18.48 0.20 2 593 . 53 VAL CG2 C 18.51 0.20 2 594 . 53 VAL N N 119.35 0.20 1 595 . 54 ASP H H 8.38 0.01 1 596 . 54 ASP HA H 4.17 0.01 1 597 . 54 ASP HB2 H 2.79 0.01 2 598 . 54 ASP HB3 H 2.87 0.01 2 599 . 54 ASP C C 178.55 0.20 1 600 . 54 ASP CA C 57.90 0.20 1 601 . 54 ASP CB C 39.56 0.20 1 602 . 54 ASP N N 120.93 0.20 1 603 . 55 LYS H H 7.62 0.01 1 604 . 55 LYS HA H 4.17 0.01 1 605 . 55 LYS HB2 H 1.98 0.01 1 606 . 55 LYS HB3 H 1.98 0.01 1 607 . 55 LYS HG2 H 1.54 0.01 1 608 . 55 LYS HG3 H 1.54 0.01 1 609 . 55 LYS HD2 H 1.63 0.01 1 610 . 55 LYS HD3 H 1.63 0.01 1 611 . 55 LYS HE2 H 3.06 0.01 2 612 . 55 LYS HE3 H 3.15 0.01 2 613 . 55 LYS C C 179.65 0.20 1 614 . 55 LYS CA C 58.63 0.20 1 615 . 55 LYS CB C 32.32 0.20 1 616 . 55 LYS CG C 25.41 0.20 1 617 . 55 LYS CD C 28.90 0.20 1 618 . 55 LYS CE C 42.40 0.20 1 619 . 55 LYS N N 121.37 0.20 1 620 . 56 VAL H H 8.50 0.01 1 621 . 56 VAL HA H 3.52 0.01 1 622 . 56 VAL HB H 1.95 0.01 1 623 . 56 VAL HG1 H 0.97 0.01 2 624 . 56 VAL HG2 H 0.74 0.01 2 625 . 56 VAL C C 177.77 0.20 1 626 . 56 VAL CA C 67.11 0.20 1 627 . 56 VAL CB C 31.57 0.20 1 628 . 56 VAL CG1 C 22.48 0.20 2 629 . 56 VAL CG2 C 21.92 0.20 2 630 . 56 VAL N N 122.31 0.20 1 631 . 57 MET H H 8.35 0.01 1 632 . 57 MET HA H 4.28 0.01 1 633 . 57 MET HB2 H 2.05 0.01 1 634 . 57 MET HB3 H 2.05 0.01 1 635 . 57 MET HG2 H 2.43 0.01 1 636 . 57 MET HG3 H 2.43 0.01 1 637 . 57 MET HE H 1.93 0.01 1 638 . 57 MET CA C 57.62 0.20 1 639 . 57 MET CB C 30.73 0.20 1 640 . 57 MET CG C 32.02 0.20 1 641 . 57 MET CE C 18.00 0.20 1 642 . 57 MET N N 118.05 0.20 1 643 . 58 GLU H H 8.18 0.01 1 644 . 58 GLU HA H 4.08 0.01 1 645 . 58 GLU HB2 H 2.19 0.01 1 646 . 58 GLU HB3 H 2.19 0.01 1 647 . 58 GLU HG2 H 2.35 0.01 2 648 . 58 GLU HG3 H 2.47 0.01 2 649 . 58 GLU C C 178.70 0.20 1 650 . 58 GLU CA C 58.88 0.20 1 651 . 58 GLU CB C 29.90 0.20 1 652 . 58 GLU CG C 36.35 0.20 1 653 . 58 GLU N N 117.29 0.20 1 654 . 59 THR H H 7.70 0.01 1 655 . 59 THR HA H 4.07 0.01 1 656 . 59 THR HB H 4.46 0.01 1 657 . 59 THR HG2 H 1.39 0.01 1 658 . 59 THR C C 175.16 0.20 1 659 . 59 THR CA C 65.94 0.20 1 660 . 59 THR CB C 68.96 0.20 1 661 . 59 THR CG2 C 20.70 0.20 1 662 . 59 THR N N 114.43 0.20 1 663 . 60 LEU H H 7.68 0.01 1 664 . 60 LEU HA H 4.35 0.01 1 665 . 60 LEU HB2 H 1.58 0.01 2 666 . 60 LEU HB3 H 1.73 0.01 2 667 . 60 LEU HG H 2.05 0.01 1 668 . 60 LEU HD1 H 0.88 0.01 2 669 . 60 LEU HD2 H 0.63 0.01 2 670 . 60 LEU C C 177.89 0.20 1 671 . 60 LEU CA C 55.67 0.20 1 672 . 60 LEU CB C 43.29 0.20 1 673 . 60 LEU CG C 25.71 0.20 1 674 . 60 LEU CD1 C 21.64 0.20 2 675 . 60 LEU CD2 C 20.55 0.20 2 676 . 60 LEU N N 119.72 0.20 1 677 . 61 ASP H H 8.14 0.01 1 678 . 61 ASP HA H 4.56 0.01 1 679 . 61 ASP HB2 H 2.50 0.01 2 680 . 61 ASP HB3 H 2.88 0.01 2 681 . 61 ASP C C 176.32 0.20 1 682 . 61 ASP CA C 54.60 0.20 1 683 . 61 ASP CB C 40.03 0.20 1 684 . 61 ASP N N 116.88 0.20 1 685 . 62 ASN H H 9.19 0.01 1 686 . 62 ASN HA H 4.84 0.01 1 687 . 62 ASN HB2 H 2.93 0.01 1 688 . 62 ASN HB3 H 2.93 0.01 1 689 . 62 ASN HD21 H 6.94 0.01 2 690 . 62 ASN HD22 H 7.75 0.01 2 691 . 62 ASN C C 176.31 0.20 1 692 . 62 ASN CA C 54.55 0.20 1 693 . 62 ASN CB C 40.21 0.20 1 694 . 62 ASN CG C 176.11 0.20 1 695 . 62 ASN N N 127.87 0.20 1 696 . 62 ASN ND2 N 113.50 0.20 1 697 . 63 ASP H H 8.31 0.01 1 698 . 63 ASP HA H 4.76 0.01 1 699 . 63 ASP HB2 H 2.71 0.01 2 700 . 63 ASP HB3 H 3.07 0.01 2 701 . 63 ASP C C 177.95 0.20 1 702 . 63 ASP CA C 53.29 0.20 1 703 . 63 ASP CB C 40.10 0.20 1 704 . 63 ASP N N 116.28 0.20 1 705 . 64 GLY H H 7.70 0.01 1 706 . 64 GLY HA2 H 3.92 0.01 2 707 . 64 GLY HA3 H 4.05 0.01 2 708 . 64 GLY C C 175.19 0.20 1 709 . 64 GLY CA C 47.50 0.20 1 710 . 64 GLY N N 109.35 0.20 1 711 . 65 ASP H H 8.40 0.01 1 712 . 65 ASP HA H 4.60 0.01 1 713 . 65 ASP HB2 H 2.62 0.01 2 714 . 65 ASP HB3 H 3.09 0.01 2 715 . 65 ASP C C 177.39 0.20 1 716 . 65 ASP CA C 53.60 0.20 1 717 . 65 ASP CB C 40.02 0.20 1 718 . 65 ASP N N 120.93 0.20 1 719 . 66 GLY H H 10.18 0.01 1 720 . 66 GLY HA2 H 3.49 0.01 2 721 . 66 GLY HA3 H 4.09 0.01 2 722 . 66 GLY C C 172.69 0.20 1 723 . 66 GLY CA C 45.82 0.20 1 724 . 66 GLY N N 113.95 0.20 1 725 . 67 GLU H H 7.94 0.01 1 726 . 67 GLU HA H 4.82 0.01 1 727 . 67 GLU HB2 H 1.51 0.01 2 728 . 67 GLU HB3 H 2.12 0.01 2 729 . 67 GLU HG2 H 2.07 0.01 2 730 . 67 GLU HG3 H 2.17 0.01 2 731 . 67 GLU C C 175.05 0.20 1 732 . 67 GLU CA C 54.98 0.20 1 733 . 67 GLU CB C 34.33 0.20 1 734 . 67 GLU CG C 36.11 0.20 1 735 . 67 GLU N N 118.20 0.20 1 736 . 68 CYS H H 9.49 0.01 1 737 . 68 CYS HA H 5.77 0.01 1 738 . 68 CYS HB2 H 2.47 0.01 2 739 . 68 CYS HB3 H 3.30 0.01 2 740 . 68 CYS C C 174.74 0.20 1 741 . 68 CYS CA C 56.74 0.20 1 742 . 68 CYS CB C 27.95 0.20 1 743 . 68 CYS N N 124.85 0.20 1 744 . 69 ASP H H 9.94 0.01 1 745 . 69 ASP HA H 5.22 0.01 1 746 . 69 ASP HB2 H 2.98 0.01 2 747 . 69 ASP HB3 H 3.60 0.01 2 748 . 69 ASP C C 175.54 0.20 1 749 . 69 ASP CA C 52.95 0.20 1 750 . 69 ASP CB C 40.21 0.20 1 751 . 69 ASP N N 132.25 0.20 1 752 . 70 PHE H H 8.97 0.01 1 753 . 70 PHE HA H 3.14 0.01 1 754 . 70 PHE HB2 H 2.22 0.01 2 755 . 70 PHE HB3 H 2.46 0.01 2 756 . 70 PHE HD1 H 6.95 0.01 1 757 . 70 PHE HD2 H 6.95 0.01 1 758 . 70 PHE HE1 H 7.01 0.01 1 759 . 70 PHE HE2 H 7.01 0.01 1 760 . 70 PHE C C 176.63 0.20 1 761 . 70 PHE CA C 63.23 0.20 1 762 . 70 PHE CB C 38.90 0.20 1 763 . 70 PHE CD1 C 131.46 0.20 1 764 . 70 PHE CD2 C 131.46 0.20 1 765 . 70 PHE CE1 C 129.63 0.20 1 766 . 70 PHE CE2 C 129.63 0.20 1 767 . 70 PHE N N 118.52 0.20 1 768 . 71 GLN H H 8.03 0.01 1 769 . 71 GLN HA H 3.78 0.01 1 770 . 71 GLN HB2 H 2.27 0.01 1 771 . 71 GLN HB3 H 2.27 0.01 1 772 . 71 GLN HG2 H 2.45 0.01 1 773 . 71 GLN HG3 H 2.45 0.01 1 774 . 71 GLN HE21 H 6.91 0.01 2 775 . 71 GLN HE22 H 7.64 0.01 2 776 . 71 GLN C C 179.80 0.20 1 777 . 71 GLN CA C 59.67 0.20 1 778 . 71 GLN CB C 30.02 0.20 1 779 . 71 GLN CG C 34.24 0.20 1 780 . 71 GLN CD C 180.32 0.20 1 781 . 71 GLN N N 119.23 0.20 1 782 . 71 GLN NE2 N 112.54 0.20 1 783 . 72 GLU H H 8.97 0.01 1 784 . 72 GLU HA H 4.20 0.01 1 785 . 72 GLU HB2 H 2.11 0.01 2 786 . 72 GLU HB3 H 2.21 0.01 2 787 . 72 GLU HG2 H 2.57 0.01 2 788 . 72 GLU HG3 H 2.83 0.01 2 789 . 72 GLU C C 179.47 0.20 1 790 . 72 GLU CA C 58.82 0.20 1 791 . 72 GLU CB C 29.83 0.20 1 792 . 72 GLU CG C 37.35 0.20 1 793 . 72 GLU N N 123.33 0.20 1 794 . 73 PHE H H 8.80 0.01 1 795 . 73 PHE HA H 4.21 0.01 1 796 . 73 PHE HB2 H 3.04 0.01 2 797 . 73 PHE HB3 H 3.23 0.01 2 798 . 73 PHE HE1 H 6.88 0.01 1 799 . 73 PHE HE2 H 6.88 0.01 1 800 . 73 PHE CA C 60.28 0.20 1 801 . 73 PHE CB C 39.23 0.20 1 802 . 73 PHE N N 122.31 0.20 1 803 . 74 MET H H 8.33 0.01 1 804 . 74 MET HA H 4.10 0.01 1 805 . 74 MET HB3 H 2.05 0.01 2 806 . 74 MET HG2 H 1.69 0.01 2 807 . 74 MET HG3 H 2.26 0.01 2 808 . 74 MET C C 179.17 0.20 1 809 . 74 MET CA C 55.21 0.20 1 810 . 74 MET CB C 29.29 0.20 1 811 . 74 MET N N 119.19 0.20 1 812 . 75 ALA H H 7.60 0.01 1 813 . 75 ALA HA H 4.18 0.01 1 814 . 75 ALA HB H 1.64 0.01 1 815 . 75 ALA C C 180.60 0.20 1 816 . 75 ALA CA C 55.17 0.20 1 817 . 75 ALA CB C 17.63 0.20 1 818 . 75 ALA N N 123.80 0.20 1 819 . 76 PHE H H 7.61 0.01 1 820 . 76 PHE HA H 4.51 0.01 1 821 . 76 PHE HB2 H 3.45 0.01 2 822 . 76 PHE HB3 H 3.55 0.01 2 823 . 76 PHE HD1 H 7.09 0.01 1 824 . 76 PHE HD2 H 7.09 0.01 1 825 . 76 PHE C C 176.72 0.20 1 826 . 76 PHE CA C 59.91 0.20 1 827 . 76 PHE CB C 37.98 0.20 1 828 . 76 PHE CD1 C 131.88 0.20 1 829 . 76 PHE CD2 C 131.88 0.20 1 830 . 76 PHE N N 121.74 0.20 1 831 . 77 VAL H H 8.49 0.01 1 832 . 77 VAL HA H 2.91 0.01 1 833 . 77 VAL HB H 1.97 0.01 1 834 . 77 VAL HG1 H 0.69 0.01 2 835 . 77 VAL HG2 H 0.35 0.01 2 836 . 77 VAL C C 179.69 0.20 1 837 . 77 VAL CA C 66.70 0.20 1 838 . 77 VAL CB C 31.36 0.20 1 839 . 77 VAL CG1 C 20.57 0.20 2 840 . 77 VAL CG2 C 23.29 0.20 2 841 . 77 VAL N N 120.52 0.20 1 842 . 78 ALA H H 8.51 0.01 1 843 . 78 ALA HA H 3.96 0.01 1 844 . 78 ALA HB H 1.46 0.01 1 845 . 78 ALA C C 179.26 0.20 1 846 . 78 ALA CA C 56.17 0.20 1 847 . 78 ALA CB C 17.74 0.20 1 848 . 78 ALA N N 125.09 0.20 1 849 . 79 MET H H 8.05 0.01 1 850 . 79 MET HA H 4.15 0.01 1 851 . 79 MET HB2 H 2.08 0.01 2 852 . 79 MET HB3 H 2.46 0.01 2 853 . 79 MET HG2 H 2.65 0.01 2 854 . 79 MET HG3 H 2.72 0.01 2 855 . 79 MET C C 178.99 0.20 1 856 . 79 MET CA C 59.47 0.20 1 857 . 79 MET CB C 33.61 0.20 1 858 . 79 MET CG C 31.60 0.20 1 859 . 79 MET CE C 16.81 0.20 1 860 . 79 MET N N 120.90 0.20 1 861 . 80 VAL H H 8.40 0.01 1 862 . 80 VAL HA H 3.46 0.01 1 863 . 80 VAL HB H 1.67 0.01 1 864 . 80 VAL HG1 H 0.77 0.01 2 865 . 80 VAL HG2 H 0.37 0.01 2 866 . 80 VAL C C 178.90 0.20 1 867 . 80 VAL CA C 66.63 0.20 1 868 . 80 VAL CB C 31.81 0.20 1 869 . 80 VAL CG1 C 22.46 0.20 2 870 . 80 VAL CG2 C 22.49 0.20 2 871 . 80 VAL N N 120.00 0.20 1 872 . 81 THR H H 8.70 0.01 1 873 . 81 THR HA H 3.98 0.01 1 874 . 81 THR HB H 3.77 0.01 1 875 . 81 THR HG2 H 1.55 0.01 1 876 . 81 THR CA C 68.45 0.20 1 877 . 81 THR CB C 68.18 0.20 1 878 . 81 THR CG2 C 23.14 0.20 1 879 . 81 THR N N 117.53 0.20 1 880 . 82 THR H H 8.19 0.01 1 881 . 82 THR HA H 4.08 0.01 1 882 . 82 THR HB H 4.26 0.01 1 883 . 82 THR HG2 H 1.31 0.01 1 884 . 82 THR C C 176.42 0.20 1 885 . 82 THR CA C 67.81 0.20 1 886 . 82 THR CB C 68.12 0.20 1 887 . 82 THR CG2 C 21.96 0.20 1 888 . 82 THR N N 116.89 0.20 1 889 . 83 ALA H H 7.57 0.01 1 890 . 83 ALA HA H 4.27 0.01 1 891 . 83 ALA HB H 1.50 0.01 1 892 . 83 ALA C C 179.86 0.20 1 893 . 83 ALA CA C 55.15 0.20 1 894 . 83 ALA CB C 18.10 0.20 1 895 . 83 ALA N N 124.59 0.20 1 896 . 84 CYS H H 8.34 0.01 1 897 . 84 CYS HA H 3.58 0.01 1 898 . 84 CYS HB2 H 2.03 0.01 2 899 . 84 CYS HB3 H 2.82 0.01 2 900 . 84 CYS C C 175.88 0.20 1 901 . 84 CYS CA C 62.44 0.20 1 902 . 84 CYS CB C 26.46 0.20 1 903 . 84 CYS N N 116.71 0.20 1 904 . 85 HIS H H 8.17 0.01 1 905 . 85 HIS HA H 4.01 0.01 1 906 . 85 HIS HB2 H 2.64 0.01 2 907 . 85 HIS HB3 H 3.15 0.01 2 908 . 85 HIS HD2 H 6.46 0.01 1 909 . 85 HIS HE1 H 8.13 0.01 1 910 . 85 HIS C C 177.48 0.20 1 911 . 85 HIS CA C 59.41 0.20 1 912 . 85 HIS CB C 29.14 0.20 1 913 . 85 HIS CD2 C 121.87 0.20 1 914 . 85 HIS CE1 C 136.68 0.20 1 915 . 85 HIS N N 119.13 0.20 1 916 . 86 GLU H H 7.65 0.01 1 917 . 86 GLU HA H 3.94 0.01 1 918 . 86 GLU HB2 H 1.93 0.01 1 919 . 86 GLU HB3 H 1.93 0.01 1 920 . 86 GLU HG2 H 2.27 0.01 1 921 . 86 GLU HG3 H 2.27 0.01 1 922 . 86 GLU C C 177.66 0.20 1 923 . 86 GLU CA C 58.47 0.20 1 924 . 86 GLU CB C 29.57 0.20 1 925 . 86 GLU CG C 36.66 0.20 1 926 . 86 GLU N N 116.75 0.20 1 927 . 87 PHE H H 7.65 0.01 1 928 . 87 PHE HA H 4.50 0.01 1 929 . 87 PHE HB3 H 2.87 0.01 2 930 . 87 PHE HD1 H 7.12 0.01 1 931 . 87 PHE HD2 H 7.12 0.01 1 932 . 87 PHE CA C 58.65 0.20 1 933 . 87 PHE CB C 40.63 0.20 1 934 . 87 PHE CD1 C 131.43 0.20 1 935 . 87 PHE CD2 C 131.43 0.20 1 936 . 87 PHE N N 117.13 0.20 1 937 . 88 PHE H H 7.66 0.01 1 938 . 88 PHE HA H 4.50 0.01 1 939 . 88 PHE HB2 H 2.87 0.01 2 940 . 88 PHE HB3 H 3.02 0.01 2 941 . 88 PHE C C 175.75 0.20 1 942 . 88 PHE CA C 58.65 0.20 1 943 . 88 PHE CB C 39.34 0.20 1 944 . 88 PHE N N 117.13 0.20 1 945 . 89 GLU H H 7.89 0.01 1 946 . 89 GLU HA H 4.18 0.01 1 947 . 89 GLU HB2 H 2.03 0.01 1 948 . 89 GLU HB3 H 2.03 0.01 1 949 . 89 GLU HG2 H 2.17 0.01 1 950 . 89 GLU HG3 H 2.17 0.01 1 951 . 89 GLU C C 175.70 0.20 1 952 . 89 GLU CA C 56.73 0.20 1 953 . 89 GLU CB C 30.17 0.20 1 954 . 89 GLU CG C 36.21 0.20 1 955 . 89 GLU N N 121.69 0.20 1 956 . 90 HIS H H 8.05 0.01 1 957 . 90 HIS HA H 4.56 0.01 1 958 . 90 HIS HB2 H 3.08 0.01 2 959 . 90 HIS HB3 H 3.17 0.01 2 960 . 90 HIS HD2 H 7.14 0.01 1 961 . 90 HIS HE1 H 8.17 0.01 1 962 . 90 HIS C C 173.81 0.20 1 963 . 90 HIS CA C 55.59 0.20 1 964 . 90 HIS CB C 30.02 0.20 1 965 . 90 HIS CD2 C 120.69 0.20 1 966 . 90 HIS CE1 C 137.22 0.20 1 967 . 90 HIS N N 119.32 0.20 1 968 . 91 GLU H H 8.17 0.01 1 969 . 91 GLU HA H 4.14 0.01 1 970 . 91 GLU HB2 H 1.93 0.01 2 971 . 91 GLU HB3 H 2.08 0.01 2 972 . 91 GLU HG2 H 2.21 0.01 1 973 . 91 GLU HG3 H 2.21 0.01 1 974 . 91 GLU CA C 58.25 0.20 1 975 . 91 GLU CB C 30.64 0.20 1 976 . 91 GLU CG C 36.70 0.20 1 977 . 91 GLU N N 127.85 0.20 1 stop_ save_ save_chemical_shifts_set_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 $sample_3 stop_ _Sample_conditions_label $experimental_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'TRTK-12 molecule 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 THR H H 7.59 0.01 1 2 . 2 THR HA H 4.27 0.01 1 3 . 2 THR HB H 3.88 0.01 1 4 . 2 THR HG2 H 1.18 0.01 1 5 . 2 THR CA C 65.14 0.20 1 6 . 2 THR CG2 C 21.79 0.20 1 7 . 3 ARG H H 7.90 0.01 1 8 . 3 ARG HA H 4.42 0.01 1 9 . 3 ARG HB2 H 1.78 0.01 2 10 . 3 ARG HB3 H 1.87 0.01 2 11 . 3 ARG HG2 H 1.64 0.01 1 12 . 3 ARG HG3 H 1.64 0.01 1 13 . 3 ARG HD2 H 3.17 0.01 1 14 . 3 ARG HD3 H 3.17 0.01 1 15 . 3 ARG CG C 27.16 0.20 1 16 . 3 ARG CD C 42.46 0.20 1 17 . 4 THR H H 7.74 0.01 1 18 . 4 THR HA H 4.23 0.01 1 19 . 4 THR HB H 3.82 0.01 1 20 . 4 THR HG2 H 1.13 0.01 1 21 . 4 THR CA C 65.06 0.20 1 22 . 4 THR CG2 C 21.68 0.20 1 23 . 5 LYS H H 7.88 0.01 1 24 . 5 LYS HA H 4.35 0.01 1 25 . 5 LYS HB2 H 1.87 0.01 1 26 . 5 LYS HB3 H 1.87 0.01 1 27 . 5 LYS HG2 H 1.54 0.01 1 28 . 5 LYS HG3 H 1.54 0.01 1 29 . 5 LYS HD2 H 1.75 0.01 1 30 . 5 LYS HD3 H 1.75 0.01 1 31 . 5 LYS HE2 H 2.92 0.01 1 32 . 5 LYS HE3 H 2.92 0.01 1 33 . 6 ILE H H 8.33 0.01 1 34 . 6 ILE HA H 3.72 0.01 1 35 . 6 ILE HB H 1.52 0.01 1 36 . 6 ILE HG12 H 1.06 0.01 2 37 . 6 ILE HG13 H 1.26 0.01 2 38 . 6 ILE HG2 H 0.62 0.01 1 39 . 6 ILE HD1 H 0.58 0.01 1 40 . 6 ILE CA C 61.60 0.20 1 41 . 6 ILE CB C 38.58 0.20 1 42 . 6 ILE CG1 C 27.61 0.20 1 43 . 6 ILE CG2 C 17.98 0.20 1 44 . 6 ILE CD1 C 14.20 0.20 1 45 . 7 ASP H H 7.99 0.01 1 46 . 7 ASP HA H 3.73 0.01 1 47 . 7 ASP HB2 H 2.64 0.01 2 48 . 7 ASP HB3 H 2.74 0.01 2 49 . 8 TRP H H 7.48 0.01 1 50 . 8 TRP HA H 4.18 0.01 1 51 . 8 TRP HB2 H 3.09 0.01 2 52 . 8 TRP HB3 H 3.30 0.01 2 53 . 8 TRP HE1 H 10.28 0.01 1 54 . 8 TRP HD1 H 7.38 0.01 1 55 . 8 TRP HE3 H 7.48 0.01 1 56 . 8 TRP HZ3 H 6.96 0.01 1 57 . 8 TRP HH2 H 7.11 0.01 1 58 . 8 TRP HZ2 H 7.44 0.01 1 59 . 9 ASN H H 7.64 0.01 1 60 . 9 ASN HA H 3.65 0.01 1 61 . 9 ASN HB2 H 3.15 0.01 1 62 . 9 ASN HB3 H 2.94 0.01 2 63 . 9 ASN CB C 42.48 0.20 1 64 . 10 LYS H H 7.82 0.01 1 65 . 10 LYS HA H 4.20 0.01 1 66 . 10 LYS HB2 H 1.84 0.01 1 67 . 10 LYS HB3 H 1.84 0.01 1 68 . 10 LYS HG2 H 1.43 0.01 1 69 . 10 LYS HG3 H 1.43 0.01 1 70 . 10 LYS HD2 H 1.65 0.01 1 71 . 10 LYS HD3 H 1.65 0.01 1 72 . 10 LYS HE2 H 2.92 0.01 1 73 . 10 LYS HE3 H 2.92 0.01 1 74 . 10 LYS CG C 24.85 0.20 1 75 . 10 LYS CD C 27.25 0.20 1 76 . 11 ILE H H 7.48 0.01 1 77 . 11 ILE HA H 3.88 0.01 1 78 . 11 ILE HB H 2.05 0.01 1 79 . 11 ILE HG12 H 0.73 0.01 2 80 . 11 ILE HG13 H 1.36 0.01 2 81 . 11 ILE HG2 H 0.97 0.01 1 82 . 11 ILE HD1 H 0.38 0.01 1 83 . 11 ILE CA C 62.99 0.20 1 84 . 11 ILE CB C 38.08 0.20 1 85 . 11 ILE CG1 C 27.72 0.20 1 86 . 11 ILE CG2 C 17.71 0.20 1 87 . 11 ILE CD1 C 12.19 0.20 1 88 . 12 LEU H H 7.73 0.01 1 89 . 12 LEU HA H 4.21 0.01 1 90 . 12 LEU HB2 H 1.85 0.01 2 91 . 12 LEU HB3 H 1.60 0.01 2 92 . 12 LEU HG H 1.39 0.01 1 93 . 12 LEU HD1 H 0.91 0.01 2 94 . 12 LEU HD2 H 0.85 0.01 2 95 . 12 LEU CB C 42.48 0.20 1 96 . 12 LEU CG C 24.77 0.20 1 97 . 12 LEU CD1 C 25.28 0.20 2 98 . 12 LEU CD2 C 12.95 0.20 2 99 . 13 SER H H 8.09 0.01 1 100 . 13 SER HA H 4.03 0.01 1 101 . 13 SER HB2 H 3.62 0.01 2 102 . 13 SER HB3 H 3.54 0.01 2 stop_ save_