data_4841 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C chemical shift assignments for the PAH2 domain of mSin3B complexed to Mad1-SID ; _BMRB_accession_number 4841 _BMRB_flat_file_name bmr4841.str _Entry_type original _Submission_date 2000-09-27 _Accession_date 2000-09-27 _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 Spronk Christian A.E.M. . 2 Jansen Jacobus F.A. . 3 Tessari Marco . . 4 Kaan Anita M. . 5 Aelen Jan . . 6 Lasonder Edwin . . 7 Stunnenberg Hendrik G. . 8 Vuister Geerten W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 706 "13C chemical shifts" 439 "15N chemical shifts" 114 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-06-02 update BMRB 'addition of the relationship loop' 2001-04-26 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 5457 'assignment of SID24 in complex with PAH2 domain of mSin3B' 5808 'PAH2 domain of mSin3B with SID24 complex' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Sequence-specific Assignment of the PAH2 Domain of Sin3B free and bound to Mad1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21262923 _PubMed_ID 11370785 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Spronk Christian A.E.M. . 2 Jansen Jacobus F.A. . 3 Tessari Marco . . 4 Kaan Anita M. . 5 Aelen Jan . . 6 Lasonder Edwin . . 7 Stunnenberg Hendrik G. . 8 Vuister Geerten W. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 19 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 377 _Page_last 378 _Year 2001 _Details . loop_ _Keyword Sin3 Mad1 'transcriptional regulator' 'protein-peptide complex' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full 'Delaglio, F. et al. J. Biomol. NMR 6, 277-293 (1995)' _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 'Ch. Bartels, et al. J. Biomol. NMR 5, 1-10 (1995)' _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_ save_ref_3 _Saveframe_category citation _Citation_full 'Brunger, A.T. et al. Acta Cryst. D54, 905-921 (1998)' _Citation_title 'Crystallography & NMR system: A new software suite for macromolecular structure determination.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9757107 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Brunger 'A. T.' T. . 2 Adams 'P. D.' D. . 3 Clore 'G. M.' M. . 4 DeLano 'W. L.' L. . 5 Gros P. . . 6 Grosse-Kunstleve 'R. W.' W. . 7 Jiang 'J. S.' S. . 8 Kuszewski J. . . 9 Nilges M. . . 10 Pannu 'N. S.' S. . 11 Read 'R. J.' J. . 12 Rice 'L. M.' M. . 13 Simonson T. . . 14 Warren 'G. L.' L. . stop_ _Journal_abbreviation 'Acta Crystallogr. D Biol. Crystallogr.' _Journal_name_full 'Acta crystallographica. Section D, Biological crystallography' _Journal_volume 54 _Journal_issue 'Pt 5' _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 905 _Page_last 921 _Year 1998 _Details ; A new software suite, called Crystallography & NMR System (CNS), has been developed for macromolecular structure determination by X-ray crystallography or solution nuclear magnetic resonance (NMR) spectroscopy. In contrast to existing structure-determination programs, the architecture of CNS is highly flexible, allowing for extension to other structure-determination methods, such as electron microscopy and solid-state NMR spectroscopy. CNS has a hierarchical structure: a high-level hypertext markup language (HTML) user interface, task-oriented user input files, module files, a symbolic structure-determination language (CNS language), and low-level source code. Each layer is accessible to the user. The novice user may just use the HTML interface, while the more advanced user may use any of the other layers. The source code will be distributed, thus source-code modification is possible. The CNS language is sufficiently powerful and flexible that many new algorithms can be easily implemented in the CNS language without changes to the source code. The CNS language allows the user to perform operations on data structures, such as structure factors, electron-density maps, and atomic properties. The power of the CNS language has been demonstrated by the implementation of a comprehensive set of crystallographic procedures for phasing, density modification and refinement. User-friendly task-oriented input files are available for nearly all aspects of macromolecular structure determination by X-ray crystallography and solution NMR. ; save_ save_ref_4 _Saveframe_category citation _Citation_full 'Nilges, M. et al. J. Mol. Biol. 269, 408-422 (1997)' _Citation_title 'Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9199409 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nilges M. . . 2 Macias 'M. J.' J. . 3 O'Donoghue 'S. I.' I. . 4 Oschkinat H. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 269 _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 408 _Page_last 422 _Year 1997 _Details ; We have used a novel, largely automated, calculation method to refine the NMR solution structure of the pleckstrin homology domain of beta-spectrin. The method is called ARIA for Ambiguous Restraints for Iterative Assignment. The starting point for ARIA is an almost complete assignment of the proton chemical shifts, and a list of partially assigned NOEs, mostly sequential and secondary structure NOEs. The restraint list is then augmented by automatically interpreting peak lists generated by automated peak-picking. The central task of ARIA is the assignment of ambiguous NOEs during the structure calculation using a combination of ambiguous distance restraints and an iterative assignment strategy. In addition, ARIA calibrates ambiguous NOEs to derive distance restraints, merges overlapping data sets to remove duplicate information, and uses empirical rules to identify erroneous peaks. While the distance restraints for the structure calculations were exclusively extracted from homonuclear 2D experiments, ARIA is especially suited for the analysis of multidimensional spectra. Applied to the pleckstrin homology domain, ARIA generated structures of good quality, and of sufficiently high accuracy to solve the X-ray crystal structure of the same domain by molecular replacement. The comparison of the free NMR solution structure to the X-ray structure, which is complexed to D-myo-inositol-1,4,5-triphosphate, shows that the ligand primarily induces a disorder-order transition in the binding loops, which are disordered in the NMR ensemble but well ordered in the crystal. The structural core of the protein is unaffected, as evidenced by a backbone root-mean-square difference between the average NMR coordinates and the X-ray crystal structure for the secondary structure elements of less than 0.6 A. ; save_ ################################## # Molecular system description # ################################## save_mSin3B-PAH2_Mad1 _Saveframe_category molecular_system _Mol_system_name 'mSin3B-PAH2 complexed to Mad1' _Abbreviation_common 'mSin3B-PAH2 Mad1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label PAH2 $PAH2 Mad1 $Mad1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state heterodimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'transcriptional regulator' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PAH2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'mSin3B-PAH2 domain' _Abbreviation_common mSin3B-PAH2 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 105 _Mol_residue_sequence ; ESDSVEFNNAISYVNKIKTR FLDHPEIYRSFLEILHTYQK EQLHTKGRPFRGMSEEEVFT EVANLFRGQEDLLSEFGQFL PEAKRSLFTGNGSAEMNSGQ KNEEK ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 SER 3 ASP 4 SER 5 VAL 6 GLU 7 PHE 8 ASN 9 ASN 10 ALA 11 ILE 12 SER 13 TYR 14 VAL 15 ASN 16 LYS 17 ILE 18 LYS 19 THR 20 ARG 21 PHE 22 LEU 23 ASP 24 HIS 25 PRO 26 GLU 27 ILE 28 TYR 29 ARG 30 SER 31 PHE 32 LEU 33 GLU 34 ILE 35 LEU 36 HIS 37 THR 38 TYR 39 GLN 40 LYS 41 GLU 42 GLN 43 LEU 44 HIS 45 THR 46 LYS 47 GLY 48 ARG 49 PRO 50 PHE 51 ARG 52 GLY 53 MET 54 SER 55 GLU 56 GLU 57 GLU 58 VAL 59 PHE 60 THR 61 GLU 62 VAL 63 ALA 64 ASN 65 LEU 66 PHE 67 ARG 68 GLY 69 GLN 70 GLU 71 ASP 72 LEU 73 LEU 74 SER 75 GLU 76 PHE 77 GLY 78 GLN 79 PHE 80 LEU 81 PRO 82 GLU 83 ALA 84 LYS 85 ARG 86 SER 87 LEU 88 PHE 89 THR 90 GLY 91 ASN 92 GLY 93 SER 94 ALA 95 GLU 96 MET 97 ASN 98 SER 99 GLY 100 GLN 101 LYS 102 ASN 103 GLU 104 GLU 105 LYS 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 GenBank EDL90864 'rCG38713, isoform CRA_f [Rattus norvegicus]' 100.00 841 98.10 98.10 1.92e-54 GenBank EDL90863 'rCG38713, isoform CRA_e [Rattus norvegicus]' 100.00 231 98.10 98.10 1.12e-53 GenBank EDL10815 'transcriptional regulator, SIN3B (yeast), isoform CRA_c [Mus musculus]' 100.00 893 99.05 99.05 4.64e-55 GenBank AAH51536 'Sin3b protein [Mus musculus]' 100.00 190 99.05 99.05 1.52e-54 PDB 2F05 'Solution Structure Of Free Pah2 Domain Of Msin3b' 100.00 105 99.05 99.05 4.80e-54 PDB 1PD7 'Extended Sid Of Mad1 Bound To The Pah2 Domain Of Msin3b' 80.00 85 100.00 100.00 4.32e-42 PDB 1E91 'Structure Of The Complex Of The Mad1-Sin3b Interaction Domains' 80.00 85 100.00 100.00 4.32e-42 BMRB 6899 'PAH2 domain' 100.00 105 100.00 100.00 1.69e-54 BMRB 5808 'PAH2 domain' 100.00 105 100.00 100.00 1.69e-54 BMRB 5457 mSin3B 100.00 105 100.00 100.00 1.69e-54 BMRB 4874 'mSin3B-PAH2 domain' 100.00 105 100.00 100.00 1.69e-54 stop_ save_ save_Mad1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Sin interaction domain of human Mad1' _Abbreviation_common Mad1-SID _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 13 _Mol_residue_sequence NIQMLLEAADYLE loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 201 ASN 2 202 ILE 3 203 GLN 4 204 MET 5 205 LEU 6 206 LEU 7 207 GLU 8 208 ALA 9 209 ALA 10 210 ASP 11 211 TYR 12 212 LEU 13 213 GLU stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2003-08-21 save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $PAH2 mouse 10090 Eukaryota Metazoa Mus musculus SIN3B $Mad1 human 9606 Eukaryota Metazoa Homo sapiens MAD1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $PAH2 'recombinant technology' 'E. coli' . . pBL21 plasmid pGEX2T $Mad1 'chemical synthesis' . . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Typical_sample _Saveframe_category sample _Sample_type solution _Details 'Trace amounts of Sodium azide and protease inhibitors were added for conservation' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PAH2 1.0 mM '[U-100% 13C; U-100% 15N]' $Mad1 1.0 mM . Potassium_Phosphate 50 mM . NaN3 . mM . 'protease inhibitors' . mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.7 loop_ _Task 'Data processing' stop_ _Details . _Citation_label $ref_1 save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.9 loop_ _Task 'Spectral analysis' stop_ _Details . _Citation_label $ref_2 save_ save_CNS _Saveframe_category software _Name CNS _Version 1.0 loop_ _Task 'structure calculations' stop_ _Details . _Citation_label $ref_3 save_ save_ARIA _Saveframe_category software _Name ARIA _Version 1.0 loop_ _Task 'structure calculations and iterative NOE-assignment' stop_ _Details . _Citation_label $ref_4 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 750 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_13C-NOESY-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-NOESY-HSQC _Sample_label $Typical_sample save_ save_15N-NOESY-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-NOESY-HSQC _Sample_label $Typical_sample save_ save_15N-HMQC-NOESY-HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HMQC-NOESY-HSQC _Sample_label $Typical_sample save_ save_(13C-FILTERED)-NOESY-(13C-EDITED)-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name (13C-FILTERED)-NOESY-(13C-EDITED)-HSQC _Sample_label $Typical_sample save_ save_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $Typical_sample save_ save_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $Typical_sample save_ save_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $Typical_sample save_ save_CBCA(CO)NNH_8 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NNH _Sample_label $Typical_sample save_ save_HNCACB_9 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $Typical_sample save_ save_(H)CCH-TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CCH-TOCSY _Sample_label $Typical_sample save_ save_15N-HSQC_11 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _Sample_label $Typical_sample save_ save_13C-HSQC_12 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-HSQC _Sample_label $Typical_sample save_ save_(13C/15N-FILTERED)-NOESY_13 _Saveframe_category NMR_applied_experiment _Experiment_name (13C/15N-FILTERED)-NOESY _Sample_label $Typical_sample save_ save_(13C/15N-FILTERED)-TOCSY_14 _Saveframe_category NMR_applied_experiment _Experiment_name (13C/15N-FILTERED)-TOCSY _Sample_label $Typical_sample save_ save_HNHA_15 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label $Typical_sample save_ save_HBHA(CBCACO)NNH_16 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CBCACO)NNH _Sample_label $Typical_sample save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.3 0.1 n/a temperature 293 1 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 0.0 internal direct . . . . DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 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_assigned_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $Typical_sample stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name PAH2 _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 GLU N N 122.940 0.1 1 2 . 1 GLU H H 8.895 0.03 1 3 . 1 GLU CA C 57.555 0.1 1 4 . 1 GLU HA H 4.264 0.03 1 5 . 1 GLU CB C 29.435 0.1 1 6 . 1 GLU HB2 H 1.947 0.03 2 7 . 1 GLU HB3 H 2.050 0.03 2 8 . 1 GLU CG C 36.331 0.1 1 9 . 1 GLU HG2 H 2.261 0.03 1 10 . 1 GLU HG3 H 2.261 0.03 1 11 . 1 GLU C C 177.015 0.1 1 12 . 2 SER N N 115.629 0.1 1 13 . 2 SER H H 8.225 0.03 1 14 . 2 SER CA C 59.068 0.1 1 15 . 2 SER HA H 4.309 0.03 1 16 . 2 SER CB C 63.587 0.1 1 17 . 2 SER HB2 H 3.774 0.03 2 18 . 2 SER HB3 H 3.848 0.03 2 19 . 2 SER C C 174.535 0.1 1 20 . 3 ASP N N 122.099 0.1 1 21 . 3 ASP H H 8.185 0.03 1 22 . 3 ASP CA C 54.698 0.1 1 23 . 3 ASP HA H 4.649 0.03 1 24 . 3 ASP CB C 41.076 0.1 1 25 . 3 ASP HB2 H 2.705 0.03 1 26 . 3 ASP HB3 H 2.705 0.03 1 27 . 3 ASP C C 176.534 0.1 1 28 . 4 SER N N 115.866 0.1 1 29 . 4 SER H H 8.141 0.03 1 30 . 4 SER CA C 58.532 0.1 1 31 . 4 SER HA H 4.526 0.03 1 32 . 4 SER CB C 63.834 0.1 1 33 . 4 SER HB2 H 4.006 0.03 2 34 . 4 SER HB3 H 4.075 0.03 2 35 . 4 SER C C 175.519 0.1 1 36 . 5 VAL N N 124.945 0.1 1 37 . 5 VAL H H 8.411 0.03 1 38 . 5 VAL CA C 65.491 0.1 1 39 . 5 VAL HA H 3.848 0.03 1 40 . 5 VAL CB C 32.024 0.1 1 41 . 5 VAL HB H 2.079 0.03 1 42 . 5 VAL HG1 H 0.930 0.03 1 43 . 5 VAL HG2 H 1.025 0.03 1 44 . 5 VAL CG1 C 21.058 0.1 1 45 . 5 VAL CG2 C 21.947 0.1 1 46 . 5 VAL C C 177.947 0.1 1 47 . 6 GLU N N 120.522 0.1 1 48 . 6 GLU H H 8.594 0.03 1 49 . 6 GLU CA C 59.361 0.1 1 50 . 6 GLU HA H 4.212 0.03 1 51 . 6 GLU CB C 29.538 0.1 1 52 . 6 GLU HB2 H 2.055 0.03 1 53 . 6 GLU HB3 H 2.055 0.03 1 54 . 6 GLU CG C 36.882 0.1 1 55 . 6 GLU HG2 H 2.363 0.03 1 56 . 6 GLU HG3 H 2.363 0.03 1 57 . 6 GLU C C 178.794 0.1 1 58 . 7 PHE N N 121.799 0.1 1 59 . 7 PHE H H 8.535 0.03 1 60 . 7 PHE CA C 61.181 0.1 1 61 . 7 PHE HA H 4.537 0.03 1 62 . 7 PHE CB C 38.982 0.1 1 63 . 7 PHE HB2 H 3.025 0.03 2 64 . 7 PHE HB3 H 3.283 0.03 2 65 . 7 PHE HD1 H 7.212 0.03 4 66 . 7 PHE HD2 H 7.212 0.03 4 67 . 7 PHE HE1 H 7.212 0.03 4 68 . 7 PHE HE2 H 7.212 0.03 4 69 . 7 PHE HZ H 7.212 0.03 4 70 . 7 PHE CD1 C 132.286 0.1 4 71 . 7 PHE CE1 C 132.286 0.1 4 72 . 7 PHE C C 177.570 0.1 1 73 . 8 ASN N N 117.116 0.1 1 74 . 8 ASN H H 8.379 0.03 1 75 . 8 ASN CA C 56.544 0.1 1 76 . 8 ASN HA H 4.334 0.03 1 77 . 8 ASN CB C 37.953 0.1 1 78 . 8 ASN HB2 H 2.780 0.03 2 79 . 8 ASN HB3 H 2.938 0.03 2 80 . 8 ASN ND2 N 112.590 0.1 1 81 . 8 ASN HD21 H 6.995 0.03 2 82 . 8 ASN HD22 H 7.565 0.03 2 83 . 8 ASN C C 178.480 0.1 1 84 . 9 ASN N N 120.183 0.1 1 85 . 9 ASN H H 8.371 0.03 1 86 . 9 ASN CA C 55.986 0.1 1 87 . 9 ASN HA H 4.593 0.03 1 88 . 9 ASN CB C 37.859 0.1 1 89 . 9 ASN HB2 H 2.999 0.03 2 90 . 9 ASN HB3 H 3.121 0.03 2 91 . 9 ASN ND2 N 112.683 0.1 1 92 . 9 ASN HD21 H 6.907 0.03 2 93 . 9 ASN HD22 H 7.883 0.03 2 94 . 9 ASN C C 177.894 0.1 1 95 . 10 ALA N N 125.084 0.1 1 96 . 10 ALA H H 8.162 0.03 1 97 . 10 ALA CA C 55.769 0.1 1 98 . 10 ALA HA H 4.116 0.03 1 99 . 10 ALA HB H 1.440 0.03 1 100 . 10 ALA CB C 18.377 0.1 1 101 . 10 ALA C C 178.365 0.1 1 102 . 11 ILE N N 118.227 0.1 1 103 . 11 ILE H H 8.273 0.03 1 104 . 11 ILE CA C 65.587 0.1 1 105 . 11 ILE HA H 3.435 0.03 1 106 . 11 ILE CB C 37.973 0.1 1 107 . 11 ILE HB H 1.761 0.03 1 108 . 11 ILE HG2 H 0.897 0.03 1 109 . 11 ILE CG2 C 17.570 0.1 1 110 . 11 ILE CG1 C 28.694 0.1 1 111 . 11 ILE HG12 H 0.545 0.03 2 112 . 11 ILE HG13 H 1.144 0.03 2 113 . 11 ILE HD1 H 0.371 0.03 1 114 . 11 ILE CD1 C 13.673 0.1 1 115 . 11 ILE C C 177.779 0.1 1 116 . 12 SER N N 113.677 0.1 1 117 . 12 SER H H 8.013 0.03 1 118 . 12 SER CA C 61.709 0.1 1 119 . 12 SER HA H 4.185 0.03 1 120 . 12 SER CB C 62.640 0.1 1 121 . 12 SER HB2 H 4.048 0.03 1 122 . 12 SER HB3 H 4.048 0.03 1 123 . 12 SER C C 177.193 0.1 1 124 . 13 TYR N N 122.570 0.1 1 125 . 13 TYR H H 8.127 0.03 1 126 . 13 TYR CA C 61.181 0.1 1 127 . 13 TYR HA H 4.439 0.03 1 128 . 13 TYR CB C 38.651 0.1 1 129 . 13 TYR HB2 H 2.862 0.03 2 130 . 13 TYR HB3 H 3.485 0.03 2 131 . 13 TYR HD1 H 7.003 0.03 1 132 . 13 TYR HD2 H 7.003 0.03 1 133 . 13 TYR HE1 H 6.826 0.03 1 134 . 13 TYR HE2 H 6.826 0.03 1 135 . 13 TYR CD1 C 133.572 0.1 1 136 . 13 TYR CE1 C 118.096 0.1 1 137 . 13 TYR C C 176.869 0.1 1 138 . 14 VAL N N 118.191 0.1 1 139 . 14 VAL H H 8.589 0.03 1 140 . 14 VAL CA C 67.693 0.1 1 141 . 14 VAL HA H 3.386 0.03 1 142 . 14 VAL CB C 31.030 0.1 1 143 . 14 VAL HB H 2.055 0.03 1 144 . 14 VAL HG1 H 1.175 0.03 1 145 . 14 VAL HG2 H 1.246 0.03 1 146 . 14 VAL CG1 C 23.915 0.1 1 147 . 14 VAL CG2 C 24.461 0.1 1 148 . 14 VAL C C 178.208 0.1 1 149 . 15 ASN N N 116.894 0.1 1 150 . 15 ASN H H 8.580 0.03 1 151 . 15 ASN CA C 56.213 0.1 1 152 . 15 ASN HA H 4.382 0.03 1 153 . 15 ASN CB C 38.816 0.1 1 154 . 15 ASN HB2 H 2.772 0.03 2 155 . 15 ASN HB3 H 2.805 0.03 2 156 . 15 ASN ND2 N 112.498 0.1 1 157 . 15 ASN HD21 H 6.740 0.03 2 158 . 15 ASN HD22 H 7.461 0.03 2 159 . 15 ASN C C 178.020 0.1 1 160 . 16 LYS N N 123.367 0.1 1 161 . 16 LYS H H 7.959 0.03 1 162 . 16 LYS CA C 60.189 0.1 1 163 . 16 LYS HA H 3.856 0.03 1 164 . 16 LYS CB C 32.128 0.1 1 165 . 16 LYS HB2 H 1.962 0.03 1 166 . 16 LYS HB3 H 1.962 0.03 1 167 . 16 LYS CG C 25.403 0.1 1 168 . 16 LYS HG2 H 1.144 0.03 2 169 . 16 LYS HG3 H 1.535 0.03 2 170 . 16 LYS CD C 30.279 0.1 1 171 . 16 LYS HD2 H 1.659 0.03 1 172 . 16 LYS HD3 H 1.659 0.03 1 173 . 16 LYS CE C 41.633 0.1 1 174 . 16 LYS HE2 H 2.818 0.03 2 175 . 16 LYS HE3 H 2.887 0.03 2 176 . 16 LYS C C 179.014 0.1 1 177 . 17 ILE N N 120.174 0.1 1 178 . 17 ILE H H 7.648 0.03 1 179 . 17 ILE CA C 65.097 0.1 1 180 . 17 ILE HA H 3.134 0.03 1 181 . 17 ILE CB C 38.091 0.1 1 182 . 17 ILE HB H 1.839 0.03 1 183 . 17 ILE HG2 H 0.806 0.03 1 184 . 17 ILE CG2 C 18.459 0.1 1 185 . 17 ILE CG1 C 28.430 0.1 1 186 . 17 ILE HG12 H 0.366 0.03 2 187 . 17 ILE HG13 H 1.060 0.03 2 188 . 17 ILE HD1 H 0.014 0.03 1 189 . 17 ILE CD1 C 14.265 0.1 1 190 . 17 ILE C C 177.026 0.1 1 191 . 18 LYS N N 119.439 0.1 1 192 . 18 LYS H H 8.367 0.03 1 193 . 18 LYS CA C 59.858 0.1 1 194 . 18 LYS HA H 3.096 0.03 1 195 . 18 LYS CB C 32.710 0.1 1 196 . 18 LYS HB2 H 1.247 0.03 2 197 . 18 LYS HB3 H 1.602 0.03 2 198 . 18 LYS CG C 24.899 0.1 1 199 . 18 LYS HG2 H 0.518 0.03 2 200 . 18 LYS HG3 H 0.725 0.03 2 201 . 18 LYS CD C 29.468 0.1 1 202 . 18 LYS HD2 H 1.382 0.03 2 203 . 18 LYS HD3 H 1.462 0.03 2 204 . 18 LYS CE C 42.135 0.1 1 205 . 18 LYS HE2 H 2.803 0.03 1 206 . 18 LYS HE3 H 2.803 0.03 1 207 . 18 LYS C C 179.799 0.1 1 208 . 19 THR N N 111.327 0.1 1 209 . 19 THR H H 8.092 0.03 1 210 . 19 THR CA C 65.657 0.1 1 211 . 19 THR HA H 3.763 0.03 1 212 . 19 THR CB C 69.002 0.1 1 213 . 19 THR HB H 4.076 0.03 1 214 . 19 THR HG2 H 1.161 0.03 1 215 . 19 THR CG2 C 21.299 0.1 1 216 . 19 THR C C 176.691 0.1 1 217 . 20 ARG N N 124.489 0.1 1 218 . 20 ARG H H 8.000 0.03 1 219 . 20 ARG CA C 56.267 0.1 1 220 . 20 ARG HA H 3.796 0.03 1 221 . 20 ARG CB C 27.550 0.1 1 222 . 20 ARG HB2 H 1.109 0.03 2 223 . 20 ARG HB3 H 1.608 0.03 2 224 . 20 ARG CG C 24.382 0.1 1 225 . 20 ARG HG2 H 0.475 0.03 2 226 . 20 ARG HG3 H 0.890 0.03 2 227 . 20 ARG CD C 39.800 0.1 1 228 . 20 ARG HD2 H 3.047 0.03 1 229 . 20 ARG HD3 H 3.047 0.03 1 230 . 20 ARG C C 177.528 0.1 1 231 . 21 PHE N N 113.100 0.1 1 232 . 21 PHE H H 7.208 0.03 1 233 . 21 PHE CA C 56.955 0.1 1 234 . 21 PHE HA H 4.987 0.03 1 235 . 21 PHE CB C 37.988 0.1 1 236 . 21 PHE HB2 H 2.434 0.03 2 237 . 21 PHE HB3 H 3.933 0.03 2 238 . 21 PHE HD1 H 7.301 0.03 1 239 . 21 PHE HD2 H 7.301 0.03 1 240 . 21 PHE HE1 H 6.887 0.03 1 241 . 21 PHE HE2 H 6.887 0.03 1 242 . 21 PHE CD1 C 132.611 0.1 1 243 . 21 PHE CE1 C 131.420 0.1 1 244 . 21 PHE C C 177.821 0.1 1 245 . 22 LEU N N 126.379 0.1 1 246 . 22 LEU H H 7.220 0.03 1 247 . 22 LEU CA C 59.068 0.1 1 248 . 22 LEU HA H 4.017 0.03 1 249 . 22 LEU CB C 42.296 0.1 1 250 . 22 LEU HB2 H 1.585 0.03 2 251 . 22 LEU HB3 H 1.814 0.03 2 252 . 22 LEU CG C 26.548 0.1 1 253 . 22 LEU HG H 1.919 0.03 1 254 . 22 LEU HD1 H 0.922 0.03 1 255 . 22 LEU HD2 H 0.868 0.03 1 256 . 22 LEU CD1 C 24.568 0.1 1 257 . 22 LEU CD2 C 24.237 0.1 1 258 . 22 LEU C C 178.261 0.1 1 259 . 23 ASP N N 112.963 0.1 1 260 . 23 ASP H H 8.667 0.03 1 261 . 23 ASP CA C 54.462 0.1 1 262 . 23 ASP HA H 4.548 0.03 1 263 . 23 ASP CB C 40.232 0.1 1 264 . 23 ASP HB2 H 2.541 0.03 2 265 . 23 ASP HB3 H 2.577 0.03 2 266 . 23 ASP C C 175.697 0.1 1 267 . 24 HIS N N 117.097 0.1 1 268 . 24 HIS H H 7.696 0.03 1 269 . 24 HIS CA C 54.208 0.1 1 270 . 24 HIS HA H 5.201 0.03 1 271 . 24 HIS CB C 30.362 0.1 1 272 . 24 HIS HB2 H 2.993 0.03 2 273 . 24 HIS HB3 H 3.443 0.03 2 274 . 24 HIS CD2 C 120.712 0.1 1 275 . 24 HIS CE1 C 137.278 0.1 1 276 . 24 HIS HD2 H 7.380 0.03 1 277 . 24 HIS HE1 H 8.556 0.03 1 278 . 25 PRO CD C 50.414 0.1 1 279 . 25 PRO CA C 65.268 0.1 1 280 . 25 PRO HA H 4.456 0.03 1 281 . 25 PRO CB C 31.676 0.1 1 282 . 25 PRO HB2 H 2.209 0.03 2 283 . 25 PRO HB3 H 2.447 0.03 2 284 . 25 PRO CG C 27.637 0.1 1 285 . 25 PRO HG2 H 2.113 0.03 2 286 . 25 PRO HG3 H 2.175 0.03 2 287 . 25 PRO HD2 H 3.525 0.03 2 288 . 25 PRO HD3 H 3.728 0.03 2 289 . 25 PRO C C 177.507 0.1 1 290 . 26 GLU N N 121.595 0.1 1 291 . 26 GLU H H 10.319 0.03 1 292 . 26 GLU CA C 59.195 0.1 1 293 . 26 GLU HA H 4.218 0.03 1 294 . 26 GLU CB C 27.219 0.1 1 295 . 26 GLU HB2 H 2.048 0.03 2 296 . 26 GLU HB3 H 2.184 0.03 2 297 . 26 GLU CG C 35.503 0.1 1 298 . 26 GLU HG2 H 2.337 0.03 2 299 . 26 GLU HG3 H 2.555 0.03 2 300 . 26 GLU C C 178.836 0.1 1 301 . 27 ILE N N 123.579 0.1 1 302 . 27 ILE H H 8.206 0.03 1 303 . 27 ILE CA C 64.576 0.1 1 304 . 27 ILE HA H 3.674 0.03 1 305 . 27 ILE CB C 36.924 0.1 1 306 . 27 ILE HB H 1.511 0.03 1 307 . 27 ILE HG2 H -0.023 0.03 1 308 . 27 ILE CG2 C 15.542 0.1 1 309 . 27 ILE CG1 C 28.694 0.1 1 310 . 27 ILE HG12 H 1.149 0.03 2 311 . 27 ILE HG13 H 1.546 0.03 2 312 . 27 ILE HD1 H 0.742 0.03 1 313 . 27 ILE CD1 C 11.781 0.1 1 314 . 27 ILE C C 177.612 0.1 1 315 . 28 TYR N N 119.640 0.1 1 316 . 28 TYR H H 6.701 0.03 1 317 . 28 TYR CA C 61.018 0.1 1 318 . 28 TYR HA H 4.203 0.03 1 319 . 28 TYR CB C 38.982 0.1 1 320 . 28 TYR HB2 H 3.136 0.03 2 321 . 28 TYR HB3 H 3.262 0.03 2 322 . 28 TYR HD1 H 7.045 0.03 1 323 . 28 TYR HD2 H 7.045 0.03 1 324 . 28 TYR HE1 H 6.751 0.03 1 325 . 28 TYR HE2 H 6.751 0.03 1 326 . 28 TYR CD1 C 132.838 0.1 1 327 . 28 TYR CE1 C 118.377 0.1 1 328 . 28 TYR C C 176.795 0.1 1 329 . 29 ARG N N 116.094 0.1 1 330 . 29 ARG H H 8.298 0.03 1 331 . 29 ARG CA C 59.361 0.1 1 332 . 29 ARG HA H 3.753 0.03 1 333 . 29 ARG CB C 29.373 0.1 1 334 . 29 ARG HB2 H 1.894 0.03 2 335 . 29 ARG HB3 H 1.957 0.03 2 336 . 29 ARG CG C 27.219 0.1 1 337 . 29 ARG HG2 H 1.672 0.03 2 338 . 29 ARG HG3 H 1.888 0.03 2 339 . 29 ARG CD C 43.025 0.1 1 340 . 29 ARG HD2 H 3.172 0.03 2 341 . 29 ARG HD3 H 3.239 0.03 2 342 . 29 ARG C C 179.631 0.1 1 343 . 30 SER N N 117.116 0.1 1 344 . 30 SER H H 8.271 0.03 1 345 . 30 SER CA C 62.674 0.1 1 346 . 30 SER HA H 4.165 0.03 1 347 . 30 SER CB C 63.006 0.1 1 348 . 30 SER HB2 H 3.884 0.03 1 349 . 30 SER HB3 H 3.884 0.03 1 350 . 30 SER C C 175.634 0.1 1 351 . 31 PHE N N 123.907 0.1 1 352 . 31 PHE H H 8.099 0.03 1 353 . 31 PHE CA C 60.917 0.1 1 354 . 31 PHE HA H 3.879 0.03 1 355 . 31 PHE CB C 38.319 0.1 1 356 . 31 PHE HB2 H 3.026 0.03 2 357 . 31 PHE HB3 H 3.497 0.03 2 358 . 31 PHE HD1 H 6.841 0.03 1 359 . 31 PHE HD2 H 6.841 0.03 1 360 . 31 PHE CD1 C 132.591 0.1 1 361 . 31 PHE C C 175.487 0.1 1 362 . 32 LEU N N 116.662 0.1 1 363 . 32 LEU H H 7.637 0.03 1 364 . 32 LEU CA C 57.582 0.1 1 365 . 32 LEU HA H 3.455 0.03 1 366 . 32 LEU CB C 40.946 0.1 1 367 . 32 LEU HB2 H 1.147 0.03 2 368 . 32 LEU HB3 H 1.765 0.03 2 369 . 32 LEU CG C 26.225 0.1 1 370 . 32 LEU HG H 1.393 0.03 1 371 . 32 LEU HD1 H 0.614 0.03 1 372 . 32 LEU HD2 H 0.612 0.03 1 373 . 32 LEU CD1 C 25.503 0.1 1 374 . 32 LEU CD2 C 21.605 0.1 1 375 . 32 LEU C C 179.286 0.1 1 376 . 33 GLU N N 119.617 0.1 1 377 . 33 GLU H H 8.061 0.03 1 378 . 33 GLU CA C 59.596 0.1 1 379 . 33 GLU HA H 4.093 0.03 1 380 . 33 GLU CB C 29.297 0.1 1 381 . 33 GLU HB2 H 2.138 0.03 1 382 . 33 GLU HB3 H 2.138 0.03 1 383 . 33 GLU CG C 36.061 0.1 1 384 . 33 GLU C C 179.788 0.1 1 385 . 34 ILE N N 122.488 0.1 1 386 . 34 ILE H H 8.001 0.03 1 387 . 34 ILE CA C 65.129 0.1 1 388 . 34 ILE HA H 3.701 0.03 1 389 . 34 ILE CB C 37.988 0.1 1 390 . 34 ILE HB H 1.808 0.03 1 391 . 34 ILE HG2 H 0.768 0.03 1 392 . 34 ILE CG2 C 17.935 0.1 1 393 . 34 ILE CG1 C 28.876 0.1 1 394 . 34 ILE HG12 H 1.049 0.03 2 395 . 34 ILE HG13 H 1.749 0.03 2 396 . 34 ILE HD1 H 0.703 0.03 1 397 . 34 ILE CD1 C 14.835 0.1 1 398 . 34 ILE C C 178.145 0.1 1 399 . 35 LEU N N 117.570 0.1 1 400 . 35 LEU H H 7.330 0.03 1 401 . 35 LEU CA C 58.180 0.1 1 402 . 35 LEU HA H 3.837 0.03 1 403 . 35 LEU CB C 40.152 0.1 1 404 . 35 LEU HB2 H 1.141 0.03 2 405 . 35 LEU HB3 H 1.724 0.03 2 406 . 35 LEU CG C 25.921 0.1 1 407 . 35 LEU HG H 1.363 0.03 1 408 . 35 LEU HD1 H 0.416 0.03 1 409 . 35 LEU HD2 H 0.554 0.03 1 410 . 35 LEU CD1 C 25.822 0.1 1 411 . 35 LEU CD2 C 21.445 0.1 1 412 . 35 LEU C C 179.161 0.1 1 413 . 36 HIS N N 116.939 0.1 1 414 . 36 HIS H H 8.724 0.03 1 415 . 36 HIS CA C 60.024 0.1 1 416 . 36 HIS HA H 4.218 0.03 1 417 . 36 HIS CB C 29.234 0.1 1 418 . 36 HIS HB2 H 3.183 0.03 2 419 . 36 HIS HB3 H 3.300 0.03 2 420 . 36 HIS CD2 C 120.930 0.1 1 421 . 36 HIS CE1 C 137.787 0.1 1 422 . 36 HIS HD2 H 7.097 0.03 1 423 . 36 HIS HE1 H 8.355 0.03 1 424 . 36 HIS C C 178.093 0.1 1 425 . 37 THR N N 119.069 0.1 1 426 . 37 THR H H 8.551 0.03 1 427 . 37 THR CA C 67.161 0.1 1 428 . 37 THR HA H 3.861 0.03 1 429 . 37 THR CB C 68.480 0.1 1 430 . 37 THR HB H 4.439 0.03 1 431 . 37 THR HG2 H 1.274 0.03 1 432 . 37 THR CG2 C 21.881 0.1 1 433 . 37 THR C C 175.466 0.1 1 434 . 38 TYR N N 122.079 0.1 1 435 . 38 TYR H H 8.190 0.03 1 436 . 38 TYR CA C 61.846 0.1 1 437 . 38 TYR HA H 4.134 0.03 1 438 . 38 TYR CB C 38.202 0.1 1 439 . 38 TYR HB2 H 3.129 0.03 2 440 . 38 TYR HB3 H 3.210 0.03 2 441 . 38 TYR HD1 H 6.963 0.03 1 442 . 38 TYR HD2 H 6.963 0.03 1 443 . 38 TYR HE1 H 6.744 0.03 1 444 . 38 TYR HE2 H 6.744 0.03 1 445 . 38 TYR CD1 C 133.899 0.1 1 446 . 38 TYR CE1 C 118.865 0.1 1 447 . 38 TYR C C 177.559 0.1 1 448 . 39 GLN N N 118.546 0.1 1 449 . 39 GLN H H 8.361 0.03 1 450 . 39 GLN CA C 58.190 0.1 1 451 . 39 GLN HA H 3.892 0.03 1 452 . 39 GLN CB C 29.222 0.1 1 453 . 39 GLN HB2 H 2.114 0.03 2 454 . 39 GLN HB3 H 2.158 0.03 2 455 . 39 GLN CG C 33.916 0.1 1 456 . 39 GLN HG2 H 2.353 0.03 2 457 . 39 GLN HG3 H 2.386 0.03 2 458 . 39 GLN NE2 N 109.814 0.1 1 459 . 39 GLN HE21 H 6.822 0.03 2 460 . 39 GLN HE22 H 7.382 0.03 2 461 . 39 GLN C C 178.564 0.1 1 462 . 40 LYS N N 119.660 0.1 1 463 . 40 LYS H H 8.154 0.03 1 464 . 40 LYS CA C 59.068 0.1 1 465 . 40 LYS HA H 4.022 0.03 1 466 . 40 LYS CB C 32.392 0.1 1 467 . 40 LYS HB2 H 1.940 0.03 1 468 . 40 LYS HB3 H 1.940 0.03 1 469 . 40 LYS CG C 25.120 0.1 1 470 . 40 LYS HG2 H 1.464 0.03 1 471 . 40 LYS HG3 H 1.464 0.03 1 472 . 40 LYS CD C 29.373 0.1 1 473 . 40 LYS HD2 H 1.660 0.03 1 474 . 40 LYS HD3 H 1.660 0.03 1 475 . 40 LYS CE C 42.079 0.1 1 476 . 40 LYS HE2 H 2.927 0.03 1 477 . 40 LYS HE3 H 2.927 0.03 1 478 . 40 LYS C C 178.888 0.1 1 479 . 41 GLU N N 117.633 0.1 1 480 . 41 GLU H H 7.871 0.03 1 481 . 41 GLU CA C 57.373 0.1 1 482 . 41 GLU HA H 4.214 0.03 1 483 . 41 GLU CB C 29.297 0.1 1 484 . 41 GLU HB2 H 2.027 0.03 1 485 . 41 GLU HB3 H 2.027 0.03 1 486 . 41 GLU C C 177.654 0.1 1 487 . 42 GLN N N 117.089 0.1 1 488 . 42 GLN H H 7.665 0.03 1 489 . 42 GLN CA C 56.195 0.1 1 490 . 42 GLN HA H 4.080 0.03 1 491 . 42 GLN CB C 28.547 0.1 1 492 . 42 GLN HB2 H 1.899 0.03 2 493 . 42 GLN HB3 H 2.082 0.03 2 494 . 42 GLN CG C 33.249 0.1 1 495 . 42 GLN HG2 H 2.186 0.03 1 496 . 42 GLN HG3 H 2.186 0.03 1 497 . 42 GLN NE2 N 114.812 0.1 1 498 . 42 GLN HE21 H 6.779 0.03 2 499 . 42 GLN HE22 H 6.989 0.03 2 500 . 42 GLN C C 176.942 0.1 1 501 . 43 LEU N N 119.440 0.1 1 502 . 43 LEU H H 7.528 0.03 1 503 . 43 LEU CA C 55.487 0.1 1 504 . 43 LEU HA H 4.256 0.03 1 505 . 43 LEU CB C 42.293 0.1 1 506 . 43 LEU HB2 H 1.485 0.03 2 507 . 43 LEU HB3 H 1.674 0.03 2 508 . 43 LEU CG C 26.722 0.1 1 509 . 43 LEU HG H 1.625 0.03 1 510 . 43 LEU HD1 H 0.900 0.03 1 511 . 43 LEU HD2 H 0.836 0.03 1 512 . 43 LEU CD1 C 25.138 0.1 1 513 . 43 LEU CD2 C 23.243 0.1 1 514 . 43 LEU C C 177.277 0.1 1 515 . 44 HIS N N 119.393 0.1 1 516 . 44 HIS H H 8.237 0.03 1 517 . 44 HIS CA C 55.877 0.1 1 518 . 44 HIS HA H 4.686 0.03 1 519 . 44 HIS CB C 29.607 0.1 1 520 . 44 HIS HB2 H 3.091 0.03 2 521 . 44 HIS HB3 H 3.176 0.03 2 522 . 44 HIS CD2 C 120.494 0.1 1 523 . 44 HIS CE1 C 137.857 0.1 1 524 . 44 HIS HD2 H 7.078 0.03 1 525 . 44 HIS HE1 H 8.036 0.03 1 526 . 44 HIS C C 175.990 0.1 1 527 . 45 THR N N 114.477 0.1 1 528 . 45 THR H H 8.005 0.03 1 529 . 45 THR CA C 62.237 0.1 1 530 . 45 THR HA H 4.294 0.03 1 531 . 45 THR CB C 70.002 0.1 1 532 . 45 THR HB H 4.158 0.03 1 533 . 45 THR HG2 H 1.173 0.03 1 534 . 45 THR CG2 C 21.810 0.1 1 535 . 45 THR C C 174.587 0.1 1 536 . 46 LYS N N 124.157 0.1 1 537 . 46 LYS H H 8.381 0.03 1 538 . 46 LYS CA C 57.373 0.1 1 539 . 46 LYS HA H 4.182 0.03 1 540 . 46 LYS CB C 32.392 0.1 1 541 . 46 LYS HB2 H 1.825 0.03 1 542 . 46 LYS HB3 H 1.825 0.03 1 543 . 46 LYS CG C 24.751 0.1 1 544 . 46 LYS HG2 H 1.396 0.03 1 545 . 46 LYS HG3 H 1.396 0.03 1 546 . 46 LYS CD C 29.146 0.1 1 547 . 46 LYS HD2 H 1.670 0.03 1 548 . 46 LYS HD3 H 1.670 0.03 1 549 . 46 LYS CE C 42.481 0.1 1 550 . 46 LYS HE2 H 2.943 0.03 1 551 . 46 LYS HE3 H 2.943 0.03 1 552 . 46 LYS C C 177.402 0.1 1 553 . 47 GLY N N 110.858 0.1 1 554 . 47 GLY H H 8.684 0.03 1 555 . 47 GLY CA C 45.278 0.1 1 556 . 47 GLY HA2 H 3.804 0.03 2 557 . 47 GLY HA3 H 4.074 0.03 2 558 . 47 GLY C C 173.844 0.1 1 559 . 48 ARG N N 120.742 0.1 1 560 . 48 ARG H H 7.871 0.03 1 561 . 48 ARG CA C 53.562 0.1 1 562 . 48 ARG HA H 4.697 0.03 1 563 . 48 ARG CB C 30.698 0.1 1 564 . 48 ARG HB2 H 1.697 0.03 2 565 . 48 ARG HB3 H 1.820 0.03 2 566 . 48 ARG CG C 26.722 0.1 1 567 . 48 ARG HG2 H 1.564 0.03 2 568 . 48 ARG HG3 H 1.608 0.03 2 569 . 48 ARG CD C 43.649 0.1 1 570 . 48 ARG HD2 H 3.153 0.03 1 571 . 48 ARG HD3 H 3.153 0.03 1 572 . 49 PRO CD C 50.580 0.1 1 573 . 49 PRO CA C 63.310 0.1 1 574 . 49 PRO HA H 4.417 0.03 1 575 . 49 PRO CB C 31.692 0.1 1 576 . 49 PRO HB2 H 1.797 0.03 2 577 . 49 PRO HB3 H 2.183 0.03 2 578 . 49 PRO CG C 27.350 0.1 1 579 . 49 PRO HG2 H 1.966 0.03 1 580 . 49 PRO HG3 H 1.966 0.03 1 581 . 49 PRO HD2 H 3.598 0.03 2 582 . 49 PRO HD3 H 3.767 0.03 2 583 . 49 PRO C C 176.167 0.1 1 584 . 50 PHE N N 120.496 0.1 1 585 . 50 PHE H H 8.182 0.03 1 586 . 50 PHE CA C 57.500 0.1 1 587 . 50 PHE HA H 4.606 0.03 1 588 . 50 PHE CB C 40.059 0.1 1 589 . 50 PHE HB2 H 3.030 0.03 1 590 . 50 PHE HB3 H 3.030 0.03 1 591 . 50 PHE HD1 H 7.162 0.03 1 592 . 50 PHE HD2 H 7.162 0.03 1 593 . 50 PHE CD1 C 132.373 0.1 1 594 . 50 PHE C C 175.037 0.1 1 595 . 51 ARG N N 124.076 0.1 1 596 . 51 ARG H H 8.336 0.03 1 597 . 51 ARG CA C 55.898 0.1 1 598 . 51 ARG HA H 4.299 0.03 1 599 . 51 ARG CB C 31.070 0.1 1 600 . 51 ARG HB2 H 1.669 0.03 2 601 . 51 ARG HB3 H 1.802 0.03 2 602 . 51 ARG CG C 26.839 0.1 1 603 . 51 ARG HG2 H 1.550 0.03 1 604 . 51 ARG HG3 H 1.550 0.03 1 605 . 51 ARG CD C 43.335 0.1 1 606 . 51 ARG HD2 H 3.152 0.03 1 607 . 51 ARG HD3 H 3.152 0.03 1 608 . 51 ARG C C 176.105 0.1 1 609 . 52 GLY N N 109.604 0.1 1 610 . 52 GLY H H 7.770 0.03 1 611 . 52 GLY CA C 44.947 0.1 1 612 . 52 GLY HA2 H 3.778 0.03 2 613 . 52 GLY HA3 H 3.968 0.03 2 614 . 52 GLY C C 173.300 0.1 1 615 . 53 MET N N 120.947 0.1 1 616 . 53 MET H H 8.348 0.03 1 617 . 53 MET CA C 56.548 0.1 1 618 . 53 MET HA H 4.512 0.03 1 619 . 53 MET CB C 35.093 0.1 1 620 . 53 MET HB2 H 1.922 0.03 2 621 . 53 MET HB3 H 2.033 0.03 2 622 . 53 MET CG C 32.392 0.1 1 623 . 53 MET HG2 H 2.653 0.03 2 624 . 53 MET HG3 H 2.734 0.03 2 625 . 53 MET HE H 2.069 0.03 1 626 . 53 MET CE C 17.278 0.1 1 627 . 53 MET C C 175.466 0.1 1 628 . 54 SER N N 120.940 0.1 1 629 . 54 SER H H 8.962 0.03 1 630 . 54 SER CA C 57.483 0.1 1 631 . 54 SER HA H 4.807 0.03 1 632 . 54 SER CB C 65.988 0.1 1 633 . 54 SER HB2 H 4.088 0.03 2 634 . 54 SER HB3 H 4.506 0.03 2 635 . 54 SER C C 175.456 0.1 1 636 . 55 GLU N N 120.781 0.1 1 637 . 55 GLU H H 9.142 0.03 1 638 . 55 GLU CA C 61.018 0.1 1 639 . 55 GLU HA H 3.833 0.03 1 640 . 55 GLU CB C 29.222 0.1 1 641 . 55 GLU HB2 H 1.978 0.03 2 642 . 55 GLU HB3 H 2.134 0.03 2 643 . 55 GLU CG C 38.048 0.1 1 644 . 55 GLU HG2 H 2.334 0.03 2 645 . 55 GLU HG3 H 2.422 0.03 2 646 . 55 GLU C C 178.219 0.1 1 647 . 56 GLU N N 118.746 0.1 1 648 . 56 GLU H H 8.832 0.03 1 649 . 56 GLU CA C 60.189 0.1 1 650 . 56 GLU HA H 4.040 0.03 1 651 . 56 GLU CB C 29.159 0.1 1 652 . 56 GLU HB2 H 2.085 0.03 1 653 . 56 GLU HB3 H 2.085 0.03 1 654 . 56 GLU CG C 36.882 0.1 1 655 . 56 GLU HG2 H 2.382 0.03 1 656 . 56 GLU HG3 H 2.382 0.03 1 657 . 56 GLU C C 179.213 0.1 1 658 . 57 GLU N N 120.933 0.1 1 659 . 57 GLU H H 7.905 0.03 1 660 . 57 GLU CA C 59.564 0.1 1 661 . 57 GLU HA H 4.062 0.03 1 662 . 57 GLU CB C 29.712 0.1 1 663 . 57 GLU HB2 H 2.122 0.03 2 664 . 57 GLU HB3 H 2.401 0.03 2 665 . 57 GLU CG C 37.410 0.1 1 666 . 57 GLU HG2 H 2.387 0.03 1 667 . 57 GLU HG3 H 2.387 0.03 1 668 . 57 GLU C C 179.213 0.1 1 669 . 58 VAL N N 120.183 0.1 1 670 . 58 VAL H H 8.059 0.03 1 671 . 58 VAL CA C 66.438 0.1 1 672 . 58 VAL HA H 3.574 0.03 1 673 . 58 VAL CB C 31.156 0.1 1 674 . 58 VAL HB H 2.146 0.03 1 675 . 58 VAL HG1 H 0.791 0.03 1 676 . 58 VAL HG2 H 0.841 0.03 1 677 . 58 VAL CG1 C 21.217 0.1 1 678 . 58 VAL CG2 C 23.740 0.1 1 679 . 58 VAL C C 177.015 0.1 1 680 . 59 PHE N N 120.046 0.1 1 681 . 59 PHE H H 8.359 0.03 1 682 . 59 PHE CA C 62.501 0.1 1 683 . 59 PHE HA H 3.988 0.03 1 684 . 59 PHE CB C 38.984 0.1 1 685 . 59 PHE HB2 H 3.060 0.03 2 686 . 59 PHE HB3 H 3.298 0.03 2 687 . 59 PHE C C 176.816 0.1 1 688 . 60 THR N N 114.904 0.1 1 689 . 60 THR H H 8.324 0.03 1 690 . 60 THR CA C 66.916 0.1 1 691 . 60 THR HA H 3.771 0.03 1 692 . 60 THR CB C 68.970 0.1 1 693 . 60 THR HB H 4.328 0.03 1 694 . 60 THR HG2 H 1.243 0.03 1 695 . 60 THR CG2 C 21.752 0.1 1 696 . 60 THR C C 176.387 0.1 1 697 . 61 GLU N N 120.550 0.1 1 698 . 61 GLU H H 7.974 0.03 1 699 . 61 GLU CA C 59.355 0.1 1 700 . 61 GLU HA H 4.038 0.03 1 701 . 61 GLU CB C 29.505 0.1 1 702 . 61 GLU HB2 H 2.005 0.03 1 703 . 61 GLU HB3 H 2.005 0.03 1 704 . 61 GLU C C 180.144 0.1 1 705 . 62 VAL N N 122.229 0.1 1 706 . 62 VAL H H 8.345 0.03 1 707 . 62 VAL CA C 66.959 0.1 1 708 . 62 VAL HA H 2.972 0.03 1 709 . 62 VAL CB C 30.907 0.1 1 710 . 62 VAL HB H 1.532 0.03 1 711 . 62 VAL HG1 H -0.227 0.03 1 712 . 62 VAL HG2 H 0.549 0.03 1 713 . 62 VAL CG1 C 21.195 0.1 1 714 . 62 VAL CG2 C 23.246 0.1 1 715 . 62 VAL C C 176.617 0.1 1 716 . 63 ALA N N 122.183 0.1 1 717 . 63 ALA H H 8.722 0.03 1 718 . 63 ALA CA C 55.306 0.1 1 719 . 63 ALA HA H 3.760 0.03 1 720 . 63 ALA HB H 1.175 0.03 1 721 . 63 ALA CB C 17.616 0.1 1 722 . 63 ALA C C 180.113 0.1 1 723 . 64 ASN N N 114.535 0.1 1 724 . 64 ASN H H 7.523 0.03 1 725 . 64 ASN CA C 55.550 0.1 1 726 . 64 ASN HA H 4.429 0.03 1 727 . 64 ASN CB C 38.485 0.1 1 728 . 64 ASN HB2 H 2.798 0.03 1 729 . 64 ASN HB3 H 2.798 0.03 1 730 . 64 ASN ND2 N 113.423 0.1 1 731 . 64 ASN HD21 H 6.898 0.03 2 732 . 64 ASN HD22 H 7.676 0.03 2 733 . 64 ASN C C 177.790 0.1 1 734 . 65 LEU N N 121.397 0.1 1 735 . 65 LEU H H 7.531 0.03 1 736 . 65 LEU CA C 57.219 0.1 1 737 . 65 LEU HA H 4.045 0.03 1 738 . 65 LEU CB C 42.296 0.1 1 739 . 65 LEU HB2 H 1.371 0.03 2 740 . 65 LEU HB3 H 1.471 0.03 2 741 . 65 LEU CG C 26.225 0.1 1 742 . 65 LEU HG H 1.573 0.03 1 743 . 65 LEU HD1 H 0.830 0.03 1 744 . 65 LEU HD2 H 0.774 0.03 1 745 . 65 LEU CD1 C 24.402 0.1 1 746 . 65 LEU CD2 C 24.237 0.1 1 747 . 65 LEU C C 178.512 0.1 1 748 . 66 PHE N N 115.195 0.1 1 749 . 66 PHE H H 8.221 0.03 1 750 . 66 PHE CA C 53.329 0.1 1 751 . 66 PHE HA H 4.887 0.03 1 752 . 66 PHE CB C 36.199 0.1 1 753 . 66 PHE HB2 H 2.916 0.03 2 754 . 66 PHE HB3 H 3.696 0.03 2 755 . 66 PHE HD1 H 6.602 0.03 1 756 . 66 PHE HD2 H 6.602 0.03 1 757 . 66 PHE HE1 H 6.682 0.03 1 758 . 66 PHE HE2 H 6.682 0.03 1 759 . 66 PHE CD1 C 129.503 0.1 1 760 . 66 PHE CE1 C 130.956 0.1 1 761 . 66 PHE CZ C 129.567 0.1 1 762 . 66 PHE HZ H 6.013 0.03 1 763 . 66 PHE C C 174.817 0.1 1 764 . 67 ARG N N 121.387 0.1 1 765 . 67 ARG H H 6.973 0.03 1 766 . 67 ARG CA C 58.698 0.1 1 767 . 67 ARG HA H 4.124 0.03 1 768 . 67 ARG CB C 29.750 0.1 1 769 . 67 ARG HB2 H 1.862 0.03 2 770 . 67 ARG HB3 H 2.006 0.03 2 771 . 67 ARG CG C 26.839 0.1 1 772 . 67 ARG HG2 H 1.724 0.03 2 773 . 67 ARG HG3 H 1.827 0.03 2 774 . 67 ARG CD C 43.393 0.1 1 775 . 67 ARG HD2 H 3.274 0.03 2 776 . 67 ARG HD3 H 3.312 0.03 2 777 . 67 ARG C C 177.905 0.1 1 778 . 68 GLY N N 115.764 0.1 1 779 . 68 GLY H H 9.415 0.03 1 780 . 68 GLY CA C 45.444 0.1 1 781 . 68 GLY HA2 H 3.893 0.03 2 782 . 68 GLY HA3 H 4.330 0.03 2 783 . 68 GLY C C 174.169 0.1 1 784 . 69 GLN N N 120.504 0.1 1 785 . 69 GLN H H 8.491 0.03 1 786 . 69 GLN CA C 52.093 0.1 1 787 . 69 GLN HA H 4.833 0.03 1 788 . 69 GLN CB C 26.189 0.1 1 789 . 69 GLN HB2 H 1.849 0.03 1 790 . 69 GLN HB3 H 1.849 0.03 1 791 . 69 GLN CG C 31.306 0.1 1 792 . 69 GLN HG2 H 2.234 0.03 1 793 . 69 GLN HG3 H 2.234 0.03 1 794 . 69 GLN NE2 N 111.110 0.1 1 795 . 69 GLN HE21 H 6.770 0.03 2 796 . 69 GLN HE22 H 7.521 0.03 2 797 . 69 GLN C C 176.387 0.1 1 798 . 70 GLU N N 120.383 0.1 1 799 . 70 GLU H H 8.592 0.03 1 800 . 70 GLU CA C 61.181 0.1 1 801 . 70 GLU HA H 3.930 0.03 1 802 . 70 GLU CB C 29.041 0.1 1 803 . 70 GLU HB2 H 2.134 0.03 1 804 . 70 GLU HB3 H 2.134 0.03 1 805 . 70 GLU CG C 37.315 0.1 1 806 . 70 GLU HG2 H 2.388 0.03 2 807 . 70 GLU HG3 H 2.543 0.03 2 808 . 70 GLU C C 178.512 0.1 1 809 . 71 ASP N N 119.256 0.1 1 810 . 71 ASP H H 8.989 0.03 1 811 . 71 ASP CA C 56.379 0.1 1 812 . 71 ASP HA H 4.410 0.03 1 813 . 71 ASP CB C 38.319 0.1 1 814 . 71 ASP HB2 H 2.684 0.03 2 815 . 71 ASP HB3 H 2.841 0.03 2 816 . 71 ASP C C 178.543 0.1 1 817 . 72 LEU N N 119.393 0.1 1 818 . 72 LEU H H 7.780 0.03 1 819 . 72 LEU CA C 56.710 0.1 1 820 . 72 LEU HA H 4.307 0.03 1 821 . 72 LEU CB C 41.751 0.1 1 822 . 72 LEU HB2 H 1.015 0.03 2 823 . 72 LEU HB3 H 1.657 0.03 2 824 . 72 LEU CG C 26.317 0.1 1 825 . 72 LEU HG H 1.561 0.03 1 826 . 72 LEU HD1 H 0.183 0.03 1 827 . 72 LEU HD2 H 0.492 0.03 1 828 . 72 LEU CD1 C 26.095 0.1 1 829 . 72 LEU CD2 C 21.970 0.1 1 830 . 72 LEU C C 180.605 0.1 1 831 . 73 LEU N N 120.865 0.1 1 832 . 73 LEU H H 7.893 0.03 1 833 . 73 LEU CA C 57.727 0.1 1 834 . 73 LEU HA H 4.394 0.03 1 835 . 73 LEU CB C 42.133 0.1 1 836 . 73 LEU HB2 H 1.834 0.03 2 837 . 73 LEU HB3 H 2.054 0.03 2 838 . 73 LEU CG C 27.090 0.1 1 839 . 73 LEU HG H 1.866 0.03 1 840 . 73 LEU HD1 H 0.805 0.03 1 841 . 73 LEU HD2 H 0.900 0.03 1 842 . 73 LEU CD1 C 24.071 0.1 1 843 . 73 LEU CD2 C 24.568 0.1 1 844 . 73 LEU C C 178.428 0.1 1 845 . 74 SER N N 114.767 0.1 1 846 . 74 SER H H 8.318 0.03 1 847 . 74 SER CA C 61.846 0.1 1 848 . 74 SER HA H 4.321 0.03 1 849 . 74 SER CB C 62.674 0.1 1 850 . 74 SER HB2 H 4.074 0.03 1 851 . 74 SER HB3 H 4.074 0.03 1 852 . 74 SER C C 177.905 0.1 1 853 . 75 GLU N N 119.965 0.1 1 854 . 75 GLU H H 7.917 0.03 1 855 . 75 GLU CA C 58.540 0.1 1 856 . 75 GLU HA H 4.065 0.03 1 857 . 75 GLU CB C 30.764 0.1 1 858 . 75 GLU HB2 H 1.904 0.03 2 859 . 75 GLU HB3 H 2.065 0.03 2 860 . 75 GLU CG C 37.161 0.1 1 861 . 75 GLU HG2 H 2.031 0.03 2 862 . 75 GLU HG3 H 2.355 0.03 2 863 . 75 GLU C C 177.570 0.1 1 864 . 76 PHE N N 119.448 0.1 1 865 . 76 PHE H H 7.648 0.03 1 866 . 76 PHE CA C 60.653 0.1 1 867 . 76 PHE HA H 4.351 0.03 1 868 . 76 PHE CB C 38.982 0.1 1 869 . 76 PHE HB2 H 3.296 0.03 2 870 . 76 PHE HB3 H 4.097 0.03 2 871 . 76 PHE HD1 H 7.374 0.03 1 872 . 76 PHE HD2 H 7.374 0.03 1 873 . 76 PHE HE1 H 7.097 0.03 1 874 . 76 PHE HE2 H 7.097 0.03 1 875 . 76 PHE CD1 C 131.994 0.1 1 876 . 76 PHE CE1 C 130.618 0.1 1 877 . 76 PHE CZ C 129.059 0.1 1 878 . 76 PHE HZ H 6.833 0.03 1 879 . 76 PHE C C 177.151 0.1 1 880 . 77 GLY N N 100.779 0.1 1 881 . 77 GLY H H 7.753 0.03 1 882 . 77 GLY CA C 46.935 0.1 1 883 . 77 GLY HA2 H 3.481 0.03 2 884 . 77 GLY HA3 H 3.863 0.03 2 885 . 77 GLY C C 175.058 0.1 1 886 . 78 GLN N N 116.781 0.1 1 887 . 78 GLN H H 7.282 0.03 1 888 . 78 GLN CA C 57.056 0.1 1 889 . 78 GLN HA H 3.865 0.03 1 890 . 78 GLN CB C 28.047 0.1 1 891 . 78 GLN HB2 H 1.543 0.03 2 892 . 78 GLN HB3 H 1.634 0.03 2 893 . 78 GLN CG C 33.515 0.1 1 894 . 78 GLN HG2 H 1.590 0.03 2 895 . 78 GLN HG3 H 1.980 0.03 2 896 . 78 GLN NE2 N 112.128 0.1 1 897 . 78 GLN HE21 H 6.954 0.03 2 898 . 78 GLN HE22 H 7.443 0.03 2 899 . 78 GLN C C 175.895 0.1 1 900 . 79 PHE N N 115.970 0.1 1 901 . 79 PHE H H 7.625 0.03 1 902 . 79 PHE CA C 58.035 0.1 1 903 . 79 PHE HA H 4.172 0.03 1 904 . 79 PHE CB C 38.816 0.1 1 905 . 79 PHE HB2 H 2.450 0.03 2 906 . 79 PHE HB3 H 2.971 0.03 2 907 . 79 PHE HD1 H 7.158 0.03 1 908 . 79 PHE HD2 H 7.158 0.03 1 909 . 79 PHE CD1 C 132.591 0.1 1 910 . 79 PHE C C 173.112 0.1 1 911 . 80 LEU N N 118.107 0.1 1 912 . 80 LEU H H 6.858 0.03 1 913 . 80 LEU CA C 51.574 0.1 1 914 . 80 LEU HA H 4.654 0.03 1 915 . 80 LEU CB C 42.425 0.1 1 916 . 80 LEU HB2 H 1.431 0.03 1 917 . 80 LEU HB3 H 1.431 0.03 1 918 . 80 LEU CG C 26.250 0.1 1 919 . 80 LEU HG H 1.274 0.03 1 920 . 80 LEU HD1 H 0.688 0.03 1 921 . 80 LEU HD2 H 0.675 0.03 1 922 . 80 LEU CD1 C 26.187 0.1 1 923 . 80 LEU CD2 C 23.884 0.1 1 924 . 81 PRO CD C 50.580 0.1 1 925 . 81 PRO CA C 64.055 0.1 1 926 . 81 PRO HA H 4.341 0.03 1 927 . 81 PRO CB C 32.182 0.1 1 928 . 81 PRO HB2 H 1.935 0.03 2 929 . 81 PRO HB3 H 2.381 0.03 2 930 . 81 PRO CG C 27.716 0.1 1 931 . 81 PRO HG2 H 2.141 0.03 1 932 . 81 PRO HG3 H 2.141 0.03 1 933 . 81 PRO HD2 H 3.712 0.03 1 934 . 81 PRO HD3 H 3.712 0.03 1 935 . 81 PRO C C 178.145 0.1 1 936 . 82 GLU N N 121.154 0.1 1 937 . 82 GLU H H 9.150 0.03 1 938 . 82 GLU CA C 58.367 0.1 1 939 . 82 GLU HA H 4.017 0.03 1 940 . 82 GLU CB C 29.538 0.1 1 941 . 82 GLU HB2 H 1.983 0.03 2 942 . 82 GLU HB3 H 2.034 0.03 2 943 . 82 GLU C C 177.852 0.1 1 944 . 83 ALA N N 122.426 0.1 1 945 . 83 ALA H H 8.331 0.03 1 946 . 83 ALA CA C 53.365 0.1 1 947 . 83 ALA HA H 4.194 0.03 1 948 . 83 ALA HB H 1.365 0.03 1 949 . 83 ALA CB C 18.905 0.1 1 950 . 83 ALA C C 178.386 0.1 1 951 . 84 LYS N N 117.774 0.1 1 952 . 84 LYS H H 8.129 0.03 1 953 . 84 LYS CA C 56.544 0.1 1 954 . 84 LYS HA H 4.219 0.03 1 955 . 84 LYS CB C 32.686 0.1 1 956 . 84 LYS HB2 H 1.745 0.03 2 957 . 84 LYS HB3 H 1.889 0.03 2 958 . 84 LYS CG C 24.996 0.1 1 959 . 84 LYS HG2 H 1.433 0.03 1 960 . 84 LYS HG3 H 1.433 0.03 1 961 . 84 LYS CD C 29.060 0.1 1 962 . 84 LYS HD2 H 1.656 0.03 1 963 . 84 LYS HD3 H 1.656 0.03 1 964 . 84 LYS CE C 42.071 0.1 1 965 . 84 LYS HE2 H 2.943 0.03 1 966 . 84 LYS HE3 H 2.943 0.03 1 967 . 84 LYS C C 176.931 0.1 1 968 . 85 ARG N N 119.780 0.1 1 969 . 85 ARG H H 7.888 0.03 1 970 . 85 ARG CA C 57.538 0.1 1 971 . 85 ARG HA H 4.097 0.03 1 972 . 85 ARG CB C 30.543 0.1 1 973 . 85 ARG HB2 H 1.774 0.03 2 974 . 85 ARG HB3 H 1.824 0.03 2 975 . 85 ARG CG C 27.109 0.1 1 976 . 85 ARG HG2 H 1.593 0.03 2 977 . 85 ARG HG3 H 1.639 0.03 2 978 . 85 ARG CD C 43.427 0.1 1 979 . 85 ARG HD2 H 3.111 0.03 1 980 . 85 ARG HD3 H 3.111 0.03 1 981 . 85 ARG C C 177.287 0.1 1 982 . 86 SER N N 115.045 0.1 1 983 . 86 SER H H 8.167 0.03 1 984 . 86 SER CA C 59.230 0.1 1 985 . 86 SER HA H 4.279 0.03 1 986 . 86 SER CB C 63.284 0.1 1 987 . 86 SER HB2 H 3.778 0.03 1 988 . 86 SER HB3 H 3.778 0.03 1 989 . 86 SER C C 174.974 0.1 1 990 . 87 LEU N N 122.454 0.1 1 991 . 87 LEU H H 7.876 0.03 1 992 . 87 LEU CA C 55.681 0.1 1 993 . 87 LEU HA H 4.152 0.03 1 994 . 87 LEU CB C 42.054 0.1 1 995 . 87 LEU HB2 H 1.185 0.03 2 996 . 87 LEU HB3 H 1.390 0.03 2 997 . 87 LEU CG C 26.862 0.1 1 998 . 87 LEU HG H 1.489 0.03 1 999 . 87 LEU HD1 H 0.803 0.03 1 1000 . 87 LEU HD2 H 0.737 0.03 1 1001 . 87 LEU CD1 C 25.047 0.1 1 1002 . 87 LEU CD2 C 23.269 0.1 1 1003 . 87 LEU C C 177.298 0.1 1 1004 . 88 PHE N N 118.696 0.1 1 1005 . 88 PHE H H 7.895 0.03 1 1006 . 88 PHE CA C 57.636 0.1 1 1007 . 88 PHE HA H 4.644 0.03 1 1008 . 88 PHE CB C 39.432 0.1 1 1009 . 88 PHE HB2 H 2.940 0.03 2 1010 . 88 PHE HB3 H 3.150 0.03 2 1011 . 88 PHE HD1 H 7.200 0.03 1 1012 . 88 PHE HD2 H 7.200 0.03 1 1013 . 88 PHE CD1 C 132.438 0.1 1 1014 . 88 PHE C C 176.052 0.1 1 1015 . 89 THR N N 114.066 0.1 1 1016 . 89 THR H H 7.960 0.03 1 1017 . 89 THR CA C 61.846 0.1 1 1018 . 89 THR HA H 4.325 0.03 1 1019 . 89 THR CB C 69.906 0.1 1 1020 . 89 THR HB H 4.256 0.03 1 1021 . 89 THR HG2 H 1.169 0.03 1 1022 . 89 THR CG2 C 21.466 0.1 1 1023 . 89 THR C C 175.121 0.1 1 1024 . 90 GLY N N 110.382 0.1 1 1025 . 90 GLY H H 7.926 0.03 1 1026 . 90 GLY CA C 45.444 0.1 1 1027 . 90 GLY HA2 H 3.918 0.03 1 1028 . 90 GLY HA3 H 3.918 0.03 1 1029 . 90 GLY C C 174.033 0.1 1 1030 . 91 ASN N N 118.708 0.1 1 1031 . 91 ASN H H 8.386 0.03 1 1032 . 91 ASN CA C 53.327 0.1 1 1033 . 91 ASN HA H 4.770 0.03 1 1034 . 91 ASN CB C 39.107 0.1 1 1035 . 91 ASN HB2 H 2.780 0.03 1 1036 . 91 ASN HB3 H 2.780 0.03 1 1037 . 91 ASN ND2 N 113.102 0.1 1 1038 . 91 ASN HD21 H 6.943 0.03 2 1039 . 91 ASN HD22 H 7.625 0.03 2 1040 . 91 ASN C C 175.969 0.1 1 1041 . 92 GLY N N 109.669 0.1 1 1042 . 92 GLY H H 8.494 0.03 1 1043 . 92 GLY CA C 45.444 0.1 1 1044 . 92 GLY HA2 H 3.963 0.03 1 1045 . 92 GLY HA3 H 3.963 0.03 1 1046 . 92 GLY C C 174.378 0.1 1 1047 . 93 SER N N 115.747 0.1 1 1048 . 93 SER H H 8.191 0.03 1 1049 . 93 SER CA C 58.532 0.1 1 1050 . 93 SER HA H 4.419 0.03 1 1051 . 93 SER CB C 63.906 0.1 1 1052 . 93 SER HB2 H 3.874 0.03 1 1053 . 93 SER HB3 H 3.874 0.03 1 1054 . 93 SER C C 174.660 0.1 1 1055 . 94 ALA N N 125.832 0.1 1 1056 . 94 ALA H H 8.406 0.03 1 1057 . 94 ALA CA C 52.957 0.1 1 1058 . 94 ALA HA H 4.302 0.03 1 1059 . 94 ALA HB H 1.386 0.03 1 1060 . 94 ALA CB C 19.131 0.1 1 1061 . 94 ALA C C 177.988 0.1 1 1062 . 95 GLU N N 119.467 0.1 1 1063 . 95 GLU H H 8.326 0.03 1 1064 . 95 GLU CA C 56.710 0.1 1 1065 . 95 GLU HA H 4.224 0.03 1 1066 . 95 GLU CB C 29.870 0.1 1 1067 . 95 GLU HB2 H 1.946 0.03 2 1068 . 95 GLU HB3 H 2.040 0.03 2 1069 . 95 GLU C C 176.858 0.1 1 1070 . 96 MET N N 120.994 0.1 1 1071 . 96 MET H H 8.287 0.03 1 1072 . 96 MET CA C 55.750 0.1 1 1073 . 96 MET HA H 4.439 0.03 1 1074 . 96 MET CB C 32.765 0.1 1 1075 . 96 MET HB2 H 2.014 0.03 2 1076 . 96 MET HB3 H 2.081 0.03 2 1077 . 96 MET CG C 31.997 0.1 1 1078 . 96 MET HG2 H 2.519 0.03 2 1079 . 96 MET HG3 H 2.595 0.03 2 1080 . 96 MET HE H 2.080 0.03 1 1081 . 96 MET CE C 16.947 0.1 1 1082 . 96 MET C C 176.199 0.1 1 1083 . 97 ASN N N 119.689 0.1 1 1084 . 97 ASN H H 8.454 0.03 1 1085 . 97 ASN CA C 53.368 0.1 1 1086 . 97 ASN HA H 4.780 0.03 1 1087 . 97 ASN CB C 38.899 0.1 1 1088 . 97 ASN HB2 H 2.780 0.03 1 1089 . 97 ASN HB3 H 2.780 0.03 1 1090 . 97 ASN ND2 N 113.102 0.1 1 1091 . 97 ASN HD21 H 6.943 0.03 2 1092 . 97 ASN HD22 H 7.625 0.03 2 1093 . 97 ASN C C 175.435 0.1 1 1094 . 98 SER N N 116.340 0.1 1 1095 . 98 SER H H 8.337 0.03 1 1096 . 98 SER CA C 58.895 0.1 1 1097 . 98 SER HA H 4.366 0.03 1 1098 . 98 SER CB C 63.768 0.1 1 1099 . 98 SER HB2 H 3.917 0.03 1 1100 . 98 SER HB3 H 3.917 0.03 1 1101 . 98 SER C C 175.247 0.1 1 1102 . 99 GLY N N 110.656 0.1 1 1103 . 99 GLY H H 8.463 0.03 1 1104 . 99 GLY CA C 45.444 0.1 1 1105 . 99 GLY HA2 H 3.950 0.03 1 1106 . 99 GLY HA3 H 3.950 0.03 1 1107 . 99 GLY C C 174.158 0.1 1 1108 . 100 GLN N N 119.903 0.1 1 1109 . 100 GLN H H 8.160 0.03 1 1110 . 100 GLN CA C 55.898 0.1 1 1111 . 100 GLN HA H 4.306 0.03 1 1112 . 100 GLN CB C 29.485 0.1 1 1113 . 100 GLN HB2 H 1.951 0.03 2 1114 . 100 GLN HB3 H 2.078 0.03 2 1115 . 100 GLN CG C 33.785 0.1 1 1116 . 100 GLN HG2 H 2.330 0.03 1 1117 . 100 GLN HG3 H 2.330 0.03 1 1118 . 100 GLN NE2 N 112.590 0.1 1 1119 . 100 GLN HE21 H 6.846 0.03 2 1120 . 100 GLN HE22 H 7.548 0.03 2 1121 . 100 GLN C C 176.010 0.1 1 1122 . 101 LYS N N 122.891 0.1 1 1123 . 101 LYS H H 8.426 0.03 1 1124 . 101 LYS CA C 56.427 0.1 1 1125 . 101 LYS HA H 4.319 0.03 1 1126 . 101 LYS CB C 32.977 0.1 1 1127 . 101 LYS HB2 H 1.746 0.03 1 1128 . 101 LYS HB3 H 1.746 0.03 1 1129 . 101 LYS CG C 24.838 0.1 1 1130 . 101 LYS HG2 H 1.438 0.03 1 1131 . 101 LYS HG3 H 1.438 0.03 1 1132 . 101 LYS CD C 29.217 0.1 1 1133 . 101 LYS HD2 H 1.668 0.03 1 1134 . 101 LYS HD3 H 1.668 0.03 1 1135 . 101 LYS CE C 42.163 0.1 1 1136 . 101 LYS HE2 H 2.981 0.03 1 1137 . 101 LYS HE3 H 2.981 0.03 1 1138 . 101 LYS C C 176.283 0.1 1 1139 . 102 ASN N N 120.559 0.1 1 1140 . 102 ASN H H 8.545 0.03 1 1141 . 102 ASN CA C 53.452 0.1 1 1142 . 102 ASN HA H 4.706 0.03 1 1143 . 102 ASN CB C 38.968 0.1 1 1144 . 102 ASN HB2 H 2.796 0.03 1 1145 . 102 ASN HB3 H 2.796 0.03 1 1146 . 102 ASN ND2 N 113.102 0.1 1 1147 . 102 ASN HD21 H 6.943 0.03 2 1148 . 102 ASN HD22 H 7.625 0.03 2 1149 . 102 ASN C C 175.121 0.1 1 1150 . 103 GLU N N 121.429 0.1 1 1151 . 103 GLU H H 8.462 0.03 1 1152 . 103 GLU CA C 56.383 0.1 1 1153 . 103 GLU HA H 4.259 0.03 1 1154 . 103 GLU CB C 30.403 0.1 1 1155 . 103 GLU HB2 H 1.932 0.03 2 1156 . 103 GLU HB3 H 2.075 0.03 2 1157 . 103 GLU C C 176.209 0.1 1 1158 . 104 GLU N N 122.692 0.1 1 1159 . 104 GLU H H 8.399 0.03 1 1160 . 104 GLU CA C 56.571 0.1 1 1161 . 104 GLU HA H 4.250 0.03 1 1162 . 104 GLU CB C 30.195 0.1 1 1163 . 104 GLU HB2 H 2.011 0.03 1 1164 . 104 GLU HB3 H 2.011 0.03 1 1165 . 104 GLU C C 175.487 0.1 1 1166 . 105 LYS N N 127.687 0.1 1 1167 . 105 LYS H H 7.949 0.03 1 1168 . 105 LYS CA C 57.483 0.1 1 1169 . 105 LYS HA H 4.153 0.03 1 1170 . 105 LYS CB C 33.769 0.1 1 1171 . 105 LYS HB2 H 1.707 0.03 2 1172 . 105 LYS HB3 H 1.825 0.03 2 1173 . 105 LYS CG C 24.732 0.1 1 1174 . 105 LYS HG2 H 1.421 0.03 1 1175 . 105 LYS HG3 H 1.421 0.03 1 1176 . 105 LYS CD C 29.115 0.1 1 1177 . 105 LYS HD2 H 1.668 0.03 1 1178 . 105 LYS HD3 H 1.668 0.03 1 1179 . 105 LYS CE C 42.112 0.1 1 1180 . 105 LYS HE2 H 2.982 0.03 1 1181 . 105 LYS HE3 H 2.982 0.03 1 stop_ save_ save_assigned_chemical_shifts_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $Typical_sample stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Mad1 _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 ASN H H 7.530 0.03 1 2 . 1 ASN HA H 5.290 0.03 1 3 . 1 ASN HB2 H 3.164 0.03 2 4 . 1 ASN HB3 H 3.295 0.03 2 5 . 1 ASN HD21 H 7.685 0.03 2 6 . 1 ASN HD22 H 6.963 0.03 2 7 . 2 ILE H H 8.523 0.03 1 8 . 2 ILE HA H 3.769 0.03 1 9 . 2 ILE HB H 2.096 0.03 1 10 . 2 ILE HG2 H 1.000 0.03 1 11 . 2 ILE HG12 H 1.353 0.03 2 12 . 2 ILE HG13 H 1.638 0.03 2 13 . 2 ILE HD1 H 0.589 0.03 1 14 . 3 GLN H H 8.415 0.03 1 15 . 3 GLN HA H 3.963 0.03 1 16 . 3 GLN HB2 H 2.091 0.03 1 17 . 3 GLN HB3 H 2.091 0.03 1 18 . 3 GLN HG2 H 2.224 0.03 1 19 . 3 GLN HG3 H 2.224 0.03 1 20 . 3 GLN HE21 H 7.863 0.03 2 21 . 3 GLN HE22 H 6.832 0.03 2 22 . 4 MET H H 8.213 0.03 1 23 . 4 MET HA H 4.324 0.03 1 24 . 4 MET HB2 H 2.176 0.03 4 25 . 4 MET HB3 H 2.441 0.03 4 26 . 4 MET HG2 H 2.638 0.03 4 27 . 4 MET HG3 H 2.918 0.03 4 28 . 5 LEU H H 7.652 0.03 1 29 . 5 LEU HA H 3.945 0.03 1 30 . 5 LEU HD1 H 0.204 0.03 2 31 . 5 LEU HD2 H 0.870 0.03 2 32 . 5 LEU HB2 H 2.206 0.03 4 33 . 5 LEU HB3 H 1.151 0.03 4 34 . 5 LEU HG H 1.570 0.03 4 35 . 6 LEU H H 7.775 0.03 1 36 . 6 LEU HA H 3.970 0.03 1 37 . 6 LEU HB2 H 1.462 0.03 4 38 . 6 LEU HB3 H 1.561 0.03 4 39 . 6 LEU HG H 1.998 0.03 4 40 . 6 LEU HD1 H 0.497 0.03 2 41 . 6 LEU HD2 H 0.609 0.03 2 42 . 7 GLU H H 8.462 0.03 1 43 . 7 GLU HA H 4.240 0.03 1 44 . 7 GLU HB2 H 2.392 0.03 1 45 . 7 GLU HB3 H 2.392 0.03 1 46 . 7 GLU HG2 H 2.637 0.03 1 47 . 7 GLU HG3 H 2.637 0.03 1 48 . 8 ALA H H 8.839 0.03 1 49 . 8 ALA HA H 4.110 0.03 1 50 . 8 ALA HB H 1.311 0.03 1 51 . 9 ALA H H 8.458 0.03 1 52 . 9 ALA HA H 4.149 0.03 1 53 . 9 ALA HB H 1.662 0.03 1 54 . 10 ASP H H 8.071 0.03 1 55 . 10 ASP HA H 4.504 0.03 1 56 . 10 ASP HB2 H 2.785 0.03 2 57 . 10 ASP HB3 H 2.903 0.03 2 58 . 11 TYR H H 8.281 0.03 1 59 . 11 TYR HA H 4.256 0.03 1 60 . 11 TYR HB2 H 3.443 0.03 2 61 . 11 TYR HB3 H 3.492 0.03 2 62 . 11 TYR HD1 H 7.154 0.03 1 63 . 11 TYR HD2 H 7.154 0.03 1 64 . 11 TYR HE1 H 6.885 0.03 1 65 . 11 TYR HE2 H 6.885 0.03 1 66 . 12 LEU H H 8.228 0.03 1 67 . 12 LEU HA H 4.031 0.03 1 68 . 12 LEU HB2 H 1.592 0.03 4 69 . 12 LEU HB3 H 1.954 0.03 4 70 . 12 LEU HG H 2.012 0.03 4 71 . 12 LEU HD1 H 0.955 0.03 1 72 . 12 LEU HD2 H 0.955 0.03 1 73 . 13 GLU H H 7.720 0.03 1 74 . 13 GLU HA H 4.177 0.03 1 75 . 13 GLU HB2 H 2.107 0.03 4 76 . 13 GLU HB3 H 2.251 0.03 4 77 . 13 GLU HG2 H 2.470 0.03 4 78 . 13 GLU HG3 H 2.546 0.03 4 stop_ loop_ _Atom_shift_assign_ID_ambiguity 27 '26,25,24' '34,33,32' '39,38,37' '70,69,68' '78,77,76,75' stop_ save_