data_6318 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of thioredoxin h1 from Arabidopsis thaliana ; _BMRB_accession_number 6318 _BMRB_flat_file_name bmr6318.str _Entry_type original _Submission_date 2004-09-20 _Accession_date 2004-09-20 _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 Peterson F. C. . 2 Lytle B. L. . 3 Sampath S. . . 4 Vinarov D. A. . 5 Tyler E. M. . 6 Shahan M. . . 7 Markley J. L. . 8 Volkman B. F. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 685 "13C chemical shifts" 512 "15N chemical shifts" 121 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-07-08 update BMRB 'added time domain data' 2007-01-04 update author 'update the entry citation' 2005-09-08 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution structure of thioredoxin h1 from Arabidopsis thaliana' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15987893 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Peterson F. C. . 2 Lytle B. L. . 3 Sampath S. . . 4 Vinarov D. A. . 5 Tyler E. M. . 6 Shahan M. . . 7 Markley J. L. . 8 Volkman B. F. . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume 14 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2195 _Page_last 2200 _Year 2005 _Details . loop_ _Keyword At3G51030 thioredoxin 'Structural Genomics' 'Protein Structure Initiative' CESG stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. Abstract NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93. ; _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F. . . 2 Grzesiek S. . . 3 Vuister 'G. W.' W. . 4 Zhu G. . . 5 Pfeifer J. . . 6 Bax A. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Bartels, C., Xia, T.-H., Billeter, M., Guntert, P. and Wuthrich, K. (1995) J. Biomol. NMR, 6, 1-10. ; _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 ; Bartels, C., Guntert, P., Billeter, M. and Wuthrich, K. (1997) J. Comp. Chem. 18, 139-149. ; _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_4 _Saveframe_category citation _Citation_full ; Cornilescu G, Delaglio F, Bax A. Abstract Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR. 1999 Mar;13(3):289-302. ; _Citation_title 'Protein backbone angle restraints from searching a database for chemical shift and sequence homology.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10212987 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cornilescu G. . . 2 Delaglio F. . . 3 Bax A. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 13 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 289 _Page_last 302 _Year 1999 _Details ; Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local conformation, and homologous proteins show quite similar patterns of secondary chemical shifts. The inverse of this relation is used to search a database for triplets of adjacent residues with secondary chemical shifts and sequence similarity which provide the best match to the query triplet of interest. The database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached to the secondary chemical shifts of the five types of resonances relative to that of sequence similarity was optimized empirically. TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence. If the central residues in these 10 triplets exhibit similar phi and psi backbone angles, their averages can reliably be used as angular restraints for the protein whose structure is being studied. Tests carried out for proteins of known structure indicate that the root-mean-square difference (rmsd) between the output of TALOS and the X-ray derived backbone angles is about 15 degrees. Approximately 3% of the predictions made by TALOS are found to be in error. ; save_ save_ref_5 _Saveframe_category citation _Citation_full ; Herrmann T, Guntert P, Wuthrich K. Abstract Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol. 2002 May 24;319(1):209-27. ; _Citation_title 'Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12051947 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Herrmann Torsten . . 2 Guntert Peter . . 3 Wuthrich Kurt . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 319 _Journal_issue 1 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 209 _Page_last 227 _Year 2002 _Details ; Combined automated NOE assignment and structure determination module (CANDID) is a new software for efficient NMR structure determination of proteins by automated assignment of the NOESY spectra. CANDID uses an iterative approach with multiple cycles of NOE cross-peak assignment and protein structure calculation using the fast DYANA torsion angle dynamics algorithm, so that the result from each CANDID cycle consists of exhaustive, possibly ambiguous NOE cross-peak assignments in all available spectra and a three-dimensional protein structure represented by a bundle of conformers. The input for the first CANDID cycle consists of the amino acid sequence, the chemical shift list from the sequence-specific resonance assignment, and listings of the cross-peak positions and volumes in one or several two, three or four-dimensional NOESY spectra. The input for the second and subsequent CANDID cycles contains the three-dimensional protein structure from the previous cycle, in addition to the complete input used for the first cycle. CANDID includes two new elements that make it robust with respect to the presence of artifacts in the input data, i.e. network-anchoring and constraint-combination, which have a key role in de novo protein structure determinations for the successful generation of the correct polypeptide fold by the first CANDID cycle. Network-anchoring makes use of the fact that any network of correct NOE cross-peak assignments forms a self-consistent set; the initial, chemical shift-based assignments for each individual NOE cross-peak are therefore weighted by the extent to which they can be embedded into the network formed by all other NOE cross-peak assignments. Constraint-combination reduces the deleterious impact of artifact NOE upper distance constraints in the input for a protein structure calculation by combining the assignments for two or several peaks into a single upper limit distance constraint, which lowers the probability that the presence of an artifact peak will influence the outcome of the structure calculation. CANDID test calculations were performed with NMR data sets of four proteins for which high-quality structures had previously been solved by interactive protocols, and they yielded comparable results to these reference structure determinations with regard to both the residual constraint violations, and the precision and accuracy of the atomic coordinates. The CANDID approach has further been validated by de novo NMR structure determinations of four additional proteins. The experience gained in these calculations shows that once nearly complete sequence-specific resonance assignments are available, the automated CANDID approach results in greatly enhanced efficiency of the NOESY spectral analysis. The fact that the correct fold is obtained in cycle 1 of a de novo structure calculation is the single most important advance achieved with CANDID, when compared with previously proposed automated NOESY assignment methods that do not use network-anchoring and constraint-combination. ; save_ save_ref_6 _Saveframe_category citation _Citation_full ; Schwieters CD, Kuszewski JJ, Tjandra N, Marius Clore G. Abstract The Xplor-NIH NMR molecular structure determination package. J Magn Reson. 2003 Jan;160(1):65-73. ; _Citation_title 'The Xplor-NIH NMR molecular structure determination package.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12565051 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schwieters 'Charles D.' D. . 2 Kuszewski 'John J.' J. . 3 Tjandra Nico . . 4 Clore 'G. Marius' M. . stop_ _Journal_abbreviation 'J. Magn. Reson.' _Journal_name_full 'Journal of magnetic resonance (San Diego, Calif. : 1997)' _Journal_volume 160 _Journal_issue 1 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 65 _Page_last 73 _Year 2003 _Details ; We announce the availability of the Xplor-NIH software package for NMR biomolecular structure determination. This package consists of the pre-existing XPLOR program, along with many NMR-specific extensions developed at the NIH. In addition to many features which have been developed over the last 20 years, the Xplor-NIH package contains an interface with a new programmatic framework written in C++. This interface currently supports the general purpose scripting languages Python and TCL, enabling rapid development of new tools, such as new potential energy terms and new optimization methods. Support for these scripting languages also facilitates interaction with existing external programs for structure analysis, structure manipulation, visualization, and spectral analysis. ; save_ ################################## # Molecular system description # ################################## save_system_AtTRXh1 _Saveframe_category molecular_system _Mol_system_name 'Thioredoxin h1' _Abbreviation_common AtTRXh1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label AtTRXh1 $AtTRXh1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'disulfide bound and free' loop_ _Biological_function oxidoreductase stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_AtTRXh1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Thioredoxin h1' _Abbreviation_common TRXh1 _Molecular_mass . _Mol_thiol_state 'disulfide bound and free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 124 _Mol_residue_sequence ; MGHHHHHHLEMASEEGQVIA CHTVETWNEQLQKANESKTL VVVDFTASWCGPCRFIAPFF ADLAKKLPNVLFLKVDTDEL KSVASDWAIQAMPTFMFLKE GKILDKVVGAKKDELQSTIA KHLA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -9 MET 2 -8 GLY 3 -7 HIS 4 -6 HIS 5 -5 HIS 6 -4 HIS 7 -3 HIS 8 -2 HIS 9 -1 LEU 10 0 GLU 11 1 MET 12 2 ALA 13 3 SER 14 4 GLU 15 5 GLU 16 6 GLY 17 7 GLN 18 8 VAL 19 9 ILE 20 10 ALA 21 11 CYS 22 12 HIS 23 13 THR 24 14 VAL 25 15 GLU 26 16 THR 27 17 TRP 28 18 ASN 29 19 GLU 30 20 GLN 31 21 LEU 32 22 GLN 33 23 LYS 34 24 ALA 35 25 ASN 36 26 GLU 37 27 SER 38 28 LYS 39 29 THR 40 30 LEU 41 31 VAL 42 32 VAL 43 33 VAL 44 34 ASP 45 35 PHE 46 36 THR 47 37 ALA 48 38 SER 49 39 TRP 50 40 CYS 51 41 GLY 52 42 PRO 53 43 CYS 54 44 ARG 55 45 PHE 56 46 ILE 57 47 ALA 58 48 PRO 59 49 PHE 60 50 PHE 61 51 ALA 62 52 ASP 63 53 LEU 64 54 ALA 65 55 LYS 66 56 LYS 67 57 LEU 68 58 PRO 69 59 ASN 70 60 VAL 71 61 LEU 72 62 PHE 73 63 LEU 74 64 LYS 75 65 VAL 76 66 ASP 77 67 THR 78 68 ASP 79 69 GLU 80 70 LEU 81 71 LYS 82 72 SER 83 73 VAL 84 74 ALA 85 75 SER 86 76 ASP 87 77 TRP 88 78 ALA 89 79 ILE 90 80 GLN 91 81 ALA 92 82 MET 93 83 PRO 94 84 THR 95 85 PHE 96 86 MET 97 87 PHE 98 88 LEU 99 89 LYS 100 90 GLU 101 91 GLY 102 92 LYS 103 93 ILE 104 94 LEU 105 95 ASP 106 96 LYS 107 97 VAL 108 98 VAL 109 99 GLY 110 100 ALA 111 101 LYS 112 102 LYS 113 103 ASP 114 104 GLU 115 105 LEU 116 106 GLN 117 107 SER 118 108 THR 119 109 ILE 120 110 ALA 121 111 LYS 122 112 HIS 123 113 LEU 124 114 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-25 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1XFL "Solution Structure Of Thioredoxin H1 From Arabidopsis Thaliana" 100.00 124 100.00 100.00 5.23e-85 EMBL CAA78462 "Thioredoxin H [Arabidopsis thaliana]" 91.94 114 100.00 100.00 1.61e-76 EMBL CAB62625 "thioredoxin h [Arabidopsis thaliana]" 91.94 114 100.00 100.00 1.61e-76 GB AAC49354 "thioredoxin h [Arabidopsis thaliana]" 91.94 114 100.00 100.00 1.61e-76 GB AAM67008 "thioredoxin h [Arabidopsis thaliana]" 91.94 114 100.00 100.00 1.61e-76 GB AEE78739 "thioredoxin H1 [Arabidopsis thaliana]" 91.94 114 100.00 100.00 1.61e-76 GB EFH54044 "hypothetical protein ARALYDRAFT_485455 [Arabidopsis lyrata subsp. lyrata]" 91.94 114 100.00 100.00 1.61e-76 REF NP_190672 "thioredoxin H1 [Arabidopsis thaliana]" 91.94 114 100.00 100.00 1.61e-76 REF XP_002877785 "hypothetical protein ARALYDRAFT_485455 [Arabidopsis lyrata subsp. lyrata]" 91.94 114 100.00 100.00 1.61e-76 SP P29448 "RecName: Full=Thioredoxin H1; Short=AtTrxh1; AltName: Full=Thioredoxin 1; Short=AtTRX1 [Arabidopsis thaliana]" 91.94 114 100.00 100.00 1.61e-76 stop_ 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 $AtTRXh1 'Thale cress' 3702 Eukaryota Viridiplantae Arabidopsis thaliana At3g51030 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 _Details $AtTRXh1 'recombinant technology' 'Wheat germ' Triticum aestivum . plasmid pEU(N)His6 'Wheat germ cell-free expression system.' 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 $AtTRXh1 0.5 mM '[U-13C; U-15N]' KCl 50 mM . 'potassium phosphate buffer' 10 mM . H20 90 % . D20 10 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 3.1 loop_ _Task collection stop_ _Details 'Bruker Biospin' save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 2.1 loop_ _Task processing stop_ _Details . _Citation_label $ref_1 save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.1 loop_ _Task analysis stop_ _Details . _Citation_label $ref_2 save_ save_SPSCAN _Saveframe_category software _Name SPSCAN _Version 1.1.0 loop_ _Task 'peak picking' stop_ _Details 'Ralf W. Glaser' save_ save_GARANT _Saveframe_category software _Name GARANT _Version 2.1 loop_ _Task 'automated backbone assignments' stop_ _Details . _Citation_label $ref_3 save_ save_TALOS _Saveframe_category software _Name TALOS _Version . loop_ _Task 'generation of torsion angle restraints' stop_ _Details . _Citation_label $ref_4 save_ save_CYANA _Saveframe_category software _Name CYANA _Version 1.0.6 loop_ _Task 'refinement (torsion angle dynamics)' stop_ _Details 'CANDID module used for automated NOE crosspeak assignment.' _Citation_label $ref_5 save_ save_XPLOR-NIH _Saveframe_category software _Name XPLOR-NIH _Version 2.0.6 loop_ _Task 'refinement (cartesian MD in explicit solvent)' stop_ _Details . _Citation_label $ref_6 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample_1 save_ save_C(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _Sample_label $sample_1 save_ save_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_1 save_ save_3D_15N-NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-NOESY' _Sample_label $sample_1 save_ save_3D_13C-NOESY-aliphatic_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-NOESY-aliphatic' _Sample_label $sample_1 save_ save_3D_13C-NOESY-aromatic_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-NOESY-aromatic' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_7 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_8 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-NOESY-aliphatic' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-NOESY-aromatic' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 . n/a temperature 298 . K 'ionic strength' 50 . mM 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 . direct . . . 1.0 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name AtTRXh1 _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 . 10 GLU C C 177.2 0.15 1 2 . 11 MET N N 122.3 0.15 1 3 . 11 MET H H 8.48 0.02 1 4 . 11 MET CA C 56.6 0.15 1 5 . 11 MET HA H 4.29 0.02 1 6 . 11 MET CB C 36.1 0.15 1 7 . 11 MET HB2 H 2.29 0.02 1 8 . 11 MET HB3 H 2.29 0.02 1 9 . 11 MET CG C 30.2 0.15 1 10 . 11 MET HG2 H 2.08 0.02 2 11 . 11 MET HG3 H 1.92 0.02 2 12 . 11 MET C C 176.4 0.15 1 13 . 12 ALA N N 125.3 0.15 1 14 . 12 ALA H H 8.37 0.02 1 15 . 12 ALA CA C 53.1 0.15 1 16 . 12 ALA HA H 4.30 0.02 1 17 . 12 ALA HB H 1.39 0.02 1 18 . 12 ALA CB C 19.2 0.15 1 19 . 12 ALA C C 178.0 0.15 1 20 . 13 SER N N 114.6 0.15 1 21 . 13 SER H H 8.24 0.02 1 22 . 13 SER CA C 58.8 0.15 1 23 . 13 SER HA H 4.41 0.02 1 24 . 13 SER CB C 64.2 0.15 1 25 . 13 SER HB2 H 3.86 0.02 1 26 . 13 SER HB3 H 3.86 0.02 1 27 . 13 SER C C 174.7 0.15 1 28 . 14 GLU N N 122.5 0.15 1 29 . 14 GLU H H 8.32 0.02 1 30 . 14 GLU CA C 56.6 0.15 1 31 . 14 GLU HA H 4.33 0.02 1 32 . 14 GLU CB C 30.5 0.15 1 33 . 14 GLU HB2 H 2.08 0.02 2 34 . 14 GLU HB3 H 1.92 0.02 2 35 . 14 GLU CG C 36.3 0.15 1 36 . 14 GLU HG2 H 2.27 0.02 1 37 . 14 GLU HG3 H 2.27 0.02 1 38 . 14 GLU C C 176.2 0.15 1 39 . 15 GLU N N 121.0 0.15 1 40 . 15 GLU H H 8.17 0.02 1 41 . 15 GLU CA C 56.5 0.15 1 42 . 15 GLU HA H 4.41 0.02 1 43 . 15 GLU CB C 31.5 0.15 1 44 . 15 GLU HB2 H 2.01 0.02 1 45 . 15 GLU HB3 H 2.01 0.02 1 46 . 15 GLU CG C 36.4 0.15 1 47 . 15 GLU HG2 H 2.27 0.02 1 48 . 15 GLU HG3 H 2.27 0.02 1 49 . 15 GLU C C 177.5 0.15 1 50 . 16 GLY N N 110.8 0.15 1 51 . 16 GLY H H 8.66 0.02 1 52 . 16 GLY CA C 45.8 0.15 1 53 . 16 GLY HA2 H 4.04 0.02 2 54 . 16 GLY HA3 H 3.96 0.02 2 55 . 16 GLY C C 173.1 0.15 1 56 . 17 GLN N N 115.8 0.15 1 57 . 17 GLN H H 7.69 0.02 1 58 . 17 GLN CA C 54.4 0.15 1 59 . 17 GLN HA H 4.42 0.02 1 60 . 17 GLN CB C 31.5 0.15 1 61 . 17 GLN HB2 H 2.01 0.02 2 62 . 17 GLN HB3 H 1.79 0.02 2 63 . 17 GLN CG C 33.8 0.15 1 64 . 17 GLN HG2 H 2.20 0.02 1 65 . 17 GLN HG3 H 2.20 0.02 1 66 . 17 GLN NE2 N 112.7 0.15 1 67 . 17 GLN HE21 H 7.45 0.02 2 68 . 17 GLN HE22 H 6.81 0.02 2 69 . 17 GLN C C 175.1 0.15 1 70 . 18 VAL N N 122.6 0.15 1 71 . 18 VAL H H 8.27 0.02 1 72 . 18 VAL CA C 62.6 0.15 1 73 . 18 VAL HA H 4.00 0.02 1 74 . 18 VAL CB C 32.6 0.15 1 75 . 18 VAL HB H 1.96 0.02 1 76 . 18 VAL HG1 H 0.86 0.02 2 77 . 18 VAL HG2 H 0.75 0.02 2 78 . 18 VAL CG1 C 22.9 0.15 1 79 . 18 VAL CG2 C 22.8 0.15 1 80 . 18 VAL C C 176.3 0.15 1 81 . 19 ILE N N 131.3 0.15 1 82 . 19 ILE H H 8.93 0.02 1 83 . 19 ILE CA C 60.5 0.15 1 84 . 19 ILE HA H 4.18 0.02 1 85 . 19 ILE CB C 37.8 0.15 1 86 . 19 ILE HB H 2.00 0.02 1 87 . 19 ILE HG2 H 0.69 0.02 1 88 . 19 ILE CG2 C 16.6 0.15 1 89 . 19 ILE CG1 C 27.2 0.15 1 90 . 19 ILE HG12 H 1.42 0.02 2 91 . 19 ILE HG13 H 1.25 0.02 2 92 . 19 ILE HD1 H 0.74 0.02 1 93 . 19 ILE CD1 C 12.3 0.15 1 94 . 19 ILE C C 175.1 0.15 1 95 . 20 ALA N N 131.5 0.15 1 96 . 20 ALA H H 8.71 0.02 1 97 . 20 ALA CA C 51.2 0.15 1 98 . 20 ALA HA H 4.63 0.02 1 99 . 20 ALA HB H 1.14 0.02 1 100 . 20 ALA CB C 19.3 0.15 1 101 . 20 ALA C C 176.7 0.15 1 102 . 21 CYS N N 121.0 0.15 1 103 . 21 CYS H H 7.93 0.02 1 104 . 21 CYS CA C 57.8 0.15 1 105 . 21 CYS HA H 4.59 0.02 1 106 . 21 CYS CB C 28.3 0.15 1 107 . 21 CYS HB2 H 3.08 0.02 2 108 . 21 CYS HB3 H 2.58 0.02 2 109 . 21 CYS C C 174.3 0.15 1 110 . 22 HIS N N 120.7 0.15 1 111 . 22 HIS H H 9.10 0.02 1 112 . 22 HIS CA C 57.0 0.15 1 113 . 22 HIS HA H 4.68 0.02 1 114 . 22 HIS CB C 29.6 0.15 1 115 . 22 HIS HB2 H 3.49 0.02 2 116 . 22 HIS HB3 H 3.24 0.02 2 117 . 22 HIS CD2 C 120.7 0.15 1 118 . 22 HIS CE1 C 136.9 0.15 1 119 . 22 HIS HD2 H 7.36 0.02 1 120 . 22 HIS HE1 H 8.58 0.02 1 121 . 22 HIS C C 173.0 0.15 1 122 . 23 THR N N 104.6 0.15 1 123 . 23 THR H H 7.33 0.02 1 124 . 23 THR CA C 58.6 0.15 1 125 . 23 THR HA H 4.82 0.02 1 126 . 23 THR CB C 72.9 0.15 1 127 . 23 THR HB H 4.81 0.02 1 128 . 23 THR HG2 H 1.28 0.02 1 129 . 23 THR CG2 C 21.8 0.15 1 130 . 23 THR C C 174.7 0.15 1 131 . 24 VAL N N 123.3 0.15 1 132 . 24 VAL H H 9.21 0.02 1 133 . 24 VAL CA C 66.1 0.15 1 134 . 24 VAL HA H 3.77 0.02 1 135 . 24 VAL CB C 32.2 0.15 1 136 . 24 VAL HB H 2.11 0.02 1 137 . 24 VAL HG1 H 1.10 0.02 2 138 . 24 VAL HG2 H 1.06 0.02 2 139 . 24 VAL CG1 C 23.1 0.15 1 140 . 24 VAL CG2 C 21.5 0.15 1 141 . 24 VAL C C 177.2 0.15 1 142 . 25 GLU N N 120.3 0.15 1 143 . 25 GLU H H 8.78 0.02 1 144 . 25 GLU CA C 61.5 0.15 1 145 . 25 GLU HA H 4.18 0.02 1 146 . 25 GLU CB C 28.9 0.15 1 147 . 25 GLU HB2 H 2.20 0.02 2 148 . 25 GLU HB3 H 2.01 0.02 2 149 . 25 GLU CG C 37.8 0.15 1 150 . 25 GLU HG2 H 2.52 0.02 2 151 . 25 GLU HG3 H 2.33 0.02 2 152 . 25 GLU C C 179.6 0.15 1 153 . 26 THR N N 116.4 0.15 1 154 . 26 THR H H 8.12 0.02 1 155 . 26 THR CA C 66.7 0.15 1 156 . 26 THR HA H 4.15 0.02 1 157 . 26 THR CB C 69.4 0.15 1 158 . 26 THR HB H 4.23 0.02 1 159 . 26 THR HG2 H 1.50 0.02 1 160 . 26 THR CG2 C 23.0 0.15 1 161 . 26 THR C C 176.4 0.15 1 162 . 27 TRP N N 123.2 0.15 1 163 . 27 TRP H H 7.73 0.02 1 164 . 27 TRP CA C 60.7 0.15 1 165 . 27 TRP HA H 4.49 0.02 1 166 . 27 TRP CB C 30.3 0.15 1 167 . 27 TRP HB2 H 3.56 0.02 2 168 . 27 TRP HB3 H 2.99 0.02 2 169 . 27 TRP CD1 C 127.6 0.15 1 170 . 27 TRP CE3 C 120.1 0.15 1 171 . 27 TRP NE1 N 129.0 0.15 1 172 . 27 TRP HD1 H 7.19 0.02 1 173 . 27 TRP HE3 H 7.32 0.02 1 174 . 27 TRP CZ3 C 122.0 0.15 1 175 . 27 TRP CZ2 C 114.4 0.15 1 176 . 27 TRP HE1 H 10.20 0.02 1 177 . 27 TRP HZ3 H 6.35 0.02 1 178 . 27 TRP CH2 C 122.2 0.15 1 179 . 27 TRP HZ2 H 6.75 0.02 1 180 . 27 TRP HH2 H 6.31 0.02 1 181 . 27 TRP C C 175.8 0.15 1 182 . 28 ASN N N 115.3 0.15 1 183 . 28 ASN H H 8.80 0.02 1 184 . 28 ASN CA C 56.3 0.15 1 185 . 28 ASN HA H 4.13 0.02 1 186 . 28 ASN CB C 38.3 0.15 1 187 . 28 ASN HB2 H 2.93 0.02 2 188 . 28 ASN HB3 H 2.73 0.02 2 189 . 28 ASN ND2 N 111.8 0.15 1 190 . 28 ASN HD21 H 7.61 0.02 2 191 . 28 ASN HD22 H 6.97 0.02 2 192 . 28 ASN C C 178.8 0.15 1 193 . 29 GLU N N 121.0 0.15 1 194 . 29 GLU H H 8.29 0.02 1 195 . 29 GLU CA C 59.7 0.15 1 196 . 29 GLU HA H 4.00 0.02 1 197 . 29 GLU CB C 30.3 0.15 1 198 . 29 GLU HB2 H 2.25 0.02 2 199 . 29 GLU HB3 H 2.15 0.02 2 200 . 29 GLU CG C 36.7 0.15 1 201 . 29 GLU HG2 H 2.43 0.02 2 202 . 29 GLU HG3 H 2.16 0.02 2 203 . 29 GLU C C 179.4 0.15 1 204 . 30 GLN N N 118.5 0.15 1 205 . 30 GLN H H 8.31 0.02 1 206 . 30 GLN CA C 58.4 0.15 1 207 . 30 GLN HA H 3.84 0.02 1 208 . 30 GLN CB C 28.1 0.15 1 209 . 30 GLN HB2 H 2.04 0.02 2 210 . 30 GLN HB3 H 1.89 0.02 2 211 . 30 GLN CG C 33.8 0.15 1 212 . 30 GLN HG2 H 2.73 0.02 2 213 . 30 GLN HG3 H 2.03 0.02 2 214 . 30 GLN NE2 N 111.6 0.15 1 215 . 30 GLN HE21 H 7.18 0.02 2 216 . 30 GLN HE22 H 6.64 0.02 2 217 . 30 GLN C C 178.8 0.15 1 218 . 31 LEU N N 118.7 0.15 1 219 . 31 LEU H H 7.85 0.02 1 220 . 31 LEU CA C 58.2 0.15 1 221 . 31 LEU HA H 3.61 0.02 1 222 . 31 LEU CB C 40.9 0.15 1 223 . 31 LEU HB2 H 1.33 0.02 2 224 . 31 LEU HB3 H 1.12 0.02 2 225 . 31 LEU CG C 27.2 0.15 1 226 . 31 LEU HG H 0.78 0.02 1 227 . 31 LEU HD1 H 0.00 0.02 2 228 . 31 LEU HD2 H 0.07 0.02 2 229 . 31 LEU CD1 C 23.4 0.15 1 230 . 31 LEU CD2 C 21.8 0.15 1 231 . 31 LEU C C 180.0 0.15 1 232 . 32 GLN N N 119.7 0.15 1 233 . 32 GLN H H 8.06 0.02 1 234 . 32 GLN CA C 59.4 0.15 1 235 . 32 GLN HA H 3.98 0.02 1 236 . 32 GLN CB C 27.9 0.15 1 237 . 32 GLN HB2 H 2.11 0.02 1 238 . 32 GLN HB3 H 2.11 0.02 1 239 . 32 GLN CG C 33.8 0.15 1 240 . 32 GLN HG2 H 2.39 0.02 1 241 . 32 GLN HG3 H 2.39 0.02 1 242 . 32 GLN NE2 N 112.3 0.15 1 243 . 32 GLN HE21 H 7.57 0.02 2 244 . 32 GLN HE22 H 6.80 0.02 2 245 . 32 GLN C C 179.1 0.15 1 246 . 33 LYS N N 120.6 0.15 1 247 . 33 LYS H H 7.95 0.02 1 248 . 33 LYS CA C 59.3 0.15 1 249 . 33 LYS HA H 4.01 0.02 1 250 . 33 LYS CB C 32.3 0.15 1 251 . 33 LYS HB2 H 1.86 0.02 1 252 . 33 LYS HB3 H 1.86 0.02 1 253 . 33 LYS CG C 25.2 0.15 1 254 . 33 LYS HG2 H 1.55 0.02 2 255 . 33 LYS HG3 H 1.38 0.02 2 256 . 33 LYS CD C 29.6 0.15 1 257 . 33 LYS HD2 H 1.63 0.02 1 258 . 33 LYS HD3 H 1.63 0.02 1 259 . 33 LYS CE C 42.0 0.15 1 260 . 33 LYS HE2 H 2.92 0.02 1 261 . 33 LYS HE3 H 2.92 0.02 1 262 . 33 LYS C C 179.8 0.15 1 263 . 34 ALA N N 121.6 0.15 1 264 . 34 ALA H H 8.08 0.02 1 265 . 34 ALA CA C 54.5 0.15 1 266 . 34 ALA HA H 4.13 0.02 1 267 . 34 ALA HB H 1.27 0.02 1 268 . 34 ALA CB C 18.6 0.15 1 269 . 34 ALA C C 181.3 0.15 1 270 . 35 ASN N N 120.5 0.15 1 271 . 35 ASN H H 8.36 0.02 1 272 . 35 ASN CA C 56.4 0.15 1 273 . 35 ASN HA H 4.38 0.02 1 274 . 35 ASN CB C 38.1 0.15 1 275 . 35 ASN HB2 H 2.95 0.02 2 276 . 35 ASN HB3 H 2.86 0.02 2 277 . 35 ASN ND2 N 110.1 0.15 1 278 . 35 ASN HD21 H 7.37 0.02 2 279 . 35 ASN HD22 H 6.53 0.02 2 280 . 35 ASN C C 177.9 0.15 1 281 . 36 GLU N N 119.4 0.15 1 282 . 36 GLU H H 7.76 0.02 1 283 . 36 GLU CA C 58.7 0.15 1 284 . 36 GLU HA H 4.10 0.02 1 285 . 36 GLU CB C 30.0 0.15 1 286 . 36 GLU HB2 H 2.15 0.02 1 287 . 36 GLU HB3 H 2.15 0.02 1 288 . 36 GLU CG C 36.4 0.15 1 289 . 36 GLU HG2 H 2.46 0.02 2 290 . 36 GLU HG3 H 2.31 0.02 2 291 . 36 GLU C C 178.0 0.15 1 292 . 37 SER N N 112.1 0.15 1 293 . 37 SER H H 7.91 0.02 1 294 . 37 SER CA C 58.7 0.15 1 295 . 37 SER HA H 4.42 0.02 1 296 . 37 SER CB C 64.2 0.15 1 297 . 37 SER HB2 H 4.03 0.02 2 298 . 37 SER HB3 H 3.87 0.02 2 299 . 37 SER C C 174.5 0.15 1 300 . 38 LYS N N 117.6 0.15 1 301 . 38 LYS H H 7.88 0.02 1 302 . 38 LYS CA C 58.0 0.15 1 303 . 38 LYS HA H 3.78 0.02 1 304 . 38 LYS CB C 29.6 0.15 1 305 . 38 LYS HB2 H 2.18 0.02 2 306 . 38 LYS HB3 H 1.88 0.02 2 307 . 38 LYS CG C 25.7 0.15 1 308 . 38 LYS HG2 H 1.32 0.02 2 309 . 38 LYS HG3 H 1.26 0.02 2 310 . 38 LYS CD C 29.9 0.15 1 311 . 38 LYS HD2 H 1.67 0.02 1 312 . 38 LYS HD3 H 1.67 0.02 1 313 . 38 LYS CE C 42.8 0.15 1 314 . 38 LYS HE2 H 3.02 0.02 1 315 . 38 LYS HE3 H 3.02 0.02 1 316 . 38 LYS C C 174.9 0.15 1 317 . 39 THR N N 114.6 0.15 1 318 . 39 THR H H 7.75 0.02 1 319 . 39 THR CA C 62.6 0.15 1 320 . 39 THR HA H 4.27 0.02 1 321 . 39 THR CB C 70.9 0.15 1 322 . 39 THR HB H 3.86 0.02 1 323 . 39 THR HG2 H 1.25 0.02 1 324 . 39 THR CG2 C 21.8 0.15 1 325 . 39 THR C C 174.4 0.15 1 326 . 40 LEU N N 128.1 0.15 1 327 . 40 LEU H H 8.88 0.02 1 328 . 40 LEU CA C 56.4 0.15 1 329 . 40 LEU HA H 4.40 0.02 1 330 . 40 LEU CB C 42.3 0.15 1 331 . 40 LEU HB2 H 1.94 0.02 2 332 . 40 LEU HB3 H 1.48 0.02 2 333 . 40 LEU CG C 27.0 0.15 1 334 . 40 LEU HG H 1.46 0.02 1 335 . 40 LEU HD1 H 0.91 0.02 2 336 . 40 LEU HD2 H 0.98 0.02 2 337 . 40 LEU CD1 C 26.7 0.15 1 338 . 40 LEU CD2 C 24.1 0.15 1 339 . 40 LEU C C 173.7 0.15 1 340 . 41 VAL N N 128.2 0.15 1 341 . 41 VAL H H 9.02 0.02 1 342 . 41 VAL CA C 60.2 0.15 1 343 . 41 VAL HA H 4.88 0.02 1 344 . 41 VAL CB C 34.6 0.15 1 345 . 41 VAL HB H 1.83 0.02 1 346 . 41 VAL HG1 H 0.76 0.02 2 347 . 41 VAL HG2 H 0.55 0.02 2 348 . 41 VAL CG1 C 22.8 0.15 1 349 . 41 VAL CG2 C 21.6 0.15 1 350 . 41 VAL C C 175.0 0.15 1 351 . 42 VAL N N 126.4 0.15 1 352 . 42 VAL H H 8.95 0.02 1 353 . 42 VAL CA C 60.4 0.15 1 354 . 42 VAL HA H 4.44 0.02 1 355 . 42 VAL CB C 32.9 0.15 1 356 . 42 VAL HB H 1.38 0.02 1 357 . 42 VAL HG1 H 0.37 0.02 2 358 . 42 VAL HG2 H 0.14 0.02 2 359 . 42 VAL CG1 C 21.5 0.15 1 360 . 42 VAL CG2 C 20.8 0.15 1 361 . 42 VAL C C 174.6 0.15 1 362 . 43 VAL N N 125.9 0.15 1 363 . 43 VAL H H 9.16 0.02 1 364 . 43 VAL CA C 60.3 0.15 1 365 . 43 VAL HA H 4.67 0.02 1 366 . 43 VAL CB C 34.6 0.15 1 367 . 43 VAL HB H 1.77 0.02 1 368 . 43 VAL HG1 H 0.76 0.02 2 369 . 43 VAL HG2 H 0.04 0.02 2 370 . 43 VAL CG1 C 21.2 0.15 1 371 . 43 VAL CG2 C 21.5 0.15 1 372 . 43 VAL C C 175.2 0.15 1 373 . 44 ASP N N 123.5 0.15 1 374 . 44 ASP H H 8.78 0.02 1 375 . 44 ASP CA C 51.3 0.15 1 376 . 44 ASP HA H 4.29 0.02 1 377 . 44 ASP CB C 38.9 0.15 1 378 . 44 ASP HB2 H 2.27 0.02 2 379 . 44 ASP HB3 H 1.34 0.02 2 380 . 44 ASP C C 174.3 0.15 1 381 . 45 PHE N N 125.7 0.15 1 382 . 45 PHE H H 8.74 0.02 1 383 . 45 PHE CA C 58.7 0.15 1 384 . 45 PHE HA H 4.86 0.02 1 385 . 45 PHE CB C 39.3 0.15 1 386 . 45 PHE HB2 H 3.05 0.02 2 387 . 45 PHE HB3 H 2.42 0.02 2 388 . 45 PHE HD1 H 6.86 0.02 1 389 . 45 PHE HD2 H 6.86 0.02 1 390 . 45 PHE HE1 H 6.68 0.02 1 391 . 45 PHE HE2 H 6.68 0.02 1 392 . 45 PHE CD1 C 131.8 0.15 1 393 . 45 PHE CE1 C 130.2 0.15 1 394 . 45 PHE CZ C 129.2 0.15 1 395 . 45 PHE HZ H 6.38 0.02 1 396 . 45 PHE C C 173.2 0.15 1 397 . 46 THR N N 117.2 0.15 1 398 . 46 THR H H 8.46 0.02 1 399 . 46 THR CA C 58.7 0.15 1 400 . 46 THR HA H 4.42 0.02 1 401 . 46 THR CB C 71.0 0.15 1 402 . 46 THR HB H 3.44 0.02 1 403 . 46 THR HG2 H 0.75 0.02 1 404 . 46 THR CG2 C 18.9 0.15 1 405 . 46 THR C C 170.4 0.15 1 406 . 47 ALA N N 121.0 0.15 1 407 . 47 ALA H H 7.01 0.02 1 408 . 47 ALA CA C 52.0 0.15 1 409 . 47 ALA HA H 4.56 0.02 1 410 . 47 ALA HB H 0.37 0.02 1 411 . 47 ALA CB C 21.6 0.15 1 412 . 47 ALA C C 179.2 0.15 1 413 . 48 SER N N 119.8 0.15 1 414 . 48 SER H H 9.44 0.02 1 415 . 48 SER CA C 61.7 0.15 1 416 . 48 SER HA H 3.99 0.02 1 417 . 48 SER CB C 63.3 0.15 1 418 . 48 SER HB2 H 3.94 0.02 1 419 . 48 SER HB3 H 3.94 0.02 1 420 . 48 SER C C 174.8 0.15 1 421 . 49 TRP N N 116.6 0.15 1 422 . 49 TRP H H 6.63 0.02 1 423 . 49 TRP CA C 54.1 0.15 1 424 . 49 TRP HA H 4.58 0.02 1 425 . 49 TRP CB C 29.6 0.15 1 426 . 49 TRP HB2 H 3.69 0.02 2 427 . 49 TRP HB3 H 3.14 0.02 2 428 . 49 TRP CD1 C 128.9 0.15 1 429 . 49 TRP CE3 C 121.2 0.15 1 430 . 49 TRP NE1 N 134.9 0.15 1 431 . 49 TRP HD1 H 7.35 0.02 1 432 . 49 TRP HE3 H 7.36 0.02 1 433 . 49 TRP CZ3 C 122.0 0.15 1 434 . 49 TRP CZ2 C 115.5 0.15 1 435 . 49 TRP HE1 H 11.10 0.02 1 436 . 49 TRP HZ3 H 7.11 0.02 1 437 . 49 TRP CH2 C 125.2 0.15 1 438 . 49 TRP HZ2 H 7.49 0.02 1 439 . 49 TRP HH2 H 7.18 0.02 1 440 . 49 TRP C C 175.7 0.15 1 441 . 50 CYS N N 122.0 0.15 1 442 . 50 CYS H H 6.60 0.02 1 443 . 50 CYS CA C 54.0 0.15 1 444 . 50 CYS HA H 4.58 0.02 1 445 . 50 CYS CB C 44.9 0.15 1 446 . 50 CYS HB2 H 2.80 0.02 1 447 . 50 CYS HB3 H 2.80 0.02 1 448 . 50 CYS C C 174.6 0.15 1 449 . 51 GLY N N 121.4 0.15 1 450 . 51 GLY H H 9.57 0.02 1 451 . 51 GLY CA C 48.7 0.15 1 452 . 51 GLY HA2 H 4.27 0.02 2 453 . 51 GLY HA3 H 3.94 0.02 2 454 . 51 GLY C C 175.4 0.15 1 455 . 52 PRO CD C 51.9 0.15 1 456 . 52 PRO CA C 65.4 0.15 1 457 . 52 PRO HA H 4.51 0.02 1 458 . 52 PRO CB C 32.8 0.15 1 459 . 52 PRO HB2 H 2.63 0.02 2 460 . 52 PRO HB3 H 1.84 0.02 2 461 . 52 PRO CG C 28.7 0.15 1 462 . 52 PRO HG2 H 2.32 0.02 2 463 . 52 PRO HG3 H 2.08 0.02 2 464 . 52 PRO HD2 H 3.98 0.02 2 465 . 52 PRO HD3 H 3.84 0.02 2 466 . 52 PRO C C 178.0 0.15 1 467 . 53 CYS N N 110.8 0.15 1 468 . 53 CYS H H 8.09 0.02 1 469 . 53 CYS CA C 63.7 0.15 1 470 . 53 CYS HA H 4.17 0.02 1 471 . 53 CYS CB C 34.6 0.15 1 472 . 53 CYS HB2 H 3.83 0.02 2 473 . 53 CYS HB3 H 3.34 0.02 2 474 . 53 CYS C C 176.4 0.15 1 475 . 54 ARG N N 121.3 0.15 1 476 . 54 ARG H H 7.86 0.02 1 477 . 54 ARG CA C 59.2 0.15 1 478 . 54 ARG HA H 4.11 0.02 1 479 . 54 ARG CB C 30.4 0.15 1 480 . 54 ARG HB2 H 2.05 0.02 2 481 . 54 ARG HB3 H 1.95 0.02 2 482 . 54 ARG CG C 27.6 0.15 1 483 . 54 ARG HG2 H 1.86 0.02 2 484 . 54 ARG HG3 H 1.60 0.02 2 485 . 54 ARG CD C 43.6 0.15 1 486 . 54 ARG HD2 H 3.34 0.02 2 487 . 54 ARG HD3 H 3.25 0.02 2 488 . 54 ARG C C 179.3 0.15 1 489 . 55 PHE N N 118.7 0.15 1 490 . 55 PHE H H 7.84 0.02 1 491 . 55 PHE CA C 60.1 0.15 1 492 . 55 PHE HA H 4.45 0.02 1 493 . 55 PHE CB C 39.0 0.15 1 494 . 55 PHE HB2 H 3.33 0.02 1 495 . 55 PHE HB3 H 3.33 0.02 1 496 . 55 PHE HD1 H 7.32 0.02 1 497 . 55 PHE HD2 H 7.32 0.02 1 498 . 55 PHE HE1 H 7.41 0.02 1 499 . 55 PHE HE2 H 7.41 0.02 1 500 . 55 PHE CD1 C 132.3 0.15 1 501 . 55 PHE CE1 C 131.8 0.15 1 502 . 55 PHE C C 177.0 0.15 1 503 . 56 ILE N N 115.1 0.15 1 504 . 56 ILE H H 7.59 0.02 1 505 . 56 ILE CA C 60.2 0.15 1 506 . 56 ILE HA H 4.38 0.02 1 507 . 56 ILE CB C 41.6 0.15 1 508 . 56 ILE HB H 1.88 0.02 1 509 . 56 ILE HG2 H 1.27 0.02 1 510 . 56 ILE CG2 C 17.9 0.15 1 511 . 56 ILE CG1 C 31.8 0.15 1 512 . 56 ILE HG12 H 1.72 0.02 1 513 . 56 ILE HG13 H 1.72 0.02 1 514 . 56 ILE HD1 H 0.79 0.02 1 515 . 56 ILE CD1 C 15.0 0.15 1 516 . 56 ILE C C 175.3 0.15 1 517 . 57 ALA N N 127.1 0.15 1 518 . 57 ALA H H 7.41 0.02 1 519 . 57 ALA CA C 57.4 0.15 1 520 . 57 ALA HA H 4.26 0.02 1 521 . 57 ALA HB H 1.64 0.02 1 522 . 57 ALA CB C 16.3 0.15 1 523 . 57 ALA C C 177.0 0.15 1 524 . 58 PRO CD C 50.9 0.15 1 525 . 58 PRO CA C 66.1 0.15 1 526 . 58 PRO HA H 4.41 0.02 1 527 . 58 PRO CB C 31.1 0.15 1 528 . 58 PRO HB2 H 2.35 0.02 2 529 . 58 PRO HB3 H 1.90 0.02 2 530 . 58 PRO CG C 28.6 0.15 1 531 . 58 PRO HG2 H 2.08 0.02 2 532 . 58 PRO HG3 H 1.98 0.02 2 533 . 58 PRO HD2 H 3.81 0.02 2 534 . 58 PRO HD3 H 3.72 0.02 2 535 . 58 PRO C C 178.8 0.15 1 536 . 59 PHE N N 119.6 0.15 1 537 . 59 PHE H H 7.25 0.02 1 538 . 59 PHE CA C 60.9 0.15 1 539 . 59 PHE HA H 4.35 0.02 1 540 . 59 PHE CB C 39.7 0.15 1 541 . 59 PHE HB2 H 3.32 0.02 2 542 . 59 PHE HB3 H 3.16 0.02 2 543 . 59 PHE HD1 H 7.19 0.02 1 544 . 59 PHE HD2 H 7.19 0.02 1 545 . 59 PHE HE1 H 7.26 0.02 1 546 . 59 PHE HE2 H 7.26 0.02 1 547 . 59 PHE CD1 C 131.8 0.15 1 548 . 59 PHE CE1 C 128.9 0.15 1 549 . 59 PHE C C 176.9 0.15 1 550 . 60 PHE N N 120.9 0.15 1 551 . 60 PHE H H 8.19 0.02 1 552 . 60 PHE CA C 62.2 0.15 1 553 . 60 PHE HA H 3.92 0.02 1 554 . 60 PHE CB C 40.0 0.15 1 555 . 60 PHE HB2 H 3.40 0.02 2 556 . 60 PHE HB3 H 2.97 0.02 2 557 . 60 PHE HD1 H 7.29 0.02 1 558 . 60 PHE HD2 H 7.29 0.02 1 559 . 60 PHE HE1 H 7.63 0.02 1 560 . 60 PHE HE2 H 7.63 0.02 1 561 . 60 PHE CD1 C 132.4 0.15 1 562 . 60 PHE CE1 C 131.9 0.15 1 563 . 60 PHE C C 175.6 0.15 1 564 . 61 ALA N N 117.2 0.15 1 565 . 61 ALA H H 7.72 0.02 1 566 . 61 ALA CA C 54.6 0.15 1 567 . 61 ALA HA H 3.74 0.02 1 568 . 61 ALA HB H 1.43 0.02 1 569 . 61 ALA CB C 17.9 0.15 1 570 . 61 ALA C C 180.2 0.15 1 571 . 62 ASP N N 121.0 0.15 1 572 . 62 ASP H H 7.86 0.02 1 573 . 62 ASP CA C 57.4 0.15 1 574 . 62 ASP HA H 4.22 0.02 1 575 . 62 ASP CB C 41.3 0.15 1 576 . 62 ASP HB2 H 2.65 0.02 2 577 . 62 ASP HB3 H 2.45 0.02 2 578 . 62 ASP C C 178.8 0.15 1 579 . 63 LEU N N 121.0 0.15 1 580 . 63 LEU H H 7.59 0.02 1 581 . 63 LEU CA C 57.7 0.15 1 582 . 63 LEU HA H 3.50 0.02 1 583 . 63 LEU CB C 41.5 0.15 1 584 . 63 LEU HB2 H 1.34 0.02 2 585 . 63 LEU HB3 H 0.88 0.02 2 586 . 63 LEU CG C 26.2 0.15 1 587 . 63 LEU HG H 1.06 0.02 1 588 . 63 LEU HD1 H 0.58 0.02 2 589 . 63 LEU HD2 H 0.57 0.02 2 590 . 63 LEU CD1 C 26.3 0.15 1 591 . 63 LEU CD2 C 23.0 0.15 1 592 . 63 LEU C C 177.1 0.15 1 593 . 64 ALA N N 118.5 0.15 1 594 . 64 ALA H H 6.46 0.02 1 595 . 64 ALA CA C 54.0 0.15 1 596 . 64 ALA HA H 2.84 0.02 1 597 . 64 ALA HB H 0.40 0.02 1 598 . 64 ALA CB C 18.6 0.15 1 599 . 64 ALA C C 179.8 0.15 1 600 . 65 LYS N N 115.0 0.15 1 601 . 65 LYS H H 6.90 0.02 1 602 . 65 LYS CA C 58.3 0.15 1 603 . 65 LYS HA H 3.96 0.02 1 604 . 65 LYS CB C 33.1 0.15 1 605 . 65 LYS HB2 H 1.80 0.02 1 606 . 65 LYS HB3 H 1.80 0.02 1 607 . 65 LYS CG C 25.1 0.15 1 608 . 65 LYS HG2 H 1.50 0.02 2 609 . 65 LYS HG3 H 1.38 0.02 2 610 . 65 LYS CD C 29.5 0.15 1 611 . 65 LYS HD2 H 1.66 0.02 1 612 . 65 LYS HD3 H 1.66 0.02 1 613 . 65 LYS CE C 42.2 0.15 1 614 . 65 LYS HE2 H 2.93 0.02 1 615 . 65 LYS HE3 H 2.93 0.02 1 616 . 65 LYS C C 178.7 0.15 1 617 . 66 LYS N N 117.3 0.15 1 618 . 66 LYS H H 7.27 0.02 1 619 . 66 LYS CA C 57.7 0.15 1 620 . 66 LYS HA H 4.07 0.02 1 621 . 66 LYS CB C 33.9 0.15 1 622 . 66 LYS HB2 H 1.82 0.02 1 623 . 66 LYS HB3 H 1.82 0.02 1 624 . 66 LYS CG C 25.7 0.15 1 625 . 66 LYS HG2 H 1.44 0.02 1 626 . 66 LYS HG3 H 1.44 0.02 1 627 . 66 LYS CD C 29.6 0.15 1 628 . 66 LYS HD2 H 1.51 0.02 1 629 . 66 LYS HD3 H 1.51 0.02 1 630 . 66 LYS CE C 42.1 0.15 1 631 . 66 LYS HE2 H 2.87 0.02 1 632 . 66 LYS HE3 H 2.87 0.02 1 633 . 66 LYS C C 176.4 0.15 1 634 . 67 LEU N N 119.9 0.15 1 635 . 67 LEU H H 7.34 0.02 1 636 . 67 LEU CA C 52.2 0.15 1 637 . 67 LEU HA H 4.99 0.02 1 638 . 67 LEU CB C 42.5 0.15 1 639 . 67 LEU HB2 H 1.97 0.02 2 640 . 67 LEU HB3 H 1.43 0.02 2 641 . 67 LEU CG C 26.0 0.15 1 642 . 67 LEU HG H 1.46 0.02 1 643 . 67 LEU HD1 H 0.98 0.02 2 644 . 67 LEU HD2 H 0.92 0.02 2 645 . 67 LEU CD1 C 27.6 0.15 1 646 . 67 LEU CD2 C 24.1 0.15 1 647 . 67 LEU C C 173.9 0.15 1 648 . 68 PRO CD C 50.6 0.15 1 649 . 68 PRO CA C 64.2 0.15 1 650 . 68 PRO HA H 4.72 0.02 1 651 . 68 PRO CB C 32.0 0.15 1 652 . 68 PRO HB2 H 2.10 0.02 2 653 . 68 PRO HB3 H 2.02 0.02 2 654 . 68 PRO CG C 27.3 0.15 1 655 . 68 PRO HG2 H 2.00 0.02 2 656 . 68 PRO HG3 H 1.86 0.02 2 657 . 68 PRO HD2 H 3.75 0.02 2 658 . 68 PRO HD3 H 3.33 0.02 2 659 . 68 PRO C C 176.7 0.15 1 660 . 69 ASN N N 114.6 0.15 1 661 . 69 ASN H H 8.82 0.02 1 662 . 69 ASN CA C 53.6 0.15 1 663 . 69 ASN HA H 4.68 0.02 1 664 . 69 ASN CB C 37.5 0.15 1 665 . 69 ASN HB2 H 2.90 0.02 2 666 . 69 ASN HB3 H 2.81 0.02 2 667 . 69 ASN ND2 N 113.5 0.15 1 668 . 69 ASN HD21 H 7.68 0.02 2 669 . 69 ASN HD22 H 6.66 0.02 2 670 . 69 ASN C C 173.1 0.15 1 671 . 70 VAL N N 124.6 0.15 1 672 . 70 VAL H H 7.98 0.02 1 673 . 70 VAL CA C 61.8 0.15 1 674 . 70 VAL HA H 4.01 0.02 1 675 . 70 VAL CB C 34.2 0.15 1 676 . 70 VAL HB H 2.20 0.02 1 677 . 70 VAL HG1 H 0.86 0.02 2 678 . 70 VAL HG2 H 0.18 0.02 2 679 . 70 VAL CG1 C 24.1 0.15 1 680 . 70 VAL CG2 C 22.5 0.15 1 681 . 70 VAL C C 173.1 0.15 1 682 . 71 LEU N N 128.3 0.15 1 683 . 71 LEU H H 8.15 0.02 1 684 . 71 LEU CA C 54.0 0.15 1 685 . 71 LEU HA H 4.65 0.02 1 686 . 71 LEU CB C 44.1 0.15 1 687 . 71 LEU HB2 H 1.80 0.02 2 688 . 71 LEU HB3 H 1.22 0.02 2 689 . 71 LEU CG C 27.6 0.15 1 690 . 71 LEU HG H 1.24 0.02 1 691 . 71 LEU HD1 H 0.86 0.02 2 692 . 71 LEU HD2 H 0.96 0.02 2 693 . 71 LEU CD1 C 26.5 0.15 1 694 . 71 LEU CD2 C 23.4 0.15 1 695 . 71 LEU C C 173.6 0.15 1 696 . 72 PHE N N 127.6 0.15 1 697 . 72 PHE H H 9.36 0.02 1 698 . 72 PHE CA C 56.6 0.15 1 699 . 72 PHE HA H 5.28 0.02 1 700 . 72 PHE CB C 40.3 0.15 1 701 . 72 PHE HB2 H 2.82 0.02 2 702 . 72 PHE HB3 H 2.27 0.02 2 703 . 72 PHE HD1 H 6.69 0.02 1 704 . 72 PHE HD2 H 6.69 0.02 1 705 . 72 PHE HE1 H 6.99 0.02 1 706 . 72 PHE HE2 H 6.99 0.02 1 707 . 72 PHE CD1 C 132.4 0.15 1 708 . 72 PHE CE1 C 130.5 0.15 1 709 . 72 PHE CZ C 127.9 0.15 1 710 . 72 PHE HZ H 6.71 0.02 1 711 . 72 PHE C C 174.7 0.15 1 712 . 73 LEU N N 120.6 0.15 1 713 . 73 LEU H H 8.95 0.02 1 714 . 73 LEU CA C 52.4 0.15 1 715 . 73 LEU HA H 5.57 0.02 1 716 . 73 LEU CB C 46.2 0.15 1 717 . 73 LEU HB2 H 1.70 0.02 2 718 . 73 LEU HB3 H 1.38 0.02 2 719 . 73 LEU CG C 27.3 0.15 1 720 . 73 LEU HG H 1.44 0.02 1 721 . 73 LEU HD1 H 0.58 0.02 2 722 . 73 LEU HD2 H 0.78 0.02 2 723 . 73 LEU CD1 C 26.3 0.15 1 724 . 73 LEU CD2 C 24.4 0.15 1 725 . 73 LEU C C 176.1 0.15 1 726 . 74 LYS N N 121.1 0.15 1 727 . 74 LYS H H 8.48 0.02 1 728 . 74 LYS CA C 55.1 0.15 1 729 . 74 LYS HA H 4.93 0.02 1 730 . 74 LYS CB C 36.7 0.15 1 731 . 74 LYS HB2 H 1.49 0.02 2 732 . 74 LYS HB3 H 1.41 0.02 2 733 . 74 LYS CG C 25.2 0.15 1 734 . 74 LYS HG2 H 1.24 0.02 2 735 . 74 LYS HG3 H 0.98 0.02 2 736 . 74 LYS CD C 30.1 0.15 1 737 . 74 LYS HD2 H 1.64 0.02 2 738 . 74 LYS HD3 H 1.53 0.02 2 739 . 74 LYS CE C 41.8 0.15 1 740 . 74 LYS HE2 H 2.80 0.02 1 741 . 74 LYS HE3 H 2.80 0.02 1 742 . 74 LYS C C 174.7 0.15 1 743 . 75 VAL N N 128.9 0.15 1 744 . 75 VAL H H 8.53 0.02 1 745 . 75 VAL CA C 61.7 0.15 1 746 . 75 VAL HA H 3.71 0.02 1 747 . 75 VAL CB C 35.4 0.15 1 748 . 75 VAL HB H 1.00 0.02 1 749 . 75 VAL HG1 H 0.44 0.02 2 750 . 75 VAL HG2 H 0.13 0.02 2 751 . 75 VAL CG1 C 21.8 0.15 1 752 . 75 VAL CG2 C 21.8 0.15 1 753 . 75 VAL C C 172.5 0.15 1 754 . 76 ASP N N 128.9 0.15 1 755 . 76 ASP H H 9.10 0.02 1 756 . 76 ASP CA C 52.4 0.15 1 757 . 76 ASP HA H 5.02 0.02 1 758 . 76 ASP CB C 42.2 0.15 1 759 . 76 ASP HB2 H 2.90 0.02 2 760 . 76 ASP HB3 H 2.23 0.02 2 761 . 76 ASP C C 178.0 0.15 1 762 . 77 THR N N 119.1 0.15 1 763 . 77 THR H H 9.27 0.02 1 764 . 77 THR CA C 65.2 0.15 1 765 . 77 THR HA H 3.58 0.02 1 766 . 77 THR CB C 68.3 0.15 1 767 . 77 THR HB H 4.28 0.02 1 768 . 77 THR HG2 H 1.30 0.02 1 769 . 77 THR CG2 C 23.3 0.15 1 770 . 77 THR C C 175.3 0.15 1 771 . 78 ASP N N 119.3 0.15 1 772 . 78 ASP H H 8.52 0.02 1 773 . 78 ASP CA C 56.4 0.15 1 774 . 78 ASP HA H 4.83 0.02 1 775 . 78 ASP CB C 41.2 0.15 1 776 . 78 ASP HB2 H 2.91 0.02 2 777 . 78 ASP HB3 H 2.78 0.02 2 778 . 78 ASP C C 177.4 0.15 1 779 . 79 GLU N N 121.7 0.15 1 780 . 79 GLU H H 8.02 0.02 1 781 . 79 GLU CA C 58.6 0.15 1 782 . 79 GLU HA H 4.27 0.02 1 783 . 79 GLU CB C 31.5 0.15 1 784 . 79 GLU HB2 H 2.31 0.02 2 785 . 79 GLU HB3 H 2.14 0.02 2 786 . 79 GLU CG C 37.4 0.15 1 787 . 79 GLU HG2 H 2.38 0.02 1 788 . 79 GLU HG3 H 2.38 0.02 1 789 . 79 GLU C C 177.1 0.15 1 790 . 80 LEU N N 121.7 0.15 1 791 . 80 LEU H H 8.08 0.02 1 792 . 80 LEU CA C 52.2 0.15 1 793 . 80 LEU HA H 4.81 0.02 1 794 . 80 LEU CB C 40.4 0.15 1 795 . 80 LEU HB2 H 1.41 0.02 2 796 . 80 LEU HB3 H 1.34 0.02 2 797 . 80 LEU CG C 27.0 0.15 1 798 . 80 LEU HG H 1.42 0.02 1 799 . 80 LEU HD1 H 0.55 0.02 2 800 . 80 LEU HD2 H 0.59 0.02 2 801 . 80 LEU CD1 C 25.7 0.15 1 802 . 80 LEU CD2 C 24.4 0.15 1 803 . 80 LEU C C 176.3 0.15 1 804 . 81 LYS N N 121.7 0.15 1 805 . 81 LYS H H 7.29 0.02 1 806 . 81 LYS CA C 60.1 0.15 1 807 . 81 LYS HA H 4.10 0.02 1 808 . 81 LYS CB C 33.0 0.15 1 809 . 81 LYS HB2 H 1.87 0.02 1 810 . 81 LYS HB3 H 1.87 0.02 1 811 . 81 LYS CG C 25.0 0.15 1 812 . 81 LYS HG2 H 1.56 0.02 1 813 . 81 LYS HG3 H 1.56 0.02 1 814 . 81 LYS CD C 29.6 0.15 1 815 . 81 LYS HD2 H 1.77 0.02 1 816 . 81 LYS HD3 H 1.77 0.02 1 817 . 81 LYS CE C 42.1 0.15 1 818 . 81 LYS HE2 H 3.11 0.02 1 819 . 81 LYS HE3 H 3.11 0.02 1 820 . 81 LYS C C 179.9 0.15 1 821 . 82 SER N N 114.3 0.15 1 822 . 82 SER H H 8.64 0.02 1 823 . 82 SER CA C 61.2 0.15 1 824 . 82 SER HA H 4.20 0.02 1 825 . 82 SER CB C 61.9 0.15 1 826 . 82 SER HB2 H 4.00 0.02 2 827 . 82 SER HB3 H 3.85 0.02 2 828 . 82 SER C C 176.0 0.15 1 829 . 83 VAL N N 123.8 0.15 1 830 . 83 VAL H H 6.59 0.02 1 831 . 83 VAL CA C 65.8 0.15 1 832 . 83 VAL HA H 3.81 0.02 1 833 . 83 VAL CB C 32.0 0.15 1 834 . 83 VAL HB H 1.66 0.02 1 835 . 83 VAL HG1 H 0.61 0.02 2 836 . 83 VAL HG2 H 0.08 0.02 2 837 . 83 VAL CG1 C 22.8 0.15 1 838 . 83 VAL CG2 C 20.8 0.15 1 839 . 83 VAL C C 177.6 0.15 1 840 . 84 ALA N N 120.0 0.15 1 841 . 84 ALA H H 7.58 0.02 1 842 . 84 ALA CA C 55.3 0.15 1 843 . 84 ALA HA H 3.68 0.02 1 844 . 84 ALA HB H 1.35 0.02 1 845 . 84 ALA CB C 18.2 0.15 1 846 . 84 ALA C C 179.1 0.15 1 847 . 85 SER N N 111.5 0.15 1 848 . 85 SER H H 8.05 0.02 1 849 . 85 SER CA C 61.4 0.15 1 850 . 85 SER HA H 4.28 0.02 1 851 . 85 SER CB C 63.0 0.15 1 852 . 85 SER HB2 H 3.96 0.02 1 853 . 85 SER HB3 H 3.96 0.02 1 854 . 85 SER C C 178.5 0.15 1 855 . 86 ASP N N 124.2 0.15 1 856 . 86 ASP H H 8.31 0.02 1 857 . 86 ASP CA C 57.5 0.15 1 858 . 86 ASP HA H 4.30 0.02 1 859 . 86 ASP CB C 40.5 0.15 1 860 . 86 ASP HB2 H 2.94 0.02 2 861 . 86 ASP HB3 H 2.44 0.02 2 862 . 86 ASP C C 178.0 0.15 1 863 . 87 TRP N N 117.9 0.15 1 864 . 87 TRP H H 7.69 0.02 1 865 . 87 TRP CA C 57.6 0.15 1 866 . 87 TRP HA H 4.34 0.02 1 867 . 87 TRP CB C 28.0 0.15 1 868 . 87 TRP HB2 H 3.41 0.02 2 869 . 87 TRP HB3 H 2.50 0.02 2 870 . 87 TRP CD1 C 128.4 0.15 1 871 . 87 TRP CE3 C 120.7 0.15 1 872 . 87 TRP NE1 N 128.7 0.15 1 873 . 87 TRP HD1 H 7.75 0.02 1 874 . 87 TRP HE3 H 7.71 0.02 1 875 . 87 TRP CZ3 C 121.4 0.15 1 876 . 87 TRP CZ2 C 114.7 0.15 1 877 . 87 TRP HE1 H 10.56 0.02 1 878 . 87 TRP HZ3 H 7.13 0.02 1 879 . 87 TRP CH2 C 124.8 0.15 1 880 . 87 TRP HZ2 H 7.61 0.02 1 881 . 87 TRP HH2 H 7.23 0.02 1 882 . 87 TRP C C 173.5 0.15 1 883 . 88 ALA N N 121.7 0.15 1 884 . 88 ALA H H 7.82 0.02 1 885 . 88 ALA CA C 52.7 0.15 1 886 . 88 ALA HA H 3.98 0.02 1 887 . 88 ALA HB H 1.31 0.02 1 888 . 88 ALA CB C 16.8 0.15 1 889 . 88 ALA C C 176.4 0.15 1 890 . 89 ILE N N 118.7 0.15 1 891 . 89 ILE H H 7.91 0.02 1 892 . 89 ILE CA C 59.7 0.15 1 893 . 89 ILE HA H 3.87 0.02 1 894 . 89 ILE CB C 34.8 0.15 1 895 . 89 ILE HB H 1.73 0.02 1 896 . 89 ILE HG2 H 0.63 0.02 1 897 . 89 ILE CG2 C 17.9 0.15 1 898 . 89 ILE CG1 C 26.0 0.15 1 899 . 89 ILE HG12 H 1.22 0.02 2 900 . 89 ILE HG13 H -0.08 0.02 2 901 . 89 ILE HD1 H 0.09 0.02 1 902 . 89 ILE CD1 C 9.2 0.15 1 903 . 89 ILE C C 177.0 0.15 1 904 . 90 GLN N N 127.4 0.15 1 905 . 90 GLN H H 8.62 0.02 1 906 . 90 GLN CA C 56.1 0.15 1 907 . 90 GLN HA H 4.46 0.02 1 908 . 90 GLN CB C 31.7 0.15 1 909 . 90 GLN HB2 H 2.16 0.02 2 910 . 90 GLN HB3 H 1.86 0.02 2 911 . 90 GLN CG C 34.1 0.15 1 912 . 90 GLN HG2 H 2.27 0.02 1 913 . 90 GLN HG3 H 2.27 0.02 1 914 . 90 GLN NE2 N 112.0 0.15 1 915 . 90 GLN HE21 H 7.39 0.02 2 916 . 90 GLN HE22 H 6.80 0.02 2 917 . 90 GLN C C 174.5 0.15 1 918 . 91 ALA N N 122.8 0.15 1 919 . 91 ALA H H 7.72 0.02 1 920 . 91 ALA CA C 51.7 0.15 1 921 . 91 ALA HA H 4.49 0.02 1 922 . 91 ALA HB H 1.25 0.02 1 923 . 91 ALA CB C 21.6 0.15 1 924 . 91 ALA C C 175.5 0.15 1 925 . 92 MET N N 118.6 0.15 1 926 . 92 MET H H 8.46 0.02 1 927 . 92 MET CA C 52.5 0.15 1 928 . 92 MET HA H 4.91 0.02 1 929 . 92 MET CB C 34.4 0.15 1 930 . 92 MET HB2 H 1.89 0.02 2 931 . 92 MET HB3 H 1.69 0.02 2 932 . 92 MET CG C 33.1 0.15 1 933 . 92 MET HG2 H 2.31 0.02 2 934 . 92 MET HG3 H 2.24 0.02 2 935 . 92 MET HE H 1.83 0.02 1 936 . 92 MET CE C 18.3 0.15 1 937 . 92 MET C C 173.9 0.15 1 938 . 93 PRO CD C 50.2 0.15 1 939 . 93 PRO CA C 63.2 0.15 1 940 . 93 PRO HA H 5.07 0.02 1 941 . 93 PRO CB C 34.1 0.15 1 942 . 93 PRO HB2 H 2.06 0.02 2 943 . 93 PRO HB3 H 1.36 0.02 2 944 . 93 PRO CG C 24.8 0.15 1 945 . 93 PRO HG2 H 1.81 0.02 2 946 . 93 PRO HG3 H 1.68 0.02 2 947 . 93 PRO HD2 H 3.56 0.02 2 948 . 93 PRO HD3 H 3.33 0.02 2 949 . 93 PRO C C 176.1 0.15 1 950 . 94 THR N N 115.2 0.15 1 951 . 94 THR H H 8.03 0.02 1 952 . 94 THR CA C 63.4 0.15 1 953 . 94 THR HA H 4.95 0.02 1 954 . 94 THR CB C 73.0 0.15 1 955 . 94 THR HB H 3.94 0.02 1 956 . 94 THR HG2 H 1.19 0.02 1 957 . 94 THR HG1 H 5.59 0.02 1 958 . 94 THR CG2 C 21.8 0.15 1 959 . 94 THR C C 171.9 0.15 1 960 . 95 PHE N N 125.5 0.15 1 961 . 95 PHE H H 9.87 0.02 1 962 . 95 PHE CA C 55.5 0.15 1 963 . 95 PHE HA H 5.96 0.02 1 964 . 95 PHE CB C 41.0 0.15 1 965 . 95 PHE HB2 H 3.20 0.02 2 966 . 95 PHE HB3 H 2.54 0.02 2 967 . 95 PHE HD1 H 7.02 0.02 1 968 . 95 PHE HD2 H 7.02 0.02 1 969 . 95 PHE HE1 H 7.33 0.02 1 970 . 95 PHE HE2 H 7.33 0.02 1 971 . 95 PHE CD1 C 132.2 0.15 1 972 . 95 PHE CE1 C 131.8 0.15 1 973 . 95 PHE CZ C 128.5 0.15 1 974 . 95 PHE HZ H 6.88 0.02 1 975 . 95 PHE C C 175.3 0.15 1 976 . 96 MET N N 123.7 0.15 1 977 . 96 MET H H 9.32 0.02 1 978 . 96 MET CA C 54.0 0.15 1 979 . 96 MET HA H 5.31 0.02 1 980 . 96 MET CB C 36.9 0.15 1 981 . 96 MET HB2 H 2.21 0.02 2 982 . 96 MET HB3 H 1.93 0.02 2 983 . 96 MET CG C 32.7 0.15 1 984 . 96 MET HG2 H 2.61 0.02 2 985 . 96 MET HG3 H 2.46 0.02 2 986 . 96 MET C C 173.8 0.15 1 987 . 97 PHE N N 123.8 0.15 1 988 . 97 PHE H H 8.40 0.02 1 989 . 97 PHE CA C 56.6 0.15 1 990 . 97 PHE HA H 5.36 0.02 1 991 . 97 PHE CB C 40.6 0.15 1 992 . 97 PHE HB2 H 2.99 0.02 2 993 . 97 PHE HB3 H 2.36 0.02 2 994 . 97 PHE HD1 H 7.13 0.02 1 995 . 97 PHE HD2 H 7.13 0.02 1 996 . 97 PHE CD1 C 131.8 0.15 1 997 . 97 PHE C C 174.4 0.15 1 998 . 98 LEU N N 125.7 0.15 1 999 . 98 LEU H H 9.69 0.02 1 1000 . 98 LEU CA C 53.8 0.15 1 1001 . 98 LEU HA H 5.51 0.02 1 1002 . 98 LEU CB C 47.5 0.15 1 1003 . 98 LEU HB2 H 1.40 0.02 1 1004 . 98 LEU HB3 H 1.40 0.02 1 1005 . 98 LEU CG C 28.0 0.15 1 1006 . 98 LEU HG H 1.35 0.02 1 1007 . 98 LEU HD1 H 0.71 0.02 2 1008 . 98 LEU HD2 H 0.55 0.02 2 1009 . 98 LEU CD1 C 25.7 0.15 1 1010 . 98 LEU CD2 C 25.9 0.15 1 1011 . 98 LEU C C 175.6 0.15 1 1012 . 99 LYS N N 118.2 0.15 1 1013 . 99 LYS H H 8.33 0.02 1 1014 . 99 LYS CA C 58.2 0.15 1 1015 . 99 LYS HA H 4.38 0.02 1 1016 . 99 LYS CB C 37.3 0.15 1 1017 . 99 LYS HB2 H 1.77 0.02 2 1018 . 99 LYS HB3 H 1.72 0.02 2 1019 . 99 LYS CG C 26.0 0.15 1 1020 . 99 LYS HG2 H 1.33 0.02 2 1021 . 99 LYS HG3 H 1.24 0.02 2 1022 . 99 LYS CD C 30.2 0.15 1 1023 . 99 LYS HD2 H 1.70 0.02 1 1024 . 99 LYS HD3 H 1.70 0.02 1 1025 . 99 LYS CE C 42.5 0.15 1 1026 . 99 LYS HE2 H 3.01 0.02 1 1027 . 99 LYS HE3 H 3.01 0.02 1 1028 . 99 LYS C C 176.7 0.15 1 1029 . 100 GLU N N 128.0 0.15 1 1030 . 100 GLU H H 10.11 0.02 1 1031 . 100 GLU CA C 57.7 0.15 1 1032 . 100 GLU HA H 3.81 0.02 1 1033 . 100 GLU CB C 29.0 0.15 1 1034 . 100 GLU HB2 H 2.37 0.02 2 1035 . 100 GLU HB3 H 2.04 0.02 2 1036 . 100 GLU CG C 39.0 0.15 1 1037 . 100 GLU HG2 H 2.23 0.02 2 1038 . 100 GLU HG3 H 2.12 0.02 2 1039 . 100 GLU C C 176.2 0.15 1 1040 . 101 GLY N N 104.2 0.15 1 1041 . 101 GLY H H 8.85 0.02 1 1042 . 101 GLY CA C 45.7 0.15 1 1043 . 101 GLY HA2 H 4.14 0.02 2 1044 . 101 GLY HA3 H 3.52 0.02 2 1045 . 101 GLY C C 173.4 0.15 1 1046 . 102 LYS N N 120.9 0.15 1 1047 . 102 LYS H H 7.76 0.02 1 1048 . 102 LYS CA C 54.7 0.15 1 1049 . 102 LYS HA H 4.60 0.02 1 1050 . 102 LYS CB C 34.6 0.15 1 1051 . 102 LYS HB2 H 1.81 0.02 1 1052 . 102 LYS HB3 H 1.81 0.02 1 1053 . 102 LYS CG C 25.0 0.15 1 1054 . 102 LYS HG2 H 1.45 0.02 2 1055 . 102 LYS HG3 H 1.38 0.02 2 1056 . 102 LYS CD C 29.3 0.15 1 1057 . 102 LYS HD2 H 1.68 0.02 1 1058 . 102 LYS HD3 H 1.68 0.02 1 1059 . 102 LYS CE C 42.5 0.15 1 1060 . 102 LYS HE2 H 3.02 0.02 1 1061 . 102 LYS HE3 H 3.02 0.02 1 1062 . 102 LYS C C 175.6 0.15 1 1063 . 103 ILE N N 122.0 0.15 1 1064 . 103 ILE H H 8.62 0.02 1 1065 . 103 ILE CA C 62.3 0.15 1 1066 . 103 ILE HA H 4.28 0.02 1 1067 . 103 ILE CB C 38.3 0.15 1 1068 . 103 ILE HB H 1.86 0.02 1 1069 . 103 ILE HG2 H 0.98 0.02 1 1070 . 103 ILE CG2 C 18.2 0.15 1 1071 . 103 ILE CG1 C 28.6 0.15 1 1072 . 103 ILE HG12 H 1.83 0.02 2 1073 . 103 ILE HG13 H 1.16 0.02 2 1074 . 103 ILE HD1 H 0.96 0.02 1 1075 . 103 ILE CD1 C 13.9 0.15 1 1076 . 103 ILE C C 177.0 0.15 1 1077 . 104 LEU N N 128.7 0.15 1 1078 . 104 LEU H H 9.38 0.02 1 1079 . 104 LEU CA C 55.2 0.15 1 1080 . 104 LEU HA H 4.32 0.02 1 1081 . 104 LEU CB C 43.5 0.15 1 1082 . 104 LEU HB2 H 1.03 0.02 2 1083 . 104 LEU HB3 H 0.85 0.02 2 1084 . 104 LEU CG C 26.8 0.15 1 1085 . 104 LEU HG H 1.53 0.02 1 1086 . 104 LEU HD1 H 0.60 0.02 2 1087 . 104 LEU HD2 H 0.73 0.02 2 1088 . 104 LEU CD1 C 26.1 0.15 1 1089 . 104 LEU CD2 C 22.5 0.15 1 1090 . 104 LEU C C 177.1 0.15 1 1091 . 105 ASP N N 116.2 0.15 1 1092 . 105 ASP H H 7.80 0.02 1 1093 . 105 ASP CA C 54.2 0.15 1 1094 . 105 ASP HA H 4.80 0.02 1 1095 . 105 ASP CB C 47.7 0.15 1 1096 . 105 ASP HB2 H 2.23 0.02 2 1097 . 105 ASP HB3 H 1.86 0.02 2 1098 . 105 ASP C C 174.6 0.15 1 1099 . 106 LYS N N 118.2 0.15 1 1100 . 106 LYS H H 8.97 0.02 1 1101 . 106 LYS CA C 56.3 0.15 1 1102 . 106 LYS HA H 5.63 0.02 1 1103 . 106 LYS CB C 37.3 0.15 1 1104 . 106 LYS HB2 H 1.87 0.02 1 1105 . 106 LYS HB3 H 1.87 0.02 1 1106 . 106 LYS CG C 25.4 0.15 1 1107 . 106 LYS HG2 H 1.56 0.02 2 1108 . 106 LYS HG3 H 1.37 0.02 2 1109 . 106 LYS CD C 30.1 0.15 1 1110 . 106 LYS HD2 H 1.70 0.02 1 1111 . 106 LYS HD3 H 1.70 0.02 1 1112 . 106 LYS CE C 42.2 0.15 1 1113 . 106 LYS HE2 H 2.98 0.02 1 1114 . 106 LYS HE3 H 2.98 0.02 1 1115 . 106 LYS C C 175.1 0.15 1 1116 . 107 VAL N N 125.5 0.15 1 1117 . 107 VAL H H 9.57 0.02 1 1118 . 107 VAL CA C 62.3 0.15 1 1119 . 107 VAL HA H 4.48 0.02 1 1120 . 107 VAL CB C 36.0 0.15 1 1121 . 107 VAL HB H 2.41 0.02 1 1122 . 107 VAL HG1 H 1.09 0.02 2 1123 . 107 VAL HG2 H 1.15 0.02 2 1124 . 107 VAL CG1 C 22.5 0.15 1 1125 . 107 VAL CG2 C 21.2 0.15 1 1126 . 107 VAL C C 174.3 0.15 1 1127 . 108 VAL N N 128.9 0.15 1 1128 . 108 VAL H H 9.14 0.02 1 1129 . 108 VAL CA C 62.5 0.15 1 1130 . 108 VAL HA H 4.56 0.02 1 1131 . 108 VAL CB C 33.0 0.15 1 1132 . 108 VAL HB H 2.05 0.02 1 1133 . 108 VAL HG1 H 0.89 0.02 2 1134 . 108 VAL HG2 H 1.03 0.02 2 1135 . 108 VAL CG1 C 21.8 0.15 1 1136 . 108 VAL CG2 C 20.8 0.15 1 1137 . 108 VAL C C 175.7 0.15 1 1138 . 109 GLY N N 115.0 0.15 1 1139 . 109 GLY H H 8.60 0.02 1 1140 . 109 GLY CA C 43.3 0.15 1 1141 . 109 GLY HA2 H 4.58 0.02 2 1142 . 109 GLY HA3 H 3.67 0.02 2 1143 . 109 GLY C C 173.3 0.15 1 1144 . 110 ALA N N 122.2 0.15 1 1145 . 110 ALA H H 8.75 0.02 1 1146 . 110 ALA CA C 51.1 0.15 1 1147 . 110 ALA HA H 4.46 0.02 1 1148 . 110 ALA HB H 1.42 0.02 1 1149 . 110 ALA CB C 18.1 0.15 1 1150 . 110 ALA C C 176.3 0.15 1 1151 . 111 LYS N N 125.8 0.15 1 1152 . 111 LYS H H 7.58 0.02 1 1153 . 111 LYS CA C 54.7 0.15 1 1154 . 111 LYS HA H 4.53 0.02 1 1155 . 111 LYS CB C 33.5 0.15 1 1156 . 111 LYS HB2 H 2.02 0.02 2 1157 . 111 LYS HB3 H 1.53 0.02 2 1158 . 111 LYS CG C 24.9 0.15 1 1159 . 111 LYS HG2 H 1.33 0.02 2 1160 . 111 LYS HG3 H 1.22 0.02 2 1161 . 111 LYS CD C 29.6 0.15 1 1162 . 111 LYS HD2 H 1.69 0.02 2 1163 . 111 LYS HD3 H 1.64 0.02 2 1164 . 111 LYS CE C 42.9 0.15 1 1165 . 111 LYS HE2 H 3.06 0.02 1 1166 . 111 LYS HE3 H 3.06 0.02 1 1167 . 111 LYS C C 175.6 0.15 1 1168 . 112 LYS N N 124.2 0.15 1 1169 . 112 LYS H H 8.49 0.02 1 1170 . 112 LYS CA C 61.3 0.15 1 1171 . 112 LYS HA H 3.46 0.02 1 1172 . 112 LYS CB C 32.8 0.15 1 1173 . 112 LYS HB2 H 1.37 0.02 2 1174 . 112 LYS HB3 H 1.19 0.02 2 1175 . 112 LYS CG C 25.6 0.15 1 1176 . 112 LYS HG2 H 0.36 0.02 2 1177 . 112 LYS HG3 H 1.05 0.02 2 1178 . 112 LYS CD C 30.0 0.15 1 1179 . 112 LYS HD2 H 1.20 0.02 2 1180 . 112 LYS HD3 H 1.11 0.02 2 1181 . 112 LYS CE C 41.5 0.15 1 1182 . 112 LYS HE2 H 2.42 0.02 1 1183 . 112 LYS HE3 H 2.42 0.02 1 1184 . 112 LYS C C 177.8 0.15 1 1185 . 113 ASP N N 117.6 0.15 1 1186 . 113 ASP H H 8.43 0.02 1 1187 . 113 ASP CA C 57.4 0.15 1 1188 . 113 ASP HA H 4.37 0.02 1 1189 . 113 ASP CB C 39.8 0.15 1 1190 . 113 ASP HB2 H 2.68 0.02 1 1191 . 113 ASP HB3 H 2.68 0.02 1 1192 . 113 ASP C C 179.1 0.15 1 1193 . 114 GLU N N 122.0 0.15 1 1194 . 114 GLU H H 8.16 0.02 1 1195 . 114 GLU CA C 59.6 0.15 1 1196 . 114 GLU HA H 4.14 0.02 1 1197 . 114 GLU CB C 29.9 0.15 1 1198 . 114 GLU HB2 H 2.00 0.02 1 1199 . 114 GLU HB3 H 2.00 0.02 1 1200 . 114 GLU CG C 37.3 0.15 1 1201 . 114 GLU HG2 H 2.31 0.02 1 1202 . 114 GLU HG3 H 2.31 0.02 1 1203 . 114 GLU C C 180.0 0.15 1 1204 . 115 LEU N N 122.9 0.15 1 1205 . 115 LEU H H 8.40 0.02 1 1206 . 115 LEU CA C 59.4 0.15 1 1207 . 115 LEU HA H 4.13 0.02 1 1208 . 115 LEU CB C 42.0 0.15 1 1209 . 115 LEU HB2 H 1.98 0.02 2 1210 . 115 LEU HB3 H 1.46 0.02 2 1211 . 115 LEU CG C 26.9 0.15 1 1212 . 115 LEU HG H 1.47 0.02 1 1213 . 115 LEU HD1 H 0.43 0.02 2 1214 . 115 LEU HD2 H 0.59 0.02 2 1215 . 115 LEU CD1 C 25.1 0.15 1 1216 . 115 LEU CD2 C 23.4 0.15 1 1217 . 115 LEU C C 177.6 0.15 1 1218 . 116 GLN N N 117.0 0.15 1 1219 . 116 GLN H H 8.17 0.02 1 1220 . 116 GLN CA C 60.3 0.15 1 1221 . 116 GLN HA H 4.01 0.02 1 1222 . 116 GLN CB C 29.5 0.15 1 1223 . 116 GLN HB2 H 2.37 0.02 2 1224 . 116 GLN CG C 34.8 0.15 1 1225 . 116 GLN HG2 H 2.54 0.02 2 1226 . 116 GLN HG3 H 2.50 0.02 2 1227 . 116 GLN NE2 N 111.0 0.15 1 1228 . 116 GLN HE21 H 7.41 0.02 2 1229 . 116 GLN HE22 H 6.83 0.02 2 1230 . 116 GLN C C 178.8 0.15 1 1231 . 117 SER N N 115.1 0.15 1 1232 . 117 SER H H 8.66 0.02 1 1233 . 117 SER CA C 61.7 0.15 1 1234 . 117 SER HA H 4.24 0.02 1 1235 . 117 SER CB C 63.0 0.15 1 1236 . 117 SER HB2 H 3.93 0.02 1 1237 . 117 SER HB3 H 3.93 0.02 1 1238 . 117 SER C C 177.2 0.15 1 1239 . 118 THR N N 121.0 0.15 1 1240 . 118 THR H H 8.18 0.02 1 1241 . 118 THR CA C 67.4 0.15 1 1242 . 118 THR HA H 3.68 0.02 1 1243 . 118 THR CB C 68.1 0.15 1 1244 . 118 THR HB H 3.88 0.02 1 1245 . 118 THR HG2 H 0.23 0.02 1 1246 . 118 THR CG2 C 20.8 0.15 1 1247 . 118 THR C C 175.5 0.15 1 1248 . 119 ILE N N 121.3 0.15 1 1249 . 119 ILE H H 7.92 0.02 1 1250 . 119 ILE CA C 66.9 0.15 1 1251 . 119 ILE HA H 3.69 0.02 1 1252 . 119 ILE CB C 38.3 0.15 1 1253 . 119 ILE HB H 2.04 0.02 1 1254 . 119 ILE HG2 H 0.96 0.02 1 1255 . 119 ILE CG2 C 17.6 0.15 1 1256 . 119 ILE CG1 C 30.8 0.15 1 1257 . 119 ILE HG12 H 2.26 0.02 2 1258 . 119 ILE HG13 H 1.12 0.02 2 1259 . 119 ILE HD1 H 1.02 0.02 1 1260 . 119 ILE CD1 C 16.1 0.15 1 1261 . 119 ILE C C 176.9 0.15 1 1262 . 120 ALA N N 118.7 0.15 1 1263 . 120 ALA H H 7.42 0.02 1 1264 . 120 ALA CA C 55.4 0.15 1 1265 . 120 ALA HA H 3.95 0.02 1 1266 . 120 ALA HB H 1.47 0.02 1 1267 . 120 ALA CB C 18.4 0.15 1 1268 . 120 ALA C C 180.4 0.15 1 1269 . 121 LYS N N 116.5 0.15 1 1270 . 121 LYS H H 7.51 0.02 1 1271 . 121 LYS CA C 58.7 0.15 1 1272 . 121 LYS HA H 3.94 0.02 1 1273 . 121 LYS CB C 32.9 0.15 1 1274 . 121 LYS HB2 H 1.66 0.02 2 1275 . 121 LYS HB3 H 1.53 0.02 2 1276 . 121 LYS CG C 24.4 0.15 1 1277 . 121 LYS HG2 H 1.15 0.02 2 1278 . 121 LYS HG3 H 0.80 0.02 2 1279 . 121 LYS CD C 29.9 0.15 1 1280 . 121 LYS HD2 H 1.50 0.02 2 1281 . 121 LYS HD3 H 1.41 0.02 2 1282 . 121 LYS CE C 41.9 0.15 1 1283 . 121 LYS HE2 H 2.75 0.02 1 1284 . 121 LYS HE3 H 2.75 0.02 1 1285 . 121 LYS C C 177.7 0.15 1 1286 . 122 HIS N N 114.3 0.15 1 1287 . 122 HIS H H 7.23 0.02 1 1288 . 122 HIS CA C 56.6 0.15 1 1289 . 122 HIS HA H 4.88 0.02 1 1290 . 122 HIS CB C 31.7 0.15 1 1291 . 122 HIS HB2 H 3.45 0.02 2 1292 . 122 HIS HB3 H 2.76 0.02 2 1293 . 122 HIS CD2 C 120.2 0.15 1 1294 . 122 HIS CE1 C 138.5 0.15 1 1295 . 122 HIS HD2 H 6.83 0.02 1 1296 . 122 HIS HE1 H 8.27 0.02 1 1297 . 122 HIS C C 174.7 0.15 1 1298 . 123 LEU N N 121.5 0.15 1 1299 . 123 LEU H H 7.46 0.02 1 1300 . 123 LEU CA C 55.7 0.15 1 1301 . 123 LEU HA H 4.38 0.02 1 1302 . 123 LEU CB C 43.2 0.15 1 1303 . 123 LEU HB2 H 1.68 0.02 2 1304 . 123 LEU HB3 H 1.63 0.02 2 1305 . 123 LEU CG C 26.2 0.15 1 1306 . 123 LEU HG H 1.84 0.02 1 1307 . 123 LEU HD1 H 0.86 0.02 2 1308 . 123 LEU HD2 H 0.82 0.02 2 1309 . 123 LEU CD1 C 26.0 0.15 1 1310 . 123 LEU CD2 C 23.7 0.15 1 1311 . 123 LEU C C 176.3 0.15 1 1312 . 124 ALA N N 128.8 0.15 1 1313 . 124 ALA H H 7.45 0.02 1 1314 . 124 ALA CA C 54.2 0.15 1 1315 . 124 ALA HA H 4.11 0.02 1 1316 . 124 ALA HB H 1.35 0.02 1 1317 . 124 ALA CB C 20.2 0.15 1 1318 . 124 ALA C C 169.3 0.15 1 stop_ save_