data_5328 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution NMR structure of the BRCT domain from Thermus thermophilus DNA ligase ; _BMRB_accession_number 5328 _BMRB_flat_file_name bmr5328.str _Entry_type original _Submission_date 2002-03-19 _Accession_date 2002-03-20 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'NorthEast Structural Genomics Consortium (NESG) target WR64Tt.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sahota Gurmukh S. . 2 Dixon Bonnie L. . 3 Huang Yuanpeng . . 4 Aramini James M. . 5 Bhattacharya Aneerban . . 6 Monleon Daniel . . 7 Swapna Gurla V.T. . 8 Yin Cuifeng . . 9 Anderson Steve . . 10 Tejero Roberto . . 11 Montelione Gaetano T. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 461 "13C chemical shifts" 370 "15N chemical shifts" 87 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-04-06 original author . stop_ _Original_release_date 2006-04-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution NMR structure of the BRCT domain from Thermus thermophilus DNA ligase' _Citation_status submitted _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sahota Gurmukh S. . 2 Dixon Bonnie L. . 3 Huang Yuanpeng . . 4 Aramini James M. . 5 Bhattacharya Aneerban . . 6 Monleon Daniel . . 7 Swapna Gurla V.T. . 8 Yin Cuifeng . . 9 Anderson Steve . . 10 Montelione Gaetano T. . 11 Tejero Roberto . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . 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. 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 ; Zimmerman, D. E., Kulikowski, C. A., Huang, Y., Feng, W., Tashiro, M., Shimotakahara, S., Chien, C. Y., Powers, R., and Montelione, G. T. J. Mol. Biol. 269, 592-610, (1997). ; _Citation_title 'Automated analysis of protein NMR assignments using methods from artificial intelligence.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9217263 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zimmerman 'D. E.' E. . 2 Kulikowski 'C. A.' A. . 3 Huang Y. . . 4 Feng W. . . 5 Tashiro M. . . 6 Shimotakahara S. . . 7 Chien C. . . 8 Powers R. . . 9 Montelione 'G. T.' T. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 269 _Journal_issue 4 _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 592 _Page_last 610 _Year 1997 _Details ; An expert system for determining resonance assignments from NMR spectra of proteins is described. Given the amino acid sequence, a two-dimensional 15N-1H heteronuclear correlation spectrum and seven to eight three-dimensional triple-resonance NMR spectra for seven proteins, AUTOASSIGN obtained an average of 98% of sequence-specific spin-system assignments with an error rate of less than 0.5%. Execution times on a Sparc 10 workstation varied from 16 seconds for smaller proteins with simple spectra to one to nine minutes for medium size proteins exhibiting numerous extra spin systems attributed to conformational isomerization. AUTOASSIGN combines symbolic constraint satisfaction methods with a domain-specific knowledge base to exploit the logical structure of the sequential assignment problem, the specific features of the various NMR experiments, and the expected chemical shift frequencies of different amino acids. The current implementation specializes in the analysis of data derived from the most sensitive of the currently available triple-resonance experiments. Potential extensions of the system for analysis of additional types of protein NMR data are also discussed. ; save_ save_ref-3 _Saveframe_category citation _Citation_full ; Moseley, H.N., Monleon, D., Montelione, G.T. Methods Enzymol, 339, 91-108, (2001). ; _Citation_title 'Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11462827 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Moseley 'H. N.' N. . 2 Monleon D. . . 3 Montelione 'G. T.' T. . stop_ _Journal_abbreviation 'Meth. Enzymol.' _Journal_name_full 'Methods in enzymology' _Journal_volume 339 _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 91 _Page_last 108 _Year 2001 _Details . save_ ################################## # Molecular system description # ################################## save_system_abbreviation_1 _Saveframe_category molecular_system _Mol_system_name 'DNA Ligase BRCT domain' _Abbreviation_common BRCT _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label BRCT $BRCT stop_ _System_molecular_weight 10013 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'BRCT is mostly found in cell cycle regulation and DNA repair proteins' 'BRCT is probably a protein-protein interaction domain' 'Transcriptional activator' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_BRCT _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'DNA Ligase Thermus Thermophilus BRCT' _Abbreviation_common BRCT _Molecular_mass 10013 _Mol_thiol_state . _Details ; Methionine starting sequence Residues 588-676 including BRCT domain (588-676) Rinally a Glycine and Serine. ; ############################## # Polymer residue sequence # ############################## _Residue_count 92 _Mol_residue_sequence ; MEKGGEALKGLTFVITGELS RPREEVKALLRRLGAKVTDS VSRKTSYLVVGENPGSKLEK ARALGVPTLTEEELYRLLEA RTGKKAEELVGS ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLU 3 LYS 4 GLY 5 GLY 6 GLU 7 ALA 8 LEU 9 LYS 10 GLY 11 LEU 12 THR 13 PHE 14 VAL 15 ILE 16 THR 17 GLY 18 GLU 19 LEU 20 SER 21 ARG 22 PRO 23 ARG 24 GLU 25 GLU 26 VAL 27 LYS 28 ALA 29 LEU 30 LEU 31 ARG 32 ARG 33 LEU 34 GLY 35 ALA 36 LYS 37 VAL 38 THR 39 ASP 40 SER 41 VAL 42 SER 43 ARG 44 LYS 45 THR 46 SER 47 TYR 48 LEU 49 VAL 50 VAL 51 GLY 52 GLU 53 ASN 54 PRO 55 GLY 56 SER 57 LYS 58 LEU 59 GLU 60 LYS 61 ALA 62 ARG 63 ALA 64 LEU 65 GLY 66 VAL 67 PRO 68 THR 69 LEU 70 THR 71 GLU 72 GLU 73 GLU 74 LEU 75 TYR 76 ARG 77 LEU 78 LEU 79 GLU 80 ALA 81 ARG 82 THR 83 GLY 84 LYS 85 LYS 86 ALA 87 GLU 88 GLU 89 LEU 90 VAL 91 GLY 92 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 1L7B "Solution Nmr Structure Of Brct Domain Of T. Thermophilus: Northeast Structural Genomics Consortium Target Wr64tt" 100.00 92 100.00 100.00 9.75e-54 DBJ BAD70920 "DNA ligase [NAD+] [Thermus thermophilus HB8]" 96.74 676 100.00 100.00 2.21e-46 GB AAA27486 "DNA ligase [Thermus thermophilus HB8]" 96.74 676 100.00 100.00 2.21e-46 GB AAA27487 "DNA ligase [Thermus thermophilus HB8]" 96.74 676 100.00 100.00 2.21e-46 GB AAS81080 "NAD-dependent DNA ligase [Thermus thermophilus HB27]" 96.74 676 100.00 100.00 1.80e-46 GB AEG33516 "DNA ligase [Thermus thermophilus SG0.5JP17-16]" 96.74 676 98.88 98.88 7.80e-46 GB AFH38862 "DNA ligase, NAD-dependent [Thermus thermophilus JL-18]" 96.74 676 100.00 100.00 2.25e-46 PIR A40363 "DNA ligase (NAD) (EC 6.5.1.2) - Thermus aquaticus" 96.74 676 100.00 100.00 2.21e-46 REF WP_008632525 "NAD-dependent DNA ligase LigA [Thermus sp. RL]" 96.74 673 97.75 98.88 1.93e-45 REF WP_011173171 "NAD-dependent DNA ligase LigA [Thermus thermophilus]" 96.74 676 100.00 100.00 1.80e-46 REF WP_011228436 "NAD-dependent DNA ligase LigA [Thermus thermophilus]" 96.74 676 100.00 100.00 2.21e-46 REF WP_014510389 "NAD-dependent DNA ligase LigA [Thermus thermophilus]" 96.74 676 98.88 98.88 7.80e-46 REF WP_014629535 "NAD-dependent DNA ligase LigA [Thermus thermophilus]" 96.74 676 100.00 100.00 2.25e-46 SP P26996 "RecName: Full=DNA ligase; AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)]; AltName: Full=Tth DNA ligase [Thermus thermo" 96.74 676 100.00 100.00 2.21e-46 SP Q72JN8 "RecName: Full=DNA ligase; AltName: Full=Polydeoxyribonucleotide synthase [Thermus thermophilus HB27]" 96.74 676 100.00 100.00 1.80e-46 stop_ save_ #################### # Natural source # #################### save_natural_source_BRCT.BLD.1 _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $BRCT 'T. thermophilus' 274 Eubacteria Monera Thermus thermophilus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_BRCT.BLD.1 _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $BRCT 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) pET15b 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 $BRCT 1.3 mM '[U-99% 13C; U-99% 15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $BRCT 1.3 mM '[U-99% 15N]' stop_ save_ ############################# # Purity of the molecules # ############################# save_mol_purity_list _Saveframe_category sample_mol_purity _Sample_label $sample_1 loop_ _Mol_label _Mol_purity_value _Mol_purity_value_units _Mol_purity_measurement_method $BRCT 97 % 'SDS gel electrophoresis' $BRCT 97 % 'SDS gel electrophoresis' stop_ save_ ############################ # Computer software used # ############################ save_VNMR _Saveframe_category software _Name VNMR6.1B _Version 6.1B loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task 'data processing' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 97.231.15.18 loop_ _Vendor _Address _Electronic_address 'NIH Protein NMR Group' . http://spin.niddk.nih.gov/bax/software/NMRPipe/NMRPipe.html stop_ loop_ _Task 'spectral processing' stop_ _Details . _Citation_label $ref-1 save_ save_sparky _Saveframe_category software _Name SPARKY _Version 3.91 loop_ _Task 'peak picking' stop_ _Details . save_ save_autoassign _Saveframe_category software _Name AutoAssign _Version 1.7.6 loop_ _Vendor _Address _Electronic_address Montelione . http://www-nmr.cabm.rutgers.edu/NMRsoftware/nmr_software.html stop_ loop_ _Task 'automated backbone 1H, 13C and 15N assignments' stop_ _Details 'Please see references in $ref-2 and $ref-3.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'UNITY Inova' _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'UNITY Inova' _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_H_COTOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name H_COTOCSY _Sample_label $sample_1 save_ save_HBHA(CBCACO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CBCACO)NH _Sample_label $sample_1 save_ save_13C-edited_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-edited NOESY' _Sample_label $sample_1 save_ save_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_C_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name C_CBCA(CO)NH _Sample_label $sample_1 save_ save_C_CBCANH_6 _Saveframe_category NMR_applied_experiment _Experiment_name C_CBCANH _Sample_label $sample_1 save_ save_NH_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name NH_HSQC _Sample_label $sample_1 save_ save_NH_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name NH_HSQC _Sample_label $sample_2 save_ save_H_CABB_9 _Saveframe_category NMR_applied_experiment _Experiment_name H_CABB _Sample_label $sample_1 save_ save_C_COBB_10 _Saveframe_category NMR_applied_experiment _Experiment_name C_COBB _Sample_label $sample_1 save_ save_HACACOCANH_11 _Saveframe_category NMR_applied_experiment _Experiment_name HACACOCANH _Sample_label $sample_1 save_ save_H_COBB_12 _Saveframe_category NMR_applied_experiment _Experiment_name H_COBB _Sample_label $sample_1 save_ save_C_COTOCSY_13 _Saveframe_category NMR_applied_experiment _Experiment_name C_COTOCSY _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.2 . pH temperature 293 . K pressure 1 . atm 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 . . . 1.000000000 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_BRCT _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $autoassign stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name BRCT _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 3 LYS CG C 24.8 0.35 1 2 . 3 LYS HB2 H 1.767 0.02 1 3 . 3 LYS HB3 H 1.767 0.02 1 4 . 3 LYS C C 177.9 0.35 1 5 . 3 LYS HA H 4.25 0.02 1 6 . 3 LYS HE2 H 2.992 0.02 1 7 . 3 LYS CA C 56.8 0.35 1 8 . 3 LYS HE3 H 2.992 0.02 1 9 . 3 LYS CB C 32.8 0.35 1 10 . 3 LYS HG2 H 1.36 0.02 1 11 . 3 LYS CD C 28.6 0.35 1 12 . 3 LYS HG3 H 1.36 0.02 1 13 . 3 LYS CE C 42.1 0.35 1 14 . 4 GLY N N 110.958 0.25 1 15 . 4 GLY HA2 H 3.93 0.02 1 16 . 4 GLY H H 8.636 0.02 1 17 . 4 GLY HA3 H 3.93 0.02 1 18 . 4 GLY CA C 45.7 0.35 1 19 . 4 GLY C C 175.2 0.35 1 20 . 5 GLY N N 107.674 0.25 1 21 . 5 GLY HA2 H 4.05 0.02 1 22 . 5 GLY H H 8.303 0.02 1 23 . 5 GLY HA3 H 4.05 0.02 1 24 . 5 GLY CA C 45.8 0.35 1 25 . 5 GLY C C 174.4 0.35 1 26 . 6 GLU N N 117.523 0.25 1 27 . 6 GLU CG C 36.5 0.35 1 28 . 6 GLU HA H 4.39 0.02 1 29 . 6 GLU C C 178.4 0.35 1 30 . 6 GLU H H 8.256 0.02 1 31 . 6 GLU CA C 55.9 0.35 1 32 . 6 GLU CB C 30.3 0.35 1 33 . 6 GLU HG2 H 2.11 0.02 1 34 . 6 GLU HG3 H 2.11 0.02 1 35 . 7 ALA N N 124.243 0.25 1 36 . 7 ALA H H 8.087 0.02 1 37 . 7 ALA CA C 55.5 0.35 1 38 . 7 ALA CB C 19.9 0.35 1 39 . 7 ALA HA H 4.11 0.02 1 40 . 7 ALA C C 179 0.35 1 41 . 7 ALA HB H 1.39 0.02 1 42 . 8 LEU N N 112.678 0.25 1 43 . 8 LEU CG C 27.5 0.35 1 44 . 8 LEU HB2 H 1.44 0.02 2 45 . 8 LEU HB3 H 1.805 0.02 2 46 . 8 LEU HA H 4.54 0.02 1 47 . 8 LEU C C 175.1 0.35 1 48 . 8 LEU CD1 C 22 0.35 1 49 . 8 LEU CD2 C 22 0.35 1 50 . 8 LEU H H 8.679 0.02 1 51 . 8 LEU CA C 52.4 0.35 1 52 . 8 LEU HG H 0.785 0.02 1 53 . 8 LEU CB C 41.9 0.35 1 54 . 9 LYS C C 178.1 0.35 1 55 . 9 LYS H H 7.076 0.02 1 56 . 9 LYS CA C 58.5 0.35 1 57 . 9 LYS CB C 32.8 0.35 1 58 . 9 LYS CE C 42.1 0.35 1 59 . 9 LYS N N 119.281 0.25 1 60 . 9 LYS CG C 24.7 0.35 1 61 . 9 LYS HB2 H 1.805 0.02 1 62 . 9 LYS HB3 H 1.805 0.02 1 63 . 9 LYS HA H 4 0.02 1 64 . 9 LYS HD2 H 1.449 0.02 1 65 . 9 LYS HD3 H 1.449 0.02 1 66 . 9 LYS HE2 H 2.991 0.02 1 67 . 9 LYS HE3 H 2.991 0.02 1 68 . 9 LYS HG2 H 1.362 0.02 2 69 . 9 LYS HG3 H 1.46 0.02 2 70 . 10 GLY N N 114.699 0.25 1 71 . 10 GLY H H 8.871 0.02 1 72 . 10 GLY CA C 46.1 0.35 1 73 . 10 GLY HA2 H 3.59 0.02 2 74 . 10 GLY HA3 H 4.29 0.02 2 75 . 10 GLY C C 175.3 0.35 1 76 . 11 LEU N N 121.259 0.25 1 77 . 11 LEU H H 8.027 0.02 1 78 . 11 LEU CA C 54.2 0.35 1 79 . 11 LEU HB2 H 2.15 0.02 2 80 . 11 LEU CB C 44.8 0.35 1 81 . 11 LEU HB3 H 0.882 0.02 2 82 . 11 LEU HA H 4.75 0.02 1 83 . 11 LEU C C 177.353 0.35 1 84 . 12 THR N N 117.403 0.25 1 85 . 12 THR H H 8.776 0.02 1 86 . 12 THR CA C 61.4 0.35 1 87 . 12 THR CB C 70.8 0.35 1 88 . 12 THR HA H 5.3 0.02 1 89 . 12 THR C C 174.4 0.35 1 90 . 12 THR HG2 H 1.027 0.02 1 91 . 12 THR CG2 C 22.3 0.35 1 92 . 12 THR HB H 3.97 0.02 1 93 . 13 PHE N N 124.881 0.25 1 94 . 13 PHE CZ C 131.2 0.35 1 95 . 13 PHE HA H 5.52 0.02 1 96 . 13 PHE HD1 H 7.01 0.02 1 97 . 13 PHE HD2 H 7.01 0.02 1 98 . 13 PHE CD1 C 132.4 0.35 1 99 . 13 PHE CD2 C 132.4 0.35 1 100 . 13 PHE HE1 H 6.85 0.02 1 101 . 13 PHE HE2 H 6.85 0.02 1 102 . 13 PHE CE1 C 132.4 0.35 1 103 . 13 PHE H H 9.371 0.02 1 104 . 13 PHE CE2 C 132.4 0.35 1 105 . 13 PHE CA C 56.5 0.35 1 106 . 13 PHE CB C 44.1 0.35 1 107 . 13 PHE HZ H 7.03 0.02 1 108 . 14 VAL N N 119.082 0.25 1 109 . 14 VAL H H 7.974 0.02 1 110 . 14 VAL CA C 60.8 0.35 1 111 . 14 VAL CB C 35.4 0.35 1 112 . 14 VAL HG1 H 0.72 0.02 1 113 . 14 VAL CG1 C 22.2 0.35 1 114 . 14 VAL HA H 4.56 0.02 1 115 . 14 VAL C C 174.3 0.35 1 116 . 14 VAL HG2 H 0.72 0.02 1 117 . 14 VAL CG2 C 22.2 0.35 1 118 . 14 VAL HB H 1.5 0.02 1 119 . 15 ILE N N 127.26 0.25 1 120 . 15 ILE HA H 4.783 0.02 1 121 . 15 ILE C C 174.9 0.35 1 122 . 15 ILE HB H 1.45 0.02 1 123 . 15 ILE HD1 H 0.61 0.02 1 124 . 15 ILE CD1 C 14 0.35 1 125 . 15 ILE H H 9.259 0.02 1 126 . 15 ILE CA C 60.6 0.35 1 127 . 15 ILE CB C 40.8 0.35 1 128 . 15 ILE CG1 C 28.1 0.35 1 129 . 15 ILE HG2 H 0.713 0.02 1 130 . 15 ILE CG2 C 18.6 0.35 1 131 . 16 THR N N 120.907 0.25 1 132 . 16 THR H H 8.863 0.02 1 133 . 16 THR CA C 60.1 0.35 1 134 . 16 THR CB C 70.9 0.35 1 135 . 16 THR HA H 4.81 0.02 1 136 . 16 THR C C 171.9 0.35 1 137 . 16 THR HG2 H 1.16 0.02 1 138 . 16 THR CG2 C 21.2 0.35 1 139 . 16 THR HB H 3.71 0.02 1 140 . 17 GLY N N 113.108 0.25 1 141 . 17 GLY HA2 H 3.6 0.02 2 142 . 17 GLY H H 8.389 0.02 1 143 . 17 GLY HA3 H 3.74 0.02 2 144 . 17 GLY CA C 44.3 0.35 1 145 . 17 GLY C C 172.8 0.35 1 146 . 18 GLU N N 118.707 0.25 1 147 . 18 GLU CG C 35.6 0.35 1 148 . 18 GLU HB2 H 1.792 0.02 1 149 . 18 GLU HB3 H 1.792 0.02 1 150 . 18 GLU HA H 4.37 0.02 1 151 . 18 GLU C C 176.9 0.35 1 152 . 18 GLU H H 9.211 0.02 1 153 . 18 GLU CA C 56.3 0.35 1 154 . 18 GLU CB C 31.5 0.35 1 155 . 18 GLU HG2 H 2.27 0.02 1 156 . 18 GLU HG3 H 2.27 0.02 1 157 . 19 LEU N N 126.834 0.25 1 158 . 19 LEU CG C 26.5 0.35 1 159 . 19 LEU HB2 H 1.592 0.02 2 160 . 19 LEU HB3 H 1.969 0.02 2 161 . 19 LEU HA H 4.81 0.02 1 162 . 19 LEU C C 177 0.35 1 163 . 19 LEU HD1 H 0.1457 0.02 2 164 . 19 LEU HD2 H 0.621 0.02 2 165 . 19 LEU CD1 C 22.3 0.35 1 166 . 19 LEU CD2 C 22.3 0.35 1 167 . 19 LEU H H 8.76 0.02 1 168 . 19 LEU HG H 1.0681 0.02 1 169 . 19 LEU CA C 53.6 0.35 1 170 . 19 LEU CB C 42.7 0.35 1 171 . 20 SER N N 118.104 0.25 1 172 . 20 SER H H 10.411 0.02 1 173 . 20 SER HB2 H 3.93 0.02 1 174 . 20 SER CA C 61.2 0.35 1 175 . 20 SER HB3 H 3.93 0.02 1 176 . 20 SER CB C 63.4 0.35 1 177 . 20 SER HA H 4.16 0.02 1 178 . 20 SER C C 174.4 0.35 1 179 . 21 ARG N N 119.615 0.25 1 180 . 21 ARG H H 6.986 0.02 1 181 . 21 ARG HB2 H 1.27 0.02 2 182 . 21 ARG CA C 52.2 0.35 1 183 . 21 ARG HB3 H 1.702 0.02 2 184 . 21 ARG CB C 31.1 0.35 1 185 . 21 ARG HA H 4.69 0.02 1 186 . 21 ARG C C 172.9 0.35 1 187 . 22 PRO CG C 28 0.35 1 188 . 22 PRO HB2 H 2.46 0.02 2 189 . 22 PRO HB3 H 1.72 0.02 2 190 . 22 PRO HA H 4.27 0.02 1 191 . 22 PRO C C 178.4 0.35 1 192 . 22 PRO HD2 H 3.48 0.02 2 193 . 22 PRO HD3 H 3.76 0.02 2 194 . 22 PRO CA C 63.3 0.35 1 195 . 22 PRO CB C 32.6 0.35 1 196 . 22 PRO HG2 H 1.439 0.02 1 197 . 22 PRO CD C 50.9 0.35 1 198 . 22 PRO HG3 H 1.439 0.02 1 199 . 23 ARG N N 126.62 0.25 1 200 . 23 ARG HB2 H 2.07 0.02 2 201 . 23 ARG HB3 H 1.73 0.02 2 202 . 23 ARG HA H 3.6 0.02 1 203 . 23 ARG C C 179.1 0.35 1 204 . 23 ARG HD2 H 3.226 0.02 1 205 . 23 ARG HD3 H 3.226 0.02 1 206 . 23 ARG HE H 4.185 0.02 1 207 . 23 ARG H H 8.869 0.02 1 208 . 23 ARG CA C 60.7 0.35 1 209 . 23 ARG CB C 30.7 0.35 1 210 . 23 ARG HG2 H 0.5525 0.02 1 211 . 23 ARG CD C 43.2 0.35 1 212 . 23 ARG HG3 H 0.5525 0.02 1 213 . 24 GLU N N 115.755 0.25 1 214 . 24 GLU CG C 36 0.35 1 215 . 24 GLU H H 9.351 0.02 1 216 . 24 GLU CA C 59.4 0.35 1 217 . 24 GLU HB2 H 1.99 0.02 1 218 . 24 GLU CB C 28.7 0.35 1 219 . 24 GLU HB3 H 1.99 0.02 1 220 . 24 GLU HA H 3.89 0.02 1 221 . 24 GLU C C 179.9 0.35 1 222 . 25 GLU N N 119.296 0.25 1 223 . 25 GLU CG C 36.5 0.35 1 224 . 25 GLU H H 7.239 0.02 1 225 . 25 GLU CA C 59.1 0.35 1 226 . 25 GLU HB2 H 2.07 0.02 1 227 . 25 GLU CB C 29.8 0.35 1 228 . 25 GLU HB3 H 2.07 0.02 1 229 . 25 GLU HA H 4.07 0.02 1 230 . 25 GLU C C 179.8 0.35 1 231 . 26 VAL N N 121.157 0.25 1 232 . 26 VAL H H 7.375 0.02 1 233 . 26 VAL CA C 66.8 0.35 1 234 . 26 VAL CB C 31.5 0.35 1 235 . 26 VAL HG1 H 0.833 0.02 2 236 . 26 VAL CG1 C 22.4 0.35 2 237 . 26 VAL HA H 3.442 0.02 1 238 . 26 VAL C C 178 0.35 1 239 . 26 VAL HG2 H 0.62 0.02 2 240 . 26 VAL CG2 C 20.4 0.35 2 241 . 26 VAL HB H 1.893 0.02 1 242 . 27 LYS N N 118.2 0.25 1 243 . 27 LYS CG C 26 0.35 1 244 . 27 LYS HB2 H 1.64 0.02 2 245 . 27 LYS HB3 H 1.72 0.02 2 246 . 27 LYS HA H 3.56 0.02 1 247 . 27 LYS C C 178 0.35 1 248 . 27 LYS HE2 H 2.735 0.02 1 249 . 27 LYS H H 8.512 0.02 1 250 . 27 LYS HE3 H 2.735 0.02 1 251 . 27 LYS CA C 61.1 0.35 1 252 . 27 LYS CB C 32.8 0.35 1 253 . 27 LYS HG2 H 1.06 0.02 1 254 . 27 LYS HG3 H 1.06 0.02 1 255 . 27 LYS CE C 41.6 0.35 1 256 . 28 ALA N N 118.605 0.25 1 257 . 28 ALA H H 7.679 0.02 1 258 . 28 ALA CA C 55.3 0.35 1 259 . 28 ALA CB C 18.2 0.35 1 260 . 28 ALA HA H 3.97 0.02 1 261 . 28 ALA C C 180.7 0.35 1 262 . 28 ALA HB H 1.44 0.02 1 263 . 29 LEU N N 121.089 0.25 1 264 . 29 LEU CG C 25.7 0.35 1 265 . 29 LEU HB2 H 1.55 0.02 2 266 . 29 LEU HB3 H 1.96 0.02 2 267 . 29 LEU HA H 3.98 0.02 1 268 . 29 LEU C C 177.6 0.35 1 269 . 29 LEU HD1 H 0.064 0.02 1 270 . 29 LEU HD2 H 0.064 0.02 1 271 . 29 LEU CD1 C 23.9 0.35 1 272 . 29 LEU CD2 C 23.9 0.35 1 273 . 29 LEU H H 7.492 0.02 1 274 . 29 LEU HG H 0.705 0.02 1 275 . 29 LEU CA C 58.3 0.35 1 276 . 29 LEU CB C 41.5 0.35 1 277 . 30 LEU N N 115.976 0.25 1 278 . 30 LEU CG C 24.9 0.35 1 279 . 30 LEU HB2 H 1.589 0.02 2 280 . 30 LEU HB3 H 0.649 0.02 2 281 . 30 LEU HA H 3.54 0.02 1 282 . 30 LEU C C 179.9 0.35 1 283 . 30 LEU CD1 C 21.9 0.35 1 284 . 30 LEU CD2 C 21.9 0.35 1 285 . 30 LEU H H 7.795 0.02 1 286 . 30 LEU CA C 57.9 0.35 1 287 . 30 LEU HG H 0.064 0.02 1 288 . 30 LEU CB C 40.3 0.35 1 289 . 31 ARG N N 117.149 0.25 1 290 . 31 ARG HB2 H 1.78 0.02 1 291 . 31 ARG HB3 H 1.78 0.02 1 292 . 31 ARG HA H 4.488 0.02 1 293 . 31 ARG C C 181.8 0.35 1 294 . 31 ARG HD2 H 3.1 0.02 1 295 . 31 ARG HD3 H 3.1 0.02 1 296 . 31 ARG H H 8.103 0.02 1 297 . 31 ARG CA C 59.1 0.35 1 298 . 31 ARG CB C 30.45 0.35 1 299 . 31 ARG HG2 H 1.058 0.02 1 300 . 31 ARG CD C 43.4 0.35 1 301 . 31 ARG HG3 H 1.058 0.02 1 302 . 32 ARG N N 122.719 0.25 1 303 . 32 ARG HB2 H 1.925 0.02 1 304 . 32 ARG HB3 H 1.925 0.02 1 305 . 32 ARG HA H 4.111 0.02 1 306 . 32 ARG C C 178.4 0.35 1 307 . 32 ARG HD2 H 3.119 0.02 1 308 . 32 ARG HD3 H 3.119 0.02 1 309 . 32 ARG H H 8.303 0.02 1 310 . 32 ARG CA C 59.3 0.35 1 311 . 32 ARG CB C 30.2 0.35 1 312 . 32 ARG HG2 H 1.0064 0.02 1 313 . 32 ARG CD C 43.9 0.35 1 314 . 32 ARG HG3 H 1.0064 0.02 1 315 . 33 LEU N N 116.81 0.25 1 316 . 33 LEU CG C 26.6 0.35 1 317 . 33 LEU HB2 H 1.75 0.02 2 318 . 33 LEU HB3 H 1.604 0.02 2 319 . 33 LEU HA H 4.46 0.02 1 320 . 33 LEU C C 176 0.35 1 321 . 33 LEU HD1 H 0.69 0.02 1 322 . 33 LEU HD2 H 0.69 0.02 1 323 . 33 LEU CD1 C 22.3 0.35 1 324 . 33 LEU CD2 C 22.3 0.35 1 325 . 33 LEU H H 7.265 0.02 1 326 . 33 LEU HG H 1.9 0.02 1 327 . 33 LEU CA C 54.5 0.35 1 328 . 33 LEU CB C 42.0 0.35 1 329 . 34 GLY N N 105.626 0.25 1 330 . 34 GLY HA2 H 3.66 0.02 2 331 . 34 GLY H H 7.738 0.02 1 332 . 34 GLY HA3 H 4.15 0.02 2 333 . 34 GLY CA C 45.5 0.35 1 334 . 34 GLY C C 174.8 0.35 1 335 . 35 ALA N N 122.186 0.25 1 336 . 35 ALA H H 7.95 0.02 1 337 . 35 ALA CA C 51.7 0.35 1 338 . 35 ALA CB C 21.1 0.35 1 339 . 35 ALA HA H 4.6 0.02 1 340 . 35 ALA C C 177.7 0.35 1 341 . 35 ALA HB H 1.375 0.02 1 342 . 36 LYS N N 118.464 0.25 1 343 . 36 LYS CG C 25.5 0.35 1 344 . 36 LYS HB2 H 1.77 0.02 2 345 . 36 LYS HB3 H 1.84 0.02 2 346 . 36 LYS HA H 4.64 0.02 1 347 . 36 LYS C C 176.3 0.35 1 348 . 36 LYS H H 8.379 0.02 1 349 . 36 LYS CA C 55.3 0.35 1 350 . 36 LYS CB C 34.3 0.35 1 351 . 36 LYS HG2 H 1.35 0.02 1 352 . 36 LYS HG3 H 1.35 0.02 1 353 . 36 LYS CE C 42.3 0.35 1 354 . 37 VAL N N 123.294 0.25 1 355 . 37 VAL H H 8.779 0.02 1 356 . 37 VAL CA C 60.8 0.35 1 357 . 37 VAL CB C 34.4 0.35 1 358 . 37 VAL HG1 H 0.87 0.02 1 359 . 37 VAL CG1 C 21.9 0.35 1 360 . 37 VAL HA H 5.32 0.02 1 361 . 37 VAL C C 178.1 0.35 1 362 . 37 VAL HG2 H 0.87 0.02 1 363 . 37 VAL CG2 C 21.9 0.35 1 364 . 37 VAL HB H 1.75 0.02 1 365 . 38 THR N N 119.87 0.25 1 366 . 38 THR H H 8.609 0.02 1 367 . 38 THR CA C 59.3 0.35 1 368 . 38 THR CB C 70.7 0.35 1 369 . 38 THR HA H 4.8 0.02 1 370 . 38 THR C C 173.6 0.35 1 371 . 38 THR HG2 H 1.06 0.02 1 372 . 38 THR HB H 4.262 0.02 1 373 . 39 ASP N N 119.052 0.25 1 374 . 39 ASP H H 8.402 0.02 1 375 . 39 ASP HB2 H 2.5 0.02 2 376 . 39 ASP CA C 55.4 0.35 1 377 . 39 ASP HB3 H 2.76 0.02 2 378 . 39 ASP CB C 42.7 0.35 1 379 . 39 ASP HA H 4.95 0.02 1 380 . 39 ASP C C 176.3 0.35 1 381 . 40 SER N N 113.46 0.25 1 382 . 40 SER H H 7.615 0.02 1 383 . 40 SER HB2 H 3.63 0.02 1 384 . 40 SER CA C 56.9 0.35 1 385 . 40 SER HB3 H 3.63 0.02 1 386 . 40 SER CB C 64.5 0.35 1 387 . 40 SER HA H 4.66 0.02 1 388 . 40 SER C C 173.3 0.35 1 389 . 41 VAL N N 124.9 0.25 1 390 . 41 VAL H H 8.636 0.02 1 391 . 41 VAL CA C 62.1 0.35 1 392 . 41 VAL CB C 32.8 0.35 1 393 . 41 VAL HG1 H 0.71 0.02 1 394 . 41 VAL CG1 C 22.1 0.35 1 395 . 41 VAL HA H 4.02 0.02 1 396 . 41 VAL C C 174.8 0.35 1 397 . 41 VAL HG2 H 0.71 0.02 1 398 . 41 VAL CG2 C 22.1 0.35 1 399 . 41 VAL HB H 1.76 0.02 1 400 . 42 SER N N 123.968 0.25 1 401 . 42 SER H H 9.235 0.02 1 402 . 42 SER HB2 H 3.66 0.02 2 403 . 42 SER CA C 57.1 0.35 1 404 . 42 SER HB3 H 4.09 0.02 2 405 . 42 SER CB C 67.3 0.35 1 406 . 42 SER HA H 4.53 0.02 1 407 . 42 SER C C 173.3 0.35 1 408 . 43 ARG N N 117.235 0.25 1 409 . 43 ARG CG C 29.2 0.35 1 410 . 43 ARG HA H 4.02 0.02 1 411 . 43 ARG C C 177.2 0.35 1 412 . 43 ARG HD2 H 3.15 0.02 1 413 . 43 ARG HD3 H 3.15 0.02 1 414 . 43 ARG H H 8.851 0.02 1 415 . 43 ARG CA C 58.9 0.35 1 416 . 43 ARG CB C 29.5 0.35 1 417 . 43 ARG HG2 H 1.793 0.02 1 418 . 43 ARG CD C 43.2 0.35 1 419 . 43 ARG HG3 H 1.793 0.02 1 420 . 44 LYS N N 115.82 0.25 1 421 . 44 LYS CG C 24.8 0.35 1 422 . 44 LYS HB2 H 1.92 0.02 2 423 . 44 LYS HB3 H 1.33 0.02 2 424 . 44 LYS HA H 4.1 0.02 1 425 . 44 LYS C C 177.1 0.35 1 426 . 44 LYS HD2 H 1.556 0.02 1 427 . 44 LYS HD3 H 1.556 0.02 1 428 . 44 LYS HE2 H 2.868 0.02 1 429 . 44 LYS H H 7.916 0.02 1 430 . 44 LYS HE3 H 2.868 0.02 1 431 . 44 LYS CA C 55.7 0.35 1 432 . 44 LYS CB C 32.5 0.35 1 433 . 44 LYS CD C 28.1 0.35 1 434 . 44 LYS CE C 42.3 0.35 1 435 . 45 THR N N 119.963 0.25 1 436 . 45 THR H H 7.638 0.02 1 437 . 45 THR CA C 65.5 0.35 1 438 . 45 THR CB C 68.9 0.35 1 439 . 45 THR HA H 3.4 0.02 1 440 . 45 THR C C 173.1 0.35 1 441 . 45 THR HB H 4.02 0.02 1 442 . 45 THR CG2 C 21.8 0.35 1 443 . 46 SER N N 123.554 0.25 1 444 . 46 SER H H 8.652 0.02 1 445 . 46 SER HB2 H 3.47 0.02 2 446 . 46 SER CA C 60.6 0.35 1 447 . 46 SER HB3 H 3.31 0.02 2 448 . 46 SER CB C 62.1 0.35 1 449 . 46 SER HA H 3.95 0.02 1 450 . 46 SER C C 173.2 0.35 1 451 . 47 TYR N N 110.648 0.25 1 452 . 47 TYR CG C 117.7 0.35 1 453 . 47 TYR HB2 H 2.06 0.02 2 454 . 47 TYR HB3 H 2.46 0.02 2 455 . 47 TYR HA H 4.765 0.02 1 456 . 47 TYR C C 174.1 0.35 1 457 . 47 TYR HD1 H 6.256 0.02 1 458 . 47 TYR HD2 H 6.256 0.02 1 459 . 47 TYR CD1 C 133.6 0.35 1 460 . 47 TYR HE1 H 6.54 0.02 1 461 . 47 TYR CD2 C 133.6 0.35 1 462 . 47 TYR HE2 H 6.54 0.02 1 463 . 47 TYR CE1 C 118 0.35 1 464 . 47 TYR CE2 C 118 0.35 1 465 . 47 TYR H H 6.8 0.02 1 466 . 47 TYR CA C 57 0.35 1 467 . 47 TYR CB C 44.8 0.35 1 468 . 48 LEU N N 122.183 0.25 1 469 . 48 LEU CG C 27 0.35 1 470 . 48 LEU HB2 H 1.678 0.02 2 471 . 48 LEU HB3 H 0.8 0.02 2 472 . 48 LEU HA H 5.02 0.02 1 473 . 48 LEU C C 175.3 0.35 1 474 . 48 LEU HD1 H 0.64 0.02 1 475 . 48 LEU HD2 H 0.64 0.02 1 476 . 48 LEU H H 8.495 0.02 1 477 . 48 LEU HG H 1.17 0.02 1 478 . 48 LEU CA C 52.6 0.35 1 479 . 48 LEU CB C 44.6 0.35 1 480 . 49 VAL N N 129.236 0.25 1 481 . 49 VAL H H 9.543 0.02 1 482 . 49 VAL CA C 61.7 0.35 1 483 . 49 VAL CB C 32.3 0.35 1 484 . 49 VAL HG1 H 0.669 0.02 2 485 . 49 VAL CG1 C 21.1 0.35 2 486 . 49 VAL HA H 4.7 0.02 1 487 . 49 VAL C C 175 0.35 1 488 . 49 VAL HG2 H -0.08 0.02 2 489 . 49 VAL CG2 C 22.1 0.35 2 490 . 49 VAL HB H 2.05 0.02 1 491 . 50 VAL N N 126.937 0.25 1 492 . 50 VAL H H 9.066 0.02 1 493 . 50 VAL CA C 61.5 0.35 1 494 . 50 VAL CB C 33.1 0.35 1 495 . 50 VAL HG1 H 0.2561 0.02 2 496 . 50 VAL CG1 C 22.3 0.35 1 497 . 50 VAL HA H 4.216 0.02 1 498 . 50 VAL C C 176.5 0.35 1 499 . 50 VAL HG2 H 0.88 0.02 2 500 . 50 VAL CG2 C 22.3 0.35 1 501 . 50 VAL HB H 1.94 0.02 1 502 . 51 GLY N N 113.776 0.25 1 503 . 51 GLY HA2 H 3.26 0.02 2 504 . 51 GLY H H 8.712 0.02 1 505 . 51 GLY HA3 H 4.32 0.02 2 506 . 51 GLY CA C 43.9 0.35 1 507 . 51 GLY C C 173.6 0.35 1 508 . 52 GLU N N 119.877 0.25 1 509 . 52 GLU CG C 36.4 0.35 1 510 . 52 GLU HB2 H 1.94 0.02 2 511 . 52 GLU HB3 H 2.17 0.02 2 512 . 52 GLU HA H 4.13 0.02 1 513 . 52 GLU C C 177.8 0.35 1 514 . 52 GLU H H 8.588 0.02 1 515 . 52 GLU CA C 56.7 0.35 1 516 . 52 GLU CB C 30.7 0.35 1 517 . 52 GLU HG2 H 2.31 0.02 2 518 . 52 GLU HG3 H 1.267 0.02 2 519 . 53 ASN HD21 H 6.895 0.02 1 520 . 53 ASN N N 116.703 0.25 1 521 . 53 ASN HD22 H 7.728 0.02 1 522 . 53 ASN ND2 N 114.436 0.25 1 523 . 53 ASN H H 9.314 0.02 1 524 . 53 ASN CA C 54.3 0.35 1 525 . 53 ASN HB2 H 2.9 0.02 1 526 . 53 ASN CB C 37.3 0.35 1 527 . 53 ASN HB3 H 2.9 0.02 1 528 . 53 ASN HA H 4.44 0.02 1 529 . 54 PRO CG C 26.8 0.35 1 530 . 54 PRO HB2 H 1.625 0.02 1 531 . 54 PRO HB3 H 1.625 0.02 1 532 . 54 PRO HA H 3.94 0.02 1 533 . 54 PRO C C 177.8 0.35 1 534 . 54 PRO HD2 H 3.46 0.02 2 535 . 54 PRO HD3 H 3.76 0.02 2 536 . 54 PRO CA C 63.7 0.35 1 537 . 54 PRO CB C 34 0.35 1 538 . 54 PRO CD C 50.9 0.35 1 539 . 55 GLY N N 107.615 0.25 1 540 . 55 GLY HA2 H 4.200 0.02 2 541 . 55 GLY H H 8.222 0.02 1 542 . 55 GLY HA3 H 3.93 0.02 2 543 . 55 GLY CA C 44.9 0.35 1 544 . 55 GLY C C 176.3 0.35 1 545 . 56 SER N N 117.42 0.25 1 546 . 56 SER H H 8.718 0.02 1 547 . 56 SER HB2 H 3.947 0.02 1 548 . 56 SER CA C 61.4 0.35 1 549 . 56 SER HB3 H 3.947 0.02 1 550 . 56 SER CB C 63.4 0.35 1 551 . 56 SER HA H 4.217 0.02 1 552 . 56 SER C C 176.948 0.35 1 553 . 57 LYS N N 122.147 0.25 1 554 . 57 LYS H H 8.537 0.02 1 555 . 57 LYS HB2 H 1.72 0.02 2 556 . 57 LYS CA C 60.5 0.35 1 557 . 57 LYS HB3 H 1.454 0.02 2 558 . 57 LYS CB C 33.5 0.35 1 559 . 57 LYS HA H 3.75 0.02 1 560 . 57 LYS C C 178.225 0.35 1 561 . 58 LEU N N 117.365 0.25 1 562 . 58 LEU CG C 26.1 0.35 1 563 . 58 LEU HB2 H 1.12 0.02 2 564 . 58 LEU HB3 H 1.98 0.02 2 565 . 58 LEU HA H 3.94 0.02 1 566 . 58 LEU C C 177.8 0.35 1 567 . 58 LEU HD1 H 1.392 0.02 1 568 . 58 LEU HD2 H 1.392 0.02 1 569 . 58 LEU CD1 C 24.1 0.35 1 570 . 58 LEU CD2 C 24.1 0.35 1 571 . 58 LEU H H 7.506 0.02 1 572 . 58 LEU CA C 58.4 0.35 1 573 . 58 LEU HG H 0.854 0.02 1 574 . 58 LEU CB C 42.3 0.35 1 575 . 59 GLU N N 118.285 0.25 1 576 . 59 GLU CG C 36.7 0.35 1 577 . 59 GLU HB2 H 1.34 0.02 2 578 . 59 GLU HB3 H 1.975 0.02 2 579 . 59 GLU HA H 4.06 0.02 1 580 . 59 GLU C C 180 0.35 1 581 . 59 GLU H H 7.281 0.02 1 582 . 59 GLU CA C 59.3 0.35 1 583 . 59 GLU CB C 28.9 0.35 1 584 . 59 GLU HG2 H 2.81 0.02 1 585 . 59 GLU HG3 H 2.81 0.02 1 586 . 60 LYS N N 119.756 0.25 1 587 . 60 LYS CG C 25.1 0.35 1 588 . 60 LYS HB2 H 1.79 0.02 2 589 . 60 LYS HB3 H 1.73 0.02 2 590 . 60 LYS HA H 4.009 0.02 1 591 . 60 LYS C C 178.6 0.35 1 592 . 60 LYS HE2 H 2.86 0.02 1 593 . 60 LYS H H 7.634 0.02 1 594 . 60 LYS HE3 H 2.86 0.02 1 595 . 60 LYS CA C 59.0 0.35 1 596 . 60 LYS CB C 32.2 0.35 1 597 . 60 LYS HG2 H 0.88 0.02 1 598 . 60 LYS CD C 31.8 0.35 1 599 . 60 LYS HG3 H 0.88 0.02 1 600 . 60 LYS CE C 42.2 0.35 1 601 . 61 ALA N N 120.092 0.25 1 602 . 61 ALA H H 8.178 0.02 1 603 . 61 ALA CA C 55.9 0.35 1 604 . 61 ALA CB C 18.8 0.35 1 605 . 61 ALA HA H 3.76 0.02 1 606 . 61 ALA C C 180.1 0.35 1 607 . 61 ALA HB H 1.384 0.02 1 608 . 62 ARG N N 116.88 0.25 1 609 . 62 ARG HB2 H 1.82 0.02 1 610 . 62 ARG HB3 H 1.82 0.02 1 611 . 62 ARG HA H 4.024 0.02 1 612 . 62 ARG C C 180.5 0.35 1 613 . 62 ARG HD2 H 3.123 0.02 1 614 . 62 ARG HD3 H 3.123 0.02 1 615 . 62 ARG H H 8.061 0.02 1 616 . 62 ARG CA C 59.2 0.35 1 617 . 62 ARG CB C 29.9 0.35 1 618 . 62 ARG HG2 H 1.0958 0.02 1 619 . 62 ARG CD C 42.8 0.35 1 620 . 62 ARG HG3 H 1.0958 0.02 1 621 . 63 ALA N N 121.935 0.25 1 622 . 63 ALA H H 7.876 0.02 1 623 . 63 ALA CA C 54.9 0.35 1 624 . 63 ALA CB C 18.2 0.35 1 625 . 63 ALA HA H 4.16 0.02 1 626 . 63 ALA C C 180.1 0.35 1 627 . 63 ALA HB H 1.44 0.02 1 628 . 64 LEU N N 115.677 0.25 1 629 . 64 LEU CG C 26 0.35 1 630 . 64 LEU HB2 H 1.59 0.02 2 631 . 64 LEU HB3 H 1.37 0.02 2 632 . 64 LEU HA H 4.237 0.02 1 633 . 64 LEU C C 177.4 0.35 1 634 . 64 LEU HD1 H 0.5831 0.02 1 635 . 64 LEU HD2 H 0.5831 0.02 1 636 . 64 LEU CD1 C 22.3 0.35 1 637 . 64 LEU CD2 C 22.3 0.35 1 638 . 64 LEU H H 7.547 0.02 1 639 . 64 LEU HG H 1.664 0.02 1 640 . 64 LEU CA C 54.6 0.35 1 641 . 64 LEU CB C 44.2 0.35 1 642 . 65 GLY N N 108.934 0.25 1 643 . 65 GLY HA2 H 3.95 0.02 2 644 . 65 GLY H H 7.705 0.02 1 645 . 65 GLY HA3 H 3.7 0.02 2 646 . 65 GLY CA C 46.3 0.35 1 647 . 65 GLY C C 175.2 0.35 1 648 . 66 VAL N N 125.285 0.25 1 649 . 66 VAL H H 8.1 0.02 1 650 . 66 VAL CA C 60.1 0.35 1 651 . 66 VAL CB C 33.8 0.35 1 652 . 66 VAL HA H 3.94 0.02 1 653 . 66 VAL C C 173.9 0.35 1 654 . 66 VAL HB H 1.625 0.02 1 655 . 67 PRO CG C 27.3 0.35 1 656 . 67 PRO HB2 H 1.99 0.02 1 657 . 67 PRO HB3 H 1.99 0.02 1 658 . 67 PRO HA H 4.39 0.02 1 659 . 67 PRO C C 175.9 0.35 1 660 . 67 PRO HD2 H 3.95 0.02 2 661 . 67 PRO HD3 H 3.73 0.02 2 662 . 67 PRO CA C 63.2 0.35 1 663 . 67 PRO CB C 32.8 0.35 1 664 . 67 PRO CD C 50.6 0.35 1 665 . 68 THR N N 108.652 0.25 1 666 . 68 THR H H 7.984 0.02 1 667 . 68 THR CA C 58.9 0.35 1 668 . 68 THR CB C 71.7 0.35 1 669 . 68 THR HA H 5.56 0.02 1 670 . 68 THR C C 175.3 0.35 1 671 . 68 THR HG2 H 1.051 0.02 1 672 . 68 THR CG2 C 21.5 0.35 1 673 . 68 THR HB H 4.162 0.02 1 674 . 69 LEU N N 120.808 0.25 1 675 . 69 LEU HB2 H 1.37 0.02 2 676 . 69 LEU HB3 H 1.468 0.02 2 677 . 69 LEU HA H 5.07 0.02 1 678 . 69 LEU C C 177.7 0.35 1 679 . 69 LEU H H 8.798 0.02 1 680 . 69 LEU CA C 53.2 0.35 1 681 . 69 LEU HG H 0.63 0.02 1 682 . 69 LEU CB C 47.0 0.35 1 683 . 70 THR N N 112.926 0.25 1 684 . 70 THR H H 8.896 0.02 1 685 . 70 THR CA C 61.2 0.35 1 686 . 70 THR CB C 70.8 0.35 1 687 . 70 THR HA H 4.63 0.02 1 688 . 70 THR C C 175.3 0.35 1 689 . 70 THR HG2 H 1.26 0.02 1 690 . 70 THR CG2 C 22.1 0.35 1 691 . 70 THR HB H 4.742 0.02 1 692 . 71 GLU N N 122.094 0.25 1 693 . 71 GLU CG C 36.1 0.35 1 694 . 71 GLU HB2 H 1.95 0.02 1 695 . 71 GLU HB3 H 1.95 0.02 1 696 . 71 GLU HA H 3.33 0.02 1 697 . 71 GLU C C 177.6 0.35 1 698 . 71 GLU H H 9.151 0.02 1 699 . 71 GLU CA C 60.8 0.35 1 700 . 71 GLU CB C 29.8 0.35 1 701 . 71 GLU HG2 H 2.192 0.02 1 702 . 71 GLU HG3 H 2.192 0.02 1 703 . 72 GLU N N 115.702 0.25 1 704 . 72 GLU CG C 36.7 0.35 1 705 . 72 GLU HB2 H 1.94 0.02 1 706 . 72 GLU HB3 H 1.94 0.02 1 707 . 72 GLU HA H 3.96 0.02 1 708 . 72 GLU C C 180.4 0.35 1 709 . 72 GLU H H 8.359 0.02 1 710 . 72 GLU CA C 60 0.35 1 711 . 72 GLU CB C 29.5 0.35 1 712 . 72 GLU HG2 H 2.23 0.02 1 713 . 72 GLU HG3 H 2.23 0.02 1 714 . 73 GLU N N 118.975 0.25 1 715 . 73 GLU H H 7.584 0.02 1 716 . 73 GLU HB2 H 1.895 0.02 1 717 . 73 GLU CA C 59 0.35 1 718 . 73 GLU HB3 H 1.895 0.02 1 719 . 73 GLU CB C 30.4 0.35 1 720 . 73 GLU HA H 3.77 0.02 1 721 . 73 GLU C C 180.5 0.35 1 722 . 74 LEU N N 123.004 0.25 1 723 . 74 LEU CG C 24.8 0.35 1 724 . 74 LEU HB2 H 1.044 0.02 2 725 . 74 LEU HB3 H 2.1 0.02 2 726 . 74 LEU HA H 3.86 0.02 1 727 . 74 LEU C C 178.5 0.35 1 728 . 74 LEU HD1 H 0.413 0.02 1 729 . 74 LEU HD2 H 0.413 0.02 1 730 . 74 LEU CD1 C 23 0.35 1 731 . 74 LEU CD2 C 23 0.35 1 732 . 74 LEU H H 8.693 0.02 1 733 . 74 LEU HG H 0.477 0.02 1 734 . 74 LEU CA C 58.4 0.35 1 735 . 74 LEU CB C 40.1 0.35 1 736 . 75 TYR N N 117.995 0.25 1 737 . 75 TYR CG C 119.5 0.35 1 738 . 75 TYR HB2 H 3 0.02 1 739 . 75 TYR HB3 H 3 0.02 1 740 . 75 TYR HA H 4.17 0.02 1 741 . 75 TYR C C 179.1 0.35 1 742 . 75 TYR HD1 H 6.917 0.02 1 743 . 75 TYR HD2 H 6.917 0.02 1 744 . 75 TYR CD1 C 132 0.35 1 745 . 75 TYR HE1 H 6.525 0.02 1 746 . 75 TYR CD2 C 132 0.35 1 747 . 75 TYR HE2 H 6.525 0.02 1 748 . 75 TYR CE1 C 119.2 0.35 1 749 . 75 TYR CE2 C 119.2 0.35 1 750 . 75 TYR H H 7.844 0.02 1 751 . 75 TYR CA C 61.4 0.35 1 752 . 75 TYR CB C 36.1 0.35 1 753 . 76 ARG N N 119.653 0.25 1 754 . 76 ARG HB2 H 1.86 0.02 1 755 . 76 ARG HB3 H 1.86 0.02 1 756 . 76 ARG HA H 4.14 0.02 1 757 . 76 ARG C C 179.7 0.35 1 758 . 76 ARG HD2 H 3.19 0.02 1 759 . 76 ARG HD3 H 3.19 0.02 1 760 . 76 ARG H H 7.982 0.02 1 761 . 76 ARG CA C 59.8 0.35 1 762 . 76 ARG CB C 30.5 0.35 1 763 . 77 LEU N N 124.262 0.25 1 764 . 77 LEU CG C 31.8 0.35 1 765 . 77 LEU HB2 H 1.45 0.02 2 766 . 77 LEU HB3 H 1.89 0.02 2 767 . 77 LEU HA H 4.146 0.02 1 768 . 77 LEU C C 179.3 0.35 1 769 . 77 LEU HD1 H 0.042 0.02 2 770 . 77 LEU HD2 H 0.531 0.02 2 771 . 77 LEU CD1 C 24.7 0.35 1 772 . 77 LEU CD2 C 24.7 0.35 1 773 . 77 LEU H H 7.903 0.02 1 774 . 77 LEU CA C 59.1 0.35 1 775 . 77 LEU CB C 41.7 0.35 1 776 . 78 LEU N N 118.024 0.25 1 777 . 78 LEU HB2 H 1.19 0.02 2 778 . 78 LEU HB3 H 1.9 0.02 2 779 . 78 LEU HA H 3.66 0.02 1 780 . 78 LEU C C 181.5 0.35 1 781 . 78 LEU HD1 H 0.58 0.02 2 782 . 78 LEU HD2 H 0.5 0.02 2 783 . 78 LEU CD1 C 23.2 0.35 2 784 . 78 LEU CD2 C 24 0.35 2 785 . 78 LEU H H 8.497 0.02 1 786 . 78 LEU CA C 58.8 0.35 1 787 . 78 LEU CB C 41.1 0.35 1 788 . 79 GLU N N 123.046 0.25 1 789 . 79 GLU CG C 35.8 0.35 1 790 . 79 GLU HB2 H 1.95 0.02 1 791 . 79 GLU HB3 H 1.95 0.02 1 792 . 79 GLU HA H 4.25 0.02 1 793 . 79 GLU C C 180 0.35 1 794 . 79 GLU H H 8.421 0.02 1 795 . 79 GLU CA C 59.4 0.35 1 796 . 79 GLU CB C 30.1 0.35 1 797 . 79 GLU HG2 H 2.4 0.02 1 798 . 79 GLU HG3 H 2.4 0.02 1 799 . 80 ALA N N 122.974 0.25 1 800 . 80 ALA H H 8.046 0.02 1 801 . 80 ALA CA C 55.2 0.35 1 802 . 80 ALA CB C 18.2 0.35 1 803 . 80 ALA HA H 4.1 0.02 1 804 . 80 ALA C C 181.2 0.35 1 805 . 80 ALA HB H 1.52 0.02 1 806 . 81 ARG N N 112.862 0.25 1 807 . 81 ARG HB2 H 1.7 0.02 1 808 . 81 ARG HB3 H 1.7 0.02 1 809 . 81 ARG HA H 4.27 0.02 1 810 . 81 ARG C C 178.2 0.35 1 811 . 81 ARG HD2 H 3.16 0.02 1 812 . 81 ARG HD3 H 3.16 0.02 1 813 . 81 ARG H H 8.176 0.02 1 814 . 81 ARG CA C 57.1 0.35 1 815 . 81 ARG CB C 31.3 0.35 2 816 . 81 ARG CD C 42.5 0.35 2 817 . 82 THR N N 105.708 0.25 1 818 . 82 THR H H 7.964 0.02 1 819 . 82 THR CA C 62.8 0.35 1 820 . 82 THR CB C 71.8 0.35 1 821 . 82 THR HA H 4.4 0.02 1 822 . 82 THR C C 176.9 0.35 1 823 . 82 THR HG2 H 1.11 0.02 1 824 . 82 THR CG2 C 21.4 0.35 1 825 . 82 THR HB H 4.12 0.02 1 826 . 83 GLY N N 111.72 0.25 1 827 . 83 GLY HA2 H 4.09 0.02 2 828 . 83 GLY H H 8.233 0.02 1 829 . 83 GLY HA3 H 3.8 0.02 2 830 . 83 GLY CA C 46.1 0.35 1 831 . 83 GLY C C 173.8 0.35 1 832 . 84 LYS N N 120.662 0.25 1 833 . 84 LYS CG C 25 0.35 1 834 . 84 LYS HB2 H 1.54 0.02 1 835 . 84 LYS HB3 H 1.54 0.02 1 836 . 84 LYS HA H 4.47 0.02 1 837 . 84 LYS C C 175.4 0.35 1 838 . 84 LYS HD2 H 2.858 0.02 1 839 . 84 LYS HD3 H 2.858 0.02 1 840 . 84 LYS H H 8.011 0.02 1 841 . 84 LYS CA C 54.6 0.35 1 842 . 84 LYS CB C 35.1 0.35 1 843 . 84 LYS HG2 H 0.5588 0.02 2 844 . 84 LYS HG3 H 1.24 0.02 2 845 . 84 LYS CE C 42.3 0.35 1 846 . 85 LYS N N 118.111 0.25 1 847 . 85 LYS CG C 24.9 0.35 1 848 . 85 LYS HB2 H 1.515 0.02 2 849 . 85 LYS HB3 H 1.95 0.02 2 850 . 85 LYS HA H 4.16 0.02 1 851 . 85 LYS C C 179.3 0.35 1 852 . 85 LYS HE2 H 2.862 0.02 1 853 . 85 LYS H H 8.338 0.02 1 854 . 85 LYS CA C 55.4 0.35 1 855 . 85 LYS HE3 H 2.862 0.02 1 856 . 85 LYS CB C 33.4 0.35 1 857 . 85 LYS CE C 42.2 0.35 1 858 . 86 ALA N N 126.3 0.25 1 859 . 86 ALA H H 9.593 0.02 1 860 . 86 ALA CA C 56.1 0.35 1 861 . 86 ALA CB C 17.7 0.35 1 862 . 86 ALA HA H 3.687 0.02 1 863 . 86 ALA C C 179.8 0.35 1 864 . 86 ALA HB H 1.06 0.02 1 865 . 87 GLU N N 114.349 0.25 1 866 . 87 GLU CG C 36.4 0.35 1 867 . 87 GLU HB2 H 1.56 0.02 1 868 . 87 GLU HB3 H 1.56 0.02 1 869 . 87 GLU HA H 3.86 0.02 1 870 . 87 GLU C C 178.5 0.35 1 871 . 87 GLU H H 8.97 0.02 1 872 . 87 GLU CA C 59.2 0.35 1 873 . 87 GLU CB C 28.8 0.35 1 874 . 87 GLU HG2 H 2.14 0.02 1 875 . 87 GLU HG3 H 2.14 0.02 1 876 . 88 GLU N N 117.619 0.25 1 877 . 88 GLU CG C 36.1 0.35 1 878 . 88 GLU HB2 H 1.99 0.02 1 879 . 88 GLU HB3 H 1.99 0.02 1 880 . 88 GLU HA H 4.046 0.02 1 881 . 88 GLU C C 178 0.35 1 882 . 88 GLU H H 7.513 0.02 1 883 . 88 GLU CA C 57.5 0.35 1 884 . 88 GLU CB C 30.1 0.35 1 885 . 88 GLU HG2 H 2.192 0.02 1 886 . 88 GLU HG3 H 2.192 0.02 1 887 . 89 LEU N N 119.542 0.25 1 888 . 89 LEU CG C 26.2 0.35 1 889 . 89 LEU HB2 H 1.35 0.02 2 890 . 89 LEU HB3 H 1.784 0.02 2 891 . 89 LEU HA H 4.1 0.02 1 892 . 89 LEU C C 178 0.35 1 893 . 89 LEU CD1 C 23 0.35 1 894 . 89 LEU CD2 C 23 0.35 1 895 . 89 LEU H H 7.631 0.02 1 896 . 89 LEU CA C 56.2 0.35 1 897 . 89 LEU HG H 0.695 0.02 1 898 . 89 LEU CB C 43.3 0.35 1 899 . 90 VAL N N 114.352 0.25 1 900 . 90 VAL H H 7.67 0.02 1 901 . 90 VAL CA C 63.0 0.35 1 902 . 90 VAL CB C 32.8 0.35 1 903 . 90 VAL HG1 H 0.689 0.02 1 904 . 90 VAL CG1 C 24.2 0.35 2 905 . 90 VAL HA H 3.935 0.02 1 906 . 90 VAL C C 178 0.35 1 907 . 90 VAL HG2 H 0.689 0.02 1 908 . 90 VAL CG2 C 20.1 0.35 2 909 . 90 VAL HB H 1.93 0.02 1 910 . 91 GLY N N 110.175 0.25 1 911 . 91 GLY HA2 H 3.898 0.02 1 912 . 91 GLY H H 7.811 0.02 1 913 . 91 GLY HA3 H 3.898 0.02 1 914 . 91 GLY CA C 45.3 0.35 1 915 . 92 SER N N 120.726 0.25 1 916 . 92 SER H H 7.727 0.02 1 917 . 92 SER CA C 60.0 0.35 1 918 . 92 SER CB C 64.9 0.35 1 stop_ save_