data_5629 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N resonance assignments and topology of MTH187, a conserved protein from Methanobacterium thermoautotrophicum ; _BMRB_accession_number 5629 _BMRB_flat_file_name bmr5629.str _Entry_type original _Submission_date 2002-12-18 _Accession_date 2002-12-18 _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 Gignac Isabelle . . 2 Yee Adelinda . . 3 Suh 'Jeong Yong' . . 4 Ziembirka Anna . . 5 Arrowsmith Cheryl H. . 6 Sykes Brian D. . 7 Gagne Stephane M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 599 "13C chemical shifts" 440 "15N chemical shifts" 118 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-11-05 update BMRB 'complete the entry citation' 2003-04-08 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'MTH187 from Methanobacterium thermoautotrophicum has three HEAT-like Repeats' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16819590 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Julien Olivier . . 2 Gignac Isabelle . . 3 Hutton Anna . . 4 Yee Adelinda . . 5 Arrowsmith Cheryl H. . 6 Gagne Stephane M. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 35 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 149 _Page_last 154 _Year 2006 _Details . loop_ _Keyword NMR 'resonance assignments' 'Methanobacterium thermoautotrophicum' MTH187 'structural proteomics' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation _Saveframe_category citation _Citation_full ; Christendat D, Yee A, Dharamsi A, Kluger Y, Savchenko A, Cort JR, Booth V, Mackereth CD, Saridakis V, Ekiel I, Kozlov G, Maxwell KL, Wu N, McIntosh LP, Gehring K, Kennedy MA, Davidson AR, Pai EF, Gerstein M, Edwards AM, Arrowsmith CH. Structural proteomics of an archaeon. Nat Struct Biol. 2000 Oct;7(10):903-9. ; _Citation_title 'Structural proteomics of an archaeon.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11017201 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Christendat D. . . 2 Yee A. . . 3 Dharamsi A. . . 4 Kluger Y. . . 5 Savchenko A. . . 6 Cort 'J. R.' R. . 7 Booth V. . . 8 Mackereth 'C. D.' D. . 9 Saridakis V. . . 10 Ekiel I. . . 11 Kozlov G. . . 12 Maxwell 'K. L.' L. . 13 Wu N. . . 14 McIntosh 'L. P.' P. . 15 Gehring K. . . 16 Kennedy 'M. A.' A. . 17 Davidson 'A. R.' R. . 18 Pai 'E. F.' F. . 19 Gerstein M. . . 20 Edwards 'A. M.' M. . 21 Arrowsmith 'C. H.' H. . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_name_full 'Nature structural biology' _Journal_volume 7 _Journal_issue 10 _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 903 _Page_last 909 _Year 2000 _Details ; A set of 424 nonmembrane proteins from Methanobacterium thermoautotrophicum were cloned, expressed and purified for structural studies. Of these, approximately 20% were found to be suitable candidates for X-ray crystallographic or NMR spectroscopic analysis without further optimization of conditions, providing an estimate of the number of the most accessible structural targets in the proteome. A retrospective analysis of the experimental behavior of these proteins suggested some simple relations between sequence and solubility, implying that data bases of protein properties will be useful in optimizing high throughput strategies. Of the first 10 structures determined, several provided clues to biochemical functions that were not detectable from sequence analysis, and in many cases these putative functions could be readily confirmed by biochemical methods. This demonstrates that structural proteomics is feasible and can play a central role in functional genomics. ; save_ ################################## # Molecular system description # ################################## save_system_MTH187 _Saveframe_category molecular_system _Mol_system_name MTH187 _Abbreviation_common MTH187 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label MTH187 $MTH187 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MTH187 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common MTH187 _Abbreviation_common MTH187 _Molecular_mass 12395 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 111 _Mol_residue_sequence ; MADENKWVRRDVSTALSRMG DEAFEPLLESLSNEDWRIRG AAAWIIGNFQDERAVEPLIK LLEDDSGFVRSGAARSLEQI GGERVRAAMEKLAETGTGFA RKVAVNYLETH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 ASP 4 GLU 5 ASN 6 LYS 7 TRP 8 VAL 9 ARG 10 ARG 11 ASP 12 VAL 13 SER 14 THR 15 ALA 16 LEU 17 SER 18 ARG 19 MET 20 GLY 21 ASP 22 GLU 23 ALA 24 PHE 25 GLU 26 PRO 27 LEU 28 LEU 29 GLU 30 SER 31 LEU 32 SER 33 ASN 34 GLU 35 ASP 36 TRP 37 ARG 38 ILE 39 ARG 40 GLY 41 ALA 42 ALA 43 ALA 44 TRP 45 ILE 46 ILE 47 GLY 48 ASN 49 PHE 50 GLN 51 ASP 52 GLU 53 ARG 54 ALA 55 VAL 56 GLU 57 PRO 58 LEU 59 ILE 60 LYS 61 LEU 62 LEU 63 GLU 64 ASP 65 ASP 66 SER 67 GLY 68 PHE 69 VAL 70 ARG 71 SER 72 GLY 73 ALA 74 ALA 75 ARG 76 SER 77 LEU 78 GLU 79 GLN 80 ILE 81 GLY 82 GLY 83 GLU 84 ARG 85 VAL 86 ARG 87 ALA 88 ALA 89 MET 90 GLU 91 LYS 92 LEU 93 ALA 94 GLU 95 THR 96 GLY 97 THR 98 GLY 99 PHE 100 ALA 101 ARG 102 LYS 103 VAL 104 ALA 105 VAL 106 ASN 107 TYR 108 LEU 109 GLU 110 THR 111 HIS 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 1TE4 "Solution Structure Of Mth187. Ontario Centre For Structural Proteomics Target Mth0187_1_111; Northeast Structural Genomics Targ" 100.00 131 100.00 100.00 6.97e-73 GB AAB84693 "conserved protein [Methanothermobacter thermautotrophicus str. Delta H]" 100.00 111 100.00 100.00 1.84e-72 REF NP_275330 "hypothetical protein MTH187, partial [Methanothermobacter thermautotrophicus str. Delta H]" 100.00 111 100.00 100.00 1.84e-72 REF WP_010875826 "hypothetical protein, partial [Methanothermobacter thermautotrophicus]" 100.00 111 100.00 100.00 1.84e-72 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MTH187 'Methanobacteria thermoautotrophicum' 183925 Archaea . Methanobacteria thermoautotrophicum stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $MTH187 'recombinant technology' 'E. coli' Escherichia coli . . 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 $MTH187 0.47 mM '[U-13C; U-15N]' 'potassium phosphate' 25 mM . CHAPS 22 mM . NaCl 10 mM . DSS 0.5 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $MTH187 . mM 0.4 0.7 [U-15N] 'potassium phosphate' 25 mM . . . CHAPS 22 mM . . . NaCl 10 mM . . . DSS 0.5 mM . . . stop_ save_ ############################ # Computer software used # ############################ save_nmrview _Saveframe_category software _Name nmrview _Version 5.0.4 _Details ; NMRView: A computer program for the visualization and analysis of NMR data (1994) B. A. Johnson and R. A. Blevins, J. Biomolecular NMR 4:603-614. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N-TOCSY-HSQC_acquired_at_500MHz,_mix=100ms_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-TOCSY-HSQC acquired at 500MHz, mix=100ms' _Sample_label . save_ save_15N-NOESY-HSQC_acquired_at_800MHz,_mix=100ms_2 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-NOESY-HSQC acquired at 800MHz, mix=100ms' _Sample_label . save_ save_others_acquired_at_600MHz_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'others acquired at 600MHz' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__1_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__1_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__1_3 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__2_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__2_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__2_3 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__3_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__3_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__3_3 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__4_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__4_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__4_3 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__5_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__5_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__5_3 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__6_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__6_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__6_3 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__7_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__7_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__7_3 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__8_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__8_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__8_3 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__9_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__9_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__9_3 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__10_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__10_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__10_3 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_set_1 _Saveframe_category sample_conditions _Details ; The sample was equilibrated for 30 minutes under these conditions before the spectra were collected. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.2 0.2 na temperature 321.2 0.2 K 'ionic strength' 0.06 0.02 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio 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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '15N-TOCSY-HSQC acquired at 500MHz, mix=100ms' '15N-NOESY-HSQC acquired at 800MHz, mix=100ms' 'others acquired at 600MHz' stop_ _Sample_conditions_label $condition_set_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name MTH187 _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 MET CA C 55.776 0.1 1 2 . 1 MET HA H 4.423 0.02 1 3 . 1 MET CB C 33.124 0.1 1 4 . 1 MET HB3 H 2.058 0.02 2 5 . 1 MET HB2 H 1.953 0.02 2 6 . 1 MET CG C 32.132 0.1 1 7 . 1 MET HG3 H 2.446 0.02 2 8 . 1 MET HG2 H 2.506 0.02 2 9 . 1 MET C C 175.845 0.1 1 10 . 2 ALA N N 124.471 0.1 1 11 . 2 ALA H H 8.209 0.02 1 12 . 2 ALA CA C 52.857 0.1 1 13 . 2 ALA HA H 4.318 0.02 1 14 . 2 ALA CB C 19.399 0.1 1 15 . 2 ALA HB H 1.392 0.02 1 16 . 2 ALA C C 177.419 0.1 1 17 . 3 ASP N N 119.139 0.1 1 18 . 3 ASP H H 8.130 0.02 1 19 . 3 ASP CA C 54.654 0.1 1 20 . 3 ASP HA H 4.527 0.02 1 21 . 3 ASP CB C 41.350 0.1 1 22 . 3 ASP HB3 H 2.628 0.02 2 23 . 3 ASP HB2 H 2.700 0.02 2 24 . 3 ASP C C 176.586 0.1 1 25 . 4 GLU N N 120.858 0.1 1 26 . 4 GLU H H 8.306 0.02 1 27 . 4 GLU CA C 57.486 0.1 1 28 . 4 GLU HA H 4.141 0.02 1 29 . 4 GLU CB C 30.095 0.1 1 30 . 4 GLU HB3 H 2.045 0.02 2 31 . 4 GLU HB2 H 1.955 0.02 2 32 . 4 GLU CG C 36.249 0.1 1 33 . 4 GLU HG3 H 2.236 0.02 2 34 . 4 GLU HG2 H 2.235 0.02 2 35 . 4 GLU C C 176.574 0.1 1 36 . 5 ASN N N 118.298 0.1 1 37 . 5 ASN H H 8.280 0.02 1 38 . 5 ASN CA C 53.839 0.1 1 39 . 5 ASN HA H 4.614 0.02 1 40 . 5 ASN CB C 38.821 0.1 1 41 . 5 ASN HB3 H 2.740 0.02 2 42 . 5 ASN HB2 H 2.741 0.02 2 43 . 5 ASN ND2 N 112.635 0.1 1 44 . 5 ASN HD21 H 7.528 0.02 2 45 . 5 ASN HD22 H 6.819 0.02 2 46 . 5 ASN C C 175.501 0.1 1 47 . 6 LYS N N 120.257 0.1 1 48 . 6 LYS H H 7.900 0.02 1 49 . 6 LYS CA C 57.214 0.1 1 50 . 6 LYS HA H 4.143 0.02 1 51 . 6 LYS CB C 32.755 0.1 1 52 . 6 LYS HB3 H 1.600 0.02 2 53 . 6 LYS HB2 H 1.607 0.02 2 54 . 6 LYS CG C 24.550 0.1 1 55 . 6 LYS HG3 H 1.170 0.02 2 56 . 6 LYS HG2 H 1.180 0.02 2 57 . 6 LYS CD C 29.137 0.1 1 58 . 6 LYS HD3 H 1.561 0.02 2 59 . 6 LYS HD2 H 1.564 0.02 2 60 . 6 LYS CE C 42.313 0.1 1 61 . 6 LYS HE3 H 2.869 0.02 2 62 . 6 LYS HE2 H 2.879 0.02 2 63 . 6 LYS C C 176.454 0.1 1 64 . 7 TRP N N 119.922 0.1 1 65 . 7 TRP H H 7.883 0.02 1 66 . 7 TRP CA C 57.316 0.1 1 67 . 7 TRP HA H 4.683 0.02 1 68 . 7 TRP CB C 29.600 0.1 1 69 . 7 TRP HB3 H 3.221 0.02 2 70 . 7 TRP HB2 H 3.329 0.02 2 71 . 7 TRP NE1 N 129.151 0.1 1 72 . 7 TRP HE1 H 10.117 0.02 3 73 . 7 TRP C C 176.127 0.1 1 74 . 8 VAL N N 119.956 0.1 1 75 . 8 VAL H H 7.626 0.02 1 76 . 8 VAL CA C 62.583 0.1 1 77 . 8 VAL HA H 4.029 0.02 1 78 . 8 VAL CB C 32.810 0.1 1 79 . 8 VAL HB H 2.009 0.02 1 80 . 8 VAL CG2 C 20.919 0.1 1 81 . 8 VAL HG2 H 0.870 0.02 1 82 . 8 VAL CG1 C 21.800 0.1 1 83 . 8 VAL HG1 H 0.870 0.02 1 84 . 8 VAL C C 175.733 0.1 1 85 . 9 ARG N N 123.474 0.1 1 86 . 9 ARG H H 8.054 0.02 1 87 . 9 ARG CA C 56.403 0.1 1 88 . 9 ARG HA H 4.270 0.02 1 89 . 9 ARG CB C 30.901 0.1 1 90 . 9 ARG HB3 H 1.759 0.02 2 91 . 9 ARG HB2 H 1.882 0.02 2 92 . 9 ARG CG C 27.255 0.1 1 93 . 9 ARG HD3 H 3.200 0.02 1 94 . 9 ARG HD2 H 3.200 0.02 1 95 . 9 ARG C C 176.356 0.1 1 96 . 10 ARG N N 122.164 0.1 1 97 . 10 ARG H H 8.245 0.02 1 98 . 10 ARG CA C 56.570 0.1 1 99 . 10 ARG HA H 4.314 0.02 1 100 . 10 ARG CB C 30.949 0.1 1 101 . 10 ARG HB2 H 1.793 0.02 2 102 . 10 ARG CG C 27.165 0.1 1 103 . 10 ARG HG3 H 1.680 0.02 1 104 . 10 ARG HG2 H 1.680 0.02 1 105 . 10 ARG CD C 43.220 0.1 1 106 . 10 ARG HD3 H 3.150 0.02 1 107 . 10 ARG HD2 H 3.150 0.02 1 108 . 10 ARG C C 176.089 0.1 1 109 . 11 ASP N N 120.824 0.1 1 110 . 11 ASP H H 8.358 0.02 1 111 . 11 ASP CA C 54.739 0.1 1 112 . 11 ASP CB C 41.032 0.1 1 113 . 11 ASP HB3 H 2.688 0.02 1 114 . 11 ASP HB2 H 2.688 0.02 1 115 . 11 ASP C C 176.755 0.1 1 116 . 12 VAL N N 119.657 0.1 1 117 . 12 VAL H H 7.994 0.02 1 118 . 12 VAL CA C 63.424 0.1 1 119 . 12 VAL HA H 4.058 0.02 1 120 . 12 VAL CB C 32.435 0.1 1 121 . 12 VAL HB H 2.155 0.02 1 122 . 12 VAL CG2 C 21.148 0.1 1 123 . 12 VAL HG2 H 0.895 0.02 2 124 . 12 VAL CG1 C 20.700 0.1 1 125 . 12 VAL HG1 H 0.919 0.02 2 126 . 12 VAL C C 176.468 0.1 1 127 . 13 SER N N 117.339 0.1 1 128 . 13 SER H H 8.268 0.02 1 129 . 13 SER CA C 60.086 0.1 1 130 . 13 SER HA H 4.324 0.02 1 131 . 13 SER CB C 63.523 0.1 1 132 . 13 SER HB3 H 3.930 0.02 2 133 . 13 SER HB2 H 3.938 0.02 2 134 . 13 SER C C 175.869 0.1 1 135 . 14 THR N N 116.157 0.1 1 136 . 14 THR H H 8.058 0.02 1 137 . 14 THR CA C 63.656 0.1 1 138 . 14 THR HA H 4.227 0.02 1 139 . 14 THR CB C 69.413 0.1 1 140 . 14 THR HB H 4.272 0.02 1 141 . 14 THR CG2 C 21.835 0.1 1 142 . 14 THR HG2 H 1.228 0.02 1 143 . 14 THR C C 175.265 0.1 1 144 . 15 ALA N N 124.964 0.1 1 145 . 15 ALA H H 7.990 0.02 1 146 . 15 ALA CA C 54.042 0.1 1 147 . 15 ALA HA H 4.214 0.02 1 148 . 15 ALA CB C 18.875 0.1 1 149 . 15 ALA HB H 1.409 0.02 1 150 . 15 ALA C C 178.677 0.1 1 151 . 16 LEU N N 118.397 0.1 1 152 . 16 LEU H H 8.012 0.02 1 153 . 16 LEU CA C 56.556 0.1 1 154 . 16 LEU HA H 4.232 0.02 1 155 . 16 LEU CB C 42.070 0.1 1 156 . 16 LEU HB3 H 1.700 0.02 2 157 . 16 LEU HB2 H 1.701 0.02 2 158 . 16 LEU CG C 25.543 0.1 1 159 . 16 LEU HG H 1.551 0.02 1 160 . 16 LEU CD1 C 25.172 0.1 1 161 . 16 LEU HD1 H 0.873 0.02 2 162 . 16 LEU CD2 C 23.820 0.1 1 163 . 16 LEU HD2 H 0.875 0.02 2 164 . 16 LEU C C 178.073 0.1 1 165 . 17 SER N N 114.395 0.1 1 166 . 17 SER H H 7.957 0.02 1 167 . 17 SER CA C 59.920 0.1 1 168 . 17 SER HA H 4.284 0.02 1 169 . 17 SER CB C 63.625 0.1 1 170 . 17 SER HB3 H 3.898 0.02 2 171 . 17 SER HB2 H 3.921 0.02 2 172 . 17 SER C C 175.280 0.1 1 173 . 18 ARG N N 120.801 0.1 1 174 . 18 ARG H H 7.913 0.02 1 175 . 18 ARG CA C 56.635 0.1 1 176 . 18 ARG HA H 4.381 0.02 1 177 . 18 ARG CB C 30.658 0.1 1 178 . 18 ARG HB3 H 1.946 0.02 2 179 . 18 ARG HB2 H 1.819 0.02 2 180 . 18 ARG CG C 27.222 0.1 1 181 . 18 ARG HG3 H 1.670 0.02 1 182 . 18 ARG HG2 H 1.670 0.02 1 183 . 18 ARG CD C 43.626 0.1 1 184 . 18 ARG HD3 H 3.192 0.02 1 185 . 18 ARG HD2 H 3.192 0.02 1 186 . 18 ARG C C 176.781 0.1 1 187 . 19 MET N N 119.516 0.1 1 188 . 19 MET H H 8.011 0.02 1 189 . 19 MET CA C 56.812 0.1 1 190 . 19 MET HA H 4.405 0.02 1 191 . 19 MET CB C 33.752 0.1 1 192 . 19 MET HB3 H 2.113 0.02 2 193 . 19 MET HB2 H 2.110 0.02 2 194 . 19 MET CG C 32.646 0.1 1 195 . 19 MET HG3 H 2.562 0.02 2 196 . 19 MET HG2 H 2.674 0.02 2 197 . 19 MET CE C 20.972 0.1 1 198 . 19 MET HE H 0.940 0.02 1 199 . 19 MET C C 176.725 0.1 1 200 . 20 GLY N N 108.541 0.1 1 201 . 20 GLY H H 8.321 0.02 1 202 . 20 GLY CA C 45.958 0.1 1 203 . 20 GLY HA3 H 4.095 0.02 2 204 . 20 GLY HA2 H 4.092 0.02 2 205 . 20 GLY C C 174.742 0.1 1 206 . 21 ASP N N 121.101 0.1 1 207 . 21 ASP H H 8.380 0.02 1 208 . 21 ASP CA C 56.358 0.1 1 209 . 21 ASP HA H 4.684 0.02 1 210 . 21 ASP CB C 41.237 0.1 1 211 . 21 ASP HB3 H 2.822 0.02 2 212 . 21 ASP HB2 H 2.730 0.02 2 213 . 21 ASP C C 177.589 0.1 1 214 . 22 GLU N N 119.884 0.1 1 215 . 22 GLU H H 8.662 0.02 1 216 . 22 GLU CA C 58.274 0.1 1 217 . 22 GLU HA H 4.300 0.02 1 218 . 22 GLU CB C 29.430 0.1 1 219 . 22 GLU HB3 H 2.110 0.02 2 220 . 22 GLU HB2 H 2.108 0.02 2 221 . 22 GLU CG C 36.578 0.1 1 222 . 22 GLU HG3 H 2.345 0.02 2 223 . 22 GLU HG2 H 2.437 0.02 2 224 . 22 GLU C C 176.580 0.1 1 225 . 23 ALA N N 120.608 0.1 1 226 . 23 ALA H H 8.005 0.02 1 227 . 23 ALA CA C 52.616 0.1 1 228 . 23 ALA HA H 4.427 0.02 1 229 . 23 ALA CB C 20.170 0.1 1 230 . 23 ALA HB H 1.607 0.02 1 231 . 23 ALA C C 176.909 0.1 1 232 . 24 PHE N N 118.125 0.1 1 233 . 24 PHE H H 7.900 0.02 1 234 . 24 PHE CA C 62.556 0.1 1 235 . 24 PHE HA H 3.349 0.02 1 236 . 24 PHE CB C 39.806 0.1 1 237 . 24 PHE HB3 H 2.750 0.02 2 238 . 24 PHE HB2 H 2.549 0.02 2 239 . 24 PHE C C 175.992 0.1 1 240 . 25 GLU N N 116.972 0.1 1 241 . 25 GLU H H 8.605 0.02 1 242 . 25 GLU CA C 62.242 0.1 1 243 . 25 GLU HA H 3.808 0.02 1 244 . 25 GLU CB C 26.375 0.1 1 245 . 25 GLU HB3 H 2.182 0.02 2 246 . 25 GLU HB2 H 2.055 0.02 2 247 . 25 GLU CG C 37.435 0.1 1 248 . 25 GLU HG3 H 2.380 0.02 2 249 . 25 GLU HG2 H 2.433 0.02 2 250 . 25 GLU C C 176.638 0.1 1 251 . 26 PRO N N 104.666 0.1 1 252 . 26 PRO CA C 65.712 0.1 1 253 . 26 PRO HA H 4.324 0.02 1 254 . 26 PRO CB C 31.220 0.1 1 255 . 26 PRO HB3 H 2.284 0.02 2 256 . 26 PRO HB2 H 1.702 0.02 2 257 . 26 PRO CG C 28.078 0.1 1 258 . 26 PRO HG3 H 2.133 0.02 2 259 . 26 PRO HG2 H 1.977 0.02 2 260 . 26 PRO CD C 50.012 0.1 1 261 . 26 PRO HD3 H 3.542 0.02 2 262 . 26 PRO HD2 H 3.640 0.02 2 263 . 26 PRO C C 180.227 0.1 1 264 . 27 LEU N N 120.309 0.1 1 265 . 27 LEU H H 7.241 0.02 1 266 . 27 LEU CA C 58.244 0.1 1 267 . 27 LEU HA H 3.863 0.02 1 268 . 27 LEU CB C 42.076 0.1 1 269 . 27 LEU HB3 H 1.843 0.02 2 270 . 27 LEU HB2 H 1.067 0.02 2 271 . 27 LEU CG C 27.478 0.1 1 272 . 27 LEU HG H 1.744 0.02 1 273 . 27 LEU CD1 C 24.796 0.1 1 274 . 27 LEU HD1 H 0.896 0.02 2 275 . 27 LEU CD2 C 24.310 0.1 1 276 . 27 LEU HD2 H 0.894 0.02 2 277 . 27 LEU C C 177.504 0.1 1 278 . 28 LEU N N 120.825 0.1 1 279 . 28 LEU H H 8.016 0.02 1 280 . 28 LEU CA C 57.876 0.1 1 281 . 28 LEU HA H 3.498 0.02 1 282 . 28 LEU CB C 41.559 0.1 1 283 . 28 LEU HB3 H 0.759 0.02 2 284 . 28 LEU HB2 H 1.607 0.02 2 285 . 28 LEU CG C 26.545 0.1 1 286 . 28 LEU HG H 1.273 0.02 1 287 . 28 LEU CD1 C 25.416 0.1 1 288 . 28 LEU HD1 H 0.784 0.02 2 289 . 28 LEU CD2 C 24.306 0.1 1 290 . 28 LEU HD2 H 0.697 0.02 2 291 . 28 LEU C C 180.914 0.1 1 292 . 29 GLU N N 118.776 0.1 1 293 . 29 GLU H H 8.080 0.02 1 294 . 29 GLU CA C 58.995 0.1 1 295 . 29 GLU HA H 3.947 0.02 1 296 . 29 GLU CB C 29.528 0.1 1 297 . 29 GLU HB3 H 2.025 0.02 2 298 . 29 GLU HB2 H 2.026 0.02 2 299 . 29 GLU CG C 36.154 0.1 1 300 . 29 GLU HG3 H 2.203 0.02 2 301 . 29 GLU HG2 H 2.324 0.02 2 302 . 29 GLU C C 179.593 0.1 1 303 . 30 SER N N 115.608 0.1 1 304 . 30 SER H H 7.661 0.02 1 305 . 30 SER CA C 62.301 0.1 1 306 . 30 SER HA H 4.324 0.02 1 307 . 30 SER CB C 63.746 0.1 1 308 . 30 SER HB3 H 3.722 0.02 2 309 . 30 SER HB2 H 4.143 0.02 2 310 . 30 SER C C 174.835 0.1 1 311 . 31 LEU N N 118.715 0.1 1 312 . 31 LEU H H 7.356 0.02 1 313 . 31 LEU CA C 56.920 0.1 1 314 . 31 LEU HA H 4.135 0.02 1 315 . 31 LEU CB C 40.483 0.1 1 316 . 31 LEU HB3 H 1.949 0.02 2 317 . 31 LEU HB2 H 1.507 0.02 2 318 . 31 LEU CG C 25.671 0.1 1 319 . 31 LEU HG H 2.181 0.02 1 320 . 31 LEU CD1 C 27.315 0.1 1 321 . 31 LEU HD1 H 0.853 0.02 2 322 . 31 LEU CD2 C 21.715 0.1 1 323 . 31 LEU HD2 H 0.698 0.02 2 324 . 31 LEU C C 176.178 0.1 1 325 . 32 SER N N 108.905 0.1 1 326 . 32 SER H H 7.384 0.02 1 327 . 32 SER CA C 57.243 0.1 1 328 . 32 SER HA H 4.612 0.02 1 329 . 32 SER CB C 64.095 0.1 1 330 . 32 SER HB3 H 3.919 0.02 2 331 . 32 SER HB2 H 3.995 0.02 2 332 . 32 SER C C 174.322 0.1 1 333 . 33 ASN N N 123.005 0.1 1 334 . 33 ASN H H 7.501 0.02 1 335 . 33 ASN CA C 55.455 0.1 1 336 . 33 ASN HA H 4.346 0.02 1 337 . 33 ASN CB C 41.361 0.1 1 338 . 33 ASN HB3 H 2.535 0.02 2 339 . 33 ASN HB2 H 2.926 0.02 2 340 . 33 ASN ND2 N 114.090 0.1 1 341 . 33 ASN HD21 H 8.057 0.02 2 342 . 33 ASN HD22 H 6.959 0.02 2 343 . 33 ASN C C 175.248 0.1 1 344 . 34 GLU N N 124.677 0.1 1 345 . 34 GLU H H 8.916 0.02 1 346 . 34 GLU CA C 58.841 0.1 1 347 . 34 GLU HA H 4.055 0.02 1 348 . 34 GLU CB C 29.886 0.1 1 349 . 34 GLU HB3 H 2.085 0.02 2 350 . 34 GLU HB2 H 2.155 0.02 2 351 . 34 GLU CG C 36.314 0.1 1 352 . 34 GLU HG3 H 2.380 0.02 1 353 . 34 GLU HG2 H 2.380 0.02 1 354 . 34 GLU C C 176.577 0.1 1 355 . 35 ASP N N 122.980 0.1 1 356 . 35 ASP H H 9.222 0.02 1 357 . 35 ASP CA C 53.704 0.1 1 358 . 35 ASP HA H 4.816 0.02 1 359 . 35 ASP CB C 42.270 0.1 1 360 . 35 ASP HB3 H 2.572 0.02 2 361 . 35 ASP HB2 H 3.011 0.02 2 362 . 35 ASP C C 177.487 0.1 1 363 . 36 TRP N N 128.634 0.1 1 364 . 36 TRP H H 8.322 0.02 1 365 . 36 TRP CA C 59.831 0.1 1 366 . 36 TRP HA H 4.264 0.02 1 367 . 36 TRP CB C 28.018 0.1 1 368 . 36 TRP HB3 H 3.538 0.02 2 369 . 36 TRP HB2 H 3.655 0.02 2 370 . 36 TRP HD1 H 7.763 0.02 1 371 . 36 TRP NE1 N 130.318 0.1 1 372 . 36 TRP HE1 H 10.268 0.02 2 373 . 36 TRP C C 177.127 0.1 1 374 . 37 ARG N N 121.988 0.1 1 375 . 37 ARG H H 7.856 0.02 1 376 . 37 ARG CA C 59.683 0.1 1 377 . 37 ARG HA H 3.444 0.02 1 378 . 37 ARG CB C 29.378 0.1 1 379 . 37 ARG HB3 H 1.239 0.02 2 380 . 37 ARG HB2 H 1.380 0.02 2 381 . 37 ARG CG C 24.945 0.1 1 382 . 37 ARG HG3 H 0.047 0.02 2 383 . 37 ARG HG2 H -0.393 0.02 2 384 . 37 ARG CD C 43.058 0.1 1 385 . 37 ARG HD3 H 2.603 0.02 2 386 . 37 ARG HD2 H 2.680 0.02 2 387 . 37 ARG C C 178.013 0.1 1 388 . 38 ILE N N 117.623 0.1 1 389 . 38 ILE H H 6.703 0.02 1 390 . 38 ILE CA C 64.370 0.1 1 391 . 38 ILE HA H 3.617 0.02 1 392 . 38 ILE CB C 38.221 0.1 1 393 . 38 ILE HB H 1.887 0.02 1 394 . 38 ILE CG1 C 28.934 0.1 2 395 . 38 ILE HG13 H 1.510 0.02 1 396 . 38 ILE HG12 H 1.509 0.02 1 397 . 38 ILE CD1 C 11.829 0.1 1 398 . 38 ILE HD1 H 0.869 0.02 1 399 . 38 ILE CG2 C 17.346 0.1 1 400 . 38 ILE HG2 H 0.979 0.02 1 401 . 38 ILE C C 177.109 0.1 1 402 . 39 ARG N N 118.119 0.1 1 403 . 39 ARG H H 8.199 0.02 1 404 . 39 ARG CA C 59.596 0.1 1 405 . 39 ARG HA H 4.281 0.02 1 406 . 39 ARG CB C 31.761 0.1 1 407 . 39 ARG HB3 H 1.893 0.02 2 408 . 39 ARG HB2 H 2.100 0.02 2 409 . 39 ARG CG C 28.625 0.1 1 410 . 39 ARG HG3 H 1.798 0.02 2 411 . 39 ARG HG2 H 1.655 0.02 2 412 . 39 ARG CD C 43.871 0.1 1 413 . 39 ARG HD3 H 3.564 0.02 2 414 . 39 ARG HD2 H 3.240 0.02 2 415 . 39 ARG C C 178.720 0.1 1 416 . 40 GLY N N 104.188 0.1 1 417 . 40 GLY H H 8.620 0.02 1 418 . 40 GLY CA C 48.500 0.1 1 419 . 40 GLY HA3 H 3.780 0.02 1 420 . 40 GLY HA2 H 3.780 0.02 1 421 . 40 GLY C C 174.383 0.1 1 422 . 41 ALA N N 124.556 0.1 1 423 . 41 ALA H H 7.918 0.02 1 424 . 41 ALA CA C 56.244 0.1 1 425 . 41 ALA HA H 4.134 0.02 1 426 . 41 ALA CB C 18.462 0.1 1 427 . 41 ALA HB H 1.577 0.02 1 428 . 41 ALA C C 178.859 0.1 1 429 . 42 ALA N N 117.124 0.1 1 430 . 42 ALA H H 8.135 0.02 1 431 . 42 ALA CA C 55.533 0.1 1 432 . 42 ALA HA H 3.926 0.02 1 433 . 42 ALA CB C 18.941 0.1 1 434 . 42 ALA HB H 1.403 0.02 1 435 . 42 ALA C C 178.571 0.1 1 436 . 43 ALA N N 120.433 0.1 1 437 . 43 ALA H H 8.288 0.02 1 438 . 43 ALA CA C 55.647 0.1 1 439 . 43 ALA HA H 3.704 0.02 1 440 . 43 ALA CB C 17.820 0.1 1 441 . 43 ALA HB H 1.303 0.02 1 442 . 43 ALA C C 178.524 0.1 1 443 . 44 TRP N N 114.350 0.1 1 444 . 44 TRP H H 8.060 0.02 1 445 . 44 TRP CA C 61.433 0.1 1 446 . 44 TRP HA H 3.916 0.02 1 447 . 44 TRP CB C 30.065 0.1 1 448 . 44 TRP HB3 H 3.193 0.02 2 449 . 44 TRP HB2 H 3.326 0.02 2 450 . 44 TRP HD1 H 6.910 0.02 1 451 . 44 TRP NE1 N 129.236 0.1 1 452 . 44 TRP HE1 H 8.765 0.02 3 453 . 44 TRP C C 177.816 0.1 1 454 . 45 ILE N N 114.570 0.1 1 455 . 45 ILE H H 7.794 0.02 1 456 . 45 ILE CA C 63.736 0.1 1 457 . 45 ILE HA H 4.046 0.02 1 458 . 45 ILE CB C 39.820 0.1 1 459 . 45 ILE HB H 1.890 0.02 1 460 . 45 ILE CG1 C 29.247 0.1 2 461 . 45 ILE HG13 H 1.952 0.02 1 462 . 45 ILE HG12 H 1.229 0.02 1 463 . 45 ILE CD1 C 14.258 0.1 1 464 . 45 ILE HD1 H 0.878 0.02 1 465 . 45 ILE CG2 C 19.095 0.1 1 466 . 45 ILE HG2 H 1.055 0.02 1 467 . 45 ILE C C 179.210 0.1 1 468 . 46 ILE N N 119.132 0.1 1 469 . 46 ILE H H 8.490 0.02 1 470 . 46 ILE CA C 65.955 0.1 1 471 . 46 ILE HA H 4.226 0.02 1 472 . 46 ILE CB C 38.609 0.1 1 473 . 46 ILE HB H 2.118 0.02 1 474 . 46 ILE CG1 C 31.003 0.1 2 475 . 46 ILE HG13 H 1.529 0.02 1 476 . 46 ILE HG12 H 1.573 0.02 1 477 . 46 ILE CD1 C 14.761 0.1 1 478 . 46 ILE HD1 H 0.474 0.02 1 479 . 46 ILE CG2 C 18.097 0.1 1 480 . 46 ILE HG2 H 1.038 0.02 1 481 . 46 ILE C C 177.556 0.1 1 482 . 47 GLY N N 110.660 0.1 1 483 . 47 GLY H H 8.444 0.02 1 484 . 47 GLY CA C 47.288 0.1 1 485 . 47 GLY HA3 H 3.848 0.02 2 486 . 47 GLY HA2 H 3.997 0.02 2 487 . 47 GLY C C 174.417 0.1 1 488 . 48 ASN N N 116.622 0.1 1 489 . 48 ASN H H 8.065 0.02 1 490 . 48 ASN CA C 55.675 0.1 1 491 . 48 ASN HA H 4.415 0.02 1 492 . 48 ASN CB C 39.068 0.1 1 493 . 48 ASN HB3 H 2.610 0.02 2 494 . 48 ASN HB2 H 2.609 0.02 2 495 . 48 ASN ND2 N 113.156 0.1 1 496 . 48 ASN HD21 H 7.627 0.02 2 497 . 48 ASN HD22 H 7.117 0.02 2 498 . 48 ASN C C 175.992 0.1 1 499 . 49 PHE N N 115.037 0.1 1 500 . 49 PHE H H 7.659 0.02 1 501 . 49 PHE CA C 59.938 0.1 1 502 . 49 PHE HA H 4.224 0.02 1 503 . 49 PHE CB C 39.247 0.1 1 504 . 49 PHE HB3 H 3.270 0.02 2 505 . 49 PHE HB2 H 3.284 0.02 2 506 . 49 PHE C C 175.167 0.1 1 507 . 50 GLN N N 113.502 0.1 1 508 . 50 GLN H H 8.088 0.02 1 509 . 50 GLN CA C 57.507 0.1 1 510 . 50 GLN HA H 3.617 0.02 1 511 . 50 GLN CB C 27.320 0.1 1 512 . 50 GLN HB3 H 2.363 0.02 2 513 . 50 GLN HB2 H 2.184 0.02 2 514 . 50 GLN CG C 34.939 0.1 1 515 . 50 GLN HG3 H 2.327 0.02 2 516 . 50 GLN HG2 H 2.321 0.02 2 517 . 50 GLN NE2 N 111.421 0.1 1 518 . 50 GLN HE21 H 7.482 0.02 2 519 . 50 GLN HE22 H 6.795 0.02 2 520 . 50 GLN C C 172.751 0.1 1 521 . 51 ASP N N 119.167 0.1 1 522 . 51 ASP H H 8.306 0.02 1 523 . 51 ASP CA C 53.124 0.1 1 524 . 51 ASP HA H 4.814 0.02 1 525 . 51 ASP CB C 44.501 0.1 1 526 . 51 ASP HB3 H 1.835 0.02 2 527 . 51 ASP HB2 H 2.689 0.02 2 528 . 51 ASP C C 177.763 0.1 1 529 . 52 GLU N N 125.785 0.1 1 530 . 52 GLU H H 9.091 0.02 1 531 . 52 GLU CA C 58.639 0.1 1 532 . 52 GLU HA H 4.029 0.02 1 533 . 52 GLU CB C 29.658 0.1 1 534 . 52 GLU HB3 H 2.130 0.02 1 535 . 52 GLU HB2 H 2.130 0.02 1 536 . 52 GLU CG C 36.834 0.1 1 537 . 52 GLU HG3 H 2.396 0.02 2 538 . 52 GLU HG2 H 2.240 0.02 2 539 . 52 GLU C C 178.109 0.1 1 540 . 53 ARG N N 122.531 0.1 1 541 . 53 ARG H H 9.549 0.02 1 542 . 53 ARG CA C 59.466 0.1 1 543 . 53 ARG HA H 4.168 0.02 1 544 . 53 ARG CB C 30.997 0.1 1 545 . 53 ARG HB3 H 1.975 0.02 1 546 . 53 ARG HB2 H 1.975 0.02 1 547 . 53 ARG CG C 27.511 0.1 1 548 . 53 ARG HG3 H 1.920 0.02 1 549 . 53 ARG HG2 H 1.920 0.02 1 550 . 53 ARG CD C 43.815 0.1 1 551 . 53 ARG HD3 H 3.190 0.02 1 552 . 53 ARG HD2 H 3.190 0.02 1 553 . 53 ARG HE H 6.790 0.02 1 554 . 53 ARG C C 177.470 0.1 1 555 . 54 ALA N N 114.993 0.1 1 556 . 54 ALA H H 7.767 0.02 1 557 . 54 ALA CA C 52.107 0.1 1 558 . 54 ALA HA H 4.213 0.02 1 559 . 54 ALA CB C 19.945 0.1 1 560 . 54 ALA HB H 1.447 0.02 1 561 . 54 ALA C C 176.546 0.1 1 562 . 55 VAL N N 117.083 0.1 1 563 . 55 VAL H H 7.545 0.02 1 564 . 55 VAL CA C 68.699 0.1 1 565 . 55 VAL HA H 3.261 0.02 1 566 . 55 VAL CB C 31.371 0.1 1 567 . 55 VAL HB H 2.149 0.02 1 568 . 55 VAL CG2 C 20.644 0.1 1 569 . 55 VAL HG2 H 0.695 0.02 2 570 . 55 VAL CG1 C 25.351 0.1 1 571 . 55 VAL HG1 H 1.044 0.02 2 572 . 55 VAL C C 175.840 0.1 1 573 . 56 GLU N N 117.032 0.1 1 574 . 56 GLU H H 8.713 0.02 1 575 . 56 GLU CA C 62.191 0.1 1 576 . 56 GLU HA H 4.045 0.02 1 577 . 56 GLU CB C 26.649 0.1 1 578 . 56 GLU HB3 H 2.081 0.02 2 579 . 56 GLU HB2 H 2.080 0.02 2 580 . 56 GLU CG C 36.851 0.1 1 581 . 56 GLU HG3 H 2.226 0.02 2 582 . 56 GLU HG2 H 2.301 0.02 2 583 . 56 GLU C C 177.068 0.1 1 584 . 57 PRO N N 104.392 0.1 1 585 . 57 PRO CA C 65.733 0.1 1 586 . 57 PRO HA H 4.246 0.02 1 587 . 57 PRO CB C 31.265 0.1 1 588 . 57 PRO HB3 H 2.239 0.02 2 589 . 57 PRO HB2 H 1.661 0.02 2 590 . 57 PRO CG C 27.840 0.1 1 591 . 57 PRO HG3 H 1.970 0.02 1 592 . 57 PRO HG2 H 1.970 0.02 1 593 . 57 PRO C C 179.260 0.1 1 594 . 58 LEU N N 116.630 0.1 1 595 . 58 LEU H H 7.519 0.02 1 596 . 58 LEU CA C 58.219 0.1 1 597 . 58 LEU HA H 4.012 0.02 1 598 . 58 LEU CB C 41.936 0.1 1 599 . 58 LEU HB3 H 2.137 0.02 2 600 . 58 LEU HB2 H 1.129 0.02 2 601 . 58 LEU CG C 26.268 0.1 1 602 . 58 LEU HG H 2.006 0.02 1 603 . 58 LEU CD1 C 22.729 0.1 1 604 . 58 LEU HD1 H 0.932 0.02 2 605 . 58 LEU CD2 C 27.239 0.1 1 606 . 58 LEU HD2 H 0.621 0.02 2 607 . 58 LEU C C 178.747 0.1 1 608 . 59 ILE N N 118.799 0.1 1 609 . 59 ILE H H 8.290 0.02 1 610 . 59 ILE CA C 63.733 0.1 1 611 . 59 ILE HA H 3.568 0.02 1 612 . 59 ILE CB C 36.515 0.1 1 613 . 59 ILE HB H 2.147 0.02 1 614 . 59 ILE CG1 C 28.225 0.1 2 615 . 59 ILE HG13 H 1.536 0.02 1 616 . 59 ILE HG12 H 1.261 0.02 1 617 . 59 ILE CD1 C 12.950 0.1 1 618 . 59 ILE HD1 H 0.622 0.02 1 619 . 59 ILE CG2 C 17.422 0.1 1 620 . 59 ILE HG2 H 0.851 0.02 1 621 . 59 ILE C C 180.037 0.1 1 622 . 60 LYS N N 118.820 0.1 1 623 . 60 LYS H H 7.259 0.02 1 624 . 60 LYS CA C 59.066 0.1 1 625 . 60 LYS HA H 4.094 0.02 1 626 . 60 LYS CB C 31.968 0.1 1 627 . 60 LYS HB3 H 1.930 0.02 2 628 . 60 LYS HB2 H 1.931 0.02 2 629 . 60 LYS CG C 25.066 0.1 1 630 . 60 LYS HG3 H 1.584 0.02 2 631 . 60 LYS HG2 H 1.478 0.02 2 632 . 60 LYS CD C 28.941 0.1 1 633 . 60 LYS HD3 H 1.685 0.02 2 634 . 60 LYS HD2 H 1.680 0.02 2 635 . 60 LYS CE C 42.330 0.1 1 636 . 60 LYS HE3 H 2.957 0.02 2 637 . 60 LYS HE2 H 2.958 0.02 2 638 . 60 LYS C C 179.579 0.1 1 639 . 61 LEU N N 118.257 0.1 1 640 . 61 LEU H H 7.492 0.02 1 641 . 61 LEU CA C 56.494 0.1 1 642 . 61 LEU HA H 4.168 0.02 1 643 . 61 LEU CB C 41.199 0.1 1 644 . 61 LEU HB3 H 1.997 0.02 2 645 . 61 LEU HB2 H 1.520 0.02 2 646 . 61 LEU CG C 26.935 0.1 1 647 . 61 LEU HG H 0.970 0.02 1 648 . 61 LEU CD1 C 22.938 0.1 1 649 . 61 LEU HD1 H 1.016 0.02 2 650 . 61 LEU CD2 C 22.500 0.1 1 651 . 61 LEU HD2 H 1.024 0.02 2 652 . 61 LEU C C 178.146 0.1 1 653 . 62 LEU N N 118.214 0.1 1 654 . 62 LEU H H 7.548 0.02 1 655 . 62 LEU CA C 57.410 0.1 1 656 . 62 LEU HA H 4.208 0.02 1 657 . 62 LEU CB C 41.825 0.1 1 658 . 62 LEU HB3 H 2.150 0.02 2 659 . 62 LEU HB2 H 2.151 0.02 2 660 . 62 LEU HG H 1.462 0.02 1 661 . 62 LEU CD1 C 23.026 0.1 1 662 . 62 LEU HD1 H 0.900 0.02 2 663 . 62 LEU CD2 C 26.202 0.1 1 664 . 62 LEU HD2 H 0.820 0.02 2 665 . 62 LEU C C 176.768 0.1 1 666 . 63 GLU N N 112.580 0.1 1 667 . 63 GLU H H 7.257 0.02 1 668 . 63 GLU CA C 54.945 0.1 1 669 . 63 GLU HA H 4.512 0.02 1 670 . 63 GLU CB C 30.129 0.1 1 671 . 63 GLU HB3 H 1.924 0.02 2 672 . 63 GLU HB2 H 2.399 0.02 2 673 . 63 GLU CG C 36.662 0.1 1 674 . 63 GLU HG3 H 2.265 0.02 2 675 . 63 GLU HG2 H 2.271 0.02 2 676 . 63 GLU C C 176.196 0.1 1 677 . 64 ASP N N 122.241 0.1 1 678 . 64 ASP H H 7.325 0.02 1 679 . 64 ASP CA C 55.619 0.1 1 680 . 64 ASP HA H 4.238 0.02 1 681 . 64 ASP CB C 44.384 0.1 1 682 . 64 ASP HB3 H 2.945 0.02 2 683 . 64 ASP HB2 H 2.654 0.02 2 684 . 64 ASP C C 175.721 0.1 1 685 . 65 ASP N N 123.636 0.1 1 686 . 65 ASP H H 8.340 0.02 1 687 . 65 ASP CA C 56.509 0.1 1 688 . 65 ASP HA H 4.364 0.02 1 689 . 65 ASP CB C 41.572 0.1 1 690 . 65 ASP HB3 H 2.615 0.02 2 691 . 65 ASP HB2 H 2.614 0.02 2 692 . 65 ASP C C 177.074 0.1 1 693 . 66 SER N N 115.390 0.1 1 694 . 66 SER H H 9.679 0.02 1 695 . 66 SER CA C 56.826 0.1 1 696 . 66 SER HA H 4.440 0.02 1 697 . 66 SER CB C 62.980 0.1 1 698 . 66 SER HB3 H 3.719 0.02 2 699 . 66 SER HB2 H 4.087 0.02 2 700 . 66 SER C C 176.840 0.1 1 701 . 67 GLY CA C 47.400 0.1 1 702 . 67 GLY HA3 H 3.570 0.02 2 703 . 67 GLY HA2 H 3.930 0.02 2 704 . 67 GLY C C 176.070 0.1 1 705 . 68 PHE N N 122.900 0.1 1 706 . 68 PHE H H 8.130 0.02 1 707 . 68 PHE CA C 61.055 0.1 1 708 . 68 PHE HA H 4.625 0.02 1 709 . 68 PHE CB C 40.281 0.1 1 710 . 68 PHE HB3 H 3.523 0.02 2 711 . 68 PHE HB2 H 3.030 0.02 2 712 . 68 PHE C C 176.783 0.1 1 713 . 69 VAL N N 118.134 0.1 1 714 . 69 VAL H H 7.222 0.02 1 715 . 69 VAL CA C 66.188 0.1 1 716 . 69 VAL HA H 3.435 0.02 1 717 . 69 VAL CB C 32.305 0.1 1 718 . 69 VAL HB H 2.349 0.02 1 719 . 69 VAL CG2 C 23.823 0.1 1 720 . 69 VAL HG2 H 1.046 0.02 2 721 . 69 VAL CG1 C 22.681 0.1 1 722 . 69 VAL HG1 H 1.403 0.02 2 723 . 69 VAL C C 177.341 0.1 1 724 . 70 ARG N N 116.594 0.1 1 725 . 70 ARG H H 8.126 0.02 1 726 . 70 ARG CA C 59.951 0.1 1 727 . 70 ARG HA H 4.045 0.02 1 728 . 70 ARG CB C 30.703 0.1 1 729 . 70 ARG HB3 H 1.650 0.02 2 730 . 70 ARG HB2 H 1.789 0.02 2 731 . 70 ARG CG C 27.076 0.1 1 732 . 70 ARG HG3 H 1.703 0.02 2 733 . 70 ARG HG2 H 1.406 0.02 2 734 . 70 ARG CD C 43.936 0.1 1 735 . 70 ARG HD3 H 2.560 0.02 2 736 . 70 ARG HD2 H 2.563 0.02 2 737 . 70 ARG C C 178.511 0.1 1 738 . 71 SER N N 113.249 0.1 1 739 . 71 SER H H 7.924 0.02 1 740 . 71 SER CA C 62.379 0.1 1 741 . 71 SER HA H 4.074 0.02 1 742 . 71 SER CB C 63.191 0.1 1 743 . 71 SER HB3 H 4.027 0.02 1 744 . 71 SER HB2 H 4.027 0.02 1 745 . 71 SER C C 175.895 0.1 1 746 . 72 GLY N N 111.973 0.1 1 747 . 72 GLY H H 7.033 0.02 1 748 . 72 GLY CA C 44.297 0.1 1 749 . 72 GLY HA3 H 1.498 0.02 2 750 . 72 GLY HA2 H 1.963 0.02 2 751 . 72 GLY C C 174.044 0.1 1 752 . 73 ALA N N 122.869 0.1 1 753 . 73 ALA H H 8.069 0.02 1 754 . 73 ALA CA C 55.131 0.1 1 755 . 73 ALA HA H 3.900 0.02 1 756 . 73 ALA CB C 18.205 0.1 1 757 . 73 ALA HB H 1.371 0.02 1 758 . 73 ALA C C 178.814 0.1 1 759 . 74 ALA N N 118.240 0.1 1 760 . 74 ALA H H 7.807 0.02 1 761 . 74 ALA CA C 55.718 0.1 1 762 . 74 ALA HA H 3.777 0.02 1 763 . 74 ALA CB C 18.535 0.1 1 764 . 74 ALA HB H 1.484 0.02 1 765 . 74 ALA C C 179.299 0.1 1 766 . 75 ARG N N 118.288 0.1 1 767 . 75 ARG H H 7.514 0.02 1 768 . 75 ARG CA C 58.996 0.1 1 769 . 75 ARG HA H 4.011 0.02 1 770 . 75 ARG CB C 29.137 0.1 1 771 . 75 ARG HB3 H 1.626 0.02 2 772 . 75 ARG HB2 H 1.629 0.02 2 773 . 75 ARG CG C 26.733 0.1 1 774 . 75 ARG HG3 H 1.827 0.02 2 775 . 75 ARG HG2 H 1.720 0.02 2 776 . 75 ARG CD C 43.531 0.1 1 777 . 75 ARG HD3 H 3.283 0.02 2 778 . 75 ARG HD2 H 3.077 0.02 2 779 . 75 ARG HH11 H 6.570 0.02 1 780 . 75 ARG C C 179.769 0.1 1 781 . 76 SER N N 118.062 0.1 1 782 . 76 SER H H 8.645 0.02 1 783 . 76 SER CA C 63.509 0.1 1 784 . 76 SER HA H 4.292 0.02 1 785 . 76 SER CB C 63.502 0.1 1 786 . 76 SER HB3 H 3.350 0.02 2 787 . 76 SER HB2 H 3.346 0.02 2 788 . 76 SER C C 176.300 0.1 1 789 . 77 LEU N N 122.775 0.1 1 790 . 77 LEU H H 8.333 0.02 1 791 . 77 LEU CA C 58.939 0.1 1 792 . 77 LEU HA H 3.834 0.02 1 793 . 77 LEU CB C 41.857 0.1 1 794 . 77 LEU HB3 H 0.965 0.02 2 795 . 77 LEU HB2 H 1.866 0.02 2 796 . 77 LEU CG C 27.476 0.1 1 797 . 77 LEU HG H 1.695 0.02 1 798 . 77 LEU CD1 C 26.166 0.1 1 799 . 77 LEU HD1 H 0.591 0.02 2 800 . 77 LEU CD2 C 25.136 0.1 1 801 . 77 LEU HD2 H 0.861 0.02 2 802 . 77 LEU C C 178.070 0.1 1 803 . 78 GLU N N 117.352 0.1 1 804 . 78 GLU H H 7.427 0.02 1 805 . 78 GLU CA C 59.581 0.1 1 806 . 78 GLU HA H 3.962 0.02 1 807 . 78 GLU CB C 29.221 0.1 1 808 . 78 GLU HB3 H 2.317 0.02 2 809 . 78 GLU HB2 H 2.264 0.02 2 810 . 78 GLU CG C 36.522 0.1 1 811 . 78 GLU HG3 H 2.472 0.02 2 812 . 78 GLU HG2 H 2.470 0.02 2 813 . 78 GLU C C 178.079 0.1 1 814 . 79 GLN N N 117.851 0.1 1 815 . 79 GLN H H 7.787 0.02 1 816 . 79 GLN CA C 58.187 0.1 1 817 . 79 GLN HA H 4.014 0.02 1 818 . 79 GLN CB C 29.410 0.1 1 819 . 79 GLN HB3 H 2.052 0.02 2 820 . 79 GLN HB2 H 2.178 0.02 2 821 . 79 GLN CG C 33.823 0.1 1 822 . 79 GLN HG3 H 2.332 0.02 2 823 . 79 GLN HG2 H 2.386 0.02 2 824 . 79 GLN NE2 N 109.998 0.1 1 825 . 79 GLN HE21 H 7.312 0.02 2 826 . 79 GLN HE22 H 6.565 0.02 2 827 . 79 GLN C C 177.843 0.1 1 828 . 80 ILE N N 119.280 0.1 1 829 . 80 ILE H H 7.875 0.02 1 830 . 80 ILE CA C 65.778 0.1 1 831 . 80 ILE HA H 3.525 0.02 1 832 . 80 ILE CB C 39.874 0.1 1 833 . 80 ILE HB H 1.702 0.02 1 834 . 80 ILE CG1 C 29.757 0.1 2 835 . 80 ILE HG13 H 2.180 0.02 1 836 . 80 ILE HG12 H 2.180 0.02 1 837 . 80 ILE CD1 C 15.536 0.1 1 838 . 80 ILE HD1 H 0.713 0.02 1 839 . 80 ILE CG2 C 16.698 0.1 1 840 . 80 ILE HG2 H 0.833 0.02 1 841 . 80 ILE C C 177.155 0.1 1 842 . 81 GLY N N 104.195 0.1 1 843 . 81 GLY H H 7.857 0.02 1 844 . 81 GLY CA C 45.496 0.1 1 845 . 81 GLY HA3 H 3.806 0.02 2 846 . 81 GLY HA2 H 4.019 0.02 2 847 . 81 GLY C C 172.964 0.1 1 848 . 82 GLY N N 104.719 0.1 1 849 . 82 GLY H H 8.027 0.02 1 850 . 82 GLY CA C 45.039 0.1 1 851 . 82 GLY HA3 H 3.988 0.02 2 852 . 82 GLY HA2 H 4.473 0.02 2 853 . 82 GLY C C 176.157 0.1 1 854 . 83 GLU N N 119.107 0.1 1 855 . 83 GLU H H 8.810 0.02 1 856 . 83 GLU CA C 59.285 0.1 1 857 . 83 GLU HA H 4.093 0.02 1 858 . 83 GLU CB C 29.947 0.1 1 859 . 83 GLU HB3 H 2.087 0.02 2 860 . 83 GLU HB2 H 2.089 0.02 2 861 . 83 GLU CG C 36.237 0.1 1 862 . 83 GLU HG3 H 2.380 0.02 1 863 . 83 GLU HG2 H 2.380 0.02 1 864 . 83 GLU C C 179.137 0.1 1 865 . 84 ARG N N 121.215 0.1 1 866 . 84 ARG H H 8.819 0.02 1 867 . 84 ARG CA C 59.081 0.1 1 868 . 84 ARG HA H 4.165 0.02 1 869 . 84 ARG CB C 29.371 0.1 1 870 . 84 ARG HB3 H 1.849 0.02 2 871 . 84 ARG HB2 H 2.051 0.02 2 872 . 84 ARG CG C 27.907 0.1 1 873 . 84 ARG HG3 H 1.754 0.02 2 874 . 84 ARG HG2 H 1.650 0.02 2 875 . 84 ARG CD C 43.134 0.1 1 876 . 84 ARG HD3 H 3.229 0.02 2 877 . 84 ARG HD2 H 3.218 0.02 2 878 . 84 ARG HE H 6.280 0.02 1 879 . 84 ARG C C 179.943 0.1 1 880 . 85 VAL N N 119.126 0.1 1 881 . 85 VAL H H 7.368 0.02 1 882 . 85 VAL CA C 67.302 0.1 1 883 . 85 VAL HA H 3.298 0.02 1 884 . 85 VAL CB C 32.159 0.1 1 885 . 85 VAL HB H 1.654 0.02 1 886 . 85 VAL CG2 C 21.888 0.1 1 887 . 85 VAL HG2 H 0.306 0.02 2 888 . 85 VAL CG1 C 25.374 0.1 1 889 . 85 VAL HG1 H 0.982 0.02 2 890 . 85 VAL C C 177.136 0.1 1 891 . 86 ARG N N 119.381 0.1 1 892 . 86 ARG H H 7.793 0.02 1 893 . 86 ARG CA C 61.235 0.1 1 894 . 86 ARG HA H 3.563 0.02 1 895 . 86 ARG CB C 29.318 0.1 1 896 . 86 ARG HB3 H 2.128 0.02 2 897 . 86 ARG HB2 H 1.871 0.02 2 898 . 86 ARG CG C 28.085 0.1 1 899 . 86 ARG HG3 H 1.576 0.02 2 900 . 86 ARG HG2 H 1.751 0.02 2 901 . 86 ARG CD C 42.995 0.1 1 902 . 86 ARG HD3 H 3.270 0.02 2 903 . 86 ARG HD2 H 3.276 0.02 2 904 . 86 ARG HE H 7.620 0.02 1 905 . 86 ARG C C 177.761 0.1 1 906 . 87 ALA N N 118.779 0.1 1 907 . 87 ALA H H 8.044 0.02 1 908 . 87 ALA CA C 55.051 0.1 1 909 . 87 ALA HA H 4.144 0.02 1 910 . 87 ALA CB C 18.225 0.1 1 911 . 87 ALA HB H 1.484 0.02 1 912 . 87 ALA C C 180.738 0.1 1 913 . 88 ALA N N 120.572 0.1 1 914 . 88 ALA H H 7.611 0.02 1 915 . 88 ALA CA C 54.881 0.1 1 916 . 88 ALA HA H 4.114 0.02 1 917 . 88 ALA CB C 18.271 0.1 1 918 . 88 ALA HB H 1.393 0.02 1 919 . 88 ALA C C 180.645 0.1 1 920 . 89 MET N N 117.325 0.1 1 921 . 89 MET H H 8.471 0.02 1 922 . 89 MET CA C 57.088 0.1 1 923 . 89 MET HA H 4.197 0.02 1 924 . 89 MET CB C 31.355 0.1 1 925 . 89 MET HB3 H 2.060 0.02 2 926 . 89 MET HB2 H 2.285 0.02 2 927 . 89 MET CG C 32.902 0.1 1 928 . 89 MET HG3 H 2.550 0.02 1 929 . 89 MET HG2 H 2.550 0.02 1 930 . 89 MET C C 178.298 0.1 1 931 . 90 GLU N N 120.174 0.1 1 932 . 90 GLU H H 8.566 0.02 1 933 . 90 GLU CA C 60.206 0.1 1 934 . 90 GLU HA H 3.922 0.02 1 935 . 90 GLU CB C 29.637 0.1 1 936 . 90 GLU HB3 H 2.050 0.02 2 937 . 90 GLU HB2 H 2.218 0.02 2 938 . 90 GLU CG C 37.214 0.1 1 939 . 90 GLU HG3 H 2.550 0.02 1 940 . 90 GLU HG2 H 2.550 0.02 1 941 . 90 GLU C C 179.225 0.1 1 942 . 91 LYS N N 117.813 0.1 1 943 . 91 LYS H H 7.260 0.02 1 944 . 91 LYS CA C 58.876 0.1 1 945 . 91 LYS HA H 4.223 0.02 1 946 . 91 LYS CB C 31.980 0.1 1 947 . 91 LYS HB3 H 1.930 0.02 2 948 . 91 LYS HB2 H 1.943 0.02 2 949 . 91 LYS CG C 24.816 0.1 1 950 . 91 LYS HG3 H 1.446 0.02 2 951 . 91 LYS HG2 H 1.532 0.02 2 952 . 91 LYS CD C 28.756 0.1 1 953 . 91 LYS HD3 H 1.699 0.02 1 954 . 91 LYS HD2 H 1.699 0.02 1 955 . 91 LYS CE C 42.436 0.1 1 956 . 91 LYS HE3 H 2.976 0.02 2 957 . 91 LYS HE2 H 2.970 0.02 2 958 . 91 LYS C C 179.804 0.1 1 959 . 92 LEU N N 122.334 0.1 1 960 . 92 LEU H H 8.070 0.02 1 961 . 92 LEU CA C 57.399 0.1 1 962 . 92 LEU HA H 3.967 0.02 1 963 . 92 LEU CB C 43.464 0.1 1 964 . 92 LEU HB3 H 1.249 0.02 2 965 . 92 LEU HB2 H 1.767 0.02 2 966 . 92 LEU CG C 27.401 0.1 1 967 . 92 LEU HG H 1.610 0.02 1 968 . 92 LEU CD1 C 24.283 0.1 1 969 . 92 LEU HD1 H 0.829 0.02 2 970 . 92 LEU CD2 C 24.973 0.1 1 971 . 92 LEU HD2 H 0.836 0.02 2 972 . 92 LEU C C 179.013 0.1 1 973 . 93 ALA N N 120.383 0.1 1 974 . 93 ALA H H 8.423 0.02 1 975 . 93 ALA CA C 54.860 0.1 1 976 . 93 ALA HA H 3.962 0.02 1 977 . 93 ALA CB C 18.448 0.1 1 978 . 93 ALA HB H 1.371 0.02 1 979 . 93 ALA C C 178.020 0.1 1 980 . 94 GLU N N 114.261 0.1 1 981 . 94 GLU H H 7.300 0.02 1 982 . 94 GLU CA C 58.086 0.1 1 983 . 94 GLU HA H 4.358 0.02 1 984 . 94 GLU CB C 31.292 0.1 1 985 . 94 GLU HB3 H 2.200 0.02 2 986 . 94 GLU HB2 H 2.189 0.02 2 987 . 94 GLU CG C 36.161 0.1 1 988 . 94 GLU HG3 H 2.251 0.02 2 989 . 94 GLU HG2 H 2.430 0.02 2 990 . 94 GLU C C 178.529 0.1 1 991 . 95 THR N N 106.487 0.1 1 992 . 95 THR H H 8.077 0.02 1 993 . 95 THR CA C 61.889 0.1 1 994 . 95 THR HA H 4.613 0.02 1 995 . 95 THR CB C 71.092 0.1 1 996 . 95 THR HB H 4.390 0.02 1 997 . 95 THR CG2 C 21.812 0.1 1 998 . 95 THR HG2 H 1.215 0.02 1 999 . 95 THR C C 175.615 0.1 1 1000 . 96 GLY N N 111.590 0.1 1 1001 . 96 GLY H H 8.387 0.02 1 1002 . 96 GLY CA C 44.885 0.1 1 1003 . 96 GLY HA3 H 3.697 0.02 2 1004 . 96 GLY HA2 H 4.383 0.02 2 1005 . 96 GLY C C 172.647 0.1 1 1006 . 97 THR N N 109.639 0.1 1 1007 . 97 THR H H 8.306 0.02 1 1008 . 97 THR CA C 60.477 0.1 1 1009 . 97 THR HA H 4.654 0.02 1 1010 . 97 THR CB C 71.819 0.1 1 1011 . 97 THR HB H 4.244 0.02 1 1012 . 97 THR CG2 C 21.316 0.1 1 1013 . 97 THR HG2 H 1.207 0.02 1 1014 . 97 THR C C 175.108 0.1 1 1015 . 98 GLY N N 108.542 0.1 1 1016 . 98 GLY H H 8.481 0.02 1 1017 . 98 GLY CA C 46.653 0.1 1 1018 . 98 GLY HA3 H 4.567 0.02 1 1019 . 98 GLY HA2 H 4.567 0.02 1 1020 . 98 GLY C C 175.352 0.1 1 1021 . 99 PHE N N 126.862 0.1 1 1022 . 99 PHE H H 8.915 0.02 1 1023 . 99 PHE CA C 61.662 0.1 1 1024 . 99 PHE HA H 4.169 0.02 1 1025 . 99 PHE CB C 39.348 0.1 1 1026 . 99 PHE HB3 H 3.300 0.02 2 1027 . 99 PHE HB2 H 3.165 0.02 2 1028 . 99 PHE C C 176.274 0.1 1 1029 . 100 ALA N N 119.980 0.1 1 1030 . 100 ALA H H 8.581 0.02 1 1031 . 100 ALA CA C 55.619 0.1 1 1032 . 100 ALA HA H 3.781 0.02 1 1033 . 100 ALA CB C 19.246 0.1 1 1034 . 100 ALA HB H 1.511 0.02 1 1035 . 100 ALA C C 178.285 0.1 1 1036 . 101 ARG N N 114.769 0.1 1 1037 . 101 ARG H H 6.848 0.02 1 1038 . 101 ARG CA C 59.275 0.1 1 1039 . 101 ARG HA H 3.677 0.02 1 1040 . 101 ARG CB C 29.899 0.1 1 1041 . 101 ARG HB3 H 1.235 0.02 2 1042 . 101 ARG HB2 H 1.599 0.02 2 1043 . 101 ARG CG C 27.787 0.1 1 1044 . 101 ARG HG3 H 1.554 0.02 2 1045 . 101 ARG HG2 H 1.679 0.02 2 1046 . 101 ARG CD C 43.190 0.1 1 1047 . 101 ARG HD3 H 3.166 0.02 2 1048 . 101 ARG HD2 H 3.102 0.02 2 1049 . 101 ARG C C 177.194 0.1 1 1050 . 102 LYS N N 118.290 0.1 1 1051 . 102 LYS H H 7.484 0.02 1 1052 . 102 LYS CA C 59.628 0.1 1 1053 . 102 LYS HA H 3.858 0.02 1 1054 . 102 LYS CB C 32.316 0.1 1 1055 . 102 LYS HB3 H 1.822 0.02 2 1056 . 102 LYS HB2 H 1.819 0.02 2 1057 . 102 LYS CG C 24.979 0.1 1 1058 . 102 LYS HG3 H 1.353 0.02 2 1059 . 102 LYS HG2 H 1.510 0.02 2 1060 . 102 LYS CD C 29.314 0.1 1 1061 . 102 LYS HD3 H 1.666 0.02 2 1062 . 102 LYS HD2 H 1.688 0.02 2 1063 . 102 LYS CE C 42.321 0.1 1 1064 . 102 LYS HE3 H 2.968 0.02 2 1065 . 102 LYS HE2 H 2.991 0.02 2 1066 . 102 LYS C C 179.505 0.1 1 1067 . 103 VAL N N 119.101 0.1 1 1068 . 103 VAL H H 8.106 0.02 1 1069 . 103 VAL CA C 65.942 0.1 1 1070 . 103 VAL HA H 3.423 0.02 1 1071 . 103 VAL CB C 31.723 0.1 1 1072 . 103 VAL HB H 1.901 0.02 1 1073 . 103 VAL CG2 C 23.380 0.1 1 1074 . 103 VAL HG2 H 0.443 0.02 2 1075 . 103 VAL CG1 C 20.791 0.1 1 1076 . 103 VAL HG1 H 0.747 0.02 2 1077 . 103 VAL C C 178.067 0.1 1 1078 . 104 ALA N N 124.074 0.1 1 1079 . 104 ALA H H 7.740 0.02 1 1080 . 104 ALA CA C 55.641 0.1 1 1081 . 104 ALA HA H 4.451 0.02 1 1082 . 104 ALA CB C 20.032 0.1 1 1083 . 104 ALA HB H 1.595 0.02 1 1084 . 104 ALA C C 179.323 0.1 1 1085 . 105 VAL N N 117.214 0.1 1 1086 . 105 VAL H H 8.552 0.02 1 1087 . 105 VAL CA C 66.852 0.1 1 1088 . 105 VAL HA H 3.586 0.02 1 1089 . 105 VAL CB C 31.909 0.1 1 1090 . 105 VAL HB H 2.071 0.02 1 1091 . 105 VAL CG2 C 21.123 0.1 1 1092 . 105 VAL HG2 H 0.955 0.02 2 1093 . 105 VAL CG1 C 22.885 0.1 1 1094 . 105 VAL HG1 H 1.099 0.02 2 1095 . 105 VAL C C 178.822 0.1 1 1096 . 106 ASN N N 116.863 0.1 1 1097 . 106 ASN H H 7.804 0.02 1 1098 . 106 ASN CA C 56.838 0.1 1 1099 . 106 ASN HA H 4.458 0.02 1 1100 . 106 ASN CB C 39.260 0.1 1 1101 . 106 ASN HB3 H 2.783 0.02 2 1102 . 106 ASN HB2 H 2.787 0.02 2 1103 . 106 ASN ND2 N 112.785 0.1 1 1104 . 106 ASN HD21 H 7.808 0.02 2 1105 . 106 ASN HD22 H 6.866 0.02 2 1106 . 106 ASN C C 177.909 0.1 1 1107 . 107 TYR N N 122.295 0.1 1 1108 . 107 TYR H H 8.771 0.02 1 1109 . 107 TYR CA C 62.561 0.1 1 1110 . 107 TYR HA H 3.963 0.02 1 1111 . 107 TYR CB C 38.923 0.1 1 1112 . 107 TYR HB3 H 3.107 0.02 2 1113 . 107 TYR HB2 H 3.229 0.02 2 1114 . 107 TYR HD1 H 6.740 0.02 3 1115 . 107 TYR HE1 H 6.280 0.02 3 1116 . 107 TYR C C 179.078 0.1 1 1117 . 108 LEU N N 119.384 0.1 1 1118 . 108 LEU H H 8.399 0.02 1 1119 . 108 LEU CA C 57.405 0.1 1 1120 . 108 LEU HA H 4.121 0.02 1 1121 . 108 LEU CB C 41.459 0.1 1 1122 . 108 LEU HB3 H 1.632 0.02 2 1123 . 108 LEU HB2 H 1.976 0.02 2 1124 . 108 LEU CG C 25.847 0.1 1 1125 . 108 LEU HD1 H 0.830 0.02 2 1126 . 108 LEU CD2 C 22.497 0.1 1 1127 . 108 LEU HD2 H 0.986 0.02 2 1128 . 108 LEU C C 178.603 0.1 1 1129 . 109 GLU N N 116.503 0.1 1 1130 . 109 GLU H H 7.838 0.02 1 1131 . 109 GLU CA C 58.477 0.1 1 1132 . 109 GLU HA H 4.216 0.02 1 1133 . 109 GLU CB C 30.457 0.1 1 1134 . 109 GLU HB3 H 2.111 0.02 2 1135 . 109 GLU HB2 H 2.221 0.02 2 1136 . 109 GLU CG C 36.750 0.1 1 1137 . 109 GLU HG3 H 2.307 0.02 2 1138 . 109 GLU HG2 H 2.533 0.02 2 1139 . 109 GLU C C 178.095 0.1 1 1140 . 110 THR N N 105.927 0.1 1 1141 . 110 THR H H 7.363 0.02 1 1142 . 110 THR CA C 61.402 0.1 1 1143 . 110 THR HA H 4.370 0.02 1 1144 . 110 THR CB C 70.714 0.1 1 1145 . 110 THR HB H 4.163 0.02 1 1146 . 110 THR CG2 C 21.774 0.1 1 1147 . 110 THR HG2 H 1.135 0.02 1 1148 . 110 THR HG1 H 4.200 0.02 1 1149 . 110 THR C C 173.594 0.1 1 1150 . 111 HIS N N 125.239 0.1 1 1151 . 111 HIS H H 7.341 0.02 1 1152 . 111 HIS CA C 57.596 0.1 1 1153 . 111 HIS HA H 4.390 0.02 1 1154 . 111 HIS CB C 30.002 0.1 1 1155 . 111 HIS HB3 H 2.278 0.02 2 1156 . 111 HIS HB2 H 3.189 0.02 2 1157 . 111 HIS C C 178.435 0.1 1 stop_ save_