data_4183 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Expression and Assignment of 1H, 15N,and 13C Resonances of the C-terminal Domain of the Diphtheria Toxin Repressor ; _BMRB_accession_number 4183 _BMRB_flat_file_name bmr4183.str _Entry_type original _Submission_date 1998-08-13 _Accession_date 1998-08-13 _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 Twigg Pamela D. . 2 Wylie Gregory P. . 3 Wang Guangshun . . 4 Caspar Donald L.D. . 5 Murphy John R. . 6 Logan Timothy M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 497 "13C chemical shifts" 392 "15N chemical shifts" 106 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-03-01 original author . stop_ _Original_release_date 1999-03-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Twigg, P. D., Wylie, G. P., Wang, G., Caspar, D. L.D., Murphy, J. R., and Logan, T. M.,"Expression and Assignment of 1H, 15N,and 13C Resonances of the C-terminal Domain of the Diphtheria Toxin Repressor," J. Biomol. NMR 13, 197-198 (1999). ; _Citation_title ; Expression and Assignment of 1H, 15N,and 13C Resonances of the C-terminal Domain of the Diphtheria Toxin Repressor ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Twigg Pamela D. . 2 Wylie Gregory P. . 3 Wang Guangshun . . 4 Caspar Donald L.D. . 5 Murphy John R. . 6 Logan Timothy M. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 13 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 197 _Page_last 198 _Year 1999 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995). ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_DtxR(130-226) _Saveframe_category molecular_system _Mol_system_name 'DtxR subunit 3, C-terminal domain' _Abbreviation_common DtxR(130-226) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DtxR(130-226) $DtxR(130-226) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'N-TERMINAL HIS tag not cleaved; not observed in NMR spectra' save_ ######################## # Monomeric polymers # ######################## save_DtxR(130-226) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'DtxR subunit 3, C-terminal domain' _Abbreviation_common DtxR(130-226) _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 109 _Mol_residue_sequence ; MRGSHHHHHHGSNPIPGLDE LGVGNSDAAAPGTRVIDAAT SMPRKVRIVQINEIFQVETD QFTQLLDADIRVGSEVEIVD RDGHITLSHNGKDVELLDDL AHTIRIEEL ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ARG 3 GLY 4 SER 5 HIS 6 HIS 7 HIS 8 HIS 9 HIS 10 HIS 11 GLY 12 SER 13 ASN 14 PRO 15 ILE 16 PRO 17 GLY 18 LEU 19 ASP 20 GLU 21 LEU 22 GLY 23 VAL 24 GLY 25 ASN 26 SER 27 ASP 28 ALA 29 ALA 30 ALA 31 PRO 32 GLY 33 THR 34 ARG 35 VAL 36 ILE 37 ASP 38 ALA 39 ALA 40 THR 41 SER 42 MET 43 PRO 44 ARG 45 LYS 46 VAL 47 ARG 48 ILE 49 VAL 50 GLN 51 ILE 52 ASN 53 GLU 54 ILE 55 PHE 56 GLN 57 VAL 58 GLU 59 THR 60 ASP 61 GLN 62 PHE 63 THR 64 GLN 65 LEU 66 LEU 67 ASP 68 ALA 69 ASP 70 ILE 71 ARG 72 VAL 73 GLY 74 SER 75 GLU 76 VAL 77 GLU 78 ILE 79 VAL 80 ASP 81 ARG 82 ASP 83 GLY 84 HIS 85 ILE 86 THR 87 LEU 88 SER 89 HIS 90 ASN 91 GLY 92 LYS 93 ASP 94 VAL 95 GLU 96 LEU 97 LEU 98 ASP 99 ASP 100 LEU 101 ALA 102 HIS 103 THR 104 ILE 105 ARG 106 ILE 107 GLU 108 GLU 109 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-02 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 BMRB 15254 PrSH3 88.99 121 100.00 100.00 1.88e-60 BMRB 15255 SH3 76.15 87 100.00 100.00 1.58e-49 PDB 1BI0 "Structure Of Apo-And Holo-Diphtheria Toxin Repressor" 88.99 226 100.00 100.00 5.61e-60 PDB 1BI1 "Structure Of Apo-And Holo-Diphtheria Toxin Repressor" 88.99 226 100.00 100.00 5.61e-60 PDB 1BI2 "Structure Of Apo-And Holo-Diphtheria Toxin Repressor" 88.99 226 100.00 100.00 5.86e-60 PDB 1BI3 "Structure Of Apo-And Holo-Diphtheria Toxin Repressor" 88.99 226 100.00 100.00 5.61e-60 PDB 1BYM "Solution Structures Of The C-Terminal Domain Of Diphtheria Toxin Repressor" 88.99 97 100.00 100.00 1.08e-60 PDB 1C0W "Crystal Structure Of The Cobalt-Activated Diphtheria Toxin Repressor-Dna Complex Reveals A Metal Binding Sh-Like Domain" 88.99 225 100.00 100.00 6.07e-60 PDB 1DDN "Diphtheria Tox Repressor (C102d Mutant)TOX DNA OPERATOR Complex" 88.99 226 100.00 100.00 5.92e-60 PDB 1DPR "Structures Of The Apo-And Metal Ion Activated Forms Of The Diphtheria Tox Repressor From Corynebacterium Diphtheriae" 88.99 226 100.00 100.00 5.86e-60 PDB 1FWZ "Glu20ala Dtxr" 88.99 226 100.00 100.00 5.31e-60 PDB 1G3S "Cys102ser Dtxr" 88.99 226 100.00 100.00 4.98e-60 PDB 1G3T "Cys102ser Dtxr" 88.99 226 100.00 100.00 4.98e-60 PDB 1G3W "Cd-Cys102ser Dtxr" 88.99 226 100.00 100.00 4.98e-60 PDB 1G3Y "Arg80ala Dtxr" 88.99 226 100.00 100.00 5.43e-60 PDB 1P92 "Crystal Structure Of (H79a)dtxr" 88.99 226 100.00 100.00 3.88e-60 PDB 1QVP "C Terminal Sh3-Like Domain From Diphtheria Toxin Repressor Residues 144-226" 76.15 87 100.00 100.00 1.58e-49 PDB 1QW1 "Solution Structure Of The C-Terminal Domain Of Dtxr Residues 110-226" 88.99 121 100.00 100.00 1.88e-60 PDB 2DTR "Structure Of Diphtheria Toxin Repressor" 88.99 226 100.00 100.00 5.86e-60 PDB 2QQ9 "Crystal Structure Of Dtxr(D6a C102d) Complexed With Nickel(Ii)" 88.99 226 100.00 100.00 5.20e-60 PDB 2QQA "Crystal Structure Of Dtxr(E9a C102d) Complexed With Nickel(Ii)" 88.99 226 100.00 100.00 5.61e-60 PDB 2QQB "Crystal Structure Of Dtxr(m10a C102d) Complexed With Nickel(ii)" 88.99 226 100.00 100.00 5.86e-60 PDB 2TDX "Diphtheria Tox Repressor (C102d Mutant) Complexed With Nickel" 88.99 226 100.00 100.00 5.92e-60 PDB 3GLX "Crystal Structure Analysis Of The Dtxr(E175k) Complexed With Ni(Ii)" 88.99 226 97.94 98.97 8.61e-59 EMBL CAE49945 "diphtheria toxin repressor [Corynebacterium diphtheriae]" 88.99 226 97.94 98.97 6.50e-59 EMBL CCG27916 "diphtheria toxin repressor [Corynebacterium diphtheriae]" 88.07 235 98.96 100.00 1.50e-58 EMBL CCG27917 "diphtheria toxin repressor [Corynebacterium diphtheriae]" 88.99 226 100.00 100.00 5.86e-60 EMBL CCG27918 "diphtheria toxin repressor [Corynebacterium diphtheriae]" 88.99 226 100.00 100.00 5.86e-60 EMBL CCG27919 "diphtheria toxin repressor [Corynebacterium diphtheriae]" 88.99 226 100.00 100.00 5.86e-60 GB AAA23296 "toxin repressor protein (dtxR) [Corynebacterium diphtheriae]" 88.99 226 100.00 100.00 5.86e-60 GB AAA23299 "diphtheria toxin repressor [Corynebacterium diphtheriae PW8]" 88.99 226 100.00 100.00 5.86e-60 GB AAA23301 "diphtheria toxin repressor [Corynebacterium diphtheriae]" 88.99 226 100.00 100.00 6.89e-60 GB AAU93781 "diphtheria toxin repressor [Corynebacterium diphtheriae]" 88.99 226 97.94 97.94 5.31e-58 GB AAU93782 "diphtheria toxin repressor [Corynebacterium diphtheriae]" 88.99 226 97.94 98.97 1.50e-58 REF WP_003851803 "diphtheria toxin repressor [Corynebacterium diphtheriae]" 88.99 226 100.00 100.00 5.86e-60 REF WP_010935052 "diphtheria toxin repressor [Corynebacterium diphtheriae]" 88.99 226 97.94 98.97 6.50e-59 REF WP_014316797 "diphtheria toxin repressor [Corynebacterium diphtheriae]" 88.99 226 98.97 100.00 2.30e-59 REF WP_014320173 "dihydrofolate reductase [Corynebacterium diphtheriae]" 88.99 226 98.97 98.97 5.64e-59 SP H2I233 "RecName: Full=Diphtheria toxin repressor; AltName: Full=Iron-dependent diphtheria tox regulatory element; AltName: Full=Tox reg" 88.99 226 100.00 100.00 5.86e-60 SP P0DJL7 "RecName: Full=Diphtheria toxin repressor; AltName: Full=Iron-dependent diphtheria tox regulatory element; AltName: Full=Tox reg" 88.99 226 97.94 98.97 6.50e-59 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $DtxR(130-226) 'Corynebacterium diphtheriae' 1717 Bacteria . Corynebacterium diphtheriae stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $DtxR(130-226) 'recombinant technology' E.coli Escherichia coli . plasmid pQE31 'n-terminal his-tag' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $DtxR(130-226) . mM 1 2 '[U-95% 15N]' stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $DtxR(130-226) . mM 1 2 '[U-95% 15N; U-95% 13C]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.2 0.01 na pH 6.5 0.2 na temperature 303 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 _Indirect_shift_ratio_citation_label DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 $citation_one DSS H 1 'methyl protons' ppm 0.00 . direct . . . 1.0 $citation_one DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $citation_one stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details ; Residues 13-109 in the current chemical shift list correspond to DtxR(130-226) ; loop_ _Sample_label $sample_one $sample_two stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name DtxR(130-226) _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 . 11 GLY CA C 44.92 . . 2 . 12 SER H H 8.26 . . 3 . 12 SER HA H 4.46 . . 4 . 12 SER HB2 H 3.91 . . 5 . 12 SER HB3 H 3.85 . . 6 . 12 SER CA C 57.92 . . 7 . 12 SER CB C 63.62 . . 8 . 12 SER N N 113.69 . . 9 . 13 ASN H H 8.44 . . 10 . 13 ASN HA H 4.97 . . 11 . 13 ASN HB2 H 2.79 . . 12 . 13 ASN HB3 H 2.66 . . 13 . 13 ASN HD21 H 6.89 . . 14 . 13 ASN HD22 H 7.59 . . 15 . 13 ASN CA C 51.20 . . 16 . 13 ASN CB C 38.68 . . 17 . 13 ASN N N 119.54 . . 18 . 13 ASN ND2 N 110.89 . . 19 . 14 PRO HA H 4.39 . . 20 . 14 PRO HB2 H 2.17 . . 21 . 14 PRO HB3 H 1.86 . . 22 . 14 PRO HG2 H 1.96 . . 23 . 14 PRO HD2 H 3.73 . . 24 . 14 PRO HD3 H 3.66 . . 25 . 14 PRO C C 176.55 . . 26 . 14 PRO CA C 62.83 . . 27 . 14 PRO CB C 32.00 . . 28 . 14 PRO CG C 27.14 . . 29 . 14 PRO CD C 50.11 . . 30 . 15 ILE H H 8.23 . . 31 . 15 ILE HA H 4.40 . . 32 . 15 ILE HB H 1.83 . . 33 . 15 ILE HG12 H 1.49 . . 34 . 15 ILE HG13 H 1.11 . . 35 . 15 ILE HG2 H 0.89 . . 36 . 15 ILE HD1 H 0.82 . . 37 . 15 ILE CA C 58.22 . . 38 . 15 ILE CB C 38.40 . . 39 . 15 ILE CG1 C 26.60 . . 40 . 15 ILE CG2 C 16.70 . . 41 . 15 ILE CD1 C 12.40 . . 42 . 15 ILE N N 120.59 . . 43 . 16 PRO HA H 4.37 . . 44 . 16 PRO HB2 H 2.26 . . 45 . 16 PRO HB3 H 1.89 . . 46 . 16 PRO HG2 H 2.04 . . 47 . 16 PRO HG3 H 1.91 . . 48 . 16 PRO HD2 H 3.86 . . 49 . 16 PRO HD3 H 3.67 . . 50 . 16 PRO C C 176.09 . . 51 . 16 PRO CA C 63.41 . . 52 . 16 PRO CB C 31.70 . . 53 . 16 PRO CG C 27.10 . . 54 . 16 PRO CD C 50.67 . . 55 . 17 GLY H H 8.52 . . 56 . 17 GLY HA2 H 3.97 . . 57 . 17 GLY C C 176.15 . . 58 . 17 GLY CA C 45.19 . . 59 . 17 GLY N N 108.2 . . 60 . 18 LEU H H 7.95 . . 61 . 18 LEU HA H 4.33 . . 62 . 18 LEU HB2 H 1.58 . . 63 . 18 LEU HG H 1.71 . . 64 . 18 LEU HD1 H 0.91 . . 65 . 18 LEU HD2 H 0.84 . . 66 . 18 LEU C C 176.41 . . 67 . 18 LEU CA C 55.12 . . 68 . 18 LEU CB C 42.02 . . 69 . 18 LEU CG C 26.00 . . 70 . 18 LEU CD1 C 24.44 . . 71 . 18 LEU CD2 C 23.24 . . 72 . 18 LEU N N 119.99 . . 73 . 19 ASP H H 8.46 . . 74 . 19 ASP HA H 4.59 . . 75 . 19 ASP HB2 H 2.69 . . 76 . 19 ASP HB3 H 2.64 . . 77 . 19 ASP C C 177.12 . . 78 . 19 ASP CA C 54.08 . . 79 . 19 ASP CB C 40.78 . . 80 . 19 ASP N N 118.78 . . 81 . 20 GLU H H 8.28 . . 82 . 20 GLU HA H 4.24 . . 83 . 20 GLU HB2 H 2.08 . . 84 . 20 GLU HB3 H 1.96 . . 85 . 20 GLU HG2 H 2.24 . . 86 . 20 GLU C C 177.31 . . 87 . 20 GLU CA C 56.56 . . 88 . 20 GLU CB C 29.78 . . 89 . 20 GLU CG C 36.03 . . 90 . 20 GLU N N 119.28 . . 91 . 21 LEU H H 8.16 . . 92 . 21 LEU HA H 4.42 . . 93 . 21 LEU HB2 H 1.72 . . 94 . 21 LEU HB3 H 1.63 . . 95 . 21 LEU HD1 H 0.89 . . 96 . 21 LEU HD2 H 0.84 . . 97 . 21 LEU C C 178.62 . . 98 . 21 LEU CA C 55.14 . . 99 . 21 LEU CB C 42.08 . . 100 . 21 LEU N N 120.14 . . 101 . 22 GLY H H 8.28 . . 102 . 22 GLY HA2 H 3.93 . . 103 . 22 GLY C C 174.96 . . 104 . 22 GLY CA C 45.08 . . 105 . 22 GLY N N 107.58 . . 106 . 23 VAL H H 7.95 . . 107 . 23 VAL HA H 4.13 . . 108 . 23 VAL HB H 2.12 . . 109 . 23 VAL HG1 H 0.92 . . 110 . 23 VAL C C 177.42 . . 111 . 23 VAL CA C 62.10 . . 112 . 23 VAL CB C 32.22 . . 113 . 23 VAL CG1 C 20.37 . . 114 . 23 VAL N N 116.75 . . 115 . 24 GLY H H 8.52 . . 116 . 24 GLY HA2 H 3.96 . . 117 . 24 GLY C C 174.52 . . 118 . 24 GLY CA C 45.19 . . 119 . 24 GLY N N 110.49 . . 120 . 25 ASN H H 8.26 . . 121 . 25 ASN HA H 4.76 . . 122 . 25 ASN HB2 H 2.83 . . 123 . 25 ASN HD21 H 7.58 . . 124 . 25 ASN HD22 H 6.91 . . 125 . 25 ASN C C 176.12 . . 126 . 25 ASN CA C 52.89 . . 127 . 25 ASN CB C 38.68 . . 128 . 25 ASN N N 117.43 . . 129 . 25 ASN ND2 N 110.38 . . 130 . 26 SER H H 8.38 . . 131 . 26 SER HA H 4.45 . . 132 . 26 SER HB2 H 3.91 . . 133 . 26 SER C C 175.00 . . 134 . 26 SER CA C 58.36 . . 135 . 26 SER CB C 63.43 . . 136 . 26 SER N N 114.99 . . 137 . 27 ASP H H 8.37 . . 138 . 27 ASP HA H 4.62 . . 139 . 27 ASP HB2 H 2.71 . . 140 . 27 ASP HB3 H 2.64 . . 141 . 27 ASP C C 176.72 . . 142 . 27 ASP CA C 54.30 . . 143 . 27 ASP CB C 40.98 . . 144 . 27 ASP N N 120.94 . . 145 . 28 ALA H H 8.06 . . 146 . 28 ALA HA H 4.26 . . 147 . 28 ALA HB H 1.38 . . 148 . 28 ALA C C 177.99 . . 149 . 28 ALA CA C 52.33 . . 150 . 28 ALA CB C 18.84 . . 151 . 28 ALA N N 122.35 . . 152 . 29 ALA H H 8.12 . . 153 . 29 ALA HA H 4.30 . . 154 . 29 ALA HB H 1.37 . . 155 . 29 ALA C C 177.58 . . 156 . 29 ALA CA C 51.70 . . 157 . 29 ALA CB C 18.93 . . 158 . 29 ALA N N 121.07 . . 159 . 30 ALA H H 7.97 . . 160 . 30 ALA HA H 4.54 . . 161 . 30 ALA HB H 1.25 . . 162 . 30 ALA CA C 49.80 . . 163 . 30 ALA CB C 17.77 . . 164 . 30 ALA N N 123.18 . . 165 . 31 PRO HA H 4.49 . . 166 . 31 PRO HB2 H 2.21 . . 167 . 31 PRO HB3 H 1.80 . . 168 . 31 PRO HG2 H 2.01 . . 169 . 31 PRO HG3 H 1.81 . . 170 . 31 PRO HD2 H 3.69 . . 171 . 31 PRO HD3 H 3.56 . . 172 . 31 PRO C C 177.99 . . 173 . 31 PRO CA C 62.14 . . 174 . 31 PRO CB C 32.06 . . 175 . 31 PRO CG C 26.65 . . 176 . 31 PRO CD C 49.56 . . 177 . 32 GLY H H 8.39 . . 178 . 32 GLY HA2 H 3.96 . . 179 . 32 GLY HA3 H 3.88 . . 180 . 32 GLY C C 176.37 . . 181 . 32 GLY CA C 45.19 . . 182 . 32 GLY N N 105.21 . . 183 . 33 THR H H 9.23 . . 184 . 33 THR HA H 4.55 . . 185 . 33 THR HB H 3.72 . . 186 . 33 THR HG2 H 1.34 . . 187 . 33 THR C C 175.32 . . 188 . 33 THR CA C 61.10 . . 189 . 33 THR CB C 71.22 . . 190 . 33 THR CG2 C 21.52 . . 191 . 33 THR N N 116.41 . . 192 . 34 ARG H H 9.37 . . 193 . 34 ARG HA H 4.48 . . 194 . 34 ARG HB2 H 1.88 . . 195 . 34 ARG HG2 H 1.69 . . 196 . 34 ARG HD2 H 3.38 . . 197 . 34 ARG HD3 H 3.25 . . 198 . 34 ARG HE H 7.35 . . 199 . 34 ARG C C 179.72 . . 200 . 34 ARG CA C 57.17 . . 201 . 34 ARG CB C 30.97 . . 202 . 34 ARG CG C 26.94 . . 203 . 34 ARG CD C 43.54 . . 204 . 34 ARG N N 124.56 . . 205 . 34 ARG NE N 82.40 . . 206 . 35 VAL H H 8.75 . . 207 . 35 VAL HA H 3.50 . . 208 . 35 VAL HB H 2.14 . . 209 . 35 VAL HG1 H 0.91 . . 210 . 35 VAL C C 177.52 . . 211 . 35 VAL CA C 67.10 . . 212 . 35 VAL CB C 31.04 . . 213 . 35 VAL CG1 C 23.85 . . 214 . 35 VAL N N 121.83 . . 215 . 36 ILE H H 7.63 . . 216 . 36 ILE HA H 3.90 . . 217 . 36 ILE HB H 1.30 . . 218 . 36 ILE HG12 H 1.34 . . 219 . 36 ILE HG13 H 1.05 . . 220 . 36 ILE HG2 H 0.72 . . 221 . 36 ILE HD1 H 0.46 . . 222 . 36 ILE C C 175.05 . . 223 . 36 ILE CA C 61.97 . . 224 . 36 ILE CB C 38.04 . . 225 . 36 ILE CG1 C 28.20 . . 226 . 36 ILE CG2 C 14.00 . . 227 . 36 ILE CD1 C 16.20 . . 228 . 36 ILE N N 114.26 . . 229 . 37 ASP H H 6.99 . . 230 . 37 ASP HA H 4.68 . . 231 . 37 ASP HB2 H 2.78 . . 232 . 37 ASP HB3 H 2.64 . . 233 . 37 ASP C C 176.72 . . 234 . 37 ASP CA C 55.03 . . 235 . 37 ASP CB C 41.58 . . 236 . 37 ASP N N 117.61 . . 237 . 38 ALA H H 7.61 . . 238 . 38 ALA HA H 4.46 . . 239 . 38 ALA HB H 1.20 . . 240 . 38 ALA C C 178.32 . . 241 . 38 ALA CA C 51.88 . . 242 . 38 ALA CB C 21.43 . . 243 . 38 ALA N N 119.33 . . 244 . 39 ALA H H 7.64 . . 245 . 39 ALA HA H 4.12 . . 246 . 39 ALA HB H 1.25 . . 247 . 39 ALA C C 176.86 . . 248 . 39 ALA CA C 52.67 . . 249 . 39 ALA CB C 19.29 . . 250 . 39 ALA N N 119.34 . . 251 . 40 THR H H 9.21 . . 252 . 40 THR HA H 4.90 . . 253 . 40 THR HB H 4.65 . . 254 . 40 THR HG2 H 1.22 . . 255 . 40 THR C C 174.87 . . 256 . 40 THR CA C 59.53 . . 257 . 40 THR CB C 70.78 . . 258 . 40 THR CG2 C 21.13 . . 259 . 40 THR N N 113.68 . . 260 . 41 SER H H 8.48 . . 261 . 41 SER HA H 4.72 . . 262 . 41 SER HB2 H 4.13 . . 263 . 41 SER HB3 H 4.03 . . 264 . 41 SER C C 174.55 . . 265 . 41 SER CA C 59.41 . . 266 . 41 SER CB C 63.33 . . 267 . 41 SER N N 111.71 . . 268 . 42 MET H H 7.99 . . 269 . 42 MET HA H 5.11 . . 270 . 42 MET HB2 H 2.03 . . 271 . 42 MET HB3 H 1.09 . . 272 . 42 MET HG2 H 2.56 . . 273 . 42 MET CA C 51.17 . . 274 . 42 MET CB C 33.18 . . 275 . 42 MET CG C 31.40 . . 276 . 42 MET N N 120.92 . . 277 . 43 PRO HA H 4.74 . . 278 . 43 PRO HB2 H 2.11 . . 279 . 43 PRO HB3 H 1.88 . . 280 . 43 PRO HG2 H 1.97 . . 281 . 43 PRO HD2 H 3.85 . . 282 . 43 PRO HD3 H 3.93 . . 283 . 43 PRO C C 177.17 . . 284 . 43 PRO CA C 62.7 . . 285 . 43 PRO CB C 31.65 . . 286 . 43 PRO CG C 27.08 . . 287 . 43 PRO CD C 50.60 . . 288 . 44 ARG H H 8.05 . . 289 . 44 ARG HA H 4.73 . . 290 . 44 ARG HB2 H 1.85 . . 291 . 44 ARG HG2 H 1.70 . . 292 . 44 ARG HG3 H 1.48 . . 293 . 44 ARG HD2 H 3.23 . . 294 . 44 ARG HE H 8.73 . . 295 . 44 ARG C C 174.40 . . 296 . 44 ARG CA C 54.63 . . 297 . 44 ARG CB C 33.45 . . 298 . 44 ARG CG C 27.00 . . 299 . 44 ARG CD C 42.95 . . 300 . 44 ARG N N 118.27 . . 301 . 44 ARG NE N 85.20 . . 302 . 45 LYS H H 8.60 . . 303 . 45 LYS HA H 5.22 . . 304 . 45 LYS HB2 H 1.78 . . 305 . 45 LYS HB3 H 1.47 . . 306 . 45 LYS HG2 H 1.49 . . 307 . 45 LYS HG3 H 1.37 . . 308 . 45 LYS HD2 H 1.69 . . 309 . 45 LYS HE2 H 2.97 . . 310 . 45 LYS C C 176.22 . . 311 . 45 LYS CA C 55.51 . . 312 . 45 LYS CB C 33.45 . . 313 . 45 LYS CG C 24.90 . . 314 . 45 LYS CD C 28.8 . . 315 . 45 LYS CE C 41.75 . . 316 . 45 LYS N N 122.88 . . 317 . 46 VAL H H 9.23 . . 318 . 46 VAL HA H 4.70 . . 319 . 46 VAL HB H 2.32 . . 320 . 46 VAL HG1 H 0.84 . . 321 . 46 VAL HG2 H 0.64 . . 322 . 46 VAL C C 173.36 . . 323 . 46 VAL CA C 59.29 . . 324 . 46 VAL CB C 36.44 . . 325 . 46 VAL CG1 C 21.80 . . 326 . 46 VAL CG2 C 18.86 . . 327 . 46 VAL N N 115.72 . . 328 . 47 ARG H H 8.95 . . 329 . 47 ARG HA H 5.33 . . 330 . 47 ARG HB2 H 1.71 . . 331 . 47 ARG HB3 H 1.56 . . 332 . 47 ARG HG2 H 1.33 . . 333 . 47 ARG HD2 H 3.27 . . 334 . 47 ARG HE H 7.36 . . 335 . 47 ARG C C 177.22 . . 336 . 47 ARG CA C 53.55 . . 337 . 47 ARG CB C 33.45 . . 338 . 47 ARG CG C 27.70 . . 339 . 47 ARG CD C 42.65 . . 340 . 47 ARG N N 118.28 . . 341 . 47 ARG NE N 81.90 . . 342 . 48 ILE H H 8.66 . . 343 . 48 ILE HA H 4.05 . . 344 . 48 ILE HB H 2.24 . . 345 . 48 ILE HG12 H 1.42 . . 346 . 48 ILE HG13 H 1.13 . . 347 . 48 ILE HG2 H 0.72 . . 348 . 48 ILE HD1 H 0.57 . . 349 . 48 ILE C C 177.58 . . 350 . 48 ILE CA C 61.44 . . 351 . 48 ILE CB C 36.22 . . 352 . 48 ILE CG1 C 26.60 . . 353 . 48 ILE CG2 C 17.97 . . 354 . 48 ILE CD1 C 11.86 . . 355 . 48 ILE N N 123.03 . . 356 . 49 VAL H H 9.16 . . 357 . 49 VAL HA H 4.66 . . 358 . 49 VAL HB H 2.11 . . 359 . 49 VAL HG1 H 0.80 . . 360 . 49 VAL HG2 H 0.57 . . 361 . 49 VAL C C 175.62 . . 362 . 49 VAL CA C 61.08 . . 363 . 49 VAL CB C 33.20 . . 364 . 49 VAL CG1 C 21.31 . . 365 . 49 VAL CG2 C 18.96 . . 366 . 49 VAL N N 120.93 . . 367 . 50 GLN H H 7.64 . . 368 . 50 GLN HA H 4.37 . . 369 . 50 GLN HB2 H 2.05 . . 370 . 50 GLN HB3 H 1.72 . . 371 . 50 GLN HG2 H 2.35 . . 372 . 50 GLN HG3 H 2.17 . . 373 . 50 GLN HE21 H 7.73 . . 374 . 50 GLN HE22 H 6.82 . . 375 . 50 GLN C C 173.72 . . 376 . 50 GLN CA C 57.03 . . 377 . 50 GLN CB C 33.07 . . 378 . 50 GLN CG C 34.79 . . 379 . 50 GLN N N 119.33 . . 380 . 50 GLN NE2 N 109.87 . . 381 . 51 ILE H H 8.78 . . 382 . 51 ILE HA H 4.35 . . 383 . 51 ILE HB H 1.74 . . 384 . 51 ILE HG12 H 1.37 . . 385 . 51 ILE HG13 H 0.93 . . 386 . 51 ILE HG2 H 0.79 . . 387 . 51 ILE HD1 H 0.73 . . 388 . 51 ILE C C 174.32 . . 389 . 51 ILE CA C 61.45 . . 390 . 51 ILE CB C 39.83 . . 391 . 51 ILE CG1 C 28.00 . . 392 . 51 ILE CG2 C 17.30 . . 393 . 51 ILE CD1 C 13.46 . . 394 . 51 ILE N N 123.39 . . 395 . 52 ASN H H 8.22 . . 396 . 52 ASN HA H 4.77 . . 397 . 52 ASN HB2 H 2.77 . . 398 . 52 ASN HD21 H 6.80 . . 399 . 52 ASN HD22 H 7.44 . . 400 . 52 ASN C C 175.26 . . 401 . 52 ASN CA C 52.91 . . 402 . 52 ASN CB C 38.69 . . 403 . 52 ASN N N 119.97 . . 404 . 52 ASN ND2 N 109.62 . . 405 . 53 GLU H H 8.52 . . 406 . 53 GLU HA H 4.07 . . 407 . 53 GLU HB2 H 1.82 . . 408 . 53 GLU HG2 H 2.12 . . 409 . 53 GLU C C 176.92 . . 410 . 53 GLU CA C 56.65 . . 411 . 53 GLU CB C 29.86 . . 412 . 53 GLU CG C 35.99 . . 413 . 53 GLU N N 119.74 . . 414 . 54 ILE H H 7.90 . . 415 . 54 ILE HA H 3.96 . . 416 . 54 ILE HB H 1.76 . . 417 . 54 ILE HG12 H 1.24 . . 418 . 54 ILE HG13 H 1.03 . . 419 . 54 ILE HG2 H 0.73 . . 420 . 54 ILE HD1 H 0.74 . . 421 . 54 ILE C C 174.92 . . 422 . 54 ILE CA C 61.10 . . 423 . 54 ILE CB C 38.40 . . 424 . 54 ILE CG1 C 26.60 . . 425 . 54 ILE CG2 C 17.30 . . 426 . 54 ILE CD1 C 12.90 . . 427 . 54 ILE N N 118.04 . . 428 . 55 PHE H H 7.98 . . 429 . 55 PHE HA H 4.56 . . 430 . 55 PHE HB2 H 3.15 . . 431 . 55 PHE HB3 H 2.98 . . 432 . 55 PHE HD1 H 7.22 . . 433 . 55 PHE HE1 H 7.31 . . 434 . 55 PHE C C 176.06 . . 435 . 55 PHE CA C 57.38 . . 436 . 55 PHE CB C 38.88 . . 437 . 55 PHE N N 119.97 . . 438 . 56 GLN H H 8.10 . . 439 . 56 GLN HA H 4.25 . . 440 . 56 GLN HB2 H 2.08 . . 441 . 56 GLN HB3 H 1.94 . . 442 . 56 GLN HG2 H 2.24 . . 443 . 56 GLN HE21 H 7.48 . . 444 . 56 GLN HE22 H 6.74 . . 445 . 56 GLN C C 176.19 . . 446 . 56 GLN CA C 55.58 . . 447 . 56 GLN CB C 29.00 . . 448 . 56 GLN CG C 33.64 . . 449 . 56 GLN N N 119.03 . . 450 . 56 GLN NE2 N 109.62 . . 451 . 57 VAL H H 7.88 . . 452 . 57 VAL HA H 4.01 . . 453 . 57 VAL HB H 2.06 . . 454 . 57 VAL HG1 H 0.91 . . 455 . 57 VAL C C 176.52 . . 456 . 57 VAL CA C 61.96 . . 457 . 57 VAL CB C 32.60 . . 458 . 57 VAL CG1 C 20.63 . . 459 . 57 VAL N N 117.75 . . 460 . 58 GLU H H 8.50 . . 461 . 58 GLU HA H 4.30 . . 462 . 58 GLU HB2 H 2.11 . . 463 . 58 GLU HB3 H 2.04 . . 464 . 58 GLU HG2 H 2.23 . . 465 . 58 GLU C C 177.22 . . 466 . 58 GLU CA C 56.76 . . 467 . 58 GLU CB C 29.18 . . 468 . 58 GLU CG C 36.44 . . 469 . 58 GLU N N 120.84 . . 470 . 59 THR H H 7.93 . . 471 . 59 THR HA H 4.43 . . 472 . 59 THR HB H 4.35 . . 473 . 59 THR HG2 H 1.23 . . 474 . 59 THR C C 175.56 . . 475 . 59 THR CA C 61.59 . . 476 . 59 THR CB C 69.79 . . 477 . 59 THR CG2 C 21.67 . . 478 . 59 THR N N 112.69 . . 479 . 60 ASP H H 8.68 . . 480 . 60 ASP HA H 4.58 . . 481 . 60 ASP HB2 H 2.73 . . 482 . 60 ASP C C 178.29 . . 483 . 60 ASP CA C 55.71 . . 484 . 60 ASP CB C 40.26 . . 485 . 60 ASP N N 121.18 . . 486 . 61 GLN H H 8.34 . . 487 . 61 GLN HA H 4.16 . . 488 . 61 GLN HB2 H 1.94 . . 489 . 61 GLN HB3 H 1.86 . . 490 . 61 GLN HG2 H 2.22 . . 491 . 61 GLN C C 177.52 . . 492 . 61 GLN CA C 57.82 . . 493 . 61 GLN CB C 28.97 . . 494 . 61 GLN CG C 34.39 . . 495 . 61 GLN N N 117.16 . . 496 . 62 PHE H H 8.13 . . 497 . 62 PHE HA H 4.33 . . 498 . 62 PHE HB2 H 3.23 . . 499 . 62 PHE HB3 H 3.14 . . 500 . 62 PHE HD1 H 7.24 . . 501 . 62 PHE HE1 H 7.31 . . 502 . 62 PHE C C 178.22 . . 503 . 62 PHE CA C 60.27 . . 504 . 62 PHE CB C 38.59 . . 505 . 62 PHE N N 117.79 . . 506 . 63 THR H H 8.19 . . 507 . 63 THR HA H 3.93 . . 508 . 63 THR HB H 4.28 . . 509 . 63 THR HG2 H 1.29 . . 510 . 63 THR C C 176.50 . . 511 . 63 THR CA C 65.34 . . 512 . 63 THR CB C 68.37 . . 513 . 63 THR CG2 C 21.70 . . 514 . 63 THR N N 114.02 . . 515 . 64 GLN H H 7.99 . . 516 . 64 GLN HA H 4.16 . . 517 . 64 GLN HB2 H 2.12 . . 518 . 64 GLN HG2 H 2.53 . . 519 . 64 GLN HG3 H 2.37 . . 520 . 64 GLN HE21 H 7.52 . . 521 . 64 GLN HE22 H 6.93 . . 522 . 64 GLN C C 179.07 . . 523 . 64 GLN CA C 58.53 . . 524 . 64 GLN CB C 28.72 . . 525 . 64 GLN CG C 34.31 . . 526 . 64 GLN N N 119.14 . . 527 . 65 LEU H H 7.74 . . 528 . 65 LEU HA H 3.97 . . 529 . 65 LEU HB2 H 1.85 . . 530 . 65 LEU HB3 H 1.55 . . 531 . 65 LEU HG H 1.75 . . 532 . 65 LEU HD1 H 0.81 . . 533 . 65 LEU HD2 H 0.71 . . 534 . 65 LEU C C 179.22 . . 535 . 65 LEU CA C 57.76 . . 536 . 65 LEU CB C 40.66 . . 537 . 65 LEU CG C 26.71 . . 538 . 65 LEU CD1 C 25.45 . . 539 . 65 LEU CD2 C 23.31 . . 540 . 65 LEU N N 117.56 . . 541 . 66 LEU H H 7.80 . . 542 . 66 LEU HA H 4.08 . . 543 . 66 LEU HB2 H 1.59 . . 544 . 66 LEU HB3 H 1.74 . . 545 . 66 LEU HG H 1.57 . . 546 . 66 LEU HD1 H 0.85 . . 547 . 66 LEU C C 181.46 . . 548 . 66 LEU CA C 57.24 . . 549 . 66 LEU CB C 41.48 . . 550 . 66 LEU CG C 26.00 . . 551 . 66 LEU CD1 C 24.4 . . 552 . 66 LEU CD2 C 23.20 . . 553 . 66 LEU N N 118.76 . . 554 . 67 ASP H H 8.46 . . 555 . 67 ASP HA H 4.42 . . 556 . 67 ASP HB2 H 2.71 . . 557 . 67 ASP HB3 H 2.67 . . 558 . 67 ASP C C 177.58 . . 559 . 67 ASP CA C 56.13 . . 560 . 67 ASP CB C 40.56 . . 561 . 67 ASP N N 119.78 . . 562 . 68 ALA H H 7.48 . . 563 . 68 ALA HA H 4.35 . . 564 . 68 ALA HB H 1.42 . . 565 . 68 ALA C C 176.42 . . 566 . 68 ALA CA C 51.62 . . 567 . 68 ALA CB C 18.56 . . 568 . 68 ALA N N 118.27 . . 569 . 69 ASP H H 8.25 . . 570 . 69 ASP HA H 4.31 . . 571 . 69 ASP HB2 H 3.09 . . 572 . 69 ASP HB3 H 2.51 . . 573 . 69 ASP C C 174.59 . . 574 . 69 ASP CA C 54.62 . . 575 . 69 ASP CB C 39.69 . . 576 . 69 ASP N N 117.51 . . 577 . 70 ILE H H 7.87 . . 578 . 70 ILE HA H 3.58 . . 579 . 70 ILE HB H 1.59 . . 580 . 70 ILE HG12 H 1.54 . . 581 . 70 ILE HG13 H 0.46 . . 582 . 70 ILE HG2 H 0.51 . . 583 . 70 ILE HD1 H 0.68 . . 584 . 70 ILE C C 173.75 . . 585 . 70 ILE CA C 61.44 . . 586 . 70 ILE CB C 36.81 . . 587 . 70 ILE CG1 C 27.14 . . 588 . 70 ILE CG2 C 17.71 . . 589 . 70 ILE CD1 C 13.31 . . 590 . 70 ILE N N 115.98 . . 591 . 71 ARG H H 8.09 . . 592 . 71 ARG HA H 4.49 . . 593 . 71 ARG HB2 H 1.89 . . 594 . 71 ARG HB3 H 1.60 . . 595 . 71 ARG HG2 H 1.40 . . 596 . 71 ARG HG3 H 1.29 . . 597 . 71 ARG HD2 H 3.10 . . 598 . 71 ARG HE H 7.32 . . 599 . 71 ARG C C 176.42 . . 600 . 71 ARG CA C 53.00 . . 601 . 71 ARG CB C 33.10 . . 602 . 71 ARG CG C 25.50 . . 603 . 71 ARG CD C 43.00 . . 604 . 71 ARG N N 120.81 . . 605 . 71 ARG NE N 83.90 . . 606 . 72 VAL H H 8.48 . . 607 . 72 VAL HA H 3.26 . . 608 . 72 VAL HB H 1.92 . . 609 . 72 VAL HG1 H 0.93 . . 610 . 72 VAL HG2 H 0.88 . . 611 . 72 VAL C C 177.72 . . 612 . 72 VAL CA C 66.44 . . 613 . 72 VAL CB C 30.49 . . 614 . 72 VAL CG1 C 22.68 . . 615 . 72 VAL CG2 C 21.09 . . 616 . 72 VAL N N 119.06 . . 617 . 73 GLY H H 8.88 . . 618 . 73 GLY HA2 H 4.52 . . 619 . 73 GLY HA3 H 3.55 . . 620 . 73 GLY C C 175.42 . . 621 . 73 GLY CA C 44.4 . . 622 . 73 GLY N N 115.71 . . 623 . 74 SER H H 8.37 . . 624 . 74 SER HA H 4.37 . . 625 . 74 SER HB2 H 3.65 . . 626 . 74 SER HB3 H 3.43 . . 627 . 74 SER C C 173.22 . . 628 . 74 SER CA C 60.47 . . 629 . 74 SER CB C 62.80 . . 630 . 74 SER N N 116.70 . . 631 . 75 GLU H H 8.82 . . 632 . 75 GLU HA H 5.22 . . 633 . 75 GLU HB2 H 2.11 . . 634 . 75 GLU HB3 H 1.81 . . 635 . 75 GLU HG2 H 2.45 . . 636 . 75 GLU HG3 H 1.98 . . 637 . 75 GLU C C 176.72 . . 638 . 75 GLU CA C 54.95 . . 639 . 75 GLU CB C 29.5 . . 640 . 75 GLU CG C 36.44 . . 641 . 75 GLU N N 123.57 . . 642 . 76 VAL H H 8.86 . . 643 . 76 VAL HA H 5.10 . . 644 . 76 VAL HB H 2.21 . . 645 . 76 VAL HG1 H 0.63 . . 646 . 76 VAL HG2 H 0.58 . . 647 . 76 VAL C C 178.52 . . 648 . 76 VAL CA C 57.85 . . 649 . 76 VAL CB C 34.84 . . 650 . 76 VAL CG1 C 22.54 . . 651 . 76 VAL CG2 C 18.51 . . 652 . 76 VAL N N 114.91 . . 653 . 77 GLU H H 8.62 . . 654 . 77 GLU HA H 5.33 . . 655 . 77 GLU HB2 H 1.91 . . 656 . 77 GLU HG2 H 2.11 . . 657 . 77 GLU HG3 H 2.00 . . 658 . 77 GLU C C 177.12 . . 659 . 77 GLU CA C 54.91 . . 660 . 77 GLU CB C 32.10 . . 661 . 77 GLU CG C 37.52 . . 662 . 77 GLU N N 118.93 . . 663 . 78 ILE H H 8.69 . . 664 . 78 ILE HA H 5.54 . . 665 . 78 ILE HB H 1.51 . . 666 . 78 ILE HG12 H 1.51 . . 667 . 78 ILE HG13 H 1.18 . . 668 . 78 ILE HG2 H 0.84 . . 669 . 78 ILE HD1 H 0.72 . . 670 . 78 ILE C C 175.72 . . 671 . 78 ILE CA C 58.50 . . 672 . 78 ILE CB C 42.30 . . 673 . 78 ILE CG1 C 25.50 . . 674 . 78 ILE CG2 C 18.00 . . 675 . 78 ILE CD1 C 15.20 . . 676 . 78 ILE N N 114.20 . . 677 . 79 VAL H H 8.32 . . 678 . 79 VAL HA H 4.60 . . 679 . 79 VAL HB H 1.93 . . 680 . 79 VAL HG1 H 0.82 . . 681 . 79 VAL CA C 60.57 . . 682 . 79 VAL CB C 35.32 . . 683 . 79 VAL CG1 C 18.55 . . 684 . 79 VAL N N 121.02 . . 685 . 80 ASP H H 8.15 . . 686 . 80 ASP HA H 4.80 . . 687 . 80 ASP HB2 H 2.27 . . 688 . 80 ASP HB3 H 1.93 . . 689 . 80 ASP C C 176.38 . . 690 . 80 ASP CA C 52.39 . . 691 . 80 ASP CB C 41.50 . . 692 . 80 ASP N N 124.46 . . 693 . 81 ARG H H 8.45 . . 694 . 81 ARG HA H 4.50 . . 695 . 81 ARG HB2 H 1.76 . . 696 . 81 ARG HG2 H 1.56 . . 697 . 81 ARG HD2 H 3.16 . . 698 . 81 ARG HE H 7.16 . . 699 . 81 ARG C C 176.08 . . 700 . 81 ARG CA C 54.40 . . 701 . 81 ARG CB C 30.69 . . 702 . 81 ARG CG C 26.84 . . 703 . 81 ARG CD C 43.55 . . 704 . 81 ARG N N 124.18 . . 705 . 81 ARG NE N 83.00 . . 706 . 82 ASP H H 8.91 . . 707 . 82 ASP HA H 4.24 . . 708 . 82 ASP HB2 H 2.96 . . 709 . 82 ASP HB3 H 2.59 . . 710 . 82 ASP C C 175.62 . . 711 . 82 ASP CA C 55.07 . . 712 . 82 ASP CB C 39.75 . . 713 . 82 ASP N N 122.92 . . 714 . 83 GLY H H 8.88 . . 715 . 83 GLY HA2 H 4.03 . . 716 . 83 GLY HA3 H 3.63 . . 717 . 83 GLY C C 174.92 . . 718 . 83 GLY CA C 45.19 . . 719 . 83 GLY N N 104.73 . . 720 . 84 HIS H H 7.67 . . 721 . 84 HIS HA H 4.82 . . 722 . 84 HIS HB2 H 3.26 . . 723 . 84 HIS HB3 H 2.97 . . 724 . 84 HIS HD1 H 7.24 . . 725 . 84 HIS C C 174.59 . . 726 . 84 HIS CA C 53.39 . . 727 . 84 HIS CB C 29.33 . . 728 . 84 HIS N N 116.64 . . 729 . 85 ILE H H 9.69 . . 730 . 85 ILE HA H 4.75 . . 731 . 85 ILE HB H 1.90 . . 732 . 85 ILE HG12 H 1.32 . . 733 . 85 ILE HG13 H 1.14 . . 734 . 85 ILE HG2 H 0.67 . . 735 . 85 ILE HD1 H 0.69 . . 736 . 85 ILE C C 175.99 . . 737 . 85 ILE CA C 59.95 . . 738 . 85 ILE CB C 36.77 . . 739 . 85 ILE CG1 C 27.70 . . 740 . 85 ILE CG2 C 17.30 . . 741 . 85 ILE CD1 C 11.85 . . 742 . 85 ILE N N 126.93 . . 743 . 86 THR H H 8.80 . . 744 . 86 THR HA H 5.05 . . 745 . 86 THR HB H 3.76 . . 746 . 86 THR HG2 H 0.95 . . 747 . 86 THR C C 173.75 . . 748 . 86 THR CA C 61.59 . . 749 . 86 THR CB C 70.44 . . 750 . 86 THR CG2 C 20.77 . . 751 . 86 THR N N 122.24 . . 752 . 87 LEU H H 8.94 . . 753 . 87 LEU HA H 5.39 . . 754 . 87 LEU HB2 H 1.54 . . 755 . 87 LEU HB3 H 1.39 . . 756 . 87 LEU HG H 1.63 . . 757 . 87 LEU HD1 H 0.78 . . 758 . 87 LEU HD2 H 0.78 . . 759 . 87 LEU C C 176.35 . . 760 . 87 LEU CA C 52.67 . . 761 . 87 LEU CB C 44.97 . . 762 . 87 LEU CG C 27.30 . . 763 . 87 LEU CD1 C 26.27 . . 764 . 87 LEU CD2 C 24.40 . . 765 . 87 LEU N N 125.78 . . 766 . 88 SER H H 9.23 . . 767 . 88 SER HA H 5.85 . . 768 . 88 SER HB2 H 3.83 . . 769 . 88 SER HB3 H 3.55 . . 770 . 88 SER C C 175.22 . . 771 . 88 SER CA C 56.66 . . 772 . 88 SER CB C 64.88 . . 773 . 88 SER N N 116.88 . . 774 . 89 HIS H H 9.16 . . 775 . 89 HIS HA H 4.97 . . 776 . 89 HIS HB2 H 3.10 . . 777 . 89 HIS HB3 H 2.97 . . 778 . 89 HIS HD1 H 7.50 . . 779 . 89 HIS HE1 H 8.19 . . 780 . 89 HIS C C 174.66 . . 781 . 89 HIS CA C 55.50 . . 782 . 89 HIS CB C 32.27 . . 783 . 89 HIS N N 122.60 . . 784 . 90 ASN H H 9.28 . . 785 . 90 ASN HA H 4.23 . . 786 . 90 ASN HB2 H 3.00 . . 787 . 90 ASN HB3 H 2.43 . . 788 . 90 ASN HD21 H 7.34 . . 789 . 90 ASN HD22 H 6.80 . . 790 . 90 ASN C C 175.42 . . 791 . 90 ASN CA C 53.77 . . 792 . 90 ASN CB C 36.50 . . 793 . 90 ASN N N 124.12 . . 794 . 90 ASN ND2 N 109.11 . . 795 . 91 GLY H H 8.79 . . 796 . 91 GLY HA2 H 4.08 . . 797 . 91 GLY HA3 H 3.59 . . 798 . 91 GLY C C 174.32 . . 799 . 91 GLY CA C 45.15 . . 800 . 91 GLY N N 102.75 . . 801 . 92 LYS H H 7.80 . . 802 . 92 LYS HA H 4.56 . . 803 . 92 LYS HB2 H 1.88 . . 804 . 92 LYS HG2 H 1.39 . . 805 . 92 LYS HD2 H 1.67 . . 806 . 92 LYS HE2 H 3.00 . . 807 . 92 LYS C C 175.74 . . 808 . 92 LYS CA C 54.40 . . 809 . 92 LYS CB C 33.71 . . 810 . 92 LYS CG C 24.54 . . 811 . 92 LYS CD C 28.85 . . 812 . 92 LYS CE C 42.03 . . 813 . 92 LYS N N 119.79 . . 814 . 93 ASP H H 8.35 . . 815 . 93 ASP HA H 5.29 . . 816 . 93 ASP HB2 H 2.53 . . 817 . 93 ASP HB3 H 2.29 . . 818 . 93 ASP C C 176.62 . . 819 . 93 ASP CA C 52.82 . . 820 . 93 ASP CB C 42.43 . . 821 . 93 ASP N N 120.31 . . 822 . 94 VAL H H 9.25 . . 823 . 94 VAL HA H 4.20 . . 824 . 94 VAL HB H 1.93 . . 825 . 94 VAL HG1 H 0.78 . . 826 . 94 VAL C C 174.82 . . 827 . 94 VAL CA C 60.99 . . 828 . 94 VAL CB C 34.14 . . 829 . 94 VAL CG1 C 20.63 . . 830 . 94 VAL N N 121.32 . . 831 . 95 GLU H H 8.68 . . 832 . 95 GLU HA H 4.69 . . 833 . 95 GLU HB2 H 1.87 . . 834 . 95 GLU HG2 H 2.14 . . 835 . 95 GLU HG3 H 2.05 . . 836 . 95 GLU C C 176.75 . . 837 . 95 GLU CA C 55.58 . . 838 . 95 GLU CB C 29.29 . . 839 . 95 GLU CG C 36.11 . . 840 . 95 GLU N N 126.67 . . 841 . 96 LEU H H 8.82 . . 842 . 96 LEU HA H 4.50 . . 843 . 96 LEU HB2 H 1.75 . . 844 . 96 LEU HB3 H 1.40 . . 845 . 96 LEU HG H 1.55 . . 846 . 96 LEU HD1 H 0.96 . . 847 . 96 LEU HD2 H 0.74 . . 848 . 96 LEU C C 178.25 . . 849 . 96 LEU CA C 54.27 . . 850 . 96 LEU CB C 41.90 . . 851 . 96 LEU CG C 26.90 . . 852 . 96 LEU CD1 C 22.40 . . 853 . 96 LEU CD2 C 25.20 . . 854 . 96 LEU N N 124.63 . . 855 . 97 LEU H H 8.52 . . 856 . 97 LEU HA H 4.51 . . 857 . 97 LEU HB2 H 1.75 . . 858 . 97 LEU HG H 1.47 . . 859 . 97 LEU HD1 H 0.96 . . 860 . 97 LEU C C 178.52 . . 861 . 97 LEU CA C 54.48 . . 862 . 97 LEU CB C 41.94 . . 863 . 97 LEU CG C 26.90 . . 864 . 97 LEU CD1 C 22.70 . . 865 . 97 LEU CD2 C 25.20 . . 866 . 97 LEU N N 123.10 . . 867 . 98 ASP H H 8.63 . . 868 . 98 ASP HA H 4.31 . . 869 . 98 ASP HB2 H 2.75 . . 870 . 98 ASP HB3 H 2.66 . . 871 . 98 ASP C C 179.12 . . 872 . 98 ASP CA C 57.70 . . 873 . 98 ASP CB C 40.81 . . 874 . 98 ASP N N 118.78 . . 875 . 99 ASP H H 8.77 . . 876 . 99 ASP HA H 4.44 . . 877 . 99 ASP HB2 H 2.72 . . 878 . 99 ASP HB3 H 2.60 . . 879 . 99 ASP C C 179.52 . . 880 . 99 ASP CA C 56.67 . . 881 . 99 ASP CB C 39.72 . . 882 . 99 ASP N N 115.98 . . 883 . 100 LEU H H 7.80 . . 884 . 100 LEU HA H 4.40 . . 885 . 100 LEU HB2 H 1.83 . . 886 . 100 LEU HB3 H 1.56 . . 887 . 100 LEU HG H 1.72 . . 888 . 100 LEU HD1 H 0.92 . . 889 . 100 LEU HD2 H 0.82 . . 890 . 100 LEU C C 179.42 . . 891 . 100 LEU CA C 56.66 . . 892 . 100 LEU CB C 41.92 . . 893 . 100 LEU CG C 28.20 . . 894 . 100 LEU CD1 C 25.50 . . 895 . 100 LEU CD2 C 23.30 . . 896 . 100 LEU N N 119.03 . . 897 . 101 ALA H H 8.25 . . 898 . 101 ALA HA H 3.92 . . 899 . 101 ALA HB H 1.38 . . 900 . 101 ALA C C 177.68 . . 901 . 101 ALA CA C 53.93 . . 902 . 101 ALA CB C 17.71 . . 903 . 101 ALA N N 118.68 . . 904 . 102 HIS H H 7.76 . . 905 . 102 HIS HA H 4.37 . . 906 . 102 HIS HB2 H 3.33 . . 907 . 102 HIS C C 176.09 . . 908 . 102 HIS CA C 57.85 . . 909 . 102 HIS CB C 30.05 . . 910 . 102 HIS N N 109.79 . . 911 . 103 THR H H 7.75 . . 912 . 103 THR HA H 4.35 . . 913 . 103 THR HB H 4.34 . . 914 . 103 THR HG2 H 1.28 . . 915 . 103 THR C C 174.92 . . 916 . 103 THR CA C 63.17 . . 917 . 103 THR CB C 69.79 . . 918 . 103 THR CG2 C 21.67 . . 919 . 103 THR N N 108.86 . . 920 . 104 ILE H H 7.61 . . 921 . 104 ILE HA H 4.44 . . 922 . 104 ILE HB H 1.65 . . 923 . 104 ILE HG12 H 2.08 . . 924 . 104 ILE HG13 H 1.02 . . 925 . 104 ILE HG2 H 0.75 . . 926 . 104 ILE HD1 H 0.75 . . 927 . 104 ILE C C 175.65 . . 928 . 104 ILE CA C 61.64 . . 929 . 104 ILE CB C 38.08 . . 930 . 104 ILE CG1 C 28.23 . . 931 . 104 ILE CG2 C 17.30 . . 932 . 104 ILE CD1 C 14.34 . . 933 . 104 ILE N N 121.87 . . 934 . 105 ARG H H 8.68 . . 935 . 105 ARG HA H 5.20 . . 936 . 105 ARG HB2 H 1.74 . . 937 . 105 ARG HB3 H 1.44 . . 938 . 105 ARG HG2 H 1.67 . . 939 . 105 ARG HG3 H 1.05 . . 940 . 105 ARG HD2 H 3.23 . . 941 . 105 ARG HD3 H 2.90 . . 942 . 105 ARG HE H 7.19 . . 943 . 105 ARG C C 177.48 . . 944 . 105 ARG CA C 53.54 . . 945 . 105 ARG CB C 33.16 . . 946 . 105 ARG CG C 28.60 . . 947 . 105 ARG CD C 42.45 . . 948 . 105 ARG N N 122.59 . . 949 . 105 ARG NE N 82.40 . . 950 . 106 ILE H H 9.36 . . 951 . 106 ILE HA H 5.47 . . 952 . 106 ILE HB H 1.92 . . 953 . 106 ILE HG12 H 1.44 . . 954 . 106 ILE HG13 H 0.74 . . 955 . 106 ILE HG2 H 0.63 . . 956 . 106 ILE HD1 H 0.63 . . 957 . 106 ILE C C 175.32 . . 958 . 106 ILE CA C 56.70 . . 959 . 106 ILE CB C 43.39 . . 960 . 106 ILE CG1 C 26.60 . . 961 . 106 ILE CG2 C 22.70 . . 962 . 106 ILE CD1 C 14.01 . . 963 . 106 ILE N N 113.84 . . 964 . 107 GLU H H 9.29 . . 965 . 107 GLU HA H 4.81 . . 966 . 107 GLU HB2 H 2.05 . . 967 . 107 GLU HB3 H 1.94 . . 968 . 107 GLU HG2 H 2.24 . . 969 . 107 GLU C C 174.65 . . 970 . 107 GLU CA C 53.71 . . 971 . 107 GLU CB C 33.12 . . 972 . 107 GLU CG C 35.89 . . 973 . 107 GLU N N 117.94 . . 974 . 108 GLU H H 8.55 . . 975 . 108 GLU HA H 4.39 . . 976 . 108 GLU HB2 H 2.26 . . 977 . 108 GLU HB3 H 1.81 . . 978 . 108 GLU HG2 H 2.43 . . 979 . 108 GLU HG3 H 2.32 . . 980 . 108 GLU C C 176.92 . . 981 . 108 GLU CA C 55.25 . . 982 . 108 GLU CB C 28.89 . . 983 . 108 GLU CG C 35.22 . . 984 . 108 GLU N N 118.66 . . 985 . 109 LEU H H 8.67 . . 986 . 109 LEU HA H 4.08 . . 987 . 109 LEU HB2 H 1.62 . . 988 . 109 LEU HB3 H 1.56 . . 989 . 109 LEU HG H 1.65 . . 990 . 109 LEU HD1 H 0.77 . . 991 . 109 LEU CA C 56.65 . . 992 . 109 LEU CB C 42.13 . . 993 . 109 LEU CG C 27.69 . . 994 . 109 LEU CD1 C 25.5 . . 995 . 109 LEU N N 124.82 . . stop_ save_