data_4254 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C Assignments of the DNA Binding Domain of Transcription Factor Mbp1 from Sassharomyces cerevisiae in Both Its Free and DNA Bound Forms and 1H Assignments of the Free DNA ; _BMRB_accession_number 4254 _BMRB_flat_file_name bmr4254.str _Entry_type original _Submission_date 1998-10-27 _Accession_date 1998-10-27 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 McIntosh Pauline B . 2 Taylor Ian A . 3 Smerdon Steven J . 4 Frenkiel Thomas A . 5 Lane Andrew N . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 422 "13C chemical shifts" 242 "15N chemical shifts" 126 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-10-26 original author . stop_ _Original_release_date 1999-10-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; McIntosh, P.B., Taylor, I.A., Smerdon, S.J., Frenkiel, T.A., and Lane, A.N., "1H, 15N and 13C Assignments of the DNA Binding Domain of Transcription Factor Mbp1 from Saccharomyces cerevisiae in Both Its Free and DNA Bound Forms and 1H Assignments of the Free DNA", J. Biomol. NMR, 13(4), 397-398,(1999). ; _Citation_title ; 1H, 15N and 13C Assignments of the DNA Binding Domain of Transcription Factor Mbp1 from Saccharomyces cerevisiae in Both Its Free and DNA Bound Forms and 1H Assignments of the Fee DNA ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99281467 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 McIntosh Pauline B . 2 Taylor Ian A . 3 Smerdon Steven J . 4 Frenkiel Thomas A . 5 Lane Andrew N . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 13 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 397 _Page_last 398 _Year 1999 _Details . loop_ _Keyword cell_cycle MBp1 NMR_assignments stop_ 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_ save_citation_two _Saveframe_category citation _Citation_full ; Bartels, C., Xia, T., Guntert, P., Billeter, M. & Wuthrich,K. The Program Xeasy for Computer-Supported NMR Spectral Analysis. J. Biomol. NMR 5, 1-10 (1995). ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_Mbp1 _Saveframe_category molecular_system _Mol_system_name Mbp1 _Abbreviation_common Mbp1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Mbp1 $Mbp1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'Transcription factor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Mbp1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'MLU1-BOX binding protein' _Name_variant Mpb1 _Abbreviation_common Mpb1 _Molecular_mass 15436.7 _Mol_thiol_state . _Details ; Residue Methionine 1 present in the crystal structure described in the above database entry is absent from the construct studied by NMR and described in this deposition. ; ############################## # Polymer residue sequence # ############################## _Residue_count 135 _Mol_residue_sequence ; SNQIYSARYSGVDVYEFIHS TGSIMKRKKDDWVNATHILK AANFAKAKRTRILEKEVLKE THEKVQGGFGKYQGTWVPLN IAKQLAEKFSVYDQLKPLFD FTQTDGSASPPPAPKHHHAS KVDKLAAALEHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 SER 2 3 ASN 3 4 GLN 4 5 ILE 5 6 TYR 6 7 SER 7 8 ALA 8 9 ARG 9 10 TYR 10 11 SER 11 12 GLY 12 13 VAL 13 14 ASP 14 15 VAL 15 16 TYR 16 17 GLU 17 18 PHE 18 19 ILE 19 20 HIS 20 21 SER 21 22 THR 22 23 GLY 23 24 SER 24 25 ILE 25 26 MET 26 27 LYS 27 28 ARG 28 29 LYS 29 30 LYS 30 31 ASP 31 32 ASP 32 33 TRP 33 34 VAL 34 35 ASN 35 36 ALA 36 37 THR 37 38 HIS 38 39 ILE 39 40 LEU 40 41 LYS 41 42 ALA 42 43 ALA 43 44 ASN 44 45 PHE 45 46 ALA 46 47 LYS 47 48 ALA 48 49 LYS 49 50 ARG 50 51 THR 51 52 ARG 52 53 ILE 53 54 LEU 54 55 GLU 55 56 LYS 56 57 GLU 57 58 VAL 58 59 LEU 59 60 LYS 60 61 GLU 61 62 THR 62 63 HIS 63 64 GLU 64 65 LYS 65 66 VAL 66 67 GLN 67 68 GLY 68 69 GLY 69 70 PHE 70 71 GLY 71 72 LYS 72 73 TYR 73 74 GLN 74 75 GLY 75 76 THR 76 77 TRP 77 78 VAL 78 79 PRO 79 80 LEU 80 81 ASN 81 82 ILE 82 83 ALA 83 84 LYS 84 85 GLN 85 86 LEU 86 87 ALA 87 88 GLU 88 89 LYS 89 90 PHE 90 91 SER 91 92 VAL 92 93 TYR 93 94 ASP 94 95 GLN 95 96 LEU 96 97 LYS 97 98 PRO 98 99 LEU 99 100 PHE 100 101 ASP 101 102 PHE 102 103 THR 103 104 GLN 104 105 THR 105 106 ASP 106 107 GLY 107 108 SER 108 109 ALA 109 110 SER 110 111 PRO 111 112 PRO 112 113 PRO 113 114 ALA 114 115 PRO 115 116 LYS 116 117 HIS 117 118 HIS 118 119 HIS 119 120 ALA 120 121 SER 121 122 LYS 122 123 VAL 123 124 ASP 124 125 LYS 125 126 LEU 126 127 ALA 127 128 ALA 128 129 ALA 129 130 LEU 130 131 GLU 131 132 HIS 132 133 HIS 133 134 HIS 134 135 HIS 135 136 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 4256 "MLU1-BOX binding protein" 100.00 135 100.00 100.00 5.84e-94 PDB 1BM8 "Dna-Binding Domain Of Mbp1" 73.33 99 100.00 100.00 7.25e-66 PDB 1L3G "Nmr Structure Of The Dna-Binding Domain Of Cell Cycle Protein, Mbp1(2-124) From Saccharomyces Cerevisiae" 99.26 136 100.00 100.00 4.60e-93 DBJ GAA22190 "K7_Mbp1p [Saccharomyces cerevisiae Kyokai no. 7]" 91.85 833 98.39 100.00 2.95e-80 EMBL CAA52271 "mbp1 transcription factor [Saccharomyces cerevisiae]" 91.85 833 99.19 100.00 5.29e-81 EMBL CAA98618 "MBP1 [Saccharomyces cerevisiae]" 91.85 833 99.19 100.00 5.29e-81 EMBL CAY78452 "Mbp1p [Saccharomyces cerevisiae EC1118]" 91.85 833 98.39 99.19 6.80e-80 GB AAS64332 "transcription factor MBP1, partial [Saccharomyces cerevisiae]" 94.07 314 97.64 98.43 1.44e-85 GB AAS64333 "transcription factor MBP1, partial [Saccharomyces cerevisiae]" 94.07 314 97.64 98.43 1.35e-85 GB AAS64335 "transcription factor MBP1, partial [Saccharomyces cerevisiae]" 94.07 314 97.64 98.43 1.35e-85 GB AAS64336 "transcription factor MBP1, partial [Saccharomyces cerevisiae]" 94.07 314 97.64 98.43 1.35e-85 GB AAS64338 "transcription factor MBP1, partial [Saccharomyces cerevisiae]" 94.07 314 97.64 98.43 1.44e-85 REF NP_010227 "transcription factor MBP1 [Saccharomyces cerevisiae S288c]" 91.85 833 99.19 100.00 5.29e-81 SP P39678 "RecName: Full=Transcription factor MBP1; AltName: Full=MBF subunit p120" 91.85 833 99.19 100.00 5.29e-81 TPG DAA11800 "TPA: transcription factor MBP1 [Saccharomyces cerevisiae S288c]" 91.85 833 99.19 100.00 5.29e-81 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Organelle $Mbp1 'Baker's yeast' 4932 Eukaryota Fungi Saccharomyces cerevisiae Bl21/De3 nucleus 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 $Mbp1 'recombinant technology' . . . . plasmid pET22B 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 $Mbp1 . mM 0.8 1.3 [U-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 $Mbp1 . mM 0.8 1.3 [U-15N;U-13C] stop_ save_ save_sample_three _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Mbp1 . mM 0.8 1.3 . stop_ save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.6 0.2 n/a temperature 288 1.0 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one $sample_two $sample_three stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name Mbp1 _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 . 2 ASN CA C 53.208 . 1 2 . 2 ASN CB C 38.721 . 1 3 . 2 ASN HD21 H 7.669 . 1 4 . 2 ASN HD22 H 7.012 . 1 5 . 2 ASN ND2 N 113.523 . 1 6 . 3 GLN CA C 55.74 . 1 7 . 3 GLN CB C 29.611 . 1 8 . 3 GLN CG C 33.811 . 1 9 . 3 GLN H H 8.452 . 1 10 . 3 GLN HA H 4.135 . 1 11 . 3 GLN HB2 H 2.133 . 1 12 . 3 GLN HB3 H 1.937 . 1 13 . 3 GLN HE21 H 7.518 . 1 14 . 3 GLN HE22 H 6.983 . 1 15 . 3 GLN HG2 H 2.754 . 1 16 . 3 GLN HG3 H 2.754 . 1 17 . 3 GLN N N 119.773 . 1 18 . 3 GLN NE2 N 113.411 . 1 19 . 4 ILE CA C 59.413 . 1 20 . 4 ILE CB C 38.23 . 1 21 . 4 ILE H H 7.396 . 1 22 . 4 ILE HA H 4.601 . 1 23 . 4 ILE HB H 1.923 . 1 24 . 4 ILE HD1 H 0.111 . 1 25 . 4 ILE HG12 H 1.053 . 1 26 . 4 ILE HG13 H 1.053 . 1 27 . 4 ILE N N 120.876 . 1 28 . 5 TYR CA C 56.299 . 1 29 . 5 TYR CB C 41.655 . 1 30 . 5 TYR H H 8.83 . 1 31 . 5 TYR HA H 5.16 . 1 32 . 5 TYR HB2 H 3.31 . 1 33 . 5 TYR HB3 H 2.685 . 1 34 . 5 TYR N N 124.747 . 1 35 . 6 SER CA C 58.052 . 1 36 . 6 SER CB C 64.741 . 1 37 . 6 SER H H 8.877 . 1 38 . 6 SER HA H 5.24 . 1 39 . 6 SER HB2 H 3.855 . 1 40 . 6 SER HB3 H 3.855 . 1 41 . 6 SER N N 116.423 . 1 42 . 7 ALA CA C 51.529 . 1 43 . 7 ALA CB C 23.813 . 1 44 . 7 ALA H H 8.774 . 1 45 . 7 ALA HA H 4.528 . 1 46 . 7 ALA HB H 1.303 . 1 47 . 7 ALA N N 125.857 . 1 48 . 8 ARG CA C 55.246 . 1 49 . 8 ARG CB C 32.802 . 1 50 . 8 ARG H H 7.922 . 1 51 . 8 ARG HA H 5.082 . 1 52 . 8 ARG HB2 H 1.561 . 1 53 . 8 ARG HB3 H 1.352 . 1 54 . 8 ARG HG2 H 1.073 . 1 55 . 8 ARG HG3 H 1.073 . 1 56 . 8 ARG N N 121.695 . 1 57 . 10 SER CA C 58.257 . 1 58 . 10 SER CB C 61.88 . 1 59 . 11 GLY CA C 44.717 . 1 60 . 11 GLY H H 8.502 . 1 61 . 11 GLY HA2 H 4.008 . 1 62 . 11 GLY HA3 H 3.341 . 1 63 . 11 GLY N N 103.406 . 1 64 . 12 VAL CA C 61.931 . 1 65 . 12 VAL CB C 33.015 . 1 66 . 12 VAL H H 7.934 . 1 67 . 12 VAL HA H 3.905 . 1 68 . 12 VAL HB H 2.046 . 1 69 . 12 VAL HG1 H 0.779 . 1 70 . 12 VAL HG2 H 0.612 . 1 71 . 12 VAL N N 122.805 . 1 72 . 13 ASP CA C 54.824 . 1 73 . 13 ASP CB C 41.741 . 1 74 . 13 ASP H H 8.152 . 1 75 . 13 ASP HA H 5.128 . 1 76 . 13 ASP HB2 H 2.636 . 1 77 . 13 ASP HB3 H 2.445 . 1 78 . 13 ASP N N 125.857 . 1 79 . 14 VAL CA C 58.863 . 1 80 . 14 VAL CB C 36.208 . 1 81 . 14 VAL H H 9.437 . 1 82 . 14 VAL HA H 5.214 . 1 83 . 14 VAL N N 117.255 . 1 84 . 15 TYR CA C 55.789 . 1 85 . 15 TYR CB C 39.606 . 1 86 . 15 TYR H H 9.665 . 1 87 . 15 TYR HA H 5.552 . 1 88 . 15 TYR HB2 H 2.801 . 1 89 . 15 TYR HB3 H 2.801 . 1 90 . 15 TYR N N 120.307 . 1 91 . 16 GLU CA C 55.19 . 1 92 . 16 GLU CB C 33.177 . 1 93 . 16 GLU H H 9.635 . 1 94 . 16 GLU HA H 4.979 . 1 95 . 16 GLU HB2 H 1.943 . 1 96 . 16 GLU HB3 H 1.943 . 1 97 . 16 GLU N N 125.024 . 1 98 . 17 PHE CA C 54.3 . 1 99 . 17 PHE CB C 42.957 . 1 100 . 17 PHE H H 9.353 . 1 101 . 17 PHE HA H 5.413 . 1 102 . 17 PHE HB2 H 3.144 . 1 103 . 17 PHE HB3 H 3.144 . 1 104 . 17 PHE N N 127.244 . 1 105 . 18 ILE CA C 60.435 . 1 106 . 18 ILE CB C 34.965 . 1 107 . 18 ILE H H 8.642 . 1 108 . 18 ILE HA H 3.955 . 1 109 . 18 ILE HB H 1.975 . 1 110 . 18 ILE N N 128.354 . 1 111 . 19 HIS CA C 55.37 . 1 112 . 19 HIS CB C 33.602 . 1 113 . 19 HIS H H 7.959 . 1 114 . 19 HIS HA H 4.437 . 1 115 . 19 HIS HB2 H 3.184 . 1 116 . 19 HIS HB3 H 2.735 . 1 117 . 19 HIS N N 129.189 . 1 118 . 20 SER CA C 61.627 . 1 119 . 20 SER H H 7.448 . 1 120 . 20 SER N N 120.862 . 1 121 . 21 THR CA C 62.56 . 1 122 . 21 THR CB C 70.672 . 1 123 . 21 THR H H 8.357 . 1 124 . 21 THR HA H 4.322 . 1 125 . 21 THR N N 111.151 . 1 126 . 22 GLY CA C 43.891 . 1 127 . 22 GLY H H 7.485 . 1 128 . 22 GLY HA2 H 4.53 . 1 129 . 22 GLY HA3 H 3.643 . 1 130 . 22 GLY N N 110.319 . 1 131 . 23 SER CA C 59.401 . 1 132 . 23 SER CB C 63.659 . 1 133 . 23 SER H H 8.058 . 1 134 . 23 SER HA H 4.906 . 1 135 . 23 SER HB2 H 3.476 . 1 136 . 23 SER HB3 H 3.476 . 1 137 . 23 SER N N 114.481 . 1 138 . 24 ILE CA C 59.429 . 1 139 . 24 ILE CB C 39.232 . 1 140 . 24 ILE H H 9.389 . 1 141 . 24 ILE HA H 4.672 . 1 142 . 24 ILE N N 124.489 . 1 143 . 25 MET CA C 55.212 . 1 144 . 25 MET CB C 38.453 . 1 145 . 25 MET H H 9.37 . 1 146 . 25 MET HA H 6.01 . 1 147 . 25 MET HB2 H 2.228 . 1 148 . 25 MET HB3 H 2.228 . 1 149 . 25 MET N N 126.134 . 1 150 . 26 LYS CA C 54.224 . 1 151 . 26 LYS CB C 38.19 . 1 152 . 26 LYS H H 9.002 . 1 153 . 26 LYS HA H 5.691 . 1 154 . 26 LYS N N 119.752 . 1 155 . 27 ARG CA C 58.65 . 1 156 . 27 ARG CB C 32.91 . 1 157 . 27 ARG H H 10.504 . 1 158 . 27 ARG HA H 4.56 . 1 159 . 27 ARG N N 127.934 . 1 160 . 28 LYS CA C 59.423 . 1 161 . 28 LYS CB C 33.05 . 1 162 . 28 LYS H H 7.991 . 1 163 . 28 LYS HA H 4.112 . 1 164 . 28 LYS HB2 H 1.664 . 1 165 . 28 LYS HB3 H 1.397 . 1 166 . 28 LYS N N 124.211 . 1 167 . 29 LYS CA C 59.116 . 1 168 . 29 LYS CB C 32.339 . 1 169 . 29 LYS H H 9.371 . 1 170 . 29 LYS HA H 4.079 . 1 171 . 29 LYS HB2 H 1.935 . 1 172 . 29 LYS HB3 H 1.601 . 1 173 . 29 LYS N N 115.878 . 1 174 . 30 ASP CA C 52.458 . 1 175 . 30 ASP CB C 41.717 . 1 176 . 30 ASP H H 7.073 . 1 177 . 30 ASP HA H 4.887 . 1 178 . 30 ASP HB2 H 3.162 . 1 179 . 30 ASP HB3 H 2.382 . 1 180 . 30 ASP N N 112.261 . 1 181 . 31 ASP CA C 57.05 . 1 182 . 31 ASP CB C 40.35 . 1 183 . 31 ASP H H 8.221 . 1 184 . 31 ASP HA H 4.839 . 1 185 . 31 ASP HB2 H 3.441 . 1 186 . 31 ASP HB3 H 3.262 . 1 187 . 31 ASP N N 115.868 . 1 188 . 32 TRP CA C 59.255 . 1 189 . 32 TRP CB C 28.599 . 1 190 . 32 TRP H H 8.192 . 1 191 . 32 TRP HA H 5.012 . 1 192 . 32 TRP HB2 H 3.261 . 1 193 . 32 TRP HB3 H 3.053 . 1 194 . 32 TRP HE1 H 10.285 . 1 195 . 32 TRP N N 116.25 . 1 196 . 32 TRP NE1 N 128.714 . 1 197 . 33 VAL CA C 60.124 . 1 198 . 33 VAL CB C 35.634 . 1 199 . 33 VAL H H 9.482 . 1 200 . 33 VAL HA H 5.001 . 1 201 . 33 VAL HB H 1.579 . 1 202 . 33 VAL HG1 H 0.996 . 1 203 . 33 VAL N N 120.036 . 1 204 . 34 ASN CA C 53.039 . 1 205 . 34 ASN CB C 35.766 . 1 206 . 34 ASN H H 6.757 . 1 207 . 34 ASN HA H 3.162 . 1 208 . 34 ASN HD21 H 7.461 . 1 209 . 34 ASN HD22 H 6.954 . 1 210 . 34 ASN N N 125.613 . 1 211 . 34 ASN ND2 N 112.674 . 1 212 . 35 ALA CA C 54.039 . 1 213 . 35 ALA CB C 18.311 . 1 214 . 35 ALA H H 9.284 . 1 215 . 35 ALA HA H 3.863 . 1 216 . 35 ALA HB H 1.265 . 1 217 . 35 ALA N N 130.574 . 1 218 . 36 THR CA C 68.566 . 1 219 . 36 THR CB C 67.056 . 1 220 . 36 THR H H 8.047 . 1 221 . 36 THR HA H 3.628 . 1 222 . 36 THR HB H 4.439 . 1 223 . 36 THR HG2 H 1.275 . 1 224 . 36 THR N N 117.816 . 1 225 . 37 HIS CA C 56.971 . 1 226 . 37 HIS CB C 32.849 . 1 227 . 37 HIS H H 7.177 . 1 228 . 37 HIS HA H 4.321 . 1 229 . 37 HIS HB2 H 3.585 . 1 230 . 37 HIS HB3 H 3.585 . 1 231 . 37 HIS N N 119.198 . 1 232 . 38 ILE CA C 65.669 . 1 233 . 38 ILE CB C 37.287 . 1 234 . 38 ILE H H 7.338 . 1 235 . 38 ILE HA H 3.329 . 1 236 . 38 ILE HB H 2.118 . 1 237 . 38 ILE N N 118.365 . 1 238 . 39 LEU CA C 56.9 . 1 239 . 39 LEU CB C 41.214 . 1 240 . 39 LEU H H 7.841 . 1 241 . 39 LEU HA H 3.88 . 1 242 . 39 LEU HD1 H 0.77 . 1 243 . 39 LEU HD2 H 0.564 . 1 244 . 39 LEU N N 116.145 . 1 245 . 40 LYS CA C 59.882 . 1 246 . 40 LYS CB C 32.35 . 1 247 . 40 LYS H H 8.202 . 1 248 . 40 LYS HA H 4.073 . 1 249 . 40 LYS HB2 H 1.925 . 1 250 . 40 LYS HB3 H 1.925 . 1 251 . 40 LYS N N 119.752 . 1 252 . 41 ALA CA C 53.814 . 1 253 . 41 ALA CB C 16.455 . 1 254 . 41 ALA H H 7.689 . 1 255 . 41 ALA HA H 4.409 . 1 256 . 41 ALA HB H 1.016 . 1 257 . 41 ALA N N 123.637 . 1 258 . 42 ALA CA C 51.338 . 1 259 . 42 ALA CB C 17.58 . 1 260 . 42 ALA H H 7.003 . 1 261 . 42 ALA HA H 4.015 . 1 262 . 42 ALA HB H 0.872 . 1 263 . 42 ALA N N 117.853 . 1 264 . 43 ASN CA C 54.002 . 1 265 . 43 ASN CB C 36.513 . 1 266 . 43 ASN H H 7.945 . 1 267 . 43 ASN HA H 4.296 . 1 268 . 43 ASN HB2 H 3.052 . 1 269 . 43 ASN HB3 H 2.773 . 1 270 . 43 ASN HD21 H 7.528 . 1 271 . 43 ASN HD22 H 6.729 . 1 272 . 43 ASN N N 111.429 . 1 273 . 43 ASN ND2 N 112.675 . 1 274 . 44 PHE CA C 54.949 . 1 275 . 44 PHE CB C 38.897 . 1 276 . 44 PHE H H 7.179 . 1 277 . 44 PHE HA H 4.968 . 1 278 . 44 PHE HB2 H 2.727 . 1 279 . 44 PHE HB3 H 2.727 . 1 280 . 44 PHE N N 116.145 . 1 281 . 45 ALA CA C 51.752 . 1 282 . 45 ALA CB C 19.2 . 1 283 . 45 ALA H H 9.023 . 1 284 . 45 ALA HA H 4.359 . 1 285 . 45 ALA HB H 1.606 . 1 286 . 45 ALA N N 127.522 . 1 287 . 46 LYS H H 8.916 . 1 288 . 46 LYS HA H 4.863 . 1 289 . 46 LYS N N 122.24 . 1 290 . 47 ALA CA C 55.34 . 1 291 . 47 ALA CB C 17.77 . 1 292 . 47 ALA H H 9.223 . 1 293 . 47 ALA N N 118.798 . 1 294 . 48 LYS CA C 58.312 . 1 295 . 48 LYS CB C 32.667 . 1 296 . 48 LYS H H 7.29 . 1 297 . 48 LYS HA H 4.02 . 1 298 . 48 LYS HB2 H 1.83 . 2 299 . 48 LYS N N 118.67 . 1 300 . 49 ARG CA C 60.483 . 1 301 . 49 ARG CB C 30.565 . 1 302 . 49 ARG H H 8.498 . 1 303 . 49 ARG N N 117.255 . 1 304 . 50 THR CA C 66.792 . 1 305 . 50 THR CB C 68.816 . 1 306 . 50 THR H H 8.321 . 1 307 . 50 THR HA H 3.786 . 1 308 . 50 THR HB H 4.198 . 1 309 . 50 THR HG2 H 1.204 . 1 310 . 50 THR N N 114.203 . 1 311 . 51 ARG CA C 58.984 . 1 312 . 51 ARG CB C 29.813 . 1 313 . 51 ARG H H 7.43 . 1 314 . 51 ARG HA H 4.096 . 1 315 . 51 ARG HB2 H 1.895 . 1 316 . 51 ARG HB3 H 1.669 . 1 317 . 51 ARG HD2 H 3.224 . 1 318 . 51 ARG HD3 H 3.224 . 1 319 . 51 ARG N N 120.862 . 1 320 . 52 ILE CA C 64.742 . 1 321 . 52 ILE CB C 37.579 . 1 322 . 52 ILE H H 8.165 . 1 323 . 52 ILE HA H 3.699 . 1 324 . 52 ILE HB H 1.643 . 1 325 . 52 ILE N N 120.03 . 1 326 . 53 LEU CA C 58.267 . 1 327 . 53 LEU CB C 41.079 . 1 328 . 53 LEU H H 8.522 . 1 329 . 53 LEU HA H 3.784 . 1 330 . 53 LEU HD1 H 0.782 . 1 331 . 53 LEU N N 120.307 . 1 332 . 54 GLU CA C 59.175 . 1 333 . 54 GLU CB C 29.506 . 1 334 . 54 GLU H H 8.045 . 1 335 . 54 GLU HA H 3.83 . 1 336 . 54 GLU HB2 H 2.148 . 1 337 . 54 GLU HB3 H 2.01 . 1 338 . 54 GLU N N 117.261 . 1 339 . 55 LYS CA C 57.865 . 1 340 . 55 LYS CB C 33.293 . 1 341 . 55 LYS H H 7.81 . 1 342 . 55 LYS HA H 4.209 . 1 343 . 55 LYS HB2 H 1.946 . 1 344 . 55 LYS HB3 H 1.946 . 1 345 . 55 LYS N N 116.158 . 1 346 . 56 GLU CA C 57.329 . 1 347 . 56 GLU CB C 31.19 . 1 348 . 56 GLU H H 8.55 . 1 349 . 56 GLU HA H 4.482 . 1 350 . 56 GLU HB2 H 1.943 . 1 351 . 56 GLU HB3 H 1.943 . 1 352 . 56 GLU N N 114.481 . 1 353 . 57 VAL CA C 63.531 . 1 354 . 57 VAL CB C 32.371 . 1 355 . 57 VAL H H 7.925 . 1 356 . 57 VAL HA H 4.086 . 1 357 . 57 VAL HB H 2.145 . 1 358 . 57 VAL HG1 H 0.747 . 1 359 . 57 VAL HG2 H 0.64 . 1 360 . 57 VAL N N 115.313 . 1 361 . 58 LEU CA C 57.017 . 1 362 . 58 LEU CB C 40.808 . 1 363 . 58 LEU H H 7.561 . 1 364 . 58 LEU HA H 3.522 . 1 365 . 58 LEU N N 118.643 . 1 366 . 59 LYS CA C 56.201 . 1 367 . 59 LYS CB C 31.95 . 1 368 . 59 LYS H H 7.669 . 1 369 . 59 LYS HA H 4.332 . 1 370 . 59 LYS HG2 H 1.323 . 1 371 . 59 LYS HG3 H 1.323 . 1 372 . 59 LYS N N 114.505 . 1 373 . 60 GLU CA C 53.545 . 1 374 . 60 GLU CB C 31.396 . 1 375 . 60 GLU H H 7.851 . 1 376 . 60 GLU HA H 4.788 . 1 377 . 60 GLU HB2 H 2.259 . 1 378 . 60 GLU HB3 H 1.927 . 1 379 . 60 GLU N N 120.019 . 1 380 . 61 THR CA C 64.108 . 1 381 . 61 THR CB C 69.366 . 1 382 . 61 THR H H 8.807 . 1 383 . 61 THR HA H 4.164 . 1 384 . 61 THR HB H 3.872 . 1 385 . 61 THR N N 120.03 . 1 386 . 62 HIS CA C 56.416 . 1 387 . 62 HIS CB C 31.028 . 1 388 . 62 HIS H H 8.095 . 1 389 . 62 HIS HA H 5.527 . 1 390 . 62 HIS N N 117.81 . 1 391 . 63 GLU CA C 55.46 . 1 392 . 63 GLU CB C 33.813 . 1 393 . 63 GLU H H 9.609 . 1 394 . 63 GLU HA H 4.695 . 1 395 . 63 GLU HB2 H 2.08 . 1 396 . 63 GLU HB3 H 2.08 . 1 397 . 63 GLU N N 120.586 . 1 398 . 64 LYS CA C 56.397 . 1 399 . 64 LYS CB C 33.175 . 1 400 . 64 LYS H H 9.475 . 1 401 . 64 LYS N N 127.522 . 1 402 . 65 VAL H H 9.126 . 1 403 . 65 VAL HA H 4.327 . 1 404 . 65 VAL HB H 2.23 . 1 405 . 65 VAL HG2 H 0.703 . 1 406 . 65 VAL N N 127.799 . 1 407 . 66 GLN CA C 54.813 . 1 408 . 66 GLN CB C 30.821 . 1 409 . 66 GLN CG C 33.979 . 1 410 . 66 GLN HE21 H 7.684 . 1 411 . 66 GLN HE22 H 6.995 . 1 412 . 66 GLN NE2 N 112.407 . 1 413 . 67 GLY CA C 44.669 . 1 414 . 67 GLY H H 8.035 . 1 415 . 67 GLY HA2 H 4.127 . 1 416 . 67 GLY HA3 H 4.005 . 1 417 . 67 GLY N N 108.694 . 1 418 . 68 GLY CA C 44.599 . 1 419 . 68 GLY H H 8.365 . 1 420 . 68 GLY HA2 H 4.108 . 1 421 . 68 GLY HA3 H 3.884 . 1 422 . 68 GLY N N 107.267 . 1 423 . 69 PHE CA C 58.156 . 1 424 . 69 PHE CB C 39.561 . 1 425 . 69 PHE H H 8.709 . 1 426 . 69 PHE HA H 4.591 . 1 427 . 69 PHE HB2 H 3.254 . 1 428 . 69 PHE HB3 H 3.015 . 1 429 . 69 PHE N N 120.585 . 1 430 . 70 GLY CA C 47.47 . 1 431 . 70 GLY HA2 H 4.05 . 1 432 . 70 GLY HA3 H 3.69 . 1 433 . 72 TYR CA C 58.312 . 1 434 . 72 TYR CB C 40.909 . 1 435 . 73 GLN CA C 56.678 . 1 436 . 73 GLN CB C 29.816 . 1 437 . 73 GLN CG C 34.247 . 1 438 . 73 GLN H H 7.006 . 1 439 . 73 GLN HA H 3.854 . 1 440 . 73 GLN HB2 H 2.284 . 1 441 . 73 GLN HB3 H 2.284 . 1 442 . 73 GLN HE21 H 7.303 . 1 443 . 73 GLN HE22 H 6.924 . 1 444 . 73 GLN N N 113.923 . 1 445 . 73 GLN NE2 N 111.429 . 1 446 . 74 GLY CA C 44.426 . 1 447 . 74 GLY H H 8.662 . 1 448 . 74 GLY HA2 H 4.536 . 1 449 . 74 GLY HA3 H 3.917 . 1 450 . 74 GLY N N 108.376 . 1 451 . 75 THR CA C 62.418 . 1 452 . 75 THR CB C 69.212 . 1 453 . 75 THR H H 7.868 . 1 454 . 75 THR HA H 5.052 . 1 455 . 75 THR HB H 3.792 . 1 456 . 75 THR HG2 H 1.018 . 1 457 . 75 THR N N 118.365 . 1 458 . 76 TRP CA C 56.578 . 1 459 . 76 TRP CB C 30.171 . 1 460 . 76 TRP H H 9.872 . 1 461 . 76 TRP HA H 5.195 . 1 462 . 76 TRP HB2 H 3.378 . 1 463 . 76 TRP HB3 H 3.378 . 1 464 . 76 TRP HE1 H 8.63 . 1 465 . 76 TRP N N 129.777 . 1 466 . 76 TRP NE1 N 127.27 . 1 467 . 77 VAL CA C 57.358 . 1 468 . 77 VAL CB C 33.876 . 1 469 . 77 VAL H H 9.289 . 1 470 . 77 VAL HA H 4.716 . 1 471 . 77 VAL N N 113.144 . 1 472 . 78 PRO CA C 61.552 . 1 473 . 78 PRO CB C 32.468 . 1 474 . 79 LEU CA C 58.858 . 1 475 . 79 LEU CB C 40.987 . 1 476 . 79 LEU H H 8.689 . 1 477 . 79 LEU HA H 3.945 . 1 478 . 79 LEU N N 123.637 . 1 479 . 80 ASN CA C 56.651 . 1 480 . 80 ASN CB C 36.325 . 1 481 . 80 ASN H H 8.759 . 1 482 . 80 ASN HA H 4.212 . 1 483 . 80 ASN HB2 H 2.73 . 1 484 . 80 ASN HB3 H 2.73 . 1 485 . 80 ASN HD21 H 7.736 . 1 486 . 80 ASN HD22 H 6.971 . 1 487 . 80 ASN N N 113.104 . 1 488 . 80 ASN ND2 N 114.621 . 1 489 . 81 ILE CA C 62.074 . 1 490 . 81 ILE CB C 36.483 . 1 491 . 81 ILE H H 6.919 . 1 492 . 81 ILE HA H 3.758 . 1 493 . 81 ILE HB H 1.856 . 1 494 . 81 ILE N N 121.976 . 1 495 . 82 ALA CA C 55.209 . 1 496 . 82 ALA CB C 18.853 . 1 497 . 82 ALA H H 8.3 . 1 498 . 82 ALA HA H 3.664 . 1 499 . 82 ALA HB H 1.42 . 1 500 . 82 ALA N N 123.927 . 1 501 . 83 LYS CA C 60.433 . 1 502 . 83 LYS CB C 32.549 . 1 503 . 83 LYS H H 8.514 . 1 504 . 83 LYS HA H 3.462 . 1 505 . 83 LYS N N 117.273 . 1 506 . 84 GLN CA C 58.842 . 1 507 . 84 GLN CB C 28.431 . 1 508 . 84 GLN CG C 34.06 . 1 509 . 84 GLN H H 7.238 . 1 510 . 84 GLN HA H 4.047 . 1 511 . 84 GLN HB2 H 2.331 . 1 512 . 84 GLN HB3 H 2.155 . 1 513 . 84 GLN HE21 H 7.385 . 1 514 . 84 GLN HE22 H 6.875 . 1 515 . 84 GLN HG2 H 2.522 . 1 516 . 84 GLN HG3 H 2.522 . 1 517 . 84 GLN N N 118.106 . 1 518 . 84 GLN NE2 N 111.18 . 1 519 . 85 LEU CA C 57.539 . 1 520 . 85 LEU CB C 42.841 . 1 521 . 85 LEU H H 8.409 . 1 522 . 85 LEU HA H 4.071 . 1 523 . 85 LEU HB2 H 1.858 . 1 524 . 85 LEU HB3 H 1.858 . 1 525 . 85 LEU N N 121.486 . 1 526 . 86 ALA CA C 54.32 . 1 527 . 86 ALA CB C 18.253 . 1 528 . 86 ALA H H 8.612 . 1 529 . 86 ALA HA H 3.91 . 1 530 . 86 ALA HB H 1.587 . 1 531 . 86 ALA N N 118.365 . 1 532 . 87 GLU CA C 59.418 . 1 533 . 87 GLU CB C 29.58 . 1 534 . 87 GLU H H 8.496 . 1 535 . 87 GLU HA H 4.154 . 1 536 . 87 GLU HB2 H 1.918 . 1 537 . 87 GLU HB3 H 2.102 . 1 538 . 87 GLU N N 118.088 . 1 539 . 88 LYS CA C 59.37 . 1 540 . 88 LYS CB C 31.703 . 1 541 . 88 LYS H H 8.152 . 1 542 . 88 LYS HA H 3.832 . 1 543 . 88 LYS N N 121.972 . 1 544 . 89 PHE CA C 57.333 . 1 545 . 89 PHE CB C 37.67 . 1 546 . 89 PHE H H 7.5 . 1 547 . 89 PHE HA H 5.019 . 1 548 . 89 PHE HB2 H 3.654 . 1 549 . 89 PHE HB3 H 2.425 . 1 550 . 89 PHE N N 113.937 . 1 551 . 90 SER CA C 59.543 . 1 552 . 90 SER CB C 61.219 . 1 553 . 90 SER H H 7.732 . 1 554 . 90 SER HA H 4.356 . 1 555 . 90 SER HB2 H 4.26 . 1 556 . 90 SER HB3 H 4.097 . 1 557 . 90 SER N N 110.041 . 1 558 . 91 VAL CA C 59.642 . 1 559 . 91 VAL CB C 32.76 . 1 560 . 91 VAL H H 8.629 . 1 561 . 91 VAL HA H 4.917 . 1 562 . 91 VAL HB H 2.326 . 1 563 . 91 VAL N N 108.099 . 1 564 . 92 TYR CA C 62.919 . 1 565 . 92 TYR CB C 38.222 . 1 566 . 92 TYR H H 7.705 . 1 567 . 92 TYR HA H 3.74 . 1 568 . 92 TYR HB2 H 3.071 . 1 569 . 92 TYR HB3 H 2.61 . 1 570 . 92 TYR N N 124.207 . 1 571 . 93 ASP CA C 57.518 . 1 572 . 93 ASP CB C 39.526 . 1 573 . 93 ASP H H 8.633 . 1 574 . 93 ASP HA H 4.074 . 1 575 . 93 ASP HB2 H 2.648 . 1 576 . 93 ASP HB3 H 2.648 . 1 577 . 93 ASP N N 116.466 . 1 578 . 94 GLN CA C 57.7 . 1 579 . 94 GLN CB C 29.613 . 1 580 . 94 GLN CG C 34.325 . 1 581 . 94 GLN H H 7.586 . 1 582 . 94 GLN HA H 4.114 . 1 583 . 94 GLN HB2 H 2.155 . 1 584 . 94 GLN HB3 H 1.985 . 1 585 . 94 GLN HE21 H 7.932 . 1 586 . 94 GLN HE22 H 7.207 . 1 587 . 94 GLN HG2 H 2.523 . 1 588 . 94 GLN HG3 H 2.523 . 1 589 . 94 GLN N N 115.59 . 1 590 . 94 GLN NE2 N 113.359 . 1 591 . 95 LEU CA C 54.025 . 1 592 . 95 LEU CB C 42.33 . 1 593 . 95 LEU H H 7.099 . 1 594 . 95 LEU HA H 3.954 . 1 595 . 95 LEU HD1 H 0.832 . 1 596 . 95 LEU HD2 H 0.512 . 1 597 . 95 LEU N N 115.868 . 1 598 . 96 LYS CA C 61.27 . 1 599 . 96 LYS CB C 30.614 . 1 600 . 96 LYS H H 7.563 . 1 601 . 96 LYS HA H 3.553 . 1 602 . 96 LYS HB2 H 1.593 . 1 603 . 96 LYS HB3 H 1.593 . 1 604 . 96 LYS N N 123.933 . 1 605 . 97 PRO CA C 65.788 . 1 606 . 97 PRO CB C 30.915 . 1 607 . 98 LEU CA C 56.216 . 1 608 . 98 LEU CB C 41.167 . 1 609 . 98 LEU H H 6.776 . 1 610 . 98 LEU HA H 3.926 . 1 611 . 98 LEU N N 113.961 . 1 612 . 99 PHE CA C 60.004 . 1 613 . 99 PHE CB C 37.43 . 1 614 . 99 PHE H H 7.49 . 1 615 . 99 PHE HA H 4.091 . 1 616 . 99 PHE HB2 H 3.098 . 1 617 . 99 PHE HB3 H 3.098 . 1 618 . 99 PHE N N 118.088 . 1 619 . 100 ASP CA C 55.206 . 1 620 . 100 ASP CB C 40.633 . 1 621 . 100 ASP H H 8.582 . 1 622 . 100 ASP HA H 4.369 . 1 623 . 100 ASP HB2 H 2.678 . 1 624 . 100 ASP HB3 H 2.464 . 1 625 . 100 ASP N N 115.868 . 1 626 . 101 PHE CA C 61.103 . 1 627 . 101 PHE CB C 39.263 . 1 628 . 101 PHE H H 7.151 . 1 629 . 101 PHE HA H 4.008 . 1 630 . 101 PHE HB2 H 2.501 . 1 631 . 101 PHE HB3 H 2.501 . 1 632 . 101 PHE N N 120.603 . 1 633 . 102 THR CA C 60.054 . 1 634 . 102 THR CB C 70.763 . 1 635 . 102 THR H H 7.416 . 1 636 . 102 THR HA H 4.25 . 1 637 . 102 THR HB H 4.053 . 1 638 . 102 THR HG2 H 1.042 . 1 639 . 102 THR N N 121.714 . 1 640 . 103 GLN CA C 55.432 . 1 641 . 103 GLN CB C 30.243 . 1 642 . 103 GLN CG C 34.139 . 1 643 . 103 GLN H H 8.282 . 1 644 . 103 GLN HA H 4.351 . 1 645 . 103 GLN HB2 H 2.26 . 1 646 . 103 GLN HB3 H 1.553 . 1 647 . 103 GLN HE21 H 7.621 . 1 648 . 103 GLN HE22 H 7.063 . 1 649 . 103 GLN HG2 H 2.343 . 1 650 . 103 GLN HG3 H 2.343 . 1 651 . 103 GLN N N 122.242 . 1 652 . 103 GLN NE2 N 112.816 . 1 653 . 104 THR CA C 62.116 . 1 654 . 104 THR CB C 69.704 . 1 655 . 104 THR H H 8.43 . 1 656 . 104 THR HA H 4.37 . 1 657 . 104 THR HB H 4.33 . 1 658 . 104 THR HG2 H 1.21 . 1 659 . 104 THR N N 117.55 . 1 660 . 105 ASP CA C 54.578 . 1 661 . 105 ASP CB C 40.71 . 1 662 . 105 ASP H H 8.363 . 1 663 . 105 ASP HA H 4.561 . 1 664 . 105 ASP HB2 H 2.683 . 1 665 . 105 ASP HB3 H 2.683 . 1 666 . 105 ASP N N 122.527 . 1 667 . 106 GLY CA C 45.281 . 1 668 . 106 GLY H H 8.496 . 1 669 . 106 GLY HA2 H 3.984 . 1 670 . 106 GLY N N 110.327 . 1 671 . 107 SER CA C 58.651 . 1 672 . 107 SER CB C 64.259 . 1 673 . 107 SER H H 8.069 . 1 674 . 107 SER HA H 4.428 . 1 675 . 107 SER HB2 H 3.905 . 1 676 . 107 SER HB3 H 3.905 . 1 677 . 107 SER N N 116.455 . 1 678 . 108 ALA CA C 52.072 . 1 679 . 108 ALA CB C 19.245 . 1 680 . 108 ALA H H 8.456 . 1 681 . 108 ALA HB H 1.38 . 2 682 . 108 ALA N N 125.579 . 1 683 . 109 SER CA C 56.658 . 1 684 . 109 SER CB C 62.967 . 1 685 . 109 SER H H 8.52 . 1 686 . 109 SER N N 117.255 . 1 687 . 112 PRO CA C 62.177 . 1 688 . 112 PRO CB C 31.7 . 1 689 . 113 ALA CA C 50.266 . 1 690 . 113 ALA CB C 17.217 . 1 691 . 113 ALA H H 8.411 . 1 692 . 113 ALA HA H 3.969 . 1 693 . 113 ALA HB H 1.108 . 2 694 . 113 ALA N N 125.002 . 1 695 . 114 PRO CA C 62.567 . 1 696 . 114 PRO CB C 31.954 . 1 697 . 115 LYS CA C 56.243 . 1 698 . 115 LYS CB C 32.806 . 1 699 . 115 LYS H H 8.421 . 1 700 . 115 LYS HA H 4.141 . 1 701 . 115 LYS HB2 H 1.639 . 1 702 . 115 LYS HB3 H 1.335 . 1 703 . 115 LYS N N 121.722 . 1 704 . 117 HIS CA C 56.205 . 1 705 . 117 HIS CB C 30.259 . 1 706 . 118 HIS CA C 56.303 . 1 707 . 118 HIS CB C 30.859 . 1 708 . 118 HIS H H 8.262 . 1 709 . 118 HIS HA H 4.839 . 1 710 . 118 HIS HB2 H 3 . 1 711 . 118 HIS HB3 H 3 . 1 712 . 118 HIS N N 119.781 . 1 713 . 119 ALA CA C 52.496 . 1 714 . 119 ALA CB C 19.035 . 1 715 . 119 ALA H H 8.364 . 1 716 . 119 ALA HA H 4.397 . 1 717 . 119 ALA HB H 1.381 . 1 718 . 119 ALA N N 125.857 . 1 719 . 120 SER CA C 58.257 . 1 720 . 120 SER CB C 63.547 . 1 721 . 120 SER H H 8.354 . 1 722 . 120 SER N N 114.942 . 1 723 . 121 LYS CA C 56.435 . 1 724 . 121 LYS CB C 32.76 . 1 725 . 121 LYS H H 8.462 . 1 726 . 121 LYS HA H 4.3 . 1 727 . 121 LYS N N 123.65 . 1 728 . 122 VAL CA C 62.404 . 1 729 . 122 VAL CB C 32.651 . 1 730 . 122 VAL H H 8.138 . 1 731 . 122 VAL HA H 4.016 . 1 732 . 122 VAL HB H 2.021 . 1 733 . 122 VAL HG1 H 0.887 . 1 734 . 122 VAL N N 120.889 . 1 735 . 123 ASP CA C 54.286 . 1 736 . 123 ASP CB C 41.041 . 1 737 . 123 ASP H H 8.377 . 1 738 . 123 ASP HA H 4.578 . 1 739 . 123 ASP HB2 H 2.65 . 1 740 . 123 ASP HB3 H 2.65 . 1 741 . 123 ASP N N 124.492 . 1 742 . 124 LYS CA C 56.991 . 1 743 . 124 LYS CB C 32.677 . 1 744 . 124 LYS H H 8.356 . 1 745 . 124 LYS HA H 4.173 . 1 746 . 124 LYS HB2 H 1.784 . 1 747 . 124 LYS HB3 H 1.784 . 1 748 . 124 LYS N N 122.535 . 1 749 . 125 LEU CA C 55.527 . 1 750 . 125 LEU CB C 41.767 . 1 751 . 125 LEU H H 8.236 . 1 752 . 125 LEU HA H 4.269 . 1 753 . 125 LEU HB2 H 1.708 . 1 754 . 125 LEU HB3 H 1.708 . 1 755 . 125 LEU HD1 H 0.881 . 1 756 . 125 LEU HG H 1.564 . 1 757 . 125 LEU N N 122.25 . 1 758 . 126 ALA CA C 52.892 . 1 759 . 126 ALA CB C 18.872 . 1 760 . 126 ALA H H 8.068 . 1 761 . 126 ALA HA H 4.183 . 1 762 . 126 ALA HB H 1.387 . 1 763 . 126 ALA N N 123.975 . 1 764 . 127 ALA CA C 52.615 . 1 765 . 127 ALA CB C 18.823 . 1 766 . 127 ALA H H 8.065 . 1 767 . 127 ALA HA H 4.251 . 1 768 . 127 ALA HB H 1.396 . 1 769 . 127 ALA N N 121.972 . 1 770 . 128 ALA CA C 52.695 . 1 771 . 128 ALA CB C 18.826 . 1 772 . 128 ALA H H 8.149 . 1 773 . 128 ALA HA H 4.216 . 1 774 . 128 ALA HB H 1.373 . 1 775 . 128 ALA N N 122.503 . 1 776 . 129 LEU CA C 55.235 . 1 777 . 129 LEU CB C 42.12 . 1 778 . 129 LEU H H 8.038 . 1 779 . 129 LEU HA H 4.235 . 1 780 . 129 LEU HB2 H 1.646 . 1 781 . 129 LEU HB3 H 1.503 . 1 782 . 129 LEU HD1 H 0.864 . 1 783 . 129 LEU N N 120.579 . 1 784 . 130 GLU CA C 56.453 . 1 785 . 130 GLU CB C 30.237 . 1 786 . 130 GLU H H 8.172 . 1 787 . 130 GLU HA H 4.162 . 1 788 . 130 GLU HB2 H 2.155 . 1 789 . 130 GLU HB3 H 1.88 . 1 790 . 130 GLU N N 120.585 . 1 stop_ save_