data_4147 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Resonance Assignment and Secondary Structure of the Cold Shock Domain of the Human YB-1 Protein ; _BMRB_accession_number 4147 _BMRB_flat_file_name bmr4147.str _Entry_type original _Submission_date 1998-06-04 _Accession_date 1998-06-04 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; The data reported here represent the single stranded DNA binding cold shock domain fragment (methionine plus residues 52-129) of the human Y box protein YB1 ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kloks Cathelijne P.A.M. . 2 Hoffmann Astrid . . 3 Omichinski James G. . 4 Vuister Geerten W. . 5 Hilbers Cornelis W. . 6 Grzesiek Stephan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 367 "13C chemical shifts" 285 "15N chemical shifts" 71 "coupling constants" 70 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-02-07 update author 'new chemical shifts added to the file' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Kloks, C.P.A.M., Hoffmann, A., Omichinski, J. G., Vuister, G. W., Hilbers, C. W., Grzesiek, S., "Resonance Assignment and Secondary Structure of the Cold Shock Domain of the Human YB-1 Protein," J. Biomol. NMR. 12, 463-464 (1998). ; _Citation_title ; Resonance Assignment and Secondary Structure of the Cold Shock Domain of the Human YB-1 Protein ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99052121 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kloks Cathelijne P.A.M. . 2 Hoffmann Astrid . . 3 Omichinski James G. . 4 Vuister Geerten W. . 5 Hilbers Cornelis W. . 6 Grzesiek Stephan . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 12 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 463 _Page_last 464 _Year 1998 _Details . loop_ _Keyword 'cold shock domain' 'NMR assignments' 'OB fold' 'Y-box protein' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full 'Bax, A. and Subramanian, S. J. Magn. Reson., 67, 565-570 (1986).' _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_YB1-CSD _Saveframe_category molecular_system _Mol_system_name 'Cold Shock domain' _Abbreviation_common YB1-CSD _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label YB1-CSD $YB1-CSD stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_YB1-CSD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Cold Shock domain' _Abbreviation_common YB1-CSD _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 79 _Mol_residue_sequence ; MKKVIATKVLGTVKWFNVRN GYGFINRNDTKEDVFVHQTA IKKNNPRKYLRSVGDGETVE FDVVEGEKGAEAANVTGPG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 LYS 4 VAL 5 ILE 6 ALA 7 THR 8 LYS 9 VAL 10 LEU 11 GLY 12 THR 13 VAL 14 LYS 15 TRP 16 PHE 17 ASN 18 VAL 19 ARG 20 ASN 21 GLY 22 TYR 23 GLY 24 PHE 25 ILE 26 ASN 27 ARG 28 ASN 29 ASP 30 THR 31 LYS 32 GLU 33 ASP 34 VAL 35 PHE 36 VAL 37 HIS 38 GLN 39 THR 40 ALA 41 ILE 42 LYS 43 LYS 44 ASN 45 ASN 46 PRO 47 ARG 48 LYS 49 TYR 50 LEU 51 ARG 52 SER 53 VAL 54 GLY 55 ASP 56 GLY 57 GLU 58 THR 59 VAL 60 GLU 61 PHE 62 ASP 63 VAL 64 VAL 65 GLU 66 GLY 67 GLU 68 LYS 69 GLY 70 ALA 71 GLU 72 ALA 73 ALA 74 ASN 75 VAL 76 THR 77 GLY 78 PRO 79 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-29 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 17225 CSD 100.00 79 100.00 100.00 2.29e-48 PDB 1H95 "Solution Structure Of The Single-Stranded Dna-Binding Cold Shock Domain (Csd) Of Human Y-Box Protein 1 (Yb1) Determined By Nmr " 100.00 79 100.00 100.00 2.29e-48 DBJ BAA02569 "DNA binding protein B [Rattus sp.]" 98.73 322 100.00 100.00 4.70e-47 DBJ BAA03376 "dbpA murine homologue [Mus musculus domesticus]" 97.47 308 98.70 100.00 9.06e-43 DBJ BAA05380 "unnamed protein product [Gallus gallus]" 98.73 326 100.00 100.00 7.18e-47 DBJ BAA19849 "Y box protein 1 [Carassius auratus]" 98.73 311 100.00 100.00 6.21e-47 DBJ BAC45236 "Y-box binding protein [Oryzias latipes]" 98.73 306 100.00 100.00 7.52e-47 EMBL CAA40847 "Y box-binbing protein [Mus musculus]" 98.73 321 100.00 100.00 4.09e-47 EMBL CAA42778 "YB3 [Xenopus laevis]" 98.73 305 100.00 100.00 6.89e-47 EMBL CAA51261 "cold shock domain protein A [Homo sapiens]" 97.47 372 98.70 100.00 5.77e-46 EMBL CAA64631 "DNA-binding protein [Homo sapiens]" 97.47 372 98.70 100.00 5.77e-46 EMBL CAB46826 "DNA binding protein [Canis lupus familiaris]" 78.48 96 98.39 100.00 1.23e-34 GB AAA02573 "YB-1 protein [Gallus gallus]" 98.73 321 100.00 100.00 5.39e-47 GB AAA20871 "similar to dbpB protein [Homo sapiens]" 98.73 324 100.00 100.00 5.31e-47 GB AAA21677 "transcription factor EF1(A) [Bos taurus]" 72.15 110 100.00 100.00 5.88e-33 GB AAA30497 "transcription factor EF1(A) [Bos taurus]" 98.73 324 100.00 100.00 5.31e-47 GB AAA35749 "DNA-binding protein A, partial [Homo sapiens]" 97.47 412 98.70 100.00 1.18e-42 PRF 2210343A "nicotinic acetylcholine receptor repressor" 97.47 361 98.70 100.00 7.11e-46 REF NP_001003127 "Y-box-binding protein 3 [Canis lupus familiaris]" 97.47 304 97.40 98.70 4.46e-46 REF NP_001016677 "nuclease-sensitive element-binding protein 1 [Xenopus (Silurana) tropicalis]" 98.73 306 100.00 100.00 7.77e-47 REF NP_001076254 "nuclease-sensitive element-binding protein 1 [Oryctolagus cuniculus]" 98.73 324 100.00 100.00 5.08e-47 REF NP_001079367 "nuclease-sensitive element-binding protein 1 [Xenopus laevis]" 97.47 303 100.00 100.00 3.03e-46 REF NP_001080330 "B box-binding protein [Xenopus laevis]" 98.73 305 100.00 100.00 6.89e-47 SP P16989 "RecName: Full=Y-box-binding protein 3; AltName: Full=Cold shock domain-containing protein A; AltName: Full=DNA-binding protein " 97.47 372 98.70 100.00 5.77e-46 SP P21573 "RecName: Full=Nuclease-sensitive element-binding protein 1; AltName: Full=Y-box transcription factor; AltName: Full=Y-box-bindi" 97.47 303 100.00 100.00 2.84e-46 SP P62960 "RecName: Full=Nuclease-sensitive element-binding protein 1; AltName: Full=CCAAT-binding transcription factor I subunit A; Short" 98.73 322 100.00 100.00 4.70e-47 SP P62961 "RecName: Full=Nuclease-sensitive element-binding protein 1; AltName: Full=CCAAT-binding transcription factor I subunit A; Short" 98.73 322 100.00 100.00 4.70e-47 SP P67808 "RecName: Full=Nuclease-sensitive element-binding protein 1; AltName: Full=CCAAT-binding transcription factor I subunit A; Short" 98.73 324 100.00 100.00 5.31e-47 TPG DAA29365 "TPA: cold shock domain protein A [Bos taurus]" 97.47 376 98.70 100.00 1.27e-42 TPG DAA30957 "TPA: nuclease-sensitive element-binding protein 1 [Bos taurus]" 98.73 324 100.00 100.00 5.31e-47 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $YB1-CSD human 9606 Eukaryota Metazoa Homo sapiens 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 $YB1-CSD 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET11a 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 _Isotopic_labeling $YB1-CSD 1.5 mM [U-15N] H2O 90 % . D2O 10 % . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $YB1-CSD 1.5 mM [U-15N;U-13C] H2O 90 % . D2O 10 % . stop_ save_ save_sample_three _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $YB1-CSD 1.5 mM [U-15N;U-13C] D2O 100 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . 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 6.7 . n/a temperature 303 . 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 TSP C 13 'methyl protons' ppm 0.00 . indirect . . . 0.25144954 $citation_one TSP H 1 'methyl protons' ppm 0.00 . direct . . . . . 'liquid NH3' N 15 . ppm 0.00 . indirect . . . . . 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 . 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 YB1-CSD _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 LYS HA H 4.456 . 1 2 . 2 LYS HB2 H 1.638 . 2 3 . 2 LYS HB3 H 1.747 . 2 4 . 2 LYS HG2 H 1.436 . 2 5 . 2 LYS HD2 H 1.434 . 1 6 . 2 LYS HD3 H 1.434 . 1 7 . 2 LYS HE2 H 2.980 . 1 8 . 2 LYS HE3 H 2.980 . 1 9 . 2 LYS CA C 56.293 . 1 10 . 2 LYS CB C 33.425 . 1 11 . 2 LYS CG C 25.556 . 1 12 . 2 LYS CD C 29.404 . 1 13 . 2 LYS CE C 42.327 . 1 14 . 3 LYS H H 8.552 . 1 15 . 3 LYS HA H 4.214 . 1 16 . 3 LYS HB2 H 1.771 . 2 17 . 3 LYS HB3 H 1.668 . 2 18 . 3 LYS HG2 H 1.280 . 1 19 . 3 LYS HG3 H 1.280 . 1 20 . 3 LYS HD2 H 1.416 . 1 21 . 3 LYS HD3 H 1.416 . 1 22 . 3 LYS HE2 H 2.946 . 1 23 . 3 LYS HE3 H 2.946 . 1 24 . 3 LYS C C 175.500 . 1 25 . 3 LYS CA C 56.476 . 1 26 . 3 LYS CB C 33.738 . 1 27 . 3 LYS CG C 24.808 . 1 28 . 3 LYS CD C 29.387 . 1 29 . 3 LYS CE C 42.074 . 1 30 . 3 LYS N N 123.660 . 1 31 . 4 VAL H H 8.494 . 1 32 . 4 VAL HA H 4.095 . 1 33 . 4 VAL HB H 1.966 . 1 34 . 4 VAL HG1 H 0.961 . 2 35 . 4 VAL HG2 H 0.805 . 2 36 . 4 VAL C C 176.594 . 1 37 . 4 VAL CA C 63.541 . 1 38 . 4 VAL CB C 32.182 . 1 39 . 4 VAL CG1 C 21.633 . 1 40 . 4 VAL CG2 C 21.633 . 1 41 . 4 VAL N N 125.173 . 1 42 . 5 ILE H H 9.200 . 1 43 . 5 ILE HA H 4.148 . 1 44 . 5 ILE HB H 1.689 . 1 45 . 5 ILE HG2 H 0.913 . 1 46 . 5 ILE HG12 H 1.428 . 2 47 . 5 ILE HG13 H 1.065 . 2 48 . 5 ILE HD1 H 0.807 . 1 49 . 5 ILE C C 176.190 . 1 50 . 5 ILE CA C 62.275 . 1 51 . 5 ILE CB C 39.198 . 1 52 . 5 ILE CG1 C 27.717 . 1 53 . 5 ILE CG2 C 17.307 . 1 54 . 5 ILE CD1 C 13.031 . 1 55 . 5 ILE N N 127.418 . 1 56 . 6 ALA H H 8.103 . 1 57 . 6 ALA HA H 4.607 . 1 58 . 6 ALA HB H 1.277 . 1 59 . 6 ALA C C 175.294 . 1 60 . 6 ALA CA C 52.278 . 1 61 . 6 ALA CB C 22.299 . 1 62 . 6 ALA N N 121.884 . 1 63 . 7 THR H H 8.312 . 1 64 . 7 THR HA H 5.004 . 1 65 . 7 THR HB H 3.977 . 1 66 . 7 THR HG2 H 1.056 . 1 67 . 7 THR C C 173.193 . 1 68 . 7 THR CA C 59.106 . 1 69 . 7 THR CB C 71.703 . 1 70 . 7 THR CG2 C 21.793 . 1 71 . 7 THR N N 112.374 . 1 72 . 8 LYS H H 8.817 . 1 73 . 8 LYS HA H 3.444 . 1 74 . 8 LYS HB2 H 1.672 . 2 75 . 8 LYS HB3 H 1.918 . 2 76 . 8 LYS HG2 H 1.333 . 1 77 . 8 LYS HG3 H 1.333 . 1 78 . 8 LYS HD2 H 1.629 . 1 79 . 8 LYS HD3 H 1.629 . 1 80 . 8 LYS HE2 H 2.991 . 1 81 . 8 LYS HE3 H 2.991 . 1 82 . 8 LYS C C 174.805 . 1 83 . 8 LYS CA C 57.352 . 1 84 . 8 LYS CB C 30.349 . 1 85 . 8 LYS CG C 25.533 . 1 86 . 8 LYS CD C 29.277 . 1 87 . 8 LYS CE C 42.232 . 1 88 . 8 LYS N N 122.874 . 1 89 . 9 VAL H H 8.855 . 1 90 . 9 VAL HA H 3.858 . 1 91 . 9 VAL HB H 1.086 . 1 92 . 9 VAL HG1 H 0.750 . 2 93 . 9 VAL HG2 H 0.415 . 2 94 . 9 VAL C C 174.416 . 1 95 . 9 VAL CA C 61.365 . 1 96 . 9 VAL CB C 32.476 . 1 97 . 9 VAL CG1 C 22.852 . 2 98 . 9 VAL CG2 C 22.14 . 2 99 . 9 VAL N N 121.532 . 1 100 . 10 LEU H H 7.700 . 1 101 . 10 LEU HA H 5.458 . 1 102 . 10 LEU HB2 H 1.419 . 2 103 . 10 LEU HB3 H 1.742 . 2 104 . 10 LEU HG H 1.426 . 1 105 . 10 LEU HD1 H 0.931 . 2 106 . 10 LEU HD2 H 0.883 . 2 107 . 10 LEU C C 178.396 . 1 108 . 10 LEU CA C 53.037 . 1 109 . 10 LEU CB C 44.363 . 1 110 . 10 LEU CG C 27.377 . 4 111 . 10 LEU CD1 C 25.19 . 2 112 . 10 LEU CD2 C 23.95 . 2 113 . 10 LEU N N 122.006 . 1 114 . 11 GLY H H 9.191 . 1 115 . 11 GLY HA3 H 4.345 . 2 116 . 11 GLY HA2 H 4.530 . 2 117 . 11 GLY C C 179.396 . 1 118 . 11 GLY CA C 45.710 . 1 119 . 11 GLY N N 109.160 . 1 120 . 12 THR H H 8.638 . 1 121 . 12 THR HA H 5.129 . 1 122 . 12 THR HB H 3.897 . 1 123 . 12 THR CA C 60.387 . 1 124 . 12 THR CB C 71.754 . 1 125 . 12 THR CG2 C 21.121 . 1 126 . 12 THR N N 113.420 . 1 127 . 13 VAL H H 9.178 . 1 128 . 13 VAL HA H 4.481 . 1 129 . 13 VAL CA C 60.369 . 1 130 . 13 VAL N N 127.897 . 1 131 . 13 VAL HG1 H 0.544 . 2 132 . 13 VAL HG2 H 0.740 . 2 133 . 13 VAL CG1 C 21.17 . 2 134 . 13 VAL CG2 C 22.35 . 2 135 . 15 TRP HA H 4.772 . 1 136 . 15 TRP HB2 H 3.532 . 2 137 . 15 TRP HB3 H 3.316 . 2 138 . 15 TRP HE1 H 10.324 . 1 139 . 15 TRP C C 174.133 . 1 140 . 15 TRP CA C 55.928 . 1 141 . 15 TRP CB C 30.870 . 1 142 . 15 TRP NE1 N 129.243 . 1 143 . 16 PHE H H 8.845 . 1 144 . 16 PHE HA H 4.290 . 1 145 . 16 PHE CA C 59.194 . 1 146 . 16 PHE CB C 42.457 . 1 147 . 16 PHE N N 120.033 . 1 148 . 18 VAL HA H 3.735 . 1 149 . 18 VAL HB H 2.154 . 1 150 . 18 VAL HG1 H 1.147 . 2 151 . 18 VAL HG2 H 1.038 . 2 152 . 18 VAL C C 177.441 . 1 153 . 18 VAL CA C 65.177 . 1 154 . 18 VAL CB C 32.014 . 1 155 . 18 VAL CG1 C 21.306 . 2 156 . 19 ARG H H 8.033 . 1 157 . 19 ARG HA H 4.074 . 1 158 . 19 ARG HB2 H 1.871 . 1 159 . 19 ARG HB3 H 1.871 . 1 160 . 19 ARG HG2 H 1.705 . 2 161 . 19 ARG HG3 H 1.646 . 2 162 . 19 ARG HD2 H 3.218 . 1 163 . 19 ARG HD3 H 3.218 . 1 164 . 19 ARG C C 177.918 . 1 165 . 19 ARG CA C 58.800 . 1 166 . 19 ARG CB C 29.627 . 1 167 . 19 ARG CG C 27.228 . 1 168 . 19 ARG CD C 43.235 . 1 169 . 19 ARG N N 120.155 . 1 170 . 20 ASN H H 7.752 . 1 171 . 20 ASN HA H 4.723 . 1 172 . 20 ASN HB2 H 2.086 . 2 173 . 20 ASN HB3 H 2.798 . 2 174 . 20 ASN C C 175.868 . 1 175 . 20 ASN CA C 53.355 . 1 176 . 20 ASN CB C 39.087 . 1 177 . 20 ASN N N 114.409 . 1 178 . 21 GLY H H 8.077 . 1 179 . 21 GLY HA3 H 3.924 . 2 180 . 21 GLY HA2 H 3.620 . 2 181 . 21 GLY CA C 46.849 . 1 182 . 21 GLY N N 108.872 . 1 183 . 22 TYR HA H 4.375 . 1 184 . 22 TYR HB2 H 1.661 . 2 185 . 22 TYR C C 175.240 . 1 186 . 22 TYR CA C 55.301 . 1 187 . 22 TYR CB C 41.207 . 1 188 . 23 GLY H H 8.052 . 1 189 . 23 GLY HA3 H 2.893 . 2 190 . 23 GLY HA2 H 3.781 . 2 191 . 23 GLY C C 178.905 . 1 192 . 23 GLY CA C 45.337 . 1 193 . 23 GLY N N 106.060 . 1 194 . 24 PHE H H 7.743 . 1 195 . 24 PHE HA H 5.134 . 1 196 . 24 PHE HB2 H 2.151 . 2 197 . 24 PHE HB3 H 2.516 . 2 198 . 24 PHE C C 174.618 . 1 199 . 24 PHE CA C 56.837 . 1 200 . 24 PHE CB C 44.776 . 1 201 . 24 PHE N N 114.468 . 1 202 . 25 ILE H H 9.266 . 1 203 . 25 ILE HA H 4.137 . 1 204 . 25 ILE HB H 0.903 . 1 205 . 25 ILE HD1 H -0.208 . 1 206 . 25 ILE HG12 H 1.175 . 2 207 . 25 ILE HG13 H 0.292 . 2 208 . 25 ILE HG2 H 0.223 . 1 209 . 25 ILE C C 173.850 . 1 210 . 25 ILE CA C 59.603 . 1 211 . 25 ILE CB C 41.322 . 1 212 . 25 ILE CG1 C 27.447 . 1 213 . 25 ILE CG2 C 19.257 . 1 214 . 25 ILE CD1 C 13.363 . 1 215 . 25 ILE N N 121.056 . 1 216 . 26 ASN H H 9.283 . 1 217 . 26 ASN HA H 5.334 . 1 218 . 26 ASN HB2 H 2.524 . 2 219 . 26 ASN HB3 H 2.705 . 2 220 . 26 ASN HD21 H 8.299 . 2 221 . 26 ASN HD22 H 6.012 . 2 222 . 26 ASN C C 174.884 . 1 223 . 26 ASN CA C 53.612 . 1 224 . 26 ASN CB C 41.858 . 1 225 . 26 ASN N N 127.039 . 1 226 . 26 ASN ND2 N 111.437 . 1 227 . 27 ARG H H 9.152 . 1 228 . 27 ARG HA H 4.215 . 1 229 . 27 ARG HB2 H 2.858 . 2 230 . 27 ARG HB3 H 2.049 . 2 231 . 27 ARG HD2 H 3.203 . 2 232 . 27 ARG HD3 H 3.132 . 2 233 . 27 ARG HG2 H 1.813 . 2 234 . 27 ARG HG3 H 2.192 . 2 235 . 27 ARG C C 177.343 . 1 236 . 27 ARG CA C 58.037 . 1 237 . 27 ARG CB C 32.038 . 1 238 . 27 ARG CG C 27.884 . 1 239 . 27 ARG CD C 44.348 . 1 240 . 27 ARG N N 126.875 . 1 241 . 28 ASN H H 9.529 . 1 242 . 28 ASN HA H 4.535 . 1 243 . 28 ASN HB2 H 2.765 . 2 244 . 28 ASN HB3 H 2.944 . 2 245 . 28 ASN C C 175.891 . 1 246 . 28 ASN CA C 54.982 . 1 247 . 28 ASN CB C 37.534 . 1 248 . 28 ASN N N 121.600 . 1 249 . 29 ASP H H 8.864 . 1 250 . 29 ASP HA H 4.501 . 1 251 . 29 ASP HB2 H 2.817 . 2 252 . 29 ASP HB3 H 2.907 . 2 253 . 29 ASP C C 178.267 . 1 254 . 29 ASP CA C 55.488 . 1 255 . 29 ASP CB C 38.985 . 1 256 . 29 ASP N N 116.426 . 1 257 . 30 THR H H 8.620 . 1 258 . 30 THR HA H 4.383 . 1 259 . 30 THR HG2 H 1.064 . 1 260 . 30 THR C C 175.772 . 1 261 . 30 THR CA C 61.293 . 1 262 . 30 THR CB C 70.580 . 1 263 . 30 THR CG2 C 21.865 . 1 264 . 30 THR N N 109.313 . 1 265 . 31 LYS H H 7.808 . 1 266 . 31 LYS HA H 4.582 . 1 267 . 31 LYS HB2 H 2.178 . 2 268 . 31 LYS HB3 H 2.115 . 2 269 . 31 LYS HG2 H 1.439 . 2 270 . 31 LYS HG3 H 1.280 . 2 271 . 31 LYS HD2 H 1.752 . 2 272 . 31 LYS HD3 H 1.666 . 2 273 . 31 LYS HE2 H 3.015 . 1 274 . 31 LYS HE3 H 3.015 . 1 275 . 31 LYS C C 176.593 . 1 276 . 31 LYS CA C 56.794 . 1 277 . 31 LYS CB C 28.160 . 1 278 . 31 LYS CG C 24.797 . 1 279 . 31 LYS CD C 28.798 . 1 280 . 31 LYS CE C 42.720 . 1 281 . 31 LYS N N 114.845 . 1 282 . 32 GLU H H 7.217 . 1 283 . 32 GLU HA H 4.457 . 1 284 . 32 GLU HB2 H 1.721 . 2 285 . 32 GLU HB3 H 2.044 . 2 286 . 32 GLU HG2 H 2.226 . 1 287 . 32 GLU HG3 H 2.226 . 1 288 . 32 GLU C C 176.103 . 1 289 . 32 GLU CA C 55.213 . 1 290 . 32 GLU CB C 32.932 . 1 291 . 32 GLU CG C 36.827 . 1 292 . 32 GLU N N 117.870 . 1 293 . 33 ASP H H 8.656 . 1 294 . 33 ASP HA H 5.451 . 1 295 . 33 ASP HB2 H 2.310 . 2 296 . 33 ASP HB3 H 2.531 . 2 297 . 33 ASP C C 177.108 . 1 298 . 33 ASP CA C 54.333 . 1 299 . 33 ASP CB C 41.864 . 1 300 . 33 ASP N N 122.194 . 1 301 . 34 VAL H H 9.680 . 1 302 . 34 VAL HA H 4.475 . 1 303 . 34 VAL HB H 1.886 . 1 304 . 34 VAL HG1 H 0.934 . 2 305 . 34 VAL C C 174.420 . 1 306 . 34 VAL CA C 60.850 . 1 307 . 34 VAL CB C 34.946 . 1 308 . 34 VAL CG1 C 21.745 . 2 309 . 34 VAL N N 121.449 . 1 310 . 35 PHE H H 8.390 . 1 311 . 35 PHE HA H 3.860 . 1 312 . 35 PHE HB2 H 2.868 . 2 313 . 35 PHE HB3 H 3.137 . 2 314 . 35 PHE C C 181.000 . 1 315 . 35 PHE CA C 58.960 . 1 316 . 35 PHE CB C 40.456 . 1 317 . 35 PHE N N 127.409 . 1 318 . 36 VAL H H 7.663 . 1 319 . 36 VAL HA H 4.634 . 1 320 . 36 VAL HB H 1.429 . 1 321 . 36 VAL HG1 H 0.607 . 2 322 . 36 VAL HG2 H 0.409 . 2 323 . 36 VAL C C 178.693 . 1 324 . 36 VAL CA C 58.052 . 1 325 . 36 VAL CB C 34.319 . 1 326 . 36 VAL CG1 C 23.277 . 2 327 . 36 VAL CG2 C 18.213 . 2 328 . 36 VAL N N 123.438 . 1 329 . 37 HIS H H 8.691 . 1 330 . 37 HIS HA H 4.798 . 1 331 . 37 HIS HB2 H 2.986 . 2 332 . 37 HIS HB3 H 3.189 . 2 333 . 37 HIS C C 176.844 . 1 334 . 37 HIS CA C 56.031 . 1 335 . 37 HIS CB C 34.224 . 1 336 . 37 HIS N N 126.658 . 1 337 . 38 GLN H H 8.182 . 1 338 . 38 GLN HA H 3.912 . 1 339 . 38 GLN HB2 H 1.951 . 2 340 . 38 GLN HB3 H 2.218 . 2 341 . 38 GLN C C 177.443 . 1 342 . 38 GLN CA C 59.136 . 1 343 . 38 GLN CB C 28.380 . 1 344 . 38 GLN CG C 32.684 . 1 345 . 38 GLN N N 123.837 . 1 346 . 39 THR H H 9.072 . 1 347 . 39 THR HA H 4.463 . 1 348 . 39 THR HB H 4.169 . 1 349 . 39 THR HG2 H 1.559 . 1 350 . 39 THR C C 175.494 . 1 351 . 39 THR CA C 64.243 . 1 352 . 39 THR CB C 70.024 . 1 353 . 39 THR CG2 C 23.174 . 1 354 . 39 THR N N 111.399 . 1 355 . 40 ALA H H 8.272 . 1 356 . 40 ALA HA H 4.562 . 1 357 . 40 ALA HB H 1.637 . 1 358 . 40 ALA C C 176.847 . 1 359 . 40 ALA CA C 52.547 . 1 360 . 40 ALA CB C 20.858 . 1 361 . 40 ALA N N 123.190 . 1 362 . 41 ILE H H 7.277 . 1 363 . 41 ILE HA H 3.968 . 1 364 . 41 ILE HB H 1.821 . 1 365 . 41 ILE HG2 H 0.680 . 1 366 . 41 ILE HG12 H 1.415 . 2 367 . 41 ILE HG13 H 0.579 . 2 368 . 41 ILE HD1 H 0.329 . 1 369 . 41 ILE C C 175.977 . 1 370 . 41 ILE CA C 61.853 . 1 371 . 41 ILE CB C 37.485 . 1 372 . 41 ILE CG1 C 27.418 . 1 373 . 41 ILE CG2 C 17.650 . 1 374 . 41 ILE CD1 C 13.139 . 1 375 . 41 ILE N N 117.983 . 1 376 . 42 LYS H H 8.864 . 1 377 . 42 LYS HA H 4.300 . 1 378 . 42 LYS HB2 H 1.638 . 2 379 . 42 LYS HB3 H 1.800 . 2 380 . 42 LYS C C 174.250 . 1 381 . 42 LYS CA C 56.399 . 1 382 . 42 LYS CB C 32.915 . 1 383 . 42 LYS CG C 24.855 . 1 384 . 42 LYS CD C 29.141 . 1 385 . 42 LYS N N 124.764 . 1 386 . 43 LYS H H 8.193 . 1 387 . 43 LYS HA H 4.190 . 1 388 . 43 LYS N N 122.069 . 1 389 . 44 ASN HA H 4.655 . 1 390 . 44 ASN HB2 H 2.781 . 2 391 . 44 ASN HB3 H 2.783 . 2 392 . 44 ASN C C 174.613 . 1 393 . 44 ASN CA C 53.402 . 1 394 . 44 ASN CB C 38.778 . 1 395 . 45 ASN H H 8.200 . 1 396 . 45 ASN HA H 4.971 . 1 397 . 45 ASN HB2 H 2.886 . 1 398 . 45 ASN HB3 H 2.886 . 1 399 . 45 ASN CA C 51.286 . 1 400 . 45 ASN CB C 39.309 . 1 401 . 45 ASN N N 119.142 . 1 402 . 46 PRO HA H 4.297 . 1 403 . 46 PRO HB2 H 2.307 . 2 404 . 46 PRO HB3 H 1.945 . 2 405 . 46 PRO HG2 H 1.988 . 1 406 . 46 PRO HG3 H 1.988 . 1 407 . 46 PRO HD2 H 3.787 . 1 408 . 46 PRO HD3 H 3.787 . 1 409 . 46 PRO C C 177.382 . 1 410 . 46 PRO CA C 64.390 . 1 411 . 46 PRO CB C 32.270 . 1 412 . 46 PRO CG C 27.198 . 1 413 . 46 PRO CD C 50.897 . 1 414 . 47 ARG H H 8.051 . 1 415 . 47 ARG HA H 4.248 . 1 416 . 47 ARG HB2 H 1.790 . 2 417 . 47 ARG HB3 H 1.719 . 2 418 . 47 ARG HD2 H 3.194 . 1 419 . 47 ARG HD3 H 3.194 . 1 420 . 47 ARG C C 176.478 . 1 421 . 47 ARG CA C 56.545 . 1 422 . 47 ARG CB C 30.331 . 1 423 . 47 ARG CG C 27.516 . 1 424 . 47 ARG CD C 43.260 . 1 425 . 47 ARG N N 116.818 . 1 426 . 48 LYS H H 7.787 . 1 427 . 48 LYS HA H 4.253 . 1 428 . 48 LYS HB2 H 1.825 . 2 429 . 48 LYS HB3 H 1.651 . 2 430 . 48 LYS HG2 H 1.280 . 2 431 . 48 LYS HG3 H 1.199 . 2 432 . 48 LYS HD2 H 1.621 . 1 433 . 48 LYS HD3 H 1.621 . 1 434 . 48 LYS HE2 H 2.921 . 1 435 . 48 LYS HE3 H 2.921 . 1 436 . 48 LYS CA C 56.365 . 1 437 . 48 LYS CB C 33.135 . 1 438 . 48 LYS CG C 24.912 . 1 439 . 48 LYS CD C 29.313 . 1 440 . 48 LYS CE C 42.085 . 1 441 . 48 LYS N N 119.394 . 1 442 . 49 TYR H H 7.865 . 1 443 . 49 TYR HA H 4.506 . 1 444 . 49 TYR HB2 H 2.994 . 1 445 . 49 TYR HB3 H 2.994 . 1 446 . 49 TYR C C 175.516 . 1 447 . 49 TYR CA C 57.912 . 1 448 . 49 TYR CB C 38.486 . 1 449 . 49 TYR N N 120.060 . 1 450 . 50 LEU H H 7.908 . 1 451 . 50 LEU HA H 4.274 . 1 452 . 50 LEU HB2 H 1.478 . 1 453 . 50 LEU HB3 H 1.478 . 1 454 . 50 LEU HG H 1.396 . 1 455 . 50 LEU HD1 H 0.825 . 2 456 . 50 LEU HD2 H 0.772 . 2 457 . 50 LEU C C 176.574 . 1 458 . 50 LEU CA C 54.846 . 1 459 . 50 LEU CB C 42.529 . 1 460 . 50 LEU CG C 26.889 . 1 461 . 50 LEU CD1 C 25.19 . 2 462 . 50 LEU CD2 C 23.95 . 2 463 . 50 LEU N N 122.870 . 1 464 . 51 ARG H H 8.217 . 1 465 . 51 ARG HA H 4.191 . 1 466 . 51 ARG HB2 H 1.809 . 1 467 . 51 ARG HB3 H 1.809 . 1 468 . 51 ARG HG2 H 1.606 . 2 469 . 51 ARG HD2 H 3.189 . 1 470 . 51 ARG HD3 H 3.189 . 1 471 . 51 ARG C C 175.562 . 1 472 . 51 ARG CA C 56.467 . 1 473 . 51 ARG CB C 30.732 . 1 474 . 51 ARG CG C 27.236 . 1 475 . 51 ARG CD C 43.457 . 1 476 . 51 ARG N N 121.668 . 1 477 . 52 SER H H 7.811 . 1 478 . 52 SER HA H 4.453 . 1 479 . 52 SER HB2 H 3.879 . 2 480 . 52 SER C C 173.656 . 1 481 . 52 SER CA C 58.497 . 1 482 . 52 SER CB C 64.264 . 1 483 . 52 SER N N 113.641 . 1 484 . 53 VAL H H 7.998 . 1 485 . 53 VAL HA H 4.171 . 1 486 . 53 VAL HB H 1.667 . 1 487 . 53 VAL C C 174.593 . 1 488 . 53 VAL CA C 60.264 . 1 489 . 53 VAL CB C 33.236 . 1 490 . 53 VAL HG1 H 0.399 . 1 491 . 53 VAL HG2 H 0.399 . 1 492 . 53 VAL CG1 C 21.88 . 1 493 . 53 VAL CG2 C 21.88 . 1 494 . 53 VAL N N 127.623 . 1 495 . 54 GLY H H 8.228 . 1 496 . 54 GLY HA3 H 3.689 . 2 497 . 54 GLY HA2 H 4.226 . 2 498 . 54 GLY C C 181.122 . 1 499 . 54 GLY CA C 44.398 . 1 500 . 54 GLY N N 109.718 . 1 501 . 55 ASP H H 8.350 . 1 502 . 55 ASP HA H 4.041 . 1 503 . 55 ASP HB2 H 2.594 . 2 504 . 55 ASP HB3 H 2.676 . 2 505 . 55 ASP C C 177.731 . 1 506 . 55 ASP CA C 55.774 . 1 507 . 55 ASP CB C 40.082 . 1 508 . 55 ASP N N 119.999 . 1 509 . 56 GLY H H 8.808 . 1 510 . 56 GLY HA3 H 3.675 . 2 511 . 56 GLY HA2 H 4.221 . 2 512 . 56 GLY C C 174.188 . 1 513 . 56 GLY CA C 45.602 . 1 514 . 56 GLY N N 111.335 . 1 515 . 57 GLU H H 7.797 . 1 516 . 57 GLU HA H 4.243 . 1 517 . 57 GLU HB2 H 1.916 . 2 518 . 57 GLU HB3 H 2.038 . 2 519 . 57 GLU HG2 H 2.230 . 1 520 . 57 GLU HG3 H 2.230 . 1 521 . 57 GLU C C 176.189 . 1 522 . 57 GLU CA C 57.037 . 1 523 . 57 GLU CB C 30.744 . 1 524 . 57 GLU CG C 36.455 . 1 525 . 57 GLU N N 120.731 . 1 526 . 58 THR H H 8.590 . 1 527 . 58 THR HA H 5.115 . 1 528 . 58 THR HB H 4.066 . 1 529 . 58 THR HG2 H 1.280 . 1 530 . 58 THR C C 174.300 . 1 531 . 58 THR CA C 63.043 . 1 532 . 58 THR CB C 69.381 . 1 533 . 58 THR CG2 C 21.794 . 1 534 . 58 THR N N 120.330 . 1 535 . 59 VAL H H 8.877 . 1 536 . 59 VAL HA H 4.981 . 1 537 . 59 VAL HB H 2.152 . 1 538 . 59 VAL HG1 H 0.497 . 2 539 . 59 VAL HG2 H 0.595 . 2 540 . 59 VAL C C 172.883 . 1 541 . 59 VAL CA C 58.616 . 1 542 . 59 VAL CB C 35.974 . 1 543 . 59 VAL CG1 C 18.661 . 2 544 . 59 VAL CG2 C 22.676 . 2 545 . 59 VAL N N 118.354 . 1 546 . 60 GLU H H 8.696 . 1 547 . 60 GLU HA H 5.607 . 1 548 . 60 GLU HB2 H 1.674 . 2 549 . 60 GLU HB3 H 1.861 . 2 550 . 60 GLU HG2 H 2.028 . 1 551 . 60 GLU HG3 H 2.028 . 1 552 . 60 GLU C C 175.256 . 1 553 . 60 GLU CA C 54.315 . 1 554 . 60 GLU CB C 34.329 . 1 555 . 60 GLU CG C 37.744 . 1 556 . 60 GLU N N 121.838 . 1 557 . 61 PHE H H 8.932 . 1 558 . 61 PHE HA H 5.153 . 1 559 . 61 PHE HB2 H 3.148 . 1 560 . 61 PHE HB3 H 3.148 . 1 561 . 61 PHE C C 180.439 . 1 562 . 61 PHE CA C 55.989 . 1 563 . 61 PHE CB C 41.018 . 1 564 . 61 PHE N N 120.120 . 1 565 . 62 ASP H H 8.867 . 1 566 . 62 ASP HA H 5.205 . 1 567 . 62 ASP HB2 H 2.403 . 2 568 . 62 ASP HB3 H 2.829 . 2 569 . 62 ASP C C 175.414 . 1 570 . 62 ASP CA C 52.330 . 1 571 . 62 ASP CB C 43.018 . 1 572 . 62 ASP N N 116.561 . 1 573 . 63 VAL H H 9.052 . 1 574 . 63 VAL HA H 4.879 . 1 575 . 63 VAL HB H 1.874 . 1 576 . 63 VAL HG1 H 1.041 . 2 577 . 63 VAL HG2 H 0.914 . 2 578 . 63 VAL C C 175.428 . 1 579 . 63 VAL CA C 61.824 . 1 580 . 63 VAL CB C 33.303 . 1 581 . 63 VAL CG1 C 22.631 . 1 582 . 63 VAL CG2 C 22.631 . 1 583 . 63 VAL N N 120.585 . 1 584 . 64 VAL H H 9.549 . 1 585 . 64 VAL HA H 5.242 . 1 586 . 64 VAL HB H 2.029 . 1 587 . 64 VAL HG1 H 0.836 . 2 588 . 64 VAL HG2 H 0.781 . 2 589 . 64 VAL C C 174.564 . 1 590 . 64 VAL CA C 58.612 . 1 591 . 64 VAL CB C 35.371 . 1 592 . 64 VAL CG1 C 21.680 . 1 593 . 64 VAL CG2 C 19.792 . 1 594 . 64 VAL N N 122.003 . 1 595 . 65 GLU H H 8.704 . 1 596 . 65 GLU HA H 4.406 . 1 597 . 65 GLU HB2 H 1.913 . 2 598 . 65 GLU HB3 H 2.117 . 2 599 . 65 GLU HG2 H 2.208 . 1 600 . 65 GLU HG3 H 2.208 . 1 601 . 65 GLU C C 176.102 . 1 602 . 65 GLU CA C 56.496 . 1 603 . 65 GLU CB C 31.075 . 1 604 . 65 GLU CG C 36.673 . 1 605 . 65 GLU N N 121.765 . 1 606 . 66 GLY H H 7.972 . 1 607 . 66 GLY HA3 H 3.918 . 2 608 . 66 GLY HA2 H 4.520 . 2 609 . 66 GLY C C 174.756 . 1 610 . 66 GLY CA C 43.969 . 1 611 . 66 GLY N N 114.026 . 1 612 . 67 GLU H H 8.968 . 1 613 . 67 GLU HA H 4.030 . 1 614 . 67 GLU HB2 H 1.994 . 1 615 . 67 GLU HB3 H 1.994 . 1 616 . 67 GLU HG2 H 2.284 . 1 617 . 67 GLU HG3 H 2.284 . 1 618 . 67 GLU C C 178.045 . 1 619 . 67 GLU CA C 59.318 . 1 620 . 67 GLU CB C 30.004 . 1 621 . 67 GLU CG C 36.469 . 1 622 . 67 GLU N N 120.735 . 1 623 . 68 LYS H H 8.640 . 1 624 . 68 LYS HA H 4.483 . 1 625 . 68 LYS HB2 H 1.460 . 2 626 . 68 LYS HB3 H 1.848 . 2 627 . 68 LYS HG2 H 1.163 . 1 628 . 68 LYS HG3 H 1.163 . 1 629 . 68 LYS HD2 H 1.361 . 1 630 . 68 LYS HD3 H 1.361 . 1 631 . 68 LYS HE2 H 2.779 . 1 632 . 68 LYS HE3 H 2.779 . 1 633 . 68 LYS C C 175.868 . 1 634 . 68 LYS CA C 54.788 . 1 635 . 68 LYS CB C 32.277 . 1 636 . 68 LYS CG C 24.823 . 1 637 . 68 LYS CD C 28.729 . 1 638 . 68 LYS CE C 42.027 . 1 639 . 68 LYS N N 116.484 . 1 640 . 69 GLY H H 7.389 . 1 641 . 69 GLY HA3 H 3.787 . 2 642 . 69 GLY HA2 H 4.441 . 2 643 . 69 GLY C C 173.412 . 1 644 . 69 GLY CA C 44.244 . 1 645 . 69 GLY N N 107.960 . 1 646 . 70 ALA H H 8.607 . 1 647 . 70 ALA HA H 4.756 . 1 648 . 70 ALA HB H 1.427 . 1 649 . 70 ALA C C 177.841 . 1 650 . 70 ALA CA C 52.860 . 1 651 . 70 ALA CB C 19.311 . 1 652 . 70 ALA N N 124.693 . 1 653 . 71 GLU H H 9.417 . 1 654 . 71 GLU HA H 5.336 . 1 655 . 71 GLU HB2 H 2.172 . 1 656 . 71 GLU HB3 H 2.172 . 1 657 . 71 GLU C C 174.142 . 1 658 . 71 GLU CA C 54.376 . 1 659 . 71 GLU CB C 34.007 . 1 660 . 71 GLU CG C 36.213 . 1 661 . 71 GLU N N 120.582 . 1 662 . 72 ALA H H 8.835 . 1 663 . 72 ALA HA H 5.268 . 1 664 . 72 ALA HB H 1.119 . 1 665 . 72 ALA C C 177.139 . 1 666 . 72 ALA CA C 50.827 . 1 667 . 72 ALA CB C 21.175 . 1 668 . 72 ALA N N 122.371 . 1 669 . 73 ALA H H 9.342 . 1 670 . 73 ALA HA H 4.764 . 1 671 . 73 ALA HB H 1.397 . 1 672 . 73 ALA C C 175.696 . 1 673 . 73 ALA CA C 50.782 . 1 674 . 73 ALA CB C 24.057 . 1 675 . 73 ALA N N 122.550 . 1 676 . 74 ASN H H 9.251 . 1 677 . 74 ASN HA H 4.209 . 1 678 . 74 ASN HB2 H 2.943 . 1 679 . 74 ASN HB3 H 2.943 . 1 680 . 74 ASN C C 173.716 . 1 681 . 74 ASN CA C 54.325 . 1 682 . 74 ASN CB C 37.157 . 1 683 . 74 ASN N N 118.032 . 1 684 . 75 VAL H H 8.272 . 1 685 . 75 VAL HA H 4.483 . 1 686 . 75 VAL HB H 2.870 . 1 687 . 75 VAL HG1 H 0.642 . 2 688 . 75 VAL C C 176.363 . 1 689 . 75 VAL CA C 63.063 . 1 690 . 75 VAL CB C 31.641 . 1 691 . 75 VAL CG1 C 21.688 . 2 692 . 75 VAL N N 117.135 . 1 693 . 76 THR H H 9.506 . 1 694 . 76 THR HA H 4.737 . 1 695 . 76 THR HB H 4.257 . 1 696 . 76 THR HG2 H 1.209 . 1 697 . 76 THR C C 173.747 . 1 698 . 76 THR CA C 60.506 . 1 699 . 76 THR CB C 71.534 . 1 700 . 76 THR CG2 C 20.224 . 1 701 . 76 THR N N 121.561 . 1 702 . 77 GLY H H 8.257 . 1 703 . 77 GLY HA3 H 3.864 . 2 704 . 77 GLY HA2 H 4.615 . 2 705 . 77 GLY CA C 44.565 . 1 706 . 77 GLY N N 108.796 . 1 707 . 78 PRO HA H 4.453 . 1 708 . 78 PRO HB2 H 2.025 . 2 709 . 78 PRO HB3 H 2.155 . 2 710 . 78 PRO HG2 H 2.079 . 2 711 . 78 PRO HG3 H 1.883 . 2 712 . 78 PRO HD2 H 3.767 . 2 713 . 78 PRO HD3 H 3.658 . 2 714 . 78 PRO C C 176.646 . 1 715 . 78 PRO CA C 63.360 . 1 716 . 78 PRO CB C 32.370 . 1 717 . 78 PRO CG C 27.260 . 1 718 . 78 PRO CD C 49.896 . 1 719 . 79 GLY H H 8.219 . 1 720 . 79 GLY HA3 H 3.201 . 2 721 . 79 GLY HA2 H 3.748 . 2 722 . 79 GLY CA C 46.432 . 1 723 . 79 GLY N N 115.285 . 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants_one _Saveframe_category coupling_constants _Details ; Correction factor: 5% 3Jhnha ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Spectrometer_frequency_1H 600 _Mol_system_component_name YB1-CSD _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 3 LYS HA 3 LYS H 5.60 . . . 2 3JHNHA 4 VAL HA 4 VAL H 7.20 . . . 3 3JHNHA 5 ILE HA 5 ILE H 9.60 . . . 4 3JHNHA 6 ALA HA 6 ALA H 6.90 . . . 5 3JHNHA 7 THR HA 7 THR H 9.60 . . . 6 3JHNHA 8 LYS HA 8 LYS H 6.90 . . . 7 3JHNHA 9 VAL HA 9 VAL H 9.00 . . . 8 3JHNHA 10 LEU HA 10 LEU H 8.80 . . . 9 3JHNHA 11 GLY HA 11 GLY H 6.90 . . . 10 3JHNHA 12 THR HA 12 THR H 10.10 . . . 11 3JHNHA 13 VAL HA 13 VAL H 8.00 . . . 12 3JHNHA 16 PHE HA 16 PHE H 7.20 . . . 13 3JHNHA 19 ARG HA 19 ARG H 5.60 . . . 14 3JHNHA 20 ASN HA 20 ASN H 11.30 . . . 15 3JHNHA 21 GLY HA2 21 GLY H 5.70 . . . 16 3JHNHA 21 GLY HA3 21 GLY H 6.00 . . . 17 3JHNHA 23 GLY HA 23 GLY H 7.50 . . . 18 3JHNHA 24 PHE HA 24 PHE H 8.40 . . . 19 3JHNHA 25 ILE HA 25 ILE H 9.50 . . . 20 3JHNHA 26 ASN HA 26 ASN H 8.60 . . . 21 3JHNHA 27 ARG HA 27 ARG H 5.20 . . . 22 3JHNHA 28 ASN HA 28 ASN H 3.60 . . . 23 3JHNHA 29 ASP HA 29 ASP H 6.90 . . . 24 3JHNHA 30 THR HA 30 THR H 6.20 . . . 25 3JHNHA 31 LYS HA 31 LYS H 7.10 . . . 26 3JHNHA 32 GLU HA 32 GLU H 8.20 . . . 27 3JHNHA 33 ASP HA 33 ASP H 6.90 . . . 28 3JHNHA 34 VAL HA 34 VAL H 9.00 . . . 29 3JHNHA 35 PHE HA 35 PHE H 3.70 . . . 30 3JHNHA 36 VAL HA 36 VAL H 8.00 . . . 31 3JHNHA 37 HIS HA 37 HIS H 8.90 . . . 32 3JHNHA 38 GLN HA 38 GLN H 2.50 . . . 33 3JHNHA 40 ALA HA 40 ALA H 7.50 . . . 34 3JHNHA 41 ILE HA 41 ILE H 6.70 . . . 35 3JHNHA 42 LYS HA 42 LYS H 7.10 . . . 36 3JHNHA 43 LYS HA 43 LYS H 7.30 . . . 37 3JHNHA 47 ARG HA 47 ARG H 9.00 . . . 38 3JHNHA 48 LYS HA 48 LYS H 7.30 . . . 39 3JHNHA 50 LEU HA 50 LEU H 6.90 . . . 40 3JHNHA 53 VAL HA 53 VAL H 9.60 . . . 41 3JHNHA 54 GLY HA 54 GLY H 7.50 . . . 42 3JHNHA 55 ASP HA 55 ASP H 2.40 . . . 43 3JHNHA 56 GLY HA2 56 GLY H 6.60 . . . 44 3JHNHA 56 GLY HA3 56 GLY H 5.20 . . . 45 3JHNHA 57 GLU HA 57 GLU H 5.20 . . . 46 3JHNHA 58 THR HA 58 THR H 8.10 . . . 47 3JHNHA 59 VAL HA 59 VAL H 9.60 . . . 48 3JHNHA 60 GLU HA 60 GLU H 7.10 . . . 49 3JHNHA 61 PHE HA 61 PHE H 7.40 . . . 50 3JHNHA 62 ASP HA 62 ASP H 6.20 . . . 51 3JHNHA 63 VAL HA 63 VAL H 9.50 . . . 52 3JHNHA 64 VAL HA 64 VAL H 10.20 . . . 53 3JHNHA 65 GLU HA 65 GLU H 6.30 . . . 54 3JHNHA 66 GLY HA2 66 GLY H 9.30 . . . 55 3JHNHA 66 GLY HA3 66 GLY H 2.80 . . . 56 3JHNHA 67 GLU HA 67 GLU H 8.30 . . . 57 3JHNHA 68 LYS HA 68 LYS H 9.40 . . . 58 3JHNHA 69 GLY HA2 69 GLY H 8.50 . . . 59 3JHNHA 69 GLY HA3 69 GLY H 3.70 . . . 60 3JHNHA 70 ALA HA 70 ALA H 3.60 . . . 61 3JHNHA 71 GLU HA 71 GLU H 8.90 . . . 62 3JHNHA 72 ALA HA 72 ALA H 6.40 . . . 63 3JHNHA 73 ALA HA 73 ALA H 9.00 . . . 64 3JHNHA 74 ASN HA 74 ASN H 6.30 . . . 65 3JHNHA 75 VAL HA 75 VAL H 6.20 . . . 66 3JHNHA 76 THR HA 76 THR H 6.30 . . . 67 3JHNHA 77 GLY HA2 77 GLY H 6.80 . . . 68 3JHNHA 77 GLY HA3 77 GLY H 4.00 . . . 69 3JHNHA 79 GLY HA2 79 GLY H 8.40 . . . 70 3JHNHA 79 GLY HA3 79 GLY H 1.80 . . . stop_ save_