data_4664 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-Specific Resonance Assignments of Q83, a Lipocalin Highly Expressed in v-myc-Transformed Avian Fibroblasts ; _BMRB_accession_number 4664 _BMRB_flat_file_name bmr4664.str _Entry_type original _Submission_date 2000-02-07 _Accession_date 2000-02-10 _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 Kontaxis Georg . . 2 Matt Theresia . . 3 Schuler Wolfgang . . 4 Krautler Bernhard . . 5 Bister Klaus . . 6 Konrat Robert . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 465 "13C chemical shifts" 419 "15N chemical shifts" 138 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-07-05 update author 'residue 115 reassigned as a tyrosine' 2000-07-08 original author 'original release date' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Sequence-specific Resonance Assignments of Q83, a Lipocalin Highly Expressed in v-myc-transformed Avian Fibroblasts ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20377250 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kontaxis Georg . . 2 Matt Theresia . . 3 Schuler Wolfgang . . 4 Krautler Bernhard . . 5 Bister Klaus . . 6 Konrat Robert . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 17 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 177 _Page_last 178 _Year 2000 _Details 'G. Kontaxis and T. Matt contributed equally' loop_ _Keyword 'NMR assignments' 'protein structure' 'cell proliferation' oncogenes stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref-1 _Saveframe_category citation _Citation_full ; Oncogene 1993 Sep;8(9):2317-24 Suppression in transformed avian fibroblasts of a gene (crp) encoding a cysteine-rich protein containing LIM domains. Weiskirchen R, Bister K ; _Citation_title 'Suppression in transformed avian fibroblasts of a gene (crp) encoding a cysteine-rich protein containing LIM domains.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8361751 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Weiskirchen R . . 2 Bister K . . stop_ _Journal_abbreviation Oncogene _Journal_name_full Oncogene _Journal_volume 8 _Journal_issue 9 _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 2317 _Page_last 2324 _Year 1993 _Details ; Using cDNA subtraction and differential hybridization techniques, a cDNA library derived from normal quail embryo fibroblasts was screened for clones corresponding to genes whose expression was suppressed in v-myc-transformed, as compared with normal, quail embryo fibroblasts. One of the isolated cDNA clones corresponded to a 0.9-kb mRNA that was present in normal quail and chicken embryo fibroblasts, but was virtually absent from all transformed avian cells tested: quail embryo fibroblasts transformed by the v-myc, v-myc/v-mil or v-src oncogenes, cells derived from a methylcholanthrene-induced quail fibrosarcoma or v-myc-transformed chicken macrophages. Nucleotide sequence analysis of the original and supplementary cDNA clones indicated that the corresponding gene encodes a 194 amino acid cysteine-rich protein (M(r) 20,911). A database search revealed that the gene is the avian homolog of a human primary response gene (crp) of unknown function. Both the quail and human CRP proteins contain two copies of a cysteine-rich amino acid sequence motif (LIM) with putative zinc-binding activity that was previously identified in several proteins with presumed regulatory functions essential for cell growth or differentiation. ; save_ save_ref-2 _Saveframe_category citation _Citation_full ; J Biomol NMR 1995 Nov;6(3):277-93 NMRPipe: a multidimensional spectral processing system based on UNIX pipes. Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A ; _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F . . 2 Grzesiek S . . 3 Vuister 'G W' W. . 4 Zhu G . . 5 Pfeifer J . . 6 Bax A . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ save_ref-3 _Saveframe_category citation _Citation_full 'Kraulis, P.J., J. Magn. Reson. (1989) 24, 627-633' _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_Q83 _Saveframe_category molecular_system _Mol_system_name 'lipocalin Q83' _Abbreviation_common Q83 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Q83 $Q83 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Q83 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Q83 _Abbreviation_common Q83 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 157 _Mol_residue_sequence ; MTVPDRSEIAGKWYVVALAS NTEFFLREKDKMKMAMARIS FLGEDELKVSYAVPKPNGCR KWETTFKKTSDDGEVYYSEE AKKKVEVLDTDYKSYAVIYA TRVKDGRTLHMMRLYSRSPE VSPAATAIFRKLAGERNYTD EMVAMLPRQEECTVDEV ; loop_ _Residue_seq_code _Residue_label 1 MET 2 THR 3 VAL 4 PRO 5 ASP 6 ARG 7 SER 8 GLU 9 ILE 10 ALA 11 GLY 12 LYS 13 TRP 14 TYR 15 VAL 16 VAL 17 ALA 18 LEU 19 ALA 20 SER 21 ASN 22 THR 23 GLU 24 PHE 25 PHE 26 LEU 27 ARG 28 GLU 29 LYS 30 ASP 31 LYS 32 MET 33 LYS 34 MET 35 ALA 36 MET 37 ALA 38 ARG 39 ILE 40 SER 41 PHE 42 LEU 43 GLY 44 GLU 45 ASP 46 GLU 47 LEU 48 LYS 49 VAL 50 SER 51 TYR 52 ALA 53 VAL 54 PRO 55 LYS 56 PRO 57 ASN 58 GLY 59 CYS 60 ARG 61 LYS 62 TRP 63 GLU 64 THR 65 THR 66 PHE 67 LYS 68 LYS 69 THR 70 SER 71 ASP 72 ASP 73 GLY 74 GLU 75 VAL 76 TYR 77 TYR 78 SER 79 GLU 80 GLU 81 ALA 82 LYS 83 LYS 84 LYS 85 VAL 86 GLU 87 VAL 88 LEU 89 ASP 90 THR 91 ASP 92 TYR 93 LYS 94 SER 95 TYR 96 ALA 97 VAL 98 ILE 99 TYR 100 ALA 101 THR 102 ARG 103 VAL 104 LYS 105 ASP 106 GLY 107 ARG 108 THR 109 LEU 110 HIS 111 MET 112 MET 113 ARG 114 LEU 115 TYR 116 SER 117 ARG 118 SER 119 PRO 120 GLU 121 VAL 122 SER 123 PRO 124 ALA 125 ALA 126 THR 127 ALA 128 ILE 129 PHE 130 ARG 131 LYS 132 LEU 133 ALA 134 GLY 135 GLU 136 ARG 137 ASN 138 TYR 139 THR 140 ASP 141 GLU 142 MET 143 VAL 144 ALA 145 MET 146 LEU 147 PRO 148 ARG 149 GLN 150 GLU 151 GLU 152 CYS 153 THR 154 VAL 155 ASP 156 GLU 157 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-06 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 16682 Q83 100.00 157 100.00 100.00 2.18e-110 BMRB 17577 Q83 100.00 157 100.00 100.00 2.18e-110 PDB 1JZU "Cell Transformation By The Myc Oncogene Activates Expression Of A Lipocalin: Analysis Of The Gene (Q83) And Solution Structure " 100.00 157 100.00 100.00 2.18e-110 PDB 2KT4 "Lipocalin Q83 Is A Siderocalin" 100.00 157 100.00 100.00 2.18e-110 PDB 2LBV "Siderocalin Q83 Reveals A Dual Ligand Binding Mode" 100.00 157 100.00 100.00 2.18e-110 GB AAF35894 "lipocalin Q83 [Coturnix coturnix]" 99.36 178 100.00 100.00 6.85e-110 GB AAK31634 "lipocalin Q83 [Coturnix coturnix]" 99.36 178 99.36 100.00 2.96e-109 SP Q9I9P7 "RecName: Full=Extracellular fatty acid-binding protein; Short=Ex-FABP; AltName: Full=Lipocalin Q83; Flags: Precursor" 99.36 178 100.00 100.00 6.85e-110 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Q83 quail 9091 Eukaryota Metazoa Coturnix coturnix 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 $Q83 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3)pLysS plasmid pET3d-Q83 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Q83 3.0 mM '[U-13C; U-15N]' 'potassium phosphate' 20 mM . 'potassium chloride' 50 mM . dithiothreitol 0.5 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task 'spectra processing' stop_ _Details . _Citation_label $ref-2 save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version . loop_ _Task 'spectra assignment and evaluation' stop_ _Details . _Citation_label $ref-3 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity Plus' _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_CBCA(CO)NNH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NNH _Sample_label $sample_1 save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_HCCH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_1 save_ save_1H-15N_TOCSY-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY-HSQC' _Sample_label $sample_1 save_ save_1H-15N_NOESY-HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 0.2 pH temperature 299 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Q83 _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 . 4 PRO HA H 4.12 0.03 1 2 . 4 PRO HB2 H 1.93 0.03 2 3 . 4 PRO HB3 H 1.54 0.03 2 4 . 4 PRO CA C 64.12 0.50 1 5 . 4 PRO C C 176.70 0.50 1 6 . 4 PRO CB C 33.08 0.50 1 7 . 5 ASP H H 8.02 0.03 1 8 . 5 ASP HA H 4.42 0.03 1 9 . 5 ASP HB2 H 2.67 0.03 2 10 . 5 ASP HB3 H 2.50 0.03 2 11 . 5 ASP CA C 54.85 0.50 1 12 . 5 ASP C C 178.28 0.50 1 13 . 5 ASP CB C 42.58 0.50 1 14 . 5 ASP N N 119.93 0.25 1 15 . 6 ARG H H 8.53 0.03 1 16 . 6 ARG HA H 4.04 0.03 1 17 . 6 ARG HB2 H 1.76 0.03 2 18 . 6 ARG HB3 H 1.72 0.03 2 19 . 6 ARG CA C 59.37 0.50 1 20 . 6 ARG C C 178.50 0.50 1 21 . 6 ARG CB C 32.44 0.50 1 22 . 6 ARG N N 125.15 0.25 1 23 . 7 SER H H 8.32 0.03 1 24 . 7 SER HA H 4.09 0.03 1 25 . 7 SER HB2 H 3.85 0.03 1 26 . 7 SER HB3 H 3.85 0.03 1 27 . 7 SER CA C 62.36 0.50 1 28 . 7 SER C C 177.20 0.50 1 29 . 7 SER CB C 63.83 0.50 1 30 . 7 SER N N 115.20 0.25 1 31 . 8 GLU H H 7.90 0.03 1 32 . 8 GLU HA H 4.26 0.03 1 33 . 8 GLU HB2 H 2.22 0.03 2 34 . 8 GLU HB3 H 2.05 0.03 2 35 . 8 GLU CA C 58.54 0.50 1 36 . 8 GLU C C 178.00 0.50 1 37 . 8 GLU CB C 31.09 0.50 1 38 . 8 GLU N N 120.87 0.25 1 39 . 9 ILE H H 7.39 0.03 1 40 . 9 ILE HA H 4.25 0.03 1 41 . 9 ILE HB H 2.04 0.03 1 42 . 9 ILE CA C 63.47 0.50 1 43 . 9 ILE C C 176.10 0.50 1 44 . 9 ILE CB C 40.54 0.50 1 45 . 9 ILE N N 115.00 0.25 1 46 . 10 ALA H H 7.37 0.03 1 47 . 10 ALA HA H 4.08 0.03 1 48 . 10 ALA HB H 1.57 0.03 1 49 . 10 ALA CA C 53.85 0.50 1 50 . 10 ALA C C 178.40 0.50 1 51 . 10 ALA CB C 20.53 0.50 1 52 . 10 ALA N N 120.68 0.25 1 53 . 11 GLY H H 8.62 0.03 1 54 . 11 GLY HA2 H 4.60 0.03 2 55 . 11 GLY HA3 H 3.62 0.03 2 56 . 11 GLY CA C 45.31 0.50 1 57 . 11 GLY C C 174.70 0.50 1 58 . 11 GLY N N 108.75 0.25 1 59 . 12 LYS H H 8.64 0.03 1 60 . 12 LYS HA H 4.76 0.03 1 61 . 12 LYS HB2 H 1.48 0.03 1 62 . 12 LYS HB3 H 1.48 0.03 1 63 . 12 LYS CA C 58.23 0.50 1 64 . 12 LYS C C 176.90 0.50 1 65 . 12 LYS CB C 34.78 0.50 1 66 . 12 LYS N N 123.32 0.25 1 67 . 13 TRP H H 9.36 0.03 1 68 . 13 TRP HA H 4.55 0.03 1 69 . 13 TRP HB2 H 3.25 0.03 2 70 . 13 TRP HB3 H 2.68 0.03 2 71 . 13 TRP CA C 57.69 0.50 1 72 . 13 TRP C C 174.30 0.50 1 73 . 13 TRP CB C 35.17 0.50 1 74 . 13 TRP N N 126.94 0.25 1 75 . 14 TYR H H 9.29 0.03 1 76 . 14 TYR HA H 4.94 0.03 1 77 . 14 TYR HB2 H 2.85 0.03 2 78 . 14 TYR HB3 H 2.72 0.03 2 79 . 14 TYR CA C 58.93 0.50 1 80 . 14 TYR C C 176.40 0.50 1 81 . 14 TYR CB C 41.49 0.50 1 82 . 14 TYR N N 119.21 0.25 1 83 . 15 VAL H H 8.89 0.03 1 84 . 15 VAL HA H 3.95 0.03 1 85 . 15 VAL HB H 1.88 0.03 1 86 . 15 VAL CA C 62.88 0.50 1 87 . 15 VAL C C 176.50 0.50 1 88 . 15 VAL CB C 32.48 0.50 1 89 . 15 VAL N N 125.01 0.25 1 90 . 16 VAL H H 8.37 0.03 1 91 . 16 VAL HA H 4.55 0.03 1 92 . 16 VAL HB H 2.37 0.03 1 93 . 16 VAL CA C 62.31 0.50 1 94 . 16 VAL C C 176.90 0.50 1 95 . 16 VAL CB C 33.48 0.50 1 96 . 16 VAL N N 115.31 0.25 1 97 . 17 ALA H H 7.52 0.03 1 98 . 17 ALA HA H 5.19 0.03 1 99 . 17 ALA HB H 0.90 0.03 1 100 . 17 ALA CA C 53.12 0.50 1 101 . 17 ALA C C 179.90 0.50 1 102 . 17 ALA CB C 24.17 0.50 1 103 . 17 ALA N N 123.65 0.25 1 104 . 18 LEU H H 8.50 0.03 1 105 . 18 LEU HA H 5.40 0.03 1 106 . 18 LEU CA C 54.07 0.50 1 107 . 18 LEU C C 177.20 0.50 1 108 . 18 LEU CB C 50.03 0.50 1 109 . 18 LEU N N 118.93 0.25 1 110 . 19 ALA H H 8.26 0.03 1 111 . 19 ALA HA H 5.35 0.03 1 112 . 19 ALA HB H 0.71 0.03 1 113 . 19 ALA CA C 52.77 0.50 1 114 . 19 ALA C C 175.50 0.50 1 115 . 19 ALA CB C 23.21 0.50 1 116 . 19 ALA N N 120.95 0.25 1 117 . 20 SER H H 7.34 0.03 1 118 . 20 SER HA H 3.77 0.03 1 119 . 20 SER HB2 H 3.53 0.03 1 120 . 20 SER HB3 H 3.53 0.03 1 121 . 20 SER CA C 57.29 0.50 1 122 . 20 SER C C 171.80 0.50 1 123 . 20 SER CB C 64.27 0.50 1 124 . 20 SER N N 114.76 0.25 1 125 . 21 ASN H H 7.85 0.03 1 126 . 21 ASN HA H 5.14 0.03 1 127 . 21 ASN HB2 H 3.40 0.03 2 128 . 21 ASN HB3 H 3.13 0.03 2 129 . 21 ASN CA C 52.37 0.50 1 130 . 21 ASN C C 177.60 0.50 1 131 . 21 ASN CB C 40.33 0.50 1 132 . 21 ASN N N 117.99 0.25 1 133 . 22 THR H H 8.00 0.03 1 134 . 22 THR HA H 4.33 0.03 1 135 . 22 THR CA C 63.13 0.50 1 136 . 22 THR C C 175.90 0.50 1 137 . 22 THR CB C 71.56 0.50 1 138 . 22 THR N N 112.87 0.25 1 139 . 23 GLU H H 8.89 0.03 1 140 . 23 GLU HA H 4.68 0.03 1 141 . 23 GLU CA C 61.30 0.50 1 142 . 23 GLU CB C 30.31 0.50 1 143 . 23 GLU N N 123.46 0.25 1 144 . 26 LEU CA C 58.68 0.50 1 145 . 26 LEU C C 180.30 0.50 1 146 . 26 LEU CB C 41.91 0.50 1 147 . 27 ARG H H 7.63 0.03 1 148 . 27 ARG HA H 4.06 0.03 1 149 . 27 ARG HB2 H 1.74 0.03 1 150 . 27 ARG HB3 H 1.74 0.03 1 151 . 27 ARG CA C 59.10 0.50 1 152 . 27 ARG C C 179.40 0.50 1 153 . 27 ARG CB C 32.03 0.50 1 154 . 27 ARG N N 117.67 0.25 1 155 . 28 GLU H H 7.55 0.03 1 156 . 28 GLU HA H 4.29 0.03 1 157 . 28 GLU CA C 56.75 0.50 1 158 . 28 GLU C C 179.40 0.50 1 159 . 28 GLU CB C 30.93 0.50 1 160 . 28 GLU N N 116.73 0.25 1 161 . 29 LYS H H 7.80 0.03 1 162 . 29 LYS CA C 59.93 0.50 1 163 . 29 LYS C C 178.80 0.50 1 164 . 29 LYS CB C 31.45 0.50 1 165 . 29 LYS N N 121.49 0.25 1 166 . 30 ASP H H 8.29 0.03 1 167 . 30 ASP HA H 4.30 0.03 1 168 . 30 ASP HB2 H 2.59 0.03 2 169 . 30 ASP HB3 H 2.53 0.03 2 170 . 30 ASP CA C 57.11 0.50 1 171 . 30 ASP C C 178.10 0.50 1 172 . 30 ASP CB C 40.59 0.50 1 173 . 30 ASP N N 119.60 0.25 1 174 . 31 LYS H H 8.01 0.03 1 175 . 31 LYS HA H 4.29 0.03 1 176 . 31 LYS HB2 H 1.88 0.03 1 177 . 31 LYS HB3 H 1.88 0.03 1 178 . 31 LYS CA C 56.94 0.50 1 179 . 31 LYS C C 178.20 0.50 1 180 . 31 LYS CB C 34.15 0.50 1 181 . 31 LYS N N 118.77 0.25 1 182 . 32 MET H H 7.13 0.03 1 183 . 32 MET HA H 4.43 0.03 1 184 . 32 MET HB2 H 2.07 0.03 1 185 . 32 MET HB3 H 2.07 0.03 1 186 . 32 MET CA C 57.92 0.50 1 187 . 32 MET C C 177.30 0.50 1 188 . 32 MET CB C 33.55 0.50 1 189 . 32 MET N N 121.09 0.25 1 190 . 33 LYS H H 8.45 0.03 1 191 . 33 LYS HA H 4.56 0.03 1 192 . 33 LYS HB2 H 1.59 0.03 1 193 . 33 LYS HB3 H 1.59 0.03 1 194 . 33 LYS CA C 55.91 0.50 1 195 . 33 LYS C C 174.00 0.50 1 196 . 33 LYS CB C 39.29 0.50 1 197 . 33 LYS N N 120.98 0.25 1 198 . 34 MET H H 8.24 0.03 1 199 . 34 MET HA H 4.31 0.03 1 200 . 34 MET CA C 59.52 0.50 1 201 . 34 MET C C 174.80 0.50 1 202 . 34 MET CB C 35.74 0.50 1 203 . 34 MET N N 119.05 0.25 1 204 . 35 ALA H H 7.33 0.03 1 205 . 35 ALA HA H 5.19 0.03 1 206 . 35 ALA HB H 1.78 0.03 1 207 . 35 ALA CA C 50.61 0.50 1 208 . 35 ALA C C 177.20 0.50 1 209 . 35 ALA CB C 23.82 0.50 1 210 . 35 ALA N N 126.73 0.25 1 211 . 36 MET H H 8.80 0.03 1 212 . 36 MET HA H 5.13 0.03 1 213 . 36 MET HB2 H 1.83 0.03 1 214 . 36 MET HB3 H 1.83 0.03 1 215 . 36 MET CA C 56.14 0.50 1 216 . 36 MET C C 173.50 0.50 1 217 . 36 MET CB C 39.48 0.50 1 218 . 36 MET N N 117.94 0.25 1 219 . 37 ALA H H 8.89 0.03 1 220 . 37 ALA HA H 5.32 0.03 1 221 . 37 ALA HB H 1.01 0.03 1 222 . 37 ALA CA C 51.08 0.50 1 223 . 37 ALA C C 176.60 0.50 1 224 . 37 ALA CB C 24.27 0.50 1 225 . 37 ALA N N 122.70 0.25 1 226 . 38 ARG H H 9.14 0.03 1 227 . 38 ARG HA H 5.02 0.03 1 228 . 38 ARG CA C 55.29 0.50 1 229 . 38 ARG C C 176.20 0.50 1 230 . 38 ARG CB C 34.36 0.50 1 231 . 38 ARG N N 121.44 0.25 1 232 . 39 ILE H H 8.85 0.03 1 233 . 39 ILE HA H 4.92 0.03 1 234 . 39 ILE HB H 1.44 0.03 1 235 . 39 ILE CA C 60.11 0.50 1 236 . 39 ILE C C 176.10 0.50 1 237 . 39 ILE CB C 41.27 0.50 1 238 . 39 ILE N N 126.21 0.25 1 239 . 40 SER H H 8.66 0.03 1 240 . 40 SER HA H 4.55 0.03 1 241 . 40 SER HB2 H 3.69 0.03 2 242 . 40 SER HB3 H 3.57 0.03 2 243 . 40 SER CA C 57.95 0.50 1 244 . 40 SER C C 173.00 0.50 1 245 . 40 SER CB C 66.30 0.50 1 246 . 40 SER N N 121.80 0.25 1 247 . 41 PHE H H 8.96 0.03 1 248 . 41 PHE HA H 4.62 0.03 1 249 . 41 PHE HB2 H 3.17 0.03 2 250 . 41 PHE HB3 H 2.80 0.03 2 251 . 41 PHE CA C 59.92 0.50 1 252 . 41 PHE C C 176.80 0.50 1 253 . 41 PHE CB C 40.97 0.50 1 254 . 41 PHE N N 123.14 0.25 1 255 . 42 LEU H H 8.42 0.03 1 256 . 42 LEU HA H 4.53 0.03 1 257 . 42 LEU HB2 H 1.55 0.03 2 258 . 42 LEU HB3 H 1.38 0.03 2 259 . 42 LEU CA C 55.45 0.50 1 260 . 42 LEU C C 177.30 0.50 1 261 . 42 LEU CB C 43.86 0.50 1 262 . 42 LEU N N 126.05 0.25 1 263 . 43 GLY H H 8.25 0.03 1 264 . 43 GLY HA2 H 4.03 0.03 1 265 . 43 GLY HA3 H 4.03 0.03 1 266 . 43 GLY CA C 45.94 0.50 1 267 . 43 GLY C C 174.80 0.50 1 268 . 43 GLY N N 109.65 0.25 1 269 . 44 GLU H H 8.81 0.03 1 270 . 44 GLU HA H 4.06 0.03 1 271 . 44 GLU HB2 H 1.93 0.03 1 272 . 44 GLU HB3 H 1.93 0.03 1 273 . 44 GLU CA C 59.55 0.50 1 274 . 44 GLU C C 178.30 0.50 1 275 . 44 GLU CB C 30.86 0.50 1 276 . 44 GLU N N 121.22 0.25 1 277 . 45 ASP H H 8.38 0.03 1 278 . 45 ASP HA H 4.82 0.03 1 279 . 45 ASP HB2 H 2.95 0.03 2 280 . 45 ASP HB3 H 2.74 0.03 2 281 . 45 ASP CA C 54.91 0.50 1 282 . 45 ASP C C 175.60 0.50 1 283 . 45 ASP CB C 42.81 0.50 1 284 . 45 ASP N N 115.82 0.25 1 285 . 46 GLU H H 7.38 0.03 1 286 . 46 GLU HA H 5.46 0.03 1 287 . 46 GLU HB2 H 1.94 0.03 1 288 . 46 GLU HB3 H 1.94 0.03 1 289 . 46 GLU CA C 56.45 0.50 1 290 . 46 GLU C C 176.04 0.50 1 291 . 46 GLU CB C 34.83 0.50 1 292 . 46 GLU N N 118.62 0.25 1 293 . 47 LEU H H 9.04 0.03 1 294 . 47 LEU HA H 4.80 0.03 1 295 . 47 LEU CA C 55.06 0.50 1 296 . 47 LEU C C 174.80 0.50 1 297 . 47 LEU N N 125.22 0.25 1 298 . 48 LYS H H 8.93 0.03 1 299 . 48 LYS HA H 4.88 0.03 1 300 . 48 LYS CA C 56.17 0.50 1 301 . 48 LYS C C 175.40 0.50 1 302 . 48 LYS CB C 35.63 0.50 1 303 . 48 LYS N N 125.15 0.25 1 304 . 49 VAL H H 8.80 0.03 1 305 . 49 VAL HA H 4.43 0.03 1 306 . 49 VAL HB H 1.57 0.03 1 307 . 49 VAL CA C 61.58 0.50 1 308 . 49 VAL C C 174.70 0.50 1 309 . 49 VAL CB C 35.39 0.50 1 310 . 49 VAL N N 127.46 0.25 1 311 . 50 SER H H 8.26 0.03 1 312 . 50 SER HA H 4.76 0.03 1 313 . 50 SER HB2 H 3.83 0.03 2 314 . 50 SER HB3 H 3.41 0.03 2 315 . 50 SER CA C 57.17 0.50 1 316 . 50 SER C C 173.80 0.50 1 317 . 50 SER CB C 64.99 0.50 1 318 . 50 SER N N 121.67 0.25 1 319 . 51 TYR H H 8.90 0.03 1 320 . 51 TYR HA H 4.77 0.03 1 321 . 51 TYR HB2 H 3.18 0.03 2 322 . 51 TYR HB3 H 3.13 0.03 2 323 . 51 TYR CA C 58.11 0.50 1 324 . 51 TYR C C 177.90 0.50 1 325 . 51 TYR CB C 42.42 0.50 1 326 . 51 TYR N N 123.02 0.25 1 327 . 52 ALA H H 8.50 0.03 1 328 . 52 ALA HA H 4.81 0.03 1 329 . 52 ALA HB H 0.87 0.03 1 330 . 52 ALA CA C 52.98 0.50 1 331 . 52 ALA C C 175.90 0.50 1 332 . 52 ALA CB C 21.87 0.50 1 333 . 52 ALA N N 124.49 0.25 1 334 . 53 VAL H H 9.06 0.03 1 335 . 53 VAL HA H 4.64 0.03 1 336 . 53 VAL HB H 1.73 0.03 1 337 . 53 VAL CA C 59.29 0.50 1 338 . 53 VAL CB C 36.71 0.50 1 339 . 53 VAL N N 125.02 0.25 1 340 . 56 PRO CA C 66.40 0.50 1 341 . 56 PRO C C 178.20 0.50 1 342 . 56 PRO CB C 32.43 0.50 1 343 . 57 ASN H H 8.25 0.03 1 344 . 57 ASN HA H 4.65 0.03 1 345 . 57 ASN HB2 H 2.79 0.03 1 346 . 57 ASN HB3 H 2.79 0.03 1 347 . 57 ASN CA C 53.91 0.50 1 348 . 57 ASN C C 175.90 0.50 1 349 . 57 ASN CB C 39.21 0.50 1 350 . 57 ASN N N 114.85 0.25 1 351 . 58 GLY H H 7.70 0.03 1 352 . 58 GLY HA2 H 4.06 0.03 2 353 . 58 GLY HA3 H 3.94 0.03 2 354 . 58 GLY CA C 47.03 0.50 1 355 . 58 GLY N N 107.32 0.25 1 356 . 61 LYS HA H 5.40 0.03 1 357 . 61 LYS CA C 56.14 0.50 1 358 . 61 LYS C C 177.00 0.50 1 359 . 61 LYS CB C 36.25 0.50 1 360 . 62 TRP H H 7.95 0.03 1 361 . 62 TRP HA H 4.78 0.03 1 362 . 62 TRP HB2 H 3.15 0.03 1 363 . 62 TRP HB3 H 3.15 0.03 1 364 . 62 TRP CA C 57.88 0.50 1 365 . 62 TRP C C 172.80 0.50 1 366 . 62 TRP CB C 31.69 0.50 1 367 . 62 TRP N N 122.97 0.25 1 368 . 63 GLU H H 8.29 0.03 1 369 . 63 GLU HA H 5.53 0.03 1 370 . 63 GLU HB2 H 1.77 0.03 1 371 . 63 GLU HB3 H 1.77 0.03 1 372 . 63 GLU CA C 55.17 0.50 1 373 . 63 GLU C C 176.70 0.50 1 374 . 63 GLU CB C 35.01 0.50 1 375 . 63 GLU N N 118.12 0.25 1 376 . 64 THR H H 8.93 0.03 1 377 . 64 THR HA H 4.46 0.03 1 378 . 64 THR HB H 3.78 0.03 1 379 . 64 THR CA C 63.05 0.50 1 380 . 64 THR C C 172.80 0.50 1 381 . 64 THR CB C 73.12 0.50 1 382 . 64 THR N N 118.91 0.25 1 383 . 65 THR H H 8.36 0.03 1 384 . 65 THR HA H 5.13 0.03 1 385 . 65 THR HB H 3.91 0.03 1 386 . 65 THR CA C 62.69 0.50 1 387 . 65 THR C C 174.60 0.50 1 388 . 65 THR CB C 70.91 0.50 1 389 . 65 THR N N 120.74 0.25 1 390 . 66 PHE H H 8.24 0.03 1 391 . 66 PHE HA H 4.68 0.03 1 392 . 66 PHE CA C 62.43 0.50 1 393 . 66 PHE C C 175.30 0.50 1 394 . 66 PHE CB C 33.11 0.50 1 395 . 66 PHE N N 125.19 0.25 1 396 . 67 LYS H H 8.82 0.03 1 397 . 67 LYS HA H 5.41 0.03 1 398 . 67 LYS HB2 H 1.99 0.03 2 399 . 67 LYS HB3 H 1.83 0.03 2 400 . 67 LYS CA C 55.52 0.50 1 401 . 67 LYS C C 177.60 0.50 1 402 . 67 LYS CB C 37.22 0.50 1 403 . 67 LYS N N 120.68 0.25 1 404 . 68 LYS H H 8.83 0.03 1 405 . 68 LYS CA C 58.56 0.50 1 406 . 68 LYS C C 178.40 0.50 1 407 . 68 LYS CB C 35.23 0.50 1 408 . 68 LYS N N 129.88 0.25 1 409 . 69 THR H H 8.62 0.03 1 410 . 69 THR HA H 4.62 0.03 1 411 . 69 THR HB H 4.44 0.03 1 412 . 69 THR CA C 61.84 0.50 1 413 . 69 THR C C 175.70 0.50 1 414 . 69 THR CB C 70.62 0.50 1 415 . 69 THR N N 119.35 0.25 1 416 . 70 SER H H 8.24 0.03 1 417 . 70 SER HA H 4.35 0.03 1 418 . 70 SER HB2 H 3.98 0.03 2 419 . 70 SER HB3 H 3.79 0.03 2 420 . 70 SER CA C 59.21 0.50 1 421 . 70 SER C C 175.50 0.50 1 422 . 70 SER CB C 64.34 0.50 1 423 . 70 SER N N 112.71 0.25 1 424 . 71 ASP H H 7.86 0.03 1 425 . 71 ASP HA H 4.29 0.03 1 426 . 71 ASP HB2 H 2.61 0.03 2 427 . 71 ASP HB3 H 2.03 0.03 2 428 . 71 ASP CA C 56.09 0.50 1 429 . 71 ASP C C 176.60 0.50 1 430 . 71 ASP CB C 43.09 0.50 1 431 . 71 ASP N N 121.92 0.25 1 432 . 72 ASP H H 8.37 0.03 1 433 . 72 ASP HA H 4.37 0.03 1 434 . 72 ASP HB2 H 2.53 0.03 2 435 . 72 ASP HB3 H 2.45 0.03 2 436 . 72 ASP CA C 56.13 0.50 1 437 . 72 ASP C C 176.80 0.50 1 438 . 72 ASP CB C 42.11 0.50 1 439 . 72 ASP N N 121.54 0.25 1 440 . 73 GLY H H 8.08 0.03 1 441 . 73 GLY HA2 H 3.96 0.03 2 442 . 73 GLY HA3 H 3.69 0.03 2 443 . 73 GLY CA C 45.47 0.50 1 444 . 73 GLY C C 173.90 0.50 1 445 . 73 GLY N N 109.82 0.25 1 446 . 74 GLU H H 8.70 0.03 1 447 . 74 GLU HA H 4.60 0.03 1 448 . 74 GLU CA C 55.66 0.50 1 449 . 74 GLU C C 174.50 0.50 1 450 . 74 GLU CB C 30.98 0.50 1 451 . 74 GLU N N 124.18 0.25 1 452 . 75 VAL H H 7.80 0.03 1 453 . 75 VAL HA H 4.91 0.03 1 454 . 75 VAL HB H 1.96 0.03 1 455 . 75 VAL CA C 62.42 0.50 1 456 . 75 VAL C C 175.10 0.50 1 457 . 75 VAL CB C 34.24 0.50 1 458 . 75 VAL N N 124.50 0.25 1 459 . 76 TYR H H 9.19 0.03 1 460 . 76 TYR HA H 5.15 0.03 1 461 . 76 TYR HB2 H 2.64 0.03 1 462 . 76 TYR HB3 H 2.64 0.03 1 463 . 76 TYR CA C 57.72 0.50 1 464 . 76 TYR C C 175.50 0.50 1 465 . 76 TYR CB C 43.27 0.50 1 466 . 76 TYR N N 125.39 0.25 1 467 . 77 TYR H H 9.38 0.03 1 468 . 77 TYR HA H 5.79 0.03 1 469 . 77 TYR HB2 H 2.90 0.03 2 470 . 77 TYR HB3 H 2.88 0.03 2 471 . 77 TYR CA C 58.01 0.50 1 472 . 77 TYR C C 175.50 0.50 1 473 . 77 TYR CB C 44.71 0.50 1 474 . 77 TYR N N 121.32 0.25 1 475 . 78 SER H H 8.46 0.03 1 476 . 78 SER HA H 4.74 0.03 1 477 . 78 SER HB2 H 3.09 0.03 2 478 . 78 SER HB3 H 2.66 0.03 2 479 . 78 SER CA C 55.65 0.50 1 480 . 78 SER C C 175.10 0.50 1 481 . 78 SER CB C 64.41 0.50 1 482 . 78 SER N N 125.58 0.25 1 483 . 79 GLU H H 8.60 0.03 1 484 . 79 GLU HA H 3.87 0.03 1 485 . 79 GLU HB2 H 2.06 0.03 1 486 . 79 GLU HB3 H 2.06 0.03 1 487 . 79 GLU CA C 59.61 0.50 1 488 . 79 GLU C C 179.60 0.50 1 489 . 79 GLU CB C 30.58 0.50 1 490 . 79 GLU N N 130.88 0.25 1 491 . 80 GLU H H 8.42 0.03 1 492 . 80 GLU HA H 3.91 0.03 1 493 . 80 GLU HB2 H 1.96 0.03 2 494 . 80 GLU HB3 H 1.86 0.03 2 495 . 80 GLU CA C 60.16 0.50 1 496 . 80 GLU C C 178.60 0.50 1 497 . 80 GLU CB C 30.45 0.50 1 498 . 80 GLU N N 119.71 0.25 1 499 . 81 ALA H H 7.28 0.03 1 500 . 81 ALA HA H 4.28 0.03 1 501 . 81 ALA HB H 1.30 0.03 1 502 . 81 ALA CA C 52.38 0.50 1 503 . 81 ALA C C 177.10 0.50 1 504 . 81 ALA CB C 20.75 0.50 1 505 . 81 ALA N N 118.49 0.25 1 506 . 82 LYS H H 7.74 0.03 1 507 . 82 LYS HA H 3.82 0.03 1 508 . 82 LYS CA C 57.08 0.50 1 509 . 82 LYS C C 176.10 0.50 1 510 . 82 LYS CB C 30.54 0.50 1 511 . 82 LYS N N 119.08 0.25 1 512 . 83 LYS H H 7.07 0.03 1 513 . 83 LYS HA H 5.38 0.03 1 514 . 83 LYS CA C 55.50 0.50 1 515 . 83 LYS CB C 40.04 0.50 1 516 . 83 LYS N N 119.10 0.25 1 517 . 86 GLU CA C 54.75 0.50 1 518 . 86 GLU C C 176.80 0.50 1 519 . 86 GLU CB C 34.32 0.50 1 520 . 87 VAL H H 8.69 0.03 1 521 . 87 VAL HA H 4.14 0.03 1 522 . 87 VAL HB H 2.20 0.03 1 523 . 87 VAL CA C 63.37 0.50 1 524 . 87 VAL C C 177.00 0.50 1 525 . 87 VAL CB C 31.97 0.50 1 526 . 87 VAL N N 126.00 0.25 1 527 . 88 LEU H H 8.93 0.03 1 528 . 88 LEU CA C 56.94 0.50 1 529 . 88 LEU C C 178.20 0.50 1 530 . 88 LEU CB C 44.10 0.50 1 531 . 88 LEU N N 128.80 0.25 1 532 . 89 ASP H H 7.02 0.03 1 533 . 89 ASP HA H 4.70 0.03 1 534 . 89 ASP HB2 H 2.73 0.03 1 535 . 89 ASP HB3 H 2.73 0.03 1 536 . 89 ASP CA C 55.88 0.50 1 537 . 89 ASP C C 175.00 0.50 1 538 . 89 ASP CB C 46.51 0.50 1 539 . 89 ASP N N 114.58 0.25 1 540 . 90 THR H H 7.99 0.03 1 541 . 90 THR HA H 3.75 0.03 1 542 . 90 THR HB H 3.83 0.03 1 543 . 90 THR CA C 61.49 0.50 1 544 . 90 THR C C 179.86 0.50 1 545 . 90 THR CB C 69.15 0.50 1 546 . 90 THR N N 120.53 0.25 1 547 . 91 ASP H H 6.70 0.03 1 548 . 91 ASP HA H 4.76 0.03 1 549 . 91 ASP CA C 53.80 0.50 1 550 . 91 ASP C C 177.70 0.50 1 551 . 91 ASP CB C 41.90 0.50 1 552 . 91 ASP N N 123.00 0.25 1 553 . 92 TYR H H 9.30 0.03 1 554 . 92 TYR CA C 62.08 0.50 1 555 . 92 TYR C C 174.90 0.50 1 556 . 92 TYR CB C 36.77 0.50 1 557 . 92 TYR N N 115.90 0.25 1 558 . 93 LYS H H 7.99 0.03 1 559 . 93 LYS HA H 4.59 0.03 1 560 . 93 LYS HB2 H 1.62 0.03 1 561 . 93 LYS HB3 H 1.62 0.03 1 562 . 93 LYS CA C 59.30 0.50 1 563 . 93 LYS C C 176.60 0.50 1 564 . 93 LYS CB C 37.84 0.50 1 565 . 93 LYS N N 113.37 0.25 1 566 . 94 SER H H 11.29 0.03 1 567 . 94 SER HA H 4.78 0.03 1 568 . 94 SER HB2 H 4.17 0.03 2 569 . 94 SER HB3 H 3.81 0.03 2 570 . 94 SER CA C 61.05 0.50 1 571 . 94 SER C C 175.50 0.50 1 572 . 94 SER CB C 68.64 0.50 1 573 . 94 SER N N 120.95 0.25 1 574 . 95 TYR H H 8.40 0.03 1 575 . 95 TYR HA H 6.08 0.03 1 576 . 95 TYR HB2 H 3.22 0.03 2 577 . 95 TYR HB3 H 3.08 0.03 2 578 . 95 TYR CA C 58.52 0.50 1 579 . 95 TYR C C 174.60 0.50 1 580 . 95 TYR CB C 42.75 0.50 1 581 . 95 TYR N N 123.50 0.25 1 582 . 96 ALA H H 9.01 0.03 1 583 . 96 ALA HA H 4.53 0.03 1 584 . 96 ALA HB H 0.90 0.03 1 585 . 96 ALA CA C 53.37 0.50 1 586 . 96 ALA C C 175.70 0.50 1 587 . 96 ALA CB C 24.23 0.50 1 588 . 96 ALA N N 121.67 0.25 1 589 . 97 VAL H H 9.26 0.03 1 590 . 97 VAL HA H 4.95 0.03 1 591 . 97 VAL HB H 2.09 0.03 1 592 . 97 VAL CA C 63.45 0.50 1 593 . 97 VAL C C 175.00 0.50 1 594 . 97 VAL CB C 33.48 0.50 1 595 . 97 VAL N N 122.55 0.25 1 596 . 98 ILE H H 9.50 0.03 1 597 . 98 ILE HA H 5.07 0.03 1 598 . 98 ILE HB H 1.91 0.03 1 599 . 98 ILE CA C 58.91 0.50 1 600 . 98 ILE C C 175.20 0.50 1 601 . 98 ILE CB C 42.54 0.50 1 602 . 98 ILE N N 131.11 0.25 1 603 . 99 TYR H H 9.47 0.03 1 604 . 99 TYR HA H 5.19 0.03 1 605 . 99 TYR HB2 H 2.59 0.03 1 606 . 99 TYR HB3 H 2.59 0.03 1 607 . 99 TYR CA C 57.79 0.50 1 608 . 99 TYR C C 174.80 0.50 1 609 . 99 TYR CB C 42.17 0.50 1 610 . 99 TYR N N 128.87 0.25 1 611 . 100 ALA H H 9.53 0.03 1 612 . 100 ALA HA H 5.63 0.03 1 613 . 100 ALA HB H 1.42 0.03 1 614 . 100 ALA CA C 51.41 0.50 1 615 . 100 ALA C C 176.60 0.50 1 616 . 100 ALA CB C 24.85 0.50 1 617 . 100 ALA N N 135.26 0.25 1 618 . 101 THR H H 9.35 0.03 1 619 . 101 THR HA H 5.33 0.03 1 620 . 101 THR HB H 3.94 0.03 1 621 . 101 THR CA C 62.05 0.50 1 622 . 101 THR C C 174.60 0.50 1 623 . 101 THR CB C 73.12 0.50 1 624 . 101 THR N N 117.35 0.25 1 625 . 102 ARG H H 8.91 0.03 1 626 . 102 ARG HA H 5.17 0.03 1 627 . 102 ARG CA C 55.38 0.50 1 628 . 102 ARG C C 175.00 0.50 1 629 . 102 ARG CB C 36.22 0.50 1 630 . 102 ARG N N 126.75 0.25 1 631 . 103 VAL H H 7.74 0.03 1 632 . 103 VAL HA H 4.68 0.03 1 633 . 103 VAL CA C 62.43 0.50 1 634 . 103 VAL C C 176.70 0.50 1 635 . 103 VAL CB C 33.31 0.50 1 636 . 103 VAL N N 123.16 0.25 1 637 . 104 LYS H H 8.88 0.03 1 638 . 104 LYS HA H 4.33 0.03 1 639 . 104 LYS HB2 H 1.41 0.03 1 640 . 104 LYS HB3 H 1.41 0.03 1 641 . 104 LYS CA C 55.97 0.50 1 642 . 104 LYS CB C 36.55 0.50 1 643 . 104 LYS N N 130.93 0.25 1 644 . 105 ASP H H 9.39 0.03 1 645 . 105 ASP HA H 4.66 0.03 1 646 . 105 ASP CA C 56.45 0.50 1 647 . 105 ASP C C 176.80 0.50 1 648 . 105 ASP CB C 40.53 0.50 1 649 . 105 ASP N N 130.04 0.25 1 650 . 106 GLY H H 8.24 0.03 1 651 . 106 GLY HA2 H 4.02 0.03 2 652 . 106 GLY HA3 H 3.45 0.03 2 653 . 106 GLY CA C 46.34 0.50 1 654 . 106 GLY C C 174.60 0.50 1 655 . 106 GLY N N 103.63 0.25 1 656 . 107 ARG H H 7.78 0.03 1 657 . 107 ARG HA H 4.58 0.03 1 658 . 107 ARG HB2 H 1.73 0.03 1 659 . 107 ARG HB3 H 1.73 0.03 1 660 . 107 ARG CA C 55.40 0.50 1 661 . 107 ARG C C 175.60 0.50 1 662 . 107 ARG CB C 33.35 0.50 1 663 . 107 ARG N N 122.00 0.25 1 664 . 108 THR H H 8.56 0.03 1 665 . 108 THR HA H 4.40 0.03 1 666 . 108 THR HB H 3.86 0.03 1 667 . 108 THR CA C 64.18 0.50 1 668 . 108 THR C C 174.40 0.50 1 669 . 108 THR CB C 69.73 0.50 1 670 . 108 THR N N 119.62 0.25 1 671 . 109 LEU H H 9.13 0.03 1 672 . 109 LEU HA H 4.63 0.03 1 673 . 109 LEU CA C 54.27 0.50 1 674 . 109 LEU C C 176.70 0.50 1 675 . 109 LEU N N 129.73 0.25 1 676 . 110 HIS H H 8.39 0.03 1 677 . 110 HIS HA H 5.94 0.03 1 678 . 110 HIS HB2 H 2.96 0.03 2 679 . 110 HIS HB3 H 2.89 0.03 2 680 . 110 HIS CA C 55.28 0.50 1 681 . 110 HIS C C 176.10 0.50 1 682 . 110 HIS CB C 34.39 0.50 1 683 . 110 HIS N N 116.91 0.25 1 684 . 111 MET H H 9.01 0.03 1 685 . 111 MET HA H 4.49 0.03 1 686 . 111 MET HB2 H 1.83 0.03 1 687 . 111 MET HB3 H 1.83 0.03 1 688 . 111 MET CA C 56.25 0.50 1 689 . 111 MET C C 174.90 0.50 1 690 . 111 MET CB C 37.58 0.50 1 691 . 111 MET N N 124.18 0.25 1 692 . 112 MET H H 9.06 0.03 1 693 . 112 MET HA H 5.58 0.03 1 694 . 112 MET HB2 H 2.05 0.03 1 695 . 112 MET HB3 H 2.05 0.03 1 696 . 112 MET CA C 55.32 0.50 1 697 . 112 MET C C 176.50 0.50 1 698 . 112 MET CB C 37.15 0.50 1 699 . 112 MET N N 123.86 0.25 1 700 . 113 ARG H H 9.37 0.03 1 701 . 113 ARG HA H 5.00 0.03 1 702 . 113 ARG CA C 55.67 0.50 1 703 . 113 ARG C C 175.00 0.50 1 704 . 113 ARG CB C 38.27 0.50 1 705 . 113 ARG N N 120.04 0.25 1 706 . 114 LEU H H 7.96 0.03 1 707 . 114 LEU HA H 4.99 0.03 1 708 . 114 LEU HB2 H 2.24 0.03 1 709 . 114 LEU HB3 H 2.24 0.03 1 710 . 114 LEU CA C 54.25 0.50 1 711 . 114 LEU C C 175.33 0.50 1 712 . 114 LEU CB C 43.89 0.50 1 713 . 114 LEU N N 125.31 0.25 1 714 . 115 TYR H H 9.54 0.03 1 715 . 115 TYR CA C 58.11 0.50 1 716 . 115 TYR C C 177.70 0.50 1 717 . 115 TYR N N 126.76 0.25 1 718 . 116 SER H H 9.85 0.03 1 719 . 116 SER HA H 5.73 0.03 1 720 . 116 SER HB2 H 3.89 0.03 2 721 . 116 SER HB3 H 3.59 0.03 2 722 . 116 SER CA C 56.55 0.50 1 723 . 116 SER C C 176.40 0.50 1 724 . 116 SER CB C 67.66 0.50 1 725 . 116 SER N N 113.93 0.25 1 726 . 117 ARG H H 8.25 0.03 1 727 . 117 ARG HA H 3.60 0.03 1 728 . 117 ARG HB2 H 1.79 0.03 2 729 . 117 ARG HB3 H 1.28 0.03 2 730 . 117 ARG CA C 58.08 0.50 1 731 . 117 ARG C C 176.40 0.50 1 732 . 117 ARG CB C 32.45 0.50 1 733 . 117 ARG N N 131.38 0.25 1 734 . 118 SER H H 7.87 0.03 1 735 . 118 SER HA H 4.90 0.03 1 736 . 118 SER HB2 H 3.88 0.03 2 737 . 118 SER HB3 H 3.59 0.03 2 738 . 118 SER CA C 54.79 0.50 1 739 . 118 SER CB C 65.77 0.50 1 740 . 118 SER N N 111.94 0.25 1 741 . 119 PRO HA H 4.01 0.03 1 742 . 119 PRO HB2 H 2.23 0.03 2 743 . 119 PRO HB3 H 1.94 0.03 2 744 . 119 PRO CA C 64.97 0.50 1 745 . 119 PRO C C 176.50 0.50 1 746 . 119 PRO CB C 32.43 0.50 1 747 . 120 GLU H H 7.30 0.03 1 748 . 120 GLU HA H 4.17 0.03 1 749 . 120 GLU HB2 H 1.74 0.03 2 750 . 120 GLU HB3 H 1.69 0.03 2 751 . 120 GLU CA C 55.88 0.50 1 752 . 120 GLU C C 175.50 0.50 1 753 . 120 GLU CB C 29.71 0.50 1 754 . 120 GLU N N 118.13 0.25 1 755 . 121 VAL H H 7.81 0.03 1 756 . 121 VAL HA H 4.07 0.03 1 757 . 121 VAL HB H 1.76 0.03 1 758 . 121 VAL CA C 61.71 0.50 1 759 . 121 VAL C C 175.50 0.50 1 760 . 121 VAL CB C 34.22 0.50 1 761 . 121 VAL N N 125.71 0.25 1 762 . 122 SER H H 8.57 0.03 1 763 . 122 SER HA H 4.68 0.03 1 764 . 122 SER HB2 H 4.20 0.03 2 765 . 122 SER HB3 H 3.88 0.03 2 766 . 122 SER CA C 57.23 0.50 1 767 . 122 SER CB C 64.40 0.50 1 768 . 122 SER N N 125.18 0.25 1 769 . 123 PRO HA H 4.26 0.03 1 770 . 123 PRO HB2 H 2.29 0.03 2 771 . 123 PRO HB3 H 1.87 0.03 2 772 . 123 PRO CA C 65.91 0.50 1 773 . 123 PRO C C 180.40 0.50 1 774 . 123 PRO CB C 32.57 0.50 1 775 . 124 ALA H H 7.93 0.03 1 776 . 124 ALA HA H 4.01 0.03 1 777 . 124 ALA HB H 1.23 0.03 1 778 . 124 ALA CA C 55.92 0.50 1 779 . 124 ALA C C 180.90 0.50 1 780 . 124 ALA CB C 19.15 0.50 1 781 . 124 ALA N N 120.88 0.25 1 782 . 125 ALA H H 7.41 0.03 1 783 . 125 ALA HA H 3.37 0.03 1 784 . 125 ALA HB H 1.08 0.03 1 785 . 125 ALA CA C 55.59 0.50 1 786 . 125 ALA C C 180.20 0.50 1 787 . 125 ALA CB C 19.36 0.50 1 788 . 125 ALA N N 121.76 0.25 1 789 . 126 THR H H 7.73 0.03 1 790 . 126 THR HA H 4.08 0.03 1 791 . 126 THR HB H 3.52 0.03 1 792 . 126 THR CA C 67.66 0.50 1 793 . 126 THR C C 177.20 0.50 1 794 . 126 THR CB C 68.88 0.50 1 795 . 126 THR N N 113.98 0.25 1 796 . 127 ALA H H 7.80 0.03 1 797 . 127 ALA HA H 4.01 0.03 1 798 . 127 ALA HB H 1.36 0.03 1 799 . 127 ALA CA C 56.33 0.50 1 800 . 127 ALA C C 172.36 0.50 1 801 . 127 ALA CB C 18.76 0.50 1 802 . 127 ALA N N 123.92 0.25 1 803 . 128 ILE H H 7.55 0.03 1 804 . 128 ILE HA H 3.67 0.03 1 805 . 128 ILE HB H 1.62 0.03 1 806 . 128 ILE CA C 65.67 0.50 1 807 . 128 ILE C C 178.40 0.50 1 808 . 128 ILE CB C 39.51 0.50 1 809 . 128 ILE N N 121.69 0.25 1 810 . 129 PHE H H 8.16 0.03 1 811 . 129 PHE HA H 3.94 0.03 1 812 . 129 PHE HB2 H 3.20 0.03 2 813 . 129 PHE HB3 H 3.13 0.03 2 814 . 129 PHE CA C 63.35 0.50 1 815 . 129 PHE C C 177.10 0.50 1 816 . 129 PHE CB C 41.12 0.50 1 817 . 129 PHE N N 120.96 0.25 1 818 . 130 ARG H H 8.55 0.03 1 819 . 130 ARG HA H 3.48 0.03 1 820 . 130 ARG HB2 H 1.88 0.03 2 821 . 130 ARG HB3 H 1.75 0.03 2 822 . 130 ARG CA C 61.04 0.50 1 823 . 130 ARG C C 180.40 0.50 1 824 . 130 ARG CB C 30.75 0.50 1 825 . 130 ARG N N 117.06 0.25 1 826 . 131 LYS H H 7.92 0.03 1 827 . 131 LYS HA H 3.95 0.03 1 828 . 131 LYS HB2 H 1.83 0.03 1 829 . 131 LYS HB3 H 1.83 0.03 1 830 . 131 LYS CA C 60.41 0.50 1 831 . 131 LYS C C 180.30 0.50 1 832 . 131 LYS CB C 33.42 0.50 1 833 . 131 LYS N N 122.91 0.25 1 834 . 132 LEU H H 8.35 0.03 1 835 . 132 LEU HA H 3.86 0.03 1 836 . 132 LEU HB2 H 1.63 0.03 1 837 . 132 LEU HB3 H 1.63 0.03 1 838 . 132 LEU CA C 58.58 0.50 1 839 . 132 LEU C C 180.60 0.50 1 840 . 132 LEU CB C 42.45 0.50 1 841 . 132 LEU N N 120.95 0.25 1 842 . 133 ALA H H 8.66 0.03 1 843 . 133 ALA HA H 3.89 0.03 1 844 . 133 ALA HB H 0.79 0.03 1 845 . 133 ALA CA C 56.04 0.50 1 846 . 133 ALA C C 171.89 0.50 1 847 . 133 ALA CB C 16.93 0.50 1 848 . 133 ALA N N 123.18 0.25 1 849 . 134 GLY H H 8.03 0.03 1 850 . 134 GLY HA2 H 3.81 0.03 1 851 . 134 GLY HA3 H 3.81 0.03 1 852 . 134 GLY CA C 48.08 0.50 1 853 . 134 GLY C C 179.20 0.50 1 854 . 134 GLY N N 108.18 0.25 1 855 . 135 GLU H H 7.63 0.03 1 856 . 135 GLU HA H 3.98 0.03 1 857 . 135 GLU HB2 H 1.95 0.03 1 858 . 135 GLU HB3 H 1.95 0.03 1 859 . 135 GLU CA C 59.38 0.50 1 860 . 135 GLU C C 178.40 0.50 1 861 . 135 GLU CB C 30.51 0.50 1 862 . 135 GLU N N 122.63 0.25 1 863 . 136 ARG H H 7.03 0.03 1 864 . 136 ARG HA H 4.05 0.03 1 865 . 136 ARG HB2 H 1.30 0.03 1 866 . 136 ARG HB3 H 1.30 0.03 1 867 . 136 ARG CA C 55.78 0.50 1 868 . 136 ARG C C 174.50 0.50 1 869 . 136 ARG CB C 29.48 0.50 1 870 . 136 ARG N N 118.75 0.25 1 871 . 137 ASN H H 7.47 0.03 1 872 . 137 ASN HA H 4.06 0.03 1 873 . 137 ASN HB2 H 2.79 0.03 2 874 . 137 ASN HB3 H 2.72 0.03 2 875 . 137 ASN CA C 55.79 0.50 1 876 . 137 ASN C C 175.20 0.50 1 877 . 137 ASN CB C 37.14 0.50 1 878 . 137 ASN N N 110.33 0.25 1 879 . 138 TYR H H 7.92 0.03 1 880 . 138 TYR HA H 5.22 0.03 1 881 . 138 TYR HB2 H 2.50 0.03 2 882 . 138 TYR HB3 H 2.45 0.03 2 883 . 138 TYR CA C 57.67 0.50 1 884 . 138 TYR C C 176.80 0.50 1 885 . 138 TYR CB C 37.57 0.50 1 886 . 138 TYR N N 119.40 0.25 1 887 . 139 THR H H 7.64 0.03 1 888 . 139 THR HA H 4.34 0.03 1 889 . 139 THR HB H 4.63 0.03 1 890 . 139 THR CA C 61.40 0.50 1 891 . 139 THR C C 176.50 0.50 1 892 . 139 THR CB C 71.19 0.50 1 893 . 139 THR N N 115.69 0.25 1 894 . 140 ASP H H 8.52 0.03 1 895 . 140 ASP HA H 4.18 0.03 1 896 . 140 ASP HB2 H 2.61 0.03 1 897 . 140 ASP HB3 H 2.61 0.03 1 898 . 140 ASP CA C 59.04 0.50 1 899 . 140 ASP C C 179.40 0.50 1 900 . 140 ASP CB C 41.89 0.50 1 901 . 140 ASP N N 118.66 0.25 1 902 . 141 GLU H H 8.41 0.03 1 903 . 141 GLU HA H 4.19 0.03 1 904 . 141 GLU HB2 H 2.03 0.03 2 905 . 141 GLU HB3 H 1.97 0.03 2 906 . 141 GLU CA C 59.08 0.50 1 907 . 141 GLU C C 177.20 0.50 1 908 . 141 GLU CB C 30.12 0.50 1 909 . 141 GLU N N 117.55 0.25 1 910 . 142 MET H H 7.87 0.03 1 911 . 142 MET HA H 4.42 0.03 1 912 . 142 MET CA C 56.95 0.50 1 913 . 142 MET C C 173.90 0.50 1 914 . 142 MET CB C 33.63 0.50 1 915 . 142 MET N N 118.24 0.25 1 916 . 143 VAL H H 7.03 0.03 1 917 . 143 VAL HA H 4.71 0.03 1 918 . 143 VAL HB H 2.04 0.03 1 919 . 143 VAL CA C 62.32 0.50 1 920 . 143 VAL C C 176.60 0.50 1 921 . 143 VAL CB C 34.49 0.50 1 922 . 143 VAL N N 117.58 0.25 1 923 . 144 ALA H H 9.52 0.03 1 924 . 144 ALA HA H 4.74 0.03 1 925 . 144 ALA HB H 1.21 0.03 1 926 . 144 ALA CA C 51.49 0.50 1 927 . 144 ALA C C 176.80 0.50 1 928 . 144 ALA CB C 22.72 0.50 1 929 . 144 ALA N N 131.82 0.25 1 930 . 145 MET H H 8.53 0.03 1 931 . 145 MET HA H 4.85 0.03 1 932 . 145 MET HB2 H 1.99 0.03 2 933 . 145 MET HB3 H 1.93 0.03 2 934 . 145 MET CA C 54.06 0.50 1 935 . 145 MET C C 177.90 0.50 1 936 . 145 MET CB C 30.13 0.50 1 937 . 145 MET N N 123.10 0.25 1 938 . 146 LEU H H 7.81 0.03 1 939 . 146 LEU CB C 42.96 0.50 1 940 . 146 LEU N N 126.17 0.25 1 941 . 147 PRO HA H 4.49 0.03 1 942 . 147 PRO HB2 H 2.31 0.03 2 943 . 147 PRO HB3 H 1.84 0.03 2 944 . 147 PRO CA C 63.23 0.50 1 945 . 147 PRO C C 177.30 0.50 1 946 . 147 PRO CB C 33.73 0.50 1 947 . 148 ARG H H 8.43 0.03 1 948 . 148 ARG HA H 4.18 0.03 1 949 . 148 ARG HB2 H 1.74 0.03 2 950 . 148 ARG HB3 H 1.68 0.03 2 951 . 148 ARG CA C 58.35 0.50 1 952 . 148 ARG C C 176.50 0.50 1 953 . 148 ARG CB C 32.54 0.50 1 954 . 148 ARG N N 121.39 0.25 1 955 . 149 GLN H H 7.66 0.03 1 956 . 149 GLN HA H 4.61 0.03 1 957 . 149 GLN HB2 H 2.06 0.03 1 958 . 149 GLN HB3 H 2.06 0.03 1 959 . 149 GLN CA C 55.72 0.50 1 960 . 149 GLN C C 175.30 0.50 1 961 . 149 GLN CB C 29.67 0.50 1 962 . 149 GLN N N 115.79 0.25 1 963 . 150 GLU H H 8.47 0.03 1 964 . 150 GLU HA H 4.38 0.03 1 965 . 150 GLU HB2 H 2.12 0.03 2 966 . 150 GLU HB3 H 1.63 0.03 2 967 . 150 GLU CA C 56.22 0.50 1 968 . 150 GLU C C 176.70 0.50 1 969 . 150 GLU CB C 32.42 0.50 1 970 . 150 GLU N N 118.54 0.25 1 971 . 151 GLU H H 7.92 0.03 1 972 . 151 GLU HA H 4.17 0.03 1 973 . 151 GLU HB2 H 1.99 0.03 1 974 . 151 GLU HB3 H 1.99 0.03 1 975 . 151 GLU CA C 59.47 0.50 1 976 . 151 GLU C C 177.00 0.50 1 977 . 151 GLU CB C 32.29 0.50 1 978 . 151 GLU N N 119.93 0.25 1 979 . 152 CYS H H 9.52 0.03 1 980 . 152 CYS HA H 5.07 0.03 1 981 . 152 CYS HB2 H 3.01 0.03 1 982 . 152 CYS HB3 H 3.01 0.03 1 983 . 152 CYS CA C 53.99 0.50 1 984 . 152 CYS C C 173.80 0.50 1 985 . 152 CYS CB C 35.04 0.50 1 986 . 152 CYS N N 122.88 0.25 1 987 . 153 THR H H 8.40 0.03 1 988 . 153 THR HA H 4.80 0.03 1 989 . 153 THR HB H 4.03 0.03 1 990 . 153 THR CA C 59.86 0.50 1 991 . 153 THR C C 173.90 0.50 1 992 . 153 THR CB C 72.48 0.50 1 993 . 153 THR N N 118.84 0.25 1 994 . 154 VAL H H 6.85 0.03 1 995 . 154 VAL HA H 4.04 0.03 1 996 . 154 VAL HB H 1.91 0.03 1 997 . 154 VAL CA C 62.03 0.50 1 998 . 154 VAL C C 176.60 0.50 1 999 . 154 VAL CB C 33.32 0.50 1 1000 . 154 VAL N N 115.82 0.25 1 1001 . 155 ASP H H 8.29 0.03 1 1002 . 155 ASP HA H 4.42 0.03 1 1003 . 155 ASP HB2 H 2.59 0.03 2 1004 . 155 ASP HB3 H 2.34 0.03 2 1005 . 155 ASP CA C 55.77 0.50 1 1006 . 155 ASP C C 176.90 0.50 1 1007 . 155 ASP CB C 42.40 0.50 1 1008 . 155 ASP N N 124.82 0.25 1 1009 . 156 GLU H H 8.35 0.03 1 1010 . 156 GLU HA H 4.11 0.03 1 1011 . 156 GLU HB2 H 1.93 0.03 2 1012 . 156 GLU HB3 H 1.73 0.03 2 1013 . 156 GLU CA C 57.49 0.50 1 1014 . 156 GLU C C 176.45 0.50 1 1015 . 156 GLU CB C 31.50 0.50 1 1016 . 156 GLU N N 121.83 0.25 1 1017 . 157 VAL H H 7.52 0.03 1 1018 . 157 VAL HA H 3.88 0.03 1 1019 . 157 VAL HB H 1.94 0.03 1 1020 . 157 VAL CA C 64.39 0.50 1 1021 . 157 VAL CB C 34.33 0.50 1 1022 . 157 VAL N N 124.69 0.25 1 stop_ save_