data_50335 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; FLASH_1923 ; _BMRB_accession_number 50335 _BMRB_flat_file_name bmr50335.str _Entry_type original _Submission_date 2020-06-22 _Accession_date 2020-06-22 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'fragment FLASH protein 1923-1982' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bucholc Katarzyna . . 2 Skrajna Aleksandra . . 3 Adamska Kinga . . 4 Yang Xiao-Cui . . 5 Krajewski Krzysztof . . 6 Poznanski Jaroslaw . . 7 Dadlez Michal . . 8 Dominski Zbigniew . . 9 Zhukov Igor . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 415 "13C chemical shifts" 290 "15N chemical shifts" 66 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-08-25 original BMRB . stop_ _Original_release_date 2020-06-22 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural Analysis of the SANT/Myb Domain of FLASH and YARP Proteins and Their Complex with the C-Terminal Fragment of NPAT by NMR Spectroscopy and Computer Simulations ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32722282 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bucholc Katarzyna . . 2 Skrajna Aleksandra . . 3 Adamska Kinga . . 4 Yang Xiao-Cui . . 5 Krajewski Krzysztof . . 6 Poznanski Jaroslaw . . 7 Dadlez Michal . . 8 Dominski Zbigniew . . 9 Zhukov Igor . . stop_ _Journal_abbreviation 'Int. J. Mol. Sci.' _Journal_name_full 'International journal of molecular sciences' _Journal_volume 21 _Journal_issue 15 _Journal_ISSN 1422-0067 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5268 _Page_last 5268 _Year 2020 _Details . loop_ _Keyword 'Histone Locus Body, SANT domain, Myb DNA binding domain, NMR spectroscopy' stop_ save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name 'FLASH 1923' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'FLASH 1923' $entity_1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'Required for histone gene transcription and progression through S phase' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 60 _Mol_residue_sequence ; GEIIILWTRNDDREILLECQ KRGPSFKTFAYLAAKLDKNP NQVSERFQQLMKLFEKSKCR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1923 GLY 2 1924 GLU 3 1925 ILE 4 1926 ILE 5 1927 ILE 6 1928 LEU 7 1929 TRP 8 1930 THR 9 1931 ARG 10 1932 ASN 11 1933 ASP 12 1934 ASP 13 1935 ARG 14 1936 GLU 15 1937 ILE 16 1938 LEU 17 1939 LEU 18 1940 GLU 19 1941 CYS 20 1942 GLN 21 1943 LYS 22 1944 ARG 23 1945 GLY 24 1946 PRO 25 1947 SER 26 1948 PHE 27 1949 LYS 28 1950 THR 29 1951 PHE 30 1952 ALA 31 1953 TYR 32 1954 LEU 33 1955 ALA 34 1956 ALA 35 1957 LYS 36 1958 LEU 37 1959 ASP 38 1960 LYS 39 1961 ASN 40 1962 PRO 41 1963 ASN 42 1964 GLN 43 1965 VAL 44 1966 SER 45 1967 GLU 46 1968 ARG 47 1969 PHE 48 1970 GLN 49 1971 GLN 50 1972 LEU 51 1973 MET 52 1974 LYS 53 1975 LEU 54 1976 PHE 55 1977 GLU 56 1978 LYS 57 1979 SER 58 1980 LYS 59 1981 CYS 60 1982 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 UNP Q9UKL3 'CASP8-associated protein 2' . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source_1 _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $entity_1 'recombinant technology' . Escherichia coli . plasmid pET28a 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 $entity_1 0.4 mM '[U-99% 13C; U-99% 15N]' $entity_1 0.4 mM '[U-99% 15N]' TRIS-d11 25 mM 'natural abundance' KCl 250 mM 'natural abundance' Arg+Glu 50 mM 'natural abundance' TCEP 40 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name NMRPipe _Version . loop_ _Task processing stop_ _Details . save_ save_software_2 _Saveframe_category software _Name NMRFAM-SPARKY _Version . loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name CYANA _Version . loop_ _Task 'structure solution' stop_ _Details . save_ save_software_4 _Saveframe_category software _Name Chimera _Version . loop_ _Task 'data analysis' stop_ _Details . save_ save_software_5 _Saveframe_category software _Name YASARA _Version . loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Agilent _Model 'Uniform NMR System' _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aliphatic_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aromatic_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aromatic' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_3D_HCACO_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_aliphatic_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY aliphatic' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_aromatic_14 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY aromatic' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '25 mM TRIS-d11, 90%/10% H2O/D2O, 250 mM KCl, 50 mM Arg+Glu, 40 mM TCEP, pH 6.2' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 250 10 mM pH 6.2 0.2 pH pressure 1 . atm temperature 298 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_1 _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 C 13 'methyl protons' ppm 0.0 external indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 external direct . . . 1 DSS N 15 'methyl protons' ppm 0.0 external indirect . . . 0.101329118 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $software_2 stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC aliphatic' '2D 1H-13C HSQC aromatic' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name 'FLASH 1923' _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 1923 1 GLY H H 8.49 0.02 1 2 1923 1 GLY HA2 H 3.94 0.02 2 3 1923 1 GLY HA3 H 4.06 0.02 2 4 1923 1 GLY C C 173.93 0.20 1 5 1923 1 GLY CA C 45.39 0.20 1 6 1923 1 GLY N N 110.30 0.20 1 7 1924 2 GLU H H 8.14 0.02 1 8 1924 2 GLU HA H 4.13 0.02 1 9 1924 2 GLU HB2 H 1.43 0.02 2 10 1924 2 GLU HB3 H 1.79 0.02 2 11 1924 2 GLU HG2 H 1.79 0.02 2 12 1924 2 GLU HG3 H 1.80 0.02 2 13 1924 2 GLU C C 175.98 0.20 1 14 1924 2 GLU CA C 60.86 0.20 1 15 1924 2 GLU CB C 27.45 0.20 1 16 1924 2 GLU CG C 38.70 0.20 1 17 1924 2 GLU N N 120.54 0.20 1 18 1925 3 ILE H H 8.23 0.02 1 19 1925 3 ILE HA H 4.13 0.02 1 20 1925 3 ILE HB H 1.79 0.02 1 21 1925 3 ILE HG12 H 1.13 0.02 2 22 1925 3 ILE HG13 H 1.44 0.02 2 23 1925 3 ILE HG2 H 0.80 0.02 1 24 1925 3 ILE HD1 H 0.80 0.02 1 25 1925 3 ILE C C 175.66 0.20 1 26 1925 3 ILE CA C 60.81 0.20 1 27 1925 3 ILE CB C 38.74 0.20 1 28 1925 3 ILE CG1 C 27.41 0.20 1 29 1925 3 ILE CG2 C 17.56 0.20 1 30 1925 3 ILE CD1 C 12.80 0.20 1 31 1925 3 ILE N N 122.61 0.20 1 32 1926 4 ILE H H 8.23 0.02 1 33 1926 4 ILE HA H 4.14 0.02 1 34 1926 4 ILE HB H 1.76 0.02 1 35 1926 4 ILE HG12 H 1.13 0.02 2 36 1926 4 ILE HG13 H 1.44 0.02 2 37 1926 4 ILE HG2 H 0.80 0.02 1 38 1926 4 ILE HD1 H 0.80 0.02 1 39 1926 4 ILE C C 175.57 0.20 1 40 1926 4 ILE CA C 60.78 0.20 1 41 1926 4 ILE CB C 38.70 0.20 1 42 1926 4 ILE CG1 C 27.41 0.20 1 43 1926 4 ILE CG2 C 17.54 0.20 1 44 1926 4 ILE CD1 C 17.47 0.20 1 45 1926 4 ILE N N 126.59 0.20 1 46 1927 5 ILE H H 8.27 0.02 1 47 1927 5 ILE HA H 3.93 0.02 1 48 1927 5 ILE HB H 1.65 0.02 1 49 1927 5 ILE HG12 H 1.05 0.02 2 50 1927 5 ILE HG13 H 1.27 0.02 2 51 1927 5 ILE HG2 H 0.18 0.02 1 52 1927 5 ILE HD1 H 0.70 0.02 1 53 1927 5 ILE C C 174.81 0.20 1 54 1927 5 ILE CA C 59.97 0.20 1 55 1927 5 ILE CB C 38.40 0.20 1 56 1927 5 ILE CG1 C 27.16 0.20 1 57 1927 5 ILE CG2 C 17.04 0.20 1 58 1927 5 ILE CD1 C 12.52 0.20 1 59 1927 5 ILE N N 127.15 0.20 1 60 1928 6 LEU H H 8.18 0.02 1 61 1928 6 LEU HA H 4.35 0.02 1 62 1928 6 LEU HB2 H 1.34 0.02 2 63 1928 6 LEU HB3 H 1.43 0.02 2 64 1928 6 LEU HG H 1.37 0.02 1 65 1928 6 LEU HD1 H 0.77 0.02 2 66 1928 6 LEU HD2 H 0.80 0.02 2 67 1928 6 LEU C C 175.63 0.20 1 68 1928 6 LEU CA C 54.40 0.20 1 69 1928 6 LEU CB C 42.26 0.20 1 70 1928 6 LEU CG C 27.03 0.20 1 71 1928 6 LEU CD1 C 23.84 0.20 1 72 1928 6 LEU CD2 C 24.50 0.20 1 73 1928 6 LEU N N 128.04 0.20 1 74 1929 7 TRP H H 7.97 0.02 1 75 1929 7 TRP HA H 4.89 0.02 1 76 1929 7 TRP HB2 H 2.93 0.02 2 77 1929 7 TRP HB3 H 3.44 0.02 2 78 1929 7 TRP HD1 H 7.23 0.02 1 79 1929 7 TRP HE1 H 10.14 0.02 1 80 1929 7 TRP HE3 H 7.23 0.02 1 81 1929 7 TRP HZ2 H 7.23 0.02 1 82 1929 7 TRP HZ3 H 6.56 0.02 1 83 1929 7 TRP HH2 H 6.56 0.02 1 84 1929 7 TRP C C 177.50 0.20 1 85 1929 7 TRP CA C 55.67 0.20 1 86 1929 7 TRP CB C 31.13 0.20 1 87 1929 7 TRP CD1 C 128.09 0.20 1 88 1929 7 TRP CE3 C 115.00 0.20 1 89 1929 7 TRP CZ2 C 115.02 0.20 1 90 1929 7 TRP CZ3 C 121.68 0.20 1 91 1929 7 TRP CH2 C 121.69 0.20 1 92 1929 7 TRP N N 123.76 0.20 1 93 1929 7 TRP NE1 N 129.32 0.20 1 94 1930 8 THR H H 9.58 0.02 1 95 1930 8 THR HA H 4.75 0.02 1 96 1930 8 THR HB H 4.76 0.02 1 97 1930 8 THR HG1 H 3.45 0.02 1 98 1930 8 THR HG2 H 1.32 0.02 1 99 1930 8 THR C C 175.17 0.20 1 100 1930 8 THR CA C 60.28 0.20 1 101 1930 8 THR CB C 71.65 0.20 1 102 1930 8 THR CG2 C 21.88 0.20 1 103 1930 8 THR N N 117.03 0.20 1 104 1931 9 ARG H H 8.87 0.02 1 105 1931 9 ARG HA H 4.18 0.02 1 106 1931 9 ARG HB2 H 1.90 0.02 2 107 1931 9 ARG HB3 H 1.94 0.02 2 108 1931 9 ARG HG2 H 1.90 0.02 2 109 1931 9 ARG HG3 H 1.95 0.02 2 110 1931 9 ARG HD2 H 3.27 0.02 2 111 1931 9 ARG HD3 H 3.27 0.02 2 112 1931 9 ARG HE H 8.87 0.02 1 113 1931 9 ARG C C 179.44 0.20 1 114 1931 9 ARG CA C 59.25 0.20 1 115 1931 9 ARG CB C 29.83 0.20 1 116 1931 9 ARG CG C 29.81 0.20 1 117 1931 9 ARG CD C 43.39 0.20 1 118 1931 9 ARG N N 120.09 0.20 1 119 1932 10 ASN H H 8.27 0.02 1 120 1932 10 ASN HA H 4.44 0.02 1 121 1932 10 ASN HB2 H 2.75 0.02 2 122 1932 10 ASN HB3 H 2.81 0.02 2 123 1932 10 ASN HD21 H 8.00 0.02 2 124 1932 10 ASN HD22 H 8.27 0.02 2 125 1932 10 ASN C C 177.30 0.20 1 126 1932 10 ASN CA C 56.48 0.20 1 127 1932 10 ASN CB C 38.52 0.20 1 128 1932 10 ASN N N 117.33 0.20 1 129 1932 10 ASN ND2 N 117.35 0.20 1 130 1933 11 ASP H H 8.00 0.02 1 131 1933 11 ASP HA H 4.30 0.02 1 132 1933 11 ASP HB2 H 3.46 0.02 2 133 1933 11 ASP HB3 H 2.90 0.02 2 134 1933 11 ASP C C 177.29 0.20 1 135 1933 11 ASP CA C 58.02 0.20 1 136 1933 11 ASP CB C 41.90 0.20 1 137 1933 11 ASP N N 122.22 0.20 1 138 1934 12 ASP H H 7.88 0.02 1 139 1934 12 ASP HA H 4.20 0.02 1 140 1934 12 ASP HB2 H 2.44 0.02 2 141 1934 12 ASP HB3 H 2.68 0.02 2 142 1934 12 ASP C C 178.16 0.20 1 143 1934 12 ASP CA C 57.39 0.20 1 144 1934 12 ASP CB C 40.85 0.20 1 145 1934 12 ASP N N 119.31 0.20 1 146 1935 13 ARG H H 7.96 0.02 1 147 1935 13 ARG HA H 3.94 0.02 1 148 1935 13 ARG HB2 H 1.96 0.02 2 149 1935 13 ARG HB3 H 1.98 0.02 2 150 1935 13 ARG HG2 H 1.79 0.02 2 151 1935 13 ARG HG3 H 1.94 0.02 2 152 1935 13 ARG HD2 H 3.26 0.02 2 153 1935 13 ARG HD3 H 3.26 0.02 2 154 1935 13 ARG HE H 4.76 0.02 1 155 1935 13 ARG C C 178.78 0.20 1 156 1935 13 ARG CA C 59.57 0.20 1 157 1935 13 ARG CB C 30.43 0.20 1 158 1935 13 ARG CG C 27.48 0.20 1 159 1935 13 ARG CD C 43.49 0.20 1 160 1935 13 ARG N N 118.39 0.20 1 161 1936 14 GLU H H 8.01 0.02 1 162 1936 14 GLU HA H 4.14 0.02 1 163 1936 14 GLU HB2 H 2.17 0.02 2 164 1936 14 GLU HB3 H 2.17 0.02 2 165 1936 14 GLU HG2 H 2.35 0.02 2 166 1936 14 GLU HG3 H 2.35 0.02 2 167 1936 14 GLU C C 178.79 0.20 1 168 1936 14 GLU CA C 59.65 0.20 1 169 1936 14 GLU CB C 29.47 0.20 1 170 1936 14 GLU CG C 35.85 0.20 1 171 1936 14 GLU N N 119.39 0.20 1 172 1937 15 ILE H H 8.45 0.02 1 173 1937 15 ILE HA H 3.78 0.02 1 174 1937 15 ILE HB H 1.95 0.02 1 175 1937 15 ILE HG12 H 2.14 0.02 2 176 1937 15 ILE HG13 H 0.75 0.02 2 177 1937 15 ILE HG2 H 0.89 0.02 1 178 1937 15 ILE HD1 H 0.59 0.02 1 179 1937 15 ILE C C 178.12 0.20 1 180 1937 15 ILE CA C 65.47 0.20 1 181 1937 15 ILE CB C 38.58 0.20 1 182 1937 15 ILE CG1 C 29.73 0.20 1 183 1937 15 ILE CG2 C 17.61 0.20 1 184 1937 15 ILE CD1 C 14.21 0.20 1 185 1937 15 ILE N N 118.31 0.20 1 186 1938 16 LEU H H 8.16 0.02 1 187 1938 16 LEU HA H 4.04 0.02 1 188 1938 16 LEU HB2 H 1.48 0.02 2 189 1938 16 LEU HB3 H 1.86 0.02 2 190 1938 16 LEU HG H 1.84 0.02 1 191 1938 16 LEU HD1 H 0.85 0.02 2 192 1938 16 LEU HD2 H 0.85 0.02 2 193 1938 16 LEU C C 180.01 0.20 1 194 1938 16 LEU CA C 58.55 0.20 1 195 1938 16 LEU CB C 41.82 0.20 1 196 1938 16 LEU CG C 26.89 0.20 1 197 1938 16 LEU CD1 C 23.17 0.20 1 198 1938 16 LEU CD2 C 23.17 0.20 1 199 1938 16 LEU N N 118.32 0.20 1 200 1939 17 LEU H H 8.50 0.02 1 201 1939 17 LEU HA H 4.09 0.02 1 202 1939 17 LEU HB2 H 1.71 0.02 2 203 1939 17 LEU HB3 H 1.86 0.02 2 204 1939 17 LEU HG H 1.70 0.02 1 205 1939 17 LEU HD1 H 0.88 0.02 2 206 1939 17 LEU HD2 H 0.89 0.02 2 207 1939 17 LEU C C 180.16 0.20 1 208 1939 17 LEU CA C 58.45 0.20 1 209 1939 17 LEU CB C 42.22 0.20 1 210 1939 17 LEU CG C 27.30 0.20 1 211 1939 17 LEU CD1 C 24.61 0.20 1 212 1939 17 LEU CD2 C 24.65 0.20 1 213 1939 17 LEU N N 119.93 0.20 1 214 1940 18 GLU H H 8.61 0.02 1 215 1940 18 GLU HA H 4.35 0.02 1 216 1940 18 GLU HB2 H 1.95 0.02 2 217 1940 18 GLU HB3 H 2.25 0.02 2 218 1940 18 GLU HG2 H 2.32 0.02 2 219 1940 18 GLU HG3 H 2.61 0.02 2 220 1940 18 GLU C C 179.94 0.20 1 221 1940 18 GLU CA C 58.69 0.20 1 222 1940 18 GLU CB C 29.43 0.20 1 223 1940 18 GLU CG C 35.58 0.20 1 224 1940 18 GLU N N 117.66 0.20 1 225 1941 19 CYS H H 8.26 0.02 1 226 1941 19 CYS HA H 3.80 0.02 1 227 1941 19 CYS HB2 H 2.02 0.02 2 228 1941 19 CYS HB3 H 2.91 0.02 2 229 1941 19 CYS HG H 2.00 0.02 1 230 1941 19 CYS C C 177.53 0.20 1 231 1941 19 CYS CA C 64.23 0.20 1 232 1941 19 CYS CB C 27.58 0.20 1 233 1941 19 CYS N N 116.05 0.20 1 234 1942 20 GLN H H 7.92 0.02 1 235 1942 20 GLN HA H 4.09 0.02 1 236 1942 20 GLN HB2 H 2.21 0.02 2 237 1942 20 GLN HB3 H 2.23 0.02 2 238 1942 20 GLN HG2 H 1.87 0.02 2 239 1942 20 GLN HG3 H 2.34 0.02 2 240 1942 20 GLN HE21 H 7.88 0.02 2 241 1942 20 GLN HE22 H 8.47 0.02 2 242 1942 20 GLN C C 177.51 0.20 1 243 1942 20 GLN CA C 58.90 0.20 1 244 1942 20 GLN CB C 28.45 0.20 1 245 1942 20 GLN CG C 33.94 0.20 1 246 1942 20 GLN N N 119.70 0.20 1 247 1942 20 GLN NE2 N 118.01 0.20 1 248 1943 21 LYS H H 7.88 0.02 1 249 1943 21 LYS HA H 4.07 0.02 1 250 1943 21 LYS HB2 H 1.80 0.02 2 251 1943 21 LYS HB3 H 1.81 0.02 2 252 1943 21 LYS HG2 H 1.63 0.02 2 253 1943 21 LYS HG3 H 1.64 0.02 2 254 1943 21 LYS HD2 H 1.63 0.02 2 255 1943 21 LYS HD3 H 1.63 0.02 2 256 1943 21 LYS HE2 H 2.91 0.02 2 257 1943 21 LYS HE3 H 2.92 0.02 2 258 1943 21 LYS C C 178.21 0.20 1 259 1943 21 LYS CA C 59.13 0.20 1 260 1943 21 LYS CB C 33.78 0.20 1 261 1943 21 LYS CG C 29.25 0.20 1 262 1943 21 LYS CD C 28.81 0.20 1 263 1943 21 LYS CE C 42.06 0.20 1 264 1943 21 LYS N N 118.02 0.20 1 265 1944 22 ARG H H 8.47 0.02 1 266 1944 22 ARG HA H 4.30 0.02 1 267 1944 22 ARG HB2 H 1.74 0.02 2 268 1944 22 ARG HB3 H 2.00 0.02 2 269 1944 22 ARG HG2 H 1.64 0.02 2 270 1944 22 ARG HG3 H 1.65 0.02 2 271 1944 22 ARG HD2 H 2.92 0.02 2 272 1944 22 ARG HD3 H 2.94 0.02 2 273 1944 22 ARG HE H 8.47 0.02 1 274 1944 22 ARG C C 177.69 0.20 1 275 1944 22 ARG CA C 56.47 0.20 1 276 1944 22 ARG CB C 32.71 0.20 1 277 1944 22 ARG CG C 29.21 0.20 1 278 1944 22 ARG CD C 42.07 0.20 1 279 1944 22 ARG N N 114.44 0.20 1 280 1945 23 GLY H H 7.25 0.02 1 281 1945 23 GLY HA2 H 4.07 0.02 2 282 1945 23 GLY HA3 H 4.20 0.02 2 283 1945 23 GLY C C 172.15 0.20 1 284 1945 23 GLY CA C 43.32 0.20 1 285 1945 23 GLY N N 109.68 0.20 1 286 1946 24 PRO HA H 3.92 0.02 1 287 1946 24 PRO HB2 H 1.11 0.02 2 288 1946 24 PRO HB3 H 2.04 0.02 2 289 1946 24 PRO HG2 H 1.11 0.02 2 290 1946 24 PRO HG3 H 2.03 0.02 2 291 1946 24 PRO HD2 H 3.58 0.02 2 292 1946 24 PRO HD3 H 3.59 0.02 2 293 1946 24 PRO C C 174.13 0.20 1 294 1946 24 PRO CA C 62.17 0.20 1 295 1946 24 PRO CB C 29.82 0.20 1 296 1946 24 PRO CG C 29.80 0.20 1 297 1946 24 PRO CD C 49.56 0.20 1 298 1947 25 SER H H 6.89 0.02 1 299 1947 25 SER HA H 4.41 0.02 1 300 1947 25 SER HB2 H 3.92 0.02 2 301 1947 25 SER HB3 H 3.83 0.02 2 302 1947 25 SER HG H 4.78 0.02 1 303 1947 25 SER C C 173.39 0.20 1 304 1947 25 SER CA C 56.09 0.20 1 305 1947 25 SER CB C 68.31 0.20 1 306 1947 25 SER N N 116.94 0.20 1 307 1948 26 PHE H H 8.36 0.02 1 308 1948 26 PHE HA H 4.25 0.02 1 309 1948 26 PHE HB2 H 3.27 0.02 2 310 1948 26 PHE HB3 H 3.32 0.02 2 311 1948 26 PHE HD1 H 7.33 0.02 1 312 1948 26 PHE HD2 H 7.36 0.02 1 313 1948 26 PHE HE1 H 7.36 0.02 1 314 1948 26 PHE HE2 H 7.37 0.02 1 315 1948 26 PHE HZ H 7.37 0.02 1 316 1948 26 PHE C C 177.40 0.20 1 317 1948 26 PHE CA C 62.80 0.20 1 318 1948 26 PHE CB C 38.60 0.20 1 319 1948 26 PHE CD1 C 130.13 0.20 1 320 1948 26 PHE CD2 C 131.65 0.20 1 321 1948 26 PHE CE1 C 130.00 0.20 1 322 1948 26 PHE CE2 C 131.63 0.20 1 323 1948 26 PHE CZ C 130.02 0.20 1 324 1948 26 PHE N N 121.40 0.20 1 325 1949 27 LYS H H 8.14 0.02 1 326 1949 27 LYS HA H 3.92 0.02 1 327 1949 27 LYS HB2 H 1.73 0.02 2 328 1949 27 LYS HB3 H 1.73 0.02 2 329 1949 27 LYS HG2 H 1.40 0.02 2 330 1949 27 LYS HG3 H 1.41 0.02 2 331 1949 27 LYS HD2 H 1.59 0.02 2 332 1949 27 LYS HD3 H 1.73 0.02 2 333 1949 27 LYS HE2 H 2.92 0.02 2 334 1949 27 LYS HE3 H 2.92 0.02 2 335 1949 27 LYS C C 179.55 0.20 1 336 1949 27 LYS CA C 59.91 0.20 1 337 1949 27 LYS CB C 32.39 0.20 1 338 1949 27 LYS CG C 25.14 0.20 1 339 1949 27 LYS CD C 32.50 0.20 1 340 1949 27 LYS CE C 42.08 0.20 1 341 1949 27 LYS N N 118.53 0.20 1 342 1950 28 THR H H 7.71 0.02 1 343 1950 28 THR HA H 3.79 0.02 1 344 1950 28 THR HB H 3.91 0.02 1 345 1950 28 THR HG1 H 4.78 0.02 1 346 1950 28 THR HG2 H 0.95 0.02 1 347 1950 28 THR C C 176.44 0.20 1 348 1950 28 THR CA C 65.91 0.20 1 349 1950 28 THR CB C 68.35 0.20 1 350 1950 28 THR CG2 C 24.80 0.20 1 351 1950 28 THR N N 120.14 0.20 1 352 1951 29 PHE H H 8.35 0.02 1 353 1951 29 PHE HA H 4.48 0.02 1 354 1951 29 PHE HB2 H 3.26 0.02 2 355 1951 29 PHE HB3 H 2.92 0.02 2 356 1951 29 PHE HD1 H 6.83 0.02 1 357 1951 29 PHE HD2 H 6.84 0.02 1 358 1951 29 PHE HE1 H 6.91 0.02 1 359 1951 29 PHE HE2 H 7.38 0.02 1 360 1951 29 PHE HZ H 6.93 0.02 1 361 1951 29 PHE C C 178.04 0.20 1 362 1951 29 PHE CA C 59.43 0.20 1 363 1951 29 PHE CB C 36.77 0.20 1 364 1951 29 PHE CD1 C 130.23 0.20 1 365 1951 29 PHE CD2 C 130.38 0.20 1 366 1951 29 PHE CE1 C 129.72 0.20 1 367 1951 29 PHE CE2 C 131.58 0.20 1 368 1951 29 PHE CZ C 131.14 0.20 1 369 1951 29 PHE N N 121.42 0.20 1 370 1952 30 ALA H H 8.82 0.02 1 371 1952 30 ALA HA H 4.01 0.02 1 372 1952 30 ALA HB H 1.33 0.02 1 373 1952 30 ALA C C 180.20 0.20 1 374 1952 30 ALA CA C 55.44 0.20 1 375 1952 30 ALA CB C 17.64 0.20 1 376 1952 30 ALA N N 122.86 0.20 1 377 1953 31 TYR H H 7.87 0.02 1 378 1953 31 TYR HA H 4.30 0.02 1 379 1953 31 TYR HB2 H 3.24 0.02 2 380 1953 31 TYR HB3 H 3.25 0.02 2 381 1953 31 TYR HD1 H 6.99 0.02 1 382 1953 31 TYR HD2 H 7.00 0.02 1 383 1953 31 TYR HE1 H 6.70 0.02 1 384 1953 31 TYR HE2 H 6.70 0.02 1 385 1953 31 TYR HH H 4.77 0.02 1 386 1953 31 TYR C C 178.03 0.20 1 387 1953 31 TYR CA C 60.99 0.20 1 388 1953 31 TYR CB C 37.91 0.20 1 389 1953 31 TYR CD1 C 132.97 0.20 1 390 1953 31 TYR CD2 C 132.97 0.20 1 391 1953 31 TYR CE1 C 118.06 0.20 1 392 1953 31 TYR CE2 C 118.07 0.20 1 393 1953 31 TYR N N 122.62 0.20 1 394 1954 32 LEU H H 8.49 0.02 1 395 1954 32 LEU HA H 3.66 0.02 1 396 1954 32 LEU HB2 H 2.23 0.02 2 397 1954 32 LEU HB3 H 1.26 0.02 2 398 1954 32 LEU HG H 1.04 0.02 1 399 1954 32 LEU HD1 H 0.94 0.02 2 400 1954 32 LEU HD2 H 0.95 0.02 2 401 1954 32 LEU C C 177.94 0.20 1 402 1954 32 LEU CA C 57.31 0.20 1 403 1954 32 LEU CB C 44.61 0.20 1 404 1954 32 LEU CG C 28.15 0.20 1 405 1954 32 LEU CD1 C 22.97 0.20 1 406 1954 32 LEU CD2 C 26.82 0.20 1 407 1954 32 LEU N N 120.11 0.20 1 408 1955 33 ALA H H 8.70 0.02 1 409 1955 33 ALA HA H 3.54 0.02 1 410 1955 33 ALA HB H 1.39 0.02 1 411 1955 33 ALA C C 178.95 0.20 1 412 1955 33 ALA CA C 55.85 0.20 1 413 1955 33 ALA CB C 18.15 0.20 1 414 1955 33 ALA N N 121.53 0.20 1 415 1956 34 ALA H H 7.31 0.02 1 416 1956 34 ALA HA H 4.22 0.02 1 417 1956 34 ALA HB H 1.46 0.02 1 418 1956 34 ALA C C 179.97 0.20 1 419 1956 34 ALA CA C 54.45 0.20 1 420 1956 34 ALA CB C 17.94 0.20 1 421 1956 34 ALA N N 118.13 0.20 1 422 1957 35 LYS H H 7.52 0.02 1 423 1957 35 LYS HA H 4.00 0.02 1 424 1957 35 LYS HB2 H 1.58 0.02 2 425 1957 35 LYS HB3 H 1.64 0.02 2 426 1957 35 LYS HG2 H 1.29 0.02 2 427 1957 35 LYS HG3 H 1.49 0.02 2 428 1957 35 LYS HD2 H 1.32 0.02 2 429 1957 35 LYS HD3 H 1.45 0.02 2 430 1957 35 LYS HE2 H 2.88 0.02 2 431 1957 35 LYS HE3 H 2.89 0.02 2 432 1957 35 LYS C C 178.02 0.20 1 433 1957 35 LYS CA C 58.59 0.20 1 434 1957 35 LYS CB C 33.15 0.20 1 435 1957 35 LYS CG C 24.65 0.20 1 436 1957 35 LYS CD C 29.34 0.20 1 437 1957 35 LYS CE C 41.94 0.20 1 438 1957 35 LYS N N 118.12 0.20 1 439 1958 36 LEU H H 8.30 0.02 1 440 1958 36 LEU HA H 4.38 0.02 1 441 1958 36 LEU HB2 H 1.57 0.02 2 442 1958 36 LEU HB3 H 1.60 0.02 2 443 1958 36 LEU HG H 1.88 0.02 1 444 1958 36 LEU HD1 H 0.96 0.02 2 445 1958 36 LEU HD2 H 0.95 0.02 2 446 1958 36 LEU C C 176.41 0.20 1 447 1958 36 LEU CA C 54.36 0.20 1 448 1958 36 LEU CB C 42.38 0.20 1 449 1958 36 LEU CG C 26.91 0.20 1 450 1958 36 LEU CD1 C 26.70 0.20 1 451 1958 36 LEU CD2 C 21.96 0.20 1 452 1958 36 LEU N N 115.28 0.20 1 453 1959 37 ASP H H 7.73 0.02 1 454 1959 37 ASP HA H 4.38 0.02 1 455 1959 37 ASP HB2 H 2.50 0.02 2 456 1959 37 ASP HB3 H 3.12 0.02 2 457 1959 37 ASP C C 174.60 0.20 1 458 1959 37 ASP CA C 55.28 0.20 1 459 1959 37 ASP CB C 38.82 0.20 1 460 1959 37 ASP N N 120.00 0.20 1 461 1960 38 LYS H H 8.40 0.02 1 462 1960 38 LYS HA H 4.78 0.02 1 463 1960 38 LYS HB2 H 1.25 0.02 2 464 1960 38 LYS HB3 H 2.07 0.02 2 465 1960 38 LYS HG2 H 1.21 0.02 2 466 1960 38 LYS HG3 H 1.24 0.02 2 467 1960 38 LYS HD2 H 0.89 0.02 2 468 1960 38 LYS HD3 H 1.52 0.02 2 469 1960 38 LYS HE2 H 1.87 0.02 2 470 1960 38 LYS HE3 H 2.21 0.02 2 471 1960 38 LYS C C 174.61 0.20 1 472 1960 38 LYS CA C 52.79 0.20 1 473 1960 38 LYS CB C 37.47 0.20 1 474 1960 38 LYS CG C 24.62 0.20 1 475 1960 38 LYS CD C 27.86 0.20 1 476 1960 38 LYS CE C 41.94 0.20 1 477 1960 38 LYS N N 117.89 0.20 1 478 1961 39 ASN H H 8.36 0.02 1 479 1961 39 ASN HA H 5.30 0.02 1 480 1961 39 ASN HB2 H 2.76 0.02 2 481 1961 39 ASN HB3 H 2.97 0.02 2 482 1961 39 ASN HD21 H 7.71 0.02 2 483 1961 39 ASN HD22 H 7.93 0.02 2 484 1961 39 ASN C C 175.52 0.20 1 485 1961 39 ASN CA C 51.08 0.20 1 486 1961 39 ASN CB C 38.99 0.20 1 487 1961 39 ASN N N 117.85 0.20 1 488 1961 39 ASN ND2 N 119.75 0.20 1 489 1962 40 PRO HA H 3.98 0.02 1 490 1962 40 PRO HB2 H 1.99 0.02 2 491 1962 40 PRO HB3 H 1.98 0.02 2 492 1962 40 PRO HG2 H 1.99 0.02 2 493 1962 40 PRO HG3 H 2.35 0.02 2 494 1962 40 PRO HD2 H 3.95 0.02 2 495 1962 40 PRO HD3 H 3.88 0.02 2 496 1962 40 PRO C C 177.87 0.20 1 497 1962 40 PRO CA C 66.62 0.20 1 498 1962 40 PRO CB C 32.29 0.20 1 499 1962 40 PRO CG C 28.09 0.20 1 500 1962 40 PRO CD C 50.61 0.20 1 501 1963 41 ASN H H 8.52 0.02 1 502 1963 41 ASN HA H 4.46 0.02 1 503 1963 41 ASN HB2 H 2.85 0.02 2 504 1963 41 ASN HB3 H 2.87 0.02 2 505 1963 41 ASN HD21 H 8.52 0.02 2 506 1963 41 ASN HD22 H 8.52 0.02 2 507 1963 41 ASN C C 177.66 0.20 1 508 1963 41 ASN CA C 56.37 0.20 1 509 1963 41 ASN CB C 37.81 0.20 1 510 1963 41 ASN N N 115.75 0.20 1 511 1963 41 ASN ND2 N 115.73 0.20 1 512 1964 42 GLN H H 7.93 0.02 1 513 1964 42 GLN HA H 4.26 0.02 1 514 1964 42 GLN HB2 H 2.66 0.02 2 515 1964 42 GLN HB3 H 2.67 0.02 2 516 1964 42 GLN HG2 H 2.61 0.02 2 517 1964 42 GLN HG3 H 2.62 0.02 2 518 1964 42 GLN HE21 H 4.78 0.02 2 519 1964 42 GLN HE22 H 8.42 0.02 2 520 1964 42 GLN C C 179.22 0.20 1 521 1964 42 GLN CA C 58.49 0.20 1 522 1964 42 GLN CB C 28.34 0.20 1 523 1964 42 GLN CG C 34.38 0.20 1 524 1964 42 GLN N N 119.54 0.20 1 525 1964 42 GLN NE2 N 117.87 0.20 1 526 1965 43 VAL H H 7.61 0.02 1 527 1965 43 VAL HA H 3.51 0.02 1 528 1965 43 VAL HB H 2.14 0.02 1 529 1965 43 VAL HG1 H 1.04 0.02 2 530 1965 43 VAL HG2 H 1.04 0.02 2 531 1965 43 VAL C C 176.29 0.20 1 532 1965 43 VAL CA C 66.64 0.20 1 533 1965 43 VAL CB C 31.75 0.20 1 534 1965 43 VAL CG1 C 22.99 0.20 1 535 1965 43 VAL CG2 C 23.09 0.20 1 536 1965 43 VAL N N 118.25 0.20 1 537 1966 44 SER H H 7.72 0.02 1 538 1966 44 SER HA H 2.72 0.02 1 539 1966 44 SER HB2 H 3.14 0.02 2 540 1966 44 SER HB3 H 3.50 0.02 2 541 1966 44 SER HG H 3.13 0.02 1 542 1966 44 SER C C 177.06 0.20 1 543 1966 44 SER CA C 60.65 0.20 1 544 1966 44 SER CB C 62.49 0.20 1 545 1966 44 SER N N 113.98 0.20 1 546 1967 45 GLU H H 7.78 0.02 1 547 1967 45 GLU HA H 3.93 0.02 1 548 1967 45 GLU HB2 H 2.09 0.02 2 549 1967 45 GLU HB3 H 2.11 0.02 2 550 1967 45 GLU HG2 H 2.39 0.02 2 551 1967 45 GLU HG3 H 2.40 0.02 2 552 1967 45 GLU C C 178.86 0.20 1 553 1967 45 GLU CA C 59.18 0.20 1 554 1967 45 GLU CB C 29.50 0.20 1 555 1967 45 GLU CG C 36.56 0.20 1 556 1967 45 GLU N N 119.26 0.20 1 557 1968 46 ARG H H 7.88 0.02 1 558 1968 46 ARG HA H 3.85 0.02 1 559 1968 46 ARG HB2 H 1.38 0.02 2 560 1968 46 ARG HB3 H 0.94 0.02 2 561 1968 46 ARG HG2 H 0.94 0.02 2 562 1968 46 ARG HG3 H 1.37 0.02 2 563 1968 46 ARG HD2 H 3.90 0.02 2 564 1968 46 ARG HD3 H 2.92 0.02 2 565 1968 46 ARG HE H 4.77 0.02 1 566 1968 46 ARG C C 177.85 0.20 1 567 1968 46 ARG CA C 56.80 0.20 1 568 1968 46 ARG CB C 29.61 0.20 1 569 1968 46 ARG CG C 24.77 0.20 1 570 1968 46 ARG CD C 42.06 0.20 1 571 1968 46 ARG N N 121.00 0.20 1 572 1969 47 PHE H H 8.55 0.02 1 573 1969 47 PHE HA H 3.91 0.02 1 574 1969 47 PHE HB2 H 3.00 0.02 2 575 1969 47 PHE HB3 H 3.04 0.02 2 576 1969 47 PHE HD1 H 7.14 0.02 1 577 1969 47 PHE HD2 H 7.37 0.02 1 578 1969 47 PHE HE1 H 7.14 0.02 1 579 1969 47 PHE HE2 H 7.36 0.02 1 580 1969 47 PHE HZ H 7.28 0.02 1 581 1969 47 PHE C C 176.25 0.20 1 582 1969 47 PHE CA C 62.14 0.20 1 583 1969 47 PHE CB C 38.89 0.20 1 584 1969 47 PHE CD1 C 131.69 0.20 1 585 1969 47 PHE CD2 C 131.94 0.20 1 586 1969 47 PHE CE1 C 131.61 0.20 1 587 1969 47 PHE CE2 C 131.79 0.20 1 588 1969 47 PHE CZ C 131.59 0.20 1 589 1969 47 PHE N N 119.31 0.20 1 590 1970 48 GLN H H 7.74 0.02 1 591 1970 48 GLN HA H 3.61 0.02 1 592 1970 48 GLN HB2 H 2.12 0.02 2 593 1970 48 GLN HB3 H 2.13 0.02 2 594 1970 48 GLN HG2 H 2.51 0.02 2 595 1970 48 GLN HG3 H 2.55 0.02 2 596 1970 48 GLN HE21 H 7.75 0.02 2 597 1970 48 GLN HE22 H 7.76 0.02 2 598 1970 48 GLN C C 179.18 0.20 1 599 1970 48 GLN CA C 58.92 0.20 1 600 1970 48 GLN CB C 28.24 0.20 1 601 1970 48 GLN CG C 33.82 0.20 1 602 1970 48 GLN N N 115.87 0.20 1 603 1970 48 GLN NE2 N 115.81 0.20 1 604 1971 49 GLN H H 7.86 0.02 1 605 1971 49 GLN HA H 3.91 0.02 1 606 1971 49 GLN HB2 H 1.93 0.02 2 607 1971 49 GLN HB3 H 2.23 0.02 2 608 1971 49 GLN HG2 H 2.33 0.02 2 609 1971 49 GLN HG3 H 2.33 0.02 2 610 1971 49 GLN HE21 H 7.86 0.02 2 611 1971 49 GLN HE22 H 7.86 0.02 2 612 1971 49 GLN C C 179.41 0.20 1 613 1971 49 GLN CA C 58.88 0.20 1 614 1971 49 GLN CB C 28.32 0.20 1 615 1971 49 GLN CG C 33.52 0.20 1 616 1971 49 GLN N N 119.14 0.20 1 617 1971 49 GLN NE2 N 119.18 0.20 1 618 1972 50 LEU H H 8.50 0.02 1 619 1972 50 LEU HA H 3.87 0.02 1 620 1972 50 LEU HB2 H 1.19 0.02 2 621 1972 50 LEU HB3 H 1.80 0.02 2 622 1972 50 LEU HG H 0.72 0.02 1 623 1972 50 LEU HD1 H 0.66 0.02 2 624 1972 50 LEU HD2 H 0.75 0.02 2 625 1972 50 LEU C C 179.63 0.20 1 626 1972 50 LEU CA C 57.29 0.20 1 627 1972 50 LEU CB C 42.21 0.20 1 628 1972 50 LEU CG C 25.88 0.20 1 629 1972 50 LEU CD1 C 21.55 0.20 1 630 1972 50 LEU CD2 C 25.90 0.20 1 631 1972 50 LEU N N 120.30 0.20 1 632 1973 51 MET H H 7.97 0.02 1 633 1973 51 MET HA H 4.29 0.02 1 634 1973 51 MET HB2 H 1.72 0.02 2 635 1973 51 MET HB3 H 1.72 0.02 2 636 1973 51 MET HG2 H 1.57 0.02 2 637 1973 51 MET HG3 H 1.72 0.02 2 638 1973 51 MET HE H 1.83 0.02 1 639 1973 51 MET C C 178.87 0.20 1 640 1973 51 MET CA C 56.49 0.20 1 641 1973 51 MET CB C 31.86 0.20 1 642 1973 51 MET CG C 32.43 0.20 1 643 1973 51 MET CE C 17.60 0.20 1 644 1973 51 MET N N 117.49 0.20 1 645 1974 52 LYS H H 7.55 0.02 1 646 1974 52 LYS HA H 4.07 0.02 1 647 1974 52 LYS HB2 H 1.83 0.02 2 648 1974 52 LYS HB3 H 1.85 0.02 2 649 1974 52 LYS HG2 H 1.50 0.02 2 650 1974 52 LYS HG3 H 1.52 0.02 2 651 1974 52 LYS HD2 H 1.49 0.02 2 652 1974 52 LYS HD3 H 1.51 0.02 2 653 1974 52 LYS HE2 H 2.21 0.02 2 654 1974 52 LYS HE3 H 2.97 0.02 2 655 1974 52 LYS C C 178.73 0.20 1 656 1974 52 LYS CA C 58.52 0.20 1 657 1974 52 LYS CB C 32.12 0.20 1 658 1974 52 LYS CG C 25.11 0.20 1 659 1974 52 LYS CD C 25.08 0.20 1 660 1974 52 LYS CE C 42.04 0.20 1 661 1974 52 LYS N N 119.60 0.20 1 662 1975 53 LEU H H 7.59 0.02 1 663 1975 53 LEU HA H 4.07 0.02 1 664 1975 53 LEU HB2 H 1.40 0.02 2 665 1975 53 LEU HB3 H 1.64 0.02 2 666 1975 53 LEU HG H 1.62 0.02 1 667 1975 53 LEU HD1 H 0.79 0.02 2 668 1975 53 LEU HD2 H 0.80 0.02 2 669 1975 53 LEU C C 179.06 0.20 1 670 1975 53 LEU CA C 56.98 0.20 1 671 1975 53 LEU CB C 41.90 0.20 1 672 1975 53 LEU CG C 26.87 0.20 1 673 1975 53 LEU CD1 C 23.39 0.20 1 674 1975 53 LEU CD2 C 25.01 0.20 1 675 1975 53 LEU N N 119.19 0.20 1 676 1976 54 PHE H H 7.87 0.02 1 677 1976 54 PHE HA H 4.46 0.02 1 678 1976 54 PHE HB2 H 3.25 0.02 2 679 1976 54 PHE HB3 H 3.06 0.02 2 680 1976 54 PHE HD1 H 7.26 0.02 1 681 1976 54 PHE HD2 H 7.28 0.02 1 682 1976 54 PHE HE1 H 6.82 0.02 1 683 1976 54 PHE HE2 H 7.27 0.02 1 684 1976 54 PHE HZ H 7.26 0.02 1 685 1976 54 PHE C C 177.18 0.20 1 686 1976 54 PHE CA C 58.92 0.20 1 687 1976 54 PHE CB C 39.15 0.20 1 688 1976 54 PHE CD1 C 131.57 0.20 1 689 1976 54 PHE CD2 C 131.57 0.20 1 690 1976 54 PHE CE1 C 129.72 0.20 1 691 1976 54 PHE CE2 C 130.19 0.20 1 692 1976 54 PHE CZ C 129.72 0.20 1 693 1976 54 PHE N N 119.10 0.20 1 694 1977 55 GLU H H 8.01 0.02 1 695 1977 55 GLU HA H 4.08 0.02 1 696 1977 55 GLU HB2 H 2.06 0.02 2 697 1977 55 GLU HB3 H 1.85 0.02 2 698 1977 55 GLU HG2 H 2.27 0.02 2 699 1977 55 GLU HG3 H 2.34 0.02 2 700 1977 55 GLU C C 177.38 0.20 1 701 1977 55 GLU CA C 57.96 0.20 1 702 1977 55 GLU CB C 32.19 0.20 1 703 1977 55 GLU CG C 36.26 0.20 1 704 1977 55 GLU N N 120.28 0.20 1 705 1978 56 LYS H H 8.01 0.02 1 706 1978 56 LYS HA H 4.25 0.02 1 707 1978 56 LYS HB2 H 1.84 0.02 2 708 1978 56 LYS HB3 H 1.85 0.02 2 709 1978 56 LYS HG2 H 1.49 0.02 2 710 1978 56 LYS HG3 H 1.50 0.02 2 711 1978 56 LYS HD2 H 1.66 0.02 2 712 1978 56 LYS HD3 H 1.67 0.02 2 713 1978 56 LYS HE2 H 2.96 0.02 2 714 1978 56 LYS HE3 H 2.98 0.02 2 715 1978 56 LYS C C 177.34 0.20 1 716 1978 56 LYS CA C 57.22 0.20 1 717 1978 56 LYS CB C 32.86 0.20 1 718 1978 56 LYS CG C 25.03 0.20 1 719 1978 56 LYS CD C 29.21 0.20 1 720 1978 56 LYS CE C 42.11 0.20 1 721 1978 56 LYS N N 119.98 0.20 1 722 1979 57 SER H H 8.03 0.02 1 723 1979 57 SER HA H 4.36 0.02 1 724 1979 57 SER HB2 H 3.89 0.02 2 725 1979 57 SER HB3 H 3.90 0.02 2 726 1979 57 SER HG H 4.77 0.02 1 727 1979 57 SER C C 174.60 0.20 1 728 1979 57 SER CA C 59.02 0.20 1 729 1979 57 SER CB C 63.76 0.20 1 730 1979 57 SER N N 115.33 0.20 1 731 1980 58 LYS H H 7.99 0.02 1 732 1980 58 LYS HA H 4.30 0.02 1 733 1980 58 LYS HB2 H 1.88 0.02 2 734 1980 58 LYS HB3 H 1.76 0.02 2 735 1980 58 LYS HG2 H 1.37 0.02 2 736 1980 58 LYS HG3 H 1.79 0.02 2 737 1980 58 LYS HD2 H 1.78 0.02 2 738 1980 58 LYS HD3 H 1.80 0.02 2 739 1980 58 LYS HE2 H 2.85 0.02 2 740 1980 58 LYS HE3 H 3.19 0.02 2 741 1980 58 LYS C C 176.47 0.20 1 742 1980 58 LYS CA C 56.52 0.20 1 743 1980 58 LYS CB C 32.73 0.20 1 744 1980 58 LYS CG C 24.91 0.20 1 745 1980 58 LYS CD C 27.37 0.20 1 746 1980 58 LYS CE C 43.39 0.20 1 747 1980 58 LYS N N 122.11 0.20 1 748 1981 59 CYS H H 8.17 0.02 1 749 1981 59 CYS HA H 4.46 0.02 1 750 1981 59 CYS HB2 H 2.93 0.02 2 751 1981 59 CYS HB3 H 2.94 0.02 2 752 1981 59 CYS HG H 4.77 0.02 1 753 1981 59 CYS C C 173.59 0.20 1 754 1981 59 CYS CA C 58.74 0.20 1 755 1981 59 CYS CB C 28.08 0.20 1 756 1981 59 CYS N N 119.81 0.20 1 757 1982 60 ARG H H 7.94 0.02 1 758 1982 60 ARG HA H 4.15 0.02 1 759 1982 60 ARG HB2 H 1.58 0.02 2 760 1982 60 ARG HB3 H 1.71 0.02 2 761 1982 60 ARG HG2 H 1.58 0.02 2 762 1982 60 ARG HG3 H 1.58 0.02 2 763 1982 60 ARG HD2 H 3.17 0.02 2 764 1982 60 ARG HD3 H 3.17 0.02 2 765 1982 60 ARG HE H 7.70 0.02 1 766 1982 60 ARG C C 180.83 0.20 1 767 1982 60 ARG CA C 57.59 0.20 1 768 1982 60 ARG CB C 31.56 0.20 1 769 1982 60 ARG CG C 27.35 0.20 1 770 1982 60 ARG CD C 43.51 0.20 1 771 1982 60 ARG N N 127.98 0.20 1 stop_ save_