data_25988 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; BAZ2B PHD ; _BMRB_accession_number 25988 _BMRB_flat_file_name bmr25988.str _Entry_type original _Submission_date 2016-03-10 _Accession_date 2016-03-10 _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 Bortoluzzi Alessio . . 2 Ciulli Alessio . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 53 "13C chemical shifts" 160 "15N chemical shifts" 53 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-06-09 update BMRB 'update entry citation' 2017-04-13 original author 'original release' stop_ _Original_release_date 2016-03-10 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural Basis of Molecular Recognition of Helical Histone H3 Tail by PHD Finger Domains ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28341809 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bortoluzzi Alessio . . 2 Amato Anastasia . . 3 Lucas Xavier . . 4 Blank Manuel . . 5 Ciulli Alessio . . stop_ _Journal_abbreviation 'Biochem J.' _Journal_volume 474 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1633 _Page_last 1651 _Year 2017 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'PHD domain of human BAZ2B' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'BAZ2B PHD' $BAZ2B_PHD Zinc1 $entity_ZN Zinc2 $entity_ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Epigenetic reader domain' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_BAZ2B_PHD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common BAZ2B_PHD _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 58 _Mol_residue_sequence ; HMSIMKVYCQICRKGDNEEL LLLCDGCDKGCHTYCHRPKI TTIPDGDWFCPACIAKAS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1926 HIS 2 1927 MET 3 1928 SER 4 1929 ILE 5 1930 MET 6 1931 LYS 7 1932 VAL 8 1933 TYR 9 1934 CYS 10 1935 GLN 11 1936 ILE 12 1937 CYS 13 1938 ARG 14 1939 LYS 15 1940 GLY 16 1941 ASP 17 1942 ASN 18 1943 GLU 19 1944 GLU 20 1945 LEU 21 1946 LEU 22 1947 LEU 23 1948 LEU 24 1949 CYS 25 1950 ASP 26 1951 GLY 27 1952 CYS 28 1953 ASP 29 1954 LYS 30 1955 GLY 31 1956 CYS 32 1957 HIS 33 1958 THR 34 1959 TYR 35 1960 CYS 36 1961 HIS 37 1962 ARG 38 1963 PRO 39 1964 LYS 40 1965 ILE 41 1966 THR 42 1967 THR 43 1968 ILE 44 1969 PRO 45 1970 ASP 46 1971 GLY 47 1972 ASP 48 1973 TRP 49 1974 PHE 50 1975 CYS 51 1976 PRO 52 1977 ALA 53 1978 CYS 54 1979 ILE 55 1980 ALA 56 1981 LYS 57 1982 ALA 58 1983 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type NON-POLYMER _Name_common 'ZINC ION' _BMRB_code ZN _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $BAZ2B_PHD 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_name $BAZ2B_PHD 'recombinant technology' . Escherichia coli . 'Modified pET15' 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 $BAZ2B_PHD 350 uM '[U-98% 13C; U-98% 15N]' DTT 1 mM 'natural abundance' 'potassium chloride' 50 mM 'natural abundance' 'potassium phosphate' 25 mM 'natural abundance' 'sodium azide' 0.02 w/v 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_CcpNmr_Analysis _Saveframe_category software _Name CcpNmr_Analysis _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'Avance III HD' _Field_strength 500 _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_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.200 . M pH 6.5 . pH pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_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 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $CcpNmr_Analysis stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCACB' '3D HNCA' '3D CBCA(CO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'BAZ2B PHD' _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 1927 2 MET C C 175.727 0.000 1 2 1927 2 MET CA C 55.167 0.051 1 3 1927 2 MET CB C 32.996 0.000 1 4 1928 3 SER H H 8.552 0.002 1 5 1928 3 SER C C 174.396 0.000 1 6 1928 3 SER CA C 58.186 0.061 1 7 1928 3 SER CB C 63.835 0.059 1 8 1928 3 SER N N 118.117 0.023 1 9 1929 4 ILE H H 8.125 0.003 1 10 1929 4 ILE C C 175.984 0.000 1 11 1929 4 ILE CA C 61.281 0.072 1 12 1929 4 ILE CB C 38.683 0.044 1 13 1929 4 ILE N N 121.992 0.054 1 14 1930 5 MET H H 8.164 0.004 1 15 1930 5 MET C C 175.339 0.000 1 16 1930 5 MET CA C 54.950 0.060 1 17 1930 5 MET CB C 33.014 0.027 1 18 1930 5 MET N N 123.374 0.054 1 19 1931 6 LYS H H 8.150 0.004 1 20 1931 6 LYS C C 175.524 0.000 1 21 1931 6 LYS CA C 56.180 0.065 1 22 1931 6 LYS CB C 32.903 0.014 1 23 1931 6 LYS N N 123.221 0.081 1 24 1932 7 VAL H H 7.906 0.001 1 25 1932 7 VAL C C 173.853 0.000 1 26 1932 7 VAL CA C 61.668 0.097 1 27 1932 7 VAL CB C 32.905 0.087 1 28 1932 7 VAL N N 123.283 0.088 1 29 1933 8 TYR H H 7.771 0.001 1 30 1933 8 TYR C C 174.124 0.000 1 31 1933 8 TYR CA C 55.434 0.054 1 32 1933 8 TYR CB C 40.073 0.075 1 33 1933 8 TYR N N 120.588 0.031 1 34 1934 9 CYS H H 8.050 0.001 1 35 1934 9 CYS C C 177.409 0.000 1 36 1934 9 CYS CA C 58.908 0.065 1 37 1934 9 CYS CB C 31.624 0.062 1 38 1934 9 CYS N N 122.858 0.050 1 39 1935 10 GLN H H 8.677 0.002 1 40 1935 10 GLN C C 174.984 0.000 1 41 1935 10 GLN CA C 57.717 0.065 1 42 1935 10 GLN CB C 30.443 0.011 1 43 1935 10 GLN N N 127.274 0.106 1 44 1936 11 ILE H H 8.968 0.003 1 45 1936 11 ILE C C 176.846 0.000 1 46 1936 11 ILE CA C 62.180 0.050 1 47 1936 11 ILE CB C 37.265 0.058 1 48 1936 11 ILE N N 121.936 0.075 1 49 1937 12 CYS H H 8.261 0.001 1 50 1937 12 CYS C C 175.731 0.000 1 51 1937 12 CYS CA C 59.268 0.024 1 52 1937 12 CYS CB C 30.748 0.038 1 53 1937 12 CYS N N 118.181 0.039 1 54 1938 13 ARG H H 7.709 0.001 1 55 1938 13 ARG C C 174.936 0.000 1 56 1938 13 ARG CA C 57.369 0.069 1 57 1938 13 ARG CB C 26.066 0.034 1 58 1938 13 ARG N N 115.343 0.034 1 59 1939 14 LYS H H 8.398 0.003 1 60 1939 14 LYS C C 177.231 0.000 1 61 1939 14 LYS CA C 55.521 0.072 1 62 1939 14 LYS CB C 36.040 0.030 1 63 1939 14 LYS N N 118.691 0.055 1 64 1940 15 GLY H H 8.969 0.004 1 65 1940 15 GLY C C 173.525 0.000 1 66 1940 15 GLY CA C 44.569 0.078 1 67 1940 15 GLY N N 110.325 0.049 1 68 1941 16 ASP H H 7.668 0.001 1 69 1941 16 ASP C C 174.506 0.000 1 70 1941 16 ASP CA C 52.156 0.073 1 71 1941 16 ASP CB C 40.698 0.073 1 72 1941 16 ASP N N 117.044 0.022 1 73 1942 17 ASN H H 8.931 0.001 1 74 1942 17 ASN C C 176.457 0.000 1 75 1942 17 ASN CA C 54.186 0.036 1 76 1942 17 ASN CB C 38.070 0.034 1 77 1942 17 ASN N N 115.733 0.065 1 78 1943 18 GLU H H 9.055 0.002 1 79 1943 18 GLU C C 178.730 0.000 1 80 1943 18 GLU CA C 60.422 0.035 1 81 1943 18 GLU CB C 29.258 0.018 1 82 1943 18 GLU N N 117.081 0.040 1 83 1944 19 GLU H H 9.487 0.002 1 84 1944 19 GLU C C 177.002 0.000 1 85 1944 19 GLU CA C 58.761 0.047 1 86 1944 19 GLU CB C 28.188 0.010 1 87 1944 19 GLU N N 119.583 0.030 1 88 1945 20 LEU H H 8.015 0.002 1 89 1945 20 LEU C C 174.580 0.000 1 90 1945 20 LEU CA C 53.230 0.072 1 91 1945 20 LEU CB C 41.112 0.050 1 92 1945 20 LEU N N 118.569 0.033 1 93 1946 21 LEU H H 7.270 0.002 1 94 1946 21 LEU C C 174.365 0.000 1 95 1946 21 LEU CA C 54.724 0.094 1 96 1946 21 LEU CB C 42.456 0.013 1 97 1946 21 LEU N N 122.899 0.047 1 98 1947 22 LEU H H 7.865 0.002 1 99 1947 22 LEU C C 175.384 0.000 1 100 1947 22 LEU CA C 54.200 0.059 1 101 1947 22 LEU CB C 41.061 0.052 1 102 1947 22 LEU N N 127.740 0.076 1 103 1948 23 LEU H H 8.119 0.006 1 104 1948 23 LEU C C 175.754 0.000 1 105 1948 23 LEU CA C 53.147 0.071 1 106 1948 23 LEU CB C 42.499 0.035 1 107 1948 23 LEU N N 122.026 0.046 1 108 1949 24 CYS H H 8.522 0.002 1 109 1949 24 CYS C C 176.842 0.000 1 110 1949 24 CYS CA C 60.085 0.076 1 111 1949 24 CYS CB C 31.102 0.029 1 112 1949 24 CYS N N 126.502 0.042 1 113 1950 25 ASP H H 8.808 0.002 1 114 1950 25 ASP C C 176.341 0.000 1 115 1950 25 ASP CA C 57.031 0.066 1 116 1950 25 ASP CB C 41.376 0.041 1 117 1950 25 ASP N N 127.911 0.045 1 118 1951 26 GLY H H 10.180 0.003 1 119 1951 26 GLY C C 174.184 0.000 1 120 1951 26 GLY CA C 45.751 0.115 1 121 1951 26 GLY N N 114.615 0.031 1 122 1952 27 CYS H H 7.885 0.003 1 123 1952 27 CYS C C 174.249 0.000 1 124 1952 27 CYS CA C 58.604 0.032 1 125 1952 27 CYS CB C 31.792 0.051 1 126 1952 27 CYS N N 121.173 0.031 1 127 1953 28 ASP H H 7.974 0.001 1 128 1953 28 ASP C C 175.587 0.000 1 129 1953 28 ASP CA C 55.079 0.099 1 130 1953 28 ASP CB C 40.294 0.050 1 131 1953 28 ASP N N 117.787 0.046 1 132 1954 29 LYS H H 8.482 0.003 1 133 1954 29 LYS C C 176.312 0.000 1 134 1954 29 LYS CA C 56.568 0.032 1 135 1954 29 LYS CB C 34.743 0.023 1 136 1954 29 LYS N N 120.041 0.087 1 137 1955 30 GLY H H 8.282 0.003 1 138 1955 30 GLY C C 175.174 0.000 1 139 1955 30 GLY CA C 44.572 0.072 1 140 1955 30 GLY N N 105.439 0.060 1 141 1956 31 CYS H H 8.932 0.002 1 142 1956 31 CYS C C 174.193 0.000 1 143 1956 31 CYS CA C 58.184 0.044 1 144 1956 31 CYS CB C 30.317 0.036 1 145 1956 31 CYS N N 121.567 0.031 1 146 1957 32 HIS H H 9.441 0.001 1 147 1957 32 HIS CA C 59.293 0.080 1 148 1957 32 HIS CB C 30.382 0.018 1 149 1957 32 HIS N N 129.375 0.084 1 150 1958 33 THR H H 9.101 0.003 1 151 1958 33 THR C C 177.059 0.000 1 152 1958 33 THR CA C 65.616 0.059 1 153 1958 33 THR N N 116.022 0.032 1 154 1959 34 TYR H H 6.646 0.002 1 155 1959 34 TYR C C 176.454 0.000 1 156 1959 34 TYR CA C 56.697 0.024 1 157 1959 34 TYR CB C 36.838 0.063 1 158 1959 34 TYR N N 112.079 0.076 1 159 1960 35 CYS H H 7.022 0.005 1 160 1960 35 CYS C C 174.286 0.000 1 161 1960 35 CYS CA C 61.386 0.082 1 162 1960 35 CYS CB C 31.337 0.021 1 163 1960 35 CYS N N 123.506 0.046 1 164 1961 36 HIS H H 6.840 0.001 1 165 1961 36 HIS CA C 58.736 0.046 1 166 1961 36 HIS CB C 29.579 0.055 1 167 1961 36 HIS N N 119.532 0.041 1 168 1962 37 ARG H H 7.447 0.002 1 169 1962 37 ARG CA C 52.164 0.014 1 170 1962 37 ARG CB C 31.560 0.000 1 171 1962 37 ARG N N 122.824 0.047 1 172 1963 38 PRO C C 176.254 0.000 1 173 1963 38 PRO CA C 63.084 0.025 1 174 1963 38 PRO CB C 34.614 0.007 1 175 1964 39 LYS H H 8.553 0.001 1 176 1964 39 LYS C C 177.059 0.000 1 177 1964 39 LYS CA C 58.455 0.040 1 178 1964 39 LYS CB C 32.745 0.041 1 179 1964 39 LYS N N 121.230 0.035 1 180 1965 40 ILE H H 7.761 0.002 1 181 1965 40 ILE C C 176.248 0.059 1 182 1965 40 ILE CA C 60.859 0.014 1 183 1965 40 ILE CB C 39.268 0.010 1 184 1965 40 ILE N N 124.265 0.058 1 185 1966 41 THR H H 8.597 0.003 1 186 1966 41 THR C C 174.457 0.000 1 187 1966 41 THR CA C 62.754 0.085 1 188 1966 41 THR CB C 69.183 0.072 1 189 1966 41 THR N N 118.377 0.073 1 190 1967 42 THR H H 7.407 0.002 1 191 1967 42 THR C C 172.798 0.000 1 192 1967 42 THR CA C 60.728 0.075 1 193 1967 42 THR CB C 70.689 0.050 1 194 1967 42 THR N N 116.931 0.037 1 195 1968 43 ILE H H 8.440 0.001 1 196 1968 43 ILE CA C 58.975 0.040 1 197 1968 43 ILE CB C 37.411 0.000 1 198 1968 43 ILE N N 126.748 0.045 1 199 1969 44 PRO C C 176.053 0.000 1 200 1969 44 PRO CA C 63.080 0.040 1 201 1969 44 PRO CB C 32.166 0.018 1 202 1970 45 ASP H H 8.326 0.001 1 203 1970 45 ASP C C 176.408 0.000 1 204 1970 45 ASP CA C 54.068 0.065 1 205 1970 45 ASP CB C 41.397 0.005 1 206 1970 45 ASP N N 121.246 0.040 1 207 1971 46 GLY H H 7.926 0.001 1 208 1971 46 GLY C C 172.955 0.000 1 209 1971 46 GLY CA C 44.551 0.045 1 210 1971 46 GLY N N 109.797 0.026 1 211 1972 47 ASP H H 8.148 0.001 1 212 1972 47 ASP C C 175.591 0.000 1 213 1972 47 ASP CA C 54.616 0.024 1 214 1972 47 ASP CB C 41.549 0.039 1 215 1972 47 ASP N N 121.349 0.011 1 216 1973 48 TRP H H 9.269 0.002 1 217 1973 48 TRP C C 172.164 0.000 1 218 1973 48 TRP CA C 59.256 0.044 1 219 1973 48 TRP CB C 30.447 0.028 1 220 1973 48 TRP N N 124.982 0.070 1 221 1974 49 PHE H H 6.787 0.001 1 222 1974 49 PHE CA C 54.861 0.102 1 223 1974 49 PHE CB C 42.134 0.070 1 224 1974 49 PHE N N 122.986 0.040 1 225 1975 50 CYS H H 9.251 0.003 1 226 1975 50 CYS C C 173.459 0.000 1 227 1975 50 CYS CA C 57.007 0.050 1 228 1975 50 CYS CB C 29.180 0.000 1 229 1975 50 CYS N N 126.000 0.068 1 230 1976 51 PRO C C 178.945 0.000 1 231 1976 51 PRO CA C 65.738 0.018 1 232 1976 51 PRO CB C 31.881 0.003 1 233 1977 52 ALA H H 8.021 0.001 1 234 1977 52 ALA C C 180.312 0.000 1 235 1977 52 ALA CA C 54.954 0.084 1 236 1977 52 ALA CB C 18.754 0.041 1 237 1977 52 ALA N N 121.599 0.069 1 238 1978 53 CYS H H 8.357 0.001 1 239 1978 53 CYS C C 178.613 0.000 1 240 1978 53 CYS CA C 65.466 0.030 1 241 1978 53 CYS CB C 28.534 0.005 1 242 1978 53 CYS N N 122.704 0.013 1 243 1979 54 ILE H H 8.125 0.002 1 244 1979 54 ILE C C 178.015 0.000 1 245 1979 54 ILE CA C 63.235 0.041 1 246 1979 54 ILE CB C 37.327 0.051 1 247 1979 54 ILE N N 120.924 0.025 1 248 1980 55 ALA H H 7.631 0.001 1 249 1980 55 ALA C C 178.660 0.000 1 250 1980 55 ALA CA C 53.733 0.026 1 251 1980 55 ALA CB C 18.193 0.065 1 252 1980 55 ALA N N 121.906 0.052 1 253 1981 56 LYS H H 7.368 0.002 1 254 1981 56 LYS C C 176.307 0.000 1 255 1981 56 LYS CA C 57.047 0.079 1 256 1981 56 LYS CB C 32.597 0.017 1 257 1981 56 LYS N N 117.421 0.010 1 258 1982 57 ALA H H 7.544 0.001 1 259 1982 57 ALA C C 176.698 0.000 1 260 1982 57 ALA CA C 52.346 0.051 1 261 1982 57 ALA CB C 19.093 0.039 1 262 1982 57 ALA N N 123.317 0.059 1 263 1983 58 SER H H 7.561 0.001 1 264 1983 58 SER CA C 60.121 0.004 1 265 1983 58 SER CB C 64.860 0.000 1 266 1983 58 SER N N 120.376 0.034 1 stop_ save_