data_19796 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; hinge region of human Col7 ; _BMRB_accession_number 19796 _BMRB_flat_file_name bmr19796.str _Entry_type original _Submission_date 2014-02-13 _Accession_date 2014-02-13 _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 Richer Barbara . . 2 Seeger Karsten . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 63 "13C chemical shifts" 174 "15N chemical shifts" 61 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-09-05 update author 'update author sequence numbering and entry citation' 2014-05-06 original author 'original release' stop_ _Original_release_date 2014-02-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The hinge region of type VII collagen is intrinsically disordered ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24810542 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Richer Barbara . . 2 Seeger Karsten . . stop_ _Journal_abbreviation 'Matrix Biology' _Journal_volume 36 _Journal_issue . _Journal_ISSN 1569-1802 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 77 _Page_last 83 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'hinge monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'hinge monomer' $hCol7_hinge stop_ _System_molecular_weight . _System_physical_state 'molten globule' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_hCol7_hinge _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common hCol7_hinge _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 73 _Mol_residue_sequence ; GRAMGLPGERGLRGEPGSVP NVDRLLETAGIKASALREIV ETWDESSGSFLPVPERRRGP KGDSGEQGPPGKE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 GLY 2 -2 ARG 3 -1 ALA 4 0 MET 5 1925 GLY 6 1926 LEU 7 1927 PRO 8 1928 GLY 9 1929 GLU 10 1930 ARG 11 1931 GLY 12 1932 LEU 13 1933 ARG 14 1934 GLY 15 1935 GLU 16 1936 PRO 17 1937 GLY 18 1938 SER 19 1939 VAL 20 1940 PRO 21 1941 ASN 22 1942 VAL 23 1943 ASP 24 1944 ARG 25 1945 LEU 26 1946 LEU 27 1947 GLU 28 1948 THR 29 1949 ALA 30 1950 GLY 31 1951 ILE 32 1952 LYS 33 1953 ALA 34 1954 SER 35 1955 ALA 36 1956 LEU 37 1957 ARG 38 1958 GLU 39 1959 ILE 40 1960 VAL 41 1961 GLU 42 1962 THR 43 1963 TRP 44 1964 ASP 45 1965 GLU 46 1966 SER 47 1967 SER 48 1968 GLY 49 1969 SER 50 1970 PHE 51 1971 LEU 52 1972 PRO 53 1973 VAL 54 1974 PRO 55 1975 GLU 56 1976 ARG 57 1977 ARG 58 1978 ARG 59 1979 GLY 60 1980 PRO 61 1981 LYS 62 1982 GLY 63 1983 ASP 64 1984 SER 65 1985 GLY 66 1986 GLU 67 1987 GLN 68 1988 GLY 69 1989 PRO 70 1990 PRO 71 1991 GLY 72 1992 LYS 73 1993 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $hCol7_hinge 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 _Details $hCol7_hinge 'recombinant technology' . Escherichia coli . pTWIN1 'the N-terminal intein tag was used' 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 $hCol7_hinge 0.2 mM '[U-13C; U-15N]' D2O 10 % '[U-100% 2H]' H2O 90 % 'natural abundance' TSP 0.05 mM 'natural abundance' 'potassium phosphate' 10 mM '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_CCPN _Saveframe_category software _Name CCPN _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _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_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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_ ####################### # 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 . M pH 7.4 . 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 TSP-d4 C 13 'methyl protons' ppm 0 internal indirect . . . 0.251449530 TSP-d4 H 1 'methyl protons' ppm 0 internal direct . . . 1.000000000 TSP-d4 N 15 'methyl protons' ppm 0 internal 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 $CCPN stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCACB' '3D CBCA(CO)NH' '3D HN(CO)CA' 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 'hinge monomer' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 -2 2 ARG C C 176.101 0.000 1 2 -2 2 ARG CA C 56.215 0.000 1 3 -2 2 ARG CB C 30.987 0.000 1 4 -1 3 ALA H H 8.700 0.002 1 5 -1 3 ALA C C 177.718 0.000 1 6 -1 3 ALA CA C 52.544 0.01 1 7 -1 3 ALA CB C 18.975 0.005 1 8 -1 3 ALA N N 126.543 0.038 1 9 0 4 MET H H 8.637 0.001 1 10 0 4 MET C C 176.840 0.000 1 11 0 4 MET CA C 55.343 0.015 1 12 0 4 MET CB C 32.964 0.068 1 13 0 4 MET N N 120.610 0.011 1 14 1925 5 GLY H H 8.564 0.002 1 15 1925 5 GLY CA C 45.094 0.042 1 16 1925 5 GLY N N 110.197 0.033 1 17 1926 6 LEU H H 8.349 0.0 1 18 1926 6 LEU CA C 53.176 0.000 1 19 1926 6 LEU CB C 41.441 0.000 1 20 1926 6 LEU N N 122.999 0.024 1 21 1929 9 GLU C C 176.934 0.000 1 22 1929 9 GLU CA C 56.819 0.000 1 23 1929 9 GLU CB C 30.157 0.000 1 24 1930 10 ARG H H 8.590 0.001 1 25 1930 10 ARG C C 176.991 0.000 1 26 1930 10 ARG CA C 56.564 0.006 1 27 1930 10 ARG CB C 30.722 0.051 1 28 1930 10 ARG N N 121.928 0.047 1 29 1931 11 GLY H H 8.549 0.001 1 30 1931 11 GLY C C 174.253 0.000 1 31 1931 11 GLY CA C 45.307 0.019 1 32 1931 11 GLY N N 109.623 0.021 1 33 1932 12 LEU H H 8.289 0.002 1 34 1932 12 LEU C C 177.761 0.000 1 35 1932 12 LEU CA C 55.373 0.024 1 36 1932 12 LEU CB C 42.376 0.017 1 37 1932 12 LEU N N 121.813 0.04 1 38 1933 13 ARG H H 8.571 0.001 1 39 1933 13 ARG C C 176.791 0.000 1 40 1933 13 ARG CA C 56.216 0.052 1 41 1933 13 ARG CB C 30.580 0.005 1 42 1933 13 ARG N N 121.612 0.044 1 43 1934 14 GLY H H 8.466 0.004 1 44 1934 14 GLY C C 173.809 0.000 1 45 1934 14 GLY CA C 44.898 0.047 1 46 1934 14 GLY N N 110.030 0.082 1 47 1935 15 GLU H H 8.491 0.001 1 48 1935 15 GLU CA C 54.479 0.000 1 49 1935 15 GLU CB C 29.313 0.000 1 50 1935 15 GLU N N 121.819 0.034 1 51 1937 17 GLY C C 174.213 0.000 1 52 1937 17 GLY CA C 45.176 0.000 1 53 1938 18 SER H H 8.240 0.001 1 54 1938 18 SER CA C 58.404 0.002 1 55 1938 18 SER CB C 64.099 0.018 1 56 1938 18 SER N N 115.801 0.027 1 57 1939 19 VAL H H 8.364 0.001 1 58 1939 19 VAL CA C 59.991 0.000 1 59 1939 19 VAL CB C 32.614 0.000 1 60 1939 19 VAL N N 123.170 0.017 1 61 1940 20 PRO C C 176.592 0.000 1 62 1940 20 PRO CA C 63.301 0.000 1 63 1940 20 PRO CB C 32.229 0.000 1 64 1941 21 ASN H H 8.714 0.002 1 65 1941 21 ASN HD21 H 7.071 0.001 1 66 1941 21 ASN HD22 H 7.775 0.001 1 67 1941 21 ASN C C 175.645 0.000 1 68 1941 21 ASN CA C 53.560 0.006 1 69 1941 21 ASN CB C 38.857 0.004 1 70 1941 21 ASN CG C 176.968 0.000 1 71 1941 21 ASN N N 119.799 0.047 1 72 1941 21 ASN ND2 N 113.519 0.076 1 73 1942 22 VAL H H 8.296 0.002 1 74 1942 22 VAL C C 175.947 0.000 1 75 1942 22 VAL CA C 62.686 0.005 1 76 1942 22 VAL CB C 32.719 0.062 1 77 1942 22 VAL N N 120.781 0.033 1 78 1943 23 ASP H H 8.473 0.002 1 79 1943 23 ASP C C 176.737 0.000 1 80 1943 23 ASP CA C 54.782 0.007 1 81 1943 23 ASP CB C 41.074 0.066 1 82 1943 23 ASP N N 123.710 0.036 1 83 1944 24 ARG H H 8.362 0.002 1 84 1944 24 ARG C C 176.753 0.000 1 85 1944 24 ARG CA C 56.672 0.000 1 86 1944 24 ARG CB C 30.344 0.000 1 87 1944 24 ARG N N 121.983 0.042 1 88 1945 25 LEU H H 8.347 0.001 1 89 1945 25 LEU C C 177.942 0.000 1 90 1945 25 LEU CA C 55.908 0.029 1 91 1945 25 LEU CB C 41.687 0.013 1 92 1945 25 LEU N N 122.378 0.047 1 93 1946 26 LEU H H 8.194 0.002 1 94 1946 26 LEU C C 177.908 0.000 1 95 1946 26 LEU CA C 55.525 0.003 1 96 1946 26 LEU CB C 42.062 0.056 1 97 1946 26 LEU N N 122.039 0.047 1 98 1947 27 GLU H H 8.386 0.002 1 99 1947 27 GLU C C 177.169 0.000 1 100 1947 27 GLU CA C 56.964 0.013 1 101 1947 27 GLU CB C 30.207 0.025 1 102 1947 27 GLU N N 121.676 0.055 1 103 1948 28 THR H H 8.237 0.003 1 104 1948 28 THR C C 174.707 0.000 1 105 1948 28 THR CA C 62.427 0.031 1 106 1948 28 THR CB C 69.803 0.016 1 107 1948 28 THR N N 114.959 0.024 1 108 1949 29 ALA H H 8.410 0.002 1 109 1949 29 ALA C C 178.472 0.000 1 110 1949 29 ALA CA C 53.108 0.005 1 111 1949 29 ALA CB C 19.042 0.051 1 112 1949 29 ALA N N 126.306 0.055 1 113 1950 30 GLY H H 8.441 0.003 1 114 1950 30 GLY C C 174.331 0.000 1 115 1950 30 GLY CA C 45.381 0.004 1 116 1950 30 GLY N N 108.107 0.039 1 117 1951 31 ILE H H 8.067 0.001 1 118 1951 31 ILE C C 176.699 0.000 1 119 1951 31 ILE CA C 61.479 0.004 1 120 1951 31 ILE CB C 38.602 0.001 1 121 1951 31 ILE N N 121.055 0.03 1 122 1952 32 LYS H H 8.530 0.003 1 123 1952 32 LYS C C 176.682 0.000 1 124 1952 32 LYS CA C 56.433 0.016 1 125 1952 32 LYS CB C 32.983 0.004 1 126 1952 32 LYS N N 125.995 0.018 1 127 1953 33 ALA H H 8.510 0.002 1 128 1953 33 ALA CA C 52.884 0.047 1 129 1953 33 ALA CB C 19.091 0.005 1 130 1953 33 ALA N N 125.754 0.023 1 131 1954 34 SER H H 8.424 0.003 1 132 1954 34 SER C C 174.666 0.000 1 133 1954 34 SER CA C 58.738 0.048 1 134 1954 34 SER CB C 63.733 0.022 1 135 1954 34 SER N N 115.327 0.03 1 136 1955 35 ALA H H 8.379 0.004 1 137 1955 35 ALA C C 177.903 0.000 1 138 1955 35 ALA CA C 52.717 0.025 1 139 1955 35 ALA CB C 19.146 0.021 1 140 1955 35 ALA N N 126.034 0.048 1 141 1956 36 LEU H H 8.202 0.001 1 142 1956 36 LEU CA C 55.387 0.002 1 143 1956 36 LEU CB C 42.187 0.028 1 144 1956 36 LEU N N 121.081 0.025 1 145 1957 37 ARG H H 8.311 0.0 1 146 1957 37 ARG C C 176.111 0.000 1 147 1957 37 ARG CA C 56.151 0.032 1 148 1957 37 ARG CB C 30.837 0.036 1 149 1957 37 ARG N N 121.850 0.037 1 150 1958 38 GLU H H 8.502 0.002 1 151 1958 38 GLU CA C 56.613 0.022 1 152 1958 38 GLU CB C 30.296 0.055 1 153 1958 38 GLU N N 122.210 0.057 1 154 1959 39 ILE H H 8.354 0.002 1 155 1959 39 ILE C C 176.179 0.000 1 156 1959 39 ILE CA C 61.155 0.056 1 157 1959 39 ILE CB C 38.599 0.019 1 158 1959 39 ILE N N 122.945 0.024 1 159 1960 40 VAL H H 8.432 0.001 1 160 1960 40 VAL C C 175.921 0.000 1 161 1960 40 VAL CA C 62.206 0.01 1 162 1960 40 VAL CB C 32.849 0.017 1 163 1960 40 VAL N N 125.022 0.033 1 164 1961 41 GLU H H 8.575 0.003 1 165 1961 41 GLU C C 176.082 0.000 1 166 1961 41 GLU CA C 56.206 0.011 1 167 1961 41 GLU CB C 31.136 0.076 1 168 1961 41 GLU N N 124.769 0.036 1 169 1962 42 THR H H 8.607 0.002 1 170 1962 42 THR C C 173.813 0.000 1 171 1962 42 THR CA C 61.326 0.026 1 172 1962 42 THR CB C 70.579 0.036 1 173 1962 42 THR N N 115.434 0.044 1 174 1963 43 TRP H H 8.734 0.002 1 175 1963 43 TRP HE1 H 10.242 0.000 1 176 1963 43 TRP C C 174.960 0.000 1 177 1963 43 TRP CA C 57.514 0.009 1 178 1963 43 TRP CB C 29.844 0.01 1 179 1963 43 TRP N N 125.351 0.033 1 180 1963 43 TRP NE1 N 129.267 0.000 1 181 1964 44 ASP H H 8.208 0.002 1 182 1964 44 ASP C C 175.243 0.000 1 183 1964 44 ASP CA C 53.063 0.01 1 184 1964 44 ASP CB C 42.063 0.019 1 185 1964 44 ASP N N 126.354 0.068 1 186 1965 45 GLU H H 8.662 0.002 1 187 1965 45 GLU CA C 58.173 0.045 1 188 1965 45 GLU CB C 29.730 0.025 1 189 1965 45 GLU N N 124.845 0.03 1 190 1966 46 SER H H 8.437 0.003 1 191 1966 46 SER C C 175.412 0.000 1 192 1966 46 SER CA C 60.508 0.002 1 193 1966 46 SER CB C 63.286 0.002 1 194 1966 46 SER N N 115.096 0.073 1 195 1967 47 SER H H 7.888 0.001 1 196 1967 47 SER C C 175.535 0.000 1 197 1967 47 SER CA C 58.842 0.005 1 198 1967 47 SER CB C 64.306 0.005 1 199 1967 47 SER N N 115.423 0.02 1 200 1968 48 GLY H H 8.112 0.002 1 201 1968 48 GLY C C 173.989 0.000 1 202 1968 48 GLY CA C 46.512 0.023 1 203 1968 48 GLY N N 112.813 0.036 1 204 1969 49 SER H H 7.500 0.002 1 205 1969 49 SER C C 172.805 0.000 1 206 1969 49 SER CA C 57.694 0.029 1 207 1969 49 SER CB C 65.160 0.001 1 208 1969 49 SER N N 113.728 0.084 1 209 1970 50 PHE H H 8.496 0.003 1 210 1970 50 PHE C C 175.749 0.000 1 211 1970 50 PHE CA C 58.153 0.017 1 212 1970 50 PHE CB C 39.950 0.026 1 213 1970 50 PHE N N 120.478 0.041 1 214 1971 51 LEU H H 8.519 0.002 1 215 1971 51 LEU CA C 52.441 0.000 1 216 1971 51 LEU CB C 42.555 0.000 1 217 1971 51 LEU N N 125.271 0.075 1 218 1972 52 PRO C C 176.855 0.000 1 219 1972 52 PRO CA C 62.685 0.000 1 220 1972 52 PRO CB C 31.968 0.000 1 221 1973 53 VAL H H 8.393 0.001 1 222 1973 53 VAL CA C 60.465 0.000 1 223 1973 53 VAL CB C 32.357 0.000 1 224 1973 53 VAL N N 122.574 0.011 1 225 1974 54 PRO C C 177.008 0.000 1 226 1974 54 PRO CA C 63.466 0.000 1 227 1974 54 PRO CB C 32.052 0.000 1 228 1975 55 GLU H H 8.636 0.003 1 229 1975 55 GLU C C 176.662 0.000 1 230 1975 55 GLU CA C 56.885 0.008 1 231 1975 55 GLU CB C 30.149 0.03 1 232 1975 55 GLU N N 121.293 0.055 1 233 1976 56 ARG H H 8.518 0.001 1 234 1976 56 ARG C C 176.264 0.000 1 235 1976 56 ARG CA C 56.207 0.004 1 236 1976 56 ARG CB C 30.533 0.0 1 237 1976 56 ARG N N 122.877 0.006 1 238 1977 57 ARG H H 8.573 0.001 1 239 1977 57 ARG C C 176.293 0.000 1 240 1977 57 ARG CA C 56.222 0.039 1 241 1977 57 ARG CB C 30.654 0.023 1 242 1977 57 ARG N N 123.071 0.075 1 243 1978 58 ARG H H 8.625 0.003 1 244 1978 58 ARG C C 176.533 0.000 1 245 1978 58 ARG CA C 56.144 0.000 1 246 1978 58 ARG CB C 30.996 0.017 1 247 1978 58 ARG N N 123.309 0.016 1 248 1979 59 GLY H H 8.481 0.005 1 249 1979 59 GLY N N 110.422 0.073 1 250 1980 60 PRO C C 177.448 0.000 1 251 1980 60 PRO CA C 63.335 0.000 1 252 1980 60 PRO CB C 32.099 0.0 1 253 1981 61 LYS H H 8.690 0.001 1 254 1981 61 LYS C C 177.359 0.000 1 255 1981 61 LYS CA C 56.669 0.027 1 256 1981 61 LYS CB C 32.847 0.01 1 257 1981 61 LYS N N 121.362 0.032 1 258 1982 62 GLY H H 8.504 0.004 1 259 1982 62 GLY CA C 45.309 0.034 1 260 1982 62 GLY N N 110.208 0.031 1 261 1983 63 ASP H H 8.414 0.003 1 262 1983 63 ASP C C 176.724 0.000 1 263 1983 63 ASP CA C 54.310 0.011 1 264 1983 63 ASP CB C 41.412 0.002 1 265 1983 63 ASP N N 120.775 0.009 1 266 1984 64 SER H H 8.558 0.003 1 267 1984 64 SER C C 175.329 0.000 1 268 1984 64 SER CA C 58.929 0.019 1 269 1984 64 SER CB C 63.802 0.004 1 270 1984 64 SER N N 116.658 0.025 1 271 1985 65 GLY H H 8.596 0.002 1 272 1985 65 GLY CA C 45.377 0.000 1 273 1985 65 GLY N N 110.902 0.029 1 274 1986 66 GLU C C 176.714 0.000 1 275 1986 66 GLU CA C 56.621 0.015 1 276 1986 66 GLU CB C 30.234 0.000 1 277 1987 67 GLN H H 8.668 0.001 1 278 1987 67 GLN HE21 H 7.650 0.001 1 279 1987 67 GLN HE22 H 6.967 0.001 1 280 1987 67 GLN C C 176.266 0.000 1 281 1987 67 GLN CA C 55.957 0.071 1 282 1987 67 GLN CB C 29.614 0.003 1 283 1987 67 GLN CD C 180.658 0.029 1 284 1987 67 GLN N N 121.740 0.033 1 285 1987 67 GLN NE2 N 113.264 0.097 1 286 1988 68 GLY H H 8.463 0.003 1 287 1988 68 GLY CA C 44.481 0.000 1 288 1988 68 GLY N N 110.621 0.073 1 289 1991 71 GLY CA C 45.194 0.000 1 290 1992 72 LYS H H 8.302 0.004 1 291 1992 72 LYS C C 175.822 0.000 1 292 1992 72 LYS CA C 56.197 0.006 1 293 1992 72 LYS CB C 33.258 0.033 1 294 1992 72 LYS N N 121.717 0.09 1 295 1993 73 GLU H H 8.284 0.001 1 296 1993 73 GLU CA C 58.334 0.000 1 297 1993 73 GLU CB C 30.947 0.000 1 298 1993 73 GLU N N 127.929 0.029 1 stop_ save_