data_5961 #Corrected using PDB structure: 2FYJA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 12 C HA 4.68 3.80 # 21 S HA 4.43 5.85 # 22 W HA 5.23 4.34 # 23 T HA 4.48 3.43 # 25 D HA 4.94 4.22 # 45 C HA 4.72 3.34 # 50 Q HA 5.33 4.61 # 60 N HA 4.16 4.87 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 14 S N 109.78 122.90 # 32 D N 117.71 130.64 # 49 T N 104.02 114.84 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 24 C H 8.68 6.43 # 29 D H 10.06 7.58 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.07 N/A N/A N/A -0.54 -0.13 # #bmr5961.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr5961.str file): #HA CA CB CO N HN #N/A N/A N/A N/A -0.54 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.05 N/A N/A N/A +/-0.65 +/-0.11 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.426 N/A N/A N/A 0.555 0.467 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.197 N/A N/A N/A 2.598 0.460 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Binding site structure of one LRP/RAP complex - implications for a common ligand/receptor binding motif ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jensen Gitte A. . 2 Andersen Olav M. . 3 Bonvin Alexandre M.J.J. . 4 Bjerrum-Bohr Ida . . 5 Etzeroth Michael . . 6 Thoegersen Hans C. . 7 Poulsen Flemming M. . 8 Kragelund Birthe B. . stop_ _BMRB_accession_number 5961 _BMRB_flat_file_name bmr5961.str _Entry_type new _Submission_date 2003-09-30 _Accession_date 2003-10-01 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 392 '15N chemical shifts' 80 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Binding site structure of one LRP-RAP complex: implications for a common ligand-receptor binding motif ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . _PubMed_ID 16938309 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jensen Gitte A. . 2 Andersen Olav M. . 3 Bonvin Alexandre M.J.J. . 4 Bjerrum-Bohr Ida . . 5 Etzerodt Michael . . 6 Thoegersen Hans C. . 7 O'Shea C. . . 8 Poulsen Flemming M. . 9 Kragelund Birthe B. . stop_ _Journal_abbreviation "J. Mol. Biol." _Journal_volume 362 _Journal_issue 4 _Page_first 700 _Page_last 716 _Year 2006 loop_ _Keyword NMR RAP CR56 receptor "recognition helix" HADDOCK stop_ save_ ################################## # Molecular system description # ################################## save_system_CR56 _Saveframe_category molecular_system _Mol_system_name "complement type repeats 5 and 6 from LRP" _Abbreviation_common CR56 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CR56 $CR56 'CALCIUM (II) ION, 1' $CA_2+ 'CALCIUM (II) ION, 2' $CA_2+ stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function "LRP receptor unit" "minimal binding unit" "ligand binding repeat" stop_ save_ ######################## # Monomeric polymers # ######################## save_CR56 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "complement type repeats 5 and 6" _Name_variant . _Abbreviation_common CR56 _Molecular_mass 8938.61 _Mol_thiol_state 'all disulfide bound' _Details ; CR56 binds two Ca2+ ions. ; ############################## # Polymer residue sequence # ############################## _Residue_count 82 _Mol_residue_sequence ; SARTCPPNQFSCASGRCIPI SWTCDLDDDCGDRSDESASC AYPTCFPLTQFTCNNGRCIN INWRCDNDNDCGDNSDEAGC SH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 932 SER 2 933 ALA 3 934 ARG 4 935 THR 5 936 CYS 6 937 PRO 7 938 PRO 8 939 ASN 9 940 GLN 10 941 PHE 11 942 SER 12 943 CYS 13 944 ALA 14 945 SER 15 946 GLY 16 947 ARG 17 948 CYS 18 949 ILE 19 950 PRO 20 951 ILE 21 952 SER 22 953 TRP 23 954 THR 24 955 CYS 25 956 ASP 26 957 LEU 27 958 ASP 28 959 ASP 29 960 ASP 30 961 CYS 31 962 GLY 32 963 ASP 33 964 ARG 34 965 SER 35 966 ASP 36 967 GLU 37 968 SER 38 969 ALA 39 970 SER 40 971 CYS 41 972 ALA 42 973 TYR 43 974 PRO 44 975 THR 45 976 CYS 46 977 PHE 47 978 PRO 48 979 LEU 49 980 THR 50 981 GLN 51 982 PHE 52 983 THR 53 984 CYS 54 985 ASN 55 986 ASN 56 987 GLY 57 988 ARG 58 989 CYS 59 990 ILE 60 991 ASN 61 992 ILE 62 993 ASN 63 994 TRP 64 995 ARG 65 996 CYS 66 997 ASP 67 998 ASN 68 999 ASP 69 1000 ASN 70 1001 ASP 71 1002 CYS 72 1003 GLY 73 1004 ASP 74 1005 ASN 75 1006 SER 76 1007 ASP 77 1008 GLU 78 1009 ALA 79 1010 GLY 80 1011 CYS 81 1012 SER 82 1013 HIS stop_ save_ ############# # Ligands # ############# save_CA_2+ _Saveframe_category ligand _Mol_type non-polymer _Name_common 'CALCIUM (II) ION' _Abbreviation_common Ca _Name_IUPAC . _BMRB_code CA_2+ _PDB_code CA _Mol_empirical_formula CA1 _Mol_charge 2+ _Mol_paramagnetic no _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA ? 2+ ? ? stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single disulfide CR56 5 CYS SG CR56 17 CYS SG single disulfide CR56 12 CYS SG CR56 30 CYS SG single disulfide CR56 24 CYS SG CR56 40 CYS SG single disulfide CR56 45 CYS SG CR56 58 CYS SG single disulfide CR56 53 CYS SG CR56 71 CYS SG single disulfide CR56 65 CYS SG CR56 80 CYS SG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CR56 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 $CR56 'recombinant technology' "Escherichis coli" Escherichis coli BL21(DE3) pT7 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CR56 0.5 mM . CaCl2 10 mM . MgCl2 1 mM . NaCl 100 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CR56 0.5 mM "[U-99% 15N]" CaCl2 10 mM . MgCl2 1 mM . NaCl 100 mM . stop_ save_ ############################ # Computer software used # ############################ save_PRONTO _Saveframe_category software _Name PRONTO _Version 20020517 loop_ _Task "assignment tool" stop_ _Details ; 'Carlsberg A/S' Gamle Carlsberg Vej 10, DK-2500 Valby mk@crc.dk ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY _Field_strength 750 save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY _Field_strength 800 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; DQF-COSY NOESY TOCSY 15N-HSQC 15N-NOESY-HSQC 15N-TOCSY-HSQC ; save_ ####################### # Sample conditions # ####################### save_conditions _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 pH temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference 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 external indirect . . . 0.10132905 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 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) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name CR56 loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 SER H H 7.80 . 1 2 1 SER HA H 4.44 . 1 3 1 SER HB2 H 2.94 . 2 4 1 SER HB3 H 2.79 . 2 5 1 SER N N 117.87 . 1 6 2 ALA HB H 1.34 . 1 7 2 ALA HA H 4.28 . 1 8 3 ARG H H 8.39 . 1 9 3 ARG HA H 4.39 . 1 10 3 ARG HB3 H 1.82 . 2 11 3 ARG HB2 H 1.71 . 2 12 3 ARG HG2 H 1.56 . 2 13 3 ARG HD2 H 3.13 . 2 14 3 ARG N N 120.11 . 1 15 4 THR H H 8.14 . 1 16 4 THR HA H 4.28 . 1 17 4 THR HG2 H 1.13 . 1 18 4 THR HB H 4.10 . 1 19 4 THR N N 115.27 . 1 20 5 CYS H H 8.38 . 1 21 5 CYS HA H 5.06 . 1 22 5 CYS HB3 H 2.42 . 2 23 5 CYS HB2 H 2.84 . 2 24 5 CYS N N 121.81 . 1 25 6 PRO HG2 H 1.92 . 2 26 6 PRO HB3 H 1.67 . 2 27 6 PRO HB2 H 2.44 . 2 28 6 PRO HD3 H 3.41 . 2 29 6 PRO HD2 H 3.84 . 2 30 6 PRO HG3 H 1.86 . 2 31 7 PRO HD3 H 3.54 . 2 32 7 PRO HG3 H 1.97 . 2 33 7 PRO HB3 H 1.82 . 2 34 7 PRO HB2 H 2.30 . 2 35 7 PRO HA H 4.30 . 1 36 7 PRO HG2 H 2.02 . 2 37 7 PRO HD2 H 3.74 . 2 38 8 ASN HA H 4.42 . 1 39 8 ASN HB2 H 3.08 . 2 40 8 ASN HB3 H 2.89 . 2 41 8 ASN HD22 H 6.87 . 2 42 8 ASN HD21 H 7.53 . 2 43 8 ASN ND2 N 113.05 . 1 44 8 ASN H H 7.53 . 1 45 9 GLN HB3 H 1.77 . 2 46 9 GLN HB2 H 2.12 . 2 47 9 GLN H H 7.86 . 1 48 9 GLN HA H 4.79 . 1 49 9 GLN N N 117.58 . 1 50 9 GLN HE22 H 6.31 . 2 51 9 GLN HE21 H 7.04 . 2 52 9 GLN NE2 N 108.09 . 1 53 9 GLN HG3 H 1.85 . 2 54 9 GLN HG2 H 2.43 . 2 55 10 PHE H H 9.73 . 1 56 10 PHE N N 123.01 . 1 57 10 PHE HA H 4.57 . 1 58 10 PHE HB3 H 2.66 . 2 59 10 PHE HB2 H 2.73 . 2 60 10 PHE HE1 H 7.28 . 3 61 10 PHE HD1 H 7.04 . 3 62 10 PHE HZ H 7.32 . 1 63 11 SER H H 7.57 . 1 64 11 SER HA H 4.59 . 1 65 11 SER N N 120.24 . 1 66 11 SER HB3 H 3.45 . 2 67 11 SER HB2 H 3.52 . 2 68 12 CYS H H 8.70 . 1 69 12 CYS HA H 4.61 . 1 70 12 CYS N N 125.17 . 1 71 12 CYS HB3 H 3.10 . 2 72 12 CYS HB2 H 3.49 . 2 73 13 ALA H H 9.16 . 1 74 13 ALA HA H 4.05 . 1 75 13 ALA HB H 1.55 . 1 76 13 ALA N N 129.31 . 1 77 14 SER HB3 H 3.48 . 2 78 14 SER H H 7.98 . 1 79 14 SER HA H 4.21 . 1 80 14 SER N N 109.78 . 1 81 14 SER HB2 H 3.91 . 2 82 15 GLY H H 7.86 . 1 83 15 GLY HA2 H 4.41 . 2 84 15 GLY N N 110.26 . 1 85 15 GLY HA3 H 3.49 . 2 86 16 ARG H H 7.15 . 1 87 16 ARG HA H 4.16 . 1 88 16 ARG N N 120.33 . 1 89 16 ARG HB2 H 1.64 . 2 90 16 ARG HG2 H 1.71 . 2 91 16 ARG HB3 H 1.81 . 2 92 16 ARG HD2 H 3.22 . 2 93 17 CYS H H 8.52 . 1 94 17 CYS HB3 H 2.72 . 2 95 17 CYS HB2 H 3.15 . 2 96 17 CYS HA H 5.57 . 1 97 17 CYS N N 123.47 . 1 98 18 ILE HB H 1.86 . 1 99 18 ILE HG2 H 0.95 . 1 100 18 ILE HG13 H 1.33 . 2 101 18 ILE HG12 H 1.56 . 2 102 18 ILE HD1 H 0.98 . 1 103 18 ILE H H 8.94 . 1 104 18 ILE N N 116.29 . 1 105 18 ILE HA H 4.60 . 1 106 19 PRO HB2 H 1.99 . 2 107 19 PRO HB3 H 0.74 . 2 108 19 PRO HA H 4.11 . 1 109 20 ILE HA H 3.84 . 1 110 20 ILE HG13 H 1.24 . 2 111 20 ILE HG12 H 1.39 . 2 112 20 ILE HG2 H 0.89 . 1 113 20 ILE H H 7.98 . 1 114 20 ILE N N 123.36 . 1 115 20 ILE HB H 1.56 . 1 116 20 ILE HD1 H 0.91 . 1 117 21 SER HB2 H 4.17 . 2 118 21 SER HB3 H 3.92 . 2 119 21 SER HA H 4.36 . 1 120 22 TRP HE1 H 10.06 . 1 121 22 TRP HD1 H 6.96 . 1 122 22 TRP HZ2 H 7.47 . 1 123 22 TRP HH2 H 7.27 . 1 124 22 TRP H H 7.93 . 1 125 22 TRP HA H 5.16 . 1 126 22 TRP HB2 H 3.67 . 2 127 22 TRP N N 120.06 . 1 128 22 TRP NE1 N 127.64 . 1 129 22 TRP HB3 H 3.23 . 2 130 22 TRP HE3 H 7.35 . 1 131 22 TRP HZ3 H 7.23 . 1 132 23 THR HG2 H 0.51 . 1 133 23 THR HB H 4.00 . 1 134 23 THR H H 8.26 . 1 135 23 THR N N 116.02 . 1 136 23 THR HA H 4.41 . 1 137 24 CYS HB2 H 3.14 . 2 138 24 CYS HB3 H 2.97 . 2 139 24 CYS H H 8.81 . 1 140 24 CYS HA H 4.90 . 1 141 24 CYS N N 117.24 . 1 142 25 ASP HB2 H 3.07 . 2 143 25 ASP HB3 H 2.38 . 2 144 25 ASP H H 9.99 . 1 145 25 ASP HA H 4.87 . 1 146 25 ASP N N 121.84 . 1 147 26 LEU H H 9.07 . 1 148 26 LEU HA H 3.48 . 1 149 26 LEU HB2 H 2.30 . 2 150 26 LEU HB3 H 1.34 . 2 151 26 LEU HG H 1.18 . 1 152 26 LEU HD1 H 0.31 . 2 153 26 LEU HD2 H 0.62 . 2 154 26 LEU N N 113.85 . 1 155 27 ASP H H 7.62 . 1 156 27 ASP HA H 4.84 . 1 157 27 ASP HB2 H 2.59 . 2 158 27 ASP HB3 H 2.45 . 2 159 27 ASP N N 118.22 . 1 160 29 ASP H H 10.19 . 1 161 29 ASP HA H 4.83 . 1 162 29 ASP N N 126.98 . 1 163 29 ASP HB3 H 2.82 . 2 164 29 ASP HB2 H 3.02 . 2 165 30 CYS H H 8.56 . 1 166 30 CYS HB2 H 3.51 . 2 167 30 CYS N N 117.67 . 1 168 30 CYS HA H 4.77 . 1 169 30 CYS HB3 H 3.17 . 2 170 31 GLY H H 9.44 . 1 171 31 GLY HA3 H 3.66 . 2 172 31 GLY N N 114.06 . 1 173 31 GLY HA2 H 4.42 . 2 174 32 ASP H H 7.30 . 1 175 32 ASP N N 117.71 . 1 176 32 ASP HB2 H 3.70 . 2 177 32 ASP HB3 H 3.51 . 2 178 32 ASP HA H 4.74 . 1 179 33 ARG H H 9.34 . 1 180 33 ARG HA H 3.70 . 1 181 33 ARG N N 114.95 . 1 182 33 ARG HB2 H 1.94 . 2 183 33 ARG HB3 H 2.14 . 2 184 33 ARG HG2 H 1.30 . 2 185 33 ARG HG3 H 1.52 . 2 186 34 SER H H 9.16 . 1 187 34 SER HA H 4.21 . 1 188 34 SER N N 116.14 . 1 189 34 SER HB2 H 4.41 . 2 190 34 SER HB3 H 4.09 . 2 191 35 ASP HB3 H 2.51 . 2 192 35 ASP HB2 H 2.95 . 2 193 35 ASP H H 10.38 . 1 194 35 ASP HA H 4.11 . 1 195 35 ASP N N 115.31 . 1 196 36 GLU H H 7.65 . 1 197 36 GLU HB3 H 1.50 . 2 198 36 GLU N N 120.94 . 1 199 36 GLU HA H 4.89 . 1 200 36 GLU HG3 H 2.35 . 2 201 37 SER H H 7.51 . 1 202 37 SER HA H 4.63 . 1 203 37 SER N N 115.68 . 1 204 37 SER HB3 H 3.93 . 2 205 37 SER HB2 H 4.23 . 2 206 38 ALA HA H 4.29 . 1 207 38 ALA HB H 1.46 . 1 208 38 ALA H H 8.46 . 1 209 39 SER H H 8.01 . 1 210 39 SER HA H 4.22 . 1 211 39 SER N N 111.42 . 1 212 39 SER HB3 H 3.84 . 2 213 40 CYS H H 7.81 . 1 214 40 CYS HA H 4.31 . 1 215 40 CYS HB2 H 2.56 . 2 216 40 CYS HB3 H 2.16 . 2 217 40 CYS N N 119.98 . 1 218 41 ALA H H 8.17 . 1 219 41 ALA HA H 4.38 . 1 220 41 ALA HB H 1.22 . 1 221 41 ALA N N 125.48 . 1 222 42 TYR H H 7.96 . 1 223 42 TYR HB2 H 3.12 . 2 224 42 TYR HB3 H 2.65 . 2 225 42 TYR HD1 H 7.06 . 3 226 42 TYR HE1 H 6.66 . 3 227 42 TYR N N 121.27 . 1 228 42 TYR HA H 4.80 . 1 229 43 PRO HB2 H 2.27 . 2 230 43 PRO HG3 H 2.03 . 2 231 43 PRO HB3 H 1.91 . 2 232 43 PRO HD3 H 3.71 . 2 233 43 PRO HD2 H 3.87 . 2 234 43 PRO HA H 4.43 . 1 235 43 PRO HG2 H 2.56 . 2 236 44 THR H H 8.01 . 1 237 44 THR HA H 4.21 . 1 238 44 THR HG2 H 1.16 . 1 239 44 THR HB H 4.00 . 1 240 44 THR N N 114.09 . 1 241 45 CYS HB2 H 2.77 . 2 242 45 CYS HB3 H 2.43 . 2 243 45 CYS H H 8.36 . 1 244 45 CYS N N 121.65 . 1 245 45 CYS HA H 4.65 . 1 246 46 PHE HB2 H 3.18 . 2 247 46 PHE HB3 H 2.80 . 2 248 46 PHE HA H 4.82 . 1 249 46 PHE H H 8.91 . 1 250 46 PHE N N 125.83 . 1 251 46 PHE HD1 H 7.28 . 3 252 46 PHE HE1 H 7.34 . 3 253 47 PRO HD3 H 3.68 . 2 254 47 PRO HD2 H 4.01 . 2 255 47 PRO HG2 H 1.98 . 2 256 47 PRO HA H 4.41 . 1 257 47 PRO HB3 H 2.34 . 2 258 47 PRO HG3 H 1.95 . 2 259 47 PRO HB2 H 1.88 . 2 260 48 LEU HB3 H 1.50 . 2 261 48 LEU HD1 H 0.86 . 2 262 48 LEU HG H 1.55 . 1 263 48 LEU HB2 H 1.87 . 2 264 48 LEU HD2 H 0.90 . 2 265 48 LEU HA H 4.18 . 1 266 48 LEU H H 7.94 . 1 267 48 LEU N N 114.00 . 1 268 49 THR HA H 4.42 . 1 269 49 THR HB H 4.35 . 1 270 49 THR HG2 H 1.10 . 1 271 49 THR H H 7.52 . 1 272 49 THR N N 104.02 . 1 273 50 GLN H H 8.13 . 1 274 50 GLN HA H 5.26 . 1 275 50 GLN HB2 H 2.31 . 2 276 50 GLN HB3 H 1.61 . 2 277 50 GLN HG2 H 2.53 . 2 278 50 GLN HG3 H 1.98 . 2 279 50 GLN HE22 H 6.38 . 2 280 50 GLN HE21 H 7.45 . 2 281 50 GLN N N 120.62 . 1 282 50 GLN NE2 N 112.46 . 1 283 51 PHE HB2 H 2.88 . 2 284 51 PHE HB3 H 2.63 . 2 285 51 PHE H H 9.06 . 1 286 51 PHE N N 121.80 . 1 287 51 PHE HA H 4.64 . 1 288 51 PHE HE1 H 7.33 . 3 289 51 PHE HD1 H 7.10 . 3 290 51 PHE HZ H 7.25 . 1 291 52 THR H H 7.43 . 1 292 52 THR HA H 4.43 . 1 293 52 THR HG2 H 1.02 . 1 294 52 THR HB H 3.65 . 1 295 52 THR N N 123.05 . 1 296 53 CYS H H 8.82 . 1 297 53 CYS HB2 H 3.37 . 2 298 53 CYS HB3 H 2.96 . 2 299 53 CYS HA H 4.46 . 1 300 53 CYS N N 125.87 . 1 301 54 ASN HA H 4.33 . 1 302 54 ASN HB3 H 2.87 . 2 303 54 ASN HB2 H 3.08 . 2 304 54 ASN H H 9.31 . 1 305 54 ASN HD22 H 7.04 . 2 306 54 ASN N N 124.75 . 1 307 54 ASN HD21 H 7.77 . 2 308 54 ASN ND2 N 111.99 . 1 309 55 ASN H H 7.47 . 1 310 55 ASN HA H 4.41 . 1 311 55 ASN HB2 H 3.22 . 2 312 55 ASN HB3 H 2.75 . 2 313 55 ASN HD21 H 7.47 . 2 314 55 ASN N N 114.38 . 1 315 55 ASN ND2 N 105.52 . 1 316 55 ASN HD22 H 6.71 . 2 317 56 GLY H H 7.77 . 1 318 56 GLY HA2 H 4.13 . 2 319 56 GLY HA3 H 3.32 . 2 320 56 GLY N N 107.03 . 1 321 57 ARG HD2 H 3.28 . 2 322 57 ARG HG2 H 1.54 . 2 323 57 ARG HG3 H 1.59 . 2 324 57 ARG H H 7.52 . 1 325 57 ARG HA H 3.98 . 1 326 57 ARG HB3 H 1.86 . 2 327 57 ARG N N 119.65 . 1 328 57 ARG HB2 H 1.14 . 2 329 58 CYS H H 8.34 . 1 330 58 CYS HA H 5.49 . 1 331 58 CYS HB3 H 2.61 . 2 332 58 CYS N N 119.75 . 1 333 59 ILE HG13 H 1.32 . 2 334 59 ILE HG2 H 0.95 . 1 335 59 ILE HB H 2.11 . 1 336 59 ILE HD1 H 1.06 . 1 337 59 ILE HG12 H 1.53 . 2 338 59 ILE H H 8.57 . 1 339 59 ILE HA H 4.86 . 1 340 59 ILE N N 114.44 . 1 341 60 ASN HA H 4.09 . 1 342 60 ASN H H 6.85 . 1 343 60 ASN N N 120.91 . 1 344 60 ASN HB3 H 0.96 . 2 345 60 ASN HD22 H 6.93 . 2 346 60 ASN HD21 H 7.04 . 2 347 60 ASN ND2 N 112.90 . 1 348 60 ASN HB2 H 1.43 . 2 349 61 ILE HA H 3.87 . 1 350 61 ILE HB H 1.22 . 1 351 61 ILE HD1 H 0.89 . 1 352 61 ILE HG13 H 1.34 . 2 353 61 ILE H H 8.01 . 1 354 61 ILE N N 126.76 . 1 355 61 ILE HG2 H 0.81 . 1 356 62 ASN H H 8.60 . 1 357 62 ASN HA H 4.56 . 1 358 62 ASN HB3 H 2.47 . 2 359 62 ASN HB2 H 2.85 . 2 360 62 ASN N N 118.69 . 1 361 62 ASN HD22 H 6.96 . 2 362 62 ASN ND2 N 113.67 . 1 363 62 ASN HD21 H 7.60 . 2 364 63 TRP H H 8.08 . 1 365 63 TRP HA H 5.14 . 1 366 63 TRP HB3 H 3.26 . 2 367 63 TRP HB2 H 3.75 . 2 368 63 TRP HD1 H 6.75 . 1 369 63 TRP HE1 H 10.15 . 1 370 63 TRP N N 118.15 . 1 371 63 TRP NE1 N 128.47 . 1 372 63 TRP HZ2 H 7.54 . 1 373 63 TRP HH2 H 7.28 . 1 374 63 TRP HE3 H 7.40 . 1 375 63 TRP HZ3 H 7.31 . 1 376 64 ARG H H 7.59 . 1 377 64 ARG HA H 4.12 . 1 378 64 ARG HB3 H 1.99 . 2 379 64 ARG HG2 H 1.26 . 2 380 64 ARG HD3 H 2.87 . 2 381 64 ARG HB2 H 1.22 . 2 382 64 ARG N N 126.30 . 1 383 64 ARG HD2 H 2.19 . 2 384 64 ARG HG3 H 1.39 . 2 385 65 CYS H H 8.65 . 1 386 65 CYS HA H 4.98 . 1 387 65 CYS HB2 H 3.30 . 2 388 65 CYS HB3 H 3.02 . 2 389 65 CYS N N 122.63 . 1 390 66 ASP H H 9.66 . 1 391 66 ASP HB2 H 3.13 . 2 392 66 ASP HB3 H 2.94 . 2 393 66 ASP N N 121.74 . 1 394 66 ASP HA H 4.78 . 1 395 67 ASN H H 9.23 . 1 396 67 ASN HB3 H 2.94 . 2 397 67 ASN HB2 H 3.14 . 2 398 67 ASN HA H 4.08 . 1 399 67 ASN N N 113.59 . 1 400 67 ASN HD22 H 6.78 . 2 401 67 ASN ND2 N 113.04 . 1 402 67 ASN HD21 H 7.44 . 2 403 68 ASP H H 7.60 . 1 404 68 ASP HB3 H 2.45 . 2 405 68 ASP HB2 H 2.59 . 2 406 68 ASP N N 116.72 . 1 407 68 ASP HA H 4.86 . 1 408 69 ASN HD22 H 5.99 . 2 409 69 ASN HD21 H 7.70 . 2 410 69 ASN ND2 N 109.44 . 1 411 69 ASN HB3 H 2.91 . 2 412 69 ASN HB2 H 3.13 . 2 413 69 ASN H H 7.59 . 1 414 69 ASN N N 116.68 . 1 415 69 ASN HA H 4.82 . 1 416 70 ASP H H 10.27 . 1 417 70 ASP HA H 4.79 . 1 418 70 ASP N N 126.46 . 1 419 70 ASP HB3 H 2.84 . 2 420 70 ASP HB2 H 2.88 . 2 421 71 CYS H H 8.70 . 1 422 71 CYS HA H 4.47 . 1 423 71 CYS N N 116.93 . 1 424 71 CYS HB3 H 3.29 . 2 425 71 CYS HB2 H 3.34 . 2 426 72 GLY H H 8.11 . 1 427 72 GLY HA3 H 3.53 . 2 428 72 GLY N N 109.70 . 1 429 72 GLY HA2 H 4.66 . 2 430 73 ASP H H 6.90 . 1 431 73 ASP N N 117.66 . 1 432 73 ASP HA H 4.46 . 1 433 73 ASP HB3 H 2.61 . 2 434 73 ASP HB2 H 3.25 . 2 435 74 ASN H H 8.42 . 1 436 74 ASN HA H 4.46 . 1 437 74 ASN HB3 H 2.43 . 2 438 74 ASN HB2 H 3.15 . 2 439 74 ASN N N 115.68 . 1 440 74 ASN HD22 H 6.45 . 2 441 74 ASN ND2 N 107.98 . 1 442 74 ASN HD21 H 7.18 . 2 443 75 SER H H 9.22 . 1 444 75 SER N N 117.32 . 1 445 75 SER HB3 H 3.99 . 2 446 75 SER HA H 4.11 . 1 447 75 SER HB2 H 4.21 . 2 448 76 ASP H H 10.17 . 1 449 76 ASP HA H 3.96 . 1 450 76 ASP HB3 H 2.44 . 2 451 76 ASP HB2 H 3.07 . 2 452 76 ASP N N 115.64 . 1 453 77 GLU H H 7.52 . 1 454 77 GLU HA H 4.44 . 1 455 77 GLU N N 117.73 . 1 456 77 GLU HB3 H 1.49 . 2 457 77 GLU HG2 H 2.32 . 2 458 77 GLU HB2 H 1.87 . 2 459 77 GLU HG3 H 2.03 . 2 460 78 ALA H H 7.03 . 1 461 78 ALA HA H 4.42 . 1 462 78 ALA N N 124.02 . 1 463 78 ALA HB H 1.44 . 1 464 81 SER HA H 4.39 . 1 465 81 SER HB3 H 3.81 . 2 466 82 HIS H H 8.09 . 1 467 82 HIS HA H 4.45 . 1 468 82 HIS HB3 H 3.04 . 2 469 82 HIS HB2 H 3.22 . 2 470 82 HIS HD2 H 7.14 . 1 471 82 HIS HE1 H 8.37 . 1 472 82 HIS HD1 H 10.94 . 1 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_reference_1 _Saveframe_category citation _PubMed_ID 10747921 _Citation_full ; Andersen OM, Christensen LL, Christensen PA, Sorensen ES, Jacobsen C, Moestrup SK, Etzerodt M, Thogersen HC. Identification of the minimal functional unit in the low density lipoprotein receptor-related protein for binding the receptor-associated protein (RAP). A conserved acidic residue in the complement-type repeats is important for recognition of RAP. J Biol Chem. 2000 Jul 14;275(28):21017-24. ; save_ save_reference_2 _Saveframe_category citation _PubMed_ID 9207124 _Citation_full ; The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein. Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7521-5. ; save_