data_5900 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of 16th module of Immune Adherence Receptor, Cr1 (Cd35) ; _BMRB_accession_number 5900 _BMRB_flat_file_name bmr5900.str _Entry_type original _Submission_date 2003-08-07 _Accession_date 2003-08-07 _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 O'Leary J. M. . 2 Bromek K. . . 3 Black G. M. . 4 Uhrinova S. . . 5 Schmitz C. . . 6 Krych M. . . 7 Atkinson J. P. . 8 Uhrin D. . . 9 Barlow P. N. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 3 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 337 "15N chemical shifts" 65 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-07-23 original BMRB . stop_ _Original_release_date 2003-08-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone dynamics of complement control protein (CCP) modules reveals mobility in binding surfaces. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15096630 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 O'Leary J. M. . 2 Bromek K. . . 3 Black G. M. . 4 Uhrinova S. . . 5 Schmitz C. . . 6 Wang X. . . 7 Krych M. . . 8 Atkinson J. P. . 9 Uhrin D. . . 10 Barlow P. N. . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume 13 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1238 _Page_last 1250 _Year 2004 _Details . loop_ _Keyword CCP Complement Module SCR Structure Sushi stop_ save_ ################################## # Molecular system description # ################################## save_system_Cr1_module _Saveframe_category molecular_system _Mol_system_name 'complement receptor type 1' _Abbreviation_common 'complement receptor type 1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Complement receptor type 1' $Cr1_module stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Cr1_module _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'complement receptor type 1' _Abbreviation_common 'complement receptor type 1' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 68 _Mol_residue_sequence ; EAEAKSCKTPPDPVNGMVHV ITDIQVGSRITYSCTTGHRL IGHSSAECILSGNTAHWSTK PPICQRIP ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 957 GLU 2 958 ALA 3 959 GLU 4 960 ALA 5 961 LYS 6 962 SER 7 963 CYS 8 964 LYS 9 965 THR 10 966 PRO 11 967 PRO 12 968 ASP 13 969 PRO 14 970 VAL 15 971 ASN 16 972 GLY 17 973 MET 18 974 VAL 19 975 HIS 20 976 VAL 21 977 ILE 22 978 THR 23 979 ASP 24 980 ILE 25 981 GLN 26 982 VAL 27 983 GLY 28 984 SER 29 985 ARG 30 986 ILE 31 987 THR 32 988 TYR 33 989 SER 34 990 CYS 35 991 THR 36 992 THR 37 993 GLY 38 994 HIS 39 995 ARG 40 996 LEU 41 997 ILE 42 998 GLY 43 999 HIS 44 1000 SER 45 1001 SER 46 1002 ALA 47 1003 GLU 48 1004 CYS 49 1005 ILE 50 1006 LEU 51 1007 SER 52 1008 GLY 53 1009 ASN 54 1010 THR 55 1011 ALA 56 1012 HIS 57 1013 TRP 58 1014 SER 59 1015 THR 60 1016 LYS 61 1017 PRO 62 1018 PRO 63 1019 ILE 64 1020 CYS 65 1021 GLN 66 1022 ARG 67 1023 ILE 68 1024 PRO stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 PDB 1GKG 'Structure Determination And Rational Mutagenesis Reveal Binding Surface Of Immune Adherence Receptor, Cr1 (Cd35)' 100.00 136 100.00 100.00 2.47e-32 PDB 1PPQ 'Nmr Structure Of 16th Module Of Immune Adherence Receptor, Cr1 (Cd35)' 100.00 68 100.00 100.00 2.43e-32 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Cr1_module 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 $Cr1_module 'recombinant technology' . . . . . 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 $Cr1_module 1 mM [U-15N] 'phosphate buffer' 25 mM . D2O 10 % . H2O 90 % . stop_ save_ ############################ # Computer software used # ############################ save_VNMR _Saveframe_category software _Name VNMR _Version . loop_ _Task collection stop_ _Details . save_ save_AZARA _Saveframe_category software _Name AZARA _Version 2.6 loop_ _Task processing stop_ _Details 'Boucher, W.' save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version 3.3 loop_ _Task 'data analysis' stop_ _Details 'Kraulis, P.' save_ save_CNS _Saveframe_category software _Name CNS _Version 1.0 loop_ _Task refinement 'structure solution' stop_ _Details Brunger save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC' _Sample_label . save_ save_2D_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_2D_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_2D_RSCUBACOSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D RSCUBACOSY' _Sample_label . save_ save_3D_15N_HSQC-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N HSQC-TOCSY' _Sample_label . save_ save_3D_15N_HSQC-NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N HSQC-NOESY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 25 . mM pH 6.0 . n/a pressure 1 . atm temperature 310 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis . H 1 . ppm . . . . . . . N 15 . ppm . . . . . . 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '15N HSQC' '2D NOESY' '2D TOCSY' '2D RSCUBACOSY' '3D 15N HSQC-TOCSY' '3D 15N HSQC-NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Complement receptor type 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 4 ALA N N 111.1 0.3 1 2 . 4 ALA H H 8.29 0.03 1 3 . 4 ALA HA H 4.30 0.03 1 4 . 4 ALA HB H 1.30 0.03 1 5 . 5 LYS N N 121.3 0.3 1 6 . 5 LYS H H 8.27 0.03 1 7 . 5 LYS HA H 4.29 0.03 1 8 . 5 LYS HB2 H 1.62 0.03 1 9 . 5 LYS HG2 H 1.37 0.03 1 10 . 5 LYS HD2 H 1.66 0.03 1 11 . 5 LYS HE2 H 2.92 0.03 1 12 . 6 SER N N 114.4 0.3 1 13 . 6 SER H H 7.99 0.03 1 14 . 6 SER HA H 4.63 0.03 1 15 . 6 SER HB2 H 3.69 0.03 1 16 . 6 SER HB3 H 3.57 0.03 1 17 . 7 CYS N N 120.9 0.3 1 18 . 7 CYS H H 8.08 0.03 1 19 . 7 CYS HA H 4.07 0.03 1 20 . 7 CYS HB2 H 2.16 0.03 1 21 . 7 CYS HB3 H 2.07 0.03 1 22 . 8 LYS N N 119.7 0.3 1 23 . 8 LYS H H 8.42 0.03 1 24 . 8 LYS HA H 4.31 0.03 1 25 . 8 LYS HB2 H 1.88 0.03 1 26 . 8 LYS HB3 H 1.80 0.03 1 27 . 8 LYS HG2 H 1.53 0.03 1 28 . 8 LYS HD2 H 1.72 0.03 1 29 . 8 LYS HE2 H 3.04 0.03 1 30 . 9 THR N N 121.3 0.3 1 31 . 9 THR H H 8.41 0.03 1 32 . 9 THR HA H 4.11 0.03 1 33 . 9 THR HB H 3.94 0.03 1 34 . 9 THR HG2 H 1.16 0.03 1 35 . 10 PRO HA H 4.68 0.03 1 36 . 10 PRO HB2 H 1.66 0.03 1 37 . 10 PRO HB3 H 1.42 0.03 1 38 . 10 PRO HG2 H 1.77 0.03 1 39 . 10 PRO HG3 H 1.36 0.03 1 40 . 10 PRO HD2 H 3.56 0.03 1 41 . 11 PRO HA H 4.46 0.03 1 42 . 11 PRO HB2 H 2.13 0.03 1 43 . 11 PRO HB3 H 1.76 0.03 1 44 . 11 PRO HG2 H 1.96 0.03 1 45 . 11 PRO HG3 H 1.89 0.03 1 46 . 11 PRO HD2 H 3.75 0.03 1 47 . 11 PRO HD3 H 3.60 0.03 1 48 . 12 ASP N N 119.4 0.3 1 49 . 12 ASP H H 8.01 0.03 1 50 . 12 ASP HA H 4.63 0.03 1 51 . 12 ASP HB2 H 2.72 0.03 1 52 . 12 ASP HB3 H 2.29 0.03 1 53 . 13 PRO HA H 4.34 0.03 1 54 . 13 PRO HB2 H 2.16 0.03 1 55 . 13 PRO HB3 H 1.34 0.03 1 56 . 13 PRO HG2 H 1.64 0.03 1 57 . 13 PRO HG3 H 1.59 0.03 1 58 . 13 PRO HD2 H 3.91 0.03 1 59 . 13 PRO HD3 H 3.27 0.03 1 60 . 14 VAL N N 110.2 0.3 1 61 . 14 VAL H H 8.31 0.03 1 62 . 14 VAL HA H 3.64 0.03 1 63 . 14 VAL HB H 1.82 0.03 1 64 . 14 VAL HG1 H 1.00 0.03 1 65 . 14 VAL HG2 H 0.91 0.03 1 66 . 15 ASN N N 120.1 0.3 1 67 . 15 ASN H H 8.97 0.03 1 68 . 15 ASN HA H 4.05 0.03 1 69 . 15 ASN HB2 H 2.73 0.03 1 70 . 15 ASN HB3 H 1.55 0.03 1 71 . 15 ASN ND2 N 117.3 0.3 1 72 . 15 ASN HD21 H 7.46 0.03 1 73 . 15 ASN HD22 H 6.93 0.03 1 74 . 16 GLY N N 121.8 0.3 1 75 . 16 GLY H H 7.88 0.03 1 76 . 16 GLY HA2 H 4.45 0.03 1 77 . 16 GLY HA3 H 4.23 0.03 1 78 . 17 MET N N 116.5 0.3 1 79 . 17 MET H H 8.69 0.03 1 80 . 17 MET HA H 4.81 0.03 1 81 . 17 MET HB2 H 1.72 0.03 1 82 . 17 MET HB3 H 1.65 0.03 1 83 . 17 MET HG2 H 2.20 0.03 1 84 . 17 MET HG3 H 2.11 0.03 1 85 . 17 MET HE H 3.28 0.03 1 86 . 18 VAL N N 122.5 0.3 1 87 . 18 VAL H H 8.50 0.03 1 88 . 18 VAL HA H 4.46 0.03 1 89 . 18 VAL HB H 1.73 0.03 1 90 . 18 VAL HG1 H 0.58 0.03 1 91 . 18 VAL HG2 H 0.23 0.03 1 92 . 19 HIS N N 111.1 0.3 1 93 . 19 HIS H H 8.86 0.03 1 94 . 19 HIS HA H 4.61 0.03 1 95 . 19 HIS HB2 H 3.15 0.03 1 96 . 19 HIS HB3 H 2.77 0.03 1 97 . 19 HIS HD2 H 6.64 0.03 1 98 . 19 HIS HE1 H 7.51 0.03 1 99 . 20 VAL N N 111.3 0.3 1 100 . 20 VAL H H 8.46 0.03 1 101 . 20 VAL HA H 3.98 0.03 1 102 . 20 VAL HB H 1.92 0.03 1 103 . 20 VAL HG2 H 0.73 0.03 1 104 . 21 ILE N N 114.1 0.3 1 105 . 21 ILE H H 7.66 0.03 1 106 . 21 ILE HA H 3.89 0.03 1 107 . 21 ILE HB H 1.96 0.03 1 108 . 21 ILE HG12 H 1.50 0.03 1 109 . 21 ILE HG13 H 1.17 0.03 1 110 . 21 ILE HG2 H 0.95 0.03 1 111 . 21 ILE HD1 H 0.74 0.03 1 112 . 22 THR N N 113.1 0.3 1 113 . 22 THR H H 9.30 0.03 1 114 . 22 THR HA H 4.41 0.03 1 115 . 22 THR HB H 4.22 0.03 1 116 . 22 THR HG2 H 1.17 0.03 1 117 . 23 ASP N N 123.4 0.3 1 118 . 23 ASP H H 8.63 0.03 1 119 . 23 ASP HA H 4.59 0.03 1 120 . 23 ASP HB2 H 3.04 0.03 1 121 . 23 ASP HB3 H 2.71 0.03 1 122 . 24 ILE N N 110.7 0.3 1 123 . 24 ILE H H 7.63 0.03 1 124 . 24 ILE HA H 4.89 0.03 1 125 . 24 ILE HB H 2.34 0.03 1 126 . 24 ILE HG12 H 1.38 0.03 1 127 . 24 ILE HG13 H 1.09 0.03 1 128 . 24 ILE HG2 H 0.97 0.03 1 129 . 24 ILE HD1 H 0.90 0.03 1 130 . 25 GLN N N 118.7 0.3 1 131 . 25 GLN H H 7.88 0.03 1 132 . 25 GLN HA H 4.40 0.03 1 133 . 25 GLN HB2 H 2.05 0.03 1 134 . 25 GLN HB3 H 1.95 0.03 1 135 . 25 GLN HG2 H 2.27 0.03 1 136 . 25 GLN HG3 H 2.18 0.03 1 137 . 25 GLN NE2 N 112.2 0.3 1 138 . 25 GLN HE21 H 7.50 0.03 1 139 . 25 GLN HE22 H 6.63 0.03 1 140 . 26 VAL N N 120.0 0.3 1 141 . 26 VAL H H 7.74 0.03 1 142 . 26 VAL HA H 3.10 0.03 1 143 . 26 VAL HB H 1.77 0.03 1 144 . 26 VAL HG1 H 0.80 0.03 1 145 . 26 VAL HG2 H 0.69 0.03 1 146 . 27 GLY N N 117.7 0.3 1 147 . 27 GLY H H 9.19 0.03 1 148 . 27 GLY HA2 H 4.43 0.03 1 149 . 27 GLY HA3 H 3.80 0.03 1 150 . 28 SER N N 119.1 0.3 1 151 . 28 SER H H 8.29 0.03 1 152 . 28 SER HA H 4.59 0.03 1 153 . 28 SER HB2 H 4.08 0.03 1 154 . 29 ARG N N 120.9 0.3 1 155 . 29 ARG H H 8.54 0.03 1 156 . 29 ARG HA H 5.68 0.03 1 157 . 29 ARG HB2 H 1.83 0.03 1 158 . 29 ARG HB3 H 1.77 0.03 1 159 . 29 ARG HG2 H 1.69 0.03 1 160 . 29 ARG HG3 H 1.53 0.03 1 161 . 29 ARG HD2 H 3.15 0.03 1 162 . 30 ILE N N 117.2 0.3 1 163 . 30 ILE H H 8.81 0.03 1 164 . 30 ILE HA H 4.94 0.03 1 165 . 30 ILE HB H 1.30 0.03 1 166 . 30 ILE HG12 H 0.57 0.03 1 167 . 30 ILE HG13 H 0.43 0.03 1 168 . 30 ILE HG2 H 0.61 0.03 1 169 . 30 ILE HD1 H -0.59 0.03 1 170 . 31 THR N N 111.0 0.3 1 171 . 31 THR H H 8.00 0.03 1 172 . 31 THR HA H 5.17 0.03 1 173 . 31 THR HB H 4.27 0.03 1 174 . 31 THR HG2 H 1.10 0.03 1 175 . 32 TYR N N 118.7 0.3 1 176 . 32 TYR H H 8.47 0.03 1 177 . 32 TYR HA H 5.40 0.03 1 178 . 32 TYR HB2 H 2.62 0.03 1 179 . 32 TYR HB3 H 2.38 0.03 1 180 . 32 TYR HD1 H 6.61 0.03 1 181 . 32 TYR HE1 H 6.43 0.03 1 182 . 33 SER N N 113.6 0.3 1 183 . 33 SER H H 8.85 0.03 1 184 . 33 SER HA H 4.64 0.03 1 185 . 33 SER HB2 H 3.96 0.03 1 186 . 33 SER HB3 H 3.84 0.03 1 187 . 33 SER HG H 6.63 0.03 1 188 . 34 CYS N N 116.5 0.3 1 189 . 34 CYS H H 8.68 0.03 1 190 . 34 CYS HA H 5.41 0.03 1 191 . 34 CYS HB2 H 2.90 0.03 1 192 . 34 CYS HB3 H 2.48 0.03 1 193 . 35 THR N N 116.5 0.3 1 194 . 35 THR H H 8.48 0.03 1 195 . 35 THR HA H 4.22 0.03 1 196 . 35 THR HB H 4.07 0.03 1 197 . 35 THR HG2 H 1.10 0.03 1 198 . 35 THR HG1 H 6.61 0.03 1 199 . 36 THR N N 117.4 0.3 1 200 . 36 THR H H 8.11 0.03 1 201 . 36 THR HB H 4.06 0.03 1 202 . 36 THR HG2 H 1.25 0.03 1 203 . 36 THR HG1 H 6.64 0.03 1 204 . 37 GLY HA2 H 4.11 0.03 1 205 . 37 GLY HA3 H 3.64 0.03 1 206 . 38 HIS N N 117.4 0.3 1 207 . 38 HIS H H 7.93 0.03 1 208 . 38 HIS HA H 5.11 0.03 1 209 . 38 HIS HB2 H 3.14 0.03 1 210 . 38 HIS HB3 H 2.50 0.03 1 211 . 38 HIS HD2 H 6.51 0.03 1 212 . 39 ARG N N 122.5 0.3 1 213 . 39 ARG H H 9.42 0.03 1 214 . 39 ARG HA H 4.62 0.03 1 215 . 39 ARG HB2 H 1.72 0.03 1 216 . 39 ARG HB3 H 1.67 0.03 1 217 . 39 ARG HE H 7.81 0.03 1 218 . 39 ARG HG2 H 1.53 0.03 1 219 . 39 ARG HD2 H 3.11 0.03 1 220 . 40 LEU N N 112.9 0.3 1 221 . 40 LEU H H 8.33 0.03 1 222 . 40 LEU HA H 4.61 0.03 1 223 . 40 LEU HB2 H 1.61 0.03 1 224 . 40 LEU HB3 H 1.48 0.03 1 225 . 40 LEU HG H 1.16 0.03 1 226 . 40 LEU HD1 H 0.67 0.03 1 227 . 40 LEU HD2 H 0.42 0.03 1 228 . 41 ILE N N 115.1 0.3 1 229 . 41 ILE H H 9.36 0.03 1 230 . 41 ILE HA H 4.25 0.03 1 231 . 41 ILE HB H 1.87 0.03 1 232 . 41 ILE HG12 H 1.32 0.03 1 233 . 41 ILE HG13 H 1.15 0.03 1 234 . 41 ILE HG2 H 0.77 0.03 1 235 . 41 ILE HD1 H 0.67 0.03 1 236 . 42 GLY N N 117.2 0.3 1 237 . 42 GLY H H 8.39 0.03 1 238 . 42 GLY HA2 H 4.46 0.03 1 239 . 42 GLY HA3 H 3.49 0.03 1 240 . 43 HIS N N 120.9 0.3 1 241 . 43 HIS H H 8.80 0.03 1 242 . 43 HIS HB2 H 3.43 0.03 1 243 . 43 HIS HB3 H 3.14 0.03 1 244 . 43 HIS HD2 H 7.39 0.03 1 245 . 43 HIS HE1 H 8.29 0.03 1 246 . 44 SER N N 116.8 0.3 1 247 . 44 SER H H 9.00 0.03 1 248 . 44 SER HA H 4.30 0.03 1 249 . 44 SER HB2 H 3.90 0.03 1 250 . 45 SER N N 115.2 0.3 1 251 . 45 SER H H 7.75 0.03 1 252 . 45 SER HA H 5.30 0.03 1 253 . 45 SER HB2 H 3.92 0.03 1 254 . 45 SER HB3 H 3.87 0.03 1 255 . 46 ALA N N 121.6 0.3 1 256 . 46 ALA H H 8.33 0.03 1 257 . 46 ALA HA H 4.65 0.03 1 258 . 46 ALA HB H 1.56 0.03 1 259 . 47 GLU N N 119.8 0.3 1 260 . 47 GLU H H 8.87 0.03 1 261 . 47 GLU HA H 5.54 0.03 1 262 . 47 GLU HB2 H 1.86 0.03 1 263 . 47 GLU HG2 H 2.07 0.03 1 264 . 48 CYS N N 111.2 0.3 1 265 . 48 CYS H H 8.66 0.03 1 266 . 48 CYS HA H 4.04 0.03 1 267 . 48 CYS HB2 H 2.72 0.03 1 268 . 48 CYS HB3 H 1.67 0.03 1 269 . 49 ILE N N 114.1 0.3 1 270 . 49 ILE H H 8.86 0.03 1 271 . 49 ILE HA H 4.54 0.03 1 272 . 49 ILE HB H 1.66 0.03 1 273 . 49 ILE HG12 H 0.99 0.03 1 274 . 49 ILE HG13 H 0.85 0.03 1 275 . 49 ILE HG2 H 0.77 0.03 1 276 . 49 ILE HD1 H 0.67 0.03 1 277 . 50 LEU N N 122.5 0.3 1 278 . 50 LEU H H 8.25 0.03 1 279 . 50 LEU HA H 4.61 0.03 1 280 . 50 LEU HG H 1.31 0.03 1 281 . 50 LEU HB2 H 1.58 0.03 1 282 . 50 LEU HD1 H 0.68 0.03 1 283 . 51 SER N N 121.4 0.3 1 284 . 51 SER H H 8.51 0.03 1 285 . 51 SER HA H 4.60 0.03 1 286 . 51 SER HB2 H 3.73 0.03 1 287 . 51 SER HB3 H 3.63 0.03 1 288 . 51 SER HG H 7.00 0.03 1 289 . 52 GLY HA2 H 3.95 0.03 1 290 . 52 GLY HA3 H 3.61 0.03 1 291 . 53 ASN HA H 4.68 0.03 1 292 . 53 ASN HB2 H 2.89 0.03 1 293 . 53 ASN HB3 H 2.75 0.03 1 294 . 53 ASN ND2 N 113.0 0.3 1 295 . 53 ASN HD21 H 7.49 0.03 1 296 . 53 ASN HD22 H 6.82 0.03 1 297 . 54 THR N N 114.9 0.3 1 298 . 54 THR H H 7.80 0.03 1 299 . 54 THR HA H 4.40 0.03 1 300 . 54 THR HB H 4.06 0.03 1 301 . 54 THR HG2 H 1.09 0.03 1 302 . 55 ALA N N 114.5 0.3 1 303 . 55 ALA H H 8.41 0.03 1 304 . 55 ALA HA H 5.10 0.03 1 305 . 55 ALA HB H 0.80 0.03 1 306 . 56 HIS N N 120.9 0.3 1 307 . 56 HIS H H 9.08 0.03 1 308 . 56 HIS HA H 4.68 0.03 1 309 . 56 HIS HB2 H 3.16 0.03 1 310 . 56 HIS HB3 H 3.07 0.03 1 311 . 56 HIS HD2 H 7.00 0.03 1 312 . 56 HIS HE1 H 8.33 0.03 1 313 . 57 TRP N N 122.6 0.3 1 314 . 57 TRP H H 8.45 0.03 1 315 . 57 TRP HA H 4.98 0.03 1 316 . 57 TRP HB2 H 3.32 0.03 1 317 . 57 TRP HB3 H 3.16 0.03 1 318 . 57 TRP HD1 H 7.41 0.03 1 319 . 57 TRP NE1 N 128.7 0.3 1 320 . 57 TRP HE1 H 10.38 0.03 1 321 . 57 TRP HE3 H 7.12 0.03 1 322 . 57 TRP HZ2 H 7.17 0.03 1 323 . 57 TRP HZ3 H 6.91 0.03 1 324 . 57 TRP HH2 H 6.89 0.03 1 325 . 58 SER N N 118.4 0.3 1 326 . 58 SER H H 9.68 0.03 1 327 . 58 SER HA H 3.93 0.03 1 328 . 58 SER HB2 H 4.19 0.03 1 329 . 58 SER HB3 H 4.14 0.03 1 330 . 59 THR N N 112.0 0.3 1 331 . 59 THR H H 7.22 0.03 1 332 . 59 THR HA H 4.65 0.03 1 333 . 59 THR HB H 4.19 0.03 1 334 . 59 THR HG2 H 0.91 0.03 1 335 . 60 LYS N N 122.8 0.3 1 336 . 60 LYS H H 8.31 0.03 1 337 . 60 LYS HA H 4.53 0.03 1 338 . 60 LYS HB2 H 1.82 0.03 1 339 . 60 LYS HG2 H 1.55 0.03 1 340 . 60 LYS HD2 H 1.72 0.03 1 341 . 61 PRO HG2 H 1.97 0.03 1 342 . 61 PRO HG3 H 1.82 0.03 1 343 . 61 PRO HD2 H 3.81 0.03 1 344 . 61 PRO HD3 H 3.52 0.03 1 345 . 62 PRO HA H 4.59 0.03 1 346 . 62 PRO HB2 H 1.88 0.03 1 347 . 62 PRO HB3 H 1.50 0.03 1 348 . 63 ILE N N 112.8 0.3 1 349 . 63 ILE H H 7.86 0.03 1 350 . 63 ILE HA H 4.36 0.03 1 351 . 63 ILE HB H 1.74 0.03 1 352 . 63 ILE HG12 H 1.36 0.03 1 353 . 63 ILE HG13 H 1.12 0.03 1 354 . 63 ILE HG2 H 0.83 0.03 1 355 . 64 CYS N N 122.9 0.3 1 356 . 64 CYS H H 8.86 0.03 1 357 . 64 CYS HA H 5.32 0.03 1 358 . 64 CYS HB2 H 3.12 0.03 1 359 . 64 CYS HB3 H 2.33 0.03 1 360 . 65 GLN N N 110.9 0.3 1 361 . 65 GLN H H 9.13 0.03 1 362 . 65 GLN HA H 4.64 0.03 1 363 . 65 GLN HB2 H 2.00 0.03 1 364 . 65 GLN HB3 H 1.84 0.03 1 365 . 65 GLN NE2 N 111.9 0.3 1 366 . 65 GLN HE21 H 7.43 0.03 1 367 . 65 GLN HE22 H 6.77 0.03 1 368 . 65 GLN HG2 H 2.30 0.03 1 369 . 66 ARG N N 114.8 0.3 1 370 . 66 ARG H H 9.12 0.03 1 371 . 66 ARG HA H 3.72 0.03 1 372 . 66 ARG HG2 H 1.35 0.03 1 373 . 66 ARG HG3 H 1.23 0.03 1 374 . 66 ARG HB2 H 1.62 0.03 1 375 . 66 ARG HD2 H 2.99 0.03 1 376 . 67 ILE N N 113.8 0.3 1 377 . 67 ILE H H 7.90 0.03 1 378 . 67 ILE HA H 4.17 0.03 1 379 . 67 ILE HB H 1.58 0.03 1 380 . 67 ILE HG12 H 1.37 0.03 1 381 . 67 ILE HG13 H 0.83 0.03 1 382 . 67 ILE HG2 H 0.87 0.03 1 383 . 67 ILE HD1 H 0.68 0.03 1 384 . 68 PRO HG2 H 1.96 0.03 1 385 . 68 PRO HG3 H 1.83 0.03 1 386 . 68 PRO HD2 H 3.83 0.03 1 387 . 68 PRO HD3 H 3.58 0.03 1 stop_ save_ save_chemical_shift_set_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '15N HSQC' '2D NOESY' '2D TOCSY' '2D RSCUBACOSY' '3D 15N HSQC-TOCSY' '3D 15N HSQC-NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Complement receptor type 1' _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 . 17 MET N N 115.7 0.3 1 2 . 17 MET H H 8.75 0.03 1 3 . 17 MET HA H 4.91 0.03 1 4 . 18 VAL N N 123.7 0.3 1 5 . 18 VAL H H 8.75 0.03 1 6 . 18 VAL HA H 4.48 0.03 1 7 . 18 VAL HB H 1.75 0.03 1 8 . 18 VAL HG1 H 0.58 0.03 1 9 . 18 VAL HG2 H 0.21 0.03 1 10 . 66 ARG N N 115.0 0.3 1 11 . 66 ARG H H 9.01 0.03 1 12 . 66 ARG HA H 3.86 0.03 1 13 . 66 ARG HB2 H 1.62 0.03 1 stop_ save_ save_chemical_shift_set_3 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '15N HSQC' '2D NOESY' '2D TOCSY' '2D RSCUBACOSY' '3D 15N HSQC-TOCSY' '3D 15N HSQC-NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Complement receptor type 1' _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 . 17 MET N N 116.1 0.03 1 2 . 17 MET H H 8.80 0.3 1 stop_ save_