data_5750 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N Chemical Shift Assignments for the extracellular domain of BR3 ; _BMRB_accession_number 5750 _BMRB_flat_file_name bmr5750.str _Entry_type original _Submission_date 2003-03-20 _Accession_date 2003-03-24 _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 Gordon Nathaniel C. . 2 Pan Borlan . . 3 Hymowitz Sarah G. . 4 Yin JianPing . . 5 Kelley Robert F. . 6 Cochran Andrea G. . 7 Yan Minhong . . 8 Dixit Vishva M. . 9 Fairbrother Wayne J. . 10 Starovasnik Melissa A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 252 "13C chemical shifts" 176 "15N chemical shifts" 51 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-05-22 original author . stop_ _Original_release_date 2003-05-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; BAFF/BLyS Receptor 3 Comprises a Minimal TNF Receptor-like Module that Encodes a Highly Focused Ligand-binding Site ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22640578 _PubMed_ID 12755599 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gordon Nathaniel C. . 2 Pan Borlan . . 3 Hymowitz Sarah G. . 4 Yin JianPing . . 5 Kelley Robert F. . 6 Cochran Andrea G. . 7 Yan Minhong . . 8 Dixit Vishva M. . 9 Fairbrother Wayne J. . 10 Starovasnik Melissa A. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 42 _Journal_issue 20 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5977 _Page_last 5983 _Year 2003 _Details . loop_ _Keyword BR3 BAFF-R 'TNF receptor' 'cysteine-rich domain' stop_ save_ ################################## # Molecular system description # ################################## save_BR3_or_BAFF-R _Saveframe_category molecular_system _Mol_system_name 'BLyS Receptor 3' _Abbreviation_common 'BR3 or BAFF-R' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label BR3 $BR3 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'BAFF-binding domain' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_BR3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'BR3 or BAFF-R' _Abbreviation_common BR3 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 63 _Mol_residue_sequence ; AMARRGPRSLRGRDAPAPTP CVPAECFDLLVRHCVACGLL RTPRPKPAGASSPAPRTALQ PQE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 ALA 2 0 MET 3 1 ALA 4 2 ARG 5 3 ARG 6 4 GLY 7 5 PRO 8 6 ARG 9 7 SER 10 8 LEU 11 9 ARG 12 10 GLY 13 11 ARG 14 12 ASP 15 13 ALA 16 14 PRO 17 15 ALA 18 16 PRO 19 17 THR 20 18 PRO 21 19 CYS 22 20 VAL 23 21 PRO 24 22 ALA 25 23 GLU 26 24 CYS 27 25 PHE 28 26 ASP 29 27 LEU 30 28 LEU 31 29 VAL 32 30 ARG 33 31 HIS 34 32 CYS 35 33 VAL 36 34 ALA 37 35 CYS 38 36 GLY 39 37 LEU 40 38 LEU 41 39 ARG 42 40 THR 43 41 PRO 44 42 ARG 45 43 PRO 46 44 LYS 47 45 PRO 48 46 ALA 49 47 GLY 50 48 ALA 51 49 SER 52 50 SER 53 51 PRO 54 52 ALA 55 53 PRO 56 54 ARG 57 55 THR 58 56 ALA 59 57 LEU 60 58 GLN 61 59 PRO 62 60 GLN 63 61 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 1OSX "Solution Structure Of The Extracellular Domain Of Blys Receptor 3 (Br3)" 95.24 61 100.00 100.00 3.57e-32 PDB 1P0T "Crystal Structure Of The Baff-Baff-R Complex (Part Ii)" 95.24 63 100.00 100.00 2.62e-32 DBJ BAE16554 "BAFF-R [Homo sapiens]" 95.24 184 100.00 100.00 6.61e-32 DBJ BAJ20202 "tumor necrosis factor receptor superfamily, member 13C [synthetic construct]" 95.24 184 100.00 100.00 6.61e-32 EMBL CBF13296 "BAFF receptor [Homo sapiens]" 95.24 184 100.00 100.00 6.27e-32 EMBL CDG23825 "tumor necrosis factor receptor superfamily, member 13C [Homo sapiens]" 95.24 184 100.00 100.00 4.79e-32 GB AAI05124 "BAFF receptor [Homo sapiens]" 95.24 184 100.00 100.00 6.61e-32 GB AAI11586 "TNFRSF13C protein [synthetic construct]" 95.24 184 100.00 100.00 6.61e-32 GB AAI12031 "BAFF receptor [Homo sapiens]" 95.24 184 100.00 100.00 6.61e-32 GB AAK91826 "BAFF receptor [Homo sapiens]" 95.24 184 100.00 100.00 6.61e-32 GB ABK41893 "tumor necrosis factor receptor superfamily, member 13C [Homo sapiens]" 95.24 184 100.00 100.00 6.61e-32 REF NP_443177 "tumor necrosis factor receptor superfamily member 13C [Homo sapiens]" 95.24 184 100.00 100.00 6.61e-32 REF XP_004063616 "PREDICTED: tumor necrosis factor receptor superfamily member 13C [Gorilla gorilla gorilla]" 71.43 201 97.78 97.78 2.75e-21 SP Q96RJ3 "RecName: Full=Tumor necrosis factor receptor superfamily member 13C; AltName: Full=B-cell-activating factor receptor; AltName: " 95.24 184 100.00 100.00 6.61e-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 $BR3 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 $BR3 'recombinant technology' 'E. coli' Escherichia coli . . 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 $BR3 1.5 mM [U-15N] 'sodium phosphate' 25 mM . 'sodium chloride' 50 mM . stop_ save_ save_Sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $BR3 1.5 mM '[U-15N; U-13C]' 'sodium phosphate' 25 mM . 'sodium chloride' 50 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ####################### # Sample conditions # ####################### save_Cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 0.1 n/a temperature 293 1 K 'ionic strength' 0.125 0.02 M 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 _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 . direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $Sample_1 stop_ _Sample_conditions_label $Cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name BR3 _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 MET H H 8.67 0.02 1 2 . 2 MET HA H 4.49 0.02 1 3 . 2 MET CA C 55.38 0.20 1 4 . 2 MET N N 120.39 0.10 1 5 . 3 ALA H H 8.57 0.02 1 6 . 3 ALA HA H 4.33 0.02 1 7 . 3 ALA HB H 1.40 0.02 1 8 . 3 ALA C C 177.49 0.20 1 9 . 3 ALA CA C 52.31 0.20 1 10 . 3 ALA CB C 19.32 0.20 1 11 . 3 ALA N N 126.97 0.10 1 12 . 4 ARG H H 8.47 0.02 1 13 . 4 ARG HA H 4.33 0.02 1 14 . 4 ARG HB2 H 1.79 0.02 2 15 . 4 ARG HB3 H 1.85 0.02 2 16 . 4 ARG HG2 H 1.67 0.02 1 17 . 4 ARG HG3 H 1.67 0.02 1 18 . 4 ARG HD2 H 3.22 0.02 1 19 . 4 ARG HD3 H 3.22 0.02 1 20 . 4 ARG C C 176.23 0.20 1 21 . 4 ARG CA C 56.13 0.20 1 22 . 4 ARG CB C 30.65 0.20 1 23 . 4 ARG CG C 26.84 0.20 1 24 . 4 ARG CD C 43.06 0.20 1 25 . 4 ARG N N 121.40 0.10 1 26 . 5 ARG H H 8.51 0.02 1 27 . 5 ARG HA H 4.44 0.02 1 28 . 5 ARG HB2 H 1.90 0.02 2 29 . 5 ARG HB3 H 1.79 0.02 2 30 . 5 ARG HG2 H 1.68 0.02 1 31 . 5 ARG HG3 H 1.68 0.02 1 32 . 5 ARG HD2 H 3.25 0.02 1 33 . 5 ARG HD3 H 3.25 0.02 1 34 . 5 ARG C C 176.39 0.20 1 35 . 5 ARG CA C 55.80 0.20 1 36 . 5 ARG CB C 30.51 0.20 1 37 . 5 ARG CG C 27.20 0.20 1 38 . 5 ARG CD C 43.13 0.20 1 39 . 5 ARG N N 123.17 0.10 1 40 . 6 GLY H H 8.41 0.02 1 41 . 6 GLY HA2 H 4.19 0.02 2 42 . 6 GLY HA3 H 4.08 0.02 2 43 . 6 GLY CA C 44.24 0.20 1 44 . 6 GLY N N 110.61 0.10 1 45 . 7 PRO C C 177.36 0.20 1 46 . 8 ARG H H 8.59 0.02 1 47 . 8 ARG HA H 4.34 0.02 1 48 . 8 ARG HB2 H 1.90 0.02 2 49 . 8 ARG HB3 H 1.80 0.02 2 50 . 8 ARG HG2 H 1.68 0.02 1 51 . 8 ARG HG3 H 1.68 0.02 1 52 . 8 ARG HD2 H 3.23 0.02 1 53 . 8 ARG HD3 H 3.23 0.02 1 54 . 8 ARG C C 176.53 0.20 1 55 . 8 ARG CA C 55.97 0.20 1 56 . 8 ARG CB C 30.79 0.20 1 57 . 8 ARG CG C 27.05 0.20 1 58 . 8 ARG CD C 43.13 0.20 1 59 . 8 ARG N N 121.13 0.10 1 60 . 9 SER H H 8.34 0.02 1 61 . 9 SER HA H 4.45 0.02 1 62 . 9 SER HB2 H 3.91 0.02 2 63 . 9 SER HB3 H 3.85 0.02 2 64 . 9 SER C C 174.55 0.20 1 65 . 9 SER CA C 57.99 0.20 1 66 . 9 SER CB C 63.34 0.20 1 67 . 9 SER N N 116.83 0.10 1 68 . 10 LEU H H 8.39 0.02 1 69 . 10 LEU HA H 4.40 0.02 1 70 . 10 LEU HB2 H 1.67 0.02 2 71 . 10 LEU HB3 H 1.60 0.02 2 72 . 10 LEU HG H 0.95 0.02 1 73 . 10 LEU HD1 H 0.89 0.02 2 74 . 10 LEU HD2 H 0.91 0.02 2 75 . 10 LEU C C 177.29 0.20 1 76 . 10 LEU CA C 55.18 0.20 1 77 . 10 LEU CB C 42.06 0.20 1 78 . 10 LEU CG C 24.65 0.20 1 79 . 10 LEU CD1 C 23.40 0.20 2 80 . 10 LEU CD2 C 24.65 0.20 2 81 . 10 LEU N N 124.64 0.10 1 82 . 11 ARG H H 8.34 0.02 1 83 . 11 ARG HA H 4.36 0.02 1 84 . 11 ARG HB2 H 1.90 0.02 2 85 . 11 ARG HB3 H 1.81 0.02 2 86 . 11 ARG HG2 H 1.70 0.02 2 87 . 11 ARG HG3 H 1.66 0.02 2 88 . 11 ARG HD2 H 3.23 0.02 1 89 . 11 ARG HD3 H 3.23 0.02 1 90 . 11 ARG C C 176.78 0.20 1 91 . 11 ARG CA C 56.16 0.20 1 92 . 11 ARG CB C 30.52 0.20 1 93 . 11 ARG CG C 30.58 0.20 1 94 . 11 ARG CD C 42.97 0.20 1 95 . 11 ARG N N 121.33 0.10 1 96 . 12 GLY H H 8.48 0.02 1 97 . 12 GLY HA2 H 3.98 0.02 1 98 . 12 GLY HA3 H 3.98 0.02 1 99 . 12 GLY C C 174.22 0.20 1 100 . 12 GLY CA C 44.95 0.20 1 101 . 12 GLY N N 110.36 0.10 1 102 . 13 ARG H H 8.30 0.02 1 103 . 13 ARG HA H 4.34 0.02 1 104 . 13 ARG HB2 H 1.90 0.02 2 105 . 13 ARG HB3 H 1.80 0.02 2 106 . 13 ARG HG2 H 1.68 0.02 2 107 . 13 ARG HG3 H 1.64 0.02 2 108 . 13 ARG HD2 H 3.22 0.02 1 109 . 13 ARG HD3 H 3.22 0.02 1 110 . 13 ARG C C 176.12 0.20 1 111 . 13 ARG CA C 56.19 0.20 1 112 . 13 ARG CB C 30.77 0.20 1 113 . 13 ARG CG C 27.21 0.20 1 114 . 13 ARG CD C 42.99 0.20 1 115 . 13 ARG N N 120.69 0.10 1 116 . 14 ASP H H 8.43 0.02 1 117 . 14 ASP HA H 4.61 0.02 1 118 . 14 ASP HB2 H 2.71 0.02 2 119 . 14 ASP HB3 H 2.60 0.02 2 120 . 14 ASP C C 175.44 0.20 1 121 . 14 ASP CA C 53.78 0.20 1 122 . 14 ASP CB C 41.02 0.20 1 123 . 14 ASP N N 121.00 0.10 1 124 . 15 ALA H H 8.15 0.02 1 125 . 15 ALA HA H 4.59 0.02 1 126 . 15 ALA HB H 1.35 0.02 1 127 . 15 ALA CA C 50.19 0.20 1 128 . 15 ALA CB C 17.97 0.20 1 129 . 15 ALA N N 125.23 0.10 1 130 . 16 PRO HA H 4.42 0.02 1 131 . 16 PRO HD2 H 3.74 0.02 2 132 . 16 PRO HD3 H 3.54 0.02 2 133 . 17 ALA H H 8.40 0.02 1 134 . 17 ALA HA H 4.52 0.02 1 135 . 17 ALA HB H 1.32 0.02 1 136 . 17 ALA N N 125.66 0.10 1 137 . 18 PRO C C 176.50 0.20 1 138 . 19 THR H H 7.67 0.02 1 139 . 19 THR HA H 4.55 0.02 1 140 . 19 THR HB H 4.09 0.02 1 141 . 19 THR HG2 H 1.23 0.02 1 142 . 19 THR CA C 58.79 0.20 1 143 . 19 THR CB C 69.57 0.20 1 144 . 19 THR N N 115.97 0.10 1 145 . 20 PRO HA H 4.44 0.02 1 146 . 20 PRO HB2 H 2.32 0.02 2 147 . 20 PRO HB3 H 1.92 0.02 2 148 . 20 PRO HG2 H 2.04 0.02 1 149 . 20 PRO HG3 H 2.04 0.02 1 150 . 20 PRO HD2 H 3.69 0.02 1 151 . 20 PRO HD3 H 3.69 0.02 1 152 . 20 PRO C C 176.73 0.20 1 153 . 20 PRO CA C 62.88 0.20 1 154 . 20 PRO CB C 31.96 0.20 1 155 . 20 PRO CG C 27.14 0.20 1 156 . 20 PRO CD C 50.76 0.20 1 157 . 21 CYS H H 8.24 0.02 1 158 . 21 CYS HA H 5.18 0.02 1 159 . 21 CYS HB2 H 2.62 0.02 1 160 . 21 CYS HB3 H 3.42 0.02 1 161 . 21 CYS C C 175.84 0.20 1 162 . 21 CYS CA C 52.08 0.20 1 163 . 21 CYS CB C 40.08 0.20 1 164 . 21 CYS N N 118.33 0.10 1 165 . 22 VAL H H 8.86 0.02 1 166 . 22 VAL HA H 4.48 0.02 1 167 . 22 VAL HB H 2.53 0.02 1 168 . 22 VAL HG1 H 1.11 0.02 1 169 . 22 VAL HG2 H 0.88 0.02 1 170 . 22 VAL CA C 61.12 0.20 1 171 . 22 VAL CB C 29.11 0.20 1 172 . 22 VAL CG1 C 21.21 0.20 1 173 . 22 VAL CG2 C 17.66 0.20 1 174 . 22 VAL N N 118.37 0.10 1 175 . 23 PRO HA H 4.33 0.02 1 176 . 23 PRO HB2 H 2.97 0.02 2 177 . 23 PRO HB3 H 3.71 0.02 2 178 . 23 PRO HG2 H 2.39 0.02 2 179 . 23 PRO HG3 H 2.16 0.02 2 180 . 23 PRO HD2 H 3.90 0.02 2 181 . 23 PRO HD3 H 3.71 0.02 2 182 . 23 PRO C C 177.02 0.20 1 183 . 23 PRO CA C 65.47 0.20 1 184 . 23 PRO CB C 31.22 0.20 1 185 . 23 PRO CG C 27.34 0.20 1 186 . 23 PRO CD C 50.79 0.20 1 187 . 24 ALA H H 8.19 0.02 1 188 . 24 ALA HA H 4.21 0.02 1 189 . 24 ALA HB H 1.57 0.02 1 190 . 24 ALA C C 177.44 0.20 1 191 . 24 ALA CA C 53.53 0.20 1 192 . 24 ALA CB C 18.39 0.20 1 193 . 24 ALA N N 117.09 0.10 1 194 . 25 GLU H H 8.58 0.02 1 195 . 25 GLU HA H 5.01 0.02 1 196 . 25 GLU HB2 H 2.04 0.02 1 197 . 25 GLU HB3 H 2.04 0.02 1 198 . 25 GLU HG2 H 2.15 0.02 2 199 . 25 GLU HG3 H 1.91 0.02 2 200 . 25 GLU C C 175.24 0.20 1 201 . 25 GLU CA C 56.03 0.20 1 202 . 25 GLU CB C 32.33 0.20 1 203 . 25 GLU CG C 36.59 0.20 1 204 . 25 GLU N N 119.28 0.10 1 205 . 26 CYS H H 9.45 0.02 1 206 . 26 CYS HA H 5.03 0.02 1 207 . 26 CYS HB2 H 2.85 0.02 1 208 . 26 CYS HB3 H 3.00 0.02 1 209 . 26 CYS C C 173.01 0.20 1 210 . 26 CYS CA C 57.57 0.20 1 211 . 26 CYS CB C 42.25 0.20 1 212 . 26 CYS N N 116.73 0.10 1 213 . 27 PHE H H 9.26 0.02 1 214 . 27 PHE HA H 4.20 0.02 1 215 . 27 PHE HB2 H 3.04 0.02 1 216 . 27 PHE HB3 H 3.04 0.02 1 217 . 27 PHE HD1 H 7.09 0.02 1 218 . 27 PHE HD2 H 7.09 0.02 1 219 . 27 PHE HE1 H 7.22 0.02 1 220 . 27 PHE HE2 H 7.22 0.02 1 221 . 27 PHE C C 173.73 0.20 1 222 . 27 PHE CA C 59.80 0.20 1 223 . 27 PHE CB C 39.28 0.20 1 224 . 27 PHE N N 125.33 0.10 1 225 . 28 ASP H H 7.54 0.02 1 226 . 28 ASP HA H 4.64 0.02 1 227 . 28 ASP HB2 H 2.41 0.02 1 228 . 28 ASP HB3 H 2.71 0.02 1 229 . 28 ASP C C 176.32 0.20 1 230 . 28 ASP CA C 52.91 0.20 1 231 . 28 ASP CB C 43.17 0.20 1 232 . 28 ASP N N 129.52 0.10 1 233 . 29 LEU H H 8.62 0.02 1 234 . 29 LEU HA H 3.88 0.02 1 235 . 29 LEU HB2 H 1.79 0.02 1 236 . 29 LEU HB3 H 1.67 0.02 1 237 . 29 LEU HG H 1.88 0.02 1 238 . 29 LEU HD1 H 1.06 0.02 1 239 . 29 LEU HD2 H 1.06 0.02 1 240 . 29 LEU C C 177.72 0.20 1 241 . 29 LEU CA C 56.92 0.20 1 242 . 29 LEU CB C 42.10 0.20 1 243 . 29 LEU CG C 27.42 0.20 1 244 . 29 LEU CD1 C 24.93 0.20 1 245 . 29 LEU CD2 C 23.60 0.20 1 246 . 29 LEU N N 125.99 0.10 1 247 . 30 LEU H H 8.41 0.02 1 248 . 30 LEU HA H 4.26 0.02 1 249 . 30 LEU HB2 H 1.89 0.02 2 250 . 30 LEU HB3 H 1.69 0.02 2 251 . 30 LEU HG H 1.62 0.02 1 252 . 30 LEU HD1 H 0.94 0.02 1 253 . 30 LEU HD2 H 0.90 0.02 1 254 . 30 LEU C C 179.14 0.20 1 255 . 30 LEU CA C 57.29 0.20 1 256 . 30 LEU CB C 41.09 0.20 1 257 . 30 LEU CG C 27.39 0.20 1 258 . 30 LEU CD1 C 24.26 0.20 1 259 . 30 LEU CD2 C 23.63 0.20 1 260 . 30 LEU N N 118.99 0.10 1 261 . 31 VAL H H 7.25 0.02 1 262 . 31 VAL HA H 4.26 0.02 1 263 . 31 VAL HB H 2.09 0.02 1 264 . 31 VAL HG1 H 0.78 0.02 1 265 . 31 VAL HG2 H 0.45 0.02 1 266 . 31 VAL C C 175.31 0.20 1 267 . 31 VAL CA C 60.90 0.20 1 268 . 31 VAL CB C 31.81 0.20 1 269 . 31 VAL CG1 C 21.11 0.20 1 270 . 31 VAL CG2 C 18.17 0.20 1 271 . 31 VAL N N 109.54 0.10 1 272 . 32 ARG H H 7.95 0.02 1 273 . 32 ARG HA H 3.34 0.02 1 274 . 32 ARG HB2 H 1.54 0.02 1 275 . 32 ARG HB3 H 1.54 0.02 1 276 . 32 ARG HG2 H 2.08 0.02 1 277 . 32 ARG HG3 H 2.08 0.02 1 278 . 32 ARG HD2 H 3.26 0.02 1 279 . 32 ARG HD3 H 3.26 0.02 1 280 . 32 ARG C C 174.93 0.20 1 281 . 32 ARG CA C 56.56 0.20 1 282 . 32 ARG CB C 27.27 0.20 1 283 . 32 ARG CG C 25.78 0.20 1 284 . 32 ARG CD C 43.11 0.20 1 285 . 32 ARG N N 117.00 0.10 1 286 . 33 HIS H H 6.80 0.02 1 287 . 33 HIS HA H 4.10 0.02 1 288 . 33 HIS HB2 H 3.24 0.02 1 289 . 33 HIS HB3 H 3.42 0.02 1 290 . 33 HIS HD2 H 7.22 0.02 1 291 . 33 HIS HE1 H 8.50 0.02 1 292 . 33 HIS C C 173.15 0.20 1 293 . 33 HIS CA C 54.54 0.20 1 294 . 33 HIS CB C 30.86 0.20 1 295 . 33 HIS N N 110.43 0.10 1 296 . 34 CYS H H 9.09 0.02 1 297 . 34 CYS HA H 5.04 0.02 1 298 . 34 CYS HB2 H 3.18 0.02 1 299 . 34 CYS HB3 H 3.18 0.02 1 300 . 34 CYS C C 174.98 0.20 1 301 . 34 CYS CA C 57.43 0.20 1 302 . 34 CYS CB C 43.13 0.20 1 303 . 34 CYS N N 120.64 0.10 1 304 . 35 VAL H H 9.41 0.02 1 305 . 35 VAL HA H 4.70 0.02 1 306 . 35 VAL HB H 2.27 0.02 1 307 . 35 VAL HG1 H 0.88 0.02 1 308 . 35 VAL HG2 H 0.87 0.02 1 309 . 35 VAL C C 174.52 0.20 1 310 . 35 VAL CA C 59.24 0.20 1 311 . 35 VAL CB C 36.74 0.20 1 312 . 35 VAL CG1 C 21.54 0.20 1 313 . 35 VAL CG2 C 18.68 0.20 1 314 . 35 VAL N N 119.59 0.10 1 315 . 36 ALA H H 8.76 0.02 1 316 . 36 ALA HA H 4.40 0.02 1 317 . 36 ALA HB H 1.51 0.02 1 318 . 36 ALA C C 179.55 0.20 1 319 . 36 ALA CA C 53.49 0.20 1 320 . 36 ALA CB C 17.90 0.20 1 321 . 36 ALA N N 125.28 0.10 1 322 . 37 CYS H H 8.41 0.02 1 323 . 37 CYS HA H 4.30 0.02 1 324 . 37 CYS HB2 H 3.02 0.02 1 325 . 37 CYS HB3 H 3.24 0.02 1 326 . 37 CYS C C 176.25 0.20 1 327 . 37 CYS CA C 59.64 0.20 1 328 . 37 CYS CB C 44.10 0.20 1 329 . 37 CYS N N 100.48 0.10 1 330 . 38 GLY H H 8.86 0.02 1 331 . 38 GLY HA2 H 3.97 0.02 2 332 . 38 GLY HA3 H 3.90 0.02 2 333 . 38 GLY C C 174.67 0.20 1 334 . 38 GLY CA C 45.60 0.20 1 335 . 38 GLY N N 107.57 0.10 1 336 . 39 LEU H H 7.97 0.02 1 337 . 39 LEU HA H 4.34 0.02 1 338 . 39 LEU HB2 H 1.82 0.02 1 339 . 39 LEU HB3 H 1.66 0.02 1 340 . 39 LEU HG H 1.66 0.02 1 341 . 39 LEU HD1 H 1.00 0.02 1 342 . 39 LEU HD2 H 0.89 0.02 1 343 . 39 LEU C C 177.89 0.20 1 344 . 39 LEU CA C 55.31 0.20 1 345 . 39 LEU CB C 41.20 0.20 1 346 . 39 LEU CG C 28.28 0.20 1 347 . 39 LEU CD1 C 24.98 0.20 1 348 . 39 LEU CD2 C 22.78 0.20 1 349 . 39 LEU N N 119.94 0.10 1 350 . 40 LEU H H 7.73 0.02 1 351 . 40 LEU HA H 4.35 0.02 1 352 . 40 LEU HB2 H 1.82 0.02 1 353 . 40 LEU HB3 H 1.82 0.02 1 354 . 40 LEU HG H 1.68 0.02 1 355 . 40 LEU HD1 H 0.84 0.02 2 356 . 40 LEU HD2 H 0.89 0.02 2 357 . 40 LEU C C 177.32 0.20 1 358 . 40 LEU CA C 55.30 0.20 1 359 . 40 LEU CB C 42.04 0.20 1 360 . 40 LEU CG C 26.65 0.20 1 361 . 40 LEU CD1 C 23.25 0.20 2 362 . 40 LEU CD2 C 24.72 0.20 2 363 . 40 LEU N N 120.78 0.10 1 364 . 41 ARG H H 8.29 0.02 1 365 . 41 ARG HA H 4.42 0.02 1 366 . 41 ARG HB2 H 1.92 0.02 2 367 . 41 ARG HB3 H 1.83 0.02 2 368 . 41 ARG C C 176.12 0.20 1 369 . 41 ARG CA C 55.82 0.20 1 370 . 41 ARG CB C 30.79 0.20 1 371 . 41 ARG N N 121.38 0.10 1 372 . 42 THR H H 8.08 0.02 1 373 . 42 THR HA H 4.62 0.02 1 374 . 42 THR HG2 H 1.28 0.02 1 375 . 42 THR CA C 59.80 0.20 1 376 . 42 THR N N 117.27 0.10 1 377 . 43 PRO C C 176.61 0.20 1 378 . 44 ARG H H 8.51 0.02 1 379 . 44 ARG HA H 4.58 0.02 1 380 . 44 ARG CA C 53.79 0.20 1 381 . 44 ARG N N 122.96 0.10 1 382 . 45 PRO C C 176.61 0.20 1 383 . 46 LYS H H 8.51 0.02 1 384 . 46 LYS HA H 4.62 0.02 1 385 . 46 LYS CA C 54.23 0.20 1 386 . 46 LYS N N 123.29 0.10 1 387 . 47 PRO HA H 4.42 0.02 1 388 . 47 PRO C C 176.69 0.20 1 389 . 48 ALA H H 8.54 0.02 1 390 . 48 ALA HA H 4.33 0.02 1 391 . 48 ALA HB H 1.42 0.02 1 392 . 48 ALA C C 178.44 0.20 1 393 . 48 ALA CA C 52.59 0.20 1 394 . 48 ALA CB C 19.05 0.20 1 395 . 48 ALA N N 125.06 0.10 1 396 . 49 GLY H H 8.43 0.02 1 397 . 49 GLY HA2 H 3.98 0.02 1 398 . 49 GLY HA3 H 3.98 0.02 1 399 . 49 GLY C C 173.89 0.20 1 400 . 49 GLY N N 108.45 0.10 1 401 . 50 ALA H H 8.24 0.02 1 402 . 50 ALA HA H 4.39 0.02 1 403 . 50 ALA HB H 1.43 0.02 1 404 . 50 ALA C C 177.90 0.20 1 405 . 50 ALA CA C 51.66 0.20 1 406 . 50 ALA CB C 19.23 0.20 1 407 . 50 ALA N N 123.86 0.10 1 408 . 51 SER H H 8.40 0.02 1 409 . 51 SER HA H 4.52 0.02 1 410 . 51 SER HB2 H 3.88 0.02 1 411 . 51 SER HB3 H 3.88 0.02 1 412 . 51 SER C C 174.20 0.20 1 413 . 51 SER CA C 58.06 0.20 1 414 . 51 SER CB C 63.34 0.20 1 415 . 51 SER N N 115.40 0.10 1 416 . 52 SER H H 8.34 0.02 1 417 . 52 SER HA H 4.79 0.02 1 418 . 52 SER HB2 H 3.88 0.02 2 419 . 52 SER HB3 H 3.82 0.02 2 420 . 52 SER CA C 56.38 0.20 1 421 . 52 SER CB C 62.84 0.20 1 422 . 52 SER N N 118.94 0.10 1 423 . 53 PRO HA H 4.45 0.02 1 424 . 53 PRO HD2 H 3.83 0.02 2 425 . 53 PRO HD3 H 3.69 0.02 2 426 . 54 ALA H H 8.44 0.02 1 427 . 54 ALA HA H 4.58 0.02 1 428 . 54 ALA HB H 1.38 0.02 1 429 . 54 ALA N N 125.97 0.10 1 430 . 55 PRO C C 176.99 0.20 1 431 . 56 ARG H H 8.57 0.02 1 432 . 56 ARG C C 176.61 0.20 1 433 . 56 ARG N N 121.63 0.10 1 434 . 57 THR H H 8.18 0.02 1 435 . 57 THR HA H 4.31 0.02 1 436 . 57 THR HB H 4.34 0.02 1 437 . 57 THR HG2 H 1.23 0.02 1 438 . 57 THR C C 176.32 0.20 1 439 . 57 THR CA C 61.30 0.20 1 440 . 57 THR CB C 69.61 0.20 1 441 . 57 THR N N 115.36 0.10 1 442 . 58 ALA H H 8.39 0.02 1 443 . 58 ALA HA H 4.33 0.02 1 444 . 58 ALA HB H 1.41 0.02 1 445 . 58 ALA C C 177.45 0.20 1 446 . 58 ALA CA C 51.67 0.20 1 447 . 58 ALA CB C 19.28 0.20 1 448 . 58 ALA N N 126.24 0.10 1 449 . 59 LEU H H 8.23 0.02 1 450 . 59 LEU HA H 4.34 0.02 1 451 . 59 LEU HG H 1.65 0.02 1 452 . 59 LEU C C 177.14 0.20 1 453 . 59 LEU CA C 54.97 0.20 1 454 . 59 LEU CG C 26.82 0.20 1 455 . 59 LEU N N 121.31 0.10 1 456 . 60 GLN H H 8.33 0.02 1 457 . 60 GLN HA H 4.65 0.02 1 458 . 60 GLN HB2 H 2.12 0.02 2 459 . 60 GLN HB3 H 1.97 0.02 2 460 . 60 GLN HG2 H 2.40 0.02 1 461 . 60 GLN HG3 H 2.40 0.02 1 462 . 60 GLN CA C 53.38 0.20 1 463 . 60 GLN CB C 28.78 0.20 1 464 . 60 GLN CG C 33.12 0.20 1 465 . 60 GLN N N 122.30 0.10 1 466 . 61 PRO C C 176.71 0.20 1 467 . 62 GLN H H 8.59 0.02 1 468 . 62 GLN C C 175.05 0.20 1 469 . 62 GLN N N 121.34 0.10 1 470 . 63 GLU H H 8.11 0.02 1 471 . 63 GLU HA H 4.15 0.02 1 472 . 63 GLU HB2 H 2.07 0.02 2 473 . 63 GLU HB3 H 1.91 0.02 2 474 . 63 GLU HG2 H 2.21 0.02 1 475 . 63 GLU HG3 H 2.21 0.02 1 476 . 63 GLU CA C 57.67 0.20 1 477 . 63 GLU CB C 30.98 0.20 1 478 . 63 GLU CG C 36.37 0.20 1 479 . 63 GLU N N 127.61 0.10 1 stop_ save_