data_6384 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of TACI_D2 ; _BMRB_accession_number 6384 _BMRB_flat_file_name bmr6384.str _Entry_type original _Submission_date 2004-11-10 _Accession_date 2004-11-10 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hymowitz S. G. . 2 Patel D. R. . 3 Wallweber H. J.A. . 4 Runyon S. T. . 5 Yan M. . . 6 Yin J. . . 7 Shriver S. K. . 8 Gordon N. C. . 9 Pan B. . . 10 Skelton N. J. . 11 Kelley R. F. . 12 Starovasnik M. A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 242 "13C chemical shifts" 150 "15N chemical shifts" 45 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-01-14 original BMRB . stop_ _Original_release_date 2004-11-10 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structures of APRIL-receptor complexes: like BCMA, TACI employs only a single cysteine-rich domain for high-affinity ligand binding ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15542592 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hymowitz S. G. . 2 Patel D. R. . 3 Wallweber H. J.A. . 4 Runyon S. T. . 5 Yan M. . . 6 Yin J. . . 7 Shriver S. K. . 8 Gordon N. C. . 9 Pan B. . . 10 Skelton N. J. . 11 Kelley R. F. . 12 Starovasnik M. A. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 280 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7218 _Page_last 7227 _Year 2005 _Details . loop_ _Keyword 'TNF Receptor' 'cysteine-rich domain' cytokine receptor stop_ save_ ################################## # Molecular system description # ################################## save_system_TACI_D2 _Saveframe_category molecular_system _Mol_system_name 'Tumor necrosis factor receptor superfamily member 13B' _Abbreviation_common TACI_D2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label TACI_D2 $TACI_D2 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_TACI_D2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TACI_D2 _Abbreviation_common TACI_D2 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 46 _Mol_residue_sequence ; GSPWSLSCRKEQGKFYDHLL RDCISCASICGQHPKQCAYF CENKLR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 64 GLY 2 65 SER 3 66 PRO 4 67 TRP 5 68 SER 6 69 LEU 7 70 SER 8 71 CYS 9 72 ARG 10 73 LYS 11 74 GLU 12 75 GLN 13 76 GLY 14 77 LYS 15 78 PHE 16 79 TYR 17 80 ASP 18 81 HIS 19 82 LEU 20 83 LEU 21 84 ARG 22 85 ASP 23 86 CYS 24 87 ILE 25 88 SER 26 89 CYS 27 90 ALA 28 91 SER 29 92 ILE 30 93 CYS 31 94 GLY 32 95 GLN 33 96 HIS 34 97 PRO 35 98 LYS 36 99 GLN 37 100 CYS 38 101 ALA 39 102 TYR 40 103 PHE 41 104 CYS 42 105 GLU 43 106 ASN 44 107 LYS 45 108 LEU 46 109 ARG 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 1XU1 'The Crystal Structure Of April Bound To Taci' 91.30 42 100.00 100.00 2.38e-16 PDB 1XUT 'Solution Structure Of Taci-Crd2' 97.83 46 100.00 100.00 1.18e-18 DBJ BAD97173 'tumor necrosis factor receptor 13B variant [Homo sapiens]' 91.30 293 100.00 100.00 5.52e-17 DBJ BAE16555 'TACI [Homo sapiens]' 91.30 293 100.00 100.00 5.38e-17 DBJ BAG36107 'unnamed protein product [Homo sapiens]' 91.30 293 100.00 100.00 5.66e-17 DBJ BAG64372 'unnamed protein product [Homo sapiens]' 93.48 248 100.00 100.00 1.39e-18 GenBank AAC51790 'transmembrane activator and CAML interactor [Homo sapiens]' 91.30 293 100.00 100.00 5.38e-17 GenBank AAI09393 'TNFRSF13B protein [Homo sapiens]' 93.48 247 100.00 100.00 2.34e-18 GenBank AAP57629 'transmembrane activator and CAML interactor [Homo sapiens]' 93.48 247 100.00 100.00 2.34e-18 GenBank ABK41894 'tumor necrosis factor receptor superfamily, member 13B [Homo sapiens]' 91.30 293 100.00 100.00 5.38e-17 GenBank EAW55728 'tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a [Homo sapiens]' 91.30 293 100.00 100.00 5.38e-17 REF NP_036584 'tumor necrosis factor receptor 13B [Homo sapiens]' 91.30 293 100.00 100.00 5.38e-17 REF XP_001161260 'PREDICTED: similar to transmembrane activator and CAML interactor isoform 1 [Pan troglodytes]' 91.30 156 100.00 100.00 1.09e-16 REF XP_001161317 'PREDICTED: similar to transmembrane activator and CAML interactor isoform 2 [Pan troglodytes]' 91.30 293 100.00 100.00 4.30e-17 REF XP_001161361 'PREDICTED: similar to tumor necrosis factor receptor 13B variant isoform 3 [Pan troglodytes]' 91.30 295 100.00 100.00 5.76e-17 SWISS-PROT O14836 'Tumor necrosis factor receptor superfamily member 13B (Transmembrane activator and CAML interactor) (CD267 antigen)' 91.30 293 100.00 100.00 5.38e-17 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TACI_D2 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 $TACI_D2 'recombinant technology' bacteria Escherichia coli BL21 pET32-tacid2 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $TACI_D2 . mM 0.8 1.0 '[U-13C; U-15N]' 'sodium phosphate' 50 mM . . . 'sodium chloride' 150 mM . . . 'sodium azide' 1 mM . . . D2O 10 % . . . stop_ save_ ############################ # Computer software used # ############################ save_TALOS _Saveframe_category software _Name TALOS _Version 2002 loop_ _Task refinement stop_ _Details 'CORNILESCU ET AL, 1999' save_ save_CNX _Saveframe_category software _Name CNX _Version 2002 loop_ _Task refinement stop_ _Details 'ACCELRYS, SAN DIEGO, CA' save_ save_FELIX _Saveframe_category software _Name FELIX _Version 2000.1 loop_ _Task 'structure solution' stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.11 loop_ _Task 'structure solution' stop_ _Details . save_ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 3.5 loop_ _Task 'structure solution' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version 1.1 loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-SEPARATED_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-SEPARATED NOESY' _Sample_label . save_ save_3D_13C-SEPARATED_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-SEPARATED NOESY' _Sample_label . save_ save_2D_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_2D_13C_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C HSQC' _Sample_label . save_ save_3D-HNHB_5 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-HNHB _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' 200 . mM pH 7.2 . n/a pressure 1 . atm temperature 290 . 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 _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 indirect indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 indirect 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D 15N-SEPARATED 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 TACI_D2 _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 . 1 GLY CA C 43.474 0.030 1 2 . 1 GLY HA2 H 3.724 0.001 2 3 . 2 SER CA C 55.739 0.032 1 4 . 2 SER CB C 63.141 0.030 1 5 . 2 SER HA H 4.707 0.002 1 6 . 2 SER HB2 H 3.625 0.005 2 7 . 3 PRO CA C 63.574 0.029 1 8 . 3 PRO CB C 31.628 0.072 1 9 . 3 PRO CD C 50.231 0.014 1 10 . 3 PRO CG C 26.857 0.030 1 11 . 3 PRO HA H 4.380 0.001 1 12 . 3 PRO HB2 H 1.573 0.005 2 13 . 3 PRO HB3 H 2.164 0.006 2 14 . 3 PRO HD2 H 3.491 0.004 2 15 . 3 PRO HD3 H 3.748 0.003 2 16 . 3 PRO HG2 H 1.710 0.030 2 17 . 3 PRO HG3 H 1.882 0.003 2 18 . 4 TRP CA C 57.502 0.007 1 19 . 4 TRP CB C 28.723 0.010 1 20 . 4 TRP CD1 C 30.236 0.041 1 21 . 4 TRP CE3 C 120.090 0.072 1 22 . 4 TRP CH2 C 124.657 0.030 1 23 . 4 TRP CZ2 C 114.137 0.030 1 24 . 4 TRP CZ3 C 121.854 0.030 1 25 . 4 TRP HA H 4.510 0.004 1 26 . 4 TRP HB2 H 2.956 0.002 2 27 . 4 TRP HB3 H 3.119 0.002 2 28 . 4 TRP HD1 H 7.104 0.006 1 29 . 4 TRP HE1 H 10.226 0.001 1 30 . 4 TRP HE3 H 7.464 0.003 1 31 . 4 TRP HH2 H 7.263 0.005 1 32 . 4 TRP H H 7.745 0.030 1 33 . 4 TRP HZ2 H 7.520 0.004 1 34 . 4 TRP HZ3 H 7.147 0.014 1 35 . 4 TRP N N 118.905 0.030 1 36 . 4 TRP NE1 N 129.811 0.012 1 37 . 5 SER CA C 58.553 0.043 1 38 . 5 SER CB C 63.422 0.007 1 39 . 5 SER HA H 4.082 0.002 1 40 . 5 SER HB2 H 3.515 0.002 2 41 . 5 SER HB3 H 3.720 0.002 2 42 . 5 SER H H 7.644 0.030 1 43 . 5 SER N N 116.461 0.030 1 44 . 6 LEU CA C 55.863 0.068 1 45 . 6 LEU CB C 41.858 0.030 1 46 . 6 LEU CD1 C 24.443 0.039 1 47 . 6 LEU CD2 C 23.139 0.050 1 48 . 6 LEU HA H 4.181 0.008 1 49 . 6 LEU H H 7.839 0.030 1 50 . 6 LEU N N 122.053 0.030 1 51 . 6 LEU HB2 H 1.591 0.009 2 52 . 6 LEU HD1 H 0.919 0.005 2 53 . 6 LEU HD2 H 0.859 0.002 2 54 . 7 SER CA C 58.203 0.030 1 55 . 7 SER CB C 63.351 0.030 1 56 . 7 SER HA H 4.416 0.001 1 57 . 7 SER HB2 H 3.817 0.030 2 58 . 7 SER HB3 H 3.880 0.009 2 59 . 7 SER H H 7.937 0.030 1 60 . 7 SER N N 113.207 0.030 1 61 . 8 CYS CA C 55.707 0.036 1 62 . 8 CYS CB C 39.167 0.015 1 63 . 8 CYS HA H 4.687 0.001 1 64 . 8 CYS HB2 H 2.856 0.003 2 65 . 8 CYS HB3 H 3.125 0.005 2 66 . 9 ARG CA C 55.755 0.059 1 67 . 9 ARG CB C 30.961 0.013 1 68 . 9 ARG CD C 43.008 0.087 1 69 . 9 ARG CG C 26.854 0.003 1 70 . 9 ARG HA H 4.513 0.003 1 71 . 9 ARG HB2 H 1.739 0.030 2 72 . 9 ARG HB3 H 2.024 0.006 2 73 . 9 ARG HE H 7.458 0.030 2 74 . 9 ARG H H 8.301 0.001 1 75 . 9 ARG N N 121.853 0.023 1 76 . 9 ARG NE N 126.596 0.030 1 77 . 9 ARG HD2 H 3.226 0.002 2 78 . 9 ARG HG2 H 1.655 0.009 2 79 . 10 LYS CA C 58.616 0.020 1 80 . 10 LYS CB C 32.173 0.030 1 81 . 10 LYS CD C 29.061 0.030 1 82 . 10 LYS CE C 41.624 0.008 1 83 . 10 LYS CG C 24.359 0.030 1 84 . 10 LYS HA H 4.369 0.003 1 85 . 10 LYS HB2 H 1.828 0.003 2 86 . 10 LYS HD2 H 1.596 0.030 2 87 . 10 LYS HE2 H 2.786 0.002 2 88 . 10 LYS HG2 H 1.384 0.005 2 89 . 11 GLU CA C 54.669 0.001 1 90 . 11 GLU CB C 28.735 0.014 1 91 . 11 GLU CG C 34.046 0.010 1 92 . 11 GLU HA H 4.538 0.001 1 93 . 11 GLU HB2 H 1.995 0.006 2 94 . 11 GLU HB3 H 2.372 0.011 2 95 . 11 GLU HG2 H 2.326 0.030 2 96 . 11 GLU HG3 H 2.467 0.001 2 97 . 12 GLN CA C 58.542 0.005 1 98 . 12 GLN CB C 28.160 0.018 1 99 . 12 GLN CG C 36.438 0.021 1 100 . 12 GLN HA H 4.364 0.005 1 101 . 12 GLN HE21 H 6.999 0.006 2 102 . 12 GLN HE22 H 7.723 0.005 2 103 . 12 GLN NE2 N 112.250 0.005 1 104 . 12 GLN HB2 H 2.109 0.003 2 105 . 12 GLN HG2 H 2.407 0.003 2 106 . 13 GLY CA C 45.953 0.046 1 107 . 13 GLY HA2 H 3.043 0.003 2 108 . 13 GLY HA3 H 3.175 0.006 2 109 . 13 GLY H H 8.373 0.004 1 110 . 13 GLY N N 109.062 0.057 1 111 . 14 LYS CA C 53.833 0.012 1 112 . 14 LYS CB C 36.489 0.019 1 113 . 14 LYS CD C 29.248 0.046 1 114 . 14 LYS CE C 42.195 0.022 1 115 . 14 LYS CG C 25.139 0.034 1 116 . 14 LYS HA H 5.388 0.008 1 117 . 14 LYS HB2 H 1.489 0.004 2 118 . 14 LYS HB3 H 1.647 0.010 2 119 . 14 LYS HG2 H 1.081 0.006 2 120 . 14 LYS HG3 H 1.239 0.005 2 121 . 14 LYS H H 7.178 0.003 1 122 . 14 LYS N N 118.682 0.055 1 123 . 14 LYS HD2 H 1.573 0.005 2 124 . 14 LYS HE2 H 2.876 0.004 2 125 . 15 PHE CA C 55.583 0.010 1 126 . 15 PHE CB C 42.090 0.003 1 127 . 15 PHE CD1 C 131.975 0.030 3 128 . 15 PHE CE1 C 130.292 0.030 3 129 . 15 PHE CZ C 130.145 0.030 1 130 . 15 PHE HA H 4.796 0.001 1 131 . 15 PHE HB2 H 2.917 0.004 2 132 . 15 PHE HB3 H 2.963 0.003 2 133 . 15 PHE H H 8.721 0.002 1 134 . 15 PHE HZ H 7.330 0.011 1 135 . 15 PHE N N 117.014 0.015 2 136 . 15 PHE HD1 H 6.989 0.012 3 137 . 15 PHE HE1 H 7.159 0.005 3 138 . 16 TYR CA C 57.944 0.030 1 139 . 16 TYR CB C 39.199 0.002 1 140 . 16 TYR CD1 C 132.014 0.010 3 141 . 16 TYR CE1 C 116.682 0.028 3 142 . 16 TYR HA H 4.434 0.001 1 143 . 16 TYR H H 8.963 0.002 1 144 . 16 TYR N N 123.835 0.030 1 145 . 16 TYR HB2 H 2.640 0.003 2 146 . 16 TYR HD1 H 6.256 0.009 3 147 . 16 TYR HE1 H 6.310 0.002 3 148 . 17 ASP CA C 52.227 0.024 1 149 . 17 ASP CB C 43.158 0.045 1 150 . 17 ASP HA H 4.655 0.004 1 151 . 17 ASP HB2 H 2.599 0.006 2 152 . 17 ASP HB3 H 2.202 0.005 2 153 . 17 ASP H H 7.939 0.006 1 154 . 17 ASP N N 129.267 0.119 1 155 . 18 HIS CA C 58.743 0.030 1 156 . 18 HIS CB C 30.806 0.030 1 157 . 18 HIS CD2 C 118.868 0.054 1 158 . 18 HIS CE1 C 138.155 0.030 1 159 . 18 HIS HA H 4.076 0.004 1 160 . 18 HIS HB2 H 3.156 0.005 2 161 . 18 HIS HB3 H 3.191 0.001 2 162 . 18 HIS HD2 H 7.196 0.003 1 163 . 18 HIS HE1 H 7.682 0.005 1 164 . 18 HIS H H 8.593 0.010 1 165 . 18 HIS N N 123.864 0.041 1 166 . 19 LEU CA C 56.545 0.004 1 167 . 19 LEU CB C 41.115 0.011 1 168 . 19 LEU CD1 C 24.147 0.030 1 169 . 19 LEU CD2 C 23.174 0.030 1 170 . 19 LEU CG C 26.896 0.030 1 171 . 19 LEU HA H 4.276 0.005 1 172 . 19 LEU HB2 H 1.614 0.030 2 173 . 19 LEU HB3 H 1.851 0.003 2 174 . 19 LEU HG H 1.439 0.009 1 175 . 19 LEU H H 8.278 0.003 1 176 . 19 LEU N N 121.119 0.019 1 177 . 19 LEU HD1 H 0.939 0.030 2 178 . 19 LEU HD2 H 0.855 0.004 2 179 . 20 LEU CA C 54.646 0.026 1 180 . 20 LEU CB C 42.085 0.014 1 181 . 20 LEU CD1 C 24.726 0.027 1 182 . 20 LEU CD2 C 22.238 0.011 1 183 . 20 LEU CG C 26.657 0.030 1 184 . 20 LEU HA H 4.023 0.002 1 185 . 20 LEU HB2 H 1.279 0.006 2 186 . 20 LEU HB3 H 1.399 0.005 2 187 . 20 LEU HG H 1.540 0.005 1 188 . 20 LEU H H 8.013 0.002 1 189 . 20 LEU N N 119.247 0.035 1 190 . 20 LEU HD1 H 0.820 0.005 2 191 . 20 LEU HD2 H 0.766 0.002 2 192 . 21 ARG CA C 56.160 0.009 1 193 . 21 ARG CB C 25.996 0.039 1 194 . 21 ARG CD C 43.737 0.173 1 195 . 21 ARG CG C 27.037 0.029 1 196 . 21 ARG HA H 3.554 0.003 1 197 . 21 ARG HB2 H 1.801 0.007 2 198 . 21 ARG HB3 H 2.087 0.006 2 199 . 21 ARG HE H 7.197 0.030 1 200 . 21 ARG H H 8.028 0.004 1 201 . 21 ARG N N 115.788 0.041 2 202 . 21 ARG NE N 127.362 0.030 1 203 . 21 ARG HD2 H 3.208 0.006 2 204 . 21 ARG HG2 H 1.520 0.009 2 205 . 22 ASP CA C 51.501 0.023 1 206 . 22 ASP CB C 44.541 0.035 1 207 . 22 ASP HA H 4.761 0.002 1 208 . 22 ASP HB2 H 2.122 0.004 2 209 . 22 ASP HB3 H 2.305 0.006 2 210 . 22 ASP H H 6.924 0.005 1 211 . 22 ASP N N 114.402 0.068 1 212 . 23 CYS CA C 54.043 0.036 1 213 . 23 CYS CB C 40.216 0.009 1 214 . 23 CYS HA H 4.831 0.001 1 215 . 23 CYS H H 8.730 0.008 1 216 . 23 CYS N N 120.646 0.049 1 217 . 23 CYS HB2 H 2.899 0.003 2 218 . 24 ILE CA C 58.226 0.030 1 219 . 24 ILE CB C 38.238 0.019 1 220 . 24 ILE CD1 C 43.369 0.007 1 221 . 24 ILE CG1 C 26.596 0.063 1 222 . 24 ILE CG2 C 17.266 0.035 1 223 . 24 ILE HA H 4.053 0.005 1 224 . 24 ILE HB H 1.114 0.007 1 225 . 24 ILE HG12 H 0.947 0.005 2 226 . 24 ILE HG13 H 1.089 0.030 2 227 . 24 ILE H H 9.016 0.006 1 228 . 24 ILE N N 129.743 0.050 1 229 . 24 ILE HD1 H 0.585 0.004 1 230 . 24 ILE HG2 H 0.723 0.008 1 231 . 25 SER CA C 56.660 0.004 1 232 . 25 SER CB C 62.955 0.041 1 233 . 25 SER HA H 4.639 0.007 1 234 . 25 SER HB2 H 3.883 0.007 2 235 . 25 SER HB3 H 3.934 0.007 2 236 . 25 SER H H 8.564 0.003 1 237 . 25 SER N N 117.838 0.029 1 238 . 26 CYS CA C 56.815 0.011 1 239 . 26 CYS CB C 37.354 0.019 1 240 . 26 CYS HA H 4.366 0.007 1 241 . 26 CYS HB2 H 2.535 0.003 2 242 . 26 CYS HB3 H 2.881 0.005 2 243 . 26 CYS H H 9.092 0.003 1 244 . 26 CYS N N 126.070 0.020 1 245 . 27 ALA CA C 54.657 0.045 1 246 . 27 ALA CB C 18.034 0.013 1 247 . 27 ALA HA H 4.327 0.007 1 248 . 27 ALA H H 8.603 0.003 1 249 . 27 ALA N N 117.576 0.010 1 250 . 27 ALA HB H 1.451 0.007 1 251 . 28 SER CA C 59.724 0.001 1 252 . 28 SER CB C 63.628 0.003 1 253 . 28 SER HA H 4.423 0.002 1 254 . 28 SER HB2 H 4.036 0.001 2 255 . 28 SER HB3 H 4.043 0.005 2 256 . 28 SER H H 7.730 0.001 1 257 . 28 SER N N 110.014 0.029 1 258 . 29 ILE CA C 60.173 0.009 1 259 . 29 ILE CB C 39.917 0.017 1 260 . 29 ILE CD1 C 47.682 0.009 1 261 . 29 ILE CG1 C 26.318 0.030 1 262 . 29 ILE CG2 C 17.434 0.030 1 263 . 29 ILE HA H 4.835 0.003 1 264 . 29 ILE HB H 2.311 0.003 1 265 . 29 ILE H H 7.743 0.003 1 266 . 29 ILE N N 112.861 0.034 1 267 . 29 ILE HD1 H 1.064 0.006 1 268 . 29 ILE HG12 H 1.407 0.003 2 269 . 29 ILE HG2 H 0.922 0.004 1 270 . 30 CYS CA C 54.506 0.029 1 271 . 30 CYS CB C 33.363 0.012 1 272 . 30 CYS HA H 4.923 0.001 1 273 . 30 CYS HB2 H 2.844 0.006 2 274 . 30 CYS HB3 H 3.306 0.005 2 275 . 30 CYS H H 7.485 0.003 1 276 . 30 CYS N N 119.421 0.017 1 277 . 31 GLY CA C 45.299 0.015 1 278 . 31 GLY HA2 H 3.762 0.003 2 279 . 31 GLY HA3 H 4.705 0.030 2 280 . 32 GLN CA C 54.169 0.016 1 281 . 32 GLN CB C 28.441 0.036 1 282 . 32 GLN CG C 33.487 0.033 1 283 . 32 GLN HA H 4.609 0.004 1 284 . 32 GLN HB2 H 1.947 0.006 2 285 . 32 GLN HB3 H 2.265 0.008 2 286 . 32 GLN HE21 H 6.875 0.006 2 287 . 32 GLN HE22 H 7.552 0.001 2 288 . 32 GLN H H 8.562 0.001 1 289 . 32 GLN N N 122.740 0.018 1 290 . 32 GLN NE2 N 111.770 0.034 1 291 . 32 GLN HG2 H 2.326 0.001 2 292 . 33 HIS CA C 53.756 0.027 1 293 . 33 HIS CB C 30.924 0.019 1 294 . 33 HIS CD2 C 20.775 0.090 1 295 . 33 HIS CE1 C 139.176 0.030 1 296 . 33 HIS HA H 4.704 0.003 1 297 . 33 HIS HB2 H 2.869 0.006 2 298 . 33 HIS HB3 H 3.234 0.009 2 299 . 33 HIS HD2 H 6.702 0.005 1 300 . 33 HIS HE1 H 7.882 0.008 1 301 . 33 HIS H H 7.494 0.003 1 302 . 33 HIS N N 117.322 0.030 1 303 . 34 PRO CA C 61.660 0.034 1 304 . 34 PRO CB C 32.258 0.034 1 305 . 34 PRO CD C 50.007 0.020 1 306 . 34 PRO CG C 26.644 0.006 1 307 . 34 PRO HA H 4.744 0.006 1 308 . 34 PRO HB2 H 2.192 0.001 2 309 . 34 PRO HB3 H 2.301 0.007 2 310 . 34 PRO HD2 H 3.365 0.001 2 311 . 34 PRO HD3 H 3.778 0.002 2 312 . 34 PRO HG2 H 1.325 0.004 2 313 . 34 PRO HG3 H 1.819 0.003 2 314 . 35 LYS CA C 59.461 0.015 1 315 . 35 LYS CB C 31.817 0.030 1 316 . 35 LYS CD C 28.667 0.007 1 317 . 35 LYS CE C 41.677 0.030 1 318 . 35 LYS CG C 24.397 0.020 1 319 . 35 LYS HA H 4.133 0.003 1 320 . 35 LYS HB2 H 1.861 0.005 2 321 . 35 LYS HB3 H 1.874 0.008 2 322 . 35 LYS H H 8.974 0.030 1 323 . 35 LYS N N 121.738 0.030 1 324 . 35 LYS HD2 H 1.724 0.005 2 325 . 35 LYS HE2 H 3.005 0.002 2 326 . 35 LYS HG2 H 1.527 0.001 2 327 . 36 GLN CA C 58.318 0.011 1 328 . 36 GLN CB C 26.952 0.032 1 329 . 36 GLN CG C 33.422 0.009 1 330 . 36 GLN HA H 4.274 0.008 1 331 . 36 GLN HB2 H 1.615 0.005 2 332 . 36 GLN HB3 H 1.834 0.005 2 333 . 36 GLN H H 9.435 0.030 1 334 . 36 GLN N N 118.488 0.030 1 335 . 36 GLN NE2 N 112.061 0.023 1 336 . 36 GLN HE21 H 7.132 0.002 2 337 . 36 GLN HG2 H 2.249 0.003 2 338 . 37 CYS CA C 53.145 0.037 1 339 . 37 CYS CB C 39.068 0.021 1 340 . 37 CYS HA H 5.141 0.002 1 341 . 37 CYS HB2 H 2.858 0.004 2 342 . 37 CYS HB3 H 3.419 0.004 2 343 . 37 CYS H H 8.083 0.002 1 344 . 37 CYS N N 113.995 0.107 1 345 . 38 ALA CA C 56.884 0.030 1 346 . 38 ALA CB C 17.968 0.033 1 347 . 38 ALA HA H 3.764 0.001 1 348 . 38 ALA H H 8.276 0.003 1 349 . 38 ALA N N 127.297 0.011 1 350 . 38 ALA HB H 1.634 0.002 1 351 . 39 TYR CA C 60.071 0.016 1 352 . 39 TYR CB C 37.248 0.003 1 353 . 39 TYR CD1 C 132.646 0.044 3 354 . 39 TYR CE1 C 117.942 0.025 3 355 . 39 TYR HA H 4.143 0.002 1 356 . 39 TYR HB2 H 2.857 0.005 2 357 . 39 TYR HB3 H 3.058 0.007 2 358 . 39 TYR H H 8.728 0.030 1 359 . 39 TYR N N 116.197 0.030 1 360 . 39 TYR HD1 H 6.927 0.008 3 361 . 39 TYR HE1 H 6.909 0.002 3 362 . 40 PHE CA C 59.551 0.017 1 363 . 40 PHE CB C 40.185 0.038 1 364 . 40 PHE CD1 C 131.611 0.052 3 365 . 40 PHE CE1 C 131.487 0.030 3 366 . 40 PHE CZ C 130.361 0.030 1 367 . 40 PHE HA H 3.979 0.003 1 368 . 40 PHE HB2 H 2.629 0.003 2 369 . 40 PHE HB3 H 2.881 0.002 2 370 . 40 PHE H H 7.378 0.001 1 371 . 40 PHE HZ H 7.391 0.006 1 372 . 40 PHE N N 118.001 0.039 1 373 . 40 PHE HD1 H 7.189 0.006 3 374 . 40 PHE HE1 H 7.399 0.010 3 375 . 41 CYS CA C 54.575 0.068 1 376 . 41 CYS CB C 36.063 0.028 1 377 . 41 CYS HA H 4.504 0.003 1 378 . 41 CYS HB2 H 1.382 0.007 2 379 . 41 CYS HB3 H 2.544 0.003 2 380 . 41 CYS H H 8.080 0.001 1 381 . 41 CYS N N 113.885 0.079 1 382 . 42 GLU CA C 56.268 0.016 1 383 . 42 GLU CB C 29.169 0.026 1 384 . 42 GLU CG C 36.322 0.003 1 385 . 42 GLU HA H 4.317 0.005 1 386 . 42 GLU HB2 H 1.988 0.007 2 387 . 42 GLU HB3 H 2.056 0.003 2 388 . 42 GLU HG2 H 2.220 0.030 2 389 . 42 GLU HG3 H 2.322 0.003 2 390 . 42 GLU H H 8.200 0.001 1 391 . 42 GLU N N 119.403 0.028 1 392 . 43 ASN CA C 53.084 0.004 1 393 . 43 ASN CB C 38.644 0.030 1 394 . 43 ASN HA H 4.572 0.030 1 395 . 43 ASN HB2 H 2.554 0.001 2 396 . 43 ASN HB3 H 2.688 0.004 2 397 . 43 ASN HD21 H 6.880 0.004 2 398 . 43 ASN HD22 H 7.483 0.003 2 399 . 43 ASN H H 7.823 0.030 1 400 . 43 ASN N N 117.634 0.030 1 401 . 43 ASN ND2 N 113.672 0.054 1 402 . 44 LYS CA C 56.549 0.030 1 403 . 44 LYS CB C 32.597 0.015 1 404 . 44 LYS CD C 28.657 0.128 1 405 . 44 LYS CE C 41.826 0.032 1 406 . 44 LYS CG C 24.216 0.030 1 407 . 44 LYS HA H 4.224 0.006 1 408 . 44 LYS HB2 H 1.644 0.001 2 409 . 44 LYS HB3 H 1.773 0.006 2 410 . 44 LYS HG2 H 1.345 0.006 2 411 . 44 LYS HG3 H 1.356 0.024 2 412 . 44 LYS H H 8.055 0.002 1 413 . 44 LYS N N 120.648 0.036 1 414 . 44 LYS HD2 H 1.609 0.008 2 415 . 44 LYS HE2 H 2.942 0.008 2 416 . 45 LEU CA C 54.719 0.019 1 417 . 45 LEU CB C 41.670 0.030 1 418 . 45 LEU CD1 C 24.657 0.030 1 419 . 45 LEU CD2 C 23.035 0.003 1 420 . 45 LEU HA H 4.312 0.010 1 421 . 45 LEU H H 8.168 0.030 1 422 . 45 LEU N N 122.571 0.012 1 423 . 45 LEU HB2 H 1.612 0.008 2 424 . 45 LEU HD1 H 0.934 0.030 2 425 . 45 LEU HD2 H 0.854 0.006 2 426 . 46 ARG CA C 57.034 0.034 1 427 . 46 ARG CB C 31.312 0.066 1 428 . 46 ARG CD C 43.261 0.018 1 429 . 46 ARG HA H 4.135 0.004 1 430 . 46 ARG HB2 H 1.698 0.006 2 431 . 46 ARG HB3 H 1.820 0.008 2 432 . 46 ARG HE H 7.225 0.030 1 433 . 46 ARG H H 7.777 0.001 1 434 . 46 ARG N N 126.142 0.010 1 435 . 46 ARG NE N 127.104 0.030 1 436 . 46 ARG HD2 H 3.141 0.004 2 437 . 46 ARG HG2 H 1.539 0.030 2 stop_ save_