data_5593 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignments for the rat GMEB-2 SAND domain ; _BMRB_accession_number 5593 _BMRB_flat_file_name bmr5593.str _Entry_type original _Submission_date 2002-11-19 _Accession_date 2002-11-19 _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 Bottomley Matthew J. . 2 Sattler Michael . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 99 "13C chemical shifts" 195 "15N chemical shifts" 99 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-10-30 update BMRB 'complete entry, etc.' 2003-03-18 original author 'original release' stop_ _Original_release_date 2002-11-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C and 15N backbone resonance assignments of the SAND domains from glucocorticoid modulatory element binding proteins-1 and -2 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bottomley Matthew J. . 2 Sattler Michael . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 25 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 259 _Page_last 260 _Year 2003 _Details . loop_ _Keyword GMEB1 'KDWK motif' 'SAND domain' 'glucocorticoid response' 'transcriptional regulation' stop_ save_ ################################## # Molecular system description # ################################## save_system_rGMEB-2_SAND _Saveframe_category molecular_system _Mol_system_name 'rat GMEB-2 extended SAND domain' _Abbreviation_common 'rGMEB-2 SAND' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Rat GMEB-2 extended SAND domain' $rGMEB-2_SAND 'ZINC (II) ION' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'other bound and free' loop_ _Biological_function 'DNA-binding domain' 'full-length protein activates parvovirus nickase NS1 protein' 'zinc-binding domain' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_rGMEB-2_SAND _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'SAND domain from rat GMEB-2 protein' _Abbreviation_common 'rGMEB-2 SAND' _Molecular_mass 11536 _Mol_thiol_state 'other bound and free' _Details ; There is a tripeptide N-terminal tag (GAM) followed by 98 residues of the rat GMEB-2 protein, residues Glu 81 to Lys 178. Theoretical pI=8.33. The protein sequence given should be numbered according to its occurrence in the wild-type protein. Thus the first residue (G) should be numbered 78, and the last residue (K) 178. Nevertheless, it should be noted that the first three residues (GAM) are derived from an N-terminal tag. The protein studied was produced from the rat GMEB2 gene, cloned from a rat cDNA library. The corresponding GenBank code is AF059273. The protein numbering, spanning rat GMEB2 residues E81-K178) is according to the wild-type rat protein. Note, however, that for this GMEB2 construct, the corresponding region in the HUMAN GMEB2 protein has an identical amino acid sequence. The human GMEB protein is under GenBank code NM_012384, and the SAND domain therein spans residues E82-K179. ; ############################## # Polymer residue sequence # ############################## _Residue_count 101 _Mol_residue_sequence ; GAMEGENLEAEIVYPITCGD SRANLIWRKFVCPGINVKCV QYDEHVISPKEFVHLAGKST LKDWKRAIRMNGIMLRKIMD SGELDFYQHDKVCSNTCRST K ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 78 GLY 2 79 ALA 3 80 MET 4 81 GLU 5 82 GLY 6 83 GLU 7 84 ASN 8 85 LEU 9 86 GLU 10 87 ALA 11 88 GLU 12 89 ILE 13 90 VAL 14 91 TYR 15 92 PRO 16 93 ILE 17 94 THR 18 95 CYS 19 96 GLY 20 97 ASP 21 98 SER 22 99 ARG 23 100 ALA 24 101 ASN 25 102 LEU 26 103 ILE 27 104 TRP 28 105 ARG 29 106 LYS 30 107 PHE 31 108 VAL 32 109 CYS 33 110 PRO 34 111 GLY 35 112 ILE 36 113 ASN 37 114 VAL 38 115 LYS 39 116 CYS 40 117 VAL 41 118 GLN 42 119 TYR 43 120 ASP 44 121 GLU 45 122 HIS 46 123 VAL 47 124 ILE 48 125 SER 49 126 PRO 50 127 LYS 51 128 GLU 52 129 PHE 53 130 VAL 54 131 HIS 55 132 LEU 56 133 ALA 57 134 GLY 58 135 LYS 59 136 SER 60 137 THR 61 138 LEU 62 139 LYS 63 140 ASP 64 141 TRP 65 142 LYS 66 143 ARG 67 144 ALA 68 145 ILE 69 146 ARG 70 147 MET 71 148 ASN 72 149 GLY 73 150 ILE 74 151 MET 75 152 LEU 76 153 ARG 77 154 LYS 78 155 ILE 79 156 MET 80 157 ASP 81 158 SER 82 159 GLY 83 160 GLU 84 161 LEU 85 162 ASP 86 163 PHE 87 164 TYR 88 165 GLN 89 166 HIS 90 167 ASP 91 168 LYS 92 169 VAL 93 170 CYS 94 171 SER 95 172 ASN 96 173 THR 97 174 CYS 98 175 ARG 99 176 SER 100 177 THR 101 178 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jun 2 09:48:05 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $rGMEB-2_SAND Rat 10116 Eukaryota Metazoa Rattus norvegicus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name _Details $rGMEB-2_SAND 'recombinant technology' 'E. coli' Escherichia coli BL21 DE3 plasmid 'Modified pET-24d' ; Protein was expressed from an in-house modified pET-24d vector (originally supplied by NOVAGEN) in E. coli induced with IPTG at 23 degrees C for 16 hours. ; 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 $rGMEB-2_SAND 1.0 mM 0.8 1.2 '[U-98% 15N]' 'sodium phosphate' 20 mM . . . NaCl 0.2 M . . . DTT 3 mM . . . H2O 90 % . . . D2O 10 % . . . stop_ save_ save_Sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $rGMEB-2_SAND 1.0 mM 0.8 1.2 '[U-98% 13C; U-98% 15N]' 'sodium phosphate' 20 mM . . . NaCl 0.2 M . . . DTT 3 mM . . . H2O 90 % . . . D2O 10 % . . . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label . save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_CBCANH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCANH' _Sample_label . save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details ; Samples were also stored under either nitrogen or argon gas in order to limit oxidation of the numerous Cys residues (important in zinc-binding). ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.22 0.02 M pH 6.4 0.2 pH temperature 300 1.0 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 TSP C 13 'methyl protons' ppm 0.0 external indirect . external . 0.251449530 TSP H 1 'methyl protons' ppm 0.0 internal direct . internal . 1.0 TSP N 15 'methyl protons' ppm 0.0 external indirect . external . 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_CSR_1 _Saveframe_category assigned_chemical_shifts _Details ; The first three N-terminal residues, GAM, were not derived from GMEB2 but from the linker resulting from cleavage of the N-terminal Histag. The backbone NH/N HSQC cross-peak signal for some the N-terminal G residue was not observed in the NMR spectra. ; loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D CBCANH' '3D CBCA(CO)NH' stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Rat GMEB-2 extended SAND domain' _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 78 1 GLY CA C 41.24 0.12 1 2 79 2 ALA H H 8.689 0.02 1 3 79 2 ALA N N 123.87 0.05 1 4 79 2 ALA CA C 50.56 0.12 1 5 79 2 ALA CB C 17.02 0.12 1 6 80 3 MET H H 8.595 0.02 1 7 80 3 MET N N 119.488 0.05 1 8 80 3 MET CA C 53.67 0.12 1 9 80 3 MET CB C 30.67 0.12 1 10 81 4 GLU H H 8.476 0.02 1 11 81 4 GLU N N 122.126 0.05 1 12 81 4 GLU CA C 54.31 0.12 1 13 81 4 GLU CB C 28.15 0.12 1 14 82 5 GLY H H 8.481 0.02 1 15 82 5 GLY N N 110.119 0.05 1 16 82 5 GLY CA C 43.1 0.12 1 17 83 6 GLU H H 8.261 0.02 1 18 83 6 GLU N N 120.388 0.05 1 19 83 6 GLU CA C 54.28 0.12 1 20 83 6 GLU CB C 28.2 0.12 1 21 84 7 ASN H H 8.613 0.02 1 22 84 7 ASN N N 119.726 0.05 1 23 84 7 ASN CA C 51.17 0.12 1 24 84 7 ASN CB C 36.27 0.12 1 25 85 8 LEU H H 8.385 0.02 1 26 85 8 LEU N N 123.043 0.05 1 27 85 8 LEU CA C 53.66 0.12 1 28 85 8 LEU CB C 39.99 0.12 1 29 86 9 GLU H H 8.4 0.02 1 30 86 9 GLU N N 120.951 0.05 1 31 86 9 GLU CA C 54.29 0.12 1 32 86 9 GLU CB C 27.58 0.12 1 33 87 10 ALA H H 8.161 0.02 1 34 87 10 ALA N N 124.019 0.05 1 35 87 10 ALA CA C 49.94 0.12 1 36 87 10 ALA CB C 17.03 0.12 1 37 88 11 GLU H H 8.283 0.02 1 38 88 11 GLU N N 120.519 0.05 1 39 88 11 GLU CA C 54.28 0.12 1 40 88 11 GLU CB C 28.16 0.12 1 41 89 12 ILE H H 7.902 0.02 1 42 89 12 ILE N N 124.616 0.05 1 43 89 12 ILE CA C 59.86 0.12 1 44 89 12 ILE CB C 36.24 0.12 1 45 90 13 VAL H H 8.31 0.02 1 46 90 13 VAL N N 125.647 0.05 1 47 90 13 VAL CA C 56.77 0.12 1 48 90 13 VAL CB C 33.17 0.12 1 49 91 14 TYR H H 8.878 0.02 1 50 91 14 TYR N N 121.934 0.05 1 51 91 14 TYR CA C 51.8 0.12 1 52 91 14 TYR CB C 38.76 0.12 1 53 92 15 PRO CA C 61.12 0.12 1 54 92 15 PRO CB C 29.46 0.12 1 55 93 16 ILE H H 8.971 0.02 1 56 93 16 ILE N N 118.397 0.05 1 57 93 16 ILE CA C 56.77 0.12 1 58 93 16 ILE CB C 41.24 0.12 1 59 94 17 THR H H 9.386 0.02 1 60 94 17 THR N N 111.024 0.05 1 61 94 17 THR CA C 57.39 0.12 1 62 94 17 THR CB C 70.45 0.12 1 63 95 18 CYS H H 8.222 0.02 1 64 95 18 CYS N N 120.331 0.05 1 65 95 18 CYS CA C 57.5 0.12 1 66 95 18 CYS CB C 25.71 0.12 1 67 96 19 GLY H H 9.177 0.02 1 68 96 19 GLY N N 118.779 0.05 1 69 96 19 GLY CA C 45.2 0.12 1 70 97 20 ASP H H 8.979 0.02 1 71 97 20 ASP N N 127.484 0.05 1 72 97 20 ASP CA C 52.42 0.12 1 73 97 20 ASP CB C 39.38 0.12 1 74 98 21 SER H H 8.509 0.02 1 75 98 21 SER N N 117.536 0.05 1 76 98 21 SER CA C 58.0 0.12 1 77 98 21 SER CB C 62.97 0.12 1 78 99 22 ARG H H 8.997 0.02 1 79 99 22 ARG N N 123.991 0.05 1 80 99 22 ARG CA C 53.65 0.12 1 81 99 22 ARG CB C 31.38 0.12 1 82 100 23 ALA H H 8.75 0.02 1 83 100 23 ALA N N 122.337 0.05 1 84 100 23 ALA CA C 49.31 0.12 1 85 100 23 ALA CB C 21.38 0.12 1 86 101 24 ASN H H 7.998 0.02 1 87 101 24 ASN N N 115.191 0.05 1 88 101 24 ASN CA C 49.65 0.12 1 89 101 24 ASN CB C 40.0 0.12 1 90 102 25 LEU H H 9.875 0.02 1 91 102 25 LEU N N 126.152 0.05 1 92 102 25 LEU CA C 52.42 0.12 1 93 102 25 LEU CB C 42.4 0.12 1 94 103 26 ILE H H 9.15 0.02 1 95 103 26 ILE N N 129.17 0.05 1 96 103 26 ILE CA C 58.63 0.12 1 97 103 26 ILE CB C 34.42 0.12 1 98 104 27 TRP H H 7.897 0.02 1 99 104 27 TRP N N 130.265 0.05 1 100 104 27 TRP CA C 60.5 0.12 1 101 104 27 TRP CB C 26.95 0.12 1 102 104 27 TRP NE1 N 130.003 0.05 1 103 104 27 TRP HE1 H 10.909 0.02 1 104 105 28 ARG H H 9.401 0.02 1 105 105 28 ARG N N 113.082 0.05 1 106 105 28 ARG CA C 55.53 0.12 1 107 105 28 ARG CB C 26.96 0.12 1 108 106 29 LYS H H 7.147 0.02 1 109 106 29 LYS N N 112.319 0.05 1 110 106 29 LYS CA C 53.01 0.12 1 111 106 29 LYS CB C 31.93 0.12 1 112 107 30 PHE H H 8.166 0.02 1 113 107 30 PHE N N 126.8 0.05 1 114 107 30 PHE CA C 53.66 0.12 1 115 107 30 PHE CB C 36.27 0.12 1 116 108 31 VAL H H 7.352 0.02 1 117 108 31 VAL N N 119.831 0.05 1 118 108 31 VAL CA C 57.4 0.12 1 119 108 31 VAL CB C 31.92 0.12 1 120 109 32 CYS H H 8.75 0.02 1 121 109 32 CYS N N 126.191 0.05 1 122 109 32 CYS CA C 54.29 0.12 1 123 109 32 CYS CB C 26.75 0.12 1 124 110 33 PRO CA C 62.37 0.12 1 125 110 33 PRO CB C 30.06 0.12 1 126 111 34 GLY H H 9.064 0.02 1 127 111 34 GLY N N 118.198 0.05 1 128 111 34 GLY CA C 46.84 0.12 1 129 112 35 ILE H H 7.444 0.02 1 130 112 35 ILE N N 121.476 0.05 1 131 112 35 ILE CA C 62.35 0.12 1 132 112 35 ILE CB C 36.26 0.12 1 133 113 36 ASN H H 7.646 0.02 1 134 113 36 ASN N N 114.439 0.05 1 135 113 36 ASN CA C 49.93 0.12 1 136 113 36 ASN CB C 36.89 0.12 1 137 114 37 VAL H H 7.339 0.02 1 138 114 37 VAL N N 121.929 0.05 1 139 114 37 VAL CA C 59.24 0.12 1 140 114 37 VAL CB C 30.68 0.12 1 141 115 38 LYS H H 8.787 0.02 1 142 115 38 LYS N N 124.813 0.05 1 143 115 38 LYS CA C 53.68 0.12 1 144 115 38 LYS CB C 27.6 0.12 1 145 116 39 CYS H H 7.767 0.02 1 146 116 39 CYS N N 119.102 0.05 1 147 116 39 CYS CA C 54.27 0.12 1 148 116 39 CYS CB C 26.95 0.12 1 149 117 40 VAL H H 9.245 0.02 1 150 117 40 VAL N N 124.983 0.05 1 151 117 40 VAL CA C 59.25 0.12 1 152 117 40 VAL CB C 30.06 0.12 1 153 118 41 GLN H H 9.544 0.02 1 154 118 41 GLN N N 128.66 0.05 1 155 118 41 GLN CA C 53.04 0.12 1 156 118 41 GLN CB C 26.96 0.12 1 157 119 42 TYR H H 9.148 0.02 1 158 119 42 TYR N N 131.859 0.05 1 159 119 42 TYR CA C 54.89 0.12 1 160 119 42 TYR CB C 39.38 0.12 1 161 120 43 ASP H H 8.843 0.02 1 162 120 43 ASP N N 129.339 0.05 1 163 120 43 ASP CA C 53.11 0.12 1 164 120 43 ASP CB C 36.89 0.12 1 165 121 44 GLU H H 8.699 0.02 1 166 121 44 GLU N N 112.908 0.05 1 167 121 44 GLU CA C 55.39 0.12 1 168 121 44 GLU CB C 25.55 0.12 1 169 122 45 HIS H H 8.106 0.02 1 170 122 45 HIS N N 117.546 0.05 1 171 122 45 HIS CA C 52.42 0.12 1 172 122 45 HIS CB C 29.44 0.12 1 173 123 46 VAL H H 8.595 0.02 1 174 123 46 VAL N N 121.81 0.05 1 175 123 46 VAL CA C 59.89 0.12 1 176 123 46 VAL CB C 29.4 0.12 1 177 124 47 ILE H H 9.733 0.02 1 178 124 47 ILE N N 122.451 0.05 1 179 124 47 ILE CA C 57.39 0.12 1 180 124 47 ILE CB C 40.0 0.12 1 181 125 48 SER H H 9.339 0.02 1 182 125 48 SER N N 117.931 0.05 1 183 125 48 SER CA C 53.67 0.12 1 184 125 48 SER CB C 61.74 0.12 1 185 126 49 PRO CA C 64.21 0.12 1 186 126 49 PRO CB C 30.06 0.12 1 187 127 50 LYS H H 7.727 0.02 1 188 127 50 LYS N N 115.36 0.05 1 189 127 50 LYS CA C 58.02 0.12 1 190 127 50 LYS CB C 30.67 0.12 1 191 128 51 GLU H H 8.076 0.02 1 192 128 51 GLU N N 120.126 0.05 1 193 128 51 GLU CA C 56.77 0.12 1 194 128 51 GLU CB C 27.57 0.12 1 195 129 52 PHE H H 8.705 0.02 1 196 129 52 PHE N N 121.111 0.05 1 197 129 52 PHE CA C 57.37 0.12 1 198 129 52 PHE CB C 36.88 0.12 1 199 130 53 VAL H H 8.412 0.02 1 200 130 53 VAL N N 117.555 0.05 1 201 130 53 VAL CA C 62.98 0.12 1 202 130 53 VAL CB C 29.45 0.12 1 203 131 54 HIS H H 7.77 0.02 1 204 131 54 HIS N N 117.936 0.05 1 205 131 54 HIS CA C 56.75 0.12 1 206 131 54 HIS CB C 26.98 0.12 1 207 132 55 LEU H H 8.533 0.02 1 208 132 55 LEU N N 121.67 0.05 1 209 132 55 LEU CA C 55.54 0.12 1 210 132 55 LEU CB C 39.38 0.12 1 211 133 56 ALA H H 8.011 0.02 1 212 133 56 ALA N N 120.743 0.05 1 213 133 56 ALA CA C 50.55 0.12 1 214 133 56 ALA CB C 17.03 0.12 1 215 134 57 GLY H H 7.777 0.02 1 216 134 57 GLY N N 105.631 0.05 1 217 134 57 GLY CA C 43.63 0.12 1 218 135 58 LYS H H 7.921 0.02 1 219 135 58 LYS N N 118.366 0.05 1 220 135 58 LYS CA C 52.43 0.12 1 221 135 58 LYS CB C 30.05 0.12 1 222 136 59 SER H H 8.345 0.02 1 223 136 59 SER N N 115.535 0.05 1 224 136 59 SER CA C 57.9 0.12 1 225 136 59 SER CB C 61.13 0.12 1 226 137 60 THR H H 8.034 0.02 1 227 137 60 THR N N 112.905 0.05 1 228 137 60 THR CA C 60.49 0.12 1 229 137 60 THR CB C 66.71 0.12 1 230 138 61 LEU H H 7.704 0.02 1 231 138 61 LEU N N 122.649 0.05 1 232 138 61 LEU CA C 53.66 0.12 1 233 138 61 LEU CB C 39.38 0.12 1 234 139 62 LYS H H 8.054 0.02 1 235 139 62 LYS N N 119.613 0.05 1 236 139 62 LYS CA C 54.92 0.12 1 237 139 62 LYS CB C 30.07 0.12 1 238 140 63 ASP H H 8.116 0.02 1 239 140 63 ASP N N 118.435 0.05 1 240 140 63 ASP CA C 51.2 0.12 1 241 140 63 ASP CB C 39.37 0.12 1 242 141 64 TRP H H 8.841 0.02 1 243 141 64 TRP N N 128.669 0.05 1 244 141 64 TRP CA C 58.01 0.12 1 245 141 64 TRP CB C 25.09 0.12 1 246 141 64 TRP NE1 N 131.726 0.05 1 247 141 64 TRP HE1 H 10.813 0.02 1 248 142 65 LYS H H 7.328 0.02 1 249 142 65 LYS N N 117.026 0.05 1 250 142 65 LYS CA C 56.14 0.12 1 251 142 65 LYS CB C 29.43 0.12 1 252 143 66 ARG H H 7.5 0.02 1 253 143 66 ARG N N 116.065 0.05 1 254 143 66 ARG CA C 54.92 0.12 1 255 143 66 ARG CB C 29.48 0.12 1 256 144 67 ALA H H 7.707 0.02 1 257 144 67 ALA N N 119.651 0.05 1 258 144 67 ALA CA C 51.17 0.12 1 259 144 67 ALA CB C 18.29 0.12 1 260 145 68 ILE H H 7.208 0.02 1 261 145 68 ILE N N 117.291 0.05 1 262 145 68 ILE CA C 58.05 0.12 1 263 145 68 ILE CB C 36.9 0.12 1 264 146 69 ARG H H 8.997 0.02 1 265 146 69 ARG N N 123.991 0.05 1 266 146 69 ARG CA C 51.8 0.12 1 267 146 69 ARG CB C 31.31 0.12 1 268 147 70 MET H H 9.118 0.02 1 269 147 70 MET N N 119.696 0.05 1 270 147 70 MET CA C 53.03 0.12 1 271 147 70 MET CB C 34.38 0.12 1 272 148 71 ASN H H 9.651 0.02 1 273 148 71 ASN N N 125.987 0.05 1 274 148 71 ASN CA C 52.42 0.12 1 275 148 71 ASN CB C 35.02 0.12 1 276 149 72 GLY H H 8.606 0.02 1 277 149 72 GLY N N 101.48 0.05 1 278 149 72 GLY CA C 43.1 0.12 1 279 150 73 ILE H H 7.838 0.02 1 280 150 73 ILE N N 124.541 0.05 1 281 150 73 ILE CA C 56.77 0.12 1 282 150 73 ILE CB C 36.89 0.12 1 283 151 74 MET H H 8.939 0.02 1 284 151 74 MET N N 125.503 0.05 1 285 151 74 MET CA C 56.13 0.12 1 286 151 74 MET CB C 31.91 0.12 1 287 152 75 LEU H H 9.079 0.02 1 288 152 75 LEU N N 126.192 0.05 1 289 152 75 LEU CA C 56.14 0.12 1 290 152 75 LEU CB C 39.38 0.12 1 291 153 76 ARG H H 8.5 0.02 1 292 153 76 ARG N N 115.506 0.05 1 293 153 76 ARG CA C 56.16 0.12 1 294 153 76 ARG CB C 29.42 0.12 1 295 154 77 LYS H H 6.962 0.02 1 296 154 77 LYS N N 116.342 0.05 1 297 154 77 LYS CA C 56.14 0.12 1 298 154 77 LYS CB C 30.03 0.12 1 299 155 78 ILE H H 7.387 0.02 1 300 155 78 ILE N N 119.609 0.05 1 301 155 78 ILE CA C 61.74 0.12 1 302 155 78 ILE CB C 36.27 0.12 1 303 156 79 MET H H 8.553 0.02 1 304 156 79 MET N N 118.429 0.05 1 305 156 79 MET CA C 56.16 0.12 1 306 156 79 MET CB C 30.7 0.12 1 307 157 80 ASP H H 8.587 0.02 1 308 157 80 ASP N N 122.454 0.05 1 309 157 80 ASP CA C 55.54 0.12 1 310 157 80 ASP CB C 37.52 0.12 1 311 158 81 SER H H 7.818 0.02 1 312 158 81 SER N N 111.847 0.05 1 313 158 81 SER CA C 57.34 0.12 1 314 158 81 SER CB C 61.76 0.12 1 315 159 82 GLY H H 7.757 0.02 1 316 159 82 GLY N N 109.311 0.05 1 317 159 82 GLY CA C 43.12 0.12 1 318 160 83 GLU H H 7.948 0.02 1 319 160 83 GLU N N 120.431 0.05 1 320 160 83 GLU CA C 56.16 0.12 1 321 160 83 GLU CB C 27.58 0.12 1 322 161 84 LEU H H 7.132 0.02 1 323 161 84 LEU N N 118.262 0.05 1 324 161 84 LEU CA C 51.8 0.12 1 325 161 84 LEU CB C 43.72 0.12 1 326 162 85 ASP H H 8.473 0.02 1 327 162 85 ASP N N 124.621 0.05 1 328 162 85 ASP CA C 48.7 0.12 1 329 162 85 ASP CB C 41.87 0.12 1 330 163 86 PHE H H 8.295 0.02 1 331 163 86 PHE N N 117.443 0.05 1 332 163 86 PHE CA C 55.81 0.12 1 333 163 86 PHE CB C 38.14 0.12 1 334 164 87 TYR H H 8.721 0.02 1 335 164 87 TYR N N 125.855 0.05 1 336 164 87 TYR CA C 56.77 0.12 1 337 164 87 TYR CB C 35.64 0.12 1 338 165 88 GLN H H 8.547 0.02 1 339 165 88 GLN N N 121.52 0.05 1 340 165 88 GLN CA C 54.37 0.12 1 341 165 88 GLN CB C 23.87 0.12 1 342 166 89 HIS H H 7.558 0.02 1 343 166 89 HIS N N 118.668 0.05 1 344 166 89 HIS CA C 53.04 0.12 1 345 166 89 HIS CB C 27.56 0.12 1 346 167 90 ASP H H 8.871 0.02 1 347 167 90 ASP N N 112.047 0.05 1 348 167 90 ASP CA C 53.1 0.12 1 349 167 90 ASP CB C 36.89 0.12 1 350 168 91 LYS H H 7.616 0.02 1 351 168 91 LYS N N 117.948 0.05 1 352 168 91 LYS CA C 54.26 0.12 1 353 168 91 LYS CB C 33.17 0.12 1 354 169 92 VAL H H 8.416 0.02 1 355 169 92 VAL N N 122.254 0.05 1 356 169 92 VAL CA C 59.89 0.12 1 357 169 92 VAL CB C 31.29 0.12 1 358 170 93 CYS H H 8.387 0.02 1 359 170 93 CYS N N 127.312 0.05 1 360 170 93 CYS CA C 56.16 0.12 1 361 170 93 CYS CB C 29.43 0.12 1 362 171 94 SER H H 9.802 0.02 1 363 171 94 SER N N 129.231 0.05 1 364 171 94 SER CA C 57.39 0.12 1 365 171 94 SER CB C 63.6 0.12 1 366 172 95 ASN H H 10.51 0.02 1 367 172 95 ASN N N 123.11 0.05 1 368 172 95 ASN CA C 52.41 0.12 1 369 172 95 ASN CB C 35.65 0.12 1 370 173 96 THR H H 7.706 0.02 1 371 173 96 THR N N 106.741 0.05 1 372 173 96 THR CA C 59.86 0.12 1 373 173 96 THR CB C 67.33 0.12 1 374 174 97 CYS H H 7.994 0.02 1 375 174 97 CYS N N 120.743 0.05 1 376 174 97 CYS CA C 55.52 0.12 1 377 174 97 CYS CB C 29.42 0.12 1 378 175 98 ARG H H 8.026 0.02 1 379 175 98 ARG N N 121.44 0.05 1 380 175 98 ARG CA C 53.67 0.12 1 381 175 98 ARG CB C 28.8 0.12 1 382 176 99 SER H H 8.207 0.02 1 383 176 99 SER N N 116.433 0.05 1 384 176 99 SER CA C 56.16 0.12 1 385 176 99 SER CB C 61.73 0.12 1 386 177 100 THR H H 8.312 0.02 1 387 177 100 THR N N 116.404 0.05 1 388 177 100 THR CA C 59.87 0.12 1 389 177 100 THR CB C 67.35 0.12 1 390 178 101 LYS H H 8.033 0.02 1 391 178 101 LYS N N 128.555 0.05 1 392 178 101 LYS CA C 55.53 0.12 1 393 178 101 LYS CB C 31.32 0.12 1 stop_ save_