data_6500 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for SIP (74-178) ; _BMRB_accession_number 6500 _BMRB_flat_file_name bmr6500.str _Entry_type original _Submission_date 2005-02-14 _Accession_date 2005-02-16 _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 Bhattacharya Shibani . . 2 Lee Young-Tae . . 3 Michowski Wojciech . . 4 Filipek Anna . . 5 Kuznicki Jacek . . 6 Chazin Walter J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 93 "13C chemical shifts" 279 "15N chemical shifts" 93 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-08-16 original author . stop_ _Original_release_date 2005-08-16 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The Modular Structure of SIP Facilitates Its Role in Stabilizing Multiprotein Assemblies ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15996101 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bhattacharya Shibani . . 2 Lee Young-Tae . . 3 Michowski Wojciech . . 4 Filipek Anna . . 5 Kuznicki Jacek . . 6 Chazin Walter J. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 44 _Journal_issue 27 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 9462 _Page_last 9471 _Year 2005 _Details . save_ ################################## # Molecular system description # ################################## save_system_SIP_(74-178) _Saveframe_category molecular_system _Mol_system_name 'Siah-Interacting Protein (Residues 74-178)' _Abbreviation_common 'SIP (74-178)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'SIP CS-Domain' $SIP_(74-178) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'beta-catenin ubiquitination' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SIP_(74-178) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'SIP (74-178)' _Abbreviation_common 'SIP (74-178)' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 105 _Mol_residue_sequence ; VKISNYGWDQSDKFVKIYIT LTGVHQVPTENVQVHFTERS FDLLVKNLNGKNYSMIVNNL LKPISVESSSKKVKTDTVII LCRKKAENTRWDYLTQVEKE CKEKE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 74 VAL 2 75 LYS 3 76 ILE 4 77 SER 5 78 ASN 6 79 TYR 7 80 GLY 8 81 TRP 9 82 ASP 10 83 GLN 11 84 SER 12 85 ASP 13 86 LYS 14 87 PHE 15 88 VAL 16 89 LYS 17 90 ILE 18 91 TYR 19 92 ILE 20 93 THR 21 94 LEU 22 95 THR 23 96 GLY 24 97 VAL 25 98 HIS 26 99 GLN 27 100 VAL 28 101 PRO 29 102 THR 30 103 GLU 31 104 ASN 32 105 VAL 33 106 GLN 34 107 VAL 35 108 HIS 36 109 PHE 37 110 THR 38 111 GLU 39 112 ARG 40 113 SER 41 114 PHE 42 115 ASP 43 116 LEU 44 117 LEU 45 118 VAL 46 119 LYS 47 120 ASN 48 121 LEU 49 122 ASN 50 123 GLY 51 124 LYS 52 125 ASN 53 126 TYR 54 127 SER 55 128 MET 56 129 ILE 57 130 VAL 58 131 ASN 59 132 ASN 60 133 LEU 61 134 LEU 62 135 LYS 63 136 PRO 64 137 ILE 65 138 SER 66 139 VAL 67 140 GLU 68 141 SER 69 142 SER 70 143 SER 71 144 LYS 72 145 LYS 73 146 VAL 74 147 LYS 75 148 THR 76 149 ASP 77 150 THR 78 151 VAL 79 152 ILE 80 153 ILE 81 154 LEU 82 155 CYS 83 156 ARG 84 157 LYS 85 158 LYS 86 159 ALA 87 160 GLU 88 161 ASN 89 162 THR 90 163 ARG 91 164 TRP 92 165 ASP 93 166 TYR 94 167 LEU 95 168 THR 96 169 GLN 97 170 VAL 98 171 GLU 99 172 LYS 100 173 GLU 101 174 CYS 102 175 LYS 103 176 GLU 104 177 LYS 105 178 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 GB AAC16757 "calcyclin binding protein [Mus musculus]" 100.00 247 100.00 100.00 6.37e-69 GB AAH25948 "Calcyclin binding protein [Mus musculus]" 100.00 229 100.00 100.00 4.82e-69 GB AAH79007 "Calcyclin binding protein [Rattus norvegicus]" 100.00 229 99.05 99.05 1.94e-68 GB EDL39341 "calcyclin binding protein [Mus musculus]" 100.00 229 100.00 100.00 4.82e-69 GB EDM09438 "calcyclin binding protein, isoform CRA_b [Rattus norvegicus]" 100.00 229 99.05 99.05 1.94e-68 REF NP_001004208 "calcyclin-binding protein [Rattus norvegicus]" 100.00 229 99.05 99.05 1.94e-68 REF NP_033916 "calcyclin-binding protein [Mus musculus]" 100.00 229 100.00 100.00 4.82e-69 REF XP_002928087 "PREDICTED: calcyclin-binding protein-like [Ailuropoda melanoleuca]" 100.00 230 97.14 99.05 1.25e-67 REF XP_003130369 "PREDICTED: calcyclin-binding protein isoform X1 [Sus scrofa]" 100.00 230 98.10 99.05 3.67e-68 REF XP_003497720 "PREDICTED: calcyclin-binding protein isoform X2 [Cricetulus griseus]" 100.00 184 100.00 100.00 5.97e-69 SP Q6AYK6 "RecName: Full=Calcyclin-binding protein; Short=CacyBP [Rattus norvegicus]" 100.00 229 99.05 99.05 1.94e-68 SP Q9CXW3 "RecName: Full=Calcyclin-binding protein; Short=CacyBP; AltName: Full=Siah-interacting protein [Mus musculus]" 100.00 229 100.00 100.00 4.82e-69 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $SIP_(74-178) 'house mouse' 10090 Eukaryota Metazoa Mus musculus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $SIP_(74-178) 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET28 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 $SIP_(74-178) 1.0 mM '[U-100% 13C; U-100% 15N]' NaPi 20 mM . NaCl 50 mM . DTT 5 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 2000 loop_ _Task analysis processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1H-13C_CT-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C CT-HSQC' _Sample_label . save_ save_3D-HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-HNCO _Sample_label . save_ save_3D-HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-HNCACB _Sample_label . save_ save_3D-CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-CBCA(CO)NH _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C CT-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Exp_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.2 pH temperature 303 1 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 . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_CSR_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $Sample_1 stop_ _Sample_conditions_label $Exp_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'SIP CS-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 . 1 VAL N N 129.17 0.03 1 2 . 1 VAL CA C 61.55 0.50 1 3 . 1 VAL CB C 32.73 0.50 1 4 . 1 VAL H H 8.88 0.02 1 5 . 1 VAL C C 174.93 0.50 1 6 . 2 LYS N N 128.00 0.03 1 7 . 2 LYS CA C 55.65 0.50 1 8 . 2 LYS CB C 32.52 0.50 1 9 . 2 LYS H H 8.42 0.02 1 10 . 2 LYS C C 177.12 0.50 1 11 . 3 ILE N N 127.38 0.03 1 12 . 3 ILE CA C 61.57 0.50 1 13 . 3 ILE CB C 38.85 0.50 1 14 . 3 ILE H H 8.67 0.02 1 15 . 3 ILE C C 175.95 0.50 1 16 . 4 SER N N 120.25 0.03 1 17 . 4 SER CA C 58.40 0.50 1 18 . 4 SER CB C 64.76 0.50 1 19 . 4 SER H H 8.73 0.02 1 20 . 4 SER C C 173.39 0.50 1 21 . 5 ASN N N 120.73 0.03 1 22 . 5 ASN CA C 52.93 0.50 1 23 . 5 ASN CB C 40.22 0.50 1 24 . 5 ASN H H 7.81 0.02 1 25 . 5 ASN C C 173.00 0.50 1 26 . 6 TYR N N 117.92 0.03 1 27 . 6 TYR CA C 56.36 0.50 1 28 . 6 TYR CB C 39.78 0.50 1 29 . 6 TYR H H 7.59 0.02 1 30 . 6 TYR C C 173.80 0.50 1 31 . 7 GLY N N 108.19 0.03 1 32 . 7 GLY CA C 43.65 0.50 1 33 . 7 GLY H H 8.59 0.02 1 34 . 7 GLY C C 172.37 0.50 1 35 . 8 TRP N N 118.59 0.03 1 36 . 8 TRP CA C 56.33 0.50 1 37 . 8 TRP CB C 32.06 0.50 1 38 . 8 TRP H H 8.74 0.02 1 39 . 8 TRP C C 173.68 0.50 1 40 . 9 ASP N N 120.99 0.03 1 41 . 9 ASP CA C 52.96 0.50 1 42 . 9 ASP CB C 42.04 0.50 1 43 . 9 ASP H H 9.67 0.02 1 44 . 9 ASP C C 173.69 0.50 1 45 . 10 GLN N N 112.02 0.03 1 46 . 10 GLN CA C 54.29 0.50 1 47 . 10 GLN CB C 33.66 0.50 1 48 . 10 GLN H H 8.41 0.02 1 49 . 10 GLN C C 172.80 0.50 1 50 . 11 SER N N 118.25 0.03 1 51 . 11 SER CA C 54.99 0.50 1 52 . 11 SER CB C 67.23 0.50 1 53 . 11 SER H H 9.54 0.02 1 54 . 11 SER C C 174.31 0.50 1 55 . 12 ASP N N 119.48 0.03 1 56 . 12 ASP CA C 57.46 0.50 1 57 . 12 ASP CB C 39.54 0.50 1 58 . 12 ASP H H 8.82 0.02 1 59 . 12 ASP C C 176.82 0.50 1 60 . 13 LYS N N 114.30 0.03 1 61 . 13 LYS CA C 57.01 0.50 1 62 . 13 LYS CB C 36.34 0.50 1 63 . 13 LYS H H 7.66 0.02 1 64 . 13 LYS C C 175.50 0.50 1 65 . 14 PHE N N 115.80 0.03 1 66 . 14 PHE CA C 56.78 0.50 1 67 . 14 PHE CB C 43.84 0.50 1 68 . 14 PHE H H 7.50 0.02 1 69 . 14 PHE C C 175.03 0.50 1 70 . 15 VAL N N 123.04 0.03 1 71 . 15 VAL CA C 63.16 0.50 1 72 . 15 VAL CB C 32.98 0.50 1 73 . 15 VAL H H 9.11 0.02 1 74 . 15 VAL C C 173.86 0.50 1 75 . 16 LYS N N 128.26 0.03 1 76 . 16 LYS CA C 54.55 0.50 1 77 . 16 LYS CB C 33.87 0.50 1 78 . 16 LYS H H 8.99 0.02 1 79 . 16 LYS C C 173.83 0.50 1 80 . 17 ILE N N 123.28 0.03 1 81 . 17 ILE CA C 60.42 0.50 1 82 . 17 ILE CB C 39.75 0.50 1 83 . 17 ILE H H 8.67 0.02 1 84 . 17 ILE C C 174.14 0.50 1 85 . 18 TYR N N 125.44 0.03 1 86 . 18 TYR CA C 56.57 0.50 1 87 . 18 TYR CB C 39.55 0.50 1 88 . 18 TYR H H 9.05 0.02 1 89 . 18 TYR C C 175.66 0.50 1 90 . 19 ILE N N 126.94 0.03 1 91 . 19 ILE CA C 60.59 0.50 1 92 . 19 ILE CB C 40.91 0.50 1 93 . 19 ILE H H 9.23 0.02 1 94 . 19 ILE C C 175.01 0.50 1 95 . 20 THR N N 126.29 0.03 1 96 . 20 THR CA C 62.70 0.50 1 97 . 20 THR CB C 69.06 0.50 1 98 . 20 THR H H 8.73 0.02 1 99 . 20 THR C C 173.55 0.50 1 100 . 21 LEU N N 131.74 0.03 1 101 . 21 LEU CA C 53.40 0.50 1 102 . 21 LEU CB C 44.09 0.50 1 103 . 21 LEU H H 8.09 0.02 1 104 . 21 LEU C C 174.17 0.50 1 105 . 22 THR N N 123.77 0.03 1 106 . 22 THR CA C 64.97 0.50 1 107 . 22 THR CB C 68.39 0.50 1 108 . 22 THR H H 8.35 0.02 1 109 . 22 THR C C 175.79 0.50 1 110 . 23 GLY N N 113.30 0.03 1 111 . 23 GLY CA C 45.44 0.50 1 112 . 23 GLY H H 9.82 0.02 1 113 . 23 GLY C C 177.35 0.50 1 114 . 24 VAL N N 121.83 0.03 1 115 . 24 VAL CA C 64.52 0.50 1 116 . 24 VAL CB C 30.91 0.50 1 117 . 24 VAL H H 8.03 0.02 1 118 . 24 VAL C C 173.67 0.50 1 119 . 25 HIS N N 118.03 0.03 1 120 . 25 HIS CA C 57.23 0.50 1 121 . 25 HIS CB C 28.66 0.50 1 122 . 25 HIS H H 8.66 0.02 1 123 . 25 HIS C C 175.47 0.50 1 124 . 26 GLN N N 118.51 0.03 1 125 . 26 GLN CA C 55.21 0.50 1 126 . 26 GLN CB C 28.67 0.50 1 127 . 26 GLN H H 7.37 0.02 1 128 . 26 GLN C C 176.34 0.50 1 129 . 27 VAL N N 116.64 0.03 1 130 . 27 VAL CA C 59.28 0.50 1 131 . 27 VAL CB C 31.15 0.50 1 132 . 27 VAL H H 6.84 0.02 1 133 . 28 PRO CA C 63.37 0.50 1 134 . 28 PRO CB C 32.03 0.50 1 135 . 28 PRO C C 177.97 0.50 1 136 . 29 THR N N 119.08 0.03 1 137 . 29 THR CA C 65.88 0.50 1 138 . 29 THR CB C 68.61 0.50 1 139 . 29 THR H H 8.40 0.02 1 140 . 29 THR C C 176.87 0.50 1 141 . 30 GLU N N 119.77 0.03 1 142 . 30 GLU CA C 57.96 0.50 1 143 . 30 GLU CB C 27.99 0.50 1 144 . 30 GLU H H 9.24 0.02 1 145 . 30 GLU C C 176.50 0.50 1 146 . 31 ASN N N 120.07 0.03 1 147 . 31 ASN CA C 53.16 0.50 1 148 . 31 ASN CB C 37.51 0.50 1 149 . 31 ASN H H 8.25 0.02 1 150 . 31 ASN C C 173.67 0.50 1 151 . 32 VAL N N 122.22 0.03 1 152 . 32 VAL CA C 62.25 0.50 1 153 . 32 VAL CB C 30.91 0.50 1 154 . 32 VAL H H 7.49 0.02 1 155 . 32 VAL C C 174.06 0.50 1 156 . 33 GLN N N 125.22 0.03 1 157 . 33 GLN CA C 54.08 0.50 1 158 . 33 GLN CB C 30.90 0.50 1 159 . 33 GLN H H 8.90 0.02 1 160 . 33 GLN C C 174.78 0.50 1 161 . 34 VAL N N 123.82 0.03 1 162 . 34 VAL CA C 59.50 0.50 1 163 . 34 VAL CB C 34.55 0.50 1 164 . 34 VAL H H 8.44 0.02 1 165 . 34 VAL C C 173.55 0.50 1 166 . 35 HIS N N 125.47 0.03 1 167 . 35 HIS CA C 53.63 0.50 1 168 . 35 HIS CB C 30.69 0.50 1 169 . 35 HIS H H 8.40 0.02 1 170 . 35 HIS C C 172.82 0.50 1 171 . 36 PHE N N 123.20 0.03 1 172 . 36 PHE CA C 57.71 0.50 1 173 . 36 PHE CB C 43.40 0.50 1 174 . 36 PHE H H 8.83 0.02 1 175 . 36 PHE C C 176.02 0.50 1 176 . 37 THR N N 112.54 0.03 1 177 . 37 THR CA C 61.29 0.50 1 178 . 37 THR CB C 71.33 0.50 1 179 . 37 THR H H 8.80 0.02 1 180 . 37 THR C C 173.33 0.50 1 181 . 38 GLU N N 115.17 0.03 1 182 . 38 GLU CA C 59.27 0.50 1 183 . 38 GLU CB C 30.03 0.50 1 184 . 38 GLU H H 8.44 0.02 1 185 . 38 GLU C C 175.97 0.50 1 186 . 39 ARG N N 112.13 0.03 1 187 . 39 ARG CA C 52.91 0.50 1 188 . 39 ARG CB C 32.72 0.50 1 189 . 39 ARG H H 7.50 0.02 1 190 . 39 ARG C C 174.46 0.50 1 191 . 40 SER N N 115.85 0.03 1 192 . 40 SER CA C 57.91 0.50 1 193 . 40 SER CB C 68.16 0.50 1 194 . 40 SER H H 7.67 0.02 1 195 . 40 SER C C 172.13 0.50 1 196 . 41 PHE N N 112.00 0.03 1 197 . 41 PHE CA C 56.89 0.50 1 198 . 41 PHE CB C 43.41 0.50 1 199 . 41 PHE H H 8.02 0.02 1 200 . 41 PHE C C 175.25 0.50 1 201 . 42 ASP N N 118.46 0.03 1 202 . 42 ASP CA C 56.91 0.50 1 203 . 42 ASP CB C 43.84 0.50 1 204 . 42 ASP H H 8.32 0.02 1 205 . 42 ASP C C 173.55 0.50 1 206 . 43 LEU N N 125.56 0.03 1 207 . 43 LEU CA C 52.73 0.50 1 208 . 43 LEU CB C 45.46 0.50 1 209 . 43 LEU H H 9.14 0.02 1 210 . 43 LEU C C 174.39 0.50 1 211 . 44 LEU N N 131.41 0.03 1 212 . 44 LEU CA C 53.63 0.50 1 213 . 44 LEU CB C 45.44 0.50 1 214 . 44 LEU H H 9.20 0.02 1 215 . 44 LEU C C 174.46 0.50 1 216 . 45 VAL N N 127.03 0.03 1 217 . 45 VAL CA C 60.73 0.50 1 218 . 45 VAL CB C 33.43 0.50 1 219 . 45 VAL H H 9.27 0.02 1 220 . 45 VAL C C 175.15 0.50 1 221 . 46 LYS N N 126.70 0.03 1 222 . 46 LYS CA C 54.98 0.50 1 223 . 46 LYS CB C 34.10 0.50 1 224 . 46 LYS H H 8.76 0.02 1 225 . 46 LYS C C 171.81 0.50 1 226 . 47 ASN N N 118.47 0.03 1 227 . 47 ASN CA C 53.33 0.50 1 228 . 47 ASN CB C 36.83 0.50 1 229 . 47 ASN H H 8.32 0.02 1 230 . 47 ASN C C 173.28 0.50 1 231 . 48 LEU N N 122.01 0.03 1 232 . 48 LEU CA C 53.40 0.50 1 233 . 48 LEU CB C 41.57 0.50 1 234 . 48 LEU H H 8.84 0.02 1 235 . 48 LEU C C 175.65 0.50 1 236 . 49 ASN N N 126.85 0.03 1 237 . 49 ASN CA C 53.83 0.50 1 238 . 49 ASN CB C 37.50 0.50 1 239 . 49 ASN H H 9.28 0.02 1 240 . 49 ASN C C 175.38 0.50 1 241 . 50 GLY N N 125.59 0.03 1 242 . 50 GLY CA C 45.43 0.50 1 243 . 50 GLY H H 7.79 0.02 1 244 . 50 GLY C C 173.68 0.50 1 245 . 51 LYS N N 119.92 0.03 1 246 . 51 LYS CA C 54.30 0.50 1 247 . 51 LYS CB C 35.91 0.50 1 248 . 51 LYS H H 7.42 0.02 1 249 . 51 LYS C C 173.46 0.50 1 250 . 52 ASN N N 117.18 0.03 1 251 . 52 ASN CA C 50.44 0.50 1 252 . 52 ASN CB C 40.01 0.50 1 253 . 52 ASN H H 8.07 0.02 1 254 . 52 ASN C C 174.15 0.50 1 255 . 53 TYR N N 120.58 0.03 1 256 . 53 TYR CA C 56.78 0.50 1 257 . 53 TYR CB C 42.04 0.50 1 258 . 53 TYR H H 9.23 0.02 1 259 . 53 TYR C C 174.85 0.50 1 260 . 54 SER N N 115.46 0.03 1 261 . 54 SER CA C 55.44 0.50 1 262 . 54 SER CB C 66.33 0.50 1 263 . 54 SER H H 8.82 0.02 1 264 . 54 SER C C 173.13 0.50 1 265 . 55 MET N N 124.60 0.03 1 266 . 55 MET CA C 56.12 0.50 1 267 . 55 MET CB C 37.72 0.50 1 268 . 55 MET H H 8.57 0.02 1 269 . 55 MET C C 172.85 0.50 1 270 . 56 ILE N N 126.42 0.03 1 271 . 56 ILE CA C 60.22 0.50 1 272 . 56 ILE CB C 40.90 0.50 1 273 . 56 ILE H H 8.22 0.02 1 274 . 56 ILE C C 174.86 0.50 1 275 . 57 VAL N N 128.88 0.03 1 276 . 57 VAL CA C 61.78 0.50 1 277 . 57 VAL CB C 32.05 0.50 1 278 . 57 VAL H H 7.76 0.02 1 279 . 57 VAL C C 173.29 0.50 1 280 . 58 ASN N N 123.12 0.03 1 281 . 58 ASN CA C 50.88 0.50 1 282 . 58 ASN CB C 40.91 0.50 1 283 . 58 ASN H H 7.94 0.02 1 284 . 58 ASN C C 174.16 0.50 1 285 . 59 ASN N N 115.01 0.03 1 286 . 59 ASN CA C 53.60 0.50 1 287 . 59 ASN CB C 37.03 0.50 1 288 . 59 ASN H H 8.29 0.02 1 289 . 59 ASN C C 174.61 0.50 1 290 . 60 LEU N N 118.25 0.03 1 291 . 60 LEU CA C 55.97 0.50 1 292 . 60 LEU CB C 42.25 0.50 1 293 . 60 LEU H H 8.27 0.02 1 294 . 60 LEU C C 177.98 0.50 1 295 . 61 LEU N N 122.60 0.03 1 296 . 61 LEU CA C 58.63 0.50 1 297 . 61 LEU CB C 42.48 0.50 1 298 . 61 LEU H H 7.91 0.02 1 299 . 61 LEU C C 175.80 0.50 1 300 . 62 LYS N N 111.84 0.03 1 301 . 62 LYS CA C 51.14 0.50 1 302 . 62 LYS CB C 33.88 0.50 1 303 . 62 LYS H H 5.55 0.02 1 304 . 63 PRO CA C 62.26 0.50 1 305 . 63 PRO CB C 32.74 0.50 1 306 . 63 PRO C C 177.12 0.50 1 307 . 64 ILE N N 117.72 0.03 1 308 . 64 ILE CA C 58.88 0.50 1 309 . 64 ILE CB C 41.35 0.50 1 310 . 64 ILE H H 9.03 0.02 1 311 . 64 ILE C C 175.34 0.50 1 312 . 65 SER N N 114.39 0.03 1 313 . 65 SER CA C 55.46 0.50 1 314 . 65 SER CB C 62.69 0.50 1 315 . 65 SER H H 8.49 0.02 1 316 . 65 SER C C 176.18 0.50 1 317 . 66 VAL N N 132.03 0.03 1 318 . 66 VAL CA C 66.81 0.50 1 319 . 66 VAL CB C 31.61 0.50 1 320 . 66 VAL H H 8.78 0.02 1 321 . 66 VAL C C 178.07 0.50 1 322 . 67 GLU N N 117.62 0.03 1 323 . 67 GLU CA C 58.85 0.50 1 324 . 67 GLU CB C 28.42 0.50 1 325 . 67 GLU H H 9.06 0.02 1 326 . 67 GLU C C 177.12 0.50 1 327 . 68 SER N N 111.77 0.03 1 328 . 68 SER CA C 57.24 0.50 1 329 . 68 SER CB C 63.83 0.50 1 330 . 68 SER H H 6.89 0.02 1 331 . 68 SER C C 173.92 0.50 1 332 . 69 SER N N 120.94 0.03 1 333 . 69 SER CA C 59.96 0.50 1 334 . 69 SER CB C 61.57 0.50 1 335 . 69 SER H H 6.86 0.02 1 336 . 69 SER C C 172.55 0.50 1 337 . 70 SER N N 118.05 0.03 1 338 . 70 SER CA C 57.92 0.50 1 339 . 70 SER CB C 64.51 0.50 1 340 . 70 SER H H 9.15 0.02 1 341 . 70 SER C C 171.80 0.50 1 342 . 71 LYS N N 115.79 0.03 1 343 . 71 LYS CA C 53.60 0.50 1 344 . 71 LYS CB C 35.48 0.50 1 345 . 71 LYS H H 8.33 0.02 1 346 . 71 LYS C C 174.24 0.50 1 347 . 72 LYS N N 122.35 0.03 1 348 . 72 LYS CA C 54.96 0.50 1 349 . 72 LYS CB C 36.57 0.50 1 350 . 72 LYS H H 9.33 0.02 1 351 . 72 LYS C C 173.53 0.50 1 352 . 73 VAL N N 123.07 0.03 1 353 . 73 VAL CA C 61.43 0.50 1 354 . 73 VAL CB C 33.64 0.50 1 355 . 73 VAL H H 8.45 0.02 1 356 . 73 VAL C C 175.64 0.50 1 357 . 74 LYS N N 127.83 0.03 1 358 . 74 LYS CA C 53.85 0.50 1 359 . 74 LYS CB C 35.01 0.50 1 360 . 74 LYS H H 8.93 0.02 1 361 . 74 LYS C C 175.08 0.50 1 362 . 75 THR N N 116.50 0.03 1 363 . 75 THR CA C 65.18 0.50 1 364 . 75 THR CB C 67.91 0.50 1 365 . 75 THR H H 7.78 0.02 1 366 . 75 THR C C 176.19 0.50 1 367 . 76 ASP N N 128.53 0.03 1 368 . 76 ASP CA C 57.00 0.50 1 369 . 76 ASP CB C 40.69 0.50 1 370 . 76 ASP H H 9.63 0.02 1 371 . 76 ASP C C 174.11 0.50 1 372 . 77 THR N N 115.81 0.03 1 373 . 77 THR CA C 62.28 0.50 1 374 . 77 THR CB C 73.17 0.50 1 375 . 77 THR H H 8.02 0.02 1 376 . 77 THR C C 172.30 0.50 1 377 . 78 VAL N N 126.41 0.03 1 378 . 78 VAL CA C 61.79 0.50 1 379 . 78 VAL CB C 33.63 0.50 1 380 . 78 VAL H H 9.13 0.02 1 381 . 78 VAL C C 173.28 0.50 1 382 . 79 ILE N N 127.86 0.03 1 383 . 79 ILE CA C 59.53 0.50 1 384 . 79 ILE CB C 39.55 0.50 1 385 . 79 ILE H H 8.99 0.02 1 386 . 79 ILE C C 175.04 0.50 1 387 . 80 ILE N N 128.46 0.03 1 388 . 80 ILE CA C 59.53 0.50 1 389 . 80 ILE CB C 37.05 0.50 1 390 . 80 ILE H H 9.22 0.02 1 391 . 80 ILE C C 174.16 0.50 1 392 . 81 LEU N N 128.70 0.03 1 393 . 81 LEU CA C 53.64 0.50 1 394 . 81 LEU CB C 41.58 0.50 1 395 . 81 LEU H H 8.64 0.02 1 396 . 81 LEU C C 175.01 0.50 1 397 . 82 CYS N N 121.17 0.03 1 398 . 82 CYS CA C 56.81 0.50 1 399 . 82 CYS CB C 27.53 0.50 1 400 . 82 CYS H H 8.92 0.02 1 401 . 82 CYS C C 174.15 0.50 1 402 . 83 ARG N N 129.24 0.03 1 403 . 83 ARG CA C 54.28 0.50 1 404 . 83 ARG CB C 29.76 0.50 1 405 . 83 ARG H H 8.59 0.02 1 406 . 83 ARG C C 175.03 0.50 1 407 . 84 LYS N N 130.33 0.03 1 408 . 84 LYS CA C 58.18 0.50 1 409 . 84 LYS CB C 33.66 0.50 1 410 . 84 LYS H H 8.35 0.02 1 411 . 84 LYS C C 176.15 0.50 1 412 . 85 LYS N N 124.08 0.03 1 413 . 85 LYS CA C 59.29 0.50 1 414 . 85 LYS CB C 32.29 0.50 1 415 . 85 LYS H H 7.73 0.02 1 416 . 85 LYS C C 176.43 0.50 1 417 . 86 ALA N N 121.64 0.03 1 418 . 86 ALA CA C 49.78 0.50 1 419 . 86 ALA CB C 17.55 0.50 1 420 . 86 ALA H H 8.06 0.02 1 421 . 86 ALA C C 176.41 0.50 1 422 . 87 GLU N N 123.98 0.03 1 423 . 87 GLU CA C 56.36 0.50 1 424 . 87 GLU CB C 29.57 0.50 1 425 . 87 GLU H H 8.28 0.02 1 426 . 87 GLU C C 176.65 0.50 1 427 . 88 ASN N N 115.07 0.03 1 428 . 88 ASN CA C 54.55 0.50 1 429 . 88 ASN CB C 36.59 0.50 1 430 . 88 ASN H H 9.20 0.02 1 431 . 88 ASN C C 174.31 0.50 1 432 . 89 THR N N 113.09 0.03 1 433 . 89 THR CA C 61.35 0.50 1 434 . 89 THR CB C 70.64 0.50 1 435 . 89 THR H H 6.98 0.02 1 436 . 89 THR C C 173.53 0.50 1 437 . 90 ARG N N 131.88 0.03 1 438 . 90 ARG CA C 56.12 0.50 1 439 . 90 ARG CB C 30.48 0.50 1 440 . 90 ARG H H 9.05 0.02 1 441 . 90 ARG C C 176.27 0.50 1 442 . 91 TRP N N 131.31 0.03 1 443 . 91 TRP CA C 56.33 0.50 1 444 . 91 TRP CB C 28.44 0.50 1 445 . 91 TRP H H 10.06 0.02 1 446 . 91 TRP C C 176.80 0.50 1 447 . 92 ASP N N 123.47 0.03 1 448 . 92 ASP CA C 55.89 0.50 1 449 . 92 ASP CB C 40.47 0.50 1 450 . 92 ASP H H 9.03 0.02 1 451 . 92 ASP C C 174.24 0.50 1 452 . 93 TYR N N 115.22 0.03 1 453 . 93 TYR CA C 55.66 0.50 1 454 . 93 TYR CB C 42.96 0.50 1 455 . 93 TYR H H 7.43 0.02 1 456 . 93 TYR C C 172.90 0.50 1 457 . 94 LEU N N 120.04 0.03 1 458 . 94 LEU CA C 57.02 0.50 1 459 . 94 LEU CB C 41.34 0.50 1 460 . 94 LEU H H 8.27 0.02 1 461 . 94 LEU C C 177.19 0.50 1 462 . 95 THR N N 124.69 0.03 1 463 . 95 THR CA C 57.93 0.50 1 464 . 95 THR CB C 72.70 0.50 1 465 . 95 THR H H 6.98 0.02 1 stop_ save_