data_7406 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR resonance assignment of the Ccc2ab protein ; _BMRB_accession_number 7406 _BMRB_flat_file_name bmr7406.str _Entry_type original _Submission_date 2007-09-06 _Accession_date 2007-09-06 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'NMR resonance assignment of the two soluble Nterminal domains of the Ccc2 protein in the apo and Cu(i)-binded form' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Banci Lucia . . 2 Bertini Ivano . . 3 Chasapis Christos T. . 4 Rosato Antonio . . 5 Tenroi Leonardo . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 128 "13C chemical shifts" 247 "15N chemical shifts" 128 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-11-08 update BMRB 'delete the outliers of 64 PHE CG 7.0, 64 PHE CZ 7.1, 46 TYR CG 6.8, 46 TYR CZ 6.5' 2008-06-25 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15461 'ccc2 (free form)' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Interaction of the two soluble metal-binding domains of yeast Ccc2 with copper(I)-Atx1.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17961510 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Banci L. . . 2 Bertini I. . . 3 Chasapis C. T. . 4 Rosato A. . . 5 Tenori L. . . stop_ _Journal_abbreviation 'Biochem. Biophys. Res. Commun.' _Journal_volume 364 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 645 _Page_last 649 _Year 2007 _Details . loop_ _Keyword Atx1 Ccc2 coppper 'metal homeostasis' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name ccc2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label ccc2 $Ccc2 CU1 $CU1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic yes _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Ccc2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Ccc2 _Molecular_mass . _Mol_thiol_state 'free and other bound' loop_ _Biological_function 'Yeast Ccc2 is a P-type ATPase responsible for transport of copper(I) from the cytosol to the trans-Golgi network' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 150 _Mol_residue_sequence ; MREVILAVHGMTCSACTNTI NTQLRALKGVTKCDISLVTN ECQVTYDNEVTADSIKEIIE DCGFDCEILRDSEITAISTK EGLLSVQGMTCGSCVSTVTK QVEGIEGVESVVVSLVTEEC HVIYEPSKTTLETAREMIED CGFDSNIIMD ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ARG 3 GLU 4 VAL 5 ILE 6 LEU 7 ALA 8 VAL 9 HIS 10 GLY 11 MET 12 THR 13 CYS 14 SER 15 ALA 16 CYS 17 THR 18 ASN 19 THR 20 ILE 21 ASN 22 THR 23 GLN 24 LEU 25 ARG 26 ALA 27 LEU 28 LYS 29 GLY 30 VAL 31 THR 32 LYS 33 CYS 34 ASP 35 ILE 36 SER 37 LEU 38 VAL 39 THR 40 ASN 41 GLU 42 CYS 43 GLN 44 VAL 45 THR 46 TYR 47 ASP 48 ASN 49 GLU 50 VAL 51 THR 52 ALA 53 ASP 54 SER 55 ILE 56 LYS 57 GLU 58 ILE 59 ILE 60 GLU 61 ASP 62 CYS 63 GLY 64 PHE 65 ASP 66 CYS 67 GLU 68 ILE 69 LEU 70 ARG 71 ASP 72 SER 73 GLU 74 ILE 75 THR 76 ALA 77 ILE 78 SER 79 THR 80 LYS 81 GLU 82 GLY 83 LEU 84 LEU 85 SER 86 VAL 87 GLN 88 GLY 89 MET 90 THR 91 CYS 92 GLY 93 SER 94 CYS 95 VAL 96 SER 97 THR 98 VAL 99 THR 100 LYS 101 GLN 102 VAL 103 GLU 104 GLY 105 ILE 106 GLU 107 GLY 108 VAL 109 GLU 110 SER 111 VAL 112 VAL 113 VAL 114 SER 115 LEU 116 VAL 117 THR 118 GLU 119 GLU 120 CYS 121 HIS 122 VAL 123 ILE 124 TYR 125 GLU 126 PRO 127 SER 128 LYS 129 THR 130 THR 131 LEU 132 GLU 133 THR 134 ALA 135 ARG 136 GLU 137 MET 138 ILE 139 GLU 140 ASP 141 CYS 142 GLY 143 PHE 144 ASP 145 SER 146 ASN 147 ILE 148 ILE 149 MET 150 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-12 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 BMRB 15461 Ccc2 100.00 150 100.00 100.00 1.59e-100 stop_ save_ ############# # Ligands # ############# save_CU1 _Saveframe_category ligand _Mol_type non-polymer _Name_common "CU1 (COPPER (I) ION)" _BMRB_code . _PDB_code CU1 _Molecular_mass 63.546 _Mol_charge 1 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Aug 20 20:07:43 2007 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CU CU CU N 1 . ? 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 $Ccc2 'baker's yeast' 4932 Eukaryota Fungi Saccharomyces cerevisiae 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 _Details $Ccc2 'recombinant technology' . Escherichia coli . 'pET 20b(+)' 'A DNA segment corresponding to residues 1-150 of Ccc2 (Ccc2ab hereafter) was amplified by PCR and cloned into pET 20b(+) between the NcoI and XhoI restriction sites. The construct of two domains Ccc2ab has been expressed in Escherichia coli BL21(DE 3) in minimal medium cultures' 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 $Ccc2 0.2-0.5 mM '[U-100% 13C; U-100% 15N]' $CU1 . mM . stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details 'conventional multi dimensional NMR techniques based on triple resonance' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.00 . pH pressure 1 . atm temperature 298 . K viscosity 100 . mM stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 internal indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0 internal 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_Cu(I)_Ccc2ab _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $TOPSPIN stop_ loop_ _Experiment_label '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name ccc2 _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 2 ARG H H 8.15 0.02 1 2 2 2 ARG CA C 53.9 0.3 1 3 2 2 ARG CB C 27.9 0.3 1 4 2 2 ARG N N 120.0 0.3 1 5 3 3 GLU H H 8.67 0.02 1 6 3 3 GLU CA C 51.7 0.3 1 7 3 3 GLU CB C 31.0 0.3 1 8 3 3 GLU N N 117.7 0.3 1 9 4 4 VAL H H 9.45 0.02 1 10 4 4 VAL CA C 54.9 0.3 1 11 4 4 VAL CB C 31.1 0.3 1 12 4 4 VAL N N 125.8 0.3 1 13 5 5 ILE H H 8.79 0.02 1 14 5 5 ILE CA C 56.6 0.3 1 15 5 5 ILE CB C 36.0 0.3 1 16 5 5 ILE N N 126.5 0.3 1 17 6 6 LEU H H 9.39 0.02 1 18 6 6 LEU CA C 51.8 0.3 1 19 6 6 LEU CB C 41.4 0.3 1 20 6 6 LEU N N 125.4 0.3 1 21 7 7 ALA H H 8.70 0.02 1 22 7 7 ALA CA C 48.5 0.3 1 23 7 7 ALA CB C 17.0 0.3 1 24 7 7 ALA N N 125.0 0.3 1 25 8 8 VAL H H 8.08 0.02 1 26 8 8 VAL CA C 58.6 0.3 1 27 8 8 VAL CB C 30.3 0.3 1 28 8 8 VAL N N 121.5 0.3 1 29 9 9 HIS H H 9.00 0.02 1 30 9 9 HIS CA C 52.0 0.3 1 31 9 9 HIS CB C 28.0 0.3 1 32 9 9 HIS N N 127.0 0.3 1 33 10 10 GLY H H 8.56 0.02 1 34 10 10 GLY CA C 42.7 0.3 1 35 10 10 GLY N N 109.2 0.3 1 36 11 11 MET H H 8.87 0.02 1 37 11 11 MET CA C 53.4 0.3 1 38 11 11 MET CB C 30.5 0.3 1 39 11 11 MET N N 119.7 0.3 1 40 12 12 THR H H 9.24 0.02 1 41 12 12 THR CA C 59.2 0.3 1 42 12 12 THR CB C 68.0 0.3 1 43 12 12 THR N N 114.0 0.3 1 44 15 15 ALA H H 8.51 0.02 1 45 15 15 ALA CA C 52.7 0.3 1 46 15 15 ALA CB C 15.0 0.3 1 47 15 15 ALA N N 126.4 0.3 1 48 16 16 CYS H H 7.73 0.02 1 49 16 16 CYS CA C 60.3 0.3 1 50 16 16 CYS CB C 27.2 0.3 1 51 16 16 CYS N N 120.1 0.3 1 52 17 17 THR H H 6.94 0.02 1 53 17 17 THR CA C 62.0 0.3 1 54 17 17 THR CB C 64.6 0.3 1 55 17 17 THR N N 106.7 0.3 1 56 19 19 THR H H 8.05 0.02 1 57 19 19 THR CA C 64.4 0.3 1 58 19 19 THR CB C 65.8 0.3 1 59 19 19 THR N N 119.5 0.3 1 60 20 20 ILE H H 7.26 0.02 1 61 20 20 ILE CA C 63.1 0.3 1 62 20 20 ILE CB C 35.8 0.3 1 63 20 20 ILE N N 120.0 0.3 1 64 21 21 ASN H H 8.33 0.02 1 65 21 21 ASN CA C 54.5 0.3 1 66 21 21 ASN CB C 36.9 0.3 1 67 21 21 ASN N N 116.9 0.3 1 68 22 22 THR H H 8.22 0.02 1 69 22 22 THR CA C 64.2 0.3 1 70 22 22 THR CB C 66.0 0.3 1 71 22 22 THR N N 112.9 0.3 1 72 23 23 GLN H H 7.66 0.02 1 73 23 23 GLN CA C 55.4 0.3 1 74 23 23 GLN CB C 25.4 0.3 1 75 23 23 GLN N N 118.6 0.3 1 76 24 24 LEU H H 8.34 0.02 1 77 24 24 LEU CA C 54.7 0.3 1 78 24 24 LEU CB C 39.3 0.3 1 79 24 24 LEU N N 118.1 0.3 1 80 25 25 ARG H H 8.13 0.02 1 81 25 25 ARG CA C 54.8 0.3 1 82 25 25 ARG CB C 25.7 0.3 1 83 25 25 ARG N N 113.9 0.3 1 84 26 26 ALA H H 6.88 0.02 1 85 26 26 ALA CA C 49.5 0.3 1 86 26 26 ALA CB C 15.9 0.3 1 87 26 26 ALA N N 118.8 0.3 1 88 27 27 LEU H H 7.35 0.02 1 89 27 27 LEU CA C 51.4 0.3 1 90 27 27 LEU CB C 38.8 0.3 1 91 27 27 LEU N N 122.3 0.3 1 92 28 28 LYS H H 8.35 0.02 1 93 28 28 LYS CA C 55.5 0.3 1 94 28 28 LYS CB C 27.4 0.3 1 95 28 28 LYS N N 128.4 0.3 1 96 29 29 GLY H H 8.37 0.02 1 97 29 29 GLY CA C 42.2 0.3 1 98 29 29 GLY N N 110.7 0.3 1 99 30 30 VAL H H 7.64 0.02 1 100 30 30 VAL CA C 60.9 0.3 1 101 30 30 VAL CB C 28.3 0.3 1 102 30 30 VAL N N 121.0 0.3 1 103 31 31 THR H H 8.95 0.02 1 104 31 31 THR CA C 59.6 0.3 1 105 31 31 THR CB C 66.7 0.3 1 106 31 31 THR N N 120.7 0.3 1 107 32 32 LYS H H 7.52 0.02 1 108 32 32 LYS CA C 53.9 0.3 1 109 32 32 LYS CB C 33.0 0.3 1 110 32 32 LYS N N 121.0 0.3 1 111 33 33 CYS H H 8.45 0.02 1 112 33 33 CYS CA C 55.0 0.3 1 113 33 33 CYS CB C 25.9 0.3 1 114 33 33 CYS N N 122.2 0.3 1 115 34 34 ASP H H 8.88 0.02 1 116 34 34 ASP CA C 51.0 0.3 1 117 34 34 ASP CB C 41.9 0.3 1 118 34 34 ASP N N 127.3 0.3 1 119 35 35 ILE H H 8.55 0.02 1 120 35 35 ILE CA C 57.6 0.3 1 121 35 35 ILE CB C 37.9 0.3 1 122 35 35 ILE N N 123.3 0.3 1 123 37 37 LEU H H 8.98 0.02 1 124 37 37 LEU CA C 53.0 0.3 1 125 37 37 LEU CB C 38.9 0.3 1 126 37 37 LEU N N 128.0 0.3 1 127 38 38 VAL H H 8.07 0.02 1 128 38 38 VAL CA C 62.2 0.3 1 129 38 38 VAL CB C 29.4 0.3 1 130 38 38 VAL N N 118.6 0.3 1 131 39 39 THR H H 7.36 0.02 1 132 39 39 THR CA C 58.5 0.3 1 133 39 39 THR CB C 67.0 0.3 1 134 39 39 THR N N 105.4 0.3 1 135 40 40 ASN H H 7.50 0.02 1 136 40 40 ASN CA C 52.8 0.3 1 137 40 40 ASN CB C 34.0 0.3 1 138 40 40 ASN N N 115.7 0.3 1 139 41 41 GLU H H 7.34 0.02 1 140 41 41 GLU CA C 51.6 0.3 1 141 41 41 GLU CB C 30.4 0.3 1 142 41 41 GLU N N 114.5 0.3 1 143 42 42 CYS H H 9.12 0.02 1 144 42 42 CYS CA C 53.4 0.3 1 145 42 42 CYS CB C 26.6 0.3 1 146 42 42 CYS N N 122.5 0.3 1 147 43 43 GLN H H 9.20 0.02 1 148 43 43 GLN CA C 51.6 0.3 1 149 43 43 GLN CB C 27.4 0.3 1 150 43 43 GLN N N 129.1 0.3 1 151 44 44 VAL H H 9.39 0.02 1 152 44 44 VAL CA C 58.2 0.3 1 153 44 44 VAL CB C 32.0 0.3 1 154 44 44 VAL N N 127.8 0.3 1 155 45 45 THR H H 8.67 0.02 1 156 45 45 THR CA C 58.9 0.3 1 157 45 45 THR CB C 66.6 0.3 1 158 45 45 THR N N 124.6 0.3 1 159 46 46 TYR H H 9.31 0.02 1 160 46 46 TYR CA C 52.8 0.3 1 161 46 46 TYR CB C 38.5 0.3 1 162 46 46 TYR N N 124.9 0.3 1 163 47 47 ASP H H 8.71 0.02 1 164 47 47 ASP CA C 49.5 0.3 1 165 47 47 ASP CB C 40.5 0.3 1 166 47 47 ASP N N 122.4 0.3 1 167 48 48 ASN H H 8.29 0.02 1 168 48 48 ASN CA C 52.6 0.3 1 169 48 48 ASN CB C 35.5 0.3 1 170 48 48 ASN N N 111.8 0.3 1 171 49 49 GLU H H 8.81 0.02 1 172 49 49 GLU CA C 55.3 0.3 1 173 49 49 GLU CB C 26.5 0.3 1 174 49 49 GLU N N 119.2 0.3 1 175 51 51 THR H H 6.97 0.02 1 176 51 51 THR CA C 56.3 0.3 1 177 51 51 THR CB C 69.9 0.3 1 178 51 51 THR N N 108.1 0.3 1 179 52 52 ALA H H 8.77 0.02 1 180 52 52 ALA CA C 52.4 0.3 1 181 52 52 ALA CB C 14.3 0.3 1 182 52 52 ALA N N 122.8 0.3 1 183 53 53 ASP H H 7.84 0.02 1 184 53 53 ASP CA C 54.7 0.3 1 185 53 53 ASP CB C 37.6 0.3 1 186 53 53 ASP N N 114.6 0.3 1 187 54 54 SER H H 7.73 0.02 1 188 54 54 SER CA C 58.9 0.3 1 189 54 54 SER CB C 59.6 0.3 1 190 54 54 SER N N 117.2 0.3 1 191 57 57 GLU H H 7.70 0.02 1 192 57 57 GLU CA C 56.6 0.3 1 193 57 57 GLU CB C 26.6 0.3 1 194 57 57 GLU N N 116.9 0.3 1 195 58 58 ILE H H 7.54 0.02 1 196 58 58 ILE CA C 60.7 0.3 1 197 58 58 ILE CB C 33.8 0.3 1 198 58 58 ILE N N 119.5 0.3 1 199 59 59 ILE H H 7.61 0.02 1 200 59 59 ILE CA C 64.6 0.3 1 201 59 59 ILE CB C 34.8 0.3 1 202 59 59 ILE N N 121.6 0.3 1 203 60 60 GLU H H 8.28 0.02 1 204 60 60 GLU CA C 56.2 0.3 1 205 60 60 GLU CB C 25.0 0.3 1 206 60 60 GLU N N 119.5 0.3 1 207 61 61 ASP H H 8.66 0.02 1 208 61 61 ASP CA C 54.1 0.3 1 209 61 61 ASP CB C 37.7 0.3 1 210 61 61 ASP N N 122.8 0.3 1 211 62 62 CYS H H 7.80 0.02 1 212 62 62 CYS CA C 58.5 0.3 1 213 62 62 CYS CB C 24.3 0.3 1 214 62 62 CYS N N 115.8 0.3 1 215 63 63 GLY H H 7.92 0.02 1 216 63 63 GLY CA C 41.7 0.3 1 217 63 63 GLY N N 105.1 0.3 1 218 64 64 PHE H H 7.09 0.02 1 219 64 64 PHE CA C 54.1 0.3 1 220 64 64 PHE CB C 38.1 0.3 1 221 64 64 PHE N N 119.2 0.3 1 222 65 65 ASP H H 8.02 0.02 1 223 65 65 ASP CA C 51.2 0.3 1 224 65 65 ASP CB C 39.3 0.3 1 225 65 65 ASP N N 120.6 0.3 1 226 66 66 CYS H H 9.06 0.02 1 227 66 66 CYS CA C 53.2 0.3 1 228 66 66 CYS CB C 29.3 0.3 1 229 66 66 CYS N N 116.4 0.3 1 230 67 67 GLU H H 8.34 0.02 1 231 67 67 GLU CA C 51.8 0.3 1 232 67 67 GLU CB C 30.6 0.3 1 233 67 67 GLU N N 116.5 0.3 1 234 68 68 ILE H H 9.05 0.02 1 235 68 68 ILE CA C 60.7 0.3 1 236 68 68 ILE CB C 35.4 0.3 1 237 68 68 ILE N N 124.0 0.3 1 238 69 69 LEU H H 9.46 0.02 1 239 69 69 LEU CA C 53.1 0.3 1 240 69 69 LEU CB C 39.4 0.3 1 241 69 69 LEU N N 129.5 0.3 1 242 70 70 ARG H H 7.52 0.02 1 243 70 70 ARG CA C 52.9 0.3 1 244 70 70 ARG CB C 30.3 0.3 1 245 70 70 ARG N N 116.1 0.3 1 246 71 71 ASP H H 8.31 0.02 1 247 71 71 ASP CA C 51.8 0.3 1 248 71 71 ASP CB C 42.2 0.3 1 249 71 71 ASP N N 123.8 0.3 1 250 72 72 SER H H 8.65 0.02 1 251 72 72 SER CA C 54.7 0.3 1 252 72 72 SER CB C 63.3 0.3 1 253 72 72 SER N N 118.7 0.3 1 254 73 73 GLU H H 8.58 0.02 1 255 73 73 GLU CA C 54.2 0.3 1 256 73 73 GLU CB C 27.7 0.3 1 257 73 73 GLU N N 121.7 0.3 1 258 74 74 ILE H H 8.21 0.02 1 259 74 74 ILE CA C 58.2 0.3 1 260 74 74 ILE CB C 30.2 0.3 1 261 74 74 ILE N N 123.8 0.3 1 262 75 75 THR H H 8.13 0.02 1 263 75 75 THR CA C 59.0 0.3 1 264 75 75 THR CB C 67.0 0.3 1 265 75 75 THR N N 118.2 0.3 1 266 76 76 ALA H H 8.20 0.02 1 267 76 76 ALA CA C 49.7 0.3 1 268 76 76 ALA CB C 16.3 0.3 1 269 76 76 ALA N N 126.7 0.3 1 270 77 77 ILE H H 8.00 0.02 1 271 77 77 ILE CA C 58.2 0.3 1 272 77 77 ILE CB C 35.7 0.3 1 273 77 77 ILE N N 120.0 0.3 1 274 78 78 SER H H 8.27 0.02 1 275 78 78 SER CA C 55.3 0.3 1 276 78 78 SER CB C 61.0 0.3 1 277 78 78 SER N N 120.5 0.3 1 278 79 79 THR H H 8.11 0.02 1 279 79 79 THR CA C 59.1 0.3 1 280 79 79 THR CB C 66.9 0.3 1 281 79 79 THR N N 116.3 0.3 1 282 81 81 GLU H H 8.52 0.02 1 283 81 81 GLU CA C 57.5 0.3 1 284 81 81 GLU CB C 27.0 0.3 1 285 81 81 GLU N N 123.6 0.3 1 286 82 82 GLY H H 8.25 0.02 1 287 82 82 GLY CA C 42.5 0.3 1 288 82 82 GLY N N 109.4 0.3 1 289 83 83 LEU H H 7.89 0.02 1 290 83 83 LEU CA C 52.5 0.3 1 291 83 83 LEU CB C 39.6 0.3 1 292 83 83 LEU N N 121.4 0.3 1 293 84 84 LEU H H 7.64 0.02 1 294 84 84 LEU CA C 53.9 0.3 1 295 84 84 LEU CB C 40.6 0.3 1 296 84 84 LEU N N 127.8 0.3 1 297 86 86 VAL H H 7.13 0.02 1 298 86 86 VAL CA C 62.3 0.3 1 299 86 86 VAL CB C 34.6 0.3 1 300 86 86 VAL N N 123.4 0.3 1 301 88 88 GLY H H 8.33 0.02 1 302 88 88 GLY CA C 42.4 0.3 1 303 88 88 GLY N N 111.0 0.3 1 304 89 89 MET H H 8.86 0.02 1 305 89 89 MET CA C 53.4 0.3 1 306 89 89 MET CB C 27.4 0.3 1 307 89 89 MET N N 119.6 0.3 1 308 90 90 THR H H 7.98 0.02 1 309 90 90 THR CA C 59.0 0.3 1 310 90 90 THR CB C 66.9 0.3 1 311 90 90 THR N N 116.7 0.3 1 312 91 91 CYS H H 8.19 0.02 1 313 91 91 CYS CA C 53.7 0.3 1 314 91 91 CYS CB C 27.1 0.3 1 315 91 91 CYS N N 123.7 0.3 1 316 92 92 GLY H H 8.48 0.02 1 317 92 92 GLY CA C 42.4 0.3 1 318 92 92 GLY N N 110.5 0.3 1 319 93 93 SER H H 7.80 0.02 1 320 93 93 SER CA C 59.1 0.3 1 321 93 93 SER CB C 61.0 0.3 1 322 93 93 SER N N 118.8 0.3 1 323 94 94 CYS H H 8.21 0.02 1 324 94 94 CYS CA C 57.8 0.3 1 325 94 94 CYS CB C 35.9 0.3 1 326 94 94 CYS N N 124.8 0.3 1 327 95 95 VAL H H 8.21 0.02 1 328 95 95 VAL CA C 59.5 0.3 1 329 95 95 VAL CB C 36.1 0.3 1 330 95 95 VAL N N 125.8 0.3 1 331 96 96 SER H H 7.85 0.02 1 332 96 96 SER CA C 57.1 0.3 1 333 96 96 SER CB C 61.7 0.3 1 334 96 96 SER N N 125.5 0.3 1 335 97 97 THR H H 8.11 0.02 1 336 97 97 THR CA C 59.1 0.3 1 337 97 97 THR CB C 66.8 0.3 1 338 97 97 THR N N 116.1 0.3 1 339 98 98 VAL H H 8.14 0.02 1 340 98 98 VAL CA C 59.6 0.3 1 341 98 98 VAL CB C 29.7 0.3 1 342 98 98 VAL N N 122.8 0.3 1 343 99 99 THR H H 8.25 0.02 1 344 99 99 THR CA C 58.8 0.3 1 345 99 99 THR CB C 66.9 0.3 1 346 99 99 THR N N 119.3 0.3 1 347 100 100 LYS H H 8.18 0.02 1 348 100 100 LYS CA C 53.7 0.3 1 349 100 100 LYS CB C 30.2 0.3 1 350 100 100 LYS N N 123.6 0.3 1 351 101 101 GLN H H 7.93 0.02 1 352 101 101 GLN CA C 55.2 0.3 1 353 101 101 GLN CB C 28.0 0.3 1 354 101 101 GLN N N 127.5 0.3 1 355 103 103 GLU H H 8.48 0.02 1 356 103 103 GLU CA C 53.8 0.3 1 357 103 103 GLU CB C 27.2 0.3 1 358 103 103 GLU N N 124.8 0.3 1 359 104 104 GLY H H 8.28 0.02 1 360 104 104 GLY CA C 42.6 0.3 1 361 104 104 GLY N N 109.6 0.3 1 362 105 105 ILE H H 7.84 0.02 1 363 105 105 ILE CA C 58.3 0.3 1 364 105 105 ILE CB C 35.7 0.3 1 365 105 105 ILE N N 119.5 0.3 1 366 106 106 GLU H H 8.59 0.02 1 367 106 106 GLU CA C 54.0 0.3 1 368 106 106 GLU CB C 27.0 0.3 1 369 106 106 GLU N N 124.7 0.3 1 370 107 107 GLY H H 8.35 0.02 1 371 107 107 GLY CA C 42.4 0.3 1 372 107 107 GLY N N 110.2 0.3 1 373 108 108 VAL H H 7.81 0.02 1 374 108 108 VAL CA C 59.4 0.3 1 375 108 108 VAL CB C 29.8 0.3 1 376 108 108 VAL N N 119.0 0.3 1 377 109 109 GLU H H 8.24 0.02 1 378 109 109 GLU CA C 54.9 0.3 1 379 109 109 GLU CB C 29.9 0.3 1 380 109 109 GLU N N 125.2 0.3 1 381 110 110 SER H H 8.26 0.02 1 382 110 110 SER CA C 55.3 0.3 1 383 110 110 SER CB C 61.0 0.3 1 384 110 110 SER N N 119.3 0.3 1 385 111 111 VAL H H 8.08 0.02 1 386 111 111 VAL CA C 59.5 0.3 1 387 111 111 VAL CB C 29.9 0.3 1 388 111 111 VAL N N 122.3 0.3 1 389 112 112 VAL H H 8.20 0.02 1 390 112 112 VAL CA C 59.5 0.3 1 391 112 112 VAL CB C 29.8 0.3 1 392 112 112 VAL N N 125.5 0.3 1 393 113 113 VAL H H 8.21 0.02 1 394 113 113 VAL CA C 59.6 0.3 1 395 113 113 VAL CB C 29.6 0.3 1 396 113 113 VAL N N 125.3 0.3 1 397 115 115 LEU H H 7.85 0.02 1 398 115 115 LEU CA C 58.1 0.3 1 399 115 115 LEU CB C 40.4 0.3 1 400 115 115 LEU N N 130.0 0.3 1 401 116 116 VAL H H 8.25 0.02 1 402 116 116 VAL CA C 58.8 0.3 1 403 116 116 VAL CB C 30.0 0.3 1 404 116 116 VAL N N 125.6 0.3 1 405 117 117 THR H H 8.24 0.02 1 406 117 117 THR CA C 58.8 0.3 1 407 117 117 THR CB C 66.8 0.3 1 408 117 117 THR N N 118.9 0.3 1 409 118 118 GLU H H 8.24 0.02 1 410 118 118 GLU CA C 53.5 0.3 1 411 118 118 GLU CB C 30.1 0.3 1 412 118 118 GLU N N 124.3 0.3 1 413 119 119 GLU H H 8.37 0.02 1 414 119 119 GLU CA C 53.0 0.3 1 415 119 119 GLU CB C 26.5 0.3 1 416 119 119 GLU N N 122.8 0.3 1 417 120 120 CYS H H 8.14 0.02 1 418 120 120 CYS CA C 60.4 0.3 1 419 120 120 CYS CB C 29.9 0.3 1 420 120 120 CYS N N 122.0 0.3 1 421 121 121 HIS H H 8.42 0.02 1 422 121 121 HIS CA C 53.7 0.3 1 423 121 121 HIS CB C 27.3 0.3 1 424 121 121 HIS N N 125.0 0.3 1 425 122 122 VAL H H 8.28 0.02 1 426 122 122 VAL CA C 60.3 0.3 1 427 122 122 VAL CB C 29.1 0.3 1 428 122 122 VAL N N 122.5 0.3 1 429 127 127 SER H H 8.10 0.02 1 430 127 127 SER CA C 59.0 0.3 1 431 127 127 SER CB C 66.8 0.3 1 432 127 127 SER N N 115.8 0.3 1 433 128 128 LYS H H 8.21 0.02 1 434 128 128 LYS CA C 53.8 0.3 1 435 128 128 LYS CB C 29.9 0.3 1 436 128 128 LYS N N 122.9 0.3 1 437 129 129 THR H H 8.08 0.02 1 438 129 129 THR CA C 58.7 0.3 1 439 129 129 THR CB C 66.9 0.3 1 440 129 129 THR N N 115.3 0.3 1 441 130 130 THR H H 8.13 0.02 1 442 130 130 THR CA C 59.0 0.3 1 443 130 130 THR CB C 66.8 0.3 1 444 130 130 THR N N 116.2 0.3 1 445 131 131 LEU H H 9.24 0.02 1 446 131 131 LEU CA C 52.8 0.3 1 447 131 131 LEU CB C 38.7 0.3 1 448 131 131 LEU N N 124.3 0.3 1 449 133 133 THR H H 8.01 0.02 1 450 133 133 THR CA C 59.1 0.3 1 451 133 133 THR CB C 66.8 0.3 1 452 133 133 THR N N 115.6 0.3 1 453 134 134 ALA H H 8.14 0.02 1 454 134 134 ALA CA C 49.7 0.3 1 455 134 134 ALA CB C 16.3 0.3 1 456 134 134 ALA N N 126.4 0.3 1 457 135 135 ARG H H 8.02 0.02 1 458 135 135 ARG CA C 54.1 0.3 1 459 135 135 ARG CB C 35.7 0.3 1 460 135 135 ARG N N 120.2 0.3 1 461 136 136 GLU H H 8.48 0.02 1 462 136 136 GLU CA C 58.4 0.3 1 463 136 136 GLU CB C 27.6 0.3 1 464 136 136 GLU N N 125.0 0.3 1 465 140 140 ASP H H 8.36 0.02 1 466 140 140 ASP CA C 52.4 0.3 1 467 140 140 ASP CB C 39.6 0.3 1 468 140 140 ASP N N 126.0 0.3 1 469 141 141 CYS H H 8.21 0.02 1 470 141 141 CYS CA C 51.3 0.3 1 471 141 141 CYS CB C 38.5 0.3 1 472 141 141 CYS N N 121.2 0.3 1 473 142 142 GLY H H 8.23 0.02 1 474 142 142 GLY CA C 42.7 0.3 1 475 142 142 GLY N N 108.6 0.3 1 476 143 143 PHE H H 7.90 0.02 1 477 143 143 PHE CA C 58.1 0.3 1 478 143 143 PHE CB C 36.8 0.3 1 479 143 143 PHE N N 119.6 0.3 1 480 144 144 ASP H H 8.22 0.02 1 481 144 144 ASP CA C 51.2 0.3 1 482 144 144 ASP CB C 38.4 0.3 1 483 144 144 ASP N N 122.1 0.3 1 484 145 145 SER H H 8.11 0.02 1 485 145 145 SER CA C 56.0 0.3 1 486 145 145 SER CB C 60.7 0.3 1 487 145 145 SER N N 116.8 0.3 1 488 146 146 ASN H H 8.34 0.02 1 489 146 146 ASN CA C 50.7 0.3 1 490 146 146 ASN CB C 35.7 0.3 1 491 146 146 ASN N N 120.6 0.3 1 492 148 148 ILE H H 7.97 0.02 1 493 148 148 ILE CA C 58.2 0.3 1 494 148 148 ILE CB C 27.2 0.3 1 495 148 148 ILE N N 123.6 0.3 1 496 149 149 MET H H 8.37 0.02 1 497 149 149 MET CA C 53.8 0.3 1 498 149 149 MET CB C 27.5 0.3 1 499 149 149 MET N N 124.8 0.3 1 500 150 150 ASP H H 8.31 0.02 1 501 150 150 ASP CA C 51.4 0.3 1 502 150 150 ASP CB C 38.4 0.3 1 503 150 150 ASP N N 121.9 0.3 1 stop_ save_