data_5584 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 13C Chemical Shift Assignments of Cu(II) plastocyanin from Synechocystis sp. PCC6803 ; _BMRB_accession_number 5584 _BMRB_flat_file_name bmr5584.str _Entry_type original _Submission_date 2002-11-07 _Accession_date 2002-11-07 _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 Gelis Ioannis . . 2 Katsaros Nikolaos . . 3 Luchinat Claudio . . 4 Piccioli Mario . . 5 Poggi Luisa . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 224 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-04-10 original author . stop_ _Original_release_date 2003-04-10 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'A Simple Protocol to study Blue Copper Proteins by NMR' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22469432 _PubMed_ID 12581200 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gelis Ioannis . . 2 Katsaros Nikolaos . . 3 Luchinat Claudio . . 4 Piccioli Mario . . 5 Poggi Luisa . . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_volume 270 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 600 _Page_last 609 _Year 2003 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Bertini I, Ciurli S, Dikiy A, Fernandez CO, Luchinat C, Safarov N, Shumilin S, The first solution structure of a paramagnetic copper(II) protein: the case of oxidized plastocyanin from the cyanobacterium Synechocystis PCC6803 J Am Chem Soc. 2001 Mar 14, 123(10):2405-13 ; _Citation_title 'The first solution structure of a paramagnetic copper(II) protein: the case of oxidized plastocyanin from the cyanobacterium Synechocystis PCC6803.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11456890 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bertini I. . . 2 Ciurli S. . . 3 Dikiy A. . . 4 Fernandez 'C. O.' O. . 5 Luchinat C. . . 6 Safarov N. . . 7 Shumilin S. . . 8 Vila 'A. J.' J. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full 'Journal of the American Chemical Society' _Journal_volume 123 _Journal_issue 10 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 2405 _Page_last 2413 _Year 2001 _Details ; The NMR solution structure of oxidized plastocyanin from the cyanobacterium Synechocystis PCC6803 is here reported. The protein contains paramagnetic copper(II), whose electronic relaxation times are quite unfavorable for NMR solution studies. The structure has been solved on the basis of 1041 meaningful NOESY cross-peaks, 18 1D NOEs, 26 T(1) values, 96 dihedral angle constraints, and 18 H-bonds. The detection of broad hyperfine-shifted signals and their full assignment allowed the identification of the copper(II) ligands and the determination of the Cu-S-C-H dihedral angle for the coordinated cysteine. The global root-mean-square deviation from the mean structure for the solution structure family is 0.72 +/- 0.14 and 1.16 +/- 0.17 A for backbone and heavy atoms, respectively. The structure is overall quite satisfactory and represents a breakthrough, in that it includes paramagnetic copper proteins among the metalloproteins for which solution structures can be afforded. The comparison with the available X-ray structure of a triple mutant is also performed. ; save_ ################################## # Molecular system description # ################################## save_system_pcn _Saveframe_category molecular_system _Mol_system_name plastocyanin _Abbreviation_common pcn _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'plastocyanin monomer' $pcn 'copper ion' $CU stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state 'all other bound' loop_ _Biological_function 'Electron-transfer protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_pcn _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Plastocyanin _Abbreviation_common pcn _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 98 _Mol_residue_sequence ; ANATVKMGSDSGALVFEPST VTIKAGEEVKWVNNKLSPHN IVFAADGVDADTAAKLSHKG LAFAAGESFTSTFTEPGTYT YYCEPHRGAGMVGKVVVD ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ASN 3 ALA 4 THR 5 VAL 6 LYS 7 MET 8 GLY 9 SER 10 ASP 11 SER 12 GLY 13 ALA 14 LEU 15 VAL 16 PHE 17 GLU 18 PRO 19 SER 20 THR 21 VAL 22 THR 23 ILE 24 LYS 25 ALA 26 GLY 27 GLU 28 GLU 29 VAL 30 LYS 31 TRP 32 VAL 33 ASN 34 ASN 35 LYS 36 LEU 37 SER 38 PRO 39 HIS 40 ASN 41 ILE 42 VAL 43 PHE 44 ALA 45 ALA 46 ASP 47 GLY 48 VAL 49 ASP 50 ALA 51 ASP 52 THR 53 ALA 54 ALA 55 LYS 56 LEU 57 SER 58 HIS 59 LYS 60 GLY 61 LEU 62 ALA 63 PHE 64 ALA 65 ALA 66 GLY 67 GLU 68 SER 69 PHE 70 THR 71 SER 72 THR 73 PHE 74 THR 75 GLU 76 PRO 77 GLY 78 THR 79 TYR 80 THR 81 TYR 82 TYR 83 CYS 84 GLU 85 PRO 86 HIS 87 ARG 88 GLY 89 ALA 90 GLY 91 MET 92 VAL 93 GLY 94 LYS 95 VAL 96 VAL 97 VAL 98 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-06-11 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 5475 plasto 100.00 98 98.98 100.00 1.83e-63 PDB 1J5C "Solution Structure Of Oxidized Paramagnetic Cu(Ii) Plastocyanin From Synechocystis Pcc6803" 98.98 98 100.00 100.00 1.63e-63 PDB 1J5D "Solution Structure Of Oxidized Paramagnetic Cu(Ii) Plastocyanin From Synechocystis Pcc6803-Minimized Average Structure" 100.00 98 100.00 100.00 4.49e-64 PDB 1JXD "Solution Structure Of Reduced Cu(i) Plastocyanin From Synechocystis Pcc6803" 100.00 98 100.00 100.00 4.49e-64 PDB 1JXF "Solution Structure Of Reduced Cu(I) Plastocyanin From Synechocystis Pcc6803" 98.98 98 100.00 100.00 1.63e-63 PDB 1M9W "Study Of Electrostatic Potential Surface Distribution Using High Resolution Side-Chain Conformation Determined By Nmr" 100.00 98 98.98 100.00 1.83e-63 DBJ BAA10227 "plastocyanin [Synechocystis sp. PCC 6803]" 100.00 126 98.98 100.00 6.12e-64 DBJ BAK51011 "plastocyanin [Synechocystis sp. PCC 6803]" 100.00 126 98.98 100.00 6.12e-64 DBJ BAL30009 "plastocyanin [Synechocystis sp. PCC 6803 substr. GT-I]" 100.00 126 98.98 100.00 6.12e-64 DBJ BAL33178 "plastocyanin [Synechocystis sp. PCC 6803 substr. PCC-N]" 100.00 126 98.98 100.00 6.12e-64 DBJ BAL36347 "plastocyanin [Synechocystis sp. PCC 6803 substr. PCC-P]" 100.00 126 98.98 100.00 6.12e-64 EMBL CAA38038 "plastocyanin [Synechocystis sp. PCC 6803]" 100.00 126 98.98 100.00 6.12e-64 GB AGF52520 "plastocyanin [Synechocystis sp. PCC 6803]" 100.00 126 98.98 100.00 6.12e-64 REF NP_442157 "plastocyanin [Synechocystis sp. PCC 6803]" 100.00 126 98.98 100.00 6.12e-64 REF WP_010873453 "plasmid stabilization protein [Synechocystis sp. PCC 6803]" 100.00 126 98.98 100.00 6.12e-64 REF YP_005384024 "plastocyanin [Synechocystis sp. PCC 6803 substr. GT-I]" 100.00 126 98.98 100.00 6.12e-64 REF YP_005387193 "plastocyanin [Synechocystis sp. PCC 6803 substr. PCC-P]" 100.00 126 98.98 100.00 6.12e-64 REF YP_005409900 "plastocyanin [Synechocystis sp. PCC 6803 substr. PCC-N]" 100.00 126 98.98 100.00 6.12e-64 SP P21697 "RecName: Full=Plastocyanin; Flags: Precursor [Synechocystis sp. PCC 6803 substr. Kazusa]" 100.00 126 98.98 100.00 6.12e-64 stop_ save_ ############# # Ligands # ############# save_CU _Saveframe_category ligand _Mol_type non-polymer _Name_common "CU (COPPER (II) ION)" _BMRB_code . _PDB_code CU _Molecular_mass 63.546 _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 Mon Jul 25 13:20:59 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CU CU CU . 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 $pcn . 1148 Eubacteria . Synechocystis 'sp. PCC 6803' 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 $pcn 'recombinant technology' 'E. coli' Escherichia coli . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $pcn 2.0 mM '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_Sparky _Saveframe_category software _Name Sparky _Version 3 loop_ _Task 'spectra assignment' stop_ _Details . save_ save_Xwinnmr _Saveframe_category software _Name Xwinnmr _Version 3.1 loop_ _Task 'data processing' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _Sample_label $sample_1 save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_CBCANH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label $sample_1 save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details 'All experiments were tailored to detect fast-relaxing signals' save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details 'All experiments were tailored to detect fast-relaxing signals' save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details 'All experiments were tailored to detect fast-relaxing signals' save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _BMRB_pulse_sequence_accession_number . _Details 'All experiments were tailored to detect fast-relaxing signals' save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details 'All experiments were tailored to detect fast-relaxing signals' save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.2 0.1 na temperature 295 0.1 K 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 stop_ save_ save_chemical_shift_reference_2 _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 TMS H 1 'methyl protons' ppm 0.0 external indirect cylindrical external_to_the_sample parallel_to_Bo stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N HSQC' '1H-13C HSQC' CBCA(CO)NH CBCANH HNCO stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'plastocyanin monomer' _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 ALA C C 167.9 0.1 1 2 . 1 ALA CA C 48.9 0.2 1 3 . 1 ALA CB C 17.6 0.2 1 4 . 2 ASN C C 172.5 0.1 1 5 . 2 ASN CA C 51.7 0.2 1 6 . 2 ASN CB C 36.3 0.2 1 7 . 3 ALA C C 174.0 0.1 1 8 . 3 ALA CA C 48.9 0.2 1 9 . 3 ALA CB C 20.0 0.2 1 10 . 4 THR C C 170.9 0.1 1 11 . 4 THR CA C 59.2 0.2 1 12 . 4 THR CB C 68.2 0.2 1 13 . 5 VAL C C 173.2 0.1 1 14 . 5 VAL CA C 58.1 0.2 1 15 . 5 VAL CB C 33.3 0.2 1 16 . 6 LYS CA C 54.1 0.2 1 17 . 6 LYS CB C 32.8 0.2 1 18 . 7 MET CA C 56.3 0.2 1 19 . 7 MET CB C 27.9 0.2 1 20 . 8 GLY C C 170.4 0.1 1 21 . 8 GLY CA C 43.8 0.2 1 22 . 9 SER C C 173.6 0.1 1 23 . 9 SER CA C 52.7 0.2 1 24 . 9 SER CB C 62.7 0.2 1 25 . 10 ASP C C 175.3 0.1 1 26 . 10 ASP CA C 55.3 0.2 1 27 . 10 ASP CB C 37.5 0.2 1 28 . 11 SER C C 172.4 0.1 1 29 . 11 SER CA C 55.9 0.2 1 30 . 11 SER CB C 61.0 0.2 1 31 . 12 GLY C C 170.2 0.1 1 32 . 12 GLY CA C 43.4 0.2 1 33 . 13 ALA CA C 48.6 0.2 1 34 . 13 ALA CB C 18.7 0.2 1 35 . 15 VAL CA C 56.3 0.2 1 36 . 15 VAL CB C 33.1 0.2 1 37 . 16 PHE C C 173.2 0.1 1 38 . 16 PHE CA C 56.4 0.2 1 39 . 16 PHE CB C 37.8 0.2 1 40 . 17 GLU CA C 49.8 0.2 1 41 . 17 GLU CB C 32.0 0.2 1 42 . 18 PRO C C 173.9 0.1 1 43 . 19 SER C C 173.0 0.1 1 44 . 19 SER CA C 58.8 0.2 1 45 . 19 SER CB C 61.0 0.2 1 46 . 20 THR C C 170.9 0.1 1 47 . 20 THR CA C 59.9 0.2 1 48 . 20 THR CB C 68.4 0.2 1 49 . 21 VAL C C 170.6 0.1 1 50 . 21 VAL CA C 57.0 0.2 1 51 . 21 VAL CB C 32.9 0.2 1 52 . 22 THR C C 171.8 0.1 1 53 . 22 THR CA C 58.2 0.2 1 54 . 22 THR CB C 67.7 0.2 1 55 . 23 ILE C C 171.6 0.1 1 56 . 23 ILE CA C 57.0 0.2 1 57 . 23 ILE CB C 39.4 0.2 1 58 . 24 LYS C C 174.3 0.1 1 59 . 24 LYS CA C 51.1 0.2 1 60 . 24 LYS CB C 31.4 0.2 1 61 . 25 ALA C C 176.0 0.1 1 62 . 25 ALA CA C 51.8 0.2 1 63 . 25 ALA CB C 15.2 0.2 1 64 . 26 GLY C C 170.9 0.1 1 65 . 26 GLY CA C 42.3 0.2 1 66 . 27 GLU C C 170.5 0.1 1 67 . 27 GLU CA C 53.8 0.2 1 68 . 27 GLU CB C 28.2 0.2 1 69 . 28 GLU C C 173.3 0.1 1 70 . 28 GLU CA C 51.3 0.2 1 71 . 28 GLU CB C 32.2 0.2 1 72 . 29 VAL C C 170.1 0.1 1 73 . 29 VAL CA C 58.3 0.2 1 74 . 29 VAL CB C 30.9 0.2 1 75 . 30 LYS C C 172.2 0.1 1 76 . 30 LYS CA C 50.9 0.2 1 77 . 30 LYS CB C 33.6 0.2 1 78 . 31 TRP C C 173.9 0.1 1 79 . 31 TRP CA C 55.4 0.2 1 80 . 31 TRP CB C 30.5 0.2 1 81 . 32 VAL C C 173.6 0.1 1 82 . 32 VAL CA C 57.6 0.2 1 83 . 32 VAL CB C 32.7 0.2 1 84 . 33 ASN C C 171.2 0.1 1 85 . 33 ASN CA C 52.4 0.2 1 86 . 33 ASN CB C 36.4 0.2 1 87 . 34 ASN CA C 55.2 0.2 1 88 . 34 ASN CB C 39.5 0.2 1 89 . 35 LYS C C 171.8 0.1 1 90 . 35 LYS CA C 52.9 0.2 1 91 . 35 LYS CB C 34.8 0.2 1 92 . 36 LEU CA C 52.6 0.2 1 93 . 41 ILE CA C 56.7 0.2 1 94 . 41 ILE CB C 36.3 0.2 1 95 . 42 VAL C C 172.1 0.1 1 96 . 42 VAL CA C 59.2 0.2 1 97 . 42 VAL CB C 30.8 0.2 1 98 . 43 PHE C C 173.3 0.1 1 99 . 43 PHE CA C 55.7 0.2 1 100 . 43 PHE CB C 37.2 0.2 1 101 . 44 ALA C C 175.2 0.1 1 102 . 44 ALA CA C 48.8 0.2 1 103 . 44 ALA CB C 18.6 0.2 1 104 . 45 ALA C C 173.9 0.1 1 105 . 45 ALA CA C 48.8 0.2 1 106 . 45 ALA CB C 15.7 0.2 1 107 . 46 ASP C C 174.2 0.1 1 108 . 46 ASP CA C 51.2 0.2 1 109 . 46 ASP CB C 38.8 0.2 1 110 . 47 GLY C C 170.7 0.1 1 111 . 47 GLY CA C 43.3 0.2 1 112 . 48 VAL C C 172.0 0.1 1 113 . 48 VAL CA C 57.2 0.2 1 114 . 48 VAL CB C 33.4 0.2 1 115 . 49 ASP C C 173.7 0.1 1 116 . 49 ASP CA C 51.5 0.2 1 117 . 49 ASP CB C 39.9 0.2 1 118 . 50 ALA C C 178.1 0.1 1 119 . 50 ALA CA C 53.1 0.2 1 120 . 50 ALA CB C 17.0 0.2 1 121 . 51 ASP C C 176.2 0.1 1 122 . 51 ASP CA C 54.9 0.2 1 123 . 51 ASP CB C 38.3 0.2 1 124 . 52 THR C C 173.4 0.1 1 125 . 53 ALA C C 175.7 0.1 1 126 . 54 ALA C C 176.1 0.1 1 127 . 54 ALA CA C 53.0 0.2 1 128 . 54 ALA CB C 16.3 0.2 1 129 . 55 LYS C C 175.6 0.1 1 130 . 55 LYS CA C 56.3 0.2 1 131 . 55 LYS CB C 30.4 0.2 1 132 . 56 LEU C C 174.9 0.1 1 133 . 56 LEU CA C 52.9 0.2 1 134 . 56 LEU CB C 41.4 0.2 1 135 . 57 SER C C 168.7 0.1 1 136 . 57 SER CA C 57.6 0.2 1 137 . 57 SER CB C 62.3 0.2 1 138 . 58 HIS C C 169.9 0.1 1 139 . 58 HIS CA C 51.6 0.2 1 140 . 58 HIS CB C 31.0 0.2 1 141 . 59 LYS C C 176.3 0.1 1 142 . 59 LYS CA C 55.5 0.2 1 143 . 59 LYS CB C 39.1 0.2 1 144 . 60 GLY CA C 43.1 0.2 1 145 . 61 LEU CA C 53.2 0.2 1 146 . 61 LEU CB C 40.3 0.2 1 147 . 62 ALA C C 174.1 0.1 1 148 . 62 ALA CA C 48.9 0.2 1 149 . 62 ALA CB C 17.3 0.2 1 150 . 63 PHE C C 174.1 0.1 1 151 . 63 PHE CA C 57.0 0.2 1 152 . 63 PHE CB C 40.1 0.2 1 153 . 64 ALA C C 176.2 0.1 1 154 . 64 ALA CA C 49.4 0.2 1 155 . 64 ALA CB C 18.4 0.2 1 156 . 65 ALA C C 176.7 0.1 1 157 . 65 ALA CA C 51.4 0.2 1 158 . 65 ALA CB C 16.4 0.2 1 159 . 66 GLY C C 171.6 0.1 1 160 . 66 GLY CA C 43.2 0.2 1 161 . 67 GLU C C 172.7 0.1 1 162 . 67 GLU CA C 55.7 0.2 1 163 . 67 GLU CB C 29.0 0.2 1 164 . 68 SER C C 170.4 0.1 1 165 . 68 SER CA C 53.8 0.2 1 166 . 68 SER CB C 64.8 0.2 1 167 . 69 PHE C C 172.4 0.1 1 168 . 69 PHE CA C 52.6 0.2 1 169 . 69 PHE CB C 40.7 0.2 1 170 . 70 THR C C 172.8 0.1 1 171 . 70 THR CA C 58.1 0.2 1 172 . 70 THR CB C 69.2 0.2 1 173 . 71 SER C C 168.7 0.1 1 174 . 71 SER CA C 55.6 0.2 1 175 . 71 SER CB C 63.9 0.2 1 176 . 72 THR C C 170.5 0.1 1 177 . 72 THR CA C 59.8 0.2 1 178 . 72 THR CB C 67.1 0.2 1 179 . 73 PHE C C 173.3 0.1 1 180 . 73 PHE CA C 53.7 0.2 1 181 . 73 PHE CB C 38.5 0.2 1 182 . 74 THR C C 171.7 0.1 1 183 . 74 THR CA C 61.1 0.2 1 184 . 74 THR CB C 66.3 0.2 1 185 . 75 GLU CA C 50.4 0.2 1 186 . 75 GLU CB C 28.8 0.2 1 187 . 77 GLY C C 169.1 0.1 1 188 . 77 GLY CA C 42.5 0.2 1 189 . 78 THR C C 171.2 0.1 1 190 . 78 THR CA C 60.4 0.2 1 191 . 78 THR CB C 66.4 0.2 1 192 . 79 TYR C C 173.1 0.1 1 193 . 79 TYR CA C 54.2 0.2 1 194 . 79 TYR CB C 38.4 0.2 1 195 . 80 THR C C 170.5 0.1 1 196 . 80 THR CA C 59.7 0.2 1 197 . 80 THR CB C 67.7 0.2 1 198 . 86 HIS CA C 52.2 0.2 1 199 . 86 HIS CB C 35.6 0.2 1 200 . 87 ARG CA C 55.0 0.2 1 201 . 87 ARG CB C 38.0 0.2 1 202 . 88 GLY CA C 42.3 0.2 1 203 . 89 ALA C C 175.8 0.1 1 204 . 89 ALA CA C 49.2 0.2 1 205 . 89 ALA CB C 17.2 0.2 1 206 . 90 GLY CA C 43.0 0.2 1 207 . 92 VAL CA C 58.1 0.2 1 208 . 92 VAL CB C 33.7 0.2 1 209 . 93 GLY C C 169.3 0.1 1 210 . 93 GLY CA C 42.3 0.2 1 211 . 94 LYS C C 173.4 0.1 1 212 . 94 LYS CA C 52.9 0.2 1 213 . 94 LYS CB C 35.4 0.2 1 214 . 95 VAL C C 172.0 0.1 1 215 . 95 VAL CA C 59.0 0.2 1 216 . 95 VAL CB C 33.0 0.2 1 217 . 96 VAL C C 171.4 0.1 1 218 . 96 VAL CA C 59.8 0.2 1 219 . 96 VAL CB C 30.3 0.2 1 220 . 97 VAL C C 173.7 0.1 1 221 . 97 VAL CA C 57.7 0.2 1 222 . 97 VAL CB C 30.4 0.2 1 223 . 98 ASP CA C 52.3 0.2 1 224 . 98 ASP CB C 40.0 0.2 1 stop_ save_