data_5656 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Resonance Assignments for the Z Domain of Staphylococcal Protein A using a 2H, 13C, 15N enriched, selective methyl protonated sample ; _BMRB_accession_number 5656 _BMRB_flat_file_name bmr5656.str _Entry_type original _Submission_date 2003-01-09 _Accession_date 2003-01-13 _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 Zheng Deyou . . 2 Swapna G.V.T. . . 3 Hunter Moseley N.B. . 4 Montelione Gaetano T. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 122 "13C chemical shifts" 235 "15N chemical shifts" 83 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-07-13 update BMRB 'added time domain data' 2005-05-03 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Validation of helical tilt angles in the solution NMR structure of the Z domain of Staphylococcal protein A by combined analysis of residual dipolar coupling and NOE data. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14718654 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zheng D. . . 2 Aramini J. M. . 3 Montelione G. T. . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume 13 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 549 _Page_last 554 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_system_staphylococcal_protein_A_Z_domain _Saveframe_category molecular_system _Mol_system_name 'staphylococcal protein A Z domain' _Abbreviation_common 'staphylococcal protein A Z domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'staphylococcal protein A Z domain' $staphylococcal_protein_A_Z_domain stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_staphylococcal_protein_A_Z_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'staphylococcal protein A Z domain' _Abbreviation_common 'staphylococcal protein A Z domain' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 71 _Mol_residue_sequence ; KAIFVLNAQHDEAVDNKFNK EQQNAFYEILHLPNLNEEQR NAFIQSLKDDPSQSANLLAE AKKLNDAQAPK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -13 LYS 2 -12 ALA 3 -11 ILE 4 -10 PHE 5 -9 VAL 6 -8 LEU 7 -7 ASN 8 -6 ALA 9 -5 GLN 10 -4 HIS 11 -3 ASP 12 -2 GLU 13 -1 ALA 14 1 VAL 15 2 ASP 16 3 ASN 17 4 LYS 18 5 PHE 19 6 ASN 20 7 LYS 21 8 GLU 22 9 GLN 23 10 GLN 24 11 ASN 25 12 ALA 26 13 PHE 27 14 TYR 28 15 GLU 29 16 ILE 30 17 LEU 31 18 HIS 32 19 LEU 33 20 PRO 34 21 ASN 35 22 LEU 36 23 ASN 37 24 GLU 38 25 GLU 39 26 GLN 40 27 ARG 41 28 ASN 42 29 ALA 43 30 PHE 44 31 ILE 45 32 GLN 46 33 SER 47 34 LEU 48 35 LYS 49 36 ASP 50 37 ASP 51 38 PRO 52 39 SER 53 40 GLN 54 41 SER 55 42 ALA 56 43 ASN 57 44 LEU 58 45 LEU 59 46 ALA 60 47 GLU 61 48 ALA 62 49 LYS 63 50 LYS 64 51 LEU 65 52 ASN 66 53 ASP 67 54 ALA 68 55 GLN 69 56 ALA 70 57 PRO 71 58 LYS 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 BMRB 19043 Z_domain 81.69 58 100.00 100.00 4.97e-31 BMRB 4023 staphylococcal_protein_A_Z_domain 100.00 71 100.00 100.00 1.47e-40 PDB 1H0T "An Affibody In Complex With A Target Protein: Structure And Coupled Folding" 81.69 58 100.00 100.00 4.97e-31 PDB 1LP1 "Protein Z In Complex With An In Vitro Selected Affibody" 81.69 58 100.00 100.00 4.97e-31 PDB 1Q2N "Refined Solution Nmr Structure Of The Z Domain Of Staphylococcal Protein A" 81.69 58 100.00 100.00 4.97e-31 PDB 2M5A "Protein A Binding By An Engineered Affibody Molecule" 81.69 58 100.00 100.00 4.97e-31 PDB 2SPZ "Staphylococcal Protein A, Z-Domain, Nmr, 10 Structures" 81.69 58 100.00 100.00 4.97e-31 PDB 4GWP "Structure Of The Mediator Head Module From S. Cerevisiae" 81.69 407 98.28 98.28 1.56e-28 PDB 4GWQ "Structure Of The Mediator Head Module From S. Cerevisiae In Complex With The Carboxy-Terminal Domain (Ctd) Of Rna Polymerase Ii" 81.69 407 98.28 98.28 1.56e-28 DBJ BAC76617 "protein A doublet [Cloning vector pscFvCA-E8VHd]" 90.14 68 100.00 100.00 1.72e-35 DBJ BAC76619 "protein A doublet [Cloning vector pFCAH9-E8d]" 81.69 126 100.00 100.00 3.56e-30 DBJ BAL27690 "FLAG-TEV cut site-protein A tag [Cloning vector pCtFLATAki-kanMX6]" 90.14 86 100.00 100.00 2.16e-35 DBJ BAL27694 "Spac323.08-FLATA [Targeting vector pCtFLATAki-Pspac323.08-SalI-spac323.08(+)-kanMX6T]" 90.14 298 100.00 100.00 1.70e-34 DBJ BAL27697 "HA-TEV cut site-protein A tag [Schizosaccharomyces pombe expression vector pFOX1-CHATA]" 90.14 87 100.00 100.00 2.85e-35 EMBL CAA49867 "staphylococcal protein A [synthetic construct]" 80.28 88 98.25 98.25 6.37e-30 EMBL CAA65431 "protein A [synthetic construct]" 81.69 318 100.00 100.00 8.07e-29 GB AAA72944 "bifunctional fusion protein, partial [synthetic construct]" 80.28 308 98.25 98.25 9.08e-31 GB AAB00807 "ZZ:beta-Gal' IgG-binding fusion protein [Cloning vector pKP497]" 81.69 215 100.00 100.00 7.78e-30 GB AAR10383 "C-terminal TAP tag [synthetic construct]" 81.69 194 100.00 100.00 2.01e-30 GB AAR10384 "N-terminal TAP tag [synthetic construct]" 81.69 199 100.00 100.00 1.75e-30 GB AAR10385 "N-terminal TAP tag [synthetic construct]" 81.69 200 100.00 100.00 1.27e-30 REF WP_000298178 "hypothetical protein, partial [Staphylococcus aureus]" 54.93 254 97.44 97.44 3.45e-15 REF WP_000298179 "hypothetical protein, partial [Staphylococcus aureus]" 54.93 254 97.44 97.44 3.52e-15 REF WP_000316486 "hypothetical protein, partial [Staphylococcus aureus]" 52.11 264 97.30 97.30 1.39e-13 REF WP_000363686 "hypothetical protein, partial [Staphylococcus aureus]" 71.83 290 98.04 98.04 2.05e-24 REF WP_000496862 "hypothetical protein, partial [Staphylococcus aureus]" 57.75 240 97.56 97.56 6.28e-17 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $staphylococcal_protein_A_Z_domain 'S. aureus' 1280 Eubacteria . Staphylococcus aureus 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 $staphylococcal_protein_A_Z_domain 'recombinant technology' 'E. coli' Escherichia coli . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $staphylococcal_protein_A_Z_domain 1.1 mM '[U-13C; U-15N; U-2H] with Val, Leu, Ile(delta) methyl protonated' stop_ save_ ############################ # Computer software used # ############################ save_AutoAssign _Saveframe_category software _Name AutoAssign _Version 1.9 loop_ _Task 'automated backbone assignments' stop_ _Details ; 1. Moseley, H.N., Monleon, D., and Montelione, G.T. (2001) Methods Enzymol. 339: 91-108. 2. Zimmerman, D.E., Kulikowski, C.A., Huang, Y., Feng, W., Tashiro, M., Shimotakahara, S., Chien, C., Powers, R., and Montelione, G.T. (1997). J. Mol. Biol. 269: 592-610. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _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_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _Sample_label . save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HN(CO)CACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _Sample_label . save_ save_H(CCCO)NH-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCCO)NH-TOCSY _Sample_label . save_ save_(H)CC(CO)NH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CC(CO)NH-TOCSY _Sample_label . save_ save_NMR_spectrometer_expt_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . pH temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 0.00 . . . . . 1.0 DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.25144953 DSS N 15 'methyl protons' ppm 0.00 . 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_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'staphylococcal protein A Z 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 LYS C C 175.7 . 1 2 . 1 LYS CA C 56.08 . 1 3 . 1 LYS CB C 32.40 . 1 4 . 2 ALA H H 8.41 . 1 5 . 2 ALA C C 177.3 . 1 6 . 2 ALA CA C 52.02 . 1 7 . 2 ALA CB C 18.66 . 1 8 . 2 ALA N N 126.4 . 1 9 . 3 ILE H H 8.05 . 1 10 . 3 ILE C C 175.8 . 1 11 . 3 ILE CA C 60.66 . 1 12 . 3 ILE CB C 38.18 . 1 13 . 3 ILE CD1 C 12.63 . 1 14 . 3 ILE HD1 H 0.77 . 1 15 . 3 ILE N N 120.0 . 1 16 . 4 PHE H H 8.25 . 1 17 . 4 PHE C C 175.1 . 1 18 . 4 PHE CA C 57.16 . 1 19 . 4 PHE CB C 39.24 . 1 20 . 4 PHE N N 124.2 . 1 21 . 5 VAL H H 8.01 . 1 22 . 5 VAL C C 175.4 . 1 23 . 5 VAL CA C 61.66 . 1 24 . 5 VAL CB C 32.76 . 1 25 . 5 VAL CG1 C 20.51 . 2 26 . 5 VAL CG2 C 20.89 . 2 27 . 5 VAL HG1 H 0.83 . 2 28 . 5 VAL HG2 H 0.82 . 2 29 . 5 VAL N N 123.2 . 1 30 . 6 LEU H H 8.25 . 1 31 . 6 LEU C C 177.0 . 1 32 . 6 LEU CA C 55.17 . 1 33 . 6 LEU CB C 41.50 . 1 34 . 6 LEU CD1 C 23.78 . 2 35 . 6 LEU CD2 C 25.09 . 2 36 . 6 LEU HD1 H 0.84 . 2 37 . 6 LEU HD2 H 0.86 . 2 38 . 6 LEU N N 126.0 . 1 39 . 7 ASN H H 8.43 . 1 40 . 7 ASN C C 174.8 . 1 41 . 7 ASN CA C 53.03 . 1 42 . 7 ASN CB C 38.31 . 1 43 . 7 ASN HD21 H 6.90 . 2 44 . 7 ASN HD22 H 7.60 . 2 45 . 7 ASN ND2 N 112.89 . 1 46 . 7 ASN N N 119.5 . 1 47 . 8 ALA H H 8.22 . 1 48 . 8 ALA C C 177.6 . 1 49 . 8 ALA CA C 52.39 . 1 50 . 8 ALA CB C 18.56 . 1 51 . 8 ALA N N 124.0 . 1 52 . 9 GLN H H 8.29 . 1 53 . 9 GLN C C 175.9 . 1 54 . 9 GLN CA C 55.69 . 1 55 . 9 GLN CB C 28.69 . 1 56 . 9 GLN HE21 H 7.56 . 2 57 . 9 GLN HE22 H 6.86 . 2 58 . 9 GLN NE2 N 112.8 . 1 59 . 9 GLN N N 118.7 . 1 60 . 10 HIS H H 8.23 . 1 61 . 10 HIS C C 174.1 . 1 62 . 10 HIS CA C 55.29 . 1 63 . 10 HIS CB C 29.03 . 1 64 . 10 HIS N N 119.6 . 1 65 . 11 ASP H H 8.39 . 1 66 . 11 ASP C C 176.2 . 1 67 . 11 ASP CA C 54.01 . 1 68 . 11 ASP CB C 40.96 . 1 69 . 11 ASP N N 122.0 . 1 70 . 12 GLU H H 8.54 . 1 71 . 12 GLU C C 176.5 . 1 72 . 12 GLU CA C 56.83 . 1 73 . 12 GLU CB C 29.42 . 1 74 . 12 GLU N N 122.1 . 1 75 . 13 ALA H H 8.28 . 1 76 . 13 ALA C C 178.2 . 1 77 . 13 ALA CA C 52.60 . 1 78 . 13 ALA CB C 18.32 . 1 79 . 13 ALA N N 123.8 . 1 80 . 14 VAL H H 7.85 . 1 81 . 14 VAL C C 176.1 . 1 82 . 14 VAL CA C 62.40 . 1 83 . 14 VAL CB C 32.17 . 1 84 . 14 VAL CG1 C 20.51 . 2 85 . 14 VAL CG2 C 20.68 . 2 86 . 14 VAL HG1 H 0.70 . 2 87 . 14 VAL HG2 H 0.73 . 2 88 . 14 VAL N N 118.2 . 1 89 . 15 ASP H H 8.00 . 1 90 . 15 ASP C C 176.5 . 1 91 . 15 ASP CA C 54.40 . 1 92 . 15 ASP CB C 40.60 . 1 93 . 15 ASP N N 122.0 . 1 94 . 16 ASN H H 8.13 . 1 95 . 16 ASN C C 175.4 . 1 96 . 16 ASN CA C 53.82 . 1 97 . 16 ASN CB C 38.31 . 1 98 . 16 ASN HD21 H 7.50 . 2 99 . 16 ASN HD22 H 6.82 . 2 100 . 16 ASN ND2 N 112.69 . 1 101 . 16 ASN N N 118.9 . 1 102 . 17 LYS H H 8.21 . 1 103 . 17 LYS C C 176.8 . 1 104 . 17 LYS CA C 56.58 . 1 105 . 17 LYS CB C 31.40 . 1 106 . 17 LYS N N 119.4 . 1 107 . 18 PHE H H 7.87 . 1 108 . 18 PHE C C 177.0 . 1 109 . 18 PHE CA C 55.06 . 1 110 . 18 PHE CB C 39.12 . 1 111 . 18 PHE N N 118.8 . 1 112 . 19 ASN H H 8.43 . 1 113 . 19 ASN C C 175.8 . 1 114 . 19 ASN CA C 51.79 . 1 115 . 19 ASN CB C 37.64 . 1 116 . 19 ASN HD21 H 7.48 . 2 117 . 19 ASN HD22 H 6.91 . 2 118 . 19 ASN ND2 N 110.38 . 1 119 . 19 ASN N N 120.4 . 1 120 . 20 LYS H H 8.33 . 1 121 . 20 LYS C C 178.6 . 1 122 . 20 LYS CA C 59.67 . 1 123 . 20 LYS CB C 31.30 . 1 124 . 20 LYS N N 118.5 . 1 125 . 21 GLU H H 8.22 . 1 126 . 21 GLU C C 180.2 . 1 127 . 21 GLU CA C 59.47 . 1 128 . 21 GLU CB C 28.36 . 1 129 . 21 GLU N N 119.5 . 1 130 . 22 GLN H H 8.52 . 1 131 . 22 GLN C C 177.8 . 1 132 . 22 GLN CA C 58.44 . 1 133 . 22 GLN CB C 26.35 . 1 134 . 22 GLN HE21 H 6.96 . 2 135 . 22 GLN HE22 H 7.27 . 2 136 . 22 GLN NE2 N 111.06 . 1 137 . 22 GLN N N 121.4 . 1 138 . 23 GLN H H 8.75 . 1 139 . 23 GLN C C 178.4 . 1 140 . 23 GLN CA C 58.66 . 1 141 . 23 GLN CB C 27.86 . 1 142 . 23 GLN HE21 H 6.88 . 2 143 . 23 GLN HE22 H 7.24 . 2 144 . 23 GLN NE2 N 111.88 . 1 145 . 23 GLN N N 118.8 . 1 146 . 24 ASN H H 8.29 . 1 147 . 24 ASN C C 177.5 . 1 148 . 24 ASN CA C 55.99 . 1 149 . 24 ASN CB C 37.76 . 1 150 . 24 ASN HD21 H 7.74 . 2 151 . 24 ASN HD22 H 7.07 . 2 152 . 24 ASN ND2 N 112.69 . 1 153 . 24 ASN N N 117.4 . 1 154 . 25 ALA H H 7.88 . 1 155 . 25 ALA C C 178.2 . 1 156 . 25 ALA CA C 55.20 . 1 157 . 25 ALA CB C 17.50 . 1 158 . 25 ALA N N 122.1 . 1 159 . 26 PHE H H 8.13 . 1 160 . 26 PHE C C 176.2 . 1 161 . 26 PHE CA C 60.82 . 1 162 . 26 PHE CB C 38.31 . 1 163 . 26 PHE N N 117.8 . 1 164 . 27 TYR H H 8.15 . 1 165 . 27 TYR C C 178.9 . 1 166 . 27 TYR CA C 61.88 . 1 167 . 27 TYR CB C 37.64 . 1 168 . 27 TYR N N 116.6 . 1 169 . 28 GLU H H 8.54 . 1 170 . 28 GLU C C 180.6 . 1 171 . 28 GLU CA C 60.08 . 1 172 . 28 GLU CB C 29.35 . 1 173 . 28 GLU N N 119.0 . 1 174 . 29 ILE H H 8.41 . 1 175 . 29 ILE C C 178.1 . 1 176 . 29 ILE CA C 65.36 . 1 177 . 29 ILE CB C 36.74 . 1 178 . 29 ILE CD1 C 12.38 . 1 179 . 29 ILE HD1 H 0.47 . 1 180 . 29 ILE N N 119.5 . 1 181 . 30 LEU H H 7.88 . 1 182 . 30 LEU C C 177.1 . 1 183 . 30 LEU CA C 56.94 . 1 184 . 30 LEU CB C 41.09 . 1 185 . 30 LEU CD1 C 23.52 . 2 186 . 30 LEU CD2 C 24.57 . 2 187 . 30 LEU HD1 H 0.60 . 2 188 . 30 LEU HD2 H 0.50 . 2 189 . 30 LEU N N 117.4 . 1 190 . 31 HIS H H 7.19 . 1 191 . 31 HIS C C 174.7 . 1 192 . 31 HIS CA C 55.39 . 1 193 . 31 HIS CB C 28.89 . 1 194 . 31 HIS N N 111.4 . 1 195 . 32 LEU H H 7.19 . 1 196 . 32 LEU C C 177.7 . 1 197 . 32 LEU CA C 53.26 . 1 198 . 32 LEU CB C 39.61 . 1 199 . 32 LEU CD1 C 23.15 . 2 200 . 32 LEU CD2 C 27.07 . 2 201 . 32 LEU HD1 H 0.82 . 2 202 . 32 LEU HD2 H 0.63 . 2 203 . 32 LEU N N 124.2 . 1 204 . 33 PRO C C 178.2 . 1 205 . 33 PRO CA C 64.74 . 1 206 . 33 PRO CB C 31.84 . 1 207 . 34 ASN H H 8.89 . 1 208 . 34 ASN C C 176.4 . 1 209 . 34 ASN CA C 52.46 . 1 210 . 34 ASN CB C 38.22 . 1 211 . 34 ASN HD21 H 6.96 . 2 212 . 34 ASN HD22 H 7.44 . 2 213 . 34 ASN ND2 N 114.88 . 1 214 . 34 ASN N N 113.6 . 1 215 . 35 LEU H H 6.48 . 1 216 . 35 LEU C C 176.6 . 1 217 . 35 LEU CA C 54.09 . 1 218 . 35 LEU CB C 42.22 . 1 219 . 35 LEU CD1 C 22.15 . 2 220 . 35 LEU CD2 C 26.42 . 2 221 . 35 LEU HD1 H 0.84 . 2 222 . 35 LEU HD2 H 0.92 . 2 223 . 35 LEU N N 117.2 . 1 224 . 36 ASN H H 8.54 . 1 225 . 36 ASN C C 175.8 . 1 226 . 36 ASN CA C 51.15 . 1 227 . 36 ASN CB C 38.28 . 1 228 . 36 ASN HD21 H 7.05 . 2 229 . 36 ASN HD22 H 7.51 . 2 230 . 36 ASN ND2 N 112.18 . 1 231 . 36 ASN N N 119.0 . 1 232 . 37 GLU H H 8.61 . 1 233 . 37 GLU C C 178.3 . 1 234 . 37 GLU CA C 59.41 . 1 235 . 37 GLU CB C 28.77 . 1 236 . 37 GLU N N 118.0 . 1 237 . 38 GLU H H 8.23 . 1 238 . 38 GLU C C 178.3 . 1 239 . 38 GLU CA C 59.47 . 1 240 . 38 GLU CB C 28.36 . 1 241 . 38 GLU N N 119.6 . 1 242 . 39 GLN H H 8.50 . 1 243 . 39 GLN C C 178.6 . 1 244 . 39 GLN CA C 57.69 . 1 245 . 39 GLN CB C 28.37 . 1 246 . 39 GLN HE21 H 7.67 . 2 247 . 39 GLN HE22 H 8.25 . 2 248 . 39 GLN NE2 N 113.01 . 1 249 . 39 GLN N N 119.6 . 1 250 . 40 ARG H H 8.54 . 1 251 . 40 ARG C C 177.9 . 1 252 . 40 ARG CA C 60.11 . 1 253 . 40 ARG CB C 29.35 . 1 254 . 40 ARG N N 118.7 . 1 255 . 41 ASN H H 8.45 . 1 256 . 41 ASN C C 177.9 . 1 257 . 41 ASN CA C 55.72 . 1 258 . 41 ASN CB C 37.55 . 1 259 . 41 ASN HD21 H 7.64 . 2 260 . 41 ASN HD22 H 7.01 . 2 261 . 41 ASN ND2 N 112.46 . 1 262 . 41 ASN N N 114.8 . 1 263 . 42 ALA H H 7.84 . 1 264 . 42 ALA C C 181.0 . 1 265 . 42 ALA CA C 54.89 . 1 266 . 42 ALA CB C 17.19 . 1 267 . 42 ALA N N 123.0 . 1 268 . 43 PHE H H 7.95 . 1 269 . 43 PHE C C 178.2 . 1 270 . 43 PHE CA C 62.07 . 1 271 . 43 PHE CB C 39.11 . 1 272 . 43 PHE N N 116.8 . 1 273 . 44 ILE H H 8.24 . 1 274 . 44 ILE C C 177.8 . 1 275 . 44 ILE CA C 63.73 . 1 276 . 44 ILE CB C 35.83 . 1 277 . 44 ILE CD1 C 11.60 . 1 278 . 44 ILE HD1 H 0.56 . 1 279 . 44 ILE N N 118.1 . 1 280 . 45 GLN H H 8.40 . 1 281 . 45 GLN C C 178.4 . 1 282 . 45 GLN CA C 58.33 . 1 283 . 45 GLN CB C 27.53 . 1 284 . 45 GLN HE21 H 7.86 . 2 285 . 45 GLN HE22 H 6.95 . 2 286 . 45 GLN NE2 N 116.61 . 1 287 . 45 GLN N N 119.2 . 1 288 . 46 SER H H 8.05 . 1 289 . 46 SER C C 176.2 . 1 290 . 46 SER CA C 62.19 . 1 291 . 46 SER CB C 62.16 . 1 292 . 46 SER N N 114.9 . 1 293 . 47 LEU H H 8.09 . 1 294 . 47 LEU C C 177.5 . 1 295 . 47 LEU CA C 57.42 . 1 296 . 47 LEU CB C 41.54 . 1 297 . 47 LEU CD1 C 25.05 . 2 298 . 47 LEU CD2 C 26.07 . 2 299 . 47 LEU HD1 H 0.74 . 2 300 . 47 LEU HD2 H 0.71 . 2 301 . 47 LEU N N 124.1 . 1 302 . 48 LYS H H 7.98 . 1 303 . 48 LYS C C 179.2 . 1 304 . 48 LYS CA C 59.37 . 1 305 . 48 LYS CB C 31.80 . 1 306 . 48 LYS N N 115.4 . 1 307 . 49 ASP H H 8.15 . 1 308 . 49 ASP C C 177.5 . 1 309 . 49 ASP CA C 56.43 . 1 310 . 49 ASP CB C 40.41 . 1 311 . 49 ASP N N 117.8 . 1 312 . 50 ASP H H 7.56 . 1 313 . 50 ASP CA C 51.61 . 1 314 . 50 ASP CB C 39.84 . 1 315 . 50 ASP N N 113.6 . 1 316 . 51 PRO C C 178.5 . 1 317 . 51 PRO CA C 64.33 . 1 318 . 51 PRO CB C 31.18 . 1 319 . 52 SER H H 7.98 . 1 320 . 52 SER C C 176.4 . 1 321 . 52 SER CA C 60.90 . 1 322 . 52 SER CB C 61.97 . 1 323 . 52 SER N N 112.5 . 1 324 . 53 GLN H H 7.85 . 1 325 . 53 GLN C C 176.4 . 1 326 . 53 GLN CA C 54.78 . 1 327 . 53 GLN CB C 27.46 . 1 328 . 53 GLN HE21 H 7.59 . 2 329 . 53 GLN HE22 H 6.86 . 2 330 . 53 GLN NE2 N 114.41 . 1 331 . 53 GLN N N 120.3 . 1 332 . 54 SER H H 7.76 . 1 333 . 54 SER C C 174.3 . 1 334 . 54 SER CA C 63.13 . 1 335 . 54 SER CB C 62.22 . 1 336 . 54 SER N N 115.3 . 1 337 . 55 ALA H H 8.47 . 1 338 . 55 ALA C C 181.2 . 1 339 . 55 ALA CA C 55.26 . 1 340 . 55 ALA CB C 17.29 . 1 341 . 55 ALA N N 122.8 . 1 342 . 56 ASN H H 7.91 . 1 343 . 56 ASN C C 178.0 . 1 344 . 56 ASN CA C 55.58 . 1 345 . 56 ASN CB C 37.67 . 1 346 . 56 ASN HD21 H 7.77 . 2 347 . 56 ASN HD22 H 7.01 . 2 348 . 56 ASN ND2 N 113.13 . 1 349 . 56 ASN N N 118.4 . 1 350 . 57 LEU H H 8.59 . 1 351 . 57 LEU C C 178.5 . 1 352 . 57 LEU CA C 57.49 . 1 353 . 57 LEU CB C 41.60 . 1 354 . 57 LEU CD1 C 23.07 . 2 355 . 57 LEU CD2 C 26.02 . 2 356 . 57 LEU HD1 H 1.08 . 2 357 . 57 LEU HD2 H 0.74 . 2 358 . 57 LEU N N 121.3 . 1 359 . 58 LEU H H 8.40 . 1 360 . 58 LEU C C 178.1 . 1 361 . 58 LEU CA C 57.52 . 1 362 . 58 LEU CB C 41.17 . 1 363 . 58 LEU CD1 C 23.51 . 2 364 . 58 LEU CD2 C 24.41 . 2 365 . 58 LEU HD1 H 0.87 . 2 366 . 58 LEU HD2 H 0.90 . 2 367 . 58 LEU N N 118.5 . 1 368 . 59 ALA H H 7.58 . 1 369 . 59 ALA C C 181.4 . 1 370 . 59 ALA CA C 54.95 . 1 371 . 59 ALA CB C 17.20 . 1 372 . 59 ALA N N 119.2 . 1 373 . 60 GLU H H 8.06 . 1 374 . 60 GLU C C 179.1 . 1 375 . 60 GLU CA C 58.80 . 1 376 . 60 GLU CB C 28.88 . 1 377 . 60 GLU N N 119.2 . 1 378 . 61 ALA H H 8.45 . 1 379 . 61 ALA C C 179.7 . 1 380 . 61 ALA CA C 55.01 . 1 381 . 61 ALA CB C 16.68 . 1 382 . 61 ALA N N 123.8 . 1 383 . 62 LYS H H 8.47 . 1 384 . 62 LYS C C 178.9 . 1 385 . 62 LYS CA C 60.01 . 1 386 . 62 LYS CB C 31.29 . 1 387 . 62 LYS N N 117.9 . 1 388 . 63 LYS H H 7.66 . 1 389 . 63 LYS C C 179.9 . 1 390 . 63 LYS CA C 59.47 . 1 391 . 63 LYS CB C 31.58 . 1 392 . 63 LYS N N 119.9 . 1 393 . 64 LEU H H 7.89 . 1 394 . 64 LEU C C 178.2 . 1 395 . 64 LEU CA C 57.20 . 1 396 . 64 LEU CB C 41.21 . 1 397 . 64 LEU CD1 C 23.48 . 2 398 . 64 LEU CD2 C 24.68 . 2 399 . 64 LEU HD1 H 0.95 . 2 400 . 64 LEU HD2 H 0.98 . 2 401 . 64 LEU N N 122.0 . 1 402 . 65 ASN H H 8.54 . 1 403 . 65 ASN C C 177.7 . 1 404 . 65 ASN CA C 57.46 . 1 405 . 65 ASN CB C 41.20 . 1 406 . 65 ASN HD21 H 7.94 . 2 407 . 65 ASN HD22 H 6.85 . 2 408 . 65 ASN ND2 N 116.30 . 1 409 . 65 ASN N N 116.7 . 1 410 . 66 ASP H H 8.24 . 1 411 . 66 ASP C C 179.1 . 1 412 . 66 ASP CA C 56.79 . 1 413 . 66 ASP CB C 39.46 . 1 414 . 66 ASP N N 118.6 . 1 415 . 67 ALA H H 8.00 . 1 416 . 67 ALA C C 179.5 . 1 417 . 67 ALA CA C 54.11 . 1 418 . 67 ALA CB C 17.88 . 1 419 . 67 ALA N N 122.7 . 1 420 . 68 GLN H H 7.51 . 1 421 . 68 GLN C C 174.2 . 1 422 . 68 GLN CA C 54.66 . 1 423 . 68 GLN CB C 27.46 . 1 424 . 68 GLN HE21 H 8.75 . 2 425 . 68 GLN HE22 H 7.27 . 2 426 . 68 GLN NE2 N 111.17 . 1 427 . 68 GLN N N 114.8 . 1 428 . 69 ALA H H 7.08 . 1 429 . 69 ALA C C 175.6 . 1 430 . 69 ALA CA C 50.77 . 1 431 . 69 ALA CB C 17.23 . 1 432 . 69 ALA N N 124.2 . 1 433 . 70 PRO C C 176.3 . 1 434 . 70 PRO CA C 63.02 . 1 435 . 70 PRO CB C 31.21 . 1 436 . 71 LYS H H 8.08 . 1 437 . 71 LYS C C 181.7 . 1 438 . 71 LYS CA C 57.13 . 1 439 . 71 LYS CB C 32.96 . 1 440 . 71 LYS N N 127.4 . 1 stop_ save_