data_5619 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Resonance assignments for the methionine sulfoxide reductase B from Bacillus subtilis, Northeast Structural Genomics Consortium target SR10 ; _BMRB_accession_number 5619 _BMRB_flat_file_name bmr5619.str _Entry_type original _Submission_date 2002-12-09 _Accession_date 2002-12-09 _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 Cort John R. . 3 Chiang Yiwen . . 4 Kennedy Michael A. . 5 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" 181 "13C chemical shifts" 447 "15N chemical shifts" 136 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-12-27 original author . stop_ _Original_release_date 2002-12-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C and 15N resonance assignments for methionine sulfoxide reductase B from Bacillus subtilis ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zheng Deyou . . 2 Cort John R. . 3 Chiang Yiwen . . 4 Acton Thomas . . 5 Kennedy Michael A. . 6 Montelione Gaetano T. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 27 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 183 _Page_last 184 _Year 2003 _Details . loop_ _Keyword 'methionine sulfoxide reductase' AutoAssign 'structural proteomics' stop_ save_ ################################## # Molecular system description # ################################## save_system_MsrB _Saveframe_category molecular_system _Mol_system_name 'methionine sulfoxide reductase B' _Abbreviation_common MsrB _Enzyme_commission_number 1.8.4.6 loop_ _Mol_system_component_name _Mol_label 'Methionine sulfoxide reductase' $MsrB stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'peptide methionine sulfoxide reductase msrB' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MsrB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'methionine sulfoxide reductase msrB' _Abbreviation_common MsrB _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 151 _Mol_residue_sequence ; MAYNKEEKIKSLNRMQYEVT QNNGTEPPFQNEYWDHKEEG LYVDIVSGKPLFTSKDKFDS QCGWPSFTKPIEEEVEEKLD TSHGMIRTEVRSRTADSHLG HVFNDGPGPNGLRYCINSAA LRFVPKHKLKEEGYESYLHL FNKLEHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 TYR 4 ASN 5 LYS 6 GLU 7 GLU 8 LYS 9 ILE 10 LYS 11 SER 12 LEU 13 ASN 14 ARG 15 MET 16 GLN 17 TYR 18 GLU 19 VAL 20 THR 21 GLN 22 ASN 23 ASN 24 GLY 25 THR 26 GLU 27 PRO 28 PRO 29 PHE 30 GLN 31 ASN 32 GLU 33 TYR 34 TRP 35 ASP 36 HIS 37 LYS 38 GLU 39 GLU 40 GLY 41 LEU 42 TYR 43 VAL 44 ASP 45 ILE 46 VAL 47 SER 48 GLY 49 LYS 50 PRO 51 LEU 52 PHE 53 THR 54 SER 55 LYS 56 ASP 57 LYS 58 PHE 59 ASP 60 SER 61 GLN 62 CYS 63 GLY 64 TRP 65 PRO 66 SER 67 PHE 68 THR 69 LYS 70 PRO 71 ILE 72 GLU 73 GLU 74 GLU 75 VAL 76 GLU 77 GLU 78 LYS 79 LEU 80 ASP 81 THR 82 SER 83 HIS 84 GLY 85 MET 86 ILE 87 ARG 88 THR 89 GLU 90 VAL 91 ARG 92 SER 93 ARG 94 THR 95 ALA 96 ASP 97 SER 98 HIS 99 LEU 100 GLY 101 HIS 102 VAL 103 PHE 104 ASN 105 ASP 106 GLY 107 PRO 108 GLY 109 PRO 110 ASN 111 GLY 112 LEU 113 ARG 114 TYR 115 CYS 116 ILE 117 ASN 118 SER 119 ALA 120 ALA 121 LEU 122 ARG 123 PHE 124 VAL 125 PRO 126 LYS 127 HIS 128 LYS 129 LEU 130 LYS 131 GLU 132 GLU 133 GLY 134 TYR 135 GLU 136 SER 137 TYR 138 LEU 139 HIS 140 LEU 141 PHE 142 ASN 143 LYS 144 LEU 145 GLU 146 HIS 147 HIS 148 HIS 149 HIS 150 HIS 151 HIS 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 17008 SR10 100.00 151 100.00 100.00 3.00e-108 PDB 2KZN "Solution Nmr Structure Of Peptide Methionine Sulfoxide Reductase Msrb From Bacillus Subtilis, Northeast Structural Genomics Con" 100.00 151 100.00 100.00 3.00e-108 PDB 3E0O "Crystal Structure Of Msrb" 94.70 144 100.00 100.00 5.60e-102 DBJ BAI85662 "methionine sulfoxide reductase B [Bacillus subtilis subsp. natto BEST195]" 95.36 144 98.61 98.61 4.44e-99 DBJ BAM52650 "methionine sulfoxide reductase B [Bacillus subtilis BEST7613]" 94.70 143 100.00 100.00 5.24e-102 DBJ BAM58225 "methionine sulfoxide reductase B [Bacillus subtilis BEST7003]" 94.70 143 100.00 100.00 5.24e-102 DBJ GAK79338 "methionine sulfoxide reductase B [Bacillus subtilis Miyagi-4]" 95.36 144 98.61 98.61 4.44e-99 EMBL CAB14086 "peptide methionine R-sulfoxide reductase [Bacillus subtilis subsp. subtilis str. 168]" 94.70 143 100.00 100.00 5.24e-102 EMBL CCU58667 "Peptide methionine sulfoxide reductase MsrB [Bacillus subtilis E1]" 95.36 144 97.92 98.61 1.29e-98 EMBL CEI57380 "peptide methionine sulfoxide reductase MsrB [Bacillus subtilis]" 94.70 143 100.00 100.00 5.24e-102 EMBL CEJ77805 "peptide methionine sulfoxide reductase MsrB [Bacillus sp.]" 94.70 143 100.00 100.00 5.24e-102 GB AAA96648 "54.8% identity with Neisseria gonorrhoeae regulatory protein PilB; putative [Bacillus subtilis subsp. subtilis str. 168]" 94.70 143 100.00 100.00 5.24e-102 GB ADV92894 "methionine sulfoxide reductase B [Bacillus subtilis BSn5]" 95.36 144 98.61 98.61 4.44e-99 GB AEP91184 "methionine-R-sulfoxide reductase [Bacillus subtilis subsp. subtilis str. RO-NN-1]" 95.36 144 97.92 98.61 7.58e-99 GB AFQ58114 "Peptide methionine R-sulfoxide reductase [Bacillus subtilis QB928]" 94.70 143 100.00 100.00 5.24e-102 GB AGA23472 "Peptide methionine sulfoxide reductase MsrB [Bacillus subtilis subsp. subtilis str. BSP1]" 95.36 144 98.61 98.61 4.44e-99 REF NP_390051 "peptide methionine sulfoxide reductase MsrB [Bacillus subtilis subsp. subtilis str. 168]" 94.70 143 100.00 100.00 5.24e-102 REF WP_003230813 "methionine sulfoxide reductase B [Bacillus subtilis]" 94.70 143 100.00 100.00 5.24e-102 REF WP_014477116 "methionine sulfoxide reductase B [Bacillus subtilis]" 95.36 144 97.92 98.61 7.58e-99 REF WP_014480061 "MULTISPECIES: methionine sulfoxide reductase B [Bacillales]" 95.36 144 98.61 98.61 4.44e-99 REF WP_021481498 "MULTISPECIES: methionine sulfoxide reductase B [Bacillus]" 95.36 144 97.92 98.61 1.29e-98 SP P54155 "RecName: Full=Peptide methionine sulfoxide reductase MsrB; AltName: Full=Peptide-methionine (R)-S-oxide reductase [Bacillus sub" 94.70 143 100.00 100.00 5.24e-102 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MsrB 'Bacillus subtilis' 1423 Eubacteria . Bacillus subtilis 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 $MsrB 'recombinant technology' . . . . . 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 $MsrB 1.0 mM '[U-13C; U-15N; U-2H] with Val, Leu, Ile(delta) methyl protonated' stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version . loop_ _Task process stop_ _Details . save_ 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) Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data. 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). Automated analysis of protein NMR assignments using methods from artificial intelligence. J. Mol. Biol. 269: 592-610. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 _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_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 HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCCO)NH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CC(CO)NH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.05 na temperature 293 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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' HNCO HN(CA)CO HNCACB HN(CO)CACB H(CCCO)NH-TOCSY (H)CC(CO)NH-TOCSY stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Methionine sulfoxide reductase' _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 . 3 TYR C C 173.5 0.2 1 2 . 3 TYR CA C 57.03 0.2 1 3 . 3 TYR CB C 38.25 0.2 1 4 . 4 ASN H H 8.37 0.01 1 5 . 4 ASN C C 174.1 0.2 1 6 . 4 ASN CA C 51.71 0.2 1 7 . 4 ASN CB C 38.53 0.2 1 8 . 4 ASN N N 124.5 0.1 1 9 . 5 LYS C C 176.7 0.2 1 10 . 5 LYS CA C 59.63 0.2 1 11 . 5 LYS CB C 31.95 0.2 1 12 . 5 LYS N N 126.4 0.1 1 13 . 5 LYS H H 8.51 0.01 1 14 . 6 GLU H H 8.29 0.01 1 15 . 6 GLU C C 179.1 0.2 1 16 . 6 GLU CA C 59.69 0.2 1 17 . 6 GLU CB C 28.23 0.2 1 18 . 6 GLU N N 117.5 0.1 1 19 . 7 GLU H H 7.94 0.01 1 20 . 7 GLU C C 179.4 0.2 1 21 . 7 GLU CA C 58.14 0.2 1 22 . 7 GLU CB C 28.79 0.2 1 23 . 7 GLU N N 118.1 0.1 1 24 . 8 LYS H H 8.16 0.01 1 25 . 8 LYS C C 180.7 0.2 1 26 . 8 LYS CA C 56.71 0.2 1 27 . 8 LYS CB C 30.53 0.2 1 28 . 8 LYS N N 119.7 0.1 1 29 . 9 ILE CD1 C 13.76 0.2 1 30 . 9 ILE HD1 H 0.82 0.01 1 31 . 9 ILE H H 8.67 0.01 1 32 . 9 ILE C C 178.2 0.2 1 33 . 9 ILE CA C 64.59 0.2 1 34 . 9 ILE CB C 36.51 0.2 1 35 . 9 ILE N N 119.2 0.1 1 36 . 10 LYS H H 7.59 0.01 1 37 . 10 LYS C C 176.8 0.2 1 38 . 10 LYS CA C 58.04 0.2 1 39 . 10 LYS CB C 31.57 0.2 1 40 . 10 LYS N N 118.8 0.1 1 41 . 11 SER H H 7.59 0.01 1 42 . 11 SER C C 174.1 0.2 1 43 . 11 SER CA C 58.41 0.2 1 44 . 11 SER CB C 63.71 0.2 1 45 . 11 SER N N 112.1 0.1 1 46 . 12 LEU CD1 C 21.47 0.2 1 47 . 12 LEU HD1 H 0.74 0.01 1 48 . 12 LEU CD2 C 25.89 0.2 1 49 . 12 LEU HD2 H 0.82 0.01 1 50 . 12 LEU H H 7.28 0.01 1 51 . 12 LEU C C 177.7 0.2 1 52 . 12 LEU CA C 54.56 0.2 1 53 . 12 LEU CB C 40.89 0.2 1 54 . 12 LEU N N 121.4 0.1 1 55 . 13 ASN HD21 H 6.71 0.01 2 56 . 13 ASN HD22 H 7.56 0.01 2 57 . 13 ASN ND2 N 110.2 0.1 1 58 . 13 ASN H H 8.86 0.01 1 59 . 13 ASN C C 174.9 0.2 1 60 . 13 ASN CA C 51.33 0.2 1 61 . 13 ASN CB C 36.95 0.2 1 62 . 13 ASN N N 119.8 0.1 1 63 . 14 ARG H H 8.34 0.01 1 64 . 14 ARG C C 178.6 0.2 1 65 . 14 ARG CA C 59.42 0.2 1 66 . 14 ARG CB C 28.99 0.2 1 67 . 14 ARG N N 116.4 0.1 1 68 . 15 MET H H 8.36 0.01 1 69 . 15 MET C C 178.1 0.2 1 70 . 15 MET CA C 56.45 0.2 1 71 . 15 MET CB C 30.48 0.2 1 72 . 15 MET N N 120.1 0.1 1 73 . 16 GLN HE21 H 6.80 0.01 2 74 . 16 GLN HE22 H 7.86 0.01 2 75 . 16 GLN NE2 N 111.6 0.1 1 76 . 16 GLN H H 8.86 0.01 1 77 . 16 GLN C C 180.6 0.2 1 78 . 16 GLN CA C 58.03 0.2 1 79 . 16 GLN CB C 28.57 0.2 1 80 . 16 GLN N N 117.6 0.1 1 81 . 17 TYR H H 9.17 0.01 1 82 . 17 TYR C C 176.5 0.2 1 83 . 17 TYR CA C 62.18 0.2 1 84 . 17 TYR CB C 37.99 0.2 1 85 . 17 TYR N N 122.6 0.1 1 86 . 18 GLU H H 8.92 0.01 1 87 . 18 GLU C C 180.1 0.2 1 88 . 18 GLU CA C 58.57 0.2 1 89 . 18 GLU CB C 28.57 0.2 1 90 . 18 GLU N N 121.2 0.1 1 91 . 19 VAL CG2 C 20.5 0.2 1 92 . 19 VAL HG2 H 0.95 0.01 1 93 . 19 VAL CG1 C 22.7 0.2 1 94 . 19 VAL HG1 H 0.88 0.01 1 95 . 19 VAL H H 8.64 0.01 1 96 . 19 VAL C C 176.8 0.2 1 97 . 19 VAL CA C 65.29 0.2 1 98 . 19 VAL CB C 31.75 0.2 1 99 . 19 VAL N N 116.1 0.1 1 100 . 20 THR H H 7.71 0.01 1 101 . 20 THR C C 177.9 0.2 1 102 . 20 THR CA C 64.98 0.2 1 103 . 20 THR CB C 69.10 0.2 1 104 . 20 THR N N 104.4 0.1 1 105 . 21 GLN HE21 H 7.20 0.01 2 106 . 21 GLN HE22 H 8.37 0.01 2 107 . 21 GLN NE2 N 116.3 0.1 1 108 . 21 GLN H H 8.62 0.01 1 109 . 21 GLN C C 176.3 0.2 1 110 . 21 GLN CA C 54.28 0.2 1 111 . 21 GLN CB C 27.18 0.2 1 112 . 21 GLN N N 116.1 0.1 1 113 . 22 ASN H H 6.84 0.01 1 114 . 22 ASN C C 174.8 0.2 1 115 . 22 ASN CA C 51.11 0.2 1 116 . 22 ASN CB C 38.55 0.2 1 117 . 22 ASN N N 114.4 0.1 1 118 . 23 ASN C C 174.1 0.2 1 119 . 23 ASN CA C 54.21 0.2 1 120 . 23 ASN CB C 35.25 0.2 1 121 . 23 ASN N N 113.0 0.1 1 122 . 23 ASN H H 7.11 0.01 1 123 . 24 GLY H H 8.60 0.01 1 124 . 24 GLY C C 170.1 0.2 1 125 . 24 GLY CA C 44.44 0.2 1 126 . 24 GLY N N 108.0 0.1 1 127 . 25 THR H H 7.84 0.01 1 128 . 25 THR C C 173.8 0.2 1 129 . 25 THR CA C 60.80 0.2 1 130 . 25 THR CB C 71.49 0.2 1 131 . 25 THR N N 110.5 0.1 1 132 . 26 GLU H H 8.73 0.01 1 133 . 26 GLU C C 173.9 0.2 1 134 . 26 GLU CA C 53.53 0.2 1 135 . 26 GLU CB C 26.82 0.2 1 136 . 26 GLU N N 128.2 0.1 1 137 . 28 PRO C C 177.3 0.2 1 138 . 28 PRO CA C 61.2 0.2 1 139 . 29 PHE H H 8.18 0.01 1 140 . 29 PHE N N 114.3 0.1 1 141 . 29 PHE C C 174.2 0.2 1 142 . 29 PHE CA C 59.75 0.2 1 143 . 29 PHE CB C 35.53 0.2 1 144 . 30 GLN H H 6.83 0.01 1 145 . 30 GLN C C 173.2 0.2 1 146 . 30 GLN CA C 53.36 0.2 1 147 . 30 GLN CB C 27.75 0.2 1 148 . 30 GLN N N 121.7 0.1 1 149 . 31 ASN H H 7.42 0.01 1 150 . 31 ASN C C 175.3 0.2 1 151 . 31 ASN CA C 52.77 0.2 1 152 . 31 ASN CB C 42.59 0.2 1 153 . 31 ASN N N 113.6 0.1 1 154 . 32 GLU H H 9.61 0.01 1 155 . 32 GLU C C 178.4 0.2 1 156 . 32 GLU CA C 60.41 0.2 1 157 . 32 GLU CB C 29.41 0.2 1 158 . 32 GLU N N 117.5 0.1 1 159 . 33 TYR H H 8.88 0.01 1 160 . 33 TYR C C 179.0 0.2 1 161 . 33 TYR CA C 55.28 0.2 1 162 . 33 TYR CB C 38.33 0.2 1 163 . 33 TYR N N 108.3 0.1 1 164 . 34 TRP H H 7.64 0.01 1 165 . 34 TRP C C 175.2 0.2 1 166 . 34 TRP CA C 61.74 0.2 1 167 . 34 TRP CB C 24.80 0.2 1 168 . 34 TRP N N 123.0 0.1 1 169 . 35 ASP H H 7.07 0.01 1 170 . 35 ASP C C 174.8 0.2 1 171 . 35 ASP CA C 51.14 0.2 1 172 . 35 ASP CB C 36.79 0.2 1 173 . 35 ASP N N 119.4 0.1 1 174 . 36 HIS H H 6.73 0.01 1 175 . 36 HIS C C 176.2 0.2 1 176 . 36 HIS CA C 57.34 0.2 1 177 . 36 HIS CB C 32.58 0.2 1 178 . 36 HIS N N 121.2 0.1 1 179 . 37 LYS H H 8.53 0.01 1 180 . 37 LYS C C 175.9 0.2 1 181 . 37 LYS CA C 55.10 0.2 1 182 . 37 LYS CB C 32.47 0.2 1 183 . 37 LYS N N 124.0 0.1 1 184 . 38 GLU H H 5.23 0.01 1 185 . 38 GLU C C 175.3 0.2 1 186 . 38 GLU CA C 54.90 0.2 1 187 . 38 GLU CB C 30.33 0.2 1 188 . 38 GLU N N 116.8 0.1 1 189 . 39 GLU H H 8.62 0.01 1 190 . 39 GLU C C 177.9 0.2 1 191 . 39 GLU CA C 55.43 0.2 1 192 . 39 GLU CB C 30.29 0.2 1 193 . 39 GLU N N 119.4 0.1 1 194 . 40 GLY H H 9.37 0.01 1 195 . 40 GLY C C 170.1 0.2 1 196 . 40 GLY CA C 45.23 0.2 1 197 . 40 GLY N N 112.2 0.1 1 198 . 41 LEU H H 8.00 0.01 1 199 . 41 LEU C C 173.3 0.2 1 200 . 41 LEU CA C 52.07 0.2 1 201 . 41 LEU CB C 46.26 0.2 1 202 . 41 LEU N N 118.0 0.1 1 203 . 41 LEU CD2 C 24.83 0.2 1 204 . 41 LEU HD2 H 0.22 0.01 1 205 . 41 LEU CD1 C 24.11 0.2 1 206 . 41 LEU HD1 H 0.51 0.01 1 207 . 42 TYR H H 8.98 0.01 1 208 . 42 TYR C C 174.8 0.2 1 209 . 42 TYR CA C 56.97 0.2 1 210 . 42 TYR CB C 38.22 0.2 1 211 . 42 TYR N N 118.3 0.1 1 212 . 43 VAL H H 9.18 0.01 1 213 . 43 VAL C C 173.8 0.2 1 214 . 43 VAL CA C 56.69 0.2 1 215 . 43 VAL CB C 32.71 0.2 1 216 . 43 VAL N N 118.4 0.1 1 217 . 43 VAL CG2 C 19.83 0.2 1 218 . 43 VAL HG2 H 0.08 0.01 1 219 . 43 VAL CG1 C 18.11 0.2 1 220 . 43 VAL HG1 H 0.69 0.01 1 221 . 44 ASP H H 8.59 0.01 1 222 . 44 ASP C C 178.7 0.2 1 223 . 44 ASP CA C 54.63 0.2 1 224 . 44 ASP CB C 43.45 0.2 1 225 . 44 ASP N N 121.3 0.1 1 226 . 45 ILE H H 8.45 0.01 1 227 . 45 ILE C C 173.6 0.2 1 228 . 45 ILE CA C 61.51 0.2 1 229 . 45 ILE CB C 38.59 0.2 1 230 . 45 ILE N N 130.5 0.1 1 231 . 45 ILE CD1 C 14.83 0.2 1 232 . 45 ILE HD1 H 0.92 0.01 1 233 . 46 VAL H H 8.84 0.01 1 234 . 46 VAL C C 176.2 0.2 1 235 . 46 VAL CA C 64.66 0.2 1 236 . 46 VAL CB C 31.38 0.2 1 237 . 46 VAL N N 119.8 0.1 1 238 . 46 VAL CG2 C 21.29 0.2 1 239 . 46 VAL HG2 H 0.92 0.01 1 240 . 47 SER H H 7.2 0.01 1 241 . 47 SER C C 175.8 0.2 1 242 . 47 SER CA C 58.01 0.2 1 243 . 47 SER CB C 64.63 0.2 1 244 . 47 SER N N 107.9 0.1 1 245 . 48 GLY H H 8.55 0.01 1 246 . 48 GLY C C 174.4 0.2 1 247 . 48 GLY CA C 44.72 0.2 1 248 . 48 GLY N N 110.6 0.1 1 249 . 49 LYS H H 7.85 0.01 1 250 . 49 LYS C C 174.5 0.2 1 251 . 49 LYS CA C 52.80 0.2 1 252 . 49 LYS CB C 31.05 0.2 1 253 . 49 LYS N N 120.9 0.1 1 254 . 50 PRO C C 173.0 0.2 1 255 . 50 PRO CA C 63.41 0.2 1 256 . 50 PRO CB C 31.71 0.2 1 257 . 51 LEU CD2 C 27.11 0.2 1 258 . 51 LEU HD2 H 0.78 0.01 1 259 . 51 LEU CD1 C 23.59 0.2 1 260 . 51 LEU HD1 H 0.63 0.01 1 261 . 51 LEU H H 8.04 0.01 1 262 . 51 LEU C C 173.8 0.2 1 263 . 51 LEU CA C 54.98 0.2 1 264 . 51 LEU CB C 45.85 0.2 1 265 . 51 LEU N N 119.0 0.1 1 266 . 52 PHE H H 7.73 0.01 1 267 . 52 PHE C C 174.8 0.2 1 268 . 52 PHE CA C 55.38 0.2 1 269 . 52 PHE CB C 45.13 0.2 1 270 . 52 PHE N N 110.6 0.1 1 271 . 53 THR H H 9.62 0.01 1 272 . 53 THR C C 174.9 0.2 1 273 . 53 THR CA C 59.50 0.2 1 274 . 53 THR CB C 71.40 0.2 1 275 . 53 THR N N 111.4 0.1 1 276 . 54 SER H H 9.04 0.01 1 277 . 54 SER C C 177.1 0.2 1 278 . 54 SER CA C 60.29 0.2 1 279 . 54 SER CB C 62.67 0.2 1 280 . 54 SER N N 113.8 0.1 1 281 . 55 LYS H H 7.67 0.01 1 282 . 55 LYS C C 176.8 0.2 1 283 . 55 LYS CA C 57.28 0.2 1 284 . 55 LYS CB C 30.74 0.2 1 285 . 55 LYS N N 121.9 0.1 1 286 . 56 ASP H H 7.36 0.01 1 287 . 56 ASP C C 173.9 0.2 1 288 . 56 ASP CA C 53.46 0.2 1 289 . 56 ASP CB C 41.43 0.2 1 290 . 56 ASP N N 115.4 0.1 1 291 . 57 LYS H H 7.47 0.01 1 292 . 57 LYS C C 175.6 0.2 1 293 . 57 LYS CA C 55.43 0.2 1 294 . 57 LYS CB C 34.14 0.2 1 295 . 57 LYS N N 124.6 0.1 1 296 . 58 PHE C C 173.2 0.2 1 297 . 58 PHE CA C 54.71 0.2 1 298 . 58 PHE CB C 41.05 0.2 1 299 . 59 ASP H H 8.74 0.01 1 300 . 59 ASP C C 175.2 0.2 1 301 . 59 ASP CA C 54.19 0.2 1 302 . 59 ASP CB C 39.82 0.2 1 303 . 59 ASP N N 120.9 0.1 1 304 . 60 SER H H 8.07 0.01 1 305 . 60 SER CA C 56.46 0.2 1 306 . 60 SER CB C 63.74 0.2 1 307 . 60 SER N N 117.1 0.1 1 308 . 61 GLN C C 175.1 0.2 1 309 . 61 GLN CA C 55.59 0.2 1 310 . 61 GLN CB C 27.10 0.2 1 311 . 62 CYS H H 7.96 0.01 1 312 . 62 CYS C C 173.3 0.2 1 313 . 62 CYS CA C 58.15 0.2 1 314 . 62 CYS CB C 27.83 0.2 1 315 . 62 CYS N N 114.5 0.1 1 316 . 63 GLY H H 7.53 0.01 1 317 . 63 GLY C C 172.5 0.2 1 318 . 63 GLY CA C 43.54 0.2 1 319 . 63 GLY N N 105.0 0.1 1 320 . 64 TRP H H 7.76 0.01 1 321 . 64 TRP C C 173.4 0.2 1 322 . 64 TRP CA C 58.09 0.2 1 323 . 64 TRP CB C 29.50 0.2 1 324 . 64 TRP N N 120.6 0.1 1 325 . 65 PRO CA C 63.57 0.2 1 326 . 65 PRO CB C 30.35 0.2 1 327 . 66 SER H H 8.28 0.01 1 328 . 66 SER C C 171.0 0.2 1 329 . 66 SER CA C 56.24 0.2 1 330 . 66 SER CB C 65.29 0.2 1 331 . 66 SER N N 119.2 0.1 1 332 . 67 PHE H H 8.54 0.01 1 333 . 67 PHE C C 177.1 0.2 1 334 . 67 PHE CA C 54.56 0.2 1 335 . 67 PHE CB C 44.05 0.2 1 336 . 67 PHE N N 117.5 0.1 1 337 . 68 THR H H 10.03 0.01 1 338 . 68 THR C C 174.3 0.2 1 339 . 68 THR CA C 62.97 0.2 1 340 . 68 THR CB C 68.98 0.2 1 341 . 68 THR N N 113.7 0.1 1 342 . 69 LYS H H 7.16 0.01 1 343 . 69 LYS C C 172.1 0.2 1 344 . 69 LYS CA C 53.60 0.2 1 345 . 69 LYS CB C 31.81 0.2 1 346 . 69 LYS N N 113.5 0.1 1 347 . 70 PRO C C 176.2 0.2 1 348 . 70 PRO CA C 60.4 0.2 1 349 . 70 PRO CB C 32 0.2 1 350 . 71 ILE C C 175.7 0.2 1 351 . 71 ILE CA C 61.1 0.2 1 352 . 71 ILE CB C 35.7 0.2 1 353 . 71 ILE CD1 C 13.17 0.2 1 354 . 71 ILE HD1 H 0.40 0.01 1 355 . 71 ILE H H 7.47 0.01 1 356 . 71 ILE N N 119.7 0.1 1 357 . 72 GLU H H 8.29 0.01 1 358 . 72 GLU N N 125.7 0.1 1 359 . 72 GLU C C 176.7 0.2 1 360 . 72 GLU CA C 58.60 0.2 1 361 . 72 GLU CB C 28.61 0.2 1 362 . 73 GLU H H 8.81 0.01 1 363 . 73 GLU C C 176.2 0.2 1 364 . 73 GLU CA C 57.57 0.2 1 365 . 73 GLU CB C 27.95 0.2 1 366 . 73 GLU N N 115.7 0.1 1 367 . 74 GLU H H 7.58 0.01 1 368 . 74 GLU C C 176.4 0.2 1 369 . 74 GLU CA C 54.86 0.2 1 370 . 74 GLU CB C 30.96 0.2 1 371 . 74 GLU N N 115.9 0.1 1 372 . 75 VAL CG1 C 20.97 0.2 1 373 . 75 VAL HG1 H 0.53 0.01 1 374 . 75 VAL CG2 C 21.44 0.2 1 375 . 75 VAL HG2 H 0.63 0.01 1 376 . 75 VAL H H 7.81 0.01 1 377 . 75 VAL C C 173.5 0.2 1 378 . 75 VAL CA C 60.48 0.2 1 379 . 75 VAL CB C 33.35 0.2 1 380 . 75 VAL N N 117.2 0.1 1 381 . 76 GLU H H 9.19 0.01 1 382 . 76 GLU C C 174.1 0.2 1 383 . 76 GLU CA C 54.04 0.2 1 384 . 76 GLU CB C 32.86 0.2 1 385 . 76 GLU N N 124.7 0.1 1 386 . 77 GLU H H 8.48 0.01 1 387 . 77 GLU C C 176.1 0.2 1 388 . 77 GLU CA C 54.04 0.2 1 389 . 77 GLU CB C 30.40 0.2 1 390 . 77 GLU N N 122.2 0.1 1 391 . 78 LYS H H 8.97 0.01 1 392 . 78 LYS C C 174.2 0.2 1 393 . 78 LYS CA C 54.15 0.2 1 394 . 78 LYS CB C 35.28 0.2 1 395 . 78 LYS N N 121.8 0.1 1 396 . 79 LEU CD2 C 23.36 0.2 1 397 . 79 LEU HD2 H 0.91 0.01 1 398 . 79 LEU CD1 C 25.03 0.2 1 399 . 79 LEU HD1 H 0.88 0.01 1 400 . 79 LEU H H 8.61 0.01 1 401 . 79 LEU C C 176.1 0.2 1 402 . 79 LEU CA C 56.13 0.2 1 403 . 79 LEU CB C 41.17 0.2 1 404 . 79 LEU N N 125.3 0.1 1 405 . 80 ASP H H 9.33 0.01 1 406 . 80 ASP C C 176.9 0.2 1 407 . 80 ASP CA C 52.23 0.2 1 408 . 80 ASP CB C 42.85 0.2 1 409 . 80 ASP N N 126.9 0.1 1 410 . 81 THR H H 8.99 0.01 1 411 . 81 THR C C 174.8 0.2 1 412 . 81 THR CA C 60.28 0.2 1 413 . 81 THR CB C 67.38 0.2 1 414 . 81 THR N N 118.8 0.1 1 415 . 82 SER H H 8.42 0.01 1 416 . 82 SER C C 175.3 0.2 1 417 . 82 SER CA C 59.18 0.2 1 418 . 82 SER CB C 63.44 0.2 1 419 . 82 SER N N 118.3 0.1 1 420 . 83 HIS H H 9.00 0.01 1 421 . 83 HIS C C 174.5 0.2 1 422 . 83 HIS CA C 56.47 0.2 1 423 . 83 HIS CB C 26.14 0.2 1 424 . 83 HIS N N 113.3 0.1 1 425 . 84 GLY H H 8.71 0.01 1 426 . 84 GLY C C 173.8 0.2 1 427 . 84 GLY CA C 45.90 0.2 1 428 . 84 GLY N N 105.1 0.1 1 429 . 85 MET H H 7.34 0.01 1 430 . 85 MET C C 173.3 0.2 1 431 . 85 MET CA C 53.62 0.2 1 432 . 85 MET CB C 36.08 0.2 1 433 . 85 MET N N 118.2 0.1 1 434 . 86 ILE CD1 C 12.47 0.2 1 435 . 86 ILE HD1 H 0.83 0.01 1 436 . 86 ILE H H 8.13 0.01 1 437 . 86 ILE C C 175.5 0.2 1 438 . 86 ILE CA C 60.76 0.2 1 439 . 86 ILE CB C 37.18 0.2 1 440 . 86 ILE N N 119.0 0.1 1 441 . 87 ARG H H 8.79 0.01 1 442 . 87 ARG C C 174.2 0.2 1 443 . 87 ARG CA C 53.53 0.2 1 444 . 87 ARG CB C 36.49 0.2 1 445 . 87 ARG N N 125.4 0.1 1 446 . 88 THR H H 9.47 0.01 1 447 . 88 THR C C 173.8 0.2 1 448 . 88 THR CA C 61.65 0.2 1 449 . 88 THR CB C 68.01 0.2 1 450 . 88 THR N N 119.3 0.1 1 451 . 89 GLU H H 9.41 0.01 1 452 . 89 GLU C C 174.5 0.2 1 453 . 89 GLU CA C 54.36 0.2 1 454 . 89 GLU CB C 30.30 0.2 1 455 . 89 GLU N N 129.2 0.1 1 456 . 90 VAL CG2 C 22.7 0.2 1 457 . 90 VAL HG2 H 0.88 0.01 1 458 . 90 VAL CG1 C 20.71 0.2 1 459 . 90 VAL HG1 H 0.69 0.01 1 460 . 90 VAL H H 8.09 0.01 1 461 . 90 VAL C C 174.5 0.2 1 462 . 90 VAL CA C 59.09 0.2 1 463 . 90 VAL CB C 32.92 0.2 1 464 . 90 VAL N N 120.6 0.1 1 465 . 91 ARG H H 9.00 0.01 1 466 . 91 ARG C C 175.1 0.2 1 467 . 91 ARG CA C 53.73 0.2 1 468 . 91 ARG CB C 33.71 0.2 1 469 . 91 ARG N N 124.1 0.1 1 470 . 92 SER H H 9.08 0.01 1 471 . 92 SER C C 175.3 0.2 1 472 . 92 SER CA C 54.77 0.2 1 473 . 92 SER CB C 65.38 0.2 1 474 . 92 SER N N 114.8 0.1 1 475 . 93 ARG H H 8.72 0.01 1 476 . 93 ARG C C 178.1 0.2 1 477 . 93 ARG CA C 58.97 0.2 1 478 . 93 ARG CB C 30.22 0.2 1 479 . 93 ARG N N 123.3 0.1 1 480 . 94 THR C C 175.8 0.2 1 481 . 94 THR CA C 66.89 0.2 1 482 . 94 THR CB C 66.89 0.2 1 483 . 95 ALA H H 7.89 0.01 1 484 . 95 ALA C C 176.8 0.2 1 485 . 95 ALA CA C 51.66 0.2 1 486 . 95 ALA CB C 18.67 0.2 1 487 . 95 ALA N N 118.5 0.1 1 488 . 96 ASP H H 7.37 0.01 1 489 . 96 ASP C C 176.3 0.2 1 490 . 96 ASP CA C 54.56 0.2 1 491 . 96 ASP CB C 38.87 0.2 1 492 . 96 ASP N N 119.2 0.1 1 493 . 97 SER H H 7.90 0.01 1 494 . 97 SER C C 175.9 0.2 1 495 . 97 SER CA C 56.55 0.2 1 496 . 97 SER CB C 63.17 0.2 1 497 . 97 SER N N 112.6 0.1 1 498 . 98 HIS H H 8.98 0.01 1 499 . 98 HIS C C 172.5 0.2 1 500 . 98 HIS CA C 58.29 0.2 1 501 . 98 HIS CB C 26.59 0.2 1 502 . 98 HIS N N 123.0 0.1 1 503 . 99 LEU CD1 C 23.5 0.2 1 504 . 99 LEU HD1 H 0.69 0.01 1 505 . 99 LEU CD2 C 27.2 0.2 1 506 . 99 LEU HD2 H 0.72 0.01 1 507 . 99 LEU H H 7.72 0.01 1 508 . 99 LEU C C 177.8 0.2 1 509 . 99 LEU CA C 53.68 0.2 1 510 . 99 LEU CB C 42.34 0.2 1 511 . 99 LEU N N 119.4 0.1 1 512 . 100 GLY H H 6.64 0.01 1 513 . 100 GLY C C 170.9 0.2 1 514 . 100 GLY CA C 45.32 0.2 1 515 . 100 GLY N N 103.6 0.1 1 516 . 101 HIS H H 8.51 0.01 1 517 . 101 HIS C C 171.9 0.2 1 518 . 101 HIS CA C 56.42 0.2 1 519 . 101 HIS CB C 35.90 0.2 1 520 . 101 HIS N N 121.4 0.1 1 521 . 102 VAL CG1 C 21.28 0.2 1 522 . 102 VAL HG1 H 0.06 0.01 1 523 . 102 VAL CG2 C 18.91 0.2 1 524 . 102 VAL HG2 H 0.47 0.01 1 525 . 102 VAL H H 8.24 0.01 1 526 . 102 VAL C C 173.2 0.2 1 527 . 102 VAL CA C 57.89 0.2 1 528 . 102 VAL CB C 33.93 0.2 1 529 . 102 VAL N N 117.9 0.1 1 530 . 103 PHE H H 9.05 0.01 1 531 . 103 PHE C C 175.0 0.2 1 532 . 103 PHE CA C 55.98 0.2 1 533 . 103 PHE CB C 42.41 0.2 1 534 . 103 PHE N N 127.3 0.1 1 535 . 104 ASN HD21 H 8.11 0.01 2 536 . 104 ASN HD22 H 6.9 0.01 2 537 . 104 ASN ND2 N 111.7 0.1 1 538 . 104 ASN H H 8.86 0.01 1 539 . 104 ASN C C 175.0 0.2 1 540 . 104 ASN CA C 52.43 0.2 1 541 . 104 ASN CB C 37.17 0.2 1 542 . 104 ASN N N 120.3 0.1 1 543 . 105 ASP H H 7.74 0.01 1 544 . 105 ASP C C 177.8 0.2 1 545 . 105 ASP CA C 52.36 0.2 1 546 . 105 ASP CB C 39.91 0.2 1 547 . 105 ASP N N 119.2 0.1 1 548 . 106 GLY H H 8.10 0.01 1 549 . 106 GLY C C 172.5 0.2 1 550 . 106 GLY CA C 43.72 0.2 1 551 . 106 GLY N N 106.6 0.1 1 552 . 108 GLY H H 8.56 0.01 1 553 . 108 GLY N N 109.5 0.1 1 554 . 109 PRO C C 177.6 0.2 1 555 . 109 PRO CA C 62.78 0.2 1 556 . 109 PRO CB C 33.61 0.2 1 557 . 110 ASN HD21 H 8.02 0.01 2 558 . 110 ASN HD22 H 7.68 0.01 2 559 . 110 ASN ND2 N 113.5 0.1 1 560 . 110 ASN H H 8.78 0.01 1 561 . 110 ASN C C 176.2 0.2 1 562 . 110 ASN CA C 53.80 0.2 1 563 . 110 ASN CB C 38.49 0.2 1 564 . 110 ASN N N 118.6 0.1 1 565 . 111 GLY H H 8.09 0.01 1 566 . 111 GLY C C 173.8 0.2 1 567 . 111 GLY CA C 45.55 0.2 1 568 . 111 GLY N N 107.9 0.1 1 569 . 112 LEU CD2 C 25.81 0.2 1 570 . 112 LEU HD2 H 1.05 0.01 1 571 . 112 LEU CD1 C 22.7 0.2 1 572 . 112 LEU HD1 H 0.71 0.01 1 573 . 112 LEU H H 7.54 0.01 1 574 . 112 LEU C C 175.8 0.2 1 575 . 112 LEU CA C 54.14 0.2 1 576 . 112 LEU CB C 42.79 0.2 1 577 . 112 LEU N N 118.8 0.1 1 578 . 113 ARG H H 8.91 0.01 1 579 . 113 ARG C C 174.2 0.2 1 580 . 113 ARG CA C 54.66 0.2 1 581 . 113 ARG CB C 33.48 0.2 1 582 . 113 ARG N N 120.7 0.1 1 583 . 114 TYR H H 10.10 0.01 1 584 . 114 TYR C C 173.6 0.2 1 585 . 114 TYR CA C 58.48 0.2 1 586 . 114 TYR CB C 36.96 0.2 1 587 . 114 TYR N N 128.2 0.1 1 588 . 115 CYS H H 9.40 0.01 1 589 . 115 CYS C C 172.0 0.2 1 590 . 115 CYS CA C 58.31 0.2 1 591 . 115 CYS CB C 26.84 0.2 1 592 . 115 CYS N N 129.6 0.1 1 593 . 116 ILE CD1 C 9.32 0.2 1 594 . 116 ILE HD1 H 0.43 0.01 1 595 . 116 ILE H H 8.58 0.01 1 596 . 116 ILE C C 172.7 0.2 1 597 . 116 ILE CA C 55.98 0.2 1 598 . 116 ILE CB C 37.68 0.2 1 599 . 116 ILE N N 129.9 0.1 1 600 . 117 ASN HD21 H 6.68 0.01 2 601 . 117 ASN HD22 H 7.82 0.01 2 602 . 117 ASN ND2 N 115.7 0.1 1 603 . 117 ASN H H 7.56 0.01 1 604 . 117 ASN C C 176.1 0.2 1 605 . 117 ASN CA C 53.27 0.2 1 606 . 117 ASN CB C 42.19 0.2 1 607 . 117 ASN N N 119.2 0.1 1 608 . 118 SER H H 13.13 0.01 1 609 . 118 SER C C 177.6 0.2 1 610 . 118 SER CA C 63.55 0.2 1 611 . 118 SER CB C 62.17 0.2 1 612 . 118 SER N N 128.6 0.1 1 613 . 119 ALA H H 10.07 0.01 1 614 . 119 ALA C C 175.3 0.2 1 615 . 119 ALA CA C 52.36 0.2 1 616 . 119 ALA CB C 18.53 0.2 1 617 . 119 ALA N N 121.1 0.1 1 618 . 120 ALA H H 7.35 0.01 1 619 . 120 ALA C C 176.7 0.2 1 620 . 120 ALA CA C 51.16 0.2 1 621 . 120 ALA CB C 19.66 0.2 1 622 . 120 ALA N N 112.9 0.1 1 623 . 121 LEU CD2 C 26.35 0.2 2 624 . 121 LEU HD2 H 0.68 0.01 2 625 . 121 LEU H H 8.29 0.01 1 626 . 121 LEU C C 175.2 0.2 1 627 . 121 LEU CA C 52.78 0.2 1 628 . 121 LEU CB C 46.43 0.2 1 629 . 121 LEU N N 117.4 0.1 1 630 . 122 ARG H H 8.93 0.01 1 631 . 122 ARG C C 174.7 0.2 1 632 . 122 ARG CA C 54.72 0.2 1 633 . 122 ARG CB C 32.90 0.2 1 634 . 122 ARG N N 118.4 0.1 1 635 . 123 PHE H H 7.91 0.01 1 636 . 123 PHE C C 173.8 0.2 1 637 . 123 PHE CA C 56.11 0.2 1 638 . 123 PHE CB C 38.98 0.2 1 639 . 123 PHE N N 125.2 0.1 1 640 . 124 VAL CG1 C 20.04 0.2 1 641 . 124 VAL HG1 H 0.52 0.01 1 642 . 124 VAL CG2 C 20.84 0.2 1 643 . 124 VAL HG2 H 0.56 0.01 1 644 . 124 VAL H H 8.52 0.01 1 645 . 124 VAL C C 171.5 0.2 1 646 . 124 VAL CA C 57.75 0.2 1 647 . 124 VAL CB C 32.81 0.2 1 648 . 124 VAL N N 130.7 0.1 1 649 . 125 PRO C C 177.4 0.2 1 650 . 125 PRO CA C 61.45 0.2 1 651 . 125 PRO CB C 31.99 0.2 1 652 . 126 LYS H H 7.99 0.01 1 653 . 126 LYS C C 177.4 0.2 1 654 . 126 LYS CA C 58.78 0.2 1 655 . 126 LYS CB C 31.64 0.2 1 656 . 126 LYS N N 120.4 0.1 1 657 . 127 HIS H H 8.31 0.01 1 658 . 127 HIS C C 175.3 0.2 1 659 . 127 HIS CA C 57.89 0.2 1 660 . 127 HIS CB C 28.53 0.2 1 661 . 127 HIS N N 112.8 0.1 1 662 . 128 LYS H H 7.54 0.01 1 663 . 128 LYS N N 118.8 0.1 1 664 . 128 LYS C C 175.8 0.2 1 665 . 128 LYS CA C 54.30 0.2 1 666 . 128 LYS CB C 32.47 0.2 1 667 . 129 LEU CD1 C 22.32 0.2 1 668 . 129 LEU HD1 H 0.43 0.01 1 669 . 129 LEU CD2 C 26.35 0.2 1 670 . 129 LEU HD2 H 0.68 0.01 1 671 . 129 LEU H H 7.17 0.01 1 672 . 129 LEU C C 178.7 0.2 1 673 . 129 LEU CA C 58.53 0.2 1 674 . 129 LEU CB C 39.24 0.2 1 675 . 129 LEU N N 118.0 0.1 1 676 . 130 LYS H H 8.92 0.01 1 677 . 130 LYS C C 180.0 0.2 1 678 . 130 LYS CA C 59.82 0.2 1 679 . 130 LYS CB C 30.79 0.2 1 680 . 130 LYS N N 118.2 0.1 1 681 . 131 GLU H H 8.71 0.01 1 682 . 131 GLU C C 177.5 0.2 1 683 . 131 GLU CA C 58.37 0.2 1 684 . 131 GLU CB C 28.64 0.2 1 685 . 131 GLU N N 120.9 0.1 1 686 . 132 GLU H H 7.64 0.01 1 687 . 132 GLU C C 174.9 0.2 1 688 . 132 GLU CA C 56.63 0.2 1 689 . 132 GLU CB C 28.98 0.2 1 690 . 132 GLU N N 115.1 0.1 1 691 . 133 GLY H H 7.42 0.01 1 692 . 133 GLY C C 175.7 0.2 1 693 . 133 GLY CA C 45.49 0.2 1 694 . 133 GLY N N 104.6 0.1 1 695 . 134 TYR H H 8.62 0.01 1 696 . 134 TYR C C 176.8 0.2 1 697 . 134 TYR CA C 55.77 0.2 1 698 . 134 TYR CB C 38.34 0.2 1 699 . 134 TYR N N 118.7 0.1 1 700 . 135 GLU H H 9.09 0.01 1 701 . 135 GLU C C 178.1 0.2 1 702 . 135 GLU CA C 59.70 0.2 1 703 . 135 GLU CB C 28.41 0.2 1 704 . 135 GLU N N 122.3 0.1 1 705 . 136 SER H H 8.96 0.01 1 706 . 136 SER C C 173.9 0.2 1 707 . 136 SER CA C 60.23 0.2 1 708 . 136 SER CB C 61.64 0.2 1 709 . 136 SER N N 114.4 0.1 1 710 . 137 TYR H H 8.13 0.01 1 711 . 137 TYR C C 176.2 0.2 1 712 . 137 TYR CA C 58.77 0.2 1 713 . 137 TYR CB C 38.41 0.2 1 714 . 137 TYR N N 117.2 0.1 1 715 . 138 LEU CD1 C 25.02 0.2 1 716 . 138 LEU HD1 H 1.09 0.01 1 717 . 138 LEU CD2 C 24.42 0.2 1 718 . 138 LEU HD2 H 1.00 0.01 1 719 . 138 LEU H H 7.79 0.01 1 720 . 138 LEU C C 179.3 0.2 1 721 . 138 LEU CA C 58.26 0.2 1 722 . 138 LEU CB C 40.83 0.2 1 723 . 138 LEU N N 120.8 0.1 1 724 . 139 HIS C C 176.1 0.2 1 725 . 139 HIS CA C 57.53 0.2 1 726 . 139 HIS CB C 28.52 0.2 1 727 . 140 LEU CD2 C 25.81 0.2 1 728 . 140 LEU HD2 H 0.86 0.01 1 729 . 140 LEU CD1 C 22.23 0.2 1 730 . 140 LEU HD1 H 0.68 0.01 1 731 . 140 LEU H H 6.91 0.01 1 732 . 140 LEU C C 177.1 0.2 1 733 . 140 LEU CA C 55.60 0.2 1 734 . 140 LEU CB C 40.22 0.2 1 735 . 140 LEU N N 118.9 0.1 1 736 . 141 PHE H H 7.62 0.01 1 737 . 141 PHE C C 174.9 0.2 1 738 . 141 PHE CA C 57.23 0.2 1 739 . 141 PHE CB C 38.65 0.2 1 740 . 141 PHE N N 114.0 0.1 1 741 . 142 ASN H H 7.61 0.01 1 742 . 142 ASN C C 174.9 0.2 1 743 . 142 ASN CA C 52.75 0.2 1 744 . 142 ASN CB C 38.48 0.2 1 745 . 142 ASN N N 118.9 0.1 1 746 . 143 LYS H H 8.48 0.01 1 747 . 143 LYS C C 176.1 0.2 1 748 . 143 LYS CA C 55.99 0.2 1 749 . 143 LYS CB C 31.98 0.2 1 750 . 143 LYS N N 122.2 0.1 1 751 . 144 LEU CD2 C 24.66 0.2 1 752 . 144 LEU HD2 H 0.91 0.01 1 753 . 144 LEU CD1 C 23.33 0.2 1 754 . 144 LEU HD1 H 0.84 0.01 1 755 . 144 LEU H H 8.39 0.01 1 756 . 144 LEU C C 176.9 0.2 1 757 . 144 LEU CA C 54.64 0.2 1 758 . 144 LEU CB C 41.15 0.2 1 759 . 144 LEU N N 123.7 0.1 1 760 . 145 GLU H H 8.40 0.01 1 761 . 145 GLU C C 175.7 0.2 1 762 . 145 GLU CA C 55.56 0.2 1 763 . 145 GLU CB C 29.66 0.2 1 764 . 145 GLU N N 121.9 0.1 1 stop_ save_