data_4431 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of the Soluble Methane Monooxygenase Regulatory Protein B ; _BMRB_accession_number 4431 _BMRB_flat_file_name bmr4431.str _Entry_type original _Submission_date 1999-10-04 _Accession_date 1999-10-05 _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 Walters K. J. . 2 Gassner G. T. . 3 Lippard S. J. . 4 Wagner G. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 640 "13C chemical shifts" 241 "15N chemical shifts" 151 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-01-09 update BMRB 'corrected chemical shift referencing annotation for 13C' 2000-05-11 update author 'Chemical shift for residue 89 CA removed.' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Walters, K. J., Gassner, G. T., Lippard, S. J., and Wagner, G., "Structure of the soluble methane monooxygenase regulatory protein B," Proc Natl Acad Sci U S A. 1999 96(14):7877-82. ; _Citation_title 'Structure of the soluble methane monooxygenase regulatory protein B' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99324156 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Walters K. J. . 2 Gassner G. T. . 3 Lippard S. J. . 4 Wagner G. . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U. S. A.' _Journal_name_full 'Proceedings of the National Academy of Sciences, U.S.A.' _Journal_volume 96 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7877 _Page_last 7882 _Year 1999 _Details . loop_ _Keyword 'hydroxylase regulatory protein' stop_ save_ ################################## # Molecular system description # ################################## save_system_MMOB _Saveframe_category molecular_system _Mol_system_name 'methane monooxygenase regulatory protein B' _Abbreviation_common MMOB _Enzyme_commission_number n/a loop_ _Mol_system_component_name _Mol_label MMOB $MMOB stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Biological_function 'regulatory protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MMOB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'methane monooxygenase regulatory protein B' _Name_variant none _Abbreviation_common MMOB _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 141 _Mol_residue_sequence ; MSVNSNAYDAGIMGLKGKDF ADQFFADENQVVHESDTVVL VLKKSDEINTFIEEILLTDY KKNVNPTVNVEDRAGYWWIK ANGKIEVDCDEISELLGRQF NVYDFLVDVSSTIGRAYTLG NKFTITSELMGLDRKLEDYH A ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 VAL 4 ASN 5 SER 6 ASN 7 ALA 8 TYR 9 ASP 10 ALA 11 GLY 12 ILE 13 MET 14 GLY 15 LEU 16 LYS 17 GLY 18 LYS 19 ASP 20 PHE 21 ALA 22 ASP 23 GLN 24 PHE 25 PHE 26 ALA 27 ASP 28 GLU 29 ASN 30 GLN 31 VAL 32 VAL 33 HIS 34 GLU 35 SER 36 ASP 37 THR 38 VAL 39 VAL 40 LEU 41 VAL 42 LEU 43 LYS 44 LYS 45 SER 46 ASP 47 GLU 48 ILE 49 ASN 50 THR 51 PHE 52 ILE 53 GLU 54 GLU 55 ILE 56 LEU 57 LEU 58 THR 59 ASP 60 TYR 61 LYS 62 LYS 63 ASN 64 VAL 65 ASN 66 PRO 67 THR 68 VAL 69 ASN 70 VAL 71 GLU 72 ASP 73 ARG 74 ALA 75 GLY 76 TYR 77 TRP 78 TRP 79 ILE 80 LYS 81 ALA 82 ASN 83 GLY 84 LYS 85 ILE 86 GLU 87 VAL 88 ASP 89 CYS 90 ASP 91 GLU 92 ILE 93 SER 94 GLU 95 LEU 96 LEU 97 GLY 98 ARG 99 GLN 100 PHE 101 ASN 102 VAL 103 TYR 104 ASP 105 PHE 106 LEU 107 VAL 108 ASP 109 VAL 110 SER 111 SER 112 THR 113 ILE 114 GLY 115 ARG 116 ALA 117 TYR 118 THR 119 LEU 120 GLY 121 ASN 122 LYS 123 PHE 124 THR 125 ILE 126 THR 127 SER 128 GLU 129 LEU 130 MET 131 GLY 132 LEU 133 ASP 134 ARG 135 LYS 136 LEU 137 GLU 138 ASP 139 TYR 140 HIS 141 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-11 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 17463 MMOB 100.00 141 100.00 100.00 2.76e-97 PDB 1CKV "Structure Of The Soluble Methane Monooxygenase Regulatory Protein B" 100.00 141 100.00 100.00 2.76e-97 PDB 4GAM "Complex Structure Of Methane Monooxygenase Hydroxylase And Regulatory Subunit" 100.00 141 100.00 100.00 2.76e-97 GB AAF04158 "soluble methane monooxygenase regulatory protein B [Methylococcus capsulatus]" 100.00 141 100.00 100.00 2.76e-97 GB AAU92726 "methane monooxygenase, B subunit [Methylococcus capsulatus str. Bath]" 100.00 141 100.00 100.00 2.76e-97 REF WP_010960484 "methane monooxygenase regulatory protein B [Methylococcus capsulatus]" 100.00 141 100.00 100.00 2.76e-97 SP P18797 "RecName: Full=Methane monooxygenase regulatory protein B" 100.00 141 100.00 100.00 2.76e-97 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MMOB 'Methylococcus capsulatus' 414 Eubacteria . Methylococcus capsulatus 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 $MMOB '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 $MMOB 1 mM '[U-13C 100%; U-15N 100%]' phosphate 50 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ save_NMR_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 400 _Details . save_ save_NMR_spectrometer_5 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HN(CA)CO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample_1 save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HNHA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label $sample_1 save_ save_HCCH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_1 save_ save_HC(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name HC(CO)NH _Sample_label $sample_1 save_ save_H(CCO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH _Sample_label $sample_1 save_ save_HNHB_9 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _Sample_label $sample_1 save_ save_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HC(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 n/a temperature 298 0.1 K 'ionic strength' 0.05 . M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details ; The reference is to TMS and 2.81 ppm should be added to all carbon values when compared with TSP. ; 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_citation_label _Correction_value_citation_label TSP H 1 'methyl protons' ppm 0.00 internal direct cylindrical internal parallel_to_Bo $entry_citation $entry_citation TMS C 13 'methyl protons' ppm 0.00 internal direct cylindrical internal parallel_to_Bo $entry_citation $entry_citation TSP N 15 'methyl protons' ppm 0.00 internal direct cylindrical internal parallel_to_Bo $entry_citation $entry_citation 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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HNCO HN(CA)CO HNCA HN(CO)CA HNHA HCCH-TOCSY HC(CO)NH H(CCO)NH HNHB NOESY stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name MMOB _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 . 4 ASN HB2 H 2.76 . 2 2 . 4 ASN HB3 H 2.65 . 2 3 . 5 SER N N 116.5 . 1 4 . 5 SER H H 8.26 . 1 5 . 5 SER CA C 51.1 . 1 6 . 5 SER HA H 4.30 . 1 7 . 5 SER CB C 63.8 . 1 8 . 5 SER HB2 H 3.82 . 2 9 . 5 SER HB3 H 3.73 . 2 10 . 6 ASN N N 120.2 . 1 11 . 6 ASN H H 8.36 . 1 12 . 6 ASN CA C 45.8 . 1 13 . 6 ASN HA H 4.59 . 1 14 . 6 ASN CB C 31.3 . 1 15 . 6 ASN HB2 H 2.66 . 2 16 . 7 ALA N N 123.4 . 1 17 . 7 ALA H H 8.05 . 1 18 . 7 ALA CA C 45.5 . 1 19 . 7 ALA HA H 4.13 . 1 20 . 7 ALA CB C 11.3 . 1 21 . 7 ALA HB H 1.18 . 1 22 . 8 TYR N N 118.4 . 1 23 . 8 TYR H H 7.97 . 1 24 . 8 TYR CA C 50.5 . 1 25 . 8 TYR HA H 4.38 . 1 26 . 8 TYR CB C 31.4 . 1 27 . 8 TYR HB2 H 2.89 . 2 28 . 8 TYR HB3 H 2.82 . 2 29 . 8 TYR HD1 H 6.95 . 3 30 . 8 TYR HE1 H 7.1 . 3 31 . 9 ASP N N 122.2 . 1 32 . 9 ASP H H 7.96 . 1 33 . 9 ASP CA C 45.8 . 1 34 . 9 ASP HA H 4.44 . 1 35 . 9 ASP CB C 33.6 . 1 36 . 9 ASP HB2 H 2.58 . 2 37 . 9 ASP HB3 H 2.50 . 2 38 . 10 ALA N N 124.4 . 1 39 . 10 ALA H H 8.13 . 1 40 . 10 ALA CA C 45.5 . 1 41 . 10 ALA HA H 4.09 . 1 42 . 10 ALA CB C 11.3 . 1 43 . 10 ALA HB H 1.32 . 1 44 . 11 GLY N N 106.7 . 1 45 . 11 GLY H H 8.28 . 1 46 . 11 GLY HA2 H 3.83 . 2 47 . 12 ILE N N 119.2 . 1 48 . 12 ILE H H 7.75 . 1 49 . 12 ILE CA C 54.3 . 1 50 . 12 ILE HA H 4.04 . 1 51 . 12 ILE CB C 30.8 . 1 52 . 12 ILE HB H 1.77 . 1 53 . 12 ILE HG12 H 1.32 . 2 54 . 12 ILE HG13 H 1.05 . 2 55 . 12 ILE HG2 H 0.77 . 1 56 . 12 ILE HD1 H 0.69 . 1 57 . 12 ILE CG1 C 19.8 . 4 58 . 12 ILE CG2 C 10.1 . 4 59 . 12 ILE CD1 C 5.4 . 1 60 . 13 MET N N 121.6 . 1 61 . 13 MET H H 8.21 . 1 62 . 13 MET CA C 47.7 . 1 63 . 13 MET HA H 4.34 . 1 64 . 13 MET HB2 H 1.95 . 2 65 . 13 MET HG2 H 2.48 . 2 66 . 13 MET HG3 H 2.40 . 2 67 . 13 MET HE H 1.91 . 1 68 . 13 MET CG C 24.8 . 1 69 . 13 MET CE C 9.5 . 1 70 . 14 GLY N N 108.5 . 1 71 . 14 GLY H H 8.11 . 1 72 . 14 GLY HA2 H 3.82 . 2 73 . 15 LEU N N 120.7 . 1 74 . 15 LEU H H 7.91 . 1 75 . 15 LEU CA C 48.0 . 1 76 . 15 LEU HA H 4.20 . 1 77 . 15 LEU CB C 34.8 . 1 78 . 15 LEU HB2 H 1.50 . 2 79 . 15 LEU HB3 H 1.44 . 2 80 . 15 LEU HD1 H 0.76 . 2 81 . 15 LEU CD1 C 17.3 . 2 82 . 16 LYS N N 121.0 . 1 83 . 16 LYS H H 8.20 . 1 84 . 16 LYS CA C 48.6 . 1 85 . 16 LYS HA H 4.21 . 1 86 . 16 LYS CB C 22.9 . 1 87 . 16 LYS HB2 H 1.71 . 2 88 . 16 LYS HB3 H 1.61 . 2 89 . 16 LYS HG2 H 1.29 . 2 90 . 16 LYS HD2 H 1.49 . 2 91 . 16 LYS HE2 H 3.02 . 2 92 . 17 GLY N N 109.4 . 1 93 . 17 GLY H H 8.29 . 1 94 . 17 GLY HA2 H 3.82 . 2 95 . 18 LYS N N 120.5 . 1 96 . 18 LYS H H 8.13 . 1 97 . 18 LYS CA C 48.9 . 1 98 . 18 LYS HA H 4.16 . 1 99 . 18 LYS CB C 25.4 . 1 100 . 18 LYS HB2 H 1.65 . 2 101 . 18 LYS HG2 H 1.28 . 2 102 . 18 LYS HD2 H 1.53 . 2 103 . 18 LYS HE2 H 2.85 . 2 104 . 18 LYS CG C 17.3 . 1 105 . 18 LYS CD C 21.4 . 1 106 . 18 LYS CE C 34.2 . 1 107 . 19 ASP N N 119.9 . 1 108 . 19 ASP H H 8.25 . 1 109 . 19 ASP CA C 46.4 . 1 110 . 19 ASP HA H 4.43 . 1 111 . 19 ASP CB C 33.6 . 1 112 . 19 ASP HB2 H 2.57 . 2 113 . 19 ASP HB3 H 2.48 . 2 114 . 20 PHE N N 119.7 . 1 115 . 20 PHE H H 7.95 . 1 116 . 20 PHE CA C 50.5 . 1 117 . 20 PHE HA H 4.38 . 1 118 . 20 PHE HB2 H 3.03 . 2 119 . 20 PHE HB3 H 2.90 . 2 120 . 20 PHE HD1 H 7.1 . 3 121 . 21 ALA N N 123.4 . 1 122 . 21 ALA H H 8.08 . 1 123 . 21 ALA CA C 45.8 . 1 124 . 21 ALA HA H 4.08 . 1 125 . 21 ALA HB H 1.28 . 1 126 . 22 ASP N N 118.0 . 1 127 . 22 ASP H H 8.06 . 1 128 . 22 ASP CA C 47.4 . 1 129 . 22 ASP HA H 4.39 . 1 130 . 22 ASP HB2 H 2.56 . 2 131 . 23 GLN N N 118.8 . 1 132 . 23 GLN H H 7.91 . 1 133 . 23 GLN CA C 48.3 . 1 134 . 23 GLN HA H 4.06 . 1 135 . 23 GLN CB C 21.7 . 1 136 . 23 GLN HB2 H 2.02 . 2 137 . 23 GLN HB3 H 1.76 . 2 138 . 23 GLN HG2 H 2.56 . 2 139 . 23 GLN HG3 H 2.01 . 2 140 . 23 GLN HE21 H 7.30 . 2 141 . 23 GLN HE22 H 6.67 . 2 142 . 23 GLN CG C 26.1 . 1 143 . 23 GLN NE2 N 112 . 1 144 . 24 PHE N N 119.8 . 1 145 . 24 PHE H H 8.01 . 1 146 . 24 PHE CA C 49.9 . 1 147 . 24 PHE HA H 4.34 . 1 148 . 24 PHE HB2 H 2.79 . 2 149 . 24 PHE HB3 H 2.69 . 2 150 . 24 PHE HD1 H 7.11 . 3 151 . 24 PHE HD2 H 6.88 . 3 152 . 25 PHE N N 119.7 . 1 153 . 25 PHE H H 7.94 . 1 154 . 25 PHE CA C 49.9 . 1 155 . 25 PHE HA H 4.42 . 1 156 . 25 PHE CB C 32.0 . 1 157 . 25 PHE HB2 H 3.02 . 2 158 . 25 PHE HB3 H 2.82 . 2 159 . 26 ALA N N 124.4 . 1 160 . 26 ALA H H 7.94 . 1 161 . 26 ALA CA C 49.3 . 1 162 . 26 ALA HA H 4.13 . 1 163 . 26 ALA CB C 11.9 . 1 164 . 26 ALA HB H 1.25 . 1 165 . 27 ASP N N 119.0 . 1 166 . 27 ASP H H 8.07 . 1 167 . 27 ASP CA C 46.1 . 1 168 . 27 ASP HA H 4.44 . 1 169 . 27 ASP CB C 33.6 . 1 170 . 27 ASP HB2 H 2.56 . 2 171 . 28 GLU N N 120.9 . 1 172 . 28 GLU H H 8.40 . 1 173 . 28 GLU CA C 49.2 . 1 174 . 28 GLU HA H 4.10 . 1 175 . 28 GLU CB C 22.3 . 1 176 . 28 GLU HB2 H 1.97 . 2 177 . 28 GLU HB3 H 1.86 . 2 178 . 28 GLU HG2 H 2.13 . 2 179 . 28 GLU CG C 28.9 . 1 180 . 29 ASN N N 117.5 . 1 181 . 29 ASN H H 8.31 . 1 182 . 29 ASN HA H 4.57 . 1 183 . 29 ASN HB2 H 2.67 . 2 184 . 29 ASN HD21 H 7.56 . 2 185 . 29 ASN HD22 H 6.80 . 2 186 . 29 ASN ND2 N 113.2 . 1 187 . 30 GLN N N 119.0 . 1 188 . 30 GLN H H 8.02 . 1 189 . 30 GLN CA C 47.7 . 1 190 . 30 GLN HA H 4.18 . 1 191 . 30 GLN CB C 21.7 . 1 192 . 30 GLN HB2 H 2.03 . 2 193 . 30 GLN HB3 H 1.90 . 2 194 . 30 GLN HG2 H 2.22 . 2 195 . 30 GLN HE21 H 7.52 . 2 196 . 30 GLN HE22 H 6.84 . 2 197 . 30 GLN NE2 N 112.4 . 1 198 . 31 VAL N N 120.2 . 1 199 . 31 VAL H H 7.89 . 1 200 . 31 VAL CA C 56.8 . 1 201 . 31 VAL HA H 3.96 . 1 202 . 31 VAL HG1 H 0.80 . 2 203 . 31 VAL HG2 H 0.71 . 2 204 . 32 VAL N N 123.4 . 1 205 . 32 VAL H H 8.04 . 1 206 . 32 VAL CA C 54.6 . 1 207 . 32 VAL HA H 3.94 . 1 208 . 32 VAL CB C 25.1 . 1 209 . 32 VAL HB H 1.91 . 1 210 . 32 VAL HG1 H 0.79 . 2 211 . 32 VAL CG1 C 13.2 . 2 212 . 33 HIS N N 121.8 . 1 213 . 33 HIS H H 8.47 . 1 214 . 33 HIS CA C 45.8 . 1 215 . 33 HIS HA H 4.60 . 1 216 . 33 HIS CB C 31.4 . 1 217 . 33 HIS HB2 H 2.76 . 2 218 . 33 HIS HB3 H 2.65 . 2 219 . 34 GLU N N 122.0 . 1 220 . 34 GLU H H 8.48 . 1 221 . 34 GLU CA C 48.6 . 1 222 . 34 GLU HA H 4.26 . 1 223 . 34 GLU HB2 H 2.01 . 2 224 . 34 GLU HB3 H 1.89 . 2 225 . 34 GLU HG2 H 2.19 . 2 226 . 34 GLU CG C 28.9 . 1 227 . 35 SER N N 116.4 . 1 228 . 35 SER H H 8.47 . 1 229 . 35 SER CA C 51.1 . 1 230 . 35 SER HA H 4.33 . 1 231 . 35 SER HB2 H 3.87 . 2 232 . 35 SER HB3 H 3.82 . 2 233 . 36 ASP N N 120.9 . 1 234 . 36 ASP H H 8.46 . 1 235 . 36 ASP CA C 45.8 . 1 236 . 36 ASP HA H 4.79 . 1 237 . 36 ASP CB C 33.6 . 1 238 . 36 ASP HB2 H 2.69 . 2 239 . 36 ASP HB3 H 2.64 . 2 240 . 37 THR N N 115.5 . 1 241 . 37 THR H H 7.70 . 1 242 . 37 THR CA C 55.2 . 1 243 . 37 THR HA H 4.75 . 1 244 . 37 THR CB C 63.1 . 1 245 . 37 THR HB H 3.89 . 1 246 . 37 THR HG2 H 1.03 . 1 247 . 37 THR CG2 C 14.5 . 1 248 . 38 VAL N N 118.6 . 1 249 . 38 VAL H H 8.79 . 1 250 . 38 VAL CA C 51.1 . 1 251 . 38 VAL HA H 4.63 . 1 252 . 38 VAL HB H 1.91 . 1 253 . 38 VAL HG1 H 0.67 . 2 254 . 38 VAL HG2 H 0.52 . 2 255 . 38 VAL CG1 C 15.6 . 2 256 . 39 VAL N N 118.7 . 1 257 . 39 VAL H H 8.26 . 1 258 . 39 VAL CA C 52.7 . 1 259 . 39 VAL HA H 5.05 . 1 260 . 39 VAL HB H 1.60 . 1 261 . 39 VAL HG1 H 0.74 . 2 262 . 39 VAL HG2 H 0.57 . 2 263 . 39 VAL CG1 C 14.4 . 2 264 . 39 VAL CG2 C 13.4 . 2 265 . 40 LEU N N 127.2 . 1 266 . 40 LEU H H 9.17 . 1 267 . 40 LEU HA H 4.65 . 1 268 . 40 LEU HB2 H 1.24 . 2 269 . 40 LEU HD1 H 0.90 . 2 270 . 40 LEU HD2 H 0.80 . 2 271 . 40 LEU CD1 C 17.6 . 2 272 . 40 LEU CD2 C 14.2 . 2 273 . 41 VAL N N 125.7 . 1 274 . 41 VAL H H 8.20 . 1 275 . 41 VAL CA C 53.3 . 1 276 . 41 VAL HA H 4.93 . 1 277 . 41 VAL CB C 24.2 . 1 278 . 41 VAL HB H 1.46 . 1 279 . 41 VAL HG1 H 0.0 . 2 280 . 41 VAL HG2 H -0.11 . 2 281 . 41 VAL CG1 C 12.9 . 2 282 . 42 LEU N N 125.9 . 1 283 . 42 LEU H H 9.17 . 1 284 . 42 LEU CA C 44.6 . 1 285 . 42 LEU HA H 5.23 . 1 286 . 42 LEU HB2 H 1.78 . 2 287 . 42 LEU HB3 H 1.55 . 2 288 . 42 LEU HD1 H 0.68 . 2 289 . 42 LEU HD2 H 0.52 . 2 290 . 42 LEU CD1 C 18.2 . 2 291 . 42 LEU CD2 C 12.5 . 2 292 . 43 LYS N N 123.3 . 1 293 . 43 LYS H H 8.83 . 1 294 . 43 LYS HA H 3.93 . 1 295 . 43 LYS HB2 H 1.71 . 2 296 . 43 LYS HG2 H 1.18 . 2 297 . 44 LYS N N 119.6 . 1 298 . 44 LYS H H 7.29 . 1 299 . 44 LYS HA H 4.06 . 1 300 . 44 LYS HB2 H 1.58 . 2 301 . 44 LYS HG2 H 0.74 . 2 302 . 44 LYS HG3 H 0.29 . 2 303 . 44 LYS HD2 H 1.24 . 2 304 . 45 SER N N 114.5 . 1 305 . 45 SER H H 7.42 . 1 306 . 45 SER CA C 48.9 . 1 307 . 45 SER HA H 4.49 . 1 308 . 45 SER CB C 58.0 . 1 309 . 45 SER HB2 H 4.08 . 2 310 . 45 SER HB3 H 3.94 . 2 311 . 46 ASP N N 122.1 . 1 312 . 46 ASP H H 9.14 . 1 313 . 46 ASP CA C 50.8 . 1 314 . 46 ASP HA H 4.27 . 1 315 . 46 ASP HB2 H 2.55 . 2 316 . 46 ASP HB3 H 2.43 . 2 317 . 47 GLU N N 117.8 . 1 318 . 47 GLU H H 9.16 . 1 319 . 47 GLU CA C 53.6 . 1 320 . 47 GLU HA H 3.55 . 1 321 . 47 GLU HB2 H 1.90 . 2 322 . 47 GLU HB3 H 1.65 . 2 323 . 47 GLU HG2 H 2.28 . 2 324 . 47 GLU HG3 H 2.20 . 2 325 . 48 ILE N N 118.7 . 1 326 . 48 ILE H H 7.38 . 1 327 . 48 ILE CA C 54.9 . 1 328 . 48 ILE HA H 3.76 . 1 329 . 48 ILE HB H 1.58 . 1 330 . 48 ILE HG12 H 1.125 . 2 331 . 48 ILE HG2 H 0.88 . 1 332 . 48 ILE HD1 H 0.77 . 1 333 . 48 ILE CG2 C 12.9 . 1 334 . 48 ILE CD1 C 3.8 . 1 335 . 49 ASN N N 120.2 . 1 336 . 49 ASN H H 9.24 . 1 337 . 49 ASN CA C 48.6 . 1 338 . 49 ASN HA H 4.23 . 1 339 . 49 ASN CB C 29.2 . 1 340 . 49 ASN HB2 H 3.04 . 2 341 . 49 ASN HD21 H 7.58 . 2 342 . 49 ASN HD22 H 6.27 . 2 343 . 49 ASN ND2 N 107.8 . 1 344 . 50 THR N N 116.0 . 1 345 . 50 THR H H 7.59 . 1 346 . 50 THR CA C 59.6 . 1 347 . 50 THR HA H 3.88 . 1 348 . 50 THR HB H 4.07 . 1 349 . 50 THR HG2 H 1.01 . 1 350 . 51 PHE N N 121.4 . 1 351 . 51 PHE H H 7.60 . 1 352 . 51 PHE CA C 53.0 . 1 353 . 51 PHE HA H 3.92 . 1 354 . 51 PHE HB2 H 3.32 . 2 355 . 51 PHE HB3 H 2.92 . 2 356 . 51 PHE HD1 H 6.93 . 3 357 . 52 ILE N N 121.2 . 1 358 . 52 ILE H H 8.56 . 1 359 . 52 ILE CA C 51.5 . 1 360 . 52 ILE HA H 3.75 . 1 361 . 52 ILE HB H 1.34 . 1 362 . 52 ILE HG2 H -0.34 . 1 363 . 52 ILE HD1 H -0.04 . 1 364 . 52 ILE CG1 C 15.4 . 4 365 . 52 ILE CG2 C 8.5 . 4 366 . 52 ILE CD1 C 3.2 . 1 367 . 53 GLU N N 112.6 . 1 368 . 53 GLU H H 7.58 . 1 369 . 53 GLU CA C 51.1 . 1 370 . 53 GLU HA H 3.75 . 1 371 . 53 GLU HB2 H 1.90 . 2 372 . 53 GLU HG2 H 2.29 . 2 373 . 53 GLU HG3 H 2.12 . 2 374 . 53 GLU CG C 28.9 . 1 375 . 54 GLU N N 111.0 . 1 376 . 54 GLU H H 8.22 . 1 377 . 54 GLU CA C 49.2 . 1 378 . 54 GLU HA H 4.36 . 1 379 . 54 GLU CB C 28.8 . 1 380 . 54 GLU HB2 H 2.11 . 2 381 . 54 GLU HB3 H 1.87 . 2 382 . 55 ILE N N 117.0 . 1 383 . 55 ILE H H 7.30 . 1 384 . 55 ILE CA C 55.5 . 1 385 . 55 ILE HA H 4.14 . 1 386 . 55 ILE CB C 34.2 . 1 387 . 55 ILE HB H 1.36 . 1 388 . 55 ILE HG12 H 0.85 . 2 389 . 55 ILE HG13 H 0.59 . 1 390 . 55 ILE HD1 H 0.59 . 1 391 . 55 ILE CG2 C 9.5 . 1 392 . 55 ILE CD1 C 5.1 . 1 393 . 56 LEU N N 120.9 . 1 394 . 56 LEU H H 7.88 . 1 395 . 56 LEU HA H 3.72 . 1 396 . 56 LEU HD1 H 0.62 . 2 397 . 56 LEU HD2 H 0.56 . 2 398 . 56 LEU CD1 C 19.7 . 2 399 . 56 LEU CD2 C 16.4 . 2 400 . 57 LEU N N 110.2 . 1 401 . 57 LEU H H 7.61 . 1 402 . 57 LEU HA H 4.09 . 1 403 . 57 LEU HB2 H 1.70 . 2 404 . 57 LEU HB3 H 1.53 . 2 405 . 57 LEU HG H 1.38 . 1 406 . 57 LEU HD1 H 0.65 . 2 407 . 57 LEU HD2 H -0.32 . 2 408 . 57 LEU CD1 C 17.9 . 2 409 . 58 THR N N 108.0 . 1 410 . 58 THR H H 6.85 . 1 411 . 58 THR CA C 52.0 . 1 412 . 58 THR HA H 4.30 . 1 413 . 58 THR CB C 60.5 . 1 414 . 58 THR HB H 4.14 . 1 415 . 58 THR HG2 H 1.03 . 1 416 . 58 THR CG2 C 14.5 . 1 417 . 59 ASP N N 122.6 . 1 418 . 59 ASP H H 8.43 . 1 419 . 59 ASP CA C 49.3 . 1 420 . 59 ASP HA H 4.33 . 1 421 . 59 ASP CB C 34.2 . 1 422 . 59 ASP HB2 H 2.69 . 2 423 . 60 TYR N N 120.4 . 1 424 . 60 TYR H H 8.23 . 1 425 . 60 TYR HA H 4.06 . 1 426 . 60 TYR HB2 H 3.44 . 2 427 . 60 TYR HB3 H 2.99 . 2 428 . 60 TYR HD1 H 7.12 . 2 429 . 61 LYS N N 120.7 . 1 430 . 61 LYS H H 7.46 . 1 431 . 61 LYS HA H 4.09 . 1 432 . 61 LYS HB2 H 1.84 . 2 433 . 61 LYS HG2 H 1.27 . 2 434 . 61 LYS HD2 H 1.64 . 2 435 . 62 LYS N N 113.8 . 1 436 . 62 LYS H H 7.34 . 1 437 . 62 LYS CA C 51.1 . 1 438 . 62 LYS HA H 3.88 . 1 439 . 62 LYS CB C 25.8 . 1 440 . 62 LYS HB2 H 1.68 . 2 441 . 62 LYS HB3 H 1.58 . 2 442 . 62 LYS HG2 H 1.34 . 2 443 . 62 LYS HG3 H 1.27 . 2 444 . 62 LYS HD2 H 2.67 . 2 445 . 62 LYS CG C 21.7 . 1 446 . 63 ASN N N 111.0 . 1 447 . 63 ASN H H 8.20 . 1 448 . 63 ASN HA H 4.18 . 1 449 . 63 ASN HB2 H 2.69 . 2 450 . 63 ASN HD21 H 7.58 . 2 451 . 63 ASN HD22 H 6.94 . 2 452 . 63 ASN ND2 N 113.8 . 1 453 . 64 VAL N N 119.8 . 1 454 . 64 VAL H H 7.89 . 1 455 . 64 VAL HA H 3.99 . 1 456 . 64 VAL CB C 25.1 . 1 457 . 64 VAL HB H 1.92 . 1 458 . 64 VAL HG1 H 0.78 . 2 459 . 64 VAL HG2 H 0.69 . 2 460 . 64 VAL CG1 C 14.4 . 2 461 . 64 VAL CG2 C 13.2 . 2 462 . 65 ASN N N 112.6 . 1 463 . 65 ASN H H 7.67 . 1 464 . 65 ASN CA C 43.6 . 1 465 . 65 ASN HA H 5.03 . 1 466 . 65 ASN HB2 H 3.01 . 2 467 . 65 ASN HB3 H 2.51 . 2 468 . 65 ASN HD21 H 7.51 . 2 469 . 65 ASN ND2 N 112.1 . 1 470 . 66 PRO HA H 5.02 . 1 471 . 66 PRO HG2 H 1.88 . 2 472 . 66 PRO HD2 H 3.76 . 2 473 . 66 PRO HD3 H 3.37 . 2 474 . 67 THR N N 107.4 . 1 475 . 67 THR H H 7.69 . 1 476 . 67 THR CA C 54.6 . 1 477 . 67 THR HA H 4.30 . 1 478 . 67 THR CB C 62 . 1 479 . 67 THR HB H 4.47 . 1 480 . 67 THR HG2 H 1.25 . 1 481 . 67 THR CG2 C 14.2 . 1 482 . 68 VAL N N 120.4 . 1 483 . 68 VAL H H 7.09 . 1 484 . 68 VAL HA H 4.42 . 1 485 . 68 VAL HB H 1.86 . 1 486 . 68 VAL HG1 H 1.08 . 2 487 . 68 VAL HG2 H 0.87 . 2 488 . 68 VAL CG1 C 15.4 . 2 489 . 68 VAL CG2 C 13.5 . 2 490 . 69 ASN N N 126.1 . 1 491 . 69 ASN H H 9.28 . 1 492 . 69 ASN CA C 45.2 . 1 493 . 69 ASN HA H 4.95 . 1 494 . 69 ASN CB C 35.2 . 1 495 . 69 ASN HB2 H 2.72 . 2 496 . 69 ASN HB3 H 2.59 . 2 497 . 69 ASN HD21 H 7.47 . 2 498 . 69 ASN HD22 H 6.90 . 2 499 . 69 ASN ND2 N 113.5 . 1 500 . 70 VAL N N 121.2 . 1 501 . 70 VAL H H 8.57 . 1 502 . 70 VAL CA C 53.0 . 1 503 . 70 VAL HA H 5.10 . 1 504 . 70 VAL CB C 27.2 . 1 505 . 70 VAL HB H 1.88 . 1 506 . 70 VAL HG1 H 0.86 . 2 507 . 70 VAL HG2 H 0.75 . 2 508 . 70 VAL CG1 C 15.4 . 2 509 . 70 VAL CG2 C 15.33 . 2 510 . 71 GLU N N 126.1 . 1 511 . 71 GLU H H 9.31 . 1 512 . 71 GLU CA C 46.8 . 1 513 . 71 GLU HA H 4.78 . 1 514 . 71 GLU CB C 26.1 . 1 515 . 71 GLU HB2 H 2.12 . 2 516 . 71 GLU HB3 H 1.98 . 2 517 . 71 GLU HG2 H 2.27 . 2 518 . 71 GLU CG C 28.9 . 1 519 . 72 ASP N N 125.1 . 1 520 . 72 ASP H H 8.74 . 1 521 . 72 ASP CA C 45.2 . 1 522 . 72 ASP HA H 4.77 . 1 523 . 72 ASP CB C 33.2 . 1 524 . 72 ASP HB2 H 2.73 . 2 525 . 73 ARG N N 125.4 . 1 526 . 73 ARG H H 8.73 . 1 527 . 73 ARG CA C 47.7 . 1 528 . 73 ARG HA H 4.48 . 1 529 . 73 ARG HB2 H 1.45 . 2 530 . 73 ARG HG2 H 1.21 . 2 531 . 73 ARG HD2 H 2.51 . 2 532 . 73 ARG HD3 H 2.37 . 2 533 . 73 ARG HE H 6.52 . 1 534 . 73 ARG CG C 19.1 . 1 535 . 73 ARG CD C 35.2 . 1 536 . 73 ARG NE N 111.4 . 1 537 . 74 ALA N N 126.7 . 1 538 . 74 ALA H H 8.78 . 1 539 . 74 ALA CA C 45.8 . 1 540 . 74 ALA HA H 3.93 . 1 541 . 74 ALA CB C 9.8 . 1 542 . 74 ALA HB H 1.44 . 1 543 . 75 GLY N N 106.2 . 1 544 . 75 GLY H H 8.83 . 1 545 . 75 GLY CA C 37.7 . 1 546 . 75 GLY HA2 H 3.88 . 2 547 . 75 GLY HA3 H 3.33 . 2 548 . 76 TYR N N 117.8 . 1 549 . 76 TYR H H 7.62 . 1 550 . 76 TYR CA C 48.9 . 1 551 . 76 TYR HA H 4.81 . 1 552 . 76 TYR CB C 34.5 . 1 553 . 76 TYR HB2 H 2.63 . 2 554 . 76 TYR HB3 H 2.52 . 2 555 . 76 TYR HD1 H 6.85 . 3 556 . 77 TRP N N 118.5 . 1 557 . 77 TRP H H 9.24 . 1 558 . 77 TRP CA C 47.7 . 1 559 . 77 TRP HA H 5.44 . 1 560 . 77 TRP CB C 24.1 . 1 561 . 77 TRP HB2 H 2.98 . 2 562 . 77 TRP HB3 H 2.91 . 2 563 . 77 TRP HD1 H 6.71 . 1 564 . 77 TRP HE1 H 10.67 . 1 565 . 77 TRP HE3 H 7.32 . 1 566 . 77 TRP NE1 N 127.8 . 4 567 . 78 TRP N N 125.2 . 1 568 . 78 TRP H H 9.68 . 1 569 . 78 TRP CA C 49.3 . 1 570 . 78 TRP HA H 4.78 . 1 571 . 78 TRP HB2 H 3.10 . 2 572 . 78 TRP HD1 H 7.17 . 1 573 . 78 TRP HE1 H 10.1 . 1 574 . 78 TRP NE1 N 129.8 . 4 575 . 79 ILE N N 126.6 . 1 576 . 79 ILE H H 9.09 . 1 577 . 79 ILE CA C 52.7 . 1 578 . 79 ILE HA H 4.95 . 1 579 . 79 ILE HB H 1.65 . 1 580 . 79 ILE HG12 H 0.86 . 2 581 . 79 ILE HG2 H 0.55 . 3 582 . 79 ILE HD1 H 0.76 . 1 583 . 79 ILE CD1 C 7.6 . 1 584 . 80 LYS N N 125.9 . 1 585 . 80 LYS H H 8.81 . 1 586 . 80 LYS CA C 46.1 . 1 587 . 80 LYS HA H 5.49 . 1 588 . 80 LYS CB C 28.9 . 1 589 . 80 LYS HB2 H 1.64 . 2 590 . 80 LYS HB3 H 1.59 . 2 591 . 80 LYS HG2 H 1.43 . 2 592 . 80 LYS CG C 17.6 . 1 593 . 81 ALA N N 121.4 . 1 594 . 81 ALA H H 8.41 . 1 595 . 81 ALA CA C 43.0 . 1 596 . 81 ALA HA H 4.42 . 1 597 . 81 ALA CB C 16.4 . 1 598 . 81 ALA HB H 1.06 . 1 599 . 82 ASN N N 116.2 . 1 600 . 82 ASN H H 8.89 . 1 601 . 82 ASN CA C 45.5 . 1 602 . 82 ASN HA H 5.12 . 1 603 . 82 ASN CB C 31.9 . 1 604 . 82 ASN HB2 H 2.77 . 2 605 . 82 ASN HB3 H 2.56 . 2 606 . 82 ASN HD21 H 7.48 . 2 607 . 82 ASN HD22 H 6.79 . 2 608 . 82 ASN ND2 N 111.5 . 1 609 . 83 GLY N N 112.8 . 1 610 . 83 GLY H H 8.77 . 1 611 . 83 GLY CA C 39.2 . 1 612 . 83 GLY HA2 H 4.24 . 2 613 . 83 GLY HA3 H 3.45 . 2 614 . 84 LYS N N 121.0 . 1 615 . 84 LYS H H 7.83 . 1 616 . 84 LYS CA C 47.4 . 1 617 . 84 LYS HA H 5.25 . 1 618 . 84 LYS CB C 28.3 . 1 619 . 84 LYS HB2 H 1.84 . 2 620 . 84 LYS HB3 H 1.60 . 2 621 . 84 LYS HG2 H 1.08 . 2 622 . 84 LYS HG3 H 0.87 . 2 623 . 84 LYS HD2 H 1.25 . 2 624 . 85 ILE N N 118.5 . 1 625 . 85 ILE H H 8.50 . 1 626 . 85 ILE CA C 53.3 . 1 627 . 85 ILE HA H 4.25 . 1 628 . 85 ILE HG12 H 1.09 . 2 629 . 85 ILE HG13 H 1.34 . 2 630 . 85 ILE HG2 H 0.84 . 1 631 . 85 ILE HD1 H 0.55 . 1 632 . 85 ILE CG1 C 19.8 . 4 633 . 85 ILE CG2 C 11.0 . 4 634 . 85 ILE CD1 C 6.9 . 1 635 . 86 GLU N N 123.5 . 1 636 . 86 GLU H H 7.05 . 1 637 . 86 GLU CA C 46.8 . 1 638 . 86 GLU HA H 5.00 . 1 639 . 86 GLU CB C 29.7 . 1 640 . 86 GLU HB2 H 2.04 . 2 641 . 86 GLU HB3 H 1.80 . 2 642 . 86 GLU HG2 H 2.44 . 2 643 . 86 GLU HG3 H 2.39 . 2 644 . 87 VAL N N 123.8 . 1 645 . 87 VAL H H 9.33 . 1 646 . 87 VAL CA C 53.6 . 1 647 . 87 VAL HA H 3.58 . 1 648 . 87 VAL CB C 25.8 . 1 649 . 87 VAL HB H 1.40 . 1 650 . 87 VAL HG1 H 0.35 . 2 651 . 87 VAL HG2 H -0.63 . 2 652 . 87 VAL CG1 C 11.6 . 2 653 . 87 VAL CG2 C 11.3 . 2 654 . 88 ASP N N 126.6 . 1 655 . 88 ASP H H 9.09 . 1 656 . 88 ASP HA H 4.61 . 1 657 . 88 ASP HB2 H 3.14 . 2 658 . 88 ASP HB3 H 3.09 . 2 659 . 89 CYS N N 122.2 . 1 660 . 89 CYS H H 8.47 . 1 661 . 89 CYS HA H 4.41 . 1 662 . 89 CYS CB C 22.3 . 1 663 . 89 CYS HB2 H 3.05 . 2 664 . 89 CYS HB3 H 3.00 . 2 665 . 90 ASP N N 123.4 . 1 666 . 90 ASP H H 8.61 . 1 667 . 90 ASP CA C 49.9 . 1 668 . 90 ASP HA H 4.59 . 1 669 . 90 ASP CB C 31.4 . 1 670 . 90 ASP HB2 H 3.04 . 2 671 . 90 ASP HB3 H 2.62 . 2 672 . 91 GLU N N 122.2 . 1 673 . 91 GLU H H 7.29 . 1 674 . 91 GLU CA C 50.8 . 1 675 . 91 GLU HA H 4.05 . 1 676 . 91 GLU HB2 H 2.17 . 2 677 . 91 GLU HB3 H 2.04 . 2 678 . 91 GLU HG2 H 2.33 . 2 679 . 92 ILE N N 117.7 . 1 680 . 92 ILE H H 7.47 . 1 681 . 92 ILE CA C 59.0 . 1 682 . 92 ILE HA H 3.33 . 1 683 . 92 ILE HB H 1.65 . 1 684 . 92 ILE HG12 H 0.78 . 2 685 . 92 ILE HG2 H 0.29 . 1 686 . 92 ILE HD1 H 0.24 . 1 687 . 92 ILE CG1 C 9.8 . 1 688 . 92 ILE CG2 C 7.3 . 1 689 . 92 ILE CD1 C 5.7 . 1 690 . 93 SER N N 114.8 . 1 691 . 93 SER H H 8.09 . 1 692 . 93 SER HA H 4.51 . 1 693 . 93 SER HB2 H 4.06 . 2 694 . 93 SER HB3 H 3.92 . 2 695 . 94 GLU N N 121.2 . 1 696 . 94 GLU H H 7.64 . 1 697 . 94 GLU CA C 51.5 . 1 698 . 94 GLU HA H 3.91 . 1 699 . 94 GLU CB C 21.7 . 1 700 . 94 GLU HB2 H 2.03 . 2 701 . 94 GLU HG2 H 2.25 . 2 702 . 94 GLU CG C 28.3 . 1 703 . 95 LEU N N 119.5 . 1 704 . 95 LEU H H 7.45 . 1 705 . 95 LEU CA C 49.6 . 1 706 . 95 LEU HA H 4.06 . 1 707 . 95 LEU CB C 34.8 . 1 708 . 95 LEU HB2 H 1.65 . 2 709 . 95 LEU HB3 H 1.52 . 2 710 . 95 LEU HD1 H 0.78 . 2 711 . 95 LEU HD2 H 0.67 . 2 712 . 95 LEU CD1 C 11.7 . 2 713 . 96 LEU N N 114.9 . 1 714 . 96 LEU H H 8.29 . 1 715 . 96 LEU CA C 47.6 . 1 716 . 96 LEU HA H 4.05 . 1 717 . 96 LEU HB2 H 1.77 . 2 718 . 96 LEU HB3 H 1.34 . 2 719 . 96 LEU HD1 H 0.67 . 2 720 . 96 LEU HD2 H 0.41 . 2 721 . 96 LEU CD1 C 18.8 . 2 722 . 96 LEU CD2 C 14.5 . 2 723 . 97 GLY N N 106.7 . 1 724 . 97 GLY H H 8.02 . 1 725 . 97 GLY CA C 37.4 . 1 726 . 97 GLY HA2 H 3.92 . 2 727 . 97 GLY HA3 H 3.73 . 2 728 . 98 ARG N N 114.6 . 1 729 . 98 ARG H H 7.64 . 1 730 . 98 ARG CA C 46.1 . 1 731 . 98 ARG HA H 4.51 . 1 732 . 98 ARG CB C 24.5 . 1 733 . 98 ARG HB2 H 1.84 . 2 734 . 98 ARG HB3 H 1.63 . 2 735 . 98 ARG HG2 H 1.33 . 2 736 . 98 ARG HG3 H 1.21 . 2 737 . 98 ARG HD2 H 3.05 . 2 738 . 98 ARG HE H 7.4 . 1 739 . 98 ARG CG C 18.5 . 1 740 . 98 ARG CD C 35.8 . 1 741 . 98 ARG NE N 113.9 . 1 742 . 99 GLN N N 117.8 . 1 743 . 99 GLN H H 8.27 . 1 744 . 99 GLN CA C 49.9 . 1 745 . 99 GLN HA H 3.89 . 1 746 . 99 GLN HB2 H 1.90 . 2 747 . 99 GLN HG2 H 2.23 . 2 748 . 99 GLN HE21 H 7.44 . 2 749 . 99 GLN HE22 H 6.72 . 2 750 . 99 GLN CG C 26.1 . 1 751 . 99 GLN NE2 N 112.1 . 1 752 . 100 PHE N N 131.1 . 1 753 . 100 PHE H H 8.88 . 1 754 . 100 PHE HA H 4.56 . 1 755 . 100 PHE HB2 H 2.85 . 2 756 . 100 PHE HB3 H 2.59 . 2 757 . 100 PHE HD1 H 6.98 . 3 758 . 101 ASN N N 124.1 . 1 759 . 101 ASN H H 8.85 . 1 760 . 101 ASN HA H 5.03 . 1 761 . 101 ASN HB2 H 2.72 . 2 762 . 101 ASN HB3 H 2.55 . 2 763 . 101 ASN HD21 H 7.47 . 2 764 . 101 ASN HD22 H 6.83 . 2 765 . 101 ASN ND2 N 113.2 . 1 766 . 102 VAL N N 118.4 . 1 767 . 102 VAL H H 8.18 . 1 768 . 102 VAL CA C 53.6 . 1 769 . 102 VAL HA H 3.96 . 1 770 . 102 VAL CB C 24.1 . 1 771 . 102 VAL HB H 1.77 . 1 772 . 102 VAL HG1 H 0.75 . 2 773 . 102 VAL HG2 H 0.69 . 2 774 . 103 TYR N N 118.9 . 1 775 . 103 TYR H H 7.46 . 1 776 . 103 TYR HA H 4.04 . 1 777 . 103 TYR CB C 29.2 . 1 778 . 103 TYR HB2 H 2.86 . 2 779 . 103 TYR HD1 H 6.94 . 3 780 . 104 ASP N N 119.8 . 1 781 . 104 ASP H H 7.23 . 1 782 . 104 ASP CA C 39.8 . 1 783 . 104 ASP HA H 4.12 . 1 784 . 104 ASP HB2 H 2.09 . 2 785 . 104 ASP HB3 H 1.92 . 2 786 . 105 PHE N N 119.4 . 1 787 . 105 PHE H H 7.23 . 1 788 . 105 PHE HA H 4.01 . 1 789 . 105 PHE HB2 H 2.89 . 2 790 . 105 PHE HB3 H 2.75 . 2 791 . 105 PHE HD1 H 6.43 . 3 792 . 106 LEU N N 115.7 . 1 793 . 106 LEU H H 8.01 . 1 794 . 106 LEU HA H 3.39 . 1 795 . 106 LEU HB2 H 1.72 . 2 796 . 106 LEU HD1 H 0.71 . 2 797 . 106 LEU HD2 H 0.55 . 2 798 . 106 LEU CD1 C 15.3 . 1 799 . 107 VAL N N 116.0 . 1 800 . 107 VAL H H 6.94 . 1 801 . 107 VAL CA C 57.1 . 1 802 . 107 VAL HA H 3.60 . 1 803 . 107 VAL CB C 24.2 . 1 804 . 107 VAL HB H 1.99 . 1 805 . 107 VAL HG1 H 0.92 . 2 806 . 107 VAL HG2 H 0.82 . 2 807 . 107 VAL CG1 C 14.2 . 2 808 . 107 VAL CG2 C 13.2 . 2 809 . 108 ASP N N 116.8 . 1 810 . 108 ASP H H 7.30 . 1 811 . 108 ASP CA C 48.0 . 1 812 . 108 ASP HA H 4.64 . 1 813 . 109 VAL N N 121.0 . 1 814 . 109 VAL H H 7.06 . 1 815 . 109 VAL CA C 55.5 . 1 816 . 109 VAL HA H 3.69 . 1 817 . 109 VAL CB C 23.2 . 1 818 . 109 VAL HB H 1.89 . 1 819 . 109 VAL HG1 H 0.51 . 2 820 . 109 VAL HG2 H 0.10 . 2 821 . 109 VAL CG1 C 14.8 . 2 822 . 109 VAL CG2 C 14.2 . 2 823 . 110 SER N N 123.9 . 1 824 . 110 SER H H 8.95 . 1 825 . 110 SER CA C 51.8 . 1 826 . 110 SER HA H 4.40 . 1 827 . 110 SER CB C 56.8 . 1 828 . 110 SER HB2 H 3.39 . 2 829 . 111 SER N N 111.5 . 1 830 . 111 SER H H 7.39 . 1 831 . 112 THR HA H 4.92 . 1 832 . 112 THR HB H 3.96 . 1 833 . 112 THR HG2 H 1.02 . 1 834 . 113 ILE N N 121.9 . 1 835 . 113 ILE H H 8.82 . 1 836 . 113 ILE HA H 4.13 . 1 837 . 113 ILE HB H 1.35 . 1 838 . 113 ILE HG12 H 0.91 . 2 839 . 113 ILE HG2 H 0.61 . 4 840 . 113 ILE HD1 H 0.74 . 1 841 . 113 ILE CG2 C 9.5 . 4 842 . 113 ILE CD1 C 8.5 . 1 843 . 114 GLY N N 112.1 . 1 844 . 114 GLY H H 8.06 . 1 845 . 114 GLY CA C 35.5 . 1 846 . 114 GLY HA2 H 4.36 . 2 847 . 114 GLY HA3 H 3.72 . 2 848 . 115 ARG N N 121.0 . 1 849 . 115 ARG H H 8.77 . 1 850 . 115 ARG HA H 4.46 . 1 851 . 115 ARG HB2 H 1.79 . 2 852 . 115 ARG HG2 H 1.53 . 2 853 . 115 ARG HG3 H 1.37 . 2 854 . 115 ARG HD2 H 3.15 . 2 855 . 115 ARG HD3 H 3.05 . 2 856 . 115 ARG HE H 7.26 . 1 857 . 115 ARG CG C 20.0 . 1 858 . 115 ARG CD C 37.8 . 1 859 . 115 ARG NE N 112.3 . 1 860 . 116 ALA N N 129.3 . 1 861 . 116 ALA H H 8.51 . 1 862 . 116 ALA HA H 5.35 . 1 863 . 116 ALA CB C 14.5 . 1 864 . 116 ALA HB H 1.17 . 1 865 . 117 TYR N N 118.0 . 1 866 . 117 TYR H H 8.64 . 1 867 . 117 TYR CA C 45.2 . 1 868 . 117 TYR HA H 4.81 . 1 869 . 117 TYR HB2 H 2.95 . 2 870 . 117 TYR HB3 H 2.85 . 2 871 . 117 TYR HD1 H 6.58 . 3 872 . 118 THR N N 110.6 . 1 873 . 118 THR H H 8.39 . 1 874 . 118 THR CA C 52.1 . 1 875 . 118 THR HA H 5.10 . 1 876 . 118 THR CB C 63.4 . 1 877 . 118 THR HB H 4.05 . 1 878 . 118 THR HG2 H 1.11 . 1 879 . 118 THR CG2 C 15.0 . 1 880 . 119 LEU N N 124.4 . 1 881 . 119 LEU H H 8.21 . 1 882 . 119 LEU CA C 47.4 . 1 883 . 119 LEU HA H 4.51 . 1 884 . 119 LEU CB C 36.7 . 1 885 . 119 LEU HB2 H 1.66 . 2 886 . 119 LEU HB3 H 1.46 . 2 887 . 119 LEU HD1 H 0.87 . 2 888 . 119 LEU HD2 H 0.73 . 2 889 . 120 GLY N N 118.1 . 1 890 . 120 GLY H H 9.12 . 1 891 . 120 GLY HA2 H 3.80 . 2 892 . 120 GLY HA3 H 3.66 . 2 893 . 121 ASN N N 126.9 . 1 894 . 121 ASN H H 8.96 . 1 895 . 121 ASN CA C 43.3 . 1 896 . 121 ASN HA H 5.24 . 1 897 . 121 ASN CB C 31.7 . 1 898 . 121 ASN HB2 H 2.92 . 2 899 . 121 ASN HB3 H 2.40 . 2 900 . 121 ASN HD21 H 7.89 . 2 901 . 121 ASN HD22 H 6.81 . 2 902 . 121 ASN ND2 N 111.2 . 1 903 . 122 LYS N N 117.6 . 1 904 . 122 LYS H H 7.79 . 1 905 . 122 LYS CA C 47.4 . 1 906 . 122 LYS HA H 5.04 . 1 907 . 122 LYS HB2 H 1.71 . 2 908 . 122 LYS HG2 H 1.12 . 2 909 . 123 PHE N N 127.1 . 1 910 . 123 PHE H H 8.76 . 1 911 . 123 PHE CA C 48.3 . 1 912 . 123 PHE HA H 4.78 . 1 913 . 123 PHE HB2 H 2.47 . 2 914 . 123 PHE HB3 H 2.39 . 2 915 . 123 PHE HD1 H 6.74 . 3 916 . 124 THR N N 124.4 . 1 917 . 124 THR H H 8.08 . 1 918 . 124 THR HA H 5.06 . 1 919 . 124 THR HG2 H 1.25 . 1 920 . 124 THR CG2 C 14.1 . 1 921 . 125 ILE N N 121.1 . 1 922 . 125 ILE H H 8.32 . 1 923 . 125 ILE CA C 54.9 . 1 924 . 125 ILE HA H 4.98 . 1 925 . 125 ILE HB H 1.39 . 1 926 . 125 ILE HG12 H 1.10 . 2 927 . 125 ILE HG2 H 0.68 . 1 928 . 125 ILE HD1 H 0.82 . 1 929 . 125 ILE CD1 C 9.5 . 1 930 . 126 THR N N 118.9 . 1 931 . 126 THR H H 8.93 . 1 932 . 126 THR CA C 58.8 . 1 933 . 126 THR HA H 5.26 . 1 934 . 126 THR CB C 63.7 . 1 935 . 126 THR HB H 3.94 . 1 936 . 126 THR HG2 H 1.27 . 1 937 . 126 THR CG2 C 13.2 . 1 938 . 127 SER N N 119.1 . 1 939 . 127 SER H H 8.26 . 1 940 . 127 SER CA C 50.2 . 1 941 . 127 SER HA H 4.38 . 1 942 . 127 SER HB2 H 3.65 . 2 943 . 128 GLU N N 123.7 . 1 944 . 128 GLU H H 8.56 . 1 945 . 128 GLU CA C 48.3 . 1 946 . 128 GLU HA H 4.14 . 1 947 . 128 GLU HB2 H 2.00 . 2 948 . 128 GLU HB3 H 1.89 . 2 949 . 128 GLU HG2 H 2.21 . 2 950 . 128 GLU HG3 H 2.14 . 2 951 . 128 GLU CG C 26.1 . 1 952 . 129 LEU N N 122.5 . 1 953 . 129 LEU H H 8.32 . 1 954 . 129 LEU HA H 4.13 . 1 955 . 129 LEU HB2 H 1.52 . 2 956 . 129 LEU HD1 H 0.77 . 2 957 . 130 MET N N 119.2 . 1 958 . 130 MET H H 8.12 . 1 959 . 130 MET CA C 48.2 . 1 960 . 130 MET HA H 4.29 . 1 961 . 130 MET HB2 H 1.93 . 2 962 . 130 MET HG2 H 2.41 . 2 963 . 130 MET CG C 25.1 . 1 964 . 131 GLY N N 108.9 . 1 965 . 131 GLY H H 8.29 . 1 966 . 131 GLY HA2 H 3.86 . 2 967 . 131 GLY HA3 H 3.79 . 2 968 . 132 LEU N N 121.0 . 1 969 . 132 LEU H H 7.95 . 1 970 . 132 LEU CA C 47.4 . 1 971 . 132 LEU HA H 4.30 . 1 972 . 132 LEU HB2 H 1.50 . 2 973 . 132 LEU HD1 H 0.76 . 2 974 . 133 ASP CA C 46.4 . 1 975 . 133 ASP HA H 4.43 . 1 976 . 133 ASP CB C 33.2 . 1 977 . 133 ASP HB2 H 2.58 . 2 978 . 133 ASP HB3 H 2.51 . 2 979 . 134 ARG N N 120.9 . 1 980 . 134 ARG H H 7.97 . 1 981 . 134 ARG CA C 50.2 . 1 982 . 134 ARG HA H 4.18 . 1 983 . 134 ARG HB2 H 1.72 . 2 984 . 134 ARG HB3 H 1.61 . 2 985 . 134 ARG HG2 H 1.48 . 2 986 . 134 ARG HD2 H 3.02 . 2 987 . 134 ARG HE H 7.15 . 1 988 . 134 ARG CG C 19.5 . 1 989 . 134 ARG CD C 35.5 . 1 990 . 134 ARG NE N 113.2 . 1 991 . 135 LYS N N 121.7 . 1 992 . 135 LYS H H 8.27 . 1 993 . 135 LYS HA H 4.18 . 1 994 . 135 LYS HB2 H 1.68 . 2 995 . 135 LYS HG2 H 1.31 . 2 996 . 135 LYS HD2 H 1.5 . 2 997 . 135 LYS HE2 H 3.03 . 2 998 . 136 LEU N N 122.9 . 1 999 . 136 LEU H H 8.18 . 1 1000 . 136 LEU HA H 4.19 . 1 1001 . 136 LEU HB2 H 1.69 . 2 1002 . 136 LEU HB3 H 1.51 . 2 1003 . 136 LEU HD1 H 0.74 . 2 1004 . 136 LEU CD1 C 15.7 . 2 1005 . 137 GLU N N 120.4 . 1 1006 . 137 GLU H H 8.32 . 1 1007 . 137 GLU HA H 4.13 . 1 1008 . 137 GLU HB2 H 1.90 . 2 1009 . 137 GLU HB3 H 1.81 . 2 1010 . 137 GLU HG2 H 2.15 . 2 1011 . 138 ASP N N 120.5 . 1 1012 . 138 ASP H H 8.12 . 1 1013 . 138 ASP HA H 4.47 . 1 1014 . 138 ASP HB2 H 2.55 . 2 1015 . 138 ASP HB3 H 2.45 . 2 1016 . 139 TYR N N 120.5 . 1 1017 . 139 TYR H H 7.91 . 1 1018 . 139 TYR HA H 4.35 . 1 1019 . 139 TYR CB C 31.3 . 1 1020 . 139 TYR HB2 H 2.84 . 2 1021 . 139 TYR HD1 H 6.95 . 3 1022 . 140 HIS N N 121.4 . 1 1023 . 140 HIS H H 7.91 . 1 1024 . 140 HIS HA H 4.45 . 1 1025 . 140 HIS HB2 H 3.10 . 2 1026 . 140 HIS HB3 H 3.00 . 2 1027 . 141 ALA N N 130.7 . 1 1028 . 141 ALA H H 7.98 . 1 1029 . 141 ALA CA C 45.8 . 1 1030 . 141 ALA HA H 3.97 . 1 1031 . 141 ALA CB C 12.3 . 1 1032 . 141 ALA HB H 1.24 . 1 stop_ save_