data_17357 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; PsbQ protein ; _BMRB_accession_number 17357 _BMRB_flat_file_name bmr17357.str _Entry_type original _Submission_date 2010-12-13 _Accession_date 2010-12-13 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'extrinsic protein (16kDa) from Photosystem II' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hornicakova Michaela . . 2 Muller Norbert . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 380 "13C chemical shifts" 401 "15N chemical shifts" 112 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-03-12 update BMRB 'update entry citation' 2011-02-01 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone assignment and secondary structure of the PsbQ protein from photosystem II.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21259076 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Horniakova Michaela . . 2 Kohoutova Jaroslava . . 3 Schlagnitweit Judith . . 4 Wohlschlager Christian . . 5 Ettrich Rudiger . . 6 Fiala Radovan . . 7 Schoefberger Wolfgang . . 8 Muller Norbert . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 5 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 169 _Page_last 175 _Year 2011 _Details . loop_ _Keyword 'Missing link' 'NMR resonance assignment' 'Photosystem II' 'protein-protein interaction' PsbQ stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'PsbQ protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label PsbQ $PsbQ_protein stop_ _System_molecular_weight 16000 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PsbQ_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PsbQ_protein _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 149 _Mol_residue_sequence ; EARPIVVGPPPPLSGGLPGT ENSDQARDGTLPYTKDRFYL QPLPPTEAAQRAKVSASEIL NVKQFIDRKAWPSLQNDLRL RASYLRYDLKTVISAKPKDE KKSLQELTSKLFSSIDNLDH AAKIKSPTEAEKYYGQTVSN INEVLAKLG ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 ALA 3 ARG 4 PRO 5 ILE 6 VAL 7 VAL 8 GLY 9 PRO 10 PRO 11 PRO 12 PRO 13 LEU 14 SER 15 GLY 16 GLY 17 LEU 18 PRO 19 GLY 20 THR 21 GLU 22 ASN 23 SER 24 ASP 25 GLN 26 ALA 27 ARG 28 ASP 29 GLY 30 THR 31 LEU 32 PRO 33 TYR 34 THR 35 LYS 36 ASP 37 ARG 38 PHE 39 TYR 40 LEU 41 GLN 42 PRO 43 LEU 44 PRO 45 PRO 46 THR 47 GLU 48 ALA 49 ALA 50 GLN 51 ARG 52 ALA 53 LYS 54 VAL 55 SER 56 ALA 57 SER 58 GLU 59 ILE 60 LEU 61 ASN 62 VAL 63 LYS 64 GLN 65 PHE 66 ILE 67 ASP 68 ARG 69 LYS 70 ALA 71 TRP 72 PRO 73 SER 74 LEU 75 GLN 76 ASN 77 ASP 78 LEU 79 ARG 80 LEU 81 ARG 82 ALA 83 SER 84 TYR 85 LEU 86 ARG 87 TYR 88 ASP 89 LEU 90 LYS 91 THR 92 VAL 93 ILE 94 SER 95 ALA 96 LYS 97 PRO 98 LYS 99 ASP 100 GLU 101 LYS 102 LYS 103 SER 104 LEU 105 GLN 106 GLU 107 LEU 108 THR 109 SER 110 LYS 111 LEU 112 PHE 113 SER 114 SER 115 ILE 116 ASP 117 ASN 118 LEU 119 ASP 120 HIS 121 ALA 122 ALA 123 LYS 124 ILE 125 LYS 126 SER 127 PRO 128 THR 129 GLU 130 ALA 131 GLU 132 LYS 133 TYR 134 TYR 135 GLY 136 GLN 137 THR 138 VAL 139 SER 140 ASN 141 ILE 142 ASN 143 GLU 144 VAL 145 LEU 146 ALA 147 LYS 148 LEU 149 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-12 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 25350 PsbQ 100.00 149 100.00 100.00 6.99e-102 PDB 1NZE "Crystal Structure Of Psbq Polypeptide Of Photosystem Ii From Higher Plants" 100.00 149 100.00 100.00 6.99e-102 PDB 1VYK "Crystal Structure Of Psbq Protein Of Photosystem Ii From Higher Plants" 100.00 149 100.00 100.00 6.99e-102 PDB 2MWQ "Solution Structure Of Psbq From Spinacia Oleracea" 100.00 149 100.00 100.00 6.99e-102 EMBL CAA29056 "16 kDa protein of the photosynthetic oxygen-evolving protein (OEC) [Spinacia oleracea]" 100.00 232 100.00 100.00 4.92e-103 GB KNA09121 "hypothetical protein SOVF_156430 [Spinacia oleracea]" 100.00 232 100.00 100.00 4.92e-103 PRF 1307179B "luminal protein 16kD" 100.00 232 100.00 100.00 4.92e-103 SP P12301 "RecName: Full=Oxygen-evolving enhancer protein 3, chloroplastic; Short=OEE3; AltName: Full=16 kDa subunit of oxygen evolving sy" 100.00 232 100.00 100.00 4.92e-103 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PsbQ_protein spinach 3562 Eukaryota Viridiplantae Spinacea oleracea 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 $PsbQ_protein 'recombinant technology' . Escherichia coli . JR2592 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 $PsbQ_protein 0.5 mM '[U-99% 13C; U-99% 15N]' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CARA _Saveframe_category software _Name CARA _Version 1.8.4 loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details 'Application for the NMR spectra analysis and computer aided resonance assignment' save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _Details 'equipped with TCI cryoprobe, z-gradient, at the FMP institute in Berlin-Buch, Germany' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details 'at the FMP institute in Berlin-Buch, Germany' save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'equipped with TCI cryoprobe with cold proton and carbon preamplifier, in NCBR Brno, Czech republic' save_ save_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details 'equipped with TXI cryoprobe with cold proton preamplifier, Institute of Organic Chemistry, JKU Linz, Austria' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_13C_detected_CBCACON_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C detected CBCACON' _Sample_label $sample_1 save_ save_3D_13C_detected_CBCANCO_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C detected CBCANCO' _Sample_label $sample_1 save_ save_2D_13C_detected_CON_11 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C detected CON' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_12 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 20 . mM pH 7.00 . pH pressure 1 . atm temperature 300 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0 external indirect . . . 0.25144953 DSS H 1 'methyl protons' ppm 0 external direct . . . 1.0 DSS N 15 'methyl protons' ppm 0 external indirect . . . 0.10132911 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D HNCO' '3D HN(CA)CO' '3D HBHA(CO)NH' '3D H(CCO)NH' '3D C(CO)NH' '3D 13C detected CBCACON' '3D 13C detected CBCANCO' '2D 13C detected CON' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name PsbQ _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 1 GLU HA H 4.312 0.020 1 2 1 1 GLU HB2 H 2.037 0.020 2 3 1 1 GLU HB3 H 1.930 0.020 2 4 1 1 GLU HG2 H 2.246 0.020 1 5 1 1 GLU C C 175.743 0.3 1 6 1 1 GLU CA C 56.121 0.3 1 7 1 1 GLU CB C 30.354 0.3 1 8 1 1 GLU CG C 36.119 0.3 1 9 2 2 ALA H H 8.544 0.020 1 10 2 2 ALA HA H 4.328 0.020 1 11 2 2 ALA HB H 1.350 0.020 1 12 2 2 ALA C C 177.285 0.3 1 13 2 2 ALA CA C 52.170 0.3 1 14 2 2 ALA CB C 19.130 0.3 1 15 2 2 ALA N N 126.348 0.3 1 16 3 3 ARG H H 8.367 0.020 1 17 3 3 ARG C C 174.172 0.3 1 18 3 3 ARG CA C 53.650 0.3 1 19 3 3 ARG CB C 30.174 0.3 1 20 3 3 ARG N N 121.974 0.3 1 21 4 4 PRO HA H 4.409 0.020 1 22 4 4 PRO HB2 H 2.254 0.020 1 23 4 4 PRO HG2 H 1.984 0.020 2 24 4 4 PRO HG3 H 1.827 0.020 2 25 4 4 PRO HD2 H 3.778 0.020 2 26 4 4 PRO HD3 H 3.589 0.020 2 27 4 4 PRO C C 176.611 0.3 1 28 4 4 PRO CA C 62.654 0.3 1 29 4 4 PRO CB C 31.976 0.3 1 30 4 4 PRO CG C 27.319 0.3 1 31 4 4 PRO N N 137.044 0.3 1 32 5 5 ILE H H 8.307 0.020 1 33 5 5 ILE HA H 4.112 0.020 1 34 5 5 ILE HB H 1.788 0.020 1 35 5 5 ILE HG12 H 1.498 0.020 2 36 5 5 ILE HG13 H 1.179 0.020 2 37 5 5 ILE HG2 H 0.853 0.020 1 38 5 5 ILE HD1 H 0.576 0.020 1 39 5 5 ILE C C 176.192 0.3 1 40 5 5 ILE CA C 61.118 0.3 1 41 5 5 ILE CB C 38.567 0.3 1 42 5 5 ILE CG1 C 27.300 0.3 1 43 5 5 ILE CG2 C 17.394 0.3 1 44 5 5 ILE CD1 C 13.098 0.3 1 45 5 5 ILE N N 121.848 0.3 1 46 6 6 VAL H H 8.293 0.020 1 47 6 6 VAL HA H 4.143 0.020 1 48 6 6 VAL HB H 2.000 0.020 1 49 6 6 VAL HG1 H 0.860 0.020 1 50 6 6 VAL C C 175.804 0.3 1 51 6 6 VAL CA C 62.102 0.3 1 52 6 6 VAL CB C 32.774 0.3 1 53 6 6 VAL CG1 C 20.942 0.3 1 54 6 6 VAL N N 125.954 0.3 1 55 7 7 VAL H H 8.382 0.020 1 56 7 7 VAL HA H 4.139 0.020 1 57 7 7 VAL HB H 2.037 0.020 1 58 7 7 VAL HG1 H 0.904 0.020 1 59 7 7 VAL C C 176.092 0.3 1 60 7 7 VAL CA C 62.148 0.3 1 61 7 7 VAL CB C 32.716 0.3 1 62 7 7 VAL CG1 C 20.942 0.3 1 63 7 7 VAL N N 125.834 0.3 1 64 8 8 GLY H H 8.338 0.020 1 65 8 8 GLY HA2 H 4.146 0.020 2 66 8 8 GLY HA3 H 3.986 0.020 2 67 8 8 GLY C C 170.954 0.3 1 68 8 8 GLY CA C 44.319 0.3 1 69 8 8 GLY N N 113.433 0.3 1 70 9 9 PRO C C 174.457 0.3 1 71 9 9 PRO CA C 61.279 0.3 1 72 9 9 PRO CB C 30.772 0.3 1 73 9 9 PRO N N 135.780 0.3 1 74 10 10 PRO C C 174.298 0.3 1 75 10 10 PRO CA C 61.352 0.3 1 76 10 10 PRO CB C 30.301 0.3 1 77 10 10 PRO N N 136.956 0.3 1 78 11 11 PRO C C 174.799 0.3 1 79 11 11 PRO CA C 61.382 0.3 1 80 11 11 PRO CB C 30.856 0.3 1 81 11 11 PRO N N 136.418 0.3 1 82 12 12 PRO HA H 4.403 0.020 1 83 12 12 PRO HB2 H 1.900 0.020 2 84 12 12 PRO HB3 H 2.236 0.020 2 85 12 12 PRO HG2 H 1.978 0.020 2 86 12 12 PRO HG3 H 1.334 0.020 2 87 12 12 PRO HD2 H 3.598 0.020 2 88 12 12 PRO HD3 H 3.756 0.020 2 89 12 12 PRO C C 177.050 0.3 1 90 12 12 PRO CA C 62.755 0.3 1 91 12 12 PRO CB C 31.867 0.3 1 92 12 12 PRO CG C 27.319 0.3 1 93 12 12 PRO N N 135.006 0.3 1 94 13 13 LEU H H 8.402 0.020 1 95 13 13 LEU HA H 4.316 0.020 1 96 13 13 LEU HB2 H 1.599 0.020 1 97 13 13 LEU HD1 H 0.879 0.020 1 98 13 13 LEU C C 177.667 0.3 1 99 13 13 LEU CA C 55.200 0.3 1 100 13 13 LEU CB C 42.153 0.3 1 101 13 13 LEU CG C 27.034 0.3 1 102 13 13 LEU CD1 C 25.035 0.3 1 103 13 13 LEU N N 122.288 0.3 1 104 14 14 SER H H 8.327 0.020 1 105 14 14 SER HA H 4.418 0.020 1 106 14 14 SER HB2 H 3.848 0.020 1 107 14 14 SER C C 175.007 0.3 1 108 14 14 SER CA C 58.346 0.3 1 109 14 14 SER CB C 63.652 0.3 1 110 14 14 SER N N 116.357 0.3 1 111 15 15 GLY H H 8.450 0.020 1 112 15 15 GLY HA2 H 3.967 0.020 1 113 15 15 GLY C C 174.457 0.3 1 114 15 15 GLY CA C 45.246 0.3 1 115 15 15 GLY N N 110.900 0.3 1 116 16 16 GLY H H 8.240 0.020 1 117 16 16 GLY HA2 H 3.917 0.020 1 118 16 16 GLY C C 173.717 0.3 1 119 16 16 GLY CA C 44.919 0.3 1 120 16 16 GLY N N 108.399 0.3 1 121 17 17 LEU H H 8.183 0.020 1 122 17 17 LEU C C 175.465 0.3 1 123 17 17 LEU CA C 53.028 0.3 1 124 17 17 LEU CB C 41.503 0.3 1 125 17 17 LEU N N 122.717 0.3 1 126 18 18 PRO HA H 4.424 0.020 1 127 18 18 PRO HB2 H 2.287 0.020 2 128 18 18 PRO HB3 H 1.929 0.020 2 129 18 18 PRO HG2 H 2.053 0.020 2 130 18 18 PRO HG3 H 1.990 0.020 2 131 18 18 PRO HD2 H 3.840 0.020 2 132 18 18 PRO HD3 H 3.635 0.020 2 133 18 18 PRO C C 177.505 0.3 1 134 18 18 PRO CA C 63.625 0.3 1 135 18 18 PRO CB C 31.975 0.3 1 136 18 18 PRO CG C 27.414 0.3 1 137 18 18 PRO N N 136.735 0.3 1 138 19 19 GLY H H 8.623 0.020 1 139 19 19 GLY HA2 H 4.004 0.020 1 140 19 19 GLY C C 174.710 0.3 1 141 19 19 GLY CA C 45.286 0.3 1 142 19 19 GLY N N 109.856 0.3 1 143 20 20 THR H H 8.014 0.020 1 144 20 20 THR HA H 4.300 0.020 1 145 20 20 THR HG2 H 1.156 0.020 1 146 20 20 THR C C 174.913 0.3 1 147 20 20 THR CA C 61.729 0.3 1 148 20 20 THR CB C 69.809 0.3 1 149 20 20 THR CG2 C 21.703 0.3 1 150 20 20 THR N N 112.643 0.3 1 151 21 21 GLU H H 8.730 0.020 1 152 21 21 GLU HA H 4.266 0.020 1 153 21 21 GLU HB2 H 1.975 0.020 1 154 21 21 GLU HG2 H 2.233 0.020 1 155 21 21 GLU C C 176.296 0.3 1 156 21 21 GLU CA C 56.786 0.3 1 157 21 21 GLU CB C 29.952 0.3 1 158 21 21 GLU CG C 36.077 0.3 1 159 21 21 GLU N N 123.179 0.3 1 160 22 22 ASN H H 8.513 0.020 1 161 22 22 ASN HA H 4.727 0.020 1 162 22 22 ASN HB2 H 2.784 0.020 2 163 22 22 ASN HB3 H 2.868 0.020 2 164 22 22 ASN C C 175.406 0.3 1 165 22 22 ASN CA C 53.189 0.3 1 166 22 22 ASN CB C 38.904 0.3 1 167 22 22 ASN N N 119.703 0.3 1 168 23 23 SER H H 8.335 0.020 1 169 23 23 SER HA H 4.417 0.020 1 170 23 23 SER HB2 H 3.925 0.020 2 171 23 23 SER HB3 H 3.844 0.020 2 172 23 23 SER C C 174.597 0.3 1 173 23 23 SER CA C 58.535 0.3 1 174 23 23 SER CB C 63.648 0.3 1 175 23 23 SER N N 116.494 0.3 1 176 24 24 ASP H H 8.460 0.020 1 177 24 24 ASP HA H 4.552 0.020 1 178 24 24 ASP HB2 H 2.660 0.020 1 179 24 24 ASP C C 176.498 0.3 1 180 24 24 ASP CA C 54.617 0.3 1 181 24 24 ASP CB C 40.809 0.3 1 182 24 24 ASP N N 122.401 0.3 1 183 25 25 GLN H H 8.188 0.020 1 184 25 25 GLN HA H 4.228 0.020 1 185 25 25 GLN HB2 H 2.025 0.020 1 186 25 25 GLN HG2 H 2.616 0.020 2 187 25 25 GLN HG3 H 2.326 0.020 2 188 25 25 GLN C C 176.011 0.3 1 189 25 25 GLN CA C 56.103 0.3 1 190 25 25 GLN CB C 29.329 0.3 1 191 25 25 GLN CG C 33.792 0.3 1 192 25 25 GLN N N 120.147 0.3 1 193 26 26 ALA H H 8.245 0.020 1 194 26 26 ALA HA H 4.228 0.020 1 195 26 26 ALA HB H 1.377 0.020 1 196 26 26 ALA C C 178.001 0.3 1 197 26 26 ALA CA C 52.678 0.3 1 198 26 26 ALA CB C 18.768 0.3 1 199 26 26 ALA N N 124.350 0.3 1 200 27 27 ARG H H 8.238 0.020 1 201 27 27 ARG HA H 4.291 0.020 1 202 27 27 ARG HB2 H 1.825 0.020 2 203 27 27 ARG HB3 H 1.340 0.020 2 204 27 27 ARG HD2 H 3.143 0.020 1 205 27 27 ARG C C 176.263 0.3 1 206 27 27 ARG CA C 56.042 0.3 1 207 27 27 ARG CB C 30.839 0.3 1 208 27 27 ARG N N 120.309 0.3 1 209 28 28 ASP H H 8.351 0.020 1 210 28 28 ASP HA H 4.552 0.020 1 211 28 28 ASP HB2 H 2.685 0.020 1 212 28 28 ASP C C 176.867 0.3 1 213 28 28 ASP CA C 54.314 0.3 1 214 28 28 ASP CB C 41.058 0.3 1 215 28 28 ASP N N 121.172 0.3 1 216 29 29 GLY H H 8.381 0.020 1 217 29 29 GLY HA2 H 3.967 0.020 1 218 29 29 GLY C C 174.550 0.3 1 219 29 29 GLY CA C 45.421 0.3 1 220 29 29 GLY N N 109.645 0.3 1 221 30 30 THR H H 8.121 0.020 1 222 30 30 THR HA H 4.216 0.020 1 223 30 30 THR HG2 H 1.151 0.020 1 224 30 30 THR C C 174.550 0.3 1 225 30 30 THR CA C 62.164 0.3 1 226 30 30 THR CB C 69.855 0.3 1 227 30 30 THR CG2 C 21.667 0.3 1 228 30 30 THR N N 113.599 0.3 1 229 31 31 LEU H H 8.173 0.020 1 230 31 31 LEU C C 175.354 0.3 1 231 31 31 LEU CA C 52.903 0.3 1 232 31 31 LEU CB C 41.761 0.3 1 233 31 31 LEU N N 125.505 0.3 1 234 32 32 PRO HA H 4.288 0.020 1 235 32 32 PRO HB2 H 1.772 0.020 1 236 32 32 PRO HG2 H 1.911 0.020 1 237 32 32 PRO HD2 H 3.774 0.020 2 238 32 32 PRO HD3 H 3.535 0.020 2 239 32 32 PRO C C 176.448 0.3 1 240 32 32 PRO CA C 63.250 0.3 1 241 32 32 PRO CB C 31.720 0.3 1 242 32 32 PRO N N 135.635 0.3 1 243 33 33 TYR H H 8.127 0.020 1 244 33 33 TYR HA H 4.554 0.020 1 245 33 33 TYR HB2 H 2.974 0.020 1 246 33 33 TYR C C 175.914 0.3 1 247 33 33 TYR CA C 57.785 0.3 1 248 33 33 TYR CB C 38.379 0.3 1 249 33 33 TYR N N 119.889 0.3 1 250 34 34 THR H H 7.853 0.020 1 251 34 34 THR HA H 3.917 0.020 1 252 34 34 THR C C 174.362 0.3 1 253 34 34 THR CA C 61.287 0.3 1 254 34 34 THR CB C 69.902 0.3 1 255 34 34 THR N N 115.570 0.3 1 256 35 35 LYS H H 8.207 0.020 1 257 35 35 LYS CA C 56.807 0.3 1 258 35 35 LYS CB C 32.619 0.3 1 259 35 35 LYS N N 122.771 0.3 1 260 37 37 ARG H H 8.928 0.020 1 261 37 37 ARG HA H 3.780 0.020 1 262 37 37 ARG HB2 H 1.776 0.020 1 263 37 37 ARG HG2 H 1.148 0.020 1 264 37 37 ARG HD2 H 2.744 0.020 1 265 37 37 ARG C C 178.008 0.3 1 266 37 37 ARG CA C 60.018 0.3 1 267 37 37 ARG CB C 30.364 0.3 1 268 37 37 ARG N N 118.964 0.3 1 269 38 38 PHE H H 7.570 0.020 1 270 38 38 PHE C C 178.384 0.3 1 271 38 38 PHE CA C 61.719 0.3 1 272 38 38 PHE CB C 39.083 0.3 1 273 38 38 PHE N N 117.968 0.3 1 274 39 39 TYR H H 7.766 0.020 1 275 39 39 TYR CA C 57.761 0.3 1 276 39 39 TYR CB C 40.827 0.3 1 277 39 39 TYR N N 117.979 0.3 1 278 41 41 GLN C C 173.826 0.3 1 279 41 41 GLN CA C 53.329 0.3 1 280 41 41 GLN CB C 29.121 0.3 1 281 42 42 PRO HA H 4.521 0.020 1 282 42 42 PRO HB2 H 2.299 0.020 2 283 42 42 PRO HB3 H 1.875 0.020 2 284 42 42 PRO HG2 H 2.025 0.020 1 285 42 42 PRO HD2 H 3.842 0.020 2 286 42 42 PRO HD3 H 3.668 0.020 2 287 42 42 PRO C C 176.576 0.3 1 288 42 42 PRO CA C 63.355 0.3 1 289 42 42 PRO CB C 32.351 0.3 1 290 42 42 PRO CG C 27.414 0.3 1 291 42 42 PRO N N 138.337 0.3 1 292 43 43 LEU H H 8.446 0.020 1 293 43 43 LEU C C 174.668 0.3 1 294 43 43 LEU CA C 51.696 0.3 1 295 43 43 LEU CB C 44.465 0.3 1 296 43 43 LEU N N 123.225 0.3 1 297 44 44 PRO C C 175.261 0.3 1 298 44 44 PRO CA C 61.348 0.3 1 299 44 44 PRO CB C 30.811 0.3 1 300 44 44 PRO N N 133.601 0.3 1 301 45 45 PRO HA H 3.965 0.020 1 302 45 45 PRO HB2 H 2.212 0.020 1 303 45 45 PRO C C 178.342 0.3 1 304 45 45 PRO CA C 67.129 0.3 1 305 45 45 PRO CB C 32.239 0.3 1 306 45 45 PRO N N 133.441 0.3 1 307 46 46 THR H H 8.726 0.020 1 308 46 46 THR HA H 3.979 0.020 1 309 46 46 THR HG2 H 1.251 0.020 1 310 46 46 THR C C 176.671 0.3 1 311 46 46 THR CA C 66.616 0.3 1 312 46 46 THR CB C 67.930 0.3 1 313 46 46 THR CG2 C 22.274 0.3 1 314 46 46 THR N N 113.415 0.3 1 315 47 47 GLU H H 7.770 0.020 1 316 47 47 GLU HA H 4.141 0.020 1 317 47 47 GLU HB2 H 2.062 0.020 1 318 47 47 GLU HG2 H 2.390 0.020 2 319 47 47 GLU HG3 H 2.244 0.020 2 320 47 47 GLU C C 179.288 0.3 1 321 47 47 GLU CA C 59.383 0.3 1 322 47 47 GLU CB C 30.312 0.3 1 323 47 47 GLU CG C 37.314 0.3 1 324 47 47 GLU N N 122.763 0.3 1 325 48 48 ALA H H 9.218 0.020 1 326 48 48 ALA HA H 3.992 0.020 1 327 48 48 ALA HB H 1.439 0.020 1 328 48 48 ALA C C 179.169 0.3 1 329 48 48 ALA CA C 55.240 0.3 1 330 48 48 ALA CB C 18.059 0.3 1 331 48 48 ALA N N 125.896 0.3 1 332 49 49 ALA H H 7.876 0.020 1 333 49 49 ALA HA H 3.842 0.020 1 334 49 49 ALA HB H 1.539 0.020 1 335 49 49 ALA C C 178.795 0.3 1 336 49 49 ALA CA C 55.169 0.3 1 337 49 49 ALA CB C 17.858 0.3 1 338 49 49 ALA N N 118.932 0.3 1 339 50 50 GLN H H 7.061 0.020 1 340 50 50 GLN CA C 58.353 0.3 1 341 50 50 GLN CB C 27.846 0.3 1 342 50 50 GLN N N 114.509 0.3 1 343 56 56 ALA H H 8.943 0.020 1 344 56 56 ALA HA H 3.979 0.020 1 345 56 56 ALA HB H 1.502 0.020 1 346 56 56 ALA C C 178.860 0.3 1 347 56 56 ALA CA C 55.360 0.3 1 348 56 56 ALA CB C 17.853 0.3 1 349 56 56 ALA N N 121.746 0.3 1 350 57 57 SER H H 7.899 0.020 1 351 57 57 SER CA C 61.997 0.3 1 352 57 57 SER CB C 62.748 0.3 1 353 57 57 SER N N 113.536 0.3 1 354 59 59 ILE HA H 3.773 0.020 1 355 59 59 ILE HB H 2.174 0.020 1 356 59 59 ILE HD1 H 0.769 0.020 1 357 59 59 ILE C C 177.559 0.3 1 358 59 59 ILE CA C 65.463 0.3 1 359 59 59 ILE CB C 36.571 0.3 1 360 59 59 ILE CG2 C 16.944 0.3 1 361 59 59 ILE CD1 C 13.708 0.3 1 362 60 60 LEU H H 7.680 0.020 1 363 60 60 LEU HA H 4.179 0.020 1 364 60 60 LEU HB2 H 2.137 0.020 2 365 60 60 LEU HB3 H 1.626 0.020 2 366 60 60 LEU HG H 1.502 0.020 1 367 60 60 LEU C C 180.571 0.3 1 368 60 60 LEU CA C 57.838 0.3 1 369 60 60 LEU CB C 40.440 0.3 1 370 60 60 LEU CG C 27.795 0.3 1 371 60 60 LEU CD1 C 24.464 0.3 1 372 60 60 LEU N N 117.387 0.3 1 373 61 61 ASN H H 7.640 0.020 1 374 61 61 ASN HA H 4.876 0.020 1 375 61 61 ASN HB2 H 2.983 0.020 1 376 61 61 ASN C C 176.499 0.3 1 377 61 61 ASN CA C 53.993 0.3 1 378 61 61 ASN CB C 38.238 0.3 1 379 61 61 ASN N N 115.884 0.3 1 380 62 62 VAL H H 8.077 0.020 1 381 62 62 VAL HA H 4.453 0.020 1 382 62 62 VAL HB H 2.871 0.020 1 383 62 62 VAL C C 177.001 0.3 1 384 62 62 VAL CA C 63.249 0.3 1 385 62 62 VAL CB C 31.789 0.3 1 386 62 62 VAL CG1 C 18.372 0.3 1 387 62 62 VAL CG2 C 20.561 0.3 1 388 62 62 VAL N N 113.212 0.3 1 389 63 63 LYS H H 7.060 0.020 1 390 63 63 LYS HA H 4.179 0.020 1 391 63 63 LYS HB2 H 1.676 0.020 2 392 63 63 LYS HB3 H 1.489 0.020 2 393 63 63 LYS HE2 H 2.925 0.020 1 394 63 63 LYS C C 177.215 0.3 1 395 63 63 LYS CA C 58.806 0.3 1 396 63 63 LYS CB C 31.534 0.3 1 397 63 63 LYS CG C 24.464 0.3 1 398 63 63 LYS N N 122.829 0.3 1 399 64 64 GLN H H 7.633 0.020 1 400 64 64 GLN HA H 4.067 0.020 1 401 64 64 GLN HB2 H 1.788 0.020 1 402 64 64 GLN C C 177.275 0.3 1 403 64 64 GLN CA C 58.164 0.3 1 404 64 64 GLN CB C 27.257 0.3 1 405 64 64 GLN CG C 31.888 0.3 1 406 64 64 GLN N N 115.109 0.3 1 407 65 65 PHE H H 7.171 0.020 1 408 65 65 PHE HA H 4.316 0.020 1 409 65 65 PHE HB2 H 3.376 0.020 2 410 65 65 PHE HB3 H 2.871 0.020 2 411 65 65 PHE C C 177.929 0.3 1 412 65 65 PHE CA C 59.023 0.3 1 413 65 65 PHE CB C 39.134 0.3 1 414 65 65 PHE N N 117.172 0.3 1 415 66 66 ILE H H 7.381 0.020 1 416 66 66 ILE C C 174.811 0.3 1 417 66 66 ILE CA C 65.473 0.3 1 418 66 66 ILE CB C 37.571 0.3 1 419 66 66 ILE N N 120.163 0.3 1 420 68 68 ARG H H 6.878 0.020 1 421 68 68 ARG HA H 4.266 0.020 1 422 68 68 ARG HB2 H 1.925 0.020 2 423 68 68 ARG HB3 H 1.564 0.020 2 424 68 68 ARG HD2 H 3.120 0.020 1 425 68 68 ARG C C 174.692 0.3 1 426 68 68 ARG CA C 55.516 0.3 1 427 68 68 ARG CB C 30.934 0.3 1 428 68 68 ARG CG C 25.316 0.3 1 429 68 68 ARG N N 113.972 0.3 1 430 69 69 LYS H H 7.567 0.020 1 431 69 69 LYS HA H 4.092 0.020 1 432 69 69 LYS HB2 H 2.000 0.020 2 433 69 69 LYS HB3 H 1.713 0.020 2 434 69 69 LYS C C 174.137 0.3 1 435 69 69 LYS CA C 56.617 0.3 1 436 69 69 LYS CB C 28.524 0.3 1 437 69 69 LYS CG C 25.606 0.3 1 438 69 69 LYS N N 118.903 0.3 1 439 70 70 ALA H H 8.003 0.020 1 440 70 70 ALA HA H 4.565 0.020 1 441 70 70 ALA HB H 1.265 0.020 1 442 70 70 ALA C C 177.429 0.3 1 443 70 70 ALA CA C 48.884 0.3 1 444 70 70 ALA CB C 17.392 0.3 1 445 70 70 ALA N N 122.931 0.3 1 446 71 71 TRP H H 7.032 0.020 1 447 71 71 TRP C C 175.088 0.3 1 448 71 71 TRP CA C 60.303 0.3 1 449 71 71 TRP CB C 27.607 0.3 1 450 71 71 TRP N N 119.538 0.3 1 451 72 72 PRO C C 179.767 0.3 1 452 72 72 PRO CA C 65.943 0.3 1 453 72 72 PRO CB C 29.987 0.3 1 454 72 72 PRO N N 136.568 0.3 1 455 80 80 LEU HA H 3.905 0.020 1 456 80 80 LEU HB2 H 1.701 0.020 1 457 80 80 LEU HG H 1.414 0.020 1 458 80 80 LEU HD1 H 0.742 0.020 1 459 80 80 LEU HD2 H 1.078 0.020 1 460 80 80 LEU C C 178.632 0.3 1 461 80 80 LEU CA C 58.168 0.3 1 462 80 80 LEU CB C 42.335 0.3 1 463 80 80 LEU CG C 26.748 0.3 1 464 80 80 LEU CD1 C 25.035 0.3 1 465 81 81 ARG H H 8.386 0.020 1 466 81 81 ARG HA H 3.905 0.020 1 467 81 81 ARG HB2 H 1.913 0.020 1 468 81 81 ARG HD2 H 2.949 0.020 1 469 81 81 ARG C C 179.411 0.3 1 470 81 81 ARG CA C 57.832 0.3 1 471 81 81 ARG CB C 29.602 0.3 1 472 81 81 ARG CG C 26.367 0.3 1 473 81 81 ARG N N 115.127 0.3 1 474 82 82 ALA H H 9.140 0.020 1 475 82 82 ALA HA H 4.166 0.020 1 476 82 82 ALA HB H 1.664 0.020 1 477 82 82 ALA C C 179.414 0.3 1 478 82 82 ALA CA C 55.645 0.3 1 479 82 82 ALA CB C 18.863 0.3 1 480 82 82 ALA N N 119.805 0.3 1 481 83 83 SER H H 7.751 0.020 1 482 83 83 SER CA C 61.830 0.3 1 483 83 83 SER CB C 62.762 0.3 1 484 83 83 SER N N 114.702 0.3 1 485 85 85 LEU H H 7.810 0.020 1 486 85 85 LEU HA H 3.780 0.020 1 487 85 85 LEU HB2 H 2.311 0.020 2 488 85 85 LEU HB3 H 1.564 0.020 2 489 85 85 LEU C C 177.337 0.3 1 490 85 85 LEU CA C 58.902 0.3 1 491 85 85 LEU CB C 41.570 0.3 1 492 85 85 LEU CG C 28.366 0.3 1 493 85 85 LEU CD1 C 25.891 0.3 1 494 85 85 LEU N N 121.817 0.3 1 495 86 86 ARG H H 8.088 0.020 1 496 86 86 ARG HA H 3.793 0.020 1 497 86 86 ARG HB2 H 2.174 0.020 2 498 86 86 ARG HB3 H 1.950 0.020 2 499 86 86 ARG HD2 H 2.523 0.020 1 500 86 86 ARG C C 178.060 0.3 1 501 86 86 ARG CA C 60.341 0.3 1 502 86 86 ARG CB C 29.952 0.3 1 503 86 86 ARG N N 115.425 0.3 1 504 87 87 TYR H H 8.164 0.020 1 505 87 87 TYR HA H 4.341 0.020 1 506 87 87 TYR HB2 H 2.909 0.020 2 507 87 87 TYR HB3 H 2.734 0.020 2 508 87 87 TYR C C 177.599 0.3 1 509 87 87 TYR CA C 56.311 0.3 1 510 87 87 TYR CB C 38.537 0.3 1 511 87 87 TYR N N 115.945 0.3 1 512 88 88 ASP H H 8.021 0.020 1 513 88 88 ASP HA H 4.440 0.020 1 514 88 88 ASP HB2 H 2.841 0.020 2 515 88 88 ASP HB3 H 2.572 0.020 2 516 88 88 ASP C C 178.265 0.3 1 517 88 88 ASP CA C 57.924 0.3 1 518 88 88 ASP CB C 42.257 0.3 1 519 88 88 ASP N N 120.649 0.3 1 520 89 89 LEU H H 8.665 0.020 1 521 89 89 LEU HA H 3.979 0.020 1 522 89 89 LEU HB2 H 2.037 0.020 2 523 89 89 LEU HB3 H 1.726 0.020 2 524 89 89 LEU HG H 1.437 0.020 1 525 89 89 LEU HD1 H 1.016 0.020 1 526 89 89 LEU C C 178.075 0.3 1 527 89 89 LEU CA C 58.307 0.3 1 528 89 89 LEU CB C 43.195 0.3 1 529 89 89 LEU CD1 C 26.272 0.3 1 530 89 89 LEU N N 118.115 0.3 1 531 90 90 LYS H H 8.002 0.020 1 532 90 90 LYS C C 179.669 0.3 1 533 90 90 LYS CA C 59.394 0.3 1 534 90 90 LYS CB C 30.046 0.3 1 535 90 90 LYS N N 115.802 0.3 1 536 91 91 THR C C 173.861 0.3 1 537 91 91 THR CA C 61.884 0.3 1 538 91 91 THR CB C 70.081 0.3 1 539 91 91 THR N N 116.827 0.3 1 540 94 94 SER H H 7.757 0.020 1 541 94 94 SER HA H 4.079 0.020 1 542 94 94 SER C C 174.264 0.3 1 543 94 94 SER CA C 61.437 0.3 1 544 94 94 SER CB C 62.964 0.3 1 545 94 94 SER N N 112.225 0.3 1 546 95 95 ALA H H 7.143 0.020 1 547 95 95 ALA HA H 4.540 0.020 1 548 95 95 ALA HB H 1.527 0.020 1 549 95 95 ALA C C 177.789 0.3 1 550 95 95 ALA CA C 51.437 0.3 1 551 95 95 ALA CB C 19.719 0.3 1 552 95 95 ALA N N 120.912 0.3 1 553 96 96 LYS H H 7.439 0.020 1 554 96 96 LYS C C 174.077 0.3 1 555 96 96 LYS CA C 53.269 0.3 1 556 96 96 LYS CB C 32.074 0.3 1 557 96 96 LYS N N 120.570 0.3 1 558 100 100 GLU HA H 4.515 0.020 1 559 100 100 GLU HB2 H 2.398 0.020 2 560 100 100 GLU HB3 H 2.087 0.020 2 561 100 100 GLU C C 177.275 0.3 1 562 100 100 GLU CA C 62.501 0.3 1 563 100 100 GLU CB C 32.563 0.3 1 564 100 100 GLU CG C 37.409 0.3 1 565 101 101 LYS H H 8.643 0.020 1 566 101 101 LYS HA H 3.764 0.020 1 567 101 101 LYS HB2 H 1.639 0.020 1 568 101 101 LYS HG2 H 1.315 0.020 1 569 101 101 LYS HE2 H 3.245 0.020 2 570 101 101 LYS HE3 H 3.021 0.020 2 571 101 101 LYS C C 178.250 0.3 1 572 101 101 LYS CA C 60.833 0.3 1 573 101 101 LYS CB C 32.886 0.3 1 574 101 101 LYS CG C 24.464 0.3 1 575 101 101 LYS N N 120.567 0.3 1 576 102 102 LYS H H 7.861 0.020 1 577 102 102 LYS HA H 4.017 0.020 1 578 102 102 LYS HB2 H 1.913 0.020 1 579 102 102 LYS HG2 H 1.514 0.020 1 580 102 102 LYS HD2 H 1.710 0.020 1 581 102 102 LYS HE2 H 2.978 0.020 1 582 102 102 LYS C C 179.027 0.3 1 583 102 102 LYS CA C 59.623 0.3 1 584 102 102 LYS CB C 32.220 0.3 1 585 102 102 LYS CG C 24.749 0.3 1 586 102 102 LYS N N 118.087 0.3 1 587 103 103 SER H H 7.995 0.020 1 588 103 103 SER HA H 4.278 0.020 1 589 103 103 SER HB2 H 3.955 0.020 1 590 103 103 SER C C 177.670 0.3 1 591 103 103 SER CA C 61.357 0.3 1 592 103 103 SER CB C 62.570 0.3 1 593 103 103 SER N N 113.241 0.3 1 594 104 104 LEU H H 8.066 0.020 1 595 104 104 LEU HA H 4.216 0.020 1 596 104 104 LEU HB2 H 1.863 0.020 2 597 104 104 LEU HB3 H 1.576 0.020 2 598 104 104 LEU HG H 1.701 0.020 1 599 104 104 LEU HD1 H 0.938 0.020 1 600 104 104 LEU HD2 H 0.821 0.020 1 601 104 104 LEU C C 179.883 0.3 1 602 104 104 LEU CA C 57.785 0.3 1 603 104 104 LEU CB C 41.833 0.3 1 604 104 104 LEU CG C 27.414 0.3 1 605 104 104 LEU CD1 C 25.130 0.3 1 606 104 104 LEU N N 121.281 0.3 1 607 105 105 GLN H H 8.965 0.020 1 608 105 105 GLN C C 178.833 0.3 1 609 105 105 GLN CA C 59.499 0.3 1 610 105 105 GLN CB C 28.333 0.3 1 611 105 105 GLN N N 122.396 0.3 1 612 106 106 GLU HA H 4.119 0.020 1 613 106 106 GLU HB2 H 2.174 0.020 1 614 106 106 GLU HG2 H 2.261 0.020 1 615 106 106 GLU HG3 H 2.506 0.020 2 616 106 106 GLU C C 179.692 0.3 1 617 106 106 GLU CA C 59.624 0.3 1 618 106 106 GLU CB C 29.136 0.3 1 619 106 106 GLU CG C 36.648 0.3 1 620 106 106 GLU N N 120.659 0.3 1 621 107 107 LEU H H 7.933 0.020 1 622 107 107 LEU HA H 4.116 0.020 1 623 107 107 LEU HB2 H 1.900 0.020 2 624 107 107 LEU HB3 H 1.589 0.020 2 625 107 107 LEU HD1 H 0.865 0.020 1 626 107 107 LEU C C 179.661 0.3 1 627 107 107 LEU CA C 57.664 0.3 1 628 107 107 LEU CB C 42.523 0.3 1 629 107 107 LEU CG C 26.843 0.3 1 630 107 107 LEU CD1 C 24.940 0.3 1 631 107 107 LEU N N 119.770 0.3 1 632 108 108 THR H H 8.647 0.020 1 633 108 108 THR CA C 67.339 0.3 1 634 108 108 THR CB C 68.090 0.3 1 635 108 108 THR N N 115.384 0.3 1 636 111 111 LEU H H 7.943 0.020 1 637 111 111 LEU HA H 4.092 0.020 1 638 111 111 LEU HB2 H 2.074 0.020 2 639 111 111 LEU HB3 H 1.215 0.020 2 640 111 111 LEU HG H 1.730 0.020 1 641 111 111 LEU HD1 H 0.560 0.020 1 642 111 111 LEU C C 177.917 0.3 1 643 111 111 LEU CA C 57.832 0.3 1 644 111 111 LEU CB C 41.009 0.3 1 645 111 111 LEU CG C 26.939 0.3 1 646 111 111 LEU CD1 C 24.940 0.3 1 647 111 111 LEU N N 120.455 0.3 1 648 112 112 PHE H H 8.697 0.020 1 649 112 112 PHE HA H 4.278 0.020 1 650 112 112 PHE HB2 H 3.350 0.020 2 651 112 112 PHE HB3 H 3.021 0.020 2 652 112 112 PHE C C 177.965 0.3 1 653 112 112 PHE CA C 62.679 0.3 1 654 112 112 PHE CB C 37.302 0.3 1 655 112 112 PHE N N 116.713 0.3 1 656 113 113 SER H H 8.110 0.020 1 657 113 113 SER CA C 62.106 0.3 1 658 113 113 SER CB C 63.950 0.3 1 659 113 113 SER N N 117.047 0.3 1 660 118 118 LEU H H 8.331 0.020 1 661 118 118 LEU HA H 4.228 0.020 1 662 118 118 LEU HB2 H 1.352 0.020 1 663 118 118 LEU C C 176.811 0.3 1 664 118 118 LEU CA C 57.950 0.3 1 665 118 118 LEU CB C 41.094 0.3 1 666 118 118 LEU N N 125.608 0.3 1 667 119 119 ASP H H 8.592 0.020 1 668 119 119 ASP HA H 4.104 0.020 1 669 119 119 ASP HB2 H 3.083 0.020 2 670 119 119 ASP HB3 H 2.734 0.020 2 671 119 119 ASP C C 178.310 0.3 1 672 119 119 ASP CA C 57.993 0.3 1 673 119 119 ASP CB C 42.089 0.3 1 674 119 119 ASP N N 120.339 0.3 1 675 120 120 HIS H H 8.185 0.020 1 676 120 120 HIS HA H 4.116 0.020 1 677 120 120 HIS HB2 H 3.232 0.020 1 678 120 120 HIS C C 176.573 0.3 1 679 120 120 HIS CA C 60.152 0.3 1 680 120 120 HIS CB C 28.815 0.3 1 681 120 120 HIS N N 117.407 0.3 1 682 121 121 ALA H H 8.168 0.020 1 683 121 121 ALA HA H 4.067 0.020 1 684 121 121 ALA HB H 1.639 0.020 1 685 121 121 ALA C C 178.239 0.3 1 686 121 121 ALA CA C 54.522 0.3 1 687 121 121 ALA CB C 17.953 0.3 1 688 121 121 ALA N N 121.398 0.3 1 689 122 122 ALA H H 7.822 0.020 1 690 122 122 ALA HA H 4.191 0.020 1 691 122 122 ALA HB H 1.726 0.020 1 692 122 122 ALA C C 179.738 0.3 1 693 122 122 ALA CA C 53.666 0.3 1 694 122 122 ALA CB C 19.266 0.3 1 695 122 122 ALA N N 117.609 0.3 1 696 123 123 LYS H H 8.048 0.020 1 697 123 123 LYS HA H 3.780 0.020 1 698 123 123 LYS HB2 H 1.975 0.020 1 699 123 123 LYS C C 178.828 0.3 1 700 123 123 LYS CA C 59.565 0.3 1 701 123 123 LYS CB C 32.188 0.3 1 702 123 123 LYS N N 122.209 0.3 1 703 124 124 ILE H H 7.426 0.020 1 704 124 124 ILE HA H 4.104 0.020 1 705 124 124 ILE HB H 2.025 0.020 1 706 124 124 ILE C C 174.838 0.3 1 707 124 124 ILE CA C 61.063 0.3 1 708 124 124 ILE CB C 37.112 0.3 1 709 124 124 ILE CG2 C 17.610 0.3 1 710 124 124 ILE CD1 C 14.374 0.3 1 711 124 124 ILE N N 108.565 0.3 1 712 125 125 LYS H H 7.121 0.020 1 713 125 125 LYS HB2 H 1.713 0.020 2 714 125 125 LYS HB3 H 1.278 0.020 2 715 125 125 LYS HE2 H 3.018 0.020 1 716 125 125 LYS C C 174.814 0.3 1 717 125 125 LYS CA C 55.797 0.3 1 718 125 125 LYS CB C 28.803 0.3 1 719 125 125 LYS CG C 24.749 0.3 1 720 125 125 LYS N N 120.011 0.3 1 721 126 126 SER H H 7.274 0.020 1 722 126 126 SER C C 173.482 0.3 1 723 126 126 SER CA C 53.105 0.3 1 724 126 126 SER CB C 63.922 0.3 1 725 126 126 SER N N 111.274 0.3 1 726 127 127 PRO HA H 4.453 0.020 1 727 127 127 PRO HB2 H 2.672 0.020 2 728 127 127 PRO HB3 H 2.274 0.020 2 729 127 127 PRO C C 179.083 0.3 1 730 127 127 PRO CA C 65.516 0.3 1 731 127 127 PRO CB C 32.327 0.3 1 732 127 127 PRO CG C 28.176 0.3 1 733 128 128 THR H H 7.833 0.020 1 734 128 128 THR HA H 4.139 0.020 1 735 128 128 THR HB H 4.138 0.020 1 736 128 128 THR HG2 H 1.282 0.020 1 737 128 128 THR C C 178.765 0.3 1 738 128 128 THR CA C 65.146 0.3 1 739 128 128 THR CB C 67.774 0.3 1 740 128 128 THR CG2 C 22.274 0.3 1 741 128 128 THR N N 109.654 0.3 1 742 129 129 GLU H H 8.079 0.020 1 743 129 129 GLU HA H 4.465 0.020 1 744 129 129 GLU HB2 H 2.336 0.020 1 745 129 129 GLU HB3 H 2.336 0.020 2 746 129 129 GLU C C 178.122 0.3 1 747 129 129 GLU CA C 58.657 0.3 1 748 129 129 GLU CB C 29.678 0.3 1 749 129 129 GLU CG C 36.933 0.3 1 750 129 129 GLU N N 123.057 0.3 1 751 130 130 ALA H H 8.733 0.020 1 752 130 130 ALA HA H 4.054 0.020 1 753 130 130 ALA HB H 1.502 0.020 1 754 130 130 ALA C C 179.145 0.3 1 755 130 130 ALA CA C 55.266 0.3 1 756 130 130 ALA CB C 18.293 0.3 1 757 130 130 ALA N N 122.154 0.3 1 758 131 131 GLU H H 8.348 0.020 1 759 131 131 GLU HA H 4.054 0.020 1 760 131 131 GLU HB2 H 2.138 0.020 1 761 131 131 GLU HG2 H 2.471 0.020 2 762 131 131 GLU HG3 H 2.283 0.020 2 763 131 131 GLU C C 179.714 0.3 1 764 131 131 GLU CA C 60.113 0.3 1 765 131 131 GLU CB C 29.454 0.3 1 766 131 131 GLU CG C 36.457 0.3 1 767 131 131 GLU N N 117.714 0.3 1 768 132 132 LYS H H 7.595 0.020 1 769 132 132 LYS HA H 3.979 0.020 1 770 132 132 LYS HB2 H 1.688 0.020 1 771 132 132 LYS HE2 H 2.541 0.020 1 772 132 132 LYS C C 180.047 0.3 1 773 132 132 LYS CA C 59.355 0.3 1 774 132 132 LYS CB C 32.176 0.3 1 775 132 132 LYS CG C 23.797 0.3 1 776 132 132 LYS N N 120.922 0.3 1 777 133 133 TYR H H 8.568 0.020 1 778 133 133 TYR HA H 4.453 0.020 1 779 133 133 TYR HB2 H 3.369 0.020 2 780 133 133 TYR HB3 H 2.560 0.020 2 781 133 133 TYR C C 179.167 0.3 1 782 133 133 TYR CA C 62.567 0.3 1 783 133 133 TYR CB C 37.035 0.3 1 784 133 133 TYR N N 116.687 0.3 1 785 134 134 TYR H H 9.576 0.020 1 786 134 134 TYR HA H 4.154 0.020 1 787 134 134 TYR HB2 H 3.120 0.020 1 788 134 134 TYR C C 176.382 0.3 1 789 134 134 TYR CA C 63.093 0.3 1 790 134 134 TYR CB C 38.142 0.3 1 791 134 134 TYR N N 127.198 0.3 1 792 135 135 GLY H H 8.182 0.020 1 793 135 135 GLY HA2 H 4.004 0.020 2 794 135 135 GLY HA3 H 3.681 0.020 2 795 135 135 GLY C C 177.239 0.3 1 796 135 135 GLY CA C 47.529 0.3 1 797 135 135 GLY N N 106.437 0.3 1 798 136 136 GLN H H 7.615 0.020 1 799 136 136 GLN HA H 4.104 0.020 1 800 136 136 GLN HB2 H 2.286 0.020 2 801 136 136 GLN HB3 H 2.083 0.020 2 802 136 136 GLN HG2 H 2.583 0.020 2 803 136 136 GLN HG3 H 2.443 0.020 2 804 136 136 GLN C C 177.682 0.3 1 805 136 136 GLN CA C 59.093 0.3 1 806 136 136 GLN CB C 28.905 0.3 1 807 136 136 GLN CG C 33.982 0.3 1 808 136 136 GLN N N 119.338 0.3 1 809 137 137 THR H H 8.053 0.020 1 810 137 137 THR CA C 68.667 0.3 1 811 137 137 THR CB C 67.659 0.3 1 812 137 137 THR N N 118.566 0.3 1 813 141 141 ILE H H 9.189 0.020 1 814 141 141 ILE HA H 4.428 0.020 1 815 141 141 ILE HB H 2.174 0.020 1 816 141 141 ILE HD1 H 0.814 0.020 1 817 141 141 ILE C C 177.242 0.3 1 818 141 141 ILE CA C 65.055 0.3 1 819 141 141 ILE CB C 36.351 0.3 1 820 141 141 ILE CG2 C 17.534 0.3 1 821 141 141 ILE CD1 C 13.552 0.3 1 822 141 141 ILE N N 123.371 0.3 1 823 142 142 ASN H H 8.288 0.020 1 824 142 142 ASN HA H 4.428 0.020 1 825 142 142 ASN HB2 H 2.958 0.020 2 826 142 142 ASN HB3 H 2.756 0.020 2 827 142 142 ASN C C 178.762 0.3 1 828 142 142 ASN CA C 56.522 0.3 1 829 142 142 ASN CB C 37.475 0.3 1 830 142 142 ASN N N 119.151 0.3 1 831 143 143 GLU H H 7.800 0.020 1 832 143 143 GLU HA H 4.116 0.020 1 833 143 143 GLU HB2 H 2.174 0.020 1 834 143 143 GLU C C 179.037 0.3 1 835 143 143 GLU CA C 59.643 0.3 1 836 143 143 GLU CB C 29.965 0.3 1 837 143 143 GLU CG C 36.743 0.3 1 838 143 143 GLU N N 119.853 0.3 1 839 144 144 VAL H H 7.919 0.020 1 840 144 144 VAL HA H 3.467 0.020 1 841 144 144 VAL HB H 2.199 0.020 1 842 144 144 VAL HG1 H 0.940 0.020 1 843 144 144 VAL HG2 H 0.806 0.020 1 844 144 144 VAL C C 177.908 0.3 1 845 144 144 VAL CA C 66.997 0.3 1 846 144 144 VAL CB C 31.571 0.3 1 847 144 144 VAL CG1 C 21.037 0.3 1 848 144 144 VAL CG2 C 24.368 0.3 1 849 144 144 VAL N N 119.901 0.3 1 850 145 145 LEU H H 8.982 0.020 1 851 145 145 LEU HA H 3.867 0.020 1 852 145 145 LEU HB2 H 1.952 0.020 2 853 145 145 LEU HB3 H 1.502 0.020 2 854 145 145 LEU HG H 1.167 0.020 1 855 145 145 LEU HD1 H 0.864 0.020 1 856 145 145 LEU C C 180.097 0.3 1 857 145 145 LEU CA C 58.156 0.3 1 858 145 145 LEU CB C 40.865 0.3 1 859 145 145 LEU CG C 27.129 0.3 1 860 145 145 LEU CD1 C 25.511 0.3 1 861 145 145 LEU N N 118.426 0.3 1 862 146 146 ALA H H 7.513 0.020 1 863 146 146 ALA HA H 4.191 0.020 1 864 146 146 ALA HB H 1.477 0.020 1 865 146 146 ALA C C 179.476 0.3 1 866 146 146 ALA CA C 54.351 0.3 1 867 146 146 ALA CB C 18.006 0.3 1 868 146 146 ALA N N 119.677 0.3 1 869 147 147 LYS H H 7.568 0.020 1 870 147 147 LYS HA H 4.353 0.020 1 871 147 147 LYS HB2 H 1.925 0.020 1 872 147 147 LYS HD2 H 1.621 0.020 1 873 147 147 LYS HE2 H 2.926 0.020 1 874 147 147 LYS C C 177.596 0.3 1 875 147 147 LYS CA C 55.474 0.3 1 876 147 147 LYS CB C 32.619 0.3 1 877 147 147 LYS CG C 24.844 0.3 1 878 147 147 LYS N N 115.845 0.3 1 879 148 148 LEU H H 7.664 0.020 1 880 148 148 LEU HA H 4.191 0.020 1 881 148 148 LEU HB2 H 2.338 0.020 2 882 148 148 LEU HB3 H 1.875 0.020 2 883 148 148 LEU HG H 1.984 0.020 1 884 148 148 LEU HD1 H 0.782 0.020 1 885 148 148 LEU C C 177.001 0.3 1 886 148 148 LEU CA C 55.836 0.3 1 887 148 148 LEU CB C 42.332 0.3 1 888 148 148 LEU CG C 26.082 0.3 1 889 148 148 LEU N N 119.200 0.3 1 890 149 149 GLY H H 7.560 0.020 1 891 149 149 GLY C C 179.048 0.3 1 892 149 149 GLY CA C 46.240 0.3 1 893 149 149 GLY N N 112.662 0.3 1 stop_ save_