data_4786 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N assignment of a bleomycin resistance protein in its native form and in a complex with Zn(2+) ligated bleomycin ; _BMRB_accession_number 4786 _BMRB_flat_file_name bmr4786.str _Entry_type original _Submission_date 2000-07-17 _Accession_date 2000-07-17 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Assignment of the backbone and aliphatic chain' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vanbelle Christophe . . 2 Muhle-Goll Claudia . . 3 Remy Marie-Helene . . 4 Masson Jean-Michel . . 5 Marion Dominique . . 6 Brutscher Bernhard . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 559 "13C chemical shifts" 467 "15N chemical shifts" 117 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-10-30 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4785 BRP stop_ _Original_release_date 2000-10-30 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C, and 15N assignment of a bleomycin resistance protein in its native form and in a complex with Zn2+ ligated bleomycin ; _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 Vanbelle Christophe . . 2 Muhle-Goll Claudia . . 3 Remy Marie-Helene . . 4 Masson Jean-Michel . . 5 Marion Dominique . . 6 Brutscher Bernhard . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 18 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 177 _Page_last 178 _Year 2000 _Details . loop_ _Keyword 'bleomycin resistance' 'DNA cleavage' 'molecular interaction' 'NMR assignment' stop_ save_ ################################## # Molecular system description # ################################## save_system_BRP _Saveframe_category molecular_system _Mol_system_name 'Bleomycin resistance protein of S. hindustanus' _Abbreviation_common BRP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'BRP monomer 1' $Sh_BRP 'BRP monomer 2' $Sh_BRP 'BLM 1' $BLM 'BLM 2' $BLM 'Zn 1' $ZN 'Zn 2' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'BRP monomer 1' 1 'BRP monomer 2' 1 'BLM 1' 1 'BLM 2' 1 'Zn 1' 1 'Zn 2' stop_ loop_ _Biological_function 'Bleomycin resistance by its sequestration' 'Phleomycin resistance by its sequestration' 'Tallysomycin resistance by its sequestration' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Sh_BRP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'S. hindustanus bleomycin resistance protein' _Abbreviation_common 'Sh BRP' _Molecular_mass 13796 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 124 _Mol_residue_sequence ; MAKLTSAVPVLTARDVAGAV EFWTDRLGFSRDFVEDDFAG VVRDDVTLFISAVQDQVVPD NTLAWVWVRGLDELYAEWSE VVSTNFRDASGPAMTEIGEQ PWGREFALRDPAGNCVHFVA EEQD ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 LYS 4 LEU 5 THR 6 SER 7 ALA 8 VAL 9 PRO 10 VAL 11 LEU 12 THR 13 ALA 14 ARG 15 ASP 16 VAL 17 ALA 18 GLY 19 ALA 20 VAL 21 GLU 22 PHE 23 TRP 24 THR 25 ASP 26 ARG 27 LEU 28 GLY 29 PHE 30 SER 31 ARG 32 ASP 33 PHE 34 VAL 35 GLU 36 ASP 37 ASP 38 PHE 39 ALA 40 GLY 41 VAL 42 VAL 43 ARG 44 ASP 45 ASP 46 VAL 47 THR 48 LEU 49 PHE 50 ILE 51 SER 52 ALA 53 VAL 54 GLN 55 ASP 56 GLN 57 VAL 58 VAL 59 PRO 60 ASP 61 ASN 62 THR 63 LEU 64 ALA 65 TRP 66 VAL 67 TRP 68 VAL 69 ARG 70 GLY 71 LEU 72 ASP 73 GLU 74 LEU 75 TYR 76 ALA 77 GLU 78 TRP 79 SER 80 GLU 81 VAL 82 VAL 83 SER 84 THR 85 ASN 86 PHE 87 ARG 88 ASP 89 ALA 90 SER 91 GLY 92 PRO 93 ALA 94 MET 95 THR 96 GLU 97 ILE 98 GLY 99 GLU 100 GLN 101 PRO 102 TRP 103 GLY 104 ARG 105 GLU 106 PHE 107 ALA 108 LEU 109 ARG 110 ASP 111 PRO 112 ALA 113 GLY 114 ASN 115 CYS 116 VAL 117 HIS 118 PHE 119 VAL 120 ALA 121 GLU 122 GLU 123 GLN 124 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 4785 Sh_BRP 100.00 124 100.00 100.00 2.71e-82 PDB 1BYL "Bleomycin Resistance Protein From Streptoalloteichus Hindustanus" 100.00 125 100.00 100.00 2.86e-82 PDB 2ZHP "Crystal Structure Of Bleomycin-Binding Protein From Streptoalloteichus Hindustanus Complexed With Bleomycin Derivative" 100.00 124 100.00 100.00 2.71e-82 DBJ BAC41730 "bleomycin resistance [Retroviral vector pCX4bleo]" 100.00 124 100.00 100.00 2.71e-82 DBJ BAF75469 "zeocin resistant protein [synthetic construct]" 100.00 124 100.00 100.00 2.71e-82 DBJ BAG54978 "zeocin registance [Shuttle vector pCRB15]" 100.00 124 100.00 100.00 2.71e-82 DBJ BAG71041 "zeocin resistant [synthetic construct]" 100.00 124 100.00 100.00 2.71e-82 DBJ BAI39424 "bleomycin resistance protein [Expression vector pTY2b]" 101.61 126 98.41 98.41 2.07e-80 EMBL CAA37050 "unnamed protein product [Streptoalloteichus hindustanus]" 100.00 124 100.00 100.00 2.71e-82 EMBL CAA83658 "phleomycin binding protein [synthetic construct]" 100.00 124 100.00 100.00 2.71e-82 EMBL CAD21454 "BlEomycin resistance protein [Trypanosoma brucei]" 100.00 124 100.00 100.00 2.71e-82 GB AAA72449 "phleomycin/zeocin binding protein [Cloning vector pZEO]" 100.00 124 100.00 100.00 2.71e-82 GB AAA72451 "phleomycin/zeocin binding protein [Cloning vector pZEO]" 100.00 124 100.00 100.00 2.71e-82 GB AAA73162 "synthetic fusion protein [synthetic construct]" 100.00 1149 100.00 100.00 7.68e-75 GB AAA73163 "synthetic fusion protein [synthetic construct]" 100.00 1144 100.00 100.00 6.05e-75 GB AAA93507 "(thymidine kinase):(phleomycin/zeocin binding protein) fusion protein [Cloning vector pZEO-SG1]" 100.00 740 100.00 100.00 5.25e-78 SP P17493 "RecName: Full=Bleomycin resistance protein; Short=BRP; AltName: Full=Phleomycin resistance protein [Streptoalloteichus hindusta" 100.00 124 100.00 100.00 2.71e-82 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jun 15 12:20:01 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_BLM _Saveframe_category ligand _Mol_type non-polymer _Name_common "BLM (BLEOMYCIN A2)" _BMRB_code . _PDB_code BLM _Molecular_mass 1416.560 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jun 15 12:24:53 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons NA NA N . 0 . ? C2 C2 C . 0 . ? C1 C1 C . 0 . ? O1 O1 O . 0 . ? NC NC N . 0 . ? C3 C3 C . 0 . ? NB NB N . 0 . ? ND ND N . 0 . ? C5 C5 C . 0 . ? C4 C4 C . 0 . ? O4 O4 O . 0 . ? C8 C8 C . 0 . ? C9 C9 C . 0 . ? C10 C10 C . 0 . ? NG NG N . 0 . ? C7 C7 C . 0 . ? NE NE N . 0 . ? C6 C6 C . 0 . ? NF NF N . 0 . ? CA CA C . 0 . ? C12 C12 C . 0 . ? O12 O12 O . 0 . ? NH NH N . 0 . ? C13 C13 C . 0 . ? C30 C30 C . 0 . ? O30 O30 O . 0 . ? C14 C14 C . 0 . ? C27 C27 C . 0 . ? OH1 OH1 O . 0 . ? NJ NJ N . 0 . ? C28 C28 C . 0 . ? C29 C29 C . 0 . ? NI NI N . 0 . ? NK NK N . 0 . ? C34 C34 C . 0 . ? C36 C36 C . 0 . ? O36 O36 O . 0 . ? OH2 OH2 O . 0 . ? C31 C31 C . 0 . ? CB CB C . 0 . ? C33 C33 C . 0 . ? CC CC C . 0 . ? NL NL N . 0 . ? C37 C37 C . 0 . ? C40 C40 C . 0 . ? O40 O40 O . 0 . ? C38 C38 C . 0 . ? OH3 OH3 O . 0 . ? CD CD C . 0 . ? NM NM N . 0 . ? C42 C42 C . 0 . ? C49 C49 C . 0 . ? O49 O49 O . 0 . ? C43 C43 C . 0 . ? C41 C41 C . 0 . ? S43 S43 S . 0 . ? C44 C44 C . 0 . ? C45 C45 C . 0 . ? NN NN N . 0 . ? C47 C47 C . 0 . ? C48 C48 C . 0 . ? NO NO N . 0 . ? C46 C46 C . 0 . ? S46 S46 S . 0 . ? NP NP N . 0 . ? C50 C50 C . 0 . ? C51 C51 C . 0 . ? C52 C52 C . 0 . ? S53 S53 S . 0 . ? C55 C55 C . 0 . ? C54 C54 C . 0 . ? O59 O59 O . 0 . ? O58 O58 O . 0 . ? C61 C61 C . 0 . ? O61 O61 O . 0 . ? O56 O56 O . 0 . ? C60 C60 C . 0 . ? O62 O62 O . 0 . ? C63 C63 C . 0 . ? C57 C57 C . 0 . ? C58 C58 C . 0 . ? C59 C59 C . 0 . ? C69 C69 C . 0 . ? C68 C68 C . 0 . ? C67 C67 C . 0 . ? C65 C65 C . 0 . ? O64 O64 O . 0 . ? C64 C64 C . 0 . ? O68 O68 O . 0 . ? O67 O67 O . 0 . ? O69 O69 O . 0 . ? NQ NQ N . 0 . ? C70 C70 C . 0 . ? O70 O70 O . 0 . ? O66 O66 O . 0 . ? C66 C66 C . 0 . ? HA2 HA2 H . 0 . ? HA1 HA1 H . 0 . ? H2 H2 H . 0 . ? HNC HNC H . 0 . ? H3E H3E H . 0 . ? H3X H3X H . 0 . ? HB1 HB1 H . 0 . ? HB2 HB2 H . 0 . ? HD2 HD2 H . 0 . ? HD1 HD1 H . 0 . ? H5E H5E H . 0 . ? H5X H5X H . 0 . ? H6 H6 H . 0 . ? HF2 HF2 H . 0 . ? HF1 HF1 H . 0 . ? HAA HAA H . 0 . ? HAB HAB H . 0 . ? HAC HAC H . 0 . ? HNH HNH H . 0 . ? H13 H13 H . 0 . ? H14 H14 H . 0 . ? H28 H28 H . 0 . ? H29 H29 H . 0 . ? HNI HNI H . 0 . ? HNK HNK H . 0 . ? H34 H34 H . 0 . ? HO2 HO2 H . 0 . ? H31 H31 H . 0 . ? HBA HBA H . 0 . ? HBB HBB H . 0 . ? HBC HBC H . 0 . ? H33 H33 H . 0 . ? HCB HCB H . 0 . ? HCC HCC H . 0 . ? HCA HCA H . 0 . ? HNL HNL H . 0 . ? H37 H37 H . 0 . ? H38 H38 H . 0 . ? HO3 HO3 H . 0 . ? HDB HDB H . 0 . ? HDC HDC H . 0 . ? HDA HDA H . 0 . ? HNM HNM H . 0 . ? H2E H2E H . 0 . ? H2X H2X H . 0 . ? H1E H1E H . 0 . ? H1X H1X H . 0 . ? H44 H44 H . 0 . ? H47 H47 H . 0 . ? HNP HNP H . 0 . ? H501 H501 H . 0 . ? H502 H502 H . 0 . ? H511 H511 H . 0 . ? H512 H512 H . 0 . ? H521 H521 H . 0 . ? H522 H522 H . 0 . ? H53 H53 H . 0 . ? H551 H551 H . 0 . ? H552 H552 H . 0 . ? H553 H553 H . 0 . ? H541 H541 H . 0 . ? H542 H542 H . 0 . ? H543 H543 H . 0 . ? HO59 HO59 H . 0 . ? HO58 HO58 H . 0 . ? H611 H611 H . 0 . ? H612 H612 H . 0 . ? HO61 HO61 H . 0 . ? H60 H60 H . 0 . ? H63 H63 H . 0 . ? H57 H57 H . 0 . ? H58 H58 H . 0 . ? H59 H59 H . 0 . ? H69 H69 H . 0 . ? H68 H68 H . 0 . ? H67 H67 H . 0 . ? H65 H65 H . 0 . ? H64 H64 H . 0 . ? HO67 HO67 H . 0 . ? HO69 HO69 H . 0 . ? HNQ1 HNQ1 H . 0 . ? HNQ2 HNQ2 H . 0 . ? HO66 HO66 H . 0 . ? H661 H661 H . 0 . ? H662 H662 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING NA C1 ? ? SING NA HA2 ? ? SING NA HA1 ? ? SING C2 C1 ? ? SING C2 C3 ? ? SING C2 NB ? ? SING C2 H2 ? ? DOUB C1 O1 ? ? SING NC C3 ? ? SING NC C6 ? ? SING NC HNC ? ? SING C3 H3E ? ? SING C3 H3X ? ? SING NB HB1 ? ? SING NB HB2 ? ? SING ND C4 ? ? SING ND HD2 ? ? SING ND HD1 ? ? SING C5 C4 ? ? SING C5 C6 ? ? SING C5 H5E ? ? SING C5 H5X ? ? DOUB C4 O4 ? ? DOUB C8 C9 ? ? SING C8 NE ? ? SING C8 NF ? ? SING C9 C10 ? ? SING C9 CA ? ? DOUB C10 NG ? ? SING C10 C12 ? ? SING NG C7 ? ? DOUB C7 NE ? ? SING C7 C6 ? ? SING C6 H6 ? ? SING NF HF2 ? ? SING NF HF1 ? ? SING CA HAA ? ? SING CA HAB ? ? SING CA HAC ? ? DOUB C12 O12 ? ? SING C12 NH ? ? SING NH C13 ? ? SING NH HNH ? ? SING C13 C30 ? ? SING C13 C14 ? ? SING C13 H13 ? ? DOUB C30 O30 ? ? SING C30 NK ? ? SING C14 C27 ? ? SING C14 OH1 ? ? SING C14 H14 ? ? SING C27 NJ ? ? DOUB C27 C28 ? ? SING OH1 C63 ? ? DOUB NJ C29 ? ? SING C28 NI ? ? SING C28 H28 ? ? SING C29 NI ? ? SING C29 H29 ? ? SING NI HNI ? ? SING NK C31 ? ? SING NK HNK ? ? SING C34 C36 ? ? SING C34 C33 ? ? SING C34 CC ? ? SING C34 H34 ? ? DOUB C36 O36 ? ? SING C36 NL ? ? SING OH2 C33 ? ? SING OH2 HO2 ? ? SING C31 CB ? ? SING C31 C33 ? ? SING C31 H31 ? ? SING CB HBA ? ? SING CB HBB ? ? SING CB HBC ? ? SING C33 H33 ? ? SING CC HCB ? ? SING CC HCC ? ? SING CC HCA ? ? SING NL C37 ? ? SING NL HNL ? ? SING C37 C40 ? ? SING C37 C38 ? ? SING C37 H37 ? ? DOUB C40 O40 ? ? SING C40 NM ? ? SING C38 OH3 ? ? SING C38 CD ? ? SING C38 H38 ? ? SING OH3 HO3 ? ? SING CD HDB ? ? SING CD HDC ? ? SING CD HDA ? ? SING NM C41 ? ? SING NM HNM ? ? SING C42 C43 ? ? SING C42 C41 ? ? SING C42 H2E ? ? SING C42 H2X ? ? DOUB C49 O49 ? ? SING C49 C48 ? ? SING C49 NP ? ? SING C43 S43 ? ? DOUB C43 NN ? ? SING C41 H1E ? ? SING C41 H1X ? ? SING S43 C44 ? ? DOUB C44 C45 ? ? SING C44 H44 ? ? SING C45 NN ? ? SING C45 C46 ? ? DOUB C47 C48 ? ? SING C47 S46 ? ? SING C47 H47 ? ? SING C48 NO ? ? DOUB NO C46 ? ? SING C46 S46 ? ? SING NP C50 ? ? SING NP HNP ? ? SING C50 C51 ? ? SING C50 H501 ? ? SING C50 H502 ? ? SING C51 C52 ? ? SING C51 H511 ? ? SING C51 H512 ? ? SING C52 S53 ? ? SING C52 H521 ? ? SING C52 H522 ? ? SING S53 C55 ? ? SING S53 C54 ? ? SING S53 H53 ? ? SING C55 H551 ? ? SING C55 H552 ? ? SING C55 H553 ? ? SING C54 H541 ? ? SING C54 H542 ? ? SING C54 H543 ? ? SING O59 C59 ? ? SING O59 HO59 ? ? SING O58 C58 ? ? SING O58 HO58 ? ? SING C61 O61 ? ? SING C61 C60 ? ? SING C61 H611 ? ? SING C61 H612 ? ? SING O61 HO61 ? ? SING O56 C57 ? ? SING O56 C64 ? ? SING C60 O62 ? ? SING C60 C59 ? ? SING C60 H60 ? ? SING O62 C63 ? ? SING C63 C57 ? ? SING C63 H63 ? ? SING C57 C58 ? ? SING C57 H57 ? ? SING C58 C59 ? ? SING C58 H58 ? ? SING C59 H59 ? ? SING C69 C68 ? ? SING C69 C64 ? ? SING C69 O69 ? ? SING C69 H69 ? ? SING C68 C67 ? ? SING C68 O68 ? ? SING C68 H68 ? ? SING C67 C65 ? ? SING C67 O67 ? ? SING C67 H67 ? ? SING C65 O64 ? ? SING C65 C66 ? ? SING C65 H65 ? ? SING O64 C64 ? ? SING C64 H64 ? ? SING O68 C70 ? ? SING O67 HO67 ? ? SING O69 HO69 ? ? SING NQ C70 ? ? SING NQ HNQ1 ? ? SING NQ HNQ2 ? ? DOUB C70 O70 ? ? SING O66 C66 ? ? SING O66 HO66 ? ? SING C66 H661 ? ? SING C66 H662 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Sh_BRP . 2017 Bacteria . Streptoalloteichus hindustanus 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 $Sh_BRP '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 $Sh_BRP 1 mM '[U-99% 15N]' $BLM 1.1 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Sh_BRP 1 mM '[U-98% 13C; U-99% 15N]' $BLM 1.1 mM . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 97 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_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 313 1 K 'ionic strength' 0.1 . M 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . . $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $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_BRP_COMP _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'BRP monomer 1' _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 MET HA H 4.5 0.1 1 2 . 1 MET HB2 H 2.0 0.1 2 3 . 1 MET HB3 H 1.9 0.1 2 4 . 1 MET HG2 H 2.5 0.1 2 5 . 1 MET C C 175.5 0.1 1 6 . 1 MET CA C 54.1 0.1 1 7 . 1 MET CB C 33.1 0.2 1 8 . 1 MET CG C 30.8 0.2 1 9 . 2 ALA H H 8.26 0.05 1 10 . 2 ALA HA H 4.9 0.1 1 11 . 2 ALA HB H 1.2 0.1 1 12 . 2 ALA C C 177.3 0.1 1 13 . 2 ALA CA C 50.8 0.1 1 14 . 2 ALA CB C 20.3 0.2 1 15 . 2 ALA N N 124.5 0.1 1 16 . 3 LYS H H 8.72 0.05 1 17 . 3 LYS HA H 4.8 0.1 1 18 . 3 LYS HB2 H 1.7 0.1 2 19 . 3 LYS HG2 H 1.3 0.1 2 20 . 3 LYS HG3 H 1.1 0.1 2 21 . 3 LYS HD2 H 1.6 0.1 2 22 . 3 LYS HE2 H 2.9 0.1 2 23 . 3 LYS CA C 54.1 0.1 1 24 . 3 LYS CB C 35.8 0.2 1 25 . 3 LYS CG C 24.5 0.2 1 26 . 3 LYS CD C 28.6 0.2 1 27 . 3 LYS CE C 41.4 0.2 1 28 . 3 LYS N N 120.7 0.1 1 29 . 4 LEU HA H 5.0 0.1 1 30 . 4 LEU HB2 H 1.7 0.1 2 31 . 4 LEU HG H 1.1 0.1 2 32 . 4 LEU HD1 H 2.0 0.1 2 33 . 4 LEU HD2 H 1.9 0.1 2 34 . 4 LEU C C 177.4 0.1 1 35 . 4 LEU CA C 55.5 0.1 1 36 . 4 LEU CB C 39.8 0.2 1 37 . 4 LEU CG C 25.9 0.2 1 38 . 4 LEU CD1 C 29.0 0.2 1 39 . 4 LEU CD2 C 29.0 0.2 1 40 . 5 THR H H 9.00 0.05 1 41 . 5 THR HA H 4.6 0.1 1 42 . 5 THR HB H 4.3 0.1 2 43 . 5 THR HG2 H 1.2 0.1 1 44 . 5 THR C C 175.7 0.1 1 45 . 5 THR CA C 62.7 0.1 1 46 . 5 THR CB C 68.3 0.2 1 47 . 5 THR CG2 C 22.1 0.2 1 48 . 5 THR N N 115.3 0.1 1 49 . 6 SER H H 7.61 0.05 1 50 . 6 SER HA H 4.7 0.1 1 51 . 6 SER HB2 H 3.9 0.1 2 52 . 6 SER C C 172.0 0.1 1 53 . 6 SER CA C 58.0 0.1 1 54 . 6 SER CB C 63.7 0.2 1 55 . 6 SER N N 114.2 0.1 1 56 . 7 ALA H H 8.65 0.05 1 57 . 7 ALA HA H 5.8 0.1 1 58 . 7 ALA HB H 1.6 0.1 1 59 . 7 ALA C C 175.8 0.1 1 60 . 7 ALA CA C 50.3 0.1 1 61 . 7 ALA CB C 23.2 0.2 1 62 . 7 ALA N N 123.1 0.1 1 63 . 8 VAL H H 9.61 0.05 1 64 . 8 VAL HA H 4.5 0.1 1 65 . 8 VAL HB H 1.8 0.1 2 66 . 8 VAL HG1 H 0.6 0.1 2 67 . 8 VAL HG2 H -0.2 0.1 2 68 . 8 VAL CA C 59.0 0.1 1 69 . 8 VAL CB C 35.2 0.2 1 70 . 8 VAL CG1 C 21.5 0.2 1 71 . 8 VAL CG2 C 18.5 0.2 1 72 . 8 VAL N N 121.7 0.1 1 73 . 9 PRO HA H 4.8 0.1 1 74 . 9 PRO HB2 H 2.9 0.1 2 75 . 9 PRO HB3 H 1.7 0.1 2 76 . 9 PRO HG2 H 1.6 0.1 2 77 . 9 PRO HD2 H 4.1 0.1 2 78 . 9 PRO HD3 H 3.8 0.1 2 79 . 9 PRO C C 174.5 0.1 1 80 . 9 PRO CA C 60.7 0.1 1 81 . 9 PRO CB C 32.6 0.2 1 82 . 9 PRO CG C 26.9 0.2 1 83 . 9 PRO CD C 51.0 0.2 1 84 . 10 VAL H H 8.90 0.05 1 85 . 10 VAL HA H 4.5 0.1 1 86 . 10 VAL HB H 2.4 0.1 2 87 . 10 VAL HG1 H 1.4 0.1 2 88 . 10 VAL HG2 H 1.0 0.1 2 89 . 10 VAL C C 176.3 0.1 1 90 . 10 VAL CA C 59.6 0.1 1 91 . 10 VAL CB C 30.6 0.2 1 92 . 10 VAL CG1 C 21.6 0.2 1 93 . 10 VAL CG2 C 21.6 0.2 1 94 . 10 VAL N N 122.1 0.1 1 95 . 11 LEU H H 8.86 0.05 1 96 . 11 LEU HA H 4.3 0.1 1 97 . 11 LEU HB2 H 1.5 0.1 2 98 . 11 LEU HG H 1.4 0.1 2 99 . 11 LEU HD1 H 0.5 0.1 2 100 . 11 LEU HD2 H 0.2 0.1 2 101 . 11 LEU C C 176.5 0.1 1 102 . 11 LEU CA C 53.3 0.1 1 103 . 11 LEU CB C 40.1 0.2 1 104 . 11 LEU CG C 26.6 0.2 1 105 . 11 LEU CD1 C 20.7 0.2 1 106 . 11 LEU CD2 C 24.0 0.2 1 107 . 11 LEU N N 126.3 0.1 1 108 . 12 THR H H 9.06 0.05 1 109 . 12 THR HA H 5.5 0.1 1 110 . 12 THR HB H 4.0 0.1 2 111 . 12 THR HG2 H 1.2 0.1 1 112 . 12 THR C C 175.6 0.1 1 113 . 12 THR CA C 58.9 0.1 1 114 . 12 THR CB C 71.5 0.2 1 115 . 12 THR CG2 C 22.3 0.2 1 116 . 12 THR N N 108.3 0.1 1 117 . 13 ALA H H 8.22 0.05 1 118 . 13 ALA HA H 4.4 0.1 1 119 . 13 ALA HB H 0.9 0.1 1 120 . 13 ALA C C 176.6 0.1 1 121 . 13 ALA CA C 51.4 0.1 1 122 . 13 ALA CB C 21.5 0.2 1 123 . 13 ALA N N 116.9 0.1 1 124 . 14 ARG H H 8.04 0.05 1 125 . 14 ARG HA H 4.8 0.1 1 126 . 14 ARG HB2 H 1.9 0.1 2 127 . 14 ARG HG2 H 1.5 0.1 2 128 . 14 ARG HD2 H 3.2 0.1 1 129 . 14 ARG HD3 H 3.2 0.1 1 130 . 14 ARG C C 177.4 0.1 1 131 . 14 ARG CA C 57.2 0.1 1 132 . 14 ARG CB C 28.9 0.2 1 133 . 14 ARG CG C 27.8 0.2 1 134 . 14 ARG CD C 42.7 0.2 1 135 . 14 ARG N N 119.9 0.1 1 136 . 15 ASP H H 8.02 0.05 1 137 . 15 ASP HA H 4.9 0.1 1 138 . 15 ASP HB2 H 2.8 0.1 2 139 . 15 ASP HB3 H 2.5 0.1 2 140 . 15 ASP C C 176.4 0.1 1 141 . 15 ASP CA C 50.9 0.1 1 142 . 15 ASP CB C 39.8 0.2 1 143 . 15 ASP N N 118.7 0.1 1 144 . 16 VAL H H 8.77 0.05 1 145 . 16 VAL HA H 3.1 0.1 1 146 . 16 VAL HB H 2.0 0.1 2 147 . 16 VAL HG1 H 0.8 0.1 2 148 . 16 VAL HG2 H 0.5 0.1 2 149 . 16 VAL C C 177.1 0.1 1 150 . 16 VAL CA C 66.3 0.1 1 151 . 16 VAL CB C 30.9 0.2 1 152 . 16 VAL CG1 C 22.7 0.2 1 153 . 16 VAL CG2 C 20.0 0.2 1 154 . 16 VAL N N 127.2 0.1 1 155 . 17 ALA H H 8.13 0.05 1 156 . 17 ALA HA H 3.8 0.1 1 157 . 17 ALA HB H 1.4 0.1 1 158 . 17 ALA C C 181.3 0.1 1 159 . 17 ALA CA C 55.0 0.1 1 160 . 17 ALA CB C 17.0 0.2 1 161 . 17 ALA N N 122.7 0.1 1 162 . 18 GLY H H 8.36 0.05 1 163 . 18 GLY HA2 H 3.9 0.1 1 164 . 18 GLY HA3 H 3.7 0.1 1 165 . 18 GLY C C 176.9 0.1 1 166 . 18 GLY CA C 46.2 0.1 1 167 . 18 GLY N N 106.4 0.1 1 168 . 19 ALA H H 7.57 0.05 1 169 . 19 ALA HA H 4.2 0.1 1 170 . 19 ALA HB H 1.5 0.1 1 171 . 19 ALA C C 179.5 0.1 1 172 . 19 ALA CA C 54.8 0.1 1 173 . 19 ALA CB C 17.0 0.2 1 174 . 19 ALA N N 126.2 0.1 1 175 . 20 VAL H H 8.69 0.05 1 176 . 20 VAL HA H 3.2 0.1 1 177 . 20 VAL HB H 2.0 0.1 2 178 . 20 VAL HG1 H 0.8 0.1 2 179 . 20 VAL HG2 H 0.5 0.1 2 180 . 20 VAL C C 179.4 0.1 1 181 . 20 VAL CA C 66.4 0.1 1 182 . 20 VAL CB C 30.5 0.2 1 183 . 20 VAL CG1 C 23.9 0.2 1 184 . 20 VAL CG2 C 20.5 0.2 1 185 . 20 VAL N N 119.0 0.1 1 186 . 21 GLU H H 8.15 0.05 1 187 . 21 GLU HA H 3.8 0.1 1 188 . 21 GLU HB2 H 2.1 0.1 2 189 . 21 GLU HG2 H 2.4 0.1 2 190 . 21 GLU HG3 H 2.2 0.1 2 191 . 21 GLU C C 177.0 0.1 1 192 . 21 GLU CA C 59.0 0.1 1 193 . 21 GLU CB C 28.5 0.2 1 194 . 21 GLU CG C 35.2 0.2 1 195 . 21 GLU N N 121.3 0.1 1 196 . 22 PHE H H 7.44 0.05 1 197 . 22 PHE HA H 4.1 0.1 1 198 . 22 PHE HB2 H 3.1 0.1 2 199 . 22 PHE HB3 H 3.0 0.1 2 200 . 22 PHE C C 176.9 0.1 1 201 . 22 PHE CA C 60.8 0.1 1 202 . 22 PHE CB C 38.4 0.2 1 203 . 22 PHE N N 118.0 0.1 1 204 . 23 TRP H H 8.24 0.05 1 205 . 23 TRP HA H 3.3 0.1 1 206 . 23 TRP HB2 H 2.8 0.1 2 207 . 23 TRP HB3 H 2.7 0.1 2 208 . 23 TRP C C 176.4 0.1 1 209 . 23 TRP CA C 61.3 0.1 1 210 . 23 TRP CB C 27.7 0.2 1 211 . 23 TRP N N 119.0 0.1 1 212 . 24 THR H H 7.95 0.05 1 213 . 24 THR HA H 5.0 0.1 1 214 . 24 THR HB H 4.1 0.1 2 215 . 24 THR HG2 H 1.0 0.1 1 216 . 24 THR C C 176.0 0.1 1 217 . 24 THR CA C 60.1 0.1 1 218 . 24 THR CB C 68.2 0.2 1 219 . 24 THR CG2 C 21.2 0.2 1 220 . 24 THR N N 106.4 0.1 1 221 . 25 ASP H H 8.48 0.05 1 222 . 25 ASP HA H 4.4 0.1 1 223 . 25 ASP HB2 H 2.9 0.1 2 224 . 25 ASP HB3 H 2.6 0.1 2 225 . 25 ASP C C 177.7 0.1 1 226 . 25 ASP CA C 56.3 0.1 1 227 . 25 ASP CB C 39.8 0.2 1 228 . 25 ASP N N 124.0 0.1 1 229 . 26 ARG H H 7.30 0.05 1 230 . 26 ARG HA H 4.4 0.1 1 231 . 26 ARG HB2 H 1.1 0.1 2 232 . 26 ARG HG2 H 1.5 0.1 2 233 . 26 ARG HG3 H 1.4 0.1 2 234 . 26 ARG HD2 H 3.0 0.1 2 235 . 26 ARG HD3 H 3.1 0.1 2 236 . 26 ARG C C 177.4 0.1 1 237 . 26 ARG CA C 56.2 0.1 1 238 . 26 ARG CB C 28.2 0.2 1 239 . 26 ARG CG C 25.9 0.2 1 240 . 26 ARG CD C 42.0 0.2 1 241 . 26 ARG N N 114.2 0.1 1 242 . 27 LEU H H 6.53 0.05 1 243 . 27 LEU HA H 3.9 0.1 1 244 . 27 LEU HB2 H 1.8 0.1 2 245 . 27 LEU HB3 H 1.2 0.1 2 246 . 27 LEU HG H -0.3 0.1 2 247 . 27 LEU HD1 H -1.0 0.1 2 248 . 27 LEU HD2 H -1.4 0.1 2 249 . 27 LEU C C 178.9 0.1 1 250 . 27 LEU CA C 54.4 0.1 1 251 . 27 LEU CB C 38.4 0.2 1 252 . 27 LEU CG C 24.2 0.2 1 253 . 27 LEU CD1 C 24.8 0.2 1 254 . 27 LEU CD2 C 18.1 0.2 1 255 . 27 LEU N N 112.4 0.1 1 256 . 28 GLY H H 7.52 0.05 1 257 . 28 GLY HA2 H 4.2 0.1 1 258 . 28 GLY HA3 H 4.0 0.1 1 259 . 28 GLY C C 176.9 0.1 1 260 . 28 GLY CA C 46.2 0.1 1 261 . 28 GLY N N 105.6 0.1 1 262 . 29 PHE H H 8.93 0.05 1 263 . 29 PHE HA H 4.6 0.1 1 264 . 29 PHE HB2 H 2.8 0.1 2 265 . 29 PHE HB3 H 3.2 0.1 2 266 . 29 PHE C C 175.3 0.1 1 267 . 29 PHE CA C 57.3 0.1 1 268 . 29 PHE CB C 37.7 0.2 1 269 . 29 PHE N N 121.1 0.1 1 270 . 30 SER H H 9.89 0.05 1 271 . 30 SER HA H 4.8 0.1 1 272 . 30 SER HB2 H 3.8 0.1 2 273 . 30 SER HB3 H 3.9 0.1 2 274 . 30 SER C C 175.2 0.1 1 275 . 30 SER CA C 56.7 0.1 1 276 . 30 SER CB C 63.7 0.2 1 277 . 30 SER N N 115.3 0.1 1 278 . 31 ARG H H 8.90 0.05 1 279 . 31 ARG HA H 4.0 0.1 1 280 . 31 ARG HB2 H 1.6 0.1 2 281 . 31 ARG HG2 H 1.7 0.1 2 282 . 31 ARG HG3 H 1.2 0.1 2 283 . 31 ARG HD2 H 3.1 0.1 2 284 . 31 ARG C C 175.0 0.1 1 285 . 31 ARG CA C 56.3 0.1 1 286 . 31 ARG CB C 29.5 0.2 1 287 . 31 ARG CG C 27.7 0.2 1 288 . 31 ARG CD C 42.7 0.2 1 289 . 31 ARG N N 123.4 0.1 1 290 . 32 ASP H H 8.64 0.05 1 291 . 32 ASP HA H 3.9 0.1 1 292 . 32 ASP HB2 H 2.3 0.1 2 293 . 32 ASP HB3 H 2.5 0.1 2 294 . 32 ASP C C 176.2 0.1 1 295 . 32 ASP CA C 55.4 0.1 1 296 . 32 ASP CB C 42.2 0.2 1 297 . 32 ASP N N 129.8 0.1 1 298 . 33 PHE H H 7.18 0.05 1 299 . 33 PHE HA H 4.7 0.1 1 300 . 33 PHE HB2 H 3.1 0.1 2 301 . 33 PHE HB3 H 2.9 0.1 2 302 . 33 PHE C C 172.9 0.1 1 303 . 33 PHE CA C 55.9 0.1 1 304 . 33 PHE CB C 39.3 0.2 1 305 . 33 PHE N N 110.9 0.1 1 306 . 34 VAL H H 8.58 0.05 1 307 . 34 VAL HA H 4.2 0.1 1 308 . 34 VAL HB H 2.0 0.1 2 309 . 34 VAL HG1 H 0.9 0.1 2 310 . 34 VAL HG2 H 0.8 0.1 2 311 . 34 VAL C C 174.4 0.1 1 312 . 34 VAL CA C 62.3 0.1 1 313 . 34 VAL CB C 34.5 0.2 1 314 . 34 VAL CG1 C 20.6 0.2 1 315 . 34 VAL CG2 C 20.6 0.2 1 316 . 34 VAL N N 119.7 0.1 1 317 . 35 GLU H H 8.84 0.05 1 318 . 35 GLU HA H 4.9 0.1 1 319 . 35 GLU HB2 H 2.5 0.1 2 320 . 35 GLU HB3 H 2.3 0.1 2 321 . 35 GLU HG2 H 2.6 0.1 2 322 . 35 GLU HG3 H 2.5 0.1 2 323 . 35 GLU C C 176.2 0.1 1 324 . 35 GLU CA C 53.5 0.1 1 325 . 35 GLU CB C 30.9 0.2 1 326 . 35 GLU CG C 35.1 0.2 1 327 . 35 GLU N N 127.7 0.1 1 328 . 36 ASP H H 8.69 0.05 1 329 . 36 ASP HA H 4.3 0.1 1 330 . 36 ASP HB2 H 2.7 0.1 2 331 . 36 ASP C C 177.1 0.1 1 332 . 36 ASP CA C 56.9 0.1 1 333 . 36 ASP CB C 39.6 0.2 1 334 . 36 ASP N N 119.0 0.1 1 335 . 37 ASP H H 8.31 0.05 1 336 . 37 ASP HA H 4.7 0.1 1 337 . 37 ASP HB2 H 3.0 0.1 2 338 . 37 ASP HB3 H 2.9 0.1 2 339 . 37 ASP C C 174.9 0.1 1 340 . 37 ASP CA C 52.1 0.1 1 341 . 37 ASP CB C 40.6 0.2 1 342 . 37 ASP N N 113.5 0.1 1 343 . 38 PHE H H 7.31 0.05 1 344 . 38 PHE HA H 5.2 0.1 1 345 . 38 PHE HB2 H 3.0 0.1 2 346 . 38 PHE HB3 H 2.7 0.1 2 347 . 38 PHE C C 172.7 0.1 1 348 . 38 PHE CA C 56.9 0.1 1 349 . 38 PHE CB C 42.7 0.2 1 350 . 38 PHE N N 122.3 0.1 1 351 . 39 ALA H H 8.15 0.05 1 352 . 39 ALA HA H 4.1 0.1 1 353 . 39 ALA HB H 1.0 0.1 1 354 . 39 ALA C C 173.6 0.1 1 355 . 39 ALA CA C 49.7 0.1 1 356 . 39 ALA CB C 24.2 0.2 1 357 . 39 ALA N N 126.7 0.1 1 358 . 40 GLY H H 7.25 0.05 1 359 . 40 GLY HA2 H 4.9 0.1 1 360 . 40 GLY HA3 H 2.8 0.1 1 361 . 40 GLY C C 172.6 0.1 1 362 . 40 GLY CA C 44.5 0.1 1 363 . 40 GLY N N 103.7 0.1 1 364 . 41 VAL H H 9.06 0.05 1 365 . 41 VAL HA H 5.3 0.1 1 366 . 41 VAL HB H 2.1 0.1 2 367 . 41 VAL HG1 H 0.6 0.1 2 368 . 41 VAL HG2 H 0.4 0.1 2 369 . 41 VAL C C 174.0 0.1 1 370 . 41 VAL CA C 57.7 0.1 1 371 . 41 VAL CB C 33.9 0.2 1 372 . 41 VAL CG1 C 21.5 0.2 1 373 . 41 VAL CG2 C 17.2 0.2 1 374 . 41 VAL N N 117.1 0.1 1 375 . 42 VAL H H 8.98 0.05 1 376 . 42 VAL HA H 5.5 0.1 1 377 . 42 VAL HB H 1.9 0.1 2 378 . 42 VAL HG1 H 0.8 0.1 1 379 . 42 VAL HG2 H 0.8 0.1 1 380 . 42 VAL C C 175.1 0.1 1 381 . 42 VAL CA C 59.0 0.1 1 382 . 42 VAL CB C 35.4 0.2 1 383 . 42 VAL CG1 C 20.4 0.2 1 384 . 42 VAL CG2 C 20.4 0.2 1 385 . 42 VAL N N 119.5 0.1 1 386 . 43 ARG H H 8.74 0.05 1 387 . 43 ARG HA H 4.2 0.1 1 388 . 43 ARG HB2 H 0.6 0.1 2 389 . 43 ARG HB3 H 0.5 0.1 2 390 . 43 ARG HG2 H 1.5 0.1 2 391 . 43 ARG HD2 H 2.7 0.1 2 392 . 43 ARG HD3 H 2.4 0.1 2 393 . 43 ARG C C 174.0 0.1 1 394 . 43 ARG CA C 56.3 0.1 1 395 . 43 ARG CB C 29.3 0.2 1 396 . 43 ARG CG C 25.4 0.2 1 397 . 43 ARG CD C 42.2 0.2 1 398 . 43 ARG N N 127.2 0.1 1 399 . 44 ASP H H 9.01 0.05 1 400 . 44 ASP HA H 4.1 0.1 1 401 . 44 ASP HB2 H 2.7 0.1 2 402 . 44 ASP C C 175.7 0.1 1 403 . 44 ASP CA C 55.3 0.1 1 404 . 44 ASP CB C 40.4 0.2 1 405 . 44 ASP N N 124.9 0.1 1 406 . 45 ASP H H 7.57 0.05 1 407 . 45 ASP HA H 4.9 0.1 1 408 . 45 ASP HB2 H 3.1 0.1 2 409 . 45 ASP HB3 H 2.7 0.1 2 410 . 45 ASP C C 175.4 0.1 1 411 . 45 ASP CA C 54.2 0.1 1 412 . 45 ASP CB C 40.6 0.2 1 413 . 45 ASP N N 121.6 0.1 1 414 . 46 VAL H H 8.29 0.05 1 415 . 46 VAL HA H 4.2 0.1 1 416 . 46 VAL HB H 2.2 0.1 2 417 . 46 VAL HG1 H 1.0 0.1 1 418 . 46 VAL HG2 H 1.0 0.1 1 419 . 46 VAL C C 173.2 0.1 1 420 . 46 VAL CA C 62.4 0.1 1 421 . 46 VAL CB C 33.2 0.2 1 422 . 46 VAL CG1 C 22.6 0.2 1 423 . 46 VAL CG2 C 19.7 0.2 1 424 . 46 VAL N N 122.4 0.1 1 425 . 47 THR H H 7.83 0.05 1 426 . 47 THR HA H 5.0 0.1 1 427 . 47 THR HB H 3.6 0.1 2 428 . 47 THR HG2 H 0.9 0.1 1 429 . 47 THR C C 173.0 0.1 1 430 . 47 THR CA C 60.5 0.1 1 431 . 47 THR CB C 69.3 0.2 1 432 . 47 THR CG2 C 20.6 0.2 1 433 . 47 THR N N 124.8 0.1 1 434 . 48 LEU H H 8.81 0.05 1 435 . 48 LEU HA H 4.5 0.1 1 436 . 48 LEU HB2 H 0.9 0.1 2 437 . 48 LEU HB3 H 0.6 0.1 2 438 . 48 LEU HG H 1.2 0.1 2 439 . 48 LEU HD1 H 0.4 0.1 2 440 . 48 LEU HD2 H -0.2 0.1 2 441 . 48 LEU C C 175.6 0.1 1 442 . 48 LEU CA C 52.8 0.1 1 443 . 48 LEU CB C 42.7 0.2 1 444 . 48 LEU CG C 25.4 0.2 1 445 . 48 LEU CD1 C 21.8 0.2 1 446 . 48 LEU CD2 C 24.7 0.2 1 447 . 48 LEU N N 123.3 0.1 1 448 . 49 PHE H H 8.21 0.05 1 449 . 49 PHE HA H 5.6 0.1 1 450 . 49 PHE HB2 H 3.0 0.1 2 451 . 49 PHE C C 174.9 0.1 1 452 . 49 PHE CA C 50.4 0.1 1 453 . 49 PHE CB C 38.8 0.2 1 454 . 49 PHE N N 121.3 0.1 1 455 . 50 ILE H H 8.02 0.05 1 456 . 50 ILE HA H 4.3 0.1 1 457 . 50 ILE HB H 1.0 0.1 2 458 . 50 ILE HG12 H 0.5 0.1 2 459 . 50 ILE HG2 H 0.4 0.1 1 460 . 50 ILE HD1 H 0.3 0.1 1 461 . 50 ILE C C 173.6 0.1 1 462 . 50 ILE CA C 59.2 0.1 1 463 . 50 ILE CB C 40.6 0.2 1 464 . 50 ILE CG1 C 26.2 0.2 1 465 . 50 ILE CG2 C 17.3 0.2 1 466 . 50 ILE CD1 C 13.0 0.2 1 467 . 50 ILE N N 118.7 0.1 1 468 . 51 SER H H 8.79 0.05 1 469 . 51 SER HA H 4.8 0.1 1 470 . 51 SER HB2 H 3.9 0.1 2 471 . 51 SER HB3 H 3.7 0.1 2 472 . 51 SER C C 173.5 0.1 1 473 . 51 SER CA C 54.6 0.1 1 474 . 51 SER CB C 65.7 0.2 1 475 . 51 SER N N 119.4 0.1 1 476 . 52 ALA H H 7.60 0.05 1 477 . 52 ALA HA H 5.2 0.1 1 478 . 52 ALA HB H 1.6 0.1 1 479 . 52 ALA C C 178.8 0.1 1 480 . 52 ALA CA C 51.0 0.1 1 481 . 52 ALA CB C 19.3 0.2 1 482 . 52 ALA N N 125.8 0.1 1 483 . 53 VAL H H 7.81 0.05 1 484 . 53 VAL HA H 4.7 0.1 1 485 . 53 VAL HB H 2.3 0.1 2 486 . 53 VAL HG1 H 0.7 0.1 2 487 . 53 VAL HG2 H 1.1 0.1 2 488 . 53 VAL C C 175.4 0.1 1 489 . 53 VAL CA C 58.3 0.1 1 490 . 53 VAL CB C 35.2 0.2 1 491 . 53 VAL CG1 C 17.6 0.2 1 492 . 53 VAL CG2 C 22.0 0.2 1 493 . 53 VAL N N 112.7 0.1 1 494 . 54 GLN H H 8.35 0.05 1 495 . 54 GLN HA H 4.6 0.1 1 496 . 54 GLN HB2 H 1.9 0.1 2 497 . 54 GLN HG2 H 2.4 0.1 2 498 . 54 GLN C C 175.7 0.1 1 499 . 54 GLN CA C 55.4 0.1 1 500 . 54 GLN CB C 29.2 0.2 1 501 . 54 GLN CG C 33.2 0.2 1 502 . 54 GLN N N 116.8 0.1 1 503 . 55 ASP H H 7.16 0.05 1 504 . 55 ASP HA H 4.9 0.1 1 505 . 55 ASP HB2 H 2.7 0.1 2 506 . 55 ASP HB3 H 2.4 0.1 2 507 . 55 ASP C C 176.0 0.1 1 508 . 55 ASP CA C 52.6 0.1 1 509 . 55 ASP CB C 43.1 0.2 1 510 . 55 ASP N N 118.6 0.1 1 511 . 56 GLN H H 8.82 0.05 1 512 . 56 GLN HA H 3.6 0.1 1 513 . 56 GLN HB2 H 2.1 0.1 2 514 . 56 GLN HB3 H 1.9 0.1 2 515 . 56 GLN HG2 H 2.6 0.1 2 516 . 56 GLN HG3 H 2.4 0.1 2 517 . 56 GLN C C 174.1 0.1 1 518 . 56 GLN CA C 55.8 0.1 1 519 . 56 GLN CB C 27.6 0.2 1 520 . 56 GLN CG C 32.1 0.2 1 521 . 56 GLN N N 127.5 0.1 1 522 . 57 VAL H H 8.29 0.05 1 523 . 57 VAL HA H 3.9 0.1 1 524 . 57 VAL HB H 1.9 0.1 2 525 . 57 VAL HG1 H 0.9 0.1 2 526 . 57 VAL HG2 H 0.7 0.1 2 527 . 57 VAL C C 176.1 0.1 1 528 . 57 VAL CA C 63.8 0.1 1 529 . 57 VAL CB C 30.6 0.2 1 530 . 57 VAL CG1 C 21.7 0.2 1 531 . 57 VAL CG2 C 20.4 0.2 1 532 . 57 VAL N N 116.8 0.1 1 533 . 58 VAL H H 7.59 0.05 1 534 . 58 VAL HA H 4.0 0.1 1 535 . 58 VAL HB H 2.4 0.1 2 536 . 58 VAL HG1 H 1.1 0.1 2 537 . 58 VAL HG2 H 1.0 0.1 2 538 . 58 VAL CA C 67.4 0.1 1 539 . 58 VAL CB C 28.1 0.2 1 540 . 58 VAL CG1 C 21.5 0.2 1 541 . 58 VAL CG2 C 22.4 0.2 1 542 . 58 VAL N N 116.4 0.1 1 543 . 59 PRO HA H 4.2 0.1 1 544 . 59 PRO HB2 H 2.2 0.1 2 545 . 59 PRO HB3 H 1.7 0.1 2 546 . 59 PRO HG2 H 2.4 0.1 2 547 . 59 PRO HG3 H 1.8 0.1 2 548 . 59 PRO HD2 H 4.0 0.1 2 549 . 59 PRO HD3 H 3.4 0.1 2 550 . 59 PRO C C 174.7 0.1 1 551 . 59 PRO CA C 65.6 0.1 1 552 . 59 PRO CB C 26.3 0.2 1 553 . 59 PRO CG C 28.5 0.2 1 554 . 59 PRO CD C 49.2 0.2 1 555 . 60 ASP H H 7.01 0.05 1 556 . 60 ASP HA H 4.5 0.1 1 557 . 60 ASP HB2 H 2.9 0.1 2 558 . 60 ASP HB3 H 2.6 0.1 2 559 . 60 ASP C C 176.1 0.1 1 560 . 60 ASP CA C 54.7 0.1 1 561 . 60 ASP CB C 39.8 0.2 1 562 . 60 ASP N N 111.7 0.1 1 563 . 61 ASN H H 8.07 0.05 1 564 . 61 ASN HA H 5.5 0.1 1 565 . 61 ASN HB2 H 3.2 0.1 2 566 . 61 ASN HB3 H 2.7 0.1 2 567 . 61 ASN C C 173.8 0.1 1 568 . 61 ASN CA C 52.7 0.1 1 569 . 61 ASN CB C 43.2 0.2 1 570 . 61 ASN N N 116.6 0.1 1 571 . 62 THR H H 8.09 0.05 1 572 . 62 THR HA H 4.5 0.1 1 573 . 62 THR HB H 5.0 0.1 2 574 . 62 THR HG2 H 1.6 0.1 1 575 . 62 THR C C 172.6 0.1 1 576 . 62 THR CA C 64.1 0.1 1 577 . 62 THR CB C 68.6 0.2 1 578 . 62 THR CG2 C 21.3 0.2 1 579 . 62 THR N N 119.8 0.1 1 580 . 63 LEU H H 8.49 0.05 1 581 . 63 LEU HA H 5.9 0.1 1 582 . 63 LEU HB2 H 2.0 0.1 2 583 . 63 LEU HB3 H 1.7 0.1 2 584 . 63 LEU HG H 1.9 0.1 2 585 . 63 LEU HD1 H 1.3 0.1 2 586 . 63 LEU HD2 H 1.0 0.1 2 587 . 63 LEU C C 175.7 0.1 1 588 . 63 LEU CA C 51.8 0.1 1 589 . 63 LEU CB C 48.2 0.2 1 590 . 63 LEU CG C 26.5 0.2 1 591 . 63 LEU CD1 C 26.0 0.2 1 592 . 63 LEU CD2 C 26.0 0.2 1 593 . 63 LEU N N 126.0 0.1 1 594 . 64 ALA H H 7.59 0.05 1 595 . 64 ALA HA H 4.7 0.1 1 596 . 64 ALA HB H 1.3 0.1 1 597 . 64 ALA C C 174.5 0.1 1 598 . 64 ALA CA C 51.8 0.1 1 599 . 64 ALA CB C 21.7 0.2 1 600 . 64 ALA N N 114.1 0.1 1 601 . 65 TRP H H 8.31 0.05 1 602 . 65 TRP HA H 5.3 0.1 1 603 . 65 TRP HB2 H 3.1 0.1 1 604 . 65 TRP HB3 H 3.1 0.1 1 605 . 65 TRP C C 174.9 0.1 1 606 . 65 TRP CA C 57.1 0.1 1 607 . 65 TRP CB C 34.6 0.2 1 608 . 65 TRP N N 124.1 0.1 1 609 . 66 VAL H H 9.05 0.05 1 610 . 66 VAL HA H 4.9 0.1 1 611 . 66 VAL HB H 1.5 0.1 2 612 . 66 VAL HG1 H 1.3 0.1 2 613 . 66 VAL HG2 H 0.7 0.1 2 614 . 66 VAL C C 174.2 0.1 1 615 . 66 VAL CA C 60.3 0.1 1 616 . 66 VAL CB C 35.1 0.2 1 617 . 66 VAL CG1 C 22.0 0.2 1 618 . 66 VAL CG2 C 20.5 0.2 1 619 . 66 VAL N N 122.5 0.1 1 620 . 67 TRP H H 9.31 0.05 1 621 . 67 TRP HA H 5.5 0.1 1 622 . 67 TRP HB2 H 3.3 0.1 2 623 . 67 TRP HB3 H 3.2 0.1 2 624 . 67 TRP C C 176.9 0.1 1 625 . 67 TRP CA C 57.7 0.1 1 626 . 67 TRP CB C 31.8 0.2 1 627 . 67 TRP N N 129.8 0.1 1 628 . 68 VAL H H 9.14 0.05 1 629 . 68 VAL HA H 5.1 0.1 1 630 . 68 VAL HB H 2.0 0.1 2 631 . 68 VAL HG1 H 1.0 0.1 2 632 . 68 VAL HG2 H 0.8 0.1 2 633 . 68 VAL C C 176.3 0.1 1 634 . 68 VAL CA C 59.7 0.1 1 635 . 68 VAL CB C 35.9 0.2 1 636 . 68 VAL CG1 C 22.1 0.2 1 637 . 68 VAL CG2 C 20.6 0.2 1 638 . 68 VAL N N 117.9 0.1 1 639 . 69 ARG H H 9.52 0.05 1 640 . 69 ARG HA H 4.9 0.1 1 641 . 69 ARG HB2 H 2.0 0.1 2 642 . 69 ARG HB3 H 1.8 0.1 2 643 . 69 ARG HG2 H 1.7 0.1 2 644 . 69 ARG HD2 H 3.3 0.1 2 645 . 69 ARG HD3 H 3.2 0.1 2 646 . 69 ARG C C 175.8 0.1 1 647 . 69 ARG CA C 54.8 0.1 1 648 . 69 ARG CB C 29.9 0.2 1 649 . 69 ARG CG C 26.6 0.2 1 650 . 69 ARG CD C 42.7 0.2 1 651 . 69 ARG N N 129.2 0.1 1 652 . 70 GLY H H 8.95 0.05 1 653 . 70 GLY HA2 H 4.3 0.1 1 654 . 70 GLY HA3 H 4.0 0.1 1 655 . 70 GLY C C 175.2 0.1 1 656 . 70 GLY CA C 46.3 0.1 1 657 . 70 GLY N N 116.8 0.1 1 658 . 71 LEU H H 8.43 0.05 1 659 . 71 LEU HA H 3.7 0.1 1 660 . 71 LEU HB2 H 1.8 0.1 2 661 . 71 LEU HB3 H 1.5 0.1 2 662 . 71 LEU HG H 1.9 0.1 2 663 . 71 LEU HD1 H 0.9 0.1 1 664 . 71 LEU HD2 H 0.9 0.1 1 665 . 71 LEU C C 178.4 0.1 1 666 . 71 LEU CA C 58.0 0.1 1 667 . 71 LEU CB C 42.8 0.2 1 668 . 71 LEU CG C 25.6 0.2 1 669 . 71 LEU CD1 C 25.5 0.2 1 670 . 71 LEU CD2 C 24.0 0.2 1 671 . 71 LEU N N 123.0 0.1 1 672 . 72 ASP H H 8.34 0.05 1 673 . 72 ASP HA H 4.1 0.1 1 674 . 72 ASP HB2 H 2.5 0.1 2 675 . 72 ASP HB3 H 2.4 0.1 2 676 . 72 ASP CA C 56.9 0.1 1 677 . 72 ASP CB C 39.4 0.2 1 678 . 72 ASP N N 114.3 0.1 1 679 . 73 GLU H H 7.85 0.05 1 680 . 73 GLU HA H 4.0 0.1 1 681 . 73 GLU HB2 H 2.1 0.1 2 682 . 73 GLU HB3 H 2.0 0.1 2 683 . 73 GLU HG2 H 2.2 0.1 1 684 . 73 GLU HG3 H 2.2 0.1 1 685 . 73 GLU C C 179.3 0.1 1 686 . 73 GLU CA C 58.6 0.1 1 687 . 73 GLU CB C 28.5 0.2 1 688 . 73 GLU CG C 36.3 0.2 1 689 . 73 GLU N N 120.7 0.1 1 690 . 74 LEU H H 7.63 0.05 1 691 . 74 LEU HA H 3.7 0.1 1 692 . 74 LEU HB2 H 1.7 0.1 2 693 . 74 LEU HG H 0.1 0.1 2 694 . 74 LEU HD1 H 0.2 0.1 2 695 . 74 LEU HD2 H -0.2 0.1 2 696 . 74 LEU C C 177.2 0.1 1 697 . 74 LEU CA C 56.2 0.1 1 698 . 74 LEU CB C 41.8 0.2 1 699 . 74 LEU CG C 25.2 0.2 1 700 . 74 LEU CD1 C 26.7 0.2 1 701 . 74 LEU CD2 C 20.3 0.2 1 702 . 74 LEU N N 124.1 0.1 1 703 . 75 TYR H H 8.28 0.05 1 704 . 75 TYR HA H 3.2 0.1 1 705 . 75 TYR HB2 H 2.8 0.1 2 706 . 75 TYR HB3 H 2.6 0.1 2 707 . 75 TYR C C 178.5 0.1 1 708 . 75 TYR CA C 61.1 0.1 1 709 . 75 TYR CB C 38.2 0.2 1 710 . 75 TYR N N 118.2 0.1 1 711 . 76 ALA H H 7.97 0.05 1 712 . 76 ALA HA H 3.9 0.1 1 713 . 76 ALA HB H 1.5 0.1 1 714 . 76 ALA C C 180.0 0.1 1 715 . 76 ALA CA C 54.3 0.1 1 716 . 76 ALA CB C 17.1 0.2 1 717 . 76 ALA N N 121.0 0.1 1 718 . 77 GLU H H 7.42 0.05 1 719 . 77 GLU HA H 4.0 0.1 1 720 . 77 GLU HB2 H 2.0 0.1 2 721 . 77 GLU HG2 H 2.4 0.1 2 722 . 77 GLU HG3 H 2.0 0.1 2 723 . 77 GLU C C 179.8 0.1 1 724 . 77 GLU CA C 58.2 0.1 1 725 . 77 GLU CB C 29.1 0.2 1 726 . 77 GLU CG C 34.6 0.2 1 727 . 77 GLU N N 119.4 0.1 1 728 . 78 TRP H H 8.10 0.05 1 729 . 78 TRP HA H 4.7 0.1 1 730 . 78 TRP HB2 H 2.8 0.1 2 731 . 78 TRP HB3 H 2.7 0.1 2 732 . 78 TRP C C 178.5 0.1 1 733 . 78 TRP CA C 55.9 0.1 1 734 . 78 TRP CB C 27.8 0.2 1 735 . 78 TRP N N 119.2 0.1 1 736 . 79 SER H H 8.56 0.05 1 737 . 79 SER HA H 4.1 0.1 1 738 . 79 SER HB2 H 3.7 0.1 2 739 . 79 SER HB3 H 3.3 0.1 2 740 . 79 SER C C 175.0 0.1 1 741 . 79 SER CA C 60.6 0.1 1 742 . 79 SER CB C 61.4 0.2 1 743 . 79 SER N N 116.9 0.1 1 744 . 80 GLU H H 6.93 0.05 1 745 . 80 GLU HA H 4.3 0.1 1 746 . 80 GLU HB2 H 2.2 0.1 2 747 . 80 GLU HB3 H 2.0 0.1 2 748 . 80 GLU HG2 H 2.5 0.1 2 749 . 80 GLU HG3 H 2.3 0.1 2 750 . 80 GLU C C 177.7 0.1 1 751 . 80 GLU CA C 56.9 0.1 1 752 . 80 GLU CB C 30.0 0.2 1 753 . 80 GLU CG C 35.2 0.2 1 754 . 80 GLU N N 117.4 0.1 1 755 . 81 VAL H H 7.46 0.05 1 756 . 81 VAL HA H 4.5 0.1 1 757 . 81 VAL HB H 2.2 0.1 2 758 . 81 VAL HG1 H 0.9 0.1 1 759 . 81 VAL HG2 H 0.9 0.1 1 760 . 81 VAL C C 174.9 0.1 1 761 . 81 VAL CA C 60.6 0.1 1 762 . 81 VAL CB C 33.5 0.2 1 763 . 81 VAL CG1 C 21.3 0.2 1 764 . 81 VAL CG2 C 18.1 0.2 1 765 . 81 VAL N N 109.3 0.1 1 766 . 82 VAL H H 8.01 0.05 1 767 . 82 VAL HA H 4.2 0.1 1 768 . 82 VAL HB H 1.8 0.1 2 769 . 82 VAL HG1 H 0.8 0.1 2 770 . 82 VAL HG2 H 0.6 0.1 2 771 . 82 VAL C C 174.0 0.1 1 772 . 82 VAL CA C 60.1 0.1 1 773 . 82 VAL CB C 33.2 0.2 1 774 . 82 VAL CG1 C 20.7 0.2 1 775 . 82 VAL CG2 C 21.3 0.2 1 776 . 82 VAL N N 122.9 0.1 1 777 . 83 SER H H 8.08 0.05 1 778 . 83 SER HA H 4.3 0.1 1 779 . 83 SER HB2 H 4.1 0.1 2 780 . 83 SER HB3 H 4.0 0.1 2 781 . 83 SER C C 175.2 0.1 1 782 . 83 SER CA C 57.3 0.1 1 783 . 83 SER CB C 63.4 0.2 1 784 . 83 SER N N 117.5 0.1 1 785 . 84 THR H H 8.10 0.05 1 786 . 84 THR HA H 5.2 0.1 1 787 . 84 THR HB H 4.8 0.1 2 788 . 84 THR HG2 H 1.2 0.1 1 789 . 84 THR C C 175.2 0.1 1 790 . 84 THR CA C 60.0 0.1 1 791 . 84 THR CB C 67.3 0.2 1 792 . 84 THR CG2 C 20.8 0.2 1 793 . 84 THR N N 113.4 0.1 1 794 . 85 ASN H H 8.50 0.05 1 795 . 85 ASN HA H 5.1 0.1 1 796 . 85 ASN HB2 H 3.0 0.1 2 797 . 85 ASN HB3 H 2.7 0.1 2 798 . 85 ASN C C 175.1 0.1 1 799 . 85 ASN CA C 50.3 0.1 1 800 . 85 ASN CB C 35.8 0.2 1 801 . 85 ASN N N 122.0 0.1 1 802 . 86 PHE H H 8.05 0.05 1 803 . 86 PHE HA H 3.8 0.1 1 804 . 86 PHE HB2 H 2.9 0.1 2 805 . 86 PHE HB3 H 2.6 0.1 2 806 . 86 PHE C C 176.5 0.1 1 807 . 86 PHE CA C 61.1 0.1 1 808 . 86 PHE CB C 39.6 0.2 1 809 . 86 PHE N N 123.5 0.1 1 810 . 87 ARG H H 8.05 0.05 1 811 . 87 ARG HA H 4.3 0.1 1 812 . 87 ARG HB2 H 2.0 0.1 2 813 . 87 ARG HB3 H 1.9 0.1 2 814 . 87 ARG HG2 H 1.9 0.1 2 815 . 87 ARG HD2 H 3.3 0.1 2 816 . 87 ARG C C 176.7 0.1 1 817 . 87 ARG CA C 56.4 0.1 1 818 . 87 ARG CB C 28.8 0.2 1 819 . 87 ARG CG C 26.8 0.2 1 820 . 87 ARG CD C 42.4 0.2 1 821 . 87 ARG N N 112.0 0.1 1 822 . 88 ASP H H 7.20 0.05 1 823 . 88 ASP HA H 4.6 0.1 1 824 . 88 ASP HB2 H 3.0 0.1 2 825 . 88 ASP HB3 H 2.5 0.1 2 826 . 88 ASP C C 175.6 0.1 1 827 . 88 ASP CA C 52.5 0.1 1 828 . 88 ASP CB C 39.4 0.2 1 829 . 88 ASP N N 118.1 0.1 1 830 . 89 ALA H H 8.02 0.05 1 831 . 89 ALA HA H 4.2 0.1 1 832 . 89 ALA HB H 1.3 0.1 1 833 . 89 ALA C C 177.2 0.1 1 834 . 89 ALA CA C 51.3 0.1 1 835 . 89 ALA CB C 17.5 0.2 1 836 . 89 ALA N N 126.5 0.1 1 837 . 90 SER H H 8.19 0.05 1 838 . 90 SER HA H 4.2 0.1 1 839 . 90 SER HB2 H 3.9 0.1 2 840 . 90 SER HB3 H 3.8 0.1 2 841 . 90 SER C C 174.0 0.1 1 842 . 90 SER CA C 58.7 0.1 1 843 . 90 SER CB C 62.6 0.2 1 844 . 90 SER N N 114.5 0.1 1 845 . 91 GLY H H 7.32 0.05 1 846 . 91 GLY HA2 H 4.2 0.1 1 847 . 91 GLY HA3 H 4.0 0.1 1 848 . 91 GLY CA C 43.7 0.1 1 849 . 91 GLY N N 109.8 0.1 1 850 . 92 PRO HA H 4.4 0.1 1 851 . 92 PRO HB2 H 1.7 0.1 2 852 . 92 PRO HB3 H 1.3 0.1 2 853 . 92 PRO HG2 H 2.0 0.1 2 854 . 92 PRO HG3 H 1.5 0.1 2 855 . 92 PRO HD2 H 3.7 0.1 2 856 . 92 PRO HD3 H 3.2 0.1 2 857 . 92 PRO C C 176.7 0.1 1 858 . 92 PRO CA C 61.8 0.1 1 859 . 92 PRO CB C 32.6 0.2 1 860 . 92 PRO CG C 25.9 0.2 1 861 . 92 PRO CD C 48.0 0.2 1 862 . 93 ALA H H 8.63 0.05 1 863 . 93 ALA HA H 5.0 0.1 1 864 . 93 ALA HB H 1.2 0.1 1 865 . 93 ALA C C 174.5 0.1 1 866 . 93 ALA CA C 51.4 0.1 1 867 . 93 ALA CB C 23.2 0.2 1 868 . 93 ALA N N 121.6 0.1 1 869 . 94 MET H H 8.82 0.05 1 870 . 94 MET HA H 6.0 0.1 1 871 . 94 MET HB2 H 2.1 0.1 2 872 . 94 MET HG2 H 2.3 0.1 2 873 . 94 MET C C 175.5 0.1 1 874 . 94 MET CA C 53.3 0.1 1 875 . 94 MET CB C 37.0 0.2 1 876 . 94 MET CG C 30.0 0.2 1 877 . 94 MET N N 116.5 0.1 1 878 . 95 THR H H 8.70 0.05 1 879 . 95 THR HA H 4.5 0.1 1 880 . 95 THR HB H 4.6 0.1 2 881 . 95 THR HG2 H 0.4 0.1 1 882 . 95 THR C C 175.6 0.1 1 883 . 95 THR CA C 60.1 0.1 1 884 . 95 THR CB C 71.3 0.2 1 885 . 95 THR CG2 C 19.2 0.2 1 886 . 95 THR N N 109.6 0.1 1 887 . 96 GLU H H 8.08 0.05 1 888 . 96 GLU HA H 4.5 0.1 1 889 . 96 GLU HB2 H 2.2 0.1 2 890 . 96 GLU HB3 H 2.1 0.1 2 891 . 96 GLU HG2 H 2.4 0.1 2 892 . 96 GLU C C 178.3 0.1 1 893 . 96 GLU CA C 55.7 0.1 1 894 . 96 GLU CB C 29.9 0.2 1 895 . 96 GLU CG C 35.6 0.2 1 896 . 96 GLU N N 115.5 0.1 1 897 . 97 ILE H H 8.18 0.05 1 898 . 97 ILE HA H 4.2 0.1 1 899 . 97 ILE HB H 1.3 0.1 2 900 . 97 ILE HG12 H 0.9 0.1 2 901 . 97 ILE HG2 H 0.7 0.1 1 902 . 97 ILE HD1 H 0.5 0.1 1 903 . 97 ILE CA C 61.8 0.1 1 904 . 97 ILE CB C 36.9 0.2 1 905 . 97 ILE CG1 C 28.9 0.2 1 906 . 97 ILE CG2 C 17.5 0.2 1 907 . 97 ILE CD1 C 12.3 0.2 1 908 . 97 ILE N N 122.8 0.1 1 909 . 98 GLY H H 8.93 0.05 1 910 . 98 GLY HA2 H 4.5 0.1 1 911 . 98 GLY HA3 H 3.7 0.1 1 912 . 98 GLY C C 172.2 0.1 1 913 . 98 GLY CA C 43.1 0.1 1 914 . 98 GLY N N 116.8 0.1 1 915 . 99 GLU H H 8.28 0.05 1 916 . 99 GLU HA H 4.1 0.1 1 917 . 99 GLU HB2 H 1.8 0.1 2 918 . 99 GLU HB3 H 1.7 0.1 2 919 . 99 GLU HG2 H 2.0 0.1 1 920 . 99 GLU HG3 H 2.0 0.1 1 921 . 99 GLU C C 175.4 0.1 1 922 . 99 GLU CA C 55.9 0.1 1 923 . 99 GLU CB C 29.0 0.2 1 924 . 99 GLU CG C 35.2 0.2 1 925 . 99 GLU N N 120.8 0.1 1 926 . 100 GLN H H 7.59 0.05 1 927 . 100 GLN HA H 4.5 0.1 1 928 . 100 GLN HB2 H 0.2 0.1 2 929 . 100 GLN HG2 H 1.8 0.1 2 930 . 100 GLN HG3 H 1.7 0.1 2 931 . 100 GLN CA C 51.6 0.1 1 932 . 100 GLN CB C 24.5 0.2 1 933 . 100 GLN CG C 30.3 0.2 1 934 . 100 GLN N N 124.1 0.1 1 935 . 101 PRO HA H 4.0 0.1 1 936 . 101 PRO HB2 H 2.3 0.1 2 937 . 101 PRO HB3 H 1.6 0.1 2 938 . 101 PRO HG2 H 2.2 0.1 2 939 . 101 PRO HG3 H 1.7 0.1 2 940 . 101 PRO HD2 H 3.4 0.1 2 941 . 101 PRO C C 176.4 0.1 1 942 . 101 PRO CA C 64.4 0.1 1 943 . 101 PRO CB C 30.5 0.2 1 944 . 101 PRO CG C 26.4 0.2 1 945 . 101 PRO CD C 49.4 0.2 1 946 . 102 TRP H H 5.79 0.05 1 947 . 102 TRP HA H 4.5 0.1 1 948 . 102 TRP HB2 H 3.3 0.1 2 949 . 102 TRP HB3 H 2.4 0.1 2 950 . 102 TRP C C 174.7 0.1 1 951 . 102 TRP CA C 55.7 0.1 1 952 . 102 TRP CB C 26.9 0.2 1 953 . 102 TRP N N 108.1 0.1 1 954 . 103 GLY H H 6.99 0.05 1 955 . 103 GLY HA2 H 4.5 0.1 1 956 . 103 GLY HA3 H 3.7 0.1 1 957 . 103 GLY C C 171.6 0.1 1 958 . 103 GLY CA C 43.6 0.1 1 959 . 103 GLY N N 111.5 0.1 1 960 . 104 ARG H H 8.38 0.05 1 961 . 104 ARG HA H 4.7 0.1 1 962 . 104 ARG HB2 H 1.6 0.1 2 963 . 104 ARG HG2 H 1.3 0.1 2 964 . 104 ARG HG3 H 1.6 0.1 2 965 . 104 ARG HD2 H 3.2 0.1 2 966 . 104 ARG C C 175.2 0.1 1 967 . 104 ARG CA C 55.3 0.1 1 968 . 104 ARG CB C 30.5 0.2 1 969 . 104 ARG CG C 27.9 0.2 1 970 . 104 ARG CD C 42.6 0.2 1 971 . 104 ARG N N 120.6 0.1 1 972 . 105 GLU H H 8.55 0.05 1 973 . 105 GLU HA H 6.0 0.1 1 974 . 105 GLU HB2 H 1.9 0.1 2 975 . 105 GLU C C 176.1 0.1 1 976 . 105 GLU CA C 54.0 0.1 1 977 . 105 GLU CB C 34.9 0.2 1 978 . 105 GLU N N 119.6 0.1 1 979 . 106 PHE H H 8.77 0.05 1 980 . 106 PHE HA H 4.7 0.1 1 981 . 106 PHE HB2 H 3.2 0.1 2 982 . 106 PHE HB3 H 2.6 0.1 2 983 . 106 PHE C C 171.2 0.1 1 984 . 106 PHE CA C 55.5 0.1 1 985 . 106 PHE CB C 41.6 0.2 1 986 . 106 PHE N N 118.6 0.1 1 987 . 107 ALA H H 8.59 0.05 1 988 . 107 ALA HA H 5.1 0.1 1 989 . 107 ALA HB H 0.3 0.1 1 990 . 107 ALA C C 174.5 0.1 1 991 . 107 ALA CA C 49.2 0.1 1 992 . 107 ALA CB C 20.7 0.2 1 993 . 107 ALA N N 123.2 0.1 1 994 . 108 LEU H H 9.12 0.05 1 995 . 108 LEU HA H 5.3 0.1 1 996 . 108 LEU HB2 H 2.1 0.1 2 997 . 108 LEU HB3 H 1.8 0.1 2 998 . 108 LEU HG H 1.6 0.1 2 999 . 108 LEU HD1 H 0.7 0.1 2 1000 . 108 LEU HD2 H 0.6 0.1 2 1001 . 108 LEU CA C 53.8 0.1 1 1002 . 108 LEU CB C 46.6 0.2 1 1003 . 108 LEU CG C 26.9 0.2 1 1004 . 108 LEU CD1 C 21.8 0.2 1 1005 . 108 LEU CD2 C 24.6 0.2 1 1006 . 108 LEU N N 124.2 0.1 1 1007 . 109 ARG H H 9.52 0.05 1 1008 . 109 ARG HA H 5.9 0.1 1 1009 . 109 ARG HB2 H 1.7 0.1 2 1010 . 109 ARG HG2 H 1.6 0.1 2 1011 . 109 ARG HD2 H 3.2 0.1 2 1012 . 109 ARG C C 175.2 0.1 1 1013 . 109 ARG CA C 52.7 0.1 1 1014 . 109 ARG CB C 31.9 0.2 1 1015 . 109 ARG CG C 26.8 0.2 1 1016 . 109 ARG CD C 42.5 0.2 1 1017 . 109 ARG N N 129.2 0.1 1 1018 . 110 ASP H H 8.50 0.05 1 1019 . 110 ASP HA H 3.8 0.1 1 1020 . 110 ASP HB2 H 2.9 0.1 2 1021 . 110 ASP HB3 H 2.5 0.1 2 1022 . 110 ASP CA C 51.6 0.1 1 1023 . 110 ASP CB C 39.6 0.2 1 1024 . 110 ASP N N 128.1 0.1 1 1025 . 111 PRO HA H 3.8 0.1 1 1026 . 111 PRO HB2 H 2.1 0.1 2 1027 . 111 PRO HB3 H 1.7 0.1 2 1028 . 111 PRO HG2 H 1.7 0.1 2 1029 . 111 PRO HG3 H 1.2 0.1 2 1030 . 111 PRO HD2 H 2.8 0.1 2 1031 . 111 PRO HD3 H 1.2 0.1 2 1032 . 111 PRO C C 177.1 0.1 1 1033 . 111 PRO CA C 64.4 0.1 1 1034 . 111 PRO CB C 30.2 0.2 1 1035 . 111 PRO CG C 27.4 0.2 1 1036 . 111 PRO CD C 48.7 0.2 1 1037 . 112 ALA H H 7.81 0.05 1 1038 . 112 ALA HA H 4.3 0.1 1 1039 . 112 ALA HB H 1.7 0.1 1 1040 . 112 ALA C C 177.3 0.1 1 1041 . 112 ALA CA C 51.8 0.1 1 1042 . 112 ALA CB C 18.6 0.2 1 1043 . 112 ALA N N 118.2 0.1 1 1044 . 113 GLY H H 7.83 0.05 1 1045 . 113 GLY HA2 H 4.4 0.1 1 1046 . 113 GLY HA3 H 3.3 0.1 1 1047 . 113 GLY C C 172.6 0.1 1 1048 . 113 GLY CA C 43.9 0.1 1 1049 . 113 GLY N N 106.4 0.1 1 1050 . 114 ASN H H 7.81 0.05 1 1051 . 114 ASN HA H 4.5 0.1 1 1052 . 114 ASN HB2 H 2.7 0.1 2 1053 . 114 ASN HB3 H 2.6 0.1 2 1054 . 114 ASN C C 174.8 0.1 1 1055 . 114 ASN CA C 53.8 0.1 1 1056 . 114 ASN CB C 40.8 0.2 1 1057 . 114 ASN N N 118.4 0.1 1 1058 . 115 CYS H H 8.44 0.05 1 1059 . 115 CYS HA H 5.6 0.1 1 1060 . 115 CYS HB2 H 2.8 0.1 2 1061 . 115 CYS HB3 H 2.4 0.1 2 1062 . 115 CYS C C 173.3 0.1 1 1063 . 115 CYS CA C 55.2 0.1 1 1064 . 115 CYS CB C 26.8 0.2 1 1065 . 115 CYS N N 120.8 0.1 1 1066 . 116 VAL H H 9.41 0.05 1 1067 . 116 VAL HA H 4.6 0.1 1 1068 . 116 VAL HB H 2.2 0.1 2 1069 . 116 VAL HG1 H 1.0 0.1 2 1070 . 116 VAL HG2 H 0.3 0.1 2 1071 . 116 VAL C C 175.0 0.1 1 1072 . 116 VAL CA C 59.7 0.1 1 1073 . 116 VAL CB C 32.4 0.2 1 1074 . 116 VAL CG1 C 21.3 0.2 1 1075 . 116 VAL CG2 C 22.2 0.2 1 1076 . 116 VAL N N 128.4 0.1 1 1077 . 117 HIS H H 8.61 0.05 1 1078 . 117 HIS HA H 4.4 0.1 1 1079 . 117 HIS HB2 H 2.2 0.1 2 1080 . 117 HIS C C 172.0 0.1 1 1081 . 117 HIS CA C 53.2 0.1 1 1082 . 117 HIS CB C 27.3 0.2 1 1083 . 117 HIS N N 126.1 0.1 1 1084 . 118 PHE H H 8.91 0.05 1 1085 . 118 PHE HA H 4.6 0.1 1 1086 . 118 PHE HB2 H 1.4 0.1 2 1087 . 118 PHE HB3 H 2.1 0.1 2 1088 . 118 PHE C C 173.2 0.1 1 1089 . 118 PHE CA C 55.8 0.1 1 1090 . 118 PHE CB C 39.1 0.2 1 1091 . 118 PHE N N 123.3 0.1 1 1092 . 119 VAL H H 8.96 0.05 1 1093 . 119 VAL HA H 4.9 0.1 1 1094 . 119 VAL HB H 1.9 0.1 2 1095 . 119 VAL C C 175.3 0.1 1 1096 . 119 VAL CA C 57.8 0.1 1 1097 . 119 VAL CB C 33.9 0.2 1 1098 . 119 VAL N N 122.2 0.1 1 1099 . 120 ALA H H 8.81 0.05 1 1100 . 120 ALA HA H 4.9 0.1 1 1101 . 120 ALA HB H 1.6 0.1 1 1102 . 120 ALA C C 178.6 0.1 1 1103 . 120 ALA CA C 51.8 0.1 1 1104 . 120 ALA CB C 19.0 0.2 1 1105 . 120 ALA N N 128.0 0.1 1 1106 . 121 GLU H H 9.01 0.05 1 1107 . 121 GLU HA H 4.7 0.1 1 1108 . 121 GLU HB2 H 2.2 0.1 2 1109 . 121 GLU HB3 H 2.0 0.1 2 1110 . 121 GLU HG2 H 2.5 0.1 2 1111 . 121 GLU HG3 H 2.4 0.1 2 1112 . 121 GLU C C 177.0 0.1 1 1113 . 121 GLU CA C 56.1 0.1 1 1114 . 121 GLU CB C 30.3 0.2 1 1115 . 121 GLU CG C 35.8 0.2 1 1116 . 121 GLU N N 124.9 0.1 1 1117 . 122 GLU H H 8.90 0.05 1 1118 . 122 GLU HA H 4.5 0.1 1 1119 . 122 GLU HB2 H 2.2 0.1 2 1120 . 122 GLU HB3 H 2.0 0.1 2 1121 . 122 GLU HG2 H 2.4 0.1 2 1122 . 122 GLU C C 176.3 0.1 1 1123 . 122 GLU CA C 55.9 0.1 1 1124 . 122 GLU CB C 29.8 0.2 1 1125 . 122 GLU CG C 35.0 0.2 1 1126 . 122 GLU N N 124.5 0.1 1 1127 . 123 GLN H H 8.45 0.05 1 1128 . 123 GLN HA H 4.5 0.1 1 1129 . 123 GLN HB2 H 2.2 0.1 2 1130 . 123 GLN HB3 H 2.0 0.1 2 1131 . 123 GLN HG2 H 2.4 0.1 2 1132 . 123 GLN C C 174.8 0.1 1 1133 . 123 GLN CA C 55.0 0.1 1 1134 . 123 GLN CB C 29.8 0.2 1 1135 . 123 GLN CG C 33.3 0.2 1 1136 . 123 GLN N N 121.5 0.1 1 1137 . 124 ASP H H 8.05 0.05 1 1138 . 124 ASP HA H 4.4 0.1 1 1139 . 124 ASP HB2 H 2.7 0.1 2 1140 . 124 ASP HB3 H 2.6 0.1 2 1141 . 124 ASP CA C 55.0 0.1 1 1142 . 124 ASP CB C 41.2 0.2 1 1143 . 124 ASP N N 127.7 0.1 1 stop_ save_