data_18755 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Structure of Mdm2 (6-125) with Pip-1 ; _BMRB_accession_number 18755 _BMRB_flat_file_name bmr18755.str _Entry_type original _Submission_date 2012-10-02 _Accession_date 2012-10-02 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Michelsen Klaus B. . 2 Jordan John B. . 3 Lewis Jeffrey . . 4 Long Alexander M. . 5 Yang Evelyn . . 6 Rew Yosup . . 7 Zhou Jing . . 8 Yakowec Peter . . 9 Schnier Paul D. . 10 Huang Xin . . 11 Poppe Leszek . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 489 "13C chemical shifts" 405 "15N chemical shifts" 113 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-07-02 update BMRB 'update entry citation' 2012-11-02 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Ordering of the N-terminus of human MDM2 by small molecule inhibitors.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22991965 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Michelsen Klaus . . 2 Jordan John B. . 3 Lewis Jeffrey . . 4 Long Alexander M. . 5 Yang Evelyn . . 6 Rew Yosup . . 7 Zhou Jing . . 8 Yakowec Peter . . 9 Schnier Paul D. . 10 Huang Xin . . 11 Poppe Leszek . . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full 'Journal of the American Chemical Society' _Journal_volume 134 _Journal_issue 41 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 17059 _Page_last 17067 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Mdm2 (6-125) with Pip-1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $entity_1 '(5-HYDROXY-1H-INDOL-3-YL)ACETIC ACID_1' $entity_0R3 '(5-HYDROXY-1H-INDOL-3-YL)ACETIC ACID_2' $entity_0R3 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 13882.983 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 124 _Mol_residue_sequence ; MCNTNMSVPTDGAVTTSQIP ASEQETLVRPKPLLLKLLKS VGAQKDTYTMKEVLFYLGQY IMTKRLYDEKQQIVYCSNDL LGDLFGVPSFSVKEHRKIYT MIYRNLVVVNQQESSDSGTS VSEN ; loop_ _Residue_seq_code _Residue_label 1 MET 2 CYS 3 ASN 4 THR 5 ASN 6 MET 7 SER 8 VAL 9 PRO 10 THR 11 ASP 12 GLY 13 ALA 14 VAL 15 THR 16 THR 17 SER 18 GLN 19 ILE 20 PRO 21 ALA 22 SER 23 GLU 24 GLN 25 GLU 26 THR 27 LEU 28 VAL 29 ARG 30 PRO 31 LYS 32 PRO 33 LEU 34 LEU 35 LEU 36 LYS 37 LEU 38 LEU 39 LYS 40 SER 41 VAL 42 GLY 43 ALA 44 GLN 45 LYS 46 ASP 47 THR 48 TYR 49 THR 50 MET 51 LYS 52 GLU 53 VAL 54 LEU 55 PHE 56 TYR 57 LEU 58 GLY 59 GLN 60 TYR 61 ILE 62 MET 63 THR 64 LYS 65 ARG 66 LEU 67 TYR 68 ASP 69 GLU 70 LYS 71 GLN 72 GLN 73 ILE 74 VAL 75 TYR 76 CYS 77 SER 78 ASN 79 ASP 80 LEU 81 LEU 82 GLY 83 ASP 84 LEU 85 PHE 86 GLY 87 VAL 88 PRO 89 SER 90 PHE 91 SER 92 VAL 93 LYS 94 GLU 95 HIS 96 ARG 97 LYS 98 ILE 99 TYR 100 THR 101 MET 102 ILE 103 TYR 104 ARG 105 ASN 106 LEU 107 VAL 108 VAL 109 VAL 110 ASN 111 GLN 112 GLN 113 GLU 114 SER 115 SER 116 ASP 117 SER 118 GLY 119 THR 120 SER 121 VAL 122 SER 123 GLU 124 ASN 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 11569 MIP-MDM2 79.84 131 96.97 97.98 7.05e-61 BMRB 18876 entity_1 86.29 107 99.07 99.07 7.21e-69 BMRB 2410 "N-terminal domain of the human murine double minute clone 2 protein" 95.16 119 99.15 99.15 8.80e-78 PDB 1RV1 "Crystal Structure Of Human Mdm2 With An Imidazoline Inhibitor" 68.55 85 97.65 97.65 4.07e-50 PDB 1T4E "Structure Of Human Mdm2 In Complex With A Benzodiazepine Inhibitor" 76.61 96 98.95 98.95 5.63e-59 PDB 1T4F "Structure Of Human Mdm2 In Complex With An Optimized P53 Peptide" 87.90 110 99.08 99.08 1.31e-69 PDB 1YCR "Mdm2 Bound To The Transactivation Domain Of P53" 87.90 109 99.08 99.08 1.15e-69 PDB 1Z1M "Nmr Structure Of Unliganded Mdm2" 95.16 119 99.15 99.15 8.80e-78 PDB 2AXI "Hdm2 In Complex With A Beta-hairpin" 87.90 115 99.08 99.08 3.88e-70 PDB 2GV2 "Mdm2 In Complex With An 8-Mer P53 Peptide Analogue" 87.90 110 99.08 99.08 1.31e-69 PDB 2LZG "Nmr Structure Of Mdm2 (6-125) With Pip-1" 100.81 125 99.20 99.20 4.44e-83 PDB 2M86 "Solution Structure Of Hdm2 With Engineered Cyclotide" 87.90 129 99.08 99.08 4.75e-70 PDB 2MPS "Structure Of Complex Of Mdm2(3-109) And P73 Tad(10-25)" 86.29 107 99.07 99.07 7.21e-69 PDB 2RUH "Chemical Shift Assignments For Mip And Mdm2 In Bound State" 79.84 131 96.97 97.98 7.05e-61 PDB 3EQS "Crystal Structure Of Human Mdm2 In Complex With A 12-Mer Peptide Inhibitor" 68.55 85 98.82 98.82 4.06e-51 PDB 3G03 "Structure Of Human Mdm2 In Complex With High Affinity Peptide" 87.10 109 99.07 99.07 4.49e-69 PDB 3IUX "Crystal Structure Of Human Mdm2 In Complex With A Potent Miniature Protein Inhibitor (18-Residues)" 68.55 85 98.82 98.82 4.06e-51 PDB 3IWY "Crystal Structure Of Human Mdm2 Complexed With D-peptide (12 Residues)" 68.55 85 98.82 98.82 4.06e-51 PDB 3JZK "Crystal Structure Of Mdm2 With Chromenotriazolopyrimidine 1" 76.61 96 98.95 98.95 5.63e-59 PDB 3JZR "Human Mdm2 Liganded With A 12mer Peptide Inhibitor (Pdi6w)" 87.90 110 99.08 99.08 1.31e-69 PDB 3JZS "Human Mdm2 Liganded With A 12mer Peptide Inhibitor (Pdiq)" 69.35 86 98.84 98.84 5.23e-52 PDB 3LBK "Structure Of Human Mdm2 Protein In Complex With A Small Molecule Inhibitor" 75.81 95 97.87 97.87 2.55e-57 PDB 3LBL "Structure Of Human Mdm2 Protein In Complex With Mi-63-Analog" 75.81 95 98.94 98.94 1.83e-58 PDB 3LNJ "Crystal Structure Of Human Mdm2 In Complex With D-Peptide Inhibitor (Dpmi-Alpha)" 68.55 85 98.82 98.82 4.06e-51 PDB 3LNZ "Crystal Structure Of Human Mdm2 With A 12-Mer Peptide Inhibitor Pmi (N8a Mutant)" 68.55 85 98.82 98.82 4.06e-51 PDB 3TJ2 "Structure Of A Novel Submicromolar Mdm2 Inhibitor" 75.81 95 98.94 98.94 1.83e-58 PDB 3TPX "Crystal Structure Of Human Mdm2 In Complex With A Trifluoromethylated D-peptide Inhibitor" 68.55 85 98.82 98.82 4.06e-51 PDB 3TU1 "Exhaustive Fluorine Scanning Towards Potent P53-Mdm2 Antagonist" 87.10 108 99.07 99.07 4.60e-69 PDB 3V3B "Structure Of The Stapled P53 Peptide Bound To Mdm2" 70.16 88 98.85 98.85 1.14e-52 PDB 3VBG "Structure Of Hdm2 With Dimer Inducing Indolyl Hydantoin Ro-2443" 68.55 85 97.65 97.65 4.07e-50 PDB 3VZV "Crystal Structure Of Human Mdm2 With A Dihydroimidazothiazole Inhibitor" 68.55 87 97.65 97.65 5.42e-50 PDB 3W69 "Crystal Structure Of Human Mdm2 With A Dihydroimidazothiazole Inhibitor" 68.55 87 97.65 97.65 5.42e-50 PDB 4DIJ "The Central Valine Concept Provides An Entry In A New Class Of Non Peptide Inhibitors Of The P53-Mdm2 Interaction" 76.61 96 97.89 97.89 5.92e-58 PDB 4ERE "Crystal Structure Of Mdm2 (17-111) In Complex With Compound 23" 76.61 96 98.95 98.95 5.63e-59 PDB 4ERF "Crystal Structure Of Mdm2 (17-111) In Complex With Compound 29 (Am- 8553)" 76.61 96 98.95 98.95 5.63e-59 PDB 4HBM "Ordering Of The N Terminus Of Human Mdm2 By Small Molecule Inhibitors" 96.77 120 99.17 99.17 2.17e-78 PDB 4HFZ "Crystal Structure Of An Mdm2/p53 Peptide Complex" 87.90 109 97.25 97.25 3.38e-68 PDB 4JV7 "Co-crystal Structure Of Mdm2 With Inhibitor (2s,5r,6s)-2-benzyl-5,6- Bis(4-bromophenyl)-4-methylmorpholin-3-one" 75.81 96 98.94 98.94 2.29e-58 PDB 4JV9 "Co-crystal Structure Of Mdm2 With Inhibitor (2s,5r,6s)-2-benzyl-5,6- Bis(4-chlorophenyl)-4-methylmorpholin-3-one" 75.81 96 98.94 98.94 2.29e-58 PDB 4JVE "Co-crystal Structure Of Mdm2 With Inhibitor (2r,3e)-2-[(2s,3r,6s)-2,3- Bis(4-chlorophenyl)-6-(4-fluorobenzyl)-5-oxomorpholin-4-" 75.81 96 98.94 98.94 2.29e-58 PDB 4JVR "Co-crystal Structure Of Mdm2 With Inhibitor (2's,3r,4's,5'r)-n-(2- Aminoethyl)-6-chloro-4'-(3-chloro-2-fluorophenyl)-2'-(2,2- D" 75.81 96 98.94 98.94 2.29e-58 PDB 4JWR "Co-crystal Structure Of Mdm2 With Inhibitor {(2s,5r,6s)-6-(3- Chlorophenyl)-5-(4-chlorophenyl)-4-[(2s)-1-hydroxybutan-2-yl]-3- " 76.61 95 98.95 98.95 4.74e-59 PDB 4MDN "Structure Of A Novel Submicromolar Mdm2 Inhibitor" 75.00 94 98.92 98.92 1.71e-57 PDB 4MDQ "Structure Of A Novel Submicromolar Mdm2 Inhibitor" 69.35 86 98.84 98.84 7.65e-52 PDB 4OAS "Co-crystal Structure Of Mdm2 (17-111) In Complex With Compound 25" 76.61 96 98.95 98.95 5.63e-59 PDB 4OBA "Co-crystal Structure Of Mdm2 With Inhibitor Compound 4" 76.61 96 98.95 98.95 5.63e-59 PDB 4OCC "Co-crystal Structure Of Mdm2(17-111) In Complex With Compound 48" 76.61 96 98.95 98.95 5.63e-59 PDB 4ODE "Co-crystal Structure Of Mdm2 With Inhibitor Compound 4" 84.68 105 99.05 99.05 5.43e-67 PDB 4ODF "Co-crystal Structure Of Mdm2 With Inhibitor Compound 47" 84.68 105 99.05 99.05 5.43e-67 PDB 4OGN "Co-crystal Structure Of Mdm2 With Inhbitor Compound 3" 84.68 105 99.05 99.05 5.43e-67 PDB 4OGT "Co-crystal Structure Of Mdm2 With Inhbitor Compound 46" 84.68 105 99.05 99.05 5.43e-67 PDB 4OGV "Co-crystal Structure Of Mdm2 With Inhibitor Compound 49" 76.61 95 98.95 98.95 4.74e-59 PDB 4OQ3 "Tetra-substituted Imidazoles As A New Class Of Inhibitors Of The P53- Mdm2 Interaction" 76.61 96 97.89 97.89 5.92e-58 PDB 4QO4 "Co-crystal Structure Of Mdm2 (17-111) With Compound 16, {(3r,5r,6s)-5- (3-chlorophenyl)-6-(4-chlorophenyl)-1-[(1s)-1-(6-cyclopr" 76.61 96 98.95 98.95 5.63e-59 PDB 4QOC "Crystal Structure Of Compound 16 Bound To Mdm2(17-111), {(3r,5r,6s)-5- (3-chlorophenyl)-6-(4-chlorophenyl)-1-[(1s)-1-cyclopropy" 76.61 96 98.95 98.95 5.63e-59 PDB 4UMN "Structure Of A Stapled Peptide Antagonist Bound To Nutlin- Resistant Mdm2" 96.77 120 98.33 98.33 1.77e-77 PDB 4WT2 "Co-crystal Structure Of Mdm2 In Complex With Am-7209" 84.68 105 99.05 99.05 5.43e-67 PDB 4ZYC "Discovery Of Dihydroisoquinolinone Derivatives As Novel Inhibitors Of The P53-mdm2 Interaction With A Distinct Binding Mode: Hd" 76.61 96 97.89 97.89 5.92e-58 PDB 4ZYF "Discovery Of Nvp-cgm097 - A Highly Potent And Selective Mdm2 Inhibitor Undergoing Phase 1 Clinical Trials In P53wt Tumors: Hdm2" 76.61 96 98.95 98.95 5.63e-59 PDB 4ZYI "Discovery Of Nvp-cgm097 - A Highly Potent And Selective Mdm2 Inhibitor Undergoing Phase 1 Clinical Trials In P53wt Tumors: Hdm2" 76.61 96 98.95 98.95 5.63e-59 DBJ BAF83030 "unnamed protein product [Homo sapiens]" 100.81 491 99.20 99.20 3.20e-79 DBJ BAJ17752 "Mdm2 p53 binding protein homolog [synthetic construct]" 100.81 497 99.20 99.20 3.19e-79 EMBL CAA78055 "p53 associated [Homo sapiens]" 100.81 491 99.20 99.20 3.20e-79 EMBL CAD23251 "MDM2 isoform KB9 [Homo sapiens]" 100.81 243 99.20 99.20 1.47e-81 EMBL CAD36959 "p53-binding protein [Homo sapiens]" 100.81 166 99.20 99.20 3.89e-82 EMBL CAH89564 "hypothetical protein [Pongo abelii]" 100.81 497 99.20 99.20 3.13e-79 EMBL CAP16708 "MDM2 protein [Homo sapiens]" 100.81 413 99.20 99.20 3.79e-80 GB AAA60568 "p53 associated [Homo sapiens]" 100.81 491 99.20 99.20 3.20e-79 GB AAI48523 "Mdm2 p53 binding protein homolog (mouse), partial [synthetic construct]" 100.81 497 99.20 99.20 3.19e-79 GB AAI52385 "MDM2 protein, partial [Homo sapiens]" 100.81 490 99.20 99.20 2.81e-79 GB AAI52391 "MDM2 protein, partial [Homo sapiens]" 100.81 490 99.20 99.20 2.81e-79 GB AAI53118 "Mdm2 p53 binding protein homolog (mouse) [synthetic construct]" 100.81 497 99.20 99.20 3.19e-79 PRF 1814460A "p53-associated protein" 100.81 491 99.20 99.20 3.20e-79 REF NP_001124685 "E3 ubiquitin-protein ligase Mdm2 [Pongo abelii]" 100.81 497 99.20 99.20 3.13e-79 REF NP_001138809 "E3 ubiquitin-protein ligase Mdm2 isoform g [Homo sapiens]" 100.81 444 99.20 99.20 1.28e-79 REF NP_001138811 "E3 ubiquitin-protein ligase Mdm2 isoform h [Homo sapiens]" 91.94 442 99.12 99.12 1.98e-62 REF NP_001253331 "E3 ubiquitin-protein ligase Mdm2 [Macaca mulatta]" 100.81 497 99.20 99.20 2.81e-79 REF NP_002383 "E3 ubiquitin-protein ligase Mdm2 isoform a [Homo sapiens]" 100.81 497 99.20 99.20 3.19e-79 SP Q00987 "RecName: Full=E3 ubiquitin-protein ligase Mdm2; AltName: Full=Double minute 2 protein; Short=Hdm2; AltName: Full=Oncoprotein Md" 100.81 491 99.20 99.20 3.20e-79 stop_ save_ ############# # Ligands # ############# save_0R3 _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common '{(3R,5R,6S)-5-(3-chlorophenyl)-6-(4-chlorophenyl)-1-[(2S,3S)-2-hydroxypentan-3-yl]-3-methyl-2-oxopiperidin-3-yl}acetic acid' _BMRB_code 0R3 _PDB_code 0R3 _Molecular_mass 478.408 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C17 C17 C . 0 . ? C16 C16 C . 0 . ? CL2 CL2 CL . 0 . ? C15 C15 C . 0 . ? C14 C14 C . 0 . ? C13 C13 C . 0 . ? C6 C6 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C23 C23 C . 0 . ? C25 C25 C . 0 . ? O3 O3 O . 0 . ? O2 O2 O . 0 . ? C24 C24 C . 0 . ? C5 C5 C . 0 . ? O1 O1 O . 0 . ? N1 N1 N . 0 . ? C18 C18 C . 0 . ? C19 C19 C . 0 . ? C22 C22 C . 0 . ? C20 C20 C . 0 . ? O4 O4 O . 0 . ? C21 C21 C . 0 . ? C1 C1 C . 0 . ? C7 C7 C . 0 . ? C8 C8 C . 0 . ? C9 C9 C . 0 . ? C10 C10 C . 0 . ? CL1 CL1 CL . 0 . ? C11 C11 C . 0 . ? C12 C12 C . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? H4 H4 H . 0 . ? H5 H5 H . 0 . ? H6 H6 H . 0 . ? H7 H7 H . 0 . ? H8 H8 H . 0 . ? H9 H9 H . 0 . ? H10 H10 H . 0 . ? H11 H11 H . 0 . ? H12 H12 H . 0 . ? H13 H13 H . 0 . ? H14 H14 H . 0 . ? H15 H15 H . 0 . ? H16 H16 H . 0 . ? H17 H17 H . 0 . ? H18 H18 H . 0 . ? H19 H19 H . 0 . ? H20 H20 H . 0 . ? H21 H21 H . 0 . ? H22 H22 H . 0 . ? H23 H23 H . 0 . ? H24 H24 H . 0 . ? H25 H25 H . 0 . ? H26 H26 H . 0 . ? H27 H27 H . 0 . ? H28 H28 H . 0 . ? H29 H29 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 C21 C20 ? ? SING C20 O4 ? ? SING C20 C18 ? ? SING C22 C19 ? ? DOUB C11 C12 ? ? SING C11 C10 ? ? SING C18 C19 ? ? SING C18 N1 ? ? SING C12 C7 ? ? SING CL1 C10 ? ? DOUB C10 C9 ? ? SING C7 C1 ? ? DOUB C7 C8 ? ? SING N1 C1 ? ? SING N1 C5 ? ? SING C1 C2 ? ? SING C9 C8 ? ? DOUB O1 C5 ? ? SING C5 C4 ? ? DOUB C13 C14 ? ? SING C13 C6 ? ? SING C14 C15 ? ? SING C2 C6 ? ? SING C2 C3 ? ? DOUB C6 C17 ? ? DOUB C15 C16 ? ? SING C3 C4 ? ? SING C24 C4 ? ? SING C4 C23 ? ? SING C17 C16 ? ? SING C16 CL2 ? ? SING C23 C25 ? ? DOUB C25 O3 ? ? SING C25 O2 ? ? SING C17 H1 ? ? SING C15 H2 ? ? SING C14 H3 ? ? SING C13 H4 ? ? SING C2 H5 ? ? SING C3 H6 ? ? SING C3 H7 ? ? SING C23 H8 ? ? SING C23 H9 ? ? SING O2 H10 ? ? SING C24 H11 ? ? SING C24 H12 ? ? SING C24 H13 ? ? SING C18 H14 ? ? SING C19 H15 ? ? SING C19 H16 ? ? SING C22 H17 ? ? SING C22 H18 ? ? SING C22 H19 ? ? SING C20 H20 ? ? SING O4 H21 ? ? SING C21 H22 ? ? SING C21 H23 ? ? SING C21 H24 ? ? SING C1 H25 ? ? SING C8 H26 ? ? SING C9 H27 ? ? SING C11 H28 ? ? SING C12 H29 ? ? 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 $entity_1 Human 9606 Eukaryota Metazoa . . $entity_0R3 . . . . . . 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 $entity_1 'recombinant technology' . . . . Proprietary $entity_0R3 'chemical synthesis' . . . . . 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 $entity_1 500 uM '[U-100% 13C; U-100% 15N]' 'sodium chloride' 50 mM 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' DTT 5 mM '[U-100% 2H]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' 'structure solution' stop_ _Details . save_ save_AMBER _Saveframe_category software _Name AMBER _Version . loop_ _Vendor _Address _Electronic_address 'Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman' . . stop_ loop_ _Task refinement 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _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' 50 . mM pH 7.0 . pH pressure 1 . atm temperature 288.15 . 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 TSP C 13 'methyl protons' ppm 0 internal indirect . . . 0.251449530 TSP H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 TSP N 15 'methyl protons' ppm 0 internal indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCA' '3D HNCACB' '3D CBCA(CO)NH' '3D HNCO' '3D HN(CO)CA' '3D HCCH-TOCSY' '3D 1H-15N NOESY' '3D 1H-13C NOESY' 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 entity_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 2 2 CYS H H 8.252 0.000 1 2 2 2 CYS N N 123.192 0.000 1 3 3 3 ASN H H 8.128 0.000 1 4 3 3 ASN N N 123.749 0.000 1 5 6 6 MET H H 7.099 0.001 1 6 6 6 MET CA C 53.265 0.000 1 7 6 6 MET CB C 27.431 0.000 1 8 6 6 MET N N 119.009 0.000 1 9 7 7 SER H H 8.246 0.000 1 10 7 7 SER HA H 4.337 0.000 1 11 7 7 SER C C 177.600 0.000 1 12 7 7 SER CA C 57.850 0.000 1 13 7 7 SER CB C 63.720 0.000 1 14 7 7 SER N N 119.000 0.000 1 15 8 8 VAL H H 7.988 0.130 1 16 8 8 VAL HA H 4.290 0.000 1 17 8 8 VAL C C 180.600 0.000 1 18 8 8 VAL CA C 55.790 0.000 1 19 8 8 VAL CB C 31.860 0.000 1 20 8 8 VAL N N 126.800 1.800 1 21 9 9 PRO HA H 4.351 0.000 1 22 9 9 PRO HB2 H 1.837 0.005 2 23 9 9 PRO HB3 H 2.187 0.006 2 24 9 9 PRO C C 176.757 0.000 1 25 10 10 THR H H 8.109 0.001 1 26 10 10 THR HA H 4.307 0.099 1 27 10 10 THR HB H 4.166 0.067 1 28 10 10 THR HG2 H 1.109 0.081 1 29 10 10 THR C C 174.000 0.000 1 30 10 10 THR CA C 61.265 0.185 1 31 10 10 THR CB C 69.466 0.043 1 32 10 10 THR CG2 C 21.251 0.057 1 33 10 10 THR N N 113.463 0.047 1 34 11 11 ASP H H 8.180 0.001 1 35 11 11 ASP HA H 4.459 0.080 1 36 11 11 ASP HB2 H 2.547 0.080 1 37 11 11 ASP C C 175.900 0.000 1 38 11 11 ASP CA C 54.245 0.055 1 39 11 11 ASP CB C 40.957 0.017 1 40 11 11 ASP N N 122.009 0.039 1 41 12 12 GLY H H 7.409 0.004 1 42 12 12 GLY HA2 H 2.787 0.097 2 43 12 12 GLY HA3 H 2.908 0.088 2 44 12 12 GLY C C 171.700 0.000 1 45 12 12 GLY CA C 44.481 0.081 1 46 12 12 GLY N N 108.549 0.047 1 47 13 13 ALA H H 7.288 0.005 1 48 13 13 ALA HA H 4.326 0.073 1 49 13 13 ALA HB H 1.053 0.073 1 50 13 13 ALA C C 176.400 0.000 1 51 13 13 ALA CA C 51.676 0.080 1 52 13 13 ALA CB C 20.646 0.046 1 53 13 13 ALA N N 119.600 0.000 1 54 14 14 VAL H H 8.091 0.003 1 55 14 14 VAL HA H 4.561 0.052 1 56 14 14 VAL HB H 2.134 0.057 1 57 14 14 VAL HG1 H 0.934 0.042 1 58 14 14 VAL C C 174.300 0.000 1 59 14 14 VAL CA C 60.637 0.038 1 60 14 14 VAL CB C 34.173 0.054 1 61 14 14 VAL CG1 C 21.230 0.020 1 62 14 14 VAL N N 118.098 0.005 1 63 15 15 THR H H 8.303 0.001 1 64 15 15 THR HA H 4.767 0.058 1 65 15 15 THR HB H 4.087 0.057 1 66 15 15 THR HG2 H 1.050 0.085 1 67 15 15 THR C C 173.364 0.000 1 68 15 15 THR CA C 60.011 0.027 1 69 15 15 THR CB C 71.125 0.134 1 70 15 15 THR CG2 C 21.448 0.000 1 71 15 15 THR N N 116.900 0.000 1 72 16 16 THR H H 8.352 0.003 1 73 16 16 THR HA H 4.698 0.065 1 74 16 16 THR HB H 3.153 0.059 1 75 16 16 THR HG2 H 0.838 0.057 1 76 16 16 THR C C 173.665 0.000 1 77 16 16 THR CA C 57.028 0.078 1 78 16 16 THR CB C 67.263 0.084 1 79 16 16 THR CG2 C 20.863 0.096 1 80 16 16 THR N N 116.004 0.012 1 81 17 17 SER H H 8.566 0.003 1 82 17 17 SER HA H 4.476 0.080 1 83 17 17 SER HB2 H 3.906 0.106 2 84 17 17 SER HB3 H 3.689 0.016 2 85 17 17 SER CA C 58.639 0.036 1 86 17 17 SER CB C 63.087 0.073 1 87 17 17 SER N N 121.926 0.049 1 88 18 18 GLN H H 9.115 0.060 1 89 18 18 GLN HA H 3.948 0.000 1 90 18 18 GLN C C 174.237 0.000 1 91 18 18 GLN CA C 57.485 0.000 1 92 18 18 GLN CB C 29.687 0.000 1 93 18 18 GLN N N 121.238 0.101 1 94 19 19 ILE H H 6.487 0.001 1 95 19 19 ILE HA H 4.366 0.081 1 96 19 19 ILE HB H 1.213 0.073 1 97 19 19 ILE HG12 H 0.749 0.000 2 98 19 19 ILE HG13 H 0.370 0.095 2 99 19 19 ILE HG2 H 0.514 0.084 1 100 19 19 ILE HD1 H -0.102 0.084 1 101 19 19 ILE C C 173.200 0.000 1 102 19 19 ILE CA C 54.716 0.173 1 103 19 19 ILE CB C 40.058 0.134 1 104 19 19 ILE CG1 C 25.990 0.000 1 105 19 19 ILE CG2 C 15.304 0.000 1 106 19 19 ILE CD1 C 8.136 0.000 1 107 19 19 ILE N N 117.894 0.015 1 108 20 20 PRO HB2 H 2.171 0.000 1 109 20 20 PRO HB3 H 2.336 0.000 1 110 21 21 ALA H H 8.867 0.000 1 111 21 21 ALA HA H 3.917 0.073 1 112 21 21 ALA HB H 1.418 0.075 1 113 21 21 ALA C C 180.600 0.000 1 114 21 21 ALA CA C 55.908 0.023 1 115 21 21 ALA CB C 17.767 0.034 1 116 21 21 ALA N N 128.900 0.000 1 117 22 22 SER H H 8.752 0.005 1 118 22 22 SER HA H 3.841 0.091 1 119 22 22 SER HB2 H 4.038 0.090 1 120 22 22 SER C C 178.400 0.000 1 121 22 22 SER CA C 61.138 0.201 1 122 22 22 SER CB C 60.854 0.000 1 123 22 22 SER N N 111.315 0.021 1 124 23 23 GLU H H 6.949 0.001 1 125 23 23 GLU HA H 4.034 0.072 1 126 23 23 GLU HB2 H 2.132 0.086 2 127 23 23 GLU HB3 H 1.976 0.000 2 128 23 23 GLU HG2 H 2.377 0.099 2 129 23 23 GLU HG3 H 2.416 0.082 2 130 23 23 GLU C C 179.100 0.000 1 131 23 23 GLU CA C 58.515 0.071 1 132 23 23 GLU CB C 29.358 0.173 1 133 23 23 GLU CG C 36.034 0.010 1 134 23 23 GLU N N 122.700 0.000 1 135 24 24 GLN H H 7.419 0.001 1 136 24 24 GLN HA H 4.504 0.079 1 137 24 24 GLN HB2 H 2.386 0.136 2 138 24 24 GLN HB3 H 2.322 0.000 2 139 24 24 GLN HG2 H 2.367 0.000 2 140 24 24 GLN HG3 H 2.429 0.000 2 141 24 24 GLN C C 175.200 0.000 1 142 24 24 GLN CA C 57.851 0.000 1 143 24 24 GLN CB C 29.025 0.335 1 144 24 24 GLN N N 118.007 0.015 1 145 25 25 GLU H H 7.148 0.001 1 146 25 25 GLU HA H 4.296 0.000 1 147 25 25 GLU HB2 H 1.779 0.000 1 148 25 25 GLU HB3 H 1.779 0.000 1 149 25 25 GLU C C 175.500 0.000 1 150 25 25 GLU CA C 54.850 0.000 1 151 25 25 GLU CB C 29.660 0.000 1 152 25 25 GLU N N 114.406 0.015 1 153 26 26 THR H H 7.178 0.001 1 154 26 26 THR HA H 3.851 0.087 1 155 26 26 THR HB H 4.081 0.081 1 156 26 26 THR HG2 H 1.339 0.092 1 157 26 26 THR C C 172.700 0.000 1 158 26 26 THR CA C 64.750 0.058 1 159 26 26 THR CB C 69.899 0.104 1 160 26 26 THR CG2 C 21.803 0.000 1 161 26 26 THR N N 116.297 0.007 1 162 27 27 LEU H H 8.381 0.000 1 163 27 27 LEU HA H 4.800 0.070 1 164 27 27 LEU HB2 H 1.483 0.078 2 165 27 27 LEU HB3 H 1.608 0.101 2 166 27 27 LEU HG H 2.009 0.000 1 167 27 27 LEU HD1 H 0.797 0.096 1 168 27 27 LEU C C 176.600 0.000 1 169 27 27 LEU CA C 54.566 0.007 1 170 27 27 LEU CB C 42.977 0.030 1 171 27 27 LEU CD1 C 24.816 0.075 1 172 27 27 LEU CD2 C 24.558 0.000 1 173 27 27 LEU N N 128.394 0.013 1 174 28 28 VAL H H 9.682 0.003 1 175 28 28 VAL HA H 5.151 0.088 1 176 28 28 VAL HB H 1.930 0.086 1 177 28 28 VAL HG1 H 0.924 0.104 1 178 28 28 VAL HG2 H 0.705 0.100 1 179 28 28 VAL C C 173.600 0.000 1 180 28 28 VAL CA C 58.968 0.005 1 181 28 28 VAL CB C 36.828 0.027 1 182 28 28 VAL CG1 C 21.911 0.000 1 183 28 28 VAL CG2 C 17.488 0.000 1 184 28 28 VAL N N 117.407 0.015 1 185 29 29 ARG H H 9.164 0.000 1 186 29 29 ARG HA H 5.262 0.071 1 187 29 29 ARG HB2 H 1.580 0.099 1 188 29 29 ARG HG2 H 1.876 0.091 1 189 29 29 ARG HD2 H 3.049 0.091 2 190 29 29 ARG HD3 H 3.208 0.108 2 191 29 29 ARG C C 174.700 0.000 1 192 29 29 ARG CA C 52.103 0.005 1 193 29 29 ARG CB C 32.119 0.079 1 194 29 29 ARG CG C 31.983 0.000 1 195 29 29 ARG CD C 43.023 0.015 1 196 29 29 ARG N N 121.300 0.000 1 197 33 33 LEU H H 8.807 0.001 1 198 33 33 LEU HA H 4.099 0.079 1 199 33 33 LEU HB2 H 1.438 0.094 2 200 33 33 LEU HB3 H 1.655 0.072 2 201 33 33 LEU HG H 1.561 0.094 1 202 33 33 LEU HD1 H 0.865 0.091 1 203 33 33 LEU HD2 H 0.775 0.094 1 204 33 33 LEU C C 178.140 0.000 1 205 33 33 LEU CA C 57.855 0.028 1 206 33 33 LEU CB C 41.146 0.028 1 207 33 33 LEU CG C 27.076 0.000 1 208 33 33 LEU CD1 C 24.074 0.000 1 209 33 33 LEU CD2 C 23.253 0.000 1 210 33 33 LEU N N 118.497 0.007 1 211 34 34 LEU H H 7.298 0.002 1 212 34 34 LEU HA H 3.958 0.075 1 213 34 34 LEU HB2 H 1.949 0.084 1 214 34 34 LEU HB3 H 1.339 0.085 1 215 34 34 LEU HD1 H 0.410 0.003 2 216 34 34 LEU HD2 H 0.745 0.090 2 217 34 34 LEU C C 177.700 0.000 1 218 34 34 LEU CA C 56.526 0.020 1 219 34 34 LEU CB C 40.401 0.081 1 220 34 34 LEU CD1 C 23.288 0.000 1 221 34 34 LEU CD2 C 26.130 0.033 1 222 34 34 LEU N N 118.106 0.009 1 223 35 35 LEU H H 8.521 0.000 1 224 35 35 LEU HA H 3.706 0.068 1 225 35 35 LEU HB2 H 1.247 0.095 2 226 35 35 LEU HB3 H 1.897 0.105 2 227 35 35 LEU HG H 1.498 0.089 1 228 35 35 LEU HD1 H 0.938 0.093 1 229 35 35 LEU HD2 H 1.045 0.092 1 230 35 35 LEU C C 177.500 0.000 1 231 35 35 LEU CA C 57.820 0.026 1 232 35 35 LEU CB C 41.257 0.025 1 233 35 35 LEU CG C 26.982 0.020 1 234 35 35 LEU CD1 C 24.999 0.000 1 235 35 35 LEU CD2 C 23.138 0.000 1 236 35 35 LEU N N 119.900 0.000 1 237 36 36 LYS H H 7.824 0.000 1 238 36 36 LYS HA H 3.751 0.068 1 239 36 36 LYS HB2 H 1.844 0.092 2 240 36 36 LYS HB3 H 1.970 0.092 2 241 36 36 LYS HG2 H 1.576 0.092 1 242 36 36 LYS HD2 H 1.445 0.095 2 243 36 36 LYS HD3 H 1.224 0.093 2 244 36 36 LYS HE3 H 2.862 0.094 1 245 36 36 LYS C C 179.100 0.000 1 246 36 36 LYS CA C 59.338 0.033 1 247 36 36 LYS CB C 31.912 0.011 1 248 36 36 LYS CG C 29.481 0.038 1 249 36 36 LYS CD C 24.558 0.022 1 250 36 36 LYS CE C 41.485 0.000 1 251 36 36 LYS N N 118.000 0.000 1 252 37 37 LEU H H 7.230 0.000 1 253 37 37 LEU HA H 3.692 0.065 1 254 37 37 LEU HB2 H 1.237 0.091 2 255 37 37 LEU HB3 H 1.471 0.094 2 256 37 37 LEU HG H 1.050 0.001 1 257 37 37 LEU HD1 H 0.037 0.091 2 258 37 37 LEU HD2 H 0.140 0.086 2 259 37 37 LEU C C 180.200 0.000 1 260 37 37 LEU CA C 59.088 0.048 1 261 37 37 LEU CB C 40.927 0.045 1 262 37 37 LEU CG C 27.205 0.000 1 263 37 37 LEU CD1 C 26.430 0.000 1 264 37 37 LEU CD2 C 23.783 0.000 1 265 37 37 LEU N N 120.701 0.001 1 266 38 38 LEU H H 8.124 0.001 1 267 38 38 LEU HA H 3.496 0.081 1 268 38 38 LEU HB2 H 0.862 0.071 1 269 38 38 LEU HB3 H 1.628 0.092 1 270 38 38 LEU HG H 1.707 0.105 1 271 38 38 LEU HD1 H 0.203 0.092 1 272 38 38 LEU HD2 H 0.425 0.093 1 273 38 38 LEU C C 178.900 0.000 1 274 38 38 LEU CA C 57.802 0.011 1 275 38 38 LEU CB C 39.284 0.022 1 276 38 38 LEU CG C 25.946 0.000 1 277 38 38 LEU CD1 C 25.333 0.000 1 278 38 38 LEU CD2 C 22.836 0.000 1 279 38 38 LEU N N 120.600 0.001 1 280 39 39 LYS H H 8.678 0.001 1 281 39 39 LYS HA H 4.199 0.077 1 282 39 39 LYS HB2 H 1.507 0.082 2 283 39 39 LYS HB3 H 1.696 0.000 2 284 39 39 LYS HG2 H 1.231 0.089 1 285 39 39 LYS HE2 H 2.693 0.092 1 286 39 39 LYS C C 180.108 0.000 1 287 39 39 LYS CA C 59.005 0.026 1 288 39 39 LYS CB C 29.722 0.999 1 289 39 39 LYS CG C 25.508 0.000 1 290 39 39 LYS CE C 41.680 0.000 1 291 39 39 LYS N N 118.000 0.000 1 292 40 40 SER H H 7.763 0.001 1 293 40 40 SER HA H 4.304 0.107 1 294 40 40 SER HB2 H 4.152 0.105 1 295 40 40 SER C C 175.000 0.000 1 296 40 40 SER CA C 61.287 0.054 1 297 40 40 SER CB C 62.907 0.019 1 298 40 40 SER N N 116.993 0.015 1 299 41 41 VAL H H 7.143 0.000 1 300 41 41 VAL HA H 4.698 0.077 1 301 41 41 VAL HB H 2.686 0.086 1 302 41 41 VAL HG1 H 1.205 0.092 1 303 41 41 VAL HG2 H 0.982 0.094 1 304 41 41 VAL C C 175.300 0.000 1 305 41 41 VAL CA C 60.235 0.011 1 306 41 41 VAL CB C 30.615 0.032 1 307 41 41 VAL CG1 C 19.242 0.000 1 308 41 41 VAL CG2 C 21.976 0.000 1 309 41 41 VAL N N 112.903 0.007 1 310 42 42 GLY H H 7.354 0.001 1 311 42 42 GLY HA2 H 4.407 0.086 2 312 42 42 GLY HA3 H 3.661 0.097 2 313 42 42 GLY C C 174.300 0.000 1 314 42 42 GLY CA C 45.132 0.014 1 315 42 42 GLY N N 105.906 0.008 1 316 43 43 ALA H H 7.246 0.001 1 317 43 43 ALA HA H 3.944 0.086 1 318 43 43 ALA HB H 0.443 0.089 1 319 43 43 ALA C C 177.900 0.000 1 320 43 43 ALA CA C 53.000 0.115 1 321 43 43 ALA CB C 18.064 0.038 1 322 43 43 ALA N N 125.097 0.006 1 323 44 44 GLN H H 8.676 0.000 1 324 44 44 GLN N N 118.000 0.000 1 325 45 45 LYS H H 7.247 0.000 1 326 45 45 LYS N N 117.985 0.000 1 327 46 46 ASP HA H 4.461 0.001 1 328 46 46 ASP HB2 H 2.209 0.000 2 329 46 46 ASP HB3 H 2.307 0.000 2 330 46 46 ASP CA C 55.323 0.000 1 331 47 47 THR H H 6.869 0.000 1 332 47 47 THR HA H 4.951 0.075 1 333 47 47 THR HB H 3.810 0.070 1 334 47 47 THR HG2 H 1.004 0.002 1 335 47 47 THR C C 171.900 0.000 1 336 47 47 THR CA C 60.259 0.025 1 337 47 47 THR CB C 71.478 0.024 1 338 47 47 THR CG2 C 21.448 0.000 1 339 47 47 THR N N 111.306 0.014 1 340 48 48 TYR H H 8.614 0.001 1 341 48 48 TYR HA H 4.757 0.080 1 342 48 48 TYR HB2 H 3.470 0.079 2 343 48 48 TYR HB3 H 2.041 0.096 2 344 48 48 TYR C C 175.700 0.000 1 345 48 48 TYR CA C 56.966 0.037 1 346 48 48 TYR CB C 45.567 0.038 1 347 48 48 TYR N N 119.895 0.009 1 348 49 49 THR H H 8.761 0.002 1 349 49 49 THR HA H 5.361 0.089 1 350 49 49 THR HB H 4.424 0.082 1 351 49 49 THR HG2 H 1.284 0.093 1 352 49 49 THR C C 178.400 0.000 1 353 49 49 THR CA C 61.019 0.000 1 354 49 49 THR CB C 71.104 0.048 1 355 49 49 THR CG2 C 22.510 0.000 1 356 49 49 THR N N 110.720 0.260 1 357 50 50 MET H H 7.901 0.001 1 358 50 50 MET HA H 4.226 0.079 1 359 50 50 MET HB2 H 2.019 0.106 2 360 50 50 MET HB3 H 2.185 0.053 2 361 50 50 MET HG2 H 2.753 0.094 1 362 50 50 MET C C 178.300 0.000 1 363 50 50 MET CA C 57.557 0.034 1 364 50 50 MET CB C 30.037 0.107 1 365 50 50 MET CG C 32.727 0.000 1 366 50 50 MET N N 121.906 0.010 1 367 51 51 LYS H H 8.413 0.000 1 368 51 51 LYS HA H 4.327 0.085 1 369 51 51 LYS HB2 H 1.614 0.000 2 370 51 51 LYS HB3 H 1.816 0.000 2 371 51 51 LYS C C 179.100 0.000 1 372 51 51 LYS CA C 59.322 0.014 1 373 51 51 LYS CB C 32.140 0.000 1 374 51 51 LYS N N 115.600 0.000 1 375 52 52 GLU H H 7.646 0.001 1 376 52 52 GLU HA H 4.430 0.073 1 377 52 52 GLU HB2 H 2.353 0.098 1 378 52 52 GLU HB3 H 2.931 0.093 1 379 52 52 GLU HG2 H 2.433 0.101 2 380 52 52 GLU HG3 H 2.483 0.081 2 381 52 52 GLU C C 178.200 0.000 1 382 52 52 GLU CA C 58.778 0.024 1 383 52 52 GLU CB C 31.790 0.011 1 384 52 52 GLU CG C 37.089 0.009 1 385 52 52 GLU N N 120.906 0.010 1 386 53 53 VAL H H 7.972 0.000 1 387 53 53 VAL HA H 3.224 0.085 1 388 53 53 VAL HB H 2.335 0.087 1 389 53 53 VAL HG2 H 0.655 0.093 1 390 53 53 VAL C C 177.500 0.000 1 391 53 53 VAL CA C 67.425 0.032 1 392 53 53 VAL CB C 30.360 0.035 1 393 53 53 VAL CG2 C 21.577 0.000 1 394 53 53 VAL N N 120.300 0.000 1 395 54 54 LEU H H 8.063 0.001 1 396 54 54 LEU HA H 3.705 0.066 1 397 54 54 LEU HB2 H 0.867 0.105 2 398 54 54 LEU HB3 H 1.803 0.069 2 399 54 54 LEU HG H 1.646 0.095 1 400 54 54 LEU HD1 H 0.078 0.074 1 401 54 54 LEU HD2 H 0.317 0.081 1 402 54 54 LEU C C 178.900 0.000 1 403 54 54 LEU CA C 55.110 0.049 1 404 54 54 LEU CB C 39.237 0.027 1 405 54 54 LEU CG C 28.248 0.033 1 406 54 54 LEU CD1 C 24.321 0.000 1 407 54 54 LEU CD2 C 22.804 0.000 1 408 54 54 LEU N N 120.594 0.014 1 409 55 55 PHE H H 7.339 0.000 1 410 55 55 PHE HA H 3.981 0.075 1 411 55 55 PHE HB2 H 2.841 0.080 2 412 55 55 PHE HB3 H 3.120 0.071 2 413 55 55 PHE HD1 H 6.914 0.000 1 414 55 55 PHE HE1 H 6.252 0.000 1 415 55 55 PHE C C 177.900 0.000 1 416 55 55 PHE CA C 61.017 0.046 1 417 55 55 PHE CB C 38.083 0.051 1 418 55 55 PHE N N 120.300 0.000 1 419 56 56 TYR H H 8.074 0.000 1 420 56 56 TYR HA H 3.771 0.072 1 421 56 56 TYR HB2 H 2.718 0.104 1 422 56 56 TYR C C 178.200 0.000 1 423 56 56 TYR CA C 62.737 0.132 1 424 56 56 TYR CB C 38.869 0.021 1 425 56 56 TYR N N 119.500 0.000 1 426 57 57 LEU H H 8.628 0.001 1 427 57 57 LEU HA H 3.893 0.088 1 428 57 57 LEU HB2 H 1.999 0.080 2 429 57 57 LEU HB3 H 1.450 0.010 2 430 57 57 LEU HD1 H 0.514 0.108 2 431 57 57 LEU HD2 H 0.741 0.092 2 432 57 57 LEU C C 178.800 0.000 1 433 57 57 LEU CA C 57.567 0.056 1 434 57 57 LEU CB C 42.158 0.056 1 435 57 57 LEU CD1 C 23.288 0.000 1 436 57 57 LEU CD2 C 26.742 0.000 1 437 57 57 LEU N N 119.895 0.009 1 438 58 58 GLY H H 8.245 0.002 1 439 58 58 GLY HA2 H 3.579 0.088 1 440 58 58 GLY HA3 H 2.960 0.007 1 441 58 58 GLY C C 175.028 0.000 1 442 58 58 GLY CA C 47.103 0.021 1 443 58 58 GLY N N 107.015 0.018 1 444 59 59 GLN H H 7.400 0.000 1 445 59 59 GLN HA H 3.829 0.079 1 446 59 59 GLN HB2 H 1.935 0.082 2 447 59 59 GLN HB3 H 2.136 0.002 2 448 59 59 GLN C C 178.900 0.000 1 449 59 59 GLN CA C 58.023 0.064 1 450 59 59 GLN CB C 28.883 0.487 1 451 59 59 GLN N N 119.400 0.000 1 452 60 60 TYR H H 8.521 0.002 1 453 60 60 TYR HA H 3.723 0.081 1 454 60 60 TYR HB2 H 2.817 0.093 1 455 60 60 TYR HB3 H 3.312 0.080 1 456 60 60 TYR C C 175.700 0.000 1 457 60 60 TYR CA C 62.621 0.060 1 458 60 60 TYR CB C 38.069 0.028 1 459 60 60 TYR N N 123.589 0.017 1 460 61 61 ILE H H 8.240 0.003 1 461 61 61 ILE HA H 3.168 0.091 1 462 61 61 ILE HB H 1.698 0.073 1 463 61 61 ILE HG12 H 1.807 0.000 1 464 61 61 ILE HG2 H 0.666 0.092 1 465 61 61 ILE HD1 H 0.606 0.084 1 466 61 61 ILE C C 177.600 0.000 1 467 61 61 ILE CA C 65.908 0.080 1 468 61 61 ILE CB C 38.093 0.026 1 469 61 61 ILE CG1 C 24.540 0.000 1 470 61 61 ILE CG2 C 24.553 0.013 1 471 61 61 ILE CD1 C 18.640 0.000 1 472 61 61 ILE N N 118.996 0.010 1 473 62 62 MET H H 7.750 0.002 1 474 62 62 MET HA H 4.369 0.079 1 475 62 62 MET HB2 H 1.994 0.004 1 476 62 62 MET HG2 H 2.591 0.003 1 477 62 62 MET C C 180.000 0.000 1 478 62 62 MET CA C 57.270 0.061 1 479 62 62 MET CB C 30.961 0.065 1 480 62 62 MET N N 115.500 0.000 1 481 63 63 THR H H 8.423 0.001 1 482 63 63 THR HA H 3.900 0.081 1 483 63 63 THR HB H 4.059 0.092 1 484 63 63 THR HG2 H 1.182 0.108 1 485 63 63 THR C C 176.200 0.000 1 486 63 63 THR CA C 65.992 0.054 1 487 63 63 THR CB C 68.857 0.083 1 488 63 63 THR CG2 C 20.964 0.000 1 489 63 63 THR N N 117.070 0.031 1 490 64 64 LYS H H 7.678 0.001 1 491 64 64 LYS HA H 3.974 0.062 1 492 64 64 LYS HB2 H 1.557 0.095 2 493 64 64 LYS HB3 H 1.193 0.088 2 494 64 64 LYS HG2 H 1.269 0.093 2 495 64 64 LYS HG3 H 1.257 0.086 2 496 64 64 LYS HD2 H 1.225 0.000 2 497 64 64 LYS HD3 H 0.849 0.000 2 498 64 64 LYS HE2 H 2.756 0.000 1 499 64 64 LYS C C 174.500 0.000 1 500 64 64 LYS CA C 55.027 0.016 1 501 64 64 LYS CB C 30.673 0.019 1 502 64 64 LYS CG C 27.548 0.025 1 503 64 64 LYS N N 118.512 0.019 1 504 65 65 ARG H H 7.467 0.000 1 505 65 65 ARG HA H 3.791 0.074 1 506 65 65 ARG HB2 H 1.832 0.093 2 507 65 65 ARG HB3 H 1.917 0.092 2 508 65 65 ARG HG2 H 1.434 0.004 1 509 65 65 ARG HD2 H 3.101 0.000 2 510 65 65 ARG HD3 H 3.095 0.000 2 511 65 65 ARG C C 175.900 0.000 1 512 65 65 ARG CA C 56.475 0.029 1 513 65 65 ARG CB C 25.911 0.064 1 514 65 65 ARG CD C 43.002 0.000 1 515 65 65 ARG N N 115.400 0.000 1 516 66 66 LEU H H 7.612 0.005 1 517 66 66 LEU HA H 4.388 0.088 1 518 66 66 LEU HB2 H 1.280 0.006 1 519 66 66 LEU HD1 H 0.669 0.006 1 520 66 66 LEU C C 175.400 0.000 1 521 66 66 LEU CA C 54.526 0.036 1 522 66 66 LEU CB C 41.682 0.016 1 523 66 66 LEU CD1 C 26.042 0.000 1 524 66 66 LEU N N 115.591 0.018 1 525 67 67 TYR H H 7.127 0.007 1 526 67 67 TYR HA H 4.782 0.078 1 527 67 67 TYR HB2 H 2.457 0.000 2 528 67 67 TYR HB3 H 2.570 0.000 2 529 67 67 TYR C C 173.576 0.000 1 530 67 67 TYR CA C 55.334 0.063 1 531 67 67 TYR CB C 40.410 0.000 1 532 67 67 TYR N N 116.298 0.016 1 533 68 68 ASP H H 8.205 0.012 1 534 68 68 ASP C C 175.741 0.000 1 535 68 68 ASP CA C 53.209 0.000 1 536 68 68 ASP CB C 42.503 0.000 1 537 68 68 ASP N N 124.792 0.029 1 538 69 69 GLU H H 8.440 0.005 1 539 69 69 GLU HA H 3.797 0.000 1 540 69 69 GLU HB2 H 1.884 0.000 1 541 69 69 GLU HB3 H 1.884 0.000 1 542 69 69 GLU C C 176.859 0.000 1 543 69 69 GLU CA C 57.980 0.000 1 544 69 69 GLU CB C 29.260 0.000 1 545 69 69 GLU N N 123.507 0.016 1 546 70 70 LYS H H 8.208 0.002 1 547 70 70 LYS HA H 4.325 0.000 1 548 70 70 LYS HB2 H 1.698 0.000 1 549 70 70 LYS HB3 H 1.698 0.000 1 550 70 70 LYS C C 177.016 0.000 1 551 70 70 LYS CA C 57.040 0.000 1 552 70 70 LYS CB C 32.090 0.000 1 553 70 70 LYS N N 117.904 0.008 1 554 71 71 GLN H H 7.934 0.003 1 555 71 71 GLN HA H 4.325 0.000 1 556 71 71 GLN C C 175.300 0.000 1 557 71 71 GLN CA C 54.920 0.000 1 558 71 71 GLN CB C 28.850 0.000 1 559 71 71 GLN N N 118.762 0.076 1 560 72 72 GLN H H 8.051 0.001 1 561 72 72 GLN HA H 4.035 0.000 1 562 72 72 GLN C C 175.022 0.000 1 563 72 72 GLN CA C 57.210 0.000 1 564 72 72 GLN CB C 27.880 0.000 1 565 72 72 GLN N N 118.200 0.000 1 566 74 73 ILE H H 7.367 0.005 1 567 74 73 ILE HA H 4.356 0.085 1 568 74 73 ILE HB H 1.620 0.074 1 569 74 73 ILE HG12 H 0.908 0.081 2 570 74 73 ILE HG13 H 1.038 0.096 2 571 74 73 ILE HG2 H 0.133 0.076 1 572 74 73 ILE HD1 H 0.561 0.086 1 573 74 73 ILE C C 174.400 0.000 1 574 74 73 ILE CA C 58.521 0.115 1 575 74 73 ILE CB C 38.242 0.010 1 576 74 73 ILE CG1 C 26.413 0.072 1 577 74 73 ILE CG2 C 17.058 0.000 1 578 74 73 ILE CD1 C 10.160 0.000 1 579 74 73 ILE N N 120.607 0.016 1 580 75 74 VAL H H 8.274 0.000 1 581 75 74 VAL HA H 3.796 0.079 1 582 75 74 VAL HB H 0.487 0.090 1 583 75 74 VAL HG1 H 0.385 0.104 1 584 75 74 VAL HG2 H 0.266 0.094 1 585 75 74 VAL C C 174.100 0.000 1 586 75 74 VAL CA C 60.538 0.049 1 587 75 74 VAL CB C 31.759 0.027 1 588 75 74 VAL CG1 C 21.588 0.000 1 589 75 74 VAL CG2 C 22.277 0.000 1 590 75 74 VAL N N 126.197 0.006 1 591 76 75 TYR H H 8.110 0.001 1 592 76 75 TYR HA H 4.604 0.083 1 593 76 75 TYR HB2 H 3.113 0.096 2 594 76 75 TYR HB3 H 2.721 0.002 2 595 76 75 TYR C C 175.000 0.000 1 596 76 75 TYR CA C 57.648 0.019 1 597 76 75 TYR CB C 38.188 0.006 1 598 76 75 TYR N N 126.301 0.002 1 599 77 76 CYS H H 8.295 0.004 1 600 77 76 CYS HA H 4.825 0.081 1 601 77 76 CYS HB3 H 3.367 0.092 1 602 77 76 CYS C C 173.429 0.000 1 603 77 76 CYS CA C 55.361 0.055 1 604 77 76 CYS CB C 29.255 0.028 1 605 77 76 CYS N N 117.781 0.015 1 606 78 77 SER H H 7.585 0.008 1 607 78 77 SER HA H 4.225 0.083 1 608 78 77 SER HB2 H 3.852 0.083 1 609 78 77 SER CA C 60.064 0.048 1 610 78 77 SER CB C 63.122 0.073 1 611 78 77 SER N N 116.896 0.008 1 612 79 78 ASN H H 8.609 0.001 1 613 79 78 ASN HA H 4.667 0.078 1 614 79 78 ASN HB2 H 2.937 0.105 2 615 79 78 ASN HB3 H 2.691 0.088 2 616 79 78 ASN C C 172.700 0.000 1 617 79 78 ASN CA C 52.850 0.135 1 618 79 78 ASN CB C 37.796 0.065 1 619 79 78 ASN N N 118.100 0.000 1 620 80 79 ASP H H 7.549 0.000 1 621 80 79 ASP HA H 4.817 0.084 1 622 80 79 ASP HB2 H 2.329 0.089 1 623 80 79 ASP C C 174.900 0.000 1 624 80 79 ASP CA C 52.802 0.033 1 625 80 79 ASP CB C 47.221 0.029 1 626 80 79 ASP N N 118.603 0.008 1 627 81 80 LEU H H 8.411 0.001 1 628 81 80 LEU HA H 4.136 0.072 1 629 81 80 LEU HB2 H 1.499 0.082 1 630 81 80 LEU HB3 H 1.621 0.090 1 631 81 80 LEU HD1 H 0.819 0.101 2 632 81 80 LEU HD2 H 0.928 0.100 2 633 81 80 LEU C C 177.800 0.000 1 634 81 80 LEU CA C 57.666 0.007 1 635 81 80 LEU CB C 42.026 0.005 1 636 81 80 LEU CD1 C 24.757 0.000 1 637 81 80 LEU CD2 C 23.450 0.000 1 638 81 80 LEU N N 129.094 0.013 1 639 82 81 LEU H H 9.777 0.001 1 640 82 81 LEU HA H 3.499 0.075 1 641 82 81 LEU HB2 H 1.299 0.077 2 642 82 81 LEU HB3 H 1.414 0.000 2 643 82 81 LEU HG H 1.045 0.101 1 644 82 81 LEU HD1 H -0.086 0.085 1 645 82 81 LEU HD2 H 0.638 0.099 1 646 82 81 LEU C C 178.100 0.000 1 647 82 81 LEU CA C 57.811 0.005 1 648 82 81 LEU CB C 42.416 0.077 1 649 82 81 LEU CG C 26.360 0.000 1 650 82 81 LEU CD1 C 22.445 0.000 1 651 82 81 LEU CD2 C 25.990 0.000 1 652 82 81 LEU N N 118.601 0.002 1 653 83 82 GLY H H 7.592 0.000 1 654 83 82 GLY HA2 H 4.069 0.095 1 655 83 82 GLY C C 176.900 0.000 1 656 83 82 GLY CA C 47.554 0.047 1 657 83 82 GLY N N 105.800 0.000 1 658 84 83 ASP H H 7.366 0.000 1 659 84 83 ASP HA H 4.317 0.081 1 660 84 83 ASP HB2 H 2.846 0.085 2 661 84 83 ASP HB3 H 2.600 0.087 2 662 84 83 ASP C C 178.600 0.000 1 663 84 83 ASP CA C 56.580 0.005 1 664 84 83 ASP CB C 39.895 0.045 1 665 84 83 ASP N N 123.089 0.017 1 666 85 84 LEU H H 7.981 0.001 1 667 85 84 LEU HA H 4.011 0.067 1 668 85 84 LEU HB2 H 1.541 0.090 2 669 85 84 LEU HB3 H 1.365 0.080 2 670 85 84 LEU HG H 1.610 0.080 1 671 85 84 LEU HD1 H 0.541 0.100 1 672 85 84 LEU HD2 H 0.603 0.092 1 673 85 84 LEU C C 178.900 0.000 1 674 85 84 LEU CA C 56.984 0.097 1 675 85 84 LEU CB C 41.221 0.027 1 676 85 84 LEU CG C 25.989 0.000 1 677 85 84 LEU CD1 C 26.140 0.000 1 678 85 84 LEU CD2 C 23.959 0.007 1 679 85 84 LEU N N 118.800 0.000 1 680 86 85 PHE H H 8.531 0.002 1 681 86 85 PHE HA H 4.438 0.083 1 682 86 85 PHE HB2 H 3.127 0.091 2 683 86 85 PHE HB3 H 3.786 0.086 2 684 86 85 PHE C C 176.400 0.000 1 685 86 85 PHE CA C 55.833 0.074 1 686 86 85 PHE CB C 37.328 0.089 1 687 86 85 PHE N N 117.812 0.019 1 688 87 86 GLY H H 8.150 0.000 1 689 87 86 GLY HA2 H 3.916 0.084 1 690 87 86 GLY C C 173.800 0.000 1 691 87 86 GLY CA C 45.887 0.094 1 692 87 86 GLY N N 107.899 0.001 1 693 88 87 VAL H H 7.073 0.001 1 694 88 87 VAL HA H 4.927 0.075 1 695 88 87 VAL HB H 2.363 0.082 1 696 88 87 VAL HG1 H 0.745 0.092 1 697 88 87 VAL HG2 H 0.991 0.092 1 698 88 87 VAL C C 174.100 0.000 1 699 88 87 VAL CA C 56.703 0.030 1 700 88 87 VAL CB C 34.799 0.035 1 701 88 87 VAL CG1 C 18.909 0.000 1 702 88 87 VAL CG2 C 22.471 0.000 1 703 88 87 VAL N N 108.596 0.009 1 704 89 88 PRO HA H 4.342 0.000 1 705 89 88 PRO HB2 H 1.988 0.000 2 706 89 88 PRO HB3 H 2.188 0.000 2 707 89 88 PRO CA C 62.880 0.000 1 708 89 88 PRO CB C 31.620 0.000 1 709 90 89 SER H H 7.115 0.001 1 710 90 89 SER HA H 5.398 0.083 1 711 90 89 SER HB2 H 3.445 0.090 2 712 90 89 SER HB3 H 3.984 0.092 2 713 90 89 SER C C 172.300 0.000 1 714 90 89 SER CA C 56.470 0.015 1 715 90 89 SER CB C 64.481 0.121 1 716 90 89 SER N N 110.799 0.001 1 717 91 90 PHE H H 8.008 0.002 1 718 91 90 PHE HA H 4.797 0.080 1 719 91 90 PHE HB2 H 3.114 0.100 2 720 91 90 PHE HB3 H 3.212 0.099 2 721 91 90 PHE C C 171.600 0.000 1 722 91 90 PHE CA C 56.549 0.000 1 723 91 90 PHE CB C 39.765 0.014 1 724 91 90 PHE N N 112.909 0.015 1 725 92 91 SER H H 8.708 0.002 1 726 92 91 SER HA H 5.220 0.086 1 727 92 91 SER HB2 H 3.786 0.089 2 728 92 91 SER HB3 H 3.926 0.123 2 729 92 91 SER C C 177.900 0.000 1 730 92 91 SER CA C 55.256 0.082 1 731 92 91 SER CB C 63.592 0.062 1 732 92 91 SER N N 113.293 0.015 1 733 93 92 VAL H H 8.879 0.028 1 734 93 92 VAL HA H 4.333 0.073 1 735 93 92 VAL HB H 2.509 0.098 1 736 93 92 VAL HG1 H 1.030 0.095 1 737 93 92 VAL HG2 H 0.673 0.089 1 738 93 92 VAL C C 173.760 0.000 1 739 93 92 VAL CA C 63.973 0.117 1 740 93 92 VAL CB C 31.402 0.153 1 741 93 92 VAL CG1 C 18.833 0.000 1 742 93 92 VAL CG2 C 22.481 0.000 1 743 93 92 VAL N N 121.309 0.022 1 744 94 93 LYS H H 7.836 0.006 1 745 94 93 LYS HA H 4.415 0.080 1 746 94 93 LYS HB2 H 1.882 0.100 2 747 94 93 LYS HB3 H 1.481 0.065 2 748 94 93 LYS HG2 H 1.299 0.084 2 749 94 93 LYS HG3 H 1.407 0.088 2 750 94 93 LYS HD2 H 2.416 0.085 2 751 94 93 LYS HD3 H 2.569 0.109 2 752 94 93 LYS HE2 H 2.991 0.000 2 753 94 93 LYS HE3 H 3.150 0.088 2 754 94 93 LYS C C 177.300 0.000 1 755 94 93 LYS CA C 55.036 0.007 1 756 94 93 LYS CB C 32.231 0.120 1 757 94 93 LYS CG C 27.598 0.009 1 758 94 93 LYS CD C 30.968 0.000 1 759 94 93 LYS CE C 43.008 0.005 1 760 94 93 LYS N N 113.118 0.020 1 761 95 94 GLU H H 6.901 0.000 1 762 95 94 GLU HA H 4.521 0.078 1 763 95 94 GLU HB2 H 2.069 0.000 2 764 95 94 GLU HB3 H 2.252 0.077 2 765 95 94 GLU C C 176.100 0.000 1 766 95 94 GLU CA C 54.586 0.012 1 767 95 94 GLU CB C 27.942 0.023 1 768 95 94 GLU N N 119.700 0.000 1 769 96 95 HIS H H 7.568 0.006 1 770 96 95 HIS HA H 4.386 0.080 1 771 96 95 HIS HB2 H 2.861 0.100 2 772 96 95 HIS HB3 H 2.653 0.100 2 773 96 95 HIS HD2 H 6.432 0.014 1 774 96 95 HIS C C 177.300 0.000 1 775 96 95 HIS CA C 59.278 1.751 1 776 96 95 HIS CB C 30.965 0.069 1 777 96 95 HIS N N 121.512 0.019 1 778 97 96 ARG H H 9.016 0.002 1 779 97 96 ARG HA H 3.942 0.091 1 780 97 96 ARG HB2 H 1.803 0.000 1 781 97 96 ARG HB3 H 1.803 0.000 1 782 97 96 ARG C C 177.800 0.000 1 783 97 96 ARG CA C 57.432 0.083 1 784 97 96 ARG CB C 25.850 0.000 1 785 97 96 ARG N N 120.300 0.000 1 786 98 97 LYS H H 7.741 0.000 1 787 98 97 LYS HB2 H 1.866 0.000 1 788 98 97 LYS HB3 H 1.866 0.000 1 789 98 97 LYS C C 178.500 0.000 1 790 98 97 LYS CA C 60.070 0.000 1 791 98 97 LYS CB C 31.820 0.000 1 792 98 97 LYS N N 120.600 0.001 1 793 99 98 ILE H H 7.585 0.002 1 794 99 98 ILE HA H 3.052 0.083 1 795 99 98 ILE HB H 1.944 0.092 1 796 99 98 ILE HG2 H 0.594 0.093 1 797 99 98 ILE HD1 H 1.185 0.081 1 798 99 98 ILE C C 177.000 0.000 1 799 99 98 ILE CA C 65.864 0.052 1 800 99 98 ILE CB C 37.684 0.015 1 801 99 98 ILE CG2 C 15.858 1.594 1 802 99 98 ILE N N 119.394 0.015 1 803 100 99 TYR H H 8.430 0.001 1 804 100 99 TYR HA H 3.228 0.080 1 805 100 99 TYR HB2 H 2.625 0.088 2 806 100 99 TYR HB3 H 3.131 0.094 2 807 100 99 TYR HE1 H 7.062 0.000 1 808 100 99 TYR C C 176.500 0.000 1 809 100 99 TYR CA C 63.706 0.002 1 810 100 99 TYR CB C 37.142 0.080 1 811 100 99 TYR N N 121.894 0.014 1 812 101 100 THR H H 8.232 0.001 1 813 101 100 THR HA H 3.847 0.088 1 814 101 100 THR HB H 4.282 0.081 1 815 101 100 THR HG2 H 1.146 0.088 1 816 101 100 THR C C 176.100 0.000 1 817 101 100 THR CA C 67.003 0.045 1 818 101 100 THR CB C 68.496 0.042 1 819 101 100 THR CG2 C 21.308 0.000 1 820 101 100 THR N N 113.693 0.015 1 821 102 101 MET H H 7.461 0.000 1 822 102 101 MET C C 178.000 0.000 1 823 102 101 MET CA C 59.360 0.000 1 824 102 101 MET CB C 31.110 0.000 1 825 102 101 MET N N 119.500 0.000 1 826 103 102 ILE H H 7.824 0.001 1 827 103 102 ILE HA H 3.190 0.071 1 828 103 102 ILE HB H 1.258 0.081 1 829 103 102 ILE HG12 H 1.530 0.000 1 830 103 102 ILE HG2 H 0.407 0.087 1 831 103 102 ILE HD1 H 0.349 0.092 1 832 103 102 ILE C C 178.700 0.000 1 833 103 102 ILE CA C 66.114 0.051 1 834 103 102 ILE CB C 37.384 0.002 1 835 103 102 ILE CG2 C 18.629 0.000 1 836 103 102 ILE CD1 C 17.435 0.000 1 837 103 102 ILE N N 120.103 0.008 1 838 104 103 TYR H H 8.694 0.000 1 839 104 103 TYR HA H 4.102 0.077 1 840 104 103 TYR HB2 H 3.050 0.107 2 841 104 103 TYR HB3 H 3.101 0.109 2 842 104 103 TYR C C 177.300 0.000 1 843 104 103 TYR CA C 60.505 0.052 1 844 104 103 TYR CB C 37.643 0.000 1 845 104 103 TYR N N 119.500 0.000 1 846 105 104 ARG H H 6.713 0.000 1 847 105 104 ARG HA H 4.267 0.075 1 848 105 104 ARG HB2 H 1.854 0.111 2 849 105 104 ARG HB3 H 1.808 0.000 2 850 105 104 ARG HG2 H 1.682 0.083 2 851 105 104 ARG HG3 H 1.910 0.000 2 852 105 104 ARG HD2 H 3.208 0.080 1 853 105 104 ARG C C 176.500 0.000 1 854 105 104 ARG CA C 58.128 0.041 1 855 105 104 ARG CB C 30.266 0.144 1 856 105 104 ARG CG C 27.754 0.000 1 857 105 104 ARG CD C 43.421 0.000 1 858 105 104 ARG N N 114.400 0.000 1 859 106 105 ASN H H 8.396 0.000 1 860 106 105 ASN HA H 4.870 0.079 1 861 106 105 ASN HB2 H 2.540 0.092 2 862 106 105 ASN HB3 H 3.038 0.084 2 863 106 105 ASN C C 171.800 0.000 1 864 106 105 ASN CA C 53.484 0.003 1 865 106 105 ASN CB C 41.946 0.019 1 866 106 105 ASN N N 116.011 0.018 1 867 107 106 LEU H H 7.551 0.002 1 868 107 106 LEU HA H 4.850 0.099 1 869 107 106 LEU HB2 H 1.300 0.084 2 870 107 106 LEU HB3 H 1.605 0.074 2 871 107 106 LEU HG H 1.887 0.000 1 872 107 106 LEU HD1 H 0.556 0.092 1 873 107 106 LEU HD2 H 0.752 0.096 1 874 107 106 LEU C C 173.500 0.000 1 875 107 106 LEU CA C 54.230 0.050 1 876 107 106 LEU CB C 45.490 0.017 1 877 107 106 LEU CD1 C 27.227 0.000 1 878 107 106 LEU CD2 C 24.052 0.000 1 879 107 106 LEU N N 115.594 0.009 1 880 108 107 VAL H H 7.906 0.000 1 881 108 107 VAL HA H 4.350 0.081 1 882 108 107 VAL HB H 1.950 0.079 1 883 108 107 VAL HG2 H 0.882 0.086 1 884 108 107 VAL C C 175.100 0.000 1 885 108 107 VAL CA C 60.620 0.035 1 886 108 107 VAL CB C 34.322 0.048 1 887 108 107 VAL CG2 C 21.029 0.000 1 888 108 107 VAL N N 117.493 0.015 1 889 109 108 VAL H H 8.740 0.000 1 890 109 108 VAL HA H 4.014 0.081 1 891 109 108 VAL HB H 1.933 0.095 1 892 109 108 VAL HG1 H 0.846 0.000 1 893 109 108 VAL C C 176.000 0.000 1 894 109 108 VAL CA C 63.319 0.040 1 895 109 108 VAL CB C 31.909 0.013 1 896 109 108 VAL N N 128.100 0.000 1 897 110 109 VAL H H 8.283 0.001 1 898 110 109 VAL HA H 3.785 0.000 1 899 110 109 VAL HB H 1.773 0.000 1 900 110 109 VAL C C 175.300 0.000 1 901 110 109 VAL CB C 31.890 0.000 1 902 110 109 VAL N N 127.704 0.004 1 903 111 110 ASN H H 8.488 0.001 1 904 111 110 ASN HA H 4.662 0.087 1 905 111 110 ASN HB2 H 2.792 0.094 2 906 111 110 ASN HB3 H 2.711 0.093 2 907 111 110 ASN C C 174.728 0.000 1 908 111 110 ASN CA C 52.818 0.071 1 909 111 110 ASN CB C 38.664 0.052 1 910 111 110 ASN N N 122.500 0.000 1 911 112 111 GLN H H 8.366 0.002 1 912 112 111 GLN HA H 4.221 0.071 1 913 112 111 GLN HB2 H 1.866 0.108 2 914 112 111 GLN HB3 H 2.038 0.101 2 915 112 111 GLN HG2 H 2.194 0.093 2 916 112 111 GLN HG3 H 2.235 0.000 2 917 112 111 GLN C C 175.600 0.000 1 918 112 111 GLN CA C 55.958 0.001 1 919 112 111 GLN CB C 29.975 0.398 1 920 112 111 GLN CG C 35.954 0.000 1 921 112 111 GLN N N 121.700 0.000 1 922 113 112 GLN H H 8.331 0.000 1 923 113 112 GLN C C 176.200 0.000 1 924 113 112 GLN CA C 56.500 0.000 1 925 113 112 GLN CB C 30.030 0.000 1 926 113 112 GLN N N 122.200 0.000 1 927 115 114 SER H H 8.302 0.005 1 928 115 114 SER HA H 4.428 0.084 1 929 115 114 SER HB2 H 3.813 0.098 1 930 115 114 SER C C 174.412 0.000 1 931 115 114 SER CA C 57.837 0.031 1 932 115 114 SER CB C 63.574 0.127 1 933 115 114 SER N N 116.889 0.018 1 934 116 115 SER H H 8.350 0.003 1 935 116 115 SER HA H 4.489 0.122 1 936 116 115 SER C C 174.100 0.000 1 937 116 115 SER CA C 58.062 0.017 1 938 116 115 SER CB C 63.460 0.000 1 939 116 115 SER N N 118.000 0.000 1 940 117 116 ASP H H 8.274 0.001 1 941 117 116 ASP HA H 4.551 0.000 1 942 117 116 ASP HB2 H 2.569 0.000 1 943 117 116 ASP HB3 H 2.569 0.000 1 944 117 116 ASP C C 176.200 0.000 1 945 117 116 ASP CA C 54.140 0.000 1 946 117 116 ASP CB C 40.980 0.000 1 947 117 116 ASP N N 122.400 0.001 1 948 118 117 SER H H 8.210 0.000 1 949 118 117 SER HA H 4.296 0.000 1 950 118 117 SER HB2 H 3.776 0.000 1 951 118 117 SER HB3 H 3.776 0.000 1 952 118 117 SER C C 175.000 0.000 1 953 118 117 SER CA C 58.660 0.000 1 954 118 117 SER CB C 63.550 0.000 1 955 118 117 SER N N 116.593 0.015 1 956 119 118 GLY H H 8.376 0.000 1 957 119 118 GLY HA2 H 4.098 0.210 1 958 119 118 GLY HA3 H 4.098 0.210 1 959 119 118 GLY C C 174.100 0.000 1 960 119 118 GLY CA C 45.180 0.000 1 961 119 118 GLY N N 110.896 0.009 1 962 120 119 THR H H 7.932 0.000 1 963 120 119 THR HA H 4.255 0.000 1 964 120 119 THR HB H 4.107 0.000 1 965 120 119 THR C C 174.385 0.000 1 966 120 119 THR CA C 61.490 0.000 1 967 120 119 THR CB C 69.690 0.000 1 968 120 119 THR N N 113.503 0.007 1 969 121 120 SER H H 8.284 0.005 1 970 121 120 SER HA H 4.397 0.085 1 971 121 120 SER HB2 H 3.732 0.000 1 972 121 120 SER C C 174.120 0.000 1 973 121 120 SER CA C 57.876 0.043 1 974 121 120 SER CB C 63.650 0.000 1 975 121 120 SER N N 118.800 0.000 1 976 122 121 VAL H H 8.131 0.001 1 977 122 121 VAL HA H 4.101 0.074 1 978 122 121 VAL HB H 2.032 0.087 1 979 122 121 VAL HG2 H 0.865 0.092 1 980 122 121 VAL C C 175.900 0.000 1 981 122 121 VAL CA C 61.859 0.034 1 982 122 121 VAL CB C 32.315 0.074 1 983 122 121 VAL CG2 C 19.856 0.000 1 984 122 121 VAL N N 121.801 0.001 1 985 123 122 SER H H 8.277 0.004 1 986 123 122 SER HA H 4.331 0.000 1 987 123 122 SER HB2 H 3.724 0.000 1 988 123 122 SER HB3 H 3.724 0.000 1 989 123 122 SER C C 174.000 0.000 1 990 123 122 SER CA C 57.780 0.000 1 991 123 122 SER CB C 63.720 0.000 1 992 123 122 SER N N 119.593 0.010 1 993 124 123 GLU H H 8.378 0.001 1 994 124 123 GLU HA H 4.186 0.000 1 995 124 123 GLU HB2 H 1.776 0.000 2 996 124 123 GLU HB3 H 1.954 0.000 2 997 124 123 GLU C C 175.060 0.000 1 998 124 123 GLU CA C 56.200 0.000 1 999 124 123 GLU CB C 30.270 0.000 1 1000 124 123 GLU N N 123.501 0.001 1 1001 125 124 ASN H H 7.924 0.000 1 1002 125 124 ASN HA H 4.337 0.000 1 1003 125 124 ASN HB2 H 2.571 0.000 1 1004 125 124 ASN C C 179.200 0.000 1 1005 125 124 ASN CA C 54.530 0.000 1 1006 125 124 ASN CB C 40.270 0.000 1 1007 125 124 ASN N N 124.498 0.005 1 stop_ save_