data_2410 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific 1H, 15N, and 13C assignment of the N-terminal domain of the human oncoprotein MDM2 that binds to p53 ; _BMRB_accession_number 2410 _BMRB_flat_file_name bmr2410.str _Entry_type original _Submission_date 2000-04-30 _Accession_date 2000-05-01 _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 Stoll Raphael . . 2 Renner Christian . . 3 Muhlhahn Peter . . 4 Hansen Silke . . 5 Schumacher Ralf . . 6 Hesse Friederike . . 7 Kaluza Brigitte . . 8 Engh Richard A. . 9 Voelter Wolfgang . . 10 Holak Tad A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 131 "13C chemical shifts" 150 "15N chemical shifts" 83 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-16 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Sequence-specific 1H, 15N, and 13C assignment of the N-terminal domain of the human oncoprotein MDM2 that binds to p53 ; _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 Stoll Raphael . . 2 Renner Christian . . 3 Muhlhahn Peter . . 4 Hansen Silke . . 5 Schumacher Ralf . . 6 Hesse Friederike . . 7 Kaluza Brigitte . . 8 Engh Richard A. . 9 Voelter Wolfgang . . 10 Holak Tad A. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 17 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 91 _Page_last 92 _Year 2000 _Details . loop_ _Keyword 'Human MDM2' 'NMR assignments' p53 stop_ save_ ################################## # Molecular system description # ################################## save_MDM2 _Saveframe_category molecular_system _Mol_system_name 'N-terminal domain of the human oncoprotein MDM2' _Abbreviation_common MDM2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'N-terminal domain of human MDM2' $N-terminal_domain_of_human_MDM2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_N-terminal_domain_of_human_MDM2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'N-terminal domain of the human murine double minute clone 2 protein' _Abbreviation_common 'N-terminal domain of human MDM2' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 119 _Mol_residue_sequence ; MCNTNMSVPTDGAVTTSQIP ASEQETLVRPKPLLLKLLKS VGAQKDTYTMKEVLFYLGQY IMTKRLYDEKQQHIVYCSND LLGDLFGVPSFSVKEHRKIY TMIYRNLVVVNQQESSDSS ; 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 HIS 74 ILE 75 VAL 76 TYR 77 CYS 78 SER 79 ASN 80 ASP 81 LEU 82 LEU 83 GLY 84 ASP 85 LEU 86 PHE 87 GLY 88 VAL 89 PRO 90 SER 91 PHE 92 SER 93 VAL 94 LYS 95 GLU 96 HIS 97 ARG 98 LYS 99 ILE 100 TYR 101 THR 102 MET 103 ILE 104 TYR 105 ARG 106 ASN 107 LEU 108 VAL 109 VAL 110 VAL 111 ASN 112 GLN 113 GLN 114 GLU 115 SER 116 SER 117 ASP 118 SER 119 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 83.19 131 97.98 98.99 5.88e-64 BMRB 18755 entity_1 99.16 124 99.15 99.15 9.30e-78 BMRB 18876 entity_1 89.92 107 100.00 100.00 8.57e-72 PDB 1RV1 "Crystal Structure Of Human Mdm2 With An Imidazoline Inhibitor" 71.43 85 98.82 98.82 5.07e-53 PDB 1T4E "Structure Of Human Mdm2 In Complex With A Benzodiazepine Inhibitor" 79.83 96 100.00 100.00 6.28e-62 PDB 1T4F "Structure Of Human Mdm2 In Complex With An Optimized P53 Peptide" 86.55 110 99.03 99.03 2.64e-67 PDB 1YCR "Mdm2 Bound To The Transactivation Domain Of P53" 85.71 109 100.00 100.00 1.83e-67 PDB 1Z1M "Nmr Structure Of Unliganded Mdm2" 100.00 119 100.00 100.00 1.71e-81 PDB 2AXI "Hdm2 In Complex With A Beta-hairpin" 85.71 115 100.00 100.00 1.69e-67 PDB 2GV2 "Mdm2 In Complex With An 8-Mer P53 Peptide Analogue" 86.55 110 99.03 99.03 2.64e-67 PDB 2LZG "Nmr Structure Of Mdm2 (6-125) With Pip-1" 99.16 125 100.00 100.00 7.80e-81 PDB 2M86 "Solution Structure Of Hdm2 With Engineered Cyclotide" 85.71 129 100.00 100.00 1.67e-67 PDB 2MPS "Structure Of Complex Of Mdm2(3-109) And P73 Tad(10-25)" 89.92 107 100.00 100.00 8.57e-72 PDB 2RUH "Chemical Shift Assignments For Mip And Mdm2 In Bound State" 83.19 131 97.98 98.99 5.88e-64 PDB 3EQS "Crystal Structure Of Human Mdm2 In Complex With A 12-Mer Peptide Inhibitor" 71.43 85 100.00 100.00 4.88e-54 PDB 3G03 "Structure Of Human Mdm2 In Complex With High Affinity Peptide" 85.71 109 99.02 99.02 9.16e-67 PDB 3IUX "Crystal Structure Of Human Mdm2 In Complex With A Potent Miniature Protein Inhibitor (18-Residues)" 71.43 85 100.00 100.00 4.88e-54 PDB 3IWY "Crystal Structure Of Human Mdm2 Complexed With D-peptide (12 Residues)" 71.43 85 100.00 100.00 4.88e-54 PDB 3JZK "Crystal Structure Of Mdm2 With Chromenotriazolopyrimidine 1" 79.83 96 100.00 100.00 6.28e-62 PDB 3JZR "Human Mdm2 Liganded With A 12mer Peptide Inhibitor (Pdi6w)" 86.55 110 99.03 99.03 2.64e-67 PDB 3JZS "Human Mdm2 Liganded With A 12mer Peptide Inhibitor (Pdiq)" 72.27 86 100.00 100.00 6.15e-55 PDB 3LBK "Structure Of Human Mdm2 Protein In Complex With A Small Molecule Inhibitor" 78.99 95 98.94 98.94 2.34e-60 PDB 3LBL "Structure Of Human Mdm2 Protein In Complex With Mi-63-Analog" 78.99 95 100.00 100.00 2.18e-61 PDB 3LNJ "Crystal Structure Of Human Mdm2 In Complex With D-Peptide Inhibitor (Dpmi-Alpha)" 71.43 85 100.00 100.00 4.88e-54 PDB 3LNZ "Crystal Structure Of Human Mdm2 With A 12-Mer Peptide Inhibitor Pmi (N8a Mutant)" 71.43 85 100.00 100.00 4.88e-54 PDB 3TJ2 "Structure Of A Novel Submicromolar Mdm2 Inhibitor" 78.99 95 100.00 100.00 2.18e-61 PDB 3TPX "Crystal Structure Of Human Mdm2 In Complex With A Trifluoromethylated D-peptide Inhibitor" 71.43 85 100.00 100.00 4.88e-54 PDB 3TU1 "Exhaustive Fluorine Scanning Towards Potent P53-Mdm2 Antagonist" 85.71 108 99.02 99.02 8.79e-67 PDB 3V3B "Structure Of The Stapled P53 Peptide Bound To Mdm2" 73.11 88 100.00 100.00 1.65e-55 PDB 3VBG "Structure Of Hdm2 With Dimer Inducing Indolyl Hydantoin Ro-2443" 71.43 85 98.82 98.82 5.07e-53 PDB 3VZV "Crystal Structure Of Human Mdm2 With A Dihydroimidazothiazole Inhibitor" 71.43 87 98.82 98.82 5.03e-53 PDB 3W69 "Crystal Structure Of Human Mdm2 With A Dihydroimidazothiazole Inhibitor" 71.43 87 98.82 98.82 5.03e-53 PDB 4DIJ "The Central Valine Concept Provides An Entry In A New Class Of Non Peptide Inhibitors Of The P53-Mdm2 Interaction" 79.83 96 98.95 98.95 7.37e-61 PDB 4ERE "Crystal Structure Of Mdm2 (17-111) In Complex With Compound 23" 79.83 96 100.00 100.00 6.28e-62 PDB 4ERF "Crystal Structure Of Mdm2 (17-111) In Complex With Compound 29 (Am- 8553)" 79.83 96 100.00 100.00 6.28e-62 PDB 4HBM "Ordering Of The N Terminus Of Human Mdm2 By Small Molecule Inhibitors" 94.96 120 100.00 100.00 3.35e-76 PDB 4HFZ "Crystal Structure Of An Mdm2/p53 Peptide Complex" 85.71 109 98.04 98.04 5.91e-66 PDB 4JV7 "Co-crystal Structure Of Mdm2 With Inhibitor (2s,5r,6s)-2-benzyl-5,6- Bis(4-bromophenyl)-4-methylmorpholin-3-one" 78.99 96 100.00 100.00 2.59e-61 PDB 4JV9 "Co-crystal Structure Of Mdm2 With Inhibitor (2s,5r,6s)-2-benzyl-5,6- Bis(4-chlorophenyl)-4-methylmorpholin-3-one" 78.99 96 100.00 100.00 2.59e-61 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-" 78.99 96 100.00 100.00 2.59e-61 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" 78.99 96 100.00 100.00 2.59e-61 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- " 79.83 95 100.00 100.00 5.58e-62 PDB 4MDN "Structure Of A Novel Submicromolar Mdm2 Inhibitor" 78.15 94 100.00 100.00 2.04e-60 PDB 4MDQ "Structure Of A Novel Submicromolar Mdm2 Inhibitor" 72.27 86 100.00 100.00 1.05e-54 PDB 4OAS "Co-crystal Structure Of Mdm2 (17-111) In Complex With Compound 25" 79.83 96 100.00 100.00 6.28e-62 PDB 4OBA "Co-crystal Structure Of Mdm2 With Inhibitor Compound 4" 79.83 96 100.00 100.00 6.28e-62 PDB 4OCC "Co-crystal Structure Of Mdm2(17-111) In Complex With Compound 48" 79.83 96 100.00 100.00 6.28e-62 PDB 4ODE "Co-crystal Structure Of Mdm2 With Inhibitor Compound 4" 88.24 105 100.00 100.00 8.31e-70 PDB 4ODF "Co-crystal Structure Of Mdm2 With Inhibitor Compound 47" 88.24 105 100.00 100.00 8.31e-70 PDB 4OGN "Co-crystal Structure Of Mdm2 With Inhbitor Compound 3" 88.24 105 100.00 100.00 8.31e-70 PDB 4OGT "Co-crystal Structure Of Mdm2 With Inhbitor Compound 46" 88.24 105 100.00 100.00 8.31e-70 PDB 4OGV "Co-crystal Structure Of Mdm2 With Inhibitor Compound 49" 79.83 95 100.00 100.00 5.58e-62 PDB 4OQ3 "Tetra-substituted Imidazoles As A New Class Of Inhibitors Of The P53- Mdm2 Interaction" 79.83 96 98.95 98.95 7.37e-61 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" 79.83 96 100.00 100.00 6.28e-62 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" 79.83 96 100.00 100.00 6.28e-62 PDB 4UMN "Structure Of A Stapled Peptide Antagonist Bound To Nutlin- Resistant Mdm2" 94.96 120 99.12 99.12 2.81e-75 PDB 4WT2 "Co-crystal Structure Of Mdm2 In Complex With Am-7209" 88.24 105 100.00 100.00 8.31e-70 PDB 4ZYC "Discovery Of Dihydroisoquinolinone Derivatives As Novel Inhibitors Of The P53-mdm2 Interaction With A Distinct Binding Mode: Hd" 79.83 96 98.95 98.95 7.37e-61 PDB 4ZYF "Discovery Of Nvp-cgm097 - A Highly Potent And Selective Mdm2 Inhibitor Undergoing Phase 1 Clinical Trials In P53wt Tumors: Hdm2" 79.83 96 100.00 100.00 6.28e-62 PDB 4ZYI "Discovery Of Nvp-cgm097 - A Highly Potent And Selective Mdm2 Inhibitor Undergoing Phase 1 Clinical Trials In P53wt Tumors: Hdm2" 79.83 96 100.00 100.00 6.28e-62 DBJ BAF83030 "unnamed protein product [Homo sapiens]" 99.16 491 100.00 100.00 3.65e-77 DBJ BAJ17752 "Mdm2 p53 binding protein homolog [synthetic construct]" 99.16 497 100.00 100.00 3.92e-77 EMBL CAA78055 "p53 associated [Homo sapiens]" 99.16 491 100.00 100.00 3.65e-77 EMBL CAD23251 "MDM2 isoform KB9 [Homo sapiens]" 99.16 243 100.00 100.00 3.02e-79 EMBL CAD36959 "p53-binding protein [Homo sapiens]" 100.00 166 99.16 99.16 4.54e-80 EMBL CAD79457 "HDM2-HD3 protein [Homo sapiens]" 51.26 69 100.00 100.00 8.92e-35 EMBL CAH89564 "hypothetical protein [Pongo abelii]" 99.16 497 100.00 100.00 4.09e-77 GB AAA60568 "p53 associated [Homo sapiens]" 99.16 491 100.00 100.00 3.65e-77 GB AAI48523 "Mdm2 p53 binding protein homolog (mouse), partial [synthetic construct]" 99.16 497 100.00 100.00 3.92e-77 GB AAI52385 "MDM2 protein, partial [Homo sapiens]" 99.16 490 100.00 100.00 3.38e-77 GB AAI52391 "MDM2 protein, partial [Homo sapiens]" 99.16 490 100.00 100.00 3.38e-77 GB AAI53118 "Mdm2 p53 binding protein homolog (mouse) [synthetic construct]" 99.16 497 100.00 100.00 3.92e-77 PRF 1814460A "p53-associated protein" 99.16 491 100.00 100.00 3.65e-77 REF NP_001124685 "E3 ubiquitin-protein ligase Mdm2 [Pongo abelii]" 99.16 497 100.00 100.00 4.09e-77 REF NP_001138809 "E3 ubiquitin-protein ligase Mdm2 isoform g [Homo sapiens]" 99.16 444 100.00 100.00 1.55e-77 REF NP_001138811 "E3 ubiquitin-protein ligase Mdm2 isoform h [Homo sapiens]" 95.80 442 100.00 100.00 6.24e-75 REF NP_001253331 "E3 ubiquitin-protein ligase Mdm2 [Macaca mulatta]" 99.16 497 100.00 100.00 3.52e-77 REF NP_002383 "E3 ubiquitin-protein ligase Mdm2 isoform a [Homo sapiens]" 99.16 497 100.00 100.00 3.92e-77 SP Q00987 "RecName: Full=E3 ubiquitin-protein ligase Mdm2; AltName: Full=Double minute 2 protein; Short=Hdm2; AltName: Full=Oncoprotein Md" 99.16 491 100.00 100.00 3.65e-77 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $N-terminal_domain_of_human_MDM2 Human 9606 Eukaryota Metazoa Homo sapiens 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 $N-terminal_domain_of_human_MDM2 '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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $N-terminal_domain_of_human_MDM2 . mM 0.1 0.5 [U-15N] stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $N-terminal_domain_of_human_MDM2 . mM 0.1 0.5 '[U-15N; U-13C]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 0.2 n/a temperature 300 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation H2O H 1 protons ppm 4.73 internal direct . internal . . $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_2 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'N-terminal domain of human MDM2' _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 . 7 SER CA C 56.64 0.05 1 2 . 7 SER CB C 61.87 0.05 1 3 . 8 VAL H H 8.07 0.02 1 4 . 8 VAL HA H 4.42 0.02 1 5 . 8 VAL CA C 58.09 0.05 1 6 . 8 VAL N N 124.63 0.05 1 7 . 9 PRO CA C 61.56 0.05 1 8 . 9 PRO CB C 30.29 0.05 1 9 . 10 THR H H 8.17 0.02 1 10 . 10 THR CA C 60.22 0.05 1 11 . 10 THR CB C 67.85 0.05 1 12 . 10 THR N N 116.30 0.05 1 13 . 11 ASP H H 8.27 0.02 1 14 . 11 ASP CA C 52.78 0.05 1 15 . 11 ASP CB C 39.32 0.05 1 16 . 11 ASP N N 124.24 0.05 1 17 . 12 GLY H H 8.26 0.02 1 18 . 12 GLY CA C 43.84 0.05 1 19 . 12 GLY N N 110.94 0.05 1 20 . 13 ALA H H 8.03 0.02 1 21 . 13 ALA CA C 50.89 0.05 1 22 . 13 ALA CB C 17.38 0.05 1 23 . 13 ALA N N 125.20 0.05 1 24 . 14 VAL H H 8.05 0.02 1 25 . 14 VAL CA C 60.61 0.05 1 26 . 14 VAL CB C 29.26 0.05 1 27 . 14 VAL N N 120.79 0.05 1 28 . 15 THR H H 8.22 0.02 1 29 . 15 THR CA C 57.08 0.05 1 30 . 15 THR N N 119.39 0.05 1 31 . 21 ALA CB C 16.58 0.05 1 32 . 22 SER H H 8.44 0.02 1 33 . 22 SER CA C 58.49 0.05 1 34 . 22 SER N N 113.40 0.05 1 35 . 25 GLU CA C 53.99 0.05 1 36 . 25 GLU CB C 27.91 0.05 1 37 . 26 THR H H 7.56 0.02 1 38 . 26 THR HA H 4.41 0.02 1 39 . 26 THR CA C 62.88 0.05 1 40 . 26 THR CB C 68.36 0.05 1 41 . 26 THR N N 119.46 0.05 1 42 . 27 LEU H H 8.46 0.02 1 43 . 27 LEU HA H 3.96 0.02 1 44 . 27 LEU CA C 52.9 0.05 1 45 . 27 LEU CB C 41.19 0.05 1 46 . 27 LEU N N 130.06 0.05 1 47 . 28 VAL H H 9.70 0.02 1 48 . 28 VAL HA H 4.84 0.02 1 49 . 28 VAL CA C 57.37 0.05 1 50 . 28 VAL N N 118.32 0.05 1 51 . 29 ARG H H 9.20 0.02 1 52 . 29 ARG HA H 5.09 0.02 1 53 . 29 ARG CA C 50.74 0.05 1 54 . 29 ARG N N 123.69 0.05 1 55 . 33 LEU H H 8.85 0.02 1 56 . 33 LEU CA C 56.65 0.05 1 57 . 33 LEU CB C 39.53 0.05 1 58 . 33 LEU N N 120.36 0.05 1 59 . 34 LEU H H 7.38 0.02 1 60 . 34 LEU CA C 55.00 0.05 1 61 . 34 LEU CB C 38.78 0.05 1 62 . 34 LEU N N 120.13 0.05 1 63 . 35 LEU H H 8.55 0.02 1 64 . 35 LEU CA C 56.44 0.05 1 65 . 35 LEU N N 122.29 0.05 1 66 . 36 LYS CB C 30.28 0.05 1 67 . 37 LEU H H 7.29 0.02 1 68 . 37 LEU HA H 3.68 0.02 1 69 . 37 LEU CB C 39.21 0.05 1 70 . 37 LEU N N 123.00 0.05 1 71 . 38 LEU H H 8.16 0.02 1 72 . 38 LEU CA C 56.24 0.05 1 73 . 38 LEU CB C 37.81 0.05 1 74 . 38 LEU N N 122.23 0.05 1 75 . 39 LYS H H 8.80 0.02 1 76 . 39 LYS HA H 4.22 0.02 1 77 . 39 LYS CA C 57.61 0.05 1 78 . 39 LYS CB C 30.21 0.05 1 79 . 39 LYS N N 120.16 0.05 1 80 . 40 SER H H 7.86 0.02 1 81 . 40 SER HA H 4.37 0.02 1 82 . 40 SER CA C 60.04 0.05 1 83 . 40 SER CB C 61.48 0.05 1 84 . 40 SER N N 118.50 0.05 1 85 . 41 VAL H H 7.26 0.02 1 86 . 41 VAL HA H 4.76 0.02 1 87 . 41 VAL CA C 58.76 0.05 1 88 . 41 VAL CB C 28.79 0.05 1 89 . 41 VAL N N 114.35 0.05 1 90 . 42 GLY H H 7.50 0.02 1 91 . 42 GLY HA2 H 4.37 0.02 2 92 . 42 GLY N N 107.97 0.05 1 93 . 43 ALA H H 7.36 0.02 1 94 . 43 ALA HA H 4.21 0.02 1 95 . 43 ALA CA C 51.50 0.05 1 96 . 43 ALA CB C 16.42 0.05 1 97 . 43 ALA N N 126.95 0.05 1 98 . 44 GLN H H 8.69 0.02 1 99 . 44 GLN CA C 54.07 0.05 1 100 . 44 GLN CB C 27.46 0.05 1 101 . 44 GLN N N 120.22 0.05 1 102 . 45 LYS H H 7.72 0.02 1 103 . 45 LYS CA C 58.66 0.05 1 104 . 45 LYS N N 118.13 0.05 1 105 . 46 ASP CA C 53.44 0.05 1 106 . 46 ASP CB C 40.33 0.05 1 107 . 47 THR H H 6.99 0.02 1 108 . 47 THR HA H 4.96 0.02 1 109 . 47 THR CA C 58.80 0.05 1 110 . 47 THR CB C 69.69 0.05 1 111 . 47 THR N N 112.77 0.05 1 112 . 48 TYR H H 8.73 0.02 1 113 . 48 TYR CA C 55.513 0.05 1 114 . 48 TYR CB C 43.51 0.05 1 115 . 48 TYR N N 121.87 0.05 1 116 . 49 THR H H 8.95 0.02 1 117 . 49 THR HA H 4.85 0.02 1 118 . 49 THR CA C 59.27 0.05 1 119 . 49 THR N N 112.35 0.05 1 120 . 50 MET H H 8.35 0.02 1 121 . 50 MET CA C 55.79 0.05 1 122 . 50 MET CB C 28.49 0.05 1 123 . 50 MET N N 123.58 0.05 1 124 . 51 LYS H H 8.50 0.02 1 125 . 51 LYS HA H 4.01 0.02 1 126 . 51 LYS CA C 58.28 0.05 1 127 . 51 LYS CB C 32.56 0.05 1 128 . 51 LYS N N 119.49 0.05 1 129 . 52 GLU H H 7.87 0.02 1 130 . 52 GLU HA H 4.08 0.02 1 131 . 52 GLU CA C 57.76 0.05 1 132 . 52 GLU CB C 29.53 0.05 1 133 . 52 GLU N N 122.09 0.05 1 134 . 53 VAL H H 8.26 0.02 1 135 . 53 VAL CA C 66.27 0.05 1 136 . 53 VAL N N 121.45 0.05 1 137 . 54 LEU H H 8.28 0.02 1 138 . 54 LEU CA C 56.33 0.05 1 139 . 54 LEU CB C 38.89 0.05 1 140 . 54 LEU N N 120.44 0.05 1 141 . 55 PHE H H 8.08 0.02 1 142 . 55 PHE HA H 4.17 0.02 1 143 . 55 PHE CA C 59.70 0.05 1 144 . 55 PHE CB C 36.51 0.05 1 145 . 55 PHE N N 123.77 0.05 1 146 . 56 TYR H H 8.55 0.02 1 147 . 56 TYR HA H 4.04 0.02 1 148 . 56 TYR CA C 61.19 0.05 1 149 . 56 TYR CB C 36.78 0.05 1 150 . 56 TYR N N 121.86 0.05 1 151 . 57 LEU H H 8.82 0.02 1 152 . 57 LEU CA C 56.64 0.05 1 153 . 57 LEU CB C 39.87 0.05 1 154 . 57 LEU N N 123.03 0.05 1 155 . 58 GLY H H 8.20 0.02 1 156 . 58 GLY HA2 H 3.96 0.02 2 157 . 58 GLY HA3 H 3.74 0.02 2 158 . 58 GLY CA C 45.85 0.05 1 159 . 58 GLY N N 107.86 0.05 1 160 . 59 GLN H H 7.76 0.02 1 161 . 59 GLN HA H 3.95 0.02 1 162 . 59 GLN CA C 56.67 0.05 1 163 . 59 GLN CB C 26.43 0.05 1 164 . 59 GLN N N 122.36 0.05 1 165 . 60 TYR H H 8.76 0.02 1 166 . 60 TYR HA H 3.81 0.02 1 167 . 60 TYR CA C 61.14 0.05 1 168 . 60 TYR N N 126.27 0.05 1 169 . 61 ILE H H 8.39 0.02 1 170 . 61 ILE HA H 3.42 0.02 1 171 . 61 ILE CA C 64.41 0.05 1 172 . 61 ILE CB C 36.78 0.05 1 173 . 61 ILE N N 120.64 0.05 1 174 . 62 MET H H 8.01 0.02 1 175 . 62 MET HA H 4.41 0.02 1 176 . 62 MET CA C 56.65 0.05 1 177 . 62 MET CB C 30.35 0.05 1 178 . 62 MET N N 117.71 0.05 1 179 . 63 THR H H 8.57 0.02 1 180 . 63 THR HA H 4.11 0.02 1 181 . 63 THR CA C 64.62 0.05 1 182 . 63 THR CB C 66.83 0.05 1 183 . 63 THR N N 117.93 0.05 1 184 . 64 LYS H H 7.81 0.02 1 185 . 64 LYS HA H 4.09 0.02 1 186 . 64 LYS CA C 54.03 0.05 1 187 . 64 LYS CB C 29.03 0.05 1 188 . 64 LYS N N 120.42 0.05 1 189 . 65 ARG H H 7.60 0.02 1 190 . 65 ARG HA H 3.73 0.02 1 191 . 65 ARG CA C 55.12 0.05 1 192 . 65 ARG CB C 24.73 0.05 1 193 . 65 ARG N N 118.00 0.05 1 194 . 66 LEU H H 7.63 0.02 1 195 . 66 LEU HA H 4.39 0.02 1 196 . 66 LEU CA C 53.20 0.05 1 197 . 66 LEU N N 116.96 0.05 1 198 . 67 TYR H H 8.74 0.02 1 199 . 67 TYR HA H 5.06 0.02 1 200 . 67 TYR CA C 53.45 0.05 1 201 . 67 TYR CB C 37.56 0.05 1 202 . 67 TYR N N 126.27 0.05 1 203 . 68 ASP H H 8.57 0.02 1 204 . 68 ASP HA H 4.45 0.02 1 205 . 68 ASP CA C 52.54 0.05 1 206 . 68 ASP CB C 40.93 0.05 1 207 . 68 ASP N N 125.30 0.05 1 208 . 69 GLU H H 8.57 0.02 1 209 . 69 GLU HA H 3.96 0.02 1 210 . 69 GLU CA C 57.59 0.05 1 211 . 69 GLU CB C 28.23 0.05 1 212 . 69 GLU N N 125.89 0.05 1 213 . 70 LYS H H 8.25 0.02 1 214 . 70 LYS HA H 4.37 0.02 1 215 . 70 LYS CA C 55.44 0.05 1 216 . 70 LYS CB C 31.56 0.05 1 217 . 70 LYS N N 118.53 0.05 1 218 . 71 GLN H H 8.37 0.02 1 219 . 71 GLN CA C 52.51 0.05 1 220 . 71 GLN CB C 29.23 0.05 1 221 . 71 GLN N N 122.94 0.05 1 222 . 72 GLN H H 8.22 0.02 1 223 . 72 GLN HA H 4.36 0.02 1 224 . 72 GLN CA C 57.18 0.05 1 225 . 72 GLN CB C 25.34 0.05 1 226 . 72 GLN N N 120.76 0.05 1 227 . 73 HIS H H 7.76 0.02 1 228 . 73 HIS HA H 4.55 0.02 1 229 . 73 HIS CA C 54.18 0.05 1 230 . 73 HIS CB C 28.75 0.05 1 231 . 73 HIS N N 114.08 0.05 1 232 . 74 ILE H H 7.69 0.02 1 233 . 74 ILE CA C 58.15 0.05 1 234 . 74 ILE CB C 34.95 0.05 1 235 . 74 ILE N N 124.60 0.05 1 236 . 75 VAL H H 8.34 0.02 1 237 . 75 VAL CA C 59.01 0.05 1 238 . 75 VAL CB C 30.70 0.05 1 239 . 75 VAL N N 128.08 0.05 1 240 . 76 TYR H H 8.31 0.02 1 241 . 76 TYR CA C 55.75 0.05 1 242 . 76 TYR CB C 36.53 0.05 1 243 . 76 TYR N N 127.85 0.05 1 244 . 77 CYS H H 8.38 0.02 1 245 . 77 CYS CA C 54.25 0.05 1 246 . 77 CYS N N 118.95 0.05 1 247 . 81 LEU CA C 56.30 0.05 1 248 . 81 LEU CB C 40.41 0.05 1 249 . 82 LEU H H 9.80 0.02 1 250 . 82 LEU HA H 3.60 0.02 1 251 . 82 LEU CA C 56.74 0.05 1 252 . 82 LEU CB C 40.79 0.05 1 253 . 82 LEU N N 120.48 0.05 1 254 . 83 GLY H H 7.78 0.02 1 255 . 83 GLY HA2 H 4.09 0.02 1 256 . 83 GLY HA3 H 4.09 0.02 1 257 . 83 GLY CA C 46.18 0.05 1 258 . 83 GLY N N 108.28 0.05 1 259 . 84 ASP H H 7.52 0.02 1 260 . 84 ASP HA H 4.40 0.02 1 261 . 84 ASP CA C 55.13 0.05 1 262 . 84 ASP CB C 38.34 0.05 1 263 . 84 ASP N N 124.97 0.05 1 264 . 85 LEU H H 8.07 0.02 1 265 . 85 LEU CA C 55.69 0.05 1 266 . 85 LEU N N 120.84 0.05 1 267 . 86 PHE H H 8.38 0.02 1 268 . 86 PHE CB C 36.39 0.05 1 269 . 86 PHE N N 118.28 0.05 1 270 . 87 GLY H H 8.27 0.02 1 271 . 87 GLY HA2 H 4.61 0.02 1 272 . 87 GLY HA3 H 4.61 0.02 1 273 . 87 GLY CA C 44.81 0.05 1 274 . 87 GLY N N 109.90 0.05 1 275 . 88 VAL H H 7.09 0.02 1 276 . 88 VAL HA H 4.97 0.02 1 277 . 88 VAL CA C 55.28 0.05 1 278 . 88 VAL N N 110.31 0.05 1 279 . 89 PRO CA C 61.59 0.05 1 280 . 89 PRO CB C 30.04 0.05 1 281 . 90 SER H H 7.23 0.02 1 282 . 90 SER HA H 5.43 0.02 1 283 . 90 SER CA C 54.97 0.05 1 284 . 90 SER CB C 63.20 0.05 1 285 . 90 SER N N 113.11 0.05 1 286 . 91 PHE H H 8.23 0.02 1 287 . 91 PHE CA C 55.11 0.05 1 288 . 91 PHE CB C 37.56 0.05 1 289 . 91 PHE N N 116.50 0.05 1 290 . 92 SER H H 8.70 0.02 1 291 . 92 SER CA C 52.77 0.05 1 292 . 92 SER CB C 62.36 0.05 1 293 . 92 SER N N 114.52 0.05 1 294 . 93 VAL H H 9.44 0.02 1 295 . 93 VAL HA H 5.56 0.02 1 296 . 93 VAL CA C 62.08 0.05 1 297 . 93 VAL CB C 29.50 0.05 1 298 . 93 VAL N N 125.07 0.05 1 299 . 94 LYS H H 7.99 0.02 1 300 . 94 LYS HA H 4.12 0.02 1 301 . 94 LYS CA C 55.00 0.05 1 302 . 94 LYS CB C 30.58 0.05 1 303 . 94 LYS N N 118.24 0.05 1 304 . 95 GLU H H 7.39 0.02 1 305 . 95 GLU HA H 4.49 0.02 1 306 . 95 GLU CA C 52.94 0.05 1 307 . 95 GLU CB C 25.65 0.05 1 308 . 95 GLU N N 122.03 0.05 1 309 . 96 HIS H H 7.59 0.02 1 310 . 96 HIS CA C 58.33 0.05 1 311 . 96 HIS N N 122.62 0.05 1 312 . 97 ARG CA C 56.64 0.05 1 313 . 97 ARG CB C 26.11 0.05 1 314 . 98 LYS H H 7.71 0.02 1 315 . 98 LYS HA H 3.97 0.02 1 316 . 98 LYS CA C 58.02 0.05 1 317 . 98 LYS N N 122.63 0.05 1 318 . 99 ILE H H 7.92 0.02 1 319 . 99 ILE CA C 63.54 0.05 1 320 . 99 ILE N N 120.88 0.05 1 321 . 100 TYR H H 8.48 0.02 1 322 . 100 TYR CA C 61.01 0.05 1 323 . 100 TYR CB C 35.43 0.05 1 324 . 100 TYR N N 122.55 0.05 1 325 . 101 THR H H 8.09 0.02 1 326 . 101 THR CA C 65.46 0.05 1 327 . 101 THR N N 115.80 0.05 1 328 . 102 MET H H 7.66 0.02 1 329 . 102 MET CA C 57.94 0.05 1 330 . 102 MET N N 121.89 0.05 1 331 . 103 ILE CA C 63.94 0.05 1 332 . 103 ILE CB C 39.12 0.05 1 333 . 104 TYR H H 8.77 0.02 1 334 . 104 TYR CA C 59.55 0.05 1 335 . 104 TYR N N 121.77 0.05 1 336 . 107 LEU H H 8.36 0.02 1 337 . 107 LEU N N 130.74 0.05 1 338 . 108 VAL H H 8.68 0.02 5 339 . 108 VAL HA H 4.29 0.02 5 340 . 108 VAL N N 129.42 0.05 5 341 . 109 VAL H H 8.68 0.02 5 342 . 109 VAL HA H 4.29 0.02 5 343 . 109 VAL N N 129.42 0.05 5 344 . 110 VAL H H 8.40 0.02 1 345 . 110 VAL HA H 4.11 0.02 1 346 . 110 VAL CA C 61.32 0.05 1 347 . 110 VAL CB C 30.66 0.05 1 348 . 110 VAL N N 129.05 0.05 1 349 . 111 ASN H H 8.24 0.02 1 350 . 111 ASN CA C 55.05 0.05 1 351 . 111 ASN N N 125.14 0.05 1 352 . 116 SER CA C 56.60 0.05 1 353 . 116 SER CB C 62.03 0.05 1 354 . 117 ASP H H 8.35 0.02 1 355 . 117 ASP CA C 52.78 0.05 1 356 . 117 ASP CB C 39.11 0.05 1 357 . 117 ASP N N 124.33 0.05 1 358 . 118 SER H H 8.20 0.02 1 359 . 118 SER CA C 56.62 0.05 1 360 . 118 SER CB C 62.08 0.05 1 361 . 118 SER N N 118.08 0.05 1 362 . 119 SER H H 7.99 0.02 1 363 . 119 SER CA C 58.50 0.05 1 364 . 119 SER N N 125.40 0.05 1 stop_ save_