data_15945 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; MDM2 N-terminal domain ; _BMRB_accession_number 15945 _BMRB_flat_file_name bmr15945.str _Entry_type original _Submission_date 2008-09-08 _Accession_date 2008-09-08 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details '1H, 15N, C-alpha and C-beta assignments of human MDM2 residues 17-125' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Riedinger Christiane . . 2 Mcdonnell James M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 193 "13C chemical shifts" 203 "15N chemical shifts" 101 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-03-03 update BMRB 'complete entry citation' 2008-10-13 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Analysis of chemical shift changes reveals the binding modes of isoindolinone inhibitors of the MDM2-p53 interaction' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18959403 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Riedinger Christiane . . 2 Endicott Jane A. . 3 Kemp Stuart J. . 4 Smyth Lynette A. . 5 Watson Anna . . 6 Valeur Eric . . 7 Golding Bernard T. . 8 Griffin Roger J. . 9 Hardcastle Ian R. . 10 Noble Martin E. . 11 McDonnell James M. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_volume 130 _Journal_issue 47 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 16038 _Page_last 16044 _Year 2008 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'MDM2 N-terminal domain, residues 17-125' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'N-terminal domain, p53 binding domain' $human_mdm2_N-terminal_domain stop_ _System_molecular_weight 12931.8 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_human_mdm2_N-terminal_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common human_mdm2_N-terminal_domain _Molecular_mass 12931.8 _Mol_thiol_state 'all free' loop_ _Biological_function 'p53-binding domain' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 114 _Mol_residue_sequence ; GPLGSSQIPASEQETLVRPK PLLLKLLKSVGAQKDTYTMK EVLFYLGQYIMTKRLYDEKQ QHIVYCSNDLLGDLFGVPSF SVKEHRKIYTMIYRNLVVVN QQESSDSGTSVSEN ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 12 GLY 2 13 PRO 3 14 LEU 4 15 GLY 5 16 SER 6 17 SER 7 18 GLN 8 19 ILE 9 20 PRO 10 21 ALA 11 22 SER 12 23 GLU 13 24 GLN 14 25 GLU 15 26 THR 16 27 LEU 17 28 VAL 18 29 ARG 19 30 PRO 20 31 LYS 21 32 PRO 22 33 LEU 23 34 LEU 24 35 LEU 25 36 LYS 26 37 LEU 27 38 LEU 28 39 LYS 29 40 SER 30 41 VAL 31 42 GLY 32 43 ALA 33 44 GLN 34 45 LYS 35 46 ASP 36 47 THR 37 48 TYR 38 49 THR 39 50 MET 40 51 LYS 41 52 GLU 42 53 VAL 43 54 LEU 44 55 PHE 45 56 TYR 46 57 LEU 47 58 GLY 48 59 GLN 49 60 TYR 50 61 ILE 51 62 MET 52 63 THR 53 64 LYS 54 65 ARG 55 66 LEU 56 67 TYR 57 68 ASP 58 69 GLU 59 70 LYS 60 71 GLN 61 72 GLN 62 73 HIS 63 74 ILE 64 75 VAL 65 76 TYR 66 77 CYS 67 78 SER 68 79 ASN 69 80 ASP 70 81 LEU 71 82 LEU 72 83 GLY 73 84 ASP 74 85 LEU 75 86 PHE 76 87 GLY 77 88 VAL 78 89 PRO 79 90 SER 80 91 PHE 81 92 SER 82 93 VAL 83 94 LYS 84 95 GLU 85 96 HIS 86 97 ARG 87 98 LYS 88 99 ILE 89 100 TYR 90 101 THR 91 102 MET 92 103 ILE 93 104 TYR 94 105 ARG 95 106 ASN 96 107 LEU 97 108 VAL 98 109 VAL 99 110 VAL 100 111 ASN 101 112 GLN 102 113 GLN 103 114 GLU 104 115 SER 105 116 SER 106 117 ASP 107 118 SER 108 119 GLY 109 120 THR 110 121 SER 111 122 VAL 112 123 SER 113 124 GLU 114 125 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-05 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 PDB 1RV1 "Crystal Structure Of Human Mdm2 With An Imidazoline Inhibitor" 74.56 85 98.82 98.82 6.88e-53 PDB 1T4E "Structure Of Human Mdm2 In Complex With A Benzodiazepine Inhibitor" 83.33 96 100.00 100.00 8.49e-62 PDB 1T4F "Structure Of Human Mdm2 In Complex With An Optimized P53 Peptide" 95.61 110 100.00 100.00 2.50e-72 PDB 1YCR "Mdm2 Bound To The Transactivation Domain Of P53" 95.61 109 100.00 100.00 1.73e-72 PDB 2AXI "Hdm2 In Complex With A Beta-hairpin" 95.61 115 100.00 100.00 1.61e-72 PDB 2GV2 "Mdm2 In Complex With An 8-Mer P53 Peptide Analogue" 95.61 110 100.00 100.00 2.50e-72 PDB 2M86 "Solution Structure Of Hdm2 With Engineered Cyclotide" 100.88 129 97.39 97.39 8.70e-73 PDB 3EQS "Crystal Structure Of Human Mdm2 In Complex With A 12-Mer Peptide Inhibitor" 74.56 85 100.00 100.00 5.05e-54 PDB 3G03 "Structure Of Human Mdm2 In Complex With High Affinity Peptide" 94.74 109 100.00 100.00 7.38e-72 PDB 3IUX "Crystal Structure Of Human Mdm2 In Complex With A Potent Miniature Protein Inhibitor (18-Residues)" 74.56 85 100.00 100.00 5.05e-54 PDB 3IWY "Crystal Structure Of Human Mdm2 Complexed With D-peptide (12 Residues)" 74.56 85 100.00 100.00 5.05e-54 PDB 3JZK "Crystal Structure Of Mdm2 With Chromenotriazolopyrimidine 1" 83.33 96 100.00 100.00 8.49e-62 PDB 3JZR "Human Mdm2 Liganded With A 12mer Peptide Inhibitor (Pdi6w)" 95.61 110 100.00 100.00 2.50e-72 PDB 3JZS "Human Mdm2 Liganded With A 12mer Peptide Inhibitor (Pdiq)" 75.44 86 100.00 100.00 8.81e-55 PDB 3LBK "Structure Of Human Mdm2 Protein In Complex With A Small Molecule Inhibitor" 82.46 95 98.94 98.94 3.54e-60 PDB 3LBL "Structure Of Human Mdm2 Protein In Complex With Mi-63-Analog" 82.46 95 100.00 100.00 2.73e-61 PDB 3LNJ "Crystal Structure Of Human Mdm2 In Complex With D-Peptide Inhibitor (Dpmi-Alpha)" 74.56 85 100.00 100.00 5.05e-54 PDB 3LNZ "Crystal Structure Of Human Mdm2 With A 12-Mer Peptide Inhibitor Pmi (N8a Mutant)" 74.56 85 100.00 100.00 5.05e-54 PDB 3TJ2 "Structure Of A Novel Submicromolar Mdm2 Inhibitor" 82.46 95 100.00 100.00 2.73e-61 PDB 3TPX "Crystal Structure Of Human Mdm2 In Complex With A Trifluoromethylated D-peptide Inhibitor" 74.56 85 100.00 100.00 5.05e-54 PDB 3TU1 "Exhaustive Fluorine Scanning Towards Potent P53-Mdm2 Antagonist" 94.74 108 100.00 100.00 1.01e-71 PDB 3V3B "Structure Of The Stapled P53 Peptide Bound To Mdm2" 76.32 88 100.00 100.00 1.73e-55 PDB 3VBG "Structure Of Hdm2 With Dimer Inducing Indolyl Hydantoin Ro-2443" 74.56 85 98.82 98.82 6.88e-53 PDB 3VZV "Crystal Structure Of Human Mdm2 With A Dihydroimidazothiazole Inhibitor" 74.56 87 98.82 98.82 6.98e-53 PDB 3W69 "Crystal Structure Of Human Mdm2 With A Dihydroimidazothiazole Inhibitor" 74.56 87 98.82 98.82 6.98e-53 PDB 4DIJ "The Central Valine Concept Provides An Entry In A New Class Of Non Peptide Inhibitors Of The P53-Mdm2 Interaction" 83.33 96 98.95 98.95 1.15e-60 PDB 4ERE "Crystal Structure Of Mdm2 (17-111) In Complex With Compound 23" 83.33 96 100.00 100.00 8.49e-62 PDB 4ERF "Crystal Structure Of Mdm2 (17-111) In Complex With Compound 29 (Am- 8553)" 83.33 96 100.00 100.00 8.49e-62 PDB 4HFZ "Crystal Structure Of An Mdm2/p53 Peptide Complex" 95.61 109 98.17 98.17 4.87e-71 PDB 4HG7 "Crystal Structure Of An Mdm2/nutlin-3a Complex" 85.09 97 97.94 97.94 3.14e-62 PDB 4JV7 "Co-crystal Structure Of Mdm2 With Inhibitor (2s,5r,6s)-2-benzyl-5,6- Bis(4-bromophenyl)-4-methylmorpholin-3-one" 82.46 96 100.00 100.00 3.46e-61 PDB 4JV9 "Co-crystal Structure Of Mdm2 With Inhibitor (2s,5r,6s)-2-benzyl-5,6- Bis(4-chlorophenyl)-4-methylmorpholin-3-one" 82.46 96 100.00 100.00 3.46e-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-" 82.46 96 100.00 100.00 3.46e-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" 82.46 96 100.00 100.00 3.46e-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- " 83.33 95 100.00 100.00 6.34e-62 PDB 4MDN "Structure Of A Novel Submicromolar Mdm2 Inhibitor" 81.58 94 100.00 100.00 2.56e-60 PDB 4MDQ "Structure Of A Novel Submicromolar Mdm2 Inhibitor" 75.44 86 100.00 100.00 1.38e-54 PDB 4OAS "Co-crystal Structure Of Mdm2 (17-111) In Complex With Compound 25" 83.33 96 100.00 100.00 8.49e-62 PDB 4OBA "Co-crystal Structure Of Mdm2 With Inhibitor Compound 4" 83.33 96 100.00 100.00 8.49e-62 PDB 4OCC "Co-crystal Structure Of Mdm2(17-111) In Complex With Compound 48" 83.33 96 100.00 100.00 8.49e-62 PDB 4OGV "Co-crystal Structure Of Mdm2 With Inhibitor Compound 49" 83.33 95 100.00 100.00 6.34e-62 PDB 4OQ3 "Tetra-substituted Imidazoles As A New Class Of Inhibitors Of The P53- Mdm2 Interaction" 83.33 96 98.95 98.95 1.15e-60 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" 83.33 96 100.00 100.00 8.49e-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" 83.33 96 100.00 100.00 8.49e-62 PDB 4ZYC "Discovery Of Dihydroisoquinolinone Derivatives As Novel Inhibitors Of The P53-mdm2 Interaction With A Distinct Binding Mode: Hd" 83.33 96 98.95 98.95 1.15e-60 PDB 4ZYF "Discovery Of Nvp-cgm097 - A Highly Potent And Selective Mdm2 Inhibitor Undergoing Phase 1 Clinical Trials In P53wt Tumors: Hdm2" 83.33 96 100.00 100.00 8.49e-62 PDB 4ZYI "Discovery Of Nvp-cgm097 - A Highly Potent And Selective Mdm2 Inhibitor Undergoing Phase 1 Clinical Trials In P53wt Tumors: Hdm2" 83.33 96 100.00 100.00 8.49e-62 REF XP_006719462 "PREDICTED: E3 ubiquitin-protein ligase Mdm2 isoform X2 [Homo sapiens]" 56.14 430 100.00 100.00 1.82e-35 REF XP_012911529 "PREDICTED: E3 ubiquitin-protein ligase Mdm2 isoform X2 [Mustela putorius furo]" 56.14 426 98.44 98.44 1.12e-34 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $human_mdm2_N-terminal_domain 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 _Variant _Vector_name _Details $human_mdm2_N-terminal_domain 'recombinant technology' . Escherichia coli BL21 DE3 'pGEX 6P1' 'GST-tagged, 3C precision protease cleavable' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_mdm2_17-125 _Saveframe_category sample _Sample_type solution _Details 'prepared as GST-fusion in a 3-step purification procedure comprising affinity chromatography, 3C precision protease cleavage and a final gel filtration step.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling H2O 90 % 'natural abundance' D2O 5 % 'natural abundance' DMSO 5 % 'natural abundance' NaCl 50 mM 'natural abundance' 'Sodium Phosphate pH 6.5' 25 mM 'natural abundance' Mono-Thioglycerol 0.02 % 'natural abundance' 'Sodium Azide' 0.02 % 'natural abundance' glycerol 5 % 'natural abundance' $human_mdm2_N-terminal_domain . mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version 5.2.2 loop_ _Vendor _Address _Electronic_address 'bruce johnson, onemoonscientific' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details 'tcl version' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details 'a GE/Oxford instruments magnet fitted with a bruker cryogenic probe and console.' save_ ############################# # NMR applied experiments # ############################# save_3D_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $mdm2_17-125 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $mdm2_17-125 save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 125 . mM pH 6.5 . pH pressure 1 . atm temperature 293.15 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_DSS _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.0 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 CBCA(CO)NH' '3D HNCA' stop_ loop_ _Sample_label $mdm2_17-125 stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $DSS _Mol_system_component_name 'N-terminal domain, p53 binding domain' _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 14 3 LEU CA C 54.9110 0.087 1 2 14 3 LEU CB C 42.0810 0.087 1 3 15 4 GLY H H 8.4230 0.00425 1 4 15 4 GLY CA C 45.3620 0.087 1 5 15 4 GLY N N 109.6860 0.07 1 6 16 5 SER H H 8.2650 0.00425 1 7 16 5 SER CA C 58.9600 0.087 1 8 16 5 SER CB C 63.5400 0.087 1 9 16 5 SER N N 114.4660 0.07 1 10 17 6 SER H H 8.6100 0.00425 1 11 17 6 SER CA C 57.9270 0.087 1 12 17 6 SER CB C 63.2310 0.087 1 13 17 6 SER N N 121.1110 0.07 1 14 18 7 GLN H H 9.2520 0.00425 1 15 18 7 GLN CA C 56.1160 0.087 1 16 18 7 GLN CB C 29.2090 0.087 1 17 18 7 GLN N N 121.6550 0.07 1 18 19 8 ILE H H 7.9390 0.00425 1 19 19 8 ILE HA H 4.3070 0.00425 1 20 19 8 ILE HB H 1.7700 0.00425 1 21 19 8 ILE CA C 56.9460 0.087 1 22 19 8 ILE N N 122.6140 0.07 1 23 20 9 PRO CA C 63.5450 0.087 1 24 20 9 PRO CB C 32.4930 0.087 1 25 21 10 ALA H H 8.8350 0.00425 1 26 21 10 ALA CA C 55.5420 0.087 1 27 21 10 ALA CB C 18.4230 0.087 1 28 21 10 ALA N N 126.9740 0.07 1 29 22 11 SER H H 8.5820 0.00425 1 30 22 11 SER CA C 60.5210 0.087 1 31 22 11 SER CB C 62.1500 0.087 1 32 22 11 SER N N 111.1830 0.07 1 33 23 12 GLU H H 7.5520 0.00425 1 34 23 12 GLU CA C 58.0990 0.087 1 35 23 12 GLU CB C 29.9790 0.087 1 36 23 12 GLU N N 122.9790 0.07 1 37 24 13 GLN H H 7.9260 0.00425 1 38 24 13 GLN CA C 58.6730 0.087 1 39 24 13 GLN CB C 29.1900 0.087 1 40 24 13 GLN N N 118.9380 0.07 1 41 25 14 GLU H H 7.6430 0.00425 1 42 25 14 GLU CA C 55.7850 0.087 1 43 25 14 GLU CB C 29.8210 0.087 1 44 25 14 GLU N N 114.6480 0.07 1 45 26 15 THR H H 7.4970 0.00425 1 46 26 15 THR HA H 4.0230 0.00425 1 47 26 15 THR CA C 64.8870 0.087 1 48 26 15 THR CB C 70.2140 0.087 1 49 26 15 THR N N 117.4120 0.07 1 50 27 16 LEU H H 8.4840 0.00425 1 51 27 16 LEU CA C 54.6710 0.087 1 52 27 16 LEU CB C 43.2660 0.087 1 53 27 16 LEU N N 128.2150 0.07 1 54 28 17 VAL H H 9.8030 0.00425 1 55 28 17 VAL CA C 59.1520 0.087 1 56 28 17 VAL CB C 36.5240 0.087 1 57 28 17 VAL N N 116.9750 0.07 1 58 29 18 ARG H H 9.2500 0.00425 1 59 29 18 ARG CA C 52.4880 0.087 1 60 29 18 ARG N N 121.6550 0.07 1 61 30 19 PRO CA C 62.9490 0.087 1 62 30 19 PRO CB C 32.6750 0.087 1 63 31 20 LYS H H 8.3120 0.00425 1 64 31 20 LYS CA C 56.7750 0.087 1 65 31 20 LYS N N 123.2810 0.07 1 66 32 21 PRO CA C 67.5880 0.087 1 67 32 21 PRO CB C 32.6510 0.087 1 68 33 22 LEU H H 8.9210 0.00425 1 69 33 22 LEU CA C 58.3380 0.087 1 70 33 22 LEU CB C 41.4550 0.087 1 71 33 22 LEU N N 118.4450 0.07 1 72 34 23 LEU H H 7.4390 0.00425 1 73 34 23 LEU HA H 4.0760 0.00425 1 74 34 23 LEU CA C 56.7990 0.087 1 75 34 23 LEU CB C 40.7980 0.087 1 76 34 23 LEU N N 118.2640 0.07 1 77 35 24 LEU H H 8.5920 0.00425 1 78 35 24 LEU CA C 58.1860 0.087 1 79 35 24 LEU CB C 41.4150 0.087 1 80 35 24 LEU N N 120.1010 0.07 1 81 36 25 LYS H H 7.9480 0.00425 1 82 36 25 LYS HA H 3.8420 0.00425 1 83 36 25 LYS CA C 59.7300 0.087 1 84 36 25 LYS CB C 32.2680 0.087 1 85 36 25 LYS N N 118.2050 0.07 1 86 37 26 LEU H H 7.3380 0.00425 1 87 37 26 LEU CA C 59.6420 0.087 1 88 37 26 LEU CB C 41.1600 0.087 1 89 37 26 LEU N N 121.0970 0.07 1 90 38 27 LEU H H 8.1990 0.00425 1 91 38 27 LEU CA C 57.9800 0.087 1 92 38 27 LEU CB C 39.1310 0.087 1 93 38 27 LEU N N 120.4260 0.07 1 94 39 28 LYS H H 8.8530 0.00425 1 95 39 28 LYS CA C 59.3680 0.087 1 96 39 28 LYS N N 118.1960 0.07 1 97 40 29 SER H H 7.8690 0.00425 1 98 40 29 SER HA H 4.4340 0.00425 1 99 40 29 SER CA C 61.9030 0.087 1 100 40 29 SER CB C 63.0050 0.087 1 101 40 29 SER N N 116.7260 0.07 1 102 41 30 VAL H H 7.2900 0.00425 1 103 41 30 VAL HA H 4.8130 0.00425 1 104 41 30 VAL CA C 60.4970 0.087 1 105 41 30 VAL CB C 30.8010 0.087 1 106 41 30 VAL N N 112.5690 0.07 1 107 42 31 GLY H H 7.5510 0.00425 1 108 42 31 GLY HA2 H 4.4400 0.00425 2 109 42 31 GLY HA3 H 3.7800 0.00425 2 110 42 31 GLY CA C 45.5990 0.087 1 111 42 31 GLY N N 106.2630 0.07 1 112 43 32 ALA H H 7.3800 0.00425 1 113 43 32 ALA HA H 4.0530 0.00425 1 114 43 32 ALA CA C 53.2060 0.087 1 115 43 32 ALA CB C 18.4730 0.087 1 116 43 32 ALA N N 124.9500 0.07 1 117 44 33 GLN H H 8.7780 0.00425 1 118 44 33 GLN HA H 4.5920 0.00425 1 119 44 33 GLN CA C 55.7290 0.087 1 120 44 33 GLN CB C 31.0640 0.087 1 121 44 33 GLN N N 118.1150 0.07 1 122 45 34 LYS H H 7.3830 0.00425 1 123 45 34 LYS HA H 4.6990 0.00425 1 124 45 34 LYS CA C 63.3850 0.087 1 125 45 34 LYS CB C 32.4550 0.087 1 126 45 34 LYS N N 118.1590 0.07 1 127 46 35 ASP H H 8.3750 0.00425 1 128 46 35 ASP CA C 55.1780 0.087 1 129 46 35 ASP N N 120.8770 0.07 1 130 47 36 THR H H 6.9960 0.00425 1 131 47 36 THR HA H 5.0100 0.00425 1 132 47 36 THR HB H 3.9130 0.00425 1 133 47 36 THR CA C 60.6660 0.087 1 134 47 36 THR CB C 71.7840 0.087 1 135 47 36 THR N N 111.2880 0.07 1 136 48 37 TYR H H 8.7630 0.00425 1 137 48 37 TYR HA H 4.8230 0.00425 1 138 48 37 TYR CA C 57.2970 0.087 1 139 48 37 TYR CB C 45.6810 0.087 1 140 48 37 TYR N N 120.0200 0.07 1 141 49 38 THR H H 9.0050 0.00425 1 142 49 38 THR HA H 5.3990 0.00425 1 143 49 38 THR CA C 61.0680 0.087 1 144 49 38 THR CB C 70.8700 0.087 1 145 49 38 THR N N 110.5870 0.07 1 146 50 39 MET H H 8.2610 0.00425 1 147 50 39 MET CA C 57.5000 0.087 1 148 50 39 MET CB C 30.4630 0.087 1 149 50 39 MET N N 121.7140 0.07 1 150 51 40 LYS H H 8.6180 0.00425 1 151 51 40 LYS HA H 4.0160 0.00425 1 152 51 40 LYS CA C 59.7380 0.087 1 153 51 40 LYS CB C 32.7750 0.087 1 154 51 40 LYS N N 117.7770 0.07 1 155 52 41 GLU H H 7.9570 0.00425 1 156 52 41 GLU HA H 4.1270 0.00425 1 157 52 41 GLU CA C 59.5420 0.087 1 158 52 41 GLU CB C 31.7390 0.087 1 159 52 41 GLU N N 120.5100 0.07 1 160 53 42 VAL H H 8.3100 0.00425 1 161 53 42 VAL HA H 3.3420 0.00425 1 162 53 42 VAL CA C 68.0980 0.087 1 163 53 42 VAL CB C 30.5200 0.087 1 164 53 42 VAL N N 119.6920 0.07 1 165 54 43 LEU H H 8.2930 0.00425 1 166 54 43 LEU HA H 3.9720 0.00425 1 167 54 43 LEU CA C 58.1040 0.087 1 168 54 43 LEU CB C 40.8290 0.087 1 169 54 43 LEU N N 118.8360 0.07 1 170 55 44 PHE H H 8.0610 0.00425 1 171 55 44 PHE HA H 3.9040 0.00425 1 172 55 44 PHE CA C 61.5350 0.087 1 173 55 44 PHE CB C 38.4080 0.087 1 174 55 44 PHE N N 121.8260 0.07 1 175 56 45 TYR H H 8.6110 0.00425 1 176 56 45 TYR CA C 63.0010 0.087 1 177 56 45 TYR CB C 38.8580 0.087 1 178 56 45 TYR N N 120.1010 0.07 1 179 57 46 LEU H H 8.9270 0.00425 1 180 57 46 LEU HA H 4.0010 0.00425 1 181 57 46 LEU CA C 58.3290 0.087 1 182 57 46 LEU CB C 41.8170 0.087 1 183 57 46 LEU N N 121.1520 0.07 1 184 58 47 GLY H H 8.2530 0.00425 1 185 58 47 GLY CA C 47.5570 0.087 1 186 58 47 GLY N N 106.1730 0.07 1 187 59 48 GLN H H 7.7460 0.00425 1 188 59 48 GLN CA C 59.1980 0.087 1 189 59 48 GLN CB C 28.6150 0.087 1 190 59 48 GLN N N 120.6310 0.07 1 191 60 49 TYR H H 8.7810 0.00425 1 192 60 49 TYR HA H 3.9250 0.00425 1 193 60 49 TYR CA C 62.8470 0.087 1 194 60 49 TYR CB C 38.4840 0.087 1 195 60 49 TYR N N 124.3580 0.07 1 196 61 50 ILE H H 8.4390 0.00425 1 197 61 50 ILE CA C 66.1310 0.087 1 198 61 50 ILE CB C 39.0330 0.087 1 199 61 50 ILE N N 118.7020 0.07 1 200 62 51 MET H H 7.9020 0.00425 1 201 62 51 MET HA H 4.3000 0.00425 1 202 62 51 MET HB2 H 3.2190 0.00425 2 203 62 51 MET HB3 H 3.2190 0.00425 2 204 62 51 MET CA C 58.2790 0.087 1 205 62 51 MET CB C 31.9160 0.087 1 206 62 51 MET N N 115.6230 0.07 1 207 63 52 THR H H 8.6020 0.00425 1 208 63 52 THR HA H 4.0240 0.00425 1 209 63 52 THR CA C 66.3750 0.087 1 210 63 52 THR CB C 69.0830 0.087 1 211 63 52 THR N N 116.4020 0.07 1 212 64 53 LYS H H 4.1080 0.00425 1 213 64 53 LYS CA C 55.6860 0.087 1 214 64 53 LYS CB C 30.9720 0.087 1 215 64 53 LYS N N 118.4860 0.07 1 216 65 54 ARG H H 7.6270 0.00425 1 217 65 54 ARG HA H 3.8130 0.00425 1 218 65 54 ARG CA C 56.8240 0.087 1 219 65 54 ARG CB C 26.6320 0.087 1 220 65 54 ARG N N 116.0430 0.07 1 221 66 55 LEU H H 7.6460 0.00425 1 222 66 55 LEU HA H 4.4410 0.00425 1 223 66 55 LEU CA C 54.8120 0.087 1 224 66 55 LEU CB C 42.2060 0.087 1 225 66 55 LEU N N 115.1580 0.07 1 226 67 56 TYR H H 6.8910 0.00425 1 227 67 56 TYR HA H 5.0880 0.00425 1 228 67 56 TYR CA C 55.2980 0.087 1 229 67 56 TYR CB C 39.4060 0.087 1 230 67 56 TYR N N 114.2860 0.07 1 231 68 57 ASP H H 8.6170 0.00425 1 232 68 57 ASP CA C 54.1670 0.087 1 233 68 57 ASP CB C 42.8470 0.087 1 234 68 57 ASP N N 123.6520 0.07 1 235 69 58 GLU H H 8.6360 0.00425 1 236 69 58 GLU HA H 3.9940 0.00425 1 237 69 58 GLU CA C 59.1270 0.087 1 238 69 58 GLU CB C 30.1480 0.087 1 239 69 58 GLU N N 124.1810 0.07 1 240 70 59 LYS H H 8.2850 0.00425 1 241 70 59 LYS HA H 4.3920 0.00425 1 242 70 59 LYS HB2 H 1.9060 0.00425 2 243 70 59 LYS HB3 H 1.9060 0.00425 2 244 70 59 LYS CA C 57.1700 0.087 1 245 70 59 LYS CB C 33.0740 0.087 1 246 70 59 LYS N N 116.6370 0.07 1 247 71 60 GLN H H 8.3660 0.00425 1 248 71 60 GLN HA H 4.6320 0.00425 1 249 71 60 GLN HB2 H 1.8500 0.00425 2 250 71 60 GLN HB3 H 1.8500 0.00425 2 251 71 60 GLN CA C 54.3050 0.087 1 252 71 60 GLN CB C 29.3710 0.087 1 253 71 60 GLN N N 120.8770 0.07 1 254 72 61 GLN H H 8.2990 0.00425 1 255 72 61 GLN HA H 4.2580 0.00425 1 256 72 61 GLN CA C 58.8560 0.087 1 257 72 61 GLN CB C 27.7050 0.087 1 258 72 61 GLN N N 118.8360 0.07 1 259 73 62 HIS H H 7.8380 0.00425 1 260 73 62 HIS CA C 56.0170 0.087 1 261 73 62 HIS CB C 30.6850 0.087 1 262 73 62 HIS N N 112.8170 0.07 1 263 74 63 ILE H H 7.6430 0.00425 1 264 74 63 ILE HA H 4.1250 0.00425 1 265 74 63 ILE CA C 59.8430 0.087 1 266 74 63 ILE CB C 36.7430 0.087 1 267 74 63 ILE N N 122.4810 0.07 1 268 75 64 VAL H H 8.3710 0.00425 1 269 75 64 VAL HA H 3.8280 0.00425 1 270 75 64 VAL CA C 60.7980 0.087 1 271 75 64 VAL CB C 32.5070 0.087 1 272 75 64 VAL N N 126.2080 0.07 1 273 76 65 TYR H H 8.3780 0.00425 1 274 76 65 TYR CA C 58.4630 0.087 1 275 76 65 TYR CB C 41.7690 0.087 1 276 76 65 TYR N N 125.8160 0.07 1 277 77 66 CYS H H 8.4710 0.00425 1 278 77 66 CYS CA C 55.9760 0.087 1 279 77 66 CYS CB C 29.4820 0.087 1 280 78 67 SER H H 7.7560 0.00425 1 281 78 67 SER CA C 60.3890 0.087 1 282 78 67 SER CB C 47.3620 0.087 1 283 78 67 SER N N 116.5510 0.07 1 284 79 68 ASN H H 8.7580 0.00425 1 285 79 68 ASN CA C 55.0580 0.087 1 286 79 68 ASN CB C 37.9430 0.087 1 287 79 68 ASN N N 118.1150 0.07 1 288 80 69 ASP H H 7.6920 0.00425 1 289 80 69 ASP CA C 53.3520 0.087 1 290 80 69 ASP N N 118.3520 0.07 1 291 81 70 LEU H H 9.8590 0.00425 1 292 81 70 LEU CA C 58.2290 0.087 1 293 81 70 LEU CB C 42.1530 0.087 1 294 82 71 LEU H H 9.8680 0.00425 1 295 82 71 LEU CA C 58.1690 0.087 1 296 82 71 LEU CB C 42.6100 0.087 1 297 82 71 LEU N N 118.5690 0.07 1 298 83 72 GLY H H 7.7760 0.00425 1 299 83 72 GLY HA2 H 4.1160 0.00425 2 300 83 72 GLY HA3 H 4.1160 0.00425 2 301 83 72 GLY CA C 47.9710 0.087 1 302 83 72 GLY N N 106.6110 0.07 1 303 84 73 ASP H H 7.5520 0.00425 1 304 84 73 ASP HA H 4.4330 0.00425 1 305 84 73 ASP HB2 H 2.9050 0.00425 2 306 84 73 ASP HB3 H 2.9050 0.00425 2 307 84 73 ASP CA C 56.9970 0.087 1 308 84 73 ASP CB C 40.1860 0.087 1 309 84 73 ASP N N 122.9790 0.07 1 310 85 74 LEU H H 8.0690 0.00425 1 311 85 74 LEU HA H 4.1380 0.00425 1 312 85 74 LEU CA C 57.2570 0.087 1 313 85 74 LEU CB C 38.5680 0.087 1 314 85 74 LEU N N 118.9220 0.07 1 315 86 75 PHE H H 8.4360 0.00425 1 316 86 75 PHE CA C 56.0650 0.087 1 317 86 75 PHE CB C 38.2720 0.087 1 318 86 75 PHE N N 117.2560 0.07 1 319 87 76 GLY H H 8.3380 0.00425 1 320 87 76 GLY HA2 H 3.9870 0.00425 2 321 87 76 GLY HA3 H 3.9870 0.00425 2 322 87 76 GLY CA C 46.5250 0.087 1 323 87 76 GLY N N 108.3950 0.07 1 324 88 77 VAL H H 7.1310 0.00425 1 325 88 77 VAL HA H 5.0090 0.00425 1 326 88 77 VAL CA C 56.9990 0.087 1 327 88 77 VAL N N 108.5000 0.07 1 328 89 78 PRO CA C 63.3300 0.087 1 329 89 78 PRO CB C 32.1140 0.087 1 330 90 79 SER H H 7.2630 0.00425 1 331 90 79 SER HA H 5.4810 0.00425 1 332 90 79 SER CA C 56.7170 0.087 1 333 90 79 SER CB C 64.9870 0.087 1 334 90 79 SER N N 111.3020 0.07 1 335 91 80 PHE H H 8.2650 0.00425 1 336 91 80 PHE CA C 56.7880 0.087 1 337 91 80 PHE CB C 39.6600 0.087 1 338 91 80 PHE N N 114.4660 0.07 1 339 92 81 SER H H 8.7780 0.00425 1 340 92 81 SER CA C 54.4560 0.087 1 341 92 81 SER CB C 63.9620 0.087 1 342 92 81 SER N N 112.7840 0.07 1 343 93 82 VAL H H 9.3910 0.00425 1 344 93 82 VAL HA H 4.3400 0.00425 1 345 93 82 VAL CA C 63.6320 0.087 1 346 93 82 VAL CB C 30.7900 0.087 1 347 93 82 VAL N N 122.7960 0.07 1 348 94 83 LYS H H 8.0760 0.00425 1 349 94 83 LYS HA H 4.2000 0.00425 1 350 94 83 LYS CA C 56.8610 0.087 1 351 94 83 LYS CB C 32.5850 0.087 1 352 94 83 LYS N N 116.6400 0.07 1 353 95 84 GLU H H 7.4250 0.00425 1 354 95 84 GLU HA H 4.6000 0.00425 1 355 95 84 GLU CA C 54.6950 0.087 1 356 95 84 GLU CB C 27.9050 0.087 1 357 95 84 GLU N N 120.0340 0.07 1 358 96 85 HIS H H 7.6800 0.00425 1 359 96 85 HIS CA C 59.9200 0.087 1 360 96 85 HIS N N 120.7610 0.07 1 361 97 86 ARG CA C 58.5830 0.087 1 362 97 86 ARG CB C 27.5590 0.087 1 363 98 87 LYS H H 7.7230 0.00425 1 364 98 87 LYS HA H 4.0320 0.00425 1 365 98 87 LYS HE2 H 2.7860 0.00425 2 366 98 87 LYS HE3 H 2.7860 0.00425 2 367 98 87 LYS HG2 H -0.2330 0.00425 2 368 98 87 LYS HG3 H -0.2330 0.00425 2 369 98 87 LYS CA C 59.8750 0.087 1 370 98 87 LYS CB C 32.3960 0.087 1 371 98 87 LYS N N 120.6310 0.07 1 372 99 88 ILE H H 7.9260 0.00425 1 373 99 88 ILE CA C 65.3590 0.087 1 374 99 88 ILE CB C 37.5260 0.087 1 375 99 88 ILE N N 118.9380 0.07 1 376 100 89 TYR H H 8.5540 0.00425 1 377 100 89 TYR CA C 62.9100 0.087 1 378 100 89 TYR CB C 37.2000 0.087 1 379 100 89 TYR N N 121.1110 0.07 1 380 101 90 THR H H 8.1970 0.00425 1 381 101 90 THR CA C 67.3790 0.087 1 382 101 90 THR CB C 68.8080 0.087 1 383 101 90 THR N N 114.0790 0.07 1 384 102 91 MET H H 7.6580 0.00425 1 385 102 91 MET CA C 59.7450 0.087 1 386 102 91 MET N N 119.9490 0.07 1 387 103 92 ILE H H 8.2030 0.00425 1 388 103 92 ILE CA C 66.0120 0.087 1 389 103 92 ILE CB C 37.4200 0.087 1 390 103 92 ILE N N 119.9770 0.07 1 391 104 93 TYR H H 8.8790 0.00425 1 392 104 93 TYR CA C 61.3870 0.087 1 393 104 93 TYR CB C 37.7290 0.087 1 394 104 93 TYR N N 119.7260 0.07 1 395 105 94 ARG H H 7.1070 0.00425 1 396 105 94 ARG N N 114.7490 0.07 1 397 107 96 LEU CA C 53.3270 0.087 1 398 107 96 LEU CB C 47.0890 0.087 1 399 108 97 VAL H H 8.6070 0.00425 1 400 108 97 VAL CA C 58.1990 0.087 1 401 108 97 VAL N N 128.3180 0.07 1 402 109 98 VAL H H 8.7600 0.00425 1 403 109 98 VAL HA H 4.1110 0.00425 1 404 109 98 VAL CA C 63.1770 0.087 1 405 109 98 VAL CB C 32.4540 0.087 1 406 109 98 VAL N N 127.7890 0.07 1 407 110 99 VAL H H 8.4310 0.00425 1 408 110 99 VAL HA H 3.9820 0.00425 1 409 110 99 VAL CA C 63.1060 0.087 1 410 110 99 VAL CB C 32.3450 0.087 1 411 110 99 VAL N N 127.0140 0.07 1 412 111 100 ASN H H 8.3050 0.00425 1 413 111 100 ASN HB2 H 2.8210 0.00425 2 414 111 100 ASN HB3 H 2.8210 0.00425 2 415 111 100 ASN CA C 53.3300 0.087 1 416 111 100 ASN CB C 40.0530 0.087 1 417 111 100 ASN N N 122.4470 0.07 1 418 112 101 GLN H H 8.4870 0.00425 1 419 112 101 GLN CA C 56.2040 0.087 1 420 112 101 GLN CB C 29.6120 0.087 1 421 112 101 GLN N N 121.6150 0.07 1 422 113 102 GLN H H 8.4600 0.00425 1 423 113 102 GLN HA H 4.3230 0.00425 1 424 113 102 GLN HB2 H 2.0480 0.00425 2 425 113 102 GLN HB3 H 2.0480 0.00425 2 426 113 102 GLN CA C 56.0210 0.087 1 427 113 102 GLN CB C 29.5940 0.087 1 428 113 102 GLN N N 121.2230 0.07 1 429 114 103 GLU H H 8.4510 0.00425 1 430 114 103 GLU HA H 4.3330 0.00425 1 431 114 103 GLU HB2 H 2.3510 0.00425 2 432 114 103 GLU HB3 H 2.0270 0.00425 2 433 114 103 GLU CA C 56.5400 0.087 1 434 114 103 GLU CB C 30.1020 0.087 1 435 114 103 GLU N N 122.1270 0.07 1 436 115 104 SER H H 8.0980 0.00425 1 437 115 104 SER HA H 4.5140 0.00425 1 438 115 104 SER HB2 H 3.8960 0.00425 2 439 115 104 SER HB3 H 3.8960 0.00425 2 440 115 104 SER CA C 58.2800 0.087 1 441 115 104 SER CB C 63.8670 0.087 1 442 115 104 SER N N 116.8540 0.07 1 443 116 105 SER H H 8.4890 0.00425 1 444 116 105 SER CA C 58.4630 0.087 1 445 116 105 SER CB C 63.8270 0.087 1 446 116 105 SER N N 118.0520 0.07 1 447 117 106 ASP H H 8.4110 0.00425 1 448 117 106 ASP HA H 4.5620 0.00425 1 449 117 106 ASP HB2 H 2.7000 0.00425 2 450 117 106 ASP HB3 H 2.7000 0.00425 2 451 117 106 ASP CA C 54.5810 0.087 1 452 117 106 ASP CB C 40.4890 0.087 1 453 117 106 ASP N N 122.4130 0.07 1 454 118 107 SER H H 7.5380 0.00425 1 455 118 107 SER HA H 6.8530 0.00425 1 456 118 107 SER CA C 58.8960 0.087 1 457 118 107 SER CB C 63.7360 0.087 1 458 119 108 GLY H H 8.5150 0.00425 1 459 119 108 GLY HA2 H 4.0220 0.00425 2 460 119 108 GLY HA3 H 4.0220 0.00425 2 461 119 108 GLY CA C 45.5360 0.087 1 462 119 108 GLY N N 110.8950 0.07 1 463 120 109 THR H H 8.0790 0.00425 1 464 120 109 THR HA H 4.4180 0.00425 1 465 120 109 THR CA C 61.7920 0.087 1 466 120 109 THR CB C 69.8600 0.087 1 467 120 109 THR N N 113.5210 0.07 1 468 121 110 SER H H 8.3370 0.00425 1 469 121 110 SER HA H 4.3710 0.00425 1 470 121 110 SER HB2 H 3.9690 0.00425 2 471 121 110 SER HB3 H 3.9690 0.00425 2 472 121 110 SER CA C 58.3520 0.087 1 473 121 110 SER CB C 63.7710 0.087 1 474 121 110 SER N N 118.7020 0.07 1 475 122 111 VAL H H 8.2610 0.00425 1 476 122 111 VAL CA C 62.2050 0.087 1 477 122 111 VAL CB C 32.7580 0.087 1 478 122 111 VAL N N 121.7140 0.07 1 479 123 112 SER H H 8.3640 0.00425 1 480 123 112 SER HA H 4.4970 0.00425 1 481 123 112 SER HB2 H 3.8660 0.00425 2 482 123 112 SER HB3 H 3.8660 0.00425 2 483 123 112 SER CA C 58.1700 0.087 1 484 123 112 SER CB C 63.9060 0.087 1 485 123 112 SER N N 119.5170 0.07 1 486 124 113 GLU H H 8.4890 0.00425 1 487 124 113 GLU HA H 4.3260 0.00425 1 488 124 113 GLU HB2 H 2.2210 0.00425 2 489 124 113 GLU HB3 H 1.9400 0.00425 2 490 124 113 GLU CA C 56.6410 0.087 1 491 124 113 GLU CB C 30.5730 0.087 1 492 124 113 GLU N N 123.4980 0.07 1 493 125 114 ASN H H 8.0600 0.00425 1 494 125 114 ASN HB2 H 2.7280 0.00425 2 495 125 114 ASN HB3 H 2.7280 0.00425 2 496 125 114 ASN CA C 56.4310 0.087 1 497 125 114 ASN N N 124.4550 0.07 1 stop_ save_