data_7251 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H chemical shift assignments for wild type p53 tetramerization domain ; _BMRB_accession_number 7251 _BMRB_flat_file_name bmr7251.str _Entry_type original _Submission_date 2006-08-08 _Accession_date 2006-08-08 _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 Carbajo Rodrigo J. . 2 Mora Puig . . 3 'Sanchez del Pino' Manuel M. . 4 'Perez Paya' Enrique . . 5 Pineda-Lucena Antonio . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 199 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-17 update BMRB 'complete entry citation' 2008-02-05 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solvent-exposed residues located in the beta-sheet modulate the stability of the tetramerization domain of p53-A structural and combinatorial approach' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18076077 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mora Puig . . 2 Carbajo Rodrigo J. . 3 Pineda-Lucena Antonio . . 4 'Sanchez del Pino' Manuel M. . 5 'Perez Paya' Enrique . . stop_ _Journal_abbreviation Proteins _Journal_volume 71 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1670 _Page_last 1685 _Year 2008 _Details . loop_ _Keyword 'NMR structure' p53TD stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'p53 tetramerization domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'subunit 1' $p53TD_wild_type 'subunit 2' $p53TD_wild_type 'subunit 3' $p53TD_wild_type 'subunit 4' $p53TD_wild_type stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'subunit 1' 1 'subunit 2' 1 'subunit 3' 1 'subunit 4' stop_ _Database_query_date . _Details 'wild type p53 tetramerization domain (residues 326-356)' save_ ######################## # Monomeric polymers # ######################## save_p53TD_wild_type _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common p53TD _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 31 _Mol_residue_sequence ; EYFTLQIRGRERFEMFRELN EALELKDAQAG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 326 GLU 2 327 TYR 3 328 PHE 4 329 THR 5 330 LEU 6 331 GLN 7 332 ILE 8 333 ARG 9 334 GLY 10 335 ARG 11 336 GLU 12 337 ARG 13 338 PHE 14 339 GLU 15 340 MET 16 341 PHE 17 342 ARG 18 343 GLU 19 344 LEU 20 345 ASN 21 346 GLU 22 347 ALA 23 348 LEU 24 349 GLU 25 350 LEU 26 351 LYS 27 352 ASP 28 353 ALA 29 354 GLN 30 355 ALA 31 356 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 4048 p53tet 100.00 66 100.00 100.00 1.66e-12 BMRB 6521 p53_tetramerization_domain_polypeptide 100.00 55 100.00 100.00 2.60e-12 BMRB 6522 Mutant_p53_tetramerization_domain_polypeptide 100.00 54 100.00 100.00 2.55e-12 PDB 1AIE "P53 Tetramerization Domain Crystal Structure" 100.00 31 100.00 100.00 1.19e-11 PDB 1C26 "Crystal Structure Of P53 Tetramerization Domain" 100.00 32 100.00 100.00 1.24e-11 PDB 1OLG "High-Resolution Solution Structure Of The Oligomerization Domain Of P53 By Multi-Dimensional Nmr" 100.00 42 100.00 100.00 7.50e-12 PDB 1OLH "High-Resolution Solution Structure Of The Oligomerization Domain Of P53 By Multi-Dimensional Nmr" 100.00 42 100.00 100.00 7.50e-12 PDB 1PES "Nmr Solution Structure Of The Tetrameric Minimum Transforming Domain Of P53" 96.77 31 100.00 100.00 1.00e-10 PDB 1PET "Nmr Solution Structure Of The Tetrameric Minimum Transforming Domain Of P53" 96.77 31 100.00 100.00 1.00e-10 PDB 1SAE "High Resolution Solution Nmr Structure Of The Oligomerization Domain Of P53 By Multi-Dimensional Nmr (Sac Structures)" 100.00 42 100.00 100.00 7.50e-12 PDB 1SAF "High Resolution Solution Nmr Structure Of The Oligomerization Domain Of P53 By Multi-Dimensional Nmr (Sad Structures)" 100.00 42 100.00 100.00 7.50e-12 PDB 1SAK "High Resolution Solution Nmr Structure Of The Oligomerization Domain Of P53 By Multi-Dimensional Nmr (Sac Structures)" 100.00 42 100.00 100.00 7.50e-12 PDB 1SAL "High Resolution Solution Nmr Structure Of The Oligomerization Domain Of P53 By Multi-Dimensional Nmr (Sad Structures)" 100.00 42 100.00 100.00 7.50e-12 PDB 2J0Z "P53 Tetramerization Domain Wild Type" 100.00 31 100.00 100.00 1.19e-11 PDB 3SAK "High Resolution Solution Nmr Structure Of The Oligomerization Domain Of P53 By Multi-Dimensional Nmr (Sac Structures)" 100.00 42 100.00 100.00 7.50e-12 DBJ BAC16799 "P53 [Homo sapiens]" 100.00 393 100.00 100.00 2.00e-12 DBJ BAD96746 "tumor protein p53 variant [Homo sapiens]" 100.00 158 100.00 100.00 6.71e-11 DBJ BAG35463 "unnamed protein product [Homo sapiens]" 100.00 393 100.00 100.00 2.00e-12 DBJ BAG59884 "unnamed protein product [Homo sapiens]" 100.00 368 100.00 100.00 1.79e-12 DBJ BAG60244 "unnamed protein product [Homo sapiens]" 100.00 383 100.00 100.00 1.88e-12 EMBL CAA25652 "p53 [Homo sapiens]" 100.00 293 100.00 100.00 3.06e-12 EMBL CAA26306 "unnamed protein product [Homo sapiens]" 100.00 393 100.00 100.00 2.00e-12 EMBL CAA34420 "unnamed protein product [Chlorocebus aethiops]" 100.00 393 100.00 100.00 2.00e-12 EMBL CAA38095 "protein p53 [Homo sapiens]" 100.00 393 100.00 100.00 2.00e-12 EMBL CAA42626 "p53 transformation suppressor [Homo sapiens]" 100.00 393 100.00 100.00 2.00e-12 GB AAA17994 "p53 [Macaca mulatta]" 100.00 393 100.00 100.00 2.00e-12 GB AAA59987 "phosphoprotein p53 [Homo sapiens]" 100.00 393 100.00 100.00 2.00e-12 GB AAA59988 "phosphoprotein p53 [Homo sapiens]" 100.00 393 100.00 100.00 2.00e-12 GB AAA59989 "p53 cellular tumor antigen [Homo sapiens]" 100.00 393 100.00 100.00 2.00e-12 GB AAA61211 "p53 antigen [Homo sapiens]" 100.00 393 100.00 100.00 2.00e-12 PRF 2006287A "p53 protein" 100.00 393 100.00 100.00 2.00e-12 REF NP_000537 "cellular tumor antigen p53 isoform a [Homo sapiens]" 100.00 393 100.00 100.00 2.00e-12 REF NP_001040616 "cellular tumor antigen p53 [Macaca mulatta]" 100.00 393 100.00 100.00 2.00e-12 REF NP_001119584 "cellular tumor antigen p53 isoform a [Homo sapiens]" 100.00 393 100.00 100.00 2.00e-12 REF NP_001119587 "cellular tumor antigen p53 isoform d [Homo sapiens]" 100.00 261 100.00 100.00 4.11e-12 REF NP_001119590 "cellular tumor antigen p53 isoform g [Homo sapiens]" 100.00 354 100.00 100.00 1.52e-12 SP P04637 "RecName: Full=Cellular tumor antigen p53; AltName: Full=Antigen NY-CO-13; AltName: Full=Phosphoprotein p53; AltName: Full=Tumor" 100.00 393 100.00 100.00 2.00e-12 SP P13481 "RecName: Full=Cellular tumor antigen p53; AltName: Full=Tumor suppressor p53 [Chlorocebus aethiops]" 100.00 393 100.00 100.00 2.00e-12 SP P56423 "RecName: Full=Cellular tumor antigen p53; AltName: Full=Tumor suppressor p53 [Macaca fascicularis]" 100.00 393 100.00 100.00 2.00e-12 SP P56424 "RecName: Full=Cellular tumor antigen p53; AltName: Full=Tumor suppressor p53 [Macaca mulatta]" 100.00 393 100.00 100.00 2.00e-12 SP P61260 "RecName: Full=Cellular tumor antigen p53; AltName: Full=Tumor suppressor p53 [Macaca fuscata fuscata]" 100.00 393 100.00 100.00 2.00e-12 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $p53TD_wild_type 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 $p53TD_wild_type '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 $p53TD_wild_type 0.5 mM . 'phosphate buffer' 40 mM . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name TOPSPIN _Version 1.3 loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task Processing stop_ _Details . save_ save_software_2 _Saveframe_category software _Name SPARKY _Version 3.110 loop_ _Task Assignment stop_ _Details . save_ save_software_3 _Saveframe_category software _Name CNS _Version 1.1 loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task 'Structure calculations' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600MHz _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H,1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H,1H NOESY' _Sample_label $sample_1 save_ save_1H,1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H,1H TOCSY' _Sample_label $sample_1 save_ save_1H-1H_NOESY _Saveframe_category NMR_applied_experiment _Experiment_name '1H,1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_1H-1H_TOCSY _Saveframe_category NMR_applied_experiment _Experiment_name '1H,1H TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.1 pH temperature 300 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'subunit 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 GLU H H 8.08 0.01 1 2 1 1 GLU HA H 4.16 0.01 1 3 1 1 GLU HB2 H 1.80 0.01 1 4 1 1 GLU HB3 H 1.80 0.01 1 5 1 1 GLU HG2 H 1.98 0.01 2 6 1 1 GLU HG3 H 2.11 0.01 2 7 2 2 TYR H H 7.90 0.01 1 8 2 2 TYR HA H 5.10 0.01 1 9 2 2 TYR HB2 H 2.59 0.01 2 10 2 2 TYR HB3 H 2.64 0.01 2 11 2 2 TYR HD1 H 6.86 0.01 1 12 2 2 TYR HD2 H 6.86 0.01 1 13 2 2 TYR HE1 H 6.75 0.01 1 14 2 2 TYR HE2 H 6.75 0.01 1 15 3 3 PHE H H 9.30 0.01 1 16 3 3 PHE HA H 4.35 0.01 1 17 3 3 PHE HB2 H 1.89 0.01 2 18 3 3 PHE HB3 H 2.09 0.01 2 19 3 3 PHE HD1 H 6.75 0.01 1 20 3 3 PHE HD2 H 6.75 0.01 1 21 3 3 PHE HE1 H 7.00 0.01 1 22 3 3 PHE HE2 H 7.00 0.01 1 23 3 3 PHE HZ H 7.11 0.01 1 24 4 4 THR H H 8.38 0.01 1 25 4 4 THR HA H 5.08 0.01 1 26 4 4 THR HB H 3.91 0.01 1 27 4 4 THR HG2 H 1.06 0.01 1 28 5 5 LEU H H 8.94 0.01 1 29 5 5 LEU HA H 4.82 0.01 1 30 5 5 LEU HB2 H 1.38 0.01 2 31 5 5 LEU HB3 H 1.82 0.01 2 32 5 5 LEU HG H 1.43 0.01 1 33 5 5 LEU HD1 H 0.50 0.01 2 34 5 5 LEU HD2 H 0.88 0.01 2 35 6 6 GLN H H 8.61 0.01 1 36 6 6 GLN HA H 4.96 0.01 1 37 6 6 GLN HB2 H 1.85 0.01 2 38 6 6 GLN HB3 H 1.93 0.01 2 39 6 6 GLN HG2 H 2.14 0.01 2 40 6 6 GLN HG3 H 2.20 0.01 2 41 6 6 GLN HE21 H 6.59 0.01 2 42 6 6 GLN HE22 H 7.19 0.01 2 43 7 7 ILE H H 9.37 0.01 1 44 7 7 ILE HA H 4.35 0.01 1 45 7 7 ILE HB H 1.81 0.01 1 46 7 7 ILE HG12 H 1.08 0.01 2 47 7 7 ILE HG13 H 1.35 0.01 2 48 7 7 ILE HG2 H 0.94 0.01 1 49 7 7 ILE HD1 H 0.70 0.01 1 50 8 8 ARG H H 9.80 0.01 1 51 8 8 ARG HA H 4.24 0.01 1 52 8 8 ARG HB2 H 1.45 0.01 2 53 8 8 ARG HB3 H 1.81 0.01 2 54 8 8 ARG HG2 H 0.94 0.01 2 55 8 8 ARG HG3 H 1.21 0.01 2 56 8 8 ARG HD2 H 3.04 0.01 1 57 8 8 ARG HD3 H 3.04 0.01 1 58 9 9 GLY H H 8.71 0.01 1 59 9 9 GLY HA2 H 3.78 0.01 2 60 9 9 GLY HA3 H 4.68 0.01 2 61 10 10 ARG H H 8.90 0.01 1 62 10 10 ARG HA H 3.20 0.01 1 63 10 10 ARG HB2 H 1.71 0.01 2 64 10 10 ARG HB3 H 1.82 0.01 2 65 10 10 ARG HG2 H 1.34 0.01 2 66 10 10 ARG HG3 H 1.53 0.01 2 67 10 10 ARG HD2 H 2.98 0.01 2 68 10 10 ARG HD3 H 3.05 0.01 2 69 11 11 GLU H H 8.89 0.01 1 70 11 11 GLU HA H 3.90 0.01 1 71 11 11 GLU HB2 H 1.92 0.01 2 72 11 11 GLU HB3 H 2.04 0.01 2 73 11 11 GLU HG2 H 2.24 0.01 2 74 11 11 GLU HG3 H 2.38 0.01 2 75 12 12 ARG H H 7.91 0.01 1 76 12 12 ARG HA H 3.87 0.01 1 77 12 12 ARG HB2 H 1.96 0.01 2 78 12 12 ARG HB3 H 2.01 0.01 2 79 12 12 ARG HG2 H 1.64 0.01 2 80 12 12 ARG HD2 H 3.45 0.01 2 81 12 12 ARG HD3 H 3.65 0.01 2 82 12 12 ARG HE H 7.36 0.01 1 83 13 13 PHE H H 8.37 0.01 1 84 13 13 PHE HA H 4.13 0.01 1 85 13 13 PHE HB2 H 2.77 0.01 1 86 13 13 PHE HB3 H 2.77 0.01 1 87 13 13 PHE HD1 H 6.74 0.01 1 88 13 13 PHE HD2 H 6.74 0.01 1 89 13 13 PHE HE1 H 7.18 0.01 1 90 13 13 PHE HE2 H 7.18 0.01 1 91 13 13 PHE HZ H 7.35 0.01 1 92 14 14 GLU H H 8.56 0.01 1 93 14 14 GLU HA H 3.47 0.01 1 94 14 14 GLU HB2 H 1.91 0.01 1 95 14 14 GLU HB3 H 1.91 0.01 1 96 14 14 GLU HG2 H 2.25 0.01 2 97 14 14 GLU HG3 H 2.44 0.01 2 98 15 15 MET H H 7.57 0.01 1 99 15 15 MET HA H 4.08 0.01 1 100 15 15 MET HB2 H 1.94 0.01 2 101 15 15 MET HB3 H 2.21 0.01 2 102 15 15 MET HG2 H 1.98 0.01 2 103 15 15 MET HG3 H 2.50 0.01 2 104 15 15 MET HE H 1.46 0.01 1 105 16 16 PHE H H 8.00 0.01 1 106 16 16 PHE HA H 4.10 0.01 1 107 16 16 PHE HB2 H 2.64 0.01 2 108 16 16 PHE HB3 H 2.84 0.01 2 109 16 16 PHE HD1 H 7.09 0.01 1 110 16 16 PHE HD2 H 7.09 0.01 1 111 16 16 PHE HE1 H 7.28 0.01 1 112 16 16 PHE HE2 H 7.28 0.01 1 113 16 16 PHE HZ H 6.89 0.01 1 114 17 17 ARG H H 9.22 0.01 1 115 17 17 ARG HA H 3.63 0.01 1 116 17 17 ARG HB2 H 1.47 0.01 1 117 17 17 ARG HB3 H 1.47 0.01 1 118 17 17 ARG HG2 H 1.37 0.01 1 119 17 17 ARG HG3 H 1.37 0.01 1 120 17 17 ARG HD2 H 2.77 0.01 2 121 17 17 ARG HD3 H 3.15 0.01 2 122 18 18 GLU H H 7.82 0.01 1 123 18 18 GLU HA H 3.98 0.01 1 124 18 18 GLU HB2 H 2.05 0.01 1 125 18 18 GLU HB3 H 2.05 0.01 1 126 18 18 GLU HG2 H 2.13 0.01 2 127 18 18 GLU HG3 H 2.22 0.01 2 128 19 19 LEU H H 7.81 0.01 1 129 19 19 LEU HA H 4.04 0.01 1 130 19 19 LEU HB2 H 1.52 0.01 2 131 19 19 LEU HB3 H 2.22 0.01 2 132 19 19 LEU HG H 2.02 0.01 1 133 19 19 LEU HD1 H 0.74 0.01 2 134 19 19 LEU HD2 H 0.87 0.01 2 135 20 20 ASN H H 8.79 0.01 1 136 20 20 ASN HA H 4.54 0.01 1 137 20 20 ASN HB2 H 2.38 0.01 2 138 20 20 ASN HB3 H 2.77 0.01 2 139 20 20 ASN HD21 H 6.33 0.01 2 140 20 20 ASN HD22 H 7.67 0.01 2 141 21 21 GLU H H 8.79 0.01 1 142 21 21 GLU HA H 3.98 0.01 1 143 21 21 GLU HB2 H 2.05 0.01 2 144 21 21 GLU HB3 H 2.15 0.01 2 145 21 21 GLU HG2 H 2.20 0.01 2 146 21 21 GLU HG3 H 2.50 0.01 2 147 22 22 ALA H H 8.14 0.01 1 148 22 22 ALA HA H 4.06 0.01 1 149 22 22 ALA HB H 1.51 0.01 1 150 23 23 LEU H H 8.06 0.01 1 151 23 23 LEU HA H 4.00 0.01 1 152 23 23 LEU HB2 H 1.38 0.01 2 153 23 23 LEU HB3 H 2.15 0.01 2 154 23 23 LEU HG H 2.00 0.01 1 155 23 23 LEU HD1 H 0.83 0.01 2 156 23 23 LEU HD2 H 0.95 0.01 2 157 24 24 GLU H H 8.40 0.01 1 158 24 24 GLU HA H 4.21 0.01 1 159 24 24 GLU HB2 H 2.05 0.01 2 160 24 24 GLU HB3 H 2.15 0.01 2 161 24 24 GLU HG2 H 2.77 0.01 2 162 25 25 LEU H H 8.18 0.01 1 163 25 25 LEU HA H 4.23 0.01 1 164 25 25 LEU HB2 H 1.77 0.01 2 165 25 25 LEU HB3 H 1.93 0.01 2 166 25 25 LEU HG H 1.67 0.01 1 167 25 25 LEU HD1 H 0.86 0.01 2 168 25 25 LEU HD2 H 0.92 0.01 2 169 26 26 LYS H H 7.90 0.01 1 170 26 26 LYS HA H 3.93 0.01 1 171 26 26 LYS HB2 H 1.78 0.01 2 172 26 26 LYS HB3 H 2.29 0.01 2 173 26 26 LYS HG2 H 1.50 0.01 2 174 26 26 LYS HG3 H 1.54 0.01 2 175 26 26 LYS HD2 H 1.61 0.01 2 176 26 26 LYS HD3 H 1.67 0.01 2 177 26 26 LYS HE2 H 2.98 0.01 1 178 26 26 LYS HE3 H 2.98 0.01 1 179 27 27 ASP H H 8.25 0.01 1 180 27 27 ASP HA H 4.33 0.01 1 181 27 27 ASP HB2 H 2.70 0.01 2 182 27 27 ASP HB3 H 2.98 0.01 2 183 28 28 ALA H H 7.67 0.01 1 184 28 28 ALA HA H 4.23 0.01 1 185 28 28 ALA HB H 1.56 0.01 1 186 29 29 GLN H H 7.87 0.01 1 187 29 29 GLN HA H 4.23 0.01 1 188 29 29 GLN HB2 H 2.09 0.01 2 189 29 29 GLN HB3 H 2.25 0.01 2 190 29 29 GLN HG2 H 2.50 0.01 1 191 29 29 GLN HG3 H 2.50 0.01 1 192 29 29 GLN HE21 H 6.91 0.01 2 193 29 29 GLN HE22 H 7.44 0.01 2 194 30 30 ALA H H 7.94 0.01 1 195 30 30 ALA HA H 4.30 0.01 1 196 30 30 ALA HB H 1.46 0.01 1 197 31 31 GLY H H 8.14 0.01 1 198 31 31 GLY HA2 H 3.91 0.01 1 199 31 31 GLY HA3 H 3.91 0.01 1 stop_ save_