data_17557 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the dimerization domain of human ribosomal protein P1/P2 heterodimer ; _BMRB_accession_number 17557 _BMRB_flat_file_name bmr17557.str _Entry_type original _Submission_date 2011-03-30 _Accession_date 2011-03-30 _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 Lee Ka-Ming . . 2 Yu 'Conny Wing-Heng' . . 3 Chiu 'Teddy Yu-Hin' . . 4 Sze Kong-Hung . . 5 Shaw Pang-Chui . . 6 Wong Kam-Bo . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 605 "13C chemical shifts" 401 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-08-21 update BMRB 'update entry citation' 2011-12-14 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution structure of the dimerization domain of the eukaryotic stalk P1/P2 complex reveals the structural organization of eukaryotic stalk complex.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22135285 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lee Ka-Ming . . 2 Yu 'Conny Wing-Heng' . . 3 Chiu 'Teddy Yu-Hin' . . 4 Sze Kong-Hung . . 5 Shaw Pang-Chui . . 6 Wong Kam-Bo . . stop_ _Journal_abbreviation 'Nucleic Acids Res.' _Journal_name_full 'Nucleic acids research' _Journal_volume 40 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3172 _Page_last 3182 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'human ribosomal protein P1/P2 heterodimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $entity_1 entity_2 $entity_2 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 7088.202 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 69 _Mol_residue_sequence ; MASVSELACIYSALILHDDE VTVTEDKINALIKAAGVNVE PFWPGLFAKALANVNIGSLI CNVGAGGPA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 SER 4 VAL 5 SER 6 GLU 7 LEU 8 ALA 9 CYS 10 ILE 11 TYR 12 SER 13 ALA 14 LEU 15 ILE 16 LEU 17 HIS 18 ASP 19 ASP 20 GLU 21 VAL 22 THR 23 VAL 24 THR 25 GLU 26 ASP 27 LYS 28 ILE 29 ASN 30 ALA 31 LEU 32 ILE 33 LYS 34 ALA 35 ALA 36 GLY 37 VAL 38 ASN 39 VAL 40 GLU 41 PRO 42 PHE 43 TRP 44 PRO 45 GLY 46 LEU 47 PHE 48 ALA 49 LYS 50 ALA 51 LEU 52 ALA 53 ASN 54 VAL 55 ASN 56 ILE 57 GLY 58 SER 59 LEU 60 ILE 61 CYS 62 ASN 63 VAL 64 GLY 65 ALA 66 GLY 67 GLY 68 PRO 69 ALA 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 19086 60S_ACIDIC_RIBOSOMAL_PROTEIN_P1 100.00 114 100.00 100.00 3.11e-40 PDB 2LBF "Solution Structure Of The Dimerization Domain Of Human Ribosomal Protein P1P2 HETERODIMER" 100.00 69 100.00 100.00 3.75e-40 PDB 3J3B "Structure Of The Human 60s Ribosomal Proteins" 100.00 114 100.00 100.00 3.11e-40 PDB 4BEH "Solution Structure Of Human Ribosomal Protein P1.p2 Heterodimer" 98.55 114 100.00 100.00 3.77e-39 DBJ BAB25292 "unnamed protein product [Mus musculus]" 100.00 114 98.55 100.00 1.53e-39 DBJ BAB27095 "unnamed protein product [Mus musculus]" 100.00 114 98.55 100.00 1.53e-39 DBJ BAB79474 "ribosomal protein P1 [Homo sapiens]" 100.00 114 100.00 100.00 3.11e-40 DBJ BAC40128 "unnamed protein product [Mus musculus]" 100.00 114 98.55 100.00 1.53e-39 DBJ BAE41097 "unnamed protein product [Mus musculus]" 100.00 114 98.55 100.00 1.53e-39 EMBL CAA33200 "unnamed protein product [Rattus rattus]" 100.00 114 100.00 100.00 3.39e-40 EMBL CAG29335 "RPLP1 [Homo sapiens]" 100.00 114 98.55 100.00 5.70e-40 EMBL CAG47005 "RPLP1 [Homo sapiens]" 100.00 114 97.10 98.55 3.06e-38 GB AAA36471 "acidic ribosomal phosphoprotein (P1) [Homo sapiens]" 100.00 114 100.00 100.00 3.11e-40 GB AAA70106 "acidic ribosomal phosphoprotein P1 [Mus musculus]" 100.00 114 98.55 100.00 1.53e-39 GB AAH03369 "Ribosomal protein, large, P1 [Homo sapiens]" 100.00 114 100.00 100.00 3.11e-40 GB AAH07590 "Ribosomal protein, large, P1 [Homo sapiens]" 100.00 114 100.00 100.00 3.11e-40 GB AAH58151 "Ribosomal protein, large, P1 [Rattus norvegicus]" 100.00 114 100.00 100.00 3.39e-40 PRF 1718187B "ribosomal protein P1" 100.00 114 100.00 100.00 3.39e-40 REF NP_000994 "60S acidic ribosomal protein P1 isoform 1 [Homo sapiens]" 100.00 114 100.00 100.00 3.11e-40 REF NP_001007605 "60S acidic ribosomal protein P1 [Rattus norvegicus]" 100.00 114 100.00 100.00 3.39e-40 REF NP_001020511 "60S acidic ribosomal protein P1 [Bos taurus]" 100.00 114 100.00 100.00 3.11e-40 REF NP_001123436 "60S acidic ribosomal protein P1 [Sus scrofa]" 98.55 114 97.06 97.06 2.96e-38 REF NP_001180503 "60S acidic ribosomal protein P1 [Macaca mulatta]" 100.00 114 100.00 100.00 3.11e-40 SP A1XQU7 "RecName: Full=60S acidic ribosomal protein P1" 98.55 114 97.06 97.06 2.96e-38 SP P05386 "RecName: Full=60S acidic ribosomal protein P1" 100.00 114 100.00 100.00 3.11e-40 SP P19944 "RecName: Full=60S acidic ribosomal protein P1" 100.00 114 100.00 100.00 3.39e-40 SP P47955 "RecName: Full=60S acidic ribosomal protein P1" 100.00 114 98.55 100.00 1.53e-39 SP Q56K14 "RecName: Full=60S acidic ribosomal protein P1" 100.00 114 100.00 100.00 3.11e-40 TPG DAA21200 "TPA: ribosomal protein P1-like isoform 1 [Bos taurus]" 98.55 114 98.53 98.53 8.23e-39 TPG DAA25760 "TPA: 60S acidic ribosomal protein P1 [Bos taurus]" 100.00 114 100.00 100.00 3.11e-40 stop_ save_ save_entity_2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_2 _Molecular_mass 7207.247 _Mol_thiol_state . _Details . _Residue_count 70 _Mol_residue_sequence ; AMRYVASYLLAALGGNSSPS AKDIKKILDSVGIEADDDRL NKVISELNGKNIEDVIAQGI GKLASVPAGG ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 MET 3 ARG 4 TYR 5 VAL 6 ALA 7 SER 8 TYR 9 LEU 10 LEU 11 ALA 12 ALA 13 LEU 14 GLY 15 GLY 16 ASN 17 SER 18 SER 19 PRO 20 SER 21 ALA 22 LYS 23 ASP 24 ILE 25 LYS 26 LYS 27 ILE 28 LEU 29 ASP 30 SER 31 VAL 32 GLY 33 ILE 34 GLU 35 ALA 36 ASP 37 ASP 38 ASP 39 ARG 40 LEU 41 ASN 42 LYS 43 VAL 44 ILE 45 SER 46 GLU 47 LEU 48 ASN 49 GLY 50 LYS 51 ASN 52 ILE 53 GLU 54 ASP 55 VAL 56 ILE 57 ALA 58 GLN 59 GLY 60 ILE 61 GLY 62 LYS 63 LEU 64 ALA 65 SER 66 VAL 67 PRO 68 ALA 69 GLY 70 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 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 15997 HUMAN_RIBOSOME_PROTEIN_P2 100.00 70 100.00 100.00 4.98e-39 BMRB 19086 60S_ACIDIC_RIBOSOMAL_PROTEIN_P2 100.00 116 100.00 100.00 4.55e-39 PDB 2LBF "Solution Structure Of The Dimerization Domain Of Human Ribosomal Protein P1P2 HETERODIMER" 100.00 70 100.00 100.00 4.98e-39 PDB 2W1O "Nmr Structure Of Dimerization Domain Of Human Ribosomal Protein P2" 100.00 70 100.00 100.00 4.98e-39 PDB 3J3B "Structure Of The Human 60s Ribosomal Proteins" 98.57 115 100.00 100.00 1.52e-38 PDB 4BEH "Solution Structure Of Human Ribosomal Protein P1.p2 Heterodimer" 98.57 116 100.00 100.00 1.57e-38 DBJ BAB22086 "unnamed protein product [Mus musculus]" 98.57 115 98.55 100.00 2.43e-38 DBJ BAB25616 "unnamed protein product [Mus musculus]" 98.57 115 98.55 100.00 2.43e-38 DBJ BAB27066 "unnamed protein product [Mus musculus]" 98.57 115 98.55 100.00 2.43e-38 DBJ BAB28217 "unnamed protein product [Mus musculus]" 98.57 115 98.55 100.00 2.43e-38 DBJ BAB79475 "ribosomal protein P2 [Homo sapiens]" 98.57 115 100.00 100.00 1.52e-38 EMBL CAG47008 "RPLP2 [Homo sapiens]" 98.57 115 100.00 100.00 1.52e-38 EMBL CAG47044 "RPLP2 [Homo sapiens]" 98.57 115 100.00 100.00 1.52e-38 GB AAA36472 "acidic ribosomal phosphoprotein (P2) [Homo sapiens]" 98.57 115 100.00 100.00 1.52e-38 GB AAC48755 "acidic ribosomal protein P2 [Bos taurus]" 98.57 115 98.55 100.00 5.08e-38 GB AAH05354 "Ribosomal protein, large, P2 [Homo sapiens]" 98.57 115 100.00 100.00 1.52e-38 GB AAH05920 "Ribosomal protein, large, P2 [Homo sapiens]" 98.57 115 100.00 100.00 1.52e-38 GB AAH07573 "Ribosomal protein, large, P2 [Homo sapiens]" 98.57 115 100.00 100.00 1.52e-38 REF NP_000995 "60S acidic ribosomal protein P2 [Homo sapiens]" 98.57 115 100.00 100.00 1.52e-38 REF NP_001078905 "60S acidic ribosomal protein P2 [Equus caballus]" 98.57 115 97.10 100.00 1.60e-37 REF NP_001180505 "60S acidic ribosomal protein P2 [Macaca mulatta]" 98.57 115 100.00 100.00 1.52e-38 REF NP_001231795 "ribosomal protein, large, P2 [Sus scrofa]" 98.57 115 97.10 100.00 7.19e-38 REF NP_001270094 "uncharacterized protein LOC101866765 [Macaca fascicularis]" 98.57 115 100.00 100.00 1.52e-38 SP P05387 "RecName: Full=60S acidic ribosomal protein P2; AltName: Full=Renal carcinoma antigen NY-REN-44 [Homo sapiens]" 98.57 115 100.00 100.00 1.52e-38 SP P19943 "RecName: Full=60S acidic ribosomal protein P2; AltName: Full=Acidic phosphoprotein P3, partial [Oryctolagus cuniculus]" 62.86 44 100.00 100.00 2.81e-20 SP P42899 "RecName: Full=60S acidic ribosomal protein P2 [Bos taurus]" 98.57 115 98.55 100.00 5.08e-38 SP P99027 "RecName: Full=60S acidic ribosomal protein P2 [Mus musculus]" 98.57 115 98.55 100.00 2.43e-38 SP Q6X9Z5 "RecName: Full=60S acidic ribosomal protein P2 [Equus caballus]" 98.57 115 97.10 100.00 1.60e-37 TPG DAA13527 "TPA: 60S acidic ribosomal protein P2 [Bos taurus]" 98.57 115 98.55 100.00 5.08e-38 stop_ 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 Homo sapiens $entity_2 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 $entity_1 'recombinant technology' . Escherichia coli . pET3d $entity_2 'recombinant technology' . Escherichia coli . pRSETA 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 1 mM '[U-100% 13C; U-100% 15N]' $entity_2 1 mM '[U-100% 13C; U-100% 15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_ARIA _Saveframe_category software _Name ARIA _Version . loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . 'Linge, O'Donoghue and Nilges' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _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' 0.15 . M pH 6.5 . pH pressure 1 . atm temperature 298 . 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 DSS C 13 'methyl carbons' ppm 0 external direct . . . 1.0 DSS H 1 'methyl protons' ppm 0 external direct . . . 1.0 DSS N 15 nitrogen ppm 0 external 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' 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 1 1 MET HA H 4.108 . 1 2 1 1 MET HB2 H 2.133 . . 3 1 1 MET HG2 H 2.649 . . 4 1 1 MET HE H 2.098 . 1 5 1 1 MET CA C 54.857 . 1 6 1 1 MET CB C 33.049 . 1 7 1 1 MET CG C 30.957 . 1 8 1 1 MET CE C 16.889 . 1 9 2 2 ALA H H 8.565 . 1 10 2 2 ALA HA H 4.330 . 1 11 2 2 ALA HB H 1.243 . 1 12 2 2 ALA CA C 52.350 . 1 13 2 2 ALA CB C 19.353 . 1 14 3 3 SER H H 8.196 . 1 15 3 3 SER HA H 4.315 . 1 16 3 3 SER HB2 H 4.258 . . 17 3 3 SER HB3 H 4.053 . . 18 3 3 SER CA C 57.858 . 1 19 3 3 SER CB C 65.589 . 1 20 4 4 VAL H H 8.670 . 1 21 4 4 VAL HA H 3.490 . 1 22 4 4 VAL HB H 2.038 . 1 23 4 4 VAL HG1 H 1.094 . . 24 4 4 VAL HG2 H 0.881 . . 25 4 4 VAL CA C 66.928 . 1 26 4 4 VAL CB C 31.786 . 1 27 4 4 VAL CG1 C 23.084 . . 28 4 4 VAL CG2 C 21.138 . . 29 5 5 SER H H 7.963 . 1 30 5 5 SER CA C 63.056 . 1 31 6 6 GLU H H 7.202 . 1 32 6 6 GLU HA H 3.024 . 1 33 6 6 GLU HB2 H 1.610 . . 34 6 6 GLU HG2 H 1.038 . . 35 6 6 GLU CA C 59.574 . 1 36 6 6 GLU CB C 30.277 . 1 37 6 6 GLU CG C 37.756 . 1 38 7 7 LEU H H 8.071 . 1 39 7 7 LEU HA H 3.340 . 1 40 7 7 LEU HB2 H 1.004 . . 41 7 7 LEU HB3 H 1.596 . . 42 7 7 LEU HG H 1.408 . 1 43 7 7 LEU HD1 H 0.751 . . 44 7 7 LEU HD2 H 0.631 . . 45 7 7 LEU CA C 57.484 . 1 46 7 7 LEU CB C 41.451 . 1 47 7 7 LEU CG C 26.519 . 1 48 7 7 LEU CD1 C 22.507 . . 49 7 7 LEU CD2 C 25.183 . . 50 8 8 ALA H H 8.476 . 1 51 8 8 ALA HA H 3.629 . 1 52 8 8 ALA HB H 1.197 . 1 53 8 8 ALA CA C 54.870 . 1 54 8 8 ALA CB C 18.429 . 1 55 9 9 CYS H H 7.128 . 1 56 9 9 CYS HA H 3.569 . 1 57 9 9 CYS HB2 H 1.847 . . 58 9 9 CYS CA C 64.227 . 1 59 9 9 CYS CB C 25.122 . 1 60 10 10 ILE H H 7.802 . 1 61 10 10 ILE HA H 3.343 . 1 62 10 10 ILE HB H 1.614 . 1 63 10 10 ILE HG2 H 0.725 . 1 64 10 10 ILE HD1 H 0.729 . 1 65 10 10 ILE CA C 65.953 . 1 66 10 10 ILE CB C 37.831 . 1 67 10 10 ILE CG2 C 17.021 . 1 68 10 10 ILE CD1 C 14.101 . 1 69 11 11 TYR H H 8.691 . 1 70 11 11 TYR HA H 4.383 . 1 71 11 11 TYR HB2 H 3.253 . . 72 11 11 TYR HB3 H 2.831 . . 73 11 11 TYR HD1 H 6.595 . . 74 11 11 TYR HE1 H 6.491 . . 75 11 11 TYR CA C 58.997 . 1 76 11 11 TYR CB C 36.896 . 1 77 12 12 SER H H 7.749 . 1 78 12 12 SER HB2 H 3.962 . . 79 12 12 SER CA C 63.657 . 1 80 13 13 ALA H H 8.116 . 1 81 13 13 ALA HA H 3.837 . 1 82 13 13 ALA HB H 1.449 . 1 83 13 13 ALA CA C 55.567 . 1 84 13 13 ALA CB C 18.090 . 1 85 14 14 LEU H H 8.245 . 1 86 14 14 LEU HA H 3.981 . 1 87 14 14 LEU HB2 H 1.970 . . 88 14 14 LEU HG H 0.955 . 1 89 14 14 LEU HD1 H 0.934 . . 90 14 14 LEU HD2 H 0.863 . . 91 14 14 LEU CA C 58.154 . 1 92 14 14 LEU CB C 41.985 . 1 93 14 14 LEU CG C 26.497 . 1 94 14 14 LEU CD1 C 23.280 . . 95 15 15 ILE H H 7.743 . 1 96 15 15 ILE HA H 3.106 . 1 97 15 15 ILE HB H 2.000 . 1 98 15 15 ILE HG2 H 0.658 . 1 99 15 15 ILE HD1 H 0.707 . 1 100 15 15 ILE CA C 66.865 . 1 101 15 15 ILE CB C 38.665 . 1 102 15 15 ILE CG2 C 18.019 . 1 103 15 15 ILE CD1 C 16.956 . 1 104 16 16 LEU H H 7.369 . 1 105 16 16 LEU HA H 3.796 . 1 106 16 16 LEU HB2 H 1.921 . . 107 16 16 LEU HD1 H 0.824 . . 108 16 16 LEU HD2 H 0.793 . . 109 16 16 LEU CA C 57.627 . 1 110 16 16 LEU CB C 40.625 . 1 111 16 16 LEU CD1 C 23.005 . . 112 16 16 LEU CD2 C 27.700 . . 113 17 17 HIS H H 8.851 . 1 114 17 17 HIS HA H 4.450 . 1 115 17 17 HIS HB2 H 3.300 . . 116 17 17 HIS HB3 H 3.216 . . 117 17 17 HIS HD2 H 7.050 . 1 118 17 17 HIS HE1 H 7.773 . 1 119 17 17 HIS CA C 58.843 . 1 120 17 17 HIS CB C 29.851 . 1 121 18 18 ASP H H 7.748 . 1 122 18 18 ASP HA H 4.486 . 1 123 18 18 ASP HB2 H 2.653 . . 124 18 18 ASP CA C 56.505 . 1 125 18 18 ASP CB C 43.133 . 1 126 19 19 ASP H H 7.459 . 1 127 19 19 ASP HA H 5.135 . 1 128 19 19 ASP HB2 H 2.644 . . 129 19 19 ASP HB3 H 1.995 . . 130 19 19 ASP CA C 52.766 . 1 131 19 19 ASP CB C 43.836 . 1 132 20 20 GLU H H 7.814 . 1 133 20 20 GLU HA H 3.775 . 1 134 20 20 GLU HB2 H 2.110 . . 135 20 20 GLU HG2 H 2.115 . . 136 20 20 GLU CA C 57.195 . 1 137 20 20 GLU CB C 27.248 . 1 138 20 20 GLU CG C 36.853 . 1 139 21 21 VAL H H 7.863 . 1 140 21 21 VAL HA H 4.147 . 1 141 21 21 VAL HB H 1.966 . 1 142 21 21 VAL HG1 H 0.947 . . 143 21 21 VAL HG2 H 1.003 . . 144 21 21 VAL CA C 61.286 . 1 145 21 21 VAL CB C 32.893 . 1 146 21 21 VAL CG1 C 22.165 . . 147 21 21 VAL CG2 C 21.941 . . 148 22 22 THR H H 8.423 . 1 149 22 22 THR HA H 3.984 . 1 150 22 22 THR HB H 3.979 . 1 151 22 22 THR HG2 H 1.210 . 1 152 22 22 THR CA C 63.642 . 1 153 22 22 THR CB C 69.167 . 1 154 22 22 THR CG2 C 22.056 . 1 155 23 23 VAL H H 8.926 . 1 156 23 23 VAL HA H 3.628 . 1 157 23 23 VAL HB H 2.126 . 1 158 23 23 VAL HG1 H 0.822 . . 159 23 23 VAL HG2 H 1.103 . . 160 23 23 VAL CA C 64.279 . 1 161 23 23 VAL CB C 30.974 . 1 162 23 23 VAL CG1 C 22.294 . . 163 23 23 VAL CG2 C 21.810 . . 164 24 24 THR H H 6.627 . 1 165 24 24 THR HA H 4.704 . 1 166 24 24 THR HB H 4.616 . 1 167 24 24 THR HG2 H 1.153 . 1 168 24 24 THR CA C 58.429 . 1 169 24 24 THR CB C 71.574 . 1 170 24 24 THR CG2 C 22.069 . 1 171 25 25 GLU H H 9.423 . 1 172 25 25 GLU HA H 3.618 . 1 173 25 25 GLU HB2 H 1.992 . . 174 25 25 GLU HG2 H 2.223 . . 175 25 25 GLU CA C 60.140 . 1 176 25 25 GLU CB C 30.043 . 1 177 25 25 GLU CG C 35.654 . 1 178 26 26 ASP H H 8.606 . 1 179 26 26 ASP HA H 4.425 . 1 180 26 26 ASP HB2 H 2.663 . . 181 26 26 ASP HB3 H 2.558 . . 182 26 26 ASP CA C 56.999 . 1 183 26 26 ASP CB C 40.127 . 1 184 27 27 LYS H H 7.524 . 1 185 27 27 LYS HA H 4.124 . 1 186 27 27 LYS HB2 H 1.846 . . 187 27 27 LYS HG2 H 1.432 . . 188 27 27 LYS HG3 H 1.587 . . 189 27 27 LYS HD2 H 1.705 . . 190 27 27 LYS HE2 H 3.019 . . 191 27 27 LYS CA C 59.523 . 1 192 27 27 LYS CB C 34.493 . 1 193 27 27 LYS CG C 26.705 . 1 194 27 27 LYS CD C 29.664 . 1 195 27 27 LYS CE C 42.361 . 1 196 28 28 ILE H H 7.781 . 1 197 28 28 ILE HA H 3.584 . 1 198 28 28 ILE HB H 1.847 . 1 199 28 28 ILE HG2 H 0.883 . 1 200 28 28 ILE HD1 H 0.765 . 1 201 28 28 ILE CA C 66.355 . 1 202 28 28 ILE CB C 38.469 . 1 203 28 28 ILE CG1 C 28.871 . 1 204 28 28 ILE CG2 C 17.973 . 1 205 28 28 ILE CD1 C 13.803 . 1 206 29 29 ASN H H 8.362 . 1 207 29 29 ASN HA H 4.392 . 1 208 29 29 ASN HB2 H 2.612 . . 209 29 29 ASN HB3 H 2.834 . . 210 29 29 ASN CA C 56.273 . 1 211 29 29 ASN CB C 38.367 . 1 212 30 30 ALA H H 7.862 . 1 213 30 30 ALA HA H 4.055 . 1 214 30 30 ALA HB H 1.438 . 1 215 30 30 ALA CA C 55.391 . 1 216 30 30 ALA CB C 18.075 . 1 217 31 31 LEU H H 7.476 . 1 218 31 31 LEU HA H 4.028 . 1 219 31 31 LEU HB2 H 2.119 . . 220 31 31 LEU HB3 H 1.142 . . 221 31 31 LEU HG H 1.786 . 1 222 31 31 LEU HD1 H 0.795 . . 223 31 31 LEU HD2 H 0.853 . . 224 31 31 LEU CA C 58.290 . 1 225 31 31 LEU CB C 42.837 . 1 226 31 31 LEU CG C 26.663 . 1 227 31 31 LEU CD1 C 25.822 . . 228 31 31 LEU CD2 C 27.439 . . 229 32 32 ILE H H 8.030 . 1 230 32 32 ILE HA H 3.389 . 1 231 32 32 ILE HB H 1.866 . 1 232 32 32 ILE HG12 H 1.893 . . 233 32 32 ILE HG2 H 0.816 . 1 234 32 32 ILE HD1 H 0.660 . 1 235 32 32 ILE CA C 66.346 . 1 236 32 32 ILE CB C 38.163 . 1 237 32 32 ILE CG1 C 29.948 . 1 238 32 32 ILE CG2 C 18.700 . 1 239 32 32 ILE CD1 C 15.600 . 1 240 33 33 LYS H H 8.254 . 1 241 33 33 LYS HA H 4.164 . 1 242 33 33 LYS HB2 H 1.901 . . 243 33 33 LYS HG2 H 1.425 . . 244 33 33 LYS HG3 H 1.524 . . 245 33 33 LYS HD2 H 1.662 . . 246 33 33 LYS HE2 H 2.969 . . 247 33 33 LYS CA C 58.883 . 1 248 33 33 LYS CB C 32.184 . 1 249 33 33 LYS CG C 25.257 . 1 250 33 33 LYS CD C 29.072 . 1 251 34 34 ALA H H 8.155 . 1 252 34 34 ALA HA H 4.097 . 1 253 34 34 ALA HB H 1.590 . 1 254 34 34 ALA CA C 54.687 . 1 255 34 34 ALA CB C 19.057 . 1 256 35 35 ALA H H 7.916 . 1 257 35 35 ALA HA H 4.088 . 1 258 35 35 ALA HB H 1.338 . 1 259 35 35 ALA CA C 52.074 . 1 260 35 35 ALA CB C 20.459 . 1 261 36 36 GLY H H 7.872 . 1 262 36 36 GLY HA2 H 4.055 . . 263 36 36 GLY HA3 H 3.807 . . 264 36 36 GLY CA C 45.976 . 1 265 37 37 VAL H H 7.447 . 1 266 37 37 VAL HA H 3.864 . 1 267 37 37 VAL HB H 1.733 . 1 268 37 37 VAL HG1 H 0.651 . . 269 37 37 VAL HG2 H 0.728 . . 270 37 37 VAL CA C 61.471 . 1 271 37 37 VAL CB C 32.893 . 1 272 37 37 VAL CG1 C 22.146 . . 273 37 37 VAL CG2 C 23.004 . . 274 38 38 ASN H H 8.555 . 1 275 38 38 ASN HA H 4.754 . 1 276 38 38 ASN HB2 H 2.706 . . 277 38 38 ASN HB3 H 2.642 . . 278 38 38 ASN CA C 52.725 . 1 279 38 38 ASN CB C 38.743 . 1 280 39 39 VAL H H 7.969 . 1 281 39 39 VAL HA H 4.468 . 1 282 39 39 VAL HB H 1.895 . 1 283 39 39 VAL HG1 H 0.806 . . 284 39 39 VAL HG2 H 0.728 . . 285 39 39 VAL CA C 59.078 . 1 286 39 39 VAL CB C 35.414 . 1 287 39 39 VAL CG1 C 20.852 . . 288 39 39 VAL CG2 C 21.572 . . 289 40 40 GLU H H 8.704 . 1 290 40 40 GLU HA H 4.519 . 1 291 40 40 GLU HG2 H 2.436 . . 292 40 40 GLU CA C 55.350 . 1 293 40 40 GLU CB C 28.953 . 1 294 40 40 GLU CG C 36.593 . 1 295 41 41 PRO HA H 4.280 . 1 296 41 41 PRO HB2 H 2.336 . . 297 41 41 PRO HB3 H 2.035 . . 298 41 41 PRO HG2 H 2.095 . . 299 41 41 PRO HD2 H 3.872 . . 300 41 41 PRO HD3 H 3.839 . . 301 41 41 PRO CA C 65.195 . 1 302 41 41 PRO CB C 32.119 . 1 303 41 41 PRO CG C 27.640 . 1 304 41 41 PRO CD C 51.045 . 1 305 42 42 PHE H H 6.941 . 1 306 42 42 PHE HA H 4.614 . 1 307 42 42 PHE HB2 H 2.924 . . 308 42 42 PHE HB3 H 3.161 . . 309 42 42 PHE HD1 H 6.720 . . 310 42 42 PHE HE1 H 6.625 . . 311 42 42 PHE HZ H 7.073 . 1 312 42 42 PHE CA C 57.209 . 1 313 42 42 PHE CB C 38.260 . 1 314 43 43 TRP H H 7.206 . 1 315 43 43 TRP HA H 4.404 . 1 316 43 43 TRP HB2 H 3.286 . . 317 43 43 TRP HB3 H 2.914 . . 318 43 43 TRP HD1 H 7.096 . 1 319 43 43 TRP HE1 H 10.404 . 1 320 43 43 TRP HE3 H 7.694 . 1 321 43 43 TRP HZ2 H 7.610 . 1 322 43 43 TRP HH2 H 7.249 . 1 323 43 43 TRP CA C 62.653 . 1 324 43 43 TRP CB C 27.410 . 1 325 44 44 PRO HA H 4.236 . 1 326 44 44 PRO HB2 H 1.999 . . 327 44 44 PRO CA C 67.323 . 1 328 44 44 PRO CB C 31.878 . 1 329 45 45 GLY H H 8.579 . 1 330 45 45 GLY HA2 H 3.794 . . 331 45 45 GLY CA C 47.274 . 1 332 46 46 LEU H H 7.720 . 1 333 46 46 LEU HA H 4.121 . 1 334 46 46 LEU HB2 H 1.933 . . 335 46 46 LEU HB3 H 1.635 . . 336 46 46 LEU HG H 1.749 . 1 337 46 46 LEU HD1 H 0.701 . . 338 46 46 LEU CA C 58.075 . 1 339 46 46 LEU CB C 42.339 . 1 340 46 46 LEU CG C 26.773 . 1 341 46 46 LEU CD1 C 23.497 . . 342 46 46 LEU CD2 C 25.549 . . 343 47 47 PHE H H 8.779 . 1 344 47 47 PHE HA H 3.913 . 1 345 47 47 PHE HB2 H 3.259 . . 346 47 47 PHE HB3 H 2.735 . . 347 47 47 PHE HD1 H 7.328 . . 348 47 47 PHE HE1 H 7.104 . . 349 47 47 PHE CA C 62.371 . 1 350 47 47 PHE CB C 39.798 . 1 351 48 48 ALA H H 8.536 . 1 352 48 48 ALA HA H 3.840 . 1 353 48 48 ALA HB H 1.438 . 1 354 48 48 ALA CA C 55.758 . 1 355 48 48 ALA CB C 18.011 . 1 356 49 49 LYS H H 7.735 . 1 357 49 49 LYS HA H 4.098 . 1 358 49 49 LYS HB2 H 1.893 . . 359 49 49 LYS HG2 H 1.461 . . 360 49 49 LYS HD2 H 1.655 . . 361 49 49 LYS HE2 H 2.951 . . 362 49 49 LYS CA C 59.091 . 1 363 49 49 LYS CB C 32.550 . 1 364 49 49 LYS CG C 25.373 . 1 365 49 49 LYS CD C 29.152 . 1 366 49 49 LYS CE C 42.159 . 1 367 50 50 ALA H H 7.790 . 1 368 50 50 ALA HA H 4.105 . 1 369 50 50 ALA HB H 1.358 . 1 370 50 50 ALA CA C 54.641 . 1 371 50 50 ALA CB C 19.265 . 1 372 51 51 LEU H H 7.871 . 1 373 51 51 LEU HA H 4.520 . 1 374 51 51 LEU HB2 H 1.834 . . 375 51 51 LEU HB3 H 1.782 . . 376 51 51 LEU HD1 H 0.851 . . 377 51 51 LEU HD2 H 0.825 . . 378 51 51 LEU CA C 55.148 . 1 379 51 51 LEU CB C 41.074 . 1 380 51 51 LEU CD1 C 26.774 . . 381 51 51 LEU CD2 C 23.591 . . 382 52 52 ALA H H 7.206 . 1 383 52 52 ALA HA H 4.193 . 1 384 52 52 ALA HB H 1.475 . 1 385 52 52 ALA CA C 54.409 . 1 386 52 52 ALA CB C 18.541 . 1 387 53 53 ASN H H 8.152 . 1 388 53 53 ASN HA H 4.850 . 1 389 53 53 ASN HB2 H 2.926 . . 390 53 53 ASN HB3 H 2.693 . . 391 53 53 ASN CA C 53.296 . 1 392 53 53 ASN CB C 40.267 . 1 393 54 54 VAL H H 7.537 . 1 394 54 54 VAL HA H 4.292 . 1 395 54 54 VAL HB H 2.083 . 1 396 54 54 VAL HG1 H 0.889 . . 397 54 54 VAL HG2 H 0.859 . . 398 54 54 VAL CA C 60.958 . 1 399 54 54 VAL CB C 34.465 . 1 400 54 54 VAL CG1 C 21.147 . . 401 54 54 VAL CG2 C 20.600 . . 402 55 55 ASN H H 8.256 . 1 403 55 55 ASN HA H 4.834 . 1 404 55 55 ASN HB2 H 2.780 . . 405 55 55 ASN CA C 52.244 . 1 406 55 55 ASN CB C 39.143 . 1 407 56 56 ILE HA H 3.911 . 1 408 56 56 ILE HB H 1.846 . 1 409 56 56 ILE HG12 H 1.459 . . 410 56 56 ILE HG13 H 1.252 . . 411 56 56 ILE HG2 H 0.823 . 1 412 56 56 ILE HD1 H 0.958 . 1 413 56 56 ILE CA C 62.288 . 1 414 56 56 ILE CB C 37.993 . 1 415 56 56 ILE CG1 C 29.085 . 1 416 56 56 ILE CG2 C 18.246 . 1 417 56 56 ILE CD1 C 14.297 . 1 418 57 57 GLY H H 8.343 . 1 419 57 57 GLY HA2 H 3.735 . . 420 57 57 GLY HA3 H 3.867 . . 421 57 57 GLY CA C 46.884 . 1 422 58 58 SER H H 7.806 . 1 423 58 58 SER HA H 4.302 . 1 424 58 58 SER HB2 H 3.909 . . 425 58 58 SER CA C 60.511 . 1 426 58 58 SER CB C 63.291 . 1 427 59 59 LEU H H 7.817 . 1 428 59 59 LEU HA H 4.210 . 1 429 59 59 LEU HB2 H 1.719 . . 430 59 59 LEU HG H 1.626 . 1 431 59 59 LEU HD1 H 0.806 . . 432 59 59 LEU HD2 H 0.769 . . 433 59 59 LEU CA C 56.554 . 1 434 59 59 LEU CB C 42.601 . 1 435 59 59 LEU CG C 26.990 . 1 436 59 59 LEU CD1 C 25.313 . . 437 59 59 LEU CD2 C 23.991 . . 438 60 60 ILE H H 7.692 . 1 439 60 60 ILE HA H 4.052 . 1 440 60 60 ILE HB H 1.945 . 1 441 60 60 ILE HG12 H 1.575 . . 442 60 60 ILE HG13 H 1.207 . . 443 60 60 ILE HG2 H 0.885 . 1 444 60 60 ILE HD1 H 0.808 . 1 445 60 60 ILE CA C 62.493 . 1 446 60 60 ILE CB C 38.462 . 1 447 60 60 ILE CG1 C 27.590 . 1 448 60 60 ILE CG2 C 17.915 . 1 449 60 60 ILE CD1 C 13.884 . 1 450 61 61 CYS H H 7.919 . 1 451 61 61 CYS HA H 4.399 . 1 452 61 61 CYS HB2 H 2.911 . . 453 61 61 CYS CA C 59.707 . 1 454 61 61 CYS CB C 27.808 . 1 455 62 62 ASN H H 8.254 . 1 456 62 62 ASN HA H 4.751 . 1 457 62 62 ASN HB2 H 2.827 . . 458 62 62 ASN CA C 53.746 . 1 459 62 62 ASN CB C 38.966 . 1 460 63 63 VAL H H 7.974 . 1 461 63 63 VAL HA H 4.075 . 1 462 63 63 VAL HB H 2.130 . 1 463 63 63 VAL HG1 H 0.928 . . 464 63 63 VAL CA C 62.868 . 1 465 63 63 VAL CB C 32.401 . 1 466 63 63 VAL CG1 C 21.151 . . 467 64 64 GLY H H 8.434 . 1 468 64 64 GLY HA2 H 3.954 . . 469 64 64 GLY CA C 45.432 . 1 470 65 65 ALA H H 8.117 . 1 471 65 65 ALA HA H 4.333 . 1 472 65 65 ALA HB H 1.385 . 1 473 65 65 ALA CA C 52.527 . 1 474 65 65 ALA CB C 19.362 . 1 475 66 66 GLY H H 8.411 . 1 476 66 66 GLY HA2 H 3.984 . . 477 66 66 GLY CA C 45.293 . 1 478 67 67 GLY H H 8.072 . 1 479 67 67 GLY HA2 H 4.064 . . 480 67 67 GLY HA3 H 3.733 . . 481 67 67 GLY CA C 44.500 . 1 482 68 68 PRO HA H 4.560 . 1 483 68 68 PRO HB2 H 2.347 . . 484 68 68 PRO HB3 H 2.157 . . 485 68 68 PRO HG2 H 1.896 . . 486 68 68 PRO HD2 H 3.519 . . 487 68 68 PRO HD3 H 3.553 . . 488 68 68 PRO CA C 62.795 . 1 489 68 68 PRO CB C 34.581 . 1 490 68 68 PRO CG C 24.891 . 1 491 68 68 PRO CD C 50.439 . 1 492 69 69 ALA H H 8.201 . 1 493 69 69 ALA CA C 54.149 . 1 494 69 69 ALA CB C 19.997 . 1 stop_ save_ save_assigned_chem_shift_list_1_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' 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_2 _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 1 100 1 ALA HA H 4.300 . 1 2 100 1 ALA HB H 1.369 . 1 3 100 1 ALA CA C 52.587 . 1 4 100 1 ALA CB C 19.612 . 1 5 101 2 MET H H 8.037 . 1 6 101 2 MET HG2 H 2.653 . . 7 101 2 MET HE H 2.079 . 1 8 101 2 MET CA C 58.262 . 1 9 101 2 MET CB C 32.264 . 1 10 101 2 MET CE C 17.477 . 1 11 103 4 TYR HA H 4.402 . 1 12 103 4 TYR HB2 H 3.126 . . 13 103 4 TYR HD1 H 7.000 . . 14 103 4 TYR HE1 H 6.728 . . 15 103 4 TYR CA C 59.822 . 1 16 103 4 TYR CB C 37.979 . 1 17 104 5 VAL HA H 3.380 . 1 18 104 5 VAL HB H 1.989 . 1 19 104 5 VAL HG1 H 0.960 . . 20 104 5 VAL HG2 H 0.771 . . 21 104 5 VAL CA C 66.299 . 1 22 104 5 VAL CB C 32.322 . 1 23 104 5 VAL CG1 C 22.997 . . 24 104 5 VAL CG2 C 21.142 . . 25 105 6 ALA H H 8.722 . 1 26 105 6 ALA HA H 3.742 . 1 27 105 6 ALA HB H 1.417 . 1 28 105 6 ALA CA C 55.177 . 1 29 105 6 ALA CB C 18.654 . 1 30 106 7 SER H H 6.873 . 1 31 106 7 SER CA C 63.520 . 1 32 106 7 SER CB C 64.560 . 1 33 107 8 TYR H H 7.834 . 1 34 107 8 TYR HA H 3.634 . 1 35 107 8 TYR HB2 H 3.376 . . 36 107 8 TYR HB3 H 2.753 . . 37 107 8 TYR HD1 H 6.628 . . 38 107 8 TYR HE1 H 6.681 . . 39 107 8 TYR CA C 61.711 . 1 40 107 8 TYR CB C 38.598 . 1 41 108 9 LEU H H 7.909 . 1 42 108 9 LEU HA H 3.780 . 1 43 108 9 LEU HB2 H 0.737 . . 44 108 9 LEU HB3 H 0.890 . . 45 108 9 LEU HG H 1.681 . 1 46 108 9 LEU HD1 H 0.758 . . 47 108 9 LEU HD2 H 0.491 . . 48 108 9 LEU CA C 57.379 . 1 49 108 9 LEU CB C 40.013 . 1 50 108 9 LEU CG C 26.774 . 1 51 108 9 LEU CD1 C 25.804 . . 52 108 9 LEU CD2 C 22.691 . . 53 109 10 LEU H H 8.007 . 1 54 109 10 LEU HA H 3.952 . 1 55 109 10 LEU HB2 H 1.885 . . 56 109 10 LEU HB3 H 1.627 . . 57 109 10 LEU HG H 1.477 . 1 58 109 10 LEU HD1 H 1.004 . . 59 109 10 LEU HD2 H 0.752 . . 60 109 10 LEU CA C 58.151 . 1 61 109 10 LEU CB C 42.327 . 1 62 109 10 LEU CG C 26.530 . 1 63 109 10 LEU CD1 C 26.526 . . 64 109 10 LEU CD2 C 24.675 . . 65 110 11 ALA H H 8.261 . 1 66 110 11 ALA HA H 4.005 . 1 67 110 11 ALA HB H 1.297 . 1 68 110 11 ALA CA C 54.605 . 1 69 110 11 ALA CB C 16.808 . 1 70 111 12 ALA H H 8.239 . 1 71 111 12 ALA HA H 4.272 . 1 72 111 12 ALA HB H 1.355 . 1 73 111 12 ALA CA C 54.534 . 1 74 111 12 ALA CB C 17.454 . 1 75 112 13 LEU H H 8.234 . 1 76 112 13 LEU HA H 4.088 . 1 77 112 13 LEU HB2 H 2.096 . . 78 112 13 LEU HB3 H 1.697 . . 79 112 13 LEU HG H 2.036 . 1 80 112 13 LEU HD1 H 0.982 . . 81 112 13 LEU HD2 H 1.020 . . 82 112 13 LEU CA C 57.145 . 1 83 112 13 LEU CB C 42.105 . 1 84 112 13 LEU CG C 26.271 . 1 85 112 13 LEU CD1 C 25.551 . . 86 112 13 LEU CD2 C 24.392 . . 87 113 14 GLY H H 7.540 . 1 88 113 14 GLY HA2 H 3.755 . . 89 113 14 GLY HA3 H 4.025 . . 90 113 14 GLY CA C 45.322 . 1 91 114 15 GLY H H 7.705 . 1 92 114 15 GLY HA2 H 4.406 . . 93 114 15 GLY HA3 H 3.615 . . 94 114 15 GLY CA C 44.814 . 1 95 115 16 ASN H H 7.346 . 1 96 115 16 ASN HA H 4.704 . 1 97 115 16 ASN HB2 H 2.633 . . 98 115 16 ASN HB3 H 2.372 . . 99 115 16 ASN CA C 51.131 . 1 100 115 16 ASN CB C 37.683 . 1 101 116 17 SER H H 8.177 . 1 102 116 17 SER HA H 4.129 . 1 103 116 17 SER HB2 H 3.998 . . 104 116 17 SER HB3 H 3.884 . . 105 116 17 SER CA C 59.637 . 1 106 116 17 SER CB C 63.499 . 1 107 117 18 SER H H 7.779 . 1 108 117 18 SER HA H 4.571 . 1 109 117 18 SER HB2 H 3.630 . . 110 117 18 SER HB3 H 3.787 . . 111 117 18 SER CA C 54.844 . 1 112 117 18 SER CB C 62.961 . 1 113 118 19 PRO HA H 4.269 . 1 114 118 19 PRO HB2 H 1.646 . . 115 118 19 PRO HB3 H 1.432 . . 116 118 19 PRO HG2 H 1.150 . . 117 118 19 PRO HD2 H 2.808 . . 118 118 19 PRO HD3 H 3.167 . . 119 118 19 PRO CA C 63.156 . 1 120 118 19 PRO CB C 31.899 . 1 121 118 19 PRO CG C 27.312 . 1 122 118 19 PRO CD C 49.000 . 1 123 119 20 SER H H 9.237 . 1 124 119 20 SER HA H 4.791 . 1 125 119 20 SER HB2 H 4.290 . . 126 119 20 SER HB3 H 3.968 . . 127 119 20 SER CA C 55.648 . 1 128 119 20 SER CB C 66.944 . 1 129 120 21 ALA H H 9.185 . 1 130 120 21 ALA HA H 3.820 . 1 131 120 21 ALA HB H 1.389 . 1 132 120 21 ALA CA C 56.155 . 1 133 120 21 ALA CB C 17.750 . 1 134 121 22 LYS H H 8.027 . 1 135 121 22 LYS HA H 3.862 . 1 136 121 22 LYS HB2 H 1.733 . . 137 121 22 LYS HB3 H 1.777 . . 138 121 22 LYS HG2 H 1.485 . . 139 121 22 LYS HG3 H 1.371 . . 140 121 22 LYS HD2 H 1.650 . . 141 121 22 LYS HE2 H 2.959 . . 142 121 22 LYS CA C 59.664 . 1 143 121 22 LYS CB C 32.036 . 1 144 121 22 LYS CG C 25.047 . 1 145 121 22 LYS CD C 29.007 . 1 146 122 23 ASP H H 7.621 . 1 147 122 23 ASP HA H 4.284 . 1 148 122 23 ASP HB2 H 2.938 . . 149 122 23 ASP HB3 H 2.459 . . 150 122 23 ASP CA C 57.189 . 1 151 122 23 ASP CB C 40.697 . 1 152 123 24 ILE H H 7.799 . 1 153 123 24 ILE HA H 3.666 . 1 154 123 24 ILE HB H 2.046 . 1 155 123 24 ILE HG12 H 1.476 . . 156 123 24 ILE HG13 H 1.287 . . 157 123 24 ILE HG2 H 1.053 . 1 158 123 24 ILE HD1 H 0.795 . 1 159 123 24 ILE CA C 64.260 . 1 160 123 24 ILE CB C 36.895 . 1 161 123 24 ILE CG1 C 29.232 . 1 162 123 24 ILE CG2 C 18.242 . 1 163 123 24 ILE CD1 C 12.323 . 1 164 124 25 LYS H H 8.691 . 1 165 124 25 LYS HA H 3.805 . 1 166 124 25 LYS HB2 H 1.899 . . 167 124 25 LYS HB3 H 1.723 . . 168 124 25 LYS HG2 H 1.264 . . 169 124 25 LYS HD2 H 1.572 . . 170 124 25 LYS HD3 H 1.641 . . 171 124 25 LYS HE2 H 2.856 . . 172 124 25 LYS CA C 60.641 . 1 173 124 25 LYS CB C 31.789 . 1 174 124 25 LYS CG C 26.415 . 1 175 124 25 LYS CD C 29.214 . 1 176 124 25 LYS CE C 41.508 . 1 177 125 26 LYS H H 7.640 . 1 178 125 26 LYS HA H 4.068 . 1 179 125 26 LYS HB2 H 1.936 . . 180 125 26 LYS HG2 H 1.588 . . 181 125 26 LYS HG3 H 1.385 . . 182 125 26 LYS HD2 H 1.752 . . 183 125 26 LYS HE2 H 3.020 . . 184 125 26 LYS CA C 59.697 . 1 185 125 26 LYS CB C 32.287 . 1 186 125 26 LYS CG C 25.240 . 1 187 125 26 LYS CD C 29.360 . 1 188 125 26 LYS CE C 41.942 . 1 189 126 27 ILE H H 7.207 . 1 190 126 27 ILE HA H 3.585 . 1 191 126 27 ILE HB H 2.093 . 1 192 126 27 ILE HG2 H 0.912 . 1 193 126 27 ILE HD1 H 0.876 . 1 194 126 27 ILE CA C 65.706 . 1 195 126 27 ILE CB C 38.882 . 1 196 126 27 ILE CG2 C 18.355 . 1 197 126 27 ILE CD1 C 14.899 . 1 198 127 28 LEU H H 8.307 . 1 199 127 28 LEU HA H 3.840 . 1 200 127 28 LEU HB2 H 1.847 . . 201 127 28 LEU HG H 1.864 . 1 202 127 28 LEU HD1 H 0.607 . . 203 127 28 LEU HD2 H 0.711 . . 204 127 28 LEU CA C 58.437 . 1 205 127 28 LEU CB C 39.880 . 1 206 127 28 LEU CG C 26.350 . 1 207 127 28 LEU CD1 C 23.252 . . 208 127 28 LEU CD2 C 26.292 . . 209 128 29 ASP H H 9.056 . 1 210 128 29 ASP HA H 4.411 . 1 211 128 29 ASP HB2 H 2.833 . . 212 128 29 ASP HB3 H 2.553 . . 213 128 29 ASP CA C 56.609 . 1 214 128 29 ASP CB C 40.915 . 1 215 129 30 SER H H 7.550 . 1 216 129 30 SER HA H 4.096 . 1 217 129 30 SER HB2 H 3.890 . . 218 129 30 SER HB3 H 3.848 . . 219 129 30 SER CA C 62.486 . 1 220 129 30 SER CB C 63.093 . 1 221 130 31 VAL H H 6.934 . 1 222 130 31 VAL HA H 4.616 . 1 223 130 31 VAL HB H 2.444 . 1 224 130 31 VAL HG1 H 1.024 . . 225 130 31 VAL HG2 H 0.829 . . 226 130 31 VAL CA C 59.913 . 1 227 130 31 VAL CB C 32.026 . 1 228 130 31 VAL CG1 C 22.850 . . 229 130 31 VAL CG2 C 18.888 . . 230 131 32 GLY H H 7.654 . 1 231 131 32 GLY HA2 H 3.912 . . 232 131 32 GLY CA C 47.019 . 1 233 132 33 ILE H H 7.580 . 1 234 132 33 ILE HA H 4.004 . 1 235 132 33 ILE HB H 1.442 . 1 236 132 33 ILE HG2 H 0.764 . 1 237 132 33 ILE HD1 H 0.719 . 1 238 132 33 ILE CA C 61.197 . 1 239 132 33 ILE CB C 38.766 . 1 240 132 33 ILE CG2 C 17.743 . 1 241 132 33 ILE CD1 C 15.268 . 1 242 133 34 GLU H H 8.739 . 1 243 133 34 GLU HA H 4.147 . 1 244 133 34 GLU HB2 H 1.895 . . 245 133 34 GLU HG2 H 2.272 . . 246 133 34 GLU HG3 H 2.174 . . 247 133 34 GLU CA C 56.416 . 1 248 133 34 GLU CB C 31.085 . 1 249 133 34 GLU CG C 36.408 . 1 250 134 35 ALA H H 8.572 . 1 251 134 35 ALA HA H 4.923 . 1 252 134 35 ALA HB H 1.286 . 1 253 134 35 ALA CA C 58.702 . 1 254 134 35 ALA CB C 21.931 . 1 255 135 36 ASP H H 8.137 . 1 256 135 36 ASP HA H 4.751 . 1 257 135 36 ASP HB2 H 2.594 . . 258 135 36 ASP HB3 H 2.762 . . 259 135 36 ASP CA C 52.641 . 1 260 135 36 ASP CB C 42.603 . 1 261 136 37 ASP H H 8.792 . 1 262 136 37 ASP HA H 4.084 . 1 263 136 37 ASP HB2 H 2.500 . . 264 136 37 ASP CA C 58.451 . 1 265 136 37 ASP CB C 41.172 . 1 266 137 38 ASP H H 8.159 . 1 267 137 38 ASP HA H 4.372 . 1 268 137 38 ASP HB2 H 2.636 . . 269 137 38 ASP HB3 H 2.724 . . 270 137 38 ASP CA C 57.579 . 1 271 137 38 ASP CB C 40.821 . 1 272 138 39 ARG H H 7.901 . 1 273 138 39 ARG HA H 3.908 . 1 274 138 39 ARG HB2 H 1.779 . . 275 138 39 ARG HB3 H 1.812 . . 276 138 39 ARG HG2 H 1.723 . . 277 138 39 ARG HD2 H 3.262 . . 278 138 39 ARG CA C 58.497 . 1 279 138 39 ARG CB C 30.031 . 1 280 138 39 ARG CG C 27.715 . 1 281 138 39 ARG CD C 42.833 . 1 282 139 40 LEU H H 8.222 . 1 283 139 40 LEU HA H 3.207 . 1 284 139 40 LEU HB2 H 1.699 . . 285 139 40 LEU HG H 1.417 . 1 286 139 40 LEU HD1 H 0.868 . . 287 139 40 LEU HD2 H 0.929 . . 288 139 40 LEU CA C 58.173 . 1 289 139 40 LEU CB C 41.415 . 1 290 139 40 LEU CG C 27.164 . 1 291 139 40 LEU CD1 C 26.512 . . 292 139 40 LEU CD2 C 24.054 . . 293 140 41 ASN H H 8.246 . 1 294 140 41 ASN HA H 4.296 . 1 295 140 41 ASN HB2 H 2.856 . . 296 140 41 ASN HB3 H 2.706 . . 297 140 41 ASN CA C 56.191 . 1 298 140 41 ASN CB C 37.660 . 1 299 141 42 LYS H H 7.623 . 1 300 141 42 LYS HA H 4.034 . 1 301 141 42 LYS HB2 H 1.896 . . 302 141 42 LYS HG2 H 1.393 . . 303 141 42 LYS HD2 H 1.624 . . 304 141 42 LYS HE2 H 2.935 . . 305 141 42 LYS CA C 59.387 . 1 306 141 42 LYS CB C 32.303 . 1 307 142 43 VAL H H 7.848 . 1 308 142 43 VAL HA H 3.586 . 1 309 142 43 VAL HB H 2.100 . 1 310 142 43 VAL HG1 H 0.772 . . 311 142 43 VAL HG2 H 1.097 . . 312 142 43 VAL CA C 66.606 . 1 313 142 43 VAL CB C 31.361 . 1 314 142 43 VAL CG1 C 23.627 . . 315 142 43 VAL CG2 C 21.577 . . 316 143 44 ILE H H 8.157 . 1 317 143 44 ILE HA H 3.533 . 1 318 143 44 ILE HB H 1.986 . 1 319 143 44 ILE HG12 H 1.309 . . 320 143 44 ILE HG2 H 1.025 . 1 321 143 44 ILE HD1 H 0.780 . 1 322 143 44 ILE CA C 64.859 . 1 323 143 44 ILE CB C 37.073 . 1 324 143 44 ILE CG1 C 28.796 . 1 325 143 44 ILE CG2 C 17.669 . 1 326 143 44 ILE CD1 C 12.277 . 1 327 144 45 SER H H 7.854 . 1 328 144 45 SER HA H 4.185 . 1 329 144 45 SER HB2 H 3.961 . . 330 144 45 SER CA C 61.530 . 1 331 144 45 SER CB C 62.874 . 1 332 145 46 GLU H H 7.714 . 1 333 145 46 GLU HA H 4.099 . 1 334 145 46 GLU HB2 H 1.988 . . 335 145 46 GLU HB3 H 2.028 . . 336 145 46 GLU HG2 H 2.191 . . 337 145 46 GLU HG3 H 2.308 . . 338 145 46 GLU CA C 58.187 . 1 339 145 46 GLU CB C 29.896 . 1 340 145 46 GLU CG C 36.390 . 1 341 146 47 LEU H H 7.910 . 1 342 146 47 LEU HA H 3.937 . 1 343 146 47 LEU HB2 H 1.118 . . 344 146 47 LEU HB3 H 0.770 . . 345 146 47 LEU HG H 1.544 . 1 346 146 47 LEU HD1 H 0.492 . . 347 146 47 LEU HD2 H 0.155 . . 348 146 47 LEU CA C 56.462 . 1 349 146 47 LEU CB C 41.465 . 1 350 146 47 LEU CG C 26.456 . 1 351 146 47 LEU CD1 C 22.967 . . 352 146 47 LEU CD2 C 25.617 . . 353 147 48 ASN H H 8.043 . 1 354 147 48 ASN HA H 4.566 . 1 355 147 48 ASN HB2 H 2.953 . . 356 147 48 ASN HB3 H 2.815 . . 357 147 48 ASN CA C 54.890 . 1 358 147 48 ASN CB C 38.614 . 1 359 148 49 GLY H H 8.305 . 1 360 148 49 GLY CA C 45.596 . 1 361 149 50 LYS H H 7.734 . 1 362 149 50 LYS HA H 4.442 . 1 363 149 50 LYS HB2 H 1.735 . . 364 149 50 LYS HG2 H 1.391 . . 365 149 50 LYS HD2 H 1.566 . . 366 149 50 LYS HE2 H 2.943 . . 367 149 50 LYS CA C 54.922 . 1 368 149 50 LYS CB C 33.722 . 1 369 149 50 LYS CG C 25.248 . 1 370 149 50 LYS CD C 28.590 . 1 371 149 50 LYS CE C 42.125 . 1 372 150 51 ASN H H 8.743 . 1 373 150 51 ASN HA H 4.758 . 1 374 150 51 ASN HB2 H 2.808 . . 375 150 51 ASN HB3 H 2.992 . . 376 150 51 ASN CA C 52.720 . 1 377 150 51 ASN CB C 38.073 . 1 378 151 52 ILE HA H 3.840 . 1 379 151 52 ILE HB H 1.992 . 1 380 151 52 ILE HG12 H 1.546 . . 381 151 52 ILE HG13 H 1.362 . . 382 151 52 ILE HG2 H 0.946 . 1 383 151 52 ILE HD1 H 0.859 . 1 384 151 52 ILE CA C 63.082 . 1 385 151 52 ILE CB C 37.555 . 1 386 151 52 ILE CG1 C 28.671 . 1 387 151 52 ILE CG2 C 18.332 . 1 388 151 52 ILE CD1 C 13.119 . 1 389 152 53 GLU H H 8.688 . 1 390 152 53 GLU HA H 3.862 . 1 391 152 53 GLU HB2 H 2.041 . . 392 152 53 GLU HG2 H 2.280 . . 393 152 53 GLU CA C 60.096 . 1 394 152 53 GLU CB C 28.919 . 1 395 152 53 GLU CG C 36.805 . 1 396 153 54 ASP H H 7.675 . 1 397 153 54 ASP HA H 4.472 . 1 398 153 54 ASP HB2 H 2.752 . . 399 153 54 ASP HB3 H 2.686 . . 400 153 54 ASP CA C 56.676 . 1 401 153 54 ASP CB C 40.715 . 1 402 154 55 VAL H H 7.710 . 1 403 154 55 VAL HA H 3.583 . 1 404 154 55 VAL HB H 2.226 . 1 405 154 55 VAL HG1 H 0.852 . . 406 154 55 VAL HG2 H 0.979 . . 407 154 55 VAL CA C 66.039 . 1 408 154 55 VAL CB C 31.801 . 1 409 154 55 VAL CG1 C 21.591 . . 410 154 55 VAL CG2 C 22.609 . . 411 155 56 ILE H H 8.226 . 1 412 155 56 ILE HA H 3.713 . 1 413 155 56 ILE HB H 1.874 . 1 414 155 56 ILE HG2 H 0.936 . 1 415 155 56 ILE HD1 H 0.795 . 1 416 155 56 ILE CA C 64.423 . 1 417 155 56 ILE CB C 37.885 . 1 418 155 56 ILE CG1 C 29.076 . 1 419 155 56 ILE CG2 C 17.633 . 1 420 155 56 ILE CD1 C 13.294 . 1 421 156 57 ALA HA H 4.054 . 1 422 156 57 ALA HB H 1.522 . 1 423 156 57 ALA CA C 55.026 . 1 424 156 57 ALA CB C 18.712 . 1 425 157 58 GLN H H 7.978 . 1 426 157 58 GLN HA H 4.156 . 1 427 157 58 GLN HB2 H 2.130 . . 428 157 58 GLN HG2 H 2.422 . . 429 157 58 GLN HG3 H 2.527 . . 430 157 58 GLN CA C 57.337 . 1 431 157 58 GLN CB C 28.834 . 1 432 157 58 GLN CG C 34.008 . 1 433 158 59 GLY H H 7.931 . 1 434 158 59 GLY CA C 46.199 . 1 435 159 60 ILE H H 8.304 . 1 436 159 60 ILE HA H 3.984 . 1 437 159 60 ILE HB H 1.961 . 1 438 159 60 ILE HG12 H 1.214 . . 439 159 60 ILE HG13 H 1.520 . . 440 159 60 ILE HG2 H 0.894 . 1 441 159 60 ILE HD1 H 0.796 . 1 442 159 60 ILE CA C 62.898 . 1 443 159 60 ILE CB C 38.023 . 1 444 159 60 ILE CG1 C 28.175 . 1 445 159 60 ILE CG2 C 17.847 . 1 446 159 60 ILE CD1 C 13.520 . 1 447 160 61 GLY H H 8.307 . 1 448 160 61 GLY CA C 46.357 . 1 449 161 62 LYS H H 7.857 . 1 450 161 62 LYS HA H 4.232 . 1 451 161 62 LYS HB2 H 1.888 . . 452 161 62 LYS HB3 H 1.796 . . 453 161 62 LYS HG2 H 1.500 . . 454 161 62 LYS HG3 H 1.441 . . 455 161 62 LYS HD2 H 1.682 . . 456 161 62 LYS HE2 H 2.977 . . 457 161 62 LYS CA C 56.936 . 1 458 161 62 LYS CB C 32.518 . 1 459 161 62 LYS CG C 25.010 . 1 460 161 62 LYS CD C 28.872 . 1 461 161 62 LYS CE C 41.922 . 1 462 162 63 LEU H H 7.870 . 1 463 162 63 LEU HA H 4.200 . 1 464 162 63 LEU HB2 H 1.724 . . 465 162 63 LEU HB3 H 1.540 . . 466 162 63 LEU HG H 1.716 . 1 467 162 63 LEU HD1 H 0.801 . . 468 162 63 LEU HD2 H 0.869 . . 469 162 63 LEU CA C 55.878 . 1 470 162 63 LEU CB C 42.100 . 1 471 162 63 LEU CG C 26.985 . 1 472 162 63 LEU CD1 C 23.470 . . 473 162 63 LEU CD2 C 25.508 . . 474 163 64 ALA H H 8.006 . 1 475 163 64 ALA HA H 4.282 . 1 476 163 64 ALA HB H 1.381 . 1 477 163 64 ALA CA C 52.666 . 1 478 163 64 ALA CB C 19.291 . 1 479 164 65 SER H H 7.940 . 1 480 164 65 SER HA H 4.417 . 1 481 164 65 SER HB2 H 3.849 . . 482 164 65 SER CA C 58.187 . 1 483 164 65 SER CB C 63.791 . 1 484 165 66 VAL H H 7.963 . 1 485 165 66 VAL HA H 4.362 . 1 486 165 66 VAL HB H 2.088 . 1 487 165 66 VAL HG1 H 0.951 . . 488 165 66 VAL CA C 60.108 . 1 489 165 66 VAL CB C 32.514 . 1 490 165 66 VAL CG1 C 20.917 . . 491 166 67 PRO HA H 4.382 . 1 492 166 67 PRO HB2 H 1.918 . . 493 166 67 PRO HB3 H 2.277 . . 494 166 67 PRO HG2 H 1.974 . . 495 166 67 PRO HG3 H 2.023 . . 496 166 67 PRO HD2 H 3.870 . . 497 166 67 PRO HD3 H 3.626 . . 498 166 67 PRO CA C 63.120 . 1 499 166 67 PRO CB C 32.145 . 1 500 166 67 PRO CG C 27.480 . 1 501 166 67 PRO CD C 51.030 . 1 502 167 68 ALA H H 8.465 . 1 503 167 68 ALA HA H 4.305 . 1 504 167 68 ALA HB H 1.393 . 1 505 167 68 ALA CA C 52.791 . 1 506 167 68 ALA CB C 19.097 . 1 507 168 69 GLY H H 8.423 . 1 508 168 69 GLY HA2 H 3.935 . . 509 168 69 GLY CA C 45.279 . 1 510 169 70 GLY H H 7.966 . 1 511 169 70 GLY HA2 H 3.739 . . 512 169 70 GLY CA C 45.965 . 1 stop_ save_