data_5517 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR studies of the DNA-binding domain of B-Myb ; _BMRB_accession_number 5517 _BMRB_flat_file_name bmr5517.str _Entry_type new _Submission_date 2002-09-11 _Accession_date 2002-09-11 _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 Jones Gareth . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 541 "13C chemical shifts" 289 "15N chemical shifts" 101 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-07-14 update BMRB 'update DNA residue label to two-letter code' 2003-06-12 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Sequence-specific Assignment of the B-Myb DNA-binding Domain (B-MybR2R3) bound to a 16 Base-pair DNA Target Site Corresponding to a Regulatory Site from the tom-1 Gene ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22699289 _PubMed_ID 12815265 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jones Gareth J. . 2 Howard Mark . . 3 McIntosh Pauline . . 4 Williamson Richard A. . 5 Carr Mark D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 26 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 375 _Page_last 376 _Year 2003 _Details ; NMR studies of the minimal DNA-binding domain of chicken B-Myb (B-MybR2R3) when bound to a double stranded 16-mer DNA target containing the 6 base-pair sequence required for DNA binding by Myb proteins, 5'-AACGGA-3'" ; loop_ _Keyword DNA-binding NMR stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Bartels, C., Xia, T., Billeter, M., Guntert, P. and Wuthrich K. (1995) J. Biol. NMR 6, 1-10. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_B_MybR2R3 _Saveframe_category molecular_system _Mol_system_name B-MybR2R3 _Abbreviation_common B-MybR2R3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'B-MybR2R3 unit 1' $B_MybR2R3 'tom1a 16mer' $tom1a_1 'tom1a 16mer' $tom1a_2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state complex _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'Transcription regulatory protein' 'involved in cell-cycle regulation' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_B_MybR2R3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common B-MybR2R3-tom1a _Abbreviation_common B-MybR2R3-tom1a _Molecular_mass 13095 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 110 _Mol_residue_sequence ; GIPDLVKGPWTKEEDQKVIE LVKKYGTKQWTLIAKHLKGR LGKQCRERWHNHLNPEVKKS SWTEEEDRIIFEAHKVLGNR WAEIAKLLPGRTDNAVKNHW NSTIKRKVDT ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ILE 3 PRO 4 ASP 5 LEU 6 VAL 7 LYS 8 GLY 9 PRO 10 TRP 11 THR 12 LYS 13 GLU 14 GLU 15 ASP 16 GLN 17 LYS 18 VAL 19 ILE 20 GLU 21 LEU 22 VAL 23 LYS 24 LYS 25 TYR 26 GLY 27 THR 28 LYS 29 GLN 30 TRP 31 THR 32 LEU 33 ILE 34 ALA 35 LYS 36 HIS 37 LEU 38 LYS 39 GLY 40 ARG 41 LEU 42 GLY 43 LYS 44 GLN 45 CYS 46 ARG 47 GLU 48 ARG 49 TRP 50 HIS 51 ASN 52 HIS 53 LEU 54 ASN 55 PRO 56 GLU 57 VAL 58 LYS 59 LYS 60 SER 61 SER 62 TRP 63 THR 64 GLU 65 GLU 66 GLU 67 ASP 68 ARG 69 ILE 70 ILE 71 PHE 72 GLU 73 ALA 74 HIS 75 LYS 76 VAL 77 LEU 78 GLY 79 ASN 80 ARG 81 TRP 82 ALA 83 GLU 84 ILE 85 ALA 86 LYS 87 LEU 88 LEU 89 PRO 90 GLY 91 ARG 92 THR 93 ASP 94 ASN 95 ALA 96 VAL 97 LYS 98 ASN 99 HIS 100 TRP 101 ASN 102 SER 103 THR 104 ILE 105 LYS 106 ARG 107 LYS 108 VAL 109 ASP 110 THR 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 4114 B-MYB 100.00 110 100.00 100.00 1.97e-72 PDB 1A5J "Chicken B-Myb Dna Binding Domain, Repeat 2 And Repeat3, Nmr, 32 Structures" 99.09 110 100.00 100.00 1.58e-71 DBJ BAC25979 "unnamed protein product [Mus musculus]" 98.18 704 97.22 98.15 4.15e-66 DBJ BAG37322 "unnamed protein product [Homo sapiens]" 98.18 700 97.22 98.15 5.37e-66 DBJ BAH13925 "unnamed protein product [Homo sapiens]" 98.18 676 97.22 98.15 2.73e-66 DBJ BAI46683 "v-myb myeloblastosis viral oncogene homolog (avian)-like 2 [synthetic construct]" 98.18 700 97.22 98.15 5.37e-66 EMBL CAA31655 "unnamed protein product [Homo sapiens]" 98.18 700 97.22 98.15 5.37e-66 EMBL CAA47839 "B-myb [Gallus gallus]" 98.18 686 100.00 100.00 3.09e-68 EMBL CAA49898 "B-myb [Mus musculus]" 98.18 704 97.22 98.15 4.15e-66 GB AAH07585 "V-myb myeloblastosis viral oncogene homolog (avian)-like 2 [Homo sapiens]" 98.18 700 97.22 98.15 5.37e-66 GB AAH50842 "Myeloblastosis oncogene-like 2 [Mus musculus]" 98.18 704 97.22 98.15 4.15e-66 GB AAH53555 "V-myb myeloblastosis viral oncogene homolog (avian)-like 2 [Homo sapiens]" 98.18 700 97.22 98.15 5.37e-66 GB AAI18124 "V-myb myeloblastosis viral oncogene homolog (avian)-like 2 [Bos taurus]" 98.18 695 97.22 98.15 3.43e-66 GB AAP36828 "Homo sapiens v-myb myeloblastosis viral oncogene homolog (avian)-like 2 [synthetic construct]" 98.18 701 97.22 98.15 5.44e-66 REF NP_001068916 "myb-related protein B [Bos taurus]" 98.18 695 97.22 98.15 3.43e-66 REF NP_001100006 "myb-related protein B [Rattus norvegicus]" 98.18 704 97.22 98.15 4.42e-66 REF NP_001231398 "myb-related protein B [Sus scrofa]" 98.18 697 97.22 98.15 2.41e-66 REF NP_001252784 "myb-related protein B [Macaca mulatta]" 98.18 700 97.22 98.15 3.74e-66 REF NP_001265539 "myb-related protein B isoform 2 [Homo sapiens]" 98.18 676 97.22 98.15 2.73e-66 SP P10244 "RecName: Full=Myb-related protein B; Short=B-Myb; AltName: Full=Myb-like protein 2 [Homo sapiens]" 98.18 700 97.22 98.15 5.37e-66 SP P48972 "RecName: Full=Myb-related protein B; Short=B-Myb; AltName: Full=Myb-like protein 2 [Mus musculus]" 98.18 704 97.22 98.15 4.15e-66 SP Q03237 "RecName: Full=Myb-related protein B; Short=B-Myb; AltName: Full=Myb-like protein 2 [Gallus gallus]" 98.18 686 100.00 100.00 3.09e-68 TPG DAA23198 "TPA: v-myb myeloblastosis viral oncogene homolog-like 2 [Bos taurus]" 98.18 695 97.22 98.15 3.43e-66 stop_ save_ save_tom1a_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class DNA _Name_common tom1a _Abbreviation_common tom1a _Molecular_mass 4879 _Mol_thiol_state 'not present' _Details . _Residue_count 16 _Mol_residue_sequence CTCAGTCCGTTAAGGA loop_ _Residue_seq_code _Residue_label 1 DC 2 DT 3 DC 4 DA 5 DG 6 DT 7 DC 8 DC 9 DG 10 DT 11 DT 12 DA 13 DA 14 DG 15 DG 16 DA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_tom1a_2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class DNA _Name_common tom1a _Abbreviation_common tom1a _Molecular_mass 4879 _Mol_thiol_state 'not present' _Details . _Residue_count 16 _Mol_residue_sequence TCCTTAACGGACTGAG loop_ _Residue_seq_code _Residue_label 1 DT 2 DC 3 DC 4 DT 5 DT 6 DA 7 DA 8 DC 9 DG 10 DG 11 DA 12 DC 13 DT 14 DG 15 DA 16 DG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction _Gene_mnemonic $B_MybR2R3 Chicken 9031 Eukaryota Metazoa Gallus gallus Nucleus b-myb 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 _Vendor_name $tom1a_1 'chemical synthesis' . . . . . Oswel 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 $B_MybR2R3 1.9 mM '[U-15N; U-13C]-All but Pro' $tom1a_1 1.9 mM . $tom1a_2 1.9 mM . stop_ save_ ############################ # Computer software used # ############################ save_XEasy _Saveframe_category software _Name XEasy _Version . loop_ _Task 'peak picking' 'manual assignment' stop_ _Details . _Citation_label $ref_1 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HCCH-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.2 0.2 n/a temperature 293 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details ; In the B-MybR2R3 samples used here proline residues were unlabelled. Residues 46-49 were undetected due to conformational heterogeneity in this region of the protein. ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'B-MybR2R3 unit 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 GLY HA2 H 3.87 0.01 1 2 . 1 GLY HA3 H 3.87 0.01 1 3 . 1 GLY CA C 43.20 0.2 1 4 . 2 ILE HA H 4.50 0.01 1 5 . 2 ILE HB H 1.90 0.01 1 6 . 2 ILE HG12 H 1.51 0.01 1 7 . 2 ILE HG13 H 1.22 0.01 1 8 . 2 ILE HD1 H 0.88 0.01 1 9 . 2 ILE H H 8.65 0.01 1 10 . 2 ILE CA C 59.40 0.2 1 11 . 2 ILE CB C 38.30 0.2 1 12 . 2 ILE CD1 C 12.90 0.2 1 13 . 2 ILE CG1 C 26.70 0.2 1 14 . 2 ILE N N 121.50 0.2 1 15 . 4 ASP HA H 4.44 0.01 1 16 . 4 ASP HB2 H 2.65 0.01 1 17 . 4 ASP HB3 H 2.57 0.01 1 18 . 4 ASP H H 8.33 0.01 1 19 . 4 ASP CA C 54.70 0.2 1 20 . 4 ASP CB C 40.80 0.2 1 21 . 4 ASP N N 119.20 0.2 1 22 . 5 LEU HA H 4.30 0.01 1 23 . 5 LEU HB2 H 1.58 0.01 1 24 . 5 LEU HB3 H 1.58 0.01 1 25 . 5 LEU HD1 H 0.95 0.01 1 26 . 5 LEU HD2 H 0.84 0.01 1 27 . 5 LEU H H 7.79 0.01 1 28 . 5 LEU CA C 55.30 0.2 1 29 . 5 LEU N N 120.80 0.2 1 30 . 6 VAL HA H 4.08 0.01 1 31 . 6 VAL HB H 1.92 0.01 1 32 . 6 VAL HG1 H 0.87 0.01 1 33 . 6 VAL HG2 H 0.75 0.01 1 34 . 6 VAL H H 8.84 0.01 1 35 . 6 VAL CA C 62.10 0.2 1 36 . 6 VAL CB C 33.00 0.2 1 37 . 6 VAL CG1 C 20.80 0.2 1 38 . 6 VAL CG2 C 21.00 0.2 1 39 . 6 VAL N N 123.80 0.2 1 40 . 7 LYS HA H 4.43 0.01 1 41 . 7 LYS HB2 H 1.78 0.01 1 42 . 7 LYS HB3 H 1.70 0.01 1 43 . 7 LYS HD2 H 1.66 0.01 1 44 . 7 LYS HD3 H 1.66 0.01 1 45 . 7 LYS HE2 H 2.92 0.01 1 46 . 7 LYS HE3 H 2.92 0.01 1 47 . 7 LYS HG2 H 1.39 0.01 1 48 . 7 LYS HG3 H 1.39 0.01 1 49 . 7 LYS H H 8.24 0.01 1 50 . 7 LYS CA C 55.00 0.2 1 51 . 7 LYS CB C 34.30 0.2 1 52 . 7 LYS CD C 29.10 0.2 1 53 . 7 LYS CE C 42.10 0.2 1 54 . 7 LYS CG C 25.00 0.2 1 55 . 7 LYS N N 125.30 0.2 1 56 . 8 GLY HA2 H 4.27 0.01 1 57 . 8 GLY HA3 H 3.98 0.01 1 58 . 8 GLY H H 8.82 0.01 1 59 . 8 GLY CA C 44.40 0.2 1 60 . 8 GLY N N 111.20 0.2 1 61 . 10 TRP HA H 4.24 0.01 1 62 . 10 TRP H H 9.04 0.01 1 63 . 10 TRP CA C 58.40 0.2 1 64 . 10 TRP CB C 26.60 0.2 1 65 . 10 TRP N N 125.50 0.2 1 66 . 11 THR HA H 4.68 0.01 1 67 . 11 THR HB H 4.82 0.01 1 68 . 11 THR HG2 H 1.28 0.01 1 69 . 11 THR H H 8.87 0.01 1 70 . 11 THR CA C 59.90 0.2 1 71 . 11 THR CB C 71.80 0.2 1 72 . 11 THR CG2 C 21.60 0.2 1 73 . 11 THR N N 117.00 0.2 1 74 . 12 LYS HA H 4.19 0.01 1 75 . 12 LYS HB2 H 1.95 0.01 1 76 . 12 LYS HB3 H 1.95 0.01 1 77 . 12 LYS HD2 H 1.76 0.01 1 78 . 12 LYS HD3 H 1.68 0.01 1 79 . 12 LYS HE2 H 3.04 0.01 1 80 . 12 LYS HE3 H 3.04 0.01 1 81 . 12 LYS HG2 H 1.42 0.01 1 82 . 12 LYS HG3 H 1.36 0.01 1 83 . 12 LYS H H 8.87 0.01 1 84 . 12 LYS CA C 59.40 0.2 1 85 . 12 LYS CB C 32.10 0.2 1 86 . 12 LYS CD C 29.10 0.2 1 87 . 12 LYS CE C 41.90 0.2 1 88 . 12 LYS CG C 25.00 0.2 1 89 . 12 LYS N N 121.20 0.2 1 90 . 13 GLU HA H 4.12 0.01 1 91 . 13 GLU HB2 H 2.14 0.01 1 92 . 13 GLU HB3 H 1.96 0.01 1 93 . 13 GLU HG2 H 2.43 0.01 1 94 . 13 GLU HG3 H 2.32 0.01 1 95 . 13 GLU H H 8.66 0.01 1 96 . 13 GLU CA C 60.10 0.2 1 97 . 13 GLU CB C 29.40 0.2 1 98 . 13 GLU CG C 37.10 0.2 1 99 . 13 GLU N N 118.50 0.2 1 100 . 14 GLU HA H 4.01 0.01 1 101 . 14 GLU HB2 H 2.51 0.01 1 102 . 14 GLU HB3 H 2.47 0.01 1 103 . 14 GLU HG2 H 2.53 0.01 1 104 . 14 GLU HG3 H 2.53 0.01 1 105 . 14 GLU H H 7.91 0.01 1 106 . 14 GLU CA C 60.20 0.2 1 107 . 14 GLU CB C 31.90 0.2 1 108 . 14 GLU CG C 35.90 0.2 1 109 . 14 GLU N N 121.40 0.2 1 110 . 15 ASP HA H 4.53 0.01 1 111 . 15 ASP HB2 H 2.64 0.01 1 112 . 15 ASP HB3 H 2.51 0.01 1 113 . 15 ASP H H 8.67 0.01 1 114 . 15 ASP CA C 57.50 0.2 1 115 . 15 ASP CB C 39.80 0.2 1 116 . 15 ASP N N 120.30 0.2 1 117 . 16 GLN HA H 4.04 0.01 1 118 . 16 GLN HB2 H 2.26 0.01 1 119 . 16 GLN HB3 H 2.18 0.01 1 120 . 16 GLN HG2 H 2.57 0.01 1 121 . 16 GLN HG3 H 2.52 0.01 1 122 . 16 GLN H H 8.23 0.01 1 123 . 16 GLN CA C 58.60 0.2 1 124 . 16 GLN CB C 28.50 0.2 1 125 . 16 GLN CG C 33.90 0.2 1 126 . 16 GLN N N 116.30 0.2 1 127 . 17 LYS HA H 4.24 0.01 1 128 . 17 LYS HB2 H 2.04 0.01 1 129 . 17 LYS HB3 H 2.02 0.01 1 130 . 17 LYS HD2 H 1.80 0.01 1 131 . 17 LYS HD3 H 1.79 0.01 1 132 . 17 LYS HE2 H 3.05 0.01 1 133 . 17 LYS HE3 H 3.02 0.01 1 134 . 17 LYS HG2 H 1.57 0.01 1 135 . 17 LYS HG3 H 1.57 0.01 1 136 . 17 LYS H H 7.83 0.01 1 137 . 17 LYS CA C 59.10 0.2 1 138 . 17 LYS CB C 32.30 0.2 1 139 . 17 LYS CD C 28.80 0.2 1 140 . 17 LYS CE C 41.90 0.2 1 141 . 17 LYS CG C 26.90 0.2 1 142 . 17 LYS N N 120.00 0.2 1 143 . 18 VAL HA H 3.65 0.01 1 144 . 18 VAL H H 8.84 0.01 1 145 . 18 VAL CA C 68.40 0.2 1 146 . 18 VAL N N 119.50 0.2 1 147 . 19 ILE HA H 3.71 0.01 1 148 . 19 ILE HB H 2.08 0.01 1 149 . 19 ILE HG12 H 1.08 0.01 1 150 . 19 ILE HG13 H 1.08 0.01 1 151 . 19 ILE HD1 H 0.91 0.01 1 152 . 19 ILE H H 8.38 0.01 1 153 . 19 ILE CA C 56.80 0.2 1 154 . 19 ILE CB C 37.80 0.2 1 155 . 19 ILE CD1 C 12.90 0.2 1 156 . 19 ILE CG2 C 16.90 0.2 1 157 . 19 ILE N N 119.20 0.2 1 158 . 20 GLU HA H 4.03 0.01 1 159 . 20 GLU HB2 H 2.20 0.01 1 160 . 20 GLU HB3 H 2.17 0.01 1 161 . 20 GLU HG2 H 2.42 0.01 1 162 . 20 GLU HG3 H 2.27 0.01 1 163 . 20 GLU H H 8.09 0.01 1 164 . 20 GLU CA C 59.20 0.2 1 165 . 20 GLU CB C 29.70 0.2 1 166 . 20 GLU CG C 36.20 0.2 1 167 . 20 GLU N N 119.20 0.2 1 168 . 21 LEU HA H 4.10 0.01 1 169 . 21 LEU H H 8.65 0.01 1 170 . 21 LEU CA C 57.70 0.2 1 171 . 21 LEU N N 121.50 0.2 1 172 . 22 VAL HA H 3.49 0.01 1 173 . 22 VAL HB H 1.50 0.01 1 174 . 22 VAL HG1 H 0.38 0.01 1 175 . 22 VAL HG2 H -0.44 0.01 1 176 . 22 VAL H H 8.97 0.01 1 177 . 22 VAL CA C 65.40 0.2 1 178 . 22 VAL CB C 31.40 0.2 1 179 . 22 VAL CG1 C 23.60 0.2 1 180 . 22 VAL CG2 C 20.30 0.2 1 181 . 22 VAL N N 123.50 0.2 1 182 . 23 LYS HA H 3.88 0.01 1 183 . 23 LYS HB2 H 1.90 0.01 1 184 . 23 LYS HB3 H 1.84 0.01 1 185 . 23 LYS HD2 H 1.69 0.01 1 186 . 23 LYS HD3 H 1.63 0.01 1 187 . 23 LYS HE2 H 3.03 0.01 1 188 . 23 LYS HE3 H 3.02 0.01 1 189 . 23 LYS HG2 H 1.38 0.01 1 190 . 23 LYS HG3 H 1.34 0.01 1 191 . 23 LYS H H 7.59 0.01 1 192 . 23 LYS CA C 59.70 0.2 1 193 . 23 LYS CB C 32.10 0.2 1 194 . 23 LYS CD C 29.50 0.2 1 195 . 23 LYS CE C 41.80 0.2 1 196 . 23 LYS CG C 25.20 0.2 1 197 . 23 LYS N N 121.00 0.2 1 198 . 24 LYS HA H 3.92 0.01 1 199 . 24 LYS HB2 H 1.68 0.01 1 200 . 24 LYS HB3 H 1.55 0.01 1 201 . 24 LYS HD2 H 1.32 0.01 1 202 . 24 LYS HD3 H 1.18 0.01 1 203 . 24 LYS HE2 H 2.72 0.01 1 204 . 24 LYS HE3 H 2.69 0.01 1 205 . 24 LYS HG2 H 0.90 0.01 1 206 . 24 LYS HG3 H 0.31 0.01 1 207 . 24 LYS H H 7.05 0.01 1 208 . 24 LYS CA C 58.70 0.2 1 209 . 24 LYS CB C 34.00 0.2 1 210 . 24 LYS CD C 29.10 0.2 1 211 . 24 LYS CE C 41.80 0.2 1 212 . 24 LYS CG C 24.10 0.2 1 213 . 24 LYS N N 116.70 0.2 1 214 . 25 TYR HA H 4.55 0.01 1 215 . 25 TYR HB2 H 3.00 0.01 1 216 . 25 TYR HB3 H 2.50 0.01 1 217 . 25 TYR H H 8.73 0.01 1 218 . 25 TYR CA C 58.60 0.2 1 219 . 25 TYR CB C 39.70 0.2 1 220 . 25 TYR N N 115.00 0.2 1 221 . 26 GLY HA2 H 4.19 0.01 1 222 . 26 GLY HA3 H 3.72 0.01 1 223 . 26 GLY H H 8.49 0.01 1 224 . 26 GLY CA C 44.40 0.2 1 225 . 26 GLY N N 111.20 0.2 1 226 . 27 THR HA H 3.47 0.01 1 227 . 27 THR HG2 H 0.78 0.01 1 228 . 27 THR H H 7.73 0.01 1 229 . 27 THR CA C 60.70 0.2 1 230 . 27 THR CB C 63.50 0.2 1 231 . 27 THR CG2 C 21.50 0.2 1 232 . 27 THR N N 104.20 0.2 1 233 . 28 LYS HA H 4.46 0.01 1 234 . 28 LYS HB2 H 2.03 0.01 1 235 . 28 LYS HB3 H 2.02 0.01 1 236 . 28 LYS HD2 H 1.78 0.01 1 237 . 28 LYS HD3 H 1.68 0.01 1 238 . 28 LYS HE2 H 3.03 0.01 1 239 . 28 LYS HE3 H 3.03 0.01 1 240 . 28 LYS HG2 H 1.44 0.01 1 241 . 28 LYS HG3 H 1.44 0.01 1 242 . 28 LYS H H 8.07 0.01 1 243 . 28 LYS CA C 55.10 0.2 1 244 . 28 LYS CB C 33.60 0.2 1 245 . 28 LYS CD C 29.10 0.2 1 246 . 28 LYS CE C 41.90 0.2 1 247 . 28 LYS CG C 25.00 0.2 1 248 . 28 LYS N N 119.70 0.2 1 249 . 29 GLN HA H 4.79 0.01 1 250 . 29 GLN HB2 H 2.15 0.01 1 251 . 29 GLN HB3 H 1.41 0.01 1 252 . 29 GLN HG2 H 2.31 0.01 1 253 . 29 GLN HG3 H 2.12 0.01 1 254 . 29 GLN H H 8.05 0.01 1 255 . 29 GLN CA C 54.30 0.2 1 256 . 29 GLN CB C 29.80 0.2 1 257 . 29 GLN CG C 34.00 0.2 1 258 . 29 GLN N N 120.20 0.2 1 259 . 30 TRP HA H 4.21 0.01 1 260 . 30 TRP HB2 H 3.45 0.01 1 261 . 30 TRP HB3 H 3.45 0.01 1 262 . 30 TRP H H 7.61 0.01 1 263 . 30 TRP CA C 59.90 0.2 1 264 . 30 TRP CB C 37.90 0.2 1 265 . 30 TRP N N 122.20 0.2 1 266 . 31 THR HA H 4.05 0.01 1 267 . 31 THR HB H 4.30 0.01 1 268 . 31 THR HG2 H 1.41 0.01 1 269 . 31 THR H H 8.74 0.01 1 270 . 31 THR CA C 66.80 0.2 1 271 . 31 THR CB C 68.50 0.2 1 272 . 31 THR CG2 C 21.90 0.2 1 273 . 31 THR N N 115.70 0.2 1 274 . 32 LEU HA H 4.04 0.01 1 275 . 32 LEU H H 7.56 0.01 1 276 . 32 LEU CA C 57.80 0.2 1 277 . 32 LEU N N 124.00 0.2 1 278 . 33 ILE HA H 3.54 0.01 1 279 . 33 ILE HB H 2.25 0.01 1 280 . 33 ILE HD1 H 0.51 0.01 1 281 . 33 ILE HG12 H 1.62 0.01 1 282 . 33 ILE HG13 H 1.06 0.01 1 283 . 33 ILE HG2 H 1.13 0.01 1 284 . 33 ILE H H 7.75 0.01 1 285 . 33 ILE CA C 66.50 0.2 1 286 . 33 ILE CB C 38.30 0.2 1 287 . 33 ILE CD1 C 13.40 0.2 1 288 . 33 ILE CG1 C 30.00 0.2 1 289 . 33 ILE CG2 C 16.00 0.2 1 290 . 33 ILE N N 119.70 0.2 1 291 . 34 ALA HA H 4.08 0.01 1 292 . 34 ALA HB H 1.61 0.01 1 293 . 34 ALA H H 8.65 0.01 1 294 . 34 ALA CA C 55.40 0.2 1 295 . 34 ALA CB C 18.70 0.2 1 296 . 34 ALA N N 120.70 0.2 1 297 . 35 LYS HA H 4.09 0.01 1 298 . 35 LYS HB2 H 1.97 0.01 1 299 . 35 LYS HB3 H 1.77 0.01 1 300 . 35 LYS HD2 H 1.72 0.01 1 301 . 35 LYS HD3 H 1.62 0.01 1 302 . 35 LYS HE2 H 2.97 0.01 1 303 . 35 LYS HE3 H 2.97 0.01 1 304 . 35 LYS HG2 H 1.43 0.01 1 305 . 35 LYS HG3 H 1.43 0.01 1 306 . 35 LYS H H 7.64 0.01 1 307 . 35 LYS CA C 58.70 0.2 1 308 . 35 LYS CB C 32.40 0.2 1 309 . 35 LYS CD C 29.10 0.2 1 310 . 35 LYS CE C 41.90 0.2 1 311 . 35 LYS CG C 25.00 0.2 1 312 . 35 LYS N N 117.00 0.2 1 313 . 36 HIS HA H 4.45 0.01 1 314 . 36 HIS HB2 H 3.41 0.01 1 315 . 36 HIS HB3 H 3.26 0.01 1 316 . 36 HIS H H 7.96 0.01 1 317 . 36 HIS CA C 57.60 0.2 1 318 . 36 HIS CB C 30.80 0.2 1 319 . 36 HIS N N 115.50 0.2 1 320 . 37 LEU HA H 4.54 0.01 1 321 . 37 LEU HB2 H 1.70 0.01 1 322 . 37 LEU HB3 H 1.70 0.01 1 323 . 37 LEU HG H 1.81 0.01 1 324 . 37 LEU H H 8.04 0.01 1 325 . 37 LEU CA C 54.70 0.2 1 326 . 37 LEU N N 124.30 0.2 1 327 . 38 LYS HA H 4.20 0.01 1 328 . 38 LYS HB2 H 1.91 0.01 1 329 . 38 LYS HB3 H 1.77 0.01 1 330 . 38 LYS HD2 H 1.67 0.01 1 331 . 38 LYS HD3 H 1.67 0.01 1 332 . 38 LYS HE2 H 2.97 0.01 1 333 . 38 LYS HE3 H 2.97 0.01 1 334 . 38 LYS HG2 H 1.43 0.01 1 335 . 38 LYS HG3 H 1.35 0.01 1 336 . 38 LYS H H 8.16 0.01 1 337 . 38 LYS CA C 57.50 0.2 1 338 . 38 LYS CB C 32.60 0.2 1 339 . 38 LYS CD C 28.90 0.2 1 340 . 38 LYS CE C 41.90 0.2 1 341 . 38 LYS CG C 24.30 0.2 1 342 . 38 LYS N N 119.00 0.2 1 343 . 39 GLY HA2 H 4.07 0.01 1 344 . 39 GLY HA3 H 3.80 0.01 1 345 . 39 GLY H H 8.72 0.01 1 346 . 39 GLY CA C 46.20 0.2 1 347 . 39 GLY N N 111.20 0.2 1 348 . 40 ARG HA H 4.99 0.01 1 349 . 40 ARG HB2 H 1.62 0.01 1 350 . 40 ARG HB3 H 1.62 0.01 1 351 . 40 ARG HD2 H 2.87 0.01 1 352 . 40 ARG HD3 H 2.68 0.01 1 353 . 40 ARG H H 7.41 0.01 1 354 . 40 ARG CA C 52.50 0.2 1 355 . 40 ARG CB C 29.80 0.2 1 356 . 40 ARG CD C 38.30 0.2 1 357 . 40 ARG N N 115.50 0.2 1 358 . 41 LEU HA H 4.78 0.01 1 359 . 41 LEU HD1 H 0.95 0.01 1 360 . 41 LEU HD2 H 0.95 0.01 1 361 . 41 LEU H H 9.30 0.01 1 362 . 41 LEU CA C 53.30 0.2 1 363 . 41 LEU N N 120.00 0.2 1 364 . 42 GLY HA2 H 4.08 0.01 1 365 . 42 GLY HA3 H 3.79 0.01 1 366 . 42 GLY H H 10.00 0.01 1 367 . 42 GLY CA C 48.90 0.2 1 368 . 42 GLY N N 114.50 0.2 1 369 . 43 LYS HA H 3.90 0.01 1 370 . 43 LYS HB2 H 1.92 0.01 1 371 . 43 LYS HB3 H 1.79 0.01 1 372 . 43 LYS HD2 H 1.71 0.01 1 373 . 43 LYS HD3 H 1.65 0.01 1 374 . 43 LYS HE2 H 2.97 0.01 1 375 . 43 LYS HE3 H 2.97 0.01 1 376 . 43 LYS HG2 H 1.55 0.01 1 377 . 43 LYS HG3 H 1.37 0.01 1 378 . 43 LYS H H 8.95 0.01 1 379 . 43 LYS CA C 59.60 0.2 1 380 . 43 LYS CB C 32.20 0.2 1 381 . 43 LYS CD C 29.30 0.2 1 382 . 43 LYS CE C 41.90 0.2 1 383 . 43 LYS CG C 24.80 0.2 1 384 . 43 LYS N N 120.00 0.2 1 385 . 44 GLN HB2 H 2.54 0.01 1 386 . 44 GLN HB3 H 2.54 0.01 1 387 . 44 GLN HG2 H 2.36 0.01 1 388 . 44 GLN HG3 H 2.36 0.01 1 389 . 44 GLN H H 7.09 0.01 1 390 . 44 GLN CA C 58.30 0.2 1 391 . 44 GLN CB C 27.90 0.2 1 392 . 44 GLN CG C 34.00 0.2 1 393 . 44 GLN N N 117.00 0.2 1 394 . 45 CYS HA H 4.46 0.01 1 395 . 45 CYS HB2 H 3.73 0.01 1 396 . 45 CYS HB3 H 2.82 0.01 1 397 . 45 CYS H H 8.06 0.01 1 398 . 45 CYS CA C 63.40 0.2 1 399 . 45 CYS CB C 27.20 0.2 1 400 . 45 CYS N N 119.50 0.2 1 401 . 50 HIS HA H 3.86 0.01 1 402 . 50 HIS HB2 H 3.16 0.01 1 403 . 50 HIS HB3 H 3.02 0.01 1 404 . 50 HIS H H 9.06 0.01 1 405 . 50 HIS CA C 59.60 0.2 1 406 . 50 HIS CB C 30.00 0.2 1 407 . 50 HIS N N 113.70 0.2 1 408 . 51 ASN HA H 4.87 0.01 1 409 . 51 ASN HB2 H 3.05 0.01 1 410 . 51 ASN HB3 H 3.05 0.01 1 411 . 51 ASN H H 7.92 0.01 1 412 . 51 ASN CA C 53.70 0.2 1 413 . 51 ASN N N 107.50 0.2 1 414 . 52 HIS HA H 4.59 0.01 1 415 . 52 HIS HB2 H 3.01 0.01 1 416 . 52 HIS HB3 H 3.01 0.01 1 417 . 52 HIS H H 7.31 0.01 1 418 . 52 HIS CA C 58.10 0.2 1 419 . 52 HIS CB C 29.50 0.2 1 420 . 52 HIS N N 114.50 0.2 1 421 . 53 LEU HA H 4.12 0.01 1 422 . 53 LEU HB2 H 1.61 0.01 1 423 . 53 LEU HB3 H 1.61 0.01 1 424 . 53 LEU HG H 1.03 0.01 1 425 . 53 LEU H H 7.67 0.01 1 426 . 53 LEU CA C 55.40 0.2 1 427 . 53 LEU N N 116.70 0.2 1 428 . 54 ASN H H 7.47 0.01 1 429 . 54 ASN CA C 50.40 0.2 1 430 . 54 ASN CB C 39.00 0.2 1 431 . 54 ASN N N 119.70 0.2 1 432 . 56 GLU HA H 4.01 0.01 1 433 . 56 GLU HB2 H 2.10 0.01 1 434 . 56 GLU HB3 H 1.69 0.01 1 435 . 56 GLU HG2 H 2.37 0.01 1 436 . 56 GLU HG3 H 2.34 0.01 1 437 . 56 GLU H H 7.34 0.01 1 438 . 56 GLU CA C 56.40 0.2 1 439 . 56 GLU CB C 30.30 0.2 1 440 . 56 GLU CG C 35.90 0.2 1 441 . 56 GLU N N 115.20 0.2 1 442 . 57 VAL HA H 3.67 0.01 1 443 . 57 VAL HB H 1.72 0.01 1 444 . 57 VAL HG1 H 0.70 0.01 1 445 . 57 VAL HG2 H 0.69 0.01 1 446 . 57 VAL H H 7.38 0.01 1 447 . 57 VAL CA C 63.60 0.2 1 448 . 57 VAL CB C 31.80 0.2 1 449 . 57 VAL CG1 C 21.00 0.2 1 450 . 57 VAL CG2 C 21.00 0.2 1 451 . 57 VAL N N 119.70 0.2 1 452 . 58 LYS HA H 4.34 0.01 1 453 . 58 LYS HB2 H 1.53 0.01 1 454 . 58 LYS HB3 H 1.45 0.01 1 455 . 58 LYS HD2 H 1.66 0.01 1 456 . 58 LYS HD3 H 1.66 0.01 1 457 . 58 LYS HE2 H 2.80 0.01 1 458 . 58 LYS HE3 H 2.75 0.01 1 459 . 58 LYS HG2 H 1.30 0.01 1 460 . 58 LYS HG3 H 1.11 0.01 1 461 . 58 LYS H H 9.36 0.01 1 462 . 58 LYS CA C 55.10 0.2 1 463 . 58 LYS CB C 34.90 0.2 1 464 . 58 LYS CD C 28.80 0.2 1 465 . 58 LYS CE C 41.40 0.2 1 466 . 58 LYS CG C 24.90 0.2 1 467 . 58 LYS N N 129.80 0.2 1 468 . 59 LYS HA H 4.44 0.01 1 469 . 59 LYS HB2 H 1.57 0.01 1 470 . 59 LYS HB3 H 2.03 0.01 1 471 . 59 LYS HD2 H 1.71 0.01 1 472 . 59 LYS HD3 H 1.71 0.01 1 473 . 59 LYS HE2 H 3.03 0.01 1 474 . 59 LYS HE3 H 3.03 0.01 1 475 . 59 LYS HG2 H 1.43 0.01 1 476 . 59 LYS HG3 H 1.43 0.01 1 477 . 59 LYS H H 8.68 0.01 1 478 . 59 LYS CA C 54.70 0.2 1 479 . 59 LYS CB C 32.80 0.2 1 480 . 59 LYS CD C 29.10 0.2 1 481 . 59 LYS CE C 41.90 0.2 1 482 . 59 LYS CG C 25.00 0.2 1 483 . 59 LYS N N 123.50 0.2 1 484 . 60 SER HA H 4.32 0.01 1 485 . 60 SER HB2 H 3.97 0.01 1 486 . 60 SER HB3 H 3.80 0.01 1 487 . 60 SER H H 7.11 0.01 1 488 . 60 SER CA C 56.90 0.2 1 489 . 60 SER CB C 64.30 0.2 1 490 . 60 SER N N 113.20 0.2 1 491 . 61 SER HA H 4.19 0.01 1 492 . 61 SER HB2 H 3.94 0.01 1 493 . 61 SER HB3 H 3.80 0.01 1 494 . 61 SER H H 8.55 0.01 1 495 . 61 SER CA C 59.40 0.2 1 496 . 61 SER CB C 63.30 0.2 1 497 . 61 SER N N 116.70 0.2 1 498 . 62 TRP HA H 4.37 0.01 1 499 . 62 TRP HB2 H 3.07 0.01 1 500 . 62 TRP HB3 H 2.83 0.01 1 501 . 62 TRP H H 8.41 0.01 1 502 . 62 TRP CA C 57.20 0.2 1 503 . 62 TRP CB C 29.10 0.2 1 504 . 62 TRP N N 125.00 0.2 1 505 . 63 THR HA H 4.68 0.01 1 506 . 63 THR HB H 4.79 0.01 1 507 . 63 THR HG2 H 1.28 0.01 1 508 . 63 THR H H 9.38 0.01 1 509 . 63 THR CA C 60.00 0.2 1 510 . 63 THR CB C 71.80 0.2 1 511 . 63 THR CG2 C 21.70 0.2 1 512 . 63 THR N N 117.70 0.2 1 513 . 64 GLU HA H 4.17 0.01 1 514 . 64 GLU HB2 H 2.13 0.01 1 515 . 64 GLU HB3 H 2.08 0.01 1 516 . 64 GLU HG2 H 2.43 0.01 1 517 . 64 GLU HG3 H 2.39 0.01 1 518 . 64 GLU H H 8.95 0.01 1 519 . 64 GLU CA C 59.70 0.2 1 520 . 64 GLU CB C 29.50 0.2 1 521 . 64 GLU CG C 36.50 0.2 1 522 . 64 GLU N N 120.50 0.2 1 523 . 65 GLU HA H 4.23 0.01 1 524 . 65 GLU HB2 H 2.13 0.01 1 525 . 65 GLU HB3 H 1.95 0.01 1 526 . 65 GLU HG2 H 2.72 0.01 1 527 . 65 GLU HG3 H 2.42 0.01 1 528 . 65 GLU H H 8.44 0.01 1 529 . 65 GLU CA C 59.60 0.2 1 530 . 65 GLU CB C 29.60 0.2 1 531 . 65 GLU CG C 37.40 0.2 1 532 . 65 GLU N N 119.50 0.2 1 533 . 66 GLU HA H 4.00 0.01 1 534 . 66 GLU HB2 H 2.16 0.01 1 535 . 66 GLU HB3 H 1.95 0.01 1 536 . 66 GLU H H 7.91 0.01 1 537 . 66 GLU CA C 59.80 0.2 1 538 . 66 GLU CB C 29.60 0.2 1 539 . 66 GLU N N 119.70 0.2 1 540 . 67 ASP HA H 4.44 0.01 1 541 . 67 ASP HB2 H 2.84 0.01 1 542 . 67 ASP HB3 H 2.68 0.01 1 543 . 67 ASP H H 8.48 0.01 1 544 . 67 ASP CA C 57.80 0.2 1 545 . 67 ASP CB C 39.80 0.2 1 546 . 67 ASP N N 119.50 0.2 1 547 . 68 ARG HA H 4.21 0.01 1 548 . 68 ARG HB2 H 2.15 0.01 1 549 . 68 ARG HB3 H 2.02 0.01 1 550 . 68 ARG HD2 H 3.33 0.01 1 551 . 68 ARG HD3 H 3.23 0.01 1 552 . 68 ARG HG2 H 1.87 0.01 1 553 . 68 ARG HG3 H 1.75 0.01 1 554 . 68 ARG H H 8.16 0.01 1 555 . 68 ARG CA C 59.90 0.2 1 556 . 68 ARG CB C 30.00 0.2 1 557 . 68 ARG CD C 43.10 0.2 1 558 . 68 ARG CG C 27.20 0.2 1 559 . 68 ARG N N 121.50 0.2 1 560 . 69 ILE HA H 3.76 0.01 1 561 . 69 ILE HB H 2.22 0.01 1 562 . 69 ILE HD1 H 0.99 0.01 1 563 . 69 ILE HG12 H 1.94 0.01 1 564 . 69 ILE HG13 H 1.14 0.01 1 565 . 69 ILE HG2 H 0.96 0.01 1 566 . 69 ILE H H 8.15 0.01 1 567 . 69 ILE CA C 65.40 0.2 1 568 . 69 ILE CB C 38.10 0.2 1 569 . 69 ILE CD1 C 13.80 0.2 1 570 . 69 ILE CG1 C 29.80 0.2 1 571 . 69 ILE CG2 C 17.60 0.2 1 572 . 69 ILE N N 120.70 0.2 1 573 . 70 ILE HA H 3.61 0.01 1 574 . 70 ILE HB H 2.25 0.01 1 575 . 70 ILE HD1 H 1.13 0.01 1 576 . 70 ILE HG12 H 2.10 0.01 1 577 . 70 ILE HG13 H 0.97 0.01 1 578 . 70 ILE HG2 H 1.15 0.01 1 579 . 70 ILE H H 8.63 0.01 1 580 . 70 ILE CA C 66.50 0.2 1 581 . 70 ILE CB C 37.60 0.2 1 582 . 70 ILE CD1 C 13.70 0.2 1 583 . 70 ILE CG1 C 30.20 0.2 1 584 . 70 ILE CG2 C 18.20 0.2 1 585 . 70 ILE N N 119.00 0.2 1 586 . 71 PHE HA H 4.40 0.01 1 587 . 71 PHE HB2 H 3.42 0.01 1 588 . 71 PHE HB3 H 3.38 0.01 1 589 . 71 PHE H H 8.77 0.01 1 590 . 71 PHE CA C 62.30 0.2 1 591 . 71 PHE CB C 40.00 0.2 1 592 . 71 PHE N N 120.20 0.2 1 593 . 72 GLU HA H 3.98 0.01 1 594 . 72 GLU HB2 H 2.12 0.01 1 595 . 72 GLU HB3 H 2.12 0.01 1 596 . 72 GLU HG2 H 2.59 0.01 1 597 . 72 GLU HG3 H 2.59 0.01 1 598 . 72 GLU H H 8.75 0.01 1 599 . 72 GLU CA C 59.10 0.2 1 600 . 72 GLU CB C 29.50 0.2 1 601 . 72 GLU CG C 36.40 0.2 1 602 . 72 GLU N N 117.70 0.2 1 603 . 73 ALA HA H 4.28 0.01 1 604 . 73 ALA HB H 1.46 0.01 1 605 . 73 ALA H H 8.73 0.01 1 606 . 73 ALA CA C 54.50 0.2 1 607 . 73 ALA CB C 19.30 0.2 1 608 . 73 ALA N N 121.50 0.2 1 609 . 74 HIS HA H 3.70 0.01 1 610 . 74 HIS HB2 H 2.82 0.01 1 611 . 74 HIS HB3 H 2.82 0.01 1 612 . 74 HIS H H 9.21 0.01 1 613 . 74 HIS CA C 60.20 0.2 1 614 . 74 HIS CB C 27.80 0.2 1 615 . 74 HIS N N 117.50 0.2 1 616 . 75 LYS HA H 3.92 0.01 1 617 . 75 LYS HB2 H 1.87 0.01 1 618 . 75 LYS HB3 H 1.87 0.01 1 619 . 75 LYS HD2 H 1.68 0.01 1 620 . 75 LYS HD3 H 1.67 0.01 1 621 . 75 LYS HE2 H 2.77 0.01 1 622 . 75 LYS HE3 H 2.77 0.01 1 623 . 75 LYS HG2 H 1.54 0.01 1 624 . 75 LYS HG3 H 1.36 0.01 1 625 . 75 LYS H H 7.45 0.01 1 626 . 75 LYS CA C 59.50 0.2 1 627 . 75 LYS CB C 32.90 0.2 1 628 . 75 LYS CD C 29.50 0.2 1 629 . 75 LYS CE C 41.70 0.2 1 630 . 75 LYS CG C 24.80 0.2 1 631 . 75 LYS N N 118.50 0.2 1 632 . 76 VAL HA H 4.02 0.01 1 633 . 76 VAL HB H 2.04 0.01 1 634 . 76 VAL HG1 H 0.99 0.01 1 635 . 76 VAL HG2 H 0.88 0.01 1 636 . 76 VAL H H 6.78 0.01 1 637 . 76 VAL CA C 63.50 0.2 1 638 . 76 VAL CB C 33.60 0.2 1 639 . 76 VAL CG1 C 20.80 0.2 1 640 . 76 VAL CG2 C 21.40 0.2 1 641 . 76 VAL N N 113.20 0.2 1 642 . 77 LEU HA H 4.15 0.01 1 643 . 77 LEU HD1 H 0.77 0.01 1 644 . 77 LEU HD2 H 0.77 0.01 1 645 . 77 LEU HG H 1.62 0.01 1 646 . 77 LEU H H 8.46 0.01 1 647 . 77 LEU CA C 55.40 0.2 1 648 . 77 LEU N N 118.50 0.2 1 649 . 78 GLY HA2 H 3.45 0.01 1 650 . 78 GLY HA3 H 2.37 0.01 1 651 . 78 GLY H H 7.62 0.01 1 652 . 78 GLY CA C 44.50 0.2 1 653 . 78 GLY N N 108.20 0.2 1 654 . 79 ASN HA H 3.06 0.01 1 655 . 79 ASN HB2 H 2.48 0.01 1 656 . 79 ASN HB3 H 2.36 0.01 1 657 . 79 ASN H H 8.00 0.01 1 658 . 79 ASN CA C 51.50 0.2 1 659 . 79 ASN CB C 35.30 0.2 1 660 . 79 ASN N N 124.00 0.2 1 661 . 80 ARG HA H 4.85 0.01 1 662 . 80 ARG HB2 H 1.11 0.01 1 663 . 80 ARG HB3 H 1.11 0.01 1 664 . 80 ARG HD2 H 3.11 0.01 1 665 . 80 ARG HD3 H 3.07 0.01 1 666 . 80 ARG HG2 H 1.49 0.01 1 667 . 80 ARG HG3 H 1.28 0.01 1 668 . 80 ARG H H 7.01 0.01 1 669 . 80 ARG CA C 52.60 0.2 1 670 . 80 ARG CB C 28.40 0.2 1 671 . 80 ARG CD C 43.40 0.2 1 672 . 80 ARG CG C 26.50 0.2 1 673 . 80 ARG N N 123.80 0.2 1 674 . 81 TRP HA H 4.34 0.01 1 675 . 81 TRP HB2 H 3.63 0.01 1 676 . 81 TRP HB3 H 3.48 0.01 1 677 . 81 TRP H H 6.76 0.01 1 678 . 81 TRP CA C 59.00 0.2 1 679 . 81 TRP CB C 29.30 0.2 1 680 . 81 TRP N N 123.80 0.2 1 681 . 82 ALA HA H 4.19 0.01 1 682 . 82 ALA HB H 1.62 0.01 1 683 . 82 ALA H H 10.13 0.01 1 684 . 82 ALA CA C 55.80 0.2 1 685 . 82 ALA CB C 17.90 0.2 1 686 . 82 ALA N N 122.50 0.2 1 687 . 83 GLU HA H 4.01 0.01 1 688 . 83 GLU HB2 H 1.91 0.01 1 689 . 83 GLU HB3 H 1.91 0.01 1 690 . 83 GLU HG2 H 2.27 0.01 1 691 . 83 GLU HG3 H 2.16 0.01 1 692 . 83 GLU H H 7.93 0.01 1 693 . 83 GLU CA C 58.80 0.2 1 694 . 83 GLU CB C 30.80 0.2 1 695 . 83 GLU CG C 36.70 0.2 1 696 . 83 GLU N N 118.50 0.2 1 697 . 84 ILE HA H 3.50 0.01 1 698 . 84 ILE HD1 H 0.73 0.01 1 699 . 84 ILE HG2 H 1.02 0.01 1 700 . 84 ILE H H 8.39 0.01 1 701 . 84 ILE CA C 65.90 0.2 1 702 . 84 ILE CB C 38.60 0.2 1 703 . 84 ILE CD1 C 12.70 0.2 1 704 . 84 ILE CG2 C 18.20 0.2 1 705 . 84 ILE N N 121.20 0.2 1 706 . 85 ALA HA H 3.98 0.01 1 707 . 85 ALA HB H 1.47 0.01 1 708 . 85 ALA H H 9.03 0.01 1 709 . 85 ALA CA C 55.50 0.2 1 710 . 85 ALA CB C 17.30 0.2 1 711 . 85 ALA N N 120.00 0.2 1 712 . 86 LYS HA H 4.00 0.01 1 713 . 86 LYS HB2 H 1.92 0.01 1 714 . 86 LYS HB3 H 1.88 0.01 1 715 . 86 LYS HD2 H 1.75 0.01 1 716 . 86 LYS HD3 H 1.70 0.01 1 717 . 86 LYS HE2 H 2.99 0.01 1 718 . 86 LYS HE3 H 2.99 0.01 1 719 . 86 LYS HG2 H 1.47 0.01 1 720 . 86 LYS HG3 H 1.44 0.01 1 721 . 86 LYS H H 7.14 0.01 1 722 . 86 LYS CA C 59.20 0.2 1 723 . 86 LYS CB C 32.90 0.2 1 724 . 86 LYS CD C 29.10 0.2 1 725 . 86 LYS CE C 41.70 0.2 1 726 . 86 LYS CG C 23.60 0.2 1 727 . 86 LYS N N 115.70 0.2 1 728 . 87 LEU HA H 4.28 0.01 1 729 . 87 LEU H H 7.89 0.01 1 730 . 87 LEU CA C 54.80 0.2 1 731 . 87 LEU N N 117.00 0.2 1 732 . 88 LEU HA H 4.85 0.01 1 733 . 88 LEU H H 7.56 0.01 1 734 . 88 LEU CA C 51.10 0.2 1 735 . 88 LEU N N 120.00 0.2 1 736 . 90 GLY HA2 H 4.24 0.01 1 737 . 90 GLY HA3 H 3.98 0.01 1 738 . 90 GLY H H 8.80 0.01 1 739 . 90 GLY CA C 45.20 0.2 1 740 . 90 GLY N N 113.00 0.2 1 741 . 91 ARG HA H 4.99 0.01 1 742 . 91 ARG HB2 H 2.45 0.01 1 743 . 91 ARG HB3 H 2.45 0.01 1 744 . 91 ARG HD2 H 2.68 0.01 1 745 . 91 ARG HD3 H 2.68 0.01 1 746 . 91 ARG HG2 H 1.45 0.01 1 747 . 91 ARG HG3 H 1.12 0.01 1 748 . 91 ARG H H 8.22 0.01 1 749 . 91 ARG CA C 51.90 0.2 1 750 . 91 ARG CB C 31.20 0.2 1 751 . 91 ARG CG C 25.70 0.2 1 752 . 91 ARG N N 117.50 0.2 1 753 . 92 THR HA H 4.76 0.01 1 754 . 92 THR HB H 4.75 0.01 1 755 . 92 THR HG2 H 1.32 0.01 1 756 . 92 THR H H 7.71 0.01 1 757 . 92 THR CA C 59.30 0.2 1 758 . 92 THR CB C 72.10 0.2 1 759 . 92 THR CG2 C 21.90 0.2 1 760 . 92 THR N N 110.00 0.2 1 761 . 93 ASP HA H 4.00 0.01 1 762 . 93 ASP HB2 H 2.93 0.01 1 763 . 93 ASP HB3 H 2.93 0.01 1 764 . 93 ASP H H 9.43 0.01 1 765 . 93 ASP CA C 57.20 0.2 1 766 . 93 ASP CB C 38.60 0.2 1 767 . 93 ASP N N 121.20 0.2 1 768 . 94 ASN HA H 4.29 0.01 1 769 . 94 ASN HB2 H 2.73 0.01 1 770 . 94 ASN HB3 H 2.60 0.01 1 771 . 94 ASN H H 8.28 0.01 1 772 . 94 ASN CA C 56.50 0.2 1 773 . 94 ASN CB C 38.60 0.2 1 774 . 94 ASN N N 120.70 0.2 1 775 . 95 ALA HA H 4.53 0.01 1 776 . 95 ALA HB H 1.85 0.01 1 777 . 95 ALA H H 7.81 0.01 1 778 . 95 ALA CA C 55.10 0.2 1 779 . 95 ALA CB C 19.00 0.2 1 780 . 95 ALA N N 120.50 0.2 1 781 . 96 VAL HA H 3.54 0.01 1 782 . 96 VAL HB H 2.31 0.01 1 783 . 96 VAL HG1 H 1.31 0.01 1 784 . 96 VAL HG2 H 1.23 0.01 1 785 . 96 VAL H H 8.73 0.01 1 786 . 96 VAL CA C 67.20 0.2 1 787 . 96 VAL CB C 32.10 0.2 1 788 . 96 VAL CG1 C 24.10 0.2 1 789 . 96 VAL CG2 C 22.20 0.2 1 790 . 96 VAL N N 119.20 0.2 1 791 . 97 LYS HA H 4.25 0.01 1 792 . 97 LYS HB2 H 1.84 0.01 1 793 . 97 LYS HB3 H 1.27 0.01 1 794 . 97 LYS HD2 H 1.50 0.01 1 795 . 97 LYS HD3 H 1.50 0.01 1 796 . 97 LYS HE2 H 3.01 0.01 1 797 . 97 LYS HE3 H 2.79 0.01 1 798 . 97 LYS HG2 H 1.47 0.01 1 799 . 97 LYS HG3 H 1.30 0.01 1 800 . 97 LYS H H 7.69 0.01 1 801 . 97 LYS CA C 58.90 0.2 1 802 . 97 LYS CB C 32.70 0.2 1 803 . 97 LYS CD C 29.10 0.2 1 804 . 97 LYS CE C 41.70 0.2 1 805 . 97 LYS CG C 24.80 0.2 1 806 . 97 LYS N N 121.70 0.2 1 807 . 98 ASN HA H 4.51 0.01 1 808 . 98 ASN HB2 H 3.02 0.01 1 809 . 98 ASN HB3 H 2.90 0.01 1 810 . 98 ASN H H 8.51 0.01 1 811 . 98 ASN CA C 55.10 0.2 1 812 . 98 ASN CB C 41.30 0.2 1 813 . 98 ASN N N 116.20 0.2 1 814 . 99 HIS HA H 4.49 0.01 1 815 . 99 HIS HB2 H 2.88 0.01 1 816 . 99 HIS HB3 H 2.50 0.01 1 817 . 99 HIS H H 8.27 0.01 1 818 . 99 HIS CA C 57.70 0.2 1 819 . 99 HIS CB C 28.30 0.2 1 820 . 99 HIS N N 119.50 0.2 1 821 . 100 TRP HA H 3.78 0.01 1 822 . 100 TRP HB2 H 3.09 0.01 1 823 . 100 TRP HB3 H 3.08 0.01 1 824 . 100 TRP H H 8.93 0.01 1 825 . 100 TRP CA C 60.80 0.2 1 826 . 100 TRP N N 122.20 0.2 1 827 . 101 ASN HA H 4.22 0.01 1 828 . 101 ASN HB2 H 2.84 0.01 1 829 . 101 ASN HB3 H 2.65 0.01 1 830 . 101 ASN H H 8.48 0.01 1 831 . 101 ASN CA C 55.90 0.2 1 832 . 101 ASN CB C 38.60 0.2 1 833 . 101 ASN N N 113.70 0.2 1 834 . 102 SER HA H 4.20 0.01 1 835 . 102 SER HB2 H 3.88 0.01 1 836 . 102 SER HB3 H 3.82 0.01 1 837 . 102 SER H H 8.34 0.01 1 838 . 102 SER CA C 60.40 0.2 1 839 . 102 SER CB C 64.70 0.2 1 840 . 102 SER N N 111.50 0.2 1 841 . 103 THR HA H 4.18 0.01 1 842 . 103 THR HB H 3.43 0.01 1 843 . 103 THR HG2 H 0.99 0.01 1 844 . 103 THR H H 7.27 0.01 1 845 . 103 THR CA C 65.10 0.2 1 846 . 103 THR CB C 70.20 0.2 1 847 . 103 THR CG2 C 21.70 0.2 1 848 . 103 THR N N 113.2 0.2 1 849 . 104 ILE HA H 3.46 0.01 1 850 . 104 ILE HB H 1.40 0.01 1 851 . 104 ILE HD1 H 0.56 0.01 1 852 . 104 ILE HG12 H 0.71 0.01 1 853 . 104 ILE HG13 H 0.50 0.01 1 854 . 104 ILE HG2 H 0.57 0.01 1 855 . 104 ILE H H 7.33 0.01 1 856 . 104 ILE CA C 63.60 0.2 1 857 . 104 ILE CB C 39.30 0.2 1 858 . 104 ILE CD1 C 12.00 0.2 1 859 . 104 ILE CG1 C 27.00 0.2 1 860 . 104 ILE CG2 C 18.40 0.2 1 861 . 104 ILE N N 118.50 0.2 1 862 . 105 LYS HA H 4.14 0.01 1 863 . 105 LYS HB2 H 1.77 0.01 1 864 . 105 LYS HB3 H 1.77 0.01 1 865 . 105 LYS HD2 H 1.66 0.01 1 866 . 105 LYS HD3 H 1.66 0.01 1 867 . 105 LYS HE2 H 2.97 0.01 1 868 . 105 LYS HE3 H 2.97 0.01 1 869 . 105 LYS HG2 H 1.37 0.01 1 870 . 105 LYS HG3 H 1.37 0.01 1 871 . 105 LYS H H 7.98 0.01 1 872 . 105 LYS CA C 58.30 0.2 1 873 . 105 LYS CB C 31.50 0.2 1 874 . 105 LYS CD C 29.10 0.2 1 875 . 105 LYS CE C 41.90 0.2 1 876 . 105 LYS CG C 24.50 0.2 1 877 . 105 LYS N N 119.80 0.2 1 878 . 106 ARG HA H 4.12 0.01 1 879 . 106 ARG HB2 H 1.81 0.01 1 880 . 106 ARG HB3 H 1.72 0.01 1 881 . 106 ARG HD2 H 3.17 0.01 1 882 . 106 ARG HD3 H 3.17 0.01 1 883 . 106 ARG HG2 H 1.59 0.01 1 884 . 106 ARG HG3 H 1.45 0.01 1 885 . 106 ARG H H 7.04 0.01 1 886 . 106 ARG CA C 56.60 0.2 1 887 . 106 ARG CB C 30.30 0.2 1 888 . 106 ARG CD C 43.30 0.2 1 889 . 106 ARG CG C 27.20 0.2 1 890 . 106 ARG N N 115.50 0.2 1 891 . 107 LYS HA H 4.20 0.01 1 892 . 107 LYS HB2 H 1.88 0.01 1 893 . 107 LYS HB3 H 1.74 0.01 1 894 . 107 LYS HD2 H 1.69 0.01 1 895 . 107 LYS HD3 H 1.34 0.01 1 896 . 107 LYS HE2 H 2.99 0.01 1 897 . 107 LYS HE3 H 2.95 0.01 1 898 . 107 LYS HG2 H 1.44 0.01 1 899 . 107 LYS HG3 H 1.34 0.01 1 900 . 107 LYS H H 7.68 0.01 1 901 . 107 LYS CA C 56.70 0.2 1 902 . 107 LYS CB C 33.00 0.2 1 903 . 107 LYS CD C 29.10 0.2 1 904 . 107 LYS CE C 41.70 0.2 1 905 . 107 LYS CG C 24.60 0.2 1 906 . 107 LYS N N 120.00 0.2 1 907 . 108 VAL HA H 4.13 0.01 1 908 . 108 VAL HB H 2.07 0.01 1 909 . 108 VAL HG1 H 0.92 0.01 1 910 . 108 VAL HG2 H 0.88 0.01 1 911 . 108 VAL H H 7.62 0.01 1 912 . 108 VAL CA C 62.10 0.2 1 913 . 108 VAL CB C 33.10 0.2 1 914 . 108 VAL CG1 C 20.40 0.2 1 915 . 108 VAL CG2 C 21.08 0.2 1 916 . 108 VAL N N 118.50 0.2 1 917 . 109 ASP HA H 4.71 0.01 1 918 . 109 ASP HB2 H 2.74 0.01 1 919 . 109 ASP HB3 H 2.59 0.01 1 920 . 109 ASP H H 8.31 0.01 1 921 . 109 ASP CA C 54.40 0.2 1 922 . 109 ASP CB C 41.30 0.2 1 923 . 109 ASP N N 123.70 0.2 1 924 . 110 THR HA H 4.15 0.01 1 925 . 110 THR HB H 4.20 0.01 1 926 . 110 THR HG2 H 1.13 0.01 1 927 . 110 THR H H 7.69 0.01 1 928 . 110 THR CA C 63.10 0.2 1 929 . 110 THR CB C 71.20 0.2 1 930 . 110 THR CG2 C 21.70 0.2 1 931 . 110 THR N N 119.00 0.2 1 stop_ save_