data_6019 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of Archaeon DNA-binding protein ssh10b P62A mutant ; _BMRB_accession_number 6019 _BMRB_flat_file_name bmr6019.str _Entry_type new _Submission_date 2003-11-21 _Accession_date 2003-11-21 _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 Cui Qiu . . 2 Tong Yufeng . . 3 Wang Jinfeng . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 465 "13C chemical shifts" 317 "15N chemical shifts" 92 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-11-17 update author 'update entry citation' 2004-06-25 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 5226 'Ssh10b dimer in Sac10b family' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'A Stabilizing alpha/beta-Hydrophobic Core Greatly Contributes to Hyperthermostability of Archaeal [P62A]Ssh10b' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18821773 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Fang Xianyang . . 2 Cui Qiu . . 3 Tong Yufeng . . 4 Feng Yingang . . 5 Shan Lu . . 6 Huang Li . . 7 Wang Jinfeng . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 47 _Journal_issue 43 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 11212 _Page_last 11221 _Year 2008 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full . _Citation_title 'Two Conformations of Archaeal Ssh10b. The Origin of Its Temperature-dependent Interaction with DNA' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14523014 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cui Qiu . . 2 Tong Yufeng . . 3 Xue Hong . . 4 Huang Li . . 5 Feng Yingang . . 6 Wang Jinfeng . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of Biological Chemistry' _Journal_volume 278 _Journal_issue 51 _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 51015 _Page_last 51022 _Year 2003 _Details . save_ save_ref_2 _Saveframe_category citation _Citation_full ; J Bacteriol. 2000 Jul;182(14):3929-33. ; _Citation_title 'An abundant DNA binding protein from the hyperthermophilic archaeon Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent fashion.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10869069 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Xue H. . . 2 Guo R. . . 3 Wen Y. . . 4 Liu D. . . 5 Huang L. . . stop_ _Journal_abbreviation 'J. Bacteriol.' _Journal_name_full 'Journal of bacteriology' _Journal_volume 182 _Journal_issue 14 _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 3929 _Page_last 3933 _Year 2000 _Details ; The DNA binding protein Ssh10b, a member of the Sac10b family, has been purified from the hyperthermophilic archaeon Sulfolobus shibatae. Ssh10b constitutes about 4% of the cellular protein. Electrophoretic mobility shift assays showed that Ssh10b first bound a double-stranded DNA fragment with an estimated binding size of approximately approximately 12 bp, forming distinct shifts, until the DNA was coated with the protein. Binding of more Ssh10b resulted in the formation of smears of lower mobilities. The migration pattern of the smearing Ssh10b-DNA complexes was affected by temperature, whereas that of complexes associated with the distinct shifts was not. Interestingly, Ssh10b was capable of constraining negative DNA supercoils in a temperature-dependent fashion. While the ability of the protein to constrain supercoils was weak at 25 degrees C, it was enhanced substantially at 45 degrees C or higher temperatures (up to 80 degrees C). Taken together, our data suggest that archaeal proteins of the Sac10b family may affect the topology of chromosomal DNA in thermophilic archaea at their growth temperatures. ; save_ ################################## # Molecular system description # ################################## save_Alba _Saveframe_category molecular_system _Mol_system_name 'P62A dimer' _Abbreviation_common Alba _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'P62A subunit 1' $P62A 'P62A subunit 2' $P62A stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'P62A subunit 1' 1 'P62A subunit 2' stop_ loop_ _Biological_function 'histone-like DNA binding protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_P62A _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common P62A _Abbreviation_common P62A _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 97 _Mol_residue_sequence ; MSSGTPTPSNVVLIGKKPVM NYVLAALTLLNQGVSEIVIK ARGRAISKAVDTVEIVRNRF LADKIEIKEIRVGSQVVTSQ DGRQSRVSTIEIAIRKK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 SER 4 GLY 5 THR 6 PRO 7 THR 8 PRO 9 SER 10 ASN 11 VAL 12 VAL 13 LEU 14 ILE 15 GLY 16 LYS 17 LYS 18 PRO 19 VAL 20 MET 21 ASN 22 TYR 23 VAL 24 LEU 25 ALA 26 ALA 27 LEU 28 THR 29 LEU 30 LEU 31 ASN 32 GLN 33 GLY 34 VAL 35 SER 36 GLU 37 ILE 38 VAL 39 ILE 40 LYS 41 ALA 42 ARG 43 GLY 44 ARG 45 ALA 46 ILE 47 SER 48 LYS 49 ALA 50 VAL 51 ASP 52 THR 53 VAL 54 GLU 55 ILE 56 VAL 57 ARG 58 ASN 59 ARG 60 PHE 61 LEU 62 ALA 63 ASP 64 LYS 65 ILE 66 GLU 67 ILE 68 LYS 69 GLU 70 ILE 71 ARG 72 VAL 73 GLY 74 SER 75 GLN 76 VAL 77 VAL 78 THR 79 SER 80 GLN 81 ASP 82 GLY 83 ARG 84 GLN 85 SER 86 ARG 87 VAL 88 SER 89 THR 90 ILE 91 GLU 92 ILE 93 ALA 94 ILE 95 ARG 96 LYS 97 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-11-09 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 5226 Ssh10b 100.00 97 98.97 98.97 7.14e-59 PDB 1H0X "Structure Of Alba: An Archaeal Chromatin Protein Modulated By Acetylation" 100.00 100 98.97 98.97 6.71e-59 PDB 1H0Y "Structure Of Alba: An Archaeal Chromatin Protein Modulated By Acetylation" 100.00 100 98.97 98.97 6.71e-59 PDB 1Y9X "Solution Structure Of Archaeon Dna-Binding Protein Ssh10b" 100.00 97 100.00 100.00 7.98e-60 PDB 2BKY "Crystal Structure Of The Alba1:alba2 Heterodimer From Sulfolobus Solfataricus" 100.00 97 98.97 98.97 7.14e-59 PDB 3WBM "Crystal Structure Of Protein-rna Complex" 100.00 97 98.97 98.97 7.14e-59 EMBL CAA67066 "unknown [Sulfolobus shibatae B12]" 100.00 97 98.97 98.97 7.14e-59 EMBL CAC12668 "putative histone-like protein [Sulfolobus solfataricus]" 100.00 97 98.97 98.97 7.14e-59 GB AAK41236 "DNA binding protein SSO10b [Sulfolobus solfataricus P2]" 100.00 100 98.97 98.97 6.71e-59 GB ACP35357 "DNA-binding protein Alba [Sulfolobus islandicus L.S.2.15]" 100.00 97 98.97 98.97 7.14e-59 GB ACP38017 "DNA-binding protein Alba [Sulfolobus islandicus M.14.25]" 100.00 97 98.97 98.97 7.14e-59 GB ACP45513 "DNA-binding protein Alba [Sulfolobus islandicus Y.G.57.14]" 100.00 97 98.97 98.97 7.14e-59 GB ACP48689 "DNA-binding protein Alba [Sulfolobus islandicus Y.N.15.51]" 100.00 97 98.97 98.97 7.14e-59 REF NP_342446 "DNA/RNA-binding protein albA [Sulfolobus solfataricus P2]" 100.00 100 98.97 98.97 6.71e-59 REF WP_009992406 "MULTISPECIES: DNA-binding protein [Sulfolobus]" 100.00 97 98.97 98.97 7.14e-59 REF WP_010923153 "DNA-binding protein [Sulfolobus solfataricus]" 100.00 100 98.97 98.97 6.71e-59 REF YP_002829315 "DNA/RNA-binding protein albA [Sulfolobus islandicus M.14.25]" 100.00 97 98.97 98.97 7.14e-59 REF YP_002832002 "DNA/RNA-binding protein albA [Sulfolobus islandicus L.S.2.15]" 100.00 97 98.97 98.97 7.14e-59 SP P60848 "RecName: Full=DNA/RNA-binding protein Alba 1; AltName: Full=Ssh10b [Sulfolobus shibatae]" 100.00 97 98.97 98.97 7.14e-59 SP P60849 "RecName: Full=DNA/RNA-binding protein Alba 1; AltName: Full=Sso10b [Sulfolobus solfataricus P2]" 100.00 97 98.97 98.97 7.14e-59 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _ATCC_number $P62A 'Sulfolobus shibatae' 2286 Archaea . Sulfolobus shibatae 51178 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 $P62A 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $P62A 1.5 mM '[U-95% 13C; U-98% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name Felix _Version 98.0 loop_ _Task 'Data processing' 'Peak assignments' stop_ _Details 'Home-written macroes for processing spectra' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_C(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _Sample_label . save_ save_HCCH-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 0.1 n/a temperature 310 0.1 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_C _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'P62A 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 . 2 SER CA C 59.061 0.24 1 2 . 2 SER CB C 64.337 0.27 1 3 . 3 SER N N 117.694 0.07 1 4 . 3 SER H H 8.347 0.01 1 5 . 3 SER HA H 4.675 0.02 1 6 . 3 SER CA C 58.620 0.24 1 7 . 3 SER CB C 63.954 0.27 1 8 . 4 GLY N N 111.395 0.07 1 9 . 4 GLY H H 8.397 0.01 1 10 . 4 GLY CA C 45.325 0.24 1 11 . 5 THR N N 117.048 0.07 1 12 . 5 THR H H 8.025 0.01 1 13 . 5 THR HA H 4.607 0.02 1 14 . 5 THR HB H 4.132 0.02 1 15 . 5 THR HG2 H 1.274 0.02 1 16 . 5 THR CA C 59.837 0.24 1 17 . 5 THR CB C 70.376 0.27 1 18 . 5 THR CG2 C 21.865 0.28 1 19 . 6 PRO HA H 4.495 0.02 1 20 . 6 PRO HB2 H 2.295 0.02 2 21 . 6 PRO HB3 H 1.906 0.02 2 22 . 6 PRO HD2 H 3.861 0.02 2 23 . 6 PRO HD3 H 3.730 0.02 2 24 . 6 PRO CA C 63.282 0.24 1 25 . 6 PRO CB C 32.209 0.27 1 26 . 6 PRO CG C 27.382 0.28 1 27 . 6 PRO CD C 51.195 0.28 1 28 . 7 THR N N 118.262 0.07 1 29 . 7 THR H H 8.250 0.01 1 30 . 7 THR HA H 4.551 0.02 1 31 . 7 THR HB H 4.115 0.02 1 32 . 7 THR HG2 H 1.285 0.02 1 33 . 7 THR CA C 60.021 0.24 1 34 . 7 THR CB C 70.183 0.27 1 35 . 7 THR CG2 C 21.540 0.28 1 36 . 8 PRO HA H 4.482 0.02 1 37 . 8 PRO HB2 H 1.951 0.02 2 38 . 8 PRO HB3 H 2.340 0.02 2 39 . 8 PRO HD2 H 3.675 0.02 2 40 . 8 PRO HD3 H 3.865 0.02 2 41 . 8 PRO CA C 63.241 0.24 1 42 . 8 PRO CB C 32.302 0.27 1 43 . 8 PRO CG C 27.414 0.28 1 44 . 8 PRO CD C 51.159 0.28 1 45 . 9 SER N N 115.956 0.07 1 46 . 9 SER H H 8.364 0.01 1 47 . 9 SER HA H 4.470 0.02 1 48 . 9 SER HB2 H 3.973 0.02 2 49 . 9 SER HB3 H 3.880 0.02 2 50 . 9 SER CA C 58.662 0.24 1 51 . 9 SER CB C 63.762 0.27 1 52 . 10 ASN N N 122.154 0.07 1 53 . 10 ASN H H 8.228 0.01 1 54 . 10 ASN HA H 4.821 0.02 1 55 . 10 ASN HB2 H 3.490 0.02 2 56 . 10 ASN HB3 H 2.690 0.02 2 57 . 10 ASN CA C 52.677 0.24 1 58 . 10 ASN CB C 38.155 0.27 1 59 . 11 VAL N N 119.440 0.07 1 60 . 11 VAL H H 7.500 0.01 1 61 . 11 VAL HA H 4.906 0.02 1 62 . 11 VAL HB H 1.891 0.02 1 63 . 11 VAL HG1 H 0.779 0.02 2 64 . 11 VAL HG2 H 0.875 0.02 2 65 . 11 VAL CA C 60.885 0.24 1 66 . 11 VAL CB C 34.295 0.27 1 67 . 11 VAL CG1 C 21.437 0.28 1 68 . 12 VAL N N 129.822 0.07 1 69 . 12 VAL H H 9.163 0.01 1 70 . 12 VAL HA H 4.111 0.02 1 71 . 12 VAL HB H 2.049 0.02 1 72 . 12 VAL HG1 H 0.777 0.02 2 73 . 12 VAL HG2 H 1.020 0.02 2 74 . 12 VAL CA C 61.799 0.24 1 75 . 12 VAL CB C 33.344 0.27 1 76 . 12 VAL CG1 C 20.694 0.28 1 77 . 13 LEU N N 129.447 0.07 1 78 . 13 LEU H H 8.312 0.01 1 79 . 13 LEU HA H 4.667 0.02 1 80 . 13 LEU HB2 H 1.408 0.02 2 81 . 13 LEU HB3 H 1.634 0.02 2 82 . 13 LEU HG H 1.418 0.02 1 83 . 13 LEU HD2 H 0.825 0.02 2 84 . 13 LEU CA C 53.547 0.24 1 85 . 13 LEU CB C 42.358 0.27 1 86 . 13 LEU CG C 27.135 0.28 1 87 . 13 LEU CD1 C 24.025 0.28 1 88 . 13 LEU CD2 C 25.068 0.28 1 89 . 14 ILE N N 126.909 0.07 1 90 . 14 ILE H H 8.603 0.01 1 91 . 14 ILE HA H 2.678 0.02 1 92 . 14 ILE HB H 1.964 0.02 1 93 . 14 ILE HG2 H 0.656 0.02 1 94 . 14 ILE HD1 H 0.353 0.02 1 95 . 14 ILE CA C 59.493 0.24 1 96 . 14 ILE CB C 34.379 0.27 1 97 . 14 ILE CG1 C 27.061 0.28 1 98 . 14 ILE CG2 C 18.372 0.28 1 99 . 14 ILE CD1 C 10.109 0.28 1 100 . 15 GLY N N 118.000 0.07 1 101 . 15 GLY H H 6.174 0.01 1 102 . 15 GLY HA2 H 4.549 0.02 2 103 . 15 GLY HA3 H 3.769 0.02 2 104 . 15 GLY CA C 45.842 0.24 1 105 . 16 LYS HA H 4.255 0.02 1 106 . 16 LYS HB2 H 1.850 0.02 2 107 . 16 LYS HB3 H 2.037 0.02 2 108 . 16 LYS CA C 57.561 0.24 1 109 . 16 LYS CB C 33.597 0.27 1 110 . 16 LYS CG C 25.053 0.28 1 111 . 16 LYS CD C 29.434 0.28 1 112 . 16 LYS CE C 42.103 0.28 1 113 . 17 LYS N N 119.800 0.07 1 114 . 17 LYS H H 7.991 0.01 1 115 . 17 LYS HA H 4.468 0.02 1 116 . 17 LYS HB2 H 1.680 0.02 2 117 . 17 LYS HB3 H 1.550 0.02 2 118 . 17 LYS CA C 56.291 0.24 1 119 . 17 LYS CB C 29.300 0.27 1 120 . 17 LYS CE C 42.134 0.28 1 121 . 18 PRO HA H 4.510 0.02 1 122 . 18 PRO HB2 H 1.843 0.02 2 123 . 18 PRO HB3 H 2.510 0.02 2 124 . 18 PRO HG2 H 2.025 0.02 2 125 . 18 PRO HG3 H 2.130 0.02 2 126 . 18 PRO HD2 H 3.467 0.02 2 127 . 18 PRO HD3 H 3.865 0.02 2 128 . 18 PRO CA C 63.545 0.24 1 129 . 18 PRO CB C 32.296 0.27 1 130 . 18 PRO CG C 28.401 0.28 1 131 . 18 PRO CD C 50.604 0.28 1 132 . 19 VAL N N 122.652 0.07 1 133 . 19 VAL H H 8.700 0.01 1 134 . 19 VAL HA H 3.950 0.02 1 135 . 19 VAL HB H 2.278 0.02 1 136 . 19 VAL HG2 H 1.020 0.02 2 137 . 19 VAL CA C 66.846 0.24 1 138 . 19 VAL CB C 32.325 0.27 1 139 . 19 VAL CG1 C 20.280 0.28 1 140 . 19 VAL CG2 C 24.050 0.28 1 141 . 20 MET N N 118.285 0.07 1 142 . 20 MET H H 8.632 0.01 1 143 . 20 MET HA H 4.492 0.02 1 144 . 20 MET HB2 H 2.122 0.02 2 145 . 20 MET HB3 H 2.048 0.02 2 146 . 20 MET HG2 H 2.813 0.02 2 147 . 20 MET HG3 H 2.716 0.02 2 148 . 20 MET CA C 56.454 0.24 1 149 . 20 MET CB C 29.676 0.27 1 150 . 20 MET CG C 32.589 0.28 1 151 . 21 ASN N N 117.389 0.07 1 152 . 21 ASN H H 7.983 0.01 1 153 . 21 ASN HA H 4.110 0.02 1 154 . 21 ASN HB2 H 2.256 0.02 2 155 . 21 ASN HB3 H 2.146 0.02 2 156 . 21 ASN CA C 57.554 0.24 1 157 . 21 ASN CB C 38.457 0.27 1 158 . 22 TYR N N 120.381 0.07 1 159 . 22 TYR H H 7.186 0.01 1 160 . 22 TYR HA H 4.255 0.02 1 161 . 22 TYR HB2 H 3.115 0.02 2 162 . 22 TYR HB3 H 2.945 0.02 2 163 . 22 TYR HD1 H 7.110 0.02 3 164 . 22 TYR HE1 H 7.090 0.02 3 165 . 22 TYR CA C 60.702 0.24 1 166 . 22 TYR CB C 38.198 0.27 1 167 . 23 VAL N N 122.131 0.07 1 168 . 23 VAL H H 8.011 0.01 1 169 . 23 VAL HA H 3.400 0.02 1 170 . 23 VAL HB H 2.412 0.02 1 171 . 23 VAL HG1 H 0.802 0.02 2 172 . 23 VAL HG2 H 1.322 0.02 2 173 . 23 VAL CA C 66.469 0.24 1 174 . 23 VAL CB C 32.292 0.27 1 175 . 23 VAL CG1 C 21.131 0.28 1 176 . 23 VAL CG2 C 23.808 0.28 1 177 . 24 LEU N N 118.108 0.07 1 178 . 24 LEU H H 8.146 0.01 1 179 . 24 LEU HA H 3.930 0.02 1 180 . 24 LEU HB2 H 1.526 0.02 2 181 . 24 LEU HB3 H 1.746 0.02 2 182 . 24 LEU HG H 1.740 0.02 1 183 . 24 LEU HD1 H 0.776 0.02 2 184 . 24 LEU HD2 H 0.838 0.02 2 185 . 24 LEU CA C 58.126 0.24 1 186 . 24 LEU CB C 40.785 0.27 1 187 . 24 LEU CG C 27.370 0.28 1 188 . 24 LEU CD1 C 22.763 0.28 1 189 . 24 LEU CD2 C 24.550 0.28 1 190 . 25 ALA N N 123.895 0.07 1 191 . 25 ALA H H 7.528 0.01 1 192 . 25 ALA HA H 4.140 0.02 1 193 . 25 ALA HB H 1.638 0.02 1 194 . 25 ALA CA C 55.610 0.24 1 195 . 25 ALA CB C 18.121 0.27 1 196 . 26 ALA N N 120.853 0.07 1 197 . 26 ALA H H 8.119 0.01 1 198 . 26 ALA HA H 3.924 0.02 1 199 . 26 ALA HB H 1.382 0.02 1 200 . 26 ALA CA C 55.413 0.24 1 201 . 26 ALA CB C 17.792 0.27 1 202 . 27 LEU N N 117.428 0.07 1 203 . 27 LEU H H 8.591 0.01 1 204 . 27 LEU HA H 3.910 0.02 1 205 . 27 LEU HB2 H 1.819 0.02 2 206 . 27 LEU HB3 H 1.488 0.02 2 207 . 27 LEU HG H 0.804 0.02 1 208 . 27 LEU HD2 H 0.535 0.02 2 209 . 27 LEU CA C 58.167 0.24 1 210 . 27 LEU CB C 41.780 0.27 1 211 . 27 LEU CG C 23.529 0.28 1 212 . 27 LEU CD1 C 25.836 0.28 1 213 . 28 THR N N 116.634 0.07 1 214 . 28 THR H H 8.270 0.01 1 215 . 28 THR HA H 3.900 0.02 1 216 . 28 THR HB H 4.312 0.02 1 217 . 28 THR HG2 H 1.213 0.02 1 218 . 28 THR CA C 67.295 0.24 1 219 . 28 THR CB C 68.632 0.27 1 220 . 28 THR CG2 C 21.180 0.28 1 221 . 29 LEU N N 121.249 0.07 1 222 . 29 LEU H H 7.219 0.01 1 223 . 29 LEU HA H 4.045 0.02 1 224 . 29 LEU HB2 H 1.262 0.02 2 225 . 29 LEU HB3 H 2.036 0.02 2 226 . 29 LEU HG H 1.820 0.02 1 227 . 29 LEU HD1 H 0.839 0.02 2 228 . 29 LEU HD2 H 0.921 0.02 2 229 . 29 LEU CA C 58.364 0.24 1 230 . 29 LEU CB C 42.796 0.27 1 231 . 29 LEU CG C 27.154 0.28 1 232 . 29 LEU CD1 C 26.052 0.28 1 233 . 29 LEU CD2 C 23.229 0.28 1 234 . 30 LEU N N 119.192 0.07 1 235 . 30 LEU H H 8.013 0.01 1 236 . 30 LEU HA H 4.287 0.02 1 237 . 30 LEU HB2 H 1.249 0.02 2 238 . 30 LEU HB3 H 1.866 0.02 2 239 . 30 LEU HG H 1.783 0.02 1 240 . 30 LEU HD1 H 0.608 0.02 2 241 . 30 LEU HD2 H 0.765 0.02 2 242 . 30 LEU CA C 57.844 0.24 1 243 . 30 LEU CB C 42.060 0.27 1 244 . 30 LEU CG C 27.039 0.28 1 245 . 30 LEU CD1 C 26.111 0.28 1 246 . 30 LEU CD2 C 23.235 0.28 1 247 . 31 ASN N N 118.812 0.07 1 248 . 31 ASN H H 8.562 0.01 1 249 . 31 ASN HA H 4.660 0.02 1 250 . 31 ASN HB2 H 2.921 0.02 2 251 . 31 ASN HB3 H 2.970 0.02 2 252 . 31 ASN CA C 54.995 0.24 1 253 . 31 ASN CB C 38.448 0.27 1 254 . 32 GLN N N 119.279 0.07 1 255 . 32 GLN H H 7.771 0.01 1 256 . 32 GLN HA H 4.468 0.02 1 257 . 32 GLN HG2 H 2.618 0.02 2 258 . 32 GLN HG3 H 2.570 0.02 2 259 . 32 GLN CA C 56.065 0.24 1 260 . 32 GLN CB C 28.695 0.27 1 261 . 32 GLN CG C 34.384 0.28 1 262 . 33 GLY N N 106.656 0.07 1 263 . 33 GLY H H 7.680 0.01 1 264 . 33 GLY HA2 H 3.703 0.02 2 265 . 33 GLY HA3 H 4.285 0.02 2 266 . 33 GLY CA C 45.712 0.24 1 267 . 34 VAL N N 122.332 0.07 1 268 . 34 VAL H H 7.444 0.01 1 269 . 34 VAL HA H 4.032 0.02 1 270 . 34 VAL HB H 1.916 0.02 1 271 . 34 VAL HG1 H 0.913 0.02 2 272 . 34 VAL HG2 H 0.974 0.02 2 273 . 34 VAL CA C 62.876 0.24 1 274 . 34 VAL CB C 31.224 0.27 1 275 . 34 VAL CG1 C 21.199 0.28 1 276 . 34 VAL CG2 C 22.497 0.28 1 277 . 35 SER N N 119.635 0.07 1 278 . 35 SER H H 8.270 0.01 1 279 . 35 SER HA H 4.260 0.02 1 280 . 35 SER CA C 60.742 0.24 1 281 . 35 SER CB C 64.115 0.27 1 282 . 36 GLU N N 119.505 0.07 1 283 . 36 GLU H H 7.299 0.01 1 284 . 36 GLU HA H 5.330 0.02 1 285 . 36 GLU HG2 H 2.111 0.02 2 286 . 36 GLU HG3 H 1.920 0.02 2 287 . 36 GLU CA C 55.188 0.24 1 288 . 36 GLU CB C 32.771 0.27 1 289 . 36 GLU CG C 36.608 0.28 1 290 . 37 ILE N N 120.127 0.07 1 291 . 37 ILE H H 8.595 0.01 1 292 . 37 ILE HA H 5.010 0.02 1 293 . 37 ILE HB H 1.734 0.02 1 294 . 37 ILE HG12 H 0.948 0.02 2 295 . 37 ILE HG13 H 1.334 0.02 2 296 . 37 ILE HG2 H 0.827 0.02 1 297 . 37 ILE HD1 H 0.810 0.02 1 298 . 37 ILE CA C 59.018 0.24 1 299 . 37 ILE CB C 42.125 0.27 1 300 . 37 ILE CG1 C 27.085 0.28 1 301 . 37 ILE CG2 C 18.579 0.28 1 302 . 37 ILE CD1 C 15.294 0.28 1 303 . 38 VAL N N 123.080 0.07 1 304 . 38 VAL H H 8.508 0.01 1 305 . 38 VAL HA H 4.865 0.02 1 306 . 38 VAL HB H 1.850 0.02 1 307 . 38 VAL HG1 H 0.775 0.02 2 308 . 38 VAL HG2 H 0.855 0.02 2 309 . 38 VAL CA C 60.976 0.24 1 310 . 38 VAL CB C 34.650 0.27 1 311 . 38 VAL CG1 C 21.686 0.28 1 312 . 39 ILE N N 129.611 0.07 1 313 . 39 ILE H H 9.246 0.01 1 314 . 39 ILE HA H 4.829 0.02 1 315 . 39 ILE HB H 1.880 0.02 1 316 . 39 ILE HG12 H 1.287 0.02 2 317 . 39 ILE HG13 H 1.443 0.02 2 318 . 39 ILE HG2 H 0.887 0.02 1 319 . 39 ILE HD1 H 0.766 0.02 1 320 . 39 ILE CA C 59.675 0.24 1 321 . 39 ILE CB C 38.681 0.27 1 322 . 39 ILE CG1 C 28.946 0.28 1 323 . 39 ILE CG2 C 18.645 0.28 1 324 . 39 ILE CD1 C 12.968 0.28 1 325 . 40 LYS N N 127.046 0.07 1 326 . 40 LYS H H 8.559 0.01 1 327 . 40 LYS HA H 5.385 0.02 1 328 . 40 LYS HB2 H 1.510 0.02 2 329 . 40 LYS HB3 H 1.798 0.02 2 330 . 40 LYS HG2 H 1.169 0.02 2 331 . 40 LYS HG3 H 1.374 0.02 2 332 . 40 LYS CA C 54.818 0.24 1 333 . 40 LYS CB C 37.401 0.27 1 334 . 40 LYS CG C 26.117 0.28 1 335 . 40 LYS CD C 29.726 0.28 1 336 . 40 LYS CE C 42.062 0.28 1 337 . 41 ALA N N 121.445 0.07 1 338 . 41 ALA H H 8.387 0.01 1 339 . 41 ALA HA H 4.680 0.02 1 340 . 41 ALA HB H 1.093 0.02 1 341 . 41 ALA CA C 50.916 0.24 1 342 . 41 ALA CB C 25.927 0.27 1 343 . 42 ARG N N 117.444 0.07 1 344 . 42 ARG H H 8.417 0.01 1 345 . 42 ARG HA H 5.266 0.02 1 346 . 42 ARG HG2 H 1.489 0.02 2 347 . 42 ARG HG3 H 1.551 0.02 2 348 . 42 ARG CA C 53.863 0.24 1 349 . 42 ARG CB C 34.251 0.27 1 350 . 42 ARG CG C 26.569 0.28 1 351 . 42 ARG CD C 44.064 0.28 1 352 . 43 GLY N N 110.471 0.07 1 353 . 43 GLY H H 9.099 0.01 1 354 . 43 GLY HA2 H 4.070 0.02 2 355 . 43 GLY HA3 H 3.977 0.02 2 356 . 43 GLY CA C 46.502 0.24 1 357 . 44 ARG N N 125.147 0.07 1 358 . 44 ARG H H 8.977 0.01 1 359 . 44 ARG HA H 4.140 0.02 1 360 . 44 ARG HG2 H 1.794 0.02 2 361 . 44 ARG HG3 H 1.863 0.02 2 362 . 44 ARG CA C 58.683 0.24 1 363 . 44 ARG CB C 29.982 0.27 1 364 . 44 ARG CG C 27.598 0.28 1 365 . 44 ARG CD C 43.579 0.28 1 366 . 45 ALA N N 120.412 0.07 1 367 . 45 ALA H H 7.734 0.01 1 368 . 45 ALA HA H 4.271 0.02 1 369 . 45 ALA HB H 1.548 0.02 1 370 . 45 ALA CA C 53.304 0.24 1 371 . 45 ALA CB C 18.420 0.27 1 372 . 46 ILE N N 121.505 0.07 1 373 . 46 ILE H H 8.008 0.01 1 374 . 46 ILE HA H 3.285 0.02 1 375 . 46 ILE HB H 1.637 0.02 1 376 . 46 ILE HG12 H 1.620 0.02 2 377 . 46 ILE HG13 H 0.679 0.02 2 378 . 46 ILE HG2 H 0.680 0.02 1 379 . 46 ILE HD1 H 0.681 0.02 1 380 . 46 ILE CA C 66.565 0.24 1 381 . 46 ILE CB C 38.004 0.27 1 382 . 46 ILE CG1 C 30.229 0.28 1 383 . 46 ILE CG2 C 16.583 0.28 1 384 . 46 ILE CD1 C 13.955 0.28 1 385 . 47 SER N N 113.346 0.07 1 386 . 47 SER H H 7.480 0.01 1 387 . 47 SER HA H 3.780 0.02 1 388 . 47 SER CA C 62.558 0.24 1 389 . 47 SER CB C 62.568 0.27 1 390 . 48 LYS N N 122.979 0.07 1 391 . 48 LYS H H 6.741 0.01 1 392 . 48 LYS HA H 4.280 0.02 1 393 . 48 LYS HB2 H 1.825 0.02 2 394 . 48 LYS HB3 H 2.049 0.02 2 395 . 48 LYS HG2 H 1.770 0.02 2 396 . 48 LYS HG3 H 1.467 0.02 2 397 . 48 LYS HE2 H 3.114 0.02 2 398 . 48 LYS HE3 H 3.005 0.02 2 399 . 48 LYS CA C 58.626 0.24 1 400 . 48 LYS CB C 32.561 0.27 1 401 . 48 LYS CG C 25.085 0.28 1 402 . 48 LYS CD C 29.922 0.28 1 403 . 48 LYS CE C 41.823 0.28 1 404 . 49 ALA N N 125.060 0.07 1 405 . 49 ALA H H 8.042 0.01 1 406 . 49 ALA HA H 3.815 0.02 1 407 . 49 ALA HB H 1.299 0.02 1 408 . 49 ALA CA C 55.428 0.24 1 409 . 49 ALA CB C 18.409 0.27 1 410 . 50 VAL N N 117.652 0.07 1 411 . 50 VAL H H 7.286 0.01 1 412 . 50 VAL HA H 3.390 0.02 1 413 . 50 VAL HB H 2.134 0.02 1 414 . 50 VAL HG1 H 0.940 0.02 2 415 . 50 VAL HG2 H 1.082 0.02 2 416 . 50 VAL CA C 67.474 0.24 1 417 . 50 VAL CB C 30.789 0.27 1 418 . 50 VAL CG1 C 22.938 0.28 1 419 . 50 VAL CG2 C 22.800 0.28 1 420 . 51 ASP N N 119.145 0.07 1 421 . 51 ASP H H 8.255 0.01 1 422 . 51 ASP HA H 4.143 0.02 1 423 . 51 ASP HB2 H 2.885 0.02 2 424 . 51 ASP HB3 H 2.570 0.02 2 425 . 51 ASP CA C 58.149 0.24 1 426 . 51 ASP CB C 41.294 0.27 1 427 . 52 THR N N 115.120 0.07 1 428 . 52 THR H H 7.948 0.01 1 429 . 52 THR HA H 3.591 0.02 1 430 . 52 THR HB H 4.410 0.02 1 431 . 52 THR HG2 H 0.957 0.02 1 432 . 52 THR CA C 67.924 0.24 1 433 . 52 THR CB C 68.630 0.27 1 434 . 52 THR CG2 C 19.859 0.28 1 435 . 53 VAL N N 119.714 0.07 1 436 . 53 VAL H H 7.453 0.01 1 437 . 53 VAL HA H 3.350 0.02 1 438 . 53 VAL HB H 2.255 0.02 1 439 . 53 VAL HG1 H 1.060 0.02 2 440 . 53 VAL HG2 H 0.960 0.02 2 441 . 53 VAL CA C 67.186 0.24 1 442 . 53 VAL CB C 31.738 0.27 1 443 . 53 VAL CG1 C 24.301 0.28 1 444 . 53 VAL CG2 C 21.220 0.28 1 445 . 54 GLU N N 119.795 0.07 1 446 . 54 GLU H H 8.492 0.01 1 447 . 54 GLU HA H 3.938 0.02 1 448 . 54 GLU HG2 H 2.316 0.02 2 449 . 54 GLU HG3 H 2.133 0.02 2 450 . 54 GLU CA C 58.847 0.24 1 451 . 54 GLU CB C 30.730 0.27 1 452 . 54 GLU CG C 37.218 0.28 1 453 . 55 ILE N N 122.589 0.07 1 454 . 55 ILE H H 8.689 0.01 1 455 . 55 ILE HA H 3.750 0.02 1 456 . 55 ILE HB H 1.856 0.02 1 457 . 55 ILE HG12 H 0.935 0.02 2 458 . 55 ILE HG13 H 1.880 0.02 2 459 . 55 ILE HG2 H 1.055 0.02 1 460 . 55 ILE HD1 H 0.816 0.02 1 461 . 55 ILE CA C 66.105 0.24 1 462 . 55 ILE CB C 37.922 0.27 1 463 . 55 ILE CG1 C 29.700 0.28 1 464 . 55 ILE CG2 C 19.117 0.28 1 465 . 55 ILE CD1 C 14.149 0.28 1 466 . 56 VAL N N 120.459 0.07 1 467 . 56 VAL H H 8.202 0.01 1 468 . 56 VAL HA H 3.570 0.02 1 469 . 56 VAL HB H 2.280 0.02 1 470 . 56 VAL HG1 H 0.815 0.02 2 471 . 56 VAL HG2 H 1.116 0.02 2 472 . 56 VAL CA C 68.203 0.24 1 473 . 56 VAL CB C 31.727 0.27 1 474 . 56 VAL CG1 C 21.700 0.28 1 475 . 56 VAL CG2 C 25.102 0.28 1 476 . 57 ARG N N 116.849 0.07 1 477 . 57 ARG H H 8.587 0.01 1 478 . 57 ARG HA H 3.938 0.02 1 479 . 57 ARG HB2 H 1.771 0.02 2 480 . 57 ARG HB3 H 1.928 0.02 2 481 . 57 ARG HD2 H 3.151 0.02 2 482 . 57 ARG HD3 H 2.993 0.02 2 483 . 57 ARG CA C 59.536 0.24 1 484 . 57 ARG CB C 31.269 0.27 1 485 . 57 ARG CG C 27.101 0.28 1 486 . 57 ARG CD C 44.394 0.28 1 487 . 58 ASN N N 114.384 0.07 1 488 . 58 ASN ND2 N 113.890 0.07 1 489 . 58 ASN H H 7.763 0.01 1 490 . 58 ASN HA H 4.740 0.02 1 491 . 58 ASN HB2 H 2.683 0.02 2 492 . 58 ASN HB3 H 2.788 0.02 2 493 . 58 ASN HD21 H 7.690 0.02 1 494 . 58 ASN HD22 H 6.640 0.02 1 495 . 58 ASN CA C 55.275 0.24 1 496 . 58 ASN CB C 40.041 0.27 1 497 . 59 ARG N N 117.843 0.07 1 498 . 59 ARG H H 8.049 0.01 1 499 . 59 ARG HA H 4.311 0.02 1 500 . 59 ARG HB2 H 1.664 0.02 2 501 . 59 ARG HB3 H 1.790 0.02 2 502 . 59 ARG HG2 H 1.408 0.02 2 503 . 59 ARG HG3 H 1.310 0.02 2 504 . 59 ARG HD2 H 2.968 0.02 2 505 . 59 ARG HD3 H 3.029 0.02 2 506 . 59 ARG CA C 56.485 0.24 1 507 . 59 ARG CB C 30.747 0.27 1 508 . 59 ARG CG C 26.621 0.28 1 509 . 59 ARG CD C 42.911 0.28 1 510 . 60 PHE N N 117.100 0.07 1 511 . 60 PHE H H 7.265 0.01 1 512 . 60 PHE HA H 4.669 0.02 1 513 . 60 PHE HB2 H 2.910 0.02 2 514 . 60 PHE HB3 H 3.211 0.02 2 515 . 60 PHE HZ H 7.200 0.02 1 516 . 60 PHE HD1 H 7.320 0.02 3 517 . 60 PHE HE1 H 7.190 0.02 3 518 . 60 PHE CA C 59.065 0.24 1 519 . 60 PHE CB C 42.035 0.27 1 520 . 60 PHE CZ C 129.400 0.28 1 521 . 61 LEU N N 121.640 0.07 1 522 . 61 LEU H H 8.078 0.01 1 523 . 61 LEU HA H 4.490 0.02 1 524 . 61 LEU HB2 H 1.550 0.02 2 525 . 61 LEU HB3 H 1.660 0.02 2 526 . 61 LEU HD1 H 0.871 0.02 2 527 . 61 LEU HD2 H 0.921 0.02 2 528 . 61 LEU CA C 54.620 0.24 1 529 . 61 LEU CB C 42.858 0.27 1 530 . 61 LEU CD1 C 26.390 0.28 1 531 . 61 LEU CD2 C 23.245 0.28 1 532 . 62 ALA N N 124.346 0.07 1 533 . 62 ALA H H 7.955 0.01 1 534 . 62 ALA HA H 4.231 0.02 1 535 . 62 ALA HB H 1.369 0.02 1 536 . 62 ALA CA C 54.464 0.24 1 537 . 62 ALA CB C 18.412 0.27 1 538 . 63 ASP N N 116.007 0.07 1 539 . 63 ASP H H 8.422 0.01 1 540 . 63 ASP HA H 4.530 0.02 1 541 . 63 ASP HB2 H 2.800 0.02 2 542 . 63 ASP HB3 H 2.850 0.02 2 543 . 63 ASP CA C 55.410 0.24 1 544 . 63 ASP CB C 40.790 0.27 1 545 . 64 LYS N N 117.400 0.07 1 546 . 64 LYS H H 8.024 0.01 1 547 . 64 LYS HA H 4.500 0.02 1 548 . 64 LYS HB2 H 1.770 0.02 2 549 . 64 LYS HB3 H 2.060 0.02 2 550 . 64 LYS HG2 H 1.520 0.02 2 551 . 64 LYS HG3 H 1.420 0.02 2 552 . 64 LYS CA C 56.296 0.24 1 553 . 64 LYS CB C 33.799 0.27 1 554 . 64 LYS CG C 24.963 0.28 1 555 . 64 LYS CD C 28.711 0.28 1 556 . 64 LYS CE C 42.338 0.28 1 557 . 65 ILE N N 116.953 0.07 1 558 . 65 ILE H H 7.716 0.01 1 559 . 65 ILE HA H 5.010 0.02 1 560 . 65 ILE HB H 1.863 0.02 1 561 . 65 ILE HG12 H 1.205 0.02 2 562 . 65 ILE HG13 H 1.276 0.02 2 563 . 65 ILE HG2 H 0.727 0.02 1 564 . 65 ILE HD1 H 0.491 0.02 1 565 . 65 ILE CA C 57.748 0.24 1 566 . 65 ILE CB C 40.148 0.27 1 567 . 65 ILE CG1 C 27.042 0.28 1 568 . 65 ILE CG2 C 18.399 0.28 1 569 . 65 ILE CD1 C 11.903 0.28 1 570 . 66 GLU N N 124.666 0.07 1 571 . 66 GLU H H 9.044 0.01 1 572 . 66 GLU HA H 4.676 0.02 1 573 . 66 GLU HB2 H 1.870 0.02 2 574 . 66 GLU HB3 H 1.910 0.02 2 575 . 66 GLU HG2 H 2.030 0.02 2 576 . 66 GLU HG3 H 2.080 0.02 2 577 . 66 GLU CA C 53.998 0.24 1 578 . 66 GLU CB C 33.516 0.27 1 579 . 66 GLU CG C 35.788 0.28 1 580 . 67 ILE N N 124.691 0.07 1 581 . 67 ILE H H 8.835 0.01 1 582 . 67 ILE HA H 4.220 0.02 1 583 . 67 ILE HB H 1.948 0.02 1 584 . 67 ILE HG12 H 0.925 0.02 2 585 . 67 ILE HG13 H 1.518 0.02 2 586 . 67 ILE HG2 H 0.799 0.02 1 587 . 67 ILE HD1 H 0.763 0.02 1 588 . 67 ILE CA C 61.585 0.24 1 589 . 67 ILE CB C 36.892 0.27 1 590 . 67 ILE CG1 C 27.989 0.28 1 591 . 67 ILE CG2 C 17.898 0.28 1 592 . 67 ILE CD1 C 12.998 0.28 1 593 . 68 LYS N N 131.496 0.07 1 594 . 68 LYS H H 8.977 0.01 1 595 . 68 LYS HA H 4.204 0.02 1 596 . 68 LYS HB2 H 1.490 0.02 2 597 . 68 LYS HB3 H 1.580 0.02 2 598 . 68 LYS HG2 H 1.287 0.02 2 599 . 68 LYS HG3 H 1.430 0.02 2 600 . 68 LYS HD2 H 1.590 0.02 2 601 . 68 LYS HD3 H 1.461 0.02 2 602 . 68 LYS CA C 57.612 0.24 1 603 . 68 LYS CB C 34.133 0.27 1 604 . 68 LYS CG C 24.591 0.28 1 605 . 68 LYS CD C 29.352 0.28 1 606 . 68 LYS CE C 41.809 0.28 1 607 . 69 GLU N N 115.225 0.07 1 608 . 69 GLU H H 7.508 0.01 1 609 . 69 GLU HA H 4.546 0.02 1 610 . 69 GLU HG2 H 2.194 0.02 2 611 . 69 GLU HG3 H 2.087 0.02 2 612 . 69 GLU CA C 56.260 0.24 1 613 . 69 GLU CB C 33.151 0.27 1 614 . 69 GLU CG C 36.317 0.28 1 615 . 70 ILE N N 123.719 0.07 1 616 . 70 ILE H H 8.387 0.01 1 617 . 70 ILE HA H 4.858 0.02 1 618 . 70 ILE HB H 1.649 0.02 1 619 . 70 ILE HG12 H 0.910 0.02 2 620 . 70 ILE HG2 H 0.783 0.02 1 621 . 70 ILE HD1 H 0.875 0.02 1 622 . 70 ILE CA C 61.152 0.24 1 623 . 70 ILE CB C 40.483 0.27 1 624 . 70 ILE CG1 C 28.177 0.28 1 625 . 70 ILE CG2 C 17.864 0.28 1 626 . 70 ILE CD1 C 14.796 0.28 1 627 . 71 ARG N N 125.935 0.07 1 628 . 71 ARG H H 9.021 0.01 1 629 . 71 ARG HA H 4.863 0.02 1 630 . 71 ARG HB2 H 1.645 0.02 2 631 . 71 ARG HB3 H 1.773 0.02 2 632 . 71 ARG HG2 H 1.542 0.02 2 633 . 71 ARG HG3 H 1.490 0.02 2 634 . 71 ARG HD2 H 3.083 0.02 2 635 . 71 ARG HD3 H 3.211 0.02 2 636 . 71 ARG CA C 54.554 0.24 1 637 . 71 ARG CB C 33.764 0.27 1 638 . 71 ARG CG C 26.918 0.28 1 639 . 71 ARG CD C 43.551 0.28 1 640 . 72 VAL N N 119.722 0.07 1 641 . 72 VAL H H 8.736 0.01 1 642 . 72 VAL HA H 5.115 0.02 1 643 . 72 VAL HB H 2.229 0.02 1 644 . 72 VAL HG1 H 0.860 0.02 2 645 . 72 VAL HG2 H 0.904 0.02 2 646 . 72 VAL CA C 59.033 0.24 1 647 . 72 VAL CB C 34.388 0.27 1 648 . 72 VAL CG1 C 18.942 0.28 1 649 . 72 VAL CG2 C 22.470 0.28 1 650 . 73 GLY N N 111.220 0.07 1 651 . 73 GLY H H 7.862 0.01 1 652 . 73 GLY HA2 H 3.563 0.02 2 653 . 73 GLY HA3 H 4.218 0.02 2 654 . 73 GLY CA C 45.641 0.24 1 655 . 74 SER N N 113.020 0.07 1 656 . 74 SER H H 7.885 0.01 1 657 . 74 SER HA H 5.492 0.02 1 658 . 74 SER HB2 H 3.756 0.02 2 659 . 74 SER HB3 H 3.598 0.02 2 660 . 74 SER CA C 58.632 0.24 1 661 . 74 SER CB C 67.560 0.27 1 662 . 75 GLN N N 122.085 0.07 1 663 . 75 GLN H H 9.164 0.01 1 664 . 75 GLN HA H 4.602 0.02 1 665 . 75 GLN HB2 H 1.757 0.02 2 666 . 75 GLN HB3 H 1.913 0.02 2 667 . 75 GLN HG3 H 2.207 0.02 2 668 . 75 GLN CA C 54.253 0.24 1 669 . 75 GLN CB C 32.550 0.27 1 670 . 75 GLN CG C 33.853 0.28 1 671 . 76 VAL N N 124.445 0.07 1 672 . 76 VAL H H 8.532 0.01 1 673 . 76 VAL HA H 4.616 0.02 1 674 . 76 VAL HB H 1.903 0.02 1 675 . 76 VAL HG1 H 0.807 0.02 2 676 . 76 VAL HG2 H 0.881 0.02 2 677 . 76 VAL CA C 62.432 0.24 1 678 . 76 VAL CB C 32.477 0.27 1 679 . 76 VAL CG1 C 21.425 0.28 1 680 . 77 VAL N N 126.977 0.07 1 681 . 77 VAL H H 8.831 0.01 1 682 . 77 VAL HA H 4.454 0.02 1 683 . 77 VAL HB H 2.026 0.02 1 684 . 77 VAL HG1 H 0.790 0.02 2 685 . 77 VAL HG2 H 0.823 0.02 2 686 . 77 VAL CA C 60.447 0.24 1 687 . 77 VAL CB C 34.731 0.27 1 688 . 77 VAL CG1 C 20.031 0.28 1 689 . 77 VAL CG2 C 21.300 0.28 1 690 . 78 THR N N 121.533 0.07 1 691 . 78 THR H H 8.491 0.01 1 692 . 78 THR HA H 4.900 0.02 1 693 . 78 THR HB H 3.974 0.02 1 694 . 78 THR HG2 H 1.223 0.02 1 695 . 78 THR CA C 61.801 0.24 1 696 . 78 THR CB C 69.900 0.27 1 697 . 78 THR CG2 C 21.512 0.28 1 698 . 79 SER N N 122.818 0.07 1 699 . 79 SER H H 8.858 0.01 1 700 . 79 SER HA H 4.617 0.02 1 701 . 79 SER HB2 H 4.216 0.02 2 702 . 79 SER HB3 H 3.973 0.02 2 703 . 79 SER CA C 57.722 0.24 1 704 . 79 SER CB C 64.640 0.27 1 705 . 80 GLN N N 122.471 0.07 1 706 . 80 GLN H H 8.896 0.01 1 707 . 80 GLN HA H 4.110 0.02 1 708 . 80 GLN HE21 H 7.510 0.02 1 709 . 80 GLN HE22 H 6.810 0.02 1 710 . 80 GLN CA C 58.854 0.24 1 711 . 80 GLN CB C 28.500 0.27 1 712 . 80 GLN CG C 34.000 0.28 1 713 . 81 ASP N N 116.203 0.07 1 714 . 81 ASP H H 8.054 0.01 1 715 . 81 ASP HA H 4.549 0.02 1 716 . 81 ASP HB2 H 2.643 0.02 2 717 . 81 ASP HB3 H 2.969 0.02 2 718 . 81 ASP CA C 53.441 0.24 1 719 . 81 ASP CB C 39.990 0.27 1 720 . 82 GLY N N 108.508 0.07 1 721 . 82 GLY H H 8.002 0.01 1 722 . 82 GLY HA2 H 3.560 0.02 2 723 . 82 GLY HA3 H 4.210 0.02 2 724 . 82 GLY CA C 45.623 0.24 1 725 . 83 ARG N N 121.193 0.07 1 726 . 83 ARG H H 7.700 0.01 1 727 . 83 ARG HA H 4.350 0.02 1 728 . 83 ARG HB2 H 1.800 0.02 2 729 . 83 ARG HB3 H 1.840 0.02 2 730 . 83 ARG HD3 H 3.198 0.02 2 731 . 83 ARG CA C 56.275 0.24 1 732 . 83 ARG CB C 30.951 0.27 1 733 . 83 ARG CG C 27.144 0.28 1 734 . 83 ARG CD C 43.397 0.28 1 735 . 84 GLN N N 122.637 0.07 1 736 . 84 GLN H H 8.555 0.01 1 737 . 84 GLN HA H 5.145 0.02 1 738 . 84 GLN HB2 H 1.843 0.02 2 739 . 84 GLN HB3 H 1.976 0.02 2 740 . 84 GLN HG2 H 2.363 0.02 2 741 . 84 GLN HG3 H 2.278 0.02 2 742 . 84 GLN HE21 H 7.350 0.02 1 743 . 84 GLN HE22 H 6.690 0.02 1 744 . 84 GLN CA C 55.304 0.24 1 745 . 84 GLN CB C 30.731 0.27 1 746 . 84 GLN CG C 34.392 0.28 1 747 . 85 SER N N 118.444 0.07 1 748 . 85 SER H H 8.796 0.01 1 749 . 85 SER HA H 4.701 0.02 1 750 . 85 SER HB2 H 3.757 0.02 2 751 . 85 SER HB3 H 3.709 0.02 2 752 . 85 SER CA C 57.332 0.24 1 753 . 85 SER CB C 65.500 0.27 1 754 . 86 ARG N N 123.836 0.07 1 755 . 86 ARG H H 8.466 0.01 1 756 . 86 ARG HA H 5.025 0.02 1 757 . 86 ARG HG2 H 1.447 0.02 2 758 . 86 ARG HG3 H 1.540 0.02 2 759 . 86 ARG HD2 H 3.175 0.02 2 760 . 86 ARG HD3 H 3.040 0.02 2 761 . 86 ARG CA C 55.593 0.24 1 762 . 86 ARG CB C 31.492 0.27 1 763 . 86 ARG CG C 26.621 0.28 1 764 . 86 ARG CD C 42.332 0.28 1 765 . 87 VAL N N 125.618 0.07 1 766 . 87 VAL H H 9.030 0.01 1 767 . 87 VAL HA H 4.588 0.02 1 768 . 87 VAL HB H 1.977 0.02 1 769 . 87 VAL HG2 H 0.970 0.02 2 770 . 87 VAL CA C 60.235 0.24 1 771 . 87 VAL CB C 35.398 0.27 1 772 . 87 VAL CG1 C 21.131 0.28 1 773 . 88 SER N N 123.730 0.07 1 774 . 88 SER H H 9.169 0.01 1 775 . 88 SER HA H 5.200 0.02 1 776 . 88 SER HB2 H 3.730 0.02 2 777 . 88 SER HB3 H 3.848 0.02 2 778 . 88 SER CA C 59.282 0.24 1 779 . 88 SER CB C 64.500 0.27 1 780 . 89 THR N N 114.955 0.07 1 781 . 89 THR H H 8.929 0.01 1 782 . 89 THR HA H 5.026 0.02 1 783 . 89 THR HB H 4.205 0.02 1 784 . 89 THR HG2 H 0.961 0.02 1 785 . 89 THR CA C 60.284 0.24 1 786 . 89 THR CB C 71.600 0.27 1 787 . 89 THR CG2 C 21.202 0.28 1 788 . 90 ILE N N 117.978 0.07 1 789 . 90 ILE H H 8.536 0.01 1 790 . 90 ILE HA H 5.200 0.02 1 791 . 90 ILE HB H 1.432 0.02 1 792 . 90 ILE HG12 H 0.983 0.02 2 793 . 90 ILE HG13 H 1.684 0.02 2 794 . 90 ILE HG2 H 0.767 0.02 1 795 . 90 ILE HD1 H 0.546 0.02 1 796 . 90 ILE CA C 60.154 0.24 1 797 . 90 ILE CB C 43.382 0.27 1 798 . 90 ILE CG1 C 30.485 0.28 1 799 . 90 ILE CG2 C 18.070 0.28 1 800 . 90 ILE CD1 C 13.713 0.28 1 801 . 91 GLU N N 125.565 0.07 1 802 . 91 GLU H H 8.430 0.01 1 803 . 91 GLU HA H 5.130 0.02 1 804 . 91 GLU HG2 H 2.210 0.02 2 805 . 91 GLU HG3 H 1.990 0.02 2 806 . 91 GLU CA C 55.158 0.24 1 807 . 91 GLU CB C 33.040 0.27 1 808 . 91 GLU CG C 36.616 0.28 1 809 . 92 ILE N N 124.426 0.07 1 810 . 92 ILE H H 9.378 0.01 1 811 . 92 ILE HA H 4.715 0.02 1 812 . 92 ILE HB H 1.771 0.02 1 813 . 92 ILE HG2 H 0.899 0.02 1 814 . 92 ILE HD1 H 0.743 0.02 1 815 . 92 ILE CA C 60.745 0.24 1 816 . 92 ILE CB C 40.791 0.27 1 817 . 92 ILE CG1 C 27.874 0.28 1 818 . 92 ILE CG2 C 18.594 0.28 1 819 . 92 ILE CD1 C 14.554 0.28 1 820 . 93 ALA N N 131.485 0.07 1 821 . 93 ALA H H 9.008 0.01 1 822 . 93 ALA HA H 5.466 0.02 1 823 . 93 ALA HB H 1.421 0.02 1 824 . 93 ALA CA C 50.680 0.24 1 825 . 93 ALA CB C 20.624 0.27 1 826 . 94 ILE N N 119.886 0.07 1 827 . 94 ILE H H 9.148 0.01 1 828 . 94 ILE HA H 5.205 0.02 1 829 . 94 ILE HB H 1.746 0.02 1 830 . 94 ILE HG12 H 1.056 0.02 2 831 . 94 ILE HG13 H 1.504 0.02 2 832 . 94 ILE HG2 H 0.825 0.02 1 833 . 94 ILE HD1 H 0.731 0.02 1 834 . 94 ILE CA C 59.073 0.24 1 835 . 94 ILE CB C 41.285 0.27 1 836 . 94 ILE CG1 C 26.374 0.28 1 837 . 94 ILE CG2 C 18.847 0.28 1 838 . 94 ILE CD1 C 13.642 0.28 1 839 . 95 ARG N N 121.020 0.07 1 840 . 95 ARG H H 8.910 0.01 1 841 . 95 ARG HA H 5.453 0.02 1 842 . 95 ARG HD2 H 3.116 0.02 2 843 . 95 ARG HD3 H 3.188 0.02 2 844 . 95 ARG CA C 53.770 0.24 1 845 . 95 ARG CB C 35.328 0.27 1 846 . 95 ARG CG C 26.625 0.28 1 847 . 95 ARG CD C 43.928 0.28 1 848 . 96 LYS N N 124.776 0.07 1 849 . 96 LYS H H 8.569 0.01 1 850 . 96 LYS HA H 4.740 0.02 1 851 . 96 LYS HB2 H 1.637 0.02 2 852 . 96 LYS HB3 H 1.928 0.02 2 853 . 96 LYS HG2 H 1.430 0.02 2 854 . 96 LYS HG3 H 1.504 0.02 2 855 . 96 LYS HD2 H 1.733 0.02 2 856 . 96 LYS HD3 H 1.640 0.02 2 857 . 96 LYS CA C 56.276 0.24 1 858 . 96 LYS CB C 34.046 0.27 1 859 . 96 LYS CG C 25.294 0.28 1 860 . 96 LYS CD C 29.714 0.28 1 861 . 96 LYS CE C 42.142 0.28 1 862 . 97 LYS N N 131.756 0.07 1 863 . 97 LYS H H 8.189 0.01 1 864 . 97 LYS HA H 4.073 0.02 1 865 . 97 LYS HB2 H 1.550 0.02 2 866 . 97 LYS HB3 H 1.782 0.02 2 867 . 97 LYS HG2 H 1.286 0.02 2 868 . 97 LYS HD2 H 1.600 0.02 2 869 . 97 LYS HE2 H 2.907 0.02 2 870 . 97 LYS CA C 58.161 0.24 1 871 . 97 LYS CB C 33.816 0.27 1 872 . 97 LYS CG C 25.264 0.28 1 873 . 97 LYS CD C 29.146 0.28 1 874 . 97 LYS CE C 41.748 0.28 1 stop_ save_