data_6540 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific 1H, 13C and 15N resonance assignments of the winged-helix domain of the human Werner syndrome protein ; _BMRB_accession_number 6540 _BMRB_flat_file_name bmr6540.str _Entry_type original _Submission_date 2005-03-07 _Accession_date 2005-03-08 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sun Jian-Zhong . . 2 Feng Han-Qiao . . 3 Lin Guang-Xin . . 4 Zeng Wang-Yong . . 5 Hu Jin-Shan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 658 "13C chemical shifts" 604 "15N chemical shifts" 149 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-08-29 original author . stop_ _Original_release_date 2005-08-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR Assignments of the Winged-Helix Domain of Human Werner Syndrome Protein' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sun Jian-Zhong . . 2 Feng Han-Qiao . . 3 Lin Guang-Xin . . 4 Zeng Wangyong . . 5 Hu Jin-Shan . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 32 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 261 _Page_last 261 _Year 2005 _Details . loop_ _Keyword 'NMR assignments' 'Werner syndrome protein' WRN 'nucleolar targeting sequence' 'RQC domain' winged-helix 'WH domain' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_references_1 _Saveframe_category citation _Citation_full ; Yu CE, Oshima J, Fu YH, Wijsman EM, Hisama F, Alisch R, Matthews S, Nakura J, Miki T, Ouais S, Martin GM, Mulligan J, Schellenberg GD. Positional cloning of the Werner's syndrome gene. Science. 1996 Apr 12;272(5259):258-62. ; _Citation_title 'Positional cloning of the Werner's syndrome gene.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8602509 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yu 'C. E.' E. . 2 Oshima J. . . 3 Fu 'Y. H.' H. . 4 Wijsman 'E. M.' M. . 5 Hisama F. . . 6 Alisch R. . . 7 Matthews S. . . 8 Nakura J. . . 9 Miki T. . . 10 Ouais S. . . 11 Martin 'G. M.' M. . 12 Mulligan J. . . 13 Schellenberg 'G. D.' D. . stop_ _Journal_abbreviation Science _Journal_name_full 'Science (New York, N.Y.)' _Journal_volume 272 _Journal_issue 5259 _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 258 _Page_last 262 _Year 1996 _Details ; Werner's syndrome (WS) is an inherited disease with clinical symptoms resembling premature aging. Early susceptibility to a number of major age-related diseases is a key feature of this disorder. The gene responsible for WS (known as WRN) was identified by positional cloning. The predicted protein is 1432 amino acids in length and shows significant similarity to DNA helicases. Four mutations in WS patients were identified. Two of the mutations are splice-junction mutations, with the predicted result being the exclusion of exons from the final messenger RNA. One of the these mutations, which results in a frameshift and a predicted truncated protein, was found in the homozygous state in 60 percent of Japanese WS patients examined. The other two mutations are nonsense mutations. The identification of a mutated putative helicase as the gene product of the WS gene suggests that defective DNA metabolism is involved in the complex process of aging in WS patients. ; save_ save_references_2 _Saveframe_category citation _Citation_full ; Bachrati CZ, Hickson ID. RecQ helicases: suppressors of tumorigenesis and premature aging. Biochem J. 2003 Sep 15;374(Pt 3):577-606. ; _Citation_title 'RecQ helicases: suppressors of tumorigenesis and premature aging.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12803543 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bachrati 'Csanad Z.' Z. . 2 Hickson 'Ian D.' D. . stop_ _Journal_abbreviation 'Biochem. J.' _Journal_name_full 'The Biochemical journal' _Journal_volume 374 _Journal_issue 'Pt 3' _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 577 _Page_last 606 _Year 2003 _Details ; The RecQ helicases represent a subfamily of DNA helicases that are highly conserved in evolution. Loss of RecQ helicase function leads to a breakdown in the maintenance of genome integrity, in particular hyper-recombination. Germ-line defects in three of the five known human RecQ helicases give rise to defined genetic disorders associated with cancer predisposition and/or premature aging. These are Bloom's syndrome, Werner's syndrome and Rothmund-Thomson syndrome, which are caused by defects in the genes BLM, WRN and RECQ4 respectively. Here we review the properties of RecQ helicases in organisms from bacteria to humans, with an emphasis on the biochemical functions of these enzymes and the range of protein partners that they operate with. We will discuss models in which RecQ helicases are required to protect against replication fork demise, either through prevention of fork breakdown or restoration of productive DNA synthesis. ; save_ save_references_3 _Saveframe_category citation _Citation_full ; Morozov V, Mushegian AR, Koonin EV, Bork P. A putative nucleic acid-binding domain in Bloom's and Werner's syndrome helicases. Trends Biochem Sci. 1997 Nov;22(11):417-8. ; _Citation_title 'A putative nucleic acid-binding domain in Bloom's and Werner's syndrome helicases.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9397680 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Morozov V. . . 2 Mushegian 'A. R.' R. . 3 Koonin 'E. V.' V. . 4 Bork P. . . stop_ _Journal_abbreviation 'Trends Biochem. Sci.' _Journal_name_full 'Trends in biochemical sciences' _Journal_volume 22 _Journal_issue 11 _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 417 _Page_last 418 _Year 1997 _Details . save_ save_references_4 _Saveframe_category citation _Citation_full ; Bennett RJ, Keck JL. Structure and function of RecQ DNA helicases. Crit Rev Biochem Mol Biol. 2004 Mar-Apr;39(2):79-97. ; _Citation_title 'Structure and function of RecQ DNA helicases.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15217989 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bennett 'Richard J.' J. . 2 Keck 'James L.' L. . stop_ _Journal_abbreviation 'Crit. Rev. Biochem. Mol. Biol.' _Journal_name_full 'Critical reviews in biochemistry and molecular biology' _Journal_volume 39 _Journal_issue 2 _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 79 _Page_last 97 _Year . _Details ; RecQ family helicases play important roles in coordinating genome maintenance pathways in living cells. In the absence of functional RecQ proteins, cells exhibit a variety of phenotypes, including increased mitotic recombination, elevated chromosome missegregation, hypersensitivity to DNA-damaging agents, and defects in meiosis. Mutations in three of the five human RecQ family members give rise to genetic disorders associated with a predisposition to cancer and premature aging, highlighting the importance of RecQ proteins and their cellular activities for human health. Current evidence suggests that RecQ proteins act at multiple steps in DNA replication, including stabilization of replication forks and removal of DNA recombination intermediates, in order to maintain genome integrity. The cellular basis of RecQ helicase function may be explained through interactions with multiple components of the DNA replication and recombination machinery. This review focuses on biochemical and structural aspects of the RecQ helicases and how these features relate to their known cellular function, specifically in preventing excessive recombination. ; save_ save_references_5 _Saveframe_category citation _Citation_full ; Lee JW, Harrigan J, Opresko PL, Bohr VA. Pathways and functions of the Werner syndrome protein. Mech Ageing Dev. 2005 Jan;126(1):79-86. ; _Citation_title 'Pathways and functions of the Werner syndrome protein.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15610765 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lee 'Jae Wan' W. . 2 Harrigan Jeanine . . 3 Opresko 'Patricia L.' L. . 4 Bohr 'Vilhelm A.' A. . stop_ _Journal_abbreviation 'Mech. Ageing Dev.' _Journal_name_full 'Mechanisms of ageing and development' _Journal_volume 126 _Journal_issue 1 _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 79 _Page_last 86 _Year 2005 _Details ; Mutations in human WRN (also known as RECQ3) gene give rise to a rare autosomal recessive genetic disorder, Werner syndrome (WS). WS is a premature aging disease characterized by predisposition to cancer and early onset of symptoms related to normal aging including osteoporosis, ocular cataracts, graying and loss of hair, diabetes mellitus, arteriosclerosis, and atherosclerosis. This review focuses on the functional role of Werner protein (WRN) in guarding the genetic stability of cells, particularly by playing an integral role in the base excision repair, and at the telomere ends. Furthermore, in-depth biochemical investigations have significantly advanced our understanding of WRN protein regarding its binding partners and the site of protein-protein interaction. The mapping analysis of protein interaction sites in WRN for most of its binding partners have revealed a common site of protein-protein interaction in the RecQ conserved (RQC) region of WRN. ; save_ save_references_6 _Saveframe_category citation _Citation_full ; Gray MD, Wang L, Youssoufian H, Martin GM, Oshima J. Werner helicase is localized to transcriptionally active nucleoli of cycling cells. Exp Cell Res. 1998 Aug 1;242(2):487-94. ; _Citation_title 'Werner helicase is localized to transcriptionally active nucleoli of cycling cells.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9683536 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gray 'M. D.' D. . 2 Wang L. . . 3 Youssoufian H. . . 4 Martin 'G. M.' M. . 5 Oshima J. . . stop_ _Journal_abbreviation 'Exp. Cell Res.' _Journal_name_full 'Experimental cell research' _Journal_volume 242 _Journal_issue 2 _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 487 _Page_last 494 _Year 1998 _Details ; Mutations at the Werner helicase locus (WRN) are responsible for the Werner syndrome (WS), a "caricature of aging." We have localized the Werner protein (WRNp) to the nucleoli of replicating mammalian cells, where its appearance is associated with transcriptional activity. A dramatic reduction of the nucleolar signal and of [3H]uridine incorporation occurred when cultures were made quiescent or were exposed to 4-nitroquinoline-1-oxide (4NQO), to which WS cells are particularly susceptible. Total cellular levels of WRNp, however, did not change, and virtually all WRNp was in the nuclear fractions, consistent with translocation to the nucleoplasm and/or masking of the epitopes. The 4NQO-induced altered state of WRNp was prevented by Na3VO4, but not by okadaic acid, suggesting that WRNp localization/function is partially regulated by kinases/phosphatases for Tyr substrates on WRNp or interacting proteins. The repression of rDNA transcription by 4NQO was not reversed by Na3VO4. We suggest that physiological states and genotoxic agents modulate the interaction of WRNp with rDNA, consistent with a role of WRNp in rDNA transcription. ; save_ ################################## # Molecular system description # ################################## save_system_WRN _Saveframe_category molecular_system _Mol_system_name 'Werner syndrome protein' _Abbreviation_common WRN _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'The winged-helix domain of WRN protein' $WH_domain_of_WRN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'WRN protein plays an important role in preventing premature human aging.' 'The WRN protein is involved in the DNA replication, repair, recombination and transcription.' ; The WH subdomain of RQC domain of WRN is involved in the interaction with many proteins and specific structured DNA. ; stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_WH_domain_of_WRN _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'The winged-helix domain of WRN' _Abbreviation_common 'WH domain of WRN' _Molecular_mass 16333.65 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 144 _Mol_residue_sequence ; MDDSEDTSWDFGPQAFKLLS AVDILGEKFGIGLPILFLRG SNSQRLADQYRRHSLFGTGK DQTESWWKAFSRQLITGGFL VEVSRYNKFMKICALTKKGR NWLHKANTESQSLILQANEE LCPKKLLLPSSKTVSSGTKE HCYN ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 ASP 4 SER 5 GLU 6 ASP 7 THR 8 SER 9 TRP 10 ASP 11 PHE 12 GLY 13 PRO 14 GLN 15 ALA 16 PHE 17 LYS 18 LEU 19 LEU 20 SER 21 ALA 22 VAL 23 ASP 24 ILE 25 LEU 26 GLY 27 GLU 28 LYS 29 PHE 30 GLY 31 ILE 32 GLY 33 LEU 34 PRO 35 ILE 36 LEU 37 PHE 38 LEU 39 ARG 40 GLY 41 SER 42 ASN 43 SER 44 GLN 45 ARG 46 LEU 47 ALA 48 ASP 49 GLN 50 TYR 51 ARG 52 ARG 53 HIS 54 SER 55 LEU 56 PHE 57 GLY 58 THR 59 GLY 60 LYS 61 ASP 62 GLN 63 THR 64 GLU 65 SER 66 TRP 67 TRP 68 LYS 69 ALA 70 PHE 71 SER 72 ARG 73 GLN 74 LEU 75 ILE 76 THR 77 GLY 78 GLY 79 PHE 80 LEU 81 VAL 82 GLU 83 VAL 84 SER 85 ARG 86 TYR 87 ASN 88 LYS 89 PHE 90 MET 91 LYS 92 ILE 93 CYS 94 ALA 95 LEU 96 THR 97 LYS 98 LYS 99 GLY 100 ARG 101 ASN 102 TRP 103 LEU 104 HIS 105 LYS 106 ALA 107 ASN 108 THR 109 GLU 110 SER 111 GLN 112 SER 113 LEU 114 ILE 115 LEU 116 GLN 117 ALA 118 ASN 119 GLU 120 GLU 121 LEU 122 CYS 123 PRO 124 LYS 125 LYS 126 LEU 127 LEU 128 LEU 129 PRO 130 SER 131 SER 132 LYS 133 THR 134 VAL 135 SER 136 SER 137 GLY 138 THR 139 LYS 140 GLU 141 HIS 142 CYS 143 TYR 144 ASN 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 PDB 2AXL "Solution Structure Of A Multifunctional Dna- And Protein- Binding Domain Of Human Werner Syndrome Protein" 100.00 144 99.31 99.31 2.68e-100 PDB 3AAF "Structure Of Wrn Rqc Domain Bound To Double-Stranded Dna" 90.97 134 98.47 98.47 1.19e-88 DBJ BAD92889 "Werner syndrome protein variant [Homo sapiens]" 100.00 842 99.31 99.31 2.00e-94 DBJ BAJ17933 "Werner syndrome, RecQ helicase-like [synthetic construct]" 100.00 1432 99.31 99.31 2.57e-92 GB AAC41981 "unnamed protein product [Homo sapiens]" 100.00 1432 98.61 98.61 1.14e-91 GB AAC63361 "WRN [Homo sapiens]" 100.00 1432 98.61 98.61 1.14e-91 GB AAF06162 "WRN [Homo sapiens]" 100.00 1432 98.61 98.61 1.14e-91 GB AAI72840 "Werner syndrome protein [synthetic construct]" 100.00 863 99.31 99.31 2.68e-94 GB AAR05448 "Werner syndrome [Homo sapiens]" 100.00 1432 99.31 99.31 2.67e-92 REF NP_000544 "Werner syndrome ATP-dependent helicase [Homo sapiens]" 100.00 1432 99.31 99.31 2.67e-92 SP Q14191 "RecName: Full=Werner syndrome ATP-dependent helicase; AltName: Full=DNA helicase, RecQ-like type 3; Short=RecQ3; AltName: Full=" 100.00 1432 99.31 99.31 2.67e-92 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $WH_domain_of_WRN 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 $WH_domain_of_WRN 'recombinant technology' 'E. coli' Escherichia coli BL21 . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $WH_domain_of_WRN 0.45 mM 0.29 0.47 '[U-95% 15N]' 'potassium phosphate buffer' 25 mM . . . NaCl 25 mM . . . EDTA 1 mM . . . NaZ3 0.05 % . . . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $WH_domain_of_WRN 0.45 mM 0.40 0.50 '[U-98% 15N]' 'potassium phosphate buffer' 25 mM . . . NaCl 25 mM . . . EDTA 1 mM . . . NaZ3 0.05 % . . . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $WH_domain_of_WRN 0.45 mM 0.40 0.50 '[U-95% 13C; U-95% 15N]' 'potassium phosphate buffer' 25 mM . . . NaCl 25 mM . . . EDTA 1 mM . . . NaZ3 0.05 % . . . stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $WH_domain_of_WRN 0.29 mM 0.20 0.30 . 'potassium phosphate buffer' 25 mM . . . NaCl 25 mM . . . EDTA 1 mM . . . NaZ3 0.05 % . . . stop_ save_ ############################ # Computer software used # ############################ save_NMRPIPE _Saveframe_category software _Name NMRPIPE _Version . loop_ _Task 'data processing' analysis stop_ _Details . save_ save_PIPP _Saveframe_category software _Name PIPP _Version . loop_ _Task 'data processing' analysis stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _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_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HNCOCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCOCO _Sample_label . save_ save_HNCG_arom_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCG_arom _Sample_label . save_ save_HN(CO)CG_arom_7 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CG_arom _Sample_label . save_ save_HNCG_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNCG _Sample_label . save_ save_HN(CO)C_9 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)C _Sample_label . save_ save_HNHA_10 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_HBHA(CO)NH_11 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label . save_ save_DIPSI-H(CCO)NH_12 _Saveframe_category NMR_applied_experiment _Experiment_name DIPSI-H(CCO)NH _Sample_label . save_ save_DIPSI-C(CCO)NH_13 _Saveframe_category NMR_applied_experiment _Experiment_name DIPSI-C(CCO)NH _Sample_label . save_ save_HAHB_14 _Saveframe_category NMR_applied_experiment _Experiment_name HAHB _Sample_label . save_ save_HCCH-TOCSY_15 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_HCCH-COSY_16 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _Sample_label . save_ save_1H-13C_HSQC_17 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _Sample_label . save_ save_15N-HOHAHA-HSQC_18 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HOHAHA-HSQC _Sample_label . save_ save_15N-NOESY-HSQC_19 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-NOESY-HSQC _Sample_label . save_ save_13C-15N_NOESY_20 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-15N NOESY' _Sample_label . save_ save_13C-13C_NOESY_21 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-13C NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCOCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCG_arom _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CG_arom _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNCG _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)C _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name DIPSI-H(CCO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_13 _Saveframe_category NMR_applied_experiment _Experiment_name DIPSI-C(CCO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_14 _Saveframe_category NMR_applied_experiment _Experiment_name HAHB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_15 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_16 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_17 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_18 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HOHAHA-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_19 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-NOESY-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_20 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_21 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-13C NOESY' _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 7.36 0.2 pH temperature 295 1 K 'ionic strength' 0.025 0.005 M 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 0.00 external indirect spherical external parallel 1.0 DSS C 13 'methyl protons' ppm 0.00 external indirect spherical external parallel 0.251449519 DSS N 15 'methyl protons' ppm 0.00 external indirect spherical external parallel 0.101329112 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_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 $sample_3 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'The winged-helix domain of WRN protein' _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 MET N N 121.7340 0.25 1 2 . 1 MET H H 8.4790 0.03 1 3 . 1 MET CA C 55.6760 0.50 1 4 . 1 MET HA H 4.4400 0.03 1 5 . 1 MET CB C 32.7070 0.50 1 6 . 1 MET HB2 H 2.0800 0.03 2 7 . 1 MET HB3 H 1.9600 0.03 2 8 . 1 MET C C 176.208 0.50 1 9 . 1 MET CG C 32.1100 0.50 1 10 . 1 MET HG2 H 2.5300 0.03 2 11 . 1 MET HG3 H 2.4700 0.03 2 12 . 2 ASP N N 121.1740 0.25 1 13 . 2 ASP H H 8.2860 0.03 1 14 . 2 ASP CA C 54.4280 0.50 1 15 . 2 ASP HA H 4.5600 0.03 1 16 . 2 ASP CB C 41.2720 0.50 1 17 . 2 ASP HB2 H 2.5800 0.03 2 18 . 2 ASP C C 175.938 0.50 1 19 . 3 ASP N N 120.8620 0.25 1 20 . 3 ASP H H 8.2800 0.03 1 21 . 3 ASP CA C 54.4280 0.50 1 22 . 3 ASP HA H 4.5500 0.03 1 23 . 3 ASP CB C 41.2790 0.50 1 24 . 3 ASP HB2 H 2.6500 0.03 2 25 . 3 ASP HB3 H 2.6200 0.03 2 26 . 3 ASP C C 176.451 0.50 1 27 . 4 SER N N 115.7330 0.25 1 28 . 4 SER H H 8.2560 0.03 1 29 . 4 SER CA C 58.7550 0.50 1 30 . 4 SER HA H 4.3600 0.03 1 31 . 4 SER CB C 63.8310 0.50 1 32 . 4 SER HB2 H 3.8500 0.03 2 33 . 4 SER C C 174.760 0.50 1 34 . 5 GLU N N 122.2640 0.25 1 35 . 5 GLU H H 8.4220 0.03 1 36 . 5 GLU CA C 56.5080 0.50 1 37 . 5 GLU HA H 4.3000 0.03 1 38 . 5 GLU CB C 30.3770 0.50 1 39 . 5 GLU HB2 H 2.0400 0.03 2 40 . 5 GLU HB3 H 1.9400 0.03 2 41 . 5 GLU C C 176.391 0.50 1 42 . 5 GLU CG C 36.4100 0.50 1 43 . 5 GLU HG2 H 2.2200 0.03 2 44 . 6 ASP N N 121.3470 0.25 1 45 . 6 ASP H H 8.3410 0.03 1 46 . 6 ASP CA C 54.4280 0.50 1 47 . 6 ASP HA H 4.6600 0.03 1 48 . 6 ASP CB C 41.3620 0.50 1 49 . 6 ASP HB2 H 2.7000 0.03 2 50 . 6 ASP HB3 H 2.6100 0.03 2 51 . 6 ASP C C 176.584 0.50 1 52 . 7 THR N N 114.4030 0.25 1 53 . 7 THR H H 8.2440 0.03 1 54 . 7 THR CA C 61.5840 0.50 1 55 . 7 THR HA H 4.4000 0.03 1 56 . 7 THR CB C 69.3240 0.50 1 57 . 7 THR HB H 4.3600 0.03 1 58 . 7 THR C C 177.251 0.50 1 59 . 7 THR CG2 C 21.5500 0.50 1 60 . 7 THR HG2 H 1.1100 0.03 1 61 . 8 SER N N 118.4200 0.25 1 62 . 8 SER H H 8.1720 0.03 1 63 . 8 SER CA C 58.5050 0.50 1 64 . 8 SER HA H 4.7900 0.03 1 65 . 8 SER CB C 64.6640 0.50 1 66 . 8 SER HB2 H 3.6600 0.03 2 67 . 8 SER C C 173.221 0.50 1 68 . 9 TRP N N 123.1150 0.25 1 69 . 9 TRP H H 8.7230 0.03 1 70 . 9 TRP CA C 56.5080 0.50 1 71 . 9 TRP HA H 4.4200 0.03 1 72 . 9 TRP CB C 32.2910 0.50 1 73 . 9 TRP HB2 H 2.8300 0.03 2 74 . 9 TRP C C 175.891 0.50 1 75 . 9 TRP NE1 N 129.201 0.25 1 76 . 9 TRP HE1 H 10.423 0.03 1 77 . 9 TRP CZ2 C 114.85 0.50 1 78 . 9 TRP HZ2 H 7.68 0.03 1 79 . 9 TRP CH2 C 121.72 0.50 1 80 . 9 TRP HH2 H 7.02 0.03 1 81 . 9 TRP CZ3 C 124.22 0.50 1 82 . 9 TRP HZ3 H 7.50 0.03 1 83 . 9 TRP CE3 C 122.38 0.50 1 84 . 9 TRP HE3 H 7.45 0.03 1 85 . 10 ASP N N 121.1740 0.25 1 86 . 10 ASP H H 8.2860 0.03 1 87 . 10 ASP CA C 54.4280 0.50 1 88 . 10 ASP HA H 4.5500 0.03 1 89 . 10 ASP CB C 41.2720 0.50 1 90 . 10 ASP HB2 H 2.7000 0.03 2 91 . 10 ASP HB3 H 2.6200 0.03 2 92 . 10 ASP C C 174.500 0.50 1 93 . 11 PHE N N 112.1040 0.25 1 94 . 11 PHE H H 7.4780 0.03 1 95 . 11 PHE CA C 54.8420 0.50 1 96 . 11 PHE HA H 4.5000 0.03 1 97 . 11 PHE CB C 40.4080 0.50 1 98 . 11 PHE HB2 H 2.8900 0.03 2 99 . 11 PHE C C 175.96 0.50 1 100 . 11 PHE CD1 C 133.29 0.50 3 101 . 11 PHE HD1 H 7.08 0.03 3 102 . 11 PHE CE1 C 132.47 0.50 3 103 . 11 PHE HE1 H 7.03 0.03 3 104 . 11 PHE CZ C 132.76 0.50 1 105 . 11 PHE HZ H 7.22 0.03 1 106 . 12 GLY N N 110.1090 0.25 1 107 . 12 GLY H H 9.3540 0.03 1 108 . 12 GLY CA C 49.4340 0.50 1 109 . 12 GLY C C 175.96 0.50 1 110 . 13 PRO CA C 65.8550 0.50 1 111 . 13 PRO HA H 4.3600 0.03 1 112 . 13 PRO CB C 31.9240 0.50 1 113 . 13 PRO HB2 H 2.1000 0.03 2 114 . 13 PRO C C 180.284 0.50 1 115 . 13 PRO CG C 28.7400 0.50 1 116 . 13 PRO HG2 H 1.8100 0.03 2 117 . 14 GLN N N 116.7140 0.25 1 118 . 14 GLN H H 8.1630 0.03 1 119 . 14 GLN CA C 61.0850 0.50 1 120 . 14 GLN HA H 4.4000 0.03 1 121 . 14 GLN CB C 27.4650 0.50 1 122 . 14 GLN HB2 H 1.9600 0.03 2 123 . 14 GLN HB3 H 1.8600 0.03 2 124 . 14 GLN C C 178.765 0.50 1 125 . 14 GLN CG C 33.1600 0.50 1 126 . 14 GLN HG2 H 2.2500 0.03 2 127 . 14 GLN NE2 N 111.3540 0.25 1 128 . 14 GLN HE21 H 7.0230 0.03 1 129 . 14 GLN HE22 H 6.7930 0.03 1 130 . 15 ALA N N 123.7440 0.25 1 131 . 15 ALA H H 9.5110 0.03 1 132 . 15 ALA CA C 55.6760 0.50 1 133 . 15 ALA HA H 4.1900 0.03 1 134 . 15 ALA CB C 19.2260 0.50 1 135 . 15 ALA HB H 1.1200 0.03 1 136 . 15 ALA C C 178.741 0.50 1 137 . 16 PHE N N 118.0280 0.25 1 138 . 16 PHE H H 9.2660 0.03 1 139 . 16 PHE CA C 62.9160 0.50 1 140 . 16 PHE HA H 4.3300 0.03 1 141 . 16 PHE CB C 39.4400 0.50 1 142 . 16 PHE HB2 H 2.9900 0.03 2 143 . 16 PHE C C 178.664 0.50 1 144 . 16 PHE CD1 C 132.74 0.50 3 145 . 16 PHE HD1 H 7.30 0.03 3 146 . 16 PHE CE1 C 132.08 0.50 3 147 . 16 PHE HE1 H 7.40 0.03 3 148 . 16 PHE CZ C 131.55 0.50 1 149 . 16 PHE HZ H 7.38 0.03 1 150 . 17 LYS N N 118.8860 0.25 1 151 . 17 LYS H H 7.7180 0.03 1 152 . 17 LYS CA C 60.9050 0.50 1 153 . 17 LYS HA H 4.3200 0.03 1 154 . 17 LYS CB C 33.1850 0.50 1 155 . 17 LYS HB2 H 1.6900 0.03 2 156 . 17 LYS C C 177.135 0.50 1 157 . 17 LYS CG C 26.8300 0.50 1 158 . 17 LYS HG2 H 1.3500 0.03 2 159 . 17 LYS CD C 28.5100 0.50 1 160 . 17 LYS HD2 H 1.6000 0.03 1 161 . 17 LYS CE C 41.9100 0.50 1 162 . 17 LYS HE2 H 2.8900 0.03 1 163 . 18 LEU N N 118.0590 0.25 1 164 . 18 LEU H H 8.3990 0.03 1 165 . 18 LEU CA C 58.1720 0.50 1 166 . 18 LEU HA H 4.0700 0.03 1 167 . 18 LEU CB C 41.9450 0.50 1 168 . 18 LEU HB3 H 1.8300 0.03 2 169 . 18 LEU C C 177.859 0.50 1 170 . 18 LEU CG C 27.5500 0.50 1 171 . 18 LEU HG H 2.0400 0.03 1 172 . 18 LEU CD1 C 26.5900 0.50 1 173 . 18 LEU HD1 H 0.9000 0.03 2 174 . 18 LEU CD2 C 21.2000 0.50 1 175 . 18 LEU HD2 H 0.8100 0.03 2 176 . 19 LEU N N 117.1690 0.25 1 177 . 19 LEU H H 9.1340 0.03 1 178 . 19 LEU CA C 58.8380 0.50 1 179 . 19 LEU HA H 3.8100 0.03 1 180 . 19 LEU CB C 40.2800 0.50 1 181 . 19 LEU HB3 H 1.4600 0.03 2 182 . 19 LEU C C 178.962 0.50 1 183 . 19 LEU CG C 28.0200 0.50 1 184 . 19 LEU HG H 1.7400 0.03 1 185 . 19 LEU CD1 C 25.6300 0.50 1 186 . 19 LEU HD1 H 0.7400 0.03 2 187 . 19 LEU CD2 C 21.2000 0.50 1 188 . 19 LEU HD2 H 0.6900 0.03 2 189 . 20 SER N N 112.3770 0.25 1 190 . 20 SER H H 7.6370 0.03 1 191 . 20 SER CA C 62.9280 0.50 1 192 . 20 SER HA H 4.0100 0.03 1 193 . 20 SER CB C 62.9280 0.50 1 194 . 20 SER HB3 H 3.7800 0.03 2 195 . 20 SER C C 174.934 0.50 1 196 . 21 ALA N N 123.2350 0.25 1 197 . 21 ALA H H 8.0990 0.03 1 198 . 21 ALA CA C 55.3730 0.50 1 199 . 21 ALA HA H 3.4800 0.03 1 200 . 21 ALA CB C 18.9560 0.50 1 201 . 21 ALA HB H 1.4200 0.03 1 202 . 21 ALA C C 178.288 0.50 1 203 . 22 VAL N N 116.7890 0.25 1 204 . 22 VAL H H 8.0220 0.03 1 205 . 22 VAL CA C 66.8850 0.50 1 206 . 22 VAL HA H 4.1400 0.03 1 207 . 22 VAL CB C 31.7820 0.50 1 208 . 22 VAL HB H 2.0600 0.03 1 209 . 22 VAL C C 177.891 0.50 1 210 . 22 VAL CG1 C 22.5100 0.50 1 211 . 22 VAL HG1 H 0.8800 0.03 2 212 . 23 ASP N N 118.9730 0.25 1 213 . 23 ASP H H 7.5530 0.03 1 214 . 23 ASP CA C 57.7710 0.50 1 215 . 23 ASP HA H 4.2500 0.03 1 216 . 23 ASP CB C 42.8940 0.50 1 217 . 23 ASP HB2 H 2.5300 0.03 2 218 . 23 ASP HB3 H 2.4200 0.03 2 219 . 23 ASP C C 175.94 0.50 1 220 . 24 ILE N N 120.3220 0.25 1 221 . 24 ILE H H 7.8780 0.03 1 222 . 24 ILE CA C 62.8540 0.50 1 223 . 24 ILE HA H 4.1400 0.03 1 224 . 24 ILE CB C 41.3000 0.50 1 225 . 24 ILE HB H 2.0100 0.03 1 226 . 24 ILE C C 174.933 0.50 1 227 . 24 ILE CG1 C 24.91 0.50 1 228 . 24 ILE HG12 H 1.1100 0.03 2 229 . 24 ILE HG13 H 0.8600 0.03 2 230 . 24 ILE CG2 C 13.4000 0.50 1 231 . 24 ILE HG2 H 0.3800 0.03 1 232 . 24 ILE CD1 C 8.8700 0.50 1 233 . 24 ILE HD1 H -0.07 0.03 1 234 . 25 LEU N N 123.4800 0.25 1 235 . 25 LEU H H 8.0950 0.03 1 236 . 25 LEU CA C 54.8720 0.50 1 237 . 25 LEU HA H 4.3100 0.03 1 238 . 25 LEU CB C 42.3200 0.50 1 239 . 25 LEU HB2 H 1.5900 0.03 2 240 . 25 LEU C C 177.63 0.50 1 241 . 25 LEU CG C 26.7500 0.50 1 242 . 25 LEU HG H 1.3500 0.03 1 243 . 25 LEU CD1 C 25.1900 0.50 1 244 . 25 LEU HD1 H 0.4200 0.03 2 245 . 25 LEU CD2 C 22.6900 0.50 1 246 . 25 LEU HD2 H 0.0000 0.03 2 247 . 26 GLY N N 106.7850 0.25 1 248 . 26 GLY H H 7.9640 0.03 1 249 . 26 GLY CA C 46.6050 0.50 1 250 . 26 GLY HA2 H 4.4200 0.03 2 251 . 26 GLY C C 174.7996 0.50 1 252 . 27 GLU N N 115.1580 0.25 1 253 . 27 GLU H H 8.4030 0.03 1 254 . 27 GLU CA C 57.8750 0.50 1 255 . 27 GLU HA H 3.9100 0.03 1 256 . 27 GLU CB C 28.3200 0.50 1 257 . 27 GLU HB2 H 2.0100 0.03 2 258 . 27 GLU C C 175.22 0.50 1 259 . 27 GLU HG2 H 2.1600 0.03 2 260 . 28 LYS N N 111.8810 0.25 1 261 . 28 LYS H H 7.0270 0.03 1 262 . 28 LYS CA C 55.7860 0.50 1 263 . 28 LYS HA H 4.2800 0.03 1 264 . 28 LYS CB C 33.6020 0.50 1 265 . 28 LYS HB2 H 1.7200 0.03 2 266 . 28 LYS C C 175.019 0.50 1 267 . 28 LYS CG C 22.7700 0.50 1 268 . 28 LYS HG2 H 1.3500 0.03 2 269 . 28 LYS CD C 26.6500 0.50 1 270 . 28 LYS HD2 H 1.6000 0.03 2 271 . 28 LYS CE C 40.3400 0.50 1 272 . 28 LYS HE2 H 2.9000 0.03 2 273 . 29 PHE N N 115.2230 0.25 1 274 . 29 PHE H H 7.3930 0.03 1 275 . 29 PHE CA C 56.4670 0.50 1 276 . 29 PHE HA H 4.3500 0.03 1 277 . 29 PHE CB C 44.5490 0.50 1 278 . 29 PHE HB3 H 2.6600 0.03 2 279 . 29 PHE C C 175.02 0.50 1 280 . 29 PHE CD1 C 133.10 0.50 3 281 . 29 PHE HD1 H 7.02 0.03 3 282 . 29 PHE CE1 C 131.44 0.50 3 283 . 29 PHE HE1 H 6.85 0.03 3 284 . 29 PHE CZ C 131.39 0.50 1 285 . 29 PHE HZ H 6.75 0.03 1 286 . 30 GLY CA C 45.7110 0.50 1 287 . 30 GLY HA2 H 3.7200 0.03 2 288 . 30 GLY C C 173.340 0.50 1 289 . 31 ILE N N 118.6870 0.25 1 290 . 31 ILE H H 8.7790 0.03 1 291 . 31 ILE CA C 59.2540 0.50 1 292 . 31 ILE HA H 4.0400 0.03 1 293 . 31 ILE CB C 39.6890 0.50 1 294 . 31 ILE HB H 1.8500 0.03 1 295 . 31 ILE C C 175.08 0.50 1 296 . 31 ILE CG1 C 28.7800 0.50 1 297 . 31 ILE HG12 H 1.2700 0.03 2 298 . 31 ILE CG2 C 13.4000 0.50 1 299 . 31 ILE HG2 H 1.1500 0.03 1 300 . 31 ILE CD1 C 8.8700 0.50 1 301 . 31 ILE HD1 H 0.8700 0.03 1 302 . 32 GLY N N 108.7180 0.25 1 303 . 32 GLY H H 8.6660 0.03 1 304 . 32 GLY CA C 47.0110 0.50 1 305 . 32 GLY HA2 H 3.8100 0.03 2 306 . 32 GLY C C 176.139 0.50 1 307 . 33 LEU N N 121.6090 0.25 1 308 . 33 LEU H H 7.5150 0.03 1 309 . 33 LEU CA C 58.6110 0.50 1 310 . 33 LEU HA H 4.2200 0.03 1 311 . 33 LEU CB C 39.2510 0.50 1 312 . 33 LEU HB3 H 1.3500 0.03 2 313 . 33 LEU C C 176.14 0.50 1 314 . 33 LEU CG C 26.2800 0.50 1 315 . 33 LEU HG H 1.1600 0.03 1 316 . 33 LEU CD1 C 25.5000 0.50 1 317 . 33 LEU HD1 H 0.4800 0.03 2 318 . 33 LEU CD2 C 21.2000 0.50 1 319 . 33 LEU HD2 H 0.2500 0.03 2 320 . 34 PRO CA C 66.7500 0.50 1 321 . 34 PRO HA H 3.8000 0.03 1 322 . 34 PRO CB C 31.0570 0.50 1 323 . 34 PRO HB2 H 1.8000 0.03 2 324 . 34 PRO C C 177.105 0.50 1 325 . 35 ILE N N 115.3510 0.25 1 326 . 35 ILE H H 7.2610 0.03 1 327 . 35 ILE CA C 66.7540 0.50 1 328 . 35 ILE HA H 4.2400 0.03 1 329 . 35 ILE CB C 37.4230 0.50 1 330 . 35 ILE HB H 1.8900 0.03 1 331 . 35 ILE C C 176.855 0.50 1 332 . 35 ILE HG12 H 0.8600 0.03 2 333 . 35 ILE CG2 C 13.4000 0.50 1 334 . 35 ILE HG2 H 0.6300 0.03 1 335 . 35 ILE CD1 C 8.8700 0.50 1 336 . 35 ILE HD1 H 0.5100 0.03 1 337 . 36 LEU N N 121.6670 0.25 1 338 . 36 LEU H H 8.1730 0.03 1 339 . 36 LEU CA C 58.6030 0.50 1 340 . 36 LEU HA H 4.2000 0.03 1 341 . 36 LEU CB C 41.2350 0.50 1 342 . 36 LEU HB3 H 2.1500 0.03 2 343 . 36 LEU C C 179.154 0.50 1 344 . 36 LEU CG C 26.8300 0.50 1 345 . 36 LEU HG H 1.2800 0.03 1 346 . 36 LEU CD1 C 25.6600 0.50 1 347 . 36 LEU HD2 H 0.8700 0.03 2 348 . 37 PHE N N 118.8530 0.25 1 349 . 37 PHE H H 8.3530 0.03 1 350 . 37 PHE CA C 60.4390 0.50 1 351 . 37 PHE HA H 4.3600 0.03 1 352 . 37 PHE CB C 38.3700 0.50 1 353 . 37 PHE HB2 H 3.5600 0.03 2 354 . 37 PHE C C 177.607 0.50 1 355 . 38 LEU N N 121.8680 0.25 1 356 . 38 LEU H H 8.2010 0.03 1 357 . 38 LEU CA C 57.3500 0.50 1 358 . 38 LEU HA H 3.6700 0.03 1 359 . 38 LEU CB C 42.1280 0.50 1 360 . 38 LEU HB2 H 1.6000 0.03 2 361 . 38 LEU C C 179.514 0.50 1 362 . 38 LEU CG C 22.2200 0.50 1 363 . 38 LEU HG H 0.6000 0.03 1 364 . 38 LEU CD1 C 21.4400 0.50 1 365 . 38 LEU HD2 H -0.3500 0.03 2 366 . 39 ARG N N 114.7140 0.25 1 367 . 39 ARG H H 8.3000 0.03 1 368 . 39 ARG CA C 56.7230 0.50 1 369 . 39 ARG HA H 3.6200 0.03 1 370 . 39 ARG CB C 27.9850 0.50 1 371 . 39 ARG HB2 H 1.9900 0.03 2 372 . 39 ARG C C 175.71 0.50 1 373 . 39 ARG HG2 H 1.8600 0.03 2 374 . 39 ARG CD C 40.7300 0.50 1 375 . 39 ARG HD2 H 3.0900 0.03 2 376 . 40 GLY N N 107.0690 0.25 1 377 . 40 GLY H H 7.2030 0.03 1 378 . 40 GLY CA C 45.7320 0.50 1 379 . 40 GLY HA2 H 3.3700 0.03 2 380 . 40 GLY C C 174.500 0.50 1 381 . 41 SER N N 112.1290 0.25 1 382 . 41 SER H H 7.5980 0.03 1 383 . 41 SER CA C 58.6110 0.50 1 384 . 41 SER HA H 4.4600 0.03 1 385 . 41 SER CB C 65.1750 0.50 1 386 . 41 SER HB3 H 3.8400 0.03 2 387 . 41 SER C C 174.5 0.50 1 388 . 42 ASN CA C 53.2310 0.50 1 389 . 42 ASN HA H 4.7800 0.03 1 390 . 42 ASN CB C 38.1910 0.50 1 391 . 42 ASN HB2 H 2.9200 0.03 2 392 . 42 ASN C C 175.664 0.50 1 393 . 42 ASN ND2 N 111.7740 0.25 1 394 . 42 ASN HD21 H 7.6090 0.03 1 395 . 42 ASN HD22 H 6.8920 0.03 1 396 . 43 SER N N 114.5080 0.25 1 397 . 43 SER H H 8.5050 0.03 1 398 . 43 SER CA C 58.8380 0.50 1 399 . 43 SER HA H 4.3400 0.03 1 400 . 43 SER CB C 64.1640 0.50 1 401 . 43 SER HB2 H 3.8300 0.03 2 402 . 43 SER C C 173.945 0.50 1 403 . 44 GLN N N 122.7340 0.25 1 404 . 44 GLN H H 8.2960 0.03 1 405 . 44 GLN CA C 57.2740 0.50 1 406 . 44 GLN HA H 4.2800 0.03 1 407 . 44 GLN CB C 28.0870 0.50 1 408 . 44 GLN HB2 H 1.9000 0.03 2 409 . 44 GLN C C 176.371 0.50 1 410 . 44 GLN CG C 34.2600 0.50 1 411 . 44 GLN HG2 H 2.1900 0.03 2 412 . 44 GLN HG3 H 2.0400 0.03 2 413 . 44 GLN NE2 N 112.6700 0.25 1 414 . 44 GLN HE21 H 7.5760 0.03 1 415 . 44 GLN HE22 H 6.879 0.03 1 416 . 45 ARG N N 117.4250 0.25 1 417 . 45 ARG H H 8.2860 0.03 1 418 . 45 ARG CA C 57.6350 0.50 1 419 . 45 ARG HA H 4.4200 0.03 1 420 . 45 ARG CB C 30.8880 0.50 1 421 . 45 ARG HB2 H 1.7500 0.03 2 422 . 45 ARG C C 176.225 0.50 1 423 . 45 ARG CG C 27.5500 0.50 1 424 . 45 ARG HG2 H 1.6100 0.03 2 425 . 45 ARG CD C 43.6200 0.50 1 426 . 45 ARG HD2 H 3.2100 0.03 2 427 . 46 LEU N N 118.5910 0.25 1 428 . 46 LEU H H 7.2920 0.03 1 429 . 46 LEU CA C 52.7110 0.50 1 430 . 46 LEU HA H 4.4200 0.03 1 431 . 46 LEU CB C 43.4880 0.50 1 432 . 46 LEU HB2 H 1.8100 0.03 2 433 . 46 LEU C C 174.645 0.50 1 434 . 46 LEU CG C 27.1800 0.50 1 435 . 46 LEU HG H 1.7100 0.03 1 436 . 46 LEU CD1 C 26.9100 0.50 1 437 . 46 LEU HD1 H 0.9600 0.03 2 438 . 46 LEU CD2 C 25.9700 0.50 1 439 . 46 LEU HD2 H 0.8900 0.03 2 440 . 47 ALA N N 129.4300 0.25 1 441 . 47 ALA H H 8.6280 0.03 1 442 . 47 ALA CA C 52.7630 0.50 1 443 . 47 ALA HA H 4.3800 0.03 1 444 . 47 ALA CB C 19.1410 0.50 1 445 . 47 ALA HB H 1.5200 0.03 1 446 . 47 ALA C C 178.394 0.50 1 447 . 48 ASP N N 120.3000 0.25 1 448 . 48 ASP H H 8.6600 0.03 1 449 . 48 ASP CA C 57.6730 0.50 1 450 . 48 ASP HA H 4.1300 0.03 1 451 . 48 ASP CB C 40.7620 0.50 1 452 . 48 ASP HB3 H 2.5000 0.03 2 453 . 48 ASP C C 178.42 0.50 1 454 . 49 GLN CA C 57.9460 0.50 1 455 . 49 GLN HA H 5.2700 0.03 1 456 . 49 GLN CB C 27.3880 0.50 1 457 . 49 GLN C C 178.071 0.50 1 458 . 49 GLN CG C 32.1100 0.50 1 459 . 49 GLN HG2 H 2.8400 0.03 2 460 . 49 GLN HG3 H 2.5900 0.03 2 461 . 49 GLN NE2 N 109.9280 0.25 1 462 . 49 GLN HE21 H 6.8670 0.03 1 463 . 49 GLN HE22 H 6.7090 0.03 1 464 . 50 TYR N N 117.8200 0.25 1 465 . 50 TYR H H 7.3930 0.03 1 466 . 50 TYR CA C 60.1070 0.50 1 467 . 50 TYR HA H 4.5100 0.03 1 468 . 50 TYR CB C 37.6390 0.50 1 469 . 50 TYR HB2 H 3.5400 0.03 2 470 . 50 TYR HB3 H 3.4100 0.03 2 471 . 50 TYR C C 176.898 0.50 1 472 . 50 TYR CD1 C 129.59 0.50 3 473 . 50 TYR HD1 H 7.03 0.03 3 474 . 50 TYR CE1 C 118.82 0.50 3 475 . 50 TYR HE1 H 6.75 0.03 3 476 . 51 ARG N N 116.0280 0.25 1 477 . 51 ARG H H 7.4220 0.03 1 478 . 51 ARG CA C 57.6900 0.50 1 479 . 51 ARG HA H 4.4300 0.03 1 480 . 51 ARG CB C 28.5960 0.50 1 481 . 51 ARG HB2 H 1.8500 0.03 2 482 . 51 ARG C C 176.046 0.50 1 483 . 51 ARG CG C 28.6500 0.50 1 484 . 51 ARG HG2 H 1.4700 0.03 2 485 . 51 ARG CD C 43.6000 0.50 1 486 . 51 ARG HD2 H 2.7000 0.03 2 487 . 52 ARG N N 113.4720 0.25 1 488 . 52 ARG H H 6.8660 0.03 1 489 . 52 ARG CA C 55.2870 0.50 1 490 . 52 ARG HA H 4.2400 0.03 1 491 . 52 ARG CB C 30.5260 0.50 1 492 . 52 ARG HB2 H 1.9400 0.03 2 493 . 52 ARG HB3 H 1.5600 0.03 2 494 . 52 ARG C C 176.029 0.50 1 495 . 52 ARG CG C 27.0700 0.50 1 496 . 52 ARG HG2 H 1.6100 0.03 2 497 . 52 ARG CD C 43.3600 0.50 1 498 . 52 ARG HD2 H 3.2300 0.03 2 499 . 53 HIS N N 122.1140 0.25 1 500 . 53 HIS H H 7.5690 0.03 1 501 . 53 HIS CA C 59.1090 0.50 1 502 . 53 HIS HA H 4.2500 0.03 1 503 . 53 HIS CB C 32.8530 0.50 1 504 . 53 HIS HB3 H 3.5700 0.03 2 505 . 53 HIS C C 176.01 0.50 1 506 . 53 HIS CE1 C 139.28 0.50 1 507 . 53 HIS HE1 H 7.66 0.03 1 508 . 53 HIS CD2 C 119.56 0.50 1 509 . 53 HIS HD2 H 6.71 0.03 1 510 . 54 SER CA C 61.9150 0.50 1 511 . 54 SER HA H 4.3600 0.03 1 512 . 54 SER CB C 62.9900 0.50 1 513 . 54 SER HB2 H 3.7600 0.03 2 514 . 54 SER HB3 H 3.5600 0.03 2 515 . 54 SER C C 176.448 0.50 1 516 . 55 LEU N N 123.9010 0.25 1 517 . 55 LEU H H 11.7400 0.03 1 518 . 55 LEU CA C 55.5930 0.50 1 519 . 55 LEU HA H 4.6300 0.03 1 520 . 55 LEU CB C 42.8600 0.50 1 521 . 55 LEU HB2 H 2.1100 0.03 2 522 . 55 LEU HB3 H 1.5500 0.03 2 523 . 55 LEU C C 179.140 0.50 1 524 . 55 LEU CG C 26.1100 0.50 1 525 . 55 LEU HG H 1.0100 0.03 1 526 . 55 LEU CD1 C 24.1900 0.50 1 527 . 55 LEU HD2 H -0.1500 0.03 2 528 . 56 PHE N N 124.3680 0.25 1 529 . 56 PHE H H 7.9720 0.03 1 530 . 56 PHE CA C 59.0900 0.50 1 531 . 56 PHE HA H 4.4000 0.03 1 532 . 56 PHE CB C 38.6250 0.50 1 533 . 56 PHE HB2 H 2.8200 0.03 2 534 . 56 PHE HB3 H 2.8100 0.03 2 535 . 56 PHE C C 177.623 0.50 1 536 . 57 GLY N N 113.2250 0.25 1 537 . 57 GLY H H 7.6420 0.03 1 538 . 57 GLY CA C 45.8150 0.50 1 539 . 57 GLY HA2 H 3.6300 0.03 2 540 . 57 GLY HA3 H 2.7700 0.03 2 541 . 57 GLY C C 175.98 0.50 1 542 . 58 THR N N 108.1280 0.25 1 543 . 58 THR H H 7.5830 0.03 1 544 . 58 THR CA C 63.8460 0.50 1 545 . 58 THR HA H 4.2900 0.03 1 546 . 58 THR CB C 69.5790 0.50 1 547 . 58 THR HB H 4.3100 0.03 1 548 . 58 THR C C 175.55 0.50 1 549 . 58 THR CG2 C 22.2700 0.50 1 550 . 58 THR HG2 H 1.2100 0.03 1 551 . 59 GLY N N 110.4310 0.25 1 552 . 59 GLY H H 9.1050 0.03 1 553 . 59 GLY CA C 45.6660 0.50 1 554 . 59 GLY HA2 H 5.3800 0.03 2 555 . 59 GLY C C 175.064 0.50 1 556 . 60 LYS N N 117.8620 0.25 1 557 . 60 LYS H H 7.3350 0.03 1 558 . 60 LYS CA C 58.6800 0.50 1 559 . 60 LYS HA H 3.9200 0.03 1 560 . 60 LYS CB C 32.3540 0.50 1 561 . 60 LYS HB2 H 1.7700 0.03 2 562 . 60 LYS C C 175.150 0.50 1 563 . 60 LYS CG C 24.9100 0.50 1 564 . 60 LYS HG2 H 1.3600 0.03 2 565 . 60 LYS CD C 29.4600 0.50 1 566 . 60 LYS HD2 H 1.5900 0.03 2 567 . 60 LYS CE C 41.9400 0.50 1 568 . 60 LYS HE2 H 2.9000 0.03 2 569 . 61 ASP N N 116.7620 0.25 1 570 . 61 ASP H H 8.8710 0.03 1 571 . 61 ASP CA C 54.9270 0.50 1 572 . 61 ASP HA H 4.2500 0.03 1 573 . 61 ASP CB C 39.6980 0.50 1 574 . 61 ASP HB2 H 2.5000 0.03 2 575 . 61 ASP C C 175.174 0.50 1 576 . 62 GLN N N 116.1020 0.25 1 577 . 62 GLN H H 7.3350 0.03 1 578 . 62 GLN CA C 53.0440 0.50 1 579 . 62 GLN HA H 4.5000 0.03 1 580 . 62 GLN CB C 29.0910 0.50 1 581 . 62 GLN HB2 H 2.0000 0.03 2 582 . 62 GLN C C 175.9998 0.50 1 583 . 62 GLN CG C 31.3300 0.50 1 584 . 62 GLN HG2 H 2.4500 0.03 2 585 . 62 GLN NE2 N 107.4280 0.25 1 586 . 62 GLN HE21 H 6.004 0.03 1 587 . 62 GLN HE22 H 5.6650 0.03 1 588 . 63 THR N N 112.0910 0.25 1 589 . 63 THR H H 8.5200 0.03 1 590 . 63 THR CA C 61.5010 0.50 1 591 . 63 THR HA H 4.0800 0.03 1 592 . 63 THR CB C 70.8220 0.50 1 593 . 63 THR HB H 4.1100 0.03 1 594 . 63 THR C C 175.024 0.50 1 595 . 63 THR CG2 C 21.7900 0.50 1 596 . 63 THR HG2 H 1.1200 0.03 1 597 . 64 GLU N N 120.7700 0.25 1 598 . 64 GLU H H 9.3650 0.03 1 599 . 64 GLU CA C 61.4180 0.50 1 600 . 64 GLU HA H 4.1000 0.03 1 601 . 64 GLU CB C 29.9610 0.50 1 602 . 64 GLU HB2 H 2.0400 0.03 2 603 . 64 GLU C C 178.363 0.50 1 604 . 64 GLU CG C 37.1200 0.50 1 605 . 64 GLU HG2 H 2.5200 0.03 2 606 . 64 GLU HG3 H 2.4600 0.03 2 607 . 65 SER N N 112.3290 0.25 1 608 . 65 SER H H 8.5200 0.03 1 609 . 65 SER CA C 62.1230 0.50 1 610 . 65 SER HA H 4.0200 0.03 1 611 . 65 SER CB C 62.1200 0.50 1 612 . 65 SER HB3 H 2.8800 0.03 2 613 . 65 SER C C 176.737 0.50 1 614 . 66 TRP N N 127.3360 0.25 1 615 . 66 TRP H H 8.2660 0.03 1 616 . 66 TRP CA C 62.8830 0.50 1 617 . 66 TRP HA H 3.4700 0.03 1 618 . 66 TRP CB C 30.0440 0.50 1 619 . 66 TRP HB2 H 3.3600 0.03 2 620 . 66 TRP C C 178.412 0.50 1 621 . 66 TRP NE1 N 128.880 0.25 1 622 . 66 TRP HE1 H 10.4700 0.03 1 623 . 66 TRP CZ2 C 114.49 0.50 1 624 . 66 TRP HZ2 H 7.36 0.03 1 625 . 66 TRP CH2 C 121.86 0.50 1 626 . 66 TRP HH2 H 7.55 0.03 1 627 . 66 TRP CZ3 C 124.29 0.50 1 628 . 66 TRP HZ3 H 7.25 0.03 1 629 . 66 TRP CE3 C 124.26 0.50 1 630 . 66 TRP HE3 H 7.09 0.03 1 631 . 67 TRP N N 118.0420 0.25 1 632 . 67 TRP H H 8.6650 0.03 1 633 . 67 TRP CA C 61.2560 0.50 1 634 . 67 TRP HA H 4.4700 0.03 1 635 . 67 TRP CB C 31.4590 0.50 1 636 . 67 TRP HB2 H 2.8800 0.03 2 637 . 67 TRP C C 179.734 0.50 1 638 . 67 TRP NE1 N 128.140 0.25 1 639 . 67 TRP HE1 H 10.4700 0.03 1 640 . 67 TRP CZ2 C 114.08 0.50 1 641 . 67 TRP HZ2 H 7.14 0.03 1 642 . 67 TRP CH2 C 124.91 0.50 1 643 . 67 TRP HH2 H 6.85 0.03 1 644 . 67 TRP CZ3 C 125.45 0.50 1 645 . 67 TRP HZ3 H 6.76 0.03 1 646 . 67 TRP CE3 C 126.13 0.50 1 647 . 67 TRP HE3 H 6.76 0.03 1 648 . 68 LYS N N 119.9120 0.25 1 649 . 68 LYS H H 8.6850 0.03 1 650 . 68 LYS CA C 60.0800 0.50 1 651 . 68 LYS HA H 4.1000 0.03 1 652 . 68 LYS CB C 32.2080 0.50 1 653 . 68 LYS HB2 H 1.7200 0.03 2 654 . 68 LYS C C 179.753 0.50 1 655 . 68 LYS CG C 26.3500 0.50 1 656 . 68 LYS HG2 H 1.3500 0.03 2 657 . 68 LYS CD C 29.2200 0.50 1 658 . 68 LYS HD2 H 1.5600 0.03 2 659 . 68 LYS CE C 42.1700 0.50 1 660 . 68 LYS HE2 H 3.8900 0.03 2 661 . 69 ALA N N 124.9580 0.25 1 662 . 69 ALA H H 8.1150 0.03 1 663 . 69 ALA CA C 55.4270 0.50 1 664 . 69 ALA HA H 3.9000 0.03 1 665 . 69 ALA CB C 17.9200 0.50 1 666 . 69 ALA HB H 1.1400 0.03 1 667 . 69 ALA C C 179.76 0.50 1 668 . 70 PHE N N 121.4110 0.25 1 669 . 70 PHE H H 8.9110 0.03 1 670 . 70 PHE CA C 59.5040 0.50 1 671 . 70 PHE HA H 3.8600 0.03 1 672 . 70 PHE CB C 38.7820 0.50 1 673 . 70 PHE HB2 H 2.8400 0.03 2 674 . 70 PHE C C 178.119 0.50 1 675 . 71 SER N N 115.6210 0.25 1 676 . 71 SER H H 8.7100 0.03 1 677 . 71 SER CA C 62.6660 0.50 1 678 . 71 SER HA H 4.8900 0.03 1 679 . 71 SER CB C 66.9030 0.50 1 680 . 71 SER HB3 H 4.2400 0.03 2 681 . 71 SER C C 175.356 0.50 1 682 . 72 ARG N N 120.6340 0.25 1 683 . 72 ARG H H 7.2880 0.03 1 684 . 72 ARG CA C 59.0910 0.50 1 685 . 72 ARG HA H 3.8900 0.03 1 686 . 72 ARG CB C 29.1720 0.50 1 687 . 72 ARG HB2 H 1.8900 0.03 2 688 . 72 ARG C C 179.142 0.50 1 689 . 72 ARG CG C 26.3500 0.50 1 690 . 72 ARG HG2 H 1.7700 0.03 2 691 . 72 ARG HG3 H 1.5700 0.03 2 692 . 72 ARG CD C 43.5900 0.50 1 693 . 72 ARG HD2 H 2.9000 0.03 2 694 . 73 GLN N N 118.4830 0.25 1 695 . 73 GLN H H 7.3320 0.03 1 696 . 73 GLN CA C 57.9430 0.50 1 697 . 73 GLN HA H 4.0100 0.03 1 698 . 73 GLN CB C 27.8570 0.50 1 699 . 73 GLN HB2 H 1.8900 0.03 2 700 . 73 GLN C C 179.402 0.50 1 701 . 73 GLN CG C 33.4700 0.50 1 702 . 73 GLN HG2 H 2.1400 0.03 2 703 . 73 GLN NE2 N 111.7540 0.25 1 704 . 73 GLN HE21 H 7.30230 0.03 1 705 . 73 GLN HE22 H 6.7620 0.03 1 706 . 74 LEU N N 119.3170 0.25 1 707 . 74 LEU H H 7.6520 0.03 1 708 . 74 LEU CA C 57.1150 0.50 1 709 . 74 LEU HA H 3.9500 0.03 1 710 . 74 LEU CB C 41.3280 0.50 1 711 . 74 LEU HB2 H 1.5700 0.03 2 712 . 74 LEU C C 178.81 0.50 1 713 . 74 LEU CG C 26.5900 0.50 1 714 . 74 LEU HG H 0.6700 0.03 1 715 . 74 LEU CD1 C 26.0800 0.50 1 716 . 74 LEU HD1 H 0.0800 0.03 2 717 . 74 LEU CD2 C 22.5300 0.50 1 718 . 74 LEU HD2 H -0.0300 0.03 2 719 . 75 ILE N N 122.9910 0.25 1 720 . 75 ILE H H 8.0890 0.03 1 721 . 75 ILE CA C 64.4120 0.50 1 722 . 75 ILE HA H 4.3300 0.03 1 723 . 75 ILE CB C 38.3510 0.50 1 724 . 75 ILE HB H 1.8600 0.03 1 725 . 75 ILE C C 178.235 0.50 1 726 . 75 ILE CG1 C 26.8200 0.50 1 727 . 75 ILE HG12 H 1.5000 0.03 2 728 . 75 ILE CG2 C 17.2400 0.50 1 729 . 75 ILE HG2 H 0.7800 0.03 1 730 . 75 ILE CD1 C 8.8700 0.50 1 731 . 75 ILE HD1 H 0.7100 0.03 1 732 . 76 THR N N 119.5200 0.25 1 733 . 76 THR H H 8.5680 0.03 1 734 . 76 THR CA C 66.5780 0.50 1 735 . 76 THR HA H 3.8900 0.03 1 736 . 76 THR CB C 68.1590 0.50 1 737 . 76 THR HB H 4.1700 0.03 1 738 . 76 THR C C 176.870 0.50 1 739 . 76 THR CG2 C 22.0300 0.50 1 740 . 76 THR HG2 H 1.1200 0.03 1 741 . 77 GLY N N 105.2830 0.25 1 742 . 77 GLY H H 8.1830 0.03 1 743 . 77 GLY CA C 45.3570 0.50 1 744 . 77 GLY HA2 H 4.0100 0.03 2 745 . 77 GLY C C 173.316 0.50 1 746 . 78 GLY N N 105.3990 0.25 1 747 . 78 GLY H H 7.8350 0.03 1 748 . 78 GLY CA C 45.6490 0.50 1 749 . 78 GLY HA2 H 3.9500 0.03 2 750 . 78 GLY C C 175.937 0.50 1 751 . 79 PHE N N 120.4210 0.25 1 752 . 79 PHE H H 8.7830 0.03 1 753 . 79 PHE CA C 61.0850 0.50 1 754 . 79 PHE HA H 3.8400 0.03 1 755 . 79 PHE CB C 40.9270 0.50 1 756 . 79 PHE HB2 H 3.5900 0.03 2 757 . 79 PHE C C 173.220 0.50 1 758 . 80 LEU N N 116.2640 0.25 1 759 . 80 LEU H H 6.9690 0.03 1 760 . 80 LEU CA C 52.1070 0.50 1 761 . 80 LEU HA H 5.2300 0.03 1 762 . 80 LEU CB C 48.8060 0.50 1 763 . 80 LEU HB3 H 1.2200 0.03 2 764 . 80 LEU C C 174.338 0.50 1 765 . 80 LEU CG C 25.6300 0.50 1 766 . 80 LEU CD1 C 25.8100 0.50 1 767 . 80 LEU HD1 H 0.6500 0.03 2 768 . 80 LEU CD2 C 25.5000 0.50 1 769 . 80 LEU HD2 H 0.8300 0.03 2 770 . 81 VAL N N 119.0700 0.25 1 771 . 81 VAL H H 9.2420 0.03 1 772 . 81 VAL CA C 59.9200 0.50 1 773 . 81 VAL HA H 4.4700 0.03 1 774 . 81 VAL CB C 35.2870 0.50 1 775 . 81 VAL HB H 2.1730 0.03 1 776 . 81 VAL C C 172.260 0.50 1 777 . 81 VAL CG1 C 21.0700 0.50 1 778 . 81 VAL HG1 H 0.8500 0.03 2 779 . 81 VAL CG2 C 18.9200 0.50 1 780 . 81 VAL HG2 H 0.6500 0.03 2 781 . 82 GLU N N 124.3480 0.25 1 782 . 82 GLU H H 8.5290 0.03 1 783 . 82 GLU CA C 54.6770 0.50 1 784 . 82 GLU HA H 5.3300 0.03 1 785 . 82 GLU CB C 31.7090 0.50 1 786 . 82 GLU HB2 H 1.7000 0.03 2 787 . 82 GLU HB3 H 1.6000 0.03 2 788 . 82 GLU C C 176.315 0.50 1 789 . 82 GLU CG C 37.6900 0.50 1 790 . 82 GLU HG2 H 2.1500 0.03 2 791 . 82 GLU HG3 H 1.9300 0.03 2 792 . 83 VAL N N 122.1230 0.25 1 793 . 83 VAL H H 8.8460 0.03 1 794 . 83 VAL CA C 60.4190 0.50 1 795 . 83 VAL HA H 4.3600 0.03 1 796 . 83 VAL CB C 35.0380 0.50 1 797 . 83 VAL C C 176.31 0.50 1 798 . 83 VAL CG1 C 21.2900 0.50 1 799 . 83 VAL HG1 H 0.8000 0.03 2 800 . 83 VAL CG2 C 18.4700 0.50 1 801 . 83 VAL HG2 H 0.7200 0.03 2 802 . 84 SER CA C 57.7700 0.50 1 803 . 84 SER HA H 4.7300 0.03 1 804 . 84 SER CB C 63.7780 0.50 1 805 . 84 SER HB2 H 3.7200 0.03 2 806 . 84 SER C C 174.585 0.50 1 807 . 85 ARG N N 123.8660 0.25 1 808 . 85 ARG H H 8.3650 0.03 1 809 . 85 ARG CA C 55.9260 0.50 1 810 . 85 ARG HA H 4.2500 0.03 1 811 . 85 ARG CB C 32.7070 0.50 1 812 . 85 ARG HB2 H 1.4700 0.03 2 813 . 85 ARG C C 176.713 0.50 1 814 . 86 TYR N N 122.8390 0.25 1 815 . 86 TYR H H 8.0770 0.03 1 816 . 86 TYR CA C 54.8400 0.50 1 817 . 86 TYR HA H 3.2800 0.03 1 818 . 86 TYR CB C 42.7900 0.50 1 819 . 86 TYR C C 175.652 0.50 1 820 . 86 TYR CD1 C 129.81 0.50 3 821 . 86 TYR HD1 H 7.24 0.03 3 822 . 86 TYR CE1 C 118.17 0.50 3 823 . 86 TYR HE1 H 6.75 0.03 3 824 . 87 ASN N N 122.1150 0.25 1 825 . 87 ASN H H 7.8120 0.03 1 826 . 87 ASN CA C 52.2960 0.50 1 827 . 87 ASN HA H 4.3900 0.03 1 828 . 87 ASN CB C 43.2390 0.50 1 829 . 87 ASN HB2 H 2.7000 0.03 2 830 . 87 ASN C C 175.66 0.50 1 831 . 88 LYS CA C 53.0580 0.50 1 832 . 88 LYS HA H 4.1300 0.03 1 833 . 88 LYS CB C 28.2570 0.50 1 834 . 88 LYS HB3 H 1.7800 0.03 2 835 . 88 LYS C C 178.962 0.50 1 836 . 88 LYS CG C 25.6300 0.50 1 837 . 88 LYS HG2 H 1.3300 0.03 2 838 . 88 LYS CD C 28.0200 0.50 1 839 . 88 LYS HD2 H 1.6000 0.03 2 840 . 88 LYS CE C 40.2500 0.50 1 841 . 88 LYS HE2 H 2.9300 0.03 2 842 . 89 PHE N N 112.3370 0.25 1 843 . 89 PHE H H 7.6030 0.03 1 844 . 89 PHE CA C 58.6200 0.50 1 845 . 89 PHE HA H 4.4300 0.03 1 846 . 89 PHE CB C 40.2700 0.50 1 847 . 89 PHE HB2 H 3.2300 0.03 2 848 . 89 PHE HB3 H 3.1200 0.03 2 849 . 89 PHE C C 175.548 0.50 1 850 . 90 MET N N 119.1000 0.25 1 851 . 90 MET H H 7.8150 0.03 1 852 . 90 MET CA C 55.0660 0.50 1 853 . 90 MET HA H 4.5400 0.03 1 854 . 90 MET CB C 34.0160 0.50 1 855 . 90 MET HB2 H 1.9700 0.03 2 856 . 90 MET C C 174.848 0.50 1 857 . 90 MET CG C 31.7500 0.50 1 858 . 90 MET HG2 H 2.0600 0.03 2 859 . 91 LYS N N 123.0500 0.25 1 860 . 91 LYS H H 8.4250 0.03 1 861 . 91 LYS CA C 55.7590 0.50 1 862 . 91 LYS HA H 4.4400 0.03 1 863 . 91 LYS CB C 33.7060 0.50 1 864 . 91 LYS HB2 H 1.8400 0.03 2 865 . 91 LYS C C 176.391 0.50 1 866 . 91 LYS CG C 25.3900 0.50 1 867 . 91 LYS HG2 H 1.5600 0.03 2 868 . 91 LYS CD C 29.4600 0.50 1 869 . 91 LYS HD2 H 1.4500 0.03 2 870 . 91 LYS CE C 40.3500 0.50 1 871 . 91 LYS HE2 H 2.8300 0.03 2 872 . 92 ILE N N 119.6620 0.25 1 873 . 92 ILE H H 8.4690 0.03 1 874 . 92 ILE CA C 59.2540 0.50 1 875 . 92 ILE HA H 3.9300 0.03 1 876 . 92 ILE CB C 40.1970 0.50 1 877 . 92 ILE HB H 1.6000 0.03 1 878 . 92 ILE C C 174.806 0.50 1 879 . 92 ILE CG1 C 24.7200 0.50 1 880 . 92 ILE HG12 H 1.2800 0.03 2 881 . 92 ILE HG13 H 0.9300 0.03 2 882 . 92 ILE CG2 C 24.0600 0.50 1 883 . 92 ILE HG2 H 0.6000 0.03 1 884 . 93 CYS N N 122.6220 0.25 1 885 . 93 CYS H H 7.8790 0.03 1 886 . 93 CYS CA C 57.9760 0.50 1 887 . 93 CYS HA H 4.4600 0.03 1 888 . 93 CYS CB C 28.3200 0.50 1 889 . 93 CYS HB2 H 2.8900 0.03 2 890 . 93 CYS C C 171.773 0.50 1 891 . 94 ALA N N 128.6230 0.25 1 892 . 94 ALA H H 8.9740 0.03 1 893 . 94 ALA CA C 49.6840 0.50 1 894 . 94 ALA HA H 4.6400 0.03 1 895 . 94 ALA CB C 22.7210 0.50 1 896 . 94 ALA HB H 1.1800 0.03 1 897 . 94 ALA C C 176.224 0.50 1 898 . 95 LEU N N 119.3370 0.25 1 899 . 95 LEU H H 9.0660 0.03 1 900 . 95 LEU CA C 56.2750 0.50 1 901 . 95 LEU HA H 4.6100 0.03 1 902 . 95 LEU CB C 42.8460 0.50 1 903 . 95 LEU HB2 H 1.6500 0.03 2 904 . 95 LEU C C 179.02 0.50 1 905 . 95 LEU CG C 28.9800 0.50 1 906 . 95 LEU HG H 1.4200 0.03 1 907 . 95 LEU CD1 C 25.8700 0.50 1 908 . 95 LEU HD2 H 0.8900 0.03 2 909 . 96 THR N N 110.1970 0.25 1 910 . 96 THR H H 7.1440 0.03 1 911 . 96 THR CA C 59.2580 0.50 1 912 . 96 THR HA H 4.4200 0.03 1 913 . 96 THR CB C 71.1580 0.50 1 914 . 96 THR HB H 4.1500 0.03 1 915 . 96 THR C C 179.03 0.50 1 916 . 96 THR CG2 C 22.3700 0.50 1 917 . 96 THR HG2 H 0.8700 0.03 1 918 . 97 LYS CA C 60.2500 0.50 1 919 . 97 LYS HA H 4.3200 0.03 1 920 . 97 LYS CB C 31.6550 0.50 1 921 . 97 LYS HB2 H 1.8600 0.03 2 922 . 97 LYS C C 178.430 0.50 1 923 . 97 LYS CG C 24.9900 0.50 1 924 . 97 LYS HG2 H 1.3500 0.03 2 925 . 97 LYS CD C 29.2200 0.50 1 926 . 97 LYS HD2 H 1.7000 0.03 2 927 . 97 LYS CE C 43.3600 0.50 1 928 . 97 LYS HE2 H 2.9100 0.03 2 929 . 98 LYS N N 119.4740 0.25 1 930 . 98 LYS H H 8.1950 0.03 1 931 . 98 LYS CA C 59.7590 0.50 1 932 . 98 LYS HA H 4.1500 0.03 1 933 . 98 LYS CB C 32.8740 0.50 1 934 . 98 LYS HB2 H 1.7200 0.03 2 935 . 98 LYS C C 180.18 0.50 1 936 . 98 LYS CG C 24.9100 0.50 1 937 . 98 LYS HG2 H 1.3600 0.03 2 938 . 98 LYS CD C 28.6300 0.50 1 939 . 98 LYS HD2 H 1.6000 0.03 2 940 . 98 LYS CE C 42.2200 0.50 1 941 . 98 LYS HE2 H 2.9200 0.03 2 942 . 99 GLY N N 108.4070 0.25 1 943 . 99 GLY H H 8.4470 0.03 1 944 . 99 GLY CA C 48.3250 0.50 1 945 . 99 GLY HA2 H 4.4700 0.03 2 946 . 99 GLY C C 174.659 0.50 1 947 . 100 ARG N N 122.0230 0.25 1 948 . 100 ARG H H 9.0570 0.03 1 949 . 100 ARG CA C 60.0030 0.50 1 950 . 100 ARG HA H 3.9600 0.03 1 951 . 100 ARG CB C 29.5450 0.50 1 952 . 100 ARG HB2 H 1.6100 0.03 2 953 . 100 ARG C C 178.641 0.50 1 954 . 100 ARG CG C 25.6000 0.50 1 955 . 100 ARG HG2 H 1.7800 0.03 2 956 . 100 ARG CD C 42.4000 0.50 1 957 . 100 ARG HD2 H 2.9200 0.03 2 958 . 101 ASN N N 118.3040 0.25 1 959 . 101 ASN H H 8.7040 0.03 1 960 . 101 ASN CA C 56.0920 0.50 1 961 . 101 ASN HA H 4.5000 0.03 1 962 . 101 ASN CB C 38.2830 0.50 1 963 . 101 ASN HB2 H 2.9400 0.03 2 964 . 101 ASN C C 177.679 0.50 1 965 . 101 ASN ND2 N 111.4180 0.25 1 966 . 101 ASN HD21 H 7.6680 0.03 1 967 . 101 ASN HD22 H 6.8990 0.03 1 968 . 102 TRP N N 121.8000 0.25 1 969 . 102 TRP H H 8.3190 0.03 1 970 . 102 TRP CA C 62.8750 0.50 1 971 . 102 TRP HA H 4.4800 0.03 1 972 . 102 TRP CB C 29.3360 0.50 1 973 . 102 TRP HB2 H 2.8800 0.03 2 974 . 102 TRP C C 178.235 0.50 1 975 . 102 TRP NE1 N 128.858 0.25 1 976 . 102 TRP HE1 H 10.4700 0.03 1 977 . 102 TRP CD1 C 128.22 0.50 1 978 . 102 TRP HD1 H 7.48 0.03 1 979 . 102 TRP CZ2 C 113.16 0.50 1 980 . 102 TRP HZ2 H 6.68 0.03 1 981 . 102 TRP CH2 C 124.91 0.50 1 982 . 102 TRP HH2 H 6.85 0.03 1 983 . 102 TRP CZ3 C 120.78 0.50 1 984 . 102 TRP HZ3 H 7.209 0.03 1 985 . 102 TRP CE3 C 121.14 0.50 1 986 . 102 TRP HE3 H 7.30 0.03 1 987 . 103 LEU N N 119.6340 0.25 1 988 . 103 LEU H H 8.6170 0.03 1 989 . 103 LEU CA C 58.0890 0.50 1 990 . 103 LEU HA H 3.9900 0.03 1 991 . 103 LEU CB C 42.9800 0.50 1 992 . 103 LEU HB2 H 1.8100 0.03 2 993 . 103 LEU C C 178.425 0.50 1 994 . 103 LEU CG C 27.2200 0.50 1 995 . 103 LEU HG H 1.5900 0.03 1 996 . 103 LEU CD1 C 22.3700 0.50 1 997 . 103 LEU HD1 H 0.9000 0.03 2 998 . 103 LEU CD2 C 21.2000 0.50 1 999 . 103 LEU HD2 H 0.8100 0.03 2 1000 . 104 HIS N N 117.0270 0.25 1 1001 . 104 HIS H H 8.2990 0.03 1 1002 . 104 HIS CA C 59.2300 0.50 1 1003 . 104 HIS HA H 4.4200 0.03 1 1004 . 104 HIS CB C 30.4910 0.50 1 1005 . 104 HIS HB2 H 3.2500 0.03 2 1006 . 104 HIS C C 179.399 0.50 1 1007 . 104 HIS CE1 C 137.95 0.50 1 1008 . 104 HIS HE1 H 7.74 0.03 1 1009 . 104 HIS CD2 C 119.18 0.50 1 1010 . 104 HIS HD2 H 6.89 0.03 1 1011 . 105 LYS N N 119.5650 0.25 1 1012 . 105 LYS H H 7.6080 0.03 1 1013 . 105 LYS CA C 58.6030 0.50 1 1014 . 105 LYS HA H 3.96000 0.03 1 1015 . 105 LYS CB C 32.2030 0.50 1 1016 . 105 LYS HB2 H 1.7100 0.03 2 1017 . 105 LYS C C 174.535 0.50 1 1018 . 105 LYS CG C 25.1100 0.50 1 1019 . 105 LYS HG2 H 1.3700 0.03 2 1020 . 105 LYS CD C 28.9800 0.50 1 1021 . 105 LYS HD2 H 1.5800 0.03 2 1022 . 105 LYS CE C 42.4000 0.50 1 1023 . 105 LYS HE2 H 3.2100 0.03 2 1024 . 106 ALA N N 122.3990 0.25 1 1025 . 106 ALA H H 8.1550 0.03 1 1026 . 106 ALA CA C 53.1420 0.50 1 1027 . 106 ALA HA H 4.1000 0.03 1 1028 . 106 ALA CB C 18.4050 0.50 1 1029 . 106 ALA HB H 1.1000 0.03 1 1030 . 106 ALA C C 177.888 0.50 1 1031 . 107 ASN N N 114.5720 0.25 1 1032 . 107 ASN H H 7.8320 0.03 1 1033 . 107 ASN CA C 54.9040 0.50 1 1034 . 107 ASN HA H 4.5300 0.03 1 1035 . 107 ASN CB C 39.6930 0.50 1 1036 . 107 ASN HB2 H 2.8700 0.03 2 1037 . 107 ASN HB3 H 2.7500 0.03 2 1038 . 107 ASN C C 176.27 0.50 1 1039 . 107 ASN ND2 N 112.6330 0.25 1 1040 . 107 ASN HD21 H 7.480 0.03 1 1041 . 107 ASN HD22 H 6.984 0.03 1 1042 . 108 THR N N 109.5720 0.25 1 1043 . 108 THR H H 7.6130 0.03 1 1044 . 108 THR CA C 63.0790 0.50 1 1045 . 108 THR HA H 4.2000 0.03 1 1046 . 108 THR CB C 70.0270 0.50 1 1047 . 108 THR HB H 4.2000 0.03 1 1048 . 108 THR C C 174.393 0.50 1 1049 . 108 THR CG2 C 21.7900 0.50 1 1050 . 108 THR HG2 H 1.1100 0.03 1 1051 . 109 GLU N N 121.5470 0.25 1 1052 . 109 GLU H H 8.0820 0.03 1 1053 . 109 GLU CA C 56.1540 0.50 1 1054 . 109 GLU HA H 4.3500 0.03 1 1055 . 109 GLU CB C 31.3280 0.50 1 1056 . 109 GLU HB2 H 1.8500 0.03 2 1057 . 109 GLU C C 174.986 0.50 1 1058 . 109 GLU CG C 35.9300 0.50 1 1059 . 109 GLU HG2 H 2.0800 0.03 2 1060 . 110 SER N N 115.2660 0.25 1 1061 . 110 SER H H 7.9780 0.03 1 1062 . 110 SER CA C 58.8600 0.50 1 1063 . 110 SER HA H 4.1900 0.03 1 1064 . 110 SER CB C 63.3750 0.50 1 1065 . 110 SER HB3 H 3.7000 0.03 2 1066 . 110 SER C C 175.02 0.50 1 1067 . 111 GLN N N 110.4350 0.25 1 1068 . 111 GLN H H 8.3320 0.03 1 1069 . 111 GLN CA C 54.3890 0.50 1 1070 . 111 GLN HA H 4.3200 0.03 1 1071 . 111 GLN CB C 29.8650 0.50 1 1072 . 111 GLN HB2 H 1.9100 0.03 2 1073 . 111 GLN HB3 H 1.8300 0.03 2 1074 . 111 GLN C C 175.259 0.50 1 1075 . 111 GLN CG C 33.0600 0.50 1 1076 . 111 GLN HG2 H 2.1100 0.03 2 1077 . 111 GLN NE2 N 112.0140 0.25 1 1078 . 111 GLN HE21 H 6.6140 0.03 1 1079 . 111 GLN HE22 H 6.3520 0.03 1 1080 . 112 SER N N 117.3990 0.25 1 1081 . 112 SER H H 8.3880 0.03 1 1082 . 112 SER CA C 57.7970 0.50 1 1083 . 112 SER HA H 5.2700 0.03 1 1084 . 112 SER CB C 65.0490 0.50 1 1085 . 112 SER HB3 H 3.7400 0.03 2 1086 . 112 SER C C 174.668 0.50 1 1087 . 113 LEU N N 128.6340 0.25 1 1088 . 113 LEU H H 8.8470 0.03 1 1089 . 113 LEU CA C 57.5040 0.50 1 1090 . 113 LEU HA H 4.6500 0.03 1 1091 . 113 LEU CB C 42.9340 0.50 1 1092 . 113 LEU HB3 H 1.3700 0.03 2 1093 . 113 LEU C C 173.985 0.50 1 1094 . 114 ILE N N 127.5830 0.25 1 1095 . 114 ILE H H 8.6920 0.03 1 1096 . 114 ILE CA C 60.6500 0.50 1 1097 . 114 ILE HA H 4.1700 0.03 1 1098 . 114 ILE CB C 37.1400 0.50 1 1099 . 114 ILE HB H 1.8900 0.03 1 1100 . 114 ILE C C 176.316 0.50 1 1101 . 114 ILE HG12 H 1.5500 0.03 2 1102 . 114 ILE HG13 H 1.1100 0.03 2 1103 . 114 ILE CG2 C 17.7200 0.50 1 1104 . 114 ILE HG2 H 1.0600 0.03 1 1105 . 114 ILE CD1 C 11.5400 0.50 1 1106 . 114 ILE HD1 H 0.8600 0.03 1 1107 . 115 LEU N N 127.1480 0.25 1 1108 . 115 LEU H H 8.8160 0.03 1 1109 . 115 LEU CA C 53.2310 0.50 1 1110 . 115 LEU HA H 4.7900 0.03 1 1111 . 115 LEU CB C 45.1750 0.50 1 1112 . 115 LEU HB2 H 1.7800 0.03 2 1113 . 115 LEU C C 176.107 0.50 1 1114 . 115 LEU CG C 36.4100 0.50 1 1115 . 115 LEU HG H 1.5900 0.03 1 1116 . 115 LEU CD1 C 25.5200 0.50 1 1117 . 115 LEU HD1 H 0.5300 0.03 2 1118 . 115 LEU CD2 C 23.3100 0.50 1 1119 . 115 LEU HD2 H 0.8000 0.03 2 1120 . 116 GLN N N 119.7730 0.25 1 1121 . 116 GLN H H 8.3590 0.03 1 1122 . 116 GLN CA C 55.8060 0.50 1 1123 . 116 GLN HA H 4.3700 0.03 1 1124 . 116 GLN CB C 28.9690 0.50 1 1125 . 116 GLN HB2 H 1.9500 0.03 2 1126 . 116 GLN HB3 H 1.8500 0.03 2 1127 . 116 GLN C C 177.702 0.50 1 1128 . 116 GLN CG C 34.0200 0.50 1 1129 . 116 GLN HG2 H 2.2700 0.03 2 1130 . 116 GLN NE2 N 112.6700 0.25 1 1131 . 116 GLN HE21 H 7.5480 0.03 1 1132 . 116 GLN HE22 H 6.8370 0.03 1 1133 . 117 ALA N N 125.8220 0.25 1 1134 . 117 ALA H H 8.4120 0.03 1 1135 . 117 ALA CA C 51.9780 0.50 1 1136 . 117 ALA HA H 4.2100 0.03 1 1137 . 117 ALA CB C 20.0170 0.50 1 1138 . 117 ALA HB H 1.2800 0.03 1 1139 . 117 ALA C C 177.278 0.50 1 1140 . 118 ASN N N 117.3560 0.25 1 1141 . 118 ASN H H 7.6420 0.03 1 1142 . 118 ASN CA C 52.4350 0.50 1 1143 . 118 ASN HA H 4.6600 0.03 1 1144 . 118 ASN CB C 39.6120 0.50 1 1145 . 118 ASN HB2 H 2.9400 0.03 2 1146 . 118 ASN HB3 H 2.8000 0.03 2 1147 . 118 ASN C C 175.931 0.50 1 1148 . 118 ASN ND2 N 111.9440 0.25 1 1149 . 118 ASN HD21 H 7.5000 0.03 1 1150 . 118 ASN HD22 H 6.7360 0.03 1 1151 . 119 GLU N N 120.1790 0.25 1 1152 . 119 GLU H H 8.7580 0.03 1 1153 . 119 GLU CA C 58.6670 0.50 1 1154 . 119 GLU HA H 4.0000 0.03 1 1155 . 119 GLU CB C 29.7050 0.50 1 1156 . 119 GLU HB2 H 1.9400 0.03 2 1157 . 119 GLU C C 177.249 0.50 1 1158 . 119 GLU CG C 36.4100 0.50 1 1159 . 119 GLU HG2 H 2.2200 0.03 2 1160 . 120 GLU N N 118.0830 0.25 1 1161 . 120 GLU H H 8.1360 0.03 1 1162 . 120 GLU CA C 58.2450 0.50 1 1163 . 120 GLU HA H 4.0300 0.03 1 1164 . 120 GLU CB C 29.9120 0.50 1 1165 . 120 GLU HB2 H 1.8500 0.03 2 1166 . 120 GLU C C 177.284 0.50 1 1167 . 120 GLU CG C 36.6500 0.50 1 1168 . 120 GLU HG2 H 2.1300 0.03 2 1169 . 121 LEU N N 116.8510 0.25 1 1170 . 121 LEU H H 7.6860 0.03 1 1171 . 121 LEU CA C 54.6640 0.50 1 1172 . 121 LEU HA H 4.3100 0.03 1 1173 . 121 LEU CB C 43.3930 0.50 1 1174 . 121 LEU HB2 H 1.4700 0.03 2 1175 . 121 LEU C C 177.334 0.50 1 1176 . 121 LEU CG C 25.3900 0.50 1 1177 . 121 LEU HG H 1.3500 0.03 1 1178 . 121 LEU CD1 C 25.39000 0.50 1 1179 . 121 LEU HD1 H 0.8000 0.03 2 1180 . 121 LEU CD2 C 22.3500 0.50 1 1181 . 121 LEU HD2 H 0.7300 0.03 2 1182 . 122 CYS N N 118.3520 0.25 1 1183 . 122 CYS H H 7.8540 0.03 1 1184 . 122 CYS CA C 56.6280 0.50 1 1185 . 122 CYS HA H 4.4400 0.03 1 1186 . 122 CYS CB C 27.8670 0.50 1 1187 . 122 CYS HB2 H 2.5100 0.03 2 1188 . 122 CYS C C 177.35 0.50 1 1189 . 123 PRO CA C 63.2580 0.50 1 1190 . 123 PRO HA H 4.4400 0.03 1 1191 . 123 PRO CB C 31.8340 0.50 1 1192 . 123 PRO HB2 H 2.0500 0.03 2 1193 . 123 PRO HB3 H 2.4600 0.03 2 1194 . 123 PRO C C 177.052 0.50 1 1195 . 123 PRO CG C 27.0700 0.50 1 1196 . 123 PRO HG2 H 1.9600 0.03 2 1197 . 123 PRO CD C 50.5500 0.50 1 1198 . 123 PRO HD2 H 2.5200 0.03 2 1199 . 124 LYS N N 121.0770 0.25 1 1200 . 124 LYS H H 8.4240 0.03 1 1201 . 124 LYS CA C 56.8410 0.50 1 1202 . 124 LYS HA H 4.0830 0.03 1 1203 . 124 LYS CB C 32.9570 0.50 1 1204 . 124 LYS HB2 H 1.7100 0.03 2 1205 . 124 LYS C C 176.987 0.50 1 1206 . 124 LYS CG C 25.1500 0.50 1 1207 . 124 LYS HG2 H 1.3700 0.03 2 1208 . 124 LYS CD C 28.9800 0.50 1 1209 . 124 LYS HD2 H 1.5900 0.03 2 1210 . 124 LYS CE C 42.1700 0.50 1 1211 . 124 LYS HE2 H 2.9100 0.03 2 1212 . 125 LYS N N 121.2530 0.25 1 1213 . 125 LYS H H 8.2110 0.03 1 1214 . 125 LYS CA C 56.5080 0.50 1 1215 . 125 LYS HA H 4.2000 0.03 1 1216 . 125 LYS CB C 33.0230 0.50 1 1217 . 125 LYS HB2 H 1.7000 0.03 2 1218 . 125 LYS C C 176.666 0.50 1 1219 . 125 LYS CG C 24.9100 0.50 1 1220 . 125 LYS HG2 H 1.3100 0.03 2 1221 . 125 LYS CD C 28.9800 0.50 1 1222 . 125 LYS HD2 H 1.6000 0.03 2 1223 . 125 LYS CE C 42.1700 0.50 1 1224 . 125 LYS HE2 H 2.9000 0.03 2 1225 . 126 LEU N N 122.4080 0.25 1 1226 . 126 LEU H H 8.0870 0.03 1 1227 . 126 LEU CA C 55.0660 0.50 1 1228 . 126 LEU HA H 3.9300 0.03 1 1229 . 126 LEU CB C 42.3320 0.50 1 1230 . 126 LEU HB2 H 2.8700 0.03 2 1231 . 126 LEU C C 173.220 0.50 1 1232 . 126 LEU CG C 28.1600 0.50 1 1233 . 126 LEU HG H 0.7500 0.03 1 1234 . 126 LEU CD1 C 25.0300 0.50 1 1235 . 126 LEU HD1 H -0.0200 0.03 2 1236 . 126 LEU CD2 C 24.4100 0.50 1 1237 . 126 LEU HD2 H -0.1800 0.03 2 1238 . 127 LEU N N 122.8390 0.25 1 1239 . 127 LEU H H 8.7070 0.03 1 1240 . 127 LEU CA C 54.8400 0.50 1 1241 . 127 LEU HA H 4.3300 0.03 1 1242 . 127 LEU CB C 42.7900 0.50 1 1243 . 127 LEU HB2 H 1.5200 0.03 2 1244 . 127 LEU C C 176.665 0.50 1 1245 . 127 LEU CG C 26.8300 0.50 1 1246 . 127 LEU HG H 1.0400 0.03 1 1247 . 127 LEU CD1 C 24.9100 0.50 1 1248 . 127 LEU HD1 H 0.7800 0.03 2 1249 . 127 LEU CD2 C 23.4700 0.50 1 1250 . 127 LEU HD2 H 0.6200 0.03 2 1251 . 128 LEU N N 124.0990 0.25 1 1252 . 128 LEU H H 8.1080 0.03 1 1253 . 128 LEU CA C 52.8810 0.50 1 1254 . 128 LEU HA H 4.5800 0.03 1 1255 . 128 LEU CB C 41.8770 0.50 1 1256 . 128 LEU HB3 H 1.5800 0.03 2 1257 . 128 LEU C C 176.65 0.50 1 1258 . 128 LEU CG C 27.2200 0.50 1 1259 . 128 LEU HG H 1.4800 0.03 1 1260 . 128 LEU CD1 C 22.3700 0.50 1 1261 . 128 LEU HD2 H 0.8300 0.03 2 1262 . 129 PRO CA C 61.4500 0.50 1 1263 . 129 PRO HA H 4.4400 0.03 1 1264 . 129 PRO CB C 29.5800 0.50 1 1265 . 129 PRO HB2 H 2.2500 0.03 2 1266 . 129 PRO C C 178.361 0.50 1 1267 . 129 PRO HG2 H 1.8500 0.03 2 1268 . 129 PRO HG3 H 1.8900 0.03 2 1269 . 129 PRO HD2 H 3.7600 0.03 2 1270 . 129 PRO HD3 H 3.5600 0.03 2 1271 . 130 SER N N 112.0910 0.25 1 1272 . 130 SER H H 8.5260 0.03 1 1273 . 130 SER CA C 61.9150 0.50 1 1274 . 130 SER HA H 4.4400 0.03 1 1275 . 130 SER CB C 69.6700 0.50 1 1276 . 130 SER HB2 H 3.7900 0.03 2 1277 . 130 SER HB3 H 3.8600 0.03 2 1278 . 130 SER C C 174.535 0.50 1 1279 . 131 SER N N 122.5770 0.25 1 1280 . 131 SER H H 8.1960 0.03 1 1281 . 131 SER CA C 61.8790 0.50 1 1282 . 131 SER HA H 4.0600 0.03 1 1283 . 131 SER CB C 69.5060 0.50 1 1284 . 131 SER HB2 H 3.3400 0.03 2 1285 . 131 SER HB3 H 3.7200 0.03 2 1286 . 131 SER C C 174.599 0.50 1 1287 . 132 LYS N N 123.5290 0.25 1 1288 . 132 LYS H H 8.3670 0.03 1 1289 . 132 LYS CA C 56.3420 0.50 1 1290 . 132 LYS HA H 4.2800 0.03 1 1291 . 132 LYS CB C 33.1240 0.50 1 1292 . 132 LYS HB2 H 1.7100 0.03 2 1293 . 132 LYS C C 176.451 0.50 1 1294 . 132 LYS CG C 24.9100 0.50 1 1295 . 132 LYS HG2 H 1.3500 0.03 2 1296 . 132 LYS CD C 28.9800 0.50 1 1297 . 132 LYS HD2 H 1.6000 0.03 2 1298 . 132 LYS CE C 41.9300 0.50 1 1299 . 132 LYS HE2 H 2.9100 0.03 2 1300 . 133 THR N N 115.6760 0.25 1 1301 . 133 THR H H 8.1540 0.03 1 1302 . 133 THR CA C 61.9740 0.50 1 1303 . 133 THR HA H 4.3600 0.03 1 1304 . 133 THR CB C 69.7040 0.50 1 1305 . 133 THR HB H 4.6300 0.03 1 1306 . 133 THR C C 174.535 0.50 1 1307 . 133 THR CG2 C 21.55 0.50 1 1308 . 133 THR HG2 H 1.1100 0.03 1 1309 . 134 VAL N N 122.5770 0.25 1 1310 . 134 VAL H H 8.1960 0.03 1 1311 . 134 VAL CA C 62.0840 0.50 1 1312 . 134 VAL HA H 4.1400 0.03 1 1313 . 134 VAL CB C 33.0300 0.50 1 1314 . 134 VAL HB H 2.0100 0.03 1 1315 . 134 VAL C C 176.391 0.50 1 1316 . 134 VAL CG1 C 20.5900 0.50 1 1317 . 134 VAL HG1 H 0.8600 0.03 2 1318 . 134 VAL CG2 C 20.2500 0.50 1 1319 . 134 VAL HG2 H 0.7600 0.03 2 1320 . 135 SER N N 119.5400 0.25 1 1321 . 135 SER H H 8.4260 0.03 1 1322 . 135 SER CA C 58.0090 0.50 1 1323 . 135 SER HA H 4.3500 0.03 1 1324 . 135 SER CB C 63.6900 0.50 1 1325 . 135 SER HB2 H 3.8500 0.03 2 1326 . 135 SER C C 174.760 0.50 1 1327 . 136 SER N N 122.2640 0.25 1 1328 . 136 SER H H 8.4220 0.03 1 1329 . 136 SER CA C 58.5950 0.50 1 1330 . 136 SER HA H 4.4600 0.03 1 1331 . 136 SER CB C 63.8680 0.50 1 1332 . 136 SER HB2 H 3.8500 0.03 2 1333 . 136 SER C C 175.101 0.50 1 1334 . 137 GLY N N 111.2050 0.25 1 1335 . 137 GLY H H 8.6970 0.03 1 1336 . 137 GLY CA C 45.4860 0.50 1 1337 . 137 GLY HA2 H 3.9700 0.03 2 1338 . 137 GLY C C 174.299 0.50 1 1339 . 138 THR N N 113.8740 0.25 1 1340 . 138 THR H H 8.0520 0.03 1 1341 . 138 THR CA C 61.7920 0.50 1 1342 . 138 THR HA H 4.3200 0.03 1 1343 . 138 THR CB C 69.7040 0.50 1 1344 . 138 THR HB H 4.6300 0.03 1 1345 . 138 THR C C 174.599 0.50 1 1346 . 138 THR CG2 C 21.5500 0.50 1 1347 . 138 THR HG2 H 1.1100 0.03 1 1348 . 139 LYS N N 123.5290 0.25 1 1349 . 139 LYS H H 8.3670 0.03 1 1350 . 139 LYS CA C 56.3420 0.50 1 1351 . 139 LYS HA H 4.2800 0.03 1 1352 . 139 LYS CB C 33.1240 0.50 1 1353 . 139 LYS HB2 H 1.7100 0.03 2 1354 . 139 LYS C C 176.402 0.50 1 1355 . 139 LYS CG C 24.6700 0.50 1 1356 . 139 LYS HG2 H 1.3500 0.03 2 1357 . 139 LYS CD C 28.9800 0.50 1 1358 . 139 LYS HD2 H 1.6000 0.03 2 1359 . 139 LYS CE C 42.1700 0.50 1 1360 . 139 LYS HE2 H 2.9100 0.03 2 1361 . 140 GLU N N 121.6730 0.25 1 1362 . 140 GLU H H 8.3750 0.03 1 1363 . 140 GLU CA C 56.5080 0.50 1 1364 . 140 GLU HA H 4.3100 0.03 1 1365 . 140 GLU CB C 30.3770 0.50 1 1366 . 140 GLU HB2 H 1.8800 0.03 2 1367 . 140 GLU HB3 H 1.7900 0.03 2 1368 . 140 GLU C C 176.145 0.50 1 1369 . 140 GLU CG C 36.1700 0.50 1 1370 . 140 GLU HG2 H 2.1000 0.03 2 1371 . 141 HIS N N 120.1160 0.25 1 1372 . 141 HIS H H 8.2780 0.03 1 1373 . 141 HIS CA C 56.5080 0.50 1 1374 . 141 HIS HA H 4.4700 0.03 1 1375 . 141 HIS CB C 30.8700 0.50 1 1376 . 141 HIS HB3 H 2.9100 0.03 2 1377 . 141 HIS C C 176.369 0.50 1 1378 . 141 HIS CE1 C 139.12 0.50 1 1379 . 141 HIS HE1 H 7.62 0.03 1 1380 . 141 HIS CD2 C 117.75 0.50 1 1381 . 141 HIS HD2 H 6.75 0.03 1 1382 . 142 CYS N N 122.055 0.25 1 1383 . 142 CYS H H 8.027 0.03 1 1384 . 142 CYS CA C 58.3490 0.50 1 1385 . 142 CYS HA H 4.4700 0.03 1 1386 . 142 CYS CB C 28.0960 0.50 1 1387 . 142 CYS HB2 H 2.9000 0.03 2 1388 . 142 CYS C C 173.945 0.50 1 1389 . 143 TYR N N 122.7340 0.25 1 1390 . 143 TYR H H 8.2900 0.03 1 1391 . 143 TYR CA C 57.7080 0.50 1 1392 . 143 TYR HA H 4.5800 0.03 1 1393 . 143 TYR CB C 38.7150 0.50 1 1394 . 143 TYR HB2 H 3.2200 0.03 2 1395 . 143 TYR HB3 H 2.8100 0.03 2 1396 . 143 TYR C C 174.68 0.50 1 1397 . 143 TYR CD1 C 130.46 0.50 3 1398 . 143 TYR HD1 H 7.36 0.03 3 1399 . 143 TYR CE1 C 118.76 0.50 3 1400 . 143 TYR HE1 H 6.83 0.03 3 1401 . 144 ASN N N 124.9280 0.25 1 1402 . 144 ASN H H 7.9410 0.03 1 1403 . 144 ASN CA C 54.9010 0.50 1 1404 . 144 ASN HA H 4.4100 0.03 1 1405 . 144 ASN CB C 40.6800 0.50 1 1406 . 144 ASN HB2 H 2.7000 0.03 2 1407 . 144 ASN HB3 H 2.6100 0.03 2 1408 . 144 ASN C C 174.67 0.50 1 1409 . 144 ASN ND2 N 112.3080 0.25 1 1410 . 144 ASN HD21 H 7.4400 0.03 1 1411 . 144 ASN HD22 H 6.7410 0.03 1 stop_ save_