data_4737 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The Structure of the Transcriptional Antiterminator NusB from Escherichia Coli ; _BMRB_accession_number 4737 _BMRB_flat_file_name bmr4737.str _Entry_type original _Submission_date 2000-05-10 _Accession_date 2000-05-10 _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 Altieri Amanda S. . 2 Mazzulla Marie J. . 3 Horita David A. . 4 Coats R. Heath . 5 Wingfield Paul T. . 6 Das Asis . . 7 Court Donald L. . 8 Byrd R. Andrew . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 787 "13C chemical shifts" 474 "15N chemical shifts" 136 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-06-13 original author . stop_ _Original_release_date 2000-06-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The Structure of the Transcriptional Antiterminator NusB from Escherichia Coli' _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 Altieri Amanda S. . 2 Mazzulla Marie J. . 3 Horita David A. . 4 Coats R. Heath . 5 Wingfield Paul T. . 6 Das Asis . . 7 Court Donald L. . 8 Byrd R. Andrew . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_volume 7 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 470 _Page_last 474 _Year 2000 _Details . loop_ _Keyword antiterminator 'transcriptional regulator' 'RNA-binding protein' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_cit_1 _Saveframe_category citation _Citation_full 'Reference: A.S. Altieri et. al., FEBS Lett., 415,221-226 (1997)' _Citation_title 'Sequential assignments and secondary structure of the RNA-binding transcriptional regulator NusB.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9351000 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Altieri 'A. S.' S. . 2 Mazzulla 'M. J.' J. . 3 Zhou H. . . 4 Costantino N. . . 5 Court 'D. L.' L. . 6 Byrd 'R. A.' A. . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_name_full 'FEBS letters' _Journal_volume 415 _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 221 _Page_last 226 _Year 1997 _Details ; The NusB protein is involved in transcriptional regulation in bacteriophage lambda. NusB binds to the RNA form of the nut site and along with N, NusA, NusE and NusG, stabilizes the RNA polymerase transcription complex and allows stable, persistent antitermination. NusB contains a 10 residue Arg-rich RNA-binding motif (ARM) at the N-terminus but is not sequentially homologous to any other proteins. In contrast to other known ARM-containing proteins, NusB forms a stable structure in solution in the absence of RNA. NMR spectroscopy was used to determine that NusB contains six alpha-helices: R10-Q21, 127-F34, V45-L65, Q79-S93, Y100-F114 and D118-L127. The structure of NusB makes it a member of a newly emerging class of alpha-helical RNA-binding proteins. ; save_ save_cit_2 _Saveframe_category citation _Citation_full 'Kraulis, P.J., J. Magn. Reson. 84, 627-633 (1989)' _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_cit_3 _Saveframe_category citation _Citation_full ; "Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J. and Bax, A., J. Biomol. NMR, 6, 277-293 (1995)" ; _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F. . . 2 Grzesiek S. . . 3 Vuister 'G. W.' W. . 4 Zhu G. . . 5 Pfeifer J. . . 6 Bax A. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 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 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ save_cit_4 _Saveframe_category citation _Citation_full . _Citation_title 'Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8142349 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kraulis 'P. J.' J. . 2 Domaille 'P. J.' J. . 3 Campbell-Burk 'S. L.' L. . 4 'Van Aken' T. . . 5 Laue 'E. D.' D. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 33 _Journal_issue 12 _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 3515 _Page_last 3531 _Year 1994 _Details ; A high-resolution solution structure of the GDP form of a truncated version of the ras p21 protein (residues 1-166) has been determined using NMR spectroscopy. Ras p21 is the product of the human ras protooncogene and a member of a ubiquitous eukaryotic gene family which is highly conserved in evolution. A virtually complete assignment (13C, 15N, and 1H), including stereospecific assignments of 54 C beta methylene protons and 10 C gamma methyl protons of valine residues, was obtained by analysis of three- and four-dimensional (3D and 4D) heteronuclear NMR spectra using a newly developed 3D/4D version of the ANSIG software. A total of 40 converged structures were computed from 3369 experimental restraints consisting of 3,167 nuclear Overhauser effect (NOE) derived distances, 14 phi and 54 chi 1 torsion angle restraints, 109 hydrogen bond distance restraints, and an additional 25 restraints derived from literature data defining interactions between the GDP ligand, the magnesium ion, and the protein. The structure in the region of residues 58-66 (loop L4), and to a lesser degree residues 30-38 (loop L2), is ill-defined. Analysis of the dynamics of the backbone 15N nuclei in the protein showed that residues within the regions 58-66, 107-109, and, to a lesser degree, 30-38 are dynamically mobile on the nanosecond time scale. The root mean square (rms) deviations between the 40 solution structures and the mean atomic coordinates are 0.78 A for the backbone heavy atoms and 1.29 A for all non-hydrogen atoms if all residues (1-166) are included in the analysis. If residues 30-38 and residues 58-66 are excluded from the analysis, the rms deviations are reduced to 0.55 and 1.00 A, respectively. The structure was compared to the most highly refined X-ray crystal structure of ras p21.GDP (1-189) [Milburn, M. V., Tong, L., de Vos, A. M., Brunger, A. T., Yamaizumi, Z., Nishimura, S., & Kim, S.-H. (1990) Science 24, 939-945]. The structures are very similar except in the regions found to be mobile by NMR spectroscopy. In addition, the second alpha-helix (helix-2) has a slightly different orientation. The rms deviation between the average of the solution structures and the X-ray crystal structure is 0.94 A for the backbone heavy atoms if residues 31-37 and residues 59-73 are excluded from the analysis. ; save_ ################################## # Molecular system description # ################################## save_system_NusB _Saveframe_category molecular_system _Mol_system_name NusB _Abbreviation_common NusB _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label NusB $NusB stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'transcriptional antitermination' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_NusB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common NusB _Abbreviation_common NusB _Molecular_mass 15691 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 139 _Mol_residue_sequence ; MKPAARRRARECAVQALYSW QLSQNDIADVEYQFLAEQDV KDVDVLYFRELLAGVATNTA YLDGLMKPYLSRLLEELGQV EKAVLRIALYELSKRSDVPY KVAINEAIELAKSFGAEDSH KFVNGVLDKAAPVIRPNKK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 PRO 4 ALA 5 ALA 6 ARG 7 ARG 8 ARG 9 ALA 10 ARG 11 GLU 12 CYS 13 ALA 14 VAL 15 GLN 16 ALA 17 LEU 18 TYR 19 SER 20 TRP 21 GLN 22 LEU 23 SER 24 GLN 25 ASN 26 ASP 27 ILE 28 ALA 29 ASP 30 VAL 31 GLU 32 TYR 33 GLN 34 PHE 35 LEU 36 ALA 37 GLU 38 GLN 39 ASP 40 VAL 41 LYS 42 ASP 43 VAL 44 ASP 45 VAL 46 LEU 47 TYR 48 PHE 49 ARG 50 GLU 51 LEU 52 LEU 53 ALA 54 GLY 55 VAL 56 ALA 57 THR 58 ASN 59 THR 60 ALA 61 TYR 62 LEU 63 ASP 64 GLY 65 LEU 66 MET 67 LYS 68 PRO 69 TYR 70 LEU 71 SER 72 ARG 73 LEU 74 LEU 75 GLU 76 GLU 77 LEU 78 GLY 79 GLN 80 VAL 81 GLU 82 LYS 83 ALA 84 VAL 85 LEU 86 ARG 87 ILE 88 ALA 89 LEU 90 TYR 91 GLU 92 LEU 93 SER 94 LYS 95 ARG 96 SER 97 ASP 98 VAL 99 PRO 100 TYR 101 LYS 102 VAL 103 ALA 104 ILE 105 ASN 106 GLU 107 ALA 108 ILE 109 GLU 110 LEU 111 ALA 112 LYS 113 SER 114 PHE 115 GLY 116 ALA 117 GLU 118 ASP 119 SER 120 HIS 121 LYS 122 PHE 123 VAL 124 ASN 125 GLY 126 VAL 127 LEU 128 ASP 129 LYS 130 ALA 131 ALA 132 PRO 133 VAL 134 ILE 135 ARG 136 PRO 137 ASN 138 LYS 139 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-20 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 17526 NusB 100.00 139 99.28 99.28 3.52e-93 PDB 1EY1 "Solution Structure Of Escherichia Coli Nusb" 100.00 139 100.00 100.00 2.59e-94 PDB 3D3B "Structural And Functional Analysis Of The E. Coli Nusb-s10 Transcription Antitermination Complex." 100.00 141 99.28 100.00 7.80e-94 PDB 3D3C "Structural And Functional Analysis Of The E. Coli Nusb-S10 Transcription Antitermination Complex" 100.00 141 99.28 100.00 7.80e-94 PDB 3IMQ "Crystal Structure Of The Nusb101-S10(Delta Loop) Complex" 100.00 141 98.56 100.00 3.97e-93 DBJ BAB33892 "transcription termination factor NusB [Escherichia coli O157:H7 str. Sakai]" 100.00 139 100.00 100.00 2.59e-94 DBJ BAE76196 "transcription antitermination protein [Escherichia coli str. K12 substr. W3110]" 100.00 139 100.00 100.00 2.59e-94 DBJ BAG75962 "N utilization substance protein B [Escherichia coli SE11]" 100.00 139 100.00 100.00 2.59e-94 DBJ BAI23787 "transcription antitermination protein NusB [Escherichia coli O26:H11 str. 11368]" 100.00 139 100.00 100.00 2.59e-94 DBJ BAI29258 "transcription antitermination protein NusB [Escherichia coli O103:H2 str. 12009]" 100.00 139 100.00 100.00 2.59e-94 EMBL CAA25289 "unnamed protein product [Escherichia coli]" 100.00 139 100.00 100.00 2.59e-94 EMBL CAA45737 "nusB (ssyB) [Escherichia coli K-12]" 100.00 139 100.00 100.00 2.59e-94 EMBL CAC44764 "N utilisation substance protein B [Expression vector pNCO113-nusB/nusE]" 100.00 139 100.00 100.00 2.59e-94 EMBL CAP74950 "N utilization substance protein B [Escherichia coli LF82]" 100.00 139 100.00 100.00 2.59e-94 EMBL CAQ30885 "transcription antitermination protein NusB, subunit of NusB-NusE complex [Escherichia coli BL21(DE3)]" 100.00 139 100.00 100.00 2.59e-94 GB AAA24228 "nusB [Escherichia coli]" 100.00 139 100.00 100.00 2.59e-94 GB AAB40172 "N utilization substance protein B [Escherichia coli]" 100.00 139 100.00 100.00 2.59e-94 GB AAB95441 "NUSB [Shigella flexneri]" 72.66 101 99.01 99.01 9.50e-64 GB AAC73519 "transcription antitermination protein [Escherichia coli str. K-12 substr. MG1655]" 100.00 139 100.00 100.00 2.59e-94 GB AAG54765 "transcription termination; L factor [Escherichia coli O157:H7 str. EDL933]" 100.00 139 100.00 100.00 2.59e-94 PRF 2111328A "NusB protein" 100.00 139 100.00 100.00 2.59e-94 REF NP_308496 "transcription antitermination protein NusB [Escherichia coli O157:H7 str. Sakai]" 100.00 139 100.00 100.00 2.59e-94 REF NP_414950 "transcription antitermination protein [Escherichia coli str. K-12 substr. MG1655]" 100.00 139 100.00 100.00 2.59e-94 REF NP_459413 "transcription antitermination protein NusB [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 139 97.12 100.00 1.10e-92 REF NP_706304 "transcription antitermination protein NusB [Shigella flexneri 2a str. 301]" 100.00 139 100.00 100.00 2.59e-94 REF WP_000801121 "MULTISPECIES: N utilization substance protein B [Escherichia]" 100.00 139 99.28 100.00 3.59e-94 SP A7ZIG9 "RecName: Full=N utilization substance protein B homolog; Short=Protein NusB" 100.00 139 100.00 100.00 2.59e-94 SP A7ZX68 "RecName: Full=N utilization substance protein B homolog; Short=Protein NusB" 100.00 139 100.00 100.00 2.59e-94 SP A8AK38 "RecName: Full=N utilization substance protein B homolog; Short=Protein NusB" 100.00 139 97.12 100.00 1.10e-92 SP A9MM45 "RecName: Full=N utilization substance protein B homolog; Short=Protein NusB" 100.00 139 97.12 100.00 1.10e-92 SP A9MX13 "RecName: Full=N utilization substance protein B homolog; Short=Protein NusB" 100.00 139 97.12 100.00 1.10e-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 _Cell_line _Plasmid $NusB 'E. coli' 562 Eubacteria . Escherichia coli NC198 pJL6 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 _Details $NusB 'recombinant technology' . . . . . cit_1 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 $NusB . mM 0.7 1.2 [U-15N] 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 $NusB . mM 0.7 1.2 '[U-2H; U-15N]' 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 $NusB . mM 0.7 1.2 '[U-15N; U-13C]' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.7 loop_ _Task 'Data processing' stop_ _Details . _Citation_label $cit_2 save_ save_Ansig _Saveframe_category software _Name Ansig _Version 3.3 loop_ _Task 'Data analysis' 'graphical display' stop_ _Details . _Citation_label $cit_3 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity Plus' _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label . save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label . save_ save_3D_C(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label . save_ save_3D_H(CCO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label . save_ save_3D_HCCH-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label . save_ save_2D_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label . save_ save_2D_1H-13C_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label . save_ save_2D_CB(CGCD)HD_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CB(CGCD)HD' _Sample_label . save_ save_2D_CB(CGCDCE)HE_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CB(CGCDCE)HE' _Sample_label . save_ save_3D_1H-(15N,13C)-NOESY-HMQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-(15N,13C)-NOESY-HMQC' _Sample_label . save_ save_4D_1H-15N-15N-1H_NOESY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 1H-15N-15N-1H NOESY' _Sample_label . save_ save_4D_1H-13C-15N-1H_NOESY_12 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 1H-13C-15N-1H NOESY' _Sample_label . save_ save_4D_1H-13C-13C-1H_NOESY_13 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 1H-13C-13C-1H NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _BMRB_pulse_sequence_accession_number . _Details 'Nalorac 8mm or 5mm Z-axis PFG probes were used.' save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _BMRB_pulse_sequence_accession_number . _Details 'Nalorac 8mm or 5mm Z-axis PFG probes were used.' save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _BMRB_pulse_sequence_accession_number . _Details 'Nalorac 8mm or 5mm Z-axis PFG probes were used.' save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _BMRB_pulse_sequence_accession_number . _Details 'Nalorac 8mm or 5mm Z-axis PFG probes were used.' save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _BMRB_pulse_sequence_accession_number . _Details 'Nalorac 8mm or 5mm Z-axis PFG probes were used.' save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details 'Nalorac 8mm or 5mm Z-axis PFG probes were used.' save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details 'Nalorac 8mm or 5mm Z-axis PFG probes were used.' save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CB(CGCD)HD' _BMRB_pulse_sequence_accession_number . _Details 'Nalorac 8mm or 5mm Z-axis PFG probes were used.' save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CB(CGCDCE)HE' _BMRB_pulse_sequence_accession_number . _Details 'Nalorac 8mm or 5mm Z-axis PFG probes were used.' save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-(15N,13C)-NOESY-HMQC' _BMRB_pulse_sequence_accession_number . _Details 'Nalorac 8mm or 5mm Z-axis PFG probes were used.' save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 1H-15N-15N-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details 'Nalorac 8mm or 5mm Z-axis PFG probes were used.' save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 1H-13C-15N-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details 'Nalorac 8mm or 5mm Z-axis PFG probes were used.' save_ save_NMR_spec_expt__0_13 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 1H-13C-13C-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details 'Nalorac 8mm or 5mm Z-axis PFG probes were used.' save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.1 n/a temperature 298 2 K 'ionic strength' 0.10 . 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 H2O H 1 protons ppm 4.773 internal direct cylindrical internal . . DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . 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 NusB _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 CE C 16.2430 0.0000 1 2 . 1 MET HE H 2.1180 0.0000 1 3 . 2 LYS CA C 53.7900 0.0850 1 4 . 2 LYS CB C 31.6600 0.0020 1 5 . 2 LYS HA H 4.7250 0.0050 1 6 . 2 LYS HB3 H 1.9980 0.0000 1 7 . 2 LYS HB2 H 1.8530 0.0000 1 8 . 3 PRO CA C 64.2640 0.0620 1 9 . 3 PRO CB C 31.4170 0.2920 1 10 . 3 PRO CD C 50.1310 0.0080 1 11 . 3 PRO CG C 27.0050 0.0890 1 12 . 3 PRO HA H 4.3230 0.0170 1 13 . 3 PRO HB3 H 2.3760 0.0440 1 14 . 3 PRO HB2 H 1.9780 0.0240 1 15 . 3 PRO HD3 H 3.9460 0.0000 1 16 . 3 PRO HD2 H 3.8530 0.0000 1 17 . 3 PRO HG3 H 2.1950 0.0210 1 18 . 3 PRO HG2 H 2.0580 0.0110 1 19 . 4 ALA CA C 54.0960 0.0110 1 20 . 4 ALA CB C 17.8380 0.0000 1 21 . 4 ALA HA H 4.5430 0.0170 1 22 . 4 ALA HB H 1.5000 0.0000 1 23 . 5 ALA CA C 53.3860 0.0340 1 24 . 5 ALA CB C 17.8180 0.0000 1 25 . 5 ALA HA H 4.3240 0.0040 1 26 . 5 ALA HB H 1.5540 0.0000 1 27 . 9 ALA CA C 55.5610 0.0070 1 28 . 9 ALA CB C 18.6960 0.0000 1 29 . 9 ALA HA H 4.0140 0.0140 1 30 . 9 ALA HB H 2.0180 0.0000 1 31 . 10 ARG CA C 60.4870 0.0480 1 32 . 10 ARG CB C 30.2310 0.0210 1 33 . 10 ARG CD C 43.1140 0.0000 1 34 . 10 ARG HA H 3.9470 0.0480 1 35 . 11 GLU CA C 59.4990 0.2300 1 36 . 11 GLU CB C 29.4970 0.2220 1 37 . 11 GLU CG C 36.7730 0.0000 1 38 . 11 GLU HA H 3.9080 0.0090 1 39 . 11 GLU HB3 H 2.6140 0.0000 1 40 . 11 GLU HB2 H 2.1650 0.0090 1 41 . 11 GLU HG3 H 2.7130 0.0020 1 42 . 11 GLU HG2 H 2.3830 0.0120 1 43 . 11 GLU H H 8.4930 0.0430 1 44 . 11 GLU N N 117.1130 0.1930 1 45 . 12 CYS CA C 63.3970 0.0170 1 46 . 12 CYS CB C 26.5060 0.1990 1 47 . 12 CYS HA H 4.1290 0.0210 1 48 . 12 CYS HB3 H 2.7980 0.0000 1 49 . 12 CYS HB2 H 2.1720 0.0000 1 50 . 12 CYS H H 8.3890 0.0180 1 51 . 12 CYS N N 115.3570 0.0510 1 52 . 13 ALA CA C 55.4150 0.1460 1 53 . 13 ALA CB C 17.4140 0.1760 1 54 . 13 ALA HA H 3.9990 0.0000 1 55 . 13 ALA HB H 1.4120 0.0000 1 56 . 13 ALA H H 8.7210 0.0220 1 57 . 13 ALA N N 121.2480 0.1120 1 58 . 14 VAL CA C 67.0430 0.2130 1 59 . 14 VAL CB C 30.5920 0.0550 1 60 . 14 VAL CG1 C 25.1990 0.0000 1 61 . 14 VAL CG2 C 20.3670 0.0000 1 62 . 14 VAL HA H 3.3180 0.0000 1 63 . 14 VAL HB H 1.8890 0.0000 1 64 . 14 VAL HG1 H 1.0270 0.0000 1 65 . 14 VAL HG2 H 0.4980 0.0000 1 66 . 14 VAL H H 8.3790 0.0230 1 67 . 14 VAL N N 117.7710 0.1290 1 68 . 15 GLN CA C 58.8630 0.0940 1 69 . 15 GLN CB C 29.1060 0.1070 1 70 . 15 GLN CG C 34.3980 0.0000 1 71 . 15 GLN HA H 3.8470 0.0000 1 72 . 15 GLN HB3 H 2.2780 0.0300 1 73 . 15 GLN HB2 H 2.2780 0.0300 1 74 . 15 GLN HE21 H 7.0170 0.0000 1 75 . 15 GLN HE22 H 6.8080 0.0000 1 76 . 15 GLN HG3 H 2.3270 0.0070 1 77 . 15 GLN HG2 H 2.1700 0.0050 1 78 . 15 GLN H H 6.9760 0.0190 1 79 . 15 GLN N N 115.3310 0.0500 1 80 . 15 GLN NE2 N 109.6470 0.0130 1 81 . 16 ALA CA C 54.2560 0.2170 1 82 . 16 ALA CB C 17.9900 0.1880 1 83 . 16 ALA HA H 3.9790 0.0000 1 84 . 16 ALA HB H 1.0430 0.0000 1 85 . 16 ALA H H 8.5110 0.0170 1 86 . 16 ALA N N 121.4250 0.1050 1 87 . 17 LEU CA C 57.2550 0.0840 1 88 . 17 LEU CB C 40.6740 0.0490 1 89 . 17 LEU CD1 C 25.2870 0.0000 1 90 . 17 LEU CD2 C 22.8320 0.2710 1 91 . 17 LEU CG C 26.6680 0.0000 1 92 . 17 LEU HA H 4.2740 0.0140 1 93 . 17 LEU HB3 H 2.0160 0.0000 1 94 . 17 LEU HB2 H 1.5140 0.0000 1 95 . 17 LEU HD1 H 0.7530 0.0000 1 96 . 17 LEU HD2 H 0.7530 0.0270 1 97 . 17 LEU HG H 1.7520 0.0330 1 98 . 17 LEU H H 9.0100 0.0230 1 99 . 17 LEU N N 117.2390 0.1580 1 100 . 18 TYR CA C 61.4350 0.1300 1 101 . 18 TYR CB C 37.7410 0.0380 1 102 . 18 TYR CD1 C 132.3070 0.0000 1 103 . 18 TYR CD2 C 132.3070 0.0000 1 104 . 18 TYR CE1 C 117.6760 0.0000 1 105 . 18 TYR CE2 C 117.6760 0.0000 1 106 . 18 TYR HA H 4.1160 0.0000 1 107 . 18 TYR HB3 H 3.3460 0.0000 1 108 . 18 TYR HB2 H 2.9930 0.0000 1 109 . 18 TYR HD1 H 6.9630 0.0000 1 110 . 18 TYR HD2 H 6.9630 0.0000 1 111 . 18 TYR HE1 H 6.8370 0.0000 1 112 . 18 TYR HE2 H 6.8370 0.0000 1 113 . 18 TYR H H 8.5410 0.0220 1 114 . 18 TYR N N 119.6590 0.1350 1 115 . 19 SER CA C 61.4350 0.0850 1 116 . 19 SER CB C 62.9020 0.1560 1 117 . 19 SER HA H 4.1530 0.0000 1 118 . 19 SER HB3 H 4.2250 0.0080 1 119 . 19 SER HB2 H 4.2250 0.0080 1 120 . 19 SER H H 7.6490 0.0160 1 121 . 19 SER N N 111.3020 0.0800 1 122 . 20 TRP CA C 60.2620 0.0640 1 123 . 20 TRP CB C 28.1160 0.2930 1 124 . 20 TRP CD1 C 127.0890 0.0000 1 125 . 20 TRP CE3 C 119.6720 0.0000 1 126 . 20 TRP CH2 C 123.6440 0.0000 1 127 . 20 TRP CZ2 C 114.1090 0.0000 1 128 . 20 TRP CZ3 C 119.5370 0.0000 1 129 . 20 TRP HA H 4.4140 0.0630 1 130 . 20 TRP HB3 H 3.6960 0.0000 1 131 . 20 TRP HB2 H 3.2450 0.0000 1 132 . 20 TRP HD1 H 7.3270 0.0000 1 133 . 20 TRP HE1 H 10.0310 0.0000 1 134 . 20 TRP HE3 H 7.6070 0.0000 1 135 . 20 TRP HH2 H 7.3530 0.0000 1 136 . 20 TRP H H 8.8390 0.0170 1 137 . 20 TRP HZ2 H 7.6040 0.0000 1 138 . 20 TRP HZ3 H 6.8720 0.0000 1 139 . 20 TRP N N 122.4540 0.1190 1 140 . 20 TRP NE1 N 130.2530 0.0000 1 141 . 21 GLN CA C 58.0880 0.1210 1 142 . 21 GLN CB C 27.6300 0.0000 1 143 . 21 GLN CG C 35.8860 0.0000 1 144 . 21 GLN HA H 3.3600 0.0170 1 145 . 21 GLN HB3 H 2.2730 0.0520 1 146 . 21 GLN HB2 H 2.1200 0.0050 1 147 . 21 GLN HE21 H 7.4530 0.0000 1 148 . 21 GLN HE22 H 6.5940 0.0000 1 149 . 21 GLN HG3 H 2.7350 0.0040 1 150 . 21 GLN HG2 H 2.2560 0.0040 1 151 . 21 GLN H H 9.0640 0.0410 1 152 . 21 GLN N N 118.5770 0.0380 1 153 . 21 GLN NE2 N 109.4360 0.0710 1 154 . 22 LEU CA C 56.1570 0.0300 1 155 . 22 LEU CB C 41.9210 0.0510 1 156 . 22 LEU CD1 C 24.2540 0.0310 1 157 . 22 LEU CD2 C 22.6820 0.0010 1 158 . 22 LEU CG C 26.7210 0.0000 1 159 . 22 LEU HA H 4.1140 0.0140 1 160 . 22 LEU HB3 H 1.6650 0.0000 1 161 . 22 LEU HB2 H 1.4950 0.0000 1 162 . 22 LEU HD1 H 0.5930 0.0170 1 163 . 22 LEU HD2 H 0.7390 0.0010 1 164 . 22 LEU HG H 1.4790 0.0000 1 165 . 22 LEU H H 7.3710 0.0300 1 166 . 22 LEU N N 116.2190 0.1200 1 167 . 23 SER CA C 59.2450 0.0590 1 168 . 23 SER CB C 64.1270 0.2400 1 169 . 23 SER HA H 4.3720 0.0000 1 170 . 23 SER HB3 H 3.9080 0.0000 1 171 . 23 SER HB2 H 3.9080 0.0000 1 172 . 23 SER H H 8.1460 0.0260 1 173 . 23 SER N N 113.1870 0.0870 1 174 . 24 GLN CA C 55.8810 0.0650 1 175 . 24 GLN CB C 26.2410 0.2960 1 176 . 24 GLN CG C 33.8770 0.0000 1 177 . 24 GLN HA H 3.6840 0.0000 1 178 . 24 GLN HB3 H 2.0400 0.0000 1 179 . 24 GLN HB2 H 2.0400 0.0000 1 180 . 24 GLN HE21 H 7.0610 0.0000 1 181 . 24 GLN HE22 H 5.9160 0.0000 1 182 . 24 GLN HG3 H 2.0440 0.0000 1 183 . 24 GLN HG2 H 2.0440 0.0000 1 184 . 24 GLN H H 8.5590 0.0230 1 185 . 24 GLN N N 115.8910 0.1350 1 186 . 24 GLN NE2 N 111.2450 0.0040 1 187 . 25 ASN CA C 51.9960 0.0810 1 188 . 25 ASN CB C 38.4840 0.0770 1 189 . 25 ASN HA H 4.8190 0.0000 1 190 . 25 ASN HB3 H 2.8630 0.0000 1 191 . 25 ASN HB2 H 2.8630 0.0000 1 192 . 25 ASN HD21 H 7.4550 0.0000 1 193 . 25 ASN HD22 H 6.8400 0.0000 1 194 . 25 ASN H H 7.9690 0.0200 1 195 . 25 ASN N N 116.2590 0.1210 1 196 . 25 ASN ND2 N 109.0600 0.0330 1 197 . 26 ASP CA C 54.2150 0.1990 1 198 . 26 ASP CB C 41.6530 0.0380 1 199 . 26 ASP HA H 4.7290 0.0450 1 200 . 26 ASP HB3 H 2.8600 0.0000 1 201 . 26 ASP HB2 H 2.7330 0.0000 1 202 . 26 ASP H H 8.5650 0.0210 1 203 . 26 ASP N N 118.3930 0.1520 1 204 . 27 ILE CA C 60.7050 0.2150 1 205 . 27 ILE CB C 37.5210 0.1880 1 206 . 27 ILE CD1 C 11.8360 0.0000 1 207 . 27 ILE CG1 C 26.8210 0.0630 1 208 . 27 ILE CG2 C 17.4720 0.0000 1 209 . 27 ILE HA H 3.7510 0.0000 1 210 . 27 ILE HB H 0.9850 0.0230 1 211 . 27 ILE HD1 H -0.1370 0.0000 1 212 . 27 ILE HG13 H 0.9320 0.0390 1 213 . 27 ILE HG12 H 0.6130 0.0330 1 214 . 27 ILE HG2 H 0.6260 0.0000 1 215 . 27 ILE H H 8.8030 0.0480 1 216 . 27 ILE N N 126.2510 0.0200 1 217 . 28 ALA CA C 54.4000 0.1510 1 218 . 28 ALA CB C 17.6020 0.1980 1 219 . 28 ALA HA H 4.1920 0.0000 1 220 . 28 ALA HB H 1.3750 0.0000 1 221 . 28 ALA H H 8.5660 0.0260 1 222 . 28 ALA N N 123.6640 0.2390 1 223 . 29 ASP CA C 56.6190 0.0230 1 224 . 29 ASP CB C 39.9810 0.1200 1 225 . 29 ASP HA H 4.6660 0.0000 1 226 . 29 ASP HB3 H 2.9410 0.0000 1 227 . 29 ASP HB2 H 2.8390 0.0000 1 228 . 29 ASP H H 7.4310 0.0160 1 229 . 29 ASP N N 117.2730 0.0610 1 230 . 30 VAL CA C 65.7990 0.1280 1 231 . 30 VAL CB C 31.2920 0.2160 1 232 . 30 VAL CG1 C 21.8580 0.0000 1 233 . 30 VAL CG2 C 20.8010 0.0000 1 234 . 30 VAL HA H 3.8550 0.0000 1 235 . 30 VAL HB H 2.2080 0.0000 1 236 . 30 VAL HG1 H 1.2060 0.0000 1 237 . 30 VAL HG2 H 1.0820 0.0000 1 238 . 30 VAL H H 7.6150 0.0160 1 239 . 30 VAL N N 120.3260 0.0980 1 240 . 31 GLU CA C 60.0490 0.0330 1 241 . 31 GLU CB C 29.8720 0.1860 1 242 . 31 GLU CG C 36.3080 0.2040 1 243 . 31 GLU HA H 3.6870 0.0210 1 244 . 31 GLU HB3 H 2.0720 0.0070 1 245 . 31 GLU HB2 H 2.0720 0.0070 1 246 . 31 GLU HG3 H 2.1400 0.0050 1 247 . 31 GLU HG2 H 2.0650 0.0150 1 248 . 31 GLU H H 8.4740 0.0160 1 249 . 31 GLU N N 118.9650 0.0810 1 250 . 32 TYR CA C 61.1370 0.1020 1 251 . 32 TYR CB C 37.9150 0.0970 1 252 . 32 TYR CD1 C 131.2960 0.0000 1 253 . 32 TYR CD2 C 131.2960 0.0000 1 254 . 32 TYR CE1 C 116.8420 0.0000 1 255 . 32 TYR CE2 C 116.8420 0.0000 1 256 . 32 TYR HA H 4.1610 0.0000 1 257 . 32 TYR HB3 H 3.0630 0.0000 1 258 . 32 TYR HB2 H 2.5410 0.0000 1 259 . 32 TYR HD1 H 6.9320 0.0000 1 260 . 32 TYR HD2 H 6.9320 0.0000 1 261 . 32 TYR HE1 H 6.5810 0.0000 1 262 . 32 TYR HE2 H 6.5810 0.0000 1 263 . 32 TYR H H 7.8410 0.0150 1 264 . 32 TYR N N 115.8900 0.1430 1 265 . 33 GLN CA C 58.0880 0.1970 1 266 . 33 GLN CB C 27.6250 0.0160 1 267 . 33 GLN CG C 33.1380 0.0000 1 268 . 33 GLN HA H 3.9590 0.0000 1 269 . 33 GLN HB3 H 2.2570 0.0000 1 270 . 33 GLN HB2 H 2.2570 0.0000 1 271 . 33 GLN HE21 H 7.6570 0.0000 1 272 . 33 GLN HE22 H 6.7590 0.0000 1 273 . 33 GLN HG3 H 2.5450 0.0000 1 274 . 33 GLN HG2 H 2.4110 0.0000 1 275 . 33 GLN H H 8.2310 0.0180 1 276 . 33 GLN N N 116.7070 0.2230 1 277 . 33 GLN NE2 N 110.3440 0.0030 1 278 . 34 PHE CA C 61.4500 0.1300 1 279 . 34 PHE CB C 39.2410 0.2980 1 280 . 34 PHE CD1 C 131.3190 0.0000 1 281 . 34 PHE CD2 C 131.3190 0.0000 1 282 . 34 PHE CE1 C 131.3020 0.0000 1 283 . 34 PHE CE2 C 131.3020 0.0000 1 284 . 34 PHE HA H 4.1070 0.0270 1 285 . 34 PHE HB3 H 3.2670 0.0210 1 286 . 34 PHE HB2 H 3.1760 0.0040 1 287 . 34 PHE HD1 H 7.0990 0.0000 1 288 . 34 PHE HD2 H 7.0990 0.0000 1 289 . 34 PHE HE1 H 6.9260 0.0000 1 290 . 34 PHE HE2 H 6.9260 0.0000 1 291 . 34 PHE H H 8.4430 0.0250 1 292 . 34 PHE N N 118.3400 0.0320 1 293 . 35 LEU CA C 56.1230 0.0180 1 294 . 35 LEU CB C 40.8440 0.2560 1 295 . 35 LEU CD1 C 25.2360 0.0000 1 296 . 35 LEU CD2 C 22.4240 0.0000 1 297 . 35 LEU CG C 26.6750 0.0080 1 298 . 35 LEU HA H 4.0550 0.0160 1 299 . 35 LEU HB3 H 1.8700 0.0300 1 300 . 35 LEU HB2 H 1.4660 0.0170 1 301 . 35 LEU HD1 H 0.9580 0.0000 1 302 . 35 LEU HD2 H 0.8290 0.0000 1 303 . 35 LEU HG H 2.0190 0.0090 1 304 . 35 LEU H H 8.1130 0.0180 1 305 . 35 LEU N N 114.6180 0.0720 1 306 . 36 ALA CA C 53.4220 0.1530 1 307 . 36 ALA CB C 17.9600 0.1500 1 308 . 36 ALA HA H 4.1600 0.0000 1 309 . 36 ALA HB H 1.2910 0.0000 1 310 . 36 ALA H H 7.6920 0.0150 1 311 . 36 ALA N N 118.9010 0.1280 1 312 . 37 GLU CA C 56.1510 0.0800 1 313 . 37 GLU CB C 30.9940 0.0110 1 314 . 37 GLU CG C 35.8750 0.0000 1 315 . 37 GLU HA H 4.3640 0.0000 1 316 . 37 GLU HB3 H 2.0220 0.0000 1 317 . 37 GLU HB2 H 1.9030 0.0000 1 318 . 37 GLU HG3 H 2.3570 0.0000 1 319 . 37 GLU HG2 H 2.1950 0.0000 1 320 . 37 GLU H H 7.5180 0.0210 1 321 . 37 GLU N N 113.4270 0.0810 1 322 . 38 GLN CA C 53.9400 0.1550 1 323 . 38 GLN CB C 28.5870 0.0190 1 324 . 38 GLN CG C 32.0540 0.1640 1 325 . 38 GLN HA H 4.2600 0.0220 1 326 . 38 GLN HB3 H 1.6610 0.0280 1 327 . 38 GLN HB2 H 1.4020 0.0180 1 328 . 38 GLN HE21 H 7.2300 0.0000 1 329 . 38 GLN HE22 H 6.5800 0.0000 1 330 . 38 GLN HG3 H 1.9660 0.0160 1 331 . 38 GLN HG2 H 1.2960 0.0160 1 332 . 38 GLN H H 7.6380 0.0150 1 333 . 38 GLN N N 116.4260 0.1470 1 334 . 38 GLN NE2 N 111.3990 0.0180 1 335 . 39 ASP CA C 53.5100 0.0640 1 336 . 39 ASP CB C 40.2150 0.1460 1 337 . 39 ASP HA H 4.6180 0.0000 1 338 . 39 ASP HB3 H 2.8140 0.0000 1 339 . 39 ASP HB2 H 2.5840 0.0000 1 340 . 39 ASP H H 8.3810 0.0300 1 341 . 39 ASP N N 119.6410 0.1430 1 342 . 40 VAL CA C 60.2630 0.2340 1 343 . 40 VAL CB C 30.7050 0.0510 1 344 . 40 VAL CG1 C 20.5010 0.0870 1 345 . 40 VAL CG2 C 20.5010 0.0870 1 346 . 40 VAL HA H 4.4750 0.0100 1 347 . 40 VAL HB H 2.3400 0.0000 1 348 . 40 VAL HG1 H 0.8840 0.0000 1 349 . 40 VAL HG2 H 0.7900 0.0230 1 350 . 40 VAL H H 8.2760 0.0560 1 351 . 40 VAL N N 117.7460 0.0770 1 352 . 41 LYS CA C 58.5810 0.0230 1 353 . 41 LYS CB C 31.4600 0.0390 1 354 . 41 LYS CD C 28.5710 0.0000 1 355 . 41 LYS CE C 41.3710 0.0000 1 356 . 41 LYS CG C 23.9120 0.0000 1 357 . 41 LYS HA H 4.1610 0.0000 1 358 . 41 LYS HB3 H 1.8930 0.0750 2 359 . 41 LYS HB2 H 1.8740 0.0600 2 360 . 41 LYS HD3 H 1.7440 0.0000 1 361 . 41 LYS HD2 H 1.7440 0.0000 1 362 . 41 LYS HE3 H 3.0410 0.0000 1 363 . 41 LYS HE2 H 3.0410 0.0000 1 364 . 41 LYS HG3 H 1.4650 0.0000 1 365 . 41 LYS HG2 H 1.4650 0.0000 1 366 . 41 LYS H H 8.0970 0.0150 1 367 . 41 LYS N N 121.4290 0.1420 1 368 . 42 ASP H H 8.4840 0.0230 1 369 . 42 ASP N N 116.1780 0.0940 1 370 . 43 VAL CG2 C 17.7370 0.0000 2 371 . 43 VAL HG2 H 0.8970 0.0000 2 372 . 45 VAL CA C 66.2850 0.0490 1 373 . 45 VAL CB C 31.4840 0.0440 1 374 . 45 VAL CG1 C 22.3250 0.0000 1 375 . 45 VAL CG2 C 21.0680 0.0000 1 376 . 45 VAL HA H 3.6510 0.0000 1 377 . 45 VAL HB H 2.1810 0.0000 1 378 . 45 VAL HG1 H 1.1010 0.0000 1 379 . 45 VAL HG2 H 1.1010 0.0000 1 380 . 45 VAL H H 8.0640 0.0000 1 381 . 45 VAL N N 127.4320 0.0000 1 382 . 46 LEU CA C 58.0960 0.0990 1 383 . 46 LEU CB C 40.2250 0.2810 1 384 . 46 LEU CD1 C 23.7250 0.0000 1 385 . 46 LEU CD2 C 23.7250 0.0000 1 386 . 46 LEU CG C 26.6620 0.0000 1 387 . 46 LEU HA H 4.1560 0.0060 1 388 . 46 LEU HB3 H 1.8050 0.0550 1 389 . 46 LEU HB2 H 1.8050 0.0490 1 390 . 46 LEU HD1 H 0.9720 0.0280 1 391 . 46 LEU HD2 H 0.9720 0.0120 1 392 . 46 LEU HG H 1.7550 0.0370 1 393 . 46 LEU H H 8.0920 0.0120 1 394 . 46 LEU N N 119.2080 0.0400 1 395 . 47 TYR CA C 61.0900 0.2200 1 396 . 47 TYR CB C 38.0900 0.1800 1 397 . 47 TYR CD1 C 132.8910 0.1120 1 398 . 47 TYR CD2 C 132.8910 0.1120 1 399 . 47 TYR CE1 C 117.8550 0.0000 1 400 . 47 TYR CE2 C 117.8550 0.0000 1 401 . 47 TYR HA H 4.1710 0.0000 1 402 . 47 TYR HB3 H 3.3250 0.0000 1 403 . 47 TYR HB2 H 3.1910 0.0000 1 404 . 47 TYR HD1 H 7.1690 0.0040 1 405 . 47 TYR HD2 H 7.1690 0.0040 1 406 . 47 TYR HE1 H 6.8270 0.0000 1 407 . 47 TYR HE2 H 6.8270 0.0000 1 408 . 47 TYR H H 7.9000 0.0220 1 409 . 47 TYR N N 119.8010 0.1060 1 410 . 48 PHE CA C 60.6480 0.2200 1 411 . 48 PHE CB C 38.2010 0.1910 1 412 . 48 PHE CD1 C 131.3440 0.0000 1 413 . 48 PHE CD2 C 131.3440 0.0000 1 414 . 48 PHE CE1 C 130.6900 0.0580 1 415 . 48 PHE CE2 C 130.6900 0.0580 1 416 . 48 PHE CZ C 130.4980 0.0000 1 417 . 48 PHE HA H 3.9740 0.0230 1 418 . 48 PHE HB3 H 3.4700 0.0520 1 419 . 48 PHE HB2 H 3.0790 0.0280 1 420 . 48 PHE HD1 H 7.1960 0.0000 1 421 . 48 PHE HD2 H 7.1960 0.0000 1 422 . 48 PHE HE1 H 7.2510 0.0010 1 423 . 48 PHE HE2 H 7.2510 0.0010 1 424 . 48 PHE H H 8.2150 0.0290 1 425 . 48 PHE HZ H 7.0350 0.0000 1 426 . 48 PHE N N 116.5830 0.2120 1 427 . 49 ARG CA C 59.7040 0.1540 1 428 . 49 ARG CB C 29.5440 0.2500 1 429 . 49 ARG CD C 43.5740 0.0000 1 430 . 49 ARG CG C 27.7780 0.0000 1 431 . 49 ARG HA H 3.3190 0.0270 1 432 . 49 ARG HB3 H 1.8940 0.0240 1 433 . 49 ARG HB2 H 1.8940 0.0240 1 434 . 49 ARG HD3 H 3.1720 0.0120 1 435 . 49 ARG HD2 H 3.1720 0.0120 1 436 . 49 ARG HE H 7.6370 0.0000 1 437 . 49 ARG HG3 H 1.5540 0.0000 1 438 . 49 ARG HG2 H 1.5540 0.0000 1 439 . 49 ARG H H 8.3260 0.0180 1 440 . 49 ARG N N 116.1540 0.2590 1 441 . 49 ARG NE N 84.4740 0.0000 1 442 . 50 GLU CA C 58.9080 0.0820 1 443 . 50 GLU CB C 28.3690 0.2280 1 444 . 50 GLU CG C 36.1670 0.0000 1 445 . 50 GLU HA H 3.8270 0.0120 1 446 . 50 GLU HB3 H 2.1200 0.0000 1 447 . 50 GLU HB2 H 1.7960 0.0530 1 448 . 50 GLU HG3 H 2.5100 0.0000 1 449 . 50 GLU HG2 H 2.0850 0.0250 1 450 . 50 GLU H H 8.0530 0.0230 1 451 . 50 GLU N N 118.8600 0.0500 1 452 . 51 LEU CA C 57.0900 0.1670 1 453 . 51 LEU CB C 42.2240 0.2640 1 454 . 51 LEU CD1 C 25.7660 0.1570 1 455 . 51 LEU CD2 C 22.2980 0.1080 1 456 . 51 LEU CG C 25.3930 0.0000 1 457 . 51 LEU HA H 3.3940 0.0100 1 458 . 51 LEU HB3 H 1.5540 0.0130 1 459 . 51 LEU HB2 H 0.7830 0.0250 1 460 . 51 LEU HD1 H 0.6760 0.0340 1 461 . 51 LEU HD2 H 0.6760 0.0000 1 462 . 51 LEU HG H 1.0790 0.0000 1 463 . 51 LEU H H 8.3230 0.0150 1 464 . 51 LEU N N 119.5230 0.1130 1 465 . 52 LEU CA C 58.0960 0.0040 1 466 . 52 LEU CB C 40.5900 0.0750 1 467 . 52 LEU CD1 C 23.3730 0.0000 1 468 . 52 LEU CD2 C 23.3730 0.0000 1 469 . 52 LEU CG C 26.3340 0.0000 1 470 . 52 LEU HA H 3.3730 0.0000 1 471 . 52 LEU HB3 H 1.0410 0.0540 1 472 . 52 LEU HB2 H 1.0410 0.0540 1 473 . 52 LEU HD1 H 0.3340 0.0000 1 474 . 52 LEU HD2 H 0.1880 0.0000 1 475 . 52 LEU HG H 1.0090 0.0000 1 476 . 52 LEU H H 7.5490 0.0230 1 477 . 52 LEU N N 116.0640 0.1620 1 478 . 53 ALA CA C 54.1980 0.0000 1 479 . 53 ALA CB C 17.1940 0.2940 1 480 . 53 ALA HA H 3.7230 0.0000 1 481 . 53 ALA HB H 1.2200 0.0000 1 482 . 53 ALA H H 7.4410 0.0250 1 483 . 53 ALA N N 116.0000 0.1760 1 484 . 54 GLY CA C 46.0100 0.2710 1 485 . 54 GLY HA3 H 3.4050 0.0000 1 486 . 54 GLY HA2 H 3.0430 0.0000 1 487 . 54 GLY H H 8.1960 0.0210 1 488 . 54 GLY N N 107.3410 0.1290 1 489 . 55 VAL CA C 65.7540 0.1980 1 490 . 55 VAL CB C 30.5210 0.0350 1 491 . 55 VAL CG1 C 22.7910 0.0000 1 492 . 55 VAL CG2 C 21.5570 0.0000 1 493 . 55 VAL HA H 3.4490 0.0140 1 494 . 55 VAL HB H 1.7750 0.0000 1 495 . 55 VAL HG1 H 0.8010 0.0000 1 496 . 55 VAL HG2 H 0.6500 0.0000 1 497 . 55 VAL H H 7.8640 0.0140 1 498 . 55 VAL N N 118.8650 0.0640 1 499 . 56 ALA CA C 54.7250 0.1150 1 500 . 56 ALA CB C 17.2480 0.2440 1 501 . 56 ALA HA H 3.8260 0.0000 1 502 . 56 ALA HB H 0.7260 0.0000 1 503 . 56 ALA H H 7.8580 0.0200 1 504 . 56 ALA N N 117.5110 0.0510 1 505 . 57 THR CA C 62.9030 0.1390 1 506 . 57 THR CB C 69.2010 0.0430 1 507 . 57 THR CG2 C 20.6180 0.0000 1 508 . 57 THR HA H 4.4200 0.0000 1 509 . 57 THR HB H 4.3130 0.0440 1 510 . 57 THR HG2 H 1.2700 0.0100 1 511 . 57 THR H H 7.7000 0.0130 1 512 . 57 THR N N 105.2030 0.0980 1 513 . 58 ASN CA C 52.9340 0.0380 1 514 . 58 ASN CB C 39.7650 0.0260 1 515 . 58 ASN HA H 5.5640 0.0000 1 516 . 58 ASN HB3 H 3.2450 0.0000 1 517 . 58 ASN HB2 H 2.8930 0.0000 1 518 . 58 ASN HD21 H 8.8230 0.0000 1 519 . 58 ASN HD22 H 7.1880 0.0000 1 520 . 58 ASN H H 7.4020 0.0300 1 521 . 58 ASN N N 117.0810 0.1090 1 522 . 58 ASN ND2 N 116.1140 0.0270 1 523 . 59 THR CA C 67.6200 0.0000 1 524 . 59 THR CB C 68.2160 0.0750 1 525 . 59 THR CG2 C 23.2650 0.0000 1 526 . 59 THR HA H 3.7500 0.0000 1 527 . 59 THR HB H 4.2080 0.0000 1 528 . 59 THR HG2 H 1.5140 0.0000 1 529 . 59 THR H H 7.7200 0.0230 1 530 . 59 THR N N 112.7250 0.0390 1 531 . 60 ALA CA C 55.1610 0.1140 1 532 . 60 ALA CB C 16.9950 0.1850 1 533 . 60 ALA HA H 4.2590 0.0000 1 534 . 60 ALA HB H 1.5120 0.0000 1 535 . 60 ALA H H 8.4670 0.0220 1 536 . 60 ALA N N 120.6300 0.1070 1 537 . 61 TYR CA C 60.0220 0.0150 1 538 . 61 TYR CB C 38.2410 0.0400 1 539 . 61 TYR CD1 C 132.4710 0.0000 1 540 . 61 TYR CD2 C 132.4710 0.0000 1 541 . 61 TYR CE1 C 117.8230 0.0000 1 542 . 61 TYR CE2 C 117.8230 0.0000 1 543 . 61 TYR HA H 4.3630 0.0000 1 544 . 61 TYR HB3 H 3.3970 0.0000 1 545 . 61 TYR HB2 H 3.0250 0.0000 1 546 . 61 TYR HD1 H 7.0890 0.0000 1 547 . 61 TYR HD2 H 7.0890 0.0000 1 548 . 61 TYR HE1 H 6.8980 0.0000 1 549 . 61 TYR HE2 H 6.8980 0.0000 1 550 . 61 TYR H H 8.1300 0.0440 1 551 . 61 TYR N N 119.4920 0.0600 1 552 . 62 LEU CA C 57.3010 0.0560 1 553 . 62 LEU CB C 41.1870 0.3200 1 554 . 62 LEU CD1 C 25.8020 0.0000 1 555 . 62 LEU CD2 C 20.6230 0.0000 1 556 . 62 LEU CG C 27.7060 0.2090 1 557 . 62 LEU HA H 3.8030 0.0000 1 558 . 62 LEU HB3 H 1.9970 0.0300 1 559 . 62 LEU HB2 H 1.3600 0.0180 1 560 . 62 LEU HD1 H 2.3640 0.0000 1 561 . 62 LEU HD2 H 1.0000 0.0000 1 562 . 62 LEU HG H 1.2100 0.0190 1 563 . 62 LEU H H 8.3450 0.0180 1 564 . 62 LEU N N 117.9300 0.1640 1 565 . 63 ASP CA C 56.6320 0.0000 1 566 . 63 ASP CB C 38.7410 0.0050 1 567 . 63 ASP HA H 4.3680 0.0000 1 568 . 63 ASP HB3 H 2.7320 0.0000 1 569 . 63 ASP HB2 H 2.5330 0.0000 1 570 . 63 ASP H H 8.9260 0.0200 1 571 . 63 ASP N N 118.9680 0.0660 1 572 . 64 GLY CA C 46.2380 0.0280 1 573 . 64 GLY HA3 H 3.9600 0.0000 1 574 . 64 GLY HA2 H 3.8030 0.0000 1 575 . 64 GLY H H 7.9610 0.0130 1 576 . 64 GLY N N 105.4840 0.1640 1 577 . 65 LEU CA C 56.1660 0.1500 1 578 . 65 LEU CB C 42.3720 0.0450 1 579 . 65 LEU CD1 C 25.0580 0.0000 1 580 . 65 LEU CD2 C 21.3490 0.0000 1 581 . 65 LEU CG C 25.1700 0.2480 1 582 . 65 LEU HA H 4.1820 0.0000 1 583 . 65 LEU HB3 H 2.1330 0.0000 1 584 . 65 LEU HB2 H 1.3070 0.0000 1 585 . 65 LEU HD1 H 0.7210 0.0000 1 586 . 65 LEU HD2 H 0.7210 0.0000 1 587 . 65 LEU HG H 1.5620 0.0060 1 588 . 65 LEU H H 7.5790 0.0100 1 589 . 65 LEU N N 118.8490 0.0960 1 590 . 66 MET CA C 55.7510 0.1610 1 591 . 66 MET CB C 33.8820 0.0370 1 592 . 66 MET CE C 16.9920 0.0000 1 593 . 66 MET CG C 30.5680 0.0000 1 594 . 66 MET HA H 4.6150 0.0000 1 595 . 66 MET HB3 H 2.0280 0.0000 1 596 . 66 MET HB2 H 2.0280 0.0000 1 597 . 66 MET HE H 2.1140 0.0000 1 598 . 66 MET HG3 H 2.8380 0.0000 1 599 . 66 MET HG2 H 2.5750 0.0000 1 600 . 66 MET H H 7.2490 0.0160 1 601 . 66 MET N N 107.8150 0.0760 1 602 . 67 LYS CA C 61.5090 0.0000 1 603 . 67 LYS CB C 30.5210 0.0000 1 604 . 67 LYS CD C 24.9530 0.2450 1 605 . 67 LYS CE C 41.0780 0.0000 1 606 . 67 LYS CG C 24.9180 0.0330 1 607 . 67 LYS HA H 4.0110 0.0320 1 608 . 67 LYS HB3 H 2.0330 0.0260 1 609 . 67 LYS HB2 H 2.0330 0.0260 1 610 . 67 LYS HD3 H 1.6550 0.0640 1 611 . 67 LYS HD2 H 1.6550 0.0640 1 612 . 67 LYS HE3 H 3.0000 0.0190 1 613 . 67 LYS HE2 H 3.0000 0.0190 1 614 . 67 LYS HG3 H 1.4890 0.0160 1 615 . 67 LYS HG2 H 1.4890 0.0160 1 616 . 67 LYS H H 7.7700 0.0200 1 617 . 67 LYS N N 120.7730 0.1110 1 618 . 68 PRO CA C 64.3750 0.1080 1 619 . 68 PRO CB C 30.0020 0.2190 1 620 . 68 PRO CD C 50.2820 0.0000 1 621 . 68 PRO CG C 27.1270 0.0000 1 622 . 68 PRO HA H 4.3030 0.0000 1 623 . 68 PRO HB3 H 2.0780 0.0000 1 624 . 68 PRO HB2 H 0.4470 0.0000 1 625 . 68 PRO HD3 H 3.6980 0.0230 1 626 . 68 PRO HD2 H 3.0950 0.0000 1 627 . 68 PRO HG3 H 1.7200 0.0000 1 628 . 68 PRO HG2 H 1.5640 0.0000 1 629 . 69 TYR CA C 56.1100 0.0680 1 630 . 69 TYR CB C 38.7720 0.2960 1 631 . 69 TYR CD1 C 132.5140 0.0000 1 632 . 69 TYR CD2 C 132.5140 0.0000 1 633 . 69 TYR CE1 C 117.8700 0.0000 1 634 . 69 TYR CE2 C 117.8700 0.0000 1 635 . 69 TYR HA H 4.7700 0.0000 1 636 . 69 TYR HB3 H 3.5470 0.0000 1 637 . 69 TYR HB2 H 2.6370 0.0000 1 638 . 69 TYR HD1 H 7.0920 0.0000 1 639 . 69 TYR HD2 H 7.0920 0.0000 1 640 . 69 TYR HE1 H 6.8970 0.0000 1 641 . 69 TYR HE2 H 6.8970 0.0000 1 642 . 69 TYR H H 7.5870 0.0240 1 643 . 69 TYR N N 113.0700 0.1470 1 644 . 70 LEU CA C 55.1930 0.0000 1 645 . 70 LEU CB C 43.4940 0.0490 1 646 . 70 LEU CD1 C 25.3590 0.0000 1 647 . 70 LEU CD2 C 23.4430 0.2840 1 648 . 70 LEU CG C 25.3440 0.0000 1 649 . 70 LEU HA H 4.3400 0.0000 1 650 . 70 LEU HB3 H 2.0740 0.0000 1 651 . 70 LEU HB2 H 1.7360 0.0000 1 652 . 70 LEU HD1 H 1.0310 0.0000 1 653 . 70 LEU HD2 H 1.0200 0.0070 1 654 . 70 LEU HG H 2.0890 0.0000 1 655 . 70 LEU H H 7.2310 0.0210 1 656 . 70 LEU N N 116.9930 0.1050 1 657 . 71 SER CA C 58.7400 0.0000 1 658 . 71 SER CB C 62.6670 0.2100 1 659 . 71 SER HA H 4.2700 0.0000 1 660 . 71 SER HB3 H 4.1000 0.0000 1 661 . 71 SER HB2 H 4.1000 0.0520 1 662 . 71 SER H H 7.8850 0.0000 1 663 . 71 SER N N 120.8950 0.0000 1 664 . 72 ARG CA C 54.2160 0.0160 1 665 . 72 ARG CB C 31.4780 0.2180 1 666 . 72 ARG CD C 43.0860 0.0000 1 667 . 72 ARG CG C 25.2370 0.0360 1 668 . 72 ARG HA H 4.5190 0.0210 1 669 . 72 ARG HB3 H 2.0240 0.0080 1 670 . 72 ARG HB2 H 1.7120 0.0000 1 671 . 72 ARG HD3 H 2.9390 0.0000 1 672 . 72 ARG HD2 H 2.9390 0.0000 1 673 . 72 ARG HG3 H 1.5870 0.0030 1 674 . 72 ARG HG2 H 1.5870 0.0030 1 675 . 72 ARG H H 7.5530 0.0120 1 676 . 72 ARG N N 115.9390 0.2000 1 677 . 73 LEU CA C 54.6440 0.0940 1 678 . 73 LEU CB C 41.6010 0.1760 1 679 . 73 LEU CD1 C 24.7680 0.0000 1 680 . 73 LEU CD2 C 21.8220 0.0000 1 681 . 73 LEU CG C 26.3730 0.0000 1 682 . 73 LEU HA H 4.3600 0.0100 1 683 . 73 LEU HB3 H 1.7470 0.0030 1 684 . 73 LEU HB2 H 1.5450 0.0050 1 685 . 73 LEU HD1 H 0.9000 0.0000 1 686 . 73 LEU HD2 H 0.9000 0.0000 1 687 . 73 LEU HG H 1.7450 0.0180 1 688 . 73 LEU H H 8.3910 0.0200 1 689 . 73 LEU N N 118.3400 0.0890 1 690 . 74 LEU CA C 57.5870 0.1660 1 691 . 74 LEU CB C 41.1750 0.2550 1 692 . 74 LEU CD1 C 24.2570 0.0000 1 693 . 74 LEU CD2 C 24.2570 0.0000 1 694 . 74 LEU CG C 27.1580 0.0250 1 695 . 74 LEU HA H 3.9000 0.0100 1 696 . 74 LEU HB3 H 1.6450 0.0050 1 697 . 74 LEU HB2 H 1.6450 0.0050 1 698 . 74 LEU HD1 H 0.9300 0.0000 1 699 . 74 LEU HD2 H 0.9300 0.0000 1 700 . 74 LEU HG H 1.6600 0.0000 1 701 . 74 LEU H H 8.8090 0.0450 1 702 . 74 LEU N N 122.7300 0.1230 1 703 . 75 GLU CA C 58.0060 0.1600 1 704 . 75 GLU CB C 28.5610 0.0090 1 705 . 75 GLU CG C 36.3520 0.0000 1 706 . 75 GLU HA H 4.1430 0.0000 1 707 . 75 GLU HB3 H 2.0460 0.0190 1 708 . 75 GLU HB2 H 2.0460 0.0190 1 709 . 75 GLU HG3 H 2.2760 0.0000 1 710 . 75 GLU HG2 H 2.2760 0.0000 1 711 . 75 GLU H H 8.9680 0.0180 1 712 . 75 GLU N N 114.3740 0.0690 1 713 . 76 GLU CA C 55.2010 0.1950 1 714 . 76 GLU CB C 29.7940 0.2600 1 715 . 76 GLU CG C 36.4560 0.2980 1 716 . 76 GLU HA H 4.3030 0.0140 1 717 . 76 GLU HB3 H 2.1250 0.0150 1 718 . 76 GLU HB2 H 2.0600 0.0000 1 719 . 76 GLU HG3 H 2.2120 0.0280 1 720 . 76 GLU HG2 H 2.2120 0.0420 1 721 . 76 GLU H H 7.8330 0.0380 1 722 . 76 GLU N N 116.1610 0.1630 1 723 . 77 LEU CA C 54.8820 0.2680 1 724 . 77 LEU CB C 42.6160 0.1640 1 725 . 77 LEU CD1 C 24.9880 0.0000 1 726 . 77 LEU CD2 C 24.9880 0.0000 1 727 . 77 LEU CG C 26.4280 0.3390 1 728 . 77 LEU HA H 4.0560 0.0070 1 729 . 77 LEU HB3 H 1.7570 0.0330 1 730 . 77 LEU HB2 H 1.5930 0.0030 1 731 . 77 LEU HD1 H 0.9050 0.0620 1 732 . 77 LEU HD2 H 0.9050 0.0250 1 733 . 77 LEU HG H 1.9750 0.0560 1 734 . 77 LEU H H 7.3950 0.0170 1 735 . 77 LEU N N 121.0610 0.2000 1 736 . 78 GLY CA C 44.6660 0.1820 1 737 . 78 GLY HA3 H 4.0730 0.0000 1 738 . 78 GLY HA2 H 4.0730 0.0000 1 739 . 78 GLY H H 8.6390 0.0430 1 740 . 78 GLY N N 110.7400 0.1440 1 741 . 79 GLN CA C 58.3570 0.2870 1 742 . 79 GLN CB C 28.0260 0.0830 1 743 . 79 GLN CG C 31.5250 0.0000 1 744 . 79 GLN HA H 4.0600 0.0140 1 745 . 79 GLN HB3 H 2.0740 0.0190 1 746 . 79 GLN HB2 H 2.0740 0.0190 1 747 . 79 GLN HE21 H 7.1680 0.0000 1 748 . 79 GLN HE22 H 6.6320 0.0000 1 749 . 79 GLN HG3 H 2.6880 0.0070 1 750 . 79 GLN HG2 H 2.4040 0.0190 1 751 . 79 GLN H H 8.6120 0.0260 1 752 . 79 GLN N N 118.2950 0.1240 1 753 . 79 GLN NE2 N 106.0500 0.0190 1 754 . 80 VAL CA C 67.2810 0.0000 1 755 . 80 VAL CB C 30.5530 0.0000 1 756 . 80 VAL CG1 C 22.3820 0.0000 1 757 . 80 VAL CG2 C 20.4240 0.0000 1 758 . 80 VAL HA H 3.5930 0.0000 1 759 . 80 VAL HB H 2.0400 0.0000 1 760 . 80 VAL HG1 H 0.8550 0.0000 1 761 . 80 VAL HG2 H 0.7060 0.0000 1 762 . 80 VAL H H 8.9190 0.0430 1 763 . 80 VAL N N 118.3330 0.1410 1 764 . 81 GLU CA C 61.9340 0.0070 1 765 . 81 GLU CB C 27.9130 0.0900 1 766 . 81 GLU CG C 37.6220 0.0000 1 767 . 81 GLU HA H 3.6480 0.0000 1 768 . 81 GLU HB3 H 2.3480 0.0400 1 769 . 81 GLU HB2 H 1.7650 0.0130 1 770 . 81 GLU HG3 H 2.6500 0.0000 1 771 . 81 GLU HG2 H 2.1720 0.0060 1 772 . 81 GLU H H 9.0670 0.0000 1 773 . 81 GLU N N 118.6480 0.0000 1 774 . 82 LYS CA C 60.5180 0.0600 1 775 . 82 LYS CB C 32.1920 0.0700 1 776 . 82 LYS CD C 29.0750 0.0000 1 777 . 82 LYS CE C 41.1450 0.0000 1 778 . 82 LYS CG C 24.4710 0.0000 1 779 . 82 LYS HA H 3.8240 0.0000 1 780 . 82 LYS HB3 H 1.8950 0.0000 1 781 . 82 LYS HB2 H 1.7440 0.0000 1 782 . 82 LYS HD3 H 1.6690 0.0000 1 783 . 82 LYS HD2 H 1.6690 0.0000 1 784 . 82 LYS HE3 H 2.7410 0.0000 1 785 . 82 LYS HE2 H 2.7410 0.0000 1 786 . 82 LYS HG3 H 1.3350 0.0000 1 787 . 82 LYS HG2 H 1.3350 0.0000 1 788 . 82 LYS H H 8.3260 0.0120 1 789 . 82 LYS N N 116.3080 0.0670 1 790 . 83 ALA CA C 55.7330 0.1010 1 791 . 83 ALA CB C 17.9880 0.0890 1 792 . 83 ALA HA H 4.1590 0.0000 1 793 . 83 ALA HB H 1.6330 0.0000 1 794 . 83 ALA H H 7.9370 0.0220 1 795 . 83 ALA N N 120.3800 0.2360 1 796 . 84 VAL CA C 66.5330 0.0940 1 797 . 84 VAL CB C 31.5360 0.0460 1 798 . 84 VAL CG1 C 22.3870 0.0960 1 799 . 84 VAL CG2 C 23.4840 0.0000 1 800 . 84 VAL HA H 3.4990 0.0000 1 801 . 84 VAL HB H 2.1730 0.0000 1 802 . 84 VAL HG1 H 1.1590 0.0200 1 803 . 84 VAL HG2 H 1.0340 0.0000 1 804 . 84 VAL H H 8.6490 0.0140 1 805 . 84 VAL N N 114.6310 0.0610 1 806 . 85 LEU CA C 58.0630 0.2450 1 807 . 85 LEU CB C 41.6200 0.2090 1 808 . 85 LEU CD1 C 25.2730 0.0000 1 809 . 85 LEU CD2 C 23.5020 0.0000 1 810 . 85 LEU CG C 27.6950 0.0000 1 811 . 85 LEU HA H 4.0050 0.0210 1 812 . 85 LEU HB3 H 2.1230 0.0010 1 813 . 85 LEU HB2 H 1.4620 0.0010 1 814 . 85 LEU HD1 H 1.0010 0.0000 1 815 . 85 LEU HD2 H 0.8990 0.0000 1 816 . 85 LEU HG H 1.8650 0.0010 1 817 . 85 LEU H H 8.4830 0.0240 1 818 . 85 LEU N N 117.2270 0.2390 1 819 . 86 ARG CA C 61.0190 0.2200 1 820 . 86 ARG CB C 29.7920 0.2370 1 821 . 86 ARG CD C 44.0440 0.1080 1 822 . 86 ARG HA H 3.8570 0.0000 1 823 . 86 ARG HB3 H 1.8800 0.0520 1 824 . 86 ARG HB2 H 1.8800 0.0520 1 825 . 86 ARG HD3 H 3.1450 0.0000 1 826 . 86 ARG HD2 H 3.1450 0.0000 1 827 . 86 ARG H H 8.5980 0.0190 1 828 . 86 ARG N N 116.8300 0.0930 1 829 . 87 ILE CA C 65.8480 0.1910 1 830 . 87 ILE CB C 37.7740 0.2110 1 831 . 87 ILE CD1 C 15.0410 0.1890 1 832 . 87 ILE CG1 C 29.5840 0.2250 1 833 . 87 ILE CG2 C 16.1470 0.0200 1 834 . 87 ILE HA H 3.4350 0.0000 1 835 . 87 ILE HB H 2.0230 0.0000 1 836 . 87 ILE HD1 H 0.7410 0.0440 1 837 . 87 ILE HG13 H 0.6490 0.0000 1 838 . 87 ILE HG12 H 0.6490 0.0000 1 839 . 87 ILE HG2 H 0.9030 0.0090 1 840 . 87 ILE H H 8.0520 0.0120 1 841 . 87 ILE N N 117.0650 0.1130 1 842 . 88 ALA CA C 54.6220 0.2150 1 843 . 88 ALA CB C 18.8470 0.0960 1 844 . 88 ALA HA H 4.4990 0.0000 1 845 . 88 ALA HB H 1.4280 0.0000 1 846 . 88 ALA H H 8.2370 0.0200 1 847 . 88 ALA N N 120.0050 0.0960 1 848 . 89 LEU CA C 57.1250 0.2110 1 849 . 89 LEU CB C 40.5580 0.1050 1 850 . 89 LEU CD1 C 25.9830 0.0000 1 851 . 89 LEU CD2 C 22.4400 0.0000 1 852 . 89 LEU CG C 27.1150 0.0000 1 853 . 89 LEU HA H 3.9860 0.0000 1 854 . 89 LEU HB3 H 1.9720 0.0000 1 855 . 89 LEU HB2 H 1.9720 0.0000 1 856 . 89 LEU HD1 H 0.9040 0.0000 1 857 . 89 LEU HD2 H 0.6500 0.0000 1 858 . 89 LEU HG H 1.9610 0.0260 1 859 . 89 LEU H H 8.9210 0.0210 1 860 . 89 LEU N N 114.6260 0.2680 1 861 . 90 TYR CA C 62.5970 0.1400 1 862 . 90 TYR CB C 37.2700 0.0600 1 863 . 90 TYR CD1 C 131.8440 0.0000 1 864 . 90 TYR CD2 C 131.8440 0.0000 1 865 . 90 TYR CE1 C 117.1800 0.0000 1 866 . 90 TYR CE2 C 117.1800 0.0000 1 867 . 90 TYR HA H 3.8320 0.0000 1 868 . 90 TYR HB3 H 3.2970 0.0000 1 869 . 90 TYR HB2 H 3.0980 0.0000 1 870 . 90 TYR HD1 H 6.7510 0.0000 1 871 . 90 TYR HD2 H 6.7510 0.0000 1 872 . 90 TYR HE1 H 6.5080 0.0000 1 873 . 90 TYR HE2 H 6.5080 0.0000 1 874 . 90 TYR H H 8.7500 0.0260 1 875 . 90 TYR N N 124.4850 0.1620 1 876 . 91 GLU CA C 60.6910 0.1140 1 877 . 91 GLU CB C 29.3320 0.2020 1 878 . 91 GLU CG C 38.0210 0.0000 1 879 . 91 GLU HA H 3.6000 0.0000 1 880 . 91 GLU HB3 H 2.1130 0.0000 1 881 . 91 GLU HB2 H 2.1130 0.0000 1 882 . 91 GLU HG3 H 2.6430 0.0000 1 883 . 91 GLU HG2 H 2.6430 0.0000 1 884 . 91 GLU H H 8.8740 0.0200 1 885 . 91 GLU N N 118.7160 0.1790 1 886 . 92 LEU CA C 57.1000 0.0220 1 887 . 92 LEU CB C 42.7740 0.1130 1 888 . 92 LEU CD1 C 25.2590 0.0000 1 889 . 92 LEU CD2 C 23.3070 0.0000 1 890 . 92 LEU CG C 27.1570 0.0000 1 891 . 92 LEU HA H 3.9540 0.0000 1 892 . 92 LEU HB3 H 1.9190 0.0360 1 893 . 92 LEU HB2 H 1.1550 0.0330 1 894 . 92 LEU HD1 H 0.7300 0.0000 1 895 . 92 LEU HD2 H 0.6480 0.0000 1 896 . 92 LEU HG H 1.7320 0.0000 1 897 . 92 LEU H H 8.8630 0.0270 1 898 . 92 LEU N N 114.2170 0.0730 1 899 . 93 SER CA C 60.5400 0.0350 1 900 . 93 SER CB C 64.3590 0.4930 1 901 . 93 SER HA H 4.1870 0.0000 1 902 . 93 SER HB3 H 3.8280 0.3640 1 903 . 93 SER HB2 H 3.8280 0.0230 1 904 . 93 SER H H 8.2810 0.0160 1 905 . 93 SER N N 111.5050 0.1680 1 906 . 94 LYS CA C 55.1390 0.1680 1 907 . 94 LYS CB C 33.1210 0.1180 1 908 . 94 LYS CD C 27.6540 0.0000 1 909 . 94 LYS CE C 41.7750 0.0000 1 910 . 94 LYS CG C 23.5440 0.0490 1 911 . 94 LYS HA H 4.6210 0.0000 1 912 . 94 LYS HB3 H 1.5030 0.0000 1 913 . 94 LYS HB2 H 1.0070 0.0000 1 914 . 94 LYS HD3 H 1.6050 0.0320 1 915 . 94 LYS HD2 H 1.4930 0.0040 1 916 . 94 LYS HE3 H 2.7350 0.0000 1 917 . 94 LYS HE2 H 2.7350 0.0000 1 918 . 94 LYS HG3 H 1.4460 0.0000 1 919 . 94 LYS HG2 H 1.2200 0.0000 1 920 . 94 LYS H H 8.3740 0.0100 1 921 . 94 LYS N N 116.7550 0.1810 1 922 . 95 ARG CA C 50.8360 0.2930 1 923 . 95 ARG CB C 27.3650 0.2710 1 924 . 95 ARG CD C 40.1730 0.0000 1 925 . 95 ARG CG C 24.4440 0.0000 1 926 . 95 ARG HA H 4.9630 0.0000 1 927 . 95 ARG HB3 H 2.2360 0.0000 1 928 . 95 ARG HB2 H 2.2360 0.0000 1 929 . 95 ARG HD3 H 3.4740 0.0000 1 930 . 95 ARG HD2 H 3.2660 0.0000 1 931 . 95 ARG HE H 8.3300 0.0000 1 932 . 95 ARG HG3 H 1.2900 0.0000 1 933 . 95 ARG HG2 H 1.2900 0.0000 1 934 . 95 ARG H H 7.5690 0.0120 1 935 . 95 ARG N N 117.6960 0.0930 1 936 . 95 ARG NE N 82.7970 0.0000 1 937 . 96 SER CA C 60.2960 0.2390 1 938 . 96 SER CB C 62.4140 0.0760 1 939 . 96 SER HA H 4.1700 0.0300 1 940 . 96 SER HB3 H 3.9590 0.0210 1 941 . 96 SER HB2 H 3.9590 0.0590 1 942 . 96 SER H H 8.5360 0.0340 1 943 . 96 SER N N 117.8160 0.2060 1 944 . 97 ASP CA C 53.3010 0.2020 1 945 . 97 ASP CB C 38.7840 0.0120 1 946 . 97 ASP HA H 4.4280 0.0000 1 947 . 97 ASP HB3 H 2.8340 0.0000 1 948 . 97 ASP HB2 H 2.6860 0.0000 1 949 . 97 ASP H H 9.4320 0.0240 1 950 . 97 ASP N N 115.6250 0.1620 1 951 . 98 VAL CA C 59.5640 0.0000 1 952 . 98 VAL CB C 32.4710 0.0000 1 953 . 98 VAL CG1 C 20.7470 0.0000 1 954 . 98 VAL CG2 C 19.5910 0.0000 1 955 . 98 VAL HA H 4.3960 0.0110 1 956 . 98 VAL HB H 2.1000 0.0460 1 957 . 98 VAL HG1 H 0.9400 0.0000 1 958 . 98 VAL HG2 H 0.8700 0.0000 1 959 . 98 VAL H H 7.9030 0.0240 1 960 . 98 VAL N N 123.5670 0.0920 1 961 . 99 PRO CA C 62.4650 0.0200 1 962 . 99 PRO CB C 32.8080 0.2390 1 963 . 99 PRO CD C 51.2960 0.0610 1 964 . 99 PRO CG C 27.2430 0.0000 1 965 . 99 PRO HA H 4.5160 0.0000 1 966 . 99 PRO HB3 H 2.7720 0.0000 1 967 . 99 PRO HB2 H 1.8160 0.0000 1 968 . 99 PRO HD3 H 4.2690 0.0000 1 969 . 99 PRO HD2 H 3.4870 0.0000 1 970 . 99 PRO HG3 H 2.1620 0.0770 1 971 . 99 PRO HG2 H 2.1620 0.0770 1 972 . 100 TYR CA C 61.8120 0.2600 1 973 . 100 TYR CB C 38.7070 0.2870 1 974 . 100 TYR CD1 C 132.4210 0.0000 1 975 . 100 TYR CD2 C 132.4210 0.0000 1 976 . 100 TYR CE1 C 118.0700 0.0000 1 977 . 100 TYR CE2 C 118.0700 0.0000 1 978 . 100 TYR HA H 3.7510 0.0000 1 979 . 100 TYR HB3 H 2.8670 0.0000 1 980 . 100 TYR HB2 H 2.8670 0.0000 1 981 . 100 TYR HD1 H 6.7800 0.0000 1 982 . 100 TYR HD2 H 6.7800 0.0000 1 983 . 100 TYR HE1 H 6.6290 0.0000 1 984 . 100 TYR HE2 H 6.6290 0.0000 1 985 . 100 TYR H H 8.5080 0.0270 1 986 . 100 TYR N N 125.4210 0.1100 1 987 . 101 LYS CA C 58.5570 0.2180 1 988 . 101 LYS CB C 31.9770 0.1470 1 989 . 101 LYS CD C 28.8730 0.1100 1 990 . 101 LYS CE C 41.5240 0.0000 1 991 . 101 LYS CG C 25.0160 0.2570 1 992 . 101 LYS HA H 3.9040 0.0100 1 993 . 101 LYS HB3 H 1.8740 0.0000 1 994 . 101 LYS HB2 H 1.8740 0.0000 1 995 . 101 LYS HD3 H 1.7800 0.0000 1 996 . 101 LYS HD2 H 1.7800 0.0000 1 997 . 101 LYS HE3 H 3.0940 0.0000 1 998 . 101 LYS HE2 H 3.0940 0.0000 1 999 . 101 LYS HG3 H 1.7320 0.0120 1 1000 . 101 LYS HG2 H 1.5710 0.0090 1 1001 . 101 LYS H H 8.8110 0.0360 1 1002 . 101 LYS N N 111.4770 0.0540 1 1003 . 102 VAL CA C 65.3610 0.2040 1 1004 . 102 VAL CB C 31.0040 0.2610 1 1005 . 102 VAL CG1 C 21.6880 0.0000 1 1006 . 102 VAL CG2 C 20.2630 0.0000 1 1007 . 102 VAL HA H 3.7870 0.0000 1 1008 . 102 VAL HB H 2.1300 0.0000 1 1009 . 102 VAL HG1 H 1.0590 0.0000 1 1010 . 102 VAL HG2 H 0.9190 0.0000 1 1011 . 102 VAL H H 6.9080 0.0260 1 1012 . 102 VAL N N 117.3590 0.1010 1 1013 . 103 ALA CA C 55.1640 0.1990 1 1014 . 103 ALA CB C 16.6970 0.1820 1 1015 . 103 ALA HA H 3.8820 0.0000 1 1016 . 103 ALA HB H 1.2860 0.0000 1 1017 . 103 ALA H H 7.6640 0.0220 1 1018 . 103 ALA N N 118.9800 0.0610 1 1019 . 104 ILE CA C 64.4770 0.1080 1 1020 . 104 ILE CB C 38.2790 0.0960 1 1021 . 104 ILE CD1 C 12.5190 0.0000 1 1022 . 104 ILE CG1 C 28.5950 0.2640 1 1023 . 104 ILE CG2 C 16.2790 0.2550 1 1024 . 104 ILE HA H 3.5180 0.0000 1 1025 . 104 ILE HB H 1.5360 0.0400 1 1026 . 104 ILE HD1 H 0.2300 0.0000 1 1027 . 104 ILE HG13 H 1.4510 0.0340 1 1028 . 104 ILE HG12 H 0.6520 0.0000 1 1029 . 104 ILE HG2 H 0.8000 0.0300 1 1030 . 104 ILE H H 6.9960 0.0250 1 1031 . 104 ILE N N 111.4160 0.1390 1 1032 . 105 ASN CA C 56.7080 0.0400 1 1033 . 105 ASN CB C 38.0430 0.2040 1 1034 . 105 ASN HA H 4.4160 0.0000 1 1035 . 105 ASN HB3 H 2.9410 0.0000 1 1036 . 105 ASN HB2 H 2.8410 0.0000 1 1037 . 105 ASN HD21 H 7.8240 0.0000 1 1038 . 105 ASN HD22 H 6.9350 0.0000 1 1039 . 105 ASN H H 8.2060 0.0290 1 1040 . 105 ASN N N 116.3210 0.2570 1 1041 . 105 ASN ND2 N 111.4270 0.0320 1 1042 . 106 GLU CA C 58.8070 0.0070 1 1043 . 106 GLU CB C 29.0850 0.2850 1 1044 . 106 GLU CG C 37.5760 0.0000 1 1045 . 106 GLU HA H 4.0040 0.0000 1 1046 . 106 GLU HB3 H 1.9720 0.0000 1 1047 . 106 GLU HB2 H 1.9720 0.0130 1 1048 . 106 GLU HG3 H 2.5870 0.0200 1 1049 . 106 GLU HG2 H 2.5870 0.5710 1 1050 . 106 GLU H H 9.0540 0.0220 1 1051 . 106 GLU N N 116.4780 0.1090 1 1052 . 107 ALA CA C 54.7100 0.1640 1 1053 . 107 ALA CB C 18.6230 0.1180 1 1054 . 107 ALA HA H 4.3250 0.0000 1 1055 . 107 ALA HB H 1.4110 0.0000 1 1056 . 107 ALA H H 7.1020 0.0180 1 1057 . 107 ALA N N 120.0580 0.1480 1 1058 . 108 ILE CA C 65.3660 0.0530 1 1059 . 108 ILE CB C 37.4090 0.1620 1 1060 . 108 ILE CD1 C 12.8440 0.0390 1 1061 . 108 ILE CG1 C 28.8920 0.3010 1 1062 . 108 ILE CG2 C 17.6940 0.0010 1 1063 . 108 ILE HA H 3.5460 0.0160 1 1064 . 108 ILE HB H 2.1040 0.0080 1 1065 . 108 ILE HD1 H 0.9210 0.0000 1 1066 . 108 ILE HG13 H 1.8340 0.0380 1 1067 . 108 ILE HG12 H 1.1730 0.0510 1 1068 . 108 ILE HG2 H 0.9950 0.0100 1 1069 . 108 ILE H H 7.8030 0.0200 1 1070 . 108 ILE N N 116.2730 0.0970 1 1071 . 109 GLU CA C 59.0630 0.1560 1 1072 . 109 GLU CB C 28.1090 0.0120 1 1073 . 109 GLU CG C 35.8340 0.0000 1 1074 . 109 GLU HA H 3.9790 0.0090 1 1075 . 109 GLU HB3 H 2.0700 0.0000 1 1076 . 109 GLU HB2 H 2.0700 0.0000 1 1077 . 109 GLU HG3 H 2.3720 0.0000 1 1078 . 109 GLU HG2 H 2.3720 0.0000 1 1079 . 109 GLU H H 7.9810 0.0240 1 1080 . 109 GLU N N 117.1910 0.0630 1 1081 . 110 LEU CA C 57.6400 0.0050 1 1082 . 110 LEU CB C 42.3030 0.1570 1 1083 . 110 LEU CD1 C 25.3630 0.0790 1 1084 . 110 LEU CD2 C 23.3130 0.0390 1 1085 . 110 LEU CG C 26.3810 0.2330 1 1086 . 110 LEU HA H 4.2640 0.0040 1 1087 . 110 LEU HB3 H 2.2740 0.0000 1 1088 . 110 LEU HB2 H 1.4150 0.0000 1 1089 . 110 LEU HD1 H 0.9960 0.0000 1 1090 . 110 LEU HD2 H 1.0070 0.0430 1 1091 . 110 LEU HG H 2.1380 0.0490 1 1092 . 110 LEU H H 8.9390 0.0270 1 1093 . 110 LEU N N 120.8110 0.0470 1 1094 . 111 ALA CA C 55.1470 0.0760 1 1095 . 111 ALA CB C 16.6660 0.1980 1 1096 . 111 ALA HA H 4.0050 0.0000 1 1097 . 111 ALA HB H 1.5500 0.0000 1 1098 . 111 ALA H H 8.5870 0.0200 1 1099 . 111 ALA N N 120.2620 0.0340 1 1100 . 112 LYS CA C 59.1150 0.0510 1 1101 . 112 LYS CB C 32.3630 0.0840 1 1102 . 112 LYS CD C 29.0880 0.0000 1 1103 . 112 LYS CE C 41.1710 0.1910 1 1104 . 112 LYS CG C 25.2230 0.0000 1 1105 . 112 LYS HA H 4.2630 0.0000 1 1106 . 112 LYS HB3 H 1.8400 0.0500 1 1107 . 112 LYS HB2 H 1.8400 0.0300 1 1108 . 112 LYS HD3 H 1.3850 0.0050 1 1109 . 112 LYS HD2 H 1.3850 0.0050 1 1110 . 112 LYS HE3 H 2.4310 0.0310 1 1111 . 112 LYS HE2 H 2.2780 0.0080 1 1112 . 112 LYS HG3 H 1.4610 0.0290 1 1113 . 112 LYS HG2 H 1.0550 0.0000 1 1114 . 112 LYS H H 8.2650 0.0170 1 1115 . 112 LYS N N 117.6500 0.1460 1 1116 . 113 SER CA C 61.2550 0.0800 1 1117 . 113 SER CB C 62.9930 0.1120 1 1118 . 113 SER HA H 4.1190 0.0000 1 1119 . 113 SER HB3 H 3.6550 0.0000 1 1120 . 113 SER HB2 H 3.2420 0.0000 1 1121 . 113 SER H H 7.9880 0.0100 1 1122 . 113 SER N N 112.6400 0.1640 1 1123 . 114 PHE CA C 58.3890 0.1660 1 1124 . 114 PHE CB C 40.7660 0.0730 1 1125 . 114 PHE CD1 C 131.2250 0.0000 1 1126 . 114 PHE CD2 C 131.2250 0.0000 1 1127 . 114 PHE CE1 C 130.2990 0.0000 1 1128 . 114 PHE CE2 C 130.2990 0.0000 1 1129 . 114 PHE CZ C 128.9200 0.2600 1 1130 . 114 PHE HA H 4.8180 0.0000 1 1131 . 114 PHE HB3 H 3.2170 0.0000 1 1132 . 114 PHE HB2 H 2.5850 0.0000 1 1133 . 114 PHE HD1 H 7.4280 0.0000 1 1134 . 114 PHE HD2 H 7.4280 0.0000 1 1135 . 114 PHE HE1 H 7.3090 0.0000 1 1136 . 114 PHE HE2 H 7.3090 0.0000 1 1137 . 114 PHE H H 8.2070 0.0250 1 1138 . 114 PHE HZ H 7.1590 0.0640 1 1139 . 114 PHE N N 113.3940 0.0800 1 1140 . 115 GLY CA C 43.5910 0.0000 1 1141 . 115 GLY HA3 H 4.4410 0.0000 1 1142 . 115 GLY HA2 H 3.9680 0.0000 1 1143 . 115 GLY H H 8.0460 0.0220 1 1144 . 115 GLY N N 107.2510 0.0740 1 1145 . 116 ALA CA C 51.0550 0.1050 1 1146 . 116 ALA CB C 18.9520 0.2110 1 1147 . 116 ALA HA H 4.6250 0.0000 1 1148 . 116 ALA HB H 1.5850 0.0000 1 1149 . 116 ALA H H 8.4250 0.0210 1 1150 . 116 ALA N N 120.4650 0.1240 1 1151 . 117 GLU CA C 59.2960 0.1780 1 1152 . 117 GLU CB C 28.6790 0.1650 1 1153 . 117 GLU CG C 35.6990 0.0000 1 1154 . 117 GLU HA H 4.1550 0.0050 1 1155 . 117 GLU HB3 H 2.1600 0.0000 1 1156 . 117 GLU HB2 H 2.0700 0.0000 1 1157 . 117 GLU HG3 H 2.3790 0.0000 1 1158 . 117 GLU HG2 H 2.3790 0.0000 1 1159 . 117 GLU H H 8.8800 0.0210 1 1160 . 117 GLU N N 120.1570 0.0910 1 1161 . 118 ASP CA C 54.5110 0.1460 1 1162 . 118 ASP CB C 39.7740 0.1770 1 1163 . 118 ASP HA H 4.7330 0.0000 1 1164 . 118 ASP HB3 H 3.0150 0.0000 1 1165 . 118 ASP HB2 H 2.8380 0.0000 1 1166 . 118 ASP H H 8.7350 0.0350 1 1167 . 118 ASP N N 114.5090 0.2420 1 1168 . 119 SER CA C 62.8320 0.3780 1 1169 . 119 SER CB C 62.3530 0.0000 1 1170 . 119 SER HA H 4.4060 0.0000 1 1171 . 119 SER HB3 H 4.0010 0.0000 1 1172 . 119 SER HB2 H 4.0010 0.0000 1 1173 . 119 SER H H 8.3510 0.0220 1 1174 . 119 SER N N 118.1660 0.0810 1 1175 . 120 HIS CA C 59.0520 0.0270 1 1176 . 120 HIS CB C 29.5670 0.0960 1 1177 . 120 HIS CD2 C 119.5100 0.0000 1 1178 . 120 HIS CE1 C 138.5700 0.0000 1 1179 . 120 HIS HA H 4.1590 0.0000 1 1180 . 120 HIS HB3 H 3.2930 0.0000 1 1181 . 120 HIS HB2 H 3.0350 0.0000 1 1182 . 120 HIS HD2 H 7.2660 0.0000 1 1183 . 120 HIS HE1 H 7.8780 0.0000 1 1184 . 120 HIS H H 9.1900 0.0000 1 1185 . 120 HIS N N 118.3720 0.0000 1 1186 . 121 LYS CA C 58.5210 0.0900 1 1187 . 121 LYS CB C 31.3130 0.2530 1 1188 . 121 LYS CD C 28.8250 0.0000 1 1189 . 121 LYS CE C 41.6370 0.0000 1 1190 . 121 LYS CG C 24.3680 0.0000 1 1191 . 121 LYS HA H 3.9330 0.0000 1 1192 . 121 LYS HB3 H 1.7680 0.0000 1 1193 . 121 LYS HB2 H 1.6650 0.0000 1 1194 . 121 LYS HD3 H 1.6270 0.0000 1 1195 . 121 LYS HD2 H 1.5740 0.0000 1 1196 . 121 LYS HE3 H 2.9840 0.0000 1 1197 . 121 LYS HE2 H 2.9840 0.0000 1 1198 . 121 LYS HG3 H 1.1060 0.0000 1 1199 . 121 LYS HG2 H 0.7500 0.0000 1 1200 . 121 LYS H H 6.6440 0.0290 1 1201 . 121 LYS N N 120.3560 0.0960 1 1202 . 122 PHE CA C 60.5350 0.0140 1 1203 . 122 PHE CB C 38.2800 0.2300 1 1204 . 122 PHE CD1 C 131.3230 0.0430 1 1205 . 122 PHE CD2 C 131.3230 0.0430 1 1206 . 122 PHE CE1 C 129.3750 0.1490 1 1207 . 122 PHE CE2 C 129.3750 0.1490 1 1208 . 122 PHE HA H 4.3320 0.0000 1 1209 . 122 PHE HB3 H 3.3980 0.0000 1 1210 . 122 PHE HB2 H 3.2460 0.0000 1 1211 . 122 PHE HD1 H 7.1940 0.0000 1 1212 . 122 PHE HD2 H 6.9200 0.0000 1 1213 . 122 PHE HE1 H 6.7580 0.0080 1 1214 . 122 PHE HE2 H 6.4680 0.0030 1 1215 . 122 PHE H H 7.4760 0.0390 1 1216 . 122 PHE N N 120.7250 0.1200 1 1217 . 123 VAL CA C 66.4040 0.1760 1 1218 . 123 VAL CB C 31.4840 0.0000 1 1219 . 123 VAL CG1 C 21.9060 0.0000 1 1220 . 123 VAL CG2 C 20.1830 0.0000 1 1221 . 123 VAL HA H 3.3440 0.0000 1 1222 . 123 VAL HB H 2.0870 0.0000 1 1223 . 123 VAL HG1 H 1.1420 0.0000 1 1224 . 123 VAL HG2 H 0.8550 0.0000 1 1225 . 123 VAL H H 8.4990 0.0210 1 1226 . 123 VAL N N 117.7120 0.1370 1 1227 . 124 ASN CA C 56.1100 0.0780 1 1228 . 124 ASN CB C 39.0110 0.1030 1 1229 . 124 ASN HA H 4.1140 0.0000 1 1230 . 124 ASN HB3 H 2.9360 0.0000 1 1231 . 124 ASN HB2 H 2.9360 0.0000 1 1232 . 124 ASN HD21 H 7.3880 0.0000 1 1233 . 124 ASN HD22 H 6.8650 0.0000 1 1234 . 124 ASN H H 8.3360 0.0180 1 1235 . 124 ASN N N 115.9190 0.0620 1 1236 . 124 ASN ND2 N 112.0420 0.0210 1 1237 . 125 GLY CA C 46.5490 0.1570 1 1238 . 125 GLY HA3 H 3.9770 0.0000 1 1239 . 125 GLY HA2 H 3.8480 0.0000 1 1240 . 125 GLY H H 7.8950 0.0140 1 1241 . 125 GLY N N 104.6750 0.1130 1 1242 . 126 VAL CA C 65.8260 0.0690 1 1243 . 126 VAL CB C 31.3160 0.2120 1 1244 . 126 VAL CG1 C 20.8170 0.2560 1 1245 . 126 VAL CG2 C 22.2840 0.2390 1 1246 . 126 VAL HA H 3.5850 0.0100 1 1247 . 126 VAL HB H 1.8670 0.0000 1 1248 . 126 VAL HG1 H 0.8050 0.0150 1 1249 . 126 VAL HG2 H 0.6000 0.0000 1 1250 . 126 VAL H H 7.4700 0.0190 1 1251 . 126 VAL N N 118.9600 0.1440 1 1252 . 127 LEU CA C 57.7120 0.0870 1 1253 . 127 LEU CB C 40.5900 0.1510 1 1254 . 127 LEU CD1 C 26.8730 0.0000 1 1255 . 127 LEU CD2 C 21.5970 0.1460 1 1256 . 127 LEU CG C 25.9830 0.0620 1 1257 . 127 LEU HA H 3.8160 0.0140 1 1258 . 127 LEU HB3 H 1.8740 0.0000 1 1259 . 127 LEU HB2 H 1.2080 0.0000 1 1260 . 127 LEU HD1 H 0.7230 0.0000 1 1261 . 127 LEU HD2 H 0.5980 0.0220 1 1262 . 127 LEU HG H 1.7220 0.0000 1 1263 . 127 LEU H H 8.0560 0.0110 1 1264 . 127 LEU N N 117.1150 0.1150 1 1265 . 128 ASP CA C 56.6610 0.0310 1 1266 . 128 ASP CB C 40.6670 0.1020 1 1267 . 128 ASP HA H 4.3460 0.0000 1 1268 . 128 ASP HB3 H 2.7880 0.0000 1 1269 . 128 ASP HB2 H 2.5240 0.0000 1 1270 . 128 ASP H H 8.3760 0.0210 1 1271 . 128 ASP N N 116.5630 0.0660 1 1272 . 129 LYS CA C 56.6090 0.2820 1 1273 . 129 LYS CB C 33.0010 0.2060 1 1274 . 129 LYS CD C 28.5910 0.0000 1 1275 . 129 LYS CE C 41.9850 0.0000 1 1276 . 129 LYS CG C 24.4260 0.1690 1 1277 . 129 LYS HA H 4.1400 0.0000 1 1278 . 129 LYS HB3 H 1.5640 0.0210 1 1279 . 129 LYS HB2 H 1.4780 0.0000 1 1280 . 129 LYS HD3 H 1.8170 0.0000 1 1281 . 129 LYS HD2 H 1.8170 0.0000 1 1282 . 129 LYS HE3 H 3.0700 0.0000 1 1283 . 129 LYS HE2 H 3.0700 0.0000 1 1284 . 129 LYS HG3 H 1.6860 0.0000 1 1285 . 129 LYS HG2 H 1.4330 0.0000 1 1286 . 129 LYS H H 6.7130 0.0240 1 1287 . 129 LYS N N 112.9340 0.0940 1 1288 . 130 ALA CA C 53.4750 0.0130 1 1289 . 130 ALA CB C 18.9290 0.0350 1 1290 . 130 ALA HA H 3.7020 0.0000 1 1291 . 130 ALA HB H 1.0640 0.0000 1 1292 . 130 ALA H H 8.2520 0.0220 1 1293 . 130 ALA N N 116.7770 0.0420 1 1294 . 131 ALA CA C 57.2940 0.0000 1 1295 . 131 ALA CB C 16.0230 0.2200 1 1296 . 131 ALA HA H 4.0650 0.0000 1 1297 . 131 ALA HB H 1.3800 0.0000 1 1298 . 131 ALA H H 8.9660 0.0330 1 1299 . 131 ALA N N 118.3670 0.0590 1 1300 . 132 PRO CA C 64.4040 0.1880 1 1301 . 132 PRO CB C 30.5510 0.2120 1 1302 . 132 PRO CD C 50.3570 0.0450 1 1303 . 132 PRO CG C 27.4550 0.2150 1 1304 . 132 PRO HA H 4.4610 0.0090 1 1305 . 132 PRO HB3 H 2.2270 0.0000 1 1306 . 132 PRO HB2 H 1.7750 0.0000 1 1307 . 132 PRO HD3 H 3.6620 0.0000 2 1308 . 132 PRO HD2 H 3.3770 0.0000 2 1309 . 132 PRO HG3 H 1.9950 0.0040 1 1310 . 132 PRO HG2 H 1.9950 0.0040 1 1311 . 133 VAL CA C 64.2440 0.1730 1 1312 . 133 VAL CB C 31.3300 0.1870 1 1313 . 133 VAL CG1 C 20.9970 0.0000 1 1314 . 133 VAL CG2 C 20.4820 0.0400 1 1315 . 133 VAL HA H 3.8020 0.0220 1 1316 . 133 VAL HB H 2.2640 0.0000 1 1317 . 133 VAL HG1 H 1.0900 0.0000 1 1318 . 133 VAL HG2 H 1.0610 0.0210 1 1319 . 133 VAL H H 6.7700 0.0380 1 1320 . 133 VAL N N 114.3370 0.2450 1 1321 . 134 ILE CA C 63.2800 0.1570 1 1322 . 134 ILE CB C 38.7290 0.0030 1 1323 . 134 ILE CD1 C 15.6790 0.2310 1 1324 . 134 ILE CG1 C 27.4450 0.0000 1 1325 . 134 ILE CG2 C 17.6260 0.3450 1 1326 . 134 ILE HA H 3.9030 0.0000 1 1327 . 134 ILE HB H 1.7630 0.0000 1 1328 . 134 ILE HD1 H 0.8610 0.0000 1 1329 . 134 ILE HG13 H 1.8590 0.0090 1 1330 . 134 ILE HG12 H 1.2410 0.0000 1 1331 . 134 ILE HG2 H 0.9270 0.0000 1 1332 . 134 ILE H H 7.4290 0.0230 1 1333 . 134 ILE N N 118.7170 0.1730 1 1334 . 135 ARG CA C 52.6450 0.0000 1 1335 . 135 ARG CB C 31.0550 0.0000 1 1336 . 135 ARG CD C 45.0520 0.0040 1 1337 . 135 ARG CG C 25.5120 0.0890 1 1338 . 135 ARG HA H 5.0830 0.0370 1 1339 . 135 ARG HB3 H 2.1550 0.0350 1 1340 . 135 ARG HB2 H 1.8490 0.0360 1 1341 . 135 ARG HD3 H 3.7040 0.0000 1 1342 . 135 ARG HD2 H 3.2100 0.0000 1 1343 . 135 ARG HG3 H 1.9300 0.0000 1 1344 . 135 ARG HG2 H 1.6350 0.0000 1 1345 . 135 ARG H H 8.2820 0.0190 1 1346 . 135 ARG N N 115.3740 0.0810 1 1347 . 136 PRO CA C 64.2530 0.0260 1 1348 . 136 PRO CB C 31.4130 0.2610 1 1349 . 136 PRO CD C 49.6060 0.0000 1 1350 . 136 PRO CG C 26.9140 0.0000 1 1351 . 136 PRO HA H 4.7700 0.0000 1 1352 . 136 PRO HB3 H 2.4310 0.0000 1 1353 . 136 PRO HB2 H 1.8740 0.0000 1 1354 . 136 PRO HD3 H 3.7240 0.0000 1 1355 . 136 PRO HD2 H 3.4350 0.0000 1 1356 . 136 PRO HG3 H 2.0220 0.0000 1 1357 . 136 PRO HG2 H 2.0220 0.0000 1 1358 . 137 ASN CA C 52.4870 0.1450 1 1359 . 137 ASN CB C 36.8060 0.2440 1 1360 . 137 ASN HA H 4.5220 0.0000 1 1361 . 137 ASN HB3 H 2.9100 0.0560 1 1362 . 137 ASN HB2 H 2.8020 0.0000 1 1363 . 137 ASN HD21 H 7.5360 0.0000 1 1364 . 137 ASN HD22 H 6.9810 0.0000 1 1365 . 137 ASN H H 8.2190 0.0320 1 1366 . 137 ASN N N 111.8560 0.0950 1 1367 . 138 LYS CA C 56.6480 0.3470 1 1368 . 138 LYS CB C 29.0760 0.2540 1 1369 . 138 LYS CE C 41.5770 0.0000 1 1370 . 138 LYS CG C 24.0500 0.0000 1 1371 . 138 LYS HA H 2.5850 0.0270 1 1372 . 138 LYS HB3 H 1.5620 0.0000 1 1373 . 138 LYS HB2 H 1.0810 0.0150 1 1374 . 138 LYS HD3 H 1.1000 0.0000 1 1375 . 138 LYS HD2 H 1.1000 0.0000 1 1376 . 138 LYS HE3 H 2.9080 0.0000 1 1377 . 138 LYS HE2 H 2.9080 0.0000 1 1378 . 138 LYS HG3 H 1.1560 0.0510 1 1379 . 138 LYS HG2 H 0.8930 0.0000 1 1380 . 138 LYS H H 8.3790 0.0160 1 1381 . 138 LYS N N 114.0460 0.0730 1 1382 . 139 LYS CA C 57.2990 0.0000 1 1383 . 139 LYS CB C 34.3670 0.0000 1 1384 . 139 LYS CD C 28.8230 0.0000 1 1385 . 139 LYS CE C 41.4200 0.0000 1 1386 . 139 LYS CG C 24.1510 0.1620 1 1387 . 139 LYS HA H 4.3900 0.0000 1 1388 . 139 LYS HB3 H 1.7570 0.0430 1 1389 . 139 LYS HB2 H 1.5320 0.0410 1 1390 . 139 LYS HD3 H 1.6700 0.0000 1 1391 . 139 LYS HD2 H 1.6700 0.0000 1 1392 . 139 LYS HE3 H 2.9900 0.0000 1 1393 . 139 LYS HE2 H 2.9900 0.0000 1 1394 . 139 LYS HG3 H 1.3620 0.0700 1 1395 . 139 LYS HG2 H 1.3620 0.0700 1 1396 . 139 LYS H H 6.8060 0.0270 1 1397 . 139 LYS N N 119.1060 0.1480 1 stop_ save_