data_4097 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C and 15N Chemical Shift Assignment for the HIV-1 RNase H Domain ; _BMRB_accession_number 4097 _BMRB_flat_file_name bmr4097.str _Entry_type original _Submission_date 1998-01-16 _Accession_date 1998-01-16 _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 Gunther Kern . . 2 Handel Tracy M. . 3 Marqusee Susan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 111 "13C chemical shifts" 217 "15N chemical shifts" 111 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-01-25 original author . stop_ _Original_release_date 1999-01-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Kern, G., Handel, T., and Marqusee, S. "Characterization of a Folding Intermediate from HIV-1 Ribonuclease H," Protein Sci. 7, 2164-2174 (1998). ; _Citation_title 'Characterization of a Folding Intermediate from HIV-1 Ribonuclease H' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99006568 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gunther Kern . . 2 Handel Tracy M. . 3 Marqusee Susan . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume 7 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2164 _Page_last 2174 _Year 1998 _Details . loop_ _Keyword AIDS Folding 'H/D exchange' HIV-1 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995). ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _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 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ save_citation_two _Saveframe_category citation _Citation_full ; Assignment for a mutant RNase H from HIV-1 strain HXB2 is available Powers et al. 1991, J. Mol. Biol. 221 1081-90 ; _Citation_title 'Secondary structure of the ribonuclease H domain of the human immunodeficiency virus reverse transcriptase in solution using three-dimensional double and triple resonance heteronuclear magnetic resonance spectroscopy.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 1719214 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Powers R . . 2 Clore 'G M' M. . 3 Bax A . . 4 Garrett 'D S' S. . 5 Stahl 'S J' J. . 6 Wingfield 'P T' T. . 7 Gronenborn 'A M' M. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 221 _Journal_issue 4 _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 1081 _Page_last 1090 _Year 1991 _Details ; The solution structure of the ribonuclease H domain of HIV-1 reverse transcriptase has been investigated by three-dimensional double and triple resonance heteronuclear magnetic resonance spectroscopy. The domain studied has 138 residues and comprises residues 427 to 560 of the 66 kDa reverse transcriptase with an additional four residues at the N terminus. Initial studies on the wild-type protein were hindered by severe differential line broadening, presumably due to conformational averaging. Mutation of the single tryptophan residue located in a loop at position 113 (position 535 in the reverse transcriptase sequence) to an alanine resulted in much improved spectral properties with no apparent change in structure. 1H, 15N and 13C backbone resonances were assigned sequentially using a range of three-dimensional double and triple resonance heteronuclear experiments on samples of uniformly (greater than 95%) 15N and 15N/13C-labeled protein, and the secondary structure was elucidated from a qualitative analysis of data derived from three-dimensional 15N- and 13C-edited nuclear Overhauser enhancement spectra. The secondary structure comprises three alpha-helices and five strands arranged in a mixed parallel/antiparallel beta-sheet with a +1, +1, -3x, -1x topology. The C-terminal region from residue 114 onwards appears to be conformationally disordered in solution as evidenced by an almost complete absence of sequential and medium range nuclear Overhauser effects. ; save_ ################################## # Molecular system description # ################################## save_system_RNase_H-HIV-1 _Saveframe_category molecular_system _Mol_system_name 'RNase H domain of HIV-1 RVT strain BH10' _Abbreviation_common RNase_H-HIV-1 _Enzyme_commission_number 3.1.26.4 loop_ _Mol_system_component_name _Mol_label RNase_H-HIV-1_(RVT) $RNase_H-HIV-1_(RVT) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'cleaves the RNA moiety of RNA:DNA hybrids' stop_ _Database_query_date . _Details 'The assignment is done on the isolated RNase H domain' save_ ######################## # Monomeric polymers # ######################## save_RNase_H-HIV-1_(RVT) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Reverse Transcriptase of HIV-1' _Name_variant 'RNase H domain of HIV-1 Reverse Transcriptase RVT' _Abbreviation_common RNase_H-HIV-1_(RVT) _Molecular_mass 14885 _Mol_thiol_state . _Details 'RNase H, RVT heterodimer' ############################## # Polymer residue sequence # ############################## _Residue_count 135 _Mol_residue_sequence ; MYQLEKEPIVGAETFYVDGA ANRETKLGKAGYVTNKGRQK VVPLTNTTNQKTELQAIYLA LQDSGLEVNIVTDSQYALGI IQAQPDKSESELVNQIIEQL IKKEKVYLAWVPAHKGIGGN EQVDKLVSAGIRKIL ; loop_ _Residue_seq_code _Residue_label 1 MET 2 TYR 3 GLN 4 LEU 5 GLU 6 LYS 7 GLU 8 PRO 9 ILE 10 VAL 11 GLY 12 ALA 13 GLU 14 THR 15 PHE 16 TYR 17 VAL 18 ASP 19 GLY 20 ALA 21 ALA 22 ASN 23 ARG 24 GLU 25 THR 26 LYS 27 LEU 28 GLY 29 LYS 30 ALA 31 GLY 32 TYR 33 VAL 34 THR 35 ASN 36 LYS 37 GLY 38 ARG 39 GLN 40 LYS 41 VAL 42 VAL 43 PRO 44 LEU 45 THR 46 ASN 47 THR 48 THR 49 ASN 50 GLN 51 LYS 52 THR 53 GLU 54 LEU 55 GLN 56 ALA 57 ILE 58 TYR 59 LEU 60 ALA 61 LEU 62 GLN 63 ASP 64 SER 65 GLY 66 LEU 67 GLU 68 VAL 69 ASN 70 ILE 71 VAL 72 THR 73 ASP 74 SER 75 GLN 76 TYR 77 ALA 78 LEU 79 GLY 80 ILE 81 ILE 82 GLN 83 ALA 84 GLN 85 PRO 86 ASP 87 LYS 88 SER 89 GLU 90 SER 91 GLU 92 LEU 93 VAL 94 ASN 95 GLN 96 ILE 97 ILE 98 GLU 99 GLN 100 LEU 101 ILE 102 LYS 103 LYS 104 GLU 105 LYS 106 VAL 107 TYR 108 LEU 109 ALA 110 TRP 111 VAL 112 PRO 113 ALA 114 HIS 115 LYS 116 GLY 117 ILE 118 GLY 119 GLY 120 ASN 121 GLU 122 GLN 123 VAL 124 ASP 125 LYS 126 LEU 127 VAL 128 SER 129 ALA 130 GLY 131 ILE 132 ARG 133 LYS 134 ILE 135 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 1BQM "Hiv-1 RtHBY 097" 97.04 556 99.24 99.24 6.23e-81 PDB 1BQN "Tyr 188 Leu Hiv-1 RtHBY 097" 98.52 558 98.50 99.25 4.25e-82 PDB 1DLO "Human Immunodeficiency Virus Type 1" 97.04 556 99.24 99.24 6.23e-81 PDB 1EET "Hiv-1 Reverse Transcriptase In Complex With The Inhibitor Msc204" 97.78 557 98.48 99.24 2.24e-81 PDB 1HMV "The Structure Of Unliganded Reverse Transcriptase From The Human Immunodeficiency Virus Type 1" 100.00 560 99.26 99.26 8.46e-84 PDB 1HNI "Structure Of Hiv-1 Reverse Transcriptase In A Complex With The Nonnucleoside Inhibitor Alpha-Apa R 95845 At 2.8 Angstroms Resol" 98.52 558 99.25 99.25 1.40e-82 PDB 1HNV "Structure Of Hiv-1 Rt(Slash)tibo R 86183 Complex Reveals Similarity In The Binding Of Diverse Nonnucleoside Inhibitors" 98.52 558 99.25 99.25 1.40e-82 PDB 1HPZ "Human Immunodeficiency Virus Type 1" 100.00 560 99.26 99.26 8.02e-84 PDB 1HQE "Human Immunodeficiency Virus Type 1" 100.00 560 99.26 99.26 8.02e-84 PDB 1HQU "Human Immunodeficiency Virus Type 1" 100.00 560 99.26 99.26 8.02e-84 PDB 1HRH "Crystal Structure Of The Ribonuclease H Domain Of Hiv-1 Reverse Transcriptase" 99.26 136 100.00 100.00 5.33e-89 PDB 1HVU "Human Immunodeficiency Virus Type 1 Reverse Transcriptase Complexed With A 33-Base Nucleotide Rna Pseudoknot" 95.56 554 99.22 99.22 2.17e-79 PDB 1HYS "Crystal Structure Of Hiv-1 Reverse Transcriptase In Complex With A Polypurine Tract Rna:dna" 94.81 553 99.22 99.22 9.43e-79 PDB 1IKV "K103n Mutant Hiv-1 Reverse Transcriptase In Complex With Efivarenz" 100.00 560 98.52 99.26 3.12e-83 PDB 1IKW "Wild Type Hiv-1 Reverse Transcriptase In Complex With Efavirenz" 100.00 560 98.52 99.26 2.29e-83 PDB 1IKX "K103n Mutant Hiv-1 Reverse Transcriptase In Complex With The Inhibitor Pnu142721" 100.00 560 98.52 99.26 3.12e-83 PDB 1IKY "Hiv-1 Reverse Transcriptase In Complex With The Inhibitor Msc194" 100.00 560 98.52 99.26 3.12e-83 PDB 1J5O "Crystal Structure Of Met184ile Mutant Of Hiv-1 Reverse Transcriptase In Complex With Double Stranded Dna Template- Primer" 98.52 558 99.25 99.25 1.56e-82 PDB 1N5Y "Hiv-1 Reverse Transcriptase Crosslinked To Post- Translocation Aztmp-Terminated Dna (Complex P)" 98.52 558 99.25 99.25 1.54e-82 PDB 1N6Q "Hiv-1 Reverse Transcriptase Crosslinked To Pre- Translocation Aztmp-Terminated Dna (Complex N)" 98.52 558 99.25 99.25 1.54e-82 PDB 1QE1 "Crystal Structure Of 3tc-Resistant M184i Mutant Of Hiv-1 Reverse Transcriptase" 98.52 558 99.25 99.25 1.56e-82 PDB 1R0A "Crystal Structure Of Hiv-1 Reverse Transcriptase Covalently Tethered To Dna Template-primer Solved To 2.8 Angstroms" 98.52 558 99.25 99.25 1.54e-82 PDB 1RDH "Crystallographic Analyses Of An Active Hiv-1 Ribonuclease H Domain Show Structural Features That Distinguish It From The Inacti" 99.26 146 100.00 100.00 7.83e-89 PDB 1RTD "Structure Of A Catalytic Complex Of Hiv-1 Reverse Transcriptase: Implications For Nucleoside Analog Drug Resistance" 95.56 554 96.90 99.22 1.41e-77 PDB 1S6P "Crystal Structure Of Human Immunodeficiency Virus Type 1 Reverse Transcriptase (Rt) In Complex With Janssen-R100943" 100.00 560 99.26 99.26 6.98e-84 PDB 1S6Q "Crystal Structure Of Hiv-1 Reverse Transcriptase (Rt) In Complex With Janssen-R147681" 100.00 560 99.26 99.26 6.98e-84 PDB 1S9E "Crystal Structure Of Hiv-1 Reverse Transcriptase (Rt) In Complex With Janssen-R129385" 100.00 560 99.26 99.26 6.98e-84 PDB 1S9G "Crystal Structure Of Hiv-1 Reverse Transcriptase (Rt) In Complex With Janssen-R120394." 100.00 560 99.26 99.26 6.98e-84 PDB 1SUQ "Crystal Structure Of Hiv-1 Reverse Transcriptase (Rt) In Complex With Janssen-R185545" 100.00 560 99.26 99.26 6.98e-84 PDB 1SV5 "Crystal Structure Of K103n Mutant Hiv-1 Reverse Transcriptase (Rt) In Complex With Janssen-R165335" 100.00 560 99.26 99.26 8.02e-84 PDB 1T03 "Hiv-1 Reverse Transcriptase Crosslinked To Tenofovir Terminated Template-Primer (Complex P)" 98.52 558 99.25 99.25 1.54e-82 PDB 1T05 "Hiv-1 Reverse Transcriptase Crosslinked To Template-Primer With Tenofovir-Diphosphate Bound As The Incoming Nucleotide Substrat" 98.52 558 99.25 99.25 1.54e-82 PDB 1TV6 "Hiv-1 Reverse Transcriptase Complexed With Cp-94,707" 100.00 560 99.26 99.26 8.46e-84 PDB 1TVR "Hiv-1 Rt9-Cl Tibo" 98.52 558 99.25 99.25 1.40e-82 PDB 1UWB "Tyr 181 Cys Hiv-1 Rt8-Cl Tibo" 98.52 558 99.25 99.25 1.49e-82 PDB 2B5J "Crystal Structure Of Hiv-1 Reverse Transcriptase (Rt) In Complex With Janssen-R165481" 100.00 560 99.26 99.26 6.98e-84 PDB 2B6A "Crystal Structure Of Hiv-1 Reverse Transcriptase (Rt) In Complex With Thr-50" 100.00 560 99.26 99.26 6.98e-84 PDB 2BAN "Crystal Structure Of Hiv-1 Reverse Transcriptase (Rt) In Complex With Janssen-R157208" 100.00 560 99.26 99.26 6.98e-84 PDB 2BE2 "Crystal Structure Of Hiv-1 Reverse Transcriptase (Rt) In Complex With R221239" 100.00 560 99.26 99.26 6.98e-84 PDB 2HMI "Hiv-1 Reverse TranscriptaseFRAGMENT OF FAB 28DNA COMPLEX" 98.52 558 99.25 99.25 1.40e-82 PDB 2I5J "Crystal Structure Of Hiv-1 Reverse Transcriptase (Rt) In Complex With Dhbnh, An Rnase H Inhibitor" 94.07 552 99.21 99.21 4.56e-78 PDB 2IAJ "Crystal Structure Of K103nY181C MUTANT HIV-1 Reverse Transcriptase (Rt) In Complex With Atp" 100.00 560 99.26 99.26 9.42e-84 PDB 2IC3 "Crystal Structure Of K103nY181C MUTANT HIV-1 Reverse Transcriptase (Rt) In Complex With Nonnucleoside Inhibitor Hby 097" 100.00 560 99.26 99.26 9.42e-84 PDB 2VG5 "Crystal Structures Of Hiv-1 Reverse Transcriptase Complexes With Thiocarbamate Non-Nucleoside Inhibitors" 97.78 557 99.24 99.24 6.64e-82 PDB 2VG6 "Crystal Structures Of Hiv-1 Reverse Transcriptase Complexes With Thiocarbamate Non-Nucleoside Inhibitors" 97.78 557 99.24 99.24 6.64e-82 PDB 2VG7 "Crystal Structures Of Hiv-1 Reverse Transcriptase Complexes With Thiocarbamate Non-Nucleoside Inhibitors" 97.78 557 99.24 99.24 6.64e-82 PDB 2YKM "Crystal Structure Of Hiv-1 Reverse Transcriptase (Rt) In Complex With A Difluoromethylbenzoxazole (Dfmb) Pyrimidine Thioether D" 97.78 562 98.48 99.24 2.08e-81 PDB 2YKN "Crystal Structure Of Hiv-1 Reverse Transcriptase (Rt) In Complex With A Difluoromethylbenzoxazole (Dfmb) Pyrimidine Thioether D" 97.78 562 98.48 99.24 1.85e-81 PDB 2ZD1 "Crystal Structure Of Hiv-1 Reverse Transcriptase (rt) In Complex With Tmc278 (rilpivirine), A Non-nucleoside Rt Inhibitor" 96.30 557 99.23 99.23 2.47e-80 PDB 2ZE2 "Crystal Structure Of L100i/k103n Mutant Hiv-1 Reverse Transcriptase (rt) In Complex With Tmc278 (rilpivirine), A Non-nucleoside" 96.30 557 99.23 99.23 2.37e-80 PDB 3BGR "Crystal Structure Of K103n/y181c Mutant Hiv-1 Reverse Transcriptase (rt) In Complex With Tmc278 (rilpivirine), A Non-nucleoside" 96.30 557 99.23 99.23 2.47e-80 PDB 3DLK "Crystal Structure Of An Engineered Form Of The Hiv-1 Reverse Transcriptase, Rt69a" 96.30 556 99.23 99.23 2.37e-80 PDB 3HVT "Structural Basis Of Asymmetry In The Human Immunodeficiency Virus Type 1 Reverse Transcriptase Heterodimer" 97.04 556 99.24 99.24 6.72e-81 PDB 3IG1 "Hiv-1 Reverse Transcriptase With The Inhibitor Beta- Thujaplicinol Bound At The Rnase H Active Site" 96.30 555 99.23 99.23 2.63e-80 PDB 3IRX "Crystal Structure Of Hiv-1 Reverse Transcriptase (Rt) In Complex With The Non-Nucleoside Rt Inhibitor (E)-S-Methyl 5-(1-(3,7-Di" 96.30 558 99.23 99.23 2.81e-80 PDB 3IS9 "Crystal Structure Of The Hiv-1 Reverse Transcriptase (Rt) In Complex With The Alkenyldiarylmethane (Adam) Non-Nucleoside Rt Inh" 96.30 558 99.23 99.23 2.81e-80 PDB 3ISN "Crystal Structure Of Hiv-1 Rt Bound To A 6-Vinylpyrimidine Inhibitor" 100.00 560 98.52 99.26 2.29e-83 PDB 3ITH "Crystal Structure Of The Hiv-1 Reverse Transcriptase Bound To A 6-Vinylpyrimidine Inhibitor" 100.00 560 98.52 99.26 2.29e-83 PDB 3JSM "K65r Mutant Hiv-1 Reverse Transcriptase Cross-Linked To Ds-Dna And Complexed With Tenofovir-Diphosphate As The Incoming Nucleot" 98.52 558 99.25 99.25 1.61e-82 PDB 3JYT "K65r Mutant Hiv-1 Reverse Transcriptase Cross-Linked To Ds- Dna And Complexed With Datp As The Incoming Nucleotide Substrate" 98.52 558 99.25 99.25 1.61e-82 PDB 3K2P "Hiv-1 Reverse Transcriptase Isolated Rnaseh Domain With The Inhibitor Beta-Thujaplicinol Bound At The Active Site" 100.00 136 99.26 100.00 1.54e-89 PDB 3KLE "Crystal Structure Of Azt-Resistant Hiv-1 Reverse Transcriptase Crosslinked To A Dsdna With A Bound Excision Product, Aztppppa" 100.00 562 98.52 99.26 1.85e-83 PDB 3KLF "Crystal Structure Of Wild-Type Hiv-1 Reverse Transcriptase Crosslinked To A Dsdna With A Bound Excision Product, Aztppppa" 96.30 557 99.23 99.23 2.53e-80 PDB 3KLG "Crystal Structure Of Azt-Resistant Hiv-1 Reverse Transcriptase Crosslinked To Pre-Translocation Aztmp-Terminated Dna (Complex N" 100.00 562 98.52 99.26 1.85e-83 PDB 3KLH "Crystal Structure Of Azt-resistant Hiv-1 Reverse Transcriptase Crosslinked To Post-translocation Aztmp-terminated Dna (complex " 100.00 564 99.26 99.26 9.60e-84 PDB 3KLI "Crystal Structure Of Unliganded Azt-Resistant Hiv-1 Reverse Transcriptase" 100.00 562 98.52 99.26 1.85e-83 PDB 3LP3 "P15 Hiv Rnaseh Domain With Inhibitor Mk3" 99.26 138 100.00 100.00 3.72e-89 PDB 3QLH "Hiv-1 Reverse Transcriptase In Complex With Manicol At The Rnase H Active Site And Tmc278 (rilpivirine) At The Nnrti Binding Po" 95.56 555 99.22 99.22 1.93e-79 PDB 3QO9 "Crystal Structure Of Hiv-1 Reverse Transcriptase (rt) In Complex With Tsao-t, A Non-nucleoside Rt Inhibitor (nnrti)" 96.30 557 99.23 99.23 2.72e-80 PDB 3V4I "Crystal Structure Of Hiv-1 Reverse Transcriptase (Rt) With Dna And Azttp" 95.56 556 98.45 99.22 1.13e-78 PDB 3V6D "Crystal Structure Of Hiv-1 Reverse Transcriptase (Rt) Cross-Linked With Azt-Terminated Dna" 95.56 556 98.45 99.22 1.13e-78 PDB 3V81 "Crystal Structure Of Hiv-1 Reverse Transcriptase (Rt) With Dna And The Nonnucleoside Inhibitor Nevirapine" 95.56 556 98.45 99.22 1.13e-78 PDB 4DG1 "Crystal Structure Of Hiv-1 Reverse Transcriptase (Rt) With Polymorphism Mutation K172a And K173a" 91.85 549 99.19 99.19 2.80e-76 PDB 4G1Q "Crystal Structure Of Hiv-1 Reverse Transcriptase (rt) In Complex With Rilpivirine (tmc278, Edurant), A Non-nucleoside Rt-inhibi" 96.30 557 99.23 99.23 2.47e-80 PDB 4H4M "Crystal Structure Of Hiv-1 Reverse Transcriptase In Complex With (E)- 3-(3-Chloro-5-(4-Chloro-2-(2-(2,4-Dioxo-3,4- Dihydropyrim" 96.30 557 99.23 99.23 2.47e-80 PDB 4H4O "Crystal Structure Of Hiv-1 Reverse Transcriptase (Rt) In Complex With (E)-3-(3-(2-(2-(2,4-Dioxo-3,4-Dihydropyrimidin-1(2h)-Yl)e" 96.30 557 99.23 99.23 2.47e-80 PDB 4I2P "Crystal Structure Of Hiv-1 Reverse Transcriptase In Complex With Rilpivirine (tmc278) Based Analogue" 96.30 557 99.23 99.23 2.47e-80 PDB 4I2Q "Crystal Structure Of K103n/y181c Mutant Of Hiv-1 Reverse Transcriptase In Complex With Rilpivirine (tmc278) Analogue" 96.30 557 99.23 99.23 2.47e-80 PDB 4ICL "Hiv-1 Reverse Transcriptase With Bound Fragment At The Incoming Dntp Binding Site" 96.30 557 99.23 99.23 2.47e-80 PDB 4ID5 "Hiv-1 Reverse Transcriptase With Bound Fragment At The Rnase H Primer Grip Site" 96.30 557 99.23 99.23 2.47e-80 PDB 4IDK "Hiv-1 Reverse Transcriptase With Bound Fragment At The 428 Site" 96.30 557 99.23 99.23 2.47e-80 PDB 4IFV "Detecting Allosteric Sites Of Hiv-1 Reverse Transcriptase By X-ray Crystallographic Fragment Screening" 96.30 557 99.23 99.23 2.47e-80 PDB 4IFY "Hiv-1 Reverse Transcriptase With Bound Fragment At The Knuckles Site" 96.30 557 99.23 99.23 2.47e-80 PDB 4IG0 "Hiv-1 Reverse Transcriptase With Bound Fragment At The 507 Site" 96.30 557 99.23 99.23 2.47e-80 PDB 4IG3 "Hiv-1 Reverse Transcriptase With Bound Fragment Near Knuckles Site" 96.30 557 99.23 99.23 2.47e-80 PDB 4KFB "Hiv-1 Reverse Transcriptase With Bound Fragment At Nnrti Adjacent Site" 96.30 557 99.23 99.23 2.47e-80 PDB 4KKO "Crystal Structure Of Hiv-1 Reverse Transcriptase In Complex With 4- ((4-methoxy-6-(2-morpholinoethoxy)-1,3,5-triazin-2-yl)amino" 96.30 557 99.23 99.23 2.47e-80 PDB 4KO0 "Crystal Structure Of Hiv-1 Reverse Transcriptase (rt) In Complex With An Anilinylpyrimidine Derivative (jlj-135)" 96.30 557 99.23 99.23 2.47e-80 PDB 4LSL "Crystal Structure Of Hiv-1 Reverse Transcriptase In Complex With (e)- 3-(3-(4-chloro-2-(2-(2,4-dioxo-3,4-dihydropyrimidin-1(2h)" 96.30 557 99.23 99.23 2.47e-80 PDB 4LSN "Crystal Structure Of Hiv-1 Reverse Transcriptase In Complex With (e)- 3-(3-bromo-5-(4-chloro-2-(2-(2,4-dioxo-3,4-dihydropyrimid" 96.30 557 99.23 99.23 2.47e-80 PDB 4MFB "Crystal Structure Of Hiv-1 Reverse Transcriptase In Complex With 8-(2- (2-(2,4-dioxo-3,4-dihydropyrimidin-1(2h)-yl)ethoxy)pheno" 96.30 557 99.23 99.23 2.47e-80 PDB 4O44 "Crystal Structure Of Hiv-1 Reverse Transcriptase In Complex With 4- ((4-(mesitylamino)-6-(3-morpholinopropoxy)-1,3,5-triazin-2-" 96.30 557 99.23 99.23 2.47e-80 PDB 4O4G "Crystal Structure Of Hiv-1 Reverse Transcriptase In Complex With 4- ((4-(mesitylamino)-1,3,5-triazin-2-yl)amino)benzonitrile (j" 96.30 557 99.23 99.23 2.47e-80 PDB 4PQU "Crystal Structure Of Hiv-1 Reverse Transcriptase In Complex With Rna/dna And Datp" 95.56 556 98.45 99.22 1.13e-78 PDB 4PUO "Crystal Structure Of Hiv-1 Reverse Transcriptase In Complex With Rna/dna And Nevirapine" 95.56 556 98.45 99.22 1.13e-78 PDB 4PWD "Crystal Structure Of Hiv-1 Reverse Transcriptase In Complex With Bulge-rna/dna And Nevirapine" 95.56 556 98.45 99.22 1.13e-78 PDB 4Q0B "Crystal Structure Of Hiv-1 Reverse Transcriptase In Complex With Gap- Rna/dna And Nevirapine" 95.56 556 98.45 99.22 1.13e-78 PDB 4QAG "Structure Of A Dihydroxycoumarin Active-site Inhibitor In Complex With The Rnase H Domain Of Hiv-1 Reverse Transcriptase" 97.04 133 100.00 100.00 5.40e-87 PDB 4R5P "Crystal Structure Of Hiv-1 Reverse Transcriptase (rt) With Dna And A Nucleoside Triphosphate Mimic Alpha-carboxy Nucleoside Pho" 95.56 556 98.45 99.22 1.13e-78 PDB 4RW4 "Crystal Structure Of Hiv-1 Reverse Transcriptase (k103n,y181c) Variant In Complex With (e)-3-(3-chloro-5-(4-chloro-2-(2-(2,4-di" 96.30 557 99.23 99.23 2.47e-80 PDB 4RW6 "Crystal Structure Of Hiv-1 Reverse Transcriptase (y181c) Variant In Complex With (e)-3-(3-chloro-5-(4-chloro-2-(2-(2,4-dioxo-3," 96.30 557 99.23 99.23 2.61e-80 PDB 4RW7 "Crystal Structure Of Hiv-1 Reverse Transcriptase (k103n, Y181c) Variant In Complex With (e)-3-(3-chloro-5-(2-(2-(2,4-dioxo-3,4-" 96.30 557 99.23 99.23 2.47e-80 PDB 4RW8 "Crystal Structure Of Hiv-1 Reverse Transcriptase In Complex With (e)- 3-(3-chloro-5-(2-(2-(2,4-dioxo-3,4-dihydropyrimidin-1(2h)" 96.30 557 99.23 99.23 2.47e-80 PDB 4RW9 "Crystal Structure Of Hiv-1 Reverse Transcriptase (y181c) Variant In Complex With (e)-3-(3-chloro-5-(2-(2-(2,4-dioxo-3,4-dihydro" 96.30 557 99.23 99.23 2.61e-80 PDB 4WE1 "Crystal Structure Of Hiv-1 Reverse Transcriptase In Complex With 5-(2- (2-(2,4-dioxo-3,4-dihydropyrimidin-1(2h)-yl)ethoxy)pheno" 96.30 557 99.23 99.23 2.47e-80 PDB 5C24 "Crystal Structure Of Hiv-1 Reverse Transcriptase In Complex With 7- ((4-((4-cyanophenyl)amino)-1,3,5-triazin-2-yl)amino)-6,8- D" 88.89 537 99.17 99.17 2.04e-73 PDB 5C25 "Crystal Structure Of Hiv-1 Reverse Transcriptase In Complex With 6- ((4-((4-cyanophenyl)amino)-1,3,5-triazin-2-yl)amino)-5,7-di" 96.30 557 99.23 99.23 2.47e-80 PDB 5C42 "Crystal Structure Of Hiv-1 Reverse Transcriptase (k101p) Variant In Complex With 8-(2-(2-(2,4-dioxo-3,4-dihydropyrimidin-1(2h)-" 96.30 557 99.23 99.23 2.13e-80 PDB 5D3G "Structure Of Hiv-1 Reverse Transcriptase Bound To A Novel 38-mer Hairpin Template-primer Dna Aptamer" 96.30 555 99.23 99.23 2.89e-80 DBJ BAA12989 "Pol [Human immunodeficiency virus 1]" 100.00 1015 97.78 99.26 5.57e-80 GB AAA44198 "pol polyprotein, partial [Human immunodeficiency virus 1]" 100.00 1015 99.26 99.26 1.13e-80 GB AAB24839 "reverse transcriptase, RT [human immunodeficiency virus type 1 HIV-1, zidovudine (AZT)-sensitive, Peptide, 559 aa]" 99.26 559 97.01 99.25 2.04e-81 GB AAL28068 "pol protein [synthetic construct]" 100.00 739 98.52 99.26 1.67e-81 GB AAL29457 "pol protein [synthetic construct]" 100.00 739 98.52 99.26 1.67e-81 GB ADW78894 "truncated pol protein [synthetic construct]" 100.00 857 99.26 99.26 2.38e-81 PRF 1102247C "protein pol" 100.00 1015 99.26 99.26 1.13e-80 PRF 1103299E "pol gene" 100.00 1012 97.78 99.26 7.45e-80 SP P03366 "RecName: Full=Gag-Pol polyprotein; AltName: Full=Pr160Gag-Pol; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: " 99.26 1447 100.00 100.00 4.80e-80 SP P0C6F2 "RecName: Full=Gag-Pol polyprotein; AltName: Full=Pr160Gag-Pol; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: " 99.26 1435 100.00 100.00 4.81e-80 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _Organism_acronym _ICTVdb_decimal_code _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Variant _Details $RNase_H-HIV-1_(RVT) HIV-1 HIV-1 61.0.6.5.001 11678 . . Lentivirus HIV-1 BH10 pCC101 ; Family: Retroviridae, Genus: lentivirus, Type of species: HIV-1, Reference Strain: ICTVdb decimal code is 61.0.6.5.001 ; stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $RNase_H-HIV-1_(RVT) 'chemical construct' . . . HB10 plasmid pAED4 ; native (The gene was synthesized and cloned into a pAED4 vector under the control of a T7 promotor) ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $RNase_H-HIV-1_(RVT) 1.1 mM 1.05 1.15 '[U-99.8% 13C; U-99.9% 15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX600 _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 $sample_one save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_one save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_one 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 HNCA _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_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 .02 n/a pH 4.5 0.1 n/a temperature 298 .5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 _Indirect_shift_ratio_citation_label DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 $citation_one DSS H 1 'methyl protons' ppm 0.00 . direct . . . 1.0 $citation_one DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $citation_one stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name RNase_H-HIV-1_(RVT) _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 TYR CA C 57.3 0.06 1 2 . 2 TYR CB C 39.4 0.06 1 3 . 3 GLN N N 121.1 0.06 1 4 . 3 GLN H H 8.21 0.02 1 5 . 3 GLN CA C 54.3 0.06 1 6 . 3 GLN CB C 30.9 0.06 1 7 . 4 LEU N N 125.8 0.06 1 8 . 4 LEU H H 8.54 0.02 1 9 . 4 LEU CA C 54.1 0.06 1 10 . 4 LEU CB C 42.1 0.06 1 11 . 5 GLU N N 122.6 0.06 1 12 . 5 GLU H H 9.09 0.02 1 13 . 5 GLU CA C 54.9 0.06 1 14 . 5 GLU CB C 30.6 0.06 1 15 . 6 LYS N N 119.5 0.06 1 16 . 6 LYS H H 8.89 0.02 1 17 . 6 LYS CA C 56.9 0.06 1 18 . 6 LYS CB C 33.3 0.06 1 19 . 7 GLU N N 117.2 0.06 1 20 . 7 GLU H H 7.56 0.02 1 21 . 7 GLU CA C 52.8 0.06 1 22 . 8 PRO CA C 62.1 0.06 1 23 . 8 PRO CB C 31.1 0.06 1 24 . 9 ILE N N 124.9 0.06 1 25 . 9 ILE H H 9.37 0.02 1 26 . 9 ILE CA C 60.9 0.06 1 27 . 9 ILE CB C 38.5 0.06 1 28 . 10 VAL N N 132.3 0.06 1 29 . 10 VAL H H 8.7 0.02 1 30 . 10 VAL CA C 64.9 0.06 1 31 . 10 VAL CB C 31.1 0.06 1 32 . 11 GLY N N 115.1 0.06 1 33 . 11 GLY H H 8.86 0.02 1 34 . 11 GLY CA C 45.1 0.06 1 35 . 12 ALA N N 122.1 0.06 1 36 . 12 ALA H H 7.07 0.02 1 37 . 12 ALA CA C 50.6 0.06 1 38 . 12 ALA CB C 19.1 0.06 1 39 . 13 GLU N N 125.6 0.06 1 40 . 13 GLU H H 8.92 0.02 1 41 . 13 GLU CA C 57.3 0.06 1 42 . 13 GLU CB C 31 0.06 1 43 . 14 THR N N 121.9 0.06 1 44 . 14 THR H H 8.59 0.02 1 45 . 14 THR CA C 61.4 0.06 1 46 . 14 THR CB C 70.1 0.06 1 47 . 15 PHE N N 127.2 0.06 1 48 . 15 PHE H H 9.4 0.02 1 49 . 15 PHE CA C 56 0.06 1 50 . 15 PHE CB C 41 0.06 1 51 . 16 TYR N N 125 0.06 1 52 . 16 TYR H H 9.25 0.02 1 53 . 16 TYR CA C 57.1 0.06 1 54 . 17 VAL N N 114.9 0.06 1 55 . 17 VAL H H 8.42 0.02 1 56 . 17 VAL CA C 58.6 0.06 1 57 . 17 VAL CB C 33.6 0.06 1 58 . 18 ASP N N 118.8 0.06 1 59 . 18 ASP H H 8.59 0.02 1 60 . 18 ASP CA C 52.9 0.06 1 61 . 18 ASP CB C 43.6 0.06 1 62 . 19 GLY N N 108.9 0.06 1 63 . 19 GLY H H 7.96 0.02 1 64 . 19 GLY CA C 45.9 0.06 1 65 . 20 ALA N N 122.8 0.06 1 66 . 20 ALA H H 8.51 0.02 1 67 . 20 ALA CA C 51.8 0.06 1 68 . 20 ALA CB C 22.8 0.06 1 69 . 21 ALA N N 119.9 0.06 1 70 . 21 ALA H H 8.31 0.02 1 71 . 21 ALA CA C 63.5 0.06 1 72 . 21 ALA CB C 22.6 0.06 1 73 . 22 ASN N N 121.2 0.06 1 74 . 22 ASN H H 8.67 0.02 1 75 . 22 ASN CA C 52.3 0.06 1 76 . 22 ASN CB C 40.6 0.06 1 77 . 23 ARG N N 127.9 0.06 1 78 . 23 ARG H H 9.16 0.02 1 79 . 23 ARG CA C 58.7 0.06 1 80 . 23 ARG CB C 30.3 0.06 1 81 . 24 GLU N N 117.5 0.06 1 82 . 24 GLU H H 8.43 0.02 1 83 . 24 GLU CA C 58.7 0.06 1 84 . 24 GLU CB C 29.7 0.06 1 85 . 25 THR N N 108.2 0.06 1 86 . 25 THR H H 8.21 0.02 1 87 . 25 THR CA C 61.9 0.06 1 88 . 25 THR CB C 70.3 0.06 1 89 . 26 LYS N N 115.5 0.06 1 90 . 26 LYS H H 8.12 0.02 1 91 . 26 LYS CA C 57.8 0.06 1 92 . 26 LYS CB C 29 0.06 1 93 . 27 LEU N N 117.6 0.06 1 94 . 27 LEU H H 7.5 0.02 1 95 . 27 LEU CA C 54.1 0.06 1 96 . 27 LEU CB C 45.9 0.06 1 97 . 28 GLY N N 108.7 0.06 1 98 . 28 GLY H H 7.92 0.02 1 99 . 28 GLY CA C 45.9 0.06 1 100 . 29 LYS N N 119.4 0.06 1 101 . 29 LYS H H 9.02 0.02 1 102 . 29 LYS CA C 55.7 0.06 1 103 . 30 ALA N N 121 0.06 1 104 . 30 ALA H H 8.4 0.02 1 105 . 30 ALA CA C 50.1 0.06 1 106 . 30 ALA CB C 21.4 0.06 1 107 . 31 GLY N N 106.2 0.06 1 108 . 31 GLY H H 8.66 0.02 1 109 . 31 GLY CA C 46.8 0.06 1 110 . 32 TYR N N 111.2 0.06 1 111 . 32 TYR H H 8.54 0.02 1 112 . 32 TYR CA C 55.4 0.06 1 113 . 32 TYR CB C 43.3 0.06 1 114 . 33 VAL N N 115.3 0.06 1 115 . 33 VAL H H 8.77 0.02 1 116 . 33 VAL CA C 61 0.06 1 117 . 33 VAL CB C 36.1 0.06 1 118 . 34 THR N N 114.8 0.06 1 119 . 34 THR H H 9.06 0.02 1 120 . 34 THR CA C 57.5 0.06 1 121 . 34 THR CB C 72.8 0.06 1 122 . 35 ASN N N 119 0.06 1 123 . 35 ASN H H 9.14 0.02 1 124 . 35 ASN CA C 54.3 0.06 1 125 . 35 ASN CB C 37.5 0.06 1 126 . 36 LYS N N 118.1 0.06 1 127 . 36 LYS H H 8.04 0.02 1 128 . 36 LYS CA C 55 0.06 1 129 . 36 LYS CB C 32 0.06 1 130 . 37 GLY N N 107.6 0.06 1 131 . 37 GLY H H 7.88 0.02 1 132 . 37 GLY CA C 45.6 0.06 1 133 . 38 ARG N N 118.2 0.06 1 134 . 38 ARG H H 7.24 0.02 1 135 . 38 ARG CA C 56.3 0.06 1 136 . 38 ARG CB C 31.9 0.06 1 137 . 39 GLN N N 117.7 0.06 1 138 . 39 GLN H H 8.56 0.02 1 139 . 39 GLN CA C 54.7 0.06 1 140 . 39 GLN CB C 32.9 0.06 1 141 . 40 LYS N N 123.2 0.06 1 142 . 40 LYS H H 7.91 0.02 1 143 . 40 LYS CA C 56.5 0.06 1 144 . 40 LYS CB C 33.1 0.06 1 145 . 41 VAL N N 123.3 0.06 1 146 . 41 VAL H H 8.24 0.02 1 147 . 41 VAL CA C 60.5 0.06 1 148 . 41 VAL CB C 34.9 0.06 1 149 . 42 VAL N N 124.9 0.06 1 150 . 42 VAL H H 9.35 0.02 1 151 . 42 VAL CA C 57.6 0.06 1 152 . 43 PRO CA C 61.6 0.06 1 153 . 43 PRO CB C 32.3 0.06 1 154 . 44 LEU N N 122.1 0.06 1 155 . 44 LEU H H 8.56 0.02 1 156 . 44 LEU CA C 53.9 0.06 1 157 . 44 LEU CB C 46.9 0.06 1 158 . 45 THR N N 112.1 0.06 1 159 . 45 THR H H 8.23 0.02 1 160 . 45 THR CA C 59.8 0.06 1 161 . 45 THR CB C 71.4 0.06 1 162 . 46 ASN N N 120.7 0.06 1 163 . 46 ASN H H 8.71 0.02 1 164 . 46 ASN CA C 53.9 0.06 1 165 . 46 ASN CB C 37.3 0.06 1 166 . 47 THR N N 114.7 0.06 1 167 . 47 THR H H 9.09 0.02 1 168 . 47 THR CA C 59.8 0.06 1 169 . 47 THR CB C 70.2 0.06 1 170 . 48 THR N N 109.1 0.06 1 171 . 48 THR H H 8.15 0.02 1 172 . 48 THR CA C 58.5 0.06 1 173 . 48 THR CB C 73.1 0.06 1 174 . 49 ASN N N 121.7 0.06 1 175 . 49 ASN H H 9.2 0.02 1 176 . 49 ASN CA C 57.3 0.06 1 177 . 49 ASN CB C 38.2 0.06 1 178 . 50 GLN N N 118.7 0.06 1 179 . 50 GLN H H 8.65 0.02 1 180 . 50 GLN CA C 59.8 0.06 1 181 . 50 GLN CB C 28.4 0.06 1 182 . 51 LYS N N 117.5 0.06 1 183 . 51 LYS H H 7.5 0.02 1 184 . 51 LYS CA C 60.6 0.06 1 185 . 51 LYS CB C 32.4 0.06 1 186 . 52 THR N N 110.7 0.06 1 187 . 52 THR H H 8.33 0.02 1 188 . 52 THR CA C 52.9 0.06 1 189 . 52 THR CB C 68.4 0.06 1 190 . 53 GLU N N 121.4 0.06 1 191 . 53 GLU H H 7.56 0.02 1 192 . 53 GLU CA C 58.8 0.06 1 193 . 54 LEU N N 118.5 0.06 1 194 . 54 LEU H H 7.64 0.02 1 195 . 54 LEU CA C 57.6 0.06 1 196 . 54 LEU CB C 41.8 0.06 1 197 . 55 GLN N N 120.1 0.06 1 198 . 55 GLN H H 8.87 0.02 1 199 . 55 GLN CA C 58.6 0.06 1 200 . 55 GLN CB C 27.4 0.06 1 201 . 56 ALA N N 121.1 0.06 1 202 . 56 ALA H H 8.01 0.02 1 203 . 56 ALA CA C 55.7 0.06 1 204 . 56 ALA CB C 19.1 0.06 1 205 . 57 ILE N N 115.9 0.06 1 206 . 57 ILE H H 7.16 0.02 1 207 . 57 ILE CA C 65.6 0.06 1 208 . 57 ILE CB C 38 0.06 1 209 . 58 TYR N N 119.6 0.06 1 210 . 58 TYR H H 8.22 0.02 1 211 . 58 TYR CA C 61.2 0.06 1 212 . 58 TYR CB C 37.5 0.06 1 213 . 59 LEU N N 118.6 0.06 1 214 . 59 LEU H H 8.43 0.02 1 215 . 59 LEU CA C 57.5 0.06 1 216 . 59 LEU CB C 42.6 0.06 1 217 . 60 ALA N N 118.1 0.06 1 218 . 60 ALA H H 7.43 0.02 1 219 . 60 ALA CA C 53.8 0.06 1 220 . 60 ALA CB C 19.2 0.06 1 221 . 61 LEU N N 116.8 0.06 1 222 . 61 LEU H H 7.84 0.02 1 223 . 61 LEU CA C 57.5 0.06 1 224 . 61 LEU CB C 41.5 0.06 1 225 . 62 GLN N N 118 0.06 1 226 . 62 GLN H H 8.23 0.02 1 227 . 62 GLN CA C 58.9 0.06 1 228 . 62 GLN CB C 30 0.06 1 229 . 63 ASP N N 115.7 0.06 1 230 . 63 ASP H H 7.49 0.02 1 231 . 63 ASP CA C 54.3 0.06 1 232 . 63 ASP CB C 39.3 0.06 1 233 . 64 SER N N 113.2 0.06 1 234 . 64 SER H H 7.06 0.02 1 235 . 64 SER CA C 55.9 0.06 1 236 . 64 SER CB C 67.6 0.06 1 237 . 65 GLY N N 105.3 0.06 1 238 . 65 GLY H H 8.33 0.02 1 239 . 65 GLY CA C 43.8 0.06 1 240 . 66 LEU N N 117.9 0.06 1 241 . 66 LEU H H 8.42 0.02 1 242 . 66 LEU CA C 57.6 0.06 1 243 . 66 LEU CB C 42.9 0.06 1 244 . 67 GLU N N 115.2 0.06 1 245 . 67 GLU H H 7.67 0.02 1 246 . 67 GLU CA C 53.6 0.06 1 247 . 67 GLU CB C 31.3 0.06 1 248 . 68 VAL N N 119.6 0.06 1 249 . 68 VAL H H 8.04 0.02 1 250 . 68 VAL CA C 61 0.06 1 251 . 68 VAL CB C 34.9 0.06 1 252 . 69 ASN N N 123.2 0.06 1 253 . 69 ASN H H 7.79 0.02 1 254 . 69 ASN CA C 51.8 0.06 1 255 . 69 ASN CB C 41.5 0.06 1 256 . 70 ILE N N 125.2 0.06 1 257 . 70 ILE H H 9.76 0.02 1 258 . 70 ILE CA C 60.7 0.06 1 259 . 70 ILE CB C 40.6 0.06 1 260 . 71 VAL N N 126.5 0.06 1 261 . 71 VAL H H 8.91 0.02 1 262 . 71 VAL CA C 60.7 0.06 1 263 . 71 VAL CB C 33.7 0.06 1 264 . 75 GLN CA C 58.3 0.06 1 265 . 75 GLN CB C 27.8 0.06 1 266 . 76 TYR N N 120 0.06 1 267 . 76 TYR H H 8.23 0.02 1 268 . 76 TYR CA C 60 0.06 1 269 . 76 TYR CB C 38.7 0.06 1 270 . 77 ALA N N 121 0.06 1 271 . 77 ALA H H 8.15 0.02 1 272 . 77 ALA CA C 54.2 0.06 1 273 . 77 ALA CB C 18.6 0.06 1 274 . 78 LEU N N 115.5 0.06 1 275 . 78 LEU H H 7.39 0.02 1 276 . 78 LEU CA C 57.6 0.06 1 277 . 78 LEU CB C 41.8 0.06 1 278 . 79 GLY N N 105.1 0.06 1 279 . 79 GLY H H 7.88 0.02 1 280 . 79 GLY CA C 46.6 0.06 1 281 . 80 ILE N N 120.1 0.06 1 282 . 80 ILE H H 7.37 0.02 1 283 . 80 ILE CA C 62.3 0.06 1 284 . 80 ILE CB C 37.5 0.06 1 285 . 81 ILE N N 117.3 0.06 1 286 . 81 ILE H H 7.39 0.02 1 287 . 81 ILE CA C 63.5 0.06 1 288 . 82 GLN CA C 57 0.06 1 289 . 82 GLN CB C 29 0.06 1 290 . 83 ALA N N 121.1 0.06 1 291 . 83 ALA H H 7.44 0.02 1 292 . 83 ALA CA C 52.6 0.06 1 293 . 83 ALA CB C 19 0.06 1 294 . 84 GLN N N 116.4 0.06 1 295 . 84 GLN H H 8.06 0.02 1 296 . 84 GLN CA C 54.7 0.06 1 297 . 85 PRO CA C 63.1 0.06 1 298 . 85 PRO CB C 31.9 0.06 1 299 . 86 ASP N N 119.1 0.06 1 300 . 86 ASP H H 8.3 0.02 1 301 . 86 ASP CA C 53.7 0.06 1 302 . 86 ASP CB C 41.3 0.06 1 303 . 87 LYS N N 120.2 0.06 1 304 . 87 LYS H H 8.21 0.02 1 305 . 87 LYS CA C 56.8 0.06 1 306 . 87 LYS CB C 32.8 0.06 1 307 . 88 SER N N 115.9 0.06 1 308 . 88 SER H H 8.53 0.02 1 309 . 88 SER CA C 58.6 0.06 1 310 . 88 SER CB C 63.8 0.06 1 311 . 89 GLU N N 122.7 0.06 1 312 . 89 GLU H H 8.34 0.02 1 313 . 89 GLU CA C 56.2 0.06 1 314 . 89 GLU CB C 29 0.06 1 315 . 90 SER N N 114.8 0.06 1 316 . 90 SER H H 8.1 0.02 1 317 . 90 SER CA C 57.9 0.06 1 318 . 90 SER CB C 63.3 0.06 1 319 . 91 GLU N N 126.7 0.06 1 320 . 91 GLU H H 8.8 0.02 1 321 . 91 GLU CA C 59.1 0.06 1 322 . 91 GLU CB C 28.6 0.06 1 323 . 92 LEU N N 120 0.06 1 324 . 92 LEU H H 7.88 0.02 1 325 . 92 LEU CA C 57.3 0.06 1 326 . 92 LEU CB C 42.1 0.06 1 327 . 93 VAL N N 118.2 0.06 1 328 . 93 VAL H H 7.57 0.02 1 329 . 93 VAL CA C 67.3 0.06 1 330 . 93 VAL CB C 31.2 0.06 1 331 . 94 ASN N N 117.4 0.06 1 332 . 94 ASN H H 8.01 0.02 1 333 . 94 ASN CA C 56.7 0.06 1 334 . 94 ASN CB C 37.8 0.06 1 335 . 95 GLN N N 119.6 0.06 1 336 . 95 GLN H H 8.16 0.02 1 337 . 95 GLN CA C 59 0.06 1 338 . 95 GLN CB C 27.9 0.06 1 339 . 96 ILE N N 121.5 0.06 1 340 . 96 ILE H H 8.05 0.02 1 341 . 96 ILE CA C 66.2 0.06 1 342 . 96 ILE CB C 37.8 0.06 1 343 . 97 ILE N N 121.4 0.06 1 344 . 97 ILE H H 8.54 0.02 1 345 . 97 ILE CA C 65.5 0.06 1 346 . 97 ILE CB C 37.2 0.06 1 347 . 98 GLU N N 116.4 0.06 1 348 . 98 GLU H H 7.99 0.02 1 349 . 98 GLU CA C 59.1 0.06 1 350 . 98 GLU CB C 28.6 0.06 1 351 . 99 GLN N N 114.9 0.06 1 352 . 99 GLN H H 7.47 0.02 1 353 . 99 GLN CA C 57.4 0.06 1 354 . 99 GLN CB C 29.5 0.06 1 355 . 100 LEU N N 121.5 0.06 1 356 . 100 LEU H H 8.55 0.02 1 357 . 100 LEU CA C 58.5 0.06 1 358 . 100 LEU CB C 41.8 0.06 1 359 . 101 ILE N N 112.4 0.06 1 360 . 101 ILE H H 7.88 0.02 1 361 . 101 ILE CA C 64.1 0.06 1 362 . 101 ILE CB C 38.1 0.06 1 363 . 102 LYS N N 117.2 0.06 1 364 . 102 LYS H H 6.98 0.02 1 365 . 102 LYS CA C 56.7 0.06 1 366 . 102 LYS CB C 33.1 0.06 1 367 . 103 LYS N N 117 0.06 1 368 . 103 LYS H H 7.44 0.02 1 369 . 103 LYS CA C 54.1 0.06 1 370 . 103 LYS CB C 32.7 0.06 1 371 . 104 GLU N N 120.1 0.06 1 372 . 104 GLU H H 9.17 0.02 1 373 . 104 GLU CA C 58 0.06 1 374 . 104 GLU CB C 30.5 0.06 1 375 . 105 LYS N N 115.3 0.06 1 376 . 105 LYS H H 7.72 0.02 1 377 . 105 LYS CA C 56.1 0.06 1 378 . 105 LYS CB C 33.7 0.06 1 379 . 106 VAL N N 120.9 0.06 1 380 . 106 VAL H H 8.86 0.02 1 381 . 106 VAL CA C 60.5 0.06 1 382 . 106 VAL CB C 35.6 0.06 1 383 . 107 TYR N N 129.4 0.06 1 384 . 107 TYR H H 8.5 0.02 1 385 . 107 TYR CA C 56.3 0.06 1 386 . 107 TYR CB C 40.5 0.06 1 387 . 108 LEU N N 128.9 0.06 1 388 . 108 LEU H H 7.94 0.02 1 389 . 108 LEU CA C 52.6 0.06 1 390 . 108 LEU CB C 45.4 0.06 1 391 . 109 ALA N N 124.9 0.06 1 392 . 109 ALA H H 8.53 0.02 1 393 . 109 ALA CA C 50.8 0.06 1 394 . 112 PRO CA C 62.1 0.06 1 395 . 112 PRO CB C 31.9 0.06 1 396 . 113 ALA N N 122.2 0.06 1 397 . 113 ALA H H 8.19 0.02 1 398 . 113 ALA CA C 52.1 0.06 1 399 . 113 ALA CB C 19.5 0.06 1 400 . 114 HIS N N 115.5 0.06 1 401 . 114 HIS H H 8.58 0.02 1 402 . 114 HIS CA C 55.4 0.06 1 403 . 114 HIS CB C 28 0.06 1 404 . 115 LYS N N 120.1 0.06 1 405 . 115 LYS H H 8.19 0.02 1 406 . 115 LYS CA C 55.6 0.06 1 407 . 115 LYS CB C 33.1 0.06 1 408 . 116 GLY N N 110.1 0.06 1 409 . 116 GLY H H 8.58 0.02 1 410 . 116 GLY CA C 45.3 0.06 1 411 . 117 ILE N N 119.7 0.06 1 412 . 117 ILE H H 7.93 0.02 1 413 . 117 ILE CA C 60.8 0.06 1 414 . 117 ILE CB C 42.1 0.06 1 415 . 118 GLY N N 114.3 0.06 1 416 . 118 GLY H H 8.63 0.02 1 417 . 118 GLY CA C 45.9 0.06 1 418 . 128 SER N N 116.2 0.06 1 419 . 128 SER H H 8.37 0.02 1 420 . 128 SER CA C 58.6 0.06 1 421 . 128 SER CB C 63.6 0.06 1 422 . 129 ALA N N 122.4 0.06 1 423 . 129 ALA H H 8.33 0.02 1 424 . 129 ALA CA C 56.3 0.06 1 425 . 130 GLY N N 110.7 0.06 1 426 . 130 GLY H H 8.42 0.02 1 427 . 130 GLY CA C 45.5 0.06 1 428 . 131 ILE N N 120.3 0.06 1 429 . 131 ILE H H 8.06 0.02 1 430 . 131 ILE CA C 60.5 0.06 1 431 . 133 LYS CA C 56.2 0.06 1 432 . 133 LYS CB C 33.2 0.06 1 433 . 134 ILE N N 123.6 0.06 1 434 . 134 ILE H H 8.24 0.02 1 435 . 134 ILE CA C 61 0.06 1 436 . 134 ILE CB C 38.7 0.06 1 437 . 135 LEU N N 131.3 0.06 1 438 . 135 LEU H H 7.93 0.02 1 439 . 135 LEU CA C 56.4 0.06 1 stop_ save_