data_16694 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of the Second Bromodomain of Human Polybromo in complex with an acetylated peptide from Histone 3 ; _BMRB_accession_number 16694 _BMRB_flat_file_name bmr16694.str _Entry_type new _Submission_date 2010-01-27 _Accession_date 2010-01-27 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Solution structure of the second bromodomain of Human Polybromo with Histone 3 K14-acetyl peptide' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Charlop-Powers Zachary . . 2 Zhang Qiang . . 3 Zeng Lei . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 687 "13C chemical shifts" 379 "15N chemical shifts" 113 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-03 update BMRB 'edit assembly name' 2010-05-05 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural insights into selective histone H3 recognition by the human Polybromo bromodomain 2.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20368734 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Charlop-Powers Zachary . . 2 Zeng Lei . . 3 Zhang Qiang . . 4 Zhou Ming-Ming . . stop_ _Journal_abbreviation 'Cell Res.' _Journal_name_full 'Cell research' _Journal_volume 20 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 529 _Page_last 538 _Year 2010 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Human Polybromo/Histone 3 complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label H3_Peptide $H3_Peptide Polybromo_Bromdomain2 $Polybromo_Bromdomain2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_H3_Peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common H3_Peptide _Molecular_mass 2061.412 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 20 _Mol_residue_sequence ARTKQTARKSTGGKAPRKQL loop_ _Residue_seq_code _Residue_label 1 ALA 2 ARG 3 THR 4 LYS 5 GLN 6 THR 7 ALA 8 ARG 9 LYS 10 SER 11 THR 12 GLY 13 GLY 14 LYS 15 ALA 16 PRO 17 ARG 18 LYS 19 GLN 20 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-07 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 18385 H3(1-59) 100.00 59 100.00 100.00 1.22e-02 PDB 1EQZ "X-Ray Structure Of The Nucleosome Core Particle At 2.5 A Resolution" 100.00 136 100.00 100.00 7.86e-03 PDB 1F66 "2.6 A Crystal Structure Of A Nucleosome Core Particle Containing The Variant Histone H2a.Z" 100.00 136 100.00 100.00 6.66e-03 PDB 1HQ3 "Crystal Structure Of The Histone-Core-Octamer In KclPHOSPHATE" 100.00 136 100.00 100.00 7.86e-03 PDB 1ID3 "Crystal Structure Of The Yeast Nucleosome Core Particle Reveals Fundamental Differences In Inter-Nucleosome Interactions" 100.00 135 100.00 100.00 7.00e-03 PDB 1KX3 "X-Ray Structure Of The Nucleosome Core Particle, Ncp146, At 2.0 A Resolution" 100.00 135 100.00 100.00 7.44e-03 PDB 1KX4 "X-Ray Structure Of The Nucleosome Core Particle, Ncp146b, At 2.6 A Resolution" 100.00 135 100.00 100.00 7.44e-03 PDB 1KX5 "X-ray Structure Of The Nucleosome Core Particle, Ncp147, At 1.9 A Resolution" 100.00 135 100.00 100.00 7.44e-03 PDB 1M18 "Ligand Binding Alters The Structure And Dynamics Of Nucleosomal Dna" 100.00 135 100.00 100.00 7.37e-03 PDB 1M19 "Ligand Binding Alters The Structure And Dynamics Of Nucleosomal Dna" 100.00 135 100.00 100.00 7.37e-03 PDB 1M1A "Ligand Binding Alters The Structure And Dynamics Of Nucleosomal Dna" 100.00 135 100.00 100.00 7.37e-03 PDB 1P34 "Crystallographic Studies Of Nucleosome Core Particles Containing Histone 'sin' Mutants" 100.00 135 100.00 100.00 6.79e-03 PDB 1P3A "Crystallographic Studies Of Nucleosome Core Particles Containing Histone 'sin' Mutants" 100.00 135 100.00 100.00 6.58e-03 PDB 1P3B "Crystallographic Studies Of Nucleosome Core Particles Containing Histone 'sin' Mutants" 100.00 135 100.00 100.00 6.93e-03 PDB 1P3F "Crystallographic Studies Of Nucleosome Core Particles Containing Histone 'sin' Mutants" 100.00 135 100.00 100.00 6.93e-03 PDB 1P3G "Crystallographic Studies Of Nucleosome Core Particles Containing Histone 'sin' Mutants" 100.00 135 100.00 100.00 6.93e-03 PDB 1P3I "Crystallographic Studies Of Nucleosome Core Particles Containing Histone 'sin' Mutants" 100.00 135 100.00 100.00 6.93e-03 PDB 1P3K "Crystallographic Studies Of Nucleosome Core Particles Containing Histone 'sin' Mutants" 100.00 135 100.00 100.00 6.93e-03 PDB 1P3L "Crystallographic Studies Of Nucleosome Core Particles Containing Histone 'sin' Mutants" 100.00 135 100.00 100.00 6.86e-03 PDB 1P3M "Crystallographic Studies Of Nucleosome Core Particles Containing Histone 'sin' Mutants" 100.00 135 100.00 100.00 6.79e-03 PDB 1P3O "Crystallographic Studies Of Nucleosome Core Particles Containing Histone 'sin' Mutants" 100.00 135 100.00 100.00 6.93e-03 PDB 1P3P "Crystallographic Studies Of Nucleosome Core Particles Containing Histone 'sin' Mutants" 100.00 135 100.00 100.00 6.93e-03 PDB 1PU9 "Crystal Structure Of Tetrahymena Gcn5 With Bound Coenzyme A And A 19-Residue Histone H3 Peptide" 80.00 19 100.00 100.00 1.82e+00 PDB 1S32 "Molecular Recognition Of The Nucleosomal 'supergroove'" 100.00 135 100.00 100.00 7.44e-03 PDB 1TZY "Crystal Structure Of The Core-Histone Octamer To 1.90 Angstrom Resolution" 100.00 136 100.00 100.00 7.86e-03 PDB 1U35 "Crystal Structure Of The Nucleosome Core Particle Containing The Histone Domain Of Macroh2a" 100.00 136 100.00 100.00 8.27e-03 PDB 1ZBB "Structure Of The 4_601_167 Tetranucleosome" 100.00 135 100.00 100.00 7.44e-03 PDB 1ZLA "X-Ray Structure Of A Kaposi's Sarcoma Herpesvirus Lana Peptide Bound To The Nucleosomal Core" 100.00 135 100.00 100.00 7.00e-03 PDB 2ARO "Crystal Structure Of The Native Histone Octamer To 2.1 Angstrom Resolution, Crystalised In The Presence Of S-nitrosoglutathione" 100.00 136 100.00 100.00 7.86e-03 PDB 2CV5 "Crystal Structure Of Human Nucleosome Core Particle" 100.00 136 100.00 100.00 8.27e-03 PDB 2F8N "2.9 Angstrom X-Ray Structure Of Hybrid Macroh2a Nucleosomes" 100.00 136 100.00 100.00 7.86e-03 PDB 2FJ7 "Crystal Structure Of Nucleosome Core Particle Containing A Poly (Da.Dt) Sequence Element" 100.00 135 100.00 100.00 7.44e-03 PDB 2HIO "Histone Octamer (Chicken), Chromosomal Protein" 100.00 136 100.00 100.00 7.86e-03 PDB 2IO5 "Crystal Structure Of The Cia- Histone H3-H4 Complex" 100.00 135 100.00 100.00 8.17e-03 PDB 2KFT "Nmr Solution Structure Of The First Phd Finger Domain Of Human Autoimmune Regulator (Aire) In Complex With Histone H3(1-20cys) " 100.00 21 100.00 100.00 9.15e-03 PDB 2KWK "Solution Structures Of The Double Phd Fingers Of Human Transcriptional Protein Dpf3b Bound To A H3 Peptide Wild Type" 100.00 20 100.00 100.00 9.92e-03 PDB 2NQB "Drosophila Nucleosome Structure" 100.00 135 100.00 100.00 8.17e-03 PDB 2NZD "Nucleosome Core Particle Containing 145 Bp Of Dna" 100.00 135 100.00 100.00 7.44e-03 PDB 2PYO "Drosophila Nucleosome Core" 100.00 135 100.00 100.00 8.17e-03 PDB 2YBA "Crystal Structure Of Nurf55 In Complex With Histone H3" 95.00 19 100.00 100.00 5.92e-02 PDB 3A1B "Crystal Structure Of The Dnmt3a Add Domain In Complex With Histone H3" 100.00 159 100.00 100.00 3.72e-04 PDB 3A6N "The Nucleosome Containing A Testis-Specific Histone Variant, Human H3t" 100.00 139 100.00 100.00 7.76e-03 PDB 3AFA "The Human Nucleosome Structure" 100.00 139 100.00 100.00 8.79e-03 PDB 3AV1 "The Human Nucleosome Structure Containing The Histone Variant H3.2" 100.00 139 100.00 100.00 8.61e-03 PDB 3AV2 "The Human Nucleosome Structure Containing The Histone Variant H3.3" 100.00 139 100.00 100.00 9.26e-03 PDB 3AYW "Crystal Structure Of Human Nucleosome Core Particle Containing H3k56q Mutation" 100.00 139 100.00 100.00 8.79e-03 PDB 3AZE "Crystal Structure Of Human Nucleosome Core Particle Containing H3k64q Mutation" 100.00 139 100.00 100.00 8.79e-03 PDB 3AZF "Crystal Structure Of Human Nucleosome Core Particle Containing H3k79q Mutation" 100.00 139 100.00 100.00 8.79e-03 PDB 3AZG "Crystal Structure Of Human Nucleosome Core Particle Containing H3k115q Mutation" 100.00 139 100.00 100.00 8.79e-03 PDB 3AZH "Crystal Structure Of Human Nucleosome Core Particle Containing H3k122q Mutation" 100.00 139 100.00 100.00 8.79e-03 PDB 3AZI "Crystal Structure Of Human Nucleosome Core Particle Containing H4k31q Mutation" 100.00 139 100.00 100.00 8.79e-03 PDB 3AZJ "Crystal Structure Of Human Nucleosome Core Particle Containing H4k44q Mutation" 100.00 139 100.00 100.00 8.79e-03 PDB 3AZK "Crystal Structure Of Human Nucleosome Core Particle Containing H4k59q Mutation" 100.00 139 100.00 100.00 8.79e-03 PDB 3AZL "Crystal Structure Of Human Nucleosome Core Particle Containing H4k77q Mutation" 100.00 139 100.00 100.00 8.79e-03 PDB 3AZM "Crystal Structure Of Human Nucleosome Core Particle Containing H4k79q Mutation" 100.00 139 100.00 100.00 8.79e-03 PDB 3AZN "Crystal Structure Of Human Nucleosome Core Particle Containing H4k91q Mutation" 100.00 139 100.00 100.00 8.79e-03 PDB 3B6F "Nucleosome Core Particle Treated With Cisplatin" 100.00 135 100.00 100.00 7.44e-03 PDB 3B6G "Nucleosome Core Particle Treated With Oxaliplatin" 100.00 135 100.00 100.00 7.44e-03 PDB 3C1B "The Effect Of H3 K79 Dimethylation And H4 K20 Trimethylation On Nucleosome And Chromatin Structure" 100.00 135 100.00 100.00 7.44e-03 PDB 3C1C "The Effect Of H3 K79 Dimethylation And H4 K20 Trimethylation On Nucleosome And Chromatin Structure" 100.00 135 100.00 100.00 6.65e-03 PDB 3C9K "Model Of Histone Octamer Tubular Crystals" 100.00 135 100.00 100.00 8.17e-03 PDB 3KUY "Dna Stretching In The Nucleosome Facilitates Alkylation By An Intercalating Antitumor Agent" 100.00 135 100.00 100.00 7.44e-03 PDB 3KXB "Structural Characterization Of H3k56q Nucleosomes And Nucleosomal Arrays" 100.00 135 100.00 100.00 7.14e-03 PDB 3LEL "Structural Insight Into The Sequence-Dependence Of Nucleosom Positioning" 100.00 136 100.00 100.00 7.31e-03 PDB 3LJA "Using Soft X-rays For A Detailed Picture Of Divalent Metal Binding In The Nucleosome" 100.00 135 100.00 100.00 7.44e-03 PDB 3LZ0 "Crystal Structure Of Nucleosome Core Particle Composed Of The Widom 601 Dna Sequence (Orientation 1)" 100.00 135 100.00 100.00 7.44e-03 PDB 3LZ1 "Crystal Structure Of Nucleosome Core Particle Composed Of The Widom 601 Dna Sequence (Orientation 2)" 100.00 135 100.00 100.00 7.44e-03 PDB 3MGP "Binding Of Cobalt Ions To The Nucleosome Core Particle" 100.00 135 100.00 100.00 7.44e-03 PDB 3MGQ "Binding Of Nickel Ions To The Nucleosome Core Particle" 100.00 135 100.00 100.00 7.44e-03 PDB 3MGR "Binding Of Rubidium Ions To The Nucleosome Core Particle" 100.00 135 100.00 100.00 7.44e-03 PDB 3MGS "Binding Of Cesium Ions To The Nucleosome Core Particle" 100.00 135 100.00 100.00 7.44e-03 PDB 3MNN "A Ruthenium Antitumour Agent Forms Specific Histone Protein Adducts In The Nucleosome Core" 100.00 135 100.00 100.00 7.44e-03 PDB 3MVD "Crystal Structure Of The Chromatin Factor Rcc1 In Complex With The Nucleosome Core Particle" 100.00 135 100.00 100.00 7.44e-03 PDB 3O62 "Nucleosome Core Particle Modified With A Cisplatin 1,3-Cis-{pt(Nh3) 2}2+-D(Gptpg) Intrastrand Cross-Link" 100.00 135 100.00 100.00 7.44e-03 PDB 3REH "2.5 Angstrom Crystal Structure Of The Nucleosome Core Particle Assembled With A 145 Bp Alpha-Satellite Dna (Ncp145)" 100.00 135 100.00 100.00 7.44e-03 PDB 3REI "2.65 Angstrom Crystal Structure Of The Nucleosome Core Particle Assembled With A 145 Bp Alpha-Satellite Dna (Ncp145) Derivatize" 100.00 135 100.00 100.00 7.44e-03 PDB 3REJ "2.55 Angstrom Crystal Structure Of The Nucleosome Core Particle Assembled With A 146 Bp Alpha-Satellite Dna (Ncp146b)" 100.00 135 100.00 100.00 7.44e-03 PDB 3REK "2.6 Angstrom Crystal Structure Of The Nucleosome Core Particle Assembled With A 146 Bp Alpha-Satellite Dna (Ncp146b) Derivatize" 100.00 135 100.00 100.00 7.44e-03 PDB 3REL "2.7 Angstrom Crystal Structure Of The Nucleosome Core Particle Assembled With A 146 Bp Alpha-Satellite Dna (Ncp146b) Derivatize" 100.00 135 100.00 100.00 7.44e-03 PDB 3TU4 "Crystal Structure Of The Sir3 Bah Domain In Complex With A Nucleosome Core Particle." 100.00 135 100.00 100.00 7.44e-03 PDB 3UT9 "Crystal Structure Of Nucleosome Core Particle Assembled With A Palindromic Widom '601' Derivative (ncp-601l)" 100.00 135 100.00 100.00 7.44e-03 PDB 3UTA "Crystal Structure Of Nucleosome Core Particle Assembled With An Alpha- Satellite Sequence Containing Two Ttaaa Elements (ncp-ta" 100.00 135 100.00 100.00 7.44e-03 PDB 3UTB "Crystal Structure Of Nucleosome Core Particle Assembled With The 146b Alpha-satellite Sequence (ncp146b)" 100.00 135 100.00 100.00 7.44e-03 PDB 3W96 "Crystal Structure Of Human Nucleosome Core Particle Lacking H2a N- Terminal Region" 100.00 139 100.00 100.00 8.79e-03 PDB 3W97 "Crystal Structure Of Human Nucleosome Core Particle Lacking H2b N- Terminal Region" 100.00 139 100.00 100.00 8.79e-03 PDB 3W99 "Crystal Structure Of Human Nucleosome Core Particle Lacking H4 N- Terminal Region" 100.00 139 100.00 100.00 8.79e-03 PDB 3WA9 "The Nucleosome Containing Human H2a.z.1" 100.00 139 100.00 100.00 8.79e-03 PDB 3WAA "The Nucleosome Containing Human H2a.z.2" 100.00 139 100.00 100.00 8.79e-03 PDB 3WKJ "The Nucleosome Containing Human Tsh2b" 100.00 139 100.00 100.00 8.79e-03 PDB 3WTP "Crystal Structure Of The Heterotypic Nucleosome Containing Human Cenp- A And H3.3" 100.00 140 100.00 100.00 1.04e-02 PDB 3X1S "Crystal Structure Of The Nucleosome Core Particle" 100.00 135 100.00 100.00 8.51e-03 PDB 3X1T "Crystal Structure Of Nucleosome Core Particle Consisting Of Mouse Testis Specific Histone Variants H2aa And H2ba" 100.00 135 100.00 100.00 8.51e-03 PDB 3X1U "Crystal Structure Of Nucleosome Core Particle In The Presence Of Histone Variants Involved In Reprogramming" 100.00 135 100.00 100.00 8.51e-03 PDB 3X1V "Crystal Structure Of Nucleosome Core Particle In The Presence Of Histone Variant Involved In Reprogramming" 100.00 135 100.00 100.00 8.51e-03 PDB 4H9N "Complex Structure 1 Of DaxxH3.3(SUB5)H4" 100.00 135 100.00 100.00 8.51e-03 PDB 4H9O "Complex Structure 2 Of DaxxH3.3(SUB5,G90M)H4" 100.00 135 100.00 100.00 7.84e-03 PDB 4H9P "Complex Structure 3 Of DaxxH3.3(SUB5,G90A)H4" 100.00 135 100.00 100.00 8.08e-03 PDB 4H9Q "Complex Structure 4 Of Daxx(E225a)H3.3(SUB5)H4" 100.00 135 100.00 100.00 8.51e-03 PDB 4H9R "Complex Structure 5 Of Daxx(E225a)H3.3(SUB5,G90A)H4" 100.00 135 100.00 100.00 8.08e-03 PDB 4H9S "Complex Structure 6 Of DaxxH3.3(SUB7)H4" 100.00 135 100.00 100.00 1.04e-02 PDB 4HGA "Structure Of The Variant Histone H3.3-h4 Heterodimer In Complex With Its Chaperone Daxx" 100.00 136 100.00 100.00 8.62e-03 PDB 4J8U "X-ray Structure Of Ncp145 With Chlorido(eta-6-p-cymene)(n-phenyl-2- Pyridinecarbothioamide)osmium(ii)" 100.00 135 100.00 100.00 7.44e-03 PDB 4J8V "X-ray Structure Of Ncp145 With Bound Chlorido(eta-6-p-cymene)(n- Phenyl-2-pyridinecarbothioamide)ruthenium(ii)" 100.00 135 100.00 100.00 7.44e-03 PDB 4J8W "X-ray Structure Of Ncp145 With Chlorido(eta-6-p-cymene)(n- Fluorophenyl-2-pyridinecarbothioamide)osmium(ii)" 100.00 135 100.00 100.00 7.44e-03 PDB 4J8X "X-ray Structure Of Ncp145 With Bound Chlorido(eta-6-p-cymene)(n- Fluorophenyl-2-pyridinecarbothioamide)ruthenium(ii)" 100.00 135 100.00 100.00 7.44e-03 PDB 4JJN "Crystal Structure Of Heterochromatin Protein Sir3 In Complex With A Silenced Yeast Nucleosome" 100.00 135 100.00 100.00 7.07e-03 PDB 4KGC "Nucleosome Core Particle Containing (eta6-p-cymene)-(1, 2- Ethylenediamine)-ruthenium" 100.00 136 100.00 100.00 7.86e-03 PDB 4KUD "Crystal Structure Of N-terminal Acetylated Sir3 Bah Domain D205n Mutant In Complex With Yeast Nucleosome Core Particle" 100.00 136 100.00 100.00 6.66e-03 PDB 4LD9 "Crystal Structure Of The N-terminally Acetylated Bah Domain Of Sir3 Bound To The Nucleosome Core Particle" 100.00 136 100.00 100.00 7.86e-03 PDB 4LK9 "Crystal Structure Of Moz Double Phd Finger Histone H3 Tail Complex" 100.00 21 100.00 100.00 9.44e-03 PDB 4QLC "Crystal Structure Of Chromatosome At 3.5 Angstrom Resolution" 100.00 135 100.00 100.00 8.17e-03 PDB 4R8P "Crystal Structure Of The Ring1b/bmi1/ubch5c Prc1 Ubiquitylation Module Bound To The Nucleosome Core Particle" 100.00 135 100.00 100.00 7.44e-03 PDB 4UUZ "Mcm2-histone Complex" 100.00 136 100.00 100.00 7.86e-03 PDB 4WU8 "Structure Of Trptnap-ncp145" 100.00 135 100.00 100.00 7.44e-03 PDB 4WU9 "Structure Of Cisptnap-ncp145" 100.00 135 100.00 100.00 7.44e-03 PDB 5C3I "Crystal Structure Of The Quaternary Complex Of Histone H3-h4 Heterodimer With Chaperone Asf1 And The Replicative Helicase Subun" 100.00 136 100.00 100.00 8.27e-03 DBJ BAA20144 "Histone H3 [Drosophila simulans]" 100.00 136 100.00 100.00 7.23e-03 DBJ BAA21441 "histone H3.1 [Schizosaccharomyces pombe]" 100.00 136 100.00 100.00 8.80e-03 DBJ BAA31218 "histone H3 [Nicotiana tabacum]" 100.00 136 100.00 100.00 8.27e-03 DBJ BAA81840 "histone H3 [Oryza sativa Japonica Group]" 100.00 136 100.00 100.00 8.10e-03 DBJ BAA81841 "histone H3 [Oryza sativa Japonica Group]" 100.00 136 100.00 100.00 8.10e-03 EMBL CAA17819 "histone H3 h3.2 [Schizosaccharomyces pombe]" 100.00 136 100.00 100.00 8.80e-03 EMBL CAA23780 "unnamed protein product [Homo sapiens]" 100.00 27 100.00 100.00 7.85e-03 EMBL CAA24375 "unnamed protein product [Psammechinus miliaris]" 100.00 136 100.00 100.00 7.77e-03 EMBL CAA24647 "unnamed protein product [Strongylocentrotus purpuratus]" 100.00 136 100.00 100.00 8.19e-03 EMBL CAA24952 "unnamed protein product [Homo sapiens]" 100.00 136 100.00 100.00 8.27e-03 GB AAA19824 "H3 histone [Rattus norvegicus]" 100.00 136 100.00 100.00 8.27e-03 GB AAA29441 "histone H3 [Paracentrotus lividus]" 100.00 136 100.00 100.00 7.77e-03 GB AAA29965 "histone H3 [Spisula solidissima]" 100.00 136 100.00 100.00 8.62e-03 GB AAA30003 "histone H3 [Lytechinus pictus]" 100.00 136 100.00 100.00 7.86e-03 GB AAA30026 "histone H3 [Psammechinus miliaris]" 100.00 136 100.00 100.00 7.77e-03 PIR A56580 "histone H3 - midge (Chironomus thummi thummi)" 100.00 136 100.00 100.00 7.86e-03 PIR A56618 "histone H3 - spoonworm (Urechis caupo)" 100.00 136 100.00 100.00 7.86e-03 PIR A56654 "histone H3 - Tigriopus californicus" 100.00 136 100.00 100.00 7.86e-03 PIR I37460 "histone H3 - human (fragment)" 100.00 27 100.00 100.00 7.85e-03 PIR I48113 "histone H3.2 - Chinese hamster (fragment)" 100.00 39 100.00 100.00 9.78e-03 PRF 0710252A "histone H3" 100.00 135 100.00 100.00 8.17e-03 PRF 0806228A "histone H3 [Gallus gallus]" 100.00 135 100.00 100.00 8.17e-03 PRF 1202262D "histone H3.1" 100.00 136 100.00 100.00 8.80e-03 PRF 1202289A "histone H3" 100.00 135 100.00 100.00 8.43e-03 PRF 1303352A "histone H3" 100.00 136 100.00 100.00 8.10e-03 REF NP_001005101 "histone H3.3 [Xenopus (Silurana) tropicalis]" 100.00 136 100.00 100.00 8.62e-03 REF NP_001005464 "histone H3.2 [Homo sapiens]" 100.00 136 100.00 100.00 7.86e-03 REF NP_001013074 "histone H3.1 [Rattus norvegicus]" 100.00 136 100.00 100.00 8.27e-03 REF NP_001013721 "histone H3.3C [Homo sapiens]" 100.00 135 100.00 100.00 7.76e-03 REF NP_001014411 "histone H3.3 [Bos taurus]" 100.00 136 100.00 100.00 8.62e-03 SP A1CP80 "RecName: Full=Histone H3" 100.00 136 100.00 100.00 6.73e-03 SP A1D240 "RecName: Full=Histone H3" 100.00 136 100.00 100.00 6.73e-03 SP A2QRR5 "RecName: Full=Histone H3" 100.00 136 100.00 100.00 6.73e-03 SP A2XHJ3 "RecName: Full=Histone H3.3; AltName: Full=H3.2" 100.00 136 100.00 100.00 8.27e-03 SP A2Y533 "RecName: Full=Histone H3.2" 100.00 136 100.00 100.00 8.10e-03 TPE CBF88887 "TPA: Histone H3 [Source:UniProtKB/Swiss-Prot;Acc:P23753] [Aspergillus nidulans FGSC A4]" 100.00 136 100.00 100.00 6.73e-03 TPE CEL66806 "TPA: Histone H3, related [Neospora caninum Liverpool]" 100.00 136 100.00 100.00 7.23e-03 TPE CEL70515 "TPA: Histone H3.3, related [Neospora caninum Liverpool]" 100.00 136 100.00 100.00 7.38e-03 TPE CEL74279 "TPA: histone H3 [Toxoplasma gondii VEG]" 100.00 136 100.00 100.00 7.23e-03 TPE CEL78184 "TPA: histone H3.3 variant [Toxoplasma gondii VEG]" 100.00 136 100.00 100.00 7.38e-03 TPG DAA07131 "TPA: histone H3 [Saccharomyces cerevisiae S288c]" 100.00 136 100.00 100.00 6.66e-03 TPG DAA10514 "TPA: histone H3 [Saccharomyces cerevisiae S288c]" 100.00 136 100.00 100.00 6.66e-03 TPG DAA16173 "TPA: histone cluster 1, H3f-like [Bos taurus]" 100.00 136 100.00 100.00 8.27e-03 TPG DAA16175 "TPA: histone cluster 1, H3f-like [Bos taurus]" 100.00 136 100.00 100.00 8.27e-03 TPG DAA16178 "TPA: histone cluster 1, H3f-like [Bos taurus]" 100.00 136 100.00 100.00 8.27e-03 stop_ save_ save_Polybromo_Bromdomain2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Polybromo_Bromdomain2 _Molecular_mass 13676.851 _Mol_thiol_state 'not present' _Details . _Residue_count 121 _Mol_residue_sequence ; STEGSSPAYLKEILEQLLEA IVVATNPSGRLISELFQKLP SKVQYPDYYAIIKEPIDLKT IAQRIQNGSYKSIHAMAKDI DLLAKNAKTYNEPGSQVFKD ANSIKKIFYMKKAEIEHHEM A ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 173 SER 2 174 THR 3 175 GLU 4 176 GLY 5 177 SER 6 178 SER 7 179 PRO 8 180 ALA 9 181 TYR 10 182 LEU 11 183 LYS 12 184 GLU 13 185 ILE 14 186 LEU 15 187 GLU 16 188 GLN 17 189 LEU 18 190 LEU 19 191 GLU 20 192 ALA 21 193 ILE 22 194 VAL 23 195 VAL 24 196 ALA 25 197 THR 26 198 ASN 27 199 PRO 28 200 SER 29 201 GLY 30 202 ARG 31 203 LEU 32 204 ILE 33 205 SER 34 206 GLU 35 207 LEU 36 208 PHE 37 209 GLN 38 210 LYS 39 211 LEU 40 212 PRO 41 213 SER 42 214 LYS 43 215 VAL 44 216 GLN 45 217 TYR 46 218 PRO 47 219 ASP 48 220 TYR 49 221 TYR 50 222 ALA 51 223 ILE 52 224 ILE 53 225 LYS 54 226 GLU 55 227 PRO 56 228 ILE 57 229 ASP 58 230 LEU 59 231 LYS 60 232 THR 61 233 ILE 62 234 ALA 63 235 GLN 64 236 ARG 65 237 ILE 66 238 GLN 67 239 ASN 68 240 GLY 69 241 SER 70 242 TYR 71 243 LYS 72 244 SER 73 245 ILE 74 246 HIS 75 247 ALA 76 248 MET 77 249 ALA 78 250 LYS 79 251 ASP 80 252 ILE 81 253 ASP 82 254 LEU 83 255 LEU 84 256 ALA 85 257 LYS 86 258 ASN 87 259 ALA 88 260 LYS 89 261 THR 90 262 TYR 91 263 ASN 92 264 GLU 93 265 PRO 94 266 GLY 95 267 SER 96 268 GLN 97 269 VAL 98 270 PHE 99 271 LYS 100 272 ASP 101 273 ALA 102 274 ASN 103 275 SER 104 276 ILE 105 277 LYS 106 278 LYS 107 279 ILE 108 280 PHE 109 281 TYR 110 282 MET 111 283 LYS 112 284 LYS 113 285 ALA 114 286 GLU 115 287 ILE 116 288 GLU 117 289 HIS 118 290 HIS 119 291 GLU 120 292 MET 121 293 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 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 2KTB "Solution Structure Of The Second Bromodomain Of Human Polybr Complex With An Acetylated Peptide From Histone 3" 100.00 121 100.00 100.00 8.45e-81 PDB 3HMF "Crystal Structure Of The Second Bromodomain Of Human Poly-Bromodomain Containing Protein 1 (Pb1)" 94.21 116 100.00 100.00 2.48e-75 PDB 3LJW "Crystal Structure Of The Second Bromodomain Of Human Polybromo" 99.17 120 100.00 100.00 4.03e-80 REF XP_008563175 "PREDICTED: protein polybromo-1-like, partial [Galeopterus variegatus]" 64.46 117 100.00 100.00 2.12e-48 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $H3_Peptide Human 9606 Eukaryota Metazoa Homo sapiens HIST3H3 $Polybromo_Bromdomain2 Human 9606 Eukaryota Metazoa Homo sapiens PBRM1 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 $H3_Peptide 'obtained from a vendor' . . . . . $Polybromo_Bromdomain2 'recombinant technology' . . . BL21(DE3) . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Polybromo_Bromdomain2 0.5 mM '[U-100% 15N]' $H3_Peptide 2.5 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Polybromo_Bromdomain2 0.5 mM '[U-100% 13C; U-100% 15N]' $H3_Peptide 2.5 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Polybromo_Bromdomain2 0.8 mM '[U-100% 13C; U-100% 15N]' $H3_Peptide 8 mM 'natural abundance' D2O 100 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_ARIA _Saveframe_category software _Name ARIA _Version 2.2 loop_ _Vendor _Address _Electronic_address 'Linge, O'Donoghue and Nilges' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version 2.2 loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details MSSM save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details NYSBC save_ ############################# # NMR applied experiments # ############################# save_3D_1H-13C_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_3 save_ save_3D_1H-15N_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_2 save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 298 . K pH 6.5 . pH pressure 1 . atm 'ionic strength' 0.1 . M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 water H 1 protons ppm 4.79 external direct . . . 1.0 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_chem_shift_list_1_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $NMRView stop_ loop_ _Experiment_label '3D 1H-13C NOESY' '3D 1H-15N NOESY' '3D HNCACB' '3D HN(CO)CA' '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_3 $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name H3_Peptide _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 1 ALA HA H 4.191 . 1 2 1 1 ALA HB H 1.546 . 1 3 2 2 ARG H H 8.444 . 1 4 2 2 ARG HA H 4.388 . 1 5 2 2 ARG HB2 H 1.846 . 2 6 2 2 ARG HB3 H 1.789 . 2 7 2 2 ARG HD2 H 3.189 . 2 8 2 2 ARG HG2 H 1.642 . 2 9 3 3 THR H H 8.381 . 1 10 3 3 THR HA H 4.328 . 1 11 3 3 THR HB H 4.148 . 1 12 3 3 THR HG2 H 1.202 . 1 13 4 4 LYS H H 8.494 . 1 14 4 4 LYS HA H 4.260 . 1 15 4 4 LYS HB2 H 1.821 . 2 16 4 4 LYS HB3 H 1.749 . 2 17 4 4 LYS HD2 H 1.668 . 2 18 4 4 LYS HG2 H 1.422 . 2 19 5 5 GLN H H 8.540 . 1 20 5 5 GLN HA H 4.368 . 1 21 5 5 GLN HB2 H 2.087 . 2 22 5 5 GLN HB3 H 1.979 . 2 23 5 5 GLN HG2 H 2.364 . 2 24 5 5 GLN HG3 H 2.355 . 2 25 6 6 THR H H 8.278 . 1 26 6 6 THR HA H 4.298 . 1 27 6 6 THR HB H 4.164 . 1 28 6 6 THR HG2 H 1.189 . 1 29 7 7 ALA HA H 4.309 . 1 30 7 7 ALA HB H 1.369 . 1 31 8 8 ARG H H 8.385 . 1 32 8 8 ARG HA H 4.270 . 1 33 8 8 ARG HB2 H 1.811 . 2 34 8 8 ARG HB3 H 1.746 . 2 35 8 8 ARG HD2 H 3.171 . 2 36 8 8 ARG HE H 7.175 . 1 37 8 8 ARG HG2 H 1.629 . 2 38 9 9 LYS H H 8.411 . 1 39 9 9 LYS HA H 4.311 . 1 40 9 9 LYS HB2 H 1.812 . 2 41 9 9 LYS HB3 H 1.767 . 2 42 9 9 LYS HD2 H 1.614 . 2 43 9 9 LYS HE2 H 3.072 . 2 44 9 9 LYS HG2 H 1.406 . 2 45 10 10 SER H H 8.514 . 1 46 10 10 SER HA H 4.521 . 1 47 10 10 SER HB2 H 3.938 . 2 48 10 10 SER HB3 H 3.833 . 2 49 11 11 THR H H 8.358 . 1 50 11 11 THR HA H 4.418 . 1 51 11 11 THR HB H 3.962 . 1 52 11 11 THR HG2 H 1.192 . 1 53 12 12 GLY H H 8.475 . 1 54 12 12 GLY HA2 H 3.978 . 2 55 13 13 GLY H H 8.321 . 1 56 13 13 GLY HA2 H 3.949 . 2 57 14 14 LYS H H 8.216 . 1 58 14 14 LYS HA H 4.315 . 1 59 14 14 LYS HB2 H 1.752 . 2 60 14 14 LYS HB3 H 1.596 . 2 61 14 14 LYS HD2 H 1.477 . 2 62 14 14 LYS HE2 H 3.142 . 2 63 14 14 LYS HG2 H 1.342 . 2 64 14 14 LYS HG3 H 1.308 . 2 65 14 14 LYS HZ H 1.949 . 1 66 15 15 ALA H H 8.364 . 1 67 15 15 ALA HA H 4.558 . 1 68 15 15 ALA HB H 1.375 . 1 69 16 16 PRO HA H 4.422 . 1 70 16 16 PRO HB2 H 2.273 . 2 71 16 16 PRO HB3 H 1.860 . 2 72 16 16 PRO HD2 H 3.802 . 2 73 16 16 PRO HD3 H 3.644 . 2 74 16 16 PRO HG2 H 2.001 . 2 75 17 17 ARG H H 8.555 . 1 76 17 17 ARG HB2 H 1.865 . 2 77 17 17 ARG HB3 H 1.780 . 2 78 17 17 ARG HD2 H 3.217 . 2 79 17 17 ARG HG2 H 1.680 . 2 80 18 18 LYS H H 8.037 . 1 81 18 18 LYS HB2 H 1.795 . 2 82 18 18 LYS HB3 H 1.689 . 2 83 18 18 LYS HE2 H 2.968 . 2 84 19 19 GLN H H 8.450 . 1 85 19 19 GLN HA H 4.271 . 1 86 19 19 GLN HB2 H 2.082 . 2 87 19 19 GLN HB3 H 1.953 . 2 88 19 19 GLN HG2 H 2.340 . 2 89 20 20 LEU H H 8.097 . 1 90 20 20 LEU HA H 4.220 . 1 91 20 20 LEU HD1 H 0.870 . 2 92 20 20 LEU HD2 H 0.856 . 2 93 20 20 LEU HG H 1.578 . 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity ',' ',,' ',,,,,' ',,' ',,,,,' ',,' ',,' ',,' ',,' ',,' ',,' stop_ save_ save_assigned_chem_shift_list_1_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $NMRView stop_ loop_ _Experiment_label '3D 1H-13C NOESY' '3D 1H-15N NOESY' '3D HNCACB' '3D HN(CO)CA' '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_3 $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name Polybromo_Bromdomain2 _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 1 173 1 SER CB C 63.996 . . 2 174 2 THR H H 8.402 . . 3 174 2 THR HA H 4.356 . . 4 174 2 THR HB H 4.258 . . 5 174 2 THR HG2 H 1.171 . 1 6 174 2 THR CA C 61.992 . . 7 174 2 THR CB C 69.478 . . 8 174 2 THR CG2 C 21.620 . . 9 174 2 THR N N 115.686 . . 10 175 3 GLU H H 8.529 . . 11 175 3 GLU HA H 4.284 . . 12 175 3 GLU HB2 H 2.056 . 2 13 175 3 GLU HB3 H 1.946 . 2 14 175 3 GLU HG2 H 2.250 . . 15 175 3 GLU CA C 56.799 . . 16 175 3 GLU CB C 30.044 . . 17 175 3 GLU CG C 36.264 . . 18 175 3 GLU N N 123.281 . . 19 176 4 GLY H H 8.423 . . 20 176 4 GLY HA2 H 4.239 . . 21 176 4 GLY HA3 H 3.942 . . 22 176 4 GLY CA C 45.189 . . 23 176 4 GLY N N 109.840 . . 24 177 5 SER H H 8.165 . . 25 177 5 SER HA H 4.488 . . 26 177 5 SER HB2 H 3.862 . . 27 177 5 SER CA C 58.081 . . 28 177 5 SER CB C 64.041 . . 29 177 5 SER N N 115.167 . . 30 178 6 SER H H 8.436 . . 31 178 6 SER HA H 4.811 . . 32 178 6 SER HB2 H 3.966 . 2 33 178 6 SER HB3 H 3.905 . . 34 178 6 SER CA C 56.481 . . 35 178 6 SER CB C 63.508 . . 36 178 6 SER N N 118.546 . . 37 179 7 PRO HA H 4.387 . . 38 179 7 PRO HB2 H 2.335 . . 39 179 7 PRO HB3 H 1.808 . . 40 179 7 PRO HD2 H 3.911 . . 41 179 7 PRO HD3 H 3.765 . . 42 179 7 PRO HG2 H 2.044 . . 43 179 7 PRO CA C 64.160 . . 44 179 7 PRO CB C 31.907 . . 45 179 7 PRO CD C 50.755 . . 46 179 7 PRO CG C 27.618 . . 47 180 8 ALA H H 8.327 . . 48 180 8 ALA HA H 4.140 . . 49 180 8 ALA HB H 1.348 . . 50 180 8 ALA CA C 54.112 . . 51 180 8 ALA CB C 18.541 . . 52 180 8 ALA N N 122.550 . . 53 181 9 TYR H H 7.875 . . 54 181 9 TYR HA H 4.434 . . 55 181 9 TYR HB2 H 3.107 . . 56 181 9 TYR HD1 H 7.112 . . 57 181 9 TYR HE1 H 6.798 . . 58 181 9 TYR CA C 59.048 . . 59 181 9 TYR CB C 37.781 . . 60 181 9 TYR CE1 C 118.170 . 3 61 181 9 TYR N N 118.552 . . 62 182 10 LEU H H 7.671 . . 63 182 10 LEU HA H 3.902 . . 64 182 10 LEU HB2 H 1.724 . . 65 182 10 LEU HB3 H 1.488 . . 66 182 10 LEU HD1 H 0.765 . . 67 182 10 LEU HD2 H 0.781 . 4 68 182 10 LEU HG H 1.463 . . 69 182 10 LEU CA C 57.619 . . 70 182 10 LEU CB C 41.559 . . 71 182 10 LEU CD1 C 25.775 . . 72 182 10 LEU CD2 C 23.293 . 2 73 182 10 LEU CG C 26.906 . . 74 182 10 LEU N N 116.298 . . 75 183 11 LYS H H 7.995 . . 76 183 11 LYS HA H 3.792 . 1 77 183 11 LYS HB2 H 1.819 . 2 78 183 11 LYS HB3 H 1.762 . . 79 183 11 LYS HE2 H 2.998 . 2 80 183 11 LYS HG2 H 1.337 . 2 81 183 11 LYS CA C 60.653 . . 82 183 11 LYS CB C 32.448 . . 83 183 11 LYS CG C 24.815 . 1 84 183 11 LYS N N 117.895 . . 85 184 12 GLU H H 7.556 . . 86 184 12 GLU HA H 4.065 . . 87 184 12 GLU HB2 H 2.102 . . 88 184 12 GLU HB3 H 2.000 . . 89 184 12 GLU HG2 H 2.331 . . 90 184 12 GLU HG3 H 2.245 . . 91 184 12 GLU CA C 59.383 . . 92 184 12 GLU CB C 29.223 . . 93 184 12 GLU CG C 36.833 . . 94 184 12 GLU N N 115.560 . . 95 185 13 ILE H H 7.609 . . 96 185 13 ILE HA H 3.669 . . 97 185 13 ILE HB H 2.012 . 1 98 185 13 ILE HD1 H 0.671 . . 99 185 13 ILE HG12 H 1.479 . 9 100 185 13 ILE HG13 H 1.059 . 9 101 185 13 ILE HG2 H 0.792 . 4 102 185 13 ILE CA C 64.598 . . 103 185 13 ILE CB C 37.605 . . 104 185 13 ILE CD1 C 12.580 . . 105 185 13 ILE CG1 C 28.364 . 1 106 185 13 ILE CG2 C 15.152 . 1 107 185 13 ILE N N 120.044 . . 108 186 14 LEU H H 8.632 . . 109 186 14 LEU HA H 4.007 . 1 110 186 14 LEU HB2 H 1.900 . 2 111 186 14 LEU HB3 H 1.647 . 2 112 186 14 LEU HD1 H 0.682 . 4 113 186 14 LEU HD2 H 0.772 . 4 114 186 14 LEU CA C 58.426 . . 115 186 14 LEU CB C 40.344 . . 116 186 14 LEU CD1 C 26.370 . 2 117 186 14 LEU CD2 C 23.134 . 2 118 186 14 LEU N N 119.153 . . 119 187 15 GLU H H 8.677 . . 120 187 15 GLU HA H 3.899 . . 121 187 15 GLU HB2 H 2.283 . 2 122 187 15 GLU HB3 H 1.929 . . 123 187 15 GLU HG2 H 2.641 . . 124 187 15 GLU HG3 H 2.125 . . 125 187 15 GLU CA C 60.143 . . 126 187 15 GLU CB C 29.515 . . 127 187 15 GLU CG C 37.904 . . 128 187 15 GLU N N 116.548 . . 129 188 16 GLN H H 7.921 . . 130 188 16 GLN HA H 4.064 . . 131 188 16 GLN HB2 H 2.313 . . 132 188 16 GLN HB3 H 1.988 . 2 133 188 16 GLN HG2 H 2.643 . . 134 188 16 GLN HG3 H 2.313 . . 135 188 16 GLN CA C 59.300 . . 136 188 16 GLN CB C 28.940 . . 137 188 16 GLN CG C 34.522 . . 138 188 16 GLN N N 120.102 . . 139 189 17 LEU H H 8.013 . . 140 189 17 LEU HA H 3.815 . . 141 189 17 LEU HB2 H 2.181 . 2 142 189 17 LEU HB3 H 1.313 . 2 143 189 17 LEU HD1 H 0.681 . . 144 189 17 LEU HD2 H 0.245 . . 145 189 17 LEU HG H 1.596 . 1 146 189 17 LEU CA C 58.513 . . 147 189 17 LEU CB C 41.289 . . 148 189 17 LEU CD1 C 26.396 . . 149 189 17 LEU CD2 C 23.207 . . 150 189 17 LEU CG C 26.839 . 1 151 189 17 LEU N N 121.911 . . 152 190 18 LEU H H 8.059 . . 153 190 18 LEU HA H 3.988 . . 154 190 18 LEU HB2 H 1.951 . 2 155 190 18 LEU HB3 H 1.304 . . 156 190 18 LEU HD1 H 0.992 . . 157 190 18 LEU HD2 H 0.840 . 4 158 190 18 LEU HG H 1.720 . 1 159 190 18 LEU CA C 57.687 . . 160 190 18 LEU CB C 41.558 . . 161 190 18 LEU CD1 C 20.949 . . 162 190 18 LEU CD2 C 23.473 . 2 163 190 18 LEU CG C 26.794 . 1 164 190 18 LEU N N 116.328 . . 165 191 19 GLU H H 8.448 . . 166 191 19 GLU HA H 3.992 . . 167 191 19 GLU HB2 H 2.075 . 2 168 191 19 GLU HB3 H 1.953 . 2 169 191 19 GLU HG2 H 2.163 . . 170 191 19 GLU CA C 58.951 . . 171 191 19 GLU CB C 29.529 . . 172 191 19 GLU CG C 35.839 . . 173 191 19 GLU N N 119.130 . . 174 192 20 ALA H H 7.371 . . 175 192 20 ALA HA H 3.972 . . 176 192 20 ALA HB H 1.359 . 1 177 192 20 ALA CA C 54.651 . . 178 192 20 ALA CB C 17.501 . . 179 192 20 ALA N N 116.270 . . 180 193 21 ILE H H 7.216 . . 181 193 21 ILE HA H 3.601 . 1 182 193 21 ILE HB H 2.187 . 1 183 193 21 ILE HD1 H 0.778 . 1 184 193 21 ILE HG12 H 2.016 . 9 185 193 21 ILE HG2 H 0.763 . . 186 193 21 ILE CA C 65.119 . . 187 193 21 ILE CB C 38.698 . . 188 193 21 ILE CD1 C 15.195 . 1 189 193 21 ILE CG1 C 27.680 . 1 190 193 21 ILE CG2 C 18.354 . . 191 193 21 ILE N N 112.985 . . 192 194 22 VAL H H 8.174 . . 193 194 22 VAL HA H 3.872 . . 194 194 22 VAL HB H 2.305 . . 195 194 22 VAL HG1 H 0.936 . . 196 194 22 VAL HG2 H 1.033 . . 197 194 22 VAL CA C 65.252 . . 198 194 22 VAL CB C 31.818 . . 199 194 22 VAL CG1 C 21.516 . . 200 194 22 VAL CG2 C 20.922 . . 201 194 22 VAL N N 115.566 . . 202 195 23 VAL H H 7.749 . . 203 195 23 VAL HA H 4.452 . . 204 195 23 VAL HB H 2.306 . . 205 195 23 VAL HG1 H 0.944 . 4 206 195 23 VAL HG2 H 0.931 . 4 207 195 23 VAL CA C 60.901 . . 208 195 23 VAL CB C 31.951 . . 209 195 23 VAL CG1 C 20.705 . 2 210 195 23 VAL CG2 C 18.268 . 2 211 195 23 VAL N N 110.132 . . 212 196 24 ALA H H 6.760 . . 213 196 24 ALA HA H 4.292 . 1 214 196 24 ALA HB H 1.548 . 1 215 196 24 ALA CA C 53.128 . . 216 196 24 ALA CB C 19.851 . . 217 196 24 ALA N N 123.879 . . 218 197 25 THR H H 8.595 . . 219 197 25 THR HA H 5.337 . . 220 197 25 THR HB H 4.044 . . 221 197 25 THR HG2 H 1.077 . 1 222 197 25 THR CA C 59.082 . . 223 197 25 THR CB C 72.219 . . 224 197 25 THR CG2 C 21.503 . . 225 197 25 THR N N 112.559 . . 226 198 26 ASN H H 8.534 . . 227 198 26 ASN HA H 5.084 . . 228 198 26 ASN HB2 H 3.332 . 1 229 198 26 ASN HB3 H 2.877 . 2 230 198 26 ASN CA C 51.076 . . 231 198 26 ASN CB C 38.168 . . 232 198 26 ASN N N 120.408 . . 233 199 27 PRO HA H 4.375 . . 234 199 27 PRO HB2 H 2.448 . . 235 199 27 PRO HB3 H 1.892 . 2 236 199 27 PRO HD2 H 3.926 . . 237 199 27 PRO HD3 H 3.790 . . 238 199 27 PRO HG2 H 2.173 . 2 239 199 27 PRO HG3 H 2.001 . 2 240 199 27 PRO CA C 65.846 . . 241 199 27 PRO CB C 31.568 . 1 242 199 27 PRO CD C 51.482 . . 243 199 27 PRO CG C 28.026 . 1 244 200 28 SER H H 7.663 . . 245 200 28 SER HA H 4.472 . . 246 200 28 SER HB2 H 3.974 . . 247 200 28 SER CA C 58.743 . . 248 200 28 SER CB C 63.543 . . 249 200 28 SER N N 110.459 . . 250 201 29 GLY H H 8.544 . . 251 201 29 GLY HA2 H 4.081 . 2 252 201 29 GLY HA3 H 3.593 . 2 253 201 29 GLY CA C 44.946 . . 254 201 29 GLY N N 109.855 . . 255 202 30 ARG H H 7.603 . . 256 202 30 ARG HA H 4.315 . . 257 202 30 ARG HB2 H 1.791 . 2 258 202 30 ARG HB3 H 1.585 . . 259 202 30 ARG HD2 H 3.280 . . 260 202 30 ARG HD3 H 3.115 . . 261 202 30 ARG HG2 H 1.597 . 2 262 202 30 ARG HG3 H 1.445 . . 263 202 30 ARG CA C 55.170 . . 264 202 30 ARG CB C 31.336 . . 265 202 30 ARG CD C 42.712 . . 266 202 30 ARG CG C 27.366 . . 267 202 30 ARG N N 120.611 . . 268 203 31 LEU H H 8.834 . . 269 203 31 LEU HA H 4.559 . . 270 203 31 LEU HB2 H 1.705 . 1 271 203 31 LEU HB3 H 1.524 . . 272 203 31 LEU HD1 H 0.812 . . 273 203 31 LEU HD2 H 0.934 . . 274 203 31 LEU HG H 1.669 . 1 275 203 31 LEU CA C 54.911 . . 276 203 31 LEU CB C 41.681 . . 277 203 31 LEU CD1 C 23.392 . . 278 203 31 LEU CD2 C 25.428 . . 279 203 31 LEU CG C 26.943 . 1 280 203 31 LEU N N 124.169 . . 281 204 32 ILE H H 7.895 . . 282 204 32 ILE HA H 3.877 . . 283 204 32 ILE HB H 1.804 . . 284 204 32 ILE HD1 H 0.724 . 1 285 204 32 ILE HG12 H 1.279 . 1 286 204 32 ILE HG13 H 1.168 . 1 287 204 32 ILE HG2 H 0.881 . 1 288 204 32 ILE CA C 64.541 . . 289 204 32 ILE CB C 37.902 . . 290 204 32 ILE CD1 C 14.444 . 1 291 204 32 ILE CG1 C 27.268 . 1 292 204 32 ILE CG2 C 18.301 . 1 293 204 32 ILE N N 123.659 . . 294 205 33 SER H H 9.152 . . 295 205 33 SER HA H 3.682 . 1 296 205 33 SER HB2 H 4.090 . 2 297 205 33 SER HB3 H 4.551 . 2 298 205 33 SER CA C 58.802 . . 299 205 33 SER CB C 64.293 . . 300 205 33 SER N N 111.498 . . 301 206 34 GLU H H 7.358 . . 302 206 34 GLU HA H 3.974 . . 303 206 34 GLU HB2 H 2.283 . . 304 206 34 GLU HB3 H 2.109 . . 305 206 34 GLU HG2 H 2.335 . . 306 206 34 GLU HG3 H 2.214 . 2 307 206 34 GLU CA C 60.844 . . 308 206 34 GLU CB C 30.262 . . 309 206 34 GLU CG C 35.585 . . 310 206 34 GLU N N 123.647 . . 311 207 35 LEU H H 9.299 . . 312 207 35 LEU HA H 4.239 . . 313 207 35 LEU HB2 H 1.434 . . 314 207 35 LEU HB3 H 1.313 . . 315 207 35 LEU HD1 H 0.819 . . 316 207 35 LEU HD2 H 0.774 . . 317 207 35 LEU HG H 1.589 . . 318 207 35 LEU CA C 55.651 . . 319 207 35 LEU CB C 39.725 . . 320 207 35 LEU CD1 C 25.161 . . 321 207 35 LEU CD2 C 22.458 . . 322 207 35 LEU CG C 27.394 . . 323 207 35 LEU N N 116.589 . . 324 208 36 PHE H H 7.982 . . 325 208 36 PHE HA H 4.586 . . 326 208 36 PHE HB2 H 3.362 . . 327 208 36 PHE HB3 H 2.605 . . 328 208 36 PHE HD1 H 7.164 . . 329 208 36 PHE HE1 H 7.275 . . 330 208 36 PHE HZ H 7.528 . . 331 208 36 PHE CA C 57.056 . . 332 208 36 PHE CB C 39.981 . . 333 208 36 PHE CD1 C 132.190 . 3 334 208 36 PHE CE1 C 130.890 . 3 335 208 36 PHE CZ C 129.800 . 1 336 208 36 PHE N N 115.605 . . 337 209 37 GLN H H 7.346 . . 338 209 37 GLN HA H 4.085 . . 339 209 37 GLN HB2 H 2.168 . 2 340 209 37 GLN HB3 H 2.006 . 2 341 209 37 GLN HG2 H 2.629 . . 342 209 37 GLN HG3 H 2.495 . . 343 209 37 GLN CA C 59.582 . . 344 209 37 GLN CB C 28.473 . . 345 209 37 GLN CG C 32.588 . . 346 209 37 GLN N N 120.410 . . 347 210 38 LYS H H 7.849 . . 348 210 38 LYS HA H 4.964 . . 349 210 38 LYS HB2 H 1.716 . . 350 210 38 LYS HB3 H 1.507 . . 351 210 38 LYS HD2 H 2.043 . 2 352 210 38 LYS HD3 H 1.765 . 2 353 210 38 LYS HE2 H 2.944 . . 354 210 38 LYS HG2 H 1.450 . . 355 210 38 LYS HG3 H 1.353 . . 356 210 38 LYS CA C 53.553 . . 357 210 38 LYS CB C 35.882 . . 358 210 38 LYS CD C 31.612 . 1 359 210 38 LYS CE C 41.802 . . 360 210 38 LYS CG C 24.474 . . 361 210 38 LYS N N 114.134 . . 362 211 39 LEU H H 9.025 . . 363 211 39 LEU HA H 4.150 . . 364 211 39 LEU HB2 H 1.704 . 2 365 211 39 LEU HB3 H 1.480 . 2 366 211 39 LEU HD1 H 0.952 . 2 367 211 39 LEU HD2 H 0.838 . 2 368 211 39 LEU CA C 53.179 . . 369 211 39 LEU CB C 40.941 . 1 370 211 39 LEU N N 126.611 . . 371 212 40 PRO HA H 4.241 . . 372 212 40 PRO HB2 H 1.740 . . 373 212 40 PRO HB3 H 1.313 . . 374 212 40 PRO HD2 H 3.311 . . 375 212 40 PRO HD3 H 2.711 . . 376 212 40 PRO HG2 H 0.897 . . 377 212 40 PRO CA C 61.907 . . 378 212 40 PRO CB C 32.363 . . 379 212 40 PRO CD C 50.124 . . 380 212 40 PRO CG C 24.374 . . 381 213 41 SER H H 8.989 . . 382 213 41 SER HA H 4.421 . . 383 213 41 SER HB2 H 4.234 . . 384 213 41 SER HB3 H 3.886 . . 385 213 41 SER CA C 57.713 . . 386 213 41 SER CB C 63.563 . . 387 213 41 SER N N 117.236 . . 388 214 42 LYS H H 9.004 . . 389 214 42 LYS HA H 3.968 . . 390 214 42 LYS HB2 H 1.476 . . 391 214 42 LYS HB3 H 1.345 . . 392 214 42 LYS HD2 H 1.290 . 2 393 214 42 LYS HE2 H 2.575 . . 394 214 42 LYS HG2 H 1.059 . . 395 214 42 LYS HG3 H 0.917 . 1 396 214 42 LYS CA C 58.816 . . 397 214 42 LYS CB C 32.426 . . 398 214 42 LYS CD C 29.171 . 1 399 214 42 LYS CE C 41.490 . . 400 214 42 LYS CG C 24.761 . . 401 214 42 LYS N N 108.994 . . 402 215 43 VAL H H 7.625 . . 403 215 43 VAL HA H 3.712 . 1 404 215 43 VAL HB H 1.822 . 1 405 215 43 VAL HG1 H 0.935 . 4 406 215 43 VAL HG2 H 0.872 . . 407 215 43 VAL CA C 64.358 . . 408 215 43 VAL CB C 31.977 . . 409 215 43 VAL CG1 C 21.614 . 2 410 215 43 VAL CG2 C 20.916 . . 411 215 43 VAL N N 116.021 . . 412 216 44 GLN H H 7.134 . . 413 216 44 GLN HA H 4.010 . . 414 216 44 GLN HB2 H 1.818 . . 415 216 44 GLN HB3 H 1.638 . . 416 216 44 GLN HG2 H 2.107 . . 417 216 44 GLN HG3 H 1.942 . . 418 216 44 GLN CA C 57.015 . . 419 216 44 GLN CB C 30.343 . . 420 216 44 GLN CG C 33.980 . . 421 216 44 GLN N N 117.309 . . 422 217 45 TYR H H 8.003 . . 423 217 45 TYR HA H 5.120 . . 424 217 45 TYR HB2 H 3.196 . . 425 217 45 TYR HB3 H 2.787 . . 426 217 45 TYR HD1 H 7.399 . . 427 217 45 TYR HE1 H 6.861 . . 428 217 45 TYR CA C 55.450 . . 429 217 45 TYR CB C 37.914 . . 430 217 45 TYR CD1 C 134.340 . 3 431 217 45 TYR CE1 C 117.950 . 3 432 217 45 TYR N N 114.978 . . 433 218 46 PRO HA H 4.601 . 1 434 218 46 PRO HB2 H 2.406 . 2 435 218 46 PRO HB3 H 2.064 . 2 436 218 46 PRO HD2 H 3.659 . . 437 218 46 PRO HD3 H 3.327 . . 438 218 46 PRO HG2 H 2.082 . . 439 218 46 PRO CA C 65.922 . . 440 218 46 PRO CB C 31.088 . . 441 218 46 PRO CD C 49.920 . . 442 218 46 PRO CG C 27.441 . . 443 219 47 ASP H H 8.953 . . 444 219 47 ASP HA H 4.427 . . 445 219 47 ASP HB2 H 2.832 . . 446 219 47 ASP CA C 55.751 . . 447 219 47 ASP CB C 39.665 . . 448 219 47 ASP N N 117.599 . . 449 220 48 TYR H H 7.738 . . 450 220 48 TYR HA H 3.571 . . 451 220 48 TYR HB2 H 2.820 . 2 452 220 48 TYR HB3 H 2.311 . 2 453 220 48 TYR HD1 H 4.820 . 1 454 220 48 TYR HE1 H 5.962 . . 455 220 48 TYR CA C 61.955 . . 456 220 48 TYR CB C 38.410 . . 457 220 48 TYR N N 122.145 . . 458 221 49 TYR H H 7.007 . . 459 221 49 TYR HA H 4.022 . . 460 221 49 TYR HB2 H 3.324 . . 461 221 49 TYR HB3 H 2.768 . . 462 221 49 TYR HD1 H 7.455 . . 463 221 49 TYR HE1 H 6.636 . . 464 221 49 TYR CA C 60.149 . . 465 221 49 TYR CB C 37.997 . . 466 221 49 TYR N N 113.212 . . 467 222 50 ALA H H 7.477 . . 468 222 50 ALA HA H 4.313 . 1 469 222 50 ALA HB H 1.515 . 1 470 222 50 ALA CA C 53.371 . . 471 222 50 ALA CB C 18.760 . . 472 222 50 ALA N N 120.966 . . 473 223 51 ILE H H 7.492 . . 474 223 51 ILE HA H 4.014 . . 475 223 51 ILE HB H 1.679 . . 476 223 51 ILE HD1 H 0.915 . . 477 223 51 ILE HG12 H 1.205 . . 478 223 51 ILE HG13 H 1.614 . 9 479 223 51 ILE HG2 H 0.904 . 4 480 223 51 ILE CA C 62.164 . . 481 223 51 ILE CB C 40.439 . . 482 223 51 ILE CD1 C 13.413 . . 483 223 51 ILE CG1 C 28.315 . . 484 223 51 ILE CG2 C 17.000 . 1 485 223 51 ILE N N 121.253 . . 486 224 52 ILE H H 8.052 . . 487 224 52 ILE HA H 3.832 . 1 488 224 52 ILE HB H 1.314 . 1 489 224 52 ILE HD1 H 0.496 . . 490 224 52 ILE HG12 H 0.820 . 9 491 224 52 ILE HG13 H 0.096 . 9 492 224 52 ILE HG2 H 0.350 . . 493 224 52 ILE CA C 57.429 . . 494 224 52 ILE CB C 33.678 . . 495 224 52 ILE CD1 C 9.426 . . 496 224 52 ILE CG1 C 24.329 . 1 497 224 52 ILE CG2 C 16.447 . . 498 224 52 ILE N N 121.972 . . 499 225 53 LYS H H 7.917 . . 500 225 53 LYS HA H 4.119 . . 501 225 53 LYS HB2 H 1.859 . . 502 225 53 LYS HB3 H 1.658 . 2 503 225 53 LYS HD2 H 1.594 . 2 504 225 53 LYS HE2 H 2.953 . 2 505 225 53 LYS HG2 H 1.486 . 2 506 225 53 LYS HG3 H 1.387 . . 507 225 53 LYS CA C 56.959 . . 508 225 53 LYS CB C 32.413 . . 509 225 53 LYS CG C 24.706 . 1 510 225 53 LYS N N 125.222 . . 511 226 54 GLU H H 8.426 . . 512 226 54 GLU HA H 4.705 . 1 513 226 54 GLU HB2 H 2.074 . 2 514 226 54 GLU HB3 H 1.873 . 2 515 226 54 GLU HG2 H 2.055 . 2 516 226 54 GLU CA C 53.070 . . 517 226 54 GLU CB C 30.787 . . 518 226 54 GLU CG C 36.356 . 1 519 226 54 GLU N N 119.094 . . 520 227 55 PRO HA H 4.151 . . 521 227 55 PRO HB2 H 2.201 . . 522 227 55 PRO HB3 H 2.134 . . 523 227 55 PRO HD2 H 3.585 . 2 524 227 55 PRO HD3 H 3.467 . 2 525 227 55 PRO HG2 H 2.298 . . 526 227 55 PRO HG3 H 1.867 . . 527 227 55 PRO CA C 62.724 . 1 528 227 55 PRO CB C 33.424 . . 529 227 55 PRO CD C 49.949 . 1 530 227 55 PRO CG C 27.475 . . 531 228 56 ILE H H 9.024 . . 532 228 56 ILE HA H 4.437 . . 533 228 56 ILE HB H 1.817 . . 534 228 56 ILE HD1 H 0.903 . . 535 228 56 ILE HG12 H 1.505 . . 536 228 56 ILE HG13 H 1.337 . . 537 228 56 ILE HG2 H 0.770 . 4 538 228 56 ILE CA C 61.672 . . 539 228 56 ILE CB C 41.307 . . 540 228 56 ILE CD1 C 15.075 . . 541 228 56 ILE CG1 C 29.661 . . 542 228 56 ILE CG2 C 15.227 . 1 543 228 56 ILE N N 121.318 . . 544 229 57 ASP H H 6.964 . . 545 229 57 ASP HA H 4.733 . 1 546 229 57 ASP HB2 H 2.865 . 2 547 229 57 ASP HB3 H 2.412 . 2 548 229 57 ASP CA C 52.214 . . 549 229 57 ASP CB C 42.857 . . 550 229 57 ASP N N 121.785 . . 551 230 58 LEU HA H 4.146 . . 552 230 58 LEU HB2 H 1.783 . . 553 230 58 LEU HB3 H 1.403 . . 554 230 58 LEU HD1 H 0.765 . . 555 230 58 LEU HD2 H 0.681 . . 556 230 58 LEU CA C 57.484 . . 557 230 58 LEU CB C 41.528 . . 558 230 58 LEU CD1 C 27.355 . . 559 230 58 LEU CD2 C 23.089 . . 560 231 59 LYS H H 8.256 . . 561 231 59 LYS HA H 4.091 . . 562 231 59 LYS HB2 H 2.045 . . 563 231 59 LYS HB3 H 1.874 . . 564 231 59 LYS HD2 H 1.656 . . 565 231 59 LYS HE2 H 2.942 . . 566 231 59 LYS HG2 H 1.540 . . 567 231 59 LYS HG3 H 1.448 . . 568 231 59 LYS CA C 59.656 . . 569 231 59 LYS CB C 31.486 . . 570 231 59 LYS CD C 29.012 . . 571 231 59 LYS CE C 41.845 . . 572 231 59 LYS CG C 24.837 . . 573 231 59 LYS N N 122.489 . . 574 232 60 THR H H 8.740 . . 575 232 60 THR HA H 3.907 . . 576 232 60 THR HB H 4.321 . . 577 232 60 THR HG2 H 1.167 . 1 578 232 60 THR CA C 67.231 . . 579 232 60 THR CB C 68.360 . . 580 232 60 THR CG2 C 20.121 . 1 581 232 60 THR N N 119.001 . . 582 233 61 ILE H H 7.482 . . 583 233 61 ILE HA H 4.072 . . 584 233 61 ILE HB H 1.888 . . 585 233 61 ILE HD1 H 0.644 . 1 586 233 61 ILE HG12 H 1.447 . 9 587 233 61 ILE HG13 H 1.338 . 9 588 233 61 ILE HG2 H 1.101 . . 589 233 61 ILE CA C 65.574 . . 590 233 61 ILE CB C 38.694 . . 591 233 61 ILE CD1 C 13.830 . 1 592 233 61 ILE CG1 C 25.076 . 1 593 233 61 ILE CG2 C 16.491 . . 594 233 61 ILE N N 123.023 . . 595 234 62 ALA H H 8.568 . . 596 234 62 ALA HA H 4.015 . . 597 234 62 ALA HB H 1.529 . 1 598 234 62 ALA CA C 55.655 . . 599 234 62 ALA CB C 18.201 . . 600 234 62 ALA N N 120.633 . . 601 235 63 GLN H H 8.060 . . 602 235 63 GLN HA H 3.968 . . 603 235 63 GLN HB2 H 2.281 . . 604 235 63 GLN HB3 H 2.184 . 2 605 235 63 GLN HG2 H 2.503 . . 606 235 63 GLN HG3 H 2.329 . 2 607 235 63 GLN CA C 58.831 . . 608 235 63 GLN CB C 28.461 . . 609 235 63 GLN CG C 33.979 . . 610 235 63 GLN N N 118.744 . . 611 236 64 ARG H H 8.147 . . 612 236 64 ARG HB2 H 1.842 . 2 613 236 64 ARG HH11 H 7.279 . . 614 236 64 ARG CA C 59.239 . . 615 236 64 ARG CB C 28.961 . . 616 236 64 ARG N N 120.664 . . 617 237 65 ILE H H 7.987 . . 618 237 65 ILE HA H 3.815 . . 619 237 65 ILE HB H 2.159 . . 620 237 65 ILE HD1 H 0.920 . 1 621 237 65 ILE HG12 H 2.453 . . 622 237 65 ILE HG2 H 0.979 . . 623 237 65 ILE CA C 65.885 . . 624 237 65 ILE CB C 38.750 . . 625 237 65 ILE CD1 C 15.414 . 1 626 237 65 ILE CG1 C 28.418 . . 627 237 65 ILE CG2 C 17.741 . . 628 237 65 ILE N N 118.994 . . 629 238 66 GLN H H 7.839 . . 630 238 66 GLN HA H 3.908 . . 631 238 66 GLN HB2 H 2.145 . . 632 238 66 GLN HB3 H 2.076 . 2 633 238 66 GLN HG2 H 2.504 . . 634 238 66 GLN HG3 H 2.459 . . 635 238 66 GLN CA C 58.291 . . 636 238 66 GLN CB C 28.208 . . 637 238 66 GLN CG C 33.161 . . 638 238 66 GLN N N 117.440 . . 639 239 67 ASN H H 8.448 . . 640 239 67 ASN HA H 4.679 . 1 641 239 67 ASN HB2 H 2.761 . 2 642 239 67 ASN HB3 H 3.008 . 2 643 239 67 ASN CA C 52.183 . . 644 239 67 ASN CB C 37.930 . . 645 239 67 ASN N N 114.365 . . 646 240 68 GLY H H 7.590 . . 647 240 68 GLY HA2 H 4.058 . . 648 240 68 GLY HA3 H 3.972 . . 649 240 68 GLY CA C 46.515 . . 650 240 68 GLY N N 107.344 . . 651 241 69 SER H H 8.354 . . 652 241 69 SER HA H 4.075 . . 653 241 69 SER HB2 H 3.610 . . 654 241 69 SER HB3 H 3.355 . . 655 241 69 SER CA C 61.098 . . 656 241 69 SER CB C 62.979 . . 657 241 69 SER N N 115.099 . . 658 242 70 TYR H H 7.962 . . 659 242 70 TYR HA H 4.832 . . 660 242 70 TYR HB2 H 3.002 . 2 661 242 70 TYR HB3 H 2.934 . . 662 242 70 TYR HD1 H 6.829 . . 663 242 70 TYR HE1 H 6.837 . . 664 242 70 TYR CA C 55.116 . . 665 242 70 TYR CB C 38.045 . . 666 242 70 TYR CD1 C 131.300 . 3 667 242 70 TYR CE1 C 118.380 . 3 668 242 70 TYR N N 118.420 . . 669 243 71 LYS H H 8.862 . . 670 243 71 LYS HA H 4.518 . 1 671 243 71 LYS HB2 H 3.339 . 2 672 243 71 LYS HB3 H 3.113 . 2 673 243 71 LYS CA C 55.793 . . 674 243 71 LYS CB C 31.488 . . 675 243 71 LYS N N 120.166 . . 676 244 72 SER H H 7.664 . . 677 244 72 SER HA H 4.551 . . 678 244 72 SER HB2 H 4.165 . . 679 244 72 SER HB3 H 3.996 . . 680 244 72 SER CA C 56.725 . . 681 244 72 SER CB C 65.633 . . 682 244 72 SER N N 109.853 . . 683 245 73 ILE H H 9.119 . . 684 245 73 ILE HA H 3.615 . 1 685 245 73 ILE HB H 1.594 . 1 686 245 73 ILE HD1 H 0.782 . 1 687 245 73 ILE HG12 H 1.013 . . 688 245 73 ILE HG2 H 0.645 . . 689 245 73 ILE CA C 65.098 . . 690 245 73 ILE CB C 37.678 . . 691 245 73 ILE CD1 C 13.790 . 1 692 245 73 ILE CG1 C 27.928 . . 693 245 73 ILE CG2 C 18.019 . . 694 245 73 ILE N N 120.033 . . 695 246 74 HIS H H 8.100 . . 696 246 74 HIS HA H 4.185 . . 697 246 74 HIS HB2 H 3.066 . . 698 246 74 HIS HD2 H 6.962 . 1 699 246 74 HIS CA C 58.807 . . 700 246 74 HIS CB C 30.337 . . 701 246 74 HIS CD2 C 119.032 . 1 702 246 74 HIS N N 119.252 . . 703 247 75 ALA H H 7.791 . . 704 247 75 ALA HA H 3.964 . . 705 247 75 ALA HB H 1.662 . . 706 247 75 ALA CA C 54.882 . . 707 247 75 ALA CB C 19.166 . . 708 247 75 ALA N N 120.473 . . 709 248 76 MET H H 6.606 . . 710 248 76 MET HA H 3.044 . . 711 248 76 MET HB2 H 1.760 . 2 712 248 76 MET HB3 H 1.050 . 2 713 248 76 MET HE H 1.851 . 1 714 248 76 MET HG2 H 2.124 . 2 715 248 76 MET HG3 H 1.886 . . 716 248 76 MET CA C 58.587 . . 717 248 76 MET CB C 31.352 . . 718 248 76 MET CE C 18.528 . 1 719 248 76 MET CG C 33.187 . . 720 248 76 MET N N 117.460 . . 721 249 77 ALA H H 8.333 . . 722 249 77 ALA HA H 3.247 . . 723 249 77 ALA HB H 1.587 . . 724 249 77 ALA CA C 54.899 . . 725 249 77 ALA CB C 17.792 . . 726 249 77 ALA N N 121.870 . . 727 250 78 LYS H H 7.579 . . 728 250 78 LYS HA H 3.874 . . 729 250 78 LYS HB2 H 1.783 . . 730 250 78 LYS HG2 H 1.468 . . 731 250 78 LYS HG3 H 1.358 . 2 732 250 78 LYS CA C 59.291 . . 733 250 78 LYS CB C 32.014 . . 734 250 78 LYS CG C 24.528 . . 735 250 78 LYS N N 114.867 . . 736 251 79 ASP H H 6.963 . . 737 251 79 ASP HA H 4.670 . 1 738 251 79 ASP HB2 H 2.741 . 2 739 251 79 ASP HB3 H 2.416 . 2 740 251 79 ASP CA C 56.711 . . 741 251 79 ASP CB C 39.730 . . 742 251 79 ASP N N 121.196 . . 743 252 80 ILE H H 7.815 . . 744 252 80 ILE HA H 3.421 . 1 745 252 80 ILE HB H 1.454 . 1 746 252 80 ILE HD1 H 0.152 . . 747 252 80 ILE HG12 H 0.883 . 9 748 252 80 ILE HG13 H -0.311 . 9 749 252 80 ILE HG2 H 0.267 . . 750 252 80 ILE CA C 61.150 . . 751 252 80 ILE CB C 34.003 . 1 752 252 80 ILE CD1 C 8.233 . . 753 252 80 ILE CG1 C 25.126 . 1 754 252 80 ILE CG2 C 15.952 . . 755 252 80 ILE N N 123.525 . . 756 253 81 ASP H H 8.875 . . 757 253 81 ASP HA H 4.045 . . 758 253 81 ASP HB2 H 2.786 . . 759 253 81 ASP HB3 H 2.503 . . 760 253 81 ASP CA C 57.453 . . 761 253 81 ASP CB C 39.256 . . 762 253 81 ASP N N 120.047 . . 763 254 82 LEU H H 7.660 . . 764 254 82 LEU HA H 4.078 . . 765 254 82 LEU HB2 H 2.051 . 2 766 254 82 LEU HB3 H 1.617 . 2 767 254 82 LEU HD1 H 0.914 . . 768 254 82 LEU HD2 H 0.987 . . 769 254 82 LEU HG H 1.549 . 1 770 254 82 LEU CA C 57.983 . . 771 254 82 LEU CB C 40.829 . . 772 254 82 LEU CD1 C 25.615 . . 773 254 82 LEU CD2 C 22.982 . . 774 254 82 LEU CG C 27.098 . 1 775 254 82 LEU N N 123.120 . . 776 255 83 LEU H H 8.166 . . 777 255 83 LEU HA H 3.654 . 1 778 255 83 LEU HB2 H 2.068 . 2 779 255 83 LEU HB3 H 1.584 . . 780 255 83 LEU HD1 H 0.917 . . 781 255 83 LEU HD2 H 0.551 . . 782 255 83 LEU HG H 1.590 . 1 783 255 83 LEU CA C 59.022 . . 784 255 83 LEU CB C 42.546 . . 785 255 83 LEU CD1 C 27.229 . 2 786 255 83 LEU CD2 C 26.208 . . 787 255 83 LEU CG C 26.348 . 1 788 255 83 LEU N N 121.111 . . 789 256 84 ALA H H 8.234 . . 790 256 84 ALA HA H 3.962 . . 791 256 84 ALA HB H 1.237 . . 792 256 84 ALA CA C 54.709 . . 793 256 84 ALA CB C 18.690 . . 794 256 84 ALA N N 119.823 . . 795 257 85 LYS H H 8.604 . . 796 257 85 LYS HA H 3.834 . 1 797 257 85 LYS HB2 H 1.941 . 2 798 257 85 LYS HD2 H 2.939 . 2 799 257 85 LYS HE2 H 3.173 . 2 800 257 85 LYS HG2 H 1.495 . 2 801 257 85 LYS CA C 59.539 . . 802 257 85 LYS CB C 32.055 . . 803 257 85 LYS N N 119.959 . . 804 258 86 ASN H H 9.174 . . 805 258 86 ASN HA H 4.283 . 1 806 258 86 ASN HB2 H 3.009 . 2 807 258 86 ASN HB3 H 2.564 . 2 808 258 86 ASN CA C 55.274 . . 809 258 86 ASN CB C 37.357 . . 810 258 86 ASN N N 120.185 . . 811 259 87 ALA H H 7.275 . . 812 259 87 ALA HA H 4.302 . 1 813 259 87 ALA HB H 1.667 . . 814 259 87 ALA CA C 54.794 . . 815 259 87 ALA CB C 19.324 . . 816 259 87 ALA N N 121.393 . . 817 260 88 LYS H H 8.102 . . 818 260 88 LYS HB2 H 1.518 . 2 819 260 88 LYS HG2 H 1.753 . . 820 260 88 LYS HG3 H 1.686 . 2 821 260 88 LYS CA C 58.049 . . 822 260 88 LYS CB C 31.777 . . 823 260 88 LYS N N 117.441 . . 824 261 89 THR H H 8.117 . . 825 261 89 THR HA H 4.198 . 1 826 261 89 THR HB H 4.309 . 1 827 261 89 THR HG2 H 1.139 . . 828 261 89 THR CA C 65.071 . . 829 261 89 THR CB C 68.978 . . 830 261 89 THR CG2 C 20.662 . . 831 261 89 THR N N 116.216 . . 832 262 90 TYR H H 8.043 . . 833 262 90 TYR HA H 4.203 . . 834 262 90 TYR HB2 H 2.823 . . 835 262 90 TYR HD1 H 6.905 . . 836 262 90 TYR HE1 H 6.710 . . 837 262 90 TYR CA C 60.596 . . 838 262 90 TYR CB C 40.501 . . 839 262 90 TYR CD1 C 133.050 . 3 840 262 90 TYR CE1 C 118.170 . 3 841 262 90 TYR N N 118.234 . . 842 263 91 ASN H H 7.610 . 1 843 263 91 ASN HA H 3.824 . . 844 263 91 ASN HB2 H 2.831 . 2 845 263 91 ASN CA C 59.320 . 1 846 263 91 ASN CB C 43.355 . 1 847 263 91 ASN N N 112.470 . 1 848 264 92 GLU H H 8.860 . 1 849 264 92 GLU HA H 4.399 . . 850 264 92 GLU HB2 H 1.921 . . 851 264 92 GLU HG2 H 2.273 . . 852 264 92 GLU CA C 54.586 . . 853 264 92 GLU CB C 29.533 . . 854 264 92 GLU CG C 35.753 . . 855 264 92 GLU N N 117.950 . 1 856 265 93 PRO HB2 H 1.708 . 2 857 265 93 PRO HB3 H 1.508 . . 858 265 93 PRO HD2 H 3.818 . . 859 265 93 PRO HD3 H 3.539 . . 860 265 93 PRO HG2 H 1.968 . . 861 265 93 PRO HG3 H 1.783 . . 862 265 93 PRO CA C 63.246 . . 863 265 93 PRO CB C 31.322 . . 864 265 93 PRO CD C 50.685 . . 865 265 93 PRO CG C 27.614 . . 866 266 94 GLY H H 8.571 . . 867 266 94 GLY HA2 H 4.395 . . 868 266 94 GLY HA3 H 3.736 . . 869 266 94 GLY CA C 44.990 . . 870 266 94 GLY N N 109.392 . . 871 267 95 SER H H 7.870 . . 872 267 95 SER HA H 4.402 . . 873 267 95 SER HB2 H 4.236 . . 874 267 95 SER HB3 H 4.082 . . 875 267 95 SER CA C 58.303 . . 876 267 95 SER CB C 65.223 . . 877 267 95 SER N N 115.596 . . 878 268 96 GLN H H 9.030 . . 879 268 96 GLN HA H 4.437 . . 880 268 96 GLN HB2 H 2.110 . . 881 268 96 GLN HB3 H 1.999 . . 882 268 96 GLN CA C 58.847 . . 883 268 96 GLN CB C 29.299 . . 884 268 96 GLN N N 123.168 . . 885 269 97 VAL H H 8.269 . . 886 269 97 VAL HA H 4.092 . 1 887 269 97 VAL HB H 1.809 . 1 888 269 97 VAL HG1 H 0.828 . 4 889 269 97 VAL HG2 H 0.955 . . 890 269 97 VAL CA C 65.610 . . 891 269 97 VAL CB C 31.525 . . 892 269 97 VAL CG1 C 25.148 . 2 893 269 97 VAL CG2 C 22.717 . . 894 269 97 VAL N N 117.625 . . 895 270 98 PHE H H 7.150 . 1 896 270 98 PHE HA H 3.807 . . 897 270 98 PHE HB2 H 3.572 . 2 898 270 98 PHE HB3 H 2.610 . . 899 270 98 PHE HD1 H 7.214 . . 900 270 98 PHE HE1 H 7.275 . . 901 270 98 PHE CA C 61.478 . . 902 270 98 PHE CB C 41.083 . . 903 270 98 PHE CD1 C 132.620 . 3 904 270 98 PHE CE1 C 130.890 . 3 905 270 98 PHE N N 123.400 . 1 906 271 99 LYS H H 8.280 . 1 907 271 99 LYS HA H 4.310 . 1 908 271 99 LYS HB2 H 2.020 . 2 909 271 99 LYS HB3 H 1.740 . 2 910 271 99 LYS HD2 H 1.440 . 2 911 271 99 LYS HG2 H 1.620 . 2 912 271 99 LYS CA C 55.140 . 1 913 271 99 LYS CB C 32.014 . . 914 271 99 LYS CD C 24.826 . 1 915 271 99 LYS CE C 41.014 . 1 916 271 99 LYS CG C 28.200 . 1 917 271 99 LYS N N 117.620 . . 918 272 100 ASP H H 9.346 . . 919 272 100 ASP HA H 4.397 . 1 920 272 100 ASP HB2 H 3.127 . 2 921 272 100 ASP HB3 H 3.064 . 2 922 272 100 ASP CA C 57.757 . . 923 272 100 ASP CB C 40.229 . . 924 272 100 ASP N N 122.011 . . 925 273 101 ALA H H 8.337 . . 926 273 101 ALA HA H 3.524 . . 927 273 101 ALA HB H 1.504 . . 928 273 101 ALA CA C 55.218 . . 929 273 101 ALA CB C 18.755 . . 930 273 101 ALA N N 122.926 . . 931 274 102 ASN H H 8.334 . . 932 274 102 ASN HA H 4.422 . 1 933 274 102 ASN HB2 H 2.922 . 2 934 274 102 ASN HB3 H 2.838 . 2 935 274 102 ASN CA C 56.188 . . 936 274 102 ASN CB C 38.125 . . 937 274 102 ASN N N 122.855 . . 938 275 103 SER H H 8.638 . . 939 275 103 SER HA H 4.284 . 1 940 275 103 SER HB2 H 3.871 . 2 941 275 103 SER CB C 62.295 . 1 942 275 103 SER N N 118.944 . . 943 276 104 ILE H H 8.497 . . 944 276 104 ILE HA H 3.354 . 1 945 276 104 ILE HB H 1.720 . 1 946 276 104 ILE HD1 H -0.117 . . 947 276 104 ILE HG12 H 1.430 . 9 948 276 104 ILE HG13 H 0.571 . 9 949 276 104 ILE HG2 H 0.533 . 4 950 276 104 ILE CA C 66.143 . . 951 276 104 ILE CB C 36.896 . . 952 276 104 ILE CD1 C 12.531 . . 953 276 104 ILE CG1 C 29.475 . 1 954 276 104 ILE CG2 C 15.922 . 1 955 276 104 ILE N N 122.530 . . 956 277 105 LYS H H 7.360 . . 957 277 105 LYS HB2 H 1.793 . 2 958 277 105 LYS HE2 H 2.891 . 2 959 277 105 LYS CA C 60.416 . . 960 277 105 LYS CB C 32.438 . . 961 277 105 LYS N N 117.981 . . 962 278 106 LYS H H 8.111 . . 963 278 106 LYS CA C 59.802 . . 964 278 106 LYS CB C 32.294 . . 965 278 106 LYS N N 118.392 . . 966 279 107 ILE H H 8.695 . . 967 279 107 ILE HA H 3.632 . 9 968 279 107 ILE HB H 1.837 . 9 969 279 107 ILE HD1 H 0.771 . 1 970 279 107 ILE HG12 H 1.539 . 2 971 279 107 ILE HG13 H 1.369 . 2 972 279 107 ILE HG2 H 0.774 . 9 973 279 107 ILE CA C 63.770 . . 974 279 107 ILE CB C 37.393 . . 975 279 107 ILE CD1 C 12.358 . 1 976 279 107 ILE CG1 C 27.429 . 1 977 279 107 ILE CG2 C 17.435 . 1 978 279 107 ILE N N 119.806 . . 979 280 108 PHE H H 8.262 . . 980 280 108 PHE HA H 3.750 . . 981 280 108 PHE HB2 H 2.879 . 2 982 280 108 PHE HD1 H 6.167 . . 983 280 108 PHE HE1 H 6.835 . . 984 280 108 PHE HZ H 6.599 . 1 985 280 108 PHE CA C 62.239 . . 986 280 108 PHE CB C 39.194 . . 987 280 108 PHE CD1 C 131.780 . 3 988 280 108 PHE CE1 C 131.110 . 3 989 280 108 PHE CZ C 127.229 . 1 990 280 108 PHE N N 119.418 . . 991 281 109 TYR H H 8.512 . . 992 281 109 TYR HA H 3.889 . . 993 281 109 TYR HB2 H 3.093 . 2 994 281 109 TYR HB3 H 2.866 . 2 995 281 109 TYR HD1 H 7.297 . . 996 281 109 TYR HE1 H 6.753 . . 997 281 109 TYR CA C 64.050 . . 998 281 109 TYR CB C 37.364 . . 999 281 109 TYR CE1 C 117.100 . 3 1000 281 109 TYR N N 115.869 . . 1001 282 110 MET H H 8.728 . . 1002 282 110 MET HB2 H 2.784 . 2 1003 282 110 MET HB3 H 2.546 . 2 1004 282 110 MET HE H 2.028 . 1 1005 282 110 MET HG2 H 2.002 . 2 1006 282 110 MET CA C 59.001 . . 1007 282 110 MET CB C 32.632 . . 1008 282 110 MET CE C 16.308 . 1 1009 282 110 MET CG C 31.646 . 1 1010 282 110 MET N N 122.079 . . 1011 283 111 LYS H H 8.223 . . 1012 283 111 LYS HA H 4.130 . . 1013 283 111 LYS HB2 H 1.784 . 2 1014 283 111 LYS HB3 H 1.664 . 2 1015 283 111 LYS HD2 H 1.767 . 2 1016 283 111 LYS HD3 H 1.631 . 2 1017 283 111 LYS HE2 H 2.840 . 2 1018 283 111 LYS HE3 H 2.653 . 2 1019 283 111 LYS HG2 H 1.278 . 2 1020 283 111 LYS CA C 56.449 . . 1021 283 111 LYS CB C 29.692 . . 1022 283 111 LYS CD C 27.106 . 1 1023 283 111 LYS CE C 41.546 . 1 1024 283 111 LYS CG C 24.282 . 1 1025 283 111 LYS N N 121.601 . . 1026 284 112 LYS H H 8.363 . . 1027 284 112 LYS HA H 3.398 . 1 1028 284 112 LYS HB2 H 1.556 . 2 1029 284 112 LYS HB3 H 0.926 . 2 1030 284 112 LYS HD2 H 1.559 . 2 1031 284 112 LYS HD3 H 1.259 . 2 1032 284 112 LYS HE2 H 3.076 . 2 1033 284 112 LYS HE3 H 2.729 . 2 1034 284 112 LYS HG2 H 1.334 . 2 1035 284 112 LYS CA C 60.090 . . 1036 284 112 LYS CB C 33.181 . . 1037 284 112 LYS CD C 30.724 . 1 1038 284 112 LYS CE C 41.080 . 1 1039 284 112 LYS N N 120.530 . . 1040 285 113 ALA H H 7.548 . . 1041 285 113 ALA HA H 4.158 . 1 1042 285 113 ALA HB H 1.504 . 1 1043 285 113 ALA CA C 54.402 . . 1044 285 113 ALA CB C 17.824 . . 1045 285 113 ALA N N 118.930 . . 1046 286 114 GLU H H 7.589 . . 1047 286 114 GLU CA C 59.004 . . 1048 286 114 GLU CB C 39.539 . . 1049 286 114 GLU N N 118.288 . . 1050 287 115 ILE H H 8.041 . . 1051 287 115 ILE HA H 3.803 . . 1052 287 115 ILE HB H 1.735 . 1 1053 287 115 ILE HD1 H 0.664 . 1 1054 287 115 ILE HG12 H 1.594 . . 1055 287 115 ILE HG13 H 1.092 . . 1056 287 115 ILE HG2 H 0.801 . 4 1057 287 115 ILE CA C 63.687 . . 1058 287 115 ILE CB C 38.966 . . 1059 287 115 ILE CD1 C 14.447 . 1 1060 287 115 ILE CG1 C 28.464 . . 1061 287 115 ILE CG2 C 17.377 . 1 1062 287 115 ILE N N 118.235 . . 1063 288 116 GLU H H 8.242 . . 1064 288 116 GLU CA C 57.886 . . 1065 288 116 GLU CB C 29.257 . . 1066 288 116 GLU N N 118.766 . . 1067 289 117 HIS H H 7.945 . . 1068 289 117 HIS CA C 56.670 . . 1069 289 117 HIS CB C 28.701 . . 1070 289 117 HIS N N 117.134 . . 1071 290 118 HIS H H 8.075 . . 1072 290 118 HIS CA C 56.378 . . 1073 290 118 HIS CB C 29.539 . . 1074 290 118 HIS N N 118.822 . . 1075 291 119 GLU H H 8.421 . . 1076 291 119 GLU CA C 56.737 . . 1077 291 119 GLU CB C 29.794 . . 1078 291 119 GLU N N 120.928 . . 1079 292 120 MET H H 8.268 . . 1080 292 120 MET CA C 55.350 . . 1081 292 120 MET CB C 32.718 . . 1082 292 120 MET N N 120.959 . . 1083 293 121 ALA H H 7.876 . . 1084 293 121 ALA CA C 53.871 . . 1085 293 121 ALA CB C 19.942 . . 1086 293 121 ALA N N 110.633 . . stop_ loop_ _Atom_shift_assign_ID_ambiguity ',' ',,' ',,,,,' ',,' ',,,,,' ',,' ',,' ',,' ',,' ',,' ',,' stop_ save_