data_4866 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone Resonance Assignment of Human UBC4 ; _BMRB_accession_number 4866 _BMRB_flat_file_name bmr4866.str _Entry_type original _Submission_date 2000-10-18 _Accession_date 2000-10-18 _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 Farrow Neil A . 2 Archer Sharon J . 3 Wu Zhongren J . 4 Camac Daniel M . 5 Parsons Tom . . 6 Rolfe Mark . . 7 Domaille Peter J . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 128 "13C chemical shifts" 244 "15N chemical shifts" 128 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-12-18 original author . stop_ _Original_release_date 2000-12-18 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone resonance assignment of human UBC4 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Farrow Neil A . 2 Archer Sharon J . 3 Wu Zhongren J . 4 Camac Daniel M . 5 Parsons Tom . . 6 Rolfe Mark . . 7 Domaille Peter J . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 18 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 363 _Page_last 364 _Year 2000 _Details . loop_ _Keyword UBC4 'heteronuclear NMR' 'resonance assignments' ubiquitination stop_ save_ ################################## # Molecular system description # ################################## save_system_UBC4 _Saveframe_category molecular_system _Mol_system_name UBC4 _Abbreviation_common UBC4 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label ubc4 $ubc4 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'mediates transfer between E1 and E3 components of ubiquitination pathways' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ubc4 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ubiquition conjugating enzyme 4' _Abbreviation_common ubc4 _Molecular_mass 16735.3 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 147 _Mol_residue_sequence ; MALKRIHKELNDLARDPPAQ CSAGPVGDDMFHWQATIMGP NDSPYQGGVFFLTIHFPTDY PFKPPKVAFTTRIYHPNINS NGSICLDILRSQWSPALTIS KVLLSICSLLCDPNPDDPLV PEIARIYKTDREKYNRIARE WTQKYAM ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 LEU 4 LYS 5 ARG 6 ILE 7 HIS 8 LYS 9 GLU 10 LEU 11 ASN 12 ASP 13 LEU 14 ALA 15 ARG 16 ASP 17 PRO 18 PRO 19 ALA 20 GLN 21 CYS 22 SER 23 ALA 24 GLY 25 PRO 26 VAL 27 GLY 28 ASP 29 ASP 30 MET 31 PHE 32 HIS 33 TRP 34 GLN 35 ALA 36 THR 37 ILE 38 MET 39 GLY 40 PRO 41 ASN 42 ASP 43 SER 44 PRO 45 TYR 46 GLN 47 GLY 48 GLY 49 VAL 50 PHE 51 PHE 52 LEU 53 THR 54 ILE 55 HIS 56 PHE 57 PRO 58 THR 59 ASP 60 TYR 61 PRO 62 PHE 63 LYS 64 PRO 65 PRO 66 LYS 67 VAL 68 ALA 69 PHE 70 THR 71 THR 72 ARG 73 ILE 74 TYR 75 HIS 76 PRO 77 ASN 78 ILE 79 ASN 80 SER 81 ASN 82 GLY 83 SER 84 ILE 85 CYS 86 LEU 87 ASP 88 ILE 89 LEU 90 ARG 91 SER 92 GLN 93 TRP 94 SER 95 PRO 96 ALA 97 LEU 98 THR 99 ILE 100 SER 101 LYS 102 VAL 103 LEU 104 LEU 105 SER 106 ILE 107 CYS 108 SER 109 LEU 110 LEU 111 CYS 112 ASP 113 PRO 114 ASN 115 PRO 116 ASP 117 ASP 118 PRO 119 LEU 120 VAL 121 PRO 122 GLU 123 ILE 124 ALA 125 ARG 126 ILE 127 TYR 128 LYS 129 THR 130 ASP 131 ARG 132 GLU 133 LYS 134 TYR 135 ASN 136 ARG 137 ILE 138 ALA 139 ARG 140 GLU 141 TRP 142 THR 143 GLN 144 LYS 145 TYR 146 ALA 147 MET stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 6277 monomeric_polymer 100.00 147 100.00 100.00 4.78e-105 PDB 1UR6 "Nmr Based Structural Model Of The Ubch5b-Cnot4 Complex" 100.00 147 100.00 100.00 4.78e-105 PDB 1W4U "Nmr Solution Structure Of The Ubiquitin Conjugating Enzyme Ubch5b" 100.00 147 100.00 100.00 4.78e-105 PDB 1X23 "Crystal Structure Of Ubch5c" 100.00 155 97.28 100.00 5.43e-102 PDB 2CLW "Crystal Structure Of Human Ubiquitin-conjugating Enzyme Ubch5b" 100.00 165 100.00 100.00 7.38e-105 PDB 2ESK "Human Ubiquitin-Conjugating Enzyme (E2) Ubch5b, Wild-Type" 100.00 149 100.00 100.00 5.01e-105 PDB 2ESO "Human Ubiquitin-Conjugating Enzyme (E2) Ubch5b Mutant Ile37ala" 100.00 149 99.32 99.32 2.36e-104 PDB 2ESP "Human Ubiquitin-Conjugating Enzyme (E2) Ubch5b Mutant Ile88ala" 100.00 149 99.32 99.32 2.36e-104 PDB 2ESQ "Human Ubiquitin-Conjugating Enzyme (E2) Ubch5b Mutant Ser94gly" 100.00 149 99.32 99.32 2.50e-104 PDB 2FUH "Solution Structure Of The Ubch5cUB NON-Covalent Complex" 99.32 146 97.26 100.00 2.18e-101 PDB 3A33 "Ubch5b~ubiquitin Conjugate" 100.00 150 99.32 99.32 6.05e-104 PDB 3EB6 "Structure Of The Ciap2 Ring Domain Bound To Ubch5b" 100.00 149 100.00 100.00 4.11e-105 PDB 3JVZ E2~ubiquitin-Hect 99.32 146 97.95 97.95 2.40e-101 PDB 3JW0 E2~ubiquitin-Hect 99.32 146 97.95 97.95 2.40e-101 PDB 3L1Y "Crystal Structure Of Human Ubc4 E2 Conjugating Enzyme" 100.00 157 99.32 100.00 1.28e-104 PDB 3L1Z "Crystal Structure Of The U-Box Domain Of Human E4b Ubiquitin Ligase In Complex With Ubch5c E2 Ubiquitin Conjugating Enzyme" 100.00 157 97.28 100.00 3.47e-102 PDB 3RPG "Bmi1RING1B-Ubch5c Complex Structure" 99.32 149 97.26 100.00 1.78e-101 PDB 3TGD "Crystal Structure Of The Human Ubiquitin-Conjugating Enzyme (E2) Ubch5b" 100.00 152 100.00 100.00 3.46e-105 PDB 3ZNI "Structure Of Phosphotyr363-cbl-b - Ubch5b-ub - Zap-70 Peptide Complex" 99.32 146 98.63 98.63 6.55e-102 PDB 4A49 "Structure Of Phosphotyr371-C-Cbl-Ubch5b Complex" 100.00 147 100.00 100.00 4.78e-105 PDB 4A4B "Structure Of Modified Phosphotyr371-C-Cbl-Ubch5b-Zap-70 Complex" 100.00 147 100.00 100.00 4.78e-105 PDB 4A4C "Structure Of Phosphotyr371-C-Cbl-Ubch5b-Zap-70 Complex" 100.00 147 100.00 100.00 4.78e-105 PDB 4AUQ "Structure Of Birc7-Ubch5b-Ub Complex" 100.00 147 97.96 97.96 3.63e-102 PDB 4DDG "Crystal Structure Of Human Otub1UBCH5B~UBUB" 100.00 399 99.32 99.32 5.39e-104 PDB 4DDI "Crystal Structure Of Human Otub1UBCH5B~UBUB" 100.00 399 99.32 99.32 5.39e-104 PDB 4LDT "The Structure Of H/ceotub1-ubiquitin Aldehyde-ubch5b~ub" 100.00 148 99.32 99.32 6.45e-104 PDB 4R8P "Crystal Structure Of The Ring1b/bmi1/ubch5c Prc1 Ubiquitylation Module Bound To The Nucleosome Core Particle" 99.32 268 97.26 100.00 6.17e-101 PDB 4WZ3 "Crystal Structure Of The Complex Between Lubx/legu2/lpp2887 U-box 1 And Homo Sapiens Ube2d2" 100.00 148 99.32 99.32 6.45e-104 DBJ BAA87330 "phosphoarginine phosphatase [Rattus norvegicus]" 100.00 147 97.28 100.00 2.68e-102 DBJ BAB23116 "unnamed protein product [Mus musculus]" 100.00 147 97.28 100.00 2.68e-102 DBJ BAC28070 "unnamed protein product [Mus musculus]" 100.00 147 97.28 100.00 2.68e-102 DBJ BAC33981 "unnamed protein product [Mus musculus]" 100.00 147 97.28 100.00 2.68e-102 DBJ BAC36940 "unnamed protein product [Mus musculus]" 100.00 147 97.28 100.00 2.68e-102 EMBL CAG31534 "hypothetical protein RCJMB04_7i20 [Gallus gallus]" 100.00 147 97.28 100.00 2.68e-102 EMBL CAH93209 "hypothetical protein [Pongo abelii]" 100.00 147 97.28 100.00 2.68e-102 EMBL CAJ81618 "ubiquitin-conjugating enzyme E2D 2 (UBC4/5 homolog, yeast) [Xenopus (Silurana) tropicalis]" 100.00 147 100.00 100.00 4.78e-105 EMBL CDQ70075 "unnamed protein product [Oncorhynchus mykiss]" 100.00 148 97.28 98.64 2.35e-102 EMBL CDQ72611 "unnamed protein product [Oncorhynchus mykiss]" 100.00 147 97.96 98.64 4.87e-103 GB AAA85100 "ubiquitin conjugating enzyme [Rattus norvegicus]" 100.00 147 97.28 100.00 2.68e-102 GB AAA85101 "ubiquitin conjugating enzyme [Rattus norvegicus]" 100.00 147 100.00 100.00 4.78e-105 GB AAA85102 "ubiquitin conjugating enzyme [Rattus norvegicus]" 100.00 147 97.28 100.00 2.68e-102 GB AAA91460 "UbcH5B [Homo sapiens]" 100.00 147 100.00 100.00 4.78e-105 GB AAA91461 "UbcH5C [Homo sapiens]" 100.00 147 97.28 100.00 2.68e-102 PRF 2111484A "ubiquitin-conjugating enzyme" 100.00 147 99.32 100.00 1.76e-104 REF NP_001016064 "ubiquitin-conjugating enzyme E2D 3 [Xenopus (Silurana) tropicalis]" 100.00 147 100.00 100.00 4.78e-105 REF NP_001026324 "ubiquitin-conjugating enzyme E2 D3 [Gallus gallus]" 100.00 147 97.28 100.00 2.68e-102 REF NP_001032369 "ubiquitin-conjugating enzyme E2 D2 [Rattus norvegicus]" 100.00 147 100.00 100.00 4.78e-105 REF NP_001039961 "ubiquitin-conjugating enzyme E2 D2 [Bos taurus]" 100.00 147 100.00 100.00 4.78e-105 REF NP_001072141 "ubiquitin-conjugating enzyme E2 D2 [Sus scrofa]" 100.00 147 98.64 100.00 6.04e-104 SP P61077 "RecName: Full=Ubiquitin-conjugating enzyme E2 D3; AltName: Full=Ubiquitin carrier protein D3; AltName: Full=Ubiquitin-conjugati" 100.00 147 97.28 100.00 2.68e-102 SP P61078 "RecName: Full=Ubiquitin-conjugating enzyme E2 D3; AltName: Full=Phosphoarginine phosphatase; Short=PAPase; AltName: Full=Ubiqui" 100.00 147 97.28 100.00 2.68e-102 SP P61079 "RecName: Full=Ubiquitin-conjugating enzyme E2 D3; AltName: Full=Ubiquitin carrier protein D3; AltName: Full=Ubiquitin-conjugati" 100.00 147 97.28 100.00 2.68e-102 SP P62837 "RecName: Full=Ubiquitin-conjugating enzyme E2 D2; AltName: Full=Ubiquitin carrier protein D2; AltName: Full=Ubiquitin-conjugati" 100.00 147 100.00 100.00 4.78e-105 SP P62838 "RecName: Full=Ubiquitin-conjugating enzyme E2 D2; AltName: Full=Ubiquitin carrier protein D2; AltName: Full=Ubiquitin-conjugati" 100.00 147 100.00 100.00 4.78e-105 TPG DAA27344 "TPA: ubiquitin-conjugating enzyme E2 D2 [Bos taurus]" 100.00 147 100.00 100.00 4.78e-105 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $ubc4 human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $ubc4 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_max_value _Isotopic_labeling $ubc4 . mM 1 '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_nmrPipe _Saveframe_category software _Name nmrPipe _Version . loop_ _Task 'data processing' stop_ _Details . save_ save_PIPP _Saveframe_category software _Name PIPP _Version . loop_ _Task 'data analysis' visualization stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Task 'data analysis' visualization stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-15N-HSQC _Sample_label . save_ save_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCACONH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label . save_ save_CC-TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name CC-TOCSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-15N-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CC-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.05 n/a temperature 303 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . . DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 2 'methyl protons' ppm 0.0 . indirect . . . 0.153506088 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_ubc4_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name ubc4 _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 . 5 ARG N N 121.33 . . 2 . 5 ARG H H 7.850 . . 3 . 5 ARG CA C 57.74 . . 4 . 5 ARG CB C 28.88 . . 5 . 6 ILE N N 121.07 . . 6 . 6 ILE H H 8.210 . . 7 . 6 ILE CA C 66.65 . . 8 . 6 ILE CB C 38.0 . . 9 . 7 HIS N N 117.25 . . 10 . 7 HIS H H 8.420 . . 11 . 7 HIS CA C 59.91 . . 12 . 7 HIS CB C 29.51 . . 13 . 8 LYS N N 121.64 . . 14 . 8 LYS H H 8.020 . . 15 . 8 LYS CA C 59.85 . . 16 . 8 LYS CB C 32.49 . . 17 . 9 GLU N N 119.02 . . 18 . 9 GLU H H 8.520 . . 19 . 9 GLU CA C 60.62 . . 20 . 9 GLU CB C 29.47 . . 21 . 10 LEU N N 120.36 . . 22 . 10 LEU H H 8.460 . . 23 . 10 LEU CA C 58.05 . . 24 . 10 LEU CB C 41.44 . . 25 . 11 ASN N N 118.68 . . 26 . 11 ASN H H 8.190 . . 27 . 11 ASN CA C 56.23 . . 28 . 11 ASN CB C 38.37 . . 29 . 12 ASP N N 121.58 . . 30 . 12 ASP H H 8.730 . . 31 . 12 ASP CA C 57.49 . . 32 . 12 ASP CB C 40.37 . . 33 . 13 LEU N N 121.99 . . 34 . 13 LEU H H 8.200 . . 35 . 13 LEU CA C 57.82 . . 36 . 13 LEU CB C 42.21 . . 37 . 14 ALA N N 118.51 . . 38 . 14 ALA H H 7.850 . . 39 . 14 ALA CA C 53.98 . . 40 . 14 ALA CB C 18.39 . . 41 . 15 ARG N N 116.19 . . 42 . 15 ARG H H 7.550 . . 43 . 15 ARG CA C 57.72 . . 44 . 15 ARG CB C 31.16 . . 45 . 16 ASP N N 117.05 . . 46 . 16 ASP H H 7.770 . . 47 . 16 ASP CA C 51.83 . . 48 . 16 ASP CB C 41.20 . . 49 . 19 ALA N N 125.39 . . 50 . 19 ALA H H 8.500 . . 51 . 19 ALA CA C 53.75 . . 52 . 19 ALA CB C 18.46 . . 53 . 20 GLN N N 112.75 . . 54 . 20 GLN H H 8.580 . . 55 . 20 GLN CA C 57.52 . . 56 . 20 GLN CB C 28.05 . . 57 . 21 CYS N N 114.59 . . 58 . 21 CYS H H 7.720 . . 59 . 21 CYS CA C 57.33 . . 60 . 21 CYS CB C 31.74 . . 61 . 22 SER N N 114.46 . . 62 . 22 SER H H 8.570 . . 63 . 22 SER CA C 57.34 . . 64 . 22 SER CB C 65.63 . . 65 . 23 ALA N N 121.77 . . 66 . 23 ALA H H 8.370 . . 67 . 23 ALA CA C 52.29 . . 68 . 23 ALA CB C 23.34 . . 69 . 24 GLY N N 104.35 . . 70 . 24 GLY H H 8.160 . . 71 . 24 GLY CA C 45.10 . . 72 . 26 VAL N N 122.59 . . 73 . 26 VAL H H 8.530 . . 74 . 26 VAL CA C 62.54 . . 75 . 26 VAL CB C 31.48 . . 76 . 27 GLY N N 116.82 . . 77 . 27 GLY H H 8.710 . . 78 . 27 GLY CA C 46.46 . . 79 . 28 ASP N N 122.89 . . 80 . 28 ASP H H 8.550 . . 81 . 28 ASP CA C 54.06 . . 82 . 28 ASP CB C 40.77 . . 83 . 29 ASP N N 119.81 . . 84 . 29 ASP H H 7.900 . . 85 . 29 ASP CA C 52.88 . . 86 . 29 ASP CB C 41.40 . . 87 . 30 MET N N 121.95 . . 88 . 30 MET H H 8.580 . . 89 . 30 MET CA C 55.34 . . 90 . 30 MET CB C 31.49 . . 91 . 31 PHE N N 112.01 . . 92 . 31 PHE H H 8.420 . . 93 . 31 PHE CA C 59.34 . . 94 . 31 PHE CB C 38.44 . . 95 . 32 HIS N N 120.22 . . 96 . 32 HIS H H 7.860 . . 97 . 32 HIS CA C 54.26 . . 98 . 32 HIS CB C 31.28 . . 99 . 33 TRP N N 123.89 . . 100 . 33 TRP H H 9.700 . . 101 . 33 TRP CA C 54.14 . . 102 . 33 TRP CB C 33.28 . . 103 . 34 GLN N N 119.65 . . 104 . 34 GLN H H 8.830 . . 105 . 34 GLN CA C 54.02 . . 106 . 34 GLN CB C 32.34 . . 107 . 35 ALA N N 124.87 . . 108 . 35 ALA H H 8.840 . . 109 . 35 ALA CA C 50.39 . . 110 . 35 ALA CB C 23.92 . . 111 . 36 THR N N 113.44 . . 112 . 36 THR H H 8.880 . . 113 . 36 THR CA C 60.12 . . 114 . 36 THR CB C 71.52 . . 115 . 37 ILE N N 122.08 . . 116 . 37 ILE H H 9.130 . . 117 . 37 ILE CA C 59.92 . . 118 . 37 ILE CB C 42.48 . . 119 . 38 MET N N 125.06 . . 120 . 38 MET H H 8.310 . . 121 . 38 MET CA C 54.02 . . 122 . 38 MET CB C 32.6 . . 123 . 39 GLY N N 110.39 . . 124 . 39 GLY H H 9.240 . . 125 . 39 GLY CA C 44.29 . . 126 . 41 ASN N N 122.84 . . 127 . 41 ASN H H 8.970 . . 128 . 41 ASN CA C 55.03 . . 129 . 41 ASN CB C 38.38 . . 130 . 42 ASP N N 116.90 . . 131 . 42 ASP H H 8.870 . . 132 . 42 ASP CA C 54.90 . . 133 . 42 ASP CB C 38.98 . . 134 . 43 SER N N 114.61 . . 135 . 43 SER H H 7.900 . . 136 . 43 SER CA C 56.96 . . 137 . 43 SER CB C 66.01 . . 138 . 45 TYR N N 116.98 . . 139 . 45 TYR H H 7.360 . . 140 . 45 TYR CA C 55.70 . . 141 . 45 TYR CB C 38.41 . . 142 . 46 GLN N N 121.55 . . 143 . 46 GLN H H 7.280 . . 144 . 46 GLN CA C 57.95 . . 145 . 46 GLN CB C 28.82 . . 146 . 47 GLY N N 116.45 . . 147 . 47 GLY H H 9.210 . . 148 . 47 GLY CA C 45.15 . . 149 . 48 GLY N N 106.79 . . 150 . 48 GLY H H 8.500 . . 151 . 48 GLY CA C 44.80 . . 152 . 49 VAL N N 125.02 . . 153 . 49 VAL H H 8.840 . . 154 . 49 VAL CA C 62.38 . . 155 . 49 VAL CB C 33.08 . . 156 . 50 PHE N N 123.94 . . 157 . 50 PHE H H 8.740 . . 158 . 50 PHE CA C 56.25 . . 159 . 50 PHE CB C 41.42 . . 160 . 51 PHE N N 121.20 . . 161 . 51 PHE H H 9.280 . . 162 . 51 PHE CA C 56.86 . . 163 . 51 PHE CB C 40.79 . . 164 . 52 LEU N N 120.63 . . 165 . 52 LEU H H 9.150 . . 166 . 52 LEU CA C 54.47 . . 167 . 52 LEU CB C 45.98 . . 168 . 53 THR N N 114.64 . . 169 . 53 THR H H 9.260 . . 170 . 53 THR CA C 60.14 . . 171 . 53 THR CB C 71.17 . . 172 . 54 ILE N N 123.12 . . 173 . 54 ILE H H 8.370 . . 174 . 54 ILE CA C 59.86 . . 175 . 54 ILE CB C 41.45 . . 176 . 55 HIS N N 125.98 . . 177 . 55 HIS H H 9.08 . . 178 . 55 HIS CA C 53.52 . . 179 . 55 HIS CB C 31.88 . . 180 . 56 PHE N N 127.04 . . 181 . 56 PHE H H 9.140 . . 182 . 56 PHE CA C 56.05 . . 183 . 56 PHE CB C 39.88 . . 184 . 58 THR N N 111.87 . . 185 . 58 THR H H 8.570 . . 186 . 58 THR CA C 65.07 . . 187 . 58 THR CB C 68.39 . . 188 . 59 ASP N N 115.20 . . 189 . 59 ASP H H 8.530 . . 190 . 59 ASP CA C 52.32 . . 191 . 59 ASP CB C 38.89 . . 192 . 60 TYR N N 123.47 . . 193 . 60 TYR H H 7.720 . . 194 . 60 TYR CA C 58.43 . . 195 . 60 TYR CB C 39.75 . . 196 . 62 PHE N N 125.24 . . 197 . 62 PHE H H 9.040 . . 198 . 62 PHE CA C 60.74 . . 199 . 62 PHE CB C 37.77 . . 200 . 63 LYS N N 118.42 . . 201 . 63 LYS H H 7.070 . . 202 . 63 LYS CA C 52.18 . . 203 . 63 LYS CB C 34.89 . . 204 . 66 LYS N N 120.57 . . 205 . 66 LYS H H 8.270 . . 206 . 66 LYS CA C 54.95 . . 207 . 66 LYS CB C 32.98 . . 208 . 67 VAL N N 127.66 . . 209 . 67 VAL H H 8.750 . . 210 . 67 VAL CA C 60.38 . . 211 . 67 VAL CB C 33.95 . . 212 . 68 ALA N N 127.23 . . 213 . 68 ALA H H 8.490 . . 214 . 68 ALA CA C 50.79 . . 215 . 68 ALA CB C 22.15 . . 216 . 69 PHE N N 122.37 . . 217 . 69 PHE H H 9.800 . . 218 . 69 PHE CA C 59.17 . . 219 . 69 PHE CB C 40.13 . . 220 . 70 THR N N 116.46 . . 221 . 70 THR H H 9.540 . . 222 . 70 THR CA C 63.02 . . 223 . 71 THR N N 121.70 . . 224 . 71 THR H H 7.560 . . 225 . 71 THR CA C 63.52 . . 226 . 71 THR CB C 71.25 . . 227 . 72 ARG N N 127.88 . . 228 . 72 ARG H H 8.590 . . 229 . 72 ARG CA C 57.06 . . 230 . 72 ARG CB C 30.46 . . 231 . 73 ILE N N 120.38 . . 232 . 73 ILE H H 8.370 . . 233 . 73 ILE CA C 60.26 . . 234 . 73 ILE CB C 40.89 . . 235 . 74 TYR N N 131.90 . . 236 . 74 TYR H H 8.67 . . 237 . 74 TYR CA C 57.79 . . 238 . 74 TYR CB C 37.73 . . 239 . 75 HIS N N 129.35 . . 240 . 75 HIS H H 8.490 . . 241 . 75 HIS CA C 55.72 . . 242 . 75 HIS CB C 35.61 . . 243 . 77 ASN N N 118.52 . . 244 . 77 ASN H H 11.51 . . 245 . 77 ASN CA C 54.44 . . 246 . 77 ASN CB C 41.72 . . 247 . 78 ILE N N 120.34 . . 248 . 78 ILE H H 7.220 . . 249 . 78 ILE CA C 59.87 . . 250 . 78 ILE CB C 41.91 . . 251 . 79 ASN N N 121.58 . . 252 . 79 ASN H H 7.970 . . 253 . 79 ASN CA C 50.54 . . 254 . 79 ASN CB C 39.85 . . 255 . 80 SER N N 113.85 . . 256 . 80 SER H H 8.660 . . 257 . 80 SER CA C 60.87 . . 258 . 80 SER CB C 62.86 . . 259 . 81 ASN N N 118.23 . . 260 . 81 ASN H H 7.610 . . 261 . 81 ASN CA C 53.00 . . 262 . 81 ASN CB C 38.98 . . 263 . 82 GLY N N 109.88 . . 264 . 82 GLY H H 8.430 . . 265 . 82 GLY CA C 45.96 . . 266 . 83 SER N N 115.44 . . 267 . 83 SER H H 7.770 . . 268 . 83 SER CA C 59.11 . . 269 . 83 SER CB C 63.21 . . 270 . 84 ILE N N 119.74 . . 271 . 84 ILE H H 8.510 . . 272 . 84 ILE CA C 59.53 . . 273 . 84 ILE CB C 41.76 . . 274 . 85 CYS N N 127.67 . . 275 . 85 CYS H H 8.660 . . 276 . 85 CYS CA C 57.28 . . 277 . 85 CYS CB C 26.14 . . 278 . 86 LEU N N 126.92 . . 279 . 86 LEU H H 7.300 . . 280 . 86 LEU CA C 53.91 . . 281 . 86 LEU CB C 46.05 . . 282 . 87 ASP N N 129.33 . . 283 . 87 ASP H H 9.310 . . 284 . 87 ASP CA C 58.49 . . 285 . 87 ASP CB C 39.29 . . 286 . 88 ILE N N 116.23 . . 287 . 88 ILE H H 8.430 . . 288 . 88 ILE CA C 64.61 . . 289 . 88 ILE CB C 38.05 . . 290 . 89 LEU N N 113.54 . . 291 . 89 LEU H H 7.170 . . 292 . 89 LEU CA C 53.98 . . 293 . 89 LEU CB C 41.86 . . 294 . 90 ARG N N 121.14 . . 295 . 90 ARG H H 7.900 . . 296 . 90 ARG CA C 56.32 . . 297 . 90 ARG CB C 31.26 . . 298 . 91 SER N N 117.17 . . 299 . 91 SER H H 8.260 . . 300 . 91 SER CA C 60.80 . . 301 . 91 SER CB C 63.56 . . 302 . 92 GLN N N 117.61 . . 303 . 92 GLN H H 7.850 . . 304 . 92 GLN CA C 54.42 . . 305 . 92 GLN CB C 28.35 . . 306 . 93 TRP N N 121.16 . . 307 . 93 TRP H H 7.430 . . 308 . 93 TRP CA C 59.38 . . 309 . 93 TRP CB C 29.78 . . 310 . 94 SER N N 120.85 . . 311 . 94 SER H H 5.550 . . 312 . 94 SER CA C 54.50 . . 313 . 94 SER CB C 64.97 . . 314 . 96 ALA N N 118.48 . . 315 . 96 ALA H H 7.270 . . 316 . 96 ALA CA C 52.54 . . 317 . 96 ALA CB C 18.80 . . 318 . 97 LEU N N 119.48 . . 319 . 97 LEU H H 7.330 . . 320 . 97 LEU CA C 54.58 . . 321 . 97 LEU CB C 42.21 . . 322 . 98 THR N N 101.64 . . 323 . 98 THR H H 6.100 . . 324 . 98 THR CA C 58.01 . . 325 . 98 THR CB C 72.95 . . 326 . 99 ILE N N 122.53 . . 327 . 99 ILE H H 10.38 . . 328 . 99 ILE CA C 60.91 . . 329 . 99 ILE CB C 35.78 . . 330 . 100 SER N N 116.76 . . 331 . 100 SER H H 8.530 . . 332 . 100 SER CA C 62.64 . . 333 . 101 LYS N N 119.58 . . 334 . 101 LYS H H 7.530 . . 335 . 101 LYS CA C 58.89 . . 336 . 101 LYS CB C 32.26 . . 337 . 102 VAL N N 121.95 . . 338 . 102 VAL H H 8.420 . . 339 . 102 VAL CA C 67.16 . . 340 . 102 VAL CB C 31.70 . . 341 . 103 LEU N N 119.16 . . 342 . 103 LEU H H 8.700 . . 343 . 103 LEU CA C 58.45 . . 344 . 103 LEU CB C 40.81 . . 345 . 104 LEU N N 119.62 . . 346 . 104 LEU H H 8.360 . . 347 . 104 LEU CA C 58.45 . . 348 . 104 LEU CB C 41.71 . . 349 . 105 SER N N 117.44 . . 350 . 105 SER H H 8.260 . . 351 . 105 SER CA C 62.90 . . 352 . 106 ILE N N 124.36 . . 353 . 106 ILE H H 8.360 . . 354 . 106 ILE CA C 65.85 . . 355 . 106 ILE CB C 37.61 . . 356 . 107 CYS N N 118.77 . . 357 . 107 CYS H H 8.260 . . 358 . 107 CYS CA C 65.39 . . 359 . 107 CYS CB C 26.28 . . 360 . 108 SER N N 114.20 . . 361 . 108 SER H H 8.140 . . 362 . 108 SER CA C 56.70 . . 363 . 108 SER CB C 63.26 . . 364 . 109 LEU N N 124.04 . . 365 . 109 LEU H H 7.850 . . 366 . 109 LEU CA C 56.38 . . 367 . 109 LEU CB C 42.51 . . 368 . 110 LEU N N 118.93 . . 369 . 110 LEU H H 7.970 . . 370 . 110 LEU CA C 58.64 . . 371 . 110 LEU CB C 40.78 . . 372 . 111 CYS N N 113.70 . . 373 . 111 CYS H H 7.240 . . 374 . 111 CYS CA C 61.75 . . 375 . 111 CYS CB C 27.73 . . 376 . 112 ASP N N 118.87 . . 377 . 112 ASP H H 8.170 . . 378 . 112 ASP CA C 52.08 . . 379 . 112 ASP CB C 41.97 . . 380 . 114 ASN N N 114.99 . . 381 . 114 ASN H H 8.630 . . 382 . 114 ASN CA C 49.02 . . 383 . 114 ASN CB C 38.75 . . 384 . 116 ASP N N 118.06 . . 385 . 116 ASP H H 7.710 . . 386 . 116 ASP CA C 55.26 . . 387 . 116 ASP CB C 40.53 . . 388 . 117 ASP N N 118.46 . . 389 . 117 ASP H H 6.700 . . 390 . 117 ASP CA C 51.47 . . 391 . 117 ASP CB C 40.95 . . 392 . 119 LEU N N 117.92 . . 393 . 119 LEU H H 8.650 . . 394 . 119 LEU CA C 55.20 . . 395 . 119 LEU CB C 44.27 . . 396 . 120 VAL N N 118.01 . . 397 . 120 VAL H H 7.450 . . 398 . 120 VAL CA C 58.91 . . 399 . 120 VAL CB C 31.76 . . 400 . 122 GLU N N 118.13 . . 401 . 122 GLU H H 9.580 . . 402 . 122 GLU CA C 59.76 . . 403 . 122 GLU CB C 29.21 . . 404 . 123 ILE N N 117.27 . . 405 . 123 ILE H H 6.850 . . 406 . 123 ILE CA C 65.02 . . 407 . 124 ALA N N 121.64 . . 408 . 124 ALA H H 7.580 . . 409 . 124 ALA CA C 55.66 . . 410 . 124 ALA CB C 18.51 . . 411 . 125 ARG N N 116.55 . . 412 . 125 ARG H H 8.080 . . 413 . 125 ARG CA C 59.69 . . 414 . 125 ARG CB C 29.75 . . 415 . 126 ILE N N 121.93 . . 416 . 126 ILE H H 8.300 . . 417 . 126 ILE CA C 65.25 . . 418 . 126 ILE CB C 37.74 . . 419 . 127 TYR N N 119.25 . . 420 . 127 TYR H H 8.600 . . 421 . 127 TYR CA C 63.29 . . 422 . 127 TYR CB C 38.37 . . 423 . 128 LYS N N 112.78 . . 424 . 128 LYS H H 7.870 . . 425 . 128 LYS CA C 59.12 . . 426 . 128 LYS CB C 33.62 . . 427 . 129 THR N N 108.68 . . 428 . 129 THR H H 7.890 . . 429 . 129 THR CA C 63.25 . . 430 . 129 THR CB C 71.20 . . 431 . 130 ASP N N 125.60 . . 432 . 130 ASP H H 9.030 . . 433 . 130 ASP CA C 52.71 . . 434 . 130 ASP CB C 40.36 . . 435 . 131 ARG N N 125.14 . . 436 . 131 ARG H H 8.620 . . 437 . 131 ARG CA C 57.58 . . 438 . 131 ARG CB C 28.98 . . 439 . 132 GLU N N 116.29 . . 440 . 132 GLU H H 8.420 . . 441 . 132 GLU CA C 59.46 . . 442 . 133 LYS N N 122.96 . . 443 . 133 LYS H H 7.560 . . 444 . 133 LYS CA C 59.74 . . 445 . 133 LYS CB C 32.32 . . 446 . 134 TYR N N 118.52 . . 447 . 134 TYR H H 8.140 . . 448 . 134 TYR CA C 61.96 . . 449 . 134 TYR CB C 37.97 . . 450 . 135 ASN N N 117.24 . . 451 . 135 ASN H H 8.750 . . 452 . 135 ASN CA C 55.75 . . 453 . 135 ASN CB C 37.79 . . 454 . 136 ARG N N 120.34 . . 455 . 136 ARG H H 7.940 . . 456 . 136 ARG CA C 59.90 . . 457 . 136 ARG CB C 30.00 . . 458 . 137 ILE N N 122.39 . . 459 . 137 ILE H H 7.680 . . 460 . 137 ILE CA C 65.25 . . 461 . 137 ILE CB C 37.65 . . 462 . 138 ALA N N 121.27 . . 463 . 138 ALA H H 8.560 . . 464 . 138 ALA CA C 55.73 . . 465 . 138 ALA CB C 17.43 . . 466 . 139 ARG N N 120.89 . . 467 . 139 ARG H H 8.300 . . 468 . 139 ARG CA C 59.74 . . 469 . 139 ARG CB C 30.19 . . 470 . 140 GLU N N 123.41 . . 471 . 140 GLU H H 8.410 . . 472 . 140 GLU CA C 59.82 . . 473 . 140 GLU CB C 29.20 . . 474 . 141 TRP N N 120.07 . . 475 . 141 TRP H H 9.610 . . 476 . 141 TRP CA C 61.50 . . 477 . 141 TRP CB C 29.01 . . 478 . 142 THR N N 124.76 . . 479 . 142 THR H H 8.580 . . 480 . 142 THR CB C 68.0 . . 481 . 143 GLN N N 119.65 . . 482 . 143 GLN H H 8.140 . . 483 . 143 GLN CA C 58.33 . . 484 . 143 GLN CB C 28.41 . . 485 . 144 LYS N N 115.98 . . 486 . 144 LYS H H 7.960 . . 487 . 144 LYS CA C 58.66 . . 488 . 144 LYS CB C 33.32 . . 489 . 145 TYR N N 112.62 . . 490 . 145 TYR H H 8.060 . . 491 . 145 TYR CA C 57.95 . . 492 . 145 TYR CB C 40.42 . . 493 . 146 ALA N N 123.07 . . 494 . 146 ALA H H 8.250 . . 495 . 146 ALA CA C 51.25 . . 496 . 146 ALA CB C 21.65 . . 497 . 147 MET N N 122.59 . . 498 . 147 MET H H 7.240 . . 499 . 147 MET CA C 56.84 . . 500 . 147 MET CB C 35.54 . . stop_ save_