data_19913 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Structure of KDM5B PHD1 finger ; _BMRB_accession_number 19913 _BMRB_flat_file_name bmr19913.str _Entry_type original _Submission_date 2014-04-16 _Accession_date 2014-04-16 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhang Y. . . 2 Yang H. R. . 3 Guo X. . . 4 Rong N. Y. . 5 Song Y. J. . 6 Xu Y. W. . 7 Lan W. X. . 8 Xu Y. H. . 9 Cao C. Y. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 258 "13C chemical shifts" 189 "15N chemical shifts" 51 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-08-04 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 19914 'KDM5B PHD1 finger in complex with H3K4me0(1-10aa)' stop_ _Original_release_date 2014-08-04 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'The PHD1 finger of KDM5B recognizes unmodified H3K4 during the demethylation of histone H3K4me2/3 by KDM5B' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24952722 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhang Y. . . 2 Yang H. R. . 3 Guo X. . . 4 Rong N. Y. . 5 Song Y. J. . 6 Xu Y. W. . 7 Lan W. X. . 8 Xu Y. H. . 9 Cao C. Y. . stop_ _Journal_abbreviation 'Protein Cell' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2014 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_citations_2 _Saveframe_category citation _Citation_full . _Citation_title 'The PHD1 finger of KDM5B recognizes unmodified H3K4 during demethylation of histone H3K4me2/3 by KDM5B' _Citation_status 'in preparation' _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 Zhang Y. . . 2 Yang H. R. . 3 Guo X. . . 4 Rong N. Y. . 5 Song Y. J. . 6 Xu Y. H. . 7 Cao C. Y. . stop_ _Journal_abbreviation 'To be published' _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'KDM5B PHD1 finger' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'PHD1 finger of KDM5B' $PHD1_finger_of_KDM5B 'ZINC ION_1' $entity_ZN 'ZINC ION_2' $entity_ZN 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_PHD1_finger_of_KDM5B _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PHD1_finger_of_KDM5B _Molecular_mass 6133.026 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 55 _Mol_residue_sequence ; AVDLYVCLLCGSGNDEDRLL LCDGCDDSYHTFCLIPPLHD VPKGDWRCPKCLAQE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 306 ALA 2 307 VAL 3 308 ASP 4 309 LEU 5 310 TYR 6 311 VAL 7 312 CYS 8 313 LEU 9 314 LEU 10 315 CYS 11 316 GLY 12 317 SER 13 318 GLY 14 319 ASN 15 320 ASP 16 321 GLU 17 322 ASP 18 323 ARG 19 324 LEU 20 325 LEU 21 326 LEU 22 327 CYS 23 328 ASP 24 329 GLY 25 330 CYS 26 331 ASP 27 332 ASP 28 333 SER 29 334 TYR 30 335 HIS 31 336 THR 32 337 PHE 33 338 CYS 34 339 LEU 35 340 ILE 36 341 PRO 37 342 PRO 38 343 LEU 39 344 HIS 40 345 ASP 41 346 VAL 42 347 PRO 43 348 LYS 44 349 GLY 45 350 ASP 46 351 TRP 47 352 ARG 48 353 CYS 49 354 PRO 50 355 LYS 51 356 CYS 52 357 LEU 53 358 ALA 54 359 GLN 55 360 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 19914 entity_1 100.00 55 100.00 100.00 1.77e-30 PDB 2MNY "Nmr Structure Of Kdm5b Phd1 Finger" 100.00 55 100.00 100.00 1.77e-30 PDB 2MNZ "Nmr Structure Of Kdm5b Phd1 Finger In Complex With H3k4me0(1-10aa)" 100.00 55 100.00 100.00 1.77e-30 DBJ BAC30898 "unnamed protein product [Mus musculus]" 100.00 1433 98.18 100.00 2.78e-29 DBJ BAD90482 "mKIAA4034 protein [Mus musculus]" 100.00 1554 98.18 100.00 3.12e-29 DBJ BAE37363 "unnamed protein product [Mus musculus]" 100.00 600 98.18 100.00 4.27e-32 DBJ BAE89761 "unnamed protein product [Macaca fascicularis]" 100.00 194 100.00 100.00 2.11e-32 DBJ BAG53706 "unnamed protein product [Homo sapiens]" 100.00 1275 100.00 100.00 1.48e-29 EMBL CAB43532 "PLU-1 protein [Homo sapiens]" 100.00 1544 100.00 100.00 2.61e-29 EMBL CAB61368 "hypothetical protein [Homo sapiens]" 100.00 1350 100.00 100.00 1.57e-29 EMBL CAB63108 "RB-binding protein [Homo sapiens]" 100.00 1681 100.00 100.00 2.58e-29 EMBL CAH65222 "hypothetical protein RCJMB04_9d3 [Gallus gallus]" 100.00 1522 98.18 100.00 6.55e-29 GB AAD16061 "retinoblastoma binding protein 2 homolog 1 [Homo sapiens]" 100.00 1580 100.00 100.00 2.31e-29 GB AAH48180 "Jumonji, AT rich interactive domain 1B (Rbp2 like) [Mus musculus]" 100.00 1544 98.18 100.00 3.63e-29 GB AAH57318 "Jumonji, AT rich interactive domain 1B (Rbp2 like) [Mus musculus]" 100.00 1544 98.18 100.00 3.63e-29 GB AAI56050 "Jumonji, AT rich interactive domain 1B, partial [synthetic construct]" 100.00 1544 100.00 100.00 2.61e-29 GB AAI57032 "Jumonji, AT rich interactive domain 1B [synthetic construct]" 100.00 1544 100.00 100.00 2.61e-29 REF NP_001026200 "lysine-specific demethylase 5B [Gallus gallus]" 100.00 1522 98.18 100.00 6.55e-29 REF NP_001100647 "lysine-specific demethylase 5B [Rattus norvegicus]" 100.00 1544 98.18 100.00 4.76e-29 REF NP_001300971 "lysine-specific demethylase 5B isoform 1 [Homo sapiens]" 100.00 1580 100.00 100.00 2.43e-29 REF NP_006609 "lysine-specific demethylase 5B isoform 2 [Homo sapiens]" 100.00 1544 100.00 100.00 2.61e-29 REF NP_690855 "lysine-specific demethylase 5B [Mus musculus]" 100.00 1544 98.18 100.00 3.63e-29 SP Q5F3R2 "RecName: Full=Lysine-specific demethylase 5B; AltName: Full=Histone demethylase JARID1B; AltName: Full=Jumonji/ARID domain-cont" 100.00 1522 98.18 100.00 6.55e-29 SP Q80Y84 "RecName: Full=Lysine-specific demethylase 5B; AltName: Full=Histone demethylase JARID1B; AltName: Full=Jumonji/ARID domain-cont" 100.00 1544 98.18 100.00 3.63e-29 SP Q9UGL1 "RecName: Full=Lysine-specific demethylase 5B; AltName: Full=Cancer/testis antigen 31; Short=CT31; AltName: Full=Histone demethy" 100.00 1544 100.00 100.00 2.61e-29 TPG DAA21261 "TPA: RB-binding protein-like [Bos taurus]" 100.00 1489 98.18 100.00 1.42e-28 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'ZINC ION' _BMRB_code ZN _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . 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 $PHD1_finger_of_KDM5B Human 9606 Eukaryota Metazoa Homo sapiens KDM5B 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 $PHD1_finger_of_KDM5B 'recombinant technology' . Escherichia coli BL21(DE3) pGEX-6p-1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '50mM phosphate buffer NA; 90% H2O, 10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PHD1_finger_of_KDM5B 0.8 mM '[U-13C; U-15N]' 'Phosphate buffer' 50 mM 'natural abundance' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details '50mM phosphate buffer NA; 100% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PHD1_finger_of_KDM5B 0.8 mM '[U-13C; U-15N]' 'Phosphate buffer' 50 mM 'natural abundance' D2O 100 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CNS _Saveframe_category software _Name CNS _Version . loop_ _Vendor _Address _Electronic_address 'Brunger A. T. et.al.' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Agilent _Model DD2 _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 3D_15N-separated_NOESY _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_1 save_ save_3D_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_aliphatic_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY aliphatic' _Sample_label $sample_2 save_ save_3D_1H-13C_NOESY_aromatic_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY aromatic' _Sample_label $sample_2 save_ save_3D_HCCH-TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_2 save_ save_2D_1H-13C_HSQC_aromatic_11 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aromatic' _Sample_label $sample_2 save_ save_2D_1H-13C_HSQC_aliphatic_12 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 7.2 . pH pressure 1 . atm temperature 293 . K 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 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 DSS P 31 'methyl protons' ppm 0.00 na indirect . . . 0.404808636 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D CBCA(CO)NH' '3D 1H-15N TOCSY' '3D HNCACB' '3D HCCH-TOCSY' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'PHD1 finger of KDM5B' _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 1 306 1 ALA H H 8.304 . . 2 306 1 ALA HA H 4.523 . . 3 306 1 ALA HB H 1.320 . . 4 306 1 ALA CA C 52.562 . . 5 306 1 ALA CB C 19.232 . . 6 306 1 ALA N N 126.686 . . 7 307 2 VAL H H 7.872 . . 8 307 2 VAL HA H 3.991 . . 9 307 2 VAL HB H 1.962 . . 10 307 2 VAL HG1 H 0.788 . . 11 307 2 VAL C C 177.476 . . 12 307 2 VAL CA C 62.065 . . 13 307 2 VAL CB C 32.788 . . 14 307 2 VAL CG1 C 20.333 . . 15 307 2 VAL N N 118.179 . . 16 308 3 ASP H H 8.107 . . 17 308 3 ASP HA H 4.404 . . 18 308 3 ASP HB2 H 2.420 . . 19 308 3 ASP C C 175.590 . . 20 308 3 ASP CA C 54.414 . . 21 308 3 ASP CB C 41.163 . . 22 308 3 ASP N N 123.079 . . 23 309 4 LEU H H 7.782 . . 24 309 4 LEU HA H 4.122 . . 25 309 4 LEU HB2 H 1.301 . . 26 309 4 LEU HB3 H 1.246 . . 27 309 4 LEU HG H 1.301 . . 28 309 4 LEU HD1 H 0.711 . . 29 309 4 LEU C C 175.120 . . 30 309 4 LEU CA C 54.941 . . 31 309 4 LEU CB C 42.747 . . 32 309 4 LEU CG C 26.766 . . 33 309 4 LEU N N 121.827 . . 34 310 5 TYR H H 7.972 . . 35 310 5 TYR HA H 4.488 . . 36 310 5 TYR HB2 H 2.857 . . 37 310 5 TYR HB3 H 2.631 . . 38 310 5 TYR HD1 H 7.130 . . 39 310 5 TYR HD2 H 7.074 . . 40 310 5 TYR HE1 H 6.853 . . 41 310 5 TYR HE2 H 6.719 . . 42 310 5 TYR C C 176.521 . . 43 310 5 TYR CA C 57.274 . . 44 310 5 TYR CB C 38.499 . . 45 310 5 TYR N N 121.643 . . 46 311 6 VAL H H 7.770 . . 47 311 6 VAL HA H 3.942 . . 48 311 6 VAL HB H 1.429 . . 49 311 6 VAL HG1 H 0.547 . . 50 311 6 VAL HG2 H 0.523 . . 51 311 6 VAL C C 174.625 . . 52 311 6 VAL CA C 59.412 . . 53 311 6 VAL CB C 35.267 . . 54 311 6 VAL CG1 C 21.206 . . 55 311 6 VAL CG2 C 19.330 . . 56 311 6 VAL N N 116.085 . . 57 312 7 CYS H H 7.352 . . 58 312 7 CYS HA H 3.687 . . 59 312 7 CYS HB2 H 3.295 . . 60 312 7 CYS HB3 H 1.730 . . 61 312 7 CYS C C 173.885 . . 62 312 7 CYS CA C 58.177 . . 63 312 7 CYS CB C 31.625 . . 64 312 7 CYS N N 125.869 . . 65 313 8 LEU H H 8.618 . . 66 313 8 LEU HA H 3.837 . . 67 313 8 LEU HB2 H 1.036 . . 68 313 8 LEU HB3 H 1.286 . . 69 313 8 LEU HD1 H 0.138 . . 70 313 8 LEU HD2 H 0.782 . . 71 313 8 LEU C C 177.490 . . 72 313 8 LEU CA C 57.097 . . 73 313 8 LEU CB C 42.940 . . 74 313 8 LEU CD2 C 24.434 . . 75 313 8 LEU N N 131.350 . . 76 314 9 LEU H H 8.416 . . 77 314 9 LEU HA H 4.379 . . 78 314 9 LEU HB2 H 1.748 . . 79 314 9 LEU HB3 H 1.602 . . 80 314 9 LEU HG H 1.771 . . 81 314 9 LEU HD1 H 0.928 . . 82 314 9 LEU HD2 H 1.025 . . 83 314 9 LEU C C 178.028 . . 84 314 9 LEU CA C 56.444 . . 85 314 9 LEU CB C 42.651 . . 86 314 9 LEU CG C 27.240 . . 87 314 9 LEU CD1 C 22.121 . . 88 314 9 LEU CD2 C 26.355 . . 89 314 9 LEU N N 118.835 . . 90 315 10 CYS H H 8.083 . . 91 315 10 CYS HA H 4.987 . . 92 315 10 CYS HB2 H 3.229 . . 93 315 10 CYS HB3 H 3.068 . . 94 315 10 CYS C C 178.187 . . 95 315 10 CYS CA C 58.518 . . 96 315 10 CYS CB C 31.441 . . 97 315 10 CYS N N 117.699 . . 98 316 11 GLY H H 7.964 . . 99 316 11 GLY HA2 H 4.034 . . 100 316 11 GLY HA3 H 3.709 . . 101 316 11 GLY C C 177.322 . . 102 316 11 GLY CA C 46.379 . . 103 316 11 GLY N N 113.759 . . 104 317 12 SER H H 8.396 . . 105 317 12 SER HA H 4.799 . . 106 317 12 SER HB2 H 3.893 . . 107 317 12 SER HB3 H 4.180 . . 108 317 12 SER C C 173.213 . . 109 317 12 SER CA C 56.714 . . 110 317 12 SER CB C 65.016 . . 111 317 12 SER N N 116.224 . . 112 318 13 GLY H H 8.995 . . 113 318 13 GLY HA2 H 4.580 . . 114 318 13 GLY HA3 H 3.640 . . 115 318 13 GLY C C 175.280 . . 116 318 13 GLY CA C 44.964 . . 117 318 13 GLY N N 115.779 . . 118 319 14 ASN H H 8.100 . . 119 319 14 ASN HA H 4.755 . . 120 319 14 ASN HB2 H 2.888 . . 121 319 14 ASN HB3 H 2.687 . . 122 319 14 ASN HD21 H 6.909 . . 123 319 14 ASN HD22 H 7.681 . . 124 319 14 ASN C C 174.299 . . 125 319 14 ASN CA C 52.580 . . 126 319 14 ASN CB C 38.665 . . 127 319 14 ASN N N 117.359 . . 128 319 14 ASN ND2 N 113.587 . . 129 320 15 ASP H H 9.018 . . 130 320 15 ASP HA H 4.273 . . 131 320 15 ASP HB2 H 2.808 . . 132 320 15 ASP HB3 H 2.549 . . 133 320 15 ASP C C 173.489 . . 134 320 15 ASP CA C 55.882 . . 135 320 15 ASP CB C 40.111 . . 136 320 15 ASP N N 117.365 . . 137 321 16 GLU H H 9.270 . . 138 321 16 GLU HA H 3.803 . . 139 321 16 GLU HB2 H 2.099 . . 140 321 16 GLU HB3 H 2.012 . . 141 321 16 GLU HG2 H 2.324 . . 142 321 16 GLU HG3 H 2.391 . . 143 321 16 GLU C C 177.041 . . 144 321 16 GLU CA C 59.903 . . 145 321 16 GLU CB C 28.634 . . 146 321 16 GLU CG C 35.954 . . 147 321 16 GLU N N 117.886 . . 148 322 17 ASP H H 8.963 . . 149 322 17 ASP HA H 4.357 . . 150 322 17 ASP HB2 H 2.642 . . 151 322 17 ASP HB3 H 2.675 . . 152 322 17 ASP C C 178.105 . . 153 322 17 ASP CA C 55.433 . . 154 322 17 ASP CB C 39.282 . . 155 322 17 ASP N N 118.832 . . 156 323 18 ARG H H 8.036 . . 157 323 18 ARG HA H 4.305 . . 158 323 18 ARG HB2 H 1.649 . . 159 323 18 ARG HG2 H 1.598 . . 160 323 18 ARG HD2 H 3.178 . . 161 323 18 ARG HD3 H 3.093 . . 162 323 18 ARG C C 176.878 . . 163 323 18 ARG CA C 54.828 . . 164 323 18 ARG CB C 30.492 . . 165 323 18 ARG CG C 27.609 . . 166 323 18 ARG CD C 43.576 . . 167 323 18 ARG N N 119.537 . . 168 324 19 LEU H H 7.184 . . 169 324 19 LEU HA H 4.128 . . 170 324 19 LEU HB2 H 1.190 . . 171 324 19 LEU HB3 H 1.590 . . 172 324 19 LEU HG H 1.087 . . 173 324 19 LEU HD1 H 0.165 . . 174 324 19 LEU HD2 H 0.262 . . 175 324 19 LEU C C 173.644 . . 176 324 19 LEU CA C 54.516 . . 177 324 19 LEU CB C 43.186 . . 178 324 19 LEU CG C 25.773 . . 179 324 19 LEU CD1 C 24.110 . . 180 324 19 LEU CD2 C 24.966 . . 181 324 19 LEU N N 122.512 . . 182 325 20 LEU H H 8.663 . . 183 325 20 LEU HA H 4.085 . . 184 325 20 LEU HB2 H 0.943 . . 185 325 20 LEU HB3 H 0.399 . . 186 325 20 LEU HD1 H -0.597 . . 187 325 20 LEU HD2 H 0.212 . . 188 325 20 LEU C C 174.639 . . 189 325 20 LEU CA C 53.501 . . 190 325 20 LEU CB C 42.882 . . 191 325 20 LEU CD1 C 24.571 . . 192 325 20 LEU CD2 C 23.110 . . 193 325 20 LEU N N 127.850 . . 194 326 21 LEU H H 8.139 . . 195 326 21 LEU HB2 H 1.529 . . 196 326 21 LEU HB3 H 1.224 . . 197 326 21 LEU HD1 H 0.536 . . 198 326 21 LEU C C 175.138 . . 199 326 21 LEU CA C 53.510 . . 200 326 21 LEU CB C 43.439 . . 201 326 21 LEU CD1 C 23.661 . . 202 326 21 LEU N N 123.988 . . 203 327 22 CYS H H 8.955 . . 204 327 22 CYS HA H 4.669 . . 205 327 22 CYS HB2 H 3.491 . . 206 327 22 CYS HB3 H 2.862 . . 207 327 22 CYS C C 176.283 . . 208 327 22 CYS CA C 60.241 . . 209 327 22 CYS CB C 30.977 . . 210 327 22 CYS N N 129.096 . . 211 328 23 ASP H H 9.120 . . 212 328 23 ASP HA H 4.548 . . 213 328 23 ASP HB2 H 2.644 . . 214 328 23 ASP HB3 H 2.577 . . 215 328 23 ASP C C 176.845 . . 216 328 23 ASP CA C 56.716 . . 217 328 23 ASP CB C 41.709 . . 218 328 23 ASP N N 130.207 . . 219 329 24 GLY H H 9.925 . . 220 329 24 GLY HA2 H 4.025 . . 221 329 24 GLY HA3 H 3.993 . . 222 329 24 GLY C C 176.990 . . 223 329 24 GLY CA C 46.091 . . 224 329 24 GLY N N 113.572 . . 225 330 25 CYS H H 7.754 . . 226 330 25 CYS HA H 4.750 . . 227 330 25 CYS HB2 H 3.044 . . 228 330 25 CYS HB3 H 2.394 . . 229 330 25 CYS C C 174.598 . . 230 330 25 CYS CA C 58.591 . . 231 330 25 CYS CB C 32.793 . . 232 330 25 CYS N N 120.909 . . 233 331 26 ASP H H 8.124 . . 234 331 26 ASP HA H 4.630 . . 235 331 26 ASP HB2 H 2.686 . . 236 331 26 ASP HB3 H 3.017 . . 237 331 26 ASP C C 175.019 . . 238 331 26 ASP CA C 56.240 . . 239 331 26 ASP CB C 41.098 . . 240 331 26 ASP N N 119.370 . . 241 332 27 ASP H H 8.655 . . 242 332 27 ASP HA H 4.784 . . 243 332 27 ASP HB2 H 2.476 . . 244 332 27 ASP HB3 H 3.050 . . 245 332 27 ASP C C 174.899 . . 246 332 27 ASP CA C 55.577 . . 247 332 27 ASP CB C 42.723 . . 248 332 27 ASP N N 123.056 . . 249 333 28 SER H H 8.048 . . 250 333 28 SER HA H 5.805 . . 251 333 28 SER HB2 H 3.364 . . 252 333 28 SER HB3 H 3.285 . . 253 333 28 SER C C 175.056 . . 254 333 28 SER CA C 56.956 . . 255 333 28 SER CB C 65.816 . . 256 333 28 SER N N 114.384 . . 257 334 29 TYR H H 8.524 . . 258 334 29 TYR HA H 5.348 . . 259 334 29 TYR HB2 H 2.506 . . 260 334 29 TYR HB3 H 2.483 . . 261 334 29 TYR HD2 H 7.065 . . 262 334 29 TYR HE2 H 6.779 . . 263 334 29 TYR C C 172.769 . . 264 334 29 TYR CA C 56.301 . . 265 334 29 TYR CB C 44.519 . . 266 334 29 TYR N N 119.063 . . 267 335 30 HIS H H 9.094 . . 268 335 30 HIS HA H 5.073 . . 269 335 30 HIS HB2 H 2.846 . . 270 335 30 HIS HB3 H 1.220 . . 271 335 30 HIS HD2 H 6.543 . . 272 335 30 HIS HE1 H 7.502 . . 273 335 30 HIS C C 176.248 . . 274 335 30 HIS CA C 57.819 . . 275 335 30 HIS CB C 30.751 . . 276 335 30 HIS N N 122.478 . . 277 336 31 THR H H 8.774 . . 278 336 31 THR HA H 3.540 . . 279 336 31 THR HB H 4.335 . . 280 336 31 THR C C 178.618 . . 281 336 31 THR CA C 64.925 . . 282 336 31 THR CB C 66.144 . . 283 336 31 THR N N 113.249 . . 284 337 32 PHE H H 6.404 . . 285 337 32 PHE HA H 4.614 . . 286 337 32 PHE HB2 H 2.852 . . 287 337 32 PHE HB3 H 3.448 . . 288 337 32 PHE HD2 H 7.142 . . 289 337 32 PHE HE2 H 6.984 . . 290 337 32 PHE HZ H 6.282 . . 291 337 32 PHE C C 176.411 . . 292 337 32 PHE CA C 56.120 . . 293 337 32 PHE CB C 37.613 . . 294 337 32 PHE N N 111.508 . . 295 338 33 CYS H H 7.242 . . 296 338 33 CYS HA H 4.333 . . 297 338 33 CYS HB2 H 2.646 . . 298 338 33 CYS HB3 H 3.194 . . 299 338 33 CYS C C 176.704 . . 300 338 33 CYS CA C 61.911 . . 301 338 33 CYS CB C 31.093 . . 302 338 33 CYS N N 123.999 . . 303 339 34 LEU H H 6.373 . . 304 339 34 LEU HA H 3.905 . . 305 339 34 LEU HB2 H 1.360 . . 306 339 34 LEU HB3 H 1.635 . . 307 339 34 LEU HD1 H 0.649 . . 308 339 34 LEU C C 174.380 . . 309 339 34 LEU CA C 55.500 . . 310 339 34 LEU CB C 44.091 . . 311 339 34 LEU CD1 C 23.410 . . 312 339 34 LEU N N 119.805 . . 313 340 35 ILE H H 7.902 . . 314 340 35 ILE HA H 4.187 . . 315 340 35 ILE HB H 1.671 . . 316 340 35 ILE HG12 H 0.905 . . 317 340 35 ILE HD1 H 0.821 . . 318 340 35 ILE HD1 H 0.760 . . 319 340 35 ILE C C 175.079 . . 320 340 35 ILE CA C 57.800 . . 321 340 35 ILE CB C 40.240 . . 322 340 35 ILE CG1 C 27.043 . . 323 340 35 ILE CG2 C 17.208 . . 324 340 35 ILE CD1 C 12.777 . . 325 340 35 ILE N N 118.573 . . 326 342 37 PRO HB2 H 2.175 . . 327 342 37 PRO CA C 62.879 . . 328 342 37 PRO CB C 32.179 . . 329 343 38 LEU H H 7.545 . . 330 343 38 LEU HA H 4.409 . . 331 343 38 LEU HB2 H 1.510 . . 332 343 38 LEU HB3 H 1.247 . . 333 343 38 LEU HD1 H 0.781 . . 334 343 38 LEU HD2 H 0.710 . . 335 343 38 LEU C C 177.584 . . 336 343 38 LEU CA C 53.509 . . 337 343 38 LEU CB C 43.383 . . 338 343 38 LEU CD1 C 21.139 . . 339 343 38 LEU CD2 C 25.654 . . 340 343 38 LEU N N 120.513 . . 341 344 39 HIS HA H 4.348 . . 342 344 39 HIS HD2 H 7.062 . . 343 344 39 HIS HE1 H 7.920 . . 344 344 39 HIS CA C 57.627 . . 345 344 39 HIS CB C 30.363 . . 346 345 40 ASP H H 7.611 . . 347 345 40 ASP HA H 4.740 . . 348 345 40 ASP HB2 H 2.462 . . 349 345 40 ASP HB3 H 2.350 . . 350 345 40 ASP C C 174.506 . . 351 345 40 ASP CA C 52.254 . . 352 345 40 ASP CB C 43.198 . . 353 345 40 ASP N N 117.422 . . 354 346 41 VAL H H 8.531 . . 355 346 41 VAL HA H 3.820 . . 356 346 41 VAL HB H 1.890 . . 357 346 41 VAL HG1 H 0.880 . . 358 346 41 VAL HG2 H 0.816 . . 359 346 41 VAL C C 174.750 . . 360 346 41 VAL CA C 60.735 . . 361 346 41 VAL CB C 32.284 . . 362 346 41 VAL CG1 C 21.645 . . 363 346 41 VAL CG2 C 20.666 . . 364 346 41 VAL N N 123.018 . . 365 347 42 PRO HA H 4.345 . . 366 347 42 PRO HB2 H 2.272 . . 367 347 42 PRO HD2 H 3.682 . . 368 347 42 PRO HD3 H 3.372 . . 369 347 42 PRO CA C 62.910 . . 370 347 42 PRO CB C 32.179 . . 371 347 42 PRO CD C 51.191 . . 372 348 43 LYS H H 8.483 . . 373 348 43 LYS HA H 4.265 . . 374 348 43 LYS HB2 H 1.785 . . 375 348 43 LYS HB3 H 1.700 . . 376 348 43 LYS HG2 H 1.381 . . 377 348 43 LYS HG3 H 1.444 . . 378 348 43 LYS C C 176.355 . . 379 348 43 LYS CA C 55.928 . . 380 348 43 LYS CB C 32.714 . . 381 348 43 LYS CG C 24.917 . . 382 348 43 LYS N N 122.040 . . 383 349 44 GLY H H 8.103 . . 384 349 44 GLY HA2 H 3.949 . . 385 349 44 GLY HA3 H 3.918 . . 386 349 44 GLY C C 177.224 . . 387 349 44 GLY CA C 44.732 . . 388 349 44 GLY N N 110.439 . . 389 350 45 ASP H H 8.253 . . 390 350 45 ASP HA H 4.542 . . 391 350 45 ASP HB2 H 2.556 . . 392 350 45 ASP HB3 H 2.459 . . 393 350 45 ASP C C 172.943 . . 394 350 45 ASP CA C 54.611 . . 395 350 45 ASP CB C 41.333 . . 396 350 45 ASP N N 121.630 . . 397 351 46 TRP H H 9.050 . . 398 351 46 TRP HA H 4.336 . . 399 351 46 TRP HB2 H 3.075 . . 400 351 46 TRP HB3 H 3.004 . . 401 351 46 TRP HD1 H 7.244 . . 402 351 46 TRP HE3 H 7.189 . . 403 351 46 TRP HZ2 H 7.102 . . 404 351 46 TRP HZ3 H 6.769 . . 405 351 46 TRP HH2 H 6.525 . . 406 351 46 TRP C C 175.474 . . 407 351 46 TRP CA C 60.012 . . 408 351 46 TRP CB C 30.379 . . 409 351 46 TRP N N 126.420 . . 410 352 47 ARG H H 6.581 . . 411 352 47 ARG HA H 4.915 . . 412 352 47 ARG HB2 H 1.210 . . 413 352 47 ARG HB3 H 1.127 . . 414 352 47 ARG HG2 H 1.454 . . 415 352 47 ARG HG3 H 1.313 . . 416 352 47 ARG HD2 H 2.952 . . 417 352 47 ARG HD3 H 2.845 . . 418 352 47 ARG C C 173.419 . . 419 352 47 ARG CA C 52.612 . . 420 352 47 ARG CB C 33.712 . . 421 352 47 ARG CG C 27.656 . . 422 352 47 ARG CD C 43.241 . . 423 352 47 ARG N N 125.212 . . 424 353 48 CYS H H 8.982 . . 425 353 48 CYS HA H 3.573 . . 426 353 48 CYS HB2 H 3.007 . . 427 353 48 CYS HB3 H 2.362 . . 428 353 48 CYS C C 173.614 . . 429 353 48 CYS CA C 56.747 . . 430 353 48 CYS CB C 29.965 . . 431 353 48 CYS N N 126.478 . . 432 354 49 PRO HB2 H 1.692 . . 433 354 49 PRO HB3 H 1.762 . . 434 354 49 PRO HD2 H 3.099 . . 435 354 49 PRO CA C 65.437 . . 436 354 49 PRO CB C 32.226 . . 437 354 49 PRO CD C 49.685 . . 438 355 50 LYS H H 7.800 . . 439 355 50 LYS HA H 4.006 . . 440 355 50 LYS HB2 H 1.856 . . 441 355 50 LYS HG2 H 1.252 . . 442 355 50 LYS HG3 H 1.463 . . 443 355 50 LYS HD2 H 1.723 . . 444 355 50 LYS HD3 H 1.638 . . 445 355 50 LYS C C 179.592 . . 446 355 50 LYS CA C 59.630 . . 447 355 50 LYS CB C 32.384 . . 448 355 50 LYS CG C 25.086 . . 449 355 50 LYS CD C 25.520 . . 450 355 50 LYS N N 119.965 . . 451 356 51 CYS H H 8.513 . . 452 356 51 CYS HA H 3.771 . . 453 356 51 CYS HB2 H 2.683 . . 454 356 51 CYS C C 179.399 . . 455 356 51 CYS CA C 65.376 . . 456 356 51 CYS CB C 28.206 . . 457 356 51 CYS N N 125.452 . . 458 357 52 LEU H H 8.181 . . 459 357 52 LEU HA H 3.869 . . 460 357 52 LEU HB2 H 1.409 . . 461 357 52 LEU HB3 H 1.284 . . 462 357 52 LEU HG H 1.315 . . 463 357 52 LEU HD1 H 0.604 . . 464 357 52 LEU C C 179.011 . . 465 357 52 LEU CA C 56.974 . . 466 357 52 LEU CB C 41.807 . . 467 357 52 LEU CG C 26.081 . . 468 357 52 LEU CD1 C 23.039 . . 469 357 52 LEU N N 120.480 . . 470 358 53 ALA H H 7.422 . . 471 358 53 ALA HA H 4.098 . . 472 358 53 ALA HB H 1.359 . . 473 358 53 ALA C C 178.803 . . 474 358 53 ALA CA C 53.684 . . 475 358 53 ALA CB C 18.262 . . 476 358 53 ALA N N 121.422 . . 477 359 54 GLN H H 7.545 . . 478 359 54 GLN HA H 4.110 . . 479 359 54 GLN HB2 H 2.066 . . 480 359 54 GLN HB3 H 1.997 . . 481 359 54 GLN HG2 H 2.361 . . 482 359 54 GLN HG3 H 2.311 . . 483 359 54 GLN C C 178.826 . . 484 359 54 GLN CA C 56.722 . . 485 359 54 GLN CB C 29.099 . . 486 359 54 GLN CG C 33.831 . . 487 359 54 GLN N N 117.550 . . 488 360 55 GLU H H 7.861 . . 489 360 55 GLU HA H 4.136 . . 490 360 55 GLU HB2 H 1.961 . . 491 360 55 GLU HB3 H 1.910 . . 492 360 55 GLU HG2 H 2.233 . . 493 360 55 GLU HG3 H 2.171 . . 494 360 55 GLU C C 176.826 . . 495 360 55 GLU CA C 57.168 . . 496 360 55 GLU CB C 30.032 . . 497 360 55 GLU CG C 36.148 . . 498 360 55 GLU N N 120.736 . . stop_ save_