data_19584 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Dvl-2 DEP domain ; _BMRB_accession_number 19584 _BMRB_flat_file_name bmr19584.str _Entry_type original _Submission_date 2013-10-25 _Accession_date 2013-10-25 _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 Capelluto Daniel G.S. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 92 "13C chemical shifts" 274 "15N chemical shifts" 92 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-04-14 original author . stop_ _Original_release_date 2014-04-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Biophysical and Molecular-Dynamics Studies of Phosphatidic Acid Binding by the Dvl-2 DEP Domain.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24606934 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Capelluto Daniel G.S. . 2 Zhao Xiaolin . . 3 Lucas Andrew . . 4 Lemkul Justin A. . 5 Xiao Shuyan . . 6 Fu Xiangping . . 7 Sun Furong . . 8 Bevan David R. . 9 Finkielstein Carla V. . stop_ _Journal_abbreviation 'Biophys. J.' _Journal_name_full 'Biophysical journal' _Journal_volume 106 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1101 _Page_last 1111 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Dvl-2 DEP' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Dvl-2 DEP' $Dvl-2_DEP stop_ _System_molecular_weight 11544 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Dvl-2_DEP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Dvl-2_DEP _Molecular_mass . _Mol_thiol_state unknown _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 104 _Mol_residue_sequence ; GPLGSCEGRGLSVHMDMASV TKAMAAPESGLEVRDRMWLK ITIPNAFLGSDVVDWLYHHV EGFPERREARKYASGLLKAG LIRHTVNKITFSEQCYYVFG DLSG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -5 GLY 2 -4 PRO 3 -3 LEU 4 -2 GLY 5 -1 SER 6 412 CYS 7 413 GLU 8 414 GLY 9 415 ARG 10 416 GLY 11 417 LEU 12 418 SER 13 419 VAL 14 420 HIS 15 421 MET 16 422 ASP 17 423 MET 18 424 ALA 19 425 SER 20 426 VAL 21 427 THR 22 428 LYS 23 429 ALA 24 430 MET 25 431 ALA 26 432 ALA 27 433 PRO 28 434 GLU 29 435 SER 30 436 GLY 31 437 LEU 32 438 GLU 33 439 VAL 34 440 ARG 35 441 ASP 36 442 ARG 37 443 MET 38 444 TRP 39 445 LEU 40 446 LYS 41 447 ILE 42 448 THR 43 449 ILE 44 450 PRO 45 451 ASN 46 452 ALA 47 453 PHE 48 454 LEU 49 455 GLY 50 456 SER 51 457 ASP 52 458 VAL 53 459 VAL 54 460 ASP 55 461 TRP 56 462 LEU 57 463 TYR 58 464 HIS 59 465 HIS 60 466 VAL 61 467 GLU 62 468 GLY 63 469 PHE 64 470 PRO 65 471 GLU 66 472 ARG 67 473 ARG 68 474 GLU 69 475 ALA 70 476 ARG 71 477 LYS 72 478 TYR 73 479 ALA 74 480 SER 75 481 GLY 76 482 LEU 77 483 LEU 78 484 LYS 79 485 ALA 80 486 GLY 81 487 LEU 82 488 ILE 83 489 ARG 84 490 HIS 85 491 THR 86 492 VAL 87 493 ASN 88 494 LYS 89 495 ILE 90 496 THR 91 497 PHE 92 498 SER 93 499 GLU 94 500 GLN 95 501 CYS 96 502 TYR 97 503 TYR 98 504 VAL 99 505 PHE 100 506 GLY 101 507 ASP 102 508 LEU 103 509 SER 104 510 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 3ML6 "A Complex Between Dishevlled2 And Clathrin Adaptor Ap-2" 91.35 385 98.95 98.95 1.44e-59 DBJ BAE27460 "unnamed protein product [Mus musculus]" 95.19 736 100.00 100.00 1.87e-62 DBJ BAE35461 "unnamed protein product [Mus musculus]" 95.19 736 100.00 100.00 1.87e-62 DBJ BAE40307 "unnamed protein product [Mus musculus]" 95.19 736 100.00 100.00 1.87e-62 DBJ BAG59612 "unnamed protein product [Homo sapiens]" 95.19 730 98.99 98.99 9.73e-62 DBJ BAG65098 "unnamed protein product [Homo sapiens]" 95.19 717 98.99 98.99 8.17e-62 GB AAB65243 "dishevelled 2 [Homo sapiens]" 95.19 736 98.99 98.99 1.03e-61 GB AAC52827 "similar to Dvl-1 product encoded by GenBank Accession Number U10115; dishevelled segment polarity protein homolog [Mus musculus" 95.19 736 100.00 100.00 1.78e-62 GB AAH14844 "Dishevelled, dsh homolog 2 (Drosophila) [Homo sapiens]" 95.19 736 98.99 98.99 1.03e-61 GB AAH53050 "Dishevelled 2, dsh homolog (Drosophila) [Mus musculus]" 95.19 736 100.00 100.00 1.87e-62 GB AAH92396 "Dishevelled 2, dsh homolog (Drosophila) [Mus musculus]" 95.19 736 100.00 100.00 1.71e-62 REF NP_001165527 "segment polarity protein dishevelled homolog DVL-2 [Rattus norvegicus]" 95.19 736 100.00 100.00 1.42e-62 REF NP_001178311 "segment polarity protein dishevelled homolog DVL-2 [Bos taurus]" 95.19 740 97.98 98.99 2.05e-61 REF NP_001181735 "segment polarity protein dishevelled homolog DVL-2 [Macaca mulatta]" 95.19 730 97.98 98.99 1.73e-61 REF NP_004413 "segment polarity protein dishevelled homolog DVL-2 [Homo sapiens]" 95.19 736 98.99 98.99 1.03e-61 REF NP_031914 "segment polarity protein dishevelled homolog DVL-2 [Mus musculus]" 95.19 736 100.00 100.00 1.87e-62 SP O14641 "RecName: Full=Segment polarity protein dishevelled homolog DVL-2; Short=Dishevelled-2; AltName: Full=DSH homolog 2" 95.19 736 98.99 98.99 1.03e-61 SP Q60838 "RecName: Full=Segment polarity protein dishevelled homolog DVL-2; Short=Dishevelled-2; AltName: Full=DSH homolog 2" 95.19 736 100.00 100.00 1.87e-62 TPG DAA18923 "TPA: dishevelled, dsh homolog 2 [Bos taurus]" 95.19 736 97.98 98.99 1.65e-61 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Dvl-2_DEP Mouse 10090 Eukaryota Metazoa Mus musculus 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 $Dvl-2_DEP 'recombinant technology' . Escherichia coli Rosetta pGEX6P1 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 $Dvl-2_DEP 1 mM '[U-100% 13C; U-100% 15N]' 'sodium chloride' 100 mM 'natural abundance' 'sodium azide' 1 mM 'natural abundance' DTT-d10 1 mM '[U-98% 2H]' 'sodium citrate-d4' 20 mM '[U-98% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'data analysis' 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 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _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 'ionic strength' 100 . mM pH 6.7 . pH pressure 1 . atm temperature 298 . 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 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0 na indirect . . . 0.101329118 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 '2D 1H-15N HSQC' '3D HNCO' '3D HNCACB' '3D CBCA(CO)NH' '3D C(CO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Dvl-2 DEP' _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 1 412 6 CYS H H 8.50 . 1 2 412 6 CYS C C 174.75 . 1 3 412 6 CYS CA C 58.45 . 1 4 412 6 CYS CB C 27.98 . 1 5 412 6 CYS N N 120.80 . 1 6 413 7 GLU H H 8.47 . 1 7 413 7 GLU C C 174.60 . 1 8 413 7 GLU CA C 57.09 . 1 9 413 7 GLU CB C 30.13 . 1 10 413 7 GLU N N 122.90 . 1 11 414 8 GLY H H 8.41 . 1 12 414 8 GLY C C 176.05 . 1 13 414 8 GLY CA C 45.45 . 1 14 414 8 GLY N N 109.65 . 1 15 415 9 ARG H H 8.22 . 1 16 415 9 ARG C C 174.25 . 1 17 415 9 ARG CA C 55.49 . 1 18 415 9 ARG CB C 30.91 . 1 19 415 9 ARG N N 120.27 . 1 20 416 10 GLY H H 8.42 . 1 21 416 10 GLY C C 176.60 . 1 22 416 10 GLY CA C 45.23 . 1 23 416 10 GLY N N 109.68 . 1 24 417 11 LEU H H 8.08 . 1 25 417 11 LEU C C 173.67 . 1 26 417 11 LEU CA C 54.45 . 1 27 417 11 LEU CB C 44.06 . 1 28 417 11 LEU N N 119.88 . 1 29 418 12 SER H H 7.58 . 1 30 418 12 SER C C 174.60 . 1 31 418 12 SER CA C 56.89 . 1 32 418 12 SER CB C 66.56 . 1 33 418 12 SER N N 115.65 . 1 34 419 13 VAL H H 7.58 . 1 35 419 13 VAL C C 174.63 . 1 36 419 13 VAL CA C 63.25 . 1 37 419 13 VAL CB C 31.46 . 1 38 419 13 VAL N N 115.37 . 1 39 420 14 HIS H H 7.79 . 1 40 420 14 HIS C C 175.50 . 1 41 420 14 HIS CA C 56.08 . 1 42 420 14 HIS CB C 29.80 . 1 43 420 14 HIS N N 118.61 . 1 44 421 15 MET H H 7.38 . 1 45 421 15 MET C C 176.35 . 1 46 421 15 MET CA C 55.79 . 1 47 421 15 MET CB C 34.35 . 1 48 421 15 MET N N 119.20 . 1 49 422 16 ASP H H 8.47 . 1 50 422 16 ASP C C 174.80 . 1 51 422 16 ASP CA C 54.44 . 1 52 422 16 ASP CB C 41.58 . 1 53 422 16 ASP N N 120.06 . 1 54 423 17 MET H H 8.85 . 1 55 423 17 MET C C 176.81 . 1 56 423 17 MET CA C 59.53 . 1 57 423 17 MET CB C 33.45 . 1 58 423 17 MET N N 122.10 . 1 59 424 18 ALA H H 8.86 . 1 60 424 18 ALA C C 179.55 . 1 61 424 18 ALA CA C 55.89 . 1 62 424 18 ALA CB C 17.61 . 1 63 424 18 ALA N N 123.35 . 1 64 425 19 SER H H 7.96 . 1 65 425 19 SER C C 179.75 . 1 66 425 19 SER CA C 57.89 . 1 67 425 19 SER CB C 62.52 . 1 68 425 19 SER N N 115.90 . 1 69 426 20 VAL H H 7.70 . 1 70 426 20 VAL C C 177.35 . 1 71 426 20 VAL CA C 67.36 . 1 72 426 20 VAL CB C 32.10 . 1 73 426 20 VAL N N 124.20 . 1 74 427 21 THR H H 8.19 . 1 75 427 21 THR C C 177.25 . 1 76 427 21 THR CB C 67.48 . 1 77 427 21 THR N N 115.53 . 1 78 428 22 LYS H H 8.27 . 1 79 428 22 LYS C C 176.01 . 1 80 428 22 LYS CA C 59.82 . 1 81 428 22 LYS CB C 32.54 . 1 82 428 22 LYS N N 120.34 . 1 83 429 23 ALA H H 7.34 . 1 84 429 23 ALA C C 178.95 . 1 85 429 23 ALA CA C 54.67 . 1 86 429 23 ALA CB C 18.65 . 1 87 429 23 ALA N N 120.71 . 1 88 430 24 MET H H 7.60 . 1 89 430 24 MET C C 180.04 . 1 90 430 24 MET CA C 59.15 . 1 91 430 24 MET CB C 32.96 . 1 92 430 24 MET N N 119.80 . 1 93 431 25 ALA H H 7.37 . 1 94 431 25 ALA C C 176.39 . 1 95 431 25 ALA CA C 51.84 . 1 96 431 25 ALA CB C 17.88 . 1 97 431 25 ALA N N 118.33 . 1 98 432 26 ALA H H 6.88 . 1 99 432 26 ALA C C 177.11 . 1 100 432 26 ALA CA C 50.87 . 1 101 432 26 ALA CB C 17.52 . 1 102 432 26 ALA N N 123.87 . 1 103 433 27 PRO CA C 64.08 . 1 104 433 27 PRO CB C 31.71 . 1 105 434 28 GLU H H 8.74 . 1 106 434 28 GLU C C 178.12 . 1 107 434 28 GLU CA C 56.30 . 1 108 434 28 GLU CB C 27.51 . 1 109 434 28 GLU N N 115.62 . 1 110 435 29 SER H H 8.08 . 1 111 435 29 SER C C 177.45 . 1 112 435 29 SER CA C 59.81 . 1 113 435 29 SER CB C 64.50 . 1 114 435 29 SER N N 116.12 . 1 115 436 30 GLY H H 8.72 . 1 116 436 30 GLY C C 176.78 . 1 117 436 30 GLY CA C 44.93 . 1 118 436 30 GLY N N 111.95 . 1 119 437 31 LEU H H 7.91 . 1 120 437 31 LEU C C 174.20 . 1 121 437 31 LEU CA C 54.17 . 1 122 437 31 LEU CB C 41.74 . 1 123 437 31 LEU N N 124.41 . 1 124 438 32 GLU H H 8.93 . 1 125 438 32 GLU C C 175.82 . 1 126 438 32 GLU CA C 57.24 . 1 127 438 32 GLU CB C 29.80 . 1 128 438 32 GLU N N 130.21 . 1 129 439 33 VAL H H 8.22 . 1 130 439 33 VAL C C 174.57 . 1 131 439 33 VAL CA C 61.10 . 1 132 439 33 VAL CB C 33.56 . 1 133 439 33 VAL N N 128.25 . 1 134 440 34 ARG H H 8.91 . 1 135 440 34 ARG C C 175.71 . 1 136 440 34 ARG CA C 54.99 . 1 137 440 34 ARG CB C 33.20 . 1 138 440 34 ARG N N 121.97 . 1 139 441 35 ASP H H 8.77 . 1 140 441 35 ASP C C 174.98 . 1 141 441 35 ASP CA C 54.87 . 1 142 441 35 ASP CB C 39.94 . 1 143 441 35 ASP N N 123.89 . 1 144 442 36 ARG H H 8.77 . 1 145 442 36 ARG C C 176.40 . 1 146 442 36 ARG CA C 52.55 . 1 147 442 36 ARG CB C 32.72 . 1 148 442 36 ARG N N 121.39 . 1 149 443 37 MET H H 8.39 . 1 150 443 37 MET C C 174.77 . 1 151 443 37 MET CA C 54.69 . 1 152 443 37 MET CB C 33.43 . 1 153 443 37 MET N N 122.05 . 1 154 444 38 TRP H H 8.88 . 1 155 444 38 TRP C C 175.41 . 1 156 444 38 TRP CA C 56.40 . 1 157 444 38 TRP CB C 31.03 . 1 158 444 38 TRP N N 127.54 . 1 159 445 39 LEU H H 6.33 . 1 160 445 39 LEU C C 179.00 . 1 161 445 39 LEU CA C 53.49 . 1 162 445 39 LEU CB C 37.28 . 1 163 445 39 LEU N N 125.39 . 1 164 446 40 LYS H H 7.53 . 1 165 446 40 LYS C C 174.07 . 1 166 446 40 LYS CA C 55.46 . 1 167 446 40 LYS CB C 34.71 . 1 168 446 40 LYS N N 123.20 . 1 169 447 41 ILE H H 8.24 . 1 170 447 41 ILE C C 175.21 . 1 171 447 41 ILE CA C 62.15 . 1 172 447 41 ILE CB C 39.33 . 1 173 447 41 ILE N N 117.21 . 1 174 448 42 THR H H 7.73 . 1 175 448 42 THR C C 176.58 . 1 176 448 42 THR CA C 61.20 . 1 177 448 42 THR CB C 70.10 . 1 178 448 42 THR N N 113.13 . 1 179 450 44 PRO CA C 61.97 . 1 180 450 44 PRO CB C 32.27 . 1 181 451 45 ASN H H 8.65 . 1 182 451 45 ASN C C 177.15 . 1 183 451 45 ASN CA C 54.50 . 1 184 451 45 ASN CB C 38.07 . 1 185 451 45 ASN N N 115.80 . 1 186 452 46 ALA H H 7.61 . 1 187 452 46 ALA C C 171.70 . 1 188 452 46 ALA CA C 50.22 . 1 189 452 46 ALA CB C 22.91 . 1 190 452 46 ALA N N 119.14 . 1 191 453 47 PHE H H 8.49 . 1 192 453 47 PHE C C 178.10 . 1 193 453 47 PHE CA C 54.01 . 1 194 453 47 PHE CB C 40.63 . 1 195 453 47 PHE N N 116.60 . 1 196 454 48 LEU H H 9.50 . 1 197 454 48 LEU C C 174.41 . 1 198 454 48 LEU CA C 54.13 . 1 199 454 48 LEU CB C 44.75 . 1 200 454 48 LEU N N 124.06 . 1 201 455 49 GLY H H 9.25 . 1 202 455 49 GLY C C 179.56 . 1 203 455 49 GLY CA C 49.37 . 1 204 455 49 GLY N N 112.43 . 1 205 456 50 SER H H 8.97 . 1 206 456 50 SER C C 176.15 . 1 207 456 50 SER CA C 61.14 . 1 208 456 50 SER CB C 62.28 . 1 209 456 50 SER N N 117.53 . 1 210 457 51 ASP H H 6.89 . 1 211 457 51 ASP C C 176.08 . 1 212 457 51 ASP CA C 57.00 . 1 213 457 51 ASP CB C 39.93 . 1 214 457 51 ASP N N 120.58 . 1 215 458 52 VAL H H 7.97 . 1 216 458 52 VAL C C 179.62 . 1 217 458 52 VAL CA C 66.10 . 1 218 458 52 VAL CB C 31.57 . 1 219 458 52 VAL N N 122.42 . 1 220 459 53 VAL H H 7.81 . 1 221 459 53 VAL C C 176.75 . 1 222 459 53 VAL CA C 68.13 . 1 223 459 53 VAL CB C 31.71 . 1 224 459 53 VAL N N 119.91 . 1 225 460 54 ASP H H 8.30 . 1 226 460 54 ASP C C 177.47 . 1 227 460 54 ASP CA C 58.20 . 1 228 460 54 ASP CB C 40.77 . 1 229 460 54 ASP N N 117.92 . 1 230 461 55 TRP H H 8.66 . 1 231 461 55 TRP C C 178.11 . 1 232 461 55 TRP CA C 63.10 . 1 233 461 55 TRP CB C 29.78 . 1 234 461 55 TRP N N 121.54 . 1 235 462 56 LEU H H 8.96 . 1 236 462 56 LEU C C 180.38 . 1 237 462 56 LEU CA C 57.84 . 1 238 462 56 LEU CB C 42.87 . 1 239 462 56 LEU N N 120.81 . 1 240 463 57 TYR H H 8.37 . 1 241 463 57 TYR C C 177.48 . 1 242 463 57 TYR CA C 59.12 . 1 243 463 57 TYR CB C 38.38 . 1 244 463 57 TYR N N 115.81 . 1 245 464 58 HIS H H 7.85 . 1 246 464 58 HIS C C 177.30 . 1 247 464 58 HIS CA C 56.79 . 1 248 464 58 HIS CB C 30.12 . 1 249 464 58 HIS N N 111.64 . 1 250 465 59 HIS H H 7.97 . 1 251 465 59 HIS C C 176.15 . 1 252 465 59 HIS CA C 57.06 . 1 253 465 59 HIS CB C 28.86 . 1 254 465 59 HIS N N 113.31 . 1 255 466 60 VAL H H 7.83 . 1 256 466 60 VAL C C 173.10 . 1 257 466 60 VAL CA C 61.09 . 1 258 466 60 VAL CB C 31.77 . 1 259 466 60 VAL N N 120.99 . 1 260 467 61 GLU H H 8.16 . 1 261 467 61 GLU C C 174.00 . 1 262 467 61 GLU CA C 57.14 . 1 263 467 61 GLU CB C 30.25 . 1 264 467 61 GLU N N 127.60 . 1 265 468 62 GLY H H 8.45 . 1 266 468 62 GLY C C 176.82 . 1 267 468 62 GLY CA C 45.08 . 1 268 468 62 GLY N N 110.01 . 1 269 469 63 PHE H H 7.95 . 1 270 469 63 PHE C C 174.54 . 1 271 469 63 PHE CA C 54.45 . 1 272 469 63 PHE CB C 39.41 . 1 273 469 63 PHE N N 120.02 . 1 274 470 64 PRO CA C 64.32 . 1 275 470 64 PRO CB C 32.29 . 1 276 471 65 GLU H H 7.10 . 1 277 471 65 GLU C C 176.19 . 1 278 471 65 GLU CA C 54.07 . 1 279 471 65 GLU CB C 32.96 . 1 280 471 65 GLU N N 109.96 . 1 281 472 66 ARG CA C 59.79 . 1 282 472 66 ARG CB C 30.67 . 1 283 473 67 ARG H H 8.75 . 1 284 473 67 ARG C C 178.31 . 1 285 473 67 ARG CA C 59.49 . 1 286 473 67 ARG CB C 29.38 . 1 287 473 67 ARG N N 117.31 . 1 288 474 68 GLU H H 7.49 . 1 289 474 68 GLU C C 178.75 . 1 290 474 68 GLU CA C 58.73 . 1 291 474 68 GLU CB C 29.61 . 1 292 474 68 GLU N N 117.87 . 1 293 475 69 ALA H H 6.98 . 1 294 475 69 ALA C C 178.75 . 1 295 475 69 ALA CA C 54.10 . 1 296 475 69 ALA CB C 17.57 . 1 297 475 69 ALA N N 124.18 . 1 298 476 70 ARG H H 7.68 . 1 299 476 70 ARG C C 178.39 . 1 300 476 70 ARG CA C 59.26 . 1 301 476 70 ARG CB C 29.22 . 1 302 476 70 ARG N N 119.93 . 1 303 477 71 LYS H H 7.61 . 1 304 477 71 LYS C C 177.82 . 1 305 477 71 LYS CA C 59.39 . 1 306 477 71 LYS CB C 32.10 . 1 307 477 71 LYS N N 120.00 . 1 308 478 72 TYR H H 7.71 . 1 309 478 72 TYR C C 179.47 . 1 310 478 72 TYR CA C 61.35 . 1 311 478 72 TYR CB C 39.21 . 1 312 478 72 TYR N N 123.07 . 1 313 479 73 ALA H H 8.10 . 1 314 479 73 ALA C C 178.15 . 1 315 479 73 ALA CA C 55.30 . 1 316 479 73 ALA CB C 17.56 . 1 317 479 73 ALA N N 122.45 . 1 318 480 74 SER H H 7.58 . 1 319 480 74 SER C C 178.41 . 1 320 480 74 SER CA C 62.20 . 1 321 480 74 SER CB C 60.90 . 1 322 480 74 SER N N 111.50 . 1 323 481 75 GLY H H 7.84 . 1 324 481 75 GLY C C 176.75 . 1 325 481 75 GLY CA C 47.03 . 1 326 481 75 GLY N N 111.54 . 1 327 482 76 LEU H H 8.00 . 1 328 482 76 LEU C C 176.65 . 1 329 482 76 LEU CA C 57.67 . 1 330 482 76 LEU CB C 41.74 . 1 331 482 76 LEU N N 123.10 . 1 332 483 77 LEU H H 7.50 . 1 333 483 77 LEU C C 179.25 . 1 334 483 77 LEU CA C 56.92 . 1 335 483 77 LEU CB C 42.26 . 1 336 483 77 LEU N N 120.72 . 1 337 484 78 LYS H H 8.29 . 1 338 484 78 LYS C C 180.50 . 1 339 484 78 LYS CA C 59.26 . 1 340 484 78 LYS CB C 32.27 . 1 341 484 78 LYS N N 121.86 . 1 342 485 79 ALA H H 7.76 . 1 343 485 79 ALA C C 178.39 . 1 344 485 79 ALA CA C 52.28 . 1 345 485 79 ALA CB C 19.57 . 1 346 485 79 ALA N N 117.38 . 1 347 486 80 GLY H H 8.01 . 1 348 486 80 GLY C C 177.81 . 1 349 486 80 GLY CA C 45.36 . 1 350 486 80 GLY N N 106.97 . 1 351 487 81 LEU H H 8.00 . 1 352 487 81 LEU C C 174.56 . 1 353 487 81 LEU CA C 57.43 . 1 354 487 81 LEU CB C 42.15 . 1 355 487 81 LEU N N 121.80 . 1 356 488 82 ILE H H 7.28 . 1 357 488 82 ILE C C 178.79 . 1 358 488 82 ILE CA C 59.69 . 1 359 488 82 ILE CB C 41.00 . 1 360 488 82 ILE N N 108.87 . 1 361 489 83 ARG H H 9.22 . 1 362 489 83 ARG C C 174.00 . 1 363 489 83 ARG CA C 54.55 . 1 364 489 83 ARG CB C 33.94 . 1 365 489 83 ARG N N 117.44 . 1 366 490 84 HIS H H 8.71 . 1 367 490 84 HIS C C 175.52 . 1 368 490 84 HIS CA C 57.49 . 1 369 490 84 HIS CB C 32.99 . 1 370 490 84 HIS N N 120.98 . 1 371 491 85 THR H H 8.82 . 1 372 491 85 THR C C 176.68 . 1 373 491 85 THR CA C 61.86 . 1 374 491 85 THR CB C 69.08 . 1 375 491 85 THR N N 110.98 . 1 376 492 86 VAL H H 7.73 . 1 377 492 86 VAL C C 174.89 . 1 378 492 86 VAL CA C 60.07 . 1 379 492 86 VAL CB C 33.39 . 1 380 492 86 VAL N N 116.71 . 1 381 493 87 ASN H H 8.30 . 1 382 493 87 ASN C C 175.61 . 1 383 493 87 ASN CA C 56.37 . 1 384 493 87 ASN CB C 38.39 . 1 385 493 87 ASN N N 118.54 . 1 386 494 88 LYS H H 8.07 . 1 387 494 88 LYS C C 176.61 . 1 388 494 88 LYS CA C 56.92 . 1 389 494 88 LYS CB C 31.42 . 1 390 494 88 LYS N N 114.57 . 1 391 495 89 ILE H H 8.27 . 1 392 495 89 ILE C C 176.05 . 1 393 495 89 ILE CA C 59.98 . 1 394 495 89 ILE CB C 40.20 . 1 395 495 89 ILE N N 121.08 . 1 396 496 90 THR H H 8.32 . 1 397 496 90 THR C C 175.19 . 1 398 496 90 THR CA C 62.27 . 1 399 496 90 THR CB C 69.38 . 1 400 496 90 THR N N 120.59 . 1 401 497 91 PHE H H 9.20 . 1 402 497 91 PHE C C 174.06 . 1 403 497 91 PHE CA C 57.48 . 1 404 497 91 PHE CB C 39.22 . 1 405 497 91 PHE N N 130.03 . 1 406 500 94 GLN H H 7.88 . 1 407 500 94 GLN C C 175.80 . 1 408 500 94 GLN CA C 56.22 . 1 409 500 94 GLN CB C 28.63 . 1 410 500 94 GLN N N 114.72 . 1 411 501 95 CYS H H 6.58 . 1 412 501 95 CYS C C 175.52 . 1 413 501 95 CYS CA C 58.13 . 1 414 501 95 CYS CB C 29.48 . 1 415 501 95 CYS N N 115.40 . 1 416 502 96 TYR H H 7.90 . 1 417 502 96 TYR C C 171.50 . 1 418 502 96 TYR CA C 56.47 . 1 419 502 96 TYR CB C 40.16 . 1 420 502 96 TYR N N 117.34 . 1 421 503 97 TYR H H 9.15 . 1 422 503 97 TYR C C 175.45 . 1 423 503 97 TYR CA C 56.71 . 1 424 503 97 TYR CB C 43.64 . 1 425 503 97 TYR N N 122.90 . 1 426 504 98 VAL H H 7.96 . 1 427 504 98 VAL C C 172.20 . 1 428 504 98 VAL CA C 58.55 . 1 429 504 98 VAL CB C 35.25 . 1 430 504 98 VAL N N 106.72 . 1 431 505 99 PHE H H 8.88 . 1 432 505 99 PHE C C 176.75 . 1 433 505 99 PHE CA C 61.15 . 1 434 505 99 PHE CB C 40.03 . 1 435 505 99 PHE N N 118.92 . 1 436 506 100 GLY H H 8.15 . 1 437 506 100 GLY C C 177.72 . 1 438 506 100 GLY CA C 43.60 . 1 439 506 100 GLY N N 107.93 . 1 440 507 101 ASP H H 8.13 . 1 441 507 101 ASP C C 172.25 . 1 442 507 101 ASP CA C 54.33 . 1 443 507 101 ASP CB C 40.58 . 1 444 507 101 ASP N N 119.60 . 1 445 508 102 LEU H H 8.40 . 1 446 508 102 LEU C C 176.50 . 1 447 508 102 LEU CA C 54.33 . 1 448 508 102 LEU CB C 41.19 . 1 449 508 102 LEU N N 125.84 . 1 450 509 103 SER H H 8.25 . 1 451 509 103 SER C C 177.40 . 1 452 509 103 SER CA C 58.99 . 1 453 509 103 SER CB C 63.91 . 1 454 509 103 SER N N 116.17 . 1 455 510 104 GLY H H 8.06 . 1 456 510 104 GLY C C 174.22 . 1 457 510 104 GLY CA C 46.15 . 1 458 510 104 GLY N N 116.60 . 1 stop_ save_