data_5317 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the DNA binding domain of human TRF1 ; _BMRB_accession_number 5317 _BMRB_flat_file_name bmr5317.str _Entry_type original _Submission_date 2002-03-12 _Accession_date 2002-03-12 _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 Nishikawa T. . . 2 Okamura H. . . 3 Nagadoi A. . . 4 Konig P. . . 5 Rhodes D. . . 6 Nishimura Y. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 409 "13C chemical shifts" 196 "15N chemical shifts" 78 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-04-08 original author . stop_ _Original_release_date 2002-04-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution structure of a telomeric DNA complex of human TRF1' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11738049 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nishikawa T. . . 2 Okamura H. . . 3 Nagadoi A. . . 4 Konig P. . . 5 Rhodes D. . . 6 Nishimura Y. . . stop_ _Journal_abbreviation Structure _Journal_volume 9 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1237 _Page_last 1251 _Year 2001 _Details . loop_ _Keyword helix-turn-helix telomeres 'DNA binding' 'Myb domain' stop_ save_ ################################## # Molecular system description # ################################## save_system_TRF _Saveframe_category molecular_system _Mol_system_name 'Telomeric repeat binding factor 1' _Abbreviation_common TRF1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label TRF1 $TRF1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TRF1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TRF1 _Abbreviation_common TRF1 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 69 _Mol_residue_sequence ; TPEKHRARKRQAWLWEEDKN LRSGVRKYGEGNWSKILLHY KFNNRTSVMLKDRWRTMKKL KLISSDSED ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 371 THR 2 372 PRO 3 373 GLU 4 374 LYS 5 375 HIS 6 376 ARG 7 377 ALA 8 378 ARG 9 379 LYS 10 380 ARG 11 381 GLN 12 382 ALA 13 383 TRP 14 384 LEU 15 385 TRP 16 386 GLU 17 387 GLU 18 388 ASP 19 389 LYS 20 390 ASN 21 391 LEU 22 392 ARG 23 393 SER 24 394 GLY 25 395 VAL 26 396 ARG 27 397 LYS 28 398 TYR 29 399 GLY 30 400 GLU 31 401 GLY 32 402 ASN 33 403 TRP 34 404 SER 35 405 LYS 36 406 ILE 37 407 LEU 38 408 LEU 39 409 HIS 40 410 TYR 41 411 LYS 42 412 PHE 43 413 ASN 44 414 ASN 45 415 ARG 46 416 THR 47 417 SER 48 418 VAL 49 419 MET 50 420 LEU 51 421 LYS 52 422 ASP 53 423 ARG 54 424 TRP 55 425 ARG 56 426 THR 57 427 MET 58 428 LYS 59 429 LYS 60 430 LEU 61 431 LYS 62 432 LEU 63 433 ILE 64 434 SER 65 435 SER 66 436 ASP 67 437 SER 68 438 GLU 69 439 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 4210 hTRF1 76.81 53 100.00 100.00 7.07e-29 BMRB 5361 "Telomeric repeat binding factor 1" 100.00 70 100.00 100.00 2.64e-41 PDB 1BA5 "Dna-Binding Domain Of Human Telomeric Protein, Htrf1, Nmr, 18 Structures" 76.81 53 100.00 100.00 7.07e-29 PDB 1ITY "Solution Structure Of The Dna Binding Domain Of Human Trf1" 100.00 69 100.00 100.00 2.84e-41 PDB 1IV6 "Solution Structure Of The Dna Complex Of Human Trf1" 100.00 70 100.00 100.00 2.64e-41 PDB 1W0T "Htrf1 Dna-Binding Domain In Complex With Telomeric Dna" 76.81 53 100.00 100.00 8.41e-29 DBJ BAE88046 "unnamed protein product [Macaca fascicularis]" 100.00 282 97.10 98.55 6.06e-40 DBJ BAF85218 "unnamed protein product [Homo sapiens]" 100.00 439 100.00 100.00 2.24e-40 EMBL CAA63768 "telomeric DNA binding protein [Homo sapiens]" 100.00 111 100.00 100.00 3.89e-42 EMBL CAH92488 "hypothetical protein [Pongo abelii]" 100.00 436 98.55 98.55 9.30e-40 GB AAB53363 "telomeric repeat DNA-binding protein [Homo sapiens]" 100.00 419 100.00 100.00 2.30e-40 GB AAB54036 "telomeric repeat binding factor [Homo sapiens]" 100.00 439 100.00 100.00 2.24e-40 GB AAB81137 "TTAGGG repeat binding factor 1 [Homo sapiens]" 100.00 419 100.00 100.00 2.30e-40 GB AAC02531 "telomeric repeat binding factor 1 [Cricetulus griseus]" 98.55 438 100.00 100.00 1.84e-39 GB AAH29378 "Telomeric repeat binding factor (NIMA-interacting) 1 [Homo sapiens]" 100.00 419 100.00 100.00 2.25e-40 REF NP_001126467 "telomeric repeat-binding factor 1 [Pongo abelii]" 100.00 436 98.55 98.55 9.30e-40 REF NP_003209 "telomeric repeat-binding factor 1 isoform 2 [Homo sapiens]" 100.00 419 100.00 100.00 2.25e-40 REF NP_059523 "telomeric repeat-binding factor 1 isoform 1 [Homo sapiens]" 100.00 439 100.00 100.00 2.31e-40 REF XP_001083645 "PREDICTED: telomeric repeat-binding factor 1 isoform 1 [Macaca mulatta]" 100.00 438 97.10 98.55 2.42e-39 REF XP_001164723 "PREDICTED: telomeric repeat-binding factor 1 isoform X1 [Pan troglodytes]" 100.00 439 98.55 98.55 7.09e-40 SP O55036 "RecName: Full=Telomeric repeat-binding factor 1; AltName: Full=TTAGGG repeat-binding factor 1, partial [Cricetulus griseus]" 98.55 438 100.00 100.00 1.84e-39 SP P54274 "RecName: Full=Telomeric repeat-binding factor 1; AltName: Full=NIMA-interacting protein 2; AltName: Full=TTAGGG repeat-binding " 100.00 439 100.00 100.00 2.31e-40 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TRF1 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 $TRF1 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3)PLYSS pET13A 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_min_value _Concentration_max_value _Isotopic_labeling $TRF1 . mM 1.5 2.5 '[U-15N; U-13C]' 'phosphate buffer' 50 mM . . . NaCl 100 mM . . . H2O 90 % . . . D2O 10 % . . . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $TRF1 . mM 1.5 2.5 '[U-15N; U-13C]' 'phosphate buffer' 50 mM . . . NaCl 100 mM . . . D2O 100 % . . . stop_ save_ ############################ # Computer software used # ############################ save_EMBOSS _Saveframe_category software _Name EMBOSS _Version 5.0 loop_ _Task refinement stop_ _Details 'Nakai, T., Kidera, A., and Nakamura, H.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNHA_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label . save_ save_3D_HNHB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _Sample_label . save_ save_3D_Sequential_assignment_protocol_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D Sequential assignment protocol' _Sample_label . save_ save_3D_15N-separated_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_3D_13C-separated_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _Sample_label . save_ save_2D_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_2D_TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_2D_DQF-COSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D Sequential assignment protocol' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 . n/a temperature 300 . K pressure 1 . atm 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 . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.1013291 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.2514495 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name TRF1 _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 . 3 GLU N N 121.1 . 1 2 . 3 GLU H H 8.57 . 1 3 . 3 GLU C C 174.6 . 1 4 . 3 GLU CA C 55.2 . 1 5 . 3 GLU HA H 4.13 . 1 6 . 3 GLU CB C 28.2 . 1 7 . 3 GLU HB2 H 1.92 . 1 8 . 3 GLU HB3 H 1.92 . 1 9 . 4 LYS N N 121.8 . 1 10 . 4 LYS H H 8.27 . 1 11 . 4 LYS C C 173.6 . 1 12 . 4 LYS CA C 54.9 . 1 13 . 4 LYS HA H 4.17 . 1 14 . 4 LYS CB C 30.9 . 1 15 . 4 LYS HB2 H 1.71 . 1 16 . 4 LYS HB3 H 1.71 . 1 17 . 5 HIS N N 119.8 . 1 18 . 5 HIS H H 8.28 . 1 19 . 5 HIS C C 173.3 . 1 20 . 5 HIS CA C 54.6 . 1 21 . 5 HIS HA H 4.57 . 1 22 . 5 HIS CB C 28.6 . 1 23 . 5 HIS HB2 H 3.09 . 1 24 . 5 HIS HB3 H 3.09 . 1 25 . 6 ARG N N 122.0 . 1 26 . 6 ARG H H 8.24 . 1 27 . 6 ARG C C 173.8 . 1 28 . 6 ARG CA C 54.5 . 1 29 . 6 ARG HA H 4.17 . 1 30 . 6 ARG CB C 28.8 . 1 31 . 6 ARG HB2 H 1.76 . 1 32 . 6 ARG HB3 H 1.76 . 1 33 . 7 ALA N N 124.6 . 1 34 . 7 ALA H H 8.28 . 1 35 . 7 ALA C C 175.6 . 1 36 . 7 ALA CA C 50.7 . 1 37 . 7 ALA HA H 4.24 . 1 38 . 7 ALA CB C 17.2 . 1 39 . 7 ALA HB H 1.36 . 1 40 . 8 ARG N N 120.3 . 1 41 . 8 ARG H H 8.24 . 1 42 . 8 ARG C C 174.2 . 1 43 . 8 ARG CA C 54.2 . 1 44 . 8 ARG HA H 4.26 . 1 45 . 8 ARG CB C 28.9 . 1 46 . 8 ARG HB2 H 1.78 . 1 47 . 8 ARG HB3 H 1.78 . 1 48 . 9 LYS N N 122.5 . 1 49 . 9 LYS H H 8.34 . 1 50 . 9 LYS C C 174.3 . 1 51 . 9 LYS CA C 54.6 . 1 52 . 9 LYS HA H 4.25 . 1 53 . 9 LYS CB C 31.1 . 1 54 . 9 LYS HB2 H 1.77 . 1 55 . 9 LYS HB3 H 1.77 . 1 56 . 10 ARG N N 122.3 . 1 57 . 10 ARG H H 8.40 . 1 58 . 10 ARG C C 173.7 . 1 59 . 10 ARG CA C 54.2 . 1 60 . 10 ARG HA H 4.28 . 1 61 . 10 ARG CB C 28.8 . 1 62 . 10 ARG HB2 H 1.79 . 1 63 . 10 ARG HB3 H 1.79 . 1 64 . 11 GLN N N 122.0 . 1 65 . 11 GLN H H 8.51 . 1 66 . 11 GLN C C 173.8 . 1 67 . 11 GLN CA C 53.6 . 1 68 . 11 GLN HA H 4.30 . 1 69 . 11 GLN CB C 27.5 . 1 70 . 11 GLN HB2 H 1.98 . 1 71 . 11 GLN HB3 H 1.98 . 1 72 . 11 GLN HG2 H 2.33 . 1 73 . 11 GLN HG3 H 2.33 . 1 74 . 11 GLN HE21 H 6.89 . 2 75 . 11 GLN HE22 H 7.55 . 2 76 . 11 GLN NE2 N 112.4 . 1 77 . 12 ALA N N 127.5 . 1 78 . 12 ALA H H 8.41 . 1 79 . 12 ALA C C 175.3 . 1 80 . 12 ALA CA C 50.8 . 1 81 . 12 ALA HA H 4.34 . 1 82 . 12 ALA CB C 17.3 . 1 83 . 12 ALA HB H 1.42 . 1 84 . 13 TRP N N 122.8 . 1 85 . 13 TRP H H 8.66 . 1 86 . 13 TRP C C 175.2 . 1 87 . 13 TRP CA C 56.1 . 1 88 . 13 TRP HA H 4.16 . 1 89 . 13 TRP CB C 26.6 . 1 90 . 13 TRP HB2 H 2.95 . 1 91 . 13 TRP HB3 H 3.28 . 1 92 . 13 TRP HD1 H 7.27 . 1 93 . 13 TRP HE1 H 9.92 . 1 94 . 13 TRP HE3 H 7.73 . 1 95 . 13 TRP HZ2 H 7.02 . 1 96 . 13 TRP HZ3 H 6.93 . 1 97 . 13 TRP HH2 H 6.60 . 1 98 . 13 TRP NE1 N 128.4 . 1 99 . 14 LEU N N 127.0 . 1 100 . 14 LEU H H 9.13 . 1 101 . 14 LEU C C 176.5 . 1 102 . 14 LEU CA C 52.1 . 1 103 . 14 LEU HA H 4.67 . 1 104 . 14 LEU CB C 41.0 . 1 105 . 14 LEU HB2 H 1.78 . 2 106 . 14 LEU HB3 H 1.98 . 2 107 . 14 LEU HG H 1.81 . 1 108 . 14 LEU HD1 H 0.91 . 1 109 . 14 LEU HD2 H 0.91 . 1 110 . 15 TRP N N 124.3 . 1 111 . 15 TRP H H 9.07 . 1 112 . 15 TRP C C 176.5 . 1 113 . 15 TRP CA C 59.4 . 1 114 . 15 TRP HA H 4.47 . 1 115 . 15 TRP CB C 26.7 . 1 116 . 15 TRP HB2 H 3.31 . 2 117 . 15 TRP HB3 H 3.55 . 2 118 . 15 TRP HD1 H 7.38 . 1 119 . 15 TRP HE1 H 10.22 . 1 120 . 15 TRP HE3 H 7.58 . 1 121 . 15 TRP HZ2 H 7.48 . 1 122 . 15 TRP HZ3 H 7.50 . 1 123 . 15 TRP HH2 H 7.20 . 1 124 . 15 TRP NE1 N 129.4 . 1 125 . 16 GLU N N 117.1 . 1 126 . 16 GLU H H 8.94 . 1 127 . 16 GLU C C 176.3 . 1 128 . 16 GLU CA C 57.9 . 1 129 . 16 GLU HA H 3.58 . 1 130 . 16 GLU CB C 27.6 . 1 131 . 16 GLU HB2 H 1.82 . 1 132 . 16 GLU HB3 H 1.82 . 1 133 . 16 GLU HG2 H 1.97 . 2 134 . 16 GLU HG3 H 2.16 . 2 135 . 17 GLU N N 116.8 . 1 136 . 17 GLU H H 7.13 . 1 137 . 17 GLU C C 176.3 . 1 138 . 17 GLU CA C 58.2 . 1 139 . 17 GLU HA H 3.99 . 1 140 . 17 GLU CB C 30.5 . 1 141 . 17 GLU HB2 H 2.69 . 1 142 . 17 GLU HB3 H 2.90 . 1 143 . 17 GLU HG2 H 2.14 . 2 144 . 17 GLU HG3 H 2.46 . 2 145 . 18 ASP N N 121.4 . 1 146 . 18 ASP H H 7.95 . 1 147 . 18 ASP C C 176.8 . 1 148 . 18 ASP CA C 55.7 . 1 149 . 18 ASP HA H 4.57 . 1 150 . 18 ASP CB C 38.3 . 1 151 . 18 ASP HB2 H 2.47 . 1 152 . 18 ASP HB3 H 2.76 . 1 153 . 19 LYS N N 120.0 . 1 154 . 19 LYS H H 8.15 . 1 155 . 19 LYS C C 176.5 . 1 156 . 19 LYS CA C 57.6 . 1 157 . 19 LYS HA H 3.76 . 1 158 . 19 LYS CB C 29.9 . 1 159 . 19 LYS HB2 H 1.30 . 2 160 . 19 LYS HB3 H 1.56 . 2 161 . 19 LYS HG2 H 1.17 . 1 162 . 19 LYS HG3 H 1.17 . 1 163 . 20 ASN N N 119.9 . 1 164 . 20 ASN H H 7.96 . 1 165 . 20 ASN C C 174.4 . 1 166 . 20 ASN CA C 53.2 . 1 167 . 20 ASN HA H 4.10 . 1 168 . 20 ASN CB C 35.8 . 1 169 . 20 ASN HB2 H 1.99 . 2 170 . 20 ASN HB3 H 2.67 . 2 171 . 20 ASN HD21 H 6.91 . 2 172 . 20 ASN HD22 H 7.19 . 2 173 . 20 ASN ND2 N 110.6 . 1 174 . 21 LEU N N 122.5 . 1 175 . 21 LEU H H 8.74 . 1 176 . 21 LEU C C 175.3 . 1 177 . 21 LEU CA C 56.8 . 1 178 . 21 LEU HA H 4.16 . 1 179 . 21 LEU CB C 40.7 . 1 180 . 21 LEU HB2 H 1.93 . 1 181 . 21 LEU HB3 H 2.36 . 1 182 . 21 LEU HG H 1.91 . 1 183 . 21 LEU HD1 H 1.01 . 1 184 . 21 LEU HD2 H 1.08 . 1 185 . 22 ARG N N 117.2 . 1 186 . 22 ARG H H 8.21 . 1 187 . 22 ARG C C 177.5 . 1 188 . 22 ARG CA C 58.5 . 1 189 . 22 ARG HA H 4.03 . 1 190 . 22 ARG CB C 28.6 . 1 191 . 22 ARG HB2 H 2.00 . 1 192 . 22 ARG HB3 H 2.00 . 1 193 . 22 ARG HG2 H 1.75 . 1 194 . 22 ARG HG3 H 1.75 . 1 195 . 22 ARG HD2 H 3.22 . 2 196 . 22 ARG HD3 H 3.33 . 2 197 . 23 SER N N 116.0 . 1 198 . 23 SER H H 8.52 . 1 199 . 23 SER C C 174.3 . 1 200 . 23 SER CA C 60.6 . 1 201 . 23 SER HA H 4.07 . 1 202 . 23 SER CB C 70.0 . 1 203 . 23 SER HB2 H 3.80 . 2 204 . 23 SER HB3 H 3.88 . 2 205 . 24 GLY N N 110.8 . 1 206 . 24 GLY H H 8.62 . 1 207 . 24 GLY C C 172.9 . 1 208 . 24 GLY CA C 46.1 . 1 209 . 24 GLY HA2 H 3.53 . 2 210 . 24 GLY HA3 H 4.00 . 2 211 . 25 VAL N N 123.7 . 1 212 . 25 VAL H H 8.51 . 1 213 . 25 VAL C C 176.8 . 1 214 . 25 VAL CA C 64.4 . 1 215 . 25 VAL HA H 3.05 . 1 216 . 25 VAL CB C 28.6 . 1 217 . 25 VAL HB H 1.30 . 1 218 . 25 VAL HG1 H -0.20 . 1 219 . 25 VAL HG2 H 0.30 . 1 220 . 26 ARG N N 120.1 . 1 221 . 26 ARG H H 7.59 . 1 222 . 26 ARG C C 175.1 . 1 223 . 26 ARG CA C 57.4 . 1 224 . 26 ARG HA H 3.89 . 1 225 . 26 ARG CB C 27.8 . 1 226 . 26 ARG HB2 H 1.91 . 1 227 . 26 ARG HB3 H 1.91 . 1 228 . 26 ARG HG2 H 1.66 . 1 229 . 26 ARG HG3 H 1.66 . 1 230 . 26 ARG HD2 H 3.20 . 1 231 . 26 ARG HD3 H 3.20 . 1 232 . 27 LYS N N 117.0 . 1 233 . 27 LYS H H 7.70 . 1 234 . 27 LYS C C 175.5 . 1 235 . 27 LYS CA C 56.9 . 1 236 . 27 LYS HA H 3.89 . 1 237 . 27 LYS CB C 31.8 . 1 238 . 27 LYS HB2 H 1.31 . 2 239 . 27 LYS HB3 H 1.50 . 2 240 . 27 LYS HG2 H 0.21 . 2 241 . 27 LYS HG3 H 0.74 . 2 242 . 27 LYS HD2 H 1.30 . 1 243 . 27 LYS HD3 H 1.30 . 1 244 . 28 TYR N N 113.9 . 1 245 . 28 TYR H H 8.73 . 1 246 . 28 TYR C C 174.3 . 1 247 . 28 TYR CA C 56.7 . 1 248 . 28 TYR HA H 4.57 . 1 249 . 28 TYR CB C 37.4 . 1 250 . 28 TYR HB2 H 2.60 . 2 251 . 28 TYR HB3 H 3.05 . 2 252 . 28 TYR HD1 H 6.58 . 1 253 . 28 TYR HD2 H 6.58 . 1 254 . 28 TYR HE1 H 7.15 . 1 255 . 28 TYR HE2 H 7.15 . 1 256 . 29 GLY N N 110.5 . 1 257 . 29 GLY H H 7.90 . 1 258 . 29 GLY C C 170.7 . 1 259 . 29 GLY CA C 42.3 . 1 260 . 29 GLY HA2 H 3.69 . 2 261 . 29 GLY HA3 H 4.20 . 2 262 . 30 GLU N N 120.0 . 1 263 . 30 GLU H H 8.37 . 1 264 . 30 GLU C C 173.7 . 1 265 . 30 GLU CA C 55.6 . 1 266 . 30 GLU HA H 2.96 . 1 267 . 30 GLU CB C 27.7 . 1 268 . 30 GLU HB2 H 2.10 . 2 269 . 30 GLU HB3 H 2.19 . 2 270 . 31 GLY N N 108.6 . 1 271 . 31 GLY H H 5.33 . 1 272 . 31 GLY C C 171.5 . 1 273 . 31 GLY CA C 43.1 . 1 274 . 31 GLY HA2 H 3.41 . 2 275 . 31 GLY HA3 H 4.10 . 2 276 . 32 ASN N N 121.4 . 1 277 . 32 ASN H H 7.09 . 1 278 . 32 ASN C C 173.3 . 1 279 . 32 ASN CA C 49.7 . 1 280 . 32 ASN HA H 5.01 . 1 281 . 32 ASN CB C 35.2 . 1 282 . 32 ASN HB2 H 2.13 . 2 283 . 32 ASN HB3 H 2.61 . 2 284 . 32 ASN HD21 H 6.95 . 2 285 . 32 ASN HD22 H 7.65 . 2 286 . 32 ASN ND2 N 114.0 . 1 287 . 33 TRP N N 117.8 . 1 288 . 33 TRP H H 6.60 . 1 289 . 33 TRP C C 175.6 . 1 290 . 33 TRP CA C 56.6 . 1 291 . 33 TRP HA H 4.16 . 1 292 . 33 TRP CB C 28.4 . 1 293 . 33 TRP HB2 H 3.11 . 1 294 . 33 TRP HB3 H 3.47 . 1 295 . 33 TRP HD1 H 7.43 . 1 296 . 33 TRP HE1 H 10.83 . 1 297 . 33 TRP HE3 H 7.16 . 1 298 . 33 TRP HZ2 H 7.70 . 1 299 . 33 TRP HZ3 H 6.38 . 1 300 . 33 TRP HH2 H 6.73 . 1 301 . 33 TRP NE1 N 130.6 . 1 302 . 34 SER N N 112.8 . 1 303 . 34 SER H H 8.71 . 1 304 . 34 SER C C 174.0 . 1 305 . 34 SER CA C 56.5 . 1 306 . 34 SER HA H 3.92 . 1 307 . 34 SER CB C 60.2 . 1 308 . 34 SER HB2 H 4.17 . 1 309 . 34 SER HB3 H 4.17 . 1 310 . 35 LYS N N 121.5 . 1 311 . 35 LYS H H 7.26 . 1 312 . 35 LYS C C 176.3 . 1 313 . 35 LYS CA C 57.0 . 1 314 . 35 LYS HA H 3.90 . 1 315 . 35 LYS CB C 30.4 . 1 316 . 35 LYS HB2 H 1.09 . 2 317 . 35 LYS HB3 H 1.43 . 2 318 . 35 LYS HG2 H 1.53 . 1 319 . 35 LYS HG3 H 1.53 . 1 320 . 35 LYS HE2 H 2.71 . 1 321 . 35 LYS HE3 H 2.71 . 1 322 . 36 ILE N N 119.4 . 1 323 . 36 ILE H H 7.44 . 1 324 . 36 ILE C C 175.2 . 1 325 . 36 ILE CA C 64.9 . 1 326 . 36 ILE HA H 3.68 . 1 327 . 36 ILE CB C 36.6 . 1 328 . 36 ILE HB H 1.91 . 1 329 . 36 ILE HG12 H 0.76 . 1 330 . 36 ILE HG13 H 1.82 . 1 331 . 36 ILE HG2 H 1.23 . 1 332 . 36 ILE HD1 H 0.54 . 1 333 . 37 LEU N N 118.2 . 1 334 . 37 LEU H H 7.96 . 1 335 . 37 LEU C C 175.0 . 1 336 . 37 LEU CA C 55.7 . 1 337 . 37 LEU HA H 4.25 . 1 338 . 37 LEU CB C 41.0 . 1 339 . 37 LEU HB2 H 1.59 . 1 340 . 37 LEU HB3 H 1.83 . 1 341 . 37 LEU HG H 1.69 . 1 342 . 37 LEU HD1 H 1.75 . 1 343 . 37 LEU HD2 H 1.75 . 1 344 . 38 LEU N N 113.6 . 1 345 . 38 LEU H H 7.21 . 1 346 . 38 LEU C C 176.5 . 1 347 . 38 LEU CA C 54.2 . 1 348 . 38 LEU HA H 4.21 . 1 349 . 38 LEU CB C 40.9 . 1 350 . 38 LEU HB2 H 1.38 . 1 351 . 38 LEU HB3 H 1.58 . 1 352 . 38 LEU HG H 1.53 . 1 353 . 38 LEU HD1 H 0.77 . 1 354 . 38 LEU HD2 H 0.77 . 1 355 . 39 HIS N N 115.3 . 1 356 . 39 HIS H H 7.64 . 1 357 . 39 HIS C C 171.5 . 1 358 . 39 HIS CA C 55.9 . 1 359 . 39 HIS HA H 4.40 . 1 360 . 39 HIS CB C 30.0 . 1 361 . 39 HIS HB2 H 2.83 . 1 362 . 39 HIS HB3 H 3.09 . 1 363 . 39 HIS HD2 H 6.50 . 1 364 . 39 HIS HE1 H 7.93 . 1 365 . 40 TYR N N 116.8 . 1 366 . 40 TYR H H 7.87 . 1 367 . 40 TYR C C 171.2 . 1 368 . 40 TYR CA C 54.7 . 1 369 . 40 TYR HA H 3.58 . 1 370 . 40 TYR CB C 39.7 . 1 371 . 40 TYR HB2 H 2.47 . 2 372 . 40 TYR HB3 H 2.82 . 2 373 . 40 TYR HD1 H 7.40 . 1 374 . 40 TYR HD2 H 7.40 . 1 375 . 40 TYR HE1 H 6.74 . 1 376 . 40 TYR HE2 H 6.74 . 1 377 . 41 LYS N N 119.2 . 1 378 . 41 LYS H H 7.86 . 1 379 . 41 LYS C C 173.3 . 1 380 . 41 LYS CA C 54.4 . 1 381 . 41 LYS HA H 4.33 . 1 382 . 41 LYS CB C 30.8 . 1 383 . 41 LYS HB2 H 1.56 . 1 384 . 41 LYS HB3 H 1.56 . 1 385 . 41 LYS HG2 H 1.19 . 4 386 . 41 LYS HG3 H 1.32 . 4 387 . 41 LYS HD2 H 1.62 . 4 388 . 41 LYS HD3 H 1.62 . 4 389 . 41 LYS HE2 H 2.92 . 1 390 . 41 LYS HE3 H 2.92 . 1 391 . 42 PHE N N 123.0 . 1 392 . 42 PHE H H 8.45 . 1 393 . 42 PHE C C 172.4 . 1 394 . 42 PHE CA C 55.2 . 1 395 . 42 PHE HA H 4.66 . 1 396 . 42 PHE CB C 40.0 . 1 397 . 42 PHE HB2 H 2.89 . 1 398 . 42 PHE HB3 H 3.05 . 1 399 . 42 PHE HD1 H 7.46 . 1 400 . 42 PHE HD2 H 7.46 . 1 401 . 42 PHE HE1 H 7.66 . 1 402 . 42 PHE HE2 H 7.66 . 1 403 . 42 PHE HZ H 6.66 . 1 404 . 43 ASN N N 121.7 . 1 405 . 43 ASN H H 9.42 . 1 406 . 43 ASN C C 171.2 . 1 407 . 43 ASN CA C 49.9 . 1 408 . 43 ASN HA H 4.75 . 1 409 . 43 ASN CB C 35.2 . 1 410 . 43 ASN HB2 H 2.54 . 2 411 . 43 ASN HB3 H 2.72 . 2 412 . 43 ASN HD21 H 6.77 . 2 413 . 43 ASN HD22 H 7.32 . 2 414 . 43 ASN ND2 N 111.5 . 1 415 . 44 ASN N N 120.6 . 1 416 . 44 ASN H H 8.43 . 1 417 . 44 ASN C C 172.2 . 1 418 . 44 ASN CA C 52.2 . 1 419 . 44 ASN HA H 4.27 . 1 420 . 44 ASN CB C 35.3 . 1 421 . 44 ASN HB2 H 2.57 . 2 422 . 44 ASN HB3 H 2.89 . 2 423 . 44 ASN HD21 H 6.84 . 2 424 . 44 ASN HD22 H 7.50 . 2 425 . 44 ASN ND2 N 113.0 . 1 426 . 45 ARG N N 113.9 . 1 427 . 45 ARG H H 8.03 . 1 428 . 45 ARG C C 173.4 . 1 429 . 45 ARG CA C 50.3 . 1 430 . 45 ARG HA H 5.50 . 1 431 . 45 ARG CB C 29.6 . 1 432 . 45 ARG HB2 H 1.45 . 1 433 . 45 ARG HB3 H 1.45 . 1 434 . 45 ARG HG2 H 1.24 . 1 435 . 45 ARG HG3 H 1.24 . 1 436 . 45 ARG HD2 H 2.33 . 2 437 . 45 ARG HD3 H 2.72 . 2 438 . 45 ARG HE H 8.02 . 1 439 . 45 ARG NE N 85.9 . 1 440 . 46 THR N N 108.4 . 1 441 . 46 THR H H 7.08 . 1 442 . 46 THR C C 173.7 . 1 443 . 46 THR CA C 57.2 . 1 444 . 46 THR HA H 4.67 . 1 445 . 46 THR CB C 69.7 . 1 446 . 46 THR HB H 4.67 . 1 447 . 46 THR HG2 H 1.22 . 1 448 . 47 SER N N 117.3 . 1 449 . 47 SER H H 9.26 . 1 450 . 47 SER C C 173.7 . 1 451 . 47 SER CA C 60.2 . 1 452 . 47 SER HA H 3.76 . 1 453 . 47 SER HB2 H 3.90 . 1 454 . 47 SER HB3 H 3.90 . 1 455 . 48 VAL N N 119.5 . 1 456 . 48 VAL H H 7.47 . 1 457 . 48 VAL C C 174.6 . 1 458 . 48 VAL CA C 63.3 . 1 459 . 48 VAL HA H 3.54 . 1 460 . 48 VAL CB C 29.8 . 1 461 . 48 VAL HB H 1.92 . 1 462 . 48 VAL HG1 H 0.87 . 1 463 . 48 VAL HG2 H 0.98 . 1 464 . 49 MET N N 117.9 . 1 465 . 49 MET H H 7.32 . 1 466 . 49 MET C C 177.1 . 1 467 . 49 MET CA C 57.2 . 1 468 . 49 MET HA H 4.26 . 1 469 . 49 MET CB C 31.3 . 1 470 . 49 MET HB2 H 2.27 . 1 471 . 49 MET HB3 H 2.27 . 1 472 . 49 MET HG2 H 2.85 . 1 473 . 49 MET HG3 H 2.85 . 1 474 . 50 LEU N N 119.3 . 1 475 . 50 LEU H H 7.51 . 1 476 . 50 LEU C C 174.0 . 1 477 . 50 LEU CA C 56.8 . 1 478 . 50 LEU HA H 3.76 . 1 479 . 50 LEU CB C 39.2 . 1 480 . 50 LEU HB2 H 1.36 . 1 481 . 50 LEU HB3 H 1.80 . 1 482 . 50 LEU HG H 1.64 . 1 483 . 50 LEU HD1 H 0.28 . 1 484 . 50 LEU HD2 H 0.56 . 1 485 . 51 LYS N N 119.3 . 1 486 . 51 LYS H H 6.81 . 1 487 . 51 LYS C C 176.5 . 1 488 . 51 LYS CA C 57.0 . 1 489 . 51 LYS HA H 2.04 . 1 490 . 51 LYS CB C 29.4 . 1 491 . 51 LYS HB2 H 0.27 . 2 492 . 51 LYS HB3 H 1.41 . 2 493 . 51 LYS HG2 H 1.00 . 2 494 . 51 LYS HG3 H 1.20 . 2 495 . 52 ASP N N 118.2 . 1 496 . 52 ASP H H 8.01 . 1 497 . 52 ASP C C 176.3 . 1 498 . 52 ASP CA C 55.0 . 1 499 . 52 ASP HA H 4.22 . 1 500 . 52 ASP CB C 38.5 . 1 501 . 52 ASP HB2 H 2.55 . 1 502 . 52 ASP HB3 H 2.55 . 1 503 . 53 ARG N N 122.2 . 1 504 . 53 ARG H H 7.97 . 1 505 . 53 ARG C C 175.6 . 1 506 . 53 ARG CA C 54.8 . 1 507 . 53 ARG HA H 3.68 . 1 508 . 53 ARG CB C 27.2 . 1 509 . 53 ARG HB2 H 0.79 . 1 510 . 53 ARG HB3 H 1.30 . 1 511 . 53 ARG HG2 H -0.30 . 2 512 . 53 ARG HG3 H 0.67 . 2 513 . 53 ARG HD2 H 0.83 . 2 514 . 53 ARG HD3 H 2.58 . 2 515 . 53 ARG HE H 8.08 . 1 516 . 53 ARG NE N 86.3 . 1 517 . 54 TRP N N 120.9 . 1 518 . 54 TRP H H 8.34 . 1 519 . 54 TRP C C 174.7 . 1 520 . 54 TRP CA C 57.7 . 1 521 . 54 TRP HA H 4.33 . 1 522 . 54 TRP CB C 28.2 . 1 523 . 54 TRP HB2 H 3.12 . 1 524 . 54 TRP HB3 H 3.12 . 1 525 . 54 TRP HD1 H 7.34 . 1 526 . 54 TRP HE1 H 10.46 . 1 527 . 54 TRP HE3 H 7.47 . 1 528 . 54 TRP HZ2 H 7.47 . 1 529 . 54 TRP HZ3 H 6.77 . 1 530 . 54 TRP HH2 H 7.21 . 1 531 . 54 TRP NE1 N 128.0 . 1 532 . 55 ARG N N 116.3 . 1 533 . 55 ARG H H 7.66 . 1 534 . 55 ARG C C 177.0 . 1 535 . 55 ARG CA C 57.7 . 1 536 . 55 ARG HA H 3.73 . 1 537 . 55 ARG CB C 27.7 . 1 538 . 55 ARG HB2 H 1.93 . 1 539 . 55 ARG HB3 H 1.93 . 1 540 . 55 ARG HG2 H 1.55 . 2 541 . 55 ARG HG3 H 1.76 . 2 542 . 55 ARG HD2 H 3.18 . 1 543 . 55 ARG HD3 H 3.18 . 1 544 . 56 THR N N 115.8 . 1 545 . 56 THR H H 7.69 . 1 546 . 56 THR C C 173.4 . 1 547 . 56 THR CA C 64.2 . 1 548 . 56 THR HA H 3.77 . 1 549 . 56 THR CB C 66.5 . 1 550 . 56 THR HB H 4.17 . 1 551 . 56 THR HG2 H 1.08 . 1 552 . 57 MET N N 120.7 . 1 553 . 57 MET H H 8.30 . 1 554 . 57 MET C C 175.9 . 1 555 . 57 MET CA C 57.3 . 1 556 . 57 MET HA H 3.66 . 1 557 . 57 MET CB C 30.9 . 1 558 . 57 MET HB2 H 1.75 . 1 559 . 57 MET HB3 H 1.75 . 1 560 . 57 MET HG2 H 2.07 . 2 561 . 57 MET HG3 H 2.38 . 2 562 . 58 LYS N N 118.3 . 1 563 . 58 LYS H H 7.82 . 1 564 . 58 LYS C C 176.6 . 1 565 . 58 LYS CA C 57.0 . 1 566 . 58 LYS HA H 3.60 . 1 567 . 58 LYS CB C 29.9 . 1 568 . 58 LYS HB2 H 1.43 . 1 569 . 58 LYS HB3 H 1.43 . 1 570 . 58 LYS HG2 H 0.93 . 4 571 . 58 LYS HG3 H 0.93 . 4 572 . 58 LYS HD2 H 1.51 . 4 573 . 58 LYS HD3 H 1.51 . 4 574 . 58 LYS HE2 H 2.80 . 1 575 . 58 LYS HE3 H 2.80 . 1 576 . 59 LYS N N 119.9 . 1 577 . 59 LYS H H 7.59 . 1 578 . 59 LYS C C 175.6 . 1 579 . 59 LYS CA C 56.2 . 1 580 . 59 LYS HA H 4.02 . 1 581 . 59 LYS CB C 30.4 . 1 582 . 59 LYS HB2 H 1.84 . 1 583 . 59 LYS HB3 H 1.84 . 1 584 . 59 LYS HG2 H 1.35 . 4 585 . 59 LYS HG3 H 1.45 . 4 586 . 59 LYS HD2 H 1.56 . 4 587 . 59 LYS HD3 H 1.56 . 4 588 . 59 LYS HE2 H 2.87 . 1 589 . 59 LYS HE3 H 2.87 . 1 590 . 60 LEU N N 118.1 . 1 591 . 60 LEU H H 7.80 . 1 592 . 60 LEU C C 174.1 . 1 593 . 60 LEU CA C 56.2 . 1 594 . 60 LEU HA H 4.17 . 1 595 . 60 LEU CB C 30.4 . 1 596 . 60 LEU HB2 H 1.55 . 1 597 . 60 LEU HB3 H 1.55 . 1 598 . 60 LEU HG H 1.66 . 1 599 . 60 LEU HD1 H 0.75 . 1 600 . 60 LEU HD2 H 0.75 . 1 601 . 61 LYS N N 117.2 . 1 602 . 61 LYS H H 7.75 . 1 603 . 61 LYS C C 174.2 . 1 604 . 61 LYS CA C 55.0 . 1 605 . 61 LYS HA H 4.01 . 1 606 . 61 LYS CB C 28.5 . 1 607 . 61 LYS HB2 H 1.86 . 1 608 . 61 LYS HB3 H 1.86 . 1 609 . 61 LYS HG2 H 1.30 . 4 610 . 61 LYS HG3 H 1.61 . 4 611 . 61 LYS HD2 H 1.89 . 4 612 . 61 LYS HD3 H 1.89 . 4 613 . 61 LYS HE2 H 2.95 . 1 614 . 61 LYS HE3 H 2.95 . 1 615 . 62 LEU N N 119.3 . 1 616 . 62 LEU H H 8.09 . 1 617 . 62 LEU C C 175.0 . 1 618 . 62 LEU CA C 53.1 . 1 619 . 62 LEU HA H 4.34 . 1 620 . 62 LEU CB C 40.5 . 1 621 . 62 LEU HB2 H 1.51 . 4 622 . 62 LEU HB3 H 1.51 . 4 623 . 62 LEU HG H 1.51 . 4 624 . 62 LEU HD1 H 0.82 . 1 625 . 62 LEU HD2 H 0.82 . 1 626 . 63 ILE N N 117.7 . 1 627 . 63 ILE H H 7.61 . 1 628 . 63 ILE C C 173.6 . 1 629 . 63 ILE CA C 59.0 . 1 630 . 63 ILE HA H 4.17 . 1 631 . 63 ILE CB C 36.9 . 1 632 . 63 ILE HB H 1.71 . 1 633 . 63 ILE HG12 H 0.90 . 1 634 . 63 ILE HG13 H 1.21 . 1 635 . 63 ILE HG2 H 0.67 . 1 636 . 63 ILE HD1 H 0.56 . 1 637 . 64 SER N N 118.6 . 1 638 . 64 SER H H 8.27 . 1 639 . 64 SER C C 172.2 . 1 640 . 64 SER CA C 56.0 . 1 641 . 64 SER HA H 4.46 . 1 642 . 64 SER CB C 62.0 . 1 643 . 64 SER HB2 H 3.84 . 1 644 . 64 SER HB3 H 3.84 . 1 645 . 65 SER N N 117.6 . 1 646 . 65 SER H H 8.40 . 1 647 . 65 SER C C 172.0 . 1 648 . 65 SER CA C 56.1 . 1 649 . 65 SER HA H 4.45 . 1 650 . 65 SER CB C 61.9 . 1 651 . 65 SER HB2 H 3.85 . 1 652 . 65 SER HB3 H 3.85 . 1 653 . 66 ASP N N 121.8 . 1 654 . 66 ASP H H 8.38 . 1 655 . 66 ASP C C 173.8 . 1 656 . 66 ASP CA C 52.5 . 1 657 . 66 ASP HA H 4.65 . 1 658 . 66 ASP CB C 39.3 . 1 659 . 66 ASP HB2 H 2.67 . 1 660 . 66 ASP HB3 H 2.67 . 1 661 . 67 SER N N 114.8 . 1 662 . 67 SER H H 8.12 . 1 663 . 67 SER C C 172.0 . 1 664 . 67 SER CA C 56.4 . 1 665 . 67 SER HA H 4.45 . 1 666 . 67 SER CB C 62.0 . 1 667 . 67 SER HB2 H 3.85 . 1 668 . 67 SER HB3 H 3.85 . 1 669 . 68 GLU N N 122.6 . 1 670 . 68 GLU H H 8.39 . 1 671 . 68 GLU C C 173.0 . 1 672 . 68 GLU CA C 54.4 . 1 673 . 68 GLU HA H 4.32 . 1 674 . 68 GLU CB C 28.6 . 1 675 . 68 GLU HB2 H 1.88 . 2 676 . 68 GLU HB3 H 2.09 . 2 677 . 69 ASP N N 126.2 . 1 678 . 69 ASP H H 7.95 . 1 679 . 69 ASP CA C 53.9 . 1 680 . 69 ASP HA H 4.36 . 1 681 . 69 ASP CB C 40.1 . 1 682 . 69 ASP HB2 H 2.52 . 2 683 . 69 ASP HB3 H 2.64 . 2 stop_ save_