data_19171 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; transcriptional repressor domain of methylated DNA binding domain protein 1 ; _BMRB_accession_number 19171 _BMRB_flat_file_name bmr19171.str _Entry_type original _Submission_date 2013-04-16 _Accession_date 2013-04-16 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'transcriptional repressor domain of methylated DNA binding domain protein 1 , D507-Q605' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lim Jackwee . . 2 'Shahul Hameed' 'Umar Farook' . . 3 Yang Daiwen . . 4 Kunchithapadam Swaminathan . . 5 Wasik Mariusz A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 374 "13C chemical shifts" 258 "15N chemical shifts" 91 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-09-19 original author . stop_ _Original_release_date 2014-09-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Transcriptional repressor domain of MBD1 is intrinsically disordered and interacts with its binding partners in a selective manner.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24810720 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hameed 'Umar Farook Shahul' F. . 2 Lim Jackwee . . 3 Zhang Qian . . 4 Wasik Mariusz A. . 5 Yang Daiwen . . 6 Swaminathan Kunchithapadam . . stop_ _Journal_abbreviation 'Sci. Rep.' _Journal_name_full 'Scientific reports' _Journal_volume 4 _Journal_issue . _Journal_ISSN 2045-2322 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4896 _Page_last 4896 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'TRD of MBD1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'TRD of MBD1' $TRD_of_MBD1 stop_ _System_molecular_weight 12594 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TRD_of_MBD1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TRD_of_MBD1 _Molecular_mass . _Mol_thiol_state 'not reported' loop_ _Biological_function 'gene repression' 'recruiting binding partners for heterochromatin formation' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 117 _Mol_residue_sequence ; MHHHHHHSSGLVPRGSEFDE WTPGTAVLTSPVLVPGCPSK AVDPGLPSVKQEPPDPEEDK EENKDDSASKLAPEEEAGGA GTPVITEIFSLGGTRFRDTA VWLPRSKDLKKPGARKQ ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 HIS 3 3 HIS 4 4 HIS 5 5 HIS 6 6 HIS 7 7 HIS 8 8 SER 9 9 SER 10 10 GLY 11 11 LEU 12 12 VAL 13 13 PRO 14 14 ARG 15 15 GLY 16 16 SER 17 17 GLU 18 18 PHE 19 19 ASP 20 20 GLU 21 21 TRP 22 22 THR 23 23 PRO 24 24 GLY 25 25 THR 26 26 ALA 27 27 VAL 28 28 LEU 29 29 THR 30 30 SER 31 31 PRO 32 32 VAL 33 33 LEU 34 34 VAL 35 35 PRO 36 36 GLY 37 37 CYS 38 38 PRO 39 39 SER 40 40 LYS 41 41 ALA 42 42 VAL 43 43 ASP 44 44 PRO 45 45 GLY 46 46 LEU 47 47 PRO 48 48 SER 49 49 VAL 50 50 LYS 51 51 GLN 52 52 GLU 53 53 PRO 54 54 PRO 55 55 ASP 56 56 PRO 57 57 GLU 58 58 GLU 59 59 ASP 60 60 LYS 61 61 GLU 62 62 GLU 63 63 ASN 64 64 LYS 65 65 ASP 66 66 ASP 67 67 SER 68 68 ALA 69 69 SER 70 70 LYS 71 71 LEU 72 72 ALA 73 73 PRO 74 74 GLU 75 75 GLU 76 76 GLU 77 77 ALA 78 78 GLY 79 79 GLY 80 80 ALA 81 81 GLY 82 82 THR 83 83 PRO 84 84 VAL 85 85 ILE 86 86 THR 87 87 GLU 88 88 ILE 89 89 PHE 90 90 SER 91 91 LEU 92 92 GLY 93 93 GLY 94 94 THR 95 95 ARG 96 96 PHE 97 97 ARG 98 98 ASP 99 99 THR 100 100 ALA 101 101 VAL 102 102 TRP 103 103 LEU 104 104 PRO 105 105 ARG 106 106 SER 107 107 LYS 108 108 ASP 109 109 LEU 110 110 LYS 111 111 LYS 112 112 PRO 113 113 GLY 114 114 ALA 115 115 ARG 116 116 LYS 117 117 GLN 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 DBJ BAE02268 "unnamed protein product [Macaca fascicularis]" 84.62 432 100.00 100.00 3.39e-59 DBJ BAF84208 "unnamed protein product [Homo sapiens]" 84.62 605 100.00 100.00 5.42e-58 DBJ BAG58353 "unnamed protein product [Homo sapiens]" 84.62 656 100.00 100.00 8.04e-58 DBJ BAG63407 "unnamed protein product [Homo sapiens]" 84.62 630 100.00 100.00 6.78e-58 DBJ BAI45833 "methyl-CpG binding domain protein 1 [synthetic construct]" 84.62 630 100.00 100.00 6.78e-58 EMBL CAA71735 "methyl-CpG binding protein [Homo sapiens]" 84.62 556 100.00 100.00 3.81e-58 EMBL CAH90629 "hypothetical protein [Pongo abelii]" 84.62 605 98.99 98.99 2.63e-57 GB AAD50371 "methyl-CpG binding protein 1 [Homo sapiens]" 84.62 605 100.00 100.00 4.40e-58 GB AAD51442 "methyl-CpG binding protein splice variant 1 [Homo sapiens]" 84.62 605 100.00 100.00 5.47e-58 GB AAD51444 "methyl-CpG binding protein splice variant 3 [Homo sapiens]" 84.62 549 100.00 100.00 5.26e-58 GB AAH33242 "Methyl-CpG binding domain protein 1 [Homo sapiens]" 84.62 549 100.00 100.00 5.15e-58 GB ABM47767 "MBD1 [Saguinus labiatus]" 73.50 266 100.00 100.00 2.52e-51 REF NP_001191065 "methyl-CpG-binding domain protein 1 isoform 6 [Homo sapiens]" 73.50 655 100.00 100.00 1.17e-48 REF NP_001191066 "methyl-CpG-binding domain protein 1 isoform 7 [Homo sapiens]" 84.62 630 100.00 100.00 6.78e-58 REF NP_001191067 "methyl-CpG-binding domain protein 1 isoform 8 [Homo sapiens]" 84.62 629 100.00 100.00 7.34e-58 REF NP_001191068 "methyl-CpG-binding domain protein 1 isoform 1 [Homo sapiens]" 84.62 605 100.00 100.00 5.42e-58 REF NP_001191069 "methyl-CpG-binding domain protein 1 isoform 9 [Homo sapiens]" 84.62 574 100.00 100.00 7.28e-58 SP Q9UIS9 "RecName: Full=Methyl-CpG-binding domain protein 1; AltName: Full=CXXC-type zinc finger protein 3; AltName: Full=Methyl-CpG-bind" 84.62 605 100.00 100.00 5.42e-58 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TRD_of_MBD1 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 _Details $TRD_of_MBD1 'recombinant technology' . Escherichia coli . pET32a 'pET32a modified vector with an N-terminal His6x-tag-MBD1(TRD)' 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 $TRD_of_MBD1 1 mM '[U-99% 13C; U-99% 15N]' 'sodium phosphate' 20 mM 'natural abundance' 'sodium azide' 0.1 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRspy _Saveframe_category software _Name NMRspy _Version . loop_ _Vendor _Address _Electronic_address 'Yang Daiwen' ; Department of Biological Sciences National University of Singapore 14 Science Drive 4 Singapore 117543 ; dbsydw@nus.edu.sg 'Zheng Yu' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details In-House save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _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_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_MQ-(H)CCH-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D MQ-(H)CCH-TOCSY' _Sample_label $sample_1 save_ save_4D_timeshared_13C/15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '4D timeshared 13C/15N NOESY' _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' 0.02 . M pH 6.5 . 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 0.00 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 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 HN(CO)CA' '3D HNCA' '3D MQ-(H)CCH-TOCSY' '4D timeshared 13C/15N NOESY' 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 'TRD of MBD1' _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 9 9 SER H H 8.433 0.03 1 2 9 9 SER HA H 4.415 0.03 1 3 9 9 SER HB3 H 3.922 0.03 1 4 9 9 SER CA C 58.756 0.3 1 5 9 9 SER CB C 67.006 0.3 1 6 9 9 SER N N 117.925 0.3 1 7 10 10 GLY H H 8.352 0.03 1 8 10 10 GLY HA3 H 4.047 0.03 1 9 10 10 GLY CA C 45.693 0.3 1 10 10 10 GLY N N 110.465 0.3 1 11 11 11 LEU H H 8.009 0.03 1 12 11 11 LEU HA H 4.310 0.03 1 13 11 11 LEU HB3 H 1.540 0.03 1 14 11 11 LEU HG H 1.471 0.03 1 15 11 11 LEU HD1 H 0.793 0.03 1 16 11 11 LEU CA C 55.318 0.3 1 17 11 11 LEU CB C 42.256 0.3 1 18 11 11 LEU CG C 27.130 0.3 1 19 11 11 LEU CD1 C 23.693 0.3 1 20 11 11 LEU N N 121.412 0.3 1 21 12 12 VAL H H 8.017 0.03 1 22 12 12 VAL HA H 4.331 0.03 1 23 12 12 VAL HB H 1.988 0.03 1 24 12 12 VAL HG2 H 0.846 0.03 1 25 12 12 VAL CA C 59.443 0.3 1 26 12 12 VAL CB C 32.630 0.3 1 27 12 12 VAL CG2 C 20.256 0.3 1 28 12 12 VAL N N 122.047 0.3 1 29 15 15 GLY H H 8.573 0.03 1 30 15 15 GLY HA2 H 3.933 0.03 1 31 15 15 GLY HA3 H 3.979 0.03 1 32 15 15 GLY CA C 46.380 0.3 1 33 15 15 GLY N N 110.939 0.3 1 34 16 16 SER H H 8.230 0.03 1 35 16 16 SER HA H 4.408 0.03 1 36 16 16 SER HB3 H 3.807 0.03 1 37 16 16 SER CA C 58.756 0.3 1 38 16 16 SER CB C 64.256 0.3 1 39 16 16 SER N N 115.867 0.3 1 40 17 17 GLU H H 8.734 0.03 1 41 17 17 GLU HA H 4.139 0.03 1 42 17 17 GLU HB2 H 1.742 0.03 1 43 17 17 GLU HG2 H 1.938 0.03 1 44 17 17 GLU CA C 57.381 0.3 1 45 17 17 GLU CB C 29.880 0.3 1 46 17 17 GLU CG C 36.068 0.3 1 47 17 17 GLU N N 122.386 0.3 1 48 18 18 PHE H H 7.994 0.03 1 49 18 18 PHE HA H 4.562 0.03 1 50 18 18 PHE HB2 H 3.180 0.03 1 51 18 18 PHE HB3 H 2.861 0.03 1 52 18 18 PHE CA C 57.381 0.3 1 53 18 18 PHE CB C 39.506 0.3 1 54 18 18 PHE N N 119.049 0.3 1 55 19 19 ASP H H 8.048 0.03 1 56 19 19 ASP HA H 4.549 0.03 1 57 19 19 ASP HB3 H 2.572 0.03 1 58 19 19 ASP CA C 54.630 0.3 1 59 19 19 ASP CB C 41.568 0.3 1 60 19 19 ASP N N 121.522 0.3 1 61 20 20 GLU H H 8.188 0.03 1 62 20 20 GLU HA H 4.221 0.03 1 63 20 20 GLU HB3 H 1.812 0.03 1 64 20 20 GLU HG2 H 2.086 0.03 1 65 20 20 GLU HG3 H 2.394 0.03 1 66 20 20 GLU CA C 56.693 0.3 1 67 20 20 GLU CB C 29.880 0.3 1 68 20 20 GLU CG C 36.068 0.3 1 69 20 20 GLU N N 120.628 0.3 1 70 21 21 TRP H H 8.207 0.03 1 71 21 21 TRP HA H 4.545 0.03 1 72 21 21 TRP HB3 H 3.162 0.03 1 73 21 21 TRP HE1 H 9.963 0.03 1 74 21 21 TRP CA C 58.068 0.3 1 75 21 21 TRP CB C 29.880 0.3 1 76 21 21 TRP N N 122.535 0.3 1 77 21 21 TRP NE1 N 130.169 0.3 1 78 22 22 THR H H 7.681 0.03 1 79 22 22 THR HA H 4.404 0.03 1 80 22 22 THR HB H 3.968 0.03 1 81 22 22 THR HG2 H 1.053 0.03 1 82 22 22 THR CA C 59.443 0.3 1 83 22 22 THR CB C 69.755 0.3 1 84 22 22 THR CG2 C 21.631 0.3 1 85 22 22 THR N N 119.211 0.3 1 86 23 23 PRO HA H 4.086 0.03 1 87 23 23 PRO HB2 H 1.860 0.03 1 88 23 23 PRO HB3 H 2.215 0.03 1 89 23 23 PRO HD2 H 3.458 0.03 1 90 23 23 PRO CA C 63.568 0.3 1 91 23 23 PRO CB C 31.943 0.3 1 92 23 23 PRO CD C 50.505 0.3 1 93 24 24 GLY H H 8.310 0.03 1 94 24 24 GLY HA3 H 3.919 0.03 1 95 24 24 GLY CA C 45.006 0.3 1 96 24 24 GLY N N 108.811 0.3 1 97 25 25 THR H H 7.839 0.03 1 98 25 25 THR HA H 4.221 0.03 1 99 25 25 THR HB H 4.149 0.03 1 100 25 25 THR HG2 H 1.106 0.03 1 101 25 25 THR CA C 62.193 0.3 1 102 25 25 THR CB C 69.755 0.3 1 103 25 25 THR CG2 C 21.631 0.3 1 104 25 25 THR N N 113.503 0.3 1 105 26 26 ALA H H 8.247 0.03 1 106 26 26 ALA HA H 4.275 0.03 1 107 26 26 ALA HB H 1.279 0.03 1 108 26 26 ALA CA C 52.568 0.3 1 109 26 26 ALA CB C 19.568 0.3 1 110 26 26 ALA N N 126.679 0.3 1 111 27 27 VAL H H 8.026 0.03 1 112 27 27 VAL HA H 4.044 0.03 1 113 27 27 VAL HB H 2.001 0.03 1 114 27 27 VAL HG2 H 0.872 0.03 1 115 27 27 VAL CA C 62.193 0.3 1 116 27 27 VAL CB C 32.630 0.3 1 117 27 27 VAL CG2 C 20.943 0.3 1 118 27 27 VAL N N 119.528 0.3 1 119 28 28 LEU H H 8.227 0.03 1 120 28 28 LEU HA H 4.373 0.03 1 121 28 28 LEU HB3 H 1.543 0.03 1 122 28 28 LEU HG H 1.518 0.03 1 123 28 28 LEU HD1 H 0.846 0.03 1 124 28 28 LEU CA C 54.630 0.3 1 125 28 28 LEU CB C 42.256 0.3 1 126 28 28 LEU CG C 27.130 0.3 1 127 28 28 LEU CD1 C 25.048 0.3 1 128 28 28 LEU N N 126.588 0.3 1 129 29 29 THR H H 8.057 0.03 1 130 29 29 THR HA H 4.322 0.03 1 131 29 29 THR HB H 4.150 0.03 1 132 29 29 THR HG2 H 1.133 0.03 1 133 29 29 THR CA C 61.506 0.3 1 134 29 29 THR CB C 69.755 0.3 1 135 29 29 THR CG2 C 21.632 0.3 1 136 29 29 THR N N 114.765 0.3 1 137 30 30 SER H H 8.191 0.03 1 138 30 30 SER HA H 4.731 0.03 1 139 30 30 SER HB3 H 3.809 0.03 1 140 30 30 SER CA C 56.693 0.3 1 141 30 30 SER CB C 63.568 0.3 1 142 30 30 SER N N 119.172 0.3 1 143 31 31 PRO HA H 4.392 0.03 1 144 31 31 PRO HB2 H 1.856 0.03 1 145 31 31 PRO HB3 H 2.223 0.03 1 146 31 31 PRO HG3 H 1.934 0.03 1 147 31 31 PRO CA C 63.568 0.3 1 148 31 31 PRO CB C 31.943 0.3 1 149 31 31 PRO CG C 27.130 0.3 1 150 32 32 VAL H H 8.084 0.03 1 151 32 32 VAL HA H 4.006 0.03 1 152 32 32 VAL HB H 1.980 0.03 1 153 32 32 VAL HG2 H 0.876 0.03 1 154 32 32 VAL CA C 62.193 0.3 1 155 32 32 VAL CB C 32.630 0.3 1 156 32 32 VAL CG2 C 20.943 0.3 1 157 32 32 VAL N N 120.191 0.3 1 158 33 33 LEU H H 8.276 0.03 1 159 33 33 LEU HA H 4.235 0.053 1 160 33 33 LEU HB3 H 1.542 0.03 1 161 33 33 LEU HG H 1.366 0.03 1 162 33 33 LEU HD2 H 0.816 0.03 1 163 33 33 LEU CA C 55.005 0.3 1 164 33 33 LEU CB C 42.256 0.3 1 165 33 33 LEU CG C 24.380 0.3 1 166 33 33 LEU CD2 C 24.380 0.3 1 167 33 33 LEU N N 125.973 0.3 1 168 34 34 VAL H H 8.165 0.03 1 169 34 34 VAL HA H 4.372 0.03 1 170 34 34 VAL HB H 1.714 0.03 1 171 34 34 VAL HG2 H 0.869 0.03 1 172 34 34 VAL CA C 59.443 0.3 1 173 34 34 VAL CB C 32.630 0.3 1 174 34 34 VAL CG2 C 20.943 0.3 1 175 34 34 VAL N N 123.488 0.3 1 176 35 35 PRO HA H 4.370 0.03 1 177 35 35 PRO HB2 H 2.234 0.03 1 178 35 35 PRO HB3 H 1.951 0.03 1 179 35 35 PRO HG3 H 1.976 0.03 1 180 35 35 PRO HD3 H 3.835 0.03 1 181 35 35 PRO CA C 63.568 0.3 1 182 35 35 PRO CB C 31.943 0.3 1 183 35 35 PRO CG C 27.130 0.3 1 184 35 35 PRO CD C 50.505 0.3 1 185 36 36 GLY H H 8.446 0.03 1 186 36 36 GLY HA2 H 3.916 0.03 1 187 36 36 GLY HA3 H 3.824 0.03 1 188 36 36 GLY CA C 45.006 0.3 1 189 36 36 GLY N N 110.041 0.3 1 190 38 38 PRO HA H 4.397 0.03 1 191 38 38 PRO HB2 H 1.876 0.03 1 192 38 38 PRO HB3 H 2.264 0.03 1 193 38 38 PRO HG3 H 1.984 0.03 1 194 38 38 PRO CA C 63.568 0.3 1 195 38 38 PRO CB C 31.943 0.3 1 196 38 38 PRO CG C 27.130 0.3 1 197 39 39 SER H H 8.318 0.03 1 198 39 39 SER HA H 4.424 0.03 1 199 39 39 SER HB3 H 3.799 0.03 1 200 39 39 SER CA C 58.068 0.3 1 201 39 39 SER CB C 64.256 0.3 1 202 39 39 SER N N 116.043 0.3 1 203 40 40 LYS H H 8.231 0.03 1 204 40 40 LYS HA H 4.240 0.03 1 205 40 40 LYS CA C 56.525 0.3 1 206 40 40 LYS N N 123.275 0.3 1 207 41 41 ALA H H 8.240 0.03 1 208 41 41 ALA HA H 4.266 0.03 1 209 41 41 ALA HB H 1.276 0.03 1 210 41 41 ALA CA C 52.568 0.3 1 211 41 41 ALA CB C 19.568 0.3 1 212 41 41 ALA N N 125.719 0.3 1 213 42 42 VAL H H 8.050 0.03 1 214 42 42 VAL HA H 4.047 0.03 1 215 42 42 VAL CA C 62.292 0.3 1 216 42 42 VAL N N 119.502 0.3 1 217 44 44 PRO HA H 4.370 0.03 1 218 44 44 PRO HB2 H 2.234 0.03 1 219 44 44 PRO HB3 H 1.951 0.03 1 220 44 44 PRO HG3 H 1.976 0.03 1 221 44 44 PRO HD3 H 3.835 0.03 1 222 44 44 PRO CA C 63.568 0.3 1 223 44 44 PRO CB C 31.943 0.3 1 224 44 44 PRO CG C 27.130 0.3 1 225 44 44 PRO CD C 50.505 0.3 1 226 45 45 GLY H H 8.457 0.03 1 227 45 45 GLY HA2 H 3.914 0.03 1 228 45 45 GLY HA3 H 3.824 0.03 1 229 45 45 GLY CA C 45.006 0.3 1 230 45 45 GLY N N 108.216 0.3 1 231 46 46 LEU H H 7.840 0.03 1 232 46 46 LEU HA H 4.582 0.03 1 233 46 46 LEU HB3 H 1.587 0.03 1 234 46 46 LEU HG H 1.596 0.03 1 235 46 46 LEU HD1 H 0.883 0.03 1 236 46 46 LEU CA C 53.255 0.3 1 237 46 46 LEU CB C 41.568 0.3 1 238 46 46 LEU CG C 27.130 0.3 1 239 46 46 LEU CD1 C 25.068 0.3 1 240 46 46 LEU N N 122.594 0.3 1 241 47 47 PRO HA H 4.497 0.03 1 242 47 47 PRO HD3 H 3.831 0.03 1 243 47 47 PRO CA C 62.881 0.3 1 244 47 47 PRO CD C 50.505 0.3 1 245 48 48 SER H H 8.572 0.03 1 246 48 48 SER HA H 4.413 0.03 1 247 48 48 SER HB3 H 3.826 0.03 1 248 48 48 SER CA C 58.756 0.3 1 249 48 48 SER CB C 63.568 0.3 1 250 48 48 SER N N 116.870 0.3 1 251 49 49 VAL H H 8.067 0.03 1 252 49 49 VAL HA H 4.094 0.03 1 253 49 49 VAL HB H 2.041 0.03 1 254 49 49 VAL HG2 H 0.864 0.03 1 255 49 49 VAL CA C 62.193 0.3 1 256 49 49 VAL CB C 32.630 0.3 1 257 49 49 VAL CG2 C 20.943 0.3 1 258 49 49 VAL N N 121.794 0.3 1 259 50 50 LYS H H 8.336 0.03 1 260 50 50 LYS HA H 4.281 0.03 1 261 50 50 LYS HB3 H 1.710 0.03 1 262 50 50 LYS HG3 H 1.320 0.03 1 263 50 50 LYS HD3 H 1.6984 0.03 1 264 50 50 LYS CA C 56.005 0.3 1 265 50 50 LYS CB C 33.318 0.3 1 266 50 50 LYS CG C 24.380 0.3 1 267 50 50 LYS CD C 25.068 0.3 1 268 50 50 LYS N N 125.516 0.3 1 269 51 51 GLN H H 8.421 0.03 1 270 51 51 GLN HA H 4.327 0.03 1 271 51 51 GLN HB3 H 1.930 0.03 1 272 51 51 GLN HG2 H 2.252 0.03 1 273 51 51 GLN HG3 H 2.306 0.03 1 274 51 51 GLN HE21 H 7.499 0.03 1 275 51 51 GLN HE22 H 6.851 0.03 1 276 51 51 GLN CA C 55.318 0.3 1 277 51 51 GLN CB C 29.880 0.3 1 278 51 51 GLN CG C 34.005 0.3 1 279 51 51 GLN N N 122.985 0.3 1 280 51 51 GLN NE2 N 112.525 0.3 1 281 52 52 GLU H H 8.440 0.03 1 282 52 52 GLU HA H 4.535 0.03 1 283 52 52 GLU HB2 H 1.799 0.03 1 284 52 52 GLU HB3 H 1.991 0.03 1 285 52 52 GLU HG3 H 2.252 0.03 1 286 52 52 GLU CA C 54.630 0.3 1 287 52 52 GLU CB C 29.642 0.3 1 288 52 52 GLU CG C 36.068 0.3 1 289 52 52 GLU N N 124.305 0.3 1 290 53 53 PRO HD3 H 3.722 0.03 1 291 53 53 PRO CD C 50.505 0.3 1 292 54 54 PRO HA H 4.067 0.03 1 293 54 54 PRO CA C 62.152 0.3 1 294 56 56 PRO HA H 4.365 0.03 1 295 56 56 PRO HB2 H 2.248 0.03 1 296 56 56 PRO HB3 H 1.880 0.03 1 297 56 56 PRO HG3 H 1.990 0.03 1 298 56 56 PRO HD3 H 3.733 0.03 1 299 56 56 PRO CA C 63.568 0.3 1 300 56 56 PRO CB C 32.630 0.3 1 301 56 56 PRO CG C 27.130 0.3 1 302 56 56 PRO CD C 50.505 0.3 1 303 57 57 GLU H H 8.471 0.03 1 304 57 57 GLU HA H 4.231 0.03 1 305 57 57 GLU HB3 H 1.879 0.03 1 306 57 57 GLU HG3 H 2.228 0.03 1 307 57 57 GLU CA C 55.846 0.3 1 308 57 57 GLU CB C 30.568 0.3 1 309 57 57 GLU CG C 36.068 0.3 1 310 57 57 GLU N N 120.064 0.3 1 311 58 58 GLU HA H 4.189 0.03 1 312 58 58 GLU CA C 56.693 0.3 1 313 59 59 ASP H H 8.337 0.03 1 314 59 59 ASP HA H 4.532 0.03 1 315 59 59 ASP HB2 H 2.592 0.03 1 316 59 59 ASP HB3 H 2.684 0.03 1 317 59 59 ASP CA C 54.630 0.3 1 318 59 59 ASP CB C 40.881 0.3 1 319 59 59 ASP N N 121.649 0.3 1 320 60 60 LYS HA H 4.586 0.03 1 321 60 60 LYS CA C 54.630 0.3 1 322 61 61 GLU H H 8.300 0.03 1 323 61 61 GLU HA H 4.229 0.03 1 324 61 61 GLU HB3 H 1.927 0.03 1 325 61 61 GLU HG3 H 2.194 0.03 1 326 61 61 GLU CA C 56.693 0.3 1 327 61 61 GLU CB C 30.568 0.3 1 328 61 61 GLU CG C 36.756 0.3 1 329 61 61 GLU N N 121.972 0.3 1 330 62 62 GLU H H 8.429 0.03 1 331 62 62 GLU HA H 4.182 0.03 1 332 62 62 GLU HB3 H 1.939 0.03 1 333 62 62 GLU HG3 H 2.223 0.03 1 334 62 62 GLU CA C 56.693 0.3 1 335 62 62 GLU CB C 30.568 0.3 1 336 62 62 GLU CG C 36.068 0.3 1 337 62 62 GLU N N 121.903 0.3 1 338 63 63 ASN H H 8.471 0.03 1 339 63 63 ASN HA H 4.645 0.03 1 340 63 63 ASN HB3 H 2.715 0.03 1 341 63 63 ASN HD21 H 7.599 0.03 1 342 63 63 ASN HD22 H 6.918 0.03 1 343 63 63 ASN CA C 53.255 0.3 1 344 63 63 ASN CB C 38.818 0.3 1 345 63 63 ASN N N 120.064 0.3 1 346 63 63 ASN ND2 N 112.915 0.3 1 347 64 64 LYS H H 8.273 0.03 1 348 64 64 LYS HA H 4.223 0.03 1 349 64 64 LYS HB3 H 1.701 0.03 1 350 64 64 LYS HG3 H 1.320 0.03 1 351 64 64 LYS HE3 H 2.759 0.03 1 352 64 64 LYS CA C 56.693 0.3 1 353 64 64 LYS CB C 33.318 0.3 1 354 64 64 LYS CG C 24.380 0.3 1 355 64 64 LYS CE C 38.818 0.3 1 356 64 64 LYS N N 122.349 0.3 1 357 65 65 ASP H H 8.321 0.03 1 358 65 65 ASP HA H 4.560 0.03 1 359 65 65 ASP CA C 54.479 0.3 1 360 65 65 ASP N N 121.309 0.3 1 361 66 66 ASP H H 8.315 0.03 1 362 66 66 ASP HA H 4.587 0.03 1 363 66 66 ASP HB3 H 2.687 0.03 1 364 66 66 ASP CA C 54.630 0.3 1 365 66 66 ASP CB C 40.881 0.3 1 366 66 66 ASP N N 122.282 0.3 1 367 67 67 SER H H 8.289 0.03 1 368 67 67 SER HA H 4.281 0.03 1 369 67 67 SER HB3 H 3.868 0.03 1 370 67 67 SER CA C 59.443 0.3 1 371 67 67 SER CB C 63.568 0.3 1 372 67 67 SER N N 116.381 0.3 1 373 68 68 ALA H H 8.189 0.03 1 374 68 68 ALA HA H 4.265 0.03 1 375 68 68 ALA HB H 1.394 0.03 1 376 68 68 ALA CA C 53.255 0.3 1 377 68 68 ALA CB C 18.881 0.3 1 378 68 68 ALA N N 125.113 0.3 1 379 69 69 SER H H 8.061 0.03 1 380 69 69 SER HA H 4.324 0.03 1 381 69 69 SER HB2 H 3.820 0.03 1 382 69 69 SER HB3 H 3.866 0.03 1 383 69 69 SER CA C 58.756 0.3 1 384 69 69 SER CB C 63.568 0.3 1 385 69 69 SER N N 114.161 0.3 1 386 70 70 LYS H H 8.045 0.03 1 387 70 70 LYS HA H 4.272 0.03 1 388 70 70 LYS HB3 H 1.726 0.03 1 389 70 70 LYS HG3 H 1.375 0.03 1 390 70 70 LYS HD3 H 1.648 0.03 1 391 70 70 LYS CA C 56.005 0.3 1 392 70 70 LYS CB C 32.630 0.3 1 393 70 70 LYS CG C 25.068 0.3 1 394 70 70 LYS CD C 29.530 0.3 1 395 70 70 LYS N N 122.781 0.3 1 396 71 71 LEU HA H 4.290 0.03 1 397 71 71 LEU HB3 H 1.585 0.03 1 398 71 71 LEU HG H 1.559 0.03 1 399 71 71 LEU HD1 H 0.879 0.03 1 400 71 71 LEU CA C 54.630 0.3 1 401 71 71 LEU CB C 42.256 0.3 1 402 71 71 LEU CG C 27.130 0.3 1 403 71 71 LEU CD1 C 25.068 0.3 1 404 72 72 ALA H H 8.281 0.03 1 405 72 72 ALA HA H 4.545 0.03 1 406 72 72 ALA HB H 1.345 0.03 1 407 72 72 ALA CA C 50.505 0.3 1 408 72 72 ALA CB C 18.193 0.3 1 409 72 72 ALA N N 126.217 0.3 1 410 73 73 PRO HA H 4.362 0.03 1 411 73 73 PRO HB2 H 2.263 0.03 1 412 73 73 PRO HB3 H 1.858 0.03 1 413 73 73 PRO HG3 H 2.004 0.03 1 414 73 73 PRO HD2 H 3.627 0.03 1 415 73 73 PRO CA C 63.568 0.3 1 416 73 73 PRO CB C 31.943 0.3 1 417 73 73 PRO CG C 27.130 0.3 1 418 73 73 PRO CD C 50.505 0.3 1 419 74 74 GLU H H 8.611 0.03 1 420 74 74 GLU HA H 4.202 0.03 1 421 74 74 GLU HB3 H 1.949 0.03 1 422 74 74 GLU HG3 H 2.281 0.03 1 423 74 74 GLU CA C 56.693 0.3 1 424 74 74 GLU CB C 29.880 0.3 1 425 74 74 GLU CG C 36.068 0.3 1 426 74 74 GLU N N 120.340 0.3 1 427 75 75 GLU HA H 4.214 0.03 1 428 75 75 GLU CA C 56.900 0.3 1 429 76 76 GLU H H 8.406 0.03 1 430 76 76 GLU HA H 4.183 0.03 1 431 76 76 GLU HB3 H 1.934 0.03 1 432 76 76 GLU HG3 H 2.228 0.03 1 433 76 76 GLU CA C 56.693 0.3 1 434 76 76 GLU CB C 30.568 0.3 1 435 76 76 GLU CG C 36.068 0.3 1 436 76 76 GLU N N 121.989 0.3 1 437 77 77 ALA H H 8.324 0.03 1 438 77 77 ALA HA H 4.277 0.03 1 439 77 77 ALA HB H 1.348 0.03 1 440 77 77 ALA CA C 52.568 0.3 1 441 77 77 ALA CB C 18.881 0.3 1 442 77 77 ALA N N 125.106 0.3 1 443 78 78 GLY H H 8.335 0.03 1 444 78 78 GLY HA3 H 3.910 0.03 1 445 78 78 GLY CA C 45.693 0.3 1 446 78 78 GLY N N 108.044 0.3 1 447 79 79 GLY H H 8.185 0.03 1 448 79 79 GLY HA3 H 3.919 0.03 1 449 79 79 GLY CA C 45.006 0.3 1 450 79 79 GLY N N 108.644 0.3 1 451 80 80 ALA H H 8.241 0.03 1 452 80 80 ALA HA H 4.277 0.03 1 453 80 80 ALA HB H 1.321 0.03 1 454 80 80 ALA CA C 52.568 0.3 1 455 80 80 ALA CB C 19.568 0.3 1 456 80 80 ALA N N 123.619 0.3 1 457 81 81 GLY H H 8.369 0.03 1 458 81 81 GLY HA3 H 3.913 0.03 1 459 81 81 GLY CA C 45.006 0.3 1 460 81 81 GLY N N 107.949 0.3 1 461 82 82 THR H H 7.977 0.03 1 462 82 82 THR HA H 4.541 0.03 1 463 82 82 THR HB H 4.095 0.03 1 464 82 82 THR HG2 H 1.189 0.03 1 465 82 82 THR CA C 60.131 0.3 1 466 82 82 THR CB C 69.755 0.3 1 467 82 82 THR CG2 C 21.631 0.3 1 468 82 82 THR N N 116.454 0.3 1 469 83 83 PRO HA H 4.434 0.03 1 470 83 83 PRO HB3 H 2.214 0.03 1 471 83 83 PRO HG3 H 1.957 0.03 1 472 83 83 PRO HD3 H 3.627 0.03 1 473 83 83 PRO CA C 62.881 0.3 1 474 83 83 PRO CB C 31.943 0.3 1 475 83 83 PRO CG C 27.130 0.3 1 476 83 83 PRO CD C 51.193 0.3 1 477 84 84 VAL H H 8.211 0.03 1 478 84 84 VAL HA H 4.065 0.03 1 479 84 84 VAL HB H 1.986 0.03 1 480 84 84 VAL HG2 H 0.882 0.03 1 481 84 84 VAL CA C 62.193 0.3 1 482 84 84 VAL CB C 32.630 0.3 1 483 84 84 VAL CG2 C 20.943 0.3 1 484 84 84 VAL N N 121.079 0.3 1 485 85 85 ILE H H 8.247 0.03 1 486 85 85 ILE HA H 4.195 0.03 1 487 85 85 ILE HB H 1.834 0.03 1 488 85 85 ILE HG12 H 1.400 0.03 1 489 85 85 ILE HG13 H 1.166 0.03 1 490 85 85 ILE HG2 H 0.844 0.03 1 491 85 85 ILE HD1 H 0.797 0.03 1 492 85 85 ILE CA C 60.818 0.3 1 493 85 85 ILE CB C 38.818 0.3 1 494 85 85 ILE CG1 C 27.130 0.3 1 495 85 85 ILE CG2 C 17.506 0.3 1 496 85 85 ILE CD1 C 12.693 0.3 1 497 85 85 ILE N N 125.287 0.3 1 498 86 86 THR H H 8.130 0.03 1 499 86 86 THR HA H 4.264 0.03 1 500 86 86 THR HB H 4.143 0.03 1 501 86 86 THR HG2 H 1.121 0.03 1 502 86 86 THR CA C 62.193 0.3 1 503 86 86 THR CB C 69.755 0.3 1 504 86 86 THR CG2 C 21.631 0.3 1 505 86 86 THR N N 118.400 0.3 1 506 87 87 GLU H H 8.292 0.03 1 507 87 87 GLU HA H 4.275 0.03 1 508 87 87 GLU HB2 H 1.884 0.03 1 509 87 87 GLU HB3 H 1.843 0.03 1 510 87 87 GLU HG3 H 2.122 0.03 1 511 87 87 GLU CA C 56.693 0.3 1 512 87 87 GLU CB C 30.568 0.3 1 513 87 87 GLU CG C 36.068 0.3 1 514 87 87 GLU N N 123.487 0.3 1 515 88 88 ILE H H 8.013 0.03 1 516 88 88 ILE HA H 4.042 0.03 1 517 88 88 ILE HB H 1.705 0.03 1 518 88 88 ILE HG12 H 1.306 0.03 1 519 88 88 ILE HG13 H 1.022 0.03 1 520 88 88 ILE HG2 H 0.700 0.03 1 521 88 88 ILE HD1 H 0.753 0.03 1 522 88 88 ILE CA C 61.506 0.3 1 523 88 88 ILE CB C 38.818 0.3 1 524 88 88 ILE CG1 C 27.130 0.3 1 525 88 88 ILE CG2 C 17.506 0.3 1 526 88 88 ILE CD1 C 12.693 0.3 1 527 88 88 ILE N N 121.076 0.3 1 528 89 89 PHE H H 8.209 0.03 1 529 89 89 PHE HA H 4.594 0.03 1 530 89 89 PHE HB2 H 2.953 0.03 1 531 89 89 PHE HB3 H 3.094 0.03 1 532 89 89 PHE CA C 58.068 0.3 1 533 89 89 PHE CB C 39.506 0.3 1 534 89 89 PHE N N 123.591 0.3 1 535 90 90 SER H H 8.103 0.03 1 536 90 90 SER HA H 4.395 0.03 1 537 90 90 SER HB3 H 3.767 0.03 1 538 90 90 SER CA C 58.681 0.3 1 539 90 90 SER CB C 64.256 0.3 1 540 90 90 SER N N 117.069 0.3 1 541 91 91 LEU H H 8.191 0.03 1 542 91 91 LEU HA H 4.283 0.03 1 543 91 91 LEU HB3 H 1.570 0.03 1 544 91 91 LEU HG H 1.568 0.03 1 545 91 91 LEU HD1 H 0.878 0.03 1 546 91 91 LEU CA C 55.318 0.3 1 547 91 91 LEU CB C 42.256 0.3 1 548 91 91 LEU CG C 27.130 0.3 1 549 91 91 LEU CD1 C 25.068 0.3 1 550 91 91 LEU N N 123.939 0.3 1 551 92 92 GLY H H 8.338 0.03 1 552 92 92 GLY HA3 H 3.913 0.03 1 553 92 92 GLY CA C 45.280 0.3 1 554 92 92 GLY N N 109.234 0.3 1 555 93 93 GLY H H 8.204 0.03 1 556 93 93 GLY HA3 H 3.923 0.03 1 557 93 93 GLY CA C 45.693 0.3 1 558 93 93 GLY N N 108.687 0.3 1 559 94 94 THR H H 8.047 0.03 1 560 94 94 THR HA H 4.272 0.03 1 561 94 94 THR HB H 4.136 0.03 1 562 94 94 THR HG2 H 1.127 0.03 1 563 94 94 THR CA C 62.193 0.3 1 564 94 94 THR CB C 69.755 0.3 1 565 94 94 THR CG2 C 21.631 0.3 1 566 94 94 THR N N 113.818 0.3 1 567 95 95 ARG H H 8.258 0.03 1 568 95 95 ARG HA H 4.251 0.03 1 569 95 95 ARG HB3 H 1.626 0.03 1 570 95 95 ARG HG3 H 1.373 0.03 1 571 95 95 ARG CA C 56.005 0.3 1 572 95 95 ARG CB C 30.568 0.3 1 573 95 95 ARG CG C 27.130 0.3 1 574 95 95 ARG N N 122.910 0.3 1 575 96 96 PHE H H 8.174 0.03 1 576 96 96 PHE HA H 4.539 0.03 1 577 96 96 PHE HB2 H 3.087 0.03 1 578 96 96 PHE HB3 H 2.953 0.03 1 579 96 96 PHE CA C 58.068 0.3 1 580 96 96 PHE CB C 39.506 0.3 1 581 96 96 PHE N N 120.905 0.3 1 582 97 97 ARG H H 8.131 0.03 1 583 97 97 ARG HA H 4.247 0.03 1 584 97 97 ARG HB3 H 1.649 0.03 1 585 97 97 ARG HG3 H 1.430 0.03 1 586 97 97 ARG CA C 56.005 0.3 1 587 97 97 ARG CB C 31.255 0.3 1 588 97 97 ARG CG C 27.130 0.3 1 589 97 97 ARG N N 122.035 0.3 1 590 98 98 ASP H H 8.255 0.03 1 591 98 98 ASP HA H 4.589 0.03 1 592 98 98 ASP HB3 H 2.609 0.03 1 593 98 98 ASP CA C 54.630 0.3 1 594 98 98 ASP CB C 41.568 0.3 1 595 98 98 ASP N N 121.296 0.3 1 596 99 99 THR H H 7.974 0.03 1 597 99 99 THR HA H 4.224 0.03 1 598 99 99 THR HB H 4.225 0.03 1 599 99 99 THR HG2 H 1.166 0.03 1 600 99 99 THR CA C 62.193 0.3 1 601 99 99 THR CB C 69.755 0.3 1 602 99 99 THR CG2 C 21.631 0.3 1 603 99 99 THR N N 113.860 0.3 1 604 100 100 ALA H H 8.200 0.03 1 605 100 100 ALA HA H 4.239 0.03 1 606 100 100 ALA HB H 1.245 0.03 1 607 100 100 ALA CA C 52.568 0.3 1 608 100 100 ALA CB C 19.049 0.3 1 609 100 100 ALA N N 125.807 0.3 1 610 101 101 VAL H H 7.819 0.03 1 611 101 101 VAL HA H 4.006 0.03 1 612 101 101 VAL HB H 1.952 0.03 1 613 101 101 VAL HG2 H 0.779 0.03 1 614 101 101 VAL CA C 62.193 0.3 1 615 101 101 VAL CB C 32.630 0.3 1 616 101 101 VAL CG2 C 20.943 0.3 1 617 101 101 VAL N N 118.025 0.3 1 618 102 102 TRP H H 8.043 0.03 1 619 102 102 TRP HA H 4.659 0.03 1 620 102 102 TRP HB3 H 3.127 0.03 1 621 102 102 TRP HE1 H 10.041 0.03 1 622 102 102 TRP CA C 56.693 0.3 1 623 102 102 TRP CB C 29.880 0.3 1 624 102 102 TRP N N 124.248 0.3 1 625 102 102 TRP NE1 N 130.145 0.3 1 626 103 103 LEU H H 7.771 0.03 1 627 103 103 LEU HA H 4.498 0.03 1 628 103 103 LEU HB3 H 1.397 0.03 1 629 103 103 LEU HG H 1.422 0.03 1 630 103 103 LEU HD1 H 0.770 0.03 1 631 103 103 LEU CA C 52.568 0.3 1 632 103 103 LEU CB C 42.256 0.3 1 633 103 103 LEU CG C 27.130 0.3 1 634 103 103 LEU CD1 C 24.380 0.3 1 635 103 103 LEU N N 125.605 0.3 1 636 104 104 PRO HA H 4.189 0.03 1 637 104 104 PRO HB3 H 2.226 0.03 1 638 104 104 PRO CA C 62.881 0.3 1 639 104 104 PRO CB C 31.943 0.3 1 640 105 105 ARG H H 8.341 0.03 1 641 105 105 ARG HA H 4.289 0.03 1 642 105 105 ARG HB2 H 1.801 0.03 1 643 105 105 ARG HB3 H 1.740 0.03 1 644 105 105 ARG HG2 H 1.626 0.03 1 645 105 105 ARG HG3 H 1.566 0.03 1 646 105 105 ARG CA C 56.005 0.3 1 647 105 105 ARG CB C 31.255 0.3 1 648 105 105 ARG CG C 27.130 0.3 1 649 105 105 ARG N N 120.691 0.3 1 650 106 106 SER H H 8.259 0.03 1 651 106 106 SER HA H 4.367 0.03 1 652 106 106 SER HB3 H 3.833 0.03 1 653 106 106 SER CA C 58.756 0.3 1 654 106 106 SER CB C 63.568 0.3 1 655 106 106 SER N N 116.760 0.3 1 656 107 107 LYS H H 8.342 0.03 1 657 107 107 LYS HA H 4.234 0.03 1 658 107 107 LYS HB3 H 1.740 0.03 1 659 107 107 LYS CA C 56.330 0.3 1 660 107 107 LYS CB C 33.318 0.3 1 661 107 107 LYS N N 122.742 0.3 1 662 108 108 ASP H H 8.169 0.03 1 663 108 108 ASP HA H 4.535 0.03 1 664 108 108 ASP HB2 H 2.499 0.03 1 665 108 108 ASP HB3 H 2.733 0.03 1 666 108 108 ASP CA C 54.630 0.3 1 667 108 108 ASP CB C 40.881 0.3 1 668 108 108 ASP N N 120.717 0.3 1 669 109 109 LEU H H 8.037 0.03 1 670 109 109 LEU HA H 4.245 0.03 1 671 109 109 LEU HB3 H 1.580 0.03 1 672 109 109 LEU HG H 1.559 0.03 1 673 109 109 LEU HD1 H 0.855 0.03 1 674 109 109 LEU CA C 55.318 0.3 1 675 109 109 LEU CB C 42.256 0.3 1 676 109 109 LEU CG C 27.130 0.3 1 677 109 109 LEU CD1 C 24.473 0.3 1 678 109 109 LEU N N 122.580 0.3 1 679 110 110 LYS H H 8.211 0.03 1 680 110 110 LYS HA H 4.194 0.03 1 681 110 110 LYS HB3 H 1.713 0.03 1 682 110 110 LYS HG3 H 1.335 0.03 1 683 110 110 LYS CA C 56.696 0.3 1 684 110 110 LYS CB C 32.630 0.3 1 685 110 110 LYS CG C 25.068 0.3 1 686 110 110 LYS N N 121.500 0.3 1 687 112 112 PRO HA H 4.315 0.03 1 688 112 112 PRO CA C 63.568 0.3 1 689 113 113 GLY H H 8.431 0.03 1 690 113 113 GLY HA3 H 3.917 0.03 1 691 113 113 GLY CA C 45.006 0.3 1 692 113 113 GLY N N 109.268 0.3 1 693 114 114 ALA H H 8.054 0.03 1 694 114 114 ALA HA H 4.272 0.03 1 695 114 114 ALA HB H 1.341 0.03 1 696 114 114 ALA CA C 52.568 0.3 1 697 114 114 ALA CB C 19.568 0.3 1 698 114 114 ALA N N 123.590 0.3 1 699 115 115 ARG H H 8.293 0.03 1 700 115 115 ARG HA H 4.273 0.03 1 701 115 115 ARG HB3 H 1.748 0.03 1 702 115 115 ARG HG3 H 1.587 0.03 1 703 115 115 ARG CA C 56.005 0.3 1 704 115 115 ARG CB C 31.255 0.3 1 705 115 115 ARG CG C 26.443 0.3 1 706 115 115 ARG N N 120.563 0.3 1 707 116 116 LYS H H 8.384 0.03 1 708 116 116 LYS HA H 4.274 0.03 1 709 116 116 LYS HB3 H 1.729 0.03 1 710 116 116 LYS CA C 56.394 0.3 1 711 116 116 LYS CB C 32.930 0.3 1 712 116 116 LYS N N 123.856 0.3 1 713 117 117 GLN H H 7.993 0.03 1 714 117 117 GLN HA H 4.140 0.03 1 715 117 117 GLN HB3 H 1.887 0.03 1 716 117 117 GLN HG3 H 1.795 0.03 1 717 117 117 GLN HE21 H 7.502 0.03 1 718 117 117 GLN CA C 57.381 0.3 1 719 117 117 GLN CB C 30.568 0.3 1 720 117 117 GLN CG C 33.318 0.3 1 721 117 117 GLN CD C 6.789 0.03 1 722 117 117 GLN N N 126.988 0.3 1 723 117 117 GLN NE2 N 112.156 0.3 1 stop_ save_