data_4280 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence Specific 1H, 13C and 15N Assignment of the Methyl Binding Domain of the Methyl-CpG-binding Protein MeCP2. ; _BMRB_accession_number 4280 _BMRB_flat_file_name bmr4280.str _Entry_type original _Submission_date 1998-11-23 _Accession_date 1998-11-23 _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 Wakefield Robert I. D. 2 Smith Brian O. . 3 Nan Xinsheng . . 4 Free Andrew . . 5 Soteriou Alice . . 6 Uhrin Dusan . . 7 Bird Adrian P. . 8 Barlow Paul N. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 544 "13C chemical shifts" 291 "15N chemical shifts" 91 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-10-06 original author . stop_ _Original_release_date 1999-10-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Wakefield R.I.D., Smith B.O., Nan X.S., Free A., Soteriou A., Uhrin D., Bird A.P., and Barlow P.N., "The solution structure of the domain from MeCP2 that binds to methylated DNA", J. Mol. Biol. 291, 1055-1065 (1999). ; _Citation_title 'The solution structure of the domain from MeCP2 that binds to methylated DNA' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wakefield Robert I. D. 2 Smith Brian O. . 3 Nan Xinsheng . . 4 Free Andrew . . 5 Soteriou Alice . . 6 Uhrin Dusan . . 7 Bird Adrian P. . 8 Barlow Paul N. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 291 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1055 _Page_last 1065 _Year 1999 _Details . loop_ _Keyword MBD 'mCpG islands' MeCP2 'Methylated DNA' 'Methyl binding domain' 'NMR assignments' stop_ save_ ################################## # Molecular system description # ################################## save_system_MBD _Saveframe_category molecular_system _Mol_system_name 'Methyl binding domain of MeCP2' _Abbreviation_common MBD _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label MBD $MBD stop_ _System_molecular_weight 11400 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MBD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Methyl binding domain of MeCP2' _Abbreviation_common MBD _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 92 _Mol_residue_sequence ; ASASPKQRRSIIRDRGPMYD DPTLPEGWTRKLKQRKSGRS AGKYDVYLINPQGKAFRSKV ELIAYFEKVGDTSLDPNDFD FTVTGRGSGSGC ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 77 ALA 2 78 SER 3 79 ALA 4 80 SER 5 81 PRO 6 82 LYS 7 83 GLN 8 84 ARG 9 85 ARG 10 86 SER 11 87 ILE 12 88 ILE 13 89 ARG 14 90 ASP 15 91 ARG 16 92 GLY 17 93 PRO 18 94 MET 19 95 TYR 20 96 ASP 21 97 ASP 22 98 PRO 23 99 THR 24 100 LEU 25 101 PRO 26 102 GLU 27 103 GLY 28 104 TRP 29 105 THR 30 106 ARG 31 107 LYS 32 108 LEU 33 109 LYS 34 110 GLN 35 111 ARG 36 112 LYS 37 113 SER 38 114 GLY 39 115 ARG 40 116 SER 41 117 ALA 42 118 GLY 43 119 LYS 44 120 TYR 45 121 ASP 46 122 VAL 47 123 TYR 48 124 LEU 49 125 ILE 50 126 ASN 51 127 PRO 52 128 GLN 53 129 GLY 54 130 LYS 55 131 ALA 56 132 PHE 57 133 ARG 58 134 SER 59 135 LYS 60 136 VAL 61 137 GLU 62 138 LEU 63 139 ILE 64 140 ALA 65 141 TYR 66 142 PHE 67 143 GLU 68 144 LYS 69 145 VAL 70 146 GLY 71 147 ASP 72 148 THR 73 149 SER 74 150 LEU 75 151 ASP 76 152 PRO 77 153 ASN 78 154 ASP 79 155 PHE 80 156 ASP 81 157 PHE 82 158 THR 83 159 VAL 84 160 THR 85 161 GLY 86 162 ARG 87 163 GLY 88 164 SER 89 165 GLY 90 166 SER 91 167 GLY 92 168 CYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-06 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 4467 "Methyl-CpG-binding protein, attachment region binding protein" 97.83 125 98.89 98.89 6.60e-56 PDB 1QK9 "The Solution Structure Of The Domain From Mecp2 That Binds To Methylated Dna" 100.00 92 100.00 100.00 2.23e-59 PDB 1UB1 "Solution Structure Of The Matrix Attachment Region-Binding Domain Of Chicken Mecp2" 97.83 133 98.89 98.89 2.34e-56 DBJ BAE34602 "unnamed protein product [Mus musculus]" 97.83 501 98.89 98.89 9.53e-55 DBJ BAF82133 "unnamed protein product [Homo sapiens]" 97.83 486 98.89 98.89 6.78e-55 DBJ BAG73396 "methyl CpG binding protein 2 [synthetic construct]" 97.83 486 98.89 98.89 6.57e-55 EMBL CAA61599 "methyl CpG binding protein 2 [Homo sapiens]" 97.83 476 98.89 98.89 5.35e-55 EMBL CAA64331 "methyl-CpG-binding protein [Homo sapiens]" 97.83 477 98.89 98.89 4.51e-55 EMBL CAA68001 "methyl-CpG-binding protein 2 [Homo sapiens]" 97.83 486 98.89 98.89 6.50e-55 EMBL CAA73190 "methyl-CpG binding protein 2 [Homo sapiens]" 97.83 486 98.89 98.89 6.57e-55 EMBL CAA74577 "attachment region binding protein, partial [Gallus gallus]" 95.65 344 100.00 100.00 3.08e-56 GB AAA41584 "MeCP-2 [Rattus norvegicus]" 97.83 492 98.89 98.89 7.10e-55 GB AAC08757 "Methyl-CpG binding protein 2 [Homo sapiens]" 97.83 486 98.89 98.89 6.57e-55 GB AAC32737 "methyl-CpG-binding protein [Homo sapiens]" 97.83 486 98.89 98.89 6.57e-55 GB AAC68880 "methyl-CpG binding protein 2 [Mus musculus]" 97.83 484 98.89 98.89 8.60e-55 GB AAF33023 "methyl CpG binding protein 2 [Homo sapiens]" 97.83 486 98.89 98.89 6.57e-55 PIR S57963 "methyl CpG binding protein 2 - human (fragment)" 97.83 476 98.89 98.89 5.35e-55 REF NP_001075448 "methyl-CpG-binding protein 2 isoform 1 [Mus musculus]" 97.83 501 98.89 98.89 9.14e-55 REF NP_001104262 "methyl-CpG-binding protein 2 isoform 2 [Homo sapiens]" 97.83 498 98.89 98.89 6.33e-55 REF NP_001164841 "methyl-CpG-binding protein 2 [Oryctolagus cuniculus]" 97.83 497 98.89 98.89 6.42e-55 REF NP_001193481 "methyl-CpG-binding protein 2 [Bos taurus]" 97.83 486 98.89 98.89 5.05e-55 REF NP_001244471 "methyl-CpG-binding protein 2 [Macaca mulatta]" 97.83 486 98.89 98.89 6.44e-55 SP P51608 "RecName: Full=Methyl-CpG-binding protein 2; Short=MeCp-2 protein; Short=MeCp2" 97.83 486 98.89 98.89 6.57e-55 SP Q00566 "RecName: Full=Methyl-CpG-binding protein 2; Short=MeCp-2 protein; Short=MeCp2" 97.83 492 98.89 98.89 7.10e-55 SP Q95LG8 "RecName: Full=Methyl-CpG-binding protein 2; Short=MeCp-2 protein; Short=MeCp2" 97.83 486 98.89 98.89 6.44e-55 SP Q9Z2D6 "RecName: Full=Methyl-CpG-binding protein 2; Short=MeCp-2 protein; Short=MeCp2" 97.83 484 98.89 98.89 8.60e-55 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MBD human 9606 Eucaryota 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_type _Vector_name $MBD 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3)LysS plasmid pEH6HMBD stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MBD 1.0 mM '[U-15N; U-13C]' H2O 90 % . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 . n/a temperature 291 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 H2O C 13 protons ppm 0.00 internal indirect . . . 0.25144953 H2O H 1 protons ppm 4.78 internal direct . . . . H2O N 15 protons ppm 0.00 internal indirect . . . 0.10132905 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_chemical_shifts_ _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name MBD _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 . 1 ALA H H 8.366 0.014 1 2 . 1 ALA HA H 4.262 0.069 1 3 . 1 ALA HB H 1.328 0.026 1 4 . 1 ALA CA C 52.807 0.046 1 5 . 1 ALA CB C 19.422 0.005 1 6 . 1 ALA N N 125.592 0.000 1 7 . 2 SER H H 8.248 0.027 1 8 . 2 SER HA H 4.342 0.057 1 9 . 2 SER HB2 H 3.784 0.049 1 10 . 2 SER HB3 H 3.784 0.049 1 11 . 2 SER CA C 58.347 0.009 1 12 . 2 SER CB C 63.981 0.041 1 13 . 2 SER N N 114.940 0.000 1 14 . 3 ALA H H 8.271 0.029 1 15 . 3 ALA HA H 4.302 0.075 1 16 . 3 ALA HB H 1.316 0.044 1 17 . 3 ALA CA C 52.414 0.091 1 18 . 3 ALA CB C 19.681 0.002 1 19 . 3 ALA N N 125.752 0.000 1 20 . 4 SER H H 8.271 0.014 1 21 . 4 SER HA H 4.713 0.002 1 22 . 4 SER HB2 H 3.848 0.000 1 23 . 4 SER HB3 H 3.848 0.000 1 24 . 4 SER CA C 56.592 0.091 1 25 . 4 SER N N 116.632 0.000 1 26 . 5 PRO HA H 4.342 0.068 1 27 . 5 PRO HB2 H 2.275 0.032 2 28 . 5 PRO HB3 H 1.880 0.031 2 29 . 5 PRO HG2 H 2.007 0.010 1 30 . 5 PRO HG3 H 2.007 0.010 1 31 . 5 PRO HD2 H 3.810 0.019 2 32 . 5 PRO HD3 H 3.706 0.025 2 33 . 5 PRO CA C 63.692 0.004 1 34 . 5 PRO CB C 32.282 0.018 1 35 . 5 PRO CG C 27.620 0.000 1 36 . 5 PRO CD C 50.882 0.000 1 37 . 6 LYS H H 8.316 0.024 1 38 . 6 LYS HA H 4.182 0.036 1 39 . 6 LYS HB2 H 1.790 0.013 2 40 . 6 LYS HB3 H 1.732 0.011 2 41 . 6 LYS HG2 H 1.443 0.000 2 42 . 6 LYS HG3 H 1.415 0.000 2 43 . 6 LYS HD2 H 1.664 0.004 1 44 . 6 LYS HD3 H 1.664 0.004 1 45 . 6 LYS HE2 H 2.994 0.036 1 46 . 6 LYS HE3 H 2.994 0.036 1 47 . 6 LYS CA C 56.811 0.025 1 48 . 6 LYS CB C 33.074 0.021 1 49 . 6 LYS CG C 25.141 0.000 1 50 . 6 LYS CD C 29.430 0.000 1 51 . 6 LYS CE C 42.337 0.000 1 52 . 6 LYS N N 120.748 0.000 1 53 . 7 GLN H H 8.255 0.028 1 54 . 7 GLN HA H 4.222 0.030 1 55 . 7 GLN HB2 H 1.978 0.037 2 56 . 7 GLN HB3 H 1.969 0.022 2 57 . 7 GLN HG2 H 2.343 0.017 1 58 . 7 GLN HG3 H 2.343 0.017 1 59 . 7 GLN CA C 56.033 0.002 1 60 . 7 GLN CB C 29.757 0.016 1 61 . 7 GLN CG C 34.023 0.000 1 62 . 7 GLN N N 121.008 0.000 1 63 . 8 ARG H H 8.388 0.023 1 64 . 8 ARG HA H 4.238 0.003 1 65 . 8 ARG HB2 H 1.756 0.009 1 66 . 8 ARG HB3 H 1.756 0.009 1 67 . 8 ARG HG2 H 1.575 0.207 1 68 . 8 ARG HG3 H 1.575 0.207 1 69 . 8 ARG HD2 H 3.177 0.020 1 70 . 8 ARG HD3 H 3.177 0.020 1 71 . 8 ARG CA C 56.445 0.085 1 72 . 8 ARG CB C 30.970 0.035 1 73 . 8 ARG CG C 27.162 0.000 1 74 . 8 ARG CD C 43.501 0.000 1 75 . 8 ARG N N 122.827 0.000 1 76 . 9 ARG H H 8.403 0.044 1 77 . 9 ARG HA H 4.302 0.032 1 78 . 9 ARG HB2 H 1.777 0.005 1 79 . 9 ARG HB3 H 1.777 0.005 1 80 . 9 ARG HG2 H 1.622 0.011 1 81 . 9 ARG HG3 H 1.622 0.011 1 82 . 9 ARG HD2 H 3.185 0.012 1 83 . 9 ARG HD3 H 3.185 0.012 1 84 . 9 ARG CA C 56.345 0.046 1 85 . 9 ARG CB C 31.143 0.060 1 86 . 9 ARG CG C 27.358 0.000 1 87 . 9 ARG CD C 43.506 0.000 1 88 . 9 ARG N N 122.363 0.000 1 89 . 10 SER H H 8.362 0.033 1 90 . 10 SER HA H 4.382 0.000 1 91 . 10 SER HB2 H 3.784 0.000 1 92 . 10 SER HB3 H 3.784 0.000 1 93 . 10 SER CA C 58.429 0.076 1 94 . 10 SER CB C 63.937 0.044 1 95 . 10 SER N N 117.356 0.000 1 96 . 11 ILE H H 8.159 0.012 1 97 . 11 ILE HA H 4.143 0.035 1 98 . 11 ILE HB H 1.794 0.053 1 99 . 11 ILE HG12 H 1.419 0.007 2 100 . 11 ILE HG13 H 1.147 0.015 2 101 . 11 ILE HG2 H 0.825 0.000 1 102 . 11 ILE HD1 H 0.830 0.023 1 103 . 11 ILE CA C 61.335 0.059 1 104 . 11 ILE CB C 38.912 0.005 1 105 . 11 ILE CG1 C 27.543 0.000 1 106 . 11 ILE CG2 C 17.768 0.000 1 107 . 11 ILE CD1 C 13.298 0.000 1 108 . 11 ILE N N 122.583 0.000 1 109 . 12 ILE H H 8.194 0.014 1 110 . 12 ILE HA H 4.063 0.040 1 111 . 12 ILE HB H 1.754 0.077 1 112 . 12 ILE HG12 H 1.458 0.005 2 113 . 12 ILE HG13 H 1.156 0.012 2 114 . 12 ILE HG2 H 0.857 0.005 1 115 . 12 ILE HD1 H 0.814 0.007 1 116 . 12 ILE CA C 61.217 0.019 1 117 . 12 ILE CB C 38.510 0.031 1 118 . 12 ILE CG1 C 27.595 0.000 1 119 . 12 ILE CG2 C 17.763 0.000 1 120 . 12 ILE CD1 C 12.854 0.000 1 121 . 12 ILE N N 125.264 0.000 1 122 . 13 ARG H H 8.365 0.018 1 123 . 13 ARG HA H 4.302 0.044 1 124 . 13 ARG HB2 H 1.810 0.039 2 125 . 13 ARG HB3 H 1.739 0.028 2 126 . 13 ARG HG2 H 1.578 0.049 1 127 . 13 ARG HG3 H 1.578 0.049 1 128 . 13 ARG HD2 H 3.098 0.098 1 129 . 13 ARG HD3 H 3.098 0.098 1 130 . 13 ARG CA C 56.154 0.011 1 131 . 13 ARG CB C 31.217 0.000 1 132 . 13 ARG CG C 27.161 0.000 1 133 . 13 ARG CD C 43.488 0.000 1 134 . 13 ARG N N 125.633 0.000 1 135 . 14 ASP H H 8.307 0.029 1 136 . 14 ASP HA H 4.541 0.051 1 137 . 14 ASP HB2 H 2.628 0.000 2 138 . 14 ASP HB3 H 2.549 0.000 2 139 . 14 ASP CA C 54.474 0.005 1 140 . 14 ASP CB C 41.309 0.043 1 141 . 14 ASP N N 121.543 0.050 1 142 . 15 ARG H H 8.307 0.025 1 143 . 15 ARG HA H 4.307 0.029 1 144 . 15 ARG HB2 H 1.906 0.022 2 145 . 15 ARG HB3 H 1.707 0.006 2 146 . 15 ARG HG2 H 1.657 0.008 1 147 . 15 ARG HG3 H 1.657 0.008 1 148 . 15 ARG HD2 H 3.167 0.024 1 149 . 15 ARG HD3 H 3.167 0.024 1 150 . 15 ARG CA C 56.290 0.047 1 151 . 15 ARG CB C 31.173 0.011 1 152 . 15 ARG CG C 27.356 0.000 1 153 . 15 ARG CD C 43.568 0.000 1 154 . 15 ARG N N 121.243 0.060 1 155 . 16 GLY H H 8.308 0.042 1 156 . 16 GLY HA2 H 4.076 0.049 2 157 . 16 GLY HA3 H 3.923 0.039 2 158 . 16 GLY CA C 44.510 0.000 1 159 . 16 GLY N N 109.591 0.000 1 160 . 17 PRO HA H 3.620 0.005 1 161 . 17 PRO HB2 H 1.159 0.003 2 162 . 17 PRO HB3 H 0.777 0.008 2 163 . 17 PRO HG2 H 1.590 0.000 2 164 . 17 PRO HG3 H 1.417 0.000 2 165 . 17 PRO HD2 H 3.452 0.000 1 166 . 17 PRO HD3 H 3.452 0.000 1 167 . 17 PRO CA C 62.871 0.000 1 168 . 17 PRO CB C 32.000 0.020 1 169 . 17 PRO CG C 27.183 0.000 1 170 . 17 PRO CD C 49.740 0.000 1 171 . 18 MET H H 8.296 0.022 1 172 . 18 MET HA H 4.306 0.009 1 173 . 18 MET HB2 H 2.078 0.002 1 174 . 18 MET HB3 H 2.078 0.002 1 175 . 18 MET HE H 1.807 0.025 1 176 . 18 MET CA C 55.348 0.776 1 177 . 18 MET CB C 32.564 0.281 1 178 . 18 MET CE C 17.011 0.297 1 179 . 18 MET N N 122.540 0.000 1 180 . 19 TYR H H 7.942 0.037 1 181 . 19 TYR HA H 4.111 0.017 1 182 . 19 TYR HB2 H 3.086 0.000 2 183 . 19 TYR HB3 H 2.690 0.036 2 184 . 19 TYR HD1 H 7.154 0.009 1 185 . 19 TYR HD2 H 7.154 0.009 1 186 . 19 TYR HE1 H 6.675 0.017 1 187 . 19 TYR HE2 H 6.675 0.017 1 188 . 19 TYR CA C 61.244 0.000 1 189 . 19 TYR CB C 39.111 0.024 1 190 . 19 TYR CD1 C 133.032 0.069 1 191 . 19 TYR CE1 C 117.771 0.040 1 192 . 19 TYR N N 119.938 0.092 1 193 . 20 ASP H H 7.582 0.044 1 194 . 20 ASP HA H 4.868 0.016 1 195 . 20 ASP HB2 H 2.614 0.030 2 196 . 20 ASP HB3 H 2.438 0.017 2 197 . 20 ASP CA C 52.863 0.152 1 198 . 20 ASP CB C 44.169 0.274 1 199 . 20 ASP N N 115.810 0.000 1 200 . 21 ASP H H 8.745 0.036 1 201 . 21 ASP HA H 5.250 0.004 1 202 . 21 ASP CA C 50.335 0.000 1 203 . 21 ASP CB C 42.553 0.000 1 204 . 21 ASP N N 118.850 0.000 1 205 . 22 PRO HA H 4.564 0.046 1 206 . 22 PRO HB2 H 2.320 0.037 2 207 . 22 PRO HB3 H 2.011 0.037 2 208 . 22 PRO HG2 H 2.027 0.017 2 209 . 22 PRO HG3 H 1.900 0.019 2 210 . 22 PRO HD2 H 4.011 0.000 2 211 . 22 PRO HD3 H 3.671 0.000 2 212 . 22 PRO CA C 63.700 0.053 1 213 . 22 PRO CB C 32.561 0.048 1 214 . 22 PRO CG C 26.797 0.000 1 215 . 22 PRO CD C 51.345 0.000 1 216 . 23 THR H H 8.321 0.000 1 217 . 23 THR HA H 4.238 0.086 1 218 . 23 THR HB H 4.211 0.089 1 219 . 23 THR HG2 H 1.112 0.005 1 220 . 23 THR CA C 62.351 0.023 1 221 . 23 THR CB C 69.190 0.042 1 222 . 23 THR CG2 C 21.880 0.000 1 223 . 23 THR N N 110.323 0.226 1 224 . 24 LEU H H 6.906 0.031 1 225 . 24 LEU HA H 4.056 0.048 1 226 . 24 LEU HB2 H 1.623 0.019 2 227 . 24 LEU HB3 H 1.361 0.002 2 228 . 24 LEU HG H 1.615 0.010 1 229 . 24 LEU HD1 H 1.039 0.010 1 230 . 24 LEU HD2 H 0.826 0.018 1 231 . 24 LEU CA C 53.586 0.307 1 232 . 24 LEU CB C 42.101 0.140 1 233 . 24 LEU CG C 27.527 0.027 1 234 . 24 LEU CD1 C 26.667 0.022 1 235 . 24 LEU CD2 C 24.891 0.000 1 236 . 24 LEU N N 123.981 0.000 1 237 . 25 PRO HA H 4.297 0.009 1 238 . 25 PRO HB2 H 1.944 0.013 2 239 . 25 PRO HB3 H 1.757 0.002 2 240 . 25 PRO HG2 H 2.444 0.007 1 241 . 25 PRO HG3 H 2.444 0.007 1 242 . 25 PRO HD2 H 3.143 0.053 1 243 . 25 PRO HD3 H 3.143 0.053 1 244 . 25 PRO CA C 62.364 0.025 1 245 . 25 PRO CB C 31.416 0.399 1 246 . 25 PRO CG C 27.774 0.000 1 247 . 25 PRO CD C 50.014 0.000 1 248 . 26 GLU H H 8.357 0.039 1 249 . 26 GLU HA H 4.060 0.026 1 250 . 26 GLU HB2 H 2.060 0.002 2 251 . 26 GLU HB3 H 1.950 0.000 2 252 . 26 GLU HG2 H 2.294 0.000 1 253 . 26 GLU HG3 H 2.294 0.000 1 254 . 26 GLU CA C 58.518 0.008 1 255 . 26 GLU CB C 29.901 0.004 1 256 . 26 GLU CG C 36.098 0.000 1 257 . 26 GLU N N 120.503 0.000 1 258 . 27 GLY H H 8.884 0.019 1 259 . 27 GLY HA2 H 4.322 0.041 2 260 . 27 GLY HA3 H 3.671 0.046 2 261 . 27 GLY CA C 45.679 0.027 1 262 . 27 GLY N N 114.206 0.000 1 263 . 28 TRP H H 8.437 0.027 1 264 . 28 TRP HA H 5.156 0.029 1 265 . 28 TRP HB2 H 3.460 0.048 2 266 . 28 TRP HB3 H 3.183 0.005 2 267 . 28 TRP HD1 H 7.237 0.001 1 268 . 28 TRP HE1 H 10.715 0.018 1 269 . 28 TRP HE3 H 7.383 0.007 1 270 . 28 TRP HZ2 H 7.766 0.011 1 271 . 28 TRP HZ3 H 6.680 0.004 1 272 . 28 TRP HH2 H 6.639 0.002 1 273 . 28 TRP CA C 57.648 0.063 1 274 . 28 TRP CB C 30.161 0.232 1 275 . 28 TRP N N 122.021 0.000 1 276 . 28 TRP NE1 N 130.966 0.000 1 277 . 29 THR H H 9.146 0.026 1 278 . 29 THR HA H 4.672 0.055 1 279 . 29 THR HB H 4.027 0.066 1 280 . 29 THR HG2 H 1.125 0.031 1 281 . 29 THR CA C 61.080 0.088 1 282 . 29 THR CB C 72.998 0.014 1 283 . 29 THR CG2 C 22.538 0.000 1 284 . 29 THR N N 112.845 0.000 1 285 . 30 ARG H H 8.355 0.037 1 286 . 30 ARG HA H 5.425 0.015 1 287 . 30 ARG HB2 H 1.859 0.048 2 288 . 30 ARG HB3 H 1.671 0.003 2 289 . 30 ARG HG2 H 1.490 0.059 1 290 . 30 ARG HG3 H 1.490 0.059 1 291 . 30 ARG HD2 H 3.097 0.021 1 292 . 30 ARG HD3 H 3.097 0.021 1 293 . 30 ARG HE H 7.160 0.000 1 294 . 30 ARG CA C 54.461 0.698 1 295 . 30 ARG CB C 34.019 0.230 1 296 . 30 ARG CG C 27.425 0.000 1 297 . 30 ARG CD C 44.096 0.404 1 298 . 30 ARG N N 120.224 0.000 1 299 . 31 LYS H H 9.430 0.030 1 300 . 31 LYS HA H 4.827 0.013 1 301 . 31 LYS HB2 H 1.709 0.000 2 302 . 31 LYS HB3 H 1.559 0.000 2 303 . 31 LYS HG2 H 1.305 0.000 1 304 . 31 LYS HG3 H 1.305 0.000 1 305 . 31 LYS HE2 H 2.828 0.000 1 306 . 31 LYS HE3 H 2.828 0.000 1 307 . 31 LYS CA C 54.864 0.194 1 308 . 31 LYS CB C 36.365 0.004 1 309 . 31 LYS CG C 25.170 0.000 1 310 . 31 LYS CE C 42.172 0.000 1 311 . 31 LYS N N 124.818 0.000 1 312 . 32 LEU H H 9.036 0.027 1 313 . 32 LEU HA H 5.317 0.049 1 314 . 32 LEU HB2 H 1.623 0.051 2 315 . 32 LEU HB3 H 1.448 0.055 2 316 . 32 LEU HG H 1.521 0.047 1 317 . 32 LEU HD1 H 0.514 0.027 1 318 . 32 LEU HD2 H 0.452 0.026 1 319 . 32 LEU CA C 54.174 0.013 1 320 . 32 LEU CB C 43.725 0.066 1 321 . 32 LEU CG C 29.525 0.000 1 322 . 32 LEU CD1 C 25.799 0.089 1 323 . 32 LEU CD2 C 25.900 0.006 1 324 . 32 LEU N N 126.009 0.000 1 325 . 33 LYS H H 8.964 0.028 1 326 . 33 LYS HA H 4.802 0.043 1 327 . 33 LYS HB2 H 1.938 0.031 2 328 . 33 LYS HB3 H 1.718 0.003 2 329 . 33 LYS HG2 H 1.330 0.000 1 330 . 33 LYS HG3 H 1.330 0.000 1 331 . 33 LYS HD2 H 1.551 0.000 1 332 . 33 LYS HD3 H 1.551 0.000 1 333 . 33 LYS HE2 H 2.725 0.000 1 334 . 33 LYS HE3 H 2.725 0.000 1 335 . 33 LYS CA C 55.068 0.185 1 336 . 33 LYS CB C 36.084 0.020 1 337 . 33 LYS CG C 25.182 0.000 1 338 . 33 LYS CD C 29.540 0.000 1 339 . 33 LYS CE C 42.058 0.000 1 340 . 33 LYS N N 122.379 0.000 1 341 . 34 GLN H H 9.189 0.036 1 342 . 34 GLN HA H 4.191 0.051 1 343 . 34 GLN HB2 H 1.827 0.000 2 344 . 34 GLN HB3 H 1.624 0.000 2 345 . 34 GLN HG2 H 1.880 0.064 2 346 . 34 GLN HG3 H 1.559 0.029 2 347 . 34 GLN HE21 H 7.198 0.040 2 348 . 34 GLN HE22 H 6.817 0.040 2 349 . 34 GLN CA C 56.058 0.010 1 350 . 34 GLN CB C 30.062 0.041 1 351 . 34 GLN CG C 34.223 0.000 1 352 . 34 GLN N N 127.195 0.000 1 353 . 34 GLN NE2 N 111.533 0.002 1 354 . 35 ARG H H 8.775 0.041 1 355 . 35 ARG HA H 4.262 0.079 1 356 . 35 ARG HB2 H 1.825 0.027 2 357 . 35 ARG HB3 H 1.750 0.010 2 358 . 35 ARG HG2 H 1.625 0.021 1 359 . 35 ARG HG3 H 1.625 0.021 1 360 . 35 ARG HD2 H 3.176 0.026 1 361 . 35 ARG HD3 H 3.176 0.026 1 362 . 35 ARG HE H 7.195 0.000 1 363 . 35 ARG CA C 56.529 0.252 1 364 . 35 ARG CB C 30.906 0.022 1 365 . 35 ARG CD C 43.319 0.000 1 366 . 35 ARG N N 126.812 0.000 1 367 . 36 LYS H H 8.849 0.066 1 368 . 36 LYS HA H 4.310 0.017 1 369 . 36 LYS HB2 H 1.861 0.010 2 370 . 36 LYS HB3 H 1.696 0.000 2 371 . 36 LYS HG2 H 1.394 0.000 1 372 . 36 LYS HG3 H 1.394 0.000 1 373 . 36 LYS HD2 H 1.647 0.000 1 374 . 36 LYS HD3 H 1.647 0.000 1 375 . 36 LYS HE2 H 2.953 0.000 1 376 . 36 LYS HE3 H 2.953 0.000 1 377 . 36 LYS CA C 56.757 0.127 1 378 . 36 LYS CB C 33.607 0.070 1 379 . 36 LYS CG C 24.935 0.700 1 380 . 36 LYS CD C 29.093 0.000 1 381 . 36 LYS CE C 42.226 0.000 1 382 . 36 LYS N N 123.883 0.000 1 383 . 37 SER H H 7.898 0.025 1 384 . 37 SER HA H 4.587 0.019 1 385 . 37 SER HB2 H 3.820 0.038 2 386 . 37 SER HB3 H 3.769 0.038 2 387 . 37 SER CA C 57.454 0.126 1 388 . 37 SER CB C 65.041 0.100 1 389 . 37 SER N N 113.778 0.000 1 390 . 38 GLY H H 8.586 0.034 1 391 . 38 GLY HA2 H 4.136 0.066 2 392 . 38 GLY HA3 H 3.877 0.026 2 393 . 38 GLY CA C 45.356 0.022 1 394 . 38 GLY N N 109.505 0.000 1 395 . 39 ARG H H 8.755 0.115 1 396 . 39 ARG HA H 4.167 0.066 1 397 . 39 ARG HB2 H 1.884 0.000 2 398 . 39 ARG HB3 H 1.836 0.000 2 399 . 39 ARG HG2 H 1.610 0.032 1 400 . 39 ARG HG3 H 1.610 0.032 1 401 . 39 ARG HD2 H 3.176 0.049 1 402 . 39 ARG HD3 H 3.176 0.049 1 403 . 39 ARG CA C 57.724 0.100 1 404 . 39 ARG CB C 30.056 0.022 1 405 . 39 ARG CG C 27.172 0.000 1 406 . 39 ARG CD C 43.161 0.000 1 407 . 39 ARG N N 120.824 0.000 1 408 . 40 SER H H 8.438 0.083 1 409 . 40 SER HA H 4.456 0.017 1 410 . 40 SER HB2 H 3.855 0.016 1 411 . 40 SER HB3 H 3.855 0.016 1 412 . 40 SER CA C 57.691 0.037 1 413 . 40 SER CB C 63.240 0.241 1 414 . 40 SER N N 114.535 0.000 1 415 . 41 ALA H H 7.587 0.054 1 416 . 41 ALA HA H 3.780 0.007 1 417 . 41 ALA HB H 1.202 0.020 1 418 . 41 ALA CA C 53.584 0.015 1 419 . 41 ALA CB C 18.596 0.013 1 420 . 41 ALA N N 123.106 0.000 1 421 . 42 GLY H H 8.495 0.030 1 422 . 42 GLY HA2 H 4.133 0.060 2 423 . 42 GLY HA3 H 3.614 0.048 2 424 . 42 GLY CA C 45.153 0.008 1 425 . 42 GLY N N 109.757 0.000 1 426 . 43 LYS H H 7.934 0.019 1 427 . 43 LYS HA H 4.351 0.016 1 428 . 43 LYS HB2 H 1.762 0.034 1 429 . 43 LYS HB3 H 1.762 0.034 1 430 . 43 LYS HG2 H 1.317 0.000 1 431 . 43 LYS HG3 H 1.317 0.000 1 432 . 43 LYS HD2 H 1.630 0.000 1 433 . 43 LYS HD3 H 1.630 0.000 1 434 . 43 LYS HE2 H 2.957 0.000 1 435 . 43 LYS HE3 H 2.957 0.000 1 436 . 43 LYS CA C 56.083 0.028 1 437 . 43 LYS CB C 33.898 0.017 1 438 . 43 LYS CG C 25.274 0.000 1 439 . 43 LYS CD C 29.538 0.000 1 440 . 43 LYS CE C 42.433 0.500 1 441 . 43 LYS N N 120.690 0.000 1 442 . 44 TYR H H 8.599 0.028 1 443 . 44 TYR HA H 4.931 0.049 1 444 . 44 TYR HB2 H 2.717 0.017 2 445 . 44 TYR HB3 H 2.596 0.013 2 446 . 44 TYR HD1 H 6.896 0.014 1 447 . 44 TYR HD2 H 6.896 0.014 1 448 . 44 TYR HE1 H 6.765 0.012 1 449 . 44 TYR HE2 H 6.765 0.012 1 450 . 44 TYR CA C 58.262 0.006 1 451 . 44 TYR CB C 41.559 0.000 1 452 . 44 TYR CD1 C 133.074 0.000 1 453 . 44 TYR CE1 C 117.913 0.347 1 454 . 44 TYR N N 118.729 0.000 1 455 . 45 ASP H H 8.924 0.035 1 456 . 45 ASP HA H 4.962 0.002 1 457 . 45 ASP HB2 H 2.591 0.039 2 458 . 45 ASP HB3 H 2.455 0.036 2 459 . 45 ASP CA C 53.921 0.044 1 460 . 45 ASP CB C 44.294 0.000 1 461 . 45 ASP N N 120.463 0.000 1 462 . 46 VAL H H 8.304 0.013 1 463 . 46 VAL HA H 4.325 0.045 1 464 . 46 VAL HB H 2.046 0.027 1 465 . 46 VAL HG1 H 0.734 0.000 1 466 . 46 VAL HG2 H 0.734 0.000 1 467 . 46 VAL CA C 62.575 0.037 1 468 . 46 VAL CB C 33.604 0.079 1 469 . 46 VAL CG1 C 21.613 0.133 1 470 . 46 VAL CG2 C 21.613 0.133 1 471 . 46 VAL N N 121.764 0.000 1 472 . 47 TYR H H 8.941 0.027 1 473 . 47 TYR HA H 5.230 0.020 1 474 . 47 TYR HB2 H 3.008 0.041 2 475 . 47 TYR HB3 H 2.566 0.030 2 476 . 47 TYR HD1 H 6.946 0.011 1 477 . 47 TYR HD2 H 6.946 0.011 1 478 . 47 TYR HE1 H 6.706 0.007 1 479 . 47 TYR HE2 H 6.706 0.007 1 480 . 47 TYR CA C 56.076 0.007 1 481 . 47 TYR CB C 40.732 0.021 1 482 . 47 TYR CD1 C 132.746 0.000 1 483 . 47 TYR CE1 C 117.937 0.000 1 484 . 47 TYR N N 124.010 0.000 1 485 . 48 LEU H H 9.051 0.042 1 486 . 48 LEU HA H 5.383 0.040 1 487 . 48 LEU HB2 H 1.873 0.004 2 488 . 48 LEU HB3 H 1.540 0.031 2 489 . 48 LEU HG H 1.339 0.041 1 490 . 48 LEU HD1 H 0.705 0.037 1 491 . 48 LEU HD2 H 0.267 0.016 1 492 . 48 LEU CA C 53.593 0.006 1 493 . 48 LEU CB C 43.290 0.270 1 494 . 48 LEU CG C 28.252 0.000 1 495 . 48 LEU CD1 C 23.625 0.000 1 496 . 48 LEU CD2 C 26.034 0.000 1 497 . 48 LEU N N 121.897 0.000 1 498 . 49 ILE H H 9.530 0.026 1 499 . 49 ILE HA H 4.990 0.035 1 500 . 49 ILE HB H 1.852 0.044 1 501 . 49 ILE HG12 H 1.308 0.039 2 502 . 49 ILE HG13 H 0.989 0.025 2 503 . 49 ILE HG2 H 0.746 0.056 1 504 . 49 ILE HD1 H 0.675 0.000 1 505 . 49 ILE CA C 59.389 0.033 1 506 . 49 ILE CB C 38.673 0.362 1 507 . 49 ILE CG1 C 27.935 0.022 1 508 . 49 ILE CG2 C 17.650 0.056 1 509 . 49 ILE CD1 C 13.300 0.464 1 510 . 49 ILE N N 123.945 0.000 1 511 . 50 ASN H H 8.407 0.026 1 512 . 50 ASN HA H 3.130 0.076 1 513 . 50 ASN HB2 H 2.131 0.058 2 514 . 50 ASN HB3 H 1.558 0.026 2 515 . 50 ASN HD21 H 6.853 0.040 1 516 . 50 ASN HD22 H 6.619 0.040 1 517 . 50 ASN CA C 51.319 0.001 1 518 . 50 ASN CB C 36.638 0.273 1 519 . 50 ASN N N 126.693 0.000 1 520 . 50 ASN ND2 N 108.812 0.006 1 521 . 51 PRO HA H 4.143 0.068 1 522 . 51 PRO HB2 H 1.687 0.055 1 523 . 51 PRO HB3 H 1.687 0.055 1 524 . 51 PRO HG2 H 2.107 0.000 1 525 . 51 PRO HG3 H 2.107 0.000 1 526 . 51 PRO HD2 H 3.120 0.000 1 527 . 51 PRO HD3 H 3.120 0.000 1 528 . 51 PRO CA C 65.308 0.030 1 529 . 51 PRO CB C 31.443 0.000 1 530 . 51 PRO CG C 27.949 0.000 1 531 . 51 PRO CD C 50.293 0.000 1 532 . 52 GLN H H 6.869 0.030 1 533 . 52 GLN HA H 4.222 0.000 1 534 . 52 GLN HB2 H 2.189 0.000 2 535 . 52 GLN HB3 H 1.950 0.021 2 536 . 52 GLN HG2 H 2.453 0.000 2 537 . 52 GLN HG3 H 2.247 0.000 2 538 . 52 GLN HE21 H 7.555 0.000 1 539 . 52 GLN HE22 H 6.884 0.000 1 540 . 52 GLN CA C 56.254 0.008 1 541 . 52 GLN CB C 28.709 0.001 1 542 . 52 GLN CG C 35.068 0.000 1 543 . 52 GLN N N 112.661 0.000 1 544 . 52 GLN NE2 N 112.351 0.002 1 545 . 53 GLY H H 8.078 0.028 1 546 . 53 GLY HA2 H 4.033 0.020 2 547 . 53 GLY HA3 H 3.317 0.022 2 548 . 53 GLY CA C 45.439 0.094 1 549 . 53 GLY N N 108.280 0.000 1 550 . 54 LYS H H 7.681 0.021 1 551 . 54 LYS HA H 3.901 0.009 1 552 . 54 LYS HB2 H 1.186 0.040 1 553 . 54 LYS HB3 H 1.186 0.040 1 554 . 54 LYS HG2 H 0.975 0.005 2 555 . 54 LYS HG3 H 0.629 0.024 2 556 . 54 LYS HD2 H 1.373 0.009 2 557 . 54 LYS HD3 H 1.205 0.032 2 558 . 54 LYS HE2 H 2.839 0.042 2 559 . 54 LYS HE3 H 2.636 0.021 2 560 . 54 LYS CA C 55.716 0.085 1 561 . 54 LYS CB C 32.332 0.189 1 562 . 54 LYS CG C 24.862 0.000 1 563 . 54 LYS CD C 28.714 0.000 1 564 . 54 LYS CE C 42.294 0.000 1 565 . 54 LYS N N 123.290 0.000 1 566 . 55 ALA H H 7.884 0.031 1 567 . 55 ALA HA H 5.077 0.028 1 568 . 55 ALA HB H 1.144 0.038 1 569 . 55 ALA CA C 50.402 0.050 1 570 . 55 ALA CB C 22.421 0.004 1 571 . 55 ALA N N 125.304 0.000 1 572 . 56 PHE H H 9.579 0.027 1 573 . 56 PHE HA H 4.880 0.023 1 574 . 56 PHE HB2 H 3.082 0.029 1 575 . 56 PHE HB3 H 3.082 0.029 1 576 . 56 PHE HD1 H 7.156 0.002 1 577 . 56 PHE HD2 H 7.156 0.002 1 578 . 56 PHE HE1 H 6.725 0.001 1 579 . 56 PHE HE2 H 6.725 0.001 1 580 . 56 PHE HZ H 5.768 0.002 1 581 . 56 PHE CA C 57.442 0.004 1 582 . 56 PHE CB C 42.951 0.072 1 583 . 56 PHE CD1 C 131.957 0.000 1 584 . 56 PHE CE1 C 130.350 0.000 1 585 . 56 PHE CZ C 128.739 0.000 1 586 . 56 PHE N N 119.901 0.105 1 587 . 57 ARG H H 9.320 0.021 1 588 . 57 ARG HA H 4.824 0.026 1 589 . 57 ARG HB2 H 1.720 0.038 1 590 . 57 ARG HB3 H 1.720 0.038 1 591 . 57 ARG HG2 H 1.406 0.074 1 592 . 57 ARG HG3 H 1.406 0.074 1 593 . 57 ARG HD2 H 3.026 0.043 2 594 . 57 ARG HD3 H 2.988 0.043 2 595 . 57 ARG CA C 55.320 0.051 1 596 . 57 ARG CB C 32.286 0.070 1 597 . 57 ARG CG C 27.043 0.000 1 598 . 57 ARG CD C 43.280 0.000 1 599 . 57 ARG N N 119.801 0.000 1 600 . 58 SER H H 7.224 0.028 1 601 . 58 SER HA H 3.462 0.007 1 602 . 58 SER HB2 H 3.838 0.006 2 603 . 58 SER HB3 H 3.640 0.009 2 604 . 58 SER CA C 56.165 0.090 1 605 . 58 SER CB C 66.441 0.000 1 606 . 58 SER N N 111.498 0.000 1 607 . 59 LYS H H 8.440 0.028 1 608 . 59 LYS HA H 3.641 0.033 1 609 . 59 LYS HB2 H 1.715 0.000 1 610 . 59 LYS HB3 H 1.715 0.000 1 611 . 59 LYS HG2 H 1.406 0.000 1 612 . 59 LYS HG3 H 1.406 0.000 1 613 . 59 LYS HD2 H 1.725 0.000 1 614 . 59 LYS HD3 H 1.725 0.000 1 615 . 59 LYS HE2 H 3.047 0.000 1 616 . 59 LYS HE3 H 2.900 0.000 1 617 . 59 LYS CA C 59.589 0.009 1 618 . 59 LYS CB C 32.249 0.030 1 619 . 59 LYS CG C 25.442 0.000 1 620 . 59 LYS CD C 29.703 0.000 1 621 . 59 LYS CE C 42.143 0.000 1 622 . 59 LYS N N 122.010 0.000 1 623 . 60 VAL H H 7.582 0.027 1 624 . 60 VAL HA H 3.612 0.063 1 625 . 60 VAL HB H 1.918 0.059 1 626 . 60 VAL HG1 H 0.980 0.031 1 627 . 60 VAL HG2 H 0.913 0.027 1 628 . 60 VAL CA C 66.458 0.041 1 629 . 60 VAL CB C 32.010 0.031 1 630 . 60 VAL CG1 C 22.185 0.000 1 631 . 60 VAL CG2 C 21.121 0.000 1 632 . 60 VAL N N 116.761 0.000 1 633 . 61 GLU H H 7.352 0.024 1 634 . 61 GLU HA H 4.105 0.033 1 635 . 61 GLU HB2 H 2.360 0.000 1 636 . 61 GLU HB3 H 2.360 0.000 1 637 . 61 GLU HG2 H 2.340 0.021 1 638 . 61 GLU HG3 H 2.340 0.021 1 639 . 61 GLU CA C 59.217 0.086 1 640 . 61 GLU CB C 31.193 0.072 1 641 . 61 GLU CG C 37.031 0.000 1 642 . 61 GLU N N 119.731 0.000 1 643 . 62 LEU H H 7.465 0.014 1 644 . 62 LEU HA H 3.359 0.062 1 645 . 62 LEU HB2 H 1.333 0.072 1 646 . 62 LEU HB3 H 1.333 0.072 1 647 . 62 LEU HG H 0.814 0.028 1 648 . 62 LEU HD1 H -0.054 0.004 1 649 . 62 LEU HD2 H -0.101 0.012 1 650 . 62 LEU CA C 57.876 0.144 1 651 . 62 LEU CB C 42.663 0.031 1 652 . 62 LEU CG C 25.633 0.000 1 653 . 62 LEU CD1 C 24.880 0.000 1 654 . 62 LEU N N 121.504 0.000 1 655 . 63 ILE H H 8.351 0.030 1 656 . 63 ILE HA H 3.465 0.070 1 657 . 63 ILE HB H 1.737 0.051 1 658 . 63 ILE HG12 H 1.725 0.000 2 659 . 63 ILE HG13 H 1.076 0.006 2 660 . 63 ILE HG2 H 0.913 0.032 1 661 . 63 ILE HD1 H 0.855 0.009 1 662 . 63 ILE CA C 66.048 0.159 1 663 . 63 ILE CB C 38.819 0.017 1 664 . 63 ILE CG1 C 30.415 0.067 1 665 . 63 ILE CG2 C 17.217 0.135 1 666 . 63 ILE CD1 C 14.419 0.000 1 667 . 63 ILE N N 118.216 0.000 1 668 . 64 ALA H H 7.491 0.025 1 669 . 64 ALA HA H 4.178 0.030 1 670 . 64 ALA HB H 1.482 0.027 1 671 . 64 ALA CA C 54.963 0.019 1 672 . 64 ALA CB C 18.322 0.038 1 673 . 64 ALA N N 119.792 0.000 1 674 . 65 TYR H H 7.720 0.032 1 675 . 65 TYR HA H 4.387 0.011 1 676 . 65 TYR HB2 H 3.342 0.033 2 677 . 65 TYR HB3 H 2.886 0.036 2 678 . 65 TYR HD1 H 7.050 0.010 1 679 . 65 TYR HD2 H 7.050 0.010 1 680 . 65 TYR HE1 H 6.922 0.011 1 681 . 65 TYR HE2 H 6.922 0.011 1 682 . 65 TYR CA C 61.538 0.027 1 683 . 65 TYR CB C 39.387 0.045 1 684 . 65 TYR CD1 C 133.569 0.033 1 685 . 65 TYR CE1 C 118.001 0.033 1 686 . 65 TYR N N 120.434 0.112 1 687 . 66 PHE H H 8.728 0.026 1 688 . 66 PHE HA H 4.417 0.009 1 689 . 66 PHE HB2 H 3.597 0.024 2 690 . 66 PHE HB3 H 3.188 0.001 2 691 . 66 PHE HD1 H 7.184 0.007 1 692 . 66 PHE HD2 H 7.184 0.007 1 693 . 66 PHE HE1 H 7.028 0.001 1 694 . 66 PHE HE2 H 7.028 0.001 1 695 . 66 PHE HZ H 6.718 0.003 1 696 . 66 PHE CA C 58.270 0.036 1 697 . 66 PHE CB C 36.667 0.088 1 698 . 66 PHE CD1 C 130.073 0.088 1 699 . 66 PHE CE1 C 130.184 0.088 1 700 . 66 PHE CZ C 129.299 0.159 1 701 . 66 PHE N N 118.416 0.121 1 702 . 67 GLU H H 8.255 0.029 1 703 . 67 GLU HA H 4.066 0.007 1 704 . 67 GLU HB2 H 2.140 0.000 2 705 . 67 GLU HB3 H 2.034 0.011 2 706 . 67 GLU HG2 H 2.437 0.000 2 707 . 67 GLU HG3 H 2.198 0.000 2 708 . 67 GLU CA C 59.349 0.004 1 709 . 67 GLU CB C 29.799 0.010 1 710 . 67 GLU CG C 36.824 0.000 1 711 . 67 GLU N N 118.090 0.000 1 712 . 68 LYS H H 7.786 0.024 1 713 . 68 LYS HA H 4.023 0.000 1 714 . 68 LYS HB2 H 2.006 0.021 1 715 . 68 LYS HB3 H 2.006 0.021 1 716 . 68 LYS HG2 H 1.494 0.000 2 717 . 68 LYS HG3 H 1.398 0.000 2 718 . 68 LYS HD2 H 1.728 0.000 1 719 . 68 LYS HD3 H 1.728 0.000 1 720 . 68 LYS HE2 H 3.001 0.000 1 721 . 68 LYS HE3 H 3.001 0.000 1 722 . 68 LYS CA C 59.335 0.005 1 723 . 68 LYS CB C 32.603 0.204 1 724 . 68 LYS CG C 25.000 0.000 1 725 . 68 LYS CD C 29.294 0.000 1 726 . 68 LYS CE C 42.381 0.000 1 727 . 68 LYS N N 121.034 0.000 1 728 . 69 VAL H H 7.950 0.027 1 729 . 69 VAL HA H 4.232 0.017 1 730 . 69 VAL HB H 2.264 0.012 1 731 . 69 VAL HG1 H 0.708 0.000 1 732 . 69 VAL HG2 H 0.770 0.000 1 733 . 69 VAL CA C 61.918 0.073 1 734 . 69 VAL CB C 31.985 0.014 1 735 . 69 VAL CG1 C 21.270 0.000 1 736 . 69 VAL CG2 C 19.334 0.000 1 737 . 69 VAL N N 110.121 0.057 1 738 . 70 GLY H H 7.733 0.029 1 739 . 70 GLY HA2 H 3.939 0.007 2 740 . 70 GLY HA3 H 3.789 0.010 2 741 . 70 GLY CA C 46.771 0.015 1 742 . 70 GLY N N 111.822 0.000 1 743 . 71 ASP H H 8.050 0.013 1 744 . 71 ASP HA H 4.740 0.000 1 745 . 71 ASP HB2 H 2.606 0.033 2 746 . 71 ASP HB3 H 2.390 0.002 2 747 . 71 ASP CA C 53.862 0.020 1 748 . 71 ASP CB C 42.121 0.046 1 749 . 71 ASP N N 119.968 0.038 1 750 . 72 THR H H 8.400 0.020 1 751 . 72 THR HA H 4.430 0.004 1 752 . 72 THR HB H 4.466 0.010 1 753 . 72 THR HG2 H 1.064 0.000 1 754 . 72 THR CA C 60.801 0.415 1 755 . 72 THR CB C 68.911 0.027 1 756 . 72 THR CG2 C 21.423 0.000 1 757 . 72 THR N N 116.429 0.000 1 758 . 73 SER H H 8.604 0.027 1 759 . 73 SER HA H 4.220 0.004 1 760 . 73 SER HB2 H 3.834 0.010 1 761 . 73 SER HB3 H 3.834 0.010 1 762 . 73 SER CA C 60.474 0.049 1 763 . 73 SER CB C 64.333 0.236 1 764 . 73 SER N N 118.895 0.000 1 765 . 74 LEU H H 7.606 0.043 1 766 . 74 LEU HA H 4.354 0.046 1 767 . 74 LEU HB2 H 1.095 0.047 2 768 . 74 LEU HB3 H 0.926 0.060 2 769 . 74 LEU HG H 1.571 0.038 1 770 . 74 LEU HD1 H 0.938 0.029 1 771 . 74 LEU HD2 H 0.768 0.028 1 772 . 74 LEU CA C 53.756 0.116 1 773 . 74 LEU CB C 44.285 0.028 1 774 . 74 LEU CG C 26.800 0.000 1 775 . 74 LEU CD1 C 26.752 0.000 1 776 . 74 LEU CD2 C 23.253 0.000 1 777 . 74 LEU N N 123.172 0.000 1 778 . 75 ASP H H 8.809 0.022 1 779 . 75 ASP HA H 4.922 0.002 1 780 . 75 ASP HB2 H 3.015 0.000 2 781 . 75 ASP HB3 H 2.399 0.000 2 782 . 75 ASP CA C 50.318 0.000 1 783 . 75 ASP CB C 42.380 0.000 1 784 . 75 ASP N N 122.806 0.000 1 785 . 76 PRO HA H 4.308 0.012 1 786 . 76 PRO HB2 H 2.077 0.000 2 787 . 76 PRO HB3 H 1.912 0.000 2 788 . 76 PRO HG2 H 2.187 0.000 1 789 . 76 PRO HG3 H 2.026 0.000 1 790 . 76 PRO HD2 H 4.079 0.000 1 791 . 76 PRO HD3 H 4.079 0.000 1 792 . 76 PRO CA C 64.993 0.059 1 793 . 76 PRO CB C 33.057 0.052 1 794 . 76 PRO CG C 27.951 0.000 1 795 . 76 PRO CD C 51.237 0.415 1 796 . 77 ASN H H 8.777 0.028 1 797 . 77 ASN HA H 4.479 0.037 1 798 . 77 ASN HB2 H 2.731 0.045 1 799 . 77 ASN HB3 H 2.731 0.045 1 800 . 77 ASN HD21 H 8.126 0.000 1 801 . 77 ASN HD22 H 7.001 0.000 1 802 . 77 ASN CA C 55.421 0.032 1 803 . 77 ASN CB C 38.291 0.039 1 804 . 77 ASN N N 114.562 0.000 1 805 . 77 ASN ND2 N 115.630 0.000 1 806 . 78 ASP H H 8.292 0.021 1 807 . 78 ASP HA H 4.469 0.025 1 808 . 78 ASP HB2 H 2.496 0.042 1 809 . 78 ASP HB3 H 2.496 0.042 1 810 . 78 ASP CA C 55.463 0.063 1 811 . 78 ASP CB C 40.554 0.265 1 812 . 78 ASP N N 118.877 0.000 1 813 . 79 PHE H H 7.055 0.032 1 814 . 79 PHE HA H 3.897 0.066 1 815 . 79 PHE HB2 H 2.813 0.051 2 816 . 79 PHE HB3 H 2.089 0.029 2 817 . 79 PHE HD1 H 6.859 0.015 1 818 . 79 PHE HD2 H 6.859 0.015 1 819 . 79 PHE HE1 H 5.959 0.012 1 820 . 79 PHE HE2 H 5.959 0.012 1 821 . 79 PHE HZ H 6.341 0.011 1 822 . 79 PHE CA C 57.755 0.064 1 823 . 79 PHE CB C 39.430 0.174 1 824 . 79 PHE CD1 C 131.610 0.023 1 825 . 79 PHE CE1 C 129.831 0.125 1 826 . 79 PHE CZ C 128.670 0.290 1 827 . 79 PHE N N 119.099 0.259 1 828 . 80 ASP H H 8.913 0.032 1 829 . 80 ASP HA H 4.542 0.000 1 830 . 80 ASP HB2 H 2.811 0.000 2 831 . 80 ASP HB3 H 2.394 0.000 2 832 . 80 ASP CA C 53.756 0.182 1 833 . 80 ASP CB C 41.535 0.074 1 834 . 80 ASP N N 124.448 0.000 1 835 . 81 PHE H H 9.067 0.035 1 836 . 81 PHE HA H 4.358 0.024 1 837 . 81 PHE HB2 H 3.496 0.047 2 838 . 81 PHE HB3 H 2.712 0.011 2 839 . 81 PHE HD1 H 7.139 0.009 1 840 . 81 PHE HD2 H 7.139 0.009 1 841 . 81 PHE HE1 H 7.023 0.002 1 842 . 81 PHE HE2 H 7.023 0.002 1 843 . 81 PHE HZ H 6.665 0.002 1 844 . 81 PHE CA C 59.048 0.076 1 845 . 81 PHE CB C 39.837 0.245 1 846 . 81 PHE CD1 C 132.084 0.000 1 847 . 81 PHE CE1 C 130.316 0.000 1 848 . 81 PHE CZ C 128.181 0.000 1 849 . 81 PHE N N 125.250 0.000 1 850 . 82 THR H H 8.971 0.032 1 851 . 82 THR HA H 4.477 0.150 1 852 . 82 THR HB H 4.266 0.069 1 853 . 82 THR HG2 H 1.299 0.090 1 854 . 82 THR CA C 62.344 0.076 1 855 . 82 THR CB C 70.729 0.287 1 856 . 82 THR CG2 C 22.434 0.000 1 857 . 82 THR N N 113.186 0.000 1 858 . 83 VAL H H 9.024 0.069 1 859 . 83 VAL HA H 3.352 0.009 1 860 . 83 VAL HB H 2.068 0.015 1 861 . 83 VAL HG1 H 1.111 0.007 1 862 . 83 VAL HG2 H 0.714 0.011 1 863 . 83 VAL CA C 67.010 0.000 1 864 . 83 VAL CB C 33.083 0.177 1 865 . 83 VAL CG1 C 23.970 0.080 1 866 . 83 VAL CG2 C 21.473 0.010 1 867 . 83 VAL N N 123.327 0.000 1 868 . 84 THR H H 7.900 0.045 1 869 . 84 THR HA H 4.172 0.049 1 870 . 84 THR HB H 4.297 0.020 1 871 . 84 THR HG2 H 0.980 0.000 1 872 . 84 THR CA C 62.260 0.153 1 873 . 84 THR CB C 69.994 0.016 1 874 . 84 THR CG2 C 21.904 0.000 1 875 . 84 THR N N 105.656 0.000 1 876 . 85 GLY H H 7.371 0.034 1 877 . 85 GLY HA2 H 4.363 0.044 2 878 . 85 GLY HA3 H 3.872 0.015 2 879 . 85 GLY CA C 44.598 0.041 1 880 . 85 GLY N N 111.184 0.000 1 881 . 86 ARG H H 9.302 0.070 1 882 . 86 ARG HA H 4.104 0.044 1 883 . 86 ARG HB2 H 1.719 0.044 1 884 . 86 ARG HB3 H 1.719 0.044 1 885 . 86 ARG HG2 H 1.594 0.000 1 886 . 86 ARG HG3 H 1.594 0.000 1 887 . 86 ARG HD2 H 3.093 0.030 1 888 . 86 ARG HD3 H 3.093 0.030 1 889 . 86 ARG CA C 57.383 0.022 1 890 . 86 ARG CB C 30.900 0.012 1 891 . 86 ARG CG C 26.901 0.000 1 892 . 86 ARG CD C 44.023 0.000 1 893 . 86 ARG N N 123.749 0.000 1 894 . 87 GLY H H 8.614 0.025 1 895 . 87 GLY HA2 H 3.982 0.001 1 896 . 87 GLY HA3 H 3.982 0.001 1 897 . 87 GLY CA C 45.429 0.000 1 898 . 87 GLY N N 109.801 0.000 1 899 . 88 SER H H 8.188 0.003 1 900 . 88 SER HA H 4.350 0.016 1 901 . 88 SER HB2 H 3.833 0.017 1 902 . 88 SER HB3 H 3.833 0.017 1 903 . 88 SER CA C 58.785 0.023 1 904 . 88 SER CB C 64.082 0.205 1 905 . 88 SER N N 115.685 0.000 1 906 . 89 GLY H H 8.447 0.032 1 907 . 89 GLY HA2 H 3.905 0.004 1 908 . 89 GLY HA3 H 3.905 0.004 1 909 . 89 GLY CA C 45.436 0.000 1 910 . 89 GLY N N 110.679 0.000 1 911 . 90 SER H H 8.271 0.008 1 912 . 90 SER HA H 4.423 0.004 1 913 . 90 SER HB2 H 3.837 0.026 1 914 . 90 SER HB3 H 3.837 0.026 1 915 . 90 SER CA C 58.776 0.024 1 916 . 90 SER CB C 64.088 0.217 1 917 . 90 SER N N 115.402 0.000 1 918 . 91 GLY H H 8.512 0.023 1 919 . 91 GLY HA2 H 3.949 0.012 1 920 . 91 GLY HA3 H 3.949 0.012 1 921 . 91 GLY CA C 45.649 0.059 1 922 . 91 GLY N N 111.177 0.000 1 923 . 92 CYS H H 7.840 0.024 1 924 . 92 CYS CA C 59.594 0.000 1 925 . 92 CYS CB C 29.255 0.000 1 926 . 92 CYS N N 122.515 0.000 1 stop_ save_