data_6419 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of the C-terminal Domain from Trypanosoma brucei Variant Surface Glycoprotein MITat1.2 ; _BMRB_accession_number 6419 _BMRB_flat_file_name bmr6419.str _Entry_type original _Submission_date 2004-12-10 _Accession_date 2004-12-10 _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 Chattopadhyay A. . . 2 Jones N. G. . 3 Nietlispach D. . . 4 Nielsen P. R. . 5 Voorheis H. P. . 6 Mott H. R. . 7 Carrington M. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 383 "13C chemical shifts" 231 "15N chemical shifts" 79 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-04-26 original BMRB . stop_ _Original_release_date 2004-12-10 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure of the C-terminal Domain from Trypanosoma brucei Variant Surface Glycoprotein MITat1.2 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15557330 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chattopadhyay A. . . 2 Jones N. G. . 3 Nietlispach D. . . 4 Nielsen P. R. . 5 Voorheis H. P. . 6 Mott H. R. . 7 Carrington M. . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 280 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7228 _Page_last 7235 _Year 2005 _Details . loop_ _Keyword 'cysteine knot' stop_ save_ ################################## # Molecular system description # ################################## save_system_MITAT _Saveframe_category molecular_system _Mol_system_name 'Variant surface glycoprotein MITAT 1.2' _Abbreviation_common 'Variant surface glycoprotein MITAT 1.2' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Variant surface glycoprotein MITAT 1.2' $MITAT stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MITAT _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Variant surface glycoprotein MITAT 1.2' _Abbreviation_common 'Variant surface glycoprotein MITAT 1.2' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 80 _Mol_residue_sequence ; GSHMLEVLTQKHKPAESQQQ AAETEGSCNKKDQNECKSPC KWHNDAENKKCTLDKEEAKK VADETAKDGKTGNTNTTGSS ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 HIS 4 MET 5 LEU 6 GLU 7 VAL 8 LEU 9 THR 10 GLN 11 LYS 12 HIS 13 LYS 14 PRO 15 ALA 16 GLU 17 SER 18 GLN 19 GLN 20 GLN 21 ALA 22 ALA 23 GLU 24 THR 25 GLU 26 GLY 27 SER 28 CYS 29 ASN 30 LYS 31 LYS 32 ASP 33 GLN 34 ASN 35 GLU 36 CYS 37 LYS 38 SER 39 PRO 40 CYS 41 LYS 42 TRP 43 HIS 44 ASN 45 ASP 46 ALA 47 GLU 48 ASN 49 LYS 50 LYS 51 CYS 52 THR 53 LEU 54 ASP 55 LYS 56 GLU 57 GLU 58 ALA 59 LYS 60 LYS 61 VAL 62 ALA 63 ASP 64 GLU 65 THR 66 ALA 67 LYS 68 ASP 69 GLY 70 LYS 71 THR 72 GLY 73 ASN 74 THR 75 ASN 76 THR 77 THR 78 GLY 79 SER 80 SER stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1XU6 'Structure Of The C-Terminal Domain From Trypanosoma Brucei Variant Surface Glycoprotein Mitat1.2' 100.00 80 100.00 100.00 5.60e-38 EMBL CAA40081 'variant surface glycoprotein MITat 1.2 [Trypanosoma brucei]' 95.00 476 98.68 98.68 1.22e-36 EMBL CAQ57294 'variant surface glycoprotein [Trypanosoma brucei brucei]' 95.00 476 98.68 98.68 1.22e-36 SWISS-PROT P26332 'Variant surface glycoprotein MITAT 1.2 precursor (VSG 221)' 95.00 476 98.68 98.68 1.22e-36 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MITAT 'Trypanosoma brucei' 5691 Eukaryota . Trypanosoma brucei 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 $MITAT 'recombinant technology' 'E. coli' Escherichia coli 'BL21 TrxB' pET15b 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 $MITAT 1 mM [U-15N] 'sodium phosphate' 50 mM . 'sodium chloride' 100 mM . 'sodium azide' 0.05 % . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MITAT 1 mM '[U-13C; U-15N]' 'sodium phosphate' 50 mM . 'sodium chloride' 100 mM . 'sodium azide' 0.05 % . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_ARIA _Saveframe_category software _Name ARIA _Version 1.1 loop_ _Task refinement 'structure solution' stop_ _Details NILGES save_ save_AZARA _Saveframe_category software _Name AZARA _Version 2.7 loop_ _Task 'structure solution' stop_ _Details . save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version 3.3 loop_ _Task 'structure solution' stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version 1.1 loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-SEPARATED_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-SEPARATED NOESY' _Sample_label . save_ save_3D_13C-SEPARATED_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-SEPARATED NOESY' _Sample_label . save_ save_CLEANEX_3 _Saveframe_category NMR_applied_experiment _Experiment_name CLEANEX _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . pH pressure 1 . atm temperature 298 . K 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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D 15N-SEPARATED NOESY' '3D 13C-SEPARATED NOESY' CLEANEX stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Variant surface glycoprotein MITAT 1.2' _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 . 2 SER CA C 58.29 0.120 1 2 . 2 SER HA H 4.40 0.014 1 3 . 2 SER CB C 63.75 0.000 1 4 . 2 SER HB2 H 3.74 0.006 2 5 . 3 HIS N N 120.99 0.010 1 6 . 3 HIS H H 8.62 0.002 1 7 . 3 HIS CA C 55.74 0.060 1 8 . 3 HIS HA H 4.61 0.002 1 9 . 3 HIS CB C 29.27 0.070 1 10 . 3 HIS HB2 H 3.06 0.000 1 11 . 3 HIS HB3 H 3.17 0.000 1 12 . 4 MET N N 121.10 0.050 1 13 . 4 MET H H 8.31 0.007 1 14 . 4 MET CA C 55.73 0.040 1 15 . 4 MET HA H 4.33 0.005 1 16 . 4 MET CB C 32.58 0.060 1 17 . 4 MET HB2 H 1.91 0.006 1 18 . 4 MET HB3 H 1.98 0.003 1 19 . 4 MET CG C 31.67 0.070 1 20 . 4 MET HG2 H 2.43 0.008 1 21 . 4 MET HG3 H 2.48 0.004 1 22 . 4 MET CE C 16.78 0.000 1 23 . 4 MET HE H 2.03 0.000 1 24 . 5 LEU N N 122.60 0.050 1 25 . 5 LEU H H 8.18 0.002 1 26 . 5 LEU CA C 55.31 0.060 1 27 . 5 LEU HA H 4.23 0.008 1 28 . 5 LEU CB C 42.12 0.010 1 29 . 5 LEU HB2 H 1.90 0.000 1 30 . 5 LEU HB3 H 2.00 0.000 1 31 . 5 LEU CG C 26.81 0.110 1 32 . 5 LEU HG H 1.54 0.008 1 33 . 5 LEU CD1 C 23.11 0.010 1 34 . 5 LEU HD1 H 0.79 0.007 2 35 . 5 LEU CD2 C 24.67 0.010 1 36 . 5 LEU HD2 H 0.85 0.004 2 37 . 6 GLU N N 121.80 0.060 1 38 . 6 GLU H H 8.26 0.002 1 39 . 6 GLU CA C 56.62 0.020 1 40 . 6 GLU HA H 4.19 0.006 1 41 . 6 GLU CB C 30.14 0.020 1 42 . 6 GLU CG C 35.96 0.020 1 43 . 6 GLU HG2 H 2.15 0.011 1 44 . 6 GLU HG3 H 2.24 0.013 1 45 . 6 GLU HB2 H 1.90 0.010 2 46 . 7 VAL N N 120.84 0.060 1 47 . 7 VAL H H 8.05 0.005 1 48 . 7 VAL CA C 62.40 0.060 1 49 . 7 VAL HA H 3.98 0.008 1 50 . 7 VAL CB C 32.41 0.040 1 51 . 7 VAL HB H 1.99 0.004 1 52 . 7 VAL CG1 C 20.69 0.090 2 53 . 7 VAL HG1 H 0.84 0.004 2 54 . 8 LEU N N 124.89 0.050 1 55 . 8 LEU H H 8.23 0.003 1 56 . 8 LEU CA C 55.24 0.010 1 57 . 8 LEU HA H 4.33 0.004 1 58 . 8 LEU CB C 42.13 0.030 1 59 . 8 LEU HB2 H 1.53 0.006 1 60 . 8 LEU HB3 H 1.61 0.004 1 61 . 8 LEU CG C 26.75 0.090 1 62 . 8 LEU HG H 1.55 0.013 1 63 . 8 LEU CD1 C 22.99 0.020 1 64 . 8 LEU HD1 H 0.78 0.002 2 65 . 8 LEU CD2 C 24.68 0.030 1 66 . 8 LEU HD2 H 0.85 0.003 2 67 . 9 THR N N 114.07 0.050 1 68 . 9 THR H H 7.97 0.003 1 69 . 9 THR CA C 61.79 0.050 1 70 . 9 THR HA H 4.21 0.012 1 71 . 9 THR CB C 69.77 0.120 1 72 . 9 THR HB H 4.13 0.002 1 73 . 9 THR CG2 C 21.40 0.000 1 74 . 9 THR HG2 H 1.12 0.004 1 75 . 10 GLN N N 121.96 0.040 1 76 . 10 GLN H H 8.19 0.004 1 77 . 10 GLN CA C 55.62 0.040 1 78 . 10 GLN HA H 4.23 0.006 1 79 . 10 GLN CB C 29.27 0.060 1 80 . 10 GLN HB2 H 1.89 0.007 1 81 . 10 GLN HB3 H 2.00 0.002 1 82 . 10 GLN CG C 33.59 0.090 1 83 . 10 GLN HG2 H 2.26 0.013 2 84 . 11 LYS N N 121.90 0.050 1 85 . 11 LYS H H 8.22 0.004 1 86 . 11 LYS CA C 56.19 0.050 1 87 . 11 LYS HA H 4.17 0.010 1 88 . 11 LYS CB C 32.73 0.040 1 89 . 11 LYS HB2 H 1.74 0.003 1 90 . 11 LYS HB3 H 1.79 0.004 1 91 . 11 LYS CG C 24.52 0.020 1 92 . 11 LYS HG2 H 1.29 0.012 1 93 . 11 LYS HG3 H 1.41 0.005 1 94 . 11 LYS CD C 28.95 0.010 1 95 . 11 LYS CE C 41.90 0.010 1 96 . 11 LYS HD2 H 1.61 0.011 2 97 . 11 LYS HE2 H 2.89 0.008 2 98 . 12 HIS N N 119.46 0.060 1 99 . 12 HIS H H 8.33 0.005 1 100 . 12 HIS CA C 55.21 0.020 1 101 . 12 HIS HA H 4.59 0.013 1 102 . 12 HIS CB C 29.61 0.100 1 103 . 12 HIS HB2 H 3.04 0.003 1 104 . 12 HIS HB3 H 3.10 0.005 1 105 . 13 LYS N N 124.23 0.050 1 106 . 13 LYS H H 8.33 0.005 1 107 . 13 LYS CA C 54.21 0.070 1 108 . 13 LYS HA H 4.50 0.003 1 109 . 13 LYS CB C 32.38 0.070 1 110 . 13 LYS HB2 H 1.64 0.001 1 111 . 13 LYS HB3 H 1.74 0.001 1 112 . 13 LYS CG C 24.55 0.010 1 113 . 13 LYS CD C 28.93 0.010 1 114 . 13 LYS CE C 42.00 0.010 1 115 . 13 LYS HG2 H 1.36 0.004 2 116 . 13 LYS HD2 H 1.60 0.006 2 117 . 13 LYS HE2 H 2.91 0.005 2 118 . 14 PRO CA C 63.03 0.090 1 119 . 14 PRO HA H 4.32 0.008 1 120 . 14 PRO CB C 31.92 0.080 1 121 . 14 PRO HB2 H 1.85 0.008 1 122 . 14 PRO HB3 H 2.25 0.003 1 123 . 14 PRO CG C 27.10 0.020 1 124 . 14 PRO HG2 H 1.93 0.005 1 125 . 14 PRO HG3 H 1.98 0.005 1 126 . 14 PRO CD C 50.58 0.030 1 127 . 14 PRO HD2 H 3.55 0.004 1 128 . 14 PRO HD3 H 3.72 0.004 1 129 . 15 ALA N N 123.85 0.040 1 130 . 15 ALA H H 8.38 0.004 1 131 . 15 ALA CA C 52.51 0.010 1 132 . 15 ALA HA H 4.19 0.006 1 133 . 15 ALA CB C 19.12 0.030 1 134 . 15 ALA HB H 1.33 0.008 1 135 . 16 GLU N N 119.63 0.050 1 136 . 16 GLU H H 8.36 0.001 1 137 . 16 GLU CA C 56.52 0.010 1 138 . 16 GLU HA H 4.21 0.003 1 139 . 16 GLU CB C 30.15 0.020 1 140 . 16 GLU HB2 H 1.87 0.002 1 141 . 16 GLU HB3 H 2.00 0.004 1 142 . 16 GLU CG C 35.97 0.010 1 143 . 16 GLU HG2 H 2.19 0.004 2 144 . 17 SER N N 116.10 0.050 1 145 . 17 SER H H 8.24 0.002 1 146 . 17 SER CA C 58.18 0.090 1 147 . 17 SER HA H 4.35 0.011 1 148 . 17 SER CB C 63.74 0.030 1 149 . 17 SER HB2 H 3.80 0.009 2 150 . 18 GLN N N 121.72 0.030 1 151 . 18 GLN H H 8.34 0.003 1 152 . 18 GLN CA C 55.85 0.090 1 153 . 18 GLN HA H 4.25 0.009 1 154 . 18 GLN CB C 29.40 0.040 1 155 . 18 GLN HB2 H 1.91 0.002 1 156 . 18 GLN HB3 H 2.01 0.002 1 157 . 18 GLN CG C 33.99 0.030 1 158 . 18 GLN HG2 H 2.19 0.001 1 159 . 18 GLN HG3 H 2.29 0.006 1 160 . 19 GLN N N 121.07 0.010 1 161 . 19 GLN H H 8.30 0.001 1 162 . 19 GLN CA C 55.70 0.070 1 163 . 19 GLN HA H 4.22 0.011 1 164 . 19 GLN CB C 29.29 0.010 1 165 . 19 GLN HB2 H 1.92 0.009 1 166 . 19 GLN HB3 H 1.99 0.009 1 167 . 19 GLN CG C 33.60 0.050 1 168 . 19 GLN HG2 H 2.29 0.002 2 169 . 20 GLN N N 121.72 0.060 1 170 . 20 GLN H H 8.36 0.003 1 171 . 20 GLN CA C 55.59 0.010 1 172 . 20 GLN HA H 4.24 0.010 1 173 . 20 GLN CB C 29.53 0.010 1 174 . 20 GLN HB2 H 1.91 0.002 1 175 . 20 GLN HB3 H 2.02 0.014 1 176 . 20 GLN CG C 33.48 0.010 1 177 . 20 GLN HG2 H 2.29 0.003 2 178 . 21 ALA N N 125.52 0.040 1 179 . 21 ALA H H 8.30 0.002 1 180 . 21 ALA CA C 52.13 0.070 1 181 . 21 ALA HA H 4.22 0.004 1 182 . 21 ALA CB C 19.27 0.060 1 183 . 21 ALA HB H 1.31 0.002 1 184 . 22 ALA N N 123.40 0.030 1 185 . 22 ALA H H 8.16 0.002 1 186 . 22 ALA CA C 52.05 0.010 1 187 . 22 ALA HA H 4.28 0.004 1 188 . 22 ALA CB C 19.33 0.020 1 189 . 22 ALA HB H 1.31 0.005 1 190 . 23 GLU N N 118.89 0.040 1 191 . 23 GLU H H 8.08 0.003 1 192 . 23 GLU CA C 55.11 0.090 1 193 . 23 GLU HA H 4.39 0.008 1 194 . 23 GLU CB C 30.75 0.070 1 195 . 23 GLU HB2 H 1.45 0.003 1 196 . 23 GLU HB3 H 2.15 0.005 1 197 . 23 GLU CG C 34.92 0.070 1 198 . 23 GLU HG2 H 2.25 0.010 2 199 . 24 THR N N 111.57 0.030 1 200 . 24 THR H H 9.04 0.008 1 201 . 24 THR CA C 59.30 0.080 1 202 . 24 THR HA H 4.50 0.005 1 203 . 24 THR CB C 72.96 0.090 1 204 . 24 THR HB H 4.51 0.001 1 205 . 24 THR CG2 C 21.68 0.010 1 206 . 24 THR HG2 H 1.13 0.006 1 207 . 25 GLU N N 121.77 0.050 1 208 . 25 GLU H H 9.01 0.002 1 209 . 25 GLU CA C 59.90 0.120 1 210 . 25 GLU HA H 3.94 0.009 1 211 . 25 GLU CB C 28.86 0.100 1 212 . 25 GLU HB2 H 1.78 0.004 1 213 . 25 GLU HB3 H 2.09 0.004 1 214 . 25 GLU CG C 34.33 0.020 1 215 . 25 GLU HG2 H 2.20 0.008 1 216 . 25 GLU HG3 H 2.35 0.005 1 217 . 26 GLY N N 102.83 0.070 1 218 . 26 GLY H H 8.32 0.006 1 219 . 26 GLY CA C 46.66 0.010 1 220 . 26 GLY HA2 H 3.69 0.003 1 221 . 26 GLY HA3 H 3.75 0.011 1 222 . 27 SER N N 118.44 0.040 1 223 . 27 SER H H 8.14 0.004 1 224 . 27 SER CA C 61.82 0.010 1 225 . 27 SER HA H 4.15 0.007 1 226 . 27 SER CB C 62.08 0.010 1 227 . 27 SER HB2 H 3.81 0.016 1 228 . 27 SER HB3 H 4.01 0.017 1 229 . 28 CYS N N 123.68 0.060 1 230 . 28 CYS H H 8.59 0.003 1 231 . 28 CYS CA C 57.41 0.010 1 232 . 28 CYS HA H 4.29 0.005 1 233 . 28 CYS CB C 35.96 0.030 1 234 . 28 CYS HB2 H 2.70 0.004 2 235 . 29 ASN N N 114.86 0.030 1 236 . 29 ASN H H 8.57 0.002 1 237 . 29 ASN CA C 55.33 0.070 1 238 . 29 ASN HA H 4.85 0.007 1 239 . 29 ASN CB C 39.63 0.050 1 240 . 29 ASN ND2 N 112.37 0.710 1 241 . 29 ASN HD21 H 7.77 0.026 1 242 . 29 ASN HD22 H 8.22 0.007 1 243 . 29 ASN HB2 H 2.82 0.023 2 244 . 30 LYS N N 116.19 0.050 1 245 . 30 LYS H H 6.97 0.005 1 246 . 30 LYS CA C 56.76 0.010 1 247 . 30 LYS HA H 4.21 0.007 1 248 . 30 LYS CB C 33.28 0.010 1 249 . 30 LYS HB2 H 1.73 0.006 1 250 . 30 LYS HB3 H 2.00 0.004 1 251 . 30 LYS CG C 24.70 0.040 1 252 . 30 LYS HG2 H 1.43 0.016 1 253 . 30 LYS HG3 H 1.63 0.003 1 254 . 30 LYS CD C 28.95 0.000 1 255 . 30 LYS CE C 41.90 0.010 1 256 . 30 LYS HD2 H 1.62 0.011 2 257 . 31 LYS N N 120.36 0.050 1 258 . 31 LYS H H 7.78 0.003 1 259 . 31 LYS CA C 57.12 0.040 1 260 . 31 LYS HA H 4.28 0.005 1 261 . 31 LYS CB C 34.31 0.070 1 262 . 31 LYS HB2 H 1.58 0.011 1 263 . 31 LYS HB3 H 2.49 0.007 1 264 . 31 LYS CG C 25.99 0.030 1 265 . 31 LYS HG2 H 1.34 0.002 1 266 . 31 LYS HG3 H 1.76 0.008 1 267 . 31 LYS CD C 29.54 0.020 1 268 . 31 LYS HD2 H 1.57 0.002 1 269 . 31 LYS HD3 H 1.77 0.002 1 270 . 31 LYS CE C 42.71 0.020 1 271 . 31 LYS HE2 H 2.82 0.004 1 272 . 31 LYS HE3 H 3.05 0.003 1 273 . 32 ASP N N 120.50 0.070 1 274 . 32 ASP H H 8.31 0.001 1 275 . 32 ASP CA C 52.15 0.020 1 276 . 32 ASP HA H 4.71 0.008 1 277 . 32 ASP CB C 41.20 0.060 1 278 . 32 ASP HB2 H 2.71 0.003 1 279 . 32 ASP HB3 H 2.81 0.003 1 280 . 33 GLN N N 118.48 0.040 1 281 . 33 GLN H H 7.85 0.006 1 282 . 33 GLN CA C 60.03 0.110 1 283 . 33 GLN HA H 2.33 0.007 1 284 . 33 GLN CB C 27.31 0.110 1 285 . 33 GLN HB2 H 0.40 0.009 1 286 . 33 GLN HB3 H 1.01 0.008 1 287 . 33 GLN CG C 31.58 0.010 1 288 . 33 GLN HG2 H 0.51 0.012 1 289 . 33 GLN HG3 H 1.38 0.004 1 290 . 33 GLN NE2 N 109.41 0.000 1 291 . 33 GLN HE21 H 6.52 0.000 1 292 . 33 GLN HE22 H 6.90 0.000 1 293 . 34 ASN N N 114.06 0.070 1 294 . 34 ASN H H 8.03 0.006 1 295 . 34 ASN CA C 55.25 0.080 1 296 . 34 ASN HA H 4.09 0.010 1 297 . 34 ASN CB C 37.78 0.010 1 298 . 34 ASN HB2 H 2.58 0.003 1 299 . 34 ASN HB3 H 2.68 0.004 1 300 . 34 ASN ND2 N 113.44 0.040 1 301 . 34 ASN HD21 H 6.78 0.002 1 302 . 34 ASN HD22 H 7.60 0.002 1 303 . 35 GLU N N 115.36 0.040 1 304 . 35 GLU H H 7.39 0.005 1 305 . 35 GLU CA C 55.31 0.020 1 306 . 35 GLU HA H 4.25 0.008 1 307 . 35 GLU CB C 30.75 0.030 1 308 . 35 GLU CG C 36.11 0.020 1 309 . 35 GLU HG2 H 2.13 0.009 1 310 . 35 GLU HG3 H 2.26 0.005 1 311 . 35 GLU HB2 H 1.88 0.009 2 312 . 36 CYS N N 121.83 0.040 1 313 . 36 CYS H H 7.46 0.003 1 314 . 36 CYS CA C 57.19 0.100 1 315 . 36 CYS HA H 4.24 0.007 1 316 . 36 CYS CB C 40.70 0.010 1 317 . 36 CYS HB2 H 2.86 0.007 1 318 . 36 CYS HB3 H 3.31 0.005 1 319 . 37 LYS N N 126.76 0.070 1 320 . 37 LYS H H 7.52 0.005 1 321 . 37 LYS CA C 53.85 0.010 1 322 . 37 LYS HA H 4.57 0.010 1 323 . 37 LYS CB C 35.40 0.080 1 324 . 37 LYS HB2 H 1.59 0.004 1 325 . 37 LYS HB3 H 1.86 0.002 1 326 . 37 LYS CG C 24.35 0.010 1 327 . 37 LYS HG2 H 1.02 0.000 1 328 . 37 LYS HG3 H 1.18 0.000 1 329 . 37 LYS CD C 28.79 0.080 1 330 . 37 LYS CE C 42.10 0.010 1 331 . 37 LYS HE2 H 2.81 0.001 1 332 . 37 LYS HE3 H 2.89 0.000 1 333 . 37 LYS HD2 H 1.56 0.011 2 334 . 38 SER N N 117.22 0.040 1 335 . 38 SER H H 8.47 0.003 1 336 . 38 SER CA C 57.99 0.120 1 337 . 38 SER HA H 4.63 0.015 1 338 . 38 SER CB C 62.82 0.020 1 339 . 38 SER HB2 H 3.76 0.003 1 340 . 38 SER HB3 H 3.85 0.001 1 341 . 39 PRO CA C 64.26 0.110 1 342 . 39 PRO HA H 4.75 0.007 1 343 . 39 PRO CB C 33.31 0.040 1 344 . 39 PRO CG C 25.07 0.040 1 345 . 39 PRO HG2 H 1.41 0.006 1 346 . 39 PRO HG3 H 2.04 0.011 1 347 . 39 PRO CD C 50.30 0.120 1 348 . 39 PRO HB2 H 2.28 0.010 2 349 . 39 PRO HD2 H 3.50 0.008 2 350 . 40 CYS N N 125.77 0.050 1 351 . 40 CYS H H 8.83 0.003 1 352 . 40 CYS CA C 53.76 0.100 1 353 . 40 CYS HA H 5.19 0.006 1 354 . 40 CYS CB C 39.10 0.040 1 355 . 40 CYS HB2 H 2.57 0.006 1 356 . 40 CYS HB3 H 3.45 0.006 1 357 . 41 LYS N N 121.57 0.040 1 358 . 41 LYS H H 9.49 0.002 1 359 . 41 LYS CA C 55.38 0.070 1 360 . 41 LYS HA H 4.39 0.006 1 361 . 41 LYS CB C 36.41 0.020 1 362 . 41 LYS CG C 24.38 0.010 1 363 . 41 LYS HG2 H 1.02 0.003 1 364 . 41 LYS HG3 H 1.15 0.008 1 365 . 41 LYS CD C 28.86 0.010 1 366 . 41 LYS CE C 42.03 0.010 1 367 . 41 LYS HB2 H 1.53 0.016 2 368 . 41 LYS HD2 H 1.53 0.014 2 369 . 41 LYS HE2 H 2.81 0.002 2 370 . 42 TRP N N 126.82 0.080 1 371 . 42 TRP H H 8.65 0.006 1 372 . 42 TRP CA C 56.38 0.100 1 373 . 42 TRP HA H 5.09 0.010 1 374 . 42 TRP CB C 31.18 0.100 1 375 . 42 TRP HB2 H 2.97 0.006 1 376 . 42 TRP HB3 H 3.12 0.002 1 377 . 42 TRP NE1 N 128.64 0.000 1 378 . 42 TRP HE1 H 9.95 0.000 1 379 . 43 HIS N N 127.82 0.040 1 380 . 43 HIS H H 8.57 0.003 1 381 . 43 HIS CA C 53.85 0.010 1 382 . 43 HIS HA H 4.56 0.002 1 383 . 43 HIS CB C 29.20 0.140 1 384 . 43 HIS HB2 H 2.86 0.063 2 385 . 44 ASN N N 121.06 0.020 1 386 . 44 ASN H H 8.61 0.007 1 387 . 44 ASN CA C 53.25 0.000 1 388 . 44 ASN HA H 4.46 0.007 1 389 . 44 ASN CB C 40.92 0.000 1 390 . 44 ASN HB2 H 2.57 0.001 2 391 . 45 ASP HA H 4.60 0.000 1 392 . 46 ALA CA C 52.95 0.130 1 393 . 46 ALA HA H 4.02 0.010 1 394 . 46 ALA CB C 19.11 0.100 1 395 . 46 ALA HB H 1.22 0.003 1 396 . 47 GLU N N 117.95 0.060 1 397 . 47 GLU H H 8.45 0.004 1 398 . 47 GLU CA C 57.47 0.010 1 399 . 47 GLU HA H 4.05 0.011 1 400 . 47 GLU CB C 29.94 0.120 1 401 . 47 GLU HB2 H 1.86 0.020 1 402 . 47 GLU HB3 H 1.95 0.002 1 403 . 47 GLU CG C 35.96 0.010 1 404 . 47 GLU HG2 H 2.13 0.002 2 405 . 48 ASN N N 115.90 0.070 1 406 . 48 ASN H H 7.95 0.005 1 407 . 48 ASN CA C 52.90 0.110 1 408 . 48 ASN HA H 4.62 0.007 1 409 . 48 ASN CB C 39.77 0.040 1 410 . 48 ASN HB2 H 2.59 0.000 1 411 . 48 ASN HB3 H 2.64 0.000 1 412 . 48 ASN ND2 N 113.32 0.200 1 413 . 48 ASN HD21 H 6.82 0.005 1 414 . 48 ASN HD22 H 7.56 0.002 1 415 . 49 LYS N N 120.47 0.040 1 416 . 49 LYS H H 8.07 0.003 1 417 . 49 LYS CA C 55.50 0.040 1 418 . 49 LYS HA H 4.14 0.003 1 419 . 49 LYS CB C 31.74 0.000 1 420 . 49 LYS HB2 H 1.72 0.000 1 421 . 49 LYS HB3 H 1.79 0.000 1 422 . 49 LYS CG C 24.64 0.000 1 423 . 49 LYS HG2 H 1.28 0.003 1 424 . 49 LYS HG3 H 1.32 0.004 1 425 . 49 LYS CD C 29.00 0.070 1 426 . 49 LYS HD2 H 1.60 0.002 1 427 . 49 LYS HD3 H 1.66 0.010 1 428 . 49 LYS CE C 42.06 0.020 1 429 . 49 LYS HE2 H 2.92 0.010 2 430 . 50 LYS N N 119.04 0.040 1 431 . 50 LYS H H 7.58 0.002 1 432 . 50 LYS CA C 57.15 0.060 1 433 . 50 LYS HA H 3.69 0.007 1 434 . 50 LYS CB C 31.90 0.000 1 435 . 50 LYS CG C 24.79 0.050 1 436 . 50 LYS HG2 H 0.93 0.003 1 437 . 50 LYS HG3 H 1.01 0.007 1 438 . 50 LYS CD C 29.38 0.050 1 439 . 50 LYS CE C 42.32 0.010 1 440 . 50 LYS HD2 H 1.42 0.004 2 441 . 50 LYS HE2 H 2.80 0.005 2 442 . 51 CYS CA C 54.80 0.000 1 443 . 51 CYS HA H 5.33 0.007 1 444 . 51 CYS CB C 41.01 0.010 1 445 . 51 CYS HB2 H 3.04 0.003 1 446 . 51 CYS HB3 H 3.88 0.001 1 447 . 52 THR N N 119.66 0.060 1 448 . 52 THR H H 8.86 0.003 1 449 . 52 THR CA C 59.22 0.110 1 450 . 52 THR HA H 4.55 0.016 1 451 . 52 THR CB C 71.24 0.070 1 452 . 52 THR HB H 4.42 0.006 1 453 . 52 THR CG2 C 20.33 0.010 1 454 . 52 THR HG2 H 0.88 0.005 1 455 . 53 LEU N N 123.75 0.060 1 456 . 53 LEU H H 8.95 0.002 1 457 . 53 LEU CA C 55.81 0.090 1 458 . 53 LEU HA H 4.50 0.004 1 459 . 53 LEU CB C 42.97 0.030 1 460 . 53 LEU HB2 H 1.05 0.006 1 461 . 53 LEU HB3 H 1.75 0.005 1 462 . 53 LEU CG C 26.70 0.020 1 463 . 53 LEU HG H 1.28 0.006 1 464 . 53 LEU CD1 C 23.59 0.050 1 465 . 53 LEU HD1 H 0.63 0.005 2 466 . 53 LEU CD2 C 25.79 0.030 1 467 . 53 LEU HD2 H 0.73 0.004 2 468 . 54 ASP N N 127.15 0.100 1 469 . 54 ASP H H 8.58 0.003 1 470 . 54 ASP CA C 53.86 0.080 1 471 . 54 ASP HA H 4.59 0.013 1 472 . 54 ASP CB C 41.62 0.020 1 473 . 54 ASP HB2 H 2.27 0.004 1 474 . 54 ASP HB3 H 2.89 0.005 1 475 . 55 LYS N N 124.41 0.030 1 476 . 55 LYS H H 8.44 0.004 1 477 . 55 LYS CA C 57.57 0.010 1 478 . 55 LYS HA H 4.06 0.008 1 479 . 55 LYS CB C 32.74 0.070 1 480 . 55 LYS HB2 H 1.73 0.008 1 481 . 55 LYS HB3 H 1.78 0.003 1 482 . 55 LYS CG C 24.67 0.000 1 483 . 55 LYS HG2 H 1.35 0.000 1 484 . 55 LYS HG3 H 1.42 0.002 1 485 . 55 LYS CD C 28.90 0.010 1 486 . 55 LYS CE C 41.85 0.180 1 487 . 55 LYS HD2 H 1.67 0.001 2 488 . 55 LYS HE2 H 2.93 0.003 2 489 . 56 GLU N N 120.38 0.070 1 490 . 56 GLU H H 8.26 0.004 1 491 . 56 GLU CA C 57.52 0.020 1 492 . 56 GLU HA H 4.11 0.011 1 493 . 56 GLU CB C 29.47 0.040 1 494 . 56 GLU HB2 H 1.92 0.016 1 495 . 56 GLU HB3 H 2.02 0.000 1 496 . 56 GLU CG C 36.06 0.010 1 497 . 56 GLU HG2 H 2.19 0.000 1 498 . 56 GLU HG3 H 2.27 0.000 1 499 . 57 GLU N N 121.71 0.090 1 500 . 57 GLU H H 8.30 0.009 1 501 . 57 GLU CA C 57.27 0.010 1 502 . 57 GLU HA H 4.09 0.003 1 503 . 57 GLU CB C 29.82 0.010 1 504 . 57 GLU CG C 35.76 0.010 1 505 . 57 GLU HG2 H 2.18 0.000 1 506 . 57 GLU HG3 H 2.27 0.000 1 507 . 57 GLU HB2 H 1.95 0.016 2 508 . 58 ALA N N 122.96 0.070 1 509 . 58 ALA H H 8.32 0.005 1 510 . 58 ALA CA C 53.41 0.060 1 511 . 58 ALA HA H 4.08 0.004 1 512 . 58 ALA CB C 18.49 0.060 1 513 . 58 ALA HB H 1.35 0.008 1 514 . 59 LYS N N 119.30 0.070 1 515 . 59 LYS H H 7.83 0.004 1 516 . 59 LYS CA C 56.84 0.110 1 517 . 59 LYS HA H 4.13 0.005 1 518 . 59 LYS CB C 32.68 0.010 1 519 . 59 LYS HB2 H 1.72 0.017 1 520 . 59 LYS HB3 H 1.78 0.001 1 521 . 59 LYS CG C 24.57 0.010 1 522 . 59 LYS HG2 H 1.35 0.022 1 523 . 59 LYS HG3 H 1.44 0.003 1 524 . 59 LYS CD C 28.95 0.000 1 525 . 59 LYS CE C 41.94 0.010 1 526 . 59 LYS HD2 H 1.61 0.004 2 527 . 59 LYS HE2 H 2.90 0.004 2 528 . 60 LYS N N 121.25 0.060 1 529 . 60 LYS H H 7.89 0.009 1 530 . 60 LYS CA C 56.94 0.140 1 531 . 60 LYS HA H 4.18 0.005 1 532 . 60 LYS CB C 32.70 0.080 1 533 . 60 LYS HB2 H 1.72 0.018 1 534 . 60 LYS HB3 H 1.78 0.015 1 535 . 60 LYS CG C 24.59 0.050 1 536 . 60 LYS HG2 H 1.32 0.014 1 537 . 60 LYS HG3 H 1.42 0.015 1 538 . 60 LYS CD C 29.05 0.000 1 539 . 60 LYS CE C 41.93 0.000 1 540 . 60 LYS HD2 H 1.60 0.006 2 541 . 60 LYS HE2 H 2.89 0.006 2 542 . 61 VAL N N 119.83 0.050 1 543 . 61 VAL H H 7.98 0.006 1 544 . 61 VAL CA C 62.85 0.070 1 545 . 61 VAL HA H 3.95 0.013 1 546 . 61 VAL CB C 32.44 0.070 1 547 . 61 VAL HB H 2.02 0.013 1 548 . 61 VAL CG1 C 20.70 0.060 1 549 . 61 VAL HG1 H 0.84 0.002 2 550 . 61 VAL CG2 C 20.63 0.000 1 551 . 61 VAL HG2 H 0.89 0.001 2 552 . 62 ALA N N 126.18 0.040 1 553 . 62 ALA H H 8.13 0.002 1 554 . 62 ALA CA C 52.96 0.010 1 555 . 62 ALA HA H 4.19 0.010 1 556 . 62 ALA CB C 19.02 0.050 1 557 . 62 ALA HB H 1.35 0.006 1 558 . 63 ASP N N 119.33 0.030 1 559 . 63 ASP H H 8.21 0.007 1 560 . 63 ASP CA C 54.60 0.010 1 561 . 63 ASP HA H 4.49 0.013 1 562 . 63 ASP CB C 40.96 0.020 1 563 . 63 ASP HB2 H 2.61 0.012 2 564 . 64 GLU N N 121.12 0.040 1 565 . 64 GLU H H 8.34 0.003 1 566 . 64 GLU CA C 57.09 0.010 1 567 . 64 GLU HA H 4.23 0.027 1 568 . 64 GLU CB C 29.77 0.080 1 569 . 64 GLU HB2 H 1.94 0.013 1 570 . 64 GLU HB3 H 2.06 0.001 1 571 . 64 GLU CG C 36.16 0.020 1 572 . 64 GLU HG2 H 2.20 0.000 1 573 . 64 GLU HG3 H 2.27 0.000 1 574 . 65 THR N N 113.93 0.040 1 575 . 65 THR H H 8.12 0.003 1 576 . 65 THR CA C 62.61 0.050 1 577 . 65 THR HA H 4.17 0.010 1 578 . 65 THR CB C 69.58 0.030 1 579 . 65 THR HB H 4.16 0.000 1 580 . 65 THR CG2 C 21.42 0.000 1 581 . 65 THR HG2 H 1.17 0.012 1 582 . 66 ALA N N 125.48 0.030 1 583 . 66 ALA H H 8.03 0.005 1 584 . 66 ALA CA C 52.62 0.010 1 585 . 66 ALA HA H 4.23 0.015 1 586 . 66 ALA CB C 18.84 0.050 1 587 . 66 ALA HB H 1.33 0.014 1 588 . 67 LYS N N 119.93 0.040 1 589 . 67 LYS H H 8.09 0.006 1 590 . 67 LYS CA C 56.52 0.090 1 591 . 67 LYS HA H 4.20 0.006 1 592 . 67 LYS CB C 32.72 0.050 1 593 . 67 LYS HB2 H 1.71 0.005 1 594 . 67 LYS HB3 H 1.79 0.013 1 595 . 67 LYS CG C 24.55 0.090 1 596 . 67 LYS CD C 28.92 0.010 1 597 . 67 LYS CE C 42.00 0.070 1 598 . 67 LYS HG2 H 1.35 0.001 2 599 . 67 LYS HD2 H 1.65 0.024 2 600 . 67 LYS HE2 H 2.91 0.001 2 601 . 68 ASP N N 120.02 0.040 1 602 . 68 ASP H H 8.17 0.004 1 603 . 68 ASP CA C 54.36 0.080 1 604 . 68 ASP HA H 4.51 0.008 1 605 . 68 ASP CB C 41.00 0.040 1 606 . 68 ASP HB2 H 2.63 0.005 2 607 . 69 GLY N N 108.60 0.030 1 608 . 69 GLY H H 8.23 0.001 1 609 . 69 GLY CA C 45.43 0.010 1 610 . 69 GLY HA2 H 3.89 0.009 2 611 . 70 LYS N N 120.26 0.020 1 612 . 70 LYS H H 8.12 0.004 1 613 . 70 LYS CA C 56.32 0.080 1 614 . 70 LYS HA H 4.33 0.006 1 615 . 70 LYS CB C 32.75 0.040 1 616 . 70 LYS HB2 H 1.74 0.005 1 617 . 70 LYS HB3 H 1.80 0.011 1 618 . 70 LYS CG C 24.51 0.040 1 619 . 70 LYS HG2 H 1.33 0.000 1 620 . 70 LYS HG3 H 1.39 0.000 1 621 . 70 LYS CD C 29.17 0.010 1 622 . 70 LYS CE C 42.02 0.050 1 623 . 70 LYS HD2 H 1.61 0.007 2 624 . 70 LYS HE2 H 2.91 0.006 2 625 . 71 THR N N 114.04 0.060 1 626 . 71 THR H H 8.12 0.003 1 627 . 71 THR CA C 61.76 0.030 1 628 . 71 THR HA H 4.27 0.014 1 629 . 71 THR CB C 69.69 0.020 1 630 . 71 THR HB H 4.17 0.006 1 631 . 71 THR CG2 C 21.22 0.000 1 632 . 71 THR HG2 H 1.13 0.010 1 633 . 72 GLY N N 110.59 0.060 1 634 . 72 GLY H H 8.34 0.003 1 635 . 72 GLY CA C 45.19 0.030 1 636 . 72 GLY HA2 H 3.91 0.005 2 637 . 73 ASN N N 118.48 0.020 1 638 . 73 ASN H H 8.30 0.003 1 639 . 73 ASN CA C 53.04 0.010 1 640 . 73 ASN HA H 4.71 0.014 1 641 . 73 ASN CB C 39.02 0.010 1 642 . 73 ASN HB2 H 2.71 0.001 1 643 . 73 ASN HB3 H 2.79 0.003 1 644 . 73 ASN ND2 N 112.44 0.250 1 645 . 73 ASN HD21 H 6.85 0.004 1 646 . 73 ASN HD22 H 7.53 0.001 1 647 . 74 THR N N 114.06 0.000 1 648 . 74 THR H H 8.16 0.000 1 649 . 74 THR CA C 61.79 0.060 1 650 . 74 THR HA H 4.30 0.003 1 651 . 74 THR CB C 69.54 0.020 1 652 . 74 THR HB H 4.18 0.001 1 653 . 74 THR CG2 C 21.26 0.010 1 654 . 74 THR HG2 H 1.11 0.001 1 655 . 75 ASN N N 120.80 0.060 1 656 . 75 ASN H H 8.46 0.003 1 657 . 75 ASN CA C 53.19 0.060 1 658 . 75 ASN HA H 4.72 0.013 1 659 . 75 ASN CB C 38.80 0.030 1 660 . 75 ASN HB2 H 2.72 0.017 1 661 . 75 ASN HB3 H 2.81 0.001 1 662 . 76 THR N N 113.95 0.000 1 663 . 76 THR H H 8.16 0.000 1 664 . 76 THR CA C 61.59 0.050 1 665 . 76 THR HA H 4.36 0.001 1 666 . 76 THR CB C 69.58 0.020 1 667 . 76 THR HB H 4.22 0.003 1 668 . 76 THR CG2 C 21.21 0.020 1 669 . 76 THR HG2 H 1.11 0.002 1 670 . 77 THR N N 115.43 0.050 1 671 . 77 THR H H 8.14 0.003 1 672 . 77 THR CA C 62.01 0.050 1 673 . 77 THR HA H 4.29 0.011 1 674 . 77 THR CB C 69.58 0.130 1 675 . 77 THR HB H 4.19 0.003 1 676 . 77 THR CG2 C 21.24 0.020 1 677 . 77 THR HG2 H 1.14 0.008 1 678 . 78 GLY N N 111.13 0.080 1 679 . 78 GLY H H 8.36 0.002 1 680 . 78 GLY CA C 45.22 0.020 1 681 . 78 GLY HA2 H 3.96 0.007 2 682 . 79 SER N N 115.55 0.040 1 683 . 79 SER H H 8.16 0.002 1 684 . 79 SER CA C 58.00 0.080 1 685 . 79 SER HA H 4.47 0.010 1 686 . 79 SER CB C 64.11 0.150 1 687 . 79 SER HB2 H 3.81 0.007 2 688 . 80 SER N N 122.72 0.030 1 689 . 80 SER H H 7.98 0.003 1 690 . 80 SER CA C 59.92 0.110 1 691 . 80 SER HA H 4.22 0.009 1 692 . 80 SER CB C 64.37 0.010 1 693 . 80 SER HB2 H 3.77 0.007 2 stop_ save_