data_4680 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The Structure of a LysM Domain from E.coli Membrane-bound Lytic Murein Transglycosylase D (MltD) ; _BMRB_accession_number 4680 _BMRB_flat_file_name bmr4680.str _Entry_type original _Submission_date 2000-03-06 _Accession_date 2000-03-06 _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 Bateman Alex . . 2 Bycroft Mark . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 333 "13C chemical shifts" 219 "15N chemical shifts" 61 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-12-18 original author . stop_ _Original_release_date 2000-12-18 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Bateman, A., Bycroft, M., "The Structure of a LysM Domain from E.coli Membrane- bound Lytic Murein Transglycosylase D (MltD)," J. Mol. Biol. 299, 1113-1119 (2000). ; _Citation_title ; The Structure of a LysM Domain from E.coli Membrane-bound Lytic Murein Transglycosylase D (MltD) ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20304905 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bateman Alex . . 2 Bycroft Mark . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume 299 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1113 _Page_last 1119 _Year 2000 _Details . save_ ################################## # Molecular system description # ################################## save_LysM_Domain _Saveframe_category molecular_system _Mol_system_name 'C-terminal domain of MLTD' _Abbreviation_common 'LysM Domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label MLTD $MLTD stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MLTD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE D' _Abbreviation_common MLTD _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 65 _Mol_residue_sequence ; GSAQRLANNSDSITYRVRKG DSLSSIAKRHGVNIKDVMRW NSDTANLQPGDKLTLFVKNN NMPDS ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 ALA 4 GLN 5 ARG 6 LEU 7 ALA 8 ASN 9 ASN 10 SER 11 ASP 12 SER 13 ILE 14 THR 15 TYR 16 ARG 17 VAL 18 ARG 19 LYS 20 GLY 21 ASP 22 SER 23 LEU 24 SER 25 SER 26 ILE 27 ALA 28 LYS 29 ARG 30 HIS 31 GLY 32 VAL 33 ASN 34 ILE 35 LYS 36 ASP 37 VAL 38 MET 39 ARG 40 TRP 41 ASN 42 SER 43 ASP 44 THR 45 ALA 46 ASN 47 LEU 48 GLN 49 PRO 50 GLY 51 ASP 52 LYS 53 LEU 54 THR 55 LEU 56 PHE 57 VAL 58 LYS 59 ASN 60 ASN 61 ASN 62 MET 63 PRO 64 ASP 65 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-24 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 1E0G "Lysm Domain From E.Coli Mltd" 73.85 48 100.00 100.00 2.04e-25 GB KOA34578 "lytic murein transglycosylase, partial [Escherichia coli]" 98.46 78 100.00 100.00 2.67e-37 REF WP_032146895 "lytic transglycosylase [Escherichia coli]" 98.46 452 100.00 100.00 1.30e-34 REF WP_057103735 "hypothetical protein [Escherichia coli]" 98.46 88 100.00 100.00 4.64e-37 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MLTD 'Escherichia coli' 562 Bacteria . Escherichia coli 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 $MLTD 'recombinant technology' . . . . . 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 $MLTD 5 mM . 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_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.15 0.02 M pH 6.8 0.1 pH temperature 310 1 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name MLTD _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 3 ALA H H 8.50 0.015 1 2 . 3 ALA HA H 4.22 0.015 1 3 . 3 ALA HB H 1.26 0.015 1 4 . 3 ALA CA C 52.08 0.15 1 5 . 3 ALA CB C 18.64 0.15 1 6 . 3 ALA N N 126.70 0.2 1 7 . 4 GLN H H 8.26 0.015 1 8 . 4 GLN HA H 4.17 0.015 1 9 . 4 GLN HB2 H 1.91 0.015 1 10 . 4 GLN HB3 H 1.91 0.015 1 11 . 4 GLN HG2 H 2.25 0.015 1 12 . 4 GLN HG3 H 2.25 0.015 1 13 . 4 GLN N N 119.64 0.2 1 14 . 5 ARG H H 8.29 0.015 1 15 . 5 ARG HA H 4.21 0.015 1 16 . 5 ARG HB2 H 1.70 0.015 1 17 . 5 ARG HB3 H 1.70 0.015 1 18 . 5 ARG HG2 H 1.49 0.015 1 19 . 5 ARG HG3 H 1.49 0.015 1 20 . 5 ARG HD2 H 3.08 0.015 1 21 . 5 ARG HD3 H 3.08 0.015 1 22 . 5 ARG CA C 55.49 0.15 1 23 . 5 ARG CB C 30.17 0.15 1 24 . 5 ARG N N 122.70 0.2 1 25 . 6 LEU H H 8.25 0.015 1 26 . 6 LEU HA H 4.22 0.015 1 27 . 6 LEU HB2 H 1.50 0.015 1 28 . 6 LEU HB3 H 1.50 0.015 1 29 . 6 LEU HG H 1.49 0.015 1 30 . 6 LEU HD1 H 0.75 0.015 2 31 . 6 LEU HD2 H 0.81 0.015 2 32 . 6 LEU CA C 54.25 0.15 1 33 . 6 LEU CB C 41.78 0.15 2 34 . 6 LEU CG C 26.5 0.15 1 35 . 6 LEU CD1 C 24.1 0.15 2 36 . 6 LEU CD2 C 24.4 0.15 2 37 . 6 LEU N N 123.65 0.2 1 38 . 7 ALA H H 8.22 0.015 1 39 . 7 ALA HA H 4.14 0.015 1 40 . 7 ALA HB H 1.23 0.015 1 41 . 7 ALA CA C 51.95 0.15 1 42 . 7 ALA CB C 18.84 0.15 1 43 . 7 ALA N N 124.45 0.2 1 44 . 8 ASN H H 8.28 0.015 1 45 . 8 ASN HA H 4.56 0.015 1 46 . 8 ASN HB2 H 2.72 0.015 1 47 . 8 ASN HB3 H 2.72 0.015 1 48 . 8 ASN CA C 52.82 0.15 1 49 . 8 ASN CB C 38.45 0.15 1 50 . 8 ASN N N 118.12 0.2 1 51 . 9 ASN H H 8.47 0.015 1 52 . 9 ASN HA H 4.62 0.015 1 53 . 9 ASN HB2 H 2.70 0.015 1 54 . 9 ASN HB3 H 2.70 0.015 1 55 . 9 ASN CA C 53.05 0.15 1 56 . 9 ASN CB C 38.39 0.15 1 57 . 9 ASN N N 119.22 0.2 1 58 . 10 SER H H 8.19 0.015 1 59 . 10 SER HA H 4.43 0.015 1 60 . 10 SER HB2 H 3.73 0.015 1 61 . 10 SER HB3 H 3.73 0.015 1 62 . 10 SER CA C 58.13 0.15 1 63 . 10 SER CB C 63.68 0.15 1 64 . 10 SER N N 115.43 0.2 1 65 . 11 ASP H H 8.38 0.015 1 66 . 11 ASP HA H 4.62 0.015 1 67 . 11 ASP HB2 H 2.58 0.015 1 68 . 11 ASP HB3 H 2.58 0.015 1 69 . 11 ASP C C 172.95 0.15 1 70 . 11 ASP CA C 53.71 0.15 1 71 . 11 ASP CB C 41.08 0.15 1 72 . 11 ASP N N 121.82 0.2 1 73 . 12 SER H H 7.87 0.015 1 74 . 12 SER HA H 4.33 0.015 1 75 . 12 SER HB2 H 3.00 0.015 1 76 . 12 SER HB3 H 2.75 0.015 1 77 . 12 SER C C 171.85 0.15 1 78 . 12 SER CA C 56.17 0.15 1 79 . 12 SER CB C 64.40 0.15 1 80 . 12 SER N N 113.62 0.2 1 81 . 13 ILE H H 8.48 0.015 1 82 . 13 ILE HA H 4.44 0.015 1 83 . 13 ILE HB H 1.69 0.015 1 84 . 13 ILE HG12 H 0.87 0.015 2 85 . 13 ILE HG13 H 1.09 0.015 2 86 . 13 ILE HG2 H 0.74 0.015 1 87 . 13 ILE HD1 H 0.72 0.015 1 88 . 13 ILE C C 175.28 0.15 1 89 . 13 ILE CA C 58.7 0.15 1 90 . 13 ILE CB C 40.8 0.15 1 91 . 13 ILE CG1 C 26.1 0.15 1 92 . 13 ILE CG2 C 17.3 0.15 1 93 . 13 ILE CD1 C 13.6 0.15 1 94 . 13 ILE N N 117.2 0.2 1 95 . 14 THR H H 8.29 0.015 1 96 . 14 THR HA H 4.76 0.015 1 97 . 14 THR HB H 3.74 0.015 1 98 . 14 THR HG2 H 0.90 0.015 1 99 . 14 THR C C 171.5 0.15 1 100 . 14 THR CA C 60.7 0.15 1 101 . 14 THR CB C 69.2 0.15 1 102 . 14 THR CG2 C 21.1 0.15 1 103 . 14 THR N N 118.1 0.2 1 104 . 15 TYR H H 9.35 0.015 1 105 . 15 TYR HA H 4.41 0.015 1 106 . 15 TYR HB2 H 2.38 0.015 1 107 . 15 TYR HB3 H 2.38 0.015 1 108 . 15 TYR HD1 H 6.81 0.015 1 109 . 15 TYR HD2 H 6.81 0.015 1 110 . 15 TYR HE1 H 6.74 0.015 1 111 . 15 TYR HE2 H 6.74 0.015 1 112 . 15 TYR C C 171.2 0.15 1 113 . 15 TYR CA C 56.39 0.15 1 114 . 15 TYR CB C 41.35 0.15 1 115 . 15 TYR CD1 C 136.70 0.15 1 116 . 15 TYR CD2 C 136.70 0.15 1 117 . 15 TYR CE1 C 118.58 0.15 1 118 . 15 TYR CE2 C 118.58 0.15 1 119 . 15 TYR N N 129.07 0.2 1 120 . 16 ARG H H 7.58 0.015 1 121 . 16 ARG HA H 4.57 0.015 1 122 . 16 ARG HB2 H 1.30 0.015 1 123 . 16 ARG HB3 H 1.30 0.015 1 124 . 16 ARG C C 171.80 0.15 1 125 . 16 ARG CA C 53.24 0.15 1 126 . 16 ARG CB C 29.81 0.15 1 127 . 17 VAL H H 8.63 0.015 1 128 . 17 VAL HA H 3.62 0.015 1 129 . 17 VAL HB H 1.95 0.015 1 130 . 17 VAL HG1 H 0.72 0.015 1 131 . 17 VAL HG2 H 0.92 0.015 1 132 . 17 VAL C C 174.4 0.15 1 133 . 17 VAL CA C 63.6 0.15 1 134 . 17 VAL CB C 30.9 0.15 1 135 . 17 VAL CG1 C 21.7 0.15 1 136 . 17 VAL CG2 C 22.9 0.15 1 137 . 17 VAL N N 124.59 0.2 1 138 . 18 ARG H H 9.08 0.015 1 139 . 18 ARG HA H 4.47 0.015 1 140 . 18 ARG HB2 H 1.61 0.015 2 141 . 18 ARG HB3 H 1.80 0.015 2 142 . 18 ARG C C 174.22 0.15 1 143 . 18 ARG CA C 53.41 0.15 1 144 . 18 ARG CB C 32.52 0.15 1 145 . 18 ARG N N 130.2 0.2 1 146 . 19 LYS H H 8.70 0.015 1 147 . 19 LYS HA H 3.91 0.015 1 148 . 19 LYS HB2 H 1.67 0.015 1 149 . 19 LYS HB3 H 1.67 0.015 1 150 . 19 LYS C C 175.35 0.15 1 151 . 19 LYS CA C 58.26 0.15 1 152 . 19 LYS CB C 31.47 0.15 1 153 . 19 LYS N N 122.96 0.2 1 154 . 20 GLY H H 9.05 0.015 1 155 . 20 GLY HA2 H 3.57 0.015 2 156 . 20 GLY HA3 H 4.27 0.015 2 157 . 20 GLY C C 172.80 0.15 1 158 . 20 GLY CA C 44.44 0.15 1 159 . 20 GLY N N 115.90 0.2 1 160 . 21 ASP H H 7.93 0.015 1 161 . 21 ASP HA H 4.48 0.015 1 162 . 21 ASP HB2 H 3.06 0.015 2 163 . 21 ASP HB3 H 2.38 0.015 2 164 . 21 ASP C C 173.77 0.15 1 165 . 21 ASP CA C 54.71 0.15 1 166 . 21 ASP CB C 41.81 0.15 1 167 . 21 ASP N N 120.65 0.2 1 168 . 22 SER H H 8.44 0.015 1 169 . 22 SER HA H 4.15 0.015 1 170 . 22 SER HB2 H 3.81 0.015 1 171 . 22 SER HB3 H 3.81 0.015 1 172 . 22 SER C C 172.10 0.15 1 173 . 22 SER CA C 55.0 0.15 1 174 . 22 SER CB C 66.9 0.15 1 175 . 22 SER N N 113.8 0.2 1 176 . 23 LEU H H 9.20 0.015 1 177 . 23 LEU HA H 3.81 0.015 1 178 . 23 LEU HB2 H 1.70 0.015 2 179 . 23 LEU HB3 H 1.52 0.015 2 180 . 23 LEU HG H 1.59 0.015 1 181 . 23 LEU HD1 H 0.86 0.015 1 182 . 23 LEU HD2 H 0.79 0.015 1 183 . 23 LEU C C 176.4 0.15 1 184 . 23 LEU CA C 58.5 0.15 1 185 . 23 LEU CB C 41.0 0.15 1 186 . 23 LEU CG C 26.6 0.15 1 187 . 23 LEU CD1 C 24.3 0.15 1 188 . 23 LEU CD2 C 24.2 0.15 1 189 . 23 LEU N N 122.2 0.2 1 190 . 24 SER H H 8.34 0.015 1 191 . 24 SER HA H 3.94 0.015 1 192 . 24 SER HB2 H 3.75 0.015 2 193 . 24 SER HB3 H 3.77 0.015 2 194 . 24 SER C C 175.21 0.15 1 195 . 24 SER CA C 61.14 0.15 1 196 . 24 SER CB C 62.32 0.15 1 197 . 24 SER N N 110.02 0.2 1 198 . 25 SER H H 8.29 0.015 1 199 . 25 SER HA H 4.37 0.015 1 200 . 25 SER HB2 H 3.78 0.015 1 201 . 25 SER HB3 H 3.78 0.015 1 202 . 25 SER C C 172.92 0.15 1 203 . 25 SER CA C 57.92 0.15 1 204 . 25 SER CB C 63.53 0.15 1 205 . 25 SER N N 120.56 0.2 1 206 . 26 ILE H H 8.50 0.015 1 207 . 26 ILE HA H 3.47 0.015 1 208 . 26 ILE HB H 1.65 0.015 1 209 . 26 ILE HG12 H 0.69 0.015 2 210 . 26 ILE HG13 H 1.80 0.015 2 211 . 26 ILE HG2 H 0.29 0.015 1 212 . 26 ILE HD1 H 0.76 0.015 1 213 . 26 ILE C C 173.2 0.15 1 214 . 26 ILE CA C 64.80 0.15 1 215 . 26 ILE CB C 38.50 0.15 1 216 . 26 ILE CG1 C 28.01 0.15 1 217 . 26 ILE CG2 C 16.28 0.15 1 218 . 26 ILE CD1 C 14.93 0.15 1 219 . 26 ILE N N 126.01 0.2 1 220 . 27 ALA H H 8.29 0.015 1 221 . 27 ALA HA H 3.70 0.015 1 222 . 27 ALA HB H 1.32 0.015 1 223 . 27 ALA C C 177.07 0.15 1 224 . 27 ALA CA C 54.99 0.15 1 225 . 27 ALA CB C 17.01 0.15 1 226 . 27 ALA N N 123.48 0.2 1 227 . 28 LYS H H 8.03 0.015 1 228 . 28 LYS HA H 4.07 0.015 1 229 . 28 LYS HB2 H 1.84 0.015 2 230 . 28 LYS HB3 H 1.77 0.015 2 231 . 28 LYS HG2 H 1.33 0.015 1 232 . 28 LYS HG3 H 1.33 0.015 1 233 . 28 LYS HD2 H 1.48 0.015 1 234 . 28 LYS HD3 H 1.48 0.015 1 235 . 28 LYS HE2 H 2.82 0.015 1 236 . 28 LYS HE3 H 2.82 0.015 1 237 . 28 LYS C C 178.49 0.15 1 238 . 28 LYS CA C 58.77 0.15 1 239 . 28 LYS CB C 31.90 0.15 1 240 . 28 LYS N N 117.64 0.2 1 241 . 29 ARG H H 8.07 0.015 1 242 . 29 ARG HA H 3.90 0.015 1 243 . 29 ARG HB2 H 1.73 0.015 2 244 . 29 ARG HB3 H 1.50 0.015 2 245 . 29 ARG C C 175.02 0.15 1 246 . 29 ARG CA C 57.94 0.15 1 247 . 29 ARG CB C 29.38 0.15 1 248 . 29 ARG N N 117.98 0.2 1 249 . 30 HIS H H 7.32 0.015 1 250 . 30 HIS HA H 4.50 0.015 1 251 . 30 HIS HB2 H 2.50 0.015 1 252 . 30 HIS HB3 H 3.47 0.015 1 253 . 30 HIS HD2 H 6.74 0.015 1 254 . 30 HIS HE1 H 6.67 0.015 1 255 . 30 HIS C C 172.01 0.15 1 256 . 30 HIS CA C 57.26 0.15 1 257 . 30 HIS CB C 29.02 0.15 1 258 . 30 HIS CD2 C 118.60 0.15 1 259 . 30 HIS CE1 C 136.60 0.15 1 260 . 30 HIS N N 113.00 0.2 1 261 . 31 GLY H H 7.76 0.015 1 262 . 31 GLY HA2 H 3.92 0.015 1 263 . 31 GLY HA3 H 3.92 0.015 1 264 . 31 GLY C C 172.80 0.15 1 265 . 31 GLY CA C 46.5 0.15 1 266 . 31 GLY N N 109.1 0.2 1 267 . 32 VAL H H 7.90 0.015 1 268 . 32 VAL HA H 4.78 0.015 1 269 . 32 VAL HB H 2.52 0.015 1 270 . 32 VAL HG1 H 1.10 0.015 1 271 . 32 VAL HG2 H 0.75 0.015 1 272 . 32 VAL C C 171.87 0.15 1 273 . 32 VAL CA C 57.9 0.15 1 274 . 32 VAL CB C 33.7 0.15 1 275 . 32 VAL CG1 C 21.6 0.15 1 276 . 32 VAL CG2 C 19.0 0.15 1 277 . 32 VAL N N 110.9 0.2 1 278 . 33 ASN H H 8.84 0.015 1 279 . 33 ASN HA H 4.81 0.015 1 280 . 33 ASN HB2 H 2.62 0.015 1 281 . 33 ASN HB3 H 2.62 0.015 1 282 . 33 ASN C C 175.52 0.15 1 283 . 33 ASN CA C 51.54 0.15 1 284 . 33 ASN CB C 39.70 0.15 1 285 . 33 ASN N N 118.70 0.2 1 286 . 34 ILE H H 9.00 0.015 1 287 . 34 ILE HA H 3.37 0.015 1 288 . 34 ILE HB H 1.68 0.015 1 289 . 34 ILE HG12 H 1.40 0.015 1 290 . 34 ILE HG13 H 1.40 0.015 1 291 . 34 ILE HG2 H 0.82 0.015 1 292 . 34 ILE HD1 H 0.79 0.015 1 293 . 34 ILE C C 172.75 0.15 1 294 . 34 ILE CA C 65.74 0.15 1 295 . 34 ILE CB C 37.43 0.15 1 296 . 34 ILE CG1 C 28.30 0.15 1 297 . 34 ILE CG2 C 16.97 0.15 1 298 . 34 ILE CD1 C 13.34 0.15 1 299 . 34 ILE N N 125.50 0.2 1 300 . 35 LYS H H 8.44 0.015 1 301 . 35 LYS HA H 3.82 0.015 1 302 . 35 LYS HB2 H 1.58 0.015 1 303 . 35 LYS HB3 H 1.58 0.015 1 304 . 35 LYS HG2 H 1.18 0.015 2 305 . 35 LYS HG3 H 1.29 0.015 2 306 . 35 LYS HD2 H 1.49 0.015 1 307 . 35 LYS HD3 H 1.49 0.015 1 308 . 35 LYS HE2 H 2.78 0.015 1 309 . 35 LYS HE3 H 2.78 0.015 1 310 . 35 LYS C C 177.23 0.15 1 311 . 35 LYS CA C 58.56 0.15 1 312 . 35 LYS CB C 31.35 0.15 1 313 . 35 LYS N N 118.20 0.2 1 314 . 36 ASP H H 7.10 0.015 1 315 . 36 ASP HA H 3.67 0.015 1 316 . 36 ASP HB2 H 2.25 0.015 2 317 . 36 ASP HB3 H 1.24 0.015 2 318 . 36 ASP C C 173.72 0.15 1 319 . 36 ASP CA C 56.26 0.15 1 320 . 36 ASP CB C 39.71 0.15 1 321 . 36 ASP N N 118.64 0.2 1 322 . 37 VAL H H 6.91 0.015 1 323 . 37 VAL HA H 3.32 0.015 1 324 . 37 VAL HB H 2.08 0.015 1 325 . 37 VAL HG1 H 0.82 0.015 1 326 . 37 VAL HG2 H 0.79 0.015 1 327 . 37 VAL C C 176.81 0.15 1 328 . 37 VAL CA C 66.73 0.15 1 329 . 37 VAL CB C 30.8 0.15 1 330 . 37 VAL CG1 C 22.3 0.15 1 331 . 37 VAL CG2 C 22.6 0.15 1 332 . 37 VAL N N 116.6 0.2 1 333 . 38 MET H H 7.71 0.015 1 334 . 38 MET HA H 4.04 0.015 1 335 . 38 MET HB2 H 1.77 0.015 2 336 . 38 MET HB3 H 2.12 0.015 2 337 . 38 MET HG2 H 2.41 0.015 2 338 . 38 MET HG3 H 2.51 0.015 2 339 . 38 MET HE H 1.92 0.015 1 340 . 38 MET C C 174.52 0.15 1 341 . 38 MET CA C 58.1 0.15 1 342 . 38 MET CB C 32.8 0.15 1 343 . 38 MET CG C 31.5 0.15 1 344 . 38 MET CE C 15.9 0.15 1 345 . 38 MET N N 115.6 0.2 1 346 . 39 ARG H H 7.31 0.015 1 347 . 39 ARG HA H 4.01 0.015 1 348 . 39 ARG HB2 H 1.54 0.015 2 349 . 39 ARG HB3 H 1.64 0.015 2 350 . 39 ARG HG2 H 1.41 0.015 1 351 . 39 ARG HG3 H 1.41 0.015 1 352 . 39 ARG HD2 H 3.03 0.015 2 353 . 39 ARG HD3 H 3.07 0.015 2 354 . 39 ARG C C 176.66 0.15 1 355 . 39 ARG CA C 58.00 0.15 1 356 . 39 ARG CB C 29.46 0.15 1 357 . 39 ARG N N 119.4 0.2 1 358 . 40 TRP H H 7.62 0.015 1 359 . 40 TRP HA H 4.78 0.015 1 360 . 40 TRP HB2 H 3.26 0.015 1 361 . 40 TRP HB3 H 3.26 0.015 1 362 . 40 TRP HD1 H 7.12 0.015 1 363 . 40 TRP HE1 H 10.06 0.015 1 364 . 40 TRP HE3 H 7.70 0.015 1 365 . 40 TRP HZ2 H 7.50 0.015 1 366 . 40 TRP HZ3 H 6.80 0.015 1 367 . 40 TRP HH2 H 7.28 0.015 1 368 . 40 TRP C C 173.70 0.15 1 369 . 40 TRP CA C 55.87 0.15 1 370 . 40 TRP CB C 30.17 0.15 1 371 . 40 TRP CD1 C 129.2 0.15 1 372 . 40 TRP CE3 C 121.2 0.15 1 373 . 40 TRP CZ2 C 115.5 0.15 1 374 . 40 TRP CZ3 C 118.6 0.15 1 375 . 40 TRP CH2 C 124.9 0.15 1 376 . 40 TRP N N 117.2 0.2 1 377 . 40 TRP NE1 N 129.2 0.2 1 378 . 41 ASN H H 7.44 0.015 1 379 . 41 ASN HA H 5.09 0.015 1 380 . 41 ASN HB2 H 2.54 0.015 1 381 . 41 ASN HB3 H 2.54 0.015 1 382 . 41 ASN HD21 H 8.34 0.015 1 383 . 41 ASN HD22 H 8.80 0.015 1 384 . 41 ASN C C 170.96 0.15 1 385 . 41 ASN CA C 51.92 0.15 1 386 . 41 ASN CB C 41.93 0.15 1 387 . 41 ASN N N 115.8 0.2 1 388 . 41 ASN ND2 N 118.5 0.2 1 389 . 42 SER H H 8.60 0.015 1 390 . 42 SER HA H 4.32 0.015 1 391 . 42 SER HB2 H 3.87 0.015 1 392 . 42 SER HB3 H 3.87 0.015 1 393 . 42 SER C C 172.51 0.15 1 394 . 42 SER CA C 59.61 0.15 1 395 . 42 SER CB C 63.29 0.15 1 396 . 42 SER N N 116.1 0.2 1 397 . 43 ASP H H 8.61 0.015 1 398 . 43 ASP HA H 4.77 0.015 1 399 . 43 ASP HB2 H 2.78 0.015 2 400 . 43 ASP HB3 H 2.50 0.015 2 401 . 43 ASP C C 174.23 0.15 1 402 . 43 ASP CA C 53.59 0.15 1 403 . 43 ASP CB C 40.26 0.15 1 404 . 43 ASP N N 120.8 0.2 1 405 . 44 THR H H 8.04 0.015 1 406 . 44 THR HA H 4.16 0.015 1 407 . 44 THR HB H 4.36 0.015 1 408 . 44 THR HG2 H 0.98 0.015 1 409 . 44 THR C C 172.57 0.15 1 410 . 44 THR CA C 61.4 0.15 1 411 . 44 THR CB C 69.1 0.15 1 412 . 44 THR CG2 C 21.4 0.15 1 413 . 44 THR N N 111.5 0.2 1 414 . 45 ALA H H 8.11 0.015 1 415 . 45 ALA HA H 4.16 0.015 1 416 . 45 ALA HB H 1.31 0.015 1 417 . 45 ALA C C 175.70 0.15 1 418 . 45 ALA CA C 51.8 0.15 1 419 . 45 ALA CB C 19.0 0.15 1 420 . 45 ALA N N 124.5 0.2 1 421 . 46 ASN H H 8.32 0.015 1 422 . 46 ASN HA H 4.78 0.015 1 423 . 46 ASN HB2 H 2.72 0.015 2 424 . 46 ASN HB3 H 2.46 0.015 2 425 . 46 ASN C C 171.97 0.15 1 426 . 46 ASN CA C 51.50 0.15 1 427 . 46 ASN CB C 38.39 0.15 1 428 . 46 ASN N N 117.5 0.2 1 429 . 47 LEU H H 7.70 0.015 1 430 . 47 LEU HA H 4.18 0.015 1 431 . 47 LEU HB2 H 1.59 0.015 2 432 . 47 LEU HB3 H 1.28 0.015 2 433 . 47 LEU HG H 1.49 0.015 1 434 . 47 LEU HD1 H 0.79 0.015 1 435 . 47 LEU HD2 H 0.77 0.015 1 436 . 47 LEU C C 174.75 0.15 1 437 . 47 LEU CA C 55.1 0.15 1 438 . 47 LEU CB C 42.4 0.15 1 439 . 47 LEU CG C 26.3 0.15 1 440 . 47 LEU CD1 C 25.5 0.15 1 441 . 47 LEU CD2 C 24.1 0.15 1 442 . 47 LEU N N 121.2 0.2 1 443 . 48 GLN H H 8.90 0.015 1 444 . 48 GLN HA H 4.68 0.015 1 445 . 48 GLN HB2 H 1.71 0.015 2 446 . 48 GLN HB3 H 1.90 0.015 2 447 . 48 GLN HG2 H 2.26 0.015 2 448 . 48 GLN HG3 H 2.62 0.015 2 449 . 48 GLN N N 124.4 0.2 1 450 . 49 PRO HA H 3.72 0.015 1 451 . 49 PRO HB2 H 2.00 0.015 2 452 . 49 PRO HB3 H 1.84 0.015 2 453 . 49 PRO HG2 H 2.07 0.015 2 454 . 49 PRO HG3 H 1.58 0.015 2 455 . 49 PRO HD2 H 3.50 0.015 1 456 . 49 PRO HD3 H 3.50 0.015 1 457 . 49 PRO C C 175.23 0.15 1 458 . 49 PRO CA C 63.08 0.15 1 459 . 49 PRO CB C 30.88 0.15 1 460 . 49 PRO CG C 28.91 0.15 1 461 . 49 PRO CD C 49.65 0.15 1 462 . 50 GLY H H 9.04 0.015 1 463 . 50 GLY HA2 H 4.39 0.015 2 464 . 50 GLY HA3 H 3.30 0.015 2 465 . 50 GLY C C 172.52 0.15 1 466 . 50 GLY CA C 44.27 0.15 1 467 . 50 GLY N N 114.15 0.2 1 468 . 51 ASP H H 8.02 0.015 1 469 . 51 ASP HA H 4.44 0.015 1 470 . 51 ASP HB2 H 2.63 0.015 1 471 . 51 ASP HB3 H 2.52 0.015 1 472 . 51 ASP C C 172.78 0.15 1 473 . 51 ASP CA C 54.90 0.15 1 474 . 51 ASP CB C 40.53 0.15 1 475 . 51 ASP N N 122.57 0.2 1 476 . 52 LYS H H 8.45 0.015 1 477 . 52 LYS HA H 4.88 0.015 1 478 . 52 LYS HB2 H 1.45 0.015 1 479 . 52 LYS HB3 H 1.45 0.015 1 480 . 52 LYS HG2 H 1.31 0.015 2 481 . 52 LYS HG3 H 1.01 0.015 2 482 . 52 LYS HD2 H 1.49 0.015 1 483 . 52 LYS HD3 H 1.49 0.015 1 484 . 52 LYS HE2 H 2.81 0.015 1 485 . 52 LYS HE3 H 2.81 0.015 1 486 . 52 LYS C C 174.08 0.15 1 487 . 52 LYS CA C 54.74 0.15 1 488 . 52 LYS CB C 33.78 0.15 1 489 . 52 LYS N N 118.87 0.2 1 490 . 53 LEU H H 9.13 0.015 1 491 . 53 LEU HA H 4.63 0.015 1 492 . 53 LEU HB2 H 1.49 0.015 1 493 . 53 LEU HB3 H 1.19 0.015 1 494 . 53 LEU HG H 1.45 0.015 1 495 . 53 LEU HD1 H 0.72 0.015 1 496 . 53 LEU HD2 H 0.70 0.015 1 497 . 53 LEU C C 173.8 0.15 1 498 . 53 LEU CA C 52.2 0.15 1 499 . 53 LEU CB C 45.2 0.15 1 500 . 53 LEU CG C 26.3 0.15 1 501 . 53 LEU CD1 C 26.6 0.15 1 502 . 53 LEU CD2 C 22.5 0.15 1 503 . 53 LEU N N 122.8 0.2 1 504 . 54 THR H H 9.75 0.015 1 505 . 54 THR HA H 4.53 0.015 1 506 . 54 THR HB H 3.72 0.015 1 507 . 54 THR HG2 H 0.59 0.015 1 508 . 54 THR C C 172.12 0.15 1 509 . 54 THR CA C 62.32 0.15 1 510 . 54 THR CB C 69.16 0.15 1 511 . 54 THR CG2 C 21.4 0.15 1 512 . 54 THR N N 120.8 0.2 1 513 . 55 LEU H H 8.44 0.015 1 514 . 55 LEU HA H 4.55 0.015 1 515 . 55 LEU HB2 H 1.21 0.015 2 516 . 55 LEU HB3 H 0.87 0.015 2 517 . 55 LEU HG H 1.18 0.015 1 518 . 55 LEU HD1 H -.10 0.015 1 519 . 55 LEU HD2 H 0.67 0.015 1 520 . 55 LEU CA C 52.5 0.15 1 521 . 55 LEU CB C 44.6 0.15 1 522 . 55 LEU CG C 24.7 0.15 1 523 . 55 LEU CD1 C 24.5 0.15 1 524 . 55 LEU CD2 C 24.7 0.15 1 525 . 55 LEU N N 123.90 0.2 1 526 . 56 PHE HA H 4.34 0.015 1 527 . 56 PHE HB2 H 2.47 0.015 2 528 . 56 PHE HB3 H 1.75 0.015 2 529 . 56 PHE HD1 H 5.74 0.015 1 530 . 56 PHE HD2 H 5.74 0.015 1 531 . 56 PHE HE1 H 6.83 0.015 1 532 . 56 PHE HE2 H 6.83 0.015 1 533 . 56 PHE HZ H 6.95 0.015 1 534 . 56 PHE C C 173.37 0.15 1 535 . 56 PHE CA C 56.37 0.15 1 536 . 56 PHE CB C 37.85 0.15 1 537 . 56 PHE CD1 C 131.1 0.15 1 538 . 56 PHE CD2 C 131.1 0.15 1 539 . 56 PHE CE1 C 131.0 0.15 1 540 . 56 PHE CE2 C 131.0 0.15 1 541 . 56 PHE CZ C 129.2 0.15 1 542 . 57 VAL H H 7.73 0.015 1 543 . 57 VAL HA H 4.32 0.015 1 544 . 57 VAL HB H 2.07 0.015 1 545 . 57 VAL HG1 H 0.85 0.015 1 546 . 57 VAL HG2 H 0.70 0.015 1 547 . 57 VAL C C 173.15 0.15 1 548 . 57 VAL CA C 59.63 0.15 1 549 . 57 VAL CB C 33.71 0.15 1 550 . 57 VAL CG1 C 21.4 0.15 1 551 . 57 VAL CG2 C 19.0 0.15 1 552 . 57 VAL N N 117.0 0.2 1 553 . 58 LYS H H 8.33 0.015 1 554 . 58 LYS HA H 4.31 0.015 1 555 . 58 LYS HB2 H 1.72 0.015 1 556 . 58 LYS HB3 H 1.72 0.015 1 557 . 58 LYS C C 174.50 0.15 1 558 . 58 LYS CA C 55.55 0.15 1 559 . 58 LYS CB C 32.77 0.15 1 560 . 58 LYS N N 123.30 0.2 1 561 . 59 ASN H H 8.46 0.015 1 562 . 59 ASN HA H 4.59 0.015 1 563 . 59 ASN HB2 H 2.70 0.015 1 564 . 59 ASN HB3 H 2.70 0.015 1 565 . 59 ASN CA C 52.55 0.15 1 566 . 59 ASN CB C 38.37 0.15 1 567 . 59 ASN N N 120.4 0.2 1 568 . 60 ASN H H 8.36 0.015 1 569 . 60 ASN HA H 4.64 0.015 1 570 . 60 ASN HB2 H 2.69 0.015 1 571 . 60 ASN HB3 H 2.69 0.015 1 572 . 60 ASN CA C 52.87 0.15 1 573 . 60 ASN CB C 38.38 0.15 1 574 . 60 ASN N N 119.3 0.2 1 575 . 61 ASN H H 8.35 0.015 1 576 . 61 ASN HA H 4.57 0.015 1 577 . 61 ASN HB2 H 2.66 0.015 1 578 . 61 ASN HB3 H 2.66 0.015 1 579 . 61 ASN CA C 52.9 0.15 1 580 . 61 ASN CB C 38.4 0.15 1 581 . 61 ASN N N 118.30 0.2 1 582 . 62 MET H H 8.12 0.015 1 583 . 62 MET HA H 4.69 0.015 1 584 . 62 MET HB2 H 1.97 0.015 2 585 . 62 MET HB3 H 1.87 0.015 2 586 . 62 MET HG2 H 2.54 0.015 2 587 . 62 MET HG3 H 2.45 0.015 2 588 . 62 MET HE H 2.00 0.015 1 589 . 62 MET CG C 31.5 0.15 1 590 . 62 MET CE C 16.5 0.15 1 591 . 62 MET N N 121.0 0.2 1 592 . 63 PRO HA H 4.35 0.015 1 593 . 63 PRO HB2 H 2.22 0.015 2 594 . 63 PRO HB3 H 1.90 0.015 2 595 . 63 PRO HG2 H 2.24 0.015 1 596 . 63 PRO HG3 H 2.24 0.015 1 597 . 63 PRO HD2 H 3.61 0.015 2 598 . 63 PRO HD3 H 3.70 0.015 2 599 . 63 PRO CA C 62.7 0.15 1 600 . 63 PRO CB C 31.8 0.15 1 601 . 63 PRO CD C 50.1 0.15 1 602 . 64 ASP H H 8.43 0.015 1 603 . 64 ASP HA H 4.51 0.015 1 604 . 64 ASP HB2 H 2.61 0.015 2 605 . 64 ASP HB3 H 2.54 0.015 2 606 . 64 ASP CA C 54.0 0.15 1 607 . 64 ASP CB C 40.6 0.15 1 608 . 64 ASP N N 120.6 0.2 1 609 . 65 SER H H 7.76 0.015 1 610 . 65 SER HA H 4.12 0.015 1 611 . 65 SER HB2 H 3.73 0.015 1 612 . 65 SER HB3 H 3.73 0.015 1 613 . 65 SER N N 120.3 0.2 1 stop_ save_