data_6359 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assigned chemical shift for YGGX ; _BMRB_accession_number 6359 _BMRB_flat_file_name bmr6359.str _Entry_type original _Submission_date 2004-10-18 _Accession_date 2004-10-18 _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 Cui Qiu . Sr. 2 Westler William M. . 3 Markley John L. . 4 Thorgersen Michael P. . 5 Downs Diana M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 482 "13C chemical shifts" 352 "15N chemical shifts" 99 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-01-29 original author . stop_ _Original_release_date 2007-01-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of YggX: A prokaryotic protein involved in Fe(II) trafficking. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16329120 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cui Qiu . . 2 Thorgersen Michael P. . 3 Westler William M. . 4 Markley John L. . 5 Downs Diana M. . stop_ _Journal_abbreviation Proteins _Journal_volume 62 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 578 _Page_last 586 _Year 2005 _Details . save_ ################################## # Molecular system description # ################################## save_molecular_system_YGGX _Saveframe_category molecular_system _Mol_system_name YGGX _Abbreviation_common YGGX _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label YGGX $YGGX stop_ _System_molecular_weight 10898 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_YGGX _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common YGGX _Name_variant yggx _Abbreviation_common yggx _Molecular_mass 10898 _Mol_thiol_state 'all free' loop_ _Biological_function 'Fe(II) traffick and minimize the DNA damage caused by hydroxyl radicals' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 91 _Mol_residue_sequence ; MSRTIFCTYLQRDAEGQDFQ LYPGELGKRIYNEISKDAWA QWQHKQTMLINEKKLNMMNA EHRKLLEQEMVSFLFEGKDV HIEGYTPEDKK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 ARG 4 THR 5 ILE 6 PHE 7 CYS 8 THR 9 TYR 10 LEU 11 GLN 12 ARG 13 ASP 14 ALA 15 GLU 16 GLY 17 GLN 18 ASP 19 PHE 20 GLN 21 LEU 22 TYR 23 PRO 24 GLY 25 GLU 26 LEU 27 GLY 28 LYS 29 ARG 30 ILE 31 TYR 32 ASN 33 GLU 34 ILE 35 SER 36 LYS 37 ASP 38 ALA 39 TRP 40 ALA 41 GLN 42 TRP 43 GLN 44 HIS 45 LYS 46 GLN 47 THR 48 MET 49 LEU 50 ILE 51 ASN 52 GLU 53 LYS 54 LYS 55 LEU 56 ASN 57 MET 58 MET 59 ASN 60 ALA 61 GLU 62 HIS 63 ARG 64 LYS 65 LEU 66 LEU 67 GLU 68 GLN 69 GLU 70 MET 71 VAL 72 SER 73 PHE 74 LEU 75 PHE 76 GLU 77 GLY 78 LYS 79 ASP 80 VAL 81 HIS 82 ILE 83 GLU 84 GLY 85 TYR 86 THR 87 PRO 88 GLU 89 ASP 90 LYS 91 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-11-16 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 1XS8 "Solution Structure Of Yggx Protein Of Salmonella Enterica" 100.00 91 100.00 100.00 3.89e-61 DBJ BAJ38107 "hypothetical protein STMDT12_C31640 [Salmonella enterica subsp. enterica serovar Typhimurium str. T000240]" 100.00 91 100.00 100.00 3.89e-61 DBJ BAP09026 "conserved hypothetical protein [Salmonella enterica subsp. enterica serovar Typhimurium str. L-3553]" 100.00 91 100.00 100.00 3.89e-61 EMBL CAD02936 "conserved hypothetical protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 91 100.00 100.00 3.89e-61 EMBL CAR34531 "conserved hypothetical protein [Salmonella enterica subsp. enterica serovar Enteritidis str. P125109]" 100.00 91 100.00 100.00 3.89e-61 EMBL CAR38810 "conserved hypothetical protein [Salmonella enterica subsp. enterica serovar Gallinarum str. 287/91]" 100.00 91 100.00 100.00 3.89e-61 EMBL CAR61014 "conserved hypothetical protein [Salmonella enterica subsp. enterica serovar Paratyphi A str. AKU_12601]" 100.00 91 100.00 100.00 3.89e-61 EMBL CAX67914 "putative Fe(2+)-trafficking protein [Salmonella bongori]" 100.00 91 100.00 100.00 3.89e-61 GB AAL21986 "putative cytoplasmic protein [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 91 100.00 100.00 3.89e-61 GB AAO70576 "conserved hypothetical protein [Salmonella enterica subsp. enterica serovar Typhi str. Ty2]" 100.00 91 100.00 100.00 3.89e-61 GB AAV78812 "conserved hypothetical protein [Salmonella enterica subsp. enterica serovar Paratyphi A str. ATCC 9150]" 100.00 91 100.00 100.00 3.89e-61 GB AAX66958 "putative cytoplasmic protein [Salmonella enterica subsp. enterica serovar Choleraesuis str. SC-B67]" 100.00 91 100.00 100.00 3.89e-61 GB ABX24308 "hypothetical protein SARI_04535 [Salmonella enterica subsp. arizonae serovar 62:z4,z23:-]" 100.00 91 100.00 100.00 3.89e-61 PIR AH0879 "conserved hypothetical protein STY3266 [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 91 100.00 100.00 3.89e-61 REF NP_457504 "oxidative damage protection protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 91 100.00 100.00 3.89e-61 REF NP_462027 "Fe(2+)-trafficking protein [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 91 100.00 100.00 3.89e-61 REF NP_806716 "hypothetical protein t3024 [Salmonella enterica subsp. enterica serovar Typhi str. Ty2]" 100.00 91 100.00 100.00 3.89e-61 REF WP_000091705 "oxidative damage protection protein [Salmonella enterica]" 100.00 91 98.90 98.90 1.54e-60 REF WP_000091706 "MULTISPECIES: oxidative damage protection protein [Salmonella]" 100.00 91 100.00 100.00 3.89e-61 SP A9MQR4 "RecName: Full=Probable Fe(2+)-trafficking protein [Salmonella enterica subsp. arizonae serovar 62:z4,z23:-]" 100.00 91 100.00 100.00 3.89e-61 SP A9N4Q8 "RecName: Full=Probable Fe(2+)-trafficking protein [Salmonella enterica subsp. enterica serovar Paratyphi B str. SPB7]" 100.00 91 100.00 100.00 3.89e-61 SP B4T5L9 "RecName: Full=Probable Fe(2+)-trafficking protein [Salmonella enterica subsp. enterica serovar Newport str. SL254]" 100.00 91 100.00 100.00 3.89e-61 SP B4THJ7 "RecName: Full=Probable Fe(2+)-trafficking protein [Salmonella enterica subsp. enterica serovar Heidelberg str. SL476]" 100.00 91 100.00 100.00 3.89e-61 SP B4TV80 "RecName: Full=Probable Fe(2+)-trafficking protein [Salmonella enterica subsp. enterica serovar Schwarzengrund str. CVM19633]" 100.00 91 100.00 100.00 3.89e-61 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $YGGX 'Salmonella enterica' 28901 Bacteria . Salmonella enteritidis 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 $YGGX 'recombinant technology' 'E. coli' Escherichia coli BL21 . 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 $YGGX 19.3 mg/mL '[U-13C; U-15N]' Tris 10 mM [U-2H] D2O 10 % . H2O 90 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer VARIAN _Model Inova _Field_strength 800 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer VARIAN _Model Inova _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details ; The double labeled protein sample was 19.3 mg/mL YggX in 10 mM deuterated Tris pH7.8. 10% D2O/H2O. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.8 0.1 pH temperature 283 0.1 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 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.0 DSS C 13 'methyl protons' ppm 0 internal indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0 internal indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name YGGX _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 C C 176.200 0.12 1 2 . 3 ARG N N 122.510 0.01 1 3 . 3 ARG CA C 55.236 0.24 1 4 . 3 ARG C C 175.101 0.12 1 5 . 3 ARG CB C 32.269 0.27 1 6 . 3 ARG CG C 27.432 0.28 1 7 . 3 ARG CD C 43.580 0.28 1 8 . 3 ARG H H 8.928 0.01 1 9 . 3 ARG HA H 4.673 0.02 1 10 . 3 ARG HB2 H 1.803 0.02 2 11 . 3 ARG HB3 H 1.737 0.02 2 12 . 3 ARG HG3 H 1.468 0.02 2 13 . 3 ARG HD2 H 3.241 0.02 2 14 . 3 ARG HE H 7.150 0.02 1 15 . 4 THR N N 122.917 0.01 1 16 . 4 THR CA C 62.701 0.24 1 17 . 4 THR C C 173.965 0.12 1 18 . 4 THR CB C 69.894 0.27 1 19 . 4 THR CG2 C 21.760 0.28 1 20 . 4 THR H H 8.913 0.01 1 21 . 4 THR HA H 4.772 0.02 1 22 . 4 THR HB H 3.971 0.02 1 23 . 4 THR HG2 H 1.192 0.02 1 24 . 5 ILE N N 121.161 0.01 1 25 . 5 ILE CA C 59.013 0.24 1 26 . 5 ILE C C 173.624 0.12 1 27 . 5 ILE CB C 42.609 0.27 1 28 . 5 ILE CG1 C 25.250 0.28 1 29 . 5 ILE CG2 C 18.199 0.28 1 30 . 5 ILE CD1 C 14.664 0.28 1 31 . 5 ILE H H 9.105 0.01 1 32 . 5 ILE HA H 4.798 0.02 1 33 . 5 ILE HB H 1.899 0.02 1 34 . 5 ILE HG12 H 0.712 0.02 2 35 . 5 ILE HG13 H 1.122 0.02 2 36 . 5 ILE HG2 H 0.815 0.02 1 37 . 5 ILE HD1 H 0.638 0.02 1 38 . 6 PHE N N 121.410 0.01 1 39 . 6 PHE CA C 58.572 0.24 1 40 . 6 PHE C C 173.719 0.12 1 41 . 6 PHE CB C 38.755 0.27 1 42 . 6 PHE H H 8.446 0.01 1 43 . 6 PHE HA H 4.660 0.02 1 44 . 6 PHE HB2 H 2.978 0.02 2 45 . 6 PHE HD1 H 7.197 0.02 3 46 . 6 PHE HE1 H 6.790 0.02 3 47 . 7 CYS N N 133.330 0.01 1 48 . 7 CYS CA C 59.231 0.24 1 49 . 7 CYS C C 178.095 0.12 1 50 . 7 CYS CB C 31.500 0.27 1 51 . 7 CYS H H 7.970 0.01 1 52 . 7 CYS HA H 4.686 0.02 1 53 . 7 CYS HB2 H 3.160 0.02 2 54 . 7 CYS HB3 H 2.741 0.02 2 55 . 8 THR N N 125.126 0.01 1 56 . 8 THR CA C 64.679 0.24 1 57 . 8 THR C C 175.281 0.12 1 58 . 8 THR CB C 69.439 0.27 1 59 . 8 THR CG2 C 23.030 0.28 1 60 . 8 THR H H 9.836 0.01 1 61 . 8 THR HA H 4.066 0.02 1 62 . 8 THR HB H 4.400 0.02 1 63 . 8 THR HG2 H 1.621 0.02 1 64 . 9 TYR N N 126.196 0.01 1 65 . 9 TYR CA C 61.584 0.24 1 66 . 9 TYR C C 177.744 0.12 1 67 . 9 TYR CB C 39.460 0.27 1 68 . 9 TYR H H 9.226 0.01 1 69 . 9 TYR HA H 4.400 0.02 1 70 . 9 TYR HB2 H 3.079 0.02 2 71 . 9 TYR HD1 H 7.054 0.02 3 72 . 10 LEU N N 123.461 0.01 1 73 . 10 LEU CA C 55.796 0.24 1 74 . 10 LEU C C 177.203 0.12 1 75 . 10 LEU CB C 43.055 0.27 1 76 . 10 LEU CG C 29.350 0.28 1 77 . 10 LEU CD1 C 26.630 0.28 1 78 . 10 LEU H H 10.315 0.01 1 79 . 10 LEU HA H 3.982 0.02 1 80 . 10 LEU HB2 H 1.440 0.02 2 81 . 10 LEU HB3 H 1.730 0.02 2 82 . 10 LEU HG H 1.780 0.02 1 83 . 10 LEU HD2 H 1.019 0.02 2 84 . 11 GLN N N 114.563 0.01 1 85 . 11 GLN NE2 N 116.450 0.01 1 86 . 11 GLN CA C 56.342 0.24 1 87 . 11 GLN C C 174.635 0.12 1 88 . 11 GLN CB C 25.205 0.27 1 89 . 11 GLN CG C 33.835 0.28 1 90 . 11 GLN H H 8.534 0.01 1 91 . 11 GLN HA H 3.381 0.02 1 92 . 11 GLN HB2 H 2.406 0.02 2 93 . 11 GLN HB3 H 2.226 0.02 2 94 . 11 GLN HG2 H 2.145 0.02 2 95 . 11 GLN HG3 H 2.276 0.02 2 96 . 11 GLN HE21 H 8.429 0.02 1 97 . 11 GLN HE22 H 7.438 0.02 1 98 . 12 ARG N N 111.545 0.01 1 99 . 12 ARG CA C 54.560 0.24 1 100 . 12 ARG C C 174.040 0.12 1 101 . 12 ARG CB C 32.160 0.27 1 102 . 12 ARG CG C 26.000 0.28 1 103 . 12 ARG CD C 43.800 0.28 1 104 . 12 ARG H H 6.781 0.01 1 105 . 12 ARG HA H 4.514 0.02 1 106 . 12 ARG HB2 H 2.116 0.02 2 107 . 12 ARG HB3 H 1.724 0.02 2 108 . 12 ARG HG2 H 1.286 0.02 2 109 . 12 ARG HG3 H 1.380 0.02 2 110 . 12 ARG HD2 H 3.215 0.02 2 111 . 12 ARG HE H 7.447 0.02 1 112 . 13 ASP N N 121.330 0.01 1 113 . 13 ASP CA C 54.644 0.24 1 114 . 13 ASP C C 177.218 0.12 1 115 . 13 ASP CB C 40.669 0.27 1 116 . 13 ASP H H 8.561 0.01 1 117 . 13 ASP HA H 5.610 0.02 1 118 . 13 ASP HB2 H 2.406 0.02 2 119 . 13 ASP HB3 H 2.573 0.02 2 120 . 14 ALA N N 126.144 0.01 1 121 . 14 ALA CA C 51.810 0.24 1 122 . 14 ALA C C 175.178 0.12 1 123 . 14 ALA CB C 24.063 0.27 1 124 . 14 ALA H H 9.785 0.01 1 125 . 14 ALA HA H 4.688 0.02 1 126 . 14 ALA HB H 1.521 0.02 1 127 . 15 GLU N N 119.316 0.01 1 128 . 15 GLU CA C 57.619 0.24 1 129 . 15 GLU C C 178.272 0.12 1 130 . 15 GLU CB C 30.647 0.27 1 131 . 15 GLU CG C 36.902 0.28 1 132 . 15 GLU H H 8.529 0.01 1 133 . 15 GLU HA H 4.636 0.02 1 134 . 15 GLU HB2 H 2.079 0.02 2 135 . 15 GLU HB3 H 2.126 0.02 2 136 . 15 GLU HG2 H 2.579 0.02 2 137 . 16 GLY N N 113.629 0.01 1 138 . 16 GLY CA C 44.967 0.24 1 139 . 16 GLY C C 172.905 0.12 1 140 . 16 GLY H H 9.326 0.01 1 141 . 16 GLY HA2 H 4.167 0.02 2 142 . 16 GLY HA3 H 3.370 0.02 2 143 . 17 GLN N N 119.292 0.01 1 144 . 17 GLN NE2 N 109.210 0.01 1 145 . 17 GLN CA C 56.970 0.24 1 146 . 17 GLN C C 176.521 0.12 1 147 . 17 GLN CB C 30.662 0.27 1 148 . 17 GLN CG C 34.428 0.28 1 149 . 17 GLN H H 9.975 0.01 1 150 . 17 GLN HA H 4.094 0.02 1 151 . 17 GLN HB2 H 2.328 0.02 2 152 . 17 GLN HB3 H 1.867 0.02 2 153 . 17 GLN HG2 H 2.229 0.02 2 154 . 17 GLN HG3 H 2.615 0.02 2 155 . 17 GLN HE21 H 7.320 0.02 1 156 . 17 GLN HE22 H 4.690 0.02 1 157 . 18 ASP N N 119.536 0.01 1 158 . 18 ASP CA C 56.970 0.24 1 159 . 18 ASP C C 175.966 0.12 1 160 . 18 ASP CB C 42.078 0.27 1 161 . 18 ASP H H 8.997 0.01 1 162 . 18 ASP HA H 4.556 0.02 1 163 . 18 ASP HB2 H 2.410 0.02 2 164 . 18 ASP HB3 H 2.501 0.02 2 165 . 19 PHE N N 114.451 0.01 1 166 . 19 PHE CA C 55.808 0.24 1 167 . 19 PHE CB C 42.202 0.27 1 168 . 19 PHE H H 7.765 0.01 1 169 . 19 PHE HA H 4.810 0.02 1 170 . 19 PHE HB2 H 3.204 0.02 2 171 . 19 PHE HB3 H 2.759 0.02 2 172 . 19 PHE HD1 H 7.205 0.02 3 173 . 19 PHE HE1 H 6.850 0.02 3 174 . 20 GLN N N 118.780 0.01 1 175 . 20 GLN NE2 N 111.040 0.01 1 176 . 20 GLN CA C 56.116 0.24 1 177 . 20 GLN C C 174.708 0.12 1 178 . 20 GLN CB C 27.152 0.27 1 179 . 20 GLN CG C 33.200 0.28 1 180 . 20 GLN H H 8.010 0.01 1 181 . 20 GLN HA H 4.061 0.02 1 182 . 20 GLN HB2 H 1.380 0.02 2 183 . 20 GLN HB3 H 1.744 0.02 2 184 . 20 GLN HG2 H 2.211 0.02 2 185 . 20 GLN HG3 H 2.311 0.02 2 186 . 20 GLN HE21 H 7.971 0.02 1 187 . 20 GLN HE22 H 6.640 0.02 1 188 . 21 LEU N N 127.810 0.01 1 189 . 21 LEU CA C 55.917 0.24 1 190 . 21 LEU C C 175.807 0.12 1 191 . 21 LEU CB C 43.368 0.27 1 192 . 21 LEU CG C 27.000 0.28 1 193 . 21 LEU CD1 C 25.000 0.28 1 194 . 21 LEU H H 7.989 0.01 1 195 . 21 LEU HA H 4.320 0.02 1 196 . 21 LEU HB2 H 1.445 0.02 2 197 . 21 LEU HG H 1.519 0.02 1 198 . 21 LEU HD2 H 0.828 0.02 2 199 . 22 TYR N N 122.433 0.01 1 200 . 22 TYR CA C 56.040 0.24 1 201 . 22 TYR CB C 42.000 0.27 1 202 . 22 TYR H H 8.260 0.01 1 203 . 22 TYR HA H 4.716 0.02 1 204 . 22 TYR HB2 H 3.076 0.02 2 205 . 22 TYR HB3 H 3.148 0.02 2 206 . 22 TYR HD1 H 7.323 0.02 3 207 . 22 TYR HE1 H 7.067 0.02 3 208 . 23 PRO CA C 63.073 0.24 1 209 . 23 PRO C C 178.574 0.12 1 210 . 23 PRO CB C 33.328 0.27 1 211 . 23 PRO CG C 27.100 0.28 1 212 . 23 PRO CD C 50.500 0.28 1 213 . 23 PRO HA H 4.555 0.02 1 214 . 23 PRO HB2 H 2.269 0.02 2 215 . 23 PRO HB3 H 1.943 0.02 2 216 . 23 PRO HG2 H 1.800 0.02 2 217 . 23 PRO HG3 H 1.898 0.02 2 218 . 23 PRO HD2 H 2.720 0.02 2 219 . 23 PRO HD3 H 3.530 0.02 2 220 . 24 GLY N N 106.322 0.01 1 221 . 24 GLY CA C 45.275 0.24 1 222 . 24 GLY C C 174.452 0.12 1 223 . 24 GLY H H 8.590 0.01 1 224 . 24 GLY HA2 H 3.999 0.02 2 225 . 24 GLY HA3 H 4.201 0.02 2 226 . 25 GLU N N 120.939 0.01 1 227 . 25 GLU CA C 59.430 0.24 1 228 . 25 GLU C C 180.179 0.12 1 229 . 25 GLU CB C 29.419 0.27 1 230 . 25 GLU CG C 36.362 0.28 1 231 . 25 GLU H H 8.840 0.01 1 232 . 25 GLU HA H 4.036 0.02 1 233 . 25 GLU HB2 H 2.075 0.02 2 234 . 25 GLU HB3 H 2.105 0.02 2 235 . 25 GLU HG3 H 2.392 0.02 2 236 . 26 LEU N N 122.155 0.01 1 237 . 26 LEU CA C 57.586 0.24 1 238 . 26 LEU C C 178.689 0.12 1 239 . 26 LEU CB C 41.148 0.27 1 240 . 26 LEU CG C 27.000 0.28 1 241 . 26 LEU CD1 C 23.016 0.28 1 242 . 26 LEU H H 9.094 0.01 1 243 . 26 LEU HA H 4.280 0.02 1 244 . 26 LEU HB2 H 1.765 0.02 2 245 . 26 LEU HG H 1.514 0.02 1 246 . 26 LEU HD2 H 0.925 0.02 2 247 . 27 GLY N N 104.995 0.01 1 248 . 27 GLY CA C 47.598 0.24 1 249 . 27 GLY C C 178.001 0.12 1 250 . 27 GLY H H 7.451 0.01 1 251 . 27 GLY HA2 H 4.547 0.02 2 252 . 27 GLY HA3 H 3.869 0.02 2 253 . 28 LYS N N 125.591 0.01 1 254 . 28 LYS CA C 59.849 0.24 1 255 . 28 LYS C C 177.644 0.12 1 256 . 28 LYS CB C 32.420 0.27 1 257 . 28 LYS CG C 24.661 0.28 1 258 . 28 LYS CD C 29.200 0.28 1 259 . 28 LYS CE C 41.100 0.28 1 260 . 28 LYS H H 8.265 0.01 1 261 . 28 LYS HA H 4.014 0.02 1 262 . 28 LYS HB2 H 1.966 0.02 2 263 . 28 LYS HB3 H 2.043 0.02 2 264 . 28 LYS HG3 H 1.485 0.02 2 265 . 28 LYS HD3 H 1.780 0.02 2 266 . 28 LYS HE2 H 3.030 0.02 2 267 . 29 ARG N N 120.804 0.01 1 268 . 29 ARG CA C 60.246 0.24 1 269 . 29 ARG C C 179.160 0.12 1 270 . 29 ARG CB C 30.148 0.27 1 271 . 29 ARG CG C 27.000 0.28 1 272 . 29 ARG CD C 43.700 0.28 1 273 . 29 ARG H H 8.050 0.01 1 274 . 29 ARG HA H 4.240 0.02 1 275 . 29 ARG HB2 H 1.990 0.02 2 276 . 29 ARG HG2 H 1.819 0.02 2 277 . 29 ARG HG3 H 1.504 0.02 2 278 . 29 ARG HD2 H 2.870 0.02 2 279 . 29 ARG HD3 H 2.230 0.02 2 280 . 29 ARG HE H 7.150 0.02 1 281 . 30 ILE N N 118.729 0.01 1 282 . 30 ILE CA C 66.061 0.24 1 283 . 30 ILE C C 176.846 0.12 1 284 . 30 ILE CB C 44.358 0.27 1 285 . 30 ILE CG2 C 18.412 0.28 1 286 . 30 ILE CD1 C 14.400 0.28 1 287 . 30 ILE H H 8.532 0.01 1 288 . 30 ILE HA H 3.790 0.02 1 289 . 30 ILE HB H 2.030 0.02 1 290 . 30 ILE HG2 H 0.722 0.02 1 291 . 30 ILE HD1 H 0.880 0.02 1 292 . 31 TYR N N 118.579 0.01 1 293 . 31 TYR CA C 61.220 0.24 1 294 . 31 TYR C C 178.732 0.12 1 295 . 31 TYR CB C 38.988 0.27 1 296 . 31 TYR H H 8.116 0.01 1 297 . 31 TYR HA H 4.147 0.02 1 298 . 31 TYR HB2 H 2.970 0.02 2 299 . 31 TYR HB3 H 3.223 0.02 2 300 . 31 TYR HD1 H 6.861 0.02 3 301 . 31 TYR HE1 H 7.016 0.02 3 302 . 32 ASN N N 117.815 0.01 1 303 . 32 ASN ND2 N 111.571 0.01 1 304 . 32 ASN CA C 55.266 0.24 1 305 . 32 ASN C C 177.120 0.12 1 306 . 32 ASN CB C 39.642 0.27 1 307 . 32 ASN H H 8.688 0.01 1 308 . 32 ASN HA H 4.624 0.02 1 309 . 32 ASN HB2 H 2.983 0.02 2 310 . 32 ASN HB3 H 3.231 0.02 2 311 . 32 ASN HD21 H 7.722 0.02 1 312 . 32 ASN HD22 H 7.045 0.02 1 313 . 33 GLU N N 115.070 0.01 1 314 . 33 GLU CA C 58.161 0.24 1 315 . 33 GLU C C 174.109 0.12 1 316 . 33 GLU CB C 33.500 0.27 1 317 . 33 GLU CG C 37.000 0.28 1 318 . 33 GLU H H 8.383 0.01 1 319 . 33 GLU HA H 4.913 0.02 1 320 . 33 GLU HB2 H 2.400 0.02 2 321 . 33 GLU HB3 H 2.835 0.02 2 322 . 33 GLU HG2 H 2.556 0.02 2 323 . 34 ILE N N 118.115 0.01 1 324 . 34 ILE CA C 56.700 0.24 1 325 . 34 ILE C C 177.045 0.12 1 326 . 34 ILE CB C 35.660 0.27 1 327 . 34 ILE CG1 C 27.000 0.28 1 328 . 34 ILE CG2 C 18.318 0.28 1 329 . 34 ILE CD1 C 10.000 0.28 1 330 . 34 ILE H H 8.341 0.01 1 331 . 34 ILE HA H 5.489 0.02 1 332 . 34 ILE HB H 2.782 0.02 1 333 . 34 ILE HG12 H 1.837 0.02 2 334 . 34 ILE HG13 H 1.152 0.02 2 335 . 34 ILE HG2 H 1.251 0.02 1 336 . 34 ILE HD1 H 0.680 0.02 1 337 . 35 SER N N 132.660 0.01 1 338 . 35 SER CA C 59.478 0.24 1 339 . 35 SER C C 174.643 0.12 1 340 . 35 SER CB C 66.818 0.27 1 341 . 35 SER H H 10.930 0.01 1 342 . 35 SER HA H 4.680 0.02 1 343 . 35 SER HB2 H 4.059 0.02 2 344 . 35 SER HB3 H 4.621 0.02 2 345 . 36 LYS N N 118.217 0.01 1 346 . 36 LYS CA C 61.364 0.24 1 347 . 36 LYS C C 180.152 0.12 1 348 . 36 LYS CB C 33.417 0.27 1 349 . 36 LYS CG C 21.000 0.28 1 350 . 36 LYS CD C 26.826 0.28 1 351 . 36 LYS CE C 42.400 0.28 1 352 . 36 LYS H H 8.631 0.01 1 353 . 36 LYS HA H 4.084 0.02 1 354 . 36 LYS HB2 H 2.002 0.02 2 355 . 36 LYS HG3 H 0.860 0.02 2 356 . 36 LYS HD2 H 1.405 0.02 2 357 . 36 LYS HD3 H 1.486 0.02 2 358 . 36 LYS HE2 H 3.380 0.02 2 359 . 36 LYS HE3 H 3.112 0.02 2 360 . 37 ASP N N 120.131 0.01 1 361 . 37 ASP CA C 57.565 0.24 1 362 . 37 ASP C C 178.735 0.12 1 363 . 37 ASP CB C 41.230 0.27 1 364 . 37 ASP H H 9.131 0.01 1 365 . 37 ASP HA H 4.511 0.02 1 366 . 37 ASP HB2 H 2.800 0.02 2 367 . 38 ALA N N 123.170 0.01 1 368 . 38 ALA CA C 55.527 0.24 1 369 . 38 ALA C C 179.000 0.12 1 370 . 38 ALA CB C 22.110 0.27 1 371 . 38 ALA H H 8.333 0.01 1 372 . 38 ALA HA H 3.853 0.02 1 373 . 38 ALA HB H 1.528 0.02 1 374 . 39 TRP N N 119.059 0.01 1 375 . 39 TRP NE1 N 128.600 0.01 1 376 . 39 TRP CA C 59.717 0.24 1 377 . 39 TRP C C 177.766 0.12 1 378 . 39 TRP CB C 30.068 0.27 1 379 . 39 TRP H H 8.950 0.01 1 380 . 39 TRP HA H 4.082 0.02 1 381 . 39 TRP HB2 H 3.432 0.02 2 382 . 39 TRP HD1 H 7.230 0.02 1 383 . 39 TRP HE1 H 10.175 0.02 1 384 . 39 TRP HE3 H 7.334 0.02 1 385 . 39 TRP HZ3 H 6.000 0.02 1 386 . 39 TRP HZ2 H 7.801 0.02 1 387 . 40 ALA N N 120.172 0.01 1 388 . 40 ALA CA C 55.022 0.24 1 389 . 40 ALA C C 181.209 0.12 1 390 . 40 ALA CB C 17.844 0.27 1 391 . 40 ALA H H 8.335 0.01 1 392 . 40 ALA HA H 4.147 0.02 1 393 . 40 ALA HB H 1.660 0.02 1 394 . 41 GLN N N 118.383 0.01 1 395 . 41 GLN NE2 N 113.850 0.01 1 396 . 41 GLN CA C 59.552 0.24 1 397 . 41 GLN C C 179.664 0.12 1 398 . 41 GLN CB C 27.787 0.27 1 399 . 41 GLN CG C 34.100 0.28 1 400 . 41 GLN H H 7.814 0.01 1 401 . 41 GLN HA H 4.157 0.02 1 402 . 41 GLN HB2 H 2.490 0.02 2 403 . 41 GLN HB3 H 2.430 0.02 2 404 . 41 GLN HG2 H 2.542 0.02 2 405 . 41 GLN HG3 H 2.861 0.02 2 406 . 41 GLN HE21 H 7.809 0.02 1 407 . 41 GLN HE22 H 7.214 0.02 1 408 . 42 TRP N N 122.453 0.01 1 409 . 42 TRP NE1 N 127.420 0.01 1 410 . 42 TRP CA C 58.220 0.24 1 411 . 42 TRP C C 175.552 0.12 1 412 . 42 TRP CB C 28.893 0.27 1 413 . 42 TRP H H 8.178 0.01 1 414 . 42 TRP HA H 3.904 0.02 1 415 . 42 TRP HB2 H 2.878 0.02 2 416 . 42 TRP HB3 H 3.084 0.02 2 417 . 42 TRP HD1 H 7.300 0.02 1 418 . 42 TRP HE1 H 9.560 0.02 1 419 . 42 TRP HZ3 H 6.010 0.02 1 420 . 42 TRP HZ2 H 6.850 0.02 1 421 . 43 GLN N N 117.125 0.01 1 422 . 43 GLN NE2 N 113.520 0.01 1 423 . 43 GLN CA C 58.844 0.24 1 424 . 43 GLN C C 178.524 0.12 1 425 . 43 GLN CB C 27.610 0.27 1 426 . 43 GLN CG C 34.436 0.28 1 427 . 43 GLN H H 8.447 0.01 1 428 . 43 GLN HA H 2.850 0.02 1 429 . 43 GLN HB2 H 1.813 0.02 2 430 . 43 GLN HB3 H 1.911 0.02 2 431 . 43 GLN HG2 H 2.075 0.02 2 432 . 43 GLN HG3 H 1.651 0.02 2 433 . 43 GLN HE21 H 7.120 0.02 1 434 . 43 GLN HE22 H 6.024 0.02 1 435 . 44 HIS N N 117.655 0.01 1 436 . 44 HIS CA C 59.552 0.24 1 437 . 44 HIS C C 177.284 0.12 1 438 . 44 HIS CB C 30.729 0.27 1 439 . 44 HIS H H 7.339 0.01 1 440 . 44 HIS HA H 4.231 0.02 1 441 . 44 HIS HB2 H 3.084 0.02 2 442 . 45 LYS N N 121.927 0.01 1 443 . 45 LYS CA C 58.278 0.24 1 444 . 45 LYS C C 177.375 0.12 1 445 . 45 LYS CB C 30.904 0.27 1 446 . 45 LYS CG C 24.900 0.28 1 447 . 45 LYS CD C 28.500 0.28 1 448 . 45 LYS CE C 42.800 0.28 1 449 . 45 LYS H H 7.165 0.01 1 450 . 45 LYS HA H 3.734 0.02 1 451 . 45 LYS HB2 H 1.400 0.02 2 452 . 45 LYS HB3 H 1.357 0.02 2 453 . 45 LYS HG2 H 1.103 0.02 2 454 . 45 LYS HG3 H 1.227 0.02 2 455 . 45 LYS HD2 H 1.570 0.02 2 456 . 45 LYS HD3 H 1.690 0.02 2 457 . 45 LYS HE3 H 3.110 0.02 2 458 . 46 GLN N N 119.555 0.01 1 459 . 46 GLN NE2 N 109.400 0.01 1 460 . 46 GLN CA C 59.440 0.24 1 461 . 46 GLN C C 177.134 0.12 1 462 . 46 GLN CB C 28.118 0.27 1 463 . 46 GLN CG C 35.201 0.28 1 464 . 46 GLN H H 8.455 0.01 1 465 . 46 GLN HA H 3.000 0.02 1 466 . 46 GLN HB2 H 0.474 0.02 2 467 . 46 GLN HB3 H 1.297 0.02 2 468 . 46 GLN HG2 H 1.905 0.02 2 469 . 46 GLN HG3 H 2.048 0.02 2 470 . 46 GLN HE21 H 7.214 0.02 1 471 . 46 GLN HE22 H 6.869 0.02 1 472 . 47 THR N N 115.064 0.01 1 473 . 47 THR CA C 66.910 0.24 1 474 . 47 THR C C 175.936 0.12 1 475 . 47 THR CB C 69.100 0.27 1 476 . 47 THR CG2 C 21.790 0.28 1 477 . 47 THR H H 7.538 0.01 1 478 . 47 THR HA H 3.688 0.02 1 479 . 47 THR HB H 4.137 0.02 1 480 . 47 THR HG2 H 1.181 0.02 1 481 . 48 MET N N 120.230 0.01 1 482 . 48 MET CA C 58.952 0.24 1 483 . 48 MET C C 178.728 0.12 1 484 . 48 MET CB C 32.077 0.27 1 485 . 48 MET CG C 34.300 0.28 1 486 . 48 MET H H 7.327 0.01 1 487 . 48 MET HA H 4.151 0.02 1 488 . 48 MET HB2 H 2.335 0.02 2 489 . 48 MET HB3 H 2.542 0.02 2 490 . 48 MET HG2 H 2.528 0.02 2 491 . 48 MET HG3 H 2.631 0.02 2 492 . 49 LEU N N 121.610 0.01 1 493 . 49 LEU CA C 58.261 0.24 1 494 . 49 LEU C C 179.160 0.12 1 495 . 49 LEU CB C 43.362 0.27 1 496 . 49 LEU CG C 26.800 0.28 1 497 . 49 LEU CD1 C 23.850 0.28 1 498 . 49 LEU H H 8.535 0.01 1 499 . 49 LEU HA H 3.998 0.02 1 500 . 49 LEU HB2 H 1.920 0.02 2 501 . 49 LEU HB3 H 1.110 0.02 2 502 . 49 LEU HD2 H 0.885 0.02 2 503 . 50 ILE N N 118.723 0.01 1 504 . 50 ILE CA C 66.232 0.24 1 505 . 50 ILE C C 178.786 0.12 1 506 . 50 ILE CB C 38.905 0.27 1 507 . 50 ILE CG1 C 25.040 0.28 1 508 . 50 ILE CG2 C 16.876 0.28 1 509 . 50 ILE CD1 C 14.500 0.28 1 510 . 50 ILE H H 8.481 0.01 1 511 . 50 ILE HA H 3.394 0.02 1 512 . 50 ILE HB H 1.870 0.02 1 513 . 50 ILE HG13 H 1.040 0.02 2 514 . 50 ILE HG2 H 1.014 0.02 1 515 . 50 ILE HD1 H 0.880 0.02 1 516 . 51 ASN N N 116.070 0.01 1 517 . 51 ASN ND2 N 113.150 0.01 1 518 . 51 ASN CA C 55.864 0.24 1 519 . 51 ASN C C 177.799 0.12 1 520 . 51 ASN CB C 38.738 0.27 1 521 . 51 ASN H H 7.719 0.01 1 522 . 51 ASN HA H 4.587 0.02 1 523 . 51 ASN HB2 H 2.917 0.02 2 524 . 51 ASN HD21 H 7.752 0.02 1 525 . 51 ASN HD22 H 7.059 0.02 1 526 . 52 GLU N N 120.210 0.01 1 527 . 52 GLU CA C 59.430 0.24 1 528 . 52 GLU C C 178.757 0.12 1 529 . 52 GLU CB C 30.538 0.27 1 530 . 52 GLU CG C 36.427 0.28 1 531 . 52 GLU H H 8.952 0.01 1 532 . 52 GLU HA H 4.082 0.02 1 533 . 52 GLU HB2 H 2.060 0.02 2 534 . 52 GLU HB3 H 2.200 0.02 2 535 . 52 GLU HG2 H 2.450 0.02 2 536 . 52 GLU HG3 H 2.255 0.02 2 537 . 53 LYS N N 114.627 0.01 1 538 . 53 LYS CA C 55.852 0.24 1 539 . 53 LYS C C 174.673 0.12 1 540 . 53 LYS CB C 31.951 0.27 1 541 . 53 LYS CG C 26.130 0.28 1 542 . 53 LYS CD C 29.440 0.28 1 543 . 53 LYS CE C 42.505 0.28 1 544 . 53 LYS H H 8.307 0.01 1 545 . 53 LYS HA H 4.345 0.02 1 546 . 53 LYS HB2 H 1.923 0.02 2 547 . 53 LYS HB3 H 1.690 0.02 2 548 . 53 LYS HG2 H 1.480 0.02 2 549 . 53 LYS HD2 H 1.668 0.02 2 550 . 53 LYS HD3 H 1.540 0.02 2 551 . 53 LYS HE2 H 3.040 0.02 2 552 . 53 LYS HE3 H 2.950 0.02 2 553 . 54 LYS N N 117.138 0.01 1 554 . 54 LYS CA C 56.338 0.24 1 555 . 54 LYS C C 176.576 0.12 1 556 . 54 LYS CB C 28.413 0.27 1 557 . 54 LYS CG C 24.715 0.28 1 558 . 54 LYS CE C 42.000 0.28 1 559 . 54 LYS H H 7.513 0.01 1 560 . 54 LYS HA H 4.122 0.02 1 561 . 54 LYS HB2 H 1.851 0.02 2 562 . 54 LYS HB3 H 2.119 0.02 2 563 . 54 LYS HG2 H 1.415 0.02 2 564 . 54 LYS HE2 H 3.064 0.02 2 565 . 55 LEU N N 116.963 0.01 1 566 . 55 LEU CA C 53.973 0.24 1 567 . 55 LEU C C 176.437 0.12 1 568 . 55 LEU CB C 43.199 0.27 1 569 . 55 LEU CG C 26.101 0.28 1 570 . 55 LEU CD2 C 20.202 0.28 1 571 . 55 LEU H H 7.828 0.01 1 572 . 55 LEU HA H 4.443 0.02 1 573 . 55 LEU HB2 H 1.727 0.02 2 574 . 55 LEU HB3 H 1.182 0.02 2 575 . 55 LEU HG H 0.727 0.02 1 576 . 55 LEU HD2 H 0.160 0.02 2 577 . 56 ASN N N 124.923 0.01 1 578 . 56 ASN ND2 N 112.100 0.01 1 579 . 56 ASN CA C 52.214 0.24 1 580 . 56 ASN C C 176.716 0.12 1 581 . 56 ASN CB C 40.734 0.27 1 582 . 56 ASN H H 12.185 0.01 1 583 . 56 ASN HA H 4.931 0.02 1 584 . 56 ASN HB2 H 3.255 0.02 2 585 . 56 ASN HB3 H 2.966 0.02 2 586 . 56 ASN HD21 H 7.872 0.02 1 587 . 56 ASN HD22 H 7.140 0.02 1 588 . 57 MET N N 122.409 0.01 1 589 . 57 MET CA C 56.412 0.24 1 590 . 57 MET C C 177.528 0.12 1 591 . 57 MET CB C 31.601 0.27 1 592 . 57 MET CG C 32.800 0.28 1 593 . 57 MET CE C 17.800 0.28 1 594 . 57 MET H H 9.109 0.01 1 595 . 57 MET HA H 4.504 0.02 1 596 . 57 MET HB2 H 2.116 0.02 2 597 . 57 MET HB3 H 2.234 0.02 2 598 . 57 MET HG2 H 2.535 0.02 2 599 . 57 MET HG3 H 2.895 0.02 2 600 . 57 MET HE H 2.073 0.02 1 601 . 58 MET N N 116.645 0.01 1 602 . 58 MET CA C 55.724 0.24 1 603 . 58 MET C C 175.740 0.12 1 604 . 58 MET CB C 31.475 0.27 1 605 . 58 MET CG C 32.604 0.28 1 606 . 58 MET CE C 16.902 0.28 1 607 . 58 MET H H 8.438 0.01 1 608 . 58 MET HA H 4.532 0.02 1 609 . 58 MET HB2 H 2.264 0.02 2 610 . 58 MET HB3 H 2.114 0.02 2 611 . 58 MET HG2 H 2.586 0.02 2 612 . 58 MET HG3 H 2.789 0.02 2 613 . 58 MET HE H 2.161 0.02 1 614 . 59 ASN N N 121.186 0.01 1 615 . 59 ASN ND2 N 111.800 0.01 1 616 . 59 ASN CA C 52.126 0.24 1 617 . 59 ASN CB C 39.419 0.27 1 618 . 59 ASN H H 8.184 0.01 1 619 . 59 ASN HA H 4.757 0.02 1 620 . 59 ASN HB2 H 3.252 0.02 2 621 . 59 ASN HB3 H 2.440 0.02 2 622 . 59 ASN HD21 H 7.271 0.02 1 623 . 59 ASN HD22 H 7.008 0.02 1 624 . 60 ALA CA C 55.995 0.24 1 625 . 60 ALA C C 180.575 0.12 1 626 . 60 ALA CB C 18.692 0.27 1 627 . 60 ALA H H 8.416 0.01 1 628 . 60 ALA HA H 3.965 0.02 1 629 . 60 ALA HB H 1.590 0.02 1 630 . 61 GLU N N 117.461 0.01 1 631 . 61 GLU CA C 59.394 0.24 1 632 . 61 GLU C C 180.087 0.12 1 633 . 61 GLU CB C 28.933 0.27 1 634 . 61 GLU CG C 36.724 0.28 1 635 . 61 GLU H H 8.523 0.01 1 636 . 61 GLU HA H 4.240 0.02 1 637 . 61 GLU HB2 H 2.289 0.02 2 638 . 61 GLU HB3 H 2.239 0.02 2 639 . 61 GLU HG2 H 2.510 0.02 2 640 . 61 GLU HG3 H 2.410 0.02 2 641 . 62 HIS N N 122.501 0.01 1 642 . 62 HIS CA C 57.692 0.24 1 643 . 62 HIS C C 178.295 0.12 1 644 . 62 HIS CB C 31.885 0.27 1 645 . 62 HIS H H 7.855 0.01 1 646 . 62 HIS HA H 4.609 0.02 1 647 . 62 HIS HB2 H 4.034 0.02 2 648 . 62 HIS HB3 H 2.901 0.02 2 649 . 62 HIS HD2 H 6.824 0.02 1 650 . 63 ARG N N 118.302 0.01 1 651 . 63 ARG CA C 60.797 0.24 1 652 . 63 ARG C C 179.494 0.12 1 653 . 63 ARG CB C 30.783 0.27 1 654 . 63 ARG CD C 45.147 0.28 1 655 . 63 ARG H H 8.380 0.01 1 656 . 63 ARG HA H 4.169 0.02 1 657 . 63 ARG HB2 H 2.150 0.02 2 658 . 63 ARG HB3 H 2.002 0.02 2 659 . 63 ARG HD2 H 3.227 0.02 2 660 . 63 ARG HD3 H 2.970 0.02 2 661 . 64 LYS N N 120.692 0.01 1 662 . 64 LYS CA C 59.462 0.24 1 663 . 64 LYS C C 178.730 0.12 1 664 . 64 LYS CB C 32.100 0.27 1 665 . 64 LYS CG C 24.609 0.28 1 666 . 64 LYS CD C 29.300 0.28 1 667 . 64 LYS CE C 42.011 0.28 1 668 . 64 LYS H H 7.914 0.01 1 669 . 64 LYS HA H 4.239 0.02 1 670 . 64 LYS HB2 H 2.069 0.02 2 671 . 64 LYS HG2 H 1.561 0.02 2 672 . 64 LYS HG3 H 1.682 0.02 2 673 . 64 LYS HD2 H 1.810 0.02 2 674 . 64 LYS HE2 H 3.040 0.02 2 675 . 65 LEU N N 121.841 0.01 1 676 . 65 LEU CA C 58.823 0.24 1 677 . 65 LEU C C 179.841 0.12 1 678 . 65 LEU CB C 41.868 0.27 1 679 . 65 LEU CG C 27.220 0.28 1 680 . 65 LEU CD1 C 24.600 0.28 1 681 . 65 LEU CD2 C 25.100 0.28 1 682 . 65 LEU H H 7.848 0.01 1 683 . 65 LEU HA H 4.321 0.02 1 684 . 65 LEU HB2 H 1.965 0.02 2 685 . 65 LEU HB3 H 2.018 0.02 2 686 . 65 LEU HG H 1.911 0.02 1 687 . 65 LEU HD1 H 0.970 0.02 2 688 . 65 LEU HD2 H 1.033 0.02 2 689 . 66 LEU N N 119.374 0.01 1 690 . 66 LEU CA C 58.633 0.24 1 691 . 66 LEU C C 178.348 0.12 1 692 . 66 LEU CB C 42.293 0.27 1 693 . 66 LEU CG C 27.220 0.28 1 694 . 66 LEU CD1 C 24.900 0.28 1 695 . 66 LEU H H 8.293 0.01 1 696 . 66 LEU HA H 4.125 0.02 1 697 . 66 LEU HB2 H 1.983 0.02 2 698 . 66 LEU HG H 1.988 0.02 1 699 . 66 LEU HD2 H 1.029 0.02 2 700 . 67 GLU N N 120.423 0.01 1 701 . 67 GLU CA C 60.686 0.24 1 702 . 67 GLU C C 177.899 0.12 1 703 . 67 GLU CB C 30.297 0.27 1 704 . 67 GLU CG C 38.164 0.28 1 705 . 67 GLU H H 8.280 0.01 1 706 . 67 GLU HA H 4.007 0.02 1 707 . 67 GLU HB2 H 2.326 0.02 2 708 . 67 GLU HG2 H 2.180 0.02 2 709 . 67 GLU HG3 H 2.307 0.02 2 710 . 68 GLN N N 118.482 0.01 1 711 . 68 GLN NE2 N 112.560 0.01 1 712 . 68 GLN CA C 58.965 0.24 1 713 . 68 GLN C C 179.754 0.12 1 714 . 68 GLN CB C 28.321 0.27 1 715 . 68 GLN CG C 34.434 0.28 1 716 . 68 GLN H H 8.043 0.01 1 717 . 68 GLN HA H 4.124 0.02 1 718 . 68 GLN HB2 H 2.460 0.02 2 719 . 68 GLN HB3 H 2.301 0.02 2 720 . 68 GLN HG2 H 2.516 0.02 2 721 . 68 GLN HG3 H 2.631 0.02 2 722 . 68 GLN HE21 H 7.639 0.02 1 723 . 68 GLN HE22 H 7.052 0.02 1 724 . 69 GLU N N 120.143 0.01 1 725 . 69 GLU CA C 59.028 0.24 1 726 . 69 GLU C C 178.416 0.12 1 727 . 69 GLU CB C 28.670 0.27 1 728 . 69 GLU CG C 35.380 0.28 1 729 . 69 GLU H H 8.369 0.01 1 730 . 69 GLU HA H 4.152 0.02 1 731 . 69 GLU HB2 H 2.320 0.02 2 732 . 69 GLU HB3 H 2.401 0.02 2 733 . 69 GLU HG2 H 2.331 0.02 2 734 . 69 GLU HG3 H 2.615 0.02 2 735 . 70 MET N N 124.379 0.01 1 736 . 70 MET CA C 58.752 0.24 1 737 . 70 MET CB C 30.617 0.27 1 738 . 70 MET CG C 33.200 0.28 1 739 . 70 MET H H 8.550 0.01 1 740 . 70 MET HA H 4.002 0.02 1 741 . 70 MET HB3 H 1.761 0.02 2 742 . 70 MET HG2 H 2.201 0.02 2 743 . 70 MET HE H 1.413 0.02 1 744 . 71 VAL N N 118.447 0.01 1 745 . 71 VAL CA C 66.943 0.24 1 746 . 71 VAL C C 178.875 0.12 1 747 . 71 VAL CB C 31.882 0.27 1 748 . 71 VAL CG1 C 21.810 0.28 1 749 . 71 VAL CG2 C 24.100 0.28 1 750 . 71 VAL H H 8.016 0.01 1 751 . 71 VAL HA H 3.739 0.02 1 752 . 71 VAL HB H 2.245 0.02 1 753 . 71 VAL HG1 H 1.074 0.02 2 754 . 71 VAL HG2 H 1.179 0.02 2 755 . 72 SER N N 115.803 0.01 1 756 . 72 SER CA C 61.916 0.24 1 757 . 72 SER C C 175.556 0.12 1 758 . 72 SER CB C 63.533 0.27 1 759 . 72 SER H H 8.170 0.01 1 760 . 72 SER HA H 4.231 0.02 1 761 . 72 SER HB2 H 4.058 0.02 2 762 . 73 PHE N N 120.143 0.01 1 763 . 73 PHE CA C 61.019 0.24 1 764 . 73 PHE C C 177.259 0.12 1 765 . 73 PHE CB C 40.760 0.27 1 766 . 73 PHE H H 8.301 0.01 1 767 . 73 PHE HA H 4.352 0.02 1 768 . 73 PHE HB2 H 3.056 0.02 2 769 . 73 PHE HB3 H 3.385 0.02 2 770 . 73 PHE HE1 H 7.274 0.02 3 771 . 74 LEU N N 114.479 0.01 1 772 . 74 LEU CA C 56.556 0.24 1 773 . 74 LEU C C 177.486 0.12 1 774 . 74 LEU CB C 43.406 0.27 1 775 . 74 LEU CG C 27.100 0.28 1 776 . 74 LEU CD1 C 26.600 0.28 1 777 . 74 LEU CD2 C 22.100 0.28 1 778 . 74 LEU H H 8.480 0.01 1 779 . 74 LEU HA H 4.090 0.02 1 780 . 74 LEU HB2 H 0.480 0.02 2 781 . 74 LEU HB3 H 1.342 0.02 2 782 . 74 LEU HG H 1.750 0.02 1 783 . 74 LEU HD1 H 0.797 0.02 2 784 . 74 LEU HD2 H 0.664 0.02 2 785 . 75 PHE N N 111.436 0.01 1 786 . 75 PHE CA C 57.695 0.24 1 787 . 75 PHE C C 176.964 0.12 1 788 . 75 PHE CB C 40.594 0.27 1 789 . 75 PHE H H 8.046 0.01 1 790 . 75 PHE HA H 4.961 0.02 1 791 . 75 PHE HB2 H 3.111 0.02 2 792 . 75 PHE HB3 H 3.395 0.02 2 793 . 75 PHE HE1 H 7.366 0.02 3 794 . 76 GLU N N 119.290 0.01 1 795 . 76 GLU CA C 57.135 0.24 1 796 . 76 GLU C C 177.368 0.12 1 797 . 76 GLU CB C 30.107 0.27 1 798 . 76 GLU CG C 36.310 0.28 1 799 . 76 GLU H H 7.650 0.01 1 800 . 76 GLU HA H 4.563 0.02 1 801 . 76 GLU HB3 H 2.311 0.02 2 802 . 76 GLU HG2 H 2.310 0.02 2 803 . 77 GLY N N 110.563 0.01 1 804 . 77 GLY CA C 46.290 0.24 1 805 . 77 GLY C C 174.792 0.12 1 806 . 77 GLY H H 8.745 0.01 1 807 . 77 GLY HA2 H 4.006 0.02 2 808 . 78 LYS N N 119.903 0.01 1 809 . 78 LYS CA C 55.732 0.24 1 810 . 78 LYS C C 176.256 0.12 1 811 . 78 LYS CB C 33.241 0.27 1 812 . 78 LYS CG C 24.544 0.28 1 813 . 78 LYS CD C 28.667 0.28 1 814 . 78 LYS CE C 42.100 0.28 1 815 . 78 LYS H H 8.091 0.01 1 816 . 78 LYS HA H 4.438 0.02 1 817 . 78 LYS HB2 H 1.812 0.02 2 818 . 78 LYS HB3 H 1.892 0.02 2 819 . 78 LYS HG2 H 1.488 0.02 2 820 . 78 LYS HG3 H 1.409 0.02 2 821 . 78 LYS HD2 H 1.720 0.02 2 822 . 78 LYS HE2 H 3.060 0.02 2 823 . 79 ASP N N 121.585 0.01 1 824 . 79 ASP CA C 54.470 0.24 1 825 . 79 ASP C C 175.910 0.12 1 826 . 79 ASP CB C 41.130 0.27 1 827 . 79 ASP H H 8.559 0.01 1 828 . 79 ASP HA H 4.654 0.02 1 829 . 79 ASP HB2 H 2.748 0.02 2 830 . 79 ASP HB3 H 2.620 0.02 2 831 . 80 VAL N N 120.111 0.01 1 832 . 80 VAL CA C 62.150 0.24 1 833 . 80 VAL C C 175.641 0.12 1 834 . 80 VAL CB C 33.166 0.27 1 835 . 80 VAL CG1 C 20.561 0.28 1 836 . 80 VAL H H 8.111 0.01 1 837 . 80 VAL HA H 4.094 0.02 1 838 . 80 VAL HB H 2.015 0.02 1 839 . 80 VAL HG2 H 0.860 0.02 2 840 . 81 HIS N N 124.358 0.01 1 841 . 81 HIS CA C 55.969 0.24 1 842 . 81 HIS C C 174.928 0.12 1 843 . 81 HIS CB C 31.020 0.27 1 844 . 81 HIS H H 8.663 0.01 1 845 . 81 HIS HA H 4.711 0.02 1 846 . 81 HIS HB2 H 3.081 0.02 2 847 . 81 HIS HB3 H 3.151 0.02 2 848 . 81 HIS HD2 H 7.067 0.02 1 849 . 81 HIS HE1 H 8.001 0.02 1 850 . 82 ILE N N 123.894 0.01 1 851 . 82 ILE CA C 60.768 0.24 1 852 . 82 ILE C C 175.906 0.12 1 853 . 82 ILE CB C 39.041 0.27 1 854 . 82 ILE CG1 C 27.004 0.28 1 855 . 82 ILE CG2 C 17.544 0.28 1 856 . 82 ILE CD1 C 13.074 0.28 1 857 . 82 ILE H H 8.283 0.01 1 858 . 82 ILE HA H 4.197 0.02 1 859 . 82 ILE HB H 1.870 0.02 1 860 . 82 ILE HG12 H 1.485 0.02 2 861 . 82 ILE HG13 H 1.178 0.02 2 862 . 82 ILE HG2 H 0.934 0.02 1 863 . 82 ILE HD1 H 0.874 0.02 1 864 . 83 GLU N N 126.064 0.01 1 865 . 83 GLU CA C 57.211 0.24 1 866 . 83 GLU C C 177.083 0.12 1 867 . 83 GLU CB C 30.180 0.27 1 868 . 83 GLU CG C 36.256 0.28 1 869 . 83 GLU H H 8.776 0.01 1 870 . 83 GLU HA H 4.565 0.02 1 871 . 83 GLU HB2 H 2.306 0.02 2 872 . 83 GLU HG2 H 2.394 0.02 2 873 . 83 GLU HG3 H 2.306 0.02 2 874 . 84 GLY N N 111.452 0.01 1 875 . 84 GLY CA C 45.730 0.24 1 876 . 84 GLY C C 173.722 0.12 1 877 . 84 GLY H H 8.737 0.01 1 878 . 84 GLY HA2 H 4.020 0.02 2 879 . 84 GLY HA3 H 3.980 0.02 2 880 . 85 TYR N N 120.874 0.01 1 881 . 85 TYR CA C 58.173 0.24 1 882 . 85 TYR C C 175.463 0.12 1 883 . 85 TYR CB C 39.419 0.27 1 884 . 85 TYR H H 8.169 0.01 1 885 . 85 TYR HA H 4.616 0.02 1 886 . 85 TYR HB2 H 2.986 0.02 2 887 . 85 TYR HE1 H 7.090 0.02 3 888 . 86 THR N N 121.371 0.01 1 889 . 86 THR CA C 58.950 0.24 1 890 . 86 THR CB C 70.141 0.27 1 891 . 86 THR H H 8.275 0.01 1 892 . 86 THR HA H 4.140 0.02 1 893 . 86 THR HG2 H 1.210 0.02 1 894 . 87 PRO CA C 63.188 0.24 1 895 . 87 PRO C C 177.072 0.12 1 896 . 87 PRO CB C 32.479 0.27 1 897 . 87 PRO CG C 27.437 0.28 1 898 . 87 PRO CD C 50.974 0.28 1 899 . 87 PRO HA H 4.344 0.02 1 900 . 87 PRO HB2 H 2.328 0.02 2 901 . 87 PRO HG2 H 2.023 0.02 2 902 . 87 PRO HD2 H 3.659 0.02 2 903 . 88 GLU N N 121.048 0.01 1 904 . 88 GLU CA C 57.104 0.24 1 905 . 88 GLU C C 176.552 0.12 1 906 . 88 GLU CB C 30.338 0.27 1 907 . 88 GLU CG C 36.394 0.28 1 908 . 88 GLU H H 8.618 0.01 1 909 . 88 GLU HA H 4.213 0.02 1 910 . 88 GLU HB3 H 2.038 0.02 2 911 . 89 ASP N N 121.330 0.01 1 912 . 89 ASP CA C 54.573 0.24 1 913 . 89 ASP C C 176.641 0.12 1 914 . 89 ASP CB C 41.245 0.27 1 915 . 89 ASP H H 8.475 0.01 1 916 . 89 ASP HA H 4.661 0.02 1 917 . 89 ASP HB2 H 2.739 0.02 2 918 . 89 ASP HB3 H 2.620 0.02 2 919 . 90 LYS N N 122.030 0.01 1 920 . 90 LYS CA C 56.396 0.24 1 921 . 90 LYS C C 176.542 0.12 1 922 . 90 LYS CB C 32.834 0.27 1 923 . 90 LYS CG C 24.584 0.28 1 924 . 90 LYS CD C 28.850 0.28 1 925 . 90 LYS CE C 42.177 0.28 1 926 . 90 LYS H H 8.358 0.01 1 927 . 90 LYS HA H 4.365 0.02 1 928 . 90 LYS HB2 H 1.837 0.02 2 929 . 90 LYS HE2 H 3.037 0.02 2 930 . 91 LYS N N 123.617 0.01 1 931 . 91 LYS CA C 56.334 0.24 1 932 . 91 LYS CB C 33.196 0.27 1 933 . 91 LYS H H 8.511 0.01 1 stop_ save_