data_6311 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific backbone 1H, 13C and 15N assignments of the 25 kDa SPRY domain-containing SOCS box protein 2 (SSB-2) ; _BMRB_accession_number 6311 _BMRB_flat_file_name bmr6311.str _Entry_type original _Submission_date 2004-09-01 _Accession_date 2004-09-01 _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 Yao Shenggen . . 2 Masters Seth L . 3 Zhang Jian-Guo . . 4 Palmer Kristen R . 5 Babon Jeffrey J . 6 Hilton Douglas J . 7 Nicola Nicos A . 8 Nicholson Sandra E . 9 Norton Raymond S . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 188 "13C chemical shifts" 570 "15N chemical shifts" 187 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-02-08 original author . stop_ _Original_release_date 2005-02-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C and 15N assignments of the 25 kDa SPRY domain-containing SOCS box protein 2 (SSB-2) ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yao Shenggen . . 2 Masters Seth L. . 3 Zhang Jian-Guo . . 4 Palmer Kristen R. . 5 Babon Jeffrey J. . 6 Nicola Nicos A. . 7 Nicholson Sandra E. . 8 Norton Raymond S. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 31 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 69 _Page_last 70 _Year 2005 _Details . loop_ _Keyword 'NMR assignment' 'SOCS protein' 'SOX box' 'SPRY domain' stop_ save_ ################################## # Molecular system description # ################################## save_system_SSB-2 _Saveframe_category molecular_system _Mol_system_name 'Spry domain-containing SOCS box protein 2' _Abbreviation_common SSB-2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label SSB-2 $SSB stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SSB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Spry domain-containing SOCS box protein' _Abbreviation_common SSB _Molecular_mass . _Mol_thiol_state 'all free' _Details ; The construct studied includes residues 12-224 of the native sequence of mouse SSB2 together with six (numbered 6 to 11) and seven (numbered 225 to 231)residues from the cleveleage sites at the N- and C-termini, respectively ; ############################## # Polymer residue sequence # ############################## _Residue_count 226 _Mol_residue_sequence ; GSSARQSTPTSQALYSDFSP PEGLEELLSAPPPDLVAQRH HGWNPKDCSENIDVKEGGLC FERRPVAQSTDGVRGKRGYS RGLHAWEISWPLEQRGTHAV VGVATALAPLQADHYAALLG SNSESWGWDIGRGKLYHQSK GLEAPQYPAGPQGEQLVVPE RLLVVLDMEEGTLGYSIGGT YLGPAFRGLKGRTLYPSVSA VWGQCQVRIRYMGERRVEET RRIHRD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 6 GLY 2 7 SER 3 8 SER 4 9 ALA 5 10 ARG 6 11 GLN 7 12 SER 8 13 THR 9 14 PRO 10 15 THR 11 16 SER 12 17 GLN 13 18 ALA 14 19 LEU 15 20 TYR 16 21 SER 17 22 ASP 18 23 PHE 19 24 SER 20 25 PRO 21 26 PRO 22 27 GLU 23 28 GLY 24 29 LEU 25 30 GLU 26 31 GLU 27 32 LEU 28 33 LEU 29 34 SER 30 35 ALA 31 36 PRO 32 37 PRO 33 38 PRO 34 39 ASP 35 40 LEU 36 41 VAL 37 42 ALA 38 43 GLN 39 44 ARG 40 45 HIS 41 46 HIS 42 47 GLY 43 48 TRP 44 49 ASN 45 50 PRO 46 51 LYS 47 52 ASP 48 53 CYS 49 54 SER 50 55 GLU 51 56 ASN 52 57 ILE 53 58 ASP 54 59 VAL 55 60 LYS 56 61 GLU 57 62 GLY 58 63 GLY 59 64 LEU 60 65 CYS 61 66 PHE 62 67 GLU 63 68 ARG 64 69 ARG 65 70 PRO 66 71 VAL 67 72 ALA 68 73 GLN 69 74 SER 70 75 THR 71 76 ASP 72 77 GLY 73 78 VAL 74 79 ARG 75 80 GLY 76 81 LYS 77 82 ARG 78 83 GLY 79 84 TYR 80 85 SER 81 86 ARG 82 87 GLY 83 88 LEU 84 89 HIS 85 90 ALA 86 91 TRP 87 92 GLU 88 93 ILE 89 94 SER 90 95 TRP 91 96 PRO 92 97 LEU 93 98 GLU 94 99 GLN 95 100 ARG 96 101 GLY 97 102 THR 98 103 HIS 99 104 ALA 100 105 VAL 101 106 VAL 102 107 GLY 103 108 VAL 104 109 ALA 105 110 THR 106 111 ALA 107 112 LEU 108 113 ALA 109 114 PRO 110 115 LEU 111 116 GLN 112 117 ALA 113 118 ASP 114 119 HIS 115 120 TYR 116 121 ALA 117 122 ALA 118 123 LEU 119 124 LEU 120 125 GLY 121 126 SER 122 127 ASN 123 128 SER 124 129 GLU 125 130 SER 126 131 TRP 127 132 GLY 128 133 TRP 129 134 ASP 130 135 ILE 131 136 GLY 132 137 ARG 133 138 GLY 134 139 LYS 135 140 LEU 136 141 TYR 137 142 HIS 138 143 GLN 139 144 SER 140 145 LYS 141 146 GLY 142 147 LEU 143 148 GLU 144 149 ALA 145 150 PRO 146 151 GLN 147 152 TYR 148 153 PRO 149 154 ALA 150 155 GLY 151 156 PRO 152 157 GLN 153 158 GLY 154 159 GLU 155 160 GLN 156 161 LEU 157 162 VAL 158 163 VAL 159 164 PRO 160 165 GLU 161 166 ARG 162 167 LEU 163 168 LEU 164 169 VAL 165 170 VAL 166 171 LEU 167 172 ASP 168 173 MET 169 174 GLU 170 175 GLU 171 176 GLY 172 177 THR 173 178 LEU 174 179 GLY 175 180 TYR 176 181 SER 177 182 ILE 178 183 GLY 179 184 GLY 180 185 THR 181 186 TYR 182 187 LEU 183 188 GLY 184 189 PRO 185 190 ALA 186 191 PHE 187 192 ARG 188 193 GLY 189 194 LEU 190 195 LYS 191 196 GLY 192 197 ARG 193 198 THR 194 199 LEU 195 200 TYR 196 201 PRO 197 202 SER 198 203 VAL 199 204 SER 200 205 ALA 201 206 VAL 202 207 TRP 203 208 GLY 204 209 GLN 205 210 CYS 206 211 GLN 207 212 VAL 208 213 ARG 209 214 ILE 210 215 ARG 211 216 TYR 212 217 MET 213 218 GLY 214 219 GLU 215 220 ARG 216 221 ARG 217 222 VAL 218 223 GLU 219 224 GLU 220 225 THR 221 226 ARG 222 227 ARG 223 228 ILE 224 229 HIS 225 230 ARG 226 231 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 2AFJ "Spry Domain-Containing Socs Box Protein 2 (Ssb-2)" 100.00 226 100.00 100.00 4.50e-162 PDB 3EK9 "Spry Domain-Containing Socs Box Protein 2: Crystal Structure And Residues Critical For Protein Binding" 94.25 213 100.00 100.00 3.40e-152 DBJ BAE28397 "unnamed protein product [Mus musculus]" 96.02 264 98.16 99.08 2.59e-152 GB AAC36017 "C9 [Mus musculus]" 96.02 264 98.16 99.08 2.59e-152 GB AAH02005 "Spsb2 protein [Mus musculus]" 96.02 264 98.16 99.08 2.59e-152 GB AAH10305 "Spsb2 protein [Mus musculus]" 95.58 258 98.15 98.15 4.29e-150 GB AAL57356 "SPRY domain-containing SOCS box protein SSB-2 [Mus musculus]" 96.02 264 98.16 99.08 2.59e-152 GB EDK99761 "splA/ryanodine receptor domain and SOCS box containing 2, isoform CRA_a [Mus musculus]" 96.02 264 98.16 99.08 2.59e-152 REF NP_038567 "SPRY domain-containing SOCS box protein 2 [Mus musculus]" 96.02 264 98.16 99.08 2.59e-152 REF XP_006505628 "PREDICTED: SPRY domain-containing SOCS box protein 2 isoform X1 [Mus musculus]" 96.02 358 98.16 99.08 2.12e-151 REF XP_006505629 "PREDICTED: SPRY domain-containing SOCS box protein 2 isoform X2 [Mus musculus]" 84.51 305 100.00 100.00 6.23e-134 REF XP_006505630 "PREDICTED: SPRY domain-containing SOCS box protein 2 isoform X3 [Mus musculus]" 96.02 264 98.16 99.08 2.59e-152 REF XP_006505631 "PREDICTED: SPRY domain-containing SOCS box protein 2 isoform X4 [Mus musculus]" 96.02 264 98.16 99.08 2.59e-152 SP O88838 "RecName: Full=SPRY domain-containing SOCS box protein 2; Short=SSB-2; AltName: Full=Gene-rich cluster protein C9 [Mus musculus]" 96.02 264 98.16 99.08 2.59e-152 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $SSB 'house mouse' 10090 Eukaryota Metazoa Mus musculus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name $SSB 'recombinant technology' 'E. coli' Escherichia coli BL21 DE3 plasmid pGEX 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 $SSB 0.60 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SSB 0.40 mM [U-15N] stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SSB 0.6 mM '[U-13C; U-15N]' stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SSB 1.0 mM '[U-13C; U-15N; U-70% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 3.5 loop_ _Task 'spectral process' stop_ _Details 'Bruker system software' save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3 loop_ _Task 'spectral analysis' stop_ _Details ; Bartels, C., Xia, T-H., Billeter, M., Guntert, P., and Wuthrich, K. (1995) J. Biomol. NMR 6, 1 10. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 500 _Details . save_ save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details 'A cryoprobe on the AVANCE500 was used.' save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details 'A cryoprobe on the AVANCE500 was used.' save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details 'A cryoprobe on the AVANCE500 was used.' save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details 'A cryoprobe on the AVANCE500 was used.' save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details 'A cryoprobe on the AVANCE500 was used.' save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details 'A cryoprobe on the AVANCE500 was used.' save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details 'A cryoprobe on the AVANCE500 was used.' save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.2 n/a temperature 295 0.2 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 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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 $sample_2 $sample_3 $sample_4 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name SSB-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 . 3 SER C C 174.5 0.2 1 2 . 3 SER CA C 58.7 0.2 1 3 . 3 SER CB C 64.4 0.2 1 4 . 4 ALA H H 8.35 0.01 1 5 . 4 ALA C C 178.0 0.2 1 6 . 4 ALA CA C 52.9 0.2 1 7 . 4 ALA CB C 19.2 0.2 1 8 . 4 ALA N N 126.1 0.2 1 9 . 5 ARG H H 8.28 0.01 1 10 . 5 ARG C C 175.0 0.2 1 11 . 5 ARG CA C 56.4 0.2 1 12 . 5 ARG CB C 30.9 0.2 1 13 . 5 ARG N N 120.3 0.2 1 14 . 6 GLN H H 8.22 0.01 1 15 . 6 GLN C C 175.6 0.2 1 16 . 6 GLN CA C 55.9 0.2 1 17 . 6 GLN CB C 31.2 0.2 1 18 . 6 GLN N N 124.2 0.2 1 19 . 7 SER C C 174.5 0.2 1 20 . 7 SER CA C 58.2 0.2 1 21 . 7 SER CB C 64.0 0.2 1 22 . 8 THR H H 8.22 0.01 1 23 . 8 THR C C 173.2 0.2 1 24 . 8 THR N N 118.1 0.2 1 25 . 9 PRO C C 177.5 0.2 1 26 . 9 PRO CA C 64.1 0.2 1 27 . 9 PRO CB C 32.4 0.2 1 28 . 10 THR H H 8.24 0.01 1 29 . 10 THR C C 175.1 0.2 1 30 . 10 THR CA C 62.3 0.2 1 31 . 10 THR CB C 70.3 0.2 1 32 . 10 THR N N 114.0 0.2 1 33 . 11 SER H H 8.27 0.01 1 34 . 11 SER C C 174.8 0.2 1 35 . 11 SER CA C 58.8 0.2 1 36 . 11 SER CB C 64.4 0.2 1 37 . 11 SER N N 117.7 0.2 1 38 . 12 GLN H H 8.34 0.01 1 39 . 12 GLN C C 175.9 0.2 1 40 . 12 GLN CA C 56.2 0.2 1 41 . 12 GLN CB C 29.7 0.2 1 42 . 12 GLN N N 122.2 0.2 1 43 . 13 ALA H H 8.22 0.01 1 44 . 13 ALA C C 177.7 0.2 1 45 . 13 ALA CA C 52.8 0.2 1 46 . 13 ALA CB C 19.1 0.2 1 47 . 13 ALA N N 125.2 0.2 1 48 . 14 LEU H H 8.06 0.01 1 49 . 14 LEU C C 177.2 0.2 1 50 . 14 LEU CA C 55.4 0.2 1 51 . 14 LEU CB C 42.8 0.2 1 52 . 14 LEU N N 121.0 0.2 1 53 . 15 TYR H H 8.09 0.01 1 54 . 15 TYR C C 176.0 0.2 1 55 . 15 TYR CA C 57.8 0.2 1 56 . 15 TYR CB C 39.1 0.2 1 57 . 15 TYR N N 120.0 0.2 1 58 . 16 SER H H 8.02 0.01 1 59 . 16 SER C C 174.1 0.2 1 60 . 16 SER CA C 58.1 0.2 1 61 . 16 SER CB C 64.6 0.2 1 62 . 16 SER N N 116.2 0.2 1 63 . 17 ASP H H 8.24 0.01 1 64 . 17 ASP C C 175.9 0.2 1 65 . 17 ASP CA C 54.7 0.2 1 66 . 17 ASP CB C 41.5 0.2 1 67 . 17 ASP N N 122.3 0.2 1 68 . 18 PHE H H 7.98 0.01 1 69 . 18 PHE C C 175.7 0.2 1 70 . 18 PHE CA C 57.2 0.2 1 71 . 18 PHE CB C 40.5 0.2 1 72 . 18 PHE N N 118.7 0.2 1 73 . 19 SER H H 8.45 0.01 1 74 . 19 SER C C 172.2 0.2 1 75 . 19 SER CA C 58.5 0.2 1 76 . 19 SER CB C 63.9 0.2 1 77 . 19 SER N N 126.3 0.2 1 78 . 21 PRO C C 177.1 0.2 1 79 . 21 PRO CA C 62.7 0.2 1 80 . 21 PRO CB C 32.0 0.2 1 81 . 22 GLU H H 8.81 0.01 1 82 . 22 GLU C C 176.9 0.2 1 83 . 22 GLU CA C 58.4 0.2 1 84 . 22 GLU CB C 29.3 0.2 1 85 . 22 GLU N N 125.9 0.2 1 86 . 23 GLY H H 8.60 0.01 1 87 . 23 GLY C C 175.1 0.2 1 88 . 23 GLY CA C 45.3 0.2 1 89 . 23 GLY N N 111.6 0.2 1 90 . 24 LEU H H 7.47 0.01 1 91 . 24 LEU C C 177.5 0.2 1 92 . 24 LEU CA C 58.4 0.2 1 93 . 24 LEU CB C 41.8 0.2 1 94 . 24 LEU N N 121.7 0.2 1 95 . 25 GLU H H 8.49 0.01 1 96 . 25 GLU C C 179.7 0.2 1 97 . 25 GLU CA C 59.9 0.2 1 98 . 25 GLU CB C 29.0 0.2 1 99 . 25 GLU N N 117.7 0.2 1 100 . 26 GLU H H 8.16 0.01 1 101 . 26 GLU C C 179.5 0.2 1 102 . 26 GLU CA C 60.0 0.2 1 103 . 26 GLU CB C 29.0 0.2 1 104 . 26 GLU N N 120.3 0.2 1 105 . 27 LEU H H 7.96 0.01 1 106 . 27 LEU C C 179.8 0.2 1 107 . 27 LEU CA C 58.9 0.2 1 108 . 27 LEU CB C 43.0 0.2 1 109 . 27 LEU N N 122.7 0.2 1 110 . 28 LEU H H 7.98 0.01 1 111 . 28 LEU C C 178.2 0.2 1 112 . 28 LEU CA C 56.1 0.2 1 113 . 28 LEU CB C 40.8 0.2 1 114 . 28 LEU N N 117.7 0.2 1 115 . 29 SER H H 7.59 0.01 1 116 . 29 SER C C 173.9 0.2 1 117 . 29 SER CA C 59.0 0.2 1 118 . 29 SER CB C 64.0 0.2 1 119 . 29 SER N N 113.5 0.2 1 120 . 30 ALA H H 7.02 0.01 1 121 . 30 ALA C C 174.5 0.2 1 122 . 30 ALA CA C 50.9 0.2 1 123 . 30 ALA CB C 17.7 0.2 1 124 . 30 ALA N N 126.9 0.2 1 125 . 33 PRO C C 177.0 0.2 1 126 . 33 PRO CA C 63.4 0.2 1 127 . 33 PRO CB C 32.7 0.2 1 128 . 34 ASP H H 8.59 0.01 1 129 . 34 ASP C C 175.8 0.2 1 130 . 34 ASP CA C 53.2 0.2 1 131 . 34 ASP CB C 41.1 0.2 1 132 . 34 ASP N N 123.9 0.2 1 133 . 35 LEU H H 8.23 0.01 1 134 . 35 LEU C C 178.7 0.2 1 135 . 35 LEU CA C 58.9 0.2 1 136 . 35 LEU CB C 42.6 0.2 1 137 . 35 LEU N N 118.7 0.2 1 138 . 36 VAL H H 7.37 0.01 1 139 . 36 VAL C C 179.2 0.2 1 140 . 36 VAL CA C 58.9 0.2 1 141 . 36 VAL CB C 32.2 0.2 1 142 . 36 VAL N N 117.6 0.2 1 143 . 37 ALA H H 7.95 0.01 1 144 . 37 ALA C C 180.8 0.2 1 145 . 37 ALA CA C 55.5 0.2 1 146 . 37 ALA CB C 19.4 0.2 1 147 . 37 ALA N N 123.9 0.2 1 148 . 38 GLN H H 8.94 0.01 1 149 . 38 GLN C C 180.6 0.2 1 150 . 38 GLN CA C 60.4 0.2 1 151 . 38 GLN CB C 29.9 0.2 1 152 . 38 GLN N N 116.3 0.2 1 153 . 39 ARG H H 8.33 0.01 1 154 . 39 ARG C C 180.6 0.2 1 155 . 39 ARG CA C 61.2 0.2 1 156 . 39 ARG CB C 30.2 0.2 1 157 . 39 ARG N N 118.7 0.2 1 158 . 40 HIS H H 8.13 0.01 1 159 . 40 HIS C C 175.9 0.2 1 160 . 40 HIS CA C 59.5 0.2 1 161 . 40 HIS CB C 30.5 0.2 1 162 . 40 HIS N N 122.3 0.2 1 163 . 41 HIS H H 7.32 0.01 1 164 . 41 HIS C C 175.0 0.2 1 165 . 41 HIS CA C 56.5 0.2 1 166 . 41 HIS CB C 32.3 0.2 1 167 . 41 HIS N N 114.3 0.2 1 168 . 42 GLY H H 7.11 0.01 1 169 . 42 GLY C C 172.1 0.2 1 170 . 42 GLY CA C 43.9 0.2 1 171 . 42 GLY N N 106.4 0.2 1 172 . 43 TRP H H 9.26 0.01 1 173 . 43 TRP C C 175.4 0.2 1 174 . 43 TRP CA C 56.8 0.2 1 175 . 43 TRP CB C 29.4 0.2 1 176 . 43 TRP N N 118.7 0.2 1 177 . 44 ASN H H 8.43 0.01 1 178 . 44 ASN C C 174.5 0.2 1 179 . 44 ASN CA C 50.0 0.2 1 180 . 44 ASN CB C 40.4 0.2 1 181 . 44 ASN N N 117.6 0.2 1 182 . 45 PRO C C 177.5 0.2 1 183 . 45 PRO CA C 64.3 0.2 1 184 . 45 PRO CB C 32.9 0.2 1 185 . 46 LYS H H 7.54 0.01 1 186 . 46 LYS C C 175.6 0.2 1 187 . 46 LYS CA C 54.9 0.2 1 188 . 46 LYS CB C 31.8 0.2 1 189 . 46 LYS N N 113.8 0.2 1 190 . 47 ASP H H 7.60 0.01 1 191 . 47 ASP C C 171.3 0.2 1 192 . 47 ASP CA C 52.2 0.2 1 193 . 47 ASP CB C 40.1 0.2 1 194 . 47 ASP N N 122.8 0.2 1 195 . 48 CYS H H 7.59 0.01 1 196 . 48 CYS C C 173.4 0.2 1 197 . 48 CYS CA C 56.2 0.2 1 198 . 48 CYS CB C 31.5 0.2 1 199 . 48 CYS N N 113.5 0.2 1 200 . 49 SER H H 7.96 0.01 1 201 . 49 SER C C 175.9 0.2 1 202 . 49 SER CA C 57.3 0.2 1 203 . 49 SER CB C 63.6 0.2 1 204 . 49 SER N N 115.4 0.2 1 205 . 50 GLU H H 8.45 0.01 1 206 . 50 GLU C C 176.6 0.2 1 207 . 50 GLU CA C 58.5 0.2 1 208 . 50 GLU CB C 29.6 0.2 1 209 . 50 GLU N N 126.4 0.2 1 210 . 51 ASN H H 8.31 0.01 1 211 . 51 ASN C C 174.9 0.2 1 212 . 51 ASN CA C 52.7 0.2 1 213 . 51 ASN CB C 38.2 0.2 1 214 . 51 ASN N N 114.3 0.2 1 215 . 52 ILE H H 7.60 0.01 1 216 . 52 ILE C C 173.0 0.2 1 217 . 52 ILE CA C 60.1 0.2 1 218 . 52 ILE CB C 40.5 0.2 1 219 . 52 ILE N N 120.6 0.2 1 220 . 53 ASP H H 8.49 0.01 1 221 . 53 ASP C C 175.5 0.2 1 222 . 53 ASP CA C 53.1 0.2 1 223 . 53 ASP CB C 43.5 0.2 1 224 . 53 ASP N N 124.4 0.2 1 225 . 54 VAL H H 9.27 0.01 1 226 . 54 VAL C C 175.6 0.2 1 227 . 54 VAL CA C 64.4 0.2 1 228 . 54 VAL CB C 32.0 0.2 1 229 . 54 VAL N N 126.1 0.2 1 230 . 55 LYS H H 9.16 0.01 1 231 . 55 LYS C C 176.8 0.2 1 232 . 55 LYS CA C 55.0 0.2 1 233 . 55 LYS CB C 36.9 0.2 1 234 . 55 LYS N N 128.0 0.2 1 235 . 56 GLU H H 9.33 0.01 1 236 . 56 GLU C C 178.6 0.2 1 237 . 56 GLU CA C 57.3 0.2 1 238 . 56 GLU CB C 29.1 0.2 1 239 . 56 GLU N N 116.5 0.2 1 240 . 57 GLY H H 8.99 0.01 1 241 . 57 GLY C C 174.2 0.2 1 242 . 57 GLY CA C 47.0 0.2 1 243 . 57 GLY N N 106.4 0.2 1 244 . 58 GLY H H 7.85 0.01 1 245 . 58 GLY C C 174.6 0.2 1 246 . 58 GLY CA C 44.2 0.2 1 247 . 58 GLY N N 102.7 0.2 1 248 . 59 LEU H H 7.23 0.01 1 249 . 59 LEU C C 176.5 0.2 1 250 . 59 LEU CA C 57.2 0.2 1 251 . 59 LEU CB C 40.8 0.2 1 252 . 59 LEU N N 116.1 0.2 1 253 . 60 CYS H H 7.80 0.01 1 254 . 60 CYS C C 172.8 0.2 1 255 . 60 CYS CA C 56.3 0.2 1 256 . 60 CYS CB C 31.1 0.2 1 257 . 60 CYS N N 110.8 0.2 1 258 . 61 PHE H H 8.27 0.01 1 259 . 61 PHE C C 176.1 0.2 1 260 . 61 PHE CA C 56.4 0.2 1 261 . 61 PHE CB C 41.3 0.2 1 262 . 61 PHE N N 122.5 0.2 1 263 . 62 GLU H H 9.13 0.01 1 264 . 62 GLU C C 176.3 0.2 1 265 . 62 GLU CA C 53.7 0.2 1 266 . 62 GLU N N 120.3 0.2 1 267 . 65 PRO C C 175.5 0.2 1 268 . 65 PRO CA C 63.2 0.2 1 269 . 65 PRO CB C 29.1 0.2 1 270 . 66 VAL H H 7.82 0.01 1 271 . 66 VAL C C 175.4 0.2 1 272 . 66 VAL CA C 61.5 0.2 1 273 . 66 VAL CB C 33.9 0.2 1 274 . 66 VAL N N 123.6 0.2 1 275 . 67 ALA H H 8.55 0.01 1 276 . 67 ALA C C 177.4 0.2 1 277 . 67 ALA CA C 52.4 0.2 1 278 . 67 ALA CB C 19.7 0.2 1 279 . 71 ASP H H 8.75 0.01 1 280 . 71 ASP C C 173.8 0.2 1 281 . 71 ASP CA C 54.9 0.2 1 282 . 71 ASP CB C 42.7 0.2 1 283 . 71 ASP N N 124.4 0.2 1 284 . 72 GLY H H 9.35 0.01 1 285 . 72 GLY C C 170.8 0.2 1 286 . 72 GLY CA C 43.3 0.2 1 287 . 72 GLY N N 110.6 0.2 1 288 . 73 VAL H H 6.87 0.01 1 289 . 73 VAL C C 172.8 0.2 1 290 . 73 VAL CA C 59.6 0.2 1 291 . 73 VAL CB C 33.6 0.2 1 292 . 73 VAL N N 113.7 0.2 1 293 . 74 ARG H H 7.94 0.01 1 294 . 74 ARG C C 177.6 0.2 1 295 . 74 ARG CA C 55.1 0.2 1 296 . 74 ARG CB C 35.2 0.2 1 297 . 74 ARG N N 126.3 0.2 1 298 . 75 GLY H H 8.77 0.01 1 299 . 75 GLY C C 173.1 0.2 1 300 . 75 GLY CA C 44.5 0.2 1 301 . 75 GLY N N 104.0 0.2 1 302 . 76 LYS H H 8.72 0.01 1 303 . 76 LYS C C 176.8 0.2 1 304 . 76 LYS CA C 59.7 0.2 1 305 . 76 LYS CB C 35.8 0.2 1 306 . 76 LYS N N 118.1 0.2 1 307 . 77 ARG H H 8.80 0.01 1 308 . 77 ARG C C 171.5 0.2 1 309 . 77 ARG CA C 53.5 0.2 1 310 . 77 ARG CB C 31.1 0.2 1 311 . 77 ARG N N 117.9 0.2 1 312 . 78 GLY H H 7.24 0.01 1 313 . 78 GLY C C 174.1 0.2 1 314 . 78 GLY CA C 41.8 0.2 1 315 . 78 GLY N N 106.1 0.2 1 316 . 79 TYR H H 8.83 0.01 1 317 . 79 TYR C C 175.9 0.2 1 318 . 79 TYR CA C 56.3 0.2 1 319 . 79 TYR CB C 39.4 0.2 1 320 . 79 TYR N N 126.9 0.2 1 321 . 80 SER H H 9.25 0.01 1 322 . 80 SER C C 173.8 0.2 1 323 . 80 SER CA C 58.0 0.2 1 324 . 80 SER CB C 64.4 0.2 1 325 . 80 SER N N 115.7 0.2 1 326 . 81 ARG H H 8.15 0.01 1 327 . 81 ARG C C 175.6 0.2 1 328 . 81 ARG CA C 54.1 0.2 1 329 . 81 ARG CB C 33.4 0.2 1 330 . 81 ARG N N 121.2 0.2 1 331 . 82 GLY H H 9.85 0.01 1 332 . 82 GLY C C 171.2 0.2 1 333 . 82 GLY CA C 45.0 0.2 1 334 . 82 GLY N N 108.6 0.2 1 335 . 83 LEU H H 7.73 0.01 1 336 . 83 LEU C C 174.3 0.2 1 337 . 83 LEU CA C 53.7 0.2 1 338 . 83 LEU CB C 43.8 0.2 1 339 . 83 LEU N N 120.9 0.2 1 340 . 84 HIS H H 9.01 0.01 1 341 . 84 HIS C C 174.3 0.2 1 342 . 84 HIS CA C 54.4 0.2 1 343 . 84 HIS CB C 36.5 0.2 1 344 . 84 HIS N N 123.9 0.2 1 345 . 85 ALA H H 7.58 0.01 1 346 . 85 ALA C C 175.8 0.2 1 347 . 85 ALA CA C 50.1 0.2 1 348 . 85 ALA CB C 22.2 0.2 1 349 . 85 ALA N N 118.6 0.2 1 350 . 86 TRP H H 8.48 0.01 1 351 . 86 TRP C C 172.1 0.2 1 352 . 86 TRP CA C 56.8 0.2 1 353 . 86 TRP CB C 31.6 0.2 1 354 . 86 TRP N N 116.2 0.2 1 355 . 87 GLU H H 9.24 0.01 1 356 . 87 GLU C C 177.0 0.2 1 357 . 87 GLU CA C 54.7 0.2 1 358 . 87 GLU CB C 33.9 0.2 1 359 . 87 GLU N N 123.2 0.2 1 360 . 88 ILE H H 9.59 0.01 1 361 . 88 ILE C C 175.7 0.2 1 362 . 88 ILE CA C 56.9 0.2 1 363 . 88 ILE CB C 38.8 0.2 1 364 . 88 ILE N N 130.0 0.2 1 365 . 89 SER H H 8.50 0.01 1 366 . 89 SER C C 173.8 0.2 1 367 . 89 SER CA C 57.1 0.2 1 368 . 89 SER CB C 64.9 0.2 1 369 . 89 SER N N 120.9 0.2 1 370 . 90 TRP H H 9.45 0.01 1 371 . 90 TRP C C 173.1 0.2 1 372 . 90 TRP CA C 53.0 0.2 1 373 . 90 TRP CB C 31.0 0.2 1 374 . 90 TRP N N 127.7 0.2 1 375 . 91 PRO C C 177.3 0.2 1 376 . 91 PRO CA C 64.6 0.2 1 377 . 91 PRO CB C 32.9 0.2 1 378 . 92 LEU H H 8.76 0.01 1 379 . 92 LEU C C 179.6 0.2 1 380 . 92 LEU CA C 59.7 0.2 1 381 . 92 LEU CB C 41.9 0.2 1 382 . 92 LEU N N 126.1 0.2 1 383 . 93 GLU H H 9.25 0.01 1 384 . 93 GLU C C 176.4 0.2 1 385 . 93 GLU CA C 57.4 0.2 1 386 . 93 GLU CB C 27.9 0.2 1 387 . 93 GLU N N 115.7 0.2 1 388 . 94 GLN H H 7.37 0.01 1 389 . 94 GLN C C 175.7 0.2 1 390 . 94 GLN CA C 53.3 0.2 1 391 . 94 GLN N N 117.9 0.2 1 392 . 95 ARG H H 6.80 0.01 1 393 . 95 ARG C C 177.0 0.2 1 394 . 95 ARG CA C 58.2 0.2 1 395 . 95 ARG CB C 30.8 0.2 1 396 . 95 ARG N N 119.2 0.2 1 397 . 96 GLY H H 7.95 0.01 1 398 . 96 GLY C C 175.5 0.2 1 399 . 96 GLY CA C 46.7 0.2 1 400 . 96 GLY N N 106.1 0.2 1 401 . 97 THR H H 8.04 0.01 1 402 . 97 THR C C 175.3 0.2 1 403 . 97 THR CA C 64.0 0.2 1 404 . 97 THR CB C 69.9 0.2 1 405 . 97 THR N N 111.6 0.2 1 406 . 100 VAL H H 8.06 0.01 1 407 . 100 VAL C C 176.0 0.2 1 408 . 100 VAL CA C 61.5 0.2 1 409 . 100 VAL N N 120.9 0.2 1 410 . 101 VAL H H 8.87 0.01 1 411 . 101 VAL C C 178.4 0.2 1 412 . 101 VAL CA C 61.5 0.2 1 413 . 101 VAL CB C 35.9 0.2 1 414 . 101 VAL N N 123.6 0.2 1 415 . 102 GLY H H 9.17 0.01 1 416 . 102 GLY C C 172.5 0.2 1 417 . 102 GLY CA C 48.4 0.2 1 418 . 102 GLY N N 118.4 0.2 1 419 . 103 VAL H H 9.47 0.01 1 420 . 103 VAL C C 173.8 0.2 1 421 . 103 VAL CA C 59.5 0.2 1 422 . 103 VAL CB C 38.9 0.2 1 423 . 103 VAL N N 120.3 0.2 1 424 . 104 ALA H H 9.25 0.01 1 425 . 104 ALA C C 178.3 0.2 1 426 . 104 ALA CA C 51.4 0.2 1 427 . 104 ALA CB C 24.4 0.2 1 428 . 104 ALA N N 121.7 0.2 1 429 . 105 THR H H 9.23 0.01 1 430 . 105 THR C C 176.4 0.2 1 431 . 105 THR CA C 61.8 0.2 1 432 . 105 THR CB C 71.0 0.2 1 433 . 105 THR N N 111.6 0.2 1 434 . 106 ALA H H 9.45 0.01 1 435 . 106 ALA C C 177.0 0.2 1 436 . 106 ALA CA C 53.9 0.2 1 437 . 106 ALA CB C 18.8 0.2 1 438 . 106 ALA N N 120.9 0.2 1 439 . 107 LEU H H 7.84 0.01 1 440 . 107 LEU C C 178.4 0.2 1 441 . 107 LEU CA C 54.7 0.2 1 442 . 107 LEU CB C 42.6 0.2 1 443 . 107 LEU N N 113.1 0.2 1 444 . 108 ALA H H 6.65 0.01 1 445 . 108 ALA C C 175.4 0.2 1 446 . 108 ALA CA C 51.4 0.2 1 447 . 108 ALA CB C 17.9 0.2 1 448 . 108 ALA N N 123.1 0.2 1 449 . 109 PRO C C 176.7 0.2 1 450 . 109 PRO CA C 63.0 0.2 1 451 . 109 PRO CB C 31.7 0.2 1 452 . 110 LEU H H 8.36 0.01 1 453 . 110 LEU C C 175.4 0.2 1 454 . 110 LEU CA C 53.7 0.2 1 455 . 110 LEU CB C 41.9 0.2 1 456 . 110 LEU N N 116.5 0.2 1 457 . 111 GLN H H 7.21 0.01 1 458 . 111 GLN C C 174.8 0.2 1 459 . 111 GLN CA C 55.7 0.2 1 460 . 111 GLN CB C 32.4 0.2 1 461 . 111 GLN N N 117.9 0.2 1 462 . 112 ALA H H 8.55 0.01 1 463 . 112 ALA C C 176.6 0.2 1 464 . 112 ALA CA C 51.2 0.2 1 465 . 112 ALA CB C 22.3 0.2 1 466 . 112 ALA N N 123.9 0.2 1 467 . 113 ASP H H 8.39 0.01 1 468 . 113 ASP C C 177.1 0.2 1 469 . 113 ASP CA C 54.3 0.2 1 470 . 113 ASP N N 122.0 0.2 1 471 . 114 HIS C C 176.5 0.2 1 472 . 115 TYR H H 7.629 0.01 1 473 . 115 TYR C C 172.6 0.2 1 474 . 115 TYR CA C 56.7 0.2 1 475 . 115 TYR N N 114.9 0.2 1 476 . 120 GLY CA C 44.8 0.2 1 477 . 121 SER H H 7.63 0.01 1 478 . 121 SER C C 172.6 0.2 1 479 . 121 SER CA C 59.0 0.2 1 480 . 121 SER CB C 63.7 0.2 1 481 . 121 SER N N 114.0 0.2 1 482 . 122 ASN H H 6.79 0.01 1 483 . 122 ASN C C 175.1 0.2 1 484 . 122 ASN CA C 52.2 0.2 1 485 . 122 ASN N N 112.4 0.2 1 486 . 123 SER C C 173.3 0.2 1 487 . 123 SER CA C 59.7 0.2 1 488 . 123 SER CB C 63.0 0.2 1 489 . 124 GLU H H 7.78 0.01 1 490 . 124 GLU C C 173.9 0.2 1 491 . 124 GLU CA C 54.3 0.2 1 492 . 124 GLU CB C 29.5 0.2 1 493 . 124 GLU N N 117.6 0.2 1 494 . 125 SER H H 6.83 0.01 1 495 . 125 SER C C 172.6 0.2 1 496 . 125 SER CA C 58.6 0.2 1 497 . 125 SER CB C 66.1 0.2 1 498 . 125 SER N N 108.0 0.2 1 499 . 126 TRP H H 8.82 0.01 1 500 . 126 TRP C C 175.3 0.2 1 501 . 126 TRP CA C 58.6 0.2 1 502 . 126 TRP CB C 33.3 0.2 1 503 . 126 TRP N N 123.9 0.2 1 504 . 127 GLY H H 9.21 0.01 1 505 . 127 GLY C C 169.1 0.2 1 506 . 127 GLY CA C 46.7 0.2 1 507 . 127 GLY N N 106.9 0.2 1 508 . 128 TRP H H 8.41 0.01 1 509 . 128 TRP C C 174.8 0.2 1 510 . 128 TRP CA C 53.7 0.2 1 511 . 128 TRP CB C 32.2 0.2 1 512 . 128 TRP N N 123.1 0.2 1 513 . 129 ASP H H 9.25 0.01 1 514 . 129 ASP C C 176.3 0.2 1 515 . 129 ASP CA C 53.2 0.2 1 516 . 129 ASP CB C 40.8 0.2 1 517 . 129 ASP N N 127.7 0.2 1 518 . 130 ILE H H 7.73 0.01 1 519 . 130 ILE C C 175.9 0.2 1 520 . 130 ILE CA C 62.9 0.2 1 521 . 130 ILE N N 119.5 0.2 1 522 . 131 GLY H H 8.23 0.01 1 523 . 131 GLY C C 175.0 0.2 1 524 . 131 GLY CA C 45.7 0.2 1 525 . 131 GLY N N 108.0 0.2 1 526 . 132 ARG H H 7.64 0.01 1 527 . 132 ARG C C 177.2 0.2 1 528 . 132 ARG CA C 56.0 0.2 1 529 . 132 ARG CB C 33.0 0.2 1 530 . 132 ARG N N 117.9 0.2 1 531 . 133 GLY H H 8.40 0.01 1 532 . 133 GLY C C 174.2 0.2 1 533 . 133 GLY CA C 47.4 0.2 1 534 . 133 GLY N N 109.7 0.2 1 535 . 134 LYS H H 6.51 0.01 1 536 . 134 LYS C C 175.4 0.2 1 537 . 134 LYS CA C 54.3 0.2 1 538 . 134 LYS CB C 37.1 0.2 1 539 . 134 LYS N N 115.4 0.2 1 540 . 135 LEU H H 8.24 0.01 1 541 . 135 LEU C C 176.4 0.2 1 542 . 135 LEU CA C 56.6 0.2 1 543 . 135 LEU N N 120.1 0.2 1 544 . 136 TYR H H 9.44 0.01 1 545 . 136 TYR CA C 55.4 0.2 1 546 . 136 TYR CB C 40.8 0.2 1 547 . 136 TYR N N 119.8 0.2 1 548 . 137 HIS H H 8.21 0.01 1 549 . 137 HIS C C 174.4 0.2 1 550 . 137 HIS CA C 59.1 0.2 1 551 . 137 HIS CB C 30.4 0.2 1 552 . 137 HIS N N 121.2 0.2 1 553 . 138 GLN H H 6.78 0.01 1 554 . 138 GLN C C 175.3 0.2 1 555 . 138 GLN CA C 57.2 0.2 1 556 . 138 GLN CB C 27.3 0.2 1 557 . 138 GLN N N 123.6 0.2 1 558 . 139 SER H H 8.07 0.01 1 559 . 139 SER C C 175.1 0.2 1 560 . 139 SER CA C 59.4 0.2 1 561 . 139 SER CB C 65.2 0.2 1 562 . 139 SER N N 111.6 0.2 1 563 . 140 LYS H H 8.53 0.01 1 564 . 140 LYS C C 177.2 0.2 1 565 . 140 LYS CA C 56.5 0.2 1 566 . 140 LYS CB C 32.4 0.2 1 567 . 140 LYS N N 123.9 0.2 1 568 . 141 GLY H H 8.50 0.01 1 569 . 141 GLY C C 174.5 0.2 1 570 . 141 GLY CA C 45.8 0.2 1 571 . 141 GLY N N 109.7 0.2 1 572 . 142 LEU H H 8.09 0.01 1 573 . 142 LEU C C 177.7 0.2 1 574 . 142 LEU CA C 55.0 0.2 1 575 . 142 LEU CB C 42.5 0.2 1 576 . 142 LEU N N 120.9 0.2 1 577 . 143 GLU H H 8.41 0.01 1 578 . 143 GLU C C 175.8 0.2 1 579 . 143 GLU CA C 56.8 0.2 1 580 . 143 GLU CB C 29.5 0.2 1 581 . 143 GLU N N 120.6 0.2 1 582 . 144 ALA H H 8.19 0.01 1 583 . 144 ALA C C 174.9 0.2 1 584 . 144 ALA CA C 50.9 0.2 1 585 . 144 ALA CB C 20.2 0.2 1 586 . 144 ALA N N 128.3 0.2 1 587 . 145 PRO C C 175.8 0.2 1 588 . 145 PRO CA C 62.8 0.2 1 589 . 145 PRO CB C 33.0 0.2 1 590 . 146 GLN H H 8.32 0.01 1 591 . 146 GLN C C 175.8 0.2 1 592 . 146 GLN CA C 55.6 0.2 1 593 . 146 GLN CB C 30.9 0.2 1 594 . 146 GLN N N 120.1 0.2 1 595 . 147 TYR H H 8.46 0.01 1 596 . 147 TYR C C 175.8 0.2 1 597 . 147 TYR CA C 55.5 0.2 1 598 . 147 TYR CB C 46.2 0.2 1 599 . 147 TYR N N 125.8 0.2 1 600 . 148 PRO C C 173.3 0.2 1 601 . 148 PRO CA C 62.3 0.2 1 602 . 148 PRO CB C 33.9 0.2 1 603 . 149 ALA H H 8.41 0.01 1 604 . 149 ALA C C 178.2 0.2 1 605 . 149 ALA CA C 52.6 0.2 1 606 . 149 ALA CB C 19.9 0.2 1 607 . 149 ALA N N 123.1 0.2 1 608 . 150 GLY H H 8.26 0.01 1 609 . 150 GLY C C 173.0 0.2 1 610 . 150 GLY CA C 45.3 0.2 1 611 . 150 GLY N N 107.7 0.2 1 612 . 151 PRO C C 178.8 0.2 1 613 . 151 PRO CA C 64.3 0.2 1 614 . 151 PRO CB C 32.0 0.2 1 615 . 152 GLN H H 8.75 0.01 1 616 . 152 GLN C C 177.8 0.2 1 617 . 152 GLN CA C 57.8 0.2 1 618 . 152 GLN CB C 28.7 0.2 1 619 . 152 GLN N N 118.1 0.2 1 620 . 153 GLY H H 8.01 0.01 1 621 . 153 GLY C C 174.9 0.2 1 622 . 153 GLY CA C 46.0 0.2 1 623 . 153 GLY N N 107.3 0.2 1 624 . 154 GLU H H 7.61 0.01 1 625 . 154 GLU C C 176.8 0.2 1 626 . 154 GLU CA C 57.5 0.2 1 627 . 154 GLU CB C 30.0 0.2 1 628 . 154 GLU N N 120.3 0.2 1 629 . 155 GLN H H 8.19 0.01 1 630 . 155 GLN C C 175.4 0.2 1 631 . 155 GLN CA C 55.6 0.2 1 632 . 155 GLN CB C 28.9 0.2 1 633 . 155 GLN N N 119.3 0.2 1 634 . 156 LEU H H 7.52 0.01 1 635 . 156 LEU C C 176.6 0.2 1 636 . 156 LEU CA C 55.9 0.2 1 637 . 156 LEU CB C 42.9 0.2 1 638 . 156 LEU N N 123.8 0.2 1 639 . 157 VAL H H 8.39 0.01 1 640 . 157 VAL C C 175.7 0.2 1 641 . 157 VAL CA C 62.0 0.2 1 642 . 157 VAL CB C 33.9 0.2 1 643 . 157 VAL N N 128.1 0.2 1 644 . 158 VAL H H 8.69 0.01 1 645 . 158 VAL C C 175.1 0.2 1 646 . 158 VAL CA C 61.2 0.2 1 647 . 158 VAL CB C 32.2 0.2 1 648 . 158 VAL N N 131.1 0.2 1 649 . 159 PRO C C 177.5 0.2 1 650 . 159 PRO CA C 63.0 0.2 1 651 . 159 PRO CB C 32.5 0.2 1 652 . 160 GLU H H 8.51 0.01 1 653 . 160 GLU C C 175.0 0.2 1 654 . 160 GLU CA C 59.8 0.2 1 655 . 160 GLU CB C 30.6 0.2 1 656 . 160 GLU N N 117.6 0.2 1 657 . 161 ARG H H 7.41 0.01 1 658 . 161 ARG C C 175.4 0.2 1 659 . 161 ARG CA C 54.3 0.2 1 660 . 161 ARG CB C 32.9 0.2 1 661 . 161 ARG N N 111.9 0.2 1 662 . 162 LEU H H 9.00 0.01 1 663 . 162 LEU C C 173.4 0.2 1 664 . 162 LEU CA C 55.0 0.2 1 665 . 162 LEU CB C 45.2 0.2 1 666 . 162 LEU N N 120.0 0.2 1 667 . 163 LEU H H 9.01 0.01 1 668 . 163 LEU C C 175.0 0.2 1 669 . 163 LEU CA C 54.0 0.2 1 670 . 163 LEU CB C 44.8 0.2 1 671 . 163 LEU N N 123.9 0.2 1 672 . 164 VAL H H 9.27 0.01 1 673 . 164 VAL C C 174.4 0.2 1 674 . 164 VAL CA C 62.4 0.2 1 675 . 164 VAL CB C 31.4 0.2 1 676 . 164 VAL N N 128.5 0.2 1 677 . 165 VAL H H 8.18 0.01 1 678 . 165 VAL C C 174.0 0.2 1 679 . 165 VAL CA C 62.4 0.2 1 680 . 165 VAL CB C 32.5 0.2 1 681 . 165 VAL N N 123.6 0.2 1 682 . 166 LEU H H 8.98 0.01 1 683 . 166 LEU C C 173.3 0.2 1 684 . 166 LEU CA C 53.7 0.2 1 685 . 166 LEU CB C 44.6 0.2 1 686 . 166 LEU N N 133.1 0.2 1 687 . 167 ASP H H 8.96 0.01 1 688 . 167 ASP C C 177.9 0.2 1 689 . 167 ASP CA C 52.4 0.2 1 690 . 167 ASP CB C 41.3 0.2 1 691 . 167 ASP N N 127.0 0.2 1 692 . 168 MET H H 9.05 0.01 1 693 . 168 MET C C 177.2 0.2 1 694 . 168 MET CA C 54.1 0.2 1 695 . 168 MET N N 121.1 0.01 1 696 . 169 GLU H H 8.36 0.01 1 697 . 169 GLU C C 178.2 0.2 1 698 . 169 GLU CA C 57.9 0.2 1 699 . 169 GLU CB C 28.9 0.2 1 700 . 169 GLU N N 119.5 0.2 1 701 . 170 GLU H H 7.53 0.01 1 702 . 170 GLU C C 178.1 0.2 1 703 . 170 GLU CA C 55.9 0.2 1 704 . 170 GLU CB C 31.1 0.2 1 705 . 170 GLU N N 116.1 0.2 1 706 . 171 GLY H H 8.26 0.01 1 707 . 171 GLY C C 173.5 0.2 1 708 . 171 GLY CA C 47.9 0.2 1 709 . 171 GLY N N 110.2 0.2 1 710 . 172 THR H H 8.59 0.01 1 711 . 172 THR C C 172.3 0.2 1 712 . 172 THR CA C 59.2 0.2 1 713 . 172 THR CB C 73.2 0.2 1 714 . 172 THR N N 108.4 0.2 1 715 . 173 LEU H H 8.17 0.01 1 716 . 173 LEU C C 175.5 0.2 1 717 . 173 LEU CA C 52.9 0.2 1 718 . 173 LEU CB C 46.6 0.2 1 719 . 173 LEU N N 122.0 0.2 1 720 . 174 GLY H H 8.76 0.01 1 721 . 174 GLY C C 168.7 0.2 1 722 . 174 GLY CA C 44.8 0.2 1 723 . 174 GLY N N 115.1 0.2 1 724 . 175 TYR H H 6.81 0.01 1 725 . 175 TYR C C 173.9 0.2 1 726 . 175 TYR CA C 56.5 0.2 1 727 . 175 TYR CB C 43.0 0.2 1 728 . 175 TYR N N 114.7 0.2 1 729 . 176 SER H H 9.49 0.01 1 730 . 176 SER C C 173.9 0.2 1 731 . 176 SER CA C 56.4 0.2 1 732 . 176 SER CB C 65.6 0.2 1 733 . 176 SER N N 115.2 0.2 1 734 . 177 ILE H H 8.14 0.01 1 735 . 177 ILE C C 177.5 0.2 1 736 . 177 ILE CA C 59.9 0.2 1 737 . 177 ILE N N 121.2 0.2 1 738 . 178 GLY H H 9.31 0.01 1 739 . 178 GLY C C 175.3 0.2 1 740 . 178 GLY CA C 47.3 0.2 1 741 . 178 GLY N N 116.5 0.2 1 742 . 179 GLY H H 8.85 0.01 1 743 . 179 GLY C C 174.6 0.2 1 744 . 179 GLY CA C 45.0 0.2 1 745 . 179 GLY N N 107.4 0.2 1 746 . 180 THR H H 7.99 0.01 1 747 . 180 THR C C 172.9 0.2 1 748 . 180 THR CA C 62.0 0.2 1 749 . 180 THR CB C 70.4 0.2 1 750 . 180 THR N N 119.5 0.2 1 751 . 181 TYR H H 8.87 0.01 1 752 . 181 TYR C C 176.6 0.2 1 753 . 181 TYR CA C 58.5 0.2 1 754 . 181 TYR CB C 38.4 0.2 1 755 . 181 TYR N N 128.6 0.2 1 756 . 182 LEU H H 8.72 0.01 1 757 . 182 LEU C C 175.4 0.2 1 758 . 182 LEU CA C 55.6 0.2 1 759 . 182 LEU CB C 40.6 0.2 1 760 . 182 LEU N N 126.9 0.2 1 761 . 183 GLY H H 8.15 0.01 1 762 . 183 GLY CA C 45.9 0.2 1 763 . 183 GLY N N 120.7 0.2 1 764 . 184 PRO C C 175.8 0.2 1 765 . 184 PRO CA C 63.9 0.2 1 766 . 184 PRO CB C 30.9 0.2 1 767 . 185 ALA H H 9.43 0.01 1 768 . 185 ALA C C 176.0 0.2 1 769 . 185 ALA CA C 53.3 0.2 1 770 . 185 ALA CB C 20.1 0.2 1 771 . 185 ALA N N 131.0 0.2 1 772 . 186 PHE H H 7.67 0.01 1 773 . 186 PHE C C 174.3 0.2 1 774 . 186 PHE CA C 56.1 0.2 1 775 . 186 PHE CB C 43.9 0.2 1 776 . 186 PHE N N 111.0 0.2 1 777 . 187 ARG H H 8.69 0.01 1 778 . 187 ARG C C 176.0 0.2 1 779 . 187 ARG CA C 54.3 0.2 1 780 . 187 ARG CB C 33.4 0.2 1 781 . 187 ARG N N 119.8 0.2 1 782 . 188 GLY H H 8.70 0.01 1 783 . 188 GLY C C 177.8 0.2 1 784 . 188 GLY CA C 47.0 0.2 1 785 . 188 GLY N N 106.9 0.2 1 786 . 189 LEU H H 8.25 0.01 1 787 . 189 LEU C C 176.2 0.2 1 788 . 189 LEU CA C 55.3 0.2 1 789 . 189 LEU CB C 41.0 0.2 1 790 . 189 LEU N N 117.6 0.2 1 791 . 190 LYS H H 7.69 0.01 1 792 . 190 LYS C C 178.1 0.2 1 793 . 190 LYS CA C 59.3 0.2 1 794 . 190 LYS CB C 32.7 0.2 1 795 . 190 LYS N N 116.5 0.2 1 796 . 191 GLY H H 8.74 0.01 1 797 . 191 GLY C C 174.9 0.2 1 798 . 191 GLY CA C 45.6 0.2 1 799 . 191 GLY N N 111.6 0.2 1 800 . 192 ARG H H 7.10 0.01 1 801 . 192 ARG C C 174.9 0.2 1 802 . 192 ARG CA C 54.5 0.2 1 803 . 192 ARG CB C 32.5 0.2 1 804 . 192 ARG N N 117.9 0.2 1 805 . 193 THR H H 8.38 0.01 1 806 . 193 THR C C 174.3 0.2 1 807 . 193 THR CA C 63.1 0.2 1 808 . 193 THR CB C 70.1 0.2 1 809 . 193 THR N N 116.5 0.2 1 810 . 194 LEU H H 8.27 0.01 1 811 . 194 LEU C C 174.2 0.2 1 812 . 194 LEU CA C 53.4 0.2 1 813 . 194 LEU N N 126.4 0.2 1 814 . 195 TYR H H 9.18 0.01 1 815 . 195 TYR C C 175.2 0.2 1 816 . 195 TYR CA C 54.5 0.2 1 817 . 195 TYR N N 120.1 0.2 1 818 . 196 PRO C C 175.9 0.2 1 819 . 196 PRO CA C 64.1 0.2 1 820 . 196 PRO CB C 34.4 0.2 1 821 . 197 SER H H 8.48 0.01 1 822 . 197 SER C C 173.9 0.2 1 823 . 197 SER CA C 58.5 0.2 1 824 . 197 SER CB C 66.0 0.2 1 825 . 197 SER N N 115.1 0.2 1 826 . 198 VAL H H 7.49 0.01 1 827 . 198 VAL C C 175.0 0.2 1 828 . 198 VAL CA C 60.1 0.2 1 829 . 198 VAL CB C 37.1 0.2 1 830 . 198 VAL N N 120.1 0.2 1 831 . 199 SER H H 8.95 0.01 1 832 . 199 SER C C 172.1 0.2 1 833 . 199 SER CA C 59.1 0.2 1 834 . 199 SER CB C 66.3 0.2 1 835 . 199 SER N N 114.3 0.2 1 836 . 200 ALA H H 9.06 0.01 1 837 . 200 ALA C C 177.0 0.2 1 838 . 200 ALA CA C 51.5 0.2 1 839 . 200 ALA CB C 26.0 0.2 1 840 . 200 ALA N N 123.6 0.2 1 841 . 203 GLY C C 168.9 0.2 1 842 . 204 GLN H H 7.40 0.01 1 843 . 204 GLN C C 177.1 0.2 1 844 . 204 GLN CA C 52.5 0.2 1 845 . 204 GLN CB C 33.9 0.2 1 846 . 204 GLN N N 113.2 0.2 1 847 . 205 CYS H H 8.92 0.01 1 848 . 205 CYS C C 175.7 0.2 1 849 . 205 CYS CA C 55.0 0.2 1 850 . 205 CYS N N 125.5 0.2 1 851 . 206 GLN H H 8.26 0.01 1 852 . 206 GLN C C 175.1 0.2 1 853 . 206 GLN CA C 54.3 0.2 1 854 . 206 GLN CB C 29.7 0.2 1 855 . 206 GLN N N 122.3 0.2 1 856 . 207 VAL H H 6.91 0.01 1 857 . 207 VAL C C 177.0 0.2 1 858 . 207 VAL CA C 60.8 0.2 1 859 . 207 VAL CB C 31.9 0.2 1 860 . 207 VAL N N 122.5 0.2 1 861 . 208 ARG H H 8.94 0.01 1 862 . 208 ARG C C 175.6 0.2 1 863 . 208 ARG CA C 55.3 0.2 1 864 . 208 ARG CB C 32.2 0.2 1 865 . 208 ARG N N 127.4 0.2 1 866 . 209 ILE H H 8.56 0.01 1 867 . 209 ILE C C 174.2 0.2 1 868 . 209 ILE CA C 59.0 0.2 1 869 . 209 ILE CB C 40.9 0.2 1 870 . 209 ILE N N 119.0 0.2 1 871 . 210 ARG H H 9.17 0.01 1 872 . 210 ARG C C 175.2 0.2 1 873 . 210 ARG CA C 54.6 0.2 1 874 . 210 ARG CB C 32.8 0.2 1 875 . 210 ARG N N 130.2 0.2 1 876 . 211 TYR H H 9.28 0.01 1 877 . 211 TYR C C 175.0 0.2 1 878 . 211 TYR CA C 60.6 0.2 1 879 . 211 TYR CB C 39.9 0.2 1 880 . 211 TYR N N 131.3 0.2 1 881 . 212 MET H H 8.79 0.01 1 882 . 212 MET C C 175.5 0.2 1 883 . 212 MET CA C 53.5 0.2 1 884 . 212 MET CB C 31.9 0.2 1 885 . 212 MET N N 122.8 0.2 1 886 . 213 GLY H H 7.94 0.01 1 887 . 213 GLY C C 171.7 0.2 1 888 . 213 GLY CA C 46.7 0.2 1 889 . 213 GLY N N 106.1 0.2 1 890 . 214 GLU H H 8.26 0.01 1 891 . 214 GLU CA C 55.2 0.2 1 892 . 214 GLU N N 117.9 0.2 1 893 . 215 ARG H H 8.96 0.01 1 894 . 215 ARG C C 175.6 0.2 1 895 . 215 ARG CA C 56.6 0.2 1 896 . 215 ARG CB C 31.1 0.2 1 897 . 215 ARG N N 128.3 0.2 1 898 . 216 ARG H H 8.94 0.01 1 899 . 216 ARG C C 175.8 0.2 1 900 . 216 ARG CA C 56.0 0.2 1 901 . 216 ARG CB C 31.3 0.2 1 902 . 216 ARG N N 128.9 0.2 1 903 . 217 VAL H H 8.60 0.01 1 904 . 217 VAL C C 176.5 0.2 1 905 . 217 VAL CA C 63.0 0.2 1 906 . 217 VAL CB C 32.6 0.2 1 907 . 217 VAL N N 122.8 0.2 1 908 . 218 GLU H H 8.70 0.01 1 909 . 218 GLU C C 177.0 0.2 1 910 . 218 GLU CA C 57.2 0.2 1 911 . 218 GLU CB C 30.2 0.2 1 912 . 218 GLU N N 124.4 0.2 1 913 . 219 GLU H H 8.41 0.01 1 914 . 219 GLU C C 177.2 0.2 1 915 . 219 GLU CA C 57.3 0.2 1 916 . 219 GLU CB C 29.8 0.2 1 917 . 219 GLU N N 121.7 0.2 1 918 . 220 THR H H 8.09 0.01 1 919 . 220 THR C C 175.0 0.2 1 920 . 220 THR CA C 62.8 0.2 1 921 . 220 THR CB C 69.0 0.2 1 922 . 220 THR N N 114.6 0.2 1 923 . 221 ARG H H 8.27 0.01 1 924 . 221 ARG C C 176.3 0.2 1 925 . 221 ARG CA C 56.5 0.2 1 926 . 221 ARG CB C 30.8 0.2 1 927 . 221 ARG N N 123.1 0.2 1 928 . 222 ARG H H 8.27 0.01 1 929 . 222 ARG C C 176.1 0.2 1 930 . 222 ARG CA C 56.4 0.2 1 931 . 222 ARG CB C 30.9 0.2 1 932 . 222 ARG N N 122.5 0.2 1 933 . 223 ILE H H 8.14 0.01 1 934 . 223 ILE C C 176.1 0.2 1 935 . 223 ILE CA C 61.2 0.2 1 936 . 223 ILE CB C 38.7 0.2 1 937 . 223 ILE N N 122.3 0.2 1 938 . 224 HIS H H 8.44 0.01 1 939 . 224 HIS C C 175.0 0.2 1 940 . 224 HIS CA C 56.5 0.2 1 941 . 224 HIS CB C 30.9 0.2 1 942 . 224 HIS N N 124.4 0.2 1 943 . 225 ARG H H 8.28 0.01 1 944 . 225 ARG CA C 56.4 0.2 1 945 . 225 ARG N N 123.3 0.2 1 stop_ save_