data_6034 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N, 13C resonance assignments and 15N-1H residual dipolar couplings in 27 kDa alpha-adaptin ear-domain ; _BMRB_accession_number 6034 _BMRB_flat_file_name bmr6034.str _Entry_type original _Submission_date 2003-12-05 _Accession_date 2003-12-05 _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 Denisov Alexei Yu. . 2 Gehring Kalle . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 residual_dipolar_couplings 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 207 "13C chemical shifts" 655 "15N chemical shifts" 207 "residual dipolar couplings" 205 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-06-25 original author . stop_ _Original_release_date 2004-06-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 15N, 13C resonance assignments and 15N-1H residual dipolar couplings for the alpha-adaptin ear-domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15213459 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Denisov Alexei Yu. . 2 Ritter Brigitte . . 3 McPherson Peter S. . 4 Gehring Kalle . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 29 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 441 _Page_last 442 _Year 2004 _Details . loop_ _Keyword Alpha-adaptin endocytosis 'NMR assignments' 'residual dipolar couplings' stop_ save_ ################################## # Molecular system description # ################################## save_system_alpha-ear _Saveframe_category molecular_system _Mol_system_name 'ear-domain of alpha-adaptin C' _Abbreviation_common alpha-ear _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'alpha-ear monomer' $alpha-ear 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_alpha-ear _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ear-domain of alpha-adaptin C' _Abbreviation_common alpha-ear _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 238 _Mol_residue_sequence ; SEDNFARFVCKNNGVLFENQ LLQIGLKSEFRQNLGRMFIF YGNKTSTQFLNFTPTLICAD DLQTNLNLQTKPVDPTVDGG AQVQQVVNIECISDFTEAPV LNIQFRYGGTFQNVSVKLPI TLNKFFQPTEMASQDFFQRW KQLSNPQQEVQNIFKAKHPM DTEITKAKIIGFGSALLEEV DPNPANFVGAGIIHTKTTQI GCLLRLEPNLQAQMYRLTLR TSKDTVSQRLCELLSEQF ; loop_ _Residue_seq_code _Residue_label 1 SER 2 GLU 3 ASP 4 ASN 5 PHE 6 ALA 7 ARG 8 PHE 9 VAL 10 CYS 11 LYS 12 ASN 13 ASN 14 GLY 15 VAL 16 LEU 17 PHE 18 GLU 19 ASN 20 GLN 21 LEU 22 LEU 23 GLN 24 ILE 25 GLY 26 LEU 27 LYS 28 SER 29 GLU 30 PHE 31 ARG 32 GLN 33 ASN 34 LEU 35 GLY 36 ARG 37 MET 38 PHE 39 ILE 40 PHE 41 TYR 42 GLY 43 ASN 44 LYS 45 THR 46 SER 47 THR 48 GLN 49 PHE 50 LEU 51 ASN 52 PHE 53 THR 54 PRO 55 THR 56 LEU 57 ILE 58 CYS 59 ALA 60 ASP 61 ASP 62 LEU 63 GLN 64 THR 65 ASN 66 LEU 67 ASN 68 LEU 69 GLN 70 THR 71 LYS 72 PRO 73 VAL 74 ASP 75 PRO 76 THR 77 VAL 78 ASP 79 GLY 80 GLY 81 ALA 82 GLN 83 VAL 84 GLN 85 GLN 86 VAL 87 VAL 88 ASN 89 ILE 90 GLU 91 CYS 92 ILE 93 SER 94 ASP 95 PHE 96 THR 97 GLU 98 ALA 99 PRO 100 VAL 101 LEU 102 ASN 103 ILE 104 GLN 105 PHE 106 ARG 107 TYR 108 GLY 109 GLY 110 THR 111 PHE 112 GLN 113 ASN 114 VAL 115 SER 116 VAL 117 LYS 118 LEU 119 PRO 120 ILE 121 THR 122 LEU 123 ASN 124 LYS 125 PHE 126 PHE 127 GLN 128 PRO 129 THR 130 GLU 131 MET 132 ALA 133 SER 134 GLN 135 ASP 136 PHE 137 PHE 138 GLN 139 ARG 140 TRP 141 LYS 142 GLN 143 LEU 144 SER 145 ASN 146 PRO 147 GLN 148 GLN 149 GLU 150 VAL 151 GLN 152 ASN 153 ILE 154 PHE 155 LYS 156 ALA 157 LYS 158 HIS 159 PRO 160 MET 161 ASP 162 THR 163 GLU 164 ILE 165 THR 166 LYS 167 ALA 168 LYS 169 ILE 170 ILE 171 GLY 172 PHE 173 GLY 174 SER 175 ALA 176 LEU 177 LEU 178 GLU 179 GLU 180 VAL 181 ASP 182 PRO 183 ASN 184 PRO 185 ALA 186 ASN 187 PHE 188 VAL 189 GLY 190 ALA 191 GLY 192 ILE 193 ILE 194 HIS 195 THR 196 LYS 197 THR 198 THR 199 GLN 200 ILE 201 GLY 202 CYS 203 LEU 204 LEU 205 ARG 206 LEU 207 GLU 208 PRO 209 ASN 210 LEU 211 GLN 212 ALA 213 GLN 214 MET 215 TYR 216 ARG 217 LEU 218 THR 219 LEU 220 ARG 221 THR 222 SER 223 LYS 224 ASP 225 THR 226 VAL 227 SER 228 GLN 229 ARG 230 LEU 231 CYS 232 GLU 233 LEU 234 LEU 235 SER 236 GLU 237 GLN 238 PHE 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 1B9K "Alpha-Adaptin Appendage Domain, From Clathrin Adaptor Ap2" 100.00 238 99.58 100.00 1.80e-172 PDB 1KY6 "Ap-2 Clathrin Adaptor Alpha-Appendage In Complex With Epsin Dpw Peptide" 100.00 247 100.00 100.00 2.09e-172 PDB 1KY7 "The Ap-2 Clathrin Adaptor Alpha-Appendage In Complex With Amphiphysin Fxdxf" 100.00 247 100.00 100.00 2.09e-172 PDB 1KYD "Ap-2 Clathrin Adaptor Alpha-Appendage In Complex With Epsin Dpw Peptide" 100.00 247 100.00 100.00 2.09e-172 PDB 1KYF "Ap-2 Clathrin Adaptor Alpha-Appendage In Complex With Eps15 Dpf Peptide" 100.00 247 100.00 100.00 2.09e-172 PDB 1KYU "Ap-2 Clathrin Adaptor Alpha-Appendage In Complex With Eps15 Dpf Peptide" 100.00 247 100.00 100.00 2.09e-172 PDB 1QTP "Crystal Structure Of The Ap-2 Clathrin Adaptor Alpha- Appendage" 100.00 247 98.32 98.32 3.54e-168 PDB 1QTS "Crystal Structure Of The Ap-2 Clathrin Adaptor Alpha- Appendage" 100.00 247 100.00 100.00 2.09e-172 PDB 1W80 "Crystal Structure Of The Alpha-adaptin Appendage Domain, From The Ap2 Adaptor Complex, Bound To 2 Peptides From Synaptojanin170" 100.00 250 99.58 100.00 6.09e-172 PDB 2VJ0 "Crystal Structure Of The Alpha-Adaptin Appendage Domain, From The Ap2 Adaptor Complex, In Complex With An Fxdnf Peptide From Am" 100.00 250 99.58 100.00 6.09e-172 PDB 3HS8 "Intersectin 1-Peptide-Ap2 Alpha Ear Complex" 99.58 273 100.00 100.00 1.48e-172 DBJ BAC40392 "unnamed protein product [Mus musculus]" 100.00 938 100.00 100.00 1.20e-166 DBJ BAD32332 "mKIAA0899 protein [Mus musculus]" 100.00 967 100.00 100.00 1.75e-166 DBJ BAE31240 "unnamed protein product [Mus musculus]" 100.00 938 99.58 100.00 4.13e-166 EMBL CAA33097 "unnamed protein product [Mus musculus]" 100.00 938 99.16 99.16 2.68e-164 EMBL CAA37791 "unnamed protein product [Rattus norvegicus]" 100.00 938 99.58 100.00 1.73e-166 GB AAB62703 "alpha-adaptin C, partial [Mus musculus]" 100.00 560 99.16 99.16 2.20e-168 GB AAH10597 "Ap2a2 protein, partial [Mus musculus]" 65.97 756 100.00 100.00 3.23e-104 GB AAH58099 "Adaptor protein complex AP-2, alpha 2 subunit [Mus musculus]" 100.00 938 100.00 100.00 1.20e-166 GB AAH81786 "Adaptor-related protein complex 2, alpha 2 subunit [Rattus norvegicus]" 100.00 939 100.00 100.00 1.11e-166 GB EDL18116 "adaptor protein complex AP-2, alpha 2 subunit, isoform CRA_a [Mus musculus]" 100.00 915 100.00 100.00 5.55e-167 REF NP_031485 "AP-2 complex subunit alpha-2 [Mus musculus]" 100.00 938 100.00 100.00 1.20e-166 REF NP_112270 "AP-2 complex subunit alpha-2 [Rattus norvegicus]" 100.00 939 100.00 100.00 1.11e-166 REF XP_003461349 "PREDICTED: AP-2 complex subunit alpha-2 isoform X1 [Cavia porcellus]" 100.00 938 98.32 99.16 1.45e-164 REF XP_003509821 "PREDICTED: AP-2 complex subunit alpha-2 isoform X1 [Cricetulus griseus]" 100.00 939 99.16 99.58 7.35e-166 REF XP_003802841 "PREDICTED: AP-2 complex subunit alpha-2 [Otolemur garnettii]" 100.00 1110 97.06 99.16 1.05e-160 SP P17427 "RecName: Full=AP-2 complex subunit alpha-2; AltName: Full=100 kDa coated vesicle protein C; AltName: Full=Adaptor protein compl" 100.00 938 100.00 100.00 1.20e-166 SP P18484 "RecName: Full=AP-2 complex subunit alpha-2; AltName: Full=100 kDa coated vesicle protein C; AltName: Full=Adaptor protein compl" 100.00 938 99.58 100.00 1.73e-166 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $alpha-ear 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 _Vector_type _Vector_name $alpha-ear 'recombinant technology' 'E. coli' Escherichia coli BL21 plasmid pGET-2TK 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 $alpha-ear 1.0 mM '[U-99% 13C; U-99% 15N]' 'sodium phosphate buffer' 25 mM . NaCl 75 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $alpha-ear 1.0 mM '[U-99% 15N]' 'sodium phosphate buffer' 25 mM . NaCl 75 mM . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $alpha-ear 0.3 mM '[U-99% 15N]' 'sodium phosphate buffer' 25 mM . NaCl 75 mM . 'Pf1 phage' 2.5 mg/mL . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 3.1 loop_ _Task collection processing stop_ _Details 'Bruker firm' save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.13 loop_ _Task 'data analysis' stop_ _Details 'Bartels et al.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details 'Cryoprobe was employed' save_ ############################# # NMR applied experiments # ############################# save_3D_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label . save_ save_3D_CBCA(CO)HN_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)HN' _Sample_label . save_ save_3D_TROSY-HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCA' _Sample_label . save_ save_3D_TROSY-HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HN(CO)CA' _Sample_label . save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label . save_ save_3D_15N-HSQC-NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-HSQC-NOESY' _Sample_label . save_ save_2D_IPAP_15N-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D IPAP 15N-HSQC' _Sample_label . 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' 0.10 . M pH 7.3 0.1 n/a temperature 303 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'alpha-ear monomer' _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 GLU CB C 30.3 0.20 1 2 . 2 GLU CA C 56.4 0.20 1 3 . 2 GLU C C 175.7 0.20 1 4 . 3 ASP N N 120.5 0.25 1 5 . 3 ASP H H 8.25 0.01 1 6 . 3 ASP CB C 41.9 0.20 1 7 . 3 ASP CA C 54.2 0.20 1 8 . 3 ASP C C 176.8 0.20 1 9 . 4 ASN N N 118.5 0.25 1 10 . 4 ASN H H 8.85 0.01 1 11 . 4 ASN CB C 39.3 0.20 1 12 . 4 ASN CA C 53.5 0.20 1 13 . 4 ASN C C 173.9 0.20 1 14 . 5 PHE N N 122.5 0.25 1 15 . 5 PHE H H 8.55 0.01 1 16 . 5 PHE CB C 39.3 0.20 1 17 . 5 PHE CA C 62.7 0.20 1 18 . 5 PHE C C 176.8 0.20 1 19 . 6 ALA N N 117.6 0.25 1 20 . 6 ALA H H 8.64 0.01 1 21 . 6 ALA CB C 17.8 0.20 1 22 . 6 ALA CA C 54.2 0.20 1 23 . 6 ALA C C 180.1 0.20 1 24 . 7 ARG N N 115.6 0.25 1 25 . 7 ARG H H 7.94 0.01 1 26 . 7 ARG CB C 29.2 0.20 1 27 . 7 ARG CA C 57.5 0.20 1 28 . 7 ARG C C 177.4 0.20 1 29 . 8 PHE N N 115.6 0.25 1 30 . 8 PHE H H 7.73 0.01 1 31 . 8 PHE CB C 40.2 0.20 1 32 . 8 PHE CA C 58.3 0.20 1 33 . 8 PHE C C 175.3 0.20 1 34 . 9 VAL N N 122.4 0.25 1 35 . 9 VAL H H 7.31 0.01 1 36 . 9 VAL CB C 31.8 0.20 1 37 . 9 VAL CA C 67.1 0.20 1 38 . 10 CYS CB C 32.5 0.20 1 39 . 10 CYS CA C 62.9 0.20 1 40 . 10 CYS C C 176.6 0.20 1 41 . 11 LYS N N 115.6 0.25 1 42 . 11 LYS H H 7.85 0.01 1 43 . 11 LYS CB C 34.2 0.20 1 44 . 11 LYS CA C 59.2 0.20 1 45 . 11 LYS C C 175.7 0.20 1 46 . 12 ASN N N 127.2 0.25 1 47 . 12 ASN H H 8.55 0.01 1 48 . 12 ASN CB C 40.9 0.20 1 49 . 12 ASN CA C 52.7 0.20 1 50 . 12 ASN C C 175.1 0.20 1 51 . 13 ASN N N 114.9 0.25 1 52 . 13 ASN H H 7.47 0.01 1 53 . 13 ASN CB C 41.7 0.20 1 54 . 13 ASN CA C 51.8 0.20 1 55 . 13 ASN C C 174.2 0.20 1 56 . 14 GLY N N 107.8 0.25 1 57 . 14 GLY H H 8.69 0.01 1 58 . 14 GLY CA C 44.5 0.20 1 59 . 15 VAL CB C 30.9 0.20 1 60 . 15 VAL CA C 63.6 0.20 1 61 . 15 VAL C C 174.1 0.20 1 62 . 16 LEU N N 130.8 0.25 1 63 . 16 LEU H H 9.10 0.01 1 64 . 16 LEU CB C 44.0 0.20 1 65 . 16 LEU CA C 56.0 0.20 1 66 . 16 LEU C C 175.2 0.20 1 67 . 17 PHE N N 117.9 0.25 1 68 . 17 PHE H H 7.84 0.01 1 69 . 17 PHE CB C 43.7 0.20 1 70 . 17 PHE CA C 56.3 0.20 1 71 . 17 PHE C C 172.3 0.20 1 72 . 18 GLU N N 127.8 0.25 1 73 . 18 GLU H H 7.96 0.01 1 74 . 18 GLU CB C 32.1 0.20 1 75 . 18 GLU CA C 55.7 0.20 1 76 . 18 GLU C C 173.7 0.20 1 77 . 19 ASN N N 125.5 0.25 1 78 . 19 ASN H H 8.65 0.01 1 79 . 19 ASN CB C 38.4 0.20 1 80 . 19 ASN CA C 50.9 0.20 1 81 . 20 GLN CB C 28.3 0.20 1 82 . 20 GLN CA C 58.6 0.20 1 83 . 20 GLN C C 175.5 0.20 1 84 . 21 LEU N N 114.0 0.25 1 85 . 21 LEU H H 7.66 0.01 1 86 . 21 LEU CB C 43.3 0.20 1 87 . 21 LEU CA C 55.4 0.20 1 88 . 21 LEU C C 175.6 0.20 1 89 . 22 LEU N N 119.1 0.25 1 90 . 22 LEU H H 8.19 0.01 1 91 . 22 LEU CB C 47.1 0.20 1 92 . 22 LEU CA C 53.3 0.20 1 93 . 22 LEU C C 173.9 0.20 1 94 . 23 GLN N N 122.7 0.25 1 95 . 23 GLN H H 8.94 0.01 1 96 . 23 GLN CB C 33.5 0.20 1 97 . 23 GLN CA C 54.3 0.20 1 98 . 23 GLN C C 174.7 0.20 1 99 . 24 ILE N N 126.2 0.25 1 100 . 24 ILE H H 9.70 0.01 1 101 . 24 ILE CB C 39.2 0.20 1 102 . 24 ILE CA C 60.3 0.20 1 103 . 24 ILE C C 175.6 0.20 1 104 . 25 GLY N N 116.8 0.25 1 105 . 25 GLY H H 9.59 0.01 1 106 . 25 GLY CA C 43.5 0.20 1 107 . 25 GLY C C 171.6 0.20 1 108 . 26 LEU N N 119.0 0.25 1 109 . 26 LEU H H 8.96 0.01 1 110 . 26 LEU CB C 47.9 0.20 1 111 . 26 LEU CA C 53.7 0.20 1 112 . 26 LEU C C 178.0 0.20 1 113 . 27 LYS N N 122.9 0.25 1 114 . 27 LYS H H 8.98 0.01 1 115 . 27 LYS CB C 36.8 0.20 1 116 . 27 LYS CA C 56.3 0.20 1 117 . 27 LYS C C 175.4 0.20 1 118 . 28 SER N N 116.6 0.25 1 119 . 28 SER H H 8.36 0.01 1 120 . 28 SER CA C 57.4 0.20 1 121 . 28 SER CB C 66.7 0.20 1 122 . 28 SER C C 172.1 0.20 1 123 . 29 GLU N N 118.9 0.25 1 124 . 29 GLU H H 8.15 0.01 1 125 . 29 GLU CB C 32.9 0.20 1 126 . 29 GLU CA C 54.6 0.20 1 127 . 29 GLU C C 173.3 0.20 1 128 . 30 PHE N N 121.0 0.25 1 129 . 30 PHE H H 8.78 0.01 1 130 . 30 PHE CB C 43.9 0.20 1 131 . 30 PHE CA C 57.1 0.20 1 132 . 30 PHE C C 175.4 0.20 1 133 . 31 ARG N N 121.8 0.25 1 134 . 31 ARG H H 9.13 0.01 1 135 . 31 ARG CB C 32.0 0.20 1 136 . 31 ARG CA C 56.1 0.20 1 137 . 31 ARG C C 174.9 0.20 1 138 . 32 GLN N N 123.3 0.25 1 139 . 32 GLN H H 9.07 0.01 1 140 . 32 GLN CB C 34.1 0.20 1 141 . 32 GLN CA C 58.1 0.20 1 142 . 32 GLN C C 173.8 0.20 1 143 . 33 ASN N N 117.2 0.25 1 144 . 33 ASN H H 8.15 0.01 1 145 . 33 ASN CB C 38.8 0.20 1 146 . 33 ASN CA C 54.2 0.20 1 147 . 33 ASN C C 172.2 0.20 1 148 . 34 LEU N N 120.9 0.25 1 149 . 34 LEU H H 8.54 0.01 1 150 . 34 LEU CB C 45.5 0.20 1 151 . 34 LEU CA C 53.4 0.20 1 152 . 34 LEU C C 176.6 0.20 1 153 . 35 GLY N N 103.9 0.25 1 154 . 35 GLY H H 8.82 0.01 1 155 . 35 GLY CA C 45.9 0.20 1 156 . 35 GLY C C 172.0 0.20 1 157 . 36 ARG N N 120.6 0.25 1 158 . 36 ARG H H 8.52 0.01 1 159 . 36 ARG CB C 33.2 0.20 1 160 . 36 ARG CA C 55.4 0.20 1 161 . 36 ARG C C 173.1 0.20 1 162 . 37 MET N N 124.6 0.25 1 163 . 37 MET H H 8.90 0.01 1 164 . 37 MET CB C 37.4 0.20 1 165 . 37 MET CA C 53.7 0.20 1 166 . 37 MET C C 172.6 0.20 1 167 . 38 PHE N N 126.4 0.25 1 168 . 38 PHE H H 9.47 0.01 1 169 . 38 PHE CB C 40.1 0.20 1 170 . 38 PHE CA C 55.9 0.20 1 171 . 38 PHE C C 173.4 0.20 1 172 . 39 ILE N N 122.9 0.25 1 173 . 39 ILE H H 8.89 0.01 1 174 . 39 ILE CB C 39.3 0.20 1 175 . 39 ILE CA C 60.0 0.20 1 176 . 39 ILE C C 174.2 0.20 1 177 . 40 PHE N N 123.8 0.25 1 178 . 40 PHE H H 8.96 0.01 1 179 . 40 PHE CB C 40.4 0.20 1 180 . 40 PHE CA C 55.3 0.20 1 181 . 40 PHE C C 175.2 0.20 1 182 . 41 TYR N N 123.7 0.25 1 183 . 41 TYR H H 9.33 0.01 1 184 . 41 TYR CB C 38.5 0.20 1 185 . 41 TYR CA C 56.2 0.20 1 186 . 41 TYR C C 174.5 0.20 1 187 . 42 GLY N N 111.0 0.25 1 188 . 42 GLY H H 9.59 0.01 1 189 . 42 GLY CA C 44.4 0.20 1 190 . 42 GLY C C 172.2 0.20 1 191 . 43 ASN N N 122.5 0.25 1 192 . 43 ASN H H 8.24 0.01 1 193 . 43 ASN CB C 39.3 0.20 1 194 . 43 ASN CA C 51.8 0.20 1 195 . 44 LYS CB C 31.4 0.20 1 196 . 44 LYS C C 176.6 0.20 1 197 . 45 THR N N 112.9 0.25 1 198 . 45 THR H H 8.91 0.01 1 199 . 45 THR CA C 60.5 0.20 1 200 . 45 THR CB C 67.2 0.20 1 201 . 46 SER CA C 57.2 0.20 1 202 . 46 SER CB C 63.8 0.20 1 203 . 46 SER C C 174.5 0.20 1 204 . 47 THR N N 121.3 0.25 1 205 . 47 THR H H 9.02 0.01 1 206 . 47 THR CA C 61.4 0.20 1 207 . 47 THR CB C 71.2 0.20 1 208 . 47 THR C C 172.0 0.20 1 209 . 48 GLN N N 120.8 0.25 1 210 . 48 GLN H H 8.31 0.01 1 211 . 48 GLN CB C 29.9 0.20 1 212 . 48 GLN CA C 56.3 0.20 1 213 . 48 GLN C C 176.5 0.20 1 214 . 49 PHE N N 120.2 0.25 1 215 . 49 PHE H H 8.62 0.01 1 216 . 49 PHE CB C 38.0 0.20 1 217 . 49 PHE CA C 52.3 0.20 1 218 . 49 PHE C C 172.9 0.20 1 219 . 50 LEU N N 121.0 0.25 1 220 . 50 LEU H H 8.69 0.01 1 221 . 50 LEU CB C 44.5 0.20 1 222 . 50 LEU CA C 52.4 0.20 1 223 . 50 LEU C C 176.7 0.20 1 224 . 51 ASN N N 118.0 0.25 1 225 . 51 ASN H H 9.52 0.01 1 226 . 51 ASN CB C 37.9 0.20 1 227 . 51 ASN CA C 54.3 0.20 1 228 . 51 ASN C C 175.7 0.20 1 229 . 52 PHE N N 124.0 0.25 1 230 . 52 PHE H H 10.46 0.01 1 231 . 52 PHE CB C 39.4 0.20 1 232 . 52 PHE CA C 60.3 0.20 1 233 . 52 PHE C C 175.3 0.20 1 234 . 53 THR N N 123.4 0.25 1 235 . 53 THR H H 8.91 0.01 1 236 . 53 THR CA C 60.1 0.20 1 237 . 53 THR CB C 71.0 0.20 1 238 . 54 PRO CB C 32.2 0.20 1 239 . 54 PRO CA C 60.1 0.20 1 240 . 54 PRO C C 177.2 0.20 1 241 . 55 THR N N 121.0 0.25 1 242 . 55 THR H H 9.75 0.01 1 243 . 55 THR CA C 61.1 0.20 1 244 . 55 THR CB C 71.7 0.20 1 245 . 55 THR C C 172.1 0.20 1 246 . 56 LEU N N 124.9 0.25 1 247 . 56 LEU H H 8.44 0.01 1 248 . 56 LEU CB C 42.3 0.20 1 249 . 56 LEU CA C 53.5 0.20 1 250 . 56 LEU C C 176.0 0.20 1 251 . 57 ILE N N 126.3 0.25 1 252 . 57 ILE H H 9.65 0.01 1 253 . 57 ILE CB C 38.9 0.20 1 254 . 57 ILE CA C 60.4 0.20 1 255 . 58 CYS CB C 29.6 0.20 1 256 . 58 CYS CA C 56.7 0.20 1 257 . 58 CYS C C 173.2 0.20 1 258 . 59 ALA N N 126.6 0.25 1 259 . 59 ALA H H 8.42 0.01 1 260 . 59 ALA CB C 19.4 0.20 1 261 . 59 ALA CA C 51.8 0.20 1 262 . 59 ALA C C 175.3 0.20 1 263 . 60 ASP N N 120.7 0.25 1 264 . 60 ASP H H 8.71 0.01 1 265 . 60 ASP CB C 39.9 0.20 1 266 . 60 ASP CA C 57.1 0.20 1 267 . 60 ASP C C 177.5 0.20 1 268 . 61 ASP N N 117.3 0.25 1 269 . 61 ASP H H 8.60 0.01 1 270 . 61 ASP CB C 40.1 0.20 1 271 . 61 ASP CA C 55.7 0.20 1 272 . 61 ASP C C 177.6 0.20 1 273 . 62 LEU N N 120.6 0.25 1 274 . 62 LEU H H 7.54 0.01 1 275 . 62 LEU CB C 41.9 0.20 1 276 . 62 LEU CA C 56.8 0.20 1 277 . 62 LEU C C 177.9 0.20 1 278 . 63 GLN N N 116.2 0.25 1 279 . 63 GLN H H 7.91 0.01 1 280 . 63 GLN CB C 28.1 0.20 1 281 . 63 GLN CA C 57.5 0.20 1 282 . 63 GLN C C 176.7 0.20 1 283 . 64 THR N N 109.2 0.25 1 284 . 64 THR H H 7.42 0.01 1 285 . 64 THR CA C 63.8 0.20 1 286 . 64 THR CB C 69.3 0.20 1 287 . 64 THR C C 174.7 0.20 1 288 . 65 ASN N N 116.7 0.25 1 289 . 65 ASN H H 7.34 0.01 1 290 . 65 ASN CB C 40.8 0.20 1 291 . 65 ASN CA C 54.2 0.20 1 292 . 65 ASN C C 173.8 0.20 1 293 . 66 LEU N N 124.0 0.25 1 294 . 66 LEU H H 8.10 0.01 1 295 . 66 LEU CB C 44.6 0.20 1 296 . 66 LEU CA C 53.9 0.20 1 297 . 66 LEU C C 173.4 0.20 1 298 . 67 ASN N N 122.7 0.25 1 299 . 67 ASN H H 8.76 0.01 1 300 . 67 ASN CB C 40.2 0.20 1 301 . 67 ASN CA C 52.1 0.20 1 302 . 67 ASN C C 174.2 0.20 1 303 . 68 LEU N N 125.5 0.25 1 304 . 68 LEU H H 8.42 0.01 1 305 . 68 LEU CB C 43.5 0.20 1 306 . 68 LEU CA C 53.0 0.20 1 307 . 68 LEU C C 175.6 0.20 1 308 . 69 GLN N N 121.2 0.25 1 309 . 69 GLN H H 8.62 0.01 1 310 . 69 GLN CB C 32.0 0.20 1 311 . 69 GLN CA C 54.3 0.20 1 312 . 70 THR CA C 59.6 0.20 1 313 . 70 THR CB C 70.5 0.20 1 314 . 70 THR C C 171.7 0.20 1 315 . 71 LYS N N 123.6 0.25 1 316 . 71 LYS H H 8.26 0.01 1 317 . 71 LYS CB C 33.9 0.20 1 318 . 71 LYS CA C 53.2 0.20 1 319 . 73 VAL CB C 27.7 0.20 1 320 . 73 VAL CA C 57.8 0.20 1 321 . 73 VAL C C 172.6 0.20 1 322 . 74 ASP N N 115.7 0.25 1 323 . 74 ASP H H 6.79 0.01 1 324 . 74 ASP CB C 35.2 0.20 1 325 . 74 ASP CA C 55.1 0.20 1 326 . 75 PRO CB C 32.4 0.20 1 327 . 75 PRO CA C 63.2 0.20 1 328 . 75 PRO C C 176.4 0.20 1 329 . 76 THR N N 115.9 0.25 1 330 . 76 THR H H 7.76 0.01 1 331 . 76 THR CA C 61.0 0.20 1 332 . 76 THR CB C 69.5 0.20 1 333 . 76 THR C C 174.2 0.20 1 334 . 77 VAL N N 126.4 0.25 1 335 . 77 VAL H H 8.63 0.01 1 336 . 77 VAL CB C 32.3 0.20 1 337 . 77 VAL CA C 60.1 0.20 1 338 . 77 VAL C C 175.9 0.20 1 339 . 78 ASP N N 129.5 0.25 1 340 . 78 ASP H H 8.92 0.01 1 341 . 78 ASP CB C 40.6 0.20 1 342 . 78 ASP CA C 55.3 0.20 1 343 . 78 ASP C C 175.7 0.20 1 344 . 79 GLY N N 107.4 0.25 1 345 . 79 GLY H H 8.32 0.01 1 346 . 79 GLY CA C 46.9 0.20 1 347 . 79 GLY C C 175.9 0.20 1 348 . 80 GLY N N 115.0 0.25 1 349 . 80 GLY H H 7.49 0.01 1 350 . 80 GLY CA C 45.9 0.20 1 351 . 80 GLY C C 173.1 0.20 1 352 . 81 ALA N N 122.4 0.25 1 353 . 81 ALA H H 7.70 0.01 1 354 . 81 ALA CB C 21.2 0.20 1 355 . 81 ALA CA C 51.2 0.20 1 356 . 81 ALA C C 175.3 0.20 1 357 . 82 GLN N N 116.1 0.25 1 358 . 82 GLN H H 7.99 0.01 1 359 . 82 GLN CB C 32.3 0.20 1 360 . 82 GLN CA C 53.7 0.20 1 361 . 82 GLN C C 176.0 0.20 1 362 . 83 VAL N N 122.0 0.25 1 363 . 83 VAL H H 8.84 0.01 1 364 . 83 VAL CB C 34.7 0.20 1 365 . 83 VAL CA C 60.2 0.20 1 366 . 83 VAL C C 173.9 0.20 1 367 . 84 GLN N N 122.8 0.25 1 368 . 84 GLN H H 8.56 0.01 1 369 . 84 GLN CB C 32.4 0.20 1 370 . 84 GLN CA C 53.7 0.20 1 371 . 84 GLN C C 174.0 0.20 1 372 . 85 GLN N N 126.6 0.25 1 373 . 85 GLN H H 9.40 0.01 1 374 . 85 GLN CB C 32.9 0.20 1 375 . 85 GLN CA C 53.8 0.20 1 376 . 85 GLN C C 173.6 0.20 1 377 . 86 VAL N N 125.0 0.25 1 378 . 86 VAL H H 8.54 0.01 1 379 . 86 VAL CB C 32.9 0.20 1 380 . 86 VAL CA C 61.1 0.20 1 381 . 86 VAL C C 175.8 0.20 1 382 . 87 VAL N N 130.5 0.25 1 383 . 87 VAL H H 9.40 0.01 1 384 . 87 VAL CB C 33.4 0.20 1 385 . 87 VAL CA C 60.4 0.20 1 386 . 87 VAL C C 174.4 0.20 1 387 . 88 ASN N N 126.4 0.25 1 388 . 88 ASN H H 9.26 0.01 1 389 . 88 ASN CB C 40.0 0.20 1 390 . 88 ASN CA C 53.3 0.20 1 391 . 88 ASN C C 174.6 0.20 1 392 . 89 ILE N N 122.9 0.25 1 393 . 89 ILE H H 8.66 0.01 1 394 . 89 ILE CB C 42.1 0.20 1 395 . 89 ILE CA C 60.8 0.20 1 396 . 89 ILE C C 174.7 0.20 1 397 . 90 GLU N N 127.8 0.25 1 398 . 90 GLU H H 8.79 0.01 1 399 . 90 GLU CB C 32.7 0.20 1 400 . 90 GLU CA C 55.1 0.20 1 401 . 90 GLU C C 174.1 0.20 1 402 . 91 CYS N N 127.3 0.25 1 403 . 91 CYS H H 9.26 0.01 1 404 . 91 CYS CB C 24.5 0.20 1 405 . 91 CYS CA C 58.8 0.20 1 406 . 91 CYS C C 174.6 0.20 1 407 . 92 ILE N N 134.1 0.25 1 408 . 92 ILE H H 8.86 0.01 1 409 . 92 ILE CB C 37.5 0.20 1 410 . 92 ILE CA C 62.4 0.20 1 411 . 92 ILE C C 176.3 0.20 1 412 . 93 SER N N 113.4 0.25 1 413 . 93 SER H H 8.42 0.01 1 414 . 93 SER CA C 55.7 0.20 1 415 . 93 SER CB C 63.9 0.20 1 416 . 93 SER C C 171.9 0.20 1 417 . 94 ASP N N 114.7 0.25 1 418 . 94 ASP H H 8.53 0.01 1 419 . 94 ASP CB C 41.3 0.20 1 420 . 94 ASP CA C 54.9 0.20 1 421 . 94 ASP C C 172.4 0.20 1 422 . 95 PHE N N 110.8 0.25 1 423 . 95 PHE H H 5.89 0.01 1 424 . 95 PHE CB C 41.7 0.20 1 425 . 95 PHE CA C 57.1 0.20 1 426 . 96 THR CA C 62.9 0.20 1 427 . 96 THR CB C 70.2 0.20 1 428 . 96 THR C C 173.8 0.20 1 429 . 97 GLU N N 121.5 0.25 1 430 . 97 GLU H H 8.01 0.01 1 431 . 97 GLU CB C 30.9 0.20 1 432 . 97 GLU CA C 56.2 0.20 1 433 . 97 GLU C C 174.6 0.20 1 434 . 98 ALA N N 121.8 0.25 1 435 . 98 ALA H H 8.38 0.01 1 436 . 98 ALA CB C 19.5 0.20 1 437 . 98 ALA CA C 48.7 0.20 1 438 . 99 PRO CB C 32.0 0.20 1 439 . 99 PRO CA C 61.4 0.20 1 440 . 99 PRO C C 173.6 0.20 1 441 . 100 VAL N N 120.1 0.25 1 442 . 100 VAL H H 8.40 0.01 1 443 . 100 VAL CB C 34.8 0.20 1 444 . 100 VAL CA C 61.4 0.20 1 445 . 100 VAL C C 173.5 0.20 1 446 . 101 LEU N N 128.5 0.25 1 447 . 101 LEU H H 9.08 0.01 1 448 . 101 LEU CB C 44.2 0.20 1 449 . 101 LEU CA C 52.8 0.20 1 450 . 101 LEU C C 173.4 0.20 1 451 . 102 ASN N N 126.1 0.25 1 452 . 102 ASN H H 9.12 0.01 1 453 . 102 ASN CB C 42.3 0.20 1 454 . 102 ASN CA C 51.5 0.20 1 455 . 102 ASN C C 173.5 0.20 1 456 . 103 ILE N N 124.7 0.25 1 457 . 103 ILE H H 9.45 0.01 1 458 . 103 ILE CB C 40.6 0.20 1 459 . 103 ILE CA C 59.8 0.20 1 460 . 103 ILE C C 173.8 0.20 1 461 . 104 GLN N N 124.2 0.25 1 462 . 104 GLN H H 7.06 0.01 1 463 . 104 GLN CB C 32.0 0.20 1 464 . 104 GLN CA C 53.5 0.20 1 465 . 104 GLN C C 174.4 0.20 1 466 . 105 PHE N N 114.1 0.25 1 467 . 105 PHE H H 7.94 0.01 1 468 . 105 PHE CB C 40.2 0.20 1 469 . 105 PHE CA C 56.0 0.20 1 470 . 105 PHE C C 171.9 0.20 1 471 . 106 ARG N N 118.3 0.25 1 472 . 106 ARG H H 9.43 0.01 1 473 . 106 ARG CB C 32.0 0.20 1 474 . 106 ARG CA C 54.3 0.20 1 475 . 106 ARG C C 175.6 0.20 1 476 . 107 TYR N N 123.4 0.25 1 477 . 107 TYR H H 8.32 0.01 1 478 . 107 TYR CB C 41.2 0.20 1 479 . 107 TYR CA C 55.8 0.20 1 480 . 109 GLY N N 110.7 0.25 1 481 . 109 GLY H H 8.20 0.01 1 482 . 109 GLY CA C 44.9 0.20 1 483 . 109 GLY C C 174.2 0.20 1 484 . 110 THR N N 112.5 0.25 1 485 . 110 THR H H 7.81 0.01 1 486 . 110 THR CA C 60.5 0.20 1 487 . 110 THR CB C 71.4 0.20 1 488 . 110 THR C C 173.4 0.20 1 489 . 111 PHE N N 123.4 0.25 1 490 . 111 PHE H H 8.84 0.01 1 491 . 111 PHE CB C 39.7 0.20 1 492 . 111 PHE CA C 57.9 0.20 1 493 . 111 PHE C C 174.6 0.20 1 494 . 112 GLN N N 123.0 0.25 1 495 . 112 GLN H H 8.49 0.01 1 496 . 112 GLN CB C 28.6 0.20 1 497 . 112 GLN CA C 52.5 0.20 1 498 . 112 GLN C C 173.9 0.20 1 499 . 113 ASN N N 118.8 0.25 1 500 . 113 ASN H H 8.06 0.01 1 501 . 113 ASN CB C 41.2 0.20 1 502 . 113 ASN CA C 52.0 0.20 1 503 . 113 ASN C C 173.8 0.20 1 504 . 114 VAL N N 124.8 0.25 1 505 . 114 VAL H H 8.87 0.01 1 506 . 114 VAL CB C 35.7 0.20 1 507 . 114 VAL CA C 60.4 0.20 1 508 . 114 VAL C C 173.9 0.20 1 509 . 115 SER N N 120.5 0.25 1 510 . 115 SER H H 8.23 0.01 1 511 . 115 SER CA C 56.8 0.20 1 512 . 115 SER CB C 65.2 0.20 1 513 . 115 SER C C 172.9 0.20 1 514 . 116 VAL N N 121.0 0.25 1 515 . 116 VAL H H 8.91 0.01 1 516 . 116 VAL CB C 34.9 0.20 1 517 . 116 VAL CA C 58.8 0.20 1 518 . 116 VAL C C 173.2 0.20 1 519 . 117 LYS N N 125.0 0.25 1 520 . 117 LYS H H 8.46 0.01 1 521 . 117 LYS CB C 32.8 0.20 1 522 . 117 LYS CA C 56.8 0.20 1 523 . 117 LYS C C 175.6 0.20 1 524 . 118 LEU N N 121.9 0.25 1 525 . 118 LEU H H 8.56 0.01 1 526 . 118 LEU CB C 43.9 0.20 1 527 . 118 LEU CA C 50.8 0.20 1 528 . 119 PRO CB C 28.3 0.20 1 529 . 119 PRO CA C 62.0 0.20 1 530 . 119 PRO C C 173.6 0.20 1 531 . 120 ILE N N 124.7 0.25 1 532 . 120 ILE H H 8.50 0.01 1 533 . 120 ILE CB C 37.9 0.20 1 534 . 120 ILE CA C 61.9 0.20 1 535 . 120 ILE C C 174.2 0.20 1 536 . 121 THR N N 112.6 0.25 1 537 . 121 THR H H 6.39 0.01 1 538 . 121 THR CA C 59.0 0.20 1 539 . 121 THR CB C 70.8 0.20 1 540 . 122 LEU CB C 42.2 0.20 1 541 . 122 LEU CA C 57.6 0.20 1 542 . 122 LEU C C 175.2 0.20 1 543 . 123 ASN N N 106.3 0.25 1 544 . 123 ASN H H 7.49 0.01 1 545 . 123 ASN CB C 36.7 0.20 1 546 . 123 ASN CA C 54.7 0.20 1 547 . 123 ASN C C 174.5 0.20 1 548 . 124 LYS N N 118.5 0.25 1 549 . 124 LYS H H 7.43 0.01 1 550 . 124 LYS CB C 27.2 0.20 1 551 . 124 LYS CA C 55.0 0.20 1 552 . 124 LYS C C 175.8 0.20 1 553 . 125 PHE N N 115.2 0.25 1 554 . 125 PHE H H 6.85 0.01 1 555 . 125 PHE CB C 37.0 0.20 1 556 . 125 PHE CA C 57.1 0.20 1 557 . 125 PHE C C 174.5 0.20 1 558 . 126 PHE N N 120.3 0.25 1 559 . 126 PHE H H 6.97 0.01 1 560 . 126 PHE CB C 40.9 0.20 1 561 . 126 PHE CA C 57.4 0.20 1 562 . 126 PHE C C 177.4 0.20 1 563 . 127 GLN N N 122.4 0.25 1 564 . 127 GLN H H 9.84 0.01 1 565 . 127 GLN CB C 30.8 0.20 1 566 . 127 GLN CA C 51.9 0.20 1 567 . 128 PRO CB C 32.6 0.20 1 568 . 128 PRO CA C 63.5 0.20 1 569 . 128 PRO C C 177.1 0.20 1 570 . 129 THR N N 112.7 0.25 1 571 . 129 THR H H 7.46 0.01 1 572 . 129 THR CA C 57.1 0.20 1 573 . 129 THR CB C 71.1 0.20 1 574 . 129 THR C C 173.5 0.20 1 575 . 130 GLU N N 125.7 0.25 1 576 . 130 GLU H H 8.68 0.01 1 577 . 130 GLU CB C 29.0 0.20 1 578 . 130 GLU CA C 56.9 0.20 1 579 . 130 GLU C C 175.5 0.20 1 580 . 131 MET N N 118.8 0.25 1 581 . 131 MET H H 7.01 0.01 1 582 . 131 MET CB C 35.7 0.20 1 583 . 131 MET CA C 55.1 0.20 1 584 . 131 MET C C 173.4 0.20 1 585 . 132 ALA N N 123.0 0.25 1 586 . 132 ALA H H 8.75 0.01 1 587 . 132 ALA CB C 19.5 0.20 1 588 . 132 ALA CA C 50.8 0.20 1 589 . 132 ALA C C 175.7 0.20 1 590 . 133 SER N N 116.2 0.25 1 591 . 133 SER H H 8.94 0.01 1 592 . 133 SER CA C 62.0 0.20 1 593 . 133 SER CB C 64.9 0.20 1 594 . 133 SER C C 176.0 0.20 1 595 . 134 GLN N N 117.7 0.25 1 596 . 134 GLN H H 8.86 0.01 1 597 . 134 GLN CB C 27.2 0.20 1 598 . 134 GLN CA C 59.2 0.20 1 599 . 134 GLN C C 178.5 0.20 1 600 . 135 ASP N N 118.7 0.25 1 601 . 135 ASP H H 7.06 0.01 1 602 . 135 ASP CB C 41.1 0.20 1 603 . 135 ASP CA C 56.6 0.20 1 604 . 135 ASP C C 177.4 0.20 1 605 . 136 PHE N N 120.8 0.25 1 606 . 136 PHE H H 8.19 0.01 1 607 . 136 PHE CB C 38.4 0.20 1 608 . 136 PHE CA C 62.5 0.20 1 609 . 136 PHE C C 176.8 0.20 1 610 . 137 PHE N N 115.7 0.25 1 611 . 137 PHE H H 8.42 0.01 1 612 . 137 PHE CB C 37.9 0.20 1 613 . 137 PHE CA C 62.2 0.20 1 614 . 137 PHE C C 178.9 0.20 1 615 . 138 GLN N N 119.4 0.25 1 616 . 138 GLN H H 7.90 0.01 1 617 . 138 GLN CB C 28.1 0.20 1 618 . 138 GLN CA C 58.9 0.20 1 619 . 138 GLN C C 178.3 0.20 1 620 . 139 ARG N N 120.2 0.25 1 621 . 139 ARG H H 8.04 0.01 1 622 . 139 ARG CB C 29.0 0.20 1 623 . 139 ARG CA C 58.3 0.20 1 624 . 139 ARG C C 177.9 0.20 1 625 . 140 TRP N N 120.5 0.25 1 626 . 140 TRP H H 8.72 0.01 1 627 . 140 TRP CB C 29.0 0.20 1 628 . 140 TRP CA C 60.6 0.20 1 629 . 140 TRP C C 178.4 0.20 1 630 . 140 TRP NE1 N 129.9 0.25 1 631 . 140 TRP HE1 H 10.31 0.01 1 632 . 141 LYS N N 115.6 0.25 1 633 . 141 LYS H H 7.64 0.01 1 634 . 141 LYS CB C 32.5 0.20 1 635 . 141 LYS CA C 58.3 0.20 1 636 . 141 LYS C C 178.6 0.20 1 637 . 142 GLN N N 117.7 0.25 1 638 . 142 GLN H H 7.54 0.01 1 639 . 142 GLN CB C 28.5 0.20 1 640 . 142 GLN CA C 57.5 0.20 1 641 . 142 GLN C C 177.5 0.20 1 642 . 143 LEU N N 122.6 0.25 1 643 . 143 LEU H H 6.99 0.01 1 644 . 143 LEU CB C 40.2 0.20 1 645 . 143 LEU CA C 52.8 0.20 1 646 . 143 LEU C C 175.7 0.20 1 647 . 144 SER N N 109.1 0.25 1 648 . 144 SER H H 7.05 0.01 1 649 . 144 SER CA C 57.9 0.20 1 650 . 144 SER CB C 64.1 0.20 1 651 . 144 SER C C 175.3 0.20 1 652 . 145 ASN N N 123.8 0.25 1 653 . 145 ASN H H 8.08 0.01 1 654 . 145 ASN CB C 37.9 0.20 1 655 . 145 ASN CA C 51.7 0.20 1 656 . 146 PRO CB C 31.7 0.20 1 657 . 146 PRO CA C 65.4 0.20 1 658 . 146 PRO C C 177.9 0.20 1 659 . 147 GLN N N 113.1 0.25 1 660 . 147 GLN H H 8.39 0.01 1 661 . 147 GLN CB C 28.1 0.20 1 662 . 147 GLN CA C 57.4 0.20 1 663 . 147 GLN C C 176.7 0.20 1 664 . 148 GLN N N 114.5 0.25 1 665 . 148 GLN H H 7.84 0.01 1 666 . 148 GLN CB C 28.1 0.20 1 667 . 148 GLN CA C 56.8 0.20 1 668 . 148 GLN C C 176.6 0.20 1 669 . 149 GLU N N 122.4 0.25 1 670 . 149 GLU H H 7.40 0.01 1 671 . 149 GLU CB C 32.0 0.20 1 672 . 149 GLU CA C 54.2 0.20 1 673 . 149 GLU C C 174.9 0.20 1 674 . 150 VAL N N 125.2 0.25 1 675 . 150 VAL H H 8.72 0.01 1 676 . 150 VAL CB C 35.2 0.20 1 677 . 150 VAL CA C 61.5 0.20 1 678 . 150 VAL C C 173.3 0.20 1 679 . 151 GLN N N 125.4 0.25 1 680 . 151 GLN H H 8.71 0.01 1 681 . 151 GLN CB C 33.9 0.20 1 682 . 151 GLN CA C 53.2 0.20 1 683 . 151 GLN C C 174.9 0.20 1 684 . 152 ASN N N 121.7 0.25 1 685 . 152 ASN H H 9.30 0.01 1 686 . 152 ASN CB C 42.6 0.20 1 687 . 152 ASN CA C 51.9 0.20 1 688 . 152 ASN C C 173.2 0.20 1 689 . 153 ILE N N 127.2 0.25 1 690 . 153 ILE H H 8.26 0.01 1 691 . 153 ILE CB C 39.3 0.20 1 692 . 153 ILE CA C 60.2 0.20 1 693 . 153 ILE C C 175.1 0.20 1 694 . 154 PHE N N 122.3 0.25 1 695 . 154 PHE H H 8.46 0.01 1 696 . 154 PHE CB C 40.9 0.20 1 697 . 154 PHE CA C 54.7 0.20 1 698 . 154 PHE C C 172.9 0.20 1 699 . 155 LYS N N 121.3 0.25 1 700 . 155 LYS H H 8.71 0.01 1 701 . 155 LYS CB C 32.9 0.20 1 702 . 155 LYS CA C 55.4 0.20 1 703 . 155 LYS C C 176.2 0.20 1 704 . 156 ALA N N 126.5 0.25 1 705 . 156 ALA H H 8.33 0.01 1 706 . 156 ALA CB C 19.3 0.20 1 707 . 156 ALA CA C 53.1 0.20 1 708 . 156 ALA C C 178.3 0.20 1 709 . 157 LYS N N 126.8 0.25 1 710 . 157 LYS H H 10.62 0.01 1 711 . 157 LYS CB C 32.4 0.20 1 712 . 157 LYS CA C 57.1 0.20 1 713 . 157 LYS C C 175.1 0.20 1 714 . 158 HIS N N 119.4 0.25 1 715 . 158 HIS H H 8.28 0.01 1 716 . 158 HIS CB C 31.2 0.20 1 717 . 158 HIS CA C 53.1 0.20 1 718 . 160 MET CB C 31.1 0.20 1 719 . 160 MET CA C 55.9 0.20 1 720 . 160 MET C C 174.9 0.20 1 721 . 161 ASP N N 124.4 0.25 1 722 . 161 ASP H H 7.72 0.01 1 723 . 161 ASP CB C 43.5 0.20 1 724 . 161 ASP CA C 53.2 0.20 1 725 . 162 THR CA C 67.2 0.20 1 726 . 162 THR CB C 69.2 0.20 1 727 . 162 THR C C 176.0 0.20 1 728 . 163 GLU N N 119.3 0.25 1 729 . 163 GLU H H 8.27 0.01 1 730 . 163 GLU CB C 29.0 0.20 1 731 . 163 GLU CA C 59.4 0.20 1 732 . 163 GLU C C 180.1 0.20 1 733 . 164 ILE N N 122.1 0.25 1 734 . 164 ILE H H 8.12 0.01 1 735 . 164 ILE CB C 36.8 0.20 1 736 . 164 ILE CA C 63.6 0.20 1 737 . 164 ILE C C 178.1 0.20 1 738 . 165 THR N N 118.5 0.25 1 739 . 165 THR H H 8.31 0.01 1 740 . 165 THR CA C 67.3 0.20 1 741 . 165 THR CB C 68.3 0.20 1 742 . 165 THR C C 175.8 0.20 1 743 . 166 LYS N N 118.7 0.25 1 744 . 166 LYS H H 7.98 0.01 1 745 . 166 LYS CB C 32.7 0.20 1 746 . 166 LYS CA C 60.8 0.20 1 747 . 166 LYS C C 177.3 0.20 1 748 . 167 ALA N N 118.1 0.25 1 749 . 167 ALA H H 7.36 0.01 1 750 . 167 ALA CB C 17.5 0.20 1 751 . 167 ALA CA C 55.0 0.20 1 752 . 167 ALA C C 181.9 0.20 1 753 . 168 LYS N N 120.4 0.25 1 754 . 168 LYS H H 8.34 0.01 1 755 . 168 LYS CB C 32.8 0.20 1 756 . 168 LYS CA C 59.7 0.20 1 757 . 168 LYS C C 178.3 0.20 1 758 . 169 ILE N N 120.0 0.25 1 759 . 169 ILE H H 7.85 0.01 1 760 . 169 ILE CB C 37.2 0.20 1 761 . 169 ILE CA C 66.1 0.20 1 762 . 169 ILE C C 177.2 0.20 1 763 . 170 ILE N N 118.4 0.25 1 764 . 170 ILE H H 7.96 0.01 1 765 . 170 ILE CB C 38.0 0.20 1 766 . 170 ILE CA C 63.7 0.20 1 767 . 170 ILE C C 181.8 0.20 1 768 . 171 GLY N N 109.8 0.25 1 769 . 171 GLY H H 8.63 0.01 1 770 . 171 GLY CA C 46.4 0.20 1 771 . 171 GLY C C 174.5 0.20 1 772 . 172 PHE N N 121.3 0.25 1 773 . 172 PHE H H 8.28 0.01 1 774 . 172 PHE CB C 38.9 0.20 1 775 . 172 PHE CA C 59.5 0.20 1 776 . 172 PHE C C 176.3 0.20 1 777 . 173 GLY N N 100.4 0.25 1 778 . 173 GLY H H 7.22 0.01 1 779 . 173 GLY CA C 43.9 0.20 1 780 . 173 GLY C C 172.1 0.20 1 781 . 174 SER N N 108.4 0.25 1 782 . 174 SER H H 6.75 0.01 1 783 . 174 SER CA C 56.3 0.20 1 784 . 174 SER CB C 64.5 0.20 1 785 . 174 SER C C 174.7 0.20 1 786 . 175 ALA N N 121.7 0.25 1 787 . 175 ALA H H 8.34 0.01 1 788 . 175 ALA CB C 19.4 0.20 1 789 . 175 ALA CA C 51.7 0.20 1 790 . 175 ALA C C 177.3 0.20 1 791 . 176 LEU N N 123.8 0.25 1 792 . 176 LEU H H 8.49 0.01 1 793 . 176 LEU CB C 43.2 0.20 1 794 . 176 LEU CA C 53.5 0.20 1 795 . 176 LEU C C 176.1 0.20 1 796 . 177 LEU N N 126.8 0.25 1 797 . 177 LEU H H 8.69 0.01 1 798 . 177 LEU CB C 40.3 0.20 1 799 . 177 LEU CA C 52.9 0.20 1 800 . 177 LEU C C 176.4 0.20 1 801 . 178 GLU N N 124.4 0.25 1 802 . 178 GLU H H 8.69 0.01 1 803 . 178 GLU CB C 31.0 0.20 1 804 . 178 GLU CA C 56.4 0.20 1 805 . 178 GLU C C 175.7 0.20 1 806 . 179 GLU N N 116.1 0.25 1 807 . 179 GLU H H 8.94 0.01 1 808 . 179 GLU CB C 27.1 0.20 1 809 . 179 GLU CA C 56.7 0.20 1 810 . 179 GLU C C 175.5 0.20 1 811 . 180 VAL N N 118.3 0.25 1 812 . 180 VAL H H 7.95 0.01 1 813 . 180 VAL CB C 32.5 0.20 1 814 . 180 VAL CA C 64.0 0.20 1 815 . 180 VAL C C 175.2 0.20 1 816 . 181 ASP N N 121.3 0.25 1 817 . 181 ASP H H 8.12 0.01 1 818 . 181 ASP CB C 42.6 0.20 1 819 . 181 ASP CA C 51.2 0.20 1 820 . 182 PRO CB C 31.8 0.20 1 821 . 182 PRO CA C 63.6 0.20 1 822 . 182 PRO C C 176.6 0.20 1 823 . 183 ASN N N 119.6 0.25 1 824 . 183 ASN H H 8.85 0.01 1 825 . 183 ASN CB C 38.5 0.20 1 826 . 183 ASN CA C 49.2 0.20 1 827 . 184 PRO CB C 31.6 0.20 1 828 . 184 PRO CA C 63.5 0.20 1 829 . 184 PRO C C 176.4 0.20 1 830 . 185 ALA N N 119.4 0.25 1 831 . 185 ALA H H 7.78 0.01 1 832 . 185 ALA CB C 19.0 0.20 1 833 . 185 ALA CA C 52.0 0.20 1 834 . 186 ASN CB C 39.1 0.20 1 835 . 186 ASN CA C 51.2 0.20 1 836 . 186 ASN C C 174.8 0.20 1 837 . 187 PHE N N 116.1 0.25 1 838 . 187 PHE H H 8.62 0.01 1 839 . 187 PHE CB C 41.6 0.20 1 840 . 187 PHE CA C 55.6 0.20 1 841 . 187 PHE C C 174.8 0.20 1 842 . 188 VAL N N 122.3 0.25 1 843 . 188 VAL H H 9.02 0.01 1 844 . 188 VAL CB C 34.3 0.20 1 845 . 188 VAL CA C 60.3 0.20 1 846 . 188 VAL C C 174.0 0.20 1 847 . 189 GLY N N 110.1 0.25 1 848 . 189 GLY H H 8.87 0.01 1 849 . 189 GLY CA C 43.9 0.20 1 850 . 189 GLY C C 172.4 0.20 1 851 . 190 ALA N N 118.0 0.25 1 852 . 190 ALA H H 7.77 0.01 1 853 . 190 ALA CB C 24.7 0.20 1 854 . 190 ALA CA C 51.5 0.20 1 855 . 190 ALA C C 177.0 0.20 1 856 . 191 GLY N N 109.7 0.25 1 857 . 191 GLY H H 9.04 0.01 1 858 . 191 GLY CA C 46.4 0.20 1 859 . 191 GLY C C 171.3 0.20 1 860 . 192 ILE N N 121.3 0.25 1 861 . 192 ILE H H 9.28 0.01 1 862 . 192 ILE CB C 43.0 0.20 1 863 . 192 ILE CA C 59.2 0.20 1 864 . 192 ILE C C 175.6 0.20 1 865 . 193 ILE N N 127.4 0.25 1 866 . 193 ILE H H 9.22 0.01 1 867 . 193 ILE CB C 37.0 0.20 1 868 . 193 ILE CA C 58.0 0.20 1 869 . 193 ILE C C 174.9 0.20 1 870 . 194 HIS N N 128.7 0.25 1 871 . 194 HIS H H 8.45 0.01 1 872 . 194 HIS CB C 32.2 0.20 1 873 . 194 HIS CA C 57.1 0.20 1 874 . 194 HIS C C 173.0 0.20 1 875 . 195 THR N N 109.2 0.25 1 876 . 195 THR H H 7.52 0.01 1 877 . 195 THR CA C 58.7 0.20 1 878 . 195 THR CB C 71.0 0.20 1 879 . 195 THR C C 177.5 0.20 1 880 . 196 LYS N N 120.7 0.25 1 881 . 196 LYS H H 8.19 0.01 1 882 . 196 LYS CB C 34.8 0.20 1 883 . 196 LYS CA C 59.8 0.20 1 884 . 196 LYS C C 177.6 0.20 1 885 . 197 THR N N 104.0 0.25 1 886 . 197 THR H H 7.86 0.01 1 887 . 197 THR CA C 62.6 0.20 1 888 . 197 THR CB C 70.5 0.20 1 889 . 197 THR C C 175.0 0.20 1 890 . 198 THR N N 114.6 0.25 1 891 . 198 THR H H 7.44 0.01 1 892 . 198 THR CA C 61.3 0.20 1 893 . 198 THR CB C 70.3 0.20 1 894 . 199 GLN CB C 33.0 0.20 1 895 . 199 GLN CA C 55.5 0.20 1 896 . 199 GLN C C 177.4 0.20 1 897 . 200 ILE N N 120.7 0.25 1 898 . 200 ILE H H 8.72 0.01 1 899 . 200 ILE CB C 39.9 0.20 1 900 . 200 ILE CA C 60.6 0.20 1 901 . 201 GLY CA C 46.1 0.20 1 902 . 201 GLY C C 173.0 0.20 1 903 . 202 CYS N N 119.0 0.25 1 904 . 202 CYS H H 8.67 0.01 1 905 . 202 CYS CB C 30.8 0.20 1 906 . 202 CYS CA C 57.6 0.20 1 907 . 202 CYS C C 172.3 0.20 1 908 . 203 LEU N N 124.8 0.25 1 909 . 203 LEU H H 9.21 0.01 1 910 . 203 LEU CB C 45.6 0.20 1 911 . 203 LEU CA C 53.6 0.20 1 912 . 203 LEU C C 175.2 0.20 1 913 . 204 LEU N N 118.2 0.25 1 914 . 204 LEU H H 9.25 0.01 1 915 . 204 LEU CB C 46.7 0.20 1 916 . 204 LEU CA C 53.4 0.20 1 917 . 204 LEU C C 174.6 0.20 1 918 . 205 ARG N N 119.2 0.25 1 919 . 205 ARG H H 9.07 0.01 1 920 . 205 ARG CB C 34.4 0.20 1 921 . 205 ARG CA C 55.1 0.20 1 922 . 205 ARG C C 173.9 0.20 1 923 . 206 LEU N N 129.1 0.25 1 924 . 206 LEU H H 9.60 0.01 1 925 . 206 LEU CB C 45.4 0.20 1 926 . 206 LEU CA C 53.4 0.20 1 927 . 209 ASN CA C 54.6 0.20 1 928 . 209 ASN C C 175.7 0.20 1 929 . 210 LEU N N 124.8 0.25 1 930 . 210 LEU H H 9.02 0.01 1 931 . 210 LEU CB C 41.9 0.20 1 932 . 210 LEU CA C 60.2 0.20 1 933 . 210 LEU C C 179.3 0.20 1 934 . 211 GLN N N 117.8 0.25 1 935 . 211 GLN H H 8.19 0.01 1 936 . 211 GLN CB C 27.6 0.20 1 937 . 211 GLN CA C 58.7 0.20 1 938 . 211 GLN C C 177.2 0.20 1 939 . 212 ALA N N 118.0 0.25 1 940 . 212 ALA H H 7.25 0.01 1 941 . 212 ALA CB C 19.3 0.20 1 942 . 212 ALA CA C 50.8 0.20 1 943 . 212 ALA C C 176.1 0.20 1 944 . 213 GLN N N 115.4 0.25 1 945 . 213 GLN H H 7.71 0.01 1 946 . 213 GLN CB C 25.6 0.20 1 947 . 213 GLN CA C 56.4 0.20 1 948 . 213 GLN C C 174.2 0.20 1 949 . 214 MET N N 114.3 0.25 1 950 . 214 MET H H 7.41 0.01 1 951 . 214 MET CB C 37.9 0.20 1 952 . 214 MET CA C 52.8 0.20 1 953 . 214 MET C C 173.2 0.20 1 954 . 215 TYR N N 115.9 0.25 1 955 . 215 TYR H H 8.57 0.01 1 956 . 215 TYR CB C 43.2 0.20 1 957 . 215 TYR CA C 56.4 0.20 1 958 . 215 TYR C C 174.2 0.20 1 959 . 216 ARG N N 117.6 0.25 1 960 . 216 ARG H H 7.88 0.01 1 961 . 216 ARG CB C 33.2 0.20 1 962 . 216 ARG CA C 55.3 0.20 1 963 . 216 ARG C C 174.2 0.20 1 964 . 217 LEU N N 131.7 0.25 1 965 . 217 LEU H H 9.40 0.01 1 966 . 217 LEU CB C 45.7 0.20 1 967 . 217 LEU CA C 53.1 0.20 1 968 . 217 LEU C C 174.0 0.20 1 969 . 218 THR N N 121.8 0.25 1 970 . 218 THR H H 9.20 0.01 1 971 . 218 THR CA C 62.2 0.20 1 972 . 218 THR CB C 70.7 0.20 1 973 . 218 THR C C 172.4 0.20 1 974 . 219 LEU N N 129.4 0.25 1 975 . 219 LEU H H 9.34 0.01 1 976 . 219 LEU CB C 45.2 0.20 1 977 . 219 LEU CA C 51.8 0.20 1 978 . 219 LEU C C 176.1 0.20 1 979 . 220 ARG N N 119.1 0.25 1 980 . 220 ARG H H 8.75 0.01 1 981 . 220 ARG CB C 33.5 0.20 1 982 . 220 ARG CA C 56.4 0.20 1 983 . 221 THR CA C 59.0 0.20 1 984 . 221 THR CB C 71.8 0.20 1 985 . 221 THR C C 173.3 0.20 1 986 . 222 SER N N 107.2 0.25 1 987 . 222 SER H H 7.49 0.01 1 988 . 222 SER CA C 59.2 0.20 1 989 . 222 SER CB C 63.4 0.20 1 990 . 222 SER C C 173.9 0.20 1 991 . 223 LYS N N 123.4 0.25 1 992 . 223 LYS H H 8.56 0.01 1 993 . 223 LYS CB C 36.8 0.20 1 994 . 223 LYS CA C 56.1 0.20 1 995 . 223 LYS C C 174.1 0.20 1 996 . 224 ASP N N 130.8 0.25 1 997 . 224 ASP H H 9.09 0.01 1 998 . 224 ASP CB C 39.5 0.20 1 999 . 224 ASP CA C 57.9 0.20 1 1000 . 224 ASP C C 178.0 0.20 1 1001 . 225 THR N N 112.5 0.25 1 1002 . 225 THR H H 8.89 0.01 1 1003 . 225 THR CA C 64.9 0.20 1 1004 . 225 THR CB C 67.4 0.20 1 1005 . 225 THR C C 177.8 0.20 1 1006 . 226 VAL N N 124.7 0.25 1 1007 . 226 VAL H H 7.12 0.01 1 1008 . 226 VAL CB C 29.8 0.20 1 1009 . 226 VAL CA C 65.9 0.20 1 1010 . 226 VAL C C 177.1 0.20 1 1011 . 227 SER N N 117.1 0.25 1 1012 . 227 SER H H 8.21 0.01 1 1013 . 227 SER CA C 61.7 0.20 1 1014 . 227 SER CB C 63.1 0.20 1 1015 . 227 SER C C 175.1 0.20 1 1016 . 228 GLN N N 117.4 0.25 1 1017 . 228 GLN H H 7.91 0.01 1 1018 . 228 GLN CB C 27.5 0.20 1 1019 . 228 GLN CA C 58.8 0.20 1 1020 . 228 GLN C C 177.8 0.20 1 1021 . 229 ARG N N 119.3 0.25 1 1022 . 229 ARG H H 7.85 0.01 1 1023 . 229 ARG CB C 28.0 0.20 1 1024 . 229 ARG CA C 57.1 0.20 1 1025 . 229 ARG C C 178.6 0.20 1 1026 . 230 LEU N N 114.8 0.25 1 1027 . 230 LEU H H 8.79 0.01 1 1028 . 230 LEU CB C 43.7 0.20 1 1029 . 230 LEU CA C 57.9 0.20 1 1030 . 230 LEU C C 178.1 0.20 1 1031 . 231 CYS N N 117.9 0.25 1 1032 . 231 CYS H H 7.82 0.01 1 1033 . 231 CYS CB C 26.4 0.20 1 1034 . 231 CYS CA C 62.6 0.20 1 1035 . 231 CYS C C 177.6 0.20 1 1036 . 232 GLU N N 121.5 0.25 1 1037 . 232 GLU H H 8.15 0.01 1 1038 . 232 GLU CB C 29.0 0.20 1 1039 . 232 GLU CA C 59.2 0.20 1 1040 . 232 GLU C C 178.9 0.20 1 1041 . 233 LEU N N 117.7 0.25 1 1042 . 233 LEU H H 7.89 0.01 1 1043 . 233 LEU CB C 44.1 0.20 1 1044 . 233 LEU CA C 57.2 0.20 1 1045 . 233 LEU C C 179.2 0.20 1 1046 . 234 LEU N N 118.4 0.25 1 1047 . 234 LEU H H 8.21 0.01 1 1048 . 234 LEU CB C 41.3 0.20 1 1049 . 234 LEU CA C 56.8 0.20 1 1050 . 234 LEU C C 178.6 0.20 1 1051 . 235 SER N N 112.2 0.25 1 1052 . 235 SER H H 8.00 0.01 1 1053 . 235 SER CA C 61.8 0.20 1 1054 . 235 SER CB C 62.8 0.20 1 1055 . 235 SER C C 174.2 0.20 1 1056 . 236 GLU N N 115.6 0.25 1 1057 . 236 GLU H H 6.54 0.01 1 1058 . 236 GLU CB C 29.9 0.20 1 1059 . 236 GLU CA C 56.4 0.20 1 1060 . 236 GLU C C 176.7 0.20 1 1061 . 237 GLN N N 112.9 0.25 1 1062 . 237 GLN H H 7.30 0.01 1 1063 . 237 GLN CB C 27.0 0.20 1 1064 . 237 GLN CA C 54.5 0.20 1 1065 . 237 GLN C C 173.9 0.20 1 1066 . 238 PHE N N 119.6 0.25 1 1067 . 238 PHE H H 6.67 0.01 1 1068 . 238 PHE CB C 43.0 0.20 1 1069 . 238 PHE CA C 59.5 0.20 1 stop_ save_ save_D_values_set_1 _Saveframe_category residual_dipolar_couplings loop_ _Sample_label $sample_3 stop_ loop_ _Residual_dipolar_coupling_ID _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name _Residual_dipolar_coupling_value _Atom_one_mol_system_component_name _Atom_two_mol_system_component_name _Residual_dipolar_coupling_min_value _Residual_dipolar_coupling_max_value _Residual_dipolar_coupling_value_error DNH 3 ASP N 3 ASP H -0.2 ? ? . . . DNH 4 ASN N 4 ASN H 2.6 ? ? . . . DNH 5 PHE N 5 PHE H -5.5 ? ? . . . DNH 6 ALA N 6 ALA H -7.6 ? ? . . . DNH 7 ARG N 7 ARG H 0.1 ? ? . . . DNH 8 PHE N 8 PHE H 0.6 ? ? . . . DNH 9 VAL N 9 VAL H -10.9 ? ? . . . DNH 11 LYS N 11 LYS H -1.0 ? ? . . . DNH 12 ASN N 12 ASN H 1.8 ? ? . . . DNH 13 ASN N 13 ASN H 6.9 ? ? . . . DNH 14 GLY N 14 GLY H 5.3 ? ? . . . DNH 16 LEU N 16 LEU H 2.3 ? ? . . . DNH 17 PHE N 17 PHE H 0.2 ? ? . . . DNH 18 GLU N 18 GLU H -1.9 ? ? . . . DNH 19 ASN N 19 ASN H -1.3 ? ? . . . DNH 21 LEU N 21 LEU H 0.6 ? ? . . . DNH 22 LEU N 22 LEU H -2.5 ? ? . . . DNH 23 GLN N 23 GLN H 0.1 ? ? . . . DNH 24 ILE N 24 ILE H -2.3 ? ? . . . DNH 25 GLY N 25 GLY H 4.9 ? ? . . . DNH 26 LEU N 26 LEU H 6.7 ? ? . . . DNH 27 LYS N 27 LYS H 12.5 ? ? . . . DNH 28 SER N 28 SER H 8.9 ? ? . . . DNH 29 GLU N 29 GLU H 9.5 ? ? . . . DNH 30 PHE N 30 PHE H 7.8 ? ? . . . DNH 31 ARG N 31 ARG H 6.6 ? ? . . . DNH 32 GLN N 32 GLN H 6.5 ? ? . . . DNH 33 ASN N 33 ASN H -4.6 ? ? . . . DNH 34 LEU N 34 LEU H 0.8 ? ? . . . DNH 35 GLY N 35 GLY H 11.3 ? ? . . . DNH 36 ARG N 36 ARG H 9.7 ? ? . . . DNH 37 MET N 37 MET H 8.0 ? ? . . . DNH 38 PHE N 38 PHE H 8.6 ? ? . . . DNH 39 ILE N 39 ILE H 4.4 ? ? . . . DNH 40 PHE N 40 PHE H 5.5 ? ? . . . DNH 41 TYR N 41 TYR H -3.5 ? ? . . . DNH 42 GLY N 42 GLY H 2.6 ? ? . . . DNH 43 ASN N 43 ASN H -5.6 ? ? . . . DNH 45 THR N 45 THR H -1.9 ? ? . . . DNH 47 THR N 47 THR H 4.9 ? ? . . . DNH 48 GLN N 48 GLN H 5.0 ? ? . . . DNH 49 PHE N 49 PHE H -8.5 ? ? . . . DNH 50 LEU N 50 LEU H -9.1 ? ? . . . DNH 51 ASN N 51 ASN H -4.5 ? ? . . . DNH 52 PHE N 52 PHE H 2.9 ? ? . . . DNH 53 THR N 53 THR H -10.5 ? ? . . . DNH 55 THR N 55 THR H -7.8 ? ? . . . DNH 56 LEU N 56 LEU H -3.6 ? ? . . . DNH 57 ILE N 57 ILE H 3.2 ? ? . . . DNH 59 ALA N 59 ALA H 4.6 ? ? . . . DNH 60 ASP N 60 ASP H -8.9 ? ? . . . DNH 61 ASP N 61 ASP H -7.6 ? ? . . . DNH 62 LEU N 62 LEU H -11.4 ? ? . . . DNH 63 GLN N 63 GLN H -7.1 ? ? . . . DNH 64 THR N 64 THR H -3.1 ? ? . . . DNH 65 ASN N 65 ASN H -14.8 ? ? . . . DNH 66 LEU N 66 LEU H -1.6 ? ? . . . DNH 67 ASN N 67 ASN H -3.6 ? ? . . . DNH 68 LEU N 68 LEU H 5.2 ? ? . . . DNH 69 GLN N 69 GLN H 10.8 ? ? . . . DNH 71 LYS N 71 LYS H 6.8 ? ? . . . DNH 74 ASP N 74 ASP H 5.4 ? ? . . . DNH 76 THR N 76 THR H -14.8 ? ? . . . DNH 77 VAL N 77 VAL H -11.7 ? ? . . . DNH 78 ASP N 78 ASP H -12.2 ? ? . . . DNH 79 GLY N 79 GLY H 5.7 ? ? . . . DNH 80 GLY N 80 GLY H -6.5 ? ? . . . DNH 81 ALA N 81 ALA H 2.7 ? ? . . . DNH 82 GLN N 82 GLN H -6.4 ? ? . . . DNH 83 VAL N 83 VAL H -5.2 ? ? . . . DNH 84 GLN N 84 GLN H 4.2 ? ? . . . DNH 85 GLN N 85 GLN H 4.3 ? ? . . . DNH 86 VAL N 86 VAL H 11.1 ? ? . . . DNH 87 VAL N 87 VAL H 10.2 ? ? . . . DNH 88 ASN N 88 ASN H 6.3 ? ? . . . DNH 89 ILE N 89 ILE H 3.9 ? ? . . . DNH 90 GLU N 90 GLU H -1.3 ? ? . . . DNH 91 CYS N 91 CYS H 0.8 ? ? . . . DNH 92 ILE N 92 ILE H -13.4 ? ? . . . DNH 93 SER N 93 SER H -7.8 ? ? . . . DNH 94 ASP N 94 ASP H -2.9 ? ? . . . DNH 95 PHE N 95 PHE H 8.8 ? ? . . . DNH 97 GLU N 97 GLU H -1.6 ? ? . . . DNH 98 ALA N 98 ALA H -9.3 ? ? . . . DNH 100 VAL N 100 VAL H 7.2 ? ? . . . DNH 101 LEU N 101 LEU H 4.6 ? ? . . . DNH 102 ASN N 102 ASN H -7.0 ? ? . . . DNH 103 ILE N 103 ILE H -2.6 ? ? . . . DNH 104 GLN N 104 GLN H -12.5 ? ? . . . DNH 105 PHE N 105 PHE H -8.3 ? ? . . . DNH 106 ARG N 106 ARG H -8.6 ? ? . . . DNH 107 TYR N 107 TYR H -4.9 ? ? . . . DNH 109 GLY N 109 GLY H -9.9 ? ? . . . DNH 110 THR N 110 THR H 3.3 ? ? . . . DNH 111 PHE N 111 PHE H -12.3 ? ? . . . DNH 112 GLN N 112 GLN H -7.2 ? ? . . . DNH 113 ASN N 113 ASN H -5.6 ? ? . . . DNH 114 VAL N 114 VAL H -3.4 ? ? . . . DNH 115 SER N 115 SER H -7.6 ? ? . . . DNH 116 VAL N 116 VAL H -4.6 ? ? . . . DNH 117 LYS N 117 LYS H -2.2 ? ? . . . DNH 118 LEU N 118 LEU H 7.1 ? ? . . . DNH 120 ILE N 120 ILE H -3.4 ? ? . . . DNH 121 THR N 121 THR H -4.5 ? ? . . . DNH 123 ASN N 123 ASN H -14.8 ? ? . . . DNH 124 LYS N 124 LYS H 1.7 ? ? . . . DNH 125 PHE N 125 PHE H -5.7 ? ? . . . DNH 126 PHE N 126 PHE H -10.6 ? ? . . . DNH 127 GLN N 127 GLN H 1.5 ? ? . . . DNH 129 THR N 129 THR H -6.8 ? ? . . . DNH 130 GLU N 130 GLU H 0.3 ? ? . . . DNH 131 MET N 131 MET H -5.9 ? ? . . . DNH 132 ALA N 132 ALA H -6.0 ? ? . . . DNH 133 SER N 133 SER H 8.1 ? ? . . . DNH 134 GLN N 134 GLN H 2.6 ? ? . . . DNH 135 ASP N 135 ASP H 0.9 ? ? . . . DNH 136 PHE N 136 PHE H 6.4 ? ? . . . DNH 137 PHE N 137 PHE H 8.0 ? ? . . . DNH 138 GLN N 138 GLN H 2.0 ? ? . . . DNH 139 ARG N 139 ARG H 4.6 ? ? . . . DNH 140 TRP N 140 TRP H 5.2 ? ? . . . DNH 141 LYS N 141 LYS H -1.8 ? ? . . . DNH 142 GLN N 142 GLN H 3.0 ? ? . . . DNH 143 LEU N 143 LEU H 7.8 ? ? . . . DNH 145 ASN N 145 ASN H -1.7 ? ? . . . DNH 147 GLN N 147 GLN H -2.6 ? ? . . . DNH 148 GLN N 148 GLN H 3.5 ? ? . . . DNH 149 GLU N 149 GLU H 1.0 ? ? . . . DNH 150 VAL N 150 VAL H 3.1 ? ? . . . DNH 151 GLN N 151 GLN H 1.8 ? ? . . . DNH 152 ASN N 152 ASN H 0.5 ? ? . . . DNH 153 ILE N 153 ILE H 3.2 ? ? . . . DNH 154 PHE N 154 PHE H -4.6 ? ? . . . DNH 155 LYS N 155 LYS H 4.5 ? ? . . . DNH 156 ALA N 156 ALA H 8.0 ? ? . . . DNH 157 LYS N 157 LYS H -5.4 ? ? . . . DNH 158 HIS N 158 HIS H -5.7 ? ? . . . DNH 161 ASP N 161 ASP H 3.6 ? ? . . . DNH 163 GLU N 163 GLU H -1.7 ? ? . . . DNH 164 ILE N 164 ILE H -0.6 ? ? . . . DNH 165 THR N 165 THR H 9.8 ? ? . . . DNH 166 LYS N 166 LYS H 6.9 ? ? . . . DNH 167 ALA N 167 ALA H -0.2 ? ? . . . DNH 168 LYS N 168 LYS H 6.8 ? ? . . . DNH 169 ILE N 169 ILE H 8.4 ? ? . . . DNH 170 ILE N 170 ILE H 5.6 ? ? . . . DNH 171 GLY N 171 GLY H 1.5 ? ? . . . DNH 172 PHE N 172 PHE H 8.7 ? ? . . . DNH 173 GLY N 173 GLY H 13.6 ? ? . . . DNH 174 SER N 174 SER H -5.5 ? ? . . . DNH 175 ALA N 175 ALA H 2.9 ? ? . . . DNH 176 LEU N 176 LEU H 0.3 ? ? . . . DNH 177 LEU N 177 LEU H -6.9 ? ? . . . DNH 178 GLU N 178 GLU H -7.8 ? ? . . . DNH 179 GLU N 179 GLU H -8.5 ? ? . . . DNH 180 VAL N 180 VAL H -7.4 ? ? . . . DNH 181 ASP N 181 ASP H -0.1 ? ? . . . DNH 183 ASN N 183 ASN H 6.0 ? ? . . . DNH 185 ALA N 185 ALA H 7.3 ? ? . . . DNH 187 PHE N 187 PHE H -3.3 ? ? . . . DNH 188 VAL N 188 VAL H 5.7 ? ? . . . DNH 189 GLY N 189 GLY H 1.7 ? ? . . . DNH 190 ALA N 190 ALA H 3.6 ? ? . . . DNH 191 GLY N 191 GLY H 2.0 ? ? . . . DNH 192 ILE N 192 ILE H 1.0 ? ? . . . DNH 193 ILE N 193 ILE H 5.0 ? ? . . . DNH 194 HIS N 194 HIS H 1.1 ? ? . . . DNH 195 THR N 195 THR H -1.5 ? ? . . . DNH 196 LYS N 196 LYS H -10.0 ? ? . . . DNH 197 THR N 197 THR H -15.0 ? ? . . . DNH 198 THR N 198 THR H 0.1 ? ? . . . DNH 200 ILE N 200 ILE H -3.6 ? ? . . . DNH 202 CYS N 202 CYS H -1.8 ? ? . . . DNH 203 LEU N 203 LEU H 3.5 ? ? . . . DNH 204 LEU N 204 LEU H -2.0 ? ? . . . DNH 205 ARG N 205 ARG H -0.2 ? ? . . . DNH 206 LEU N 206 LEU H -4.6 ? ? . . . DNH 210 LEU N 210 LEU H -2.1 ? ? . . . DNH 211 GLN N 211 GLN H -4.2 ? ? . . . DNH 212 ALA N 212 ALA H -11.7 ? ? . . . DNH 213 GLN N 213 GLN H -1.1 ? ? . . . DNH 214 MET N 214 MET H 2.8 ? ? . . . DNH 215 TYR N 215 TYR H 0.7 ? ? . . . DNH 216 ARG N 216 ARG H -1.8 ? ? . . . DNH 217 LEU N 217 LEU H -6.1 ? ? . . . DNH 218 THR N 218 THR H 3.0 ? ? . . . DNH 219 LEU N 219 LEU H -0.5 ? ? . . . DNH 220 ARG N 220 ARG H 2.5 ? ? . . . DNH 222 SER N 222 SER H 3.3 ? ? . . . DNH 223 LYS N 223 LYS H 4.4 ? ? . . . DNH 224 ASP N 224 ASP H 0.4 ? ? . . . DNH 225 THR N 225 THR H 2.3 ? ? . . . DNH 226 VAL N 226 VAL H -3.1 ? ? . . . DNH 227 SER N 227 SER H 3.2 ? ? . . . DNH 228 GLN N 228 GLN H 3.8 ? ? . . . DNH 229 ARG N 229 ARG H -1.3 ? ? . . . DNH 230 LEU N 230 LEU H -1.9 ? ? . . . DNH 231 CYS N 231 CYS H 3.0 ? ? . . . DNH 232 GLU N 232 GLU H 0.1 ? ? . . . DNH 233 LEU N 233 LEU H -2.0 ? ? . . . DNH 234 LEU N 234 LEU H -0.7 ? ? . . . DNH 235 SER N 235 SER H 6.4 ? ? . . . DNH 236 GLU N 236 GLU H -4.3 ? ? . . . DNH 237 GLN N 237 GLN H -7.6 ? ? . . . DNH 238 PHE N 238 PHE H 4.5 ? ? . . . stop_ _Details '15N-1H residual dipolar couplings.' _Sample_conditions_label $Ex-cond_1 _Spectrometer_frequency_1H 600 _Text_data_format . _Text_data . save_