data_17851 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N, 13C assignments for beta phosphoglucomutase in a binary complex with BeF3- ; _BMRB_accession_number 17851 _BMRB_flat_file_name bmr17851.str _Entry_type original _Submission_date 2011-08-10 _Accession_date 2011-08-10 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Baxter Nicola J. . 2 Griffin Joanna L. . 3 Waltho Jonathan P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 208 "13C chemical shifts" 643 "15N chemical shifts" 208 "19F chemical shifts" 3 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-06-01 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 17852 'beta phosphoglucomutase in a ternary complex with glucose-6-phosphate and trifluoroberyllate' 7234 'Backbone 1H, 15N, 13C assignments for beta phosphoglucomutase in a ternary complex with glucose-6-phosphate and MgF3-' stop_ _Original_release_date 2012-06-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Near attack conformers dominate beta-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22505741 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Griffin Joanna L. . 2 Bowler Matthew W. . 3 Baxter Nicola J. . 4 Leigh Katherine N. . 5 Dannatt Hugh R.W. . 6 Hounslow Andrea M. . 7 Blackburn 'G. Michael' . . 8 Webster 'Charles Edwin' . . 9 Cliff Matthew J. . 10 Waltho Jonathan P. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U. S. A.' _Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Journal_volume 109 _Journal_issue 18 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6910 _Page_last 6915 _Year 2012 _Details . loop_ _Keyword 'beta phosphoglucomutase' 'ground state analogues' 'near attack conformers' 'phosphoryl transfer' trifluoroberyllate stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'beta phosphoglucomutase inhibited with trifluoroberyllate' _Enzyme_commission_number 5.4.2.6 loop_ _Mol_system_component_name _Mol_label 'phosphoenzyme analogue' $beta_phosphoglucomutase 'BERYLLIUM TRIFLUORIDE ION' $BEF 'Magnesium ion' $MG stop_ _System_molecular_weight 25000 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'beta phosphoglucomutase inhibited with a trifluoroberyllate ion forming a phosphoenzyme analogue' save_ ######################## # Monomeric polymers # ######################## save_beta_phosphoglucomutase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common beta_phosphoglucomutase _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'mutase reaction interconverting beta-glucose 1-phosphate and beta-glucose 6-phosphate' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 221 _Mol_residue_sequence ; MFKAVLFDLDGVITDTAEYH FRAWKALAEEIGINGVDRQF NEQLKGVSREDSLQKILDLA DKKVSAEEFKELAKRKNDNY VKMIQDVSPADVYPGILQLL KDLRSNKIKIALASASKNGP FLLERMNLTGYFDAIADPAE VAASKPAPDIFIAAAHAVGV APSESIGLEDSQAGIQAIKD SGALPIGVGRPEDLGDDIVI VPDTSHYTLEFLKEVWLQKQ K ; loop_ _Residue_seq_code _Residue_label 1 MET 2 PHE 3 LYS 4 ALA 5 VAL 6 LEU 7 PHE 8 ASP 9 LEU 10 ASP 11 GLY 12 VAL 13 ILE 14 THR 15 ASP 16 THR 17 ALA 18 GLU 19 TYR 20 HIS 21 PHE 22 ARG 23 ALA 24 TRP 25 LYS 26 ALA 27 LEU 28 ALA 29 GLU 30 GLU 31 ILE 32 GLY 33 ILE 34 ASN 35 GLY 36 VAL 37 ASP 38 ARG 39 GLN 40 PHE 41 ASN 42 GLU 43 GLN 44 LEU 45 LYS 46 GLY 47 VAL 48 SER 49 ARG 50 GLU 51 ASP 52 SER 53 LEU 54 GLN 55 LYS 56 ILE 57 LEU 58 ASP 59 LEU 60 ALA 61 ASP 62 LYS 63 LYS 64 VAL 65 SER 66 ALA 67 GLU 68 GLU 69 PHE 70 LYS 71 GLU 72 LEU 73 ALA 74 LYS 75 ARG 76 LYS 77 ASN 78 ASP 79 ASN 80 TYR 81 VAL 82 LYS 83 MET 84 ILE 85 GLN 86 ASP 87 VAL 88 SER 89 PRO 90 ALA 91 ASP 92 VAL 93 TYR 94 PRO 95 GLY 96 ILE 97 LEU 98 GLN 99 LEU 100 LEU 101 LYS 102 ASP 103 LEU 104 ARG 105 SER 106 ASN 107 LYS 108 ILE 109 LYS 110 ILE 111 ALA 112 LEU 113 ALA 114 SER 115 ALA 116 SER 117 LYS 118 ASN 119 GLY 120 PRO 121 PHE 122 LEU 123 LEU 124 GLU 125 ARG 126 MET 127 ASN 128 LEU 129 THR 130 GLY 131 TYR 132 PHE 133 ASP 134 ALA 135 ILE 136 ALA 137 ASP 138 PRO 139 ALA 140 GLU 141 VAL 142 ALA 143 ALA 144 SER 145 LYS 146 PRO 147 ALA 148 PRO 149 ASP 150 ILE 151 PHE 152 ILE 153 ALA 154 ALA 155 ALA 156 HIS 157 ALA 158 VAL 159 GLY 160 VAL 161 ALA 162 PRO 163 SER 164 GLU 165 SER 166 ILE 167 GLY 168 LEU 169 GLU 170 ASP 171 SER 172 GLN 173 ALA 174 GLY 175 ILE 176 GLN 177 ALA 178 ILE 179 LYS 180 ASP 181 SER 182 GLY 183 ALA 184 LEU 185 PRO 186 ILE 187 GLY 188 VAL 189 GLY 190 ARG 191 PRO 192 GLU 193 ASP 194 LEU 195 GLY 196 ASP 197 ASP 198 ILE 199 VAL 200 ILE 201 VAL 202 PRO 203 ASP 204 THR 205 SER 206 HIS 207 TYR 208 THR 209 LEU 210 GLU 211 PHE 212 LEU 213 LYS 214 GLU 215 VAL 216 TRP 217 LEU 218 GLN 219 LYS 220 GLN 221 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-12 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 BMRB 15467 beta_phosphoglucomutase 100.00 221 100.00 100.00 3.64e-156 BMRB 16409 beta_phosphoglucomutase 100.00 221 100.00 100.00 3.64e-156 BMRB 17852 beta_phosphoglucomutase 100.00 221 100.00 100.00 3.64e-156 PDB 1LVH "The Structure Of Phosphorylated Beta-phosphoglucomutase From Lactoccocus Lactis To 2.3 Angstrom Resolution" 100.00 221 99.55 99.55 3.10e-155 PDB 1O03 "Structure Of Pentavalent Phosphorous Intermediate Of An Enzyme Catalyzed Phosphoryl Transfer Reaction Observed On Cocrystalliza" 100.00 221 100.00 100.00 3.64e-156 PDB 1O08 "Structure Of Pentavalent Phosphorous Intermediate Of An Enzyme Catalyzed Phosphoryl Transfer Reaction Observed On Cocrystalliza" 100.00 221 100.00 100.00 3.64e-156 PDB 1Z4N "Structure Of Beta-phosphoglucomutase With Inhibitor Bound Alpha-galactose 1-phosphate Cocrystallized With Fluoride" 100.00 221 100.00 100.00 3.64e-156 PDB 1Z4O "Structure Of Beta-Phosphoglucomutase With Inhibitor Bound Alpha-Galactose 1-Phosphate" 100.00 221 100.00 100.00 3.64e-156 PDB 1ZOL "Native Beta-Pgm" 100.00 221 100.00 100.00 3.64e-156 PDB 2WF5 "Structure Of Beta-Phosphoglucomutase Inhibited With Glucose- 6-Phospahte And Trifluoromagnesate" 100.00 221 100.00 100.00 3.64e-156 PDB 2WF6 "Structure Of Beta-Phosphoglucomutase Inhibited With Glucose- 6-Phospahte And Aluminium Tetrafluoride" 100.00 221 100.00 100.00 3.64e-156 PDB 2WF7 "Structure Of Beta-phosphoglucomutase Inhibited With Glucose- 6-phosphonate And Aluminium Tetrafluoride" 100.00 221 100.00 100.00 3.64e-156 PDB 2WF8 "Structure Of Beta-Phosphoglucomutase Inhibited With Glucose- 6-Phosphate, Glucose-1-Phosphate And Beryllium Trifluoride" 100.00 221 100.00 100.00 3.64e-156 PDB 2WF9 "Structure Of Beta-Phosphoglucomutase Inhibited With Glucose- 6-Phosphate, And Beryllium Trifluoride, Crystal Form 2" 100.00 221 100.00 100.00 3.64e-156 PDB 2WFA "Structure Of Beta-Phosphoglucomutase Inhibited With Beryllium Trifluoride, In An Open Conformation." 100.00 221 100.00 100.00 3.64e-156 PDB 2WHE "Structure Of Native Beta-Phosphoglucomutase In An Open Conformation Without Bound Ligands." 100.00 221 100.00 100.00 3.64e-156 PDB 3FM9 "Analysis Of The Structural Determinants Underlying Discrimination Between Substrate And Solvent In Beta- Phosphoglucomutase Cat" 100.00 221 99.55 99.55 7.13e-155 PDB 3ZI4 "The Structure Of Beta-phosphoglucomutase Inhibited With Glucose-6-phospahte And Scandium Tetrafluoride" 100.00 221 100.00 100.00 3.64e-156 PDB 4C4R "Structure Of Beta-phosphoglucomutase In Complex With A Phosphonate Analogue Of Beta-glucose-1-phosphate And Magnesium Trifluori" 100.00 221 100.00 100.00 3.64e-156 PDB 4C4S "Structure Of Beta-phosphoglucomutase In Complex With An Alpha-fluorophosphonate Analogue Of Beta-glucose-1-phosphate And Magnes" 100.00 221 100.00 100.00 3.64e-156 PDB 4C4T "Structure Of Beta-phosphoglucomutase In Complex With A Phosphonate Analogue Of Beta-glucose-1-phosphate And Aluminium Tetrafluo" 100.00 221 100.00 100.00 3.64e-156 DBJ BAL50396 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis IO-1]" 100.00 221 100.00 100.00 3.64e-156 DBJ GAM81375 "predicted phosphatase/phosphohexomutase [Lactococcus lactis subsp. lactis]" 100.00 221 100.00 100.00 3.64e-156 EMBL CAA94734 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 100.00 100.00 3.64e-156 EMBL CDG03643 "Beta-phosphoglucomutase [Lactococcus lactis subsp. lactis A12]" 100.00 221 99.55 99.55 4.86e-155 EMBL CDI46177 "Beta-phosphoglucomutase [Lactococcus lactis subsp. lactis Dephy 1]" 100.00 221 100.00 100.00 3.64e-156 GB AAK04527 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis Il1403]" 100.00 221 99.10 100.00 1.71e-154 GB ADA64250 "Beta-phosphoglucomutase [Lactococcus lactis subsp. lactis KF147]" 100.00 221 100.00 100.00 3.64e-156 GB ADZ63078 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis CV56]" 100.00 221 99.55 100.00 4.26e-155 GB AEE43918 "beta-phosphoglucomutase [synthetic construct]" 100.00 221 99.10 100.00 1.71e-154 GB AGY43735 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis KLDS 4.0325]" 100.00 221 98.64 100.00 3.76e-154 REF NP_266585 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis Il1403]" 100.00 221 99.10 100.00 1.71e-154 REF WP_003131530 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 99.55 100.00 4.26e-155 REF WP_010905331 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 99.10 100.00 1.71e-154 REF WP_012897250 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 100.00 100.00 3.64e-156 REF WP_021469610 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 99.55 99.55 5.98e-155 SP P71447 "RecName: Full=Beta-phosphoglucomutase; Short=Beta-PGM" 100.00 221 99.10 100.00 1.71e-154 stop_ save_ ############# # Ligands # ############# save_BEF _Saveframe_category ligand _Mol_type non-polymer _Name_common "BEF (BERYLLIUM TRIFLUORIDE ION)" _BMRB_code . _PDB_code BEF _Molecular_mass 66.007 _Mol_charge -1 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Aug 12 08:34:55 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons BE BE BE . -1 . ? F1 F1 F . 0 . ? F2 F2 F . 0 . ? F3 F3 F . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING BE F1 ? ? SING BE F2 ? ? SING BE F3 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_MG _Saveframe_category ligand _Mol_type non-polymer _Name_common "MG (MAGNESIUM ION)" _BMRB_code . _PDB_code MG _Molecular_mass 24.305 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Aug 12 08:29:29 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons MG MG MG . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $beta_phosphoglucomutase 'Lactococcus lactis' 1358 Bacteria . Lactococcus lactis stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $beta_phosphoglucomutase 'recombinant technology' . Escherichia coli 'BL21 (DE3)' pET-22b(+) stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'Sample used for backbone 1H, 15N, 13C assignment of trifluoroberyllate inhibited beta phosphoglucomutase' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $beta_phosphoglucomutase 1 mM '[U-13C; U-15N; U-2H]' 'magnesium chloride' 5 mM 'natural abundance' 'ammonium fluoride' 10 mM 'natural abundance' 'beryllium chloride' 5 mM 'natural abundance' 'sodium azide' 2 mM 'natural abundance' D2O 10 % '[U-100% 2H]' 'potassium HEPES' 50 mM 'natural abundance' H2O 90 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details 'Sample used for 19F assignment of trifluoroberyllate inhibited beta phosphoglucomutase' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $beta_phosphoglucomutase 0.5 mM 'natural abundance' 'magnesium chloride' 5 mM 'natural abundance' 'ammonium fluoride' 10 mM 'natural abundance' 'beryllium chloride' 5 mM 'natural abundance' 'sodium azide' 2 mM 'natural abundance' D2O 10 % '[U-100% 2H]' 'potassium HEPES' 50 mM 'natural abundance' H2O 90 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection 'data analysis' stop_ _Details . save_ save_Felix _Saveframe_category software _Name FELIX _Version . loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'Equipped with a 1H/13C/15N/2H TXI cryoprobe' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details 'Equipped with a 1H/13C/15N/19F QXI probe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $sample_1 save_ save_3D_TROSY_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCA' _Sample_label $sample_1 save_ save_3D_TROSY_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(CO)CA' _Sample_label $sample_1 save_ save_3D_TROSY_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(CA)CO' _Sample_label $sample_1 save_ save_3D_TROSY_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCO' _Sample_label $sample_1 save_ save_3D_TROSY_HN(CA)CB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(CA)CB' _Sample_label $sample_1 save_ save_3D_TROSY_HN(COCA)CB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(COCA)CB' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_19F_1D_9 _Saveframe_category NMR_applied_experiment _Experiment_name '19F 1D' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 70 . mM pH 7.2 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 0.00 na indirect . . . 0.251449530 DSS F 19 'methyl protons' ppm 0.000 na indirect . . . 0.9409400 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N TROSY' '3D TROSY HNCA' '3D TROSY HN(CO)CA' '3D TROSY HN(CA)CO' '3D TROSY HNCO' '3D TROSY HN(CA)CB' '3D TROSY HN(COCA)CB' '19F 1D' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'phosphoenzyme analogue' _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 2 PHE H H 5.231 0.005 1 2 2 2 PHE C C 173.904 0.050 1 3 2 2 PHE CA C 55.778 0.050 1 4 2 2 PHE CB C 36.063 0.050 1 5 2 2 PHE N N 117.296 0.050 1 6 3 3 LYS H H 8.732 0.005 1 7 3 3 LYS C C 176.586 0.050 1 8 3 3 LYS CA C 55.632 0.050 1 9 3 3 LYS CB C 35.657 0.050 1 10 3 3 LYS N N 116.391 0.050 1 11 4 4 ALA H H 7.628 0.005 1 12 4 4 ALA C C 175.338 0.050 1 13 4 4 ALA CA C 50.697 0.050 1 14 4 4 ALA CB C 22.541 0.050 1 15 4 4 ALA N N 121.211 0.050 1 16 5 5 VAL H H 8.687 0.005 1 17 5 5 VAL C C 172.815 0.050 1 18 5 5 VAL CA C 60.981 0.050 1 19 5 5 VAL CB C 32.806 0.050 1 20 5 5 VAL N N 120.034 0.050 1 21 6 6 LEU H H 9.340 0.005 1 22 6 6 LEU C C 175.482 0.050 1 23 6 6 LEU CA C 51.552 0.050 1 24 6 6 LEU CB C 40.002 0.050 1 25 6 6 LEU N N 126.265 0.050 1 26 7 7 PHE H H 9.654 0.005 1 27 7 7 PHE C C 177.506 0.050 1 28 7 7 PHE CA C 58.964 0.050 1 29 7 7 PHE CB C 40.380 0.050 1 30 7 7 PHE N N 122.965 0.050 1 31 8 8 ASP H H 7.426 0.005 1 32 8 8 ASP C C 172.866 0.050 1 33 8 8 ASP CA C 53.468 0.050 1 34 8 8 ASP CB C 43.163 0.050 1 35 8 8 ASP N N 121.834 0.050 1 36 9 9 LEU H H 7.246 0.005 1 37 9 9 LEU C C 177.947 0.050 1 38 9 9 LEU CA C 56.511 0.050 1 39 9 9 LEU CB C 43.408 0.050 1 40 9 9 LEU N N 119.065 0.050 1 41 10 10 ASP H H 8.789 0.005 1 42 10 10 ASP C C 175.959 0.050 1 43 10 10 ASP CA C 55.887 0.050 1 44 10 10 ASP CB C 40.244 0.050 1 45 10 10 ASP N N 124.237 0.050 1 46 11 11 GLY H H 9.845 0.005 1 47 11 11 GLY C C 171.706 0.050 1 48 11 11 GLY CA C 44.807 0.050 1 49 11 11 GLY N N 119.318 0.050 1 50 12 12 VAL H H 7.466 0.005 1 51 12 12 VAL C C 172.403 0.050 1 52 12 12 VAL CA C 64.105 0.050 1 53 12 12 VAL CB C 33.416 0.050 1 54 12 12 VAL N N 118.696 0.050 1 55 13 13 ILE H H 8.222 0.005 1 56 13 13 ILE C C 175.333 0.050 1 57 13 13 ILE CA C 63.472 0.050 1 58 13 13 ILE CB C 38.633 0.050 1 59 13 13 ILE N N 115.356 0.050 1 60 14 14 THR H H 7.259 0.005 1 61 14 14 THR C C 172.220 0.050 1 62 14 14 THR CA C 59.287 0.050 1 63 14 14 THR CB C 67.187 0.050 1 64 14 14 THR N N 109.768 0.050 1 65 15 15 ASP H H 8.278 0.005 1 66 15 15 ASP C C 176.109 0.050 1 67 15 15 ASP CA C 53.770 0.050 1 68 15 15 ASP CB C 43.166 0.050 1 69 15 15 ASP N N 120.230 0.050 1 70 16 16 THR H H 9.256 0.005 1 71 16 16 THR C C 176.059 0.050 1 72 16 16 THR CA C 60.515 0.050 1 73 16 16 THR CB C 68.538 0.050 1 74 16 16 THR N N 114.062 0.050 1 75 17 17 ALA H H 9.191 0.005 1 76 17 17 ALA C C 181.077 0.050 1 77 17 17 ALA CA C 56.303 0.050 1 78 17 17 ALA CB C 18.204 0.050 1 79 17 17 ALA N N 129.156 0.050 1 80 18 18 GLU H H 9.278 0.005 1 81 18 18 GLU C C 178.095 0.050 1 82 18 18 GLU CA C 58.335 0.050 1 83 18 18 GLU CB C 28.574 0.050 1 84 18 18 GLU N N 119.864 0.050 1 85 19 19 TYR H H 7.301 0.005 1 86 19 19 TYR C C 178.676 0.050 1 87 19 19 TYR CA C 60.722 0.050 1 88 19 19 TYR CB C 37.101 0.050 1 89 19 19 TYR N N 118.337 0.050 1 90 20 20 HIS H H 7.995 0.005 1 91 20 20 HIS C C 177.276 0.050 1 92 20 20 HIS CA C 61.639 0.050 1 93 20 20 HIS CB C 30.848 0.050 1 94 20 20 HIS N N 119.315 0.050 1 95 21 21 PHE H H 8.297 0.005 1 96 21 21 PHE C C 176.945 0.050 1 97 21 21 PHE CA C 60.115 0.050 1 98 21 21 PHE CB C 37.449 0.050 1 99 21 21 PHE N N 119.088 0.050 1 100 22 22 ARG H H 8.355 0.005 1 101 22 22 ARG C C 179.507 0.050 1 102 22 22 ARG CA C 59.264 0.050 1 103 22 22 ARG CB C 30.126 0.050 1 104 22 22 ARG N N 117.933 0.050 1 105 23 23 ALA H H 8.146 0.005 1 106 23 23 ALA C C 179.778 0.050 1 107 23 23 ALA CA C 55.256 0.050 1 108 23 23 ALA CB C 17.955 0.050 1 109 23 23 ALA N N 123.436 0.050 1 110 24 24 TRP H H 8.491 0.005 1 111 24 24 TRP C C 178.578 0.050 1 112 24 24 TRP CA C 59.248 0.050 1 113 24 24 TRP CB C 29.935 0.050 1 114 24 24 TRP N N 120.298 0.050 1 115 25 25 LYS H H 8.773 0.005 1 116 25 25 LYS C C 178.157 0.050 1 117 25 25 LYS CA C 59.590 0.050 1 118 25 25 LYS CB C 31.613 0.050 1 119 25 25 LYS N N 120.976 0.050 1 120 26 26 ALA H H 7.782 0.005 1 121 26 26 ALA C C 180.672 0.050 1 122 26 26 ALA CA C 54.145 0.050 1 123 26 26 ALA CB C 17.209 0.050 1 124 26 26 ALA N N 119.707 0.050 1 125 27 27 LEU H H 7.430 0.005 1 126 27 27 LEU C C 178.077 0.050 1 127 27 27 LEU CA C 57.093 0.050 1 128 27 27 LEU CB C 41.584 0.050 1 129 27 27 LEU N N 120.481 0.050 1 130 28 28 ALA H H 8.626 0.005 1 131 28 28 ALA C C 179.756 0.050 1 132 28 28 ALA CA C 55.033 0.050 1 133 28 28 ALA CB C 17.386 0.050 1 134 28 28 ALA N N 120.996 0.050 1 135 29 29 GLU H H 8.259 0.005 1 136 29 29 GLU C C 180.239 0.050 1 137 29 29 GLU CA C 58.725 0.050 1 138 29 29 GLU CB C 28.457 0.050 1 139 29 29 GLU N N 117.127 0.050 1 140 30 30 GLU H H 7.802 0.005 1 141 30 30 GLU C C 178.744 0.050 1 142 30 30 GLU CA C 58.855 0.050 1 143 30 30 GLU CB C 28.921 0.050 1 144 30 30 GLU N N 121.498 0.050 1 145 31 31 ILE H H 7.607 0.005 1 146 31 31 ILE C C 175.915 0.050 1 147 31 31 ILE CA C 60.944 0.050 1 148 31 31 ILE CB C 37.008 0.050 1 149 31 31 ILE N N 111.829 0.050 1 150 32 32 GLY H H 7.554 0.005 1 151 32 32 GLY C C 174.523 0.050 1 152 32 32 GLY CA C 45.962 0.050 1 153 32 32 GLY N N 109.764 0.050 1 154 33 33 ILE H H 8.241 0.005 1 155 33 33 ILE C C 175.014 0.050 1 156 33 33 ILE CA C 60.840 0.050 1 157 33 33 ILE CB C 38.474 0.050 1 158 33 33 ILE N N 122.527 0.050 1 159 34 34 ASN H H 8.500 0.005 1 160 34 34 ASN C C 175.124 0.050 1 161 34 34 ASN CA C 52.524 0.050 1 162 34 34 ASN CB C 39.531 0.050 1 163 34 34 ASN N N 126.277 0.050 1 164 35 35 GLY H H 7.888 0.005 1 165 35 35 GLY C C 174.155 0.050 1 166 35 35 GLY CA C 44.800 0.050 1 167 35 35 GLY N N 107.564 0.050 1 168 36 36 VAL H H 8.417 0.005 1 169 36 36 VAL C C 174.023 0.050 1 170 36 36 VAL CA C 62.338 0.050 1 171 36 36 VAL CB C 28.543 0.050 1 172 36 36 VAL N N 122.346 0.050 1 173 37 37 ASP H H 7.501 0.005 1 174 37 37 ASP C C 176.423 0.050 1 175 37 37 ASP CA C 51.478 0.050 1 176 37 37 ASP CB C 41.697 0.050 1 177 37 37 ASP N N 126.345 0.050 1 178 38 38 ARG H H 8.323 0.005 1 179 38 38 ARG C C 178.574 0.050 1 180 38 38 ARG CA C 59.280 0.050 1 181 38 38 ARG CB C 28.491 0.050 1 182 38 38 ARG N N 119.561 0.050 1 183 39 39 GLN H H 7.990 0.005 1 184 39 39 GLN C C 178.783 0.050 1 185 39 39 GLN CA C 58.483 0.050 1 186 39 39 GLN CB C 27.409 0.050 1 187 39 39 GLN N N 119.865 0.050 1 188 40 40 PHE H H 8.535 0.005 1 189 40 40 PHE C C 177.595 0.050 1 190 40 40 PHE CA C 61.140 0.050 1 191 40 40 PHE CB C 38.884 0.050 1 192 40 40 PHE N N 123.976 0.050 1 193 41 41 ASN H H 8.305 0.005 1 194 41 41 ASN C C 177.504 0.050 1 195 41 41 ASN CA C 56.053 0.050 1 196 41 41 ASN CB C 39.316 0.050 1 197 41 41 ASN N N 116.116 0.050 1 198 42 42 GLU H H 7.658 0.005 1 199 42 42 GLU C C 179.033 0.050 1 200 42 42 GLU CA C 58.710 0.050 1 201 42 42 GLU CB C 28.733 0.050 1 202 42 42 GLU N N 119.240 0.050 1 203 43 43 GLN H H 7.619 0.005 1 204 43 43 GLN C C 176.230 0.050 1 205 43 43 GLN CA C 56.241 0.050 1 206 43 43 GLN CB C 27.633 0.050 1 207 43 43 GLN N N 116.065 0.050 1 208 44 44 LEU H H 7.324 0.005 1 209 44 44 LEU C C 177.920 0.050 1 210 44 44 LEU CA C 53.899 0.050 1 211 44 44 LEU CB C 39.593 0.050 1 212 44 44 LEU N N 117.428 0.050 1 213 45 45 LYS H H 7.013 0.005 1 214 45 45 LYS C C 177.920 0.050 1 215 45 45 LYS CA C 58.128 0.050 1 216 45 45 LYS CB C 31.398 0.050 1 217 45 45 LYS N N 121.797 0.050 1 218 46 46 GLY H H 8.619 0.005 1 219 46 46 GLY C C 174.083 0.050 1 220 46 46 GLY CA C 45.340 0.050 1 221 46 46 GLY N N 112.859 0.050 1 222 47 47 VAL H H 7.417 0.005 1 223 47 47 VAL C C 176.377 0.050 1 224 47 47 VAL CA C 61.162 0.050 1 225 47 47 VAL CB C 31.709 0.050 1 226 47 47 VAL N N 120.483 0.050 1 227 48 48 SER H H 8.958 0.005 1 228 48 48 SER C C 175.738 0.050 1 229 48 48 SER CA C 58.125 0.050 1 230 48 48 SER CB C 64.434 0.050 1 231 48 48 SER N N 121.591 0.050 1 232 49 49 ARG C C 177.727 0.050 1 233 49 49 ARG CA C 59.475 0.050 1 234 49 49 ARG CB C 29.664 0.050 1 235 50 50 GLU H H 8.697 0.005 1 236 50 50 GLU C C 178.001 0.050 1 237 50 50 GLU CA C 60.670 0.050 1 238 50 50 GLU CB C 28.201 0.050 1 239 50 50 GLU N N 118.615 0.050 1 240 51 51 ASP H H 7.889 0.005 1 241 51 51 ASP C C 178.965 0.050 1 242 51 51 ASP CA C 56.403 0.050 1 243 51 51 ASP CB C 39.489 0.050 1 244 51 51 ASP N N 120.437 0.050 1 245 52 52 SER H H 8.261 0.005 1 246 52 52 SER C C 174.165 0.050 1 247 52 52 SER CA C 61.610 0.050 1 248 52 52 SER CB C 61.295 0.050 1 249 52 52 SER N N 119.021 0.050 1 250 53 53 LEU H H 7.807 0.005 1 251 53 53 LEU C C 178.194 0.050 1 252 53 53 LEU CA C 57.038 0.050 1 253 53 53 LEU CB C 39.305 0.050 1 254 53 53 LEU N N 122.355 0.050 1 255 54 54 GLN H H 8.077 0.005 1 256 54 54 GLN C C 177.162 0.050 1 257 54 54 GLN CA C 58.188 0.050 1 258 54 54 GLN CB C 28.175 0.050 1 259 54 54 GLN N N 117.862 0.050 1 260 55 55 LYS H H 7.540 0.005 1 261 55 55 LYS C C 179.557 0.050 1 262 55 55 LYS CA C 59.239 0.050 1 263 55 55 LYS CB C 31.441 0.050 1 264 55 55 LYS N N 117.940 0.050 1 265 56 56 ILE H H 7.483 0.005 1 266 56 56 ILE C C 177.407 0.050 1 267 56 56 ILE CA C 64.854 0.050 1 268 56 56 ILE CB C 37.215 0.050 1 269 56 56 ILE N N 120.420 0.050 1 270 57 57 LEU H H 8.279 0.005 1 271 57 57 LEU C C 180.819 0.050 1 272 57 57 LEU CA C 57.770 0.050 1 273 57 57 LEU CB C 38.947 0.050 1 274 57 57 LEU N N 119.624 0.050 1 275 58 58 ASP H H 8.632 0.005 1 276 58 58 ASP C C 179.452 0.050 1 277 58 58 ASP CA C 56.413 0.050 1 278 58 58 ASP CB C 39.560 0.050 1 279 58 58 ASP N N 119.398 0.050 1 280 59 59 LEU H H 7.676 0.005 1 281 59 59 LEU C C 178.316 0.050 1 282 59 59 LEU CA C 57.274 0.050 1 283 59 59 LEU CB C 40.880 0.050 1 284 59 59 LEU N N 122.703 0.050 1 285 60 60 ALA H H 7.141 0.005 1 286 60 60 ALA C C 175.997 0.050 1 287 60 60 ALA CA C 50.300 0.050 1 288 60 60 ALA CB C 20.137 0.050 1 289 60 60 ALA N N 119.054 0.050 1 290 61 61 ASP H H 7.826 0.005 1 291 61 61 ASP C C 174.705 0.050 1 292 61 61 ASP CA C 55.025 0.050 1 293 61 61 ASP CB C 39.412 0.050 1 294 61 61 ASP N N 120.456 0.050 1 295 62 62 LYS H H 7.777 0.005 1 296 62 62 LYS C C 175.494 0.050 1 297 62 62 LYS CA C 55.395 0.050 1 298 62 62 LYS CB C 33.207 0.050 1 299 62 62 LYS N N 118.552 0.050 1 300 63 63 LYS H H 8.470 0.005 1 301 63 63 LYS C C 176.330 0.050 1 302 63 63 LYS CA C 54.414 0.050 1 303 63 63 LYS CB C 32.256 0.050 1 304 63 63 LYS N N 126.743 0.050 1 305 64 64 VAL H H 8.399 0.005 1 306 64 64 VAL C C 175.798 0.050 1 307 64 64 VAL CA C 58.215 0.050 1 308 64 64 VAL CB C 34.443 0.050 1 309 64 64 VAL N N 116.524 0.050 1 310 65 65 SER H H 8.987 0.005 1 311 65 65 SER C C 174.622 0.050 1 312 65 65 SER CA C 57.047 0.050 1 313 65 65 SER CB C 64.780 0.050 1 314 65 65 SER N N 119.578 0.050 1 315 66 66 ALA H H 8.887 0.005 1 316 66 66 ALA C C 181.035 0.050 1 317 66 66 ALA CA C 55.048 0.050 1 318 66 66 ALA CB C 17.210 0.050 1 319 66 66 ALA N N 124.200 0.050 1 320 67 67 GLU H H 8.556 0.005 1 321 67 67 GLU C C 179.442 0.050 1 322 67 67 GLU CA C 59.392 0.050 1 323 67 67 GLU CB C 28.495 0.050 1 324 67 67 GLU N N 118.086 0.050 1 325 68 68 GLU H H 7.856 0.005 1 326 68 68 GLU C C 178.681 0.050 1 327 68 68 GLU CA C 58.637 0.050 1 328 68 68 GLU CB C 29.514 0.050 1 329 68 68 GLU N N 122.775 0.050 1 330 69 69 PHE H H 8.853 0.005 1 331 69 69 PHE C C 176.812 0.050 1 332 69 69 PHE CA C 62.001 0.050 1 333 69 69 PHE CB C 38.829 0.050 1 334 69 69 PHE N N 121.794 0.050 1 335 70 70 LYS H H 7.599 0.005 1 336 70 70 LYS C C 179.901 0.050 1 337 70 70 LYS CA C 59.183 0.050 1 338 70 70 LYS CB C 31.736 0.050 1 339 70 70 LYS N N 116.615 0.050 1 340 71 71 GLU H H 7.695 0.005 1 341 71 71 GLU C C 179.128 0.050 1 342 71 71 GLU CA C 58.632 0.050 1 343 71 71 GLU CB C 28.471 0.050 1 344 71 71 GLU N N 121.225 0.050 1 345 72 72 LEU H H 8.432 0.005 1 346 72 72 LEU C C 178.258 0.050 1 347 72 72 LEU CA C 57.441 0.050 1 348 72 72 LEU CB C 41.581 0.050 1 349 72 72 LEU N N 122.075 0.050 1 350 73 73 ALA H H 7.939 0.005 1 351 73 73 ALA C C 180.191 0.050 1 352 73 73 ALA CA C 55.068 0.050 1 353 73 73 ALA CB C 16.268 0.050 1 354 73 73 ALA N N 121.237 0.050 1 355 74 74 LYS H H 7.622 0.005 1 356 74 74 LYS C C 178.566 0.050 1 357 74 74 LYS CA C 59.142 0.050 1 358 74 74 LYS CB C 31.273 0.050 1 359 74 74 LYS N N 120.246 0.050 1 360 75 75 ARG H H 8.242 0.005 1 361 75 75 ARG C C 179.106 0.050 1 362 75 75 ARG CA C 58.836 0.050 1 363 75 75 ARG CB C 29.101 0.050 1 364 75 75 ARG N N 121.421 0.050 1 365 76 76 LYS H H 7.835 0.005 1 366 76 76 LYS C C 178.823 0.050 1 367 76 76 LYS CA C 60.304 0.050 1 368 76 76 LYS CB C 28.884 0.050 1 369 76 76 LYS N N 119.545 0.050 1 370 77 77 ASN H H 7.465 0.005 1 371 77 77 ASN C C 176.475 0.050 1 372 77 77 ASN CA C 56.527 0.050 1 373 77 77 ASN CB C 37.953 0.050 1 374 77 77 ASN N N 119.012 0.050 1 375 78 78 ASP H H 8.654 0.005 1 376 78 78 ASP C C 179.401 0.050 1 377 78 78 ASP CA C 56.950 0.050 1 378 78 78 ASP CB C 39.130 0.050 1 379 78 78 ASP N N 121.161 0.050 1 380 79 79 ASN H H 8.279 0.005 1 381 79 79 ASN C C 176.691 0.050 1 382 79 79 ASN CA C 54.962 0.050 1 383 79 79 ASN CB C 37.188 0.050 1 384 79 79 ASN N N 119.675 0.050 1 385 80 80 TYR H H 8.236 0.005 1 386 80 80 TYR C C 175.590 0.050 1 387 80 80 TYR CA C 61.922 0.050 1 388 80 80 TYR CB C 37.877 0.050 1 389 80 80 TYR N N 122.690 0.050 1 390 81 81 VAL H H 8.255 0.005 1 391 81 81 VAL C C 177.737 0.050 1 392 81 81 VAL CA C 65.713 0.050 1 393 81 81 VAL CB C 30.567 0.050 1 394 81 81 VAL N N 118.173 0.050 1 395 82 82 LYS H H 7.219 0.005 1 396 82 82 LYS C C 179.887 0.050 1 397 82 82 LYS CA C 58.527 0.050 1 398 82 82 LYS CB C 31.325 0.050 1 399 82 82 LYS N N 119.104 0.050 1 400 83 83 MET H H 8.157 0.005 1 401 83 83 MET C C 179.318 0.050 1 402 83 83 MET CA C 58.201 0.050 1 403 83 83 MET CB C 31.666 0.050 1 404 83 83 MET N N 119.826 0.050 1 405 84 84 ILE H H 7.715 0.005 1 406 84 84 ILE C C 176.348 0.050 1 407 84 84 ILE CA C 63.498 0.050 1 408 84 84 ILE CB C 35.777 0.050 1 409 84 84 ILE N N 111.143 0.050 1 410 85 85 GLN H H 7.041 0.005 1 411 85 85 GLN C C 176.274 0.050 1 412 85 85 GLN CA C 57.806 0.050 1 413 85 85 GLN CB C 27.579 0.050 1 414 85 85 GLN N N 119.226 0.050 1 415 86 86 ASP H H 7.287 0.005 1 416 86 86 ASP C C 177.050 0.050 1 417 86 86 ASP CA C 54.296 0.050 1 418 86 86 ASP CB C 40.819 0.050 1 419 86 86 ASP N N 114.615 0.050 1 420 87 87 VAL H H 7.036 0.005 1 421 87 87 VAL C C 173.808 0.050 1 422 87 87 VAL CA C 63.672 0.050 1 423 87 87 VAL CB C 30.036 0.050 1 424 87 87 VAL N N 124.692 0.050 1 425 88 88 SER H H 9.130 0.005 1 426 88 88 SER C C 173.917 0.050 1 427 88 88 SER CA C 57.260 0.050 1 428 88 88 SER CB C 65.430 0.050 1 429 88 88 SER N N 125.437 0.050 1 430 89 89 PRO C C 177.721 0.050 1 431 89 89 PRO CA C 64.849 0.050 1 432 89 89 PRO CB C 30.844 0.050 1 433 90 90 ALA H H 7.732 0.005 1 434 90 90 ALA C C 178.052 0.050 1 435 90 90 ALA CA C 53.310 0.050 1 436 90 90 ALA CB C 17.618 0.050 1 437 90 90 ALA N N 119.956 0.050 1 438 91 91 ASP H H 8.080 0.005 1 439 91 91 ASP C C 177.062 0.050 1 440 91 91 ASP CA C 55.366 0.050 1 441 91 91 ASP CB C 40.935 0.050 1 442 91 91 ASP N N 115.843 0.050 1 443 92 92 VAL H H 7.145 0.005 1 444 92 92 VAL C C 176.848 0.050 1 445 92 92 VAL CA C 63.611 0.050 1 446 92 92 VAL CB C 31.091 0.050 1 447 92 92 VAL N N 123.323 0.050 1 448 93 93 TYR H H 9.043 0.005 1 449 93 93 TYR C C 175.208 0.050 1 450 93 93 TYR CA C 54.198 0.050 1 451 93 93 TYR CB C 34.739 0.050 1 452 93 93 TYR N N 130.984 0.050 1 453 94 94 PRO C C 177.315 0.050 1 454 94 94 PRO CA C 63.184 0.050 1 455 94 94 PRO CB C 31.495 0.050 1 456 95 95 GLY H H 8.428 0.005 1 457 95 95 GLY C C 176.015 0.050 1 458 95 95 GLY CA C 45.790 0.050 1 459 95 95 GLY N N 111.519 0.050 1 460 96 96 ILE H H 7.107 0.005 1 461 96 96 ILE C C 176.897 0.050 1 462 96 96 ILE CA C 61.116 0.050 1 463 96 96 ILE CB C 33.916 0.050 1 464 96 96 ILE N N 121.639 0.050 1 465 97 97 LEU H H 8.819 0.005 1 466 97 97 LEU C C 177.900 0.050 1 467 97 97 LEU CA C 58.199 0.050 1 468 97 97 LEU CB C 40.291 0.050 1 469 97 97 LEU N N 121.394 0.050 1 470 98 98 GLN H H 8.673 0.005 1 471 98 98 GLN C C 177.398 0.050 1 472 98 98 GLN CA C 57.581 0.050 1 473 98 98 GLN CB C 27.681 0.050 1 474 98 98 GLN N N 117.830 0.050 1 475 99 99 LEU H H 7.771 0.005 1 476 99 99 LEU C C 178.486 0.050 1 477 99 99 LEU CA C 57.806 0.050 1 478 99 99 LEU CB C 39.882 0.050 1 479 99 99 LEU N N 119.672 0.050 1 480 100 100 LEU H H 8.275 0.005 1 481 100 100 LEU C C 178.931 0.050 1 482 100 100 LEU CA C 57.990 0.050 1 483 100 100 LEU CB C 39.519 0.050 1 484 100 100 LEU N N 119.367 0.050 1 485 101 101 LYS H H 7.896 0.005 1 486 101 101 LYS C C 180.270 0.050 1 487 101 101 LYS CA C 59.996 0.050 1 488 101 101 LYS CB C 32.011 0.050 1 489 101 101 LYS N N 117.883 0.050 1 490 102 102 ASP H H 8.733 0.005 1 491 102 102 ASP C C 179.778 0.050 1 492 102 102 ASP CA C 57.071 0.050 1 493 102 102 ASP CB C 39.593 0.050 1 494 102 102 ASP N N 122.768 0.050 1 495 103 103 LEU H H 9.314 0.005 1 496 103 103 LEU C C 179.066 0.050 1 497 103 103 LEU CA C 58.209 0.050 1 498 103 103 LEU CB C 40.082 0.050 1 499 103 103 LEU N N 123.771 0.050 1 500 104 104 ARG H H 8.317 0.005 1 501 104 104 ARG C C 181.839 0.050 1 502 104 104 ARG CA C 59.030 0.050 1 503 104 104 ARG CB C 28.663 0.050 1 504 104 104 ARG N N 120.326 0.050 1 505 105 105 SER H H 8.684 0.005 1 506 105 105 SER C C 175.161 0.050 1 507 105 105 SER CA C 61.155 0.050 1 508 105 105 SER CB C 62.291 0.050 1 509 105 105 SER N N 117.425 0.050 1 510 106 106 ASN H H 7.385 0.005 1 511 106 106 ASN C C 172.377 0.050 1 512 106 106 ASN CA C 53.660 0.050 1 513 106 106 ASN CB C 39.442 0.050 1 514 106 106 ASN N N 118.334 0.050 1 515 107 107 LYS H H 7.880 0.005 1 516 107 107 LYS C C 175.076 0.050 1 517 107 107 LYS CA C 56.852 0.050 1 518 107 107 LYS CB C 27.403 0.050 1 519 107 107 LYS N N 114.922 0.050 1 520 108 108 ILE H H 7.912 0.005 1 521 108 108 ILE C C 175.795 0.050 1 522 108 108 ILE CA C 59.833 0.050 1 523 108 108 ILE CB C 36.925 0.050 1 524 108 108 ILE N N 122.453 0.050 1 525 109 109 LYS H H 7.647 0.005 1 526 109 109 LYS C C 175.790 0.050 1 527 109 109 LYS CA C 54.873 0.050 1 528 109 109 LYS CB C 32.646 0.050 1 529 109 109 LYS N N 125.239 0.050 1 530 110 110 ILE H H 9.215 0.005 1 531 110 110 ILE C C 175.791 0.050 1 532 110 110 ILE CA C 60.971 0.050 1 533 110 110 ILE CB C 40.117 0.050 1 534 110 110 ILE N N 122.155 0.050 1 535 111 111 ALA H H 8.708 0.005 1 536 111 111 ALA C C 175.909 0.050 1 537 111 111 ALA CA C 49.020 0.050 1 538 111 111 ALA CB C 23.857 0.050 1 539 111 111 ALA N N 127.940 0.050 1 540 112 112 LEU H H 8.424 0.005 1 541 112 112 LEU C C 174.127 0.050 1 542 112 112 LEU CA C 53.575 0.050 1 543 112 112 LEU CB C 43.806 0.050 1 544 112 112 LEU N N 123.453 0.050 1 545 113 113 ALA H H 9.040 0.005 1 546 113 113 ALA C C 174.968 0.050 1 547 113 113 ALA CA C 49.441 0.050 1 548 113 113 ALA CB C 18.846 0.050 1 549 113 113 ALA N N 133.229 0.050 1 550 114 114 SER H H 8.227 0.005 1 551 114 114 SER C C 174.455 0.050 1 552 114 114 SER CA C 56.000 0.050 1 553 114 114 SER CB C 64.400 0.050 1 554 114 114 SER N N 114.700 0.050 1 555 115 115 ALA H H 8.508 0.005 1 556 115 115 ALA C C 177.325 0.050 1 557 115 115 ALA CA C 52.344 0.050 1 558 115 115 ALA CB C 19.060 0.050 1 559 115 115 ALA N N 126.385 0.050 1 560 116 116 SER H H 8.492 0.005 1 561 116 116 SER C C 177.318 0.050 1 562 116 116 SER CA C 57.226 0.050 1 563 116 116 SER CB C 63.557 0.050 1 564 116 116 SER N N 112.006 0.050 1 565 117 117 LYS H H 11.168 0.005 1 566 117 117 LYS N N 133.413 0.050 1 567 118 118 ASN C C 174.547 0.050 1 568 118 118 ASN CA C 52.933 0.050 1 569 118 118 ASN CB C 38.524 0.050 1 570 119 119 GLY H H 7.241 0.005 1 571 119 119 GLY C C 171.761 0.050 1 572 119 119 GLY CA C 48.216 0.050 1 573 119 119 GLY N N 105.627 0.050 1 574 120 120 PRO C C 179.098 0.050 1 575 120 120 PRO CA C 65.610 0.050 1 576 120 120 PRO CB C 30.613 0.050 1 577 121 121 PHE H H 7.639 0.005 1 578 121 121 PHE C C 177.320 0.050 1 579 121 121 PHE CA C 60.396 0.050 1 580 121 121 PHE CB C 38.712 0.050 1 581 121 121 PHE N N 119.791 0.050 1 582 122 122 LEU H H 8.158 0.005 1 583 122 122 LEU C C 178.679 0.050 1 584 122 122 LEU CA C 57.608 0.050 1 585 122 122 LEU CB C 40.586 0.050 1 586 122 122 LEU N N 119.737 0.050 1 587 123 123 LEU H H 8.291 0.005 1 588 123 123 LEU C C 178.939 0.050 1 589 123 123 LEU CA C 58.023 0.050 1 590 123 123 LEU CB C 40.322 0.050 1 591 123 123 LEU N N 117.432 0.050 1 592 124 124 GLU H H 7.532 0.005 1 593 124 124 GLU C C 180.798 0.050 1 594 124 124 GLU CA C 58.733 0.050 1 595 124 124 GLU CB C 27.987 0.050 1 596 124 124 GLU N N 121.252 0.050 1 597 125 125 ARG H H 7.977 0.005 1 598 125 125 ARG C C 178.360 0.050 1 599 125 125 ARG CA C 56.716 0.050 1 600 125 125 ARG CB C 28.400 0.050 1 601 125 125 ARG N N 120.910 0.050 1 602 126 126 MET H H 7.243 0.005 1 603 126 126 MET C C 173.600 0.050 1 604 126 126 MET CA C 55.974 0.050 1 605 126 126 MET CB C 32.556 0.050 1 606 126 126 MET N N 113.441 0.050 1 607 127 127 ASN H H 7.957 0.005 1 608 127 127 ASN C C 175.915 0.050 1 609 127 127 ASN CA C 53.459 0.050 1 610 127 127 ASN CB C 36.511 0.050 1 611 127 127 ASN N N 117.046 0.050 1 612 128 128 LEU H H 8.665 0.005 1 613 128 128 LEU C C 177.782 0.050 1 614 128 128 LEU CA C 53.623 0.050 1 615 128 128 LEU CB C 44.212 0.050 1 616 128 128 LEU N N 114.236 0.050 1 617 129 129 THR H H 7.359 0.005 1 618 129 129 THR C C 176.369 0.050 1 619 129 129 THR CA C 66.973 0.050 1 620 129 129 THR CB C 68.532 0.050 1 621 129 129 THR N N 115.965 0.050 1 622 130 130 GLY H H 8.552 0.005 1 623 130 130 GLY C C 174.851 0.050 1 624 130 130 GLY CA C 45.631 0.050 1 625 130 130 GLY N N 106.356 0.050 1 626 131 131 TYR H H 7.686 0.005 1 627 131 131 TYR C C 174.371 0.050 1 628 131 131 TYR CA C 59.490 0.050 1 629 131 131 TYR CB C 38.739 0.050 1 630 131 131 TYR N N 116.159 0.050 1 631 132 132 PHE H H 7.307 0.005 1 632 132 132 PHE C C 175.739 0.050 1 633 132 132 PHE CA C 58.328 0.050 1 634 132 132 PHE CB C 39.069 0.050 1 635 132 132 PHE N N 115.288 0.050 1 636 133 133 ASP H H 9.159 0.005 1 637 133 133 ASP C C 176.369 0.050 1 638 133 133 ASP CA C 56.538 0.050 1 639 133 133 ASP CB C 42.371 0.050 1 640 133 133 ASP N N 124.934 0.050 1 641 134 134 ALA H H 7.599 0.005 1 642 134 134 ALA C C 175.482 0.050 1 643 134 134 ALA CA C 51.761 0.050 1 644 134 134 ALA CB C 23.534 0.050 1 645 134 134 ALA N N 115.610 0.050 1 646 135 135 ILE H H 8.618 0.005 1 647 135 135 ILE C C 175.542 0.050 1 648 135 135 ILE CA C 60.424 0.050 1 649 135 135 ILE CB C 39.999 0.050 1 650 135 135 ILE N N 121.623 0.050 1 651 136 136 ALA H H 8.464 0.005 1 652 136 136 ALA C C 175.428 0.050 1 653 136 136 ALA CA C 51.347 0.050 1 654 136 136 ALA CB C 17.881 0.050 1 655 136 136 ALA N N 130.859 0.050 1 656 137 137 ASP H H 8.472 0.005 1 657 137 137 ASP C C 176.690 0.050 1 658 137 137 ASP CA C 50.617 0.050 1 659 137 137 ASP CB C 41.396 0.050 1 660 137 137 ASP N N 125.643 0.050 1 661 138 138 PRO C C 177.792 0.050 1 662 138 138 PRO CA C 63.688 0.050 1 663 138 138 PRO CB C 31.148 0.050 1 664 139 139 ALA H H 8.601 0.005 1 665 139 139 ALA C C 178.804 0.050 1 666 139 139 ALA CA C 52.807 0.050 1 667 139 139 ALA CB C 18.155 0.050 1 668 139 139 ALA N N 121.120 0.050 1 669 140 140 GLU H H 7.477 0.005 1 670 140 140 GLU C C 176.633 0.050 1 671 140 140 GLU CA C 55.463 0.050 1 672 140 140 GLU CB C 29.776 0.050 1 673 140 140 GLU N N 116.382 0.050 1 674 141 141 VAL H H 6.830 0.005 1 675 141 141 VAL C C 175.882 0.050 1 676 141 141 VAL CA C 59.686 0.050 1 677 141 141 VAL CB C 32.148 0.050 1 678 141 141 VAL N N 113.518 0.050 1 679 142 142 ALA H H 8.579 0.005 1 680 142 142 ALA C C 177.726 0.050 1 681 142 142 ALA CA C 53.576 0.050 1 682 142 142 ALA CB C 18.172 0.050 1 683 142 142 ALA N N 125.077 0.050 1 684 143 143 ALA H H 7.261 0.005 1 685 143 143 ALA C C 176.315 0.050 1 686 143 143 ALA CA C 50.848 0.050 1 687 143 143 ALA CB C 20.925 0.050 1 688 143 143 ALA N N 119.286 0.050 1 689 144 144 SER H H 8.414 0.005 1 690 144 144 SER C C 175.314 0.050 1 691 144 144 SER CA C 56.963 0.050 1 692 144 144 SER CB C 63.908 0.050 1 693 144 144 SER N N 117.880 0.050 1 694 145 145 LYS H H 8.617 0.005 1 695 145 145 LYS C C 175.644 0.050 1 696 145 145 LYS CA C 56.893 0.050 1 697 145 145 LYS CB C 30.930 0.050 1 698 145 145 LYS N N 125.493 0.050 1 699 146 146 PRO C C 175.999 0.050 1 700 146 146 PRO CA C 62.968 0.050 1 701 146 146 PRO CB C 35.306 0.050 1 702 147 147 ALA H H 9.093 0.005 1 703 147 147 ALA C C 178.149 0.050 1 704 147 147 ALA CA C 51.535 0.050 1 705 147 147 ALA CB C 16.980 0.050 1 706 147 147 ALA N N 132.324 0.050 1 707 148 148 PRO C C 177.219 0.050 1 708 148 148 PRO CA C 63.485 0.050 1 709 148 148 PRO CB C 32.140 0.050 1 710 149 149 ASP H H 9.363 0.005 1 711 149 149 ASP C C 178.052 0.050 1 712 149 149 ASP CA C 57.985 0.050 1 713 149 149 ASP CB C 38.971 0.050 1 714 149 149 ASP N N 120.801 0.050 1 715 150 150 ILE H H 9.741 0.005 1 716 150 150 ILE C C 175.551 0.050 1 717 150 150 ILE CA C 62.910 0.050 1 718 150 150 ILE CB C 37.336 0.050 1 719 150 150 ILE N N 120.232 0.050 1 720 151 151 PHE H H 7.231 0.005 1 721 151 151 PHE C C 177.665 0.050 1 722 151 151 PHE CA C 63.188 0.050 1 723 151 151 PHE CB C 38.270 0.050 1 724 151 151 PHE N N 121.228 0.050 1 725 152 152 ILE H H 7.743 0.005 1 726 152 152 ILE C C 177.774 0.050 1 727 152 152 ILE CA C 65.616 0.050 1 728 152 152 ILE CB C 37.422 0.050 1 729 152 152 ILE N N 120.625 0.050 1 730 153 153 ALA H H 8.345 0.005 1 731 153 153 ALA C C 180.873 0.050 1 732 153 153 ALA CA C 54.294 0.050 1 733 153 153 ALA CB C 17.386 0.050 1 734 153 153 ALA N N 120.399 0.050 1 735 154 154 ALA H H 7.784 0.005 1 736 154 154 ALA C C 176.654 0.050 1 737 154 154 ALA CA C 55.033 0.050 1 738 154 154 ALA CB C 17.707 0.050 1 739 154 154 ALA N N 122.194 0.050 1 740 155 155 ALA H H 7.585 0.005 1 741 155 155 ALA C C 179.666 0.050 1 742 155 155 ALA CA C 54.217 0.050 1 743 155 155 ALA CB C 16.151 0.050 1 744 155 155 ALA N N 118.496 0.050 1 745 156 156 HIS H H 8.414 0.005 1 746 156 156 HIS C C 179.673 0.050 1 747 156 156 HIS CA C 58.225 0.050 1 748 156 156 HIS CB C 28.986 0.050 1 749 156 156 HIS N N 116.917 0.050 1 750 157 157 ALA H H 8.213 0.005 1 751 157 157 ALA C C 179.285 0.050 1 752 157 157 ALA CA C 54.068 0.050 1 753 157 157 ALA CB C 17.704 0.050 1 754 157 157 ALA N N 121.904 0.050 1 755 158 158 VAL H H 7.192 0.005 1 756 158 158 VAL C C 175.537 0.050 1 757 158 158 VAL CA C 59.384 0.050 1 758 158 158 VAL CB C 30.448 0.050 1 759 158 158 VAL N N 107.581 0.050 1 760 159 159 GLY H H 7.746 0.005 1 761 159 159 GLY C C 174.598 0.050 1 762 159 159 GLY CA C 46.056 0.050 1 763 159 159 GLY N N 110.305 0.050 1 764 160 160 VAL H H 7.622 0.005 1 765 160 160 VAL C C 174.228 0.050 1 766 160 160 VAL CA C 58.897 0.050 1 767 160 160 VAL CB C 34.023 0.050 1 768 160 160 VAL N N 117.045 0.050 1 769 161 161 ALA H H 8.646 0.005 1 770 161 161 ALA C C 178.727 0.050 1 771 161 161 ALA CA C 49.575 0.050 1 772 161 161 ALA CB C 17.217 0.050 1 773 161 161 ALA N N 126.085 0.050 1 774 162 162 PRO C C 177.474 0.050 1 775 162 162 PRO CA C 65.626 0.050 1 776 162 162 PRO CB C 30.868 0.050 1 777 163 163 SER H H 7.724 0.005 1 778 163 163 SER C C 175.943 0.050 1 779 163 163 SER CA C 59.816 0.050 1 780 163 163 SER CB C 61.853 0.050 1 781 163 163 SER N N 106.983 0.050 1 782 164 164 GLU H H 7.803 0.005 1 783 164 164 GLU C C 174.746 0.050 1 784 164 164 GLU CA C 55.587 0.050 1 785 164 164 GLU CB C 29.302 0.050 1 786 164 164 GLU N N 121.896 0.050 1 787 165 165 SER H H 7.991 0.005 1 788 165 165 SER C C 172.091 0.050 1 789 165 165 SER CA C 57.441 0.050 1 790 165 165 SER CB C 65.224 0.050 1 791 165 165 SER N N 114.851 0.050 1 792 166 166 ILE H H 7.614 0.005 1 793 166 166 ILE C C 175.278 0.050 1 794 166 166 ILE CA C 58.868 0.050 1 795 166 166 ILE CB C 40.731 0.050 1 796 166 166 ILE N N 121.759 0.050 1 797 167 167 GLY H H 8.736 0.005 1 798 167 167 GLY C C 170.467 0.050 1 799 167 167 GLY CA C 43.343 0.050 1 800 167 167 GLY N N 112.672 0.050 1 801 168 168 LEU H H 7.791 0.005 1 802 168 168 LEU C C 175.636 0.050 1 803 168 168 LEU CA C 53.364 0.050 1 804 168 168 LEU CB C 40.995 0.050 1 805 168 168 LEU N N 123.391 0.050 1 806 169 169 GLU H H 6.838 0.005 1 807 169 169 GLU C C 173.741 0.050 1 808 169 169 GLU CA C 56.328 0.050 1 809 169 169 GLU CB C 39.062 0.050 1 810 169 169 GLU N N 123.576 0.050 1 811 170 170 ASP H H 8.550 0.005 1 812 170 170 ASP C C 174.692 0.050 1 813 170 170 ASP CA C 52.210 0.050 1 814 170 170 ASP CB C 42.545 0.050 1 815 170 170 ASP N N 114.730 0.050 1 816 171 171 SER H H 8.139 0.005 1 817 171 171 SER C C 174.223 0.050 1 818 171 171 SER CA C 55.800 0.050 1 819 171 171 SER CB C 67.053 0.050 1 820 171 171 SER N N 115.784 0.050 1 821 172 172 GLN H H 9.271 0.005 1 822 172 172 GLN C C 178.471 0.050 1 823 172 172 GLN CA C 59.861 0.050 1 824 172 172 GLN CB C 27.196 0.050 1 825 172 172 GLN N N 126.628 0.050 1 826 173 173 ALA H H 8.770 0.005 1 827 173 173 ALA C C 180.253 0.050 1 828 173 173 ALA CA C 53.993 0.050 1 829 173 173 ALA CB C 17.234 0.050 1 830 173 173 ALA N N 120.579 0.050 1 831 174 174 GLY H H 7.778 0.005 1 832 174 174 GLY C C 175.378 0.050 1 833 174 174 GLY CA C 46.108 0.050 1 834 174 174 GLY N N 106.198 0.050 1 835 175 175 ILE H H 8.319 0.005 1 836 175 175 ILE C C 177.788 0.050 1 837 175 175 ILE CA C 62.007 0.050 1 838 175 175 ILE CB C 34.462 0.050 1 839 175 175 ILE N N 123.424 0.050 1 840 176 176 GLN H H 8.027 0.005 1 841 176 176 GLN C C 176.956 0.050 1 842 176 176 GLN CA C 58.232 0.050 1 843 176 176 GLN CB C 27.399 0.050 1 844 176 176 GLN N N 120.698 0.050 1 845 177 177 ALA H H 7.642 0.005 1 846 177 177 ALA C C 179.618 0.050 1 847 177 177 ALA CA C 54.735 0.050 1 848 177 177 ALA CB C 19.142 0.050 1 849 177 177 ALA N N 122.432 0.050 1 850 178 178 ILE H H 7.894 0.005 1 851 178 178 ILE C C 180.568 0.050 1 852 178 178 ILE CA C 64.762 0.050 1 853 178 178 ILE CB C 36.483 0.050 1 854 178 178 ILE N N 117.671 0.050 1 855 179 179 LYS H H 8.615 0.005 1 856 179 179 LYS C C 180.989 0.050 1 857 179 179 LYS CA C 59.694 0.050 1 858 179 179 LYS CB C 31.826 0.050 1 859 179 179 LYS N N 121.110 0.050 1 860 180 180 ASP H H 8.560 0.005 1 861 180 180 ASP C C 177.320 0.050 1 862 180 180 ASP CA C 56.230 0.050 1 863 180 180 ASP CB C 38.648 0.050 1 864 180 180 ASP N N 118.976 0.050 1 865 181 181 SER H H 8.044 0.005 1 866 181 181 SER C C 173.814 0.050 1 867 181 181 SER CA C 60.326 0.050 1 868 181 181 SER CB C 64.339 0.050 1 869 181 181 SER N N 117.286 0.050 1 870 182 182 GLY H H 7.243 0.005 1 871 182 182 GLY C C 173.425 0.050 1 872 182 182 GLY CA C 44.178 0.050 1 873 182 182 GLY N N 109.117 0.050 1 874 183 183 ALA H H 7.143 0.005 1 875 183 183 ALA C C 174.807 0.050 1 876 183 183 ALA CA C 50.831 0.050 1 877 183 183 ALA CB C 19.613 0.050 1 878 183 183 ALA N N 124.338 0.050 1 879 184 184 LEU H H 8.083 0.005 1 880 184 184 LEU C C 174.863 0.050 1 881 184 184 LEU CA C 51.797 0.050 1 882 184 184 LEU CB C 43.296 0.050 1 883 184 184 LEU N N 122.794 0.050 1 884 185 185 PRO C C 176.423 0.050 1 885 185 185 PRO CA C 61.374 0.050 1 886 185 185 PRO CB C 31.846 0.050 1 887 186 186 ILE H H 8.276 0.005 1 888 186 186 ILE C C 178.574 0.050 1 889 186 186 ILE CA C 61.481 0.050 1 890 186 186 ILE CB C 38.179 0.050 1 891 186 186 ILE N N 119.415 0.050 1 892 187 187 GLY H H 8.893 0.005 1 893 187 187 GLY C C 171.037 0.050 1 894 187 187 GLY CA C 44.930 0.050 1 895 187 187 GLY N N 116.113 0.050 1 896 188 188 VAL H H 7.947 0.005 1 897 188 188 VAL C C 173.922 0.050 1 898 188 188 VAL CA C 57.237 0.050 1 899 188 188 VAL CB C 32.032 0.050 1 900 188 188 VAL N N 119.136 0.050 1 901 189 189 GLY H H 8.225 0.005 1 902 189 189 GLY C C 171.139 0.050 1 903 189 189 GLY CA C 44.188 0.050 1 904 189 189 GLY N N 113.522 0.050 1 905 190 190 ARG H H 8.613 0.005 1 906 190 190 ARG C C 175.949 0.050 1 907 190 190 ARG CA C 52.526 0.050 1 908 190 190 ARG CB C 30.221 0.050 1 909 190 190 ARG N N 121.116 0.050 1 910 191 191 PRO C C 178.740 0.050 1 911 191 191 PRO CA C 64.423 0.050 1 912 191 191 PRO CB C 30.964 0.050 1 913 192 192 GLU H H 9.652 0.005 1 914 192 192 GLU C C 176.815 0.050 1 915 192 192 GLU CA C 59.380 0.050 1 916 192 192 GLU CB C 27.749 0.050 1 917 192 192 GLU N N 118.934 0.050 1 918 193 193 ASP H H 7.113 0.005 1 919 193 193 ASP C C 176.837 0.050 1 920 193 193 ASP CA C 54.942 0.050 1 921 193 193 ASP CB C 41.815 0.050 1 922 193 193 ASP N N 115.469 0.050 1 923 194 194 LEU H H 7.530 0.005 1 924 194 194 LEU C C 176.192 0.050 1 925 194 194 LEU CA C 55.679 0.050 1 926 194 194 LEU CB C 42.812 0.050 1 927 194 194 LEU N N 117.054 0.050 1 928 195 195 GLY H H 7.996 0.005 1 929 195 195 GLY C C 172.697 0.050 1 930 195 195 GLY CA C 43.651 0.050 1 931 195 195 GLY N N 107.554 0.050 1 932 196 196 ASP H H 7.932 0.005 1 933 196 196 ASP C C 176.941 0.050 1 934 196 196 ASP CA C 53.785 0.050 1 935 196 196 ASP CB C 41.111 0.050 1 936 196 196 ASP N N 117.122 0.050 1 937 197 197 ASP H H 8.836 0.005 1 938 197 197 ASP C C 175.325 0.050 1 939 197 197 ASP CA C 53.477 0.050 1 940 197 197 ASP CB C 39.558 0.050 1 941 197 197 ASP N N 117.279 0.050 1 942 198 198 ILE H H 6.815 0.005 1 943 198 198 ILE C C 175.435 0.050 1 944 198 198 ILE CA C 58.125 0.050 1 945 198 198 ILE CB C 40.582 0.050 1 946 198 198 ILE N N 113.798 0.050 1 947 199 199 VAL H H 8.951 0.005 1 948 199 199 VAL C C 174.331 0.050 1 949 199 199 VAL CA C 63.686 0.050 1 950 199 199 VAL CB C 30.331 0.050 1 951 199 199 VAL N N 125.916 0.050 1 952 200 200 ILE H H 7.970 0.005 1 953 200 200 ILE C C 176.068 0.050 1 954 200 200 ILE CA C 58.194 0.050 1 955 200 200 ILE CB C 41.258 0.050 1 956 200 200 ILE N N 126.260 0.050 1 957 201 201 VAL H H 8.735 0.005 1 958 201 201 VAL C C 174.287 0.050 1 959 201 201 VAL CA C 56.189 0.050 1 960 201 201 VAL CB C 31.629 0.050 1 961 201 201 VAL N N 120.137 0.050 1 962 202 202 PRO C C 177.163 0.050 1 963 202 202 PRO CA C 63.726 0.050 1 964 202 202 PRO CB C 31.143 0.050 1 965 203 203 ASP H H 6.799 0.005 1 966 203 203 ASP C C 175.692 0.050 1 967 203 203 ASP CA C 53.123 0.050 1 968 203 203 ASP CB C 41.524 0.050 1 969 203 203 ASP N N 110.292 0.050 1 970 204 204 THR H H 8.206 0.005 1 971 204 204 THR C C 176.527 0.050 1 972 204 204 THR CA C 65.208 0.050 1 973 204 204 THR CB C 68.915 0.050 1 974 204 204 THR N N 109.177 0.050 1 975 205 205 SER H H 8.852 0.005 1 976 205 205 SER C C 175.689 0.050 1 977 205 205 SER CA C 61.203 0.050 1 978 205 205 SER CB C 61.969 0.050 1 979 205 205 SER N N 119.736 0.050 1 980 206 206 HIS H H 7.134 0.005 1 981 206 206 HIS C C 176.744 0.050 1 982 206 206 HIS CA C 56.743 0.050 1 983 206 206 HIS CB C 30.325 0.050 1 984 206 206 HIS N N 118.254 0.050 1 985 207 207 TYR H H 7.745 0.005 1 986 207 207 TYR C C 173.500 0.050 1 987 207 207 TYR CA C 54.211 0.050 1 988 207 207 TYR CB C 35.398 0.050 1 989 207 207 TYR N N 119.951 0.050 1 990 208 208 THR H H 7.324 0.005 1 991 208 208 THR C C 174.698 0.050 1 992 208 208 THR CA C 57.956 0.050 1 993 208 208 THR CB C 71.169 0.050 1 994 208 208 THR N N 114.637 0.050 1 995 209 209 LEU H H 9.480 0.005 1 996 209 209 LEU C C 177.837 0.050 1 997 209 209 LEU CA C 58.315 0.050 1 998 209 209 LEU CB C 39.822 0.050 1 999 209 209 LEU N N 125.200 0.050 1 1000 210 210 GLU H H 8.554 0.005 1 1001 210 210 GLU C C 178.821 0.050 1 1002 210 210 GLU CA C 59.482 0.050 1 1003 210 210 GLU CB C 28.573 0.050 1 1004 210 210 GLU N N 116.807 0.050 1 1005 211 211 PHE H H 8.155 0.005 1 1006 211 211 PHE C C 176.792 0.050 1 1007 211 211 PHE CA C 60.831 0.050 1 1008 211 211 PHE CB C 39.437 0.050 1 1009 211 211 PHE N N 122.349 0.050 1 1010 212 212 LEU H H 8.342 0.005 1 1011 212 212 LEU C C 179.046 0.050 1 1012 212 212 LEU CA C 58.929 0.050 1 1013 212 212 LEU CB C 39.886 0.050 1 1014 212 212 LEU N N 119.684 0.050 1 1015 213 213 LYS H H 8.365 0.005 1 1016 213 213 LYS C C 178.103 0.050 1 1017 213 213 LYS CA C 60.525 0.050 1 1018 213 213 LYS CB C 31.974 0.050 1 1019 213 213 LYS N N 116.331 0.050 1 1020 214 214 GLU H H 7.767 0.005 1 1021 214 214 GLU C C 179.569 0.050 1 1022 214 214 GLU CA C 59.075 0.050 1 1023 214 214 GLU CB C 28.721 0.050 1 1024 214 214 GLU N N 120.577 0.050 1 1025 215 215 VAL H H 8.208 0.005 1 1026 215 215 VAL C C 178.396 0.050 1 1027 215 215 VAL CA C 65.710 0.050 1 1028 215 215 VAL CB C 30.712 0.050 1 1029 215 215 VAL N N 120.431 0.050 1 1030 216 216 TRP H H 8.410 0.005 1 1031 216 216 TRP C C 178.619 0.050 1 1032 216 216 TRP CA C 60.551 0.050 1 1033 216 216 TRP CB C 28.985 0.050 1 1034 216 216 TRP N N 120.709 0.050 1 1035 217 217 LEU H H 8.165 0.005 1 1036 217 217 LEU C C 179.891 0.050 1 1037 217 217 LEU CA C 57.053 0.050 1 1038 217 217 LEU CB C 40.953 0.050 1 1039 217 217 LEU N N 117.151 0.050 1 1040 218 218 GLN H H 7.811 0.005 1 1041 218 218 GLN C C 177.725 0.050 1 1042 218 218 GLN CA C 57.158 0.050 1 1043 218 218 GLN CB C 27.986 0.050 1 1044 218 218 GLN N N 118.302 0.050 1 1045 219 219 LYS H H 7.507 0.005 1 1046 219 219 LYS C C 176.588 0.050 1 1047 219 219 LYS CA C 55.387 0.050 1 1048 219 219 LYS CB C 31.349 0.050 1 1049 219 219 LYS N N 117.953 0.050 1 1050 220 220 GLN H H 7.600 0.005 1 1051 220 220 GLN C C 175.078 0.050 1 1052 220 220 GLN CA C 55.145 0.050 1 1053 220 220 GLN CB C 27.837 0.050 1 1054 220 220 GLN N N 119.917 0.050 1 1055 221 221 LYS H H 7.524 0.005 1 1056 221 221 LYS C C 181.472 0.050 1 1057 221 221 LYS CA C 57.200 0.050 1 1058 221 221 LYS CB C 32.390 0.050 1 1059 221 221 LYS N N 127.494 0.050 1 stop_ save_ save_assigned_chem_shift_list_1_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N TROSY' '3D TROSY HNCA' '3D TROSY HN(CO)CA' '3D TROSY HN(CA)CO' '3D TROSY HNCO' '3D TROSY HN(CA)CB' '3D TROSY HN(COCA)CB' '19F 1D' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'BERYLLIUM TRIFLUORIDE ION' _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 1 1 BEF F1 F -150.21 0.050 1 2 2 1 BEF F2 F -151.56 0.050 1 3 3 1 BEF F3 F -178.70 0.050 1 stop_ save_