data_7235 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N, and 13C assignments for beta phosphoglucomutase in the open form ; _BMRB_accession_number 7235 _BMRB_flat_file_name bmr7235.str _Entry_type original _Submission_date 2006-07-13 _Accession_date 2006-07-14 _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 Waltho Jonathan P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 180 "13C chemical shifts" 568 "15N chemical shifts" 180 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-09-20 update author 'complete entry citation' 2006-09-08 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'A trojan horse transition state analogue generated by MgF3- formation in an enzyme active site' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16990434 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Baxter Nicola J. . 2 Olguin Luis F. . 3 Golicnik Marko . . 4 Feng Guoqiang . . 5 Hounslow Andrea M. . 6 Bermel Wolfgang . . 7 Blackburn G. Michael . 8 Hollfelder Florian . . 9 Waltho Jonathan P. . 10 Williams Nicholas H. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 103 _Journal_issue 40 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 14732 _Page_last 14737 _Year 2006 _Details 'The first three authors contributed equally to this publication' loop_ _Keyword 'active site' 'MgF3- transition state analogue' 'NOE directed docking of fluoride ions' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'beta phosphoglucomutase' _Enzyme_commission_number 5.4.2.6 loop_ _Mol_system_component_name _Mol_label 'beta phosphoglucomutase' $beta_phosphoglucomutase 'magnesium ion' $MG stop_ _System_molecular_weight 25000 _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function mutase stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_beta_phosphoglucomutase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'beta phosphoglucomutase' _Molecular_mass 25000 _Mol_thiol_state 'not present' loop_ _Biological_function 'inhibited mutase' stop_ _Details 'A single catalytic magnsium ion is present in the protein' ############################## # 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 2014-10-25 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 2.50e-156 BMRB 16409 beta_phosphoglucomutase 100.00 221 100.00 100.00 2.50e-156 BMRB 17851 beta_phosphoglucomutase 100.00 221 100.00 100.00 2.50e-156 BMRB 17852 beta_phosphoglucomutase 100.00 221 100.00 100.00 2.50e-156 BMRB 7234 beta_phosphoglucomutase 100.00 221 100.00 100.00 2.50e-156 PDB 1LVH "The Structure Of Phosphorylated Beta-phosphoglucomutase From Lactoccocus Lactis To 2.3 Angstrom Resolution" 100.00 221 99.55 99.55 2.13e-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 2.50e-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 2.50e-156 PDB 1Z4N "Structure Of Beta-phosphoglucomutase With Inhibitor Bound Alpha-galactose 1-phosphate Cocrystallized With Fluoride" 100.00 221 100.00 100.00 2.50e-156 PDB 1Z4O "Structure Of Beta-Phosphoglucomutase With Inhibitor Bound Alpha-Galactose 1-Phosphate" 100.00 221 100.00 100.00 2.50e-156 PDB 1ZOL "Native Beta-Pgm" 100.00 221 100.00 100.00 2.50e-156 PDB 2WF5 "Structure Of Beta-Phosphoglucomutase Inhibited With Glucose- 6-Phospahte And Trifluoromagnesate" 100.00 221 100.00 100.00 2.50e-156 PDB 2WF6 "Structure Of Beta-Phosphoglucomutase Inhibited With Glucose- 6-Phospahte And Aluminium Tetrafluoride" 100.00 221 100.00 100.00 2.50e-156 PDB 2WF7 "Structure Of Beta-phosphoglucomutase Inhibited With Glucose- 6-phosphonate And Aluminium Tetrafluoride" 100.00 221 100.00 100.00 2.50e-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 2.50e-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 2.50e-156 PDB 2WFA "Structure Of Beta-Phosphoglucomutase Inhibited With Beryllium Trifluoride, In An Open Conformation." 100.00 221 100.00 100.00 2.50e-156 PDB 2WHE "Structure Of Native Beta-Phosphoglucomutase In An Open Conformation Without Bound Ligands." 100.00 221 100.00 100.00 2.50e-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 4.90e-155 PDB 3ZI4 "The Structure Of Beta-phosphoglucomutase Inhibited With Glucose-6-phospahte And Scandium Tetrafluoride" 100.00 221 100.00 100.00 2.50e-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 2.50e-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 2.50e-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 2.50e-156 DBJ BAL50396 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis IO-1]" 100.00 221 100.00 100.00 2.50e-156 EMBL CAA94734 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 100.00 100.00 2.50e-156 EMBL CDG03643 "Beta-phosphoglucomutase [Lactococcus lactis subsp. lactis A12]" 100.00 221 99.55 99.55 3.34e-155 EMBL CDI46177 "Beta-phosphoglucomutase [Lactococcus lactis subsp. lactis Dephy 1]" 100.00 221 100.00 100.00 2.50e-156 GB AAK04527 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis Il1403]" 100.00 221 99.10 100.00 1.17e-154 GB ADA64250 "Beta-phosphoglucomutase [Lactococcus lactis subsp. lactis KF147]" 100.00 221 100.00 100.00 2.50e-156 GB ADZ63078 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis CV56]" 100.00 221 99.55 100.00 2.93e-155 GB AEE43918 "beta-phosphoglucomutase [synthetic construct]" 100.00 221 99.10 100.00 1.17e-154 GB AGY43735 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis KLDS 4.0325]" 100.00 221 98.64 100.00 2.58e-154 REF NP_266585 "beta-phosphoglucomutase [Lactococcus lactis subsp. lactis Il1403]" 100.00 221 99.10 100.00 1.17e-154 REF WP_003131530 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 99.55 100.00 2.93e-155 REF WP_010905331 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 99.10 100.00 1.17e-154 REF WP_012897250 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 100.00 100.00 2.50e-156 REF WP_021469610 "beta-phosphoglucomutase [Lactococcus lactis]" 100.00 221 99.55 99.55 4.11e-155 SP P71447 "RecName: Full=Beta-phosphoglucomutase; Short=Beta-PGM [Lactococcus lactis subsp. lactis Il1403]" 100.00 221 99.10 100.00 1.17e-154 stop_ save_ ############# # Ligands # ############# 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 Sep 23 14:26:06 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 _Strain $beta_phosphoglucomutase 'Lactococcus lactis' 1360 Eubacteria Metazoa Lactococcus lactis 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_type _Vector_name _Vendor_name $beta_phosphoglucomutase 'recombinant technology' 'E. coli' . . . plasmid . Novagen stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_open_2H15N13C _Saveframe_category sample _Sample_type solution _Details 'beta phosphoglucomutase open conformation' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $beta_phosphoglucomutase 1 mM '[U-2H; U-15N; U-13C]' 'magnesium chloride' 5 mM . 'ammonium fluoride' 10 mM . 'sodium azide' 2 mM . 'deuterium oxide' 15 % . 'protease inhibitor' 1 times . 'potassium HEPES' 50 mM . stop_ save_ ############################ # Computer software used # ############################ save_software_xwinnmr _Saveframe_category software _Name xwinnmr _Version . loop_ _Vendor _Address _Electronic_address 'Bruker BioSpin Ltd' ; Banner Lane Coventry CV4 9GH ; . stop_ loop_ _Task 'data acquisition' stop_ _Details 'software for data acquisition' save_ save_software_felix _Saveframe_category software _Name FELIX _Version 2004 loop_ _Vendor _Address _Electronic_address 'Accelrys Inc' ; San Diego CA USA ; . stop_ loop_ _Task 'data analysis' 'data processing' stop_ _Details 'software for data processing and analysis' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N TROSY' _Sample_label $sample_open_2H15N13C save_ save_TROSY_ct-HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY ct-HNCA' _Sample_label $sample_open_2H15N13C save_ save_TROSY_ct-HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY ct-HN(CO)CA' _Sample_label $sample_open_2H15N13C save_ save_TROSY_HN(CA)CB_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY HN(CA)CB' _Sample_label $sample_open_2H15N13C save_ save_TROSY_HN(COCA)CB_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY HN(COCA)CB' _Sample_label $sample_open_2H15N13C save_ save_TROSY_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY HN(CA)CO' _Sample_label $sample_open_2H15N13C save_ save_TROSY_HNCO_7 _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY HNCO' _Sample_label $sample_open_2H15N13C save_ save_{19F}1H,15N-HSQC_NOE_difference_8 _Saveframe_category NMR_applied_experiment _Experiment_name '{19F}1H,15N-HSQC NOE difference' _Sample_label $sample_open_2H15N13C save_ save_19F_1D_9 _Saveframe_category NMR_applied_experiment _Experiment_name '19F 1D' _Sample_label $sample_open_2H15N13C save_ save_15N_TROSY _Saveframe_category NMR_applied_experiment _Experiment_name '15N TROSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY_ct-HNCA _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY ct-HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY_ct-HN(CO)CA _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY ct-HN(CO)CA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY_HN(CA)CB _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY HN(CA)CB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY_HN(COCA)CB _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY HN(COCA)CB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY_HN(CA)CO _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY HN(CA)CO' _BMRB_pulse_sequence_accession_number . _Details . save_ save_TROSY_HNCO _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY HNCO' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.2 pH temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $citation_1 $citation_1 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $citation_1 $citation_1 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $citation_1 $citation_1 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_chem_shift_list_open _Saveframe_category assigned_chemical_shifts _Details 'beta phosphoglucomutase open conformation' loop_ _Software_label $software_xwinnmr $software_felix stop_ loop_ _Experiment_label '15N TROSY' 'TROSY ct-HNCA' 'TROSY ct-HN(CO)CA' 'TROSY HN(CA)CB' 'TROSY HN(COCA)CB' 'TROSY HN(CA)CO' 'TROSY HNCO' stop_ loop_ _Sample_label $sample_open_2H15N13C stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'beta phosphoglucomutase' _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 5.217 0.005 1 2 2 2 PHE C C 173.799 0.050 1 3 2 2 PHE CA C 55.869 0.050 1 4 2 2 PHE CB C 35.946 0.050 1 5 2 2 PHE N N 117.471 0.050 1 6 3 3 LYS H H 8.737 0.005 1 7 3 3 LYS C C 176.570 0.050 1 8 3 3 LYS CA C 55.575 0.050 1 9 3 3 LYS CB C 35.699 0.050 1 10 3 3 LYS N N 116.620 0.050 1 11 4 4 ALA H H 7.598 0.005 1 12 4 4 ALA C C 175.264 0.050 1 13 4 4 ALA CA C 50.684 0.050 1 14 4 4 ALA CB C 22.581 0.050 1 15 4 4 ALA N N 121.443 0.050 1 16 5 5 VAL H H 8.614 0.005 1 17 5 5 VAL C C 172.703 0.050 1 18 5 5 VAL CA C 60.949 0.050 1 19 5 5 VAL CB C 32.799 0.050 1 20 5 5 VAL N N 120.215 0.050 1 21 6 6 LEU H H 9.229 0.005 1 22 6 6 LEU C C 175.517 0.050 1 23 6 6 LEU CA C 51.747 0.050 1 24 6 6 LEU CB C 40.684 0.050 1 25 6 6 LEU N N 126.438 0.050 1 26 7 7 PHE H H 9.320 0.005 1 27 7 7 PHE C C 177.287 0.050 1 28 7 7 PHE N N 122.670 0.050 1 29 16 16 THR C C 176.132 0.050 1 30 16 16 THR CA C 60.847 0.050 1 31 16 16 THR CB C 68.634 0.050 1 32 17 17 ALA H H 8.929 0.005 1 33 17 17 ALA C C 180.905 0.050 1 34 17 17 ALA CA C 56.185 0.050 1 35 17 17 ALA CB C 18.216 0.050 1 36 17 17 ALA N N 129.140 0.050 1 37 18 18 GLU H H 9.140 0.005 1 38 18 18 GLU C C 178.173 0.050 1 39 18 18 GLU CA C 58.363 0.050 1 40 18 18 GLU CB C 28.550 0.050 1 41 18 18 GLU N N 120.129 0.050 1 42 19 19 TYR H H 7.258 0.005 1 43 19 19 TYR C C 178.655 0.050 1 44 19 19 TYR CA C 60.761 0.050 1 45 19 19 TYR CB C 37.194 0.050 1 46 19 19 TYR N N 118.409 0.050 1 47 20 20 HIS H H 7.925 0.005 1 48 20 20 HIS C C 177.270 0.050 1 49 20 20 HIS CA C 61.584 0.050 1 50 20 20 HIS CB C 30.816 0.050 1 51 20 20 HIS N N 119.397 0.050 1 52 21 21 PHE H H 8.304 0.005 1 53 21 21 PHE C C 176.933 0.050 1 54 21 21 PHE CA C 60.137 0.050 1 55 21 21 PHE CB C 37.510 0.050 1 56 21 21 PHE N N 119.399 0.050 1 57 22 22 ARG H H 8.334 0.005 1 58 22 22 ARG C C 179.493 0.050 1 59 22 22 ARG CA C 59.238 0.050 1 60 22 22 ARG CB C 30.078 0.050 1 61 22 22 ARG N N 118.149 0.050 1 62 23 23 ALA H H 8.106 0.005 1 63 23 23 ALA C C 179.701 0.050 1 64 23 23 ALA CA C 55.230 0.050 1 65 23 23 ALA CB C 17.889 0.050 1 66 23 23 ALA N N 123.604 0.050 1 67 24 24 TRP H H 8.437 0.005 1 68 24 24 TRP C C 178.582 0.050 1 69 24 24 TRP CA C 59.230 0.050 1 70 24 24 TRP CB C 29.845 0.050 1 71 24 24 TRP N N 120.388 0.050 1 72 25 25 LYS H H 8.753 0.005 1 73 25 25 LYS C C 178.140 0.050 1 74 25 25 LYS CA C 59.538 0.050 1 75 25 25 LYS CB C 31.517 0.050 1 76 25 25 LYS N N 121.200 0.050 1 77 26 26 ALA H H 7.745 0.005 1 78 26 26 ALA C C 180.635 0.050 1 79 26 26 ALA CA C 54.102 0.050 1 80 26 26 ALA CB C 17.188 0.050 1 81 26 26 ALA N N 119.883 0.050 1 82 27 27 LEU H H 7.392 0.005 1 83 27 27 LEU C C 178.039 0.050 1 84 27 27 LEU CA C 57.032 0.050 1 85 27 27 LEU CB C 41.505 0.050 1 86 27 27 LEU N N 120.639 0.050 1 87 28 28 ALA H H 8.592 0.005 1 88 28 28 ALA C C 179.702 0.050 1 89 28 28 ALA CA C 55.000 0.050 1 90 28 28 ALA CB C 17.367 0.050 1 91 28 28 ALA N N 121.237 0.050 1 92 29 29 GLU H H 8.211 0.005 1 93 29 29 GLU C C 180.182 0.050 1 94 29 29 GLU CA C 58.682 0.050 1 95 29 29 GLU CB C 28.457 0.050 1 96 29 29 GLU N N 117.270 0.050 1 97 30 30 GLU H H 7.772 0.005 1 98 30 30 GLU C C 178.736 0.050 1 99 30 30 GLU CA C 58.823 0.050 1 100 30 30 GLU CB C 28.915 0.050 1 101 30 30 GLU N N 121.668 0.050 1 102 31 31 ILE H H 7.585 0.005 1 103 31 31 ILE C C 175.889 0.050 1 104 31 31 ILE CA C 60.927 0.050 1 105 31 31 ILE CB C 36.992 0.050 1 106 31 31 ILE N N 112.023 0.050 1 107 32 32 GLY H H 7.520 0.005 1 108 32 32 GLY C C 174.517 0.050 1 109 32 32 GLY CA C 45.891 0.050 1 110 32 32 GLY N N 109.881 0.050 1 111 33 33 ILE H H 8.203 0.005 1 112 33 33 ILE C C 174.974 0.050 1 113 33 33 ILE CA C 60.806 0.050 1 114 33 33 ILE CB C 38.380 0.050 1 115 33 33 ILE N N 122.676 0.050 1 116 34 34 ASN H H 8.460 0.005 1 117 34 34 ASN C C 175.080 0.050 1 118 34 34 ASN CA C 52.517 0.050 1 119 34 34 ASN CB C 39.495 0.050 1 120 34 34 ASN N N 126.401 0.050 1 121 35 35 GLY H H 7.862 0.005 1 122 35 35 GLY C C 174.149 0.050 1 123 35 35 GLY CA C 44.777 0.050 1 124 35 35 GLY N N 107.791 0.050 1 125 36 36 VAL H H 8.379 0.005 1 126 36 36 VAL C C 174.003 0.050 1 127 36 36 VAL CA C 62.312 0.050 1 128 36 36 VAL CB C 28.477 0.050 1 129 36 36 VAL N N 122.451 0.050 1 130 37 37 ASP H H 7.475 0.005 1 131 37 37 ASP C C 176.401 0.050 1 132 37 37 ASP CA C 51.491 0.050 1 133 37 37 ASP N N 126.472 0.050 1 134 38 38 ARG C C 178.540 0.050 1 135 38 38 ARG CA C 59.221 0.050 1 136 38 38 ARG CB C 28.500 0.050 1 137 39 39 GLN H H 7.969 0.005 1 138 39 39 GLN C C 178.702 0.050 1 139 39 39 GLN CA C 58.408 0.050 1 140 39 39 GLN CB C 27.375 0.050 1 141 39 39 GLN N N 120.018 0.050 1 142 40 40 PHE H H 8.496 0.005 1 143 40 40 PHE C C 177.547 0.050 1 144 40 40 PHE CA C 61.060 0.050 1 145 40 40 PHE CB C 38.837 0.050 1 146 40 40 PHE N N 124.100 0.050 1 147 41 41 ASN H H 8.266 0.005 1 148 41 41 ASN C C 177.452 0.050 1 149 41 41 ASN CA C 55.996 0.050 1 150 41 41 ASN CB C 39.264 0.050 1 151 41 41 ASN N N 116.353 0.050 1 152 42 42 GLU H H 7.640 0.005 1 153 42 42 GLU C C 179.012 0.050 1 154 42 42 GLU CA C 58.642 0.050 1 155 42 42 GLU CB C 28.649 0.050 1 156 42 42 GLU N N 119.369 0.050 1 157 43 43 GLN H H 7.634 0.005 1 158 43 43 GLN N N 116.580 0.050 1 159 53 53 LEU C C 178.188 0.050 1 160 53 53 LEU CA C 57.018 0.050 1 161 53 53 LEU CB C 39.334 0.050 1 162 54 54 GLN H H 8.069 0.005 1 163 54 54 GLN C C 177.136 0.050 1 164 54 54 GLN CA C 58.143 0.050 1 165 54 54 GLN CB C 28.087 0.050 1 166 54 54 GLN N N 118.030 0.050 1 167 55 55 LYS H H 7.497 0.005 1 168 55 55 LYS C C 179.504 0.050 1 169 55 55 LYS CA C 59.136 0.050 1 170 55 55 LYS CB C 31.421 0.050 1 171 55 55 LYS N N 118.064 0.050 1 172 56 56 ILE H H 7.445 0.005 1 173 56 56 ILE C C 177.351 0.050 1 174 56 56 ILE CA C 64.789 0.050 1 175 56 56 ILE CB C 37.191 0.050 1 176 56 56 ILE N N 120.583 0.050 1 177 57 57 LEU H H 8.237 0.005 1 178 57 57 LEU C C 180.749 0.050 1 179 57 57 LEU CA C 57.706 0.050 1 180 57 57 LEU CB C 38.936 0.050 1 181 57 57 LEU N N 119.795 0.050 1 182 58 58 ASP H H 8.587 0.005 1 183 58 58 ASP C C 179.431 0.050 1 184 58 58 ASP CA C 56.379 0.050 1 185 58 58 ASP CB C 39.510 0.050 1 186 58 58 ASP N N 119.577 0.050 1 187 59 59 LEU H H 7.643 0.005 1 188 59 59 LEU C C 178.285 0.050 1 189 59 59 LEU CA C 57.235 0.050 1 190 59 59 LEU CB C 40.891 0.050 1 191 59 59 LEU N N 122.854 0.050 1 192 60 60 ALA H H 7.122 0.005 1 193 60 60 ALA C C 175.975 0.050 1 194 60 60 ALA CA C 50.297 0.050 1 195 60 60 ALA CB C 20.059 0.050 1 196 60 60 ALA N N 119.237 0.050 1 197 61 61 ASP H H 7.802 0.005 1 198 61 61 ASP C C 174.672 0.050 1 199 61 61 ASP CA C 54.944 0.050 1 200 61 61 ASP CB C 39.393 0.050 1 201 61 61 ASP N N 120.595 0.050 1 202 62 62 LYS H H 7.754 0.005 1 203 62 62 LYS C C 175.438 0.050 1 204 62 62 LYS CA C 55.333 0.050 1 205 62 62 LYS CB C 33.241 0.050 1 206 62 62 LYS N N 118.740 0.050 1 207 63 63 LYS H H 8.436 0.005 1 208 63 63 LYS C C 176.303 0.050 1 209 63 63 LYS CA C 54.397 0.050 1 210 63 63 LYS CB C 32.218 0.050 1 211 63 63 LYS N N 126.864 0.050 1 212 64 64 VAL H H 8.367 0.005 1 213 64 64 VAL C C 175.776 0.050 1 214 64 64 VAL CA C 58.192 0.050 1 215 64 64 VAL CB C 34.413 0.050 1 216 64 64 VAL N N 116.692 0.050 1 217 65 65 SER H H 8.952 0.005 1 218 65 65 SER C C 174.601 0.050 1 219 65 65 SER CA C 57.016 0.050 1 220 65 65 SER CB C 64.736 0.050 1 221 65 65 SER N N 119.752 0.050 1 222 66 66 ALA H H 8.855 0.005 1 223 66 66 ALA C C 181.013 0.050 1 224 66 66 ALA CA C 55.020 0.050 1 225 66 66 ALA CB C 17.215 0.050 1 226 66 66 ALA N N 124.363 0.050 1 227 67 67 GLU H H 8.524 0.005 1 228 67 67 GLU C C 179.432 0.050 1 229 67 67 GLU CA C 59.365 0.050 1 230 67 67 GLU CB C 28.439 0.050 1 231 67 67 GLU N N 118.273 0.050 1 232 68 68 GLU H H 7.824 0.005 1 233 68 68 GLU C C 178.665 0.050 1 234 68 68 GLU CA C 58.606 0.050 1 235 68 68 GLU CB C 29.497 0.050 1 236 68 68 GLU N N 122.928 0.050 1 237 69 69 PHE H H 8.819 0.005 1 238 69 69 PHE C C 176.779 0.050 1 239 69 69 PHE CA C 61.965 0.050 1 240 69 69 PHE CB C 38.807 0.050 1 241 69 69 PHE N N 121.967 0.050 1 242 70 70 LYS H H 7.562 0.005 1 243 70 70 LYS C C 179.864 0.050 1 244 70 70 LYS CA C 59.150 0.050 1 245 70 70 LYS CB C 31.719 0.050 1 246 70 70 LYS N N 116.790 0.050 1 247 71 71 GLU H H 7.659 0.005 1 248 71 71 GLU C C 179.102 0.050 1 249 71 71 GLU CA C 58.603 0.050 1 250 71 71 GLU CB C 28.407 0.050 1 251 71 71 GLU N N 121.366 0.050 1 252 72 72 LEU H H 8.396 0.005 1 253 72 72 LEU C C 178.239 0.050 1 254 72 72 LEU CA C 57.414 0.050 1 255 72 72 LEU CB C 41.551 0.050 1 256 72 72 LEU N N 122.227 0.050 1 257 73 73 ALA H H 7.916 0.005 1 258 73 73 ALA C C 180.214 0.050 1 259 73 73 ALA CA C 55.039 0.050 1 260 73 73 ALA CB C 16.255 0.050 1 261 73 73 ALA N N 121.424 0.050 1 262 74 74 LYS H H 7.585 0.005 1 263 74 74 LYS C C 178.557 0.050 1 264 74 74 LYS CA C 59.120 0.050 1 265 74 74 LYS CB C 31.221 0.050 1 266 74 74 LYS N N 120.448 0.050 1 267 75 75 ARG H H 8.200 0.005 1 268 75 75 ARG C C 179.081 0.050 1 269 75 75 ARG CA C 58.779 0.050 1 270 75 75 ARG CB C 29.078 0.050 1 271 75 75 ARG N N 121.561 0.050 1 272 76 76 LYS H H 7.822 0.005 1 273 76 76 LYS C C 178.762 0.050 1 274 76 76 LYS CA C 60.278 0.050 1 275 76 76 LYS CB C 28.896 0.050 1 276 76 76 LYS N N 119.813 0.050 1 277 77 77 ASN H H 7.441 0.005 1 278 77 77 ASN C C 176.501 0.050 1 279 77 77 ASN CA C 56.492 0.050 1 280 77 77 ASN CB C 37.891 0.050 1 281 77 77 ASN N N 119.216 0.050 1 282 78 78 ASP H H 8.599 0.005 1 283 78 78 ASP C C 179.363 0.050 1 284 78 78 ASP CA C 56.935 0.050 1 285 78 78 ASP CB C 39.136 0.050 1 286 78 78 ASP N N 121.358 0.050 1 287 79 79 ASN H H 8.262 0.005 1 288 79 79 ASN C C 176.683 0.050 1 289 79 79 ASN CA C 54.952 0.050 1 290 79 79 ASN CB C 37.194 0.050 1 291 79 79 ASN N N 119.849 0.050 1 292 80 80 TYR H H 8.203 0.005 1 293 80 80 TYR C C 175.611 0.050 1 294 80 80 TYR CA C 61.916 0.050 1 295 80 80 TYR CB C 38.017 0.050 1 296 80 80 TYR N N 122.907 0.050 1 297 81 81 VAL H H 8.202 0.005 1 298 81 81 VAL C C 177.743 0.050 1 299 81 81 VAL CA C 65.698 0.050 1 300 81 81 VAL CB C 30.576 0.050 1 301 81 81 VAL N N 118.384 0.050 1 302 82 82 LYS H H 7.198 0.005 1 303 82 82 LYS C C 179.856 0.050 1 304 82 82 LYS CA C 58.520 0.050 1 305 82 82 LYS CB C 31.282 0.050 1 306 82 82 LYS N N 119.213 0.050 1 307 83 83 MET H H 8.069 0.005 1 308 83 83 MET C C 179.288 0.050 1 309 83 83 MET CA C 58.095 0.050 1 310 83 83 MET CB C 31.659 0.050 1 311 83 83 MET N N 119.805 0.050 1 312 84 84 ILE H H 7.693 0.005 1 313 84 84 ILE C C 176.344 0.050 1 314 84 84 ILE CA C 63.350 0.050 1 315 84 84 ILE CB C 35.700 0.050 1 316 84 84 ILE N N 111.488 0.050 1 317 85 85 GLN H H 6.998 0.005 1 318 85 85 GLN C C 176.298 0.050 1 319 85 85 GLN CA C 57.709 0.050 1 320 85 85 GLN CB C 27.555 0.050 1 321 85 85 GLN N N 119.205 0.050 1 322 86 86 ASP H H 7.216 0.005 1 323 86 86 ASP C C 176.978 0.050 1 324 86 86 ASP CA C 54.194 0.050 1 325 86 86 ASP CB C 40.829 0.050 1 326 86 86 ASP N N 114.731 0.050 1 327 87 87 VAL H H 7.024 0.005 1 328 87 87 VAL C C 173.820 0.050 1 329 87 87 VAL CA C 63.575 0.050 1 330 87 87 VAL CB C 30.078 0.050 1 331 87 87 VAL N N 124.741 0.050 1 332 88 88 SER H H 9.098 0.005 1 333 88 88 SER C C 173.891 0.050 1 334 88 88 SER CA C 57.156 0.050 1 335 88 88 SER CB C 65.354 0.050 1 336 88 88 SER N N 125.588 0.050 1 337 89 89 PRO C C 177.697 0.050 1 338 89 89 PRO CA C 64.817 0.050 1 339 89 89 PRO CB C 30.843 0.050 1 340 90 90 ALA H H 7.698 0.005 1 341 90 90 ALA C C 178.022 0.050 1 342 90 90 ALA CA C 53.257 0.050 1 343 90 90 ALA CB C 17.573 0.050 1 344 90 90 ALA N N 120.152 0.050 1 345 91 91 ASP H H 8.042 0.005 1 346 91 91 ASP C C 177.063 0.050 1 347 91 91 ASP CA C 55.312 0.050 1 348 91 91 ASP CB C 40.947 0.050 1 349 91 91 ASP N N 115.887 0.050 1 350 92 92 VAL H H 7.126 0.005 1 351 92 92 VAL C C 176.820 0.050 1 352 92 92 VAL CA C 63.554 0.050 1 353 92 92 VAL CB C 31.105 0.050 1 354 92 92 VAL N N 123.827 0.050 1 355 93 93 TYR H H 8.920 0.005 1 356 93 93 TYR C C 175.253 0.050 1 357 93 93 TYR CA C 54.395 0.050 1 358 93 93 TYR CB C 34.707 0.050 1 359 93 93 TYR N N 131.203 0.050 1 360 94 94 PRO C C 177.284 0.050 1 361 94 94 PRO CA C 63.154 0.050 1 362 94 94 PRO CB C 31.482 0.050 1 363 95 95 GLY H H 8.398 0.005 1 364 95 95 GLY C C 175.906 0.050 1 365 95 95 GLY CA C 45.755 0.050 1 366 95 95 GLY N N 111.715 0.050 1 367 96 96 ILE H H 7.094 0.005 1 368 96 96 ILE C C 176.870 0.050 1 369 96 96 ILE CA C 61.055 0.050 1 370 96 96 ILE CB C 33.827 0.050 1 371 96 96 ILE N N 121.803 0.050 1 372 97 97 LEU H H 8.792 0.005 1 373 97 97 LEU C C 177.869 0.050 1 374 97 97 LEU CA C 58.185 0.050 1 375 97 97 LEU CB C 40.246 0.050 1 376 97 97 LEU N N 121.541 0.050 1 377 98 98 GLN H H 8.634 0.005 1 378 98 98 GLN C C 177.353 0.050 1 379 98 98 GLN CA C 57.553 0.050 1 380 98 98 GLN CB C 27.619 0.050 1 381 98 98 GLN N N 117.974 0.050 1 382 99 99 LEU H H 7.745 0.005 1 383 99 99 LEU C C 178.452 0.050 1 384 99 99 LEU CA C 57.776 0.050 1 385 99 99 LEU CB C 39.861 0.050 1 386 99 99 LEU N N 119.883 0.050 1 387 100 100 LEU H H 8.258 0.005 1 388 100 100 LEU C C 178.957 0.050 1 389 100 100 LEU CA C 57.849 0.050 1 390 100 100 LEU CB C 39.453 0.050 1 391 100 100 LEU N N 119.401 0.050 1 392 101 101 LYS H H 7.870 0.005 1 393 101 101 LYS C C 180.234 0.050 1 394 101 101 LYS CA C 59.934 0.050 1 395 101 101 LYS CB C 32.008 0.050 1 396 101 101 LYS N N 118.088 0.050 1 397 102 102 ASP H H 8.667 0.005 1 398 102 102 ASP C C 179.731 0.050 1 399 102 102 ASP CA C 57.041 0.050 1 400 102 102 ASP CB C 39.511 0.050 1 401 102 102 ASP N N 122.857 0.050 1 402 103 103 LEU H H 9.308 0.005 1 403 103 103 LEU C C 178.998 0.050 1 404 103 103 LEU CA C 58.208 0.050 1 405 103 103 LEU CB C 39.974 0.050 1 406 103 103 LEU N N 123.988 0.050 1 407 104 104 ARG H H 8.287 0.005 1 408 104 104 ARG C C 181.801 0.050 1 409 104 104 ARG CA C 59.034 0.050 1 410 104 104 ARG CB C 28.642 0.050 1 411 104 104 ARG N N 120.452 0.050 1 412 105 105 SER H H 8.636 0.005 1 413 105 105 SER C C 175.101 0.050 1 414 105 105 SER CA C 61.095 0.050 1 415 105 105 SER CB C 62.275 0.050 1 416 105 105 SER N N 117.553 0.050 1 417 106 106 ASN H H 7.366 0.005 1 418 106 106 ASN C C 172.348 0.050 1 419 106 106 ASN CA C 53.572 0.050 1 420 106 106 ASN CB C 39.423 0.050 1 421 106 106 ASN N N 118.532 0.050 1 422 107 107 LYS H H 7.850 0.005 1 423 107 107 LYS C C 175.053 0.050 1 424 107 107 LYS CA C 56.824 0.050 1 425 107 107 LYS CB C 27.384 0.050 1 426 107 107 LYS N N 115.093 0.050 1 427 108 108 ILE H H 7.905 0.005 1 428 108 108 ILE C C 175.722 0.050 1 429 108 108 ILE CA C 59.941 0.050 1 430 108 108 ILE CB C 36.973 0.050 1 431 108 108 ILE N N 122.696 0.050 1 432 109 109 LYS H H 7.650 0.005 1 433 109 109 LYS C C 175.755 0.050 1 434 109 109 LYS CA C 54.892 0.050 1 435 109 109 LYS CB C 32.653 0.050 1 436 109 109 LYS N N 125.432 0.050 1 437 110 110 ILE H H 9.230 0.005 1 438 110 110 ILE C C 175.779 0.050 1 439 110 110 ILE CA C 60.932 0.050 1 440 110 110 ILE CB C 40.042 0.050 1 441 110 110 ILE N N 122.546 0.050 1 442 111 111 ALA H H 8.718 0.005 1 443 111 111 ALA C C 176.213 0.050 1 444 111 111 ALA CA C 48.959 0.050 1 445 111 111 ALA CB C 23.567 0.050 1 446 111 111 ALA N N 128.008 0.050 1 447 112 112 LEU H H 8.402 0.005 1 448 112 112 LEU C C 174.067 0.050 1 449 112 112 LEU CA C 53.884 0.050 1 450 112 112 LEU CB C 42.734 0.050 1 451 112 112 LEU N N 123.535 0.050 1 452 113 113 ALA H H 9.220 0.005 1 453 113 113 ALA C C 173.568 0.050 1 454 113 113 ALA CA C 49.124 0.050 1 455 113 113 ALA CB C 18.482 0.050 1 456 113 113 ALA N N 134.731 0.050 1 457 118 118 ASN C C 174.688 0.050 1 458 118 118 ASN CA C 52.980 0.050 1 459 118 118 ASN CB C 38.582 0.050 1 460 119 119 GLY H H 7.398 0.005 1 461 119 119 GLY C C 172.060 0.050 1 462 119 119 GLY CA C 48.177 0.050 1 463 119 119 GLY N N 106.502 0.050 1 464 120 120 PRO C C 179.133 0.050 1 465 120 120 PRO CA C 65.484 0.050 1 466 120 120 PRO CB C 30.551 0.050 1 467 121 121 PHE H H 7.615 0.005 1 468 121 121 PHE C C 177.277 0.050 1 469 121 121 PHE CA C 60.322 0.050 1 470 121 121 PHE CB C 38.636 0.050 1 471 121 121 PHE N N 119.866 0.050 1 472 122 122 LEU H H 8.133 0.005 1 473 122 122 LEU C C 178.706 0.050 1 474 122 122 LEU CA C 57.666 0.050 1 475 122 122 LEU CB C 40.456 0.050 1 476 122 122 LEU N N 120.190 0.050 1 477 123 123 LEU H H 8.220 0.005 1 478 123 123 LEU C C 178.875 0.050 1 479 123 123 LEU CA C 58.065 0.050 1 480 123 123 LEU CB C 40.109 0.050 1 481 123 123 LEU N N 117.659 0.050 1 482 124 124 GLU H H 7.537 0.005 1 483 124 124 GLU C C 180.801 0.050 1 484 124 124 GLU CA C 58.670 0.050 1 485 124 124 GLU CB C 27.998 0.050 1 486 124 124 GLU N N 121.438 0.050 1 487 125 125 ARG H H 7.998 0.005 1 488 125 125 ARG C C 178.356 0.050 1 489 125 125 ARG CA C 56.677 0.050 1 490 125 125 ARG CB C 28.401 0.050 1 491 125 125 ARG N N 121.235 0.050 1 492 126 126 MET H H 7.242 0.005 1 493 126 126 MET C C 173.572 0.050 1 494 126 126 MET CA C 55.947 0.050 1 495 126 126 MET CB C 32.564 0.050 1 496 126 126 MET N N 113.653 0.050 1 497 127 127 ASN H H 7.928 0.005 1 498 127 127 ASN C C 175.801 0.050 1 499 127 127 ASN CA C 53.432 0.050 1 500 127 127 ASN CB C 36.522 0.050 1 501 127 127 ASN N N 117.215 0.050 1 502 128 128 LEU H H 8.664 0.005 1 503 128 128 LEU C C 177.808 0.050 1 504 128 128 LEU CA C 53.599 0.050 1 505 128 128 LEU CB C 44.109 0.050 1 506 128 128 LEU N N 114.319 0.050 1 507 129 129 THR H H 7.304 0.005 1 508 129 129 THR C C 176.264 0.050 1 509 129 129 THR CA C 66.956 0.050 1 510 129 129 THR CB C 68.558 0.050 1 511 129 129 THR N N 115.984 0.050 1 512 130 130 GLY H H 8.512 0.005 1 513 130 130 GLY C C 174.800 0.050 1 514 130 130 GLY CA C 45.586 0.050 1 515 130 130 GLY N N 106.444 0.050 1 516 131 131 TYR H H 7.677 0.005 1 517 131 131 TYR C C 174.492 0.050 1 518 131 131 TYR CA C 59.462 0.050 1 519 131 131 TYR CB C 38.779 0.050 1 520 131 131 TYR N N 116.334 0.050 1 521 132 132 PHE H H 7.291 0.005 1 522 132 132 PHE C C 175.733 0.050 1 523 132 132 PHE CA C 58.237 0.050 1 524 132 132 PHE CB C 39.016 0.050 1 525 132 132 PHE N N 115.590 0.050 1 526 133 133 ASP H H 9.057 0.005 1 527 133 133 ASP C C 176.353 0.050 1 528 133 133 ASP CA C 56.673 0.050 1 529 133 133 ASP CB C 42.291 0.050 1 530 133 133 ASP N N 125.258 0.050 1 531 134 134 ALA H H 7.600 0.005 1 532 134 134 ALA C C 175.291 0.050 1 533 134 134 ALA CA C 51.630 0.050 1 534 134 134 ALA CB C 23.378 0.050 1 535 134 134 ALA N N 115.683 0.050 1 536 135 135 ILE H H 8.570 0.005 1 537 135 135 ILE C C 175.462 0.050 1 538 135 135 ILE CA C 60.370 0.050 1 539 135 135 ILE CB C 39.869 0.050 1 540 135 135 ILE N N 121.956 0.050 1 541 136 136 ALA H H 8.449 0.005 1 542 136 136 ALA C C 175.624 0.050 1 543 136 136 ALA CA C 52.082 0.050 1 544 136 136 ALA CB C 17.745 0.050 1 545 136 136 ALA N N 130.873 0.050 1 546 137 137 ASP H H 8.420 0.005 1 547 137 137 ASP C C 176.200 0.050 1 548 137 137 ASP CA C 50.686 0.050 1 549 137 137 ASP CB C 41.148 0.050 1 550 137 137 ASP N N 124.055 0.050 1 551 138 138 PRO C C 177.983 0.050 1 552 138 138 PRO CA C 63.676 0.050 1 553 138 138 PRO CB C 31.365 0.050 1 554 139 139 ALA H H 8.404 0.005 1 555 139 139 ALA C C 178.975 0.050 1 556 139 139 ALA CA C 53.136 0.050 1 557 139 139 ALA CB C 17.941 0.050 1 558 139 139 ALA N N 121.254 0.050 1 559 140 140 GLU H H 7.581 0.005 1 560 140 140 GLU C C 176.098 0.050 1 561 140 140 GLU CA C 55.380 0.050 1 562 140 140 GLU CB C 29.575 0.050 1 563 140 140 GLU N N 116.390 0.050 1 564 142 142 ALA C C 177.671 0.050 1 565 142 142 ALA CA C 53.397 0.050 1 566 142 142 ALA CB C 18.188 0.050 1 567 143 143 ALA H H 7.237 0.005 1 568 143 143 ALA C C 176.256 0.050 1 569 143 143 ALA CA C 50.891 0.050 1 570 143 143 ALA CB C 20.765 0.050 1 571 143 143 ALA N N 119.706 0.050 1 572 144 144 SER H H 8.400 0.005 1 573 144 144 SER C C 175.323 0.050 1 574 144 144 SER CB C 63.597 0.050 1 575 144 144 SER N N 117.953 0.050 1 576 146 146 PRO C C 175.769 0.050 1 577 146 146 PRO CA C 62.944 0.050 1 578 146 146 PRO CB C 34.882 0.050 1 579 147 147 ALA H H 8.847 0.005 1 580 147 147 ALA C C 178.019 0.050 1 581 147 147 ALA CA C 51.526 0.050 1 582 147 147 ALA CB C 16.896 0.050 1 583 147 147 ALA N N 131.756 0.050 1 584 148 148 PRO C C 177.172 0.050 1 585 148 148 PRO CA C 63.462 0.050 1 586 148 148 PRO CB C 32.086 0.050 1 587 149 149 ASP H H 9.127 0.005 1 588 149 149 ASP C C 177.858 0.050 1 589 149 149 ASP CA C 57.890 0.050 1 590 149 149 ASP CB C 39.310 0.050 1 591 149 149 ASP N N 120.910 0.050 1 592 150 150 ILE H H 9.533 0.005 1 593 150 150 ILE C C 175.725 0.050 1 594 150 150 ILE CA C 63.242 0.050 1 595 150 150 ILE CB C 37.054 0.050 1 596 150 150 ILE N N 120.061 0.050 1 597 151 151 PHE H H 7.235 0.005 1 598 151 151 PHE C C 177.666 0.050 1 599 151 151 PHE CA C 63.054 0.050 1 600 151 151 PHE CB C 38.251 0.050 1 601 151 151 PHE N N 121.387 0.050 1 602 152 152 ILE H H 7.724 0.005 1 603 152 152 ILE C C 177.681 0.050 1 604 152 152 ILE CA C 65.594 0.050 1 605 152 152 ILE CB C 37.445 0.050 1 606 152 152 ILE N N 121.221 0.050 1 607 153 153 ALA H H 8.291 0.005 1 608 153 153 ALA C C 180.944 0.050 1 609 153 153 ALA CA C 54.247 0.050 1 610 153 153 ALA CB C 17.472 0.050 1 611 153 153 ALA N N 120.469 0.050 1 612 154 154 ALA H H 7.750 0.005 1 613 154 154 ALA C C 176.673 0.050 1 614 154 154 ALA CA C 54.921 0.050 1 615 154 154 ALA CB C 17.948 0.050 1 616 154 154 ALA N N 122.721 0.050 1 617 155 155 ALA H H 7.609 0.005 1 618 155 155 ALA C C 179.684 0.050 1 619 155 155 ALA CA C 54.338 0.050 1 620 155 155 ALA CB C 16.024 0.050 1 621 155 155 ALA N N 119.190 0.050 1 622 156 156 HIS H H 8.380 0.005 1 623 156 156 HIS C C 179.319 0.050 1 624 156 156 HIS CA C 57.929 0.050 1 625 156 156 HIS CB C 28.820 0.050 1 626 156 156 HIS N N 116.887 0.050 1 627 157 157 ALA H H 8.125 0.005 1 628 157 157 ALA C C 179.077 0.050 1 629 157 157 ALA CA C 54.069 0.050 1 630 157 157 ALA CB C 17.515 0.050 1 631 157 157 ALA N N 122.136 0.050 1 632 158 158 VAL H H 7.148 0.005 1 633 158 158 VAL C C 175.491 0.050 1 634 158 158 VAL CA C 59.447 0.050 1 635 158 158 VAL CB C 30.598 0.050 1 636 158 158 VAL N N 107.813 0.050 1 637 159 159 GLY H H 7.731 0.005 1 638 159 159 GLY C C 174.570 0.050 1 639 159 159 GLY CA C 46.054 0.050 1 640 159 159 GLY N N 110.444 0.050 1 641 160 160 VAL H H 7.572 0.005 1 642 160 160 VAL C C 174.255 0.050 1 643 160 160 VAL CA C 58.931 0.050 1 644 160 160 VAL CB C 34.032 0.050 1 645 160 160 VAL N N 117.392 0.050 1 646 161 161 ALA H H 8.627 0.005 1 647 161 161 ALA C C 178.661 0.050 1 648 161 161 ALA CA C 49.648 0.050 1 649 161 161 ALA CB C 17.129 0.050 1 650 161 161 ALA N N 126.771 0.050 1 651 162 162 PRO C C 177.451 0.050 1 652 162 162 PRO CA C 65.595 0.050 1 653 162 162 PRO CB C 30.826 0.050 1 654 163 163 SER H H 7.694 0.005 1 655 163 163 SER C C 175.930 0.050 1 656 163 163 SER CA C 59.785 0.050 1 657 163 163 SER CB C 61.812 0.050 1 658 163 163 SER N N 107.124 0.050 1 659 164 164 GLU H H 7.760 0.005 1 660 164 164 GLU C C 174.727 0.050 1 661 164 164 GLU CA C 55.498 0.050 1 662 164 164 GLU CB C 29.319 0.050 1 663 164 164 GLU N N 122.021 0.050 1 664 165 165 SER H H 7.962 0.005 1 665 165 165 SER C C 172.044 0.050 1 666 165 165 SER CA C 57.453 0.050 1 667 165 165 SER CB C 65.233 0.050 1 668 165 165 SER N N 115.132 0.050 1 669 166 166 ILE H H 7.624 0.005 1 670 166 166 ILE C C 175.300 0.050 1 671 166 166 ILE CA C 58.849 0.050 1 672 166 166 ILE CB C 40.772 0.050 1 673 166 166 ILE N N 121.983 0.050 1 674 167 167 GLY H H 8.639 0.005 1 675 167 167 GLY C C 170.382 0.050 1 676 167 167 GLY CA C 43.264 0.050 1 677 167 167 GLY N N 112.709 0.050 1 678 168 168 LEU H H 7.797 0.005 1 679 168 168 LEU C C 175.401 0.050 1 680 168 168 LEU CA C 53.434 0.050 1 681 168 168 LEU CB C 41.005 0.050 1 682 168 168 LEU N N 123.604 0.050 1 683 169 169 GLU H H 6.861 0.005 1 684 169 169 GLU C C 173.839 0.050 1 685 169 169 GLU CA C 56.504 0.050 1 686 169 169 GLU CB C 39.472 0.050 1 687 169 169 GLU N N 124.172 0.050 1 688 170 170 ASP H H 8.552 0.005 1 689 170 170 ASP C C 174.812 0.050 1 690 170 170 ASP CA C 55.168 0.050 1 691 170 170 ASP N N 115.616 0.050 1 692 172 172 GLN C C 178.341 0.050 1 693 172 172 GLN CA C 59.859 0.050 1 694 172 172 GLN CB C 27.146 0.050 1 695 173 173 ALA H H 8.782 0.005 1 696 173 173 ALA C C 180.293 0.050 1 697 173 173 ALA CA C 54.227 0.050 1 698 173 173 ALA CB C 17.359 0.050 1 699 173 173 ALA N N 120.825 0.050 1 700 174 174 GLY H H 7.718 0.005 1 701 174 174 GLY C C 175.024 0.050 1 702 174 174 GLY CA C 45.993 0.050 1 703 174 174 GLY N N 106.067 0.050 1 704 175 175 ILE H H 8.224 0.005 1 705 175 175 ILE C C 177.768 0.050 1 706 175 175 ILE CA C 62.154 0.050 1 707 175 175 ILE CB C 34.469 0.050 1 708 175 175 ILE N N 123.574 0.050 1 709 176 176 GLN H H 8.023 0.005 1 710 176 176 GLN C C 176.979 0.050 1 711 176 176 GLN CA C 58.242 0.050 1 712 176 176 GLN CB C 27.354 0.050 1 713 176 176 GLN N N 120.737 0.050 1 714 177 177 ALA H H 7.573 0.005 1 715 177 177 ALA C C 179.598 0.050 1 716 177 177 ALA CA C 54.706 0.050 1 717 177 177 ALA CB C 19.134 0.050 1 718 177 177 ALA N N 122.518 0.050 1 719 178 178 ILE H H 7.870 0.005 1 720 178 178 ILE C C 180.364 0.050 1 721 178 178 ILE CA C 64.742 0.050 1 722 178 178 ILE CB C 36.566 0.050 1 723 178 178 ILE N N 118.088 0.050 1 724 179 179 LYS H H 8.582 0.005 1 725 179 179 LYS C C 180.995 0.050 1 726 179 179 LYS CA C 59.568 0.050 1 727 179 179 LYS CB C 31.779 0.050 1 728 179 179 LYS N N 121.346 0.050 1 729 180 180 ASP H H 8.591 0.005 1 730 180 180 ASP C C 177.471 0.050 1 731 180 180 ASP CA C 56.286 0.050 1 732 180 180 ASP CB C 38.687 0.050 1 733 180 180 ASP N N 119.583 0.050 1 734 181 181 SER H H 8.000 0.005 1 735 181 181 SER C C 173.768 0.050 1 736 181 181 SER CA C 60.307 0.050 1 737 181 181 SER CB C 64.237 0.050 1 738 181 181 SER N N 117.351 0.050 1 739 182 182 GLY H H 7.270 0.005 1 740 182 182 GLY C C 173.308 0.050 1 741 182 182 GLY CA C 44.072 0.050 1 742 182 182 GLY N N 109.337 0.050 1 743 183 183 ALA H H 7.099 0.005 1 744 183 183 ALA C C 174.866 0.050 1 745 183 183 ALA CA C 50.795 0.050 1 746 183 183 ALA CB C 19.648 0.050 1 747 183 183 ALA N N 124.604 0.050 1 748 184 184 LEU H H 8.084 0.005 1 749 184 184 LEU C C 174.879 0.050 1 750 184 184 LEU CA C 51.671 0.050 1 751 184 184 LEU CB C 43.269 0.050 1 752 184 184 LEU N N 122.992 0.050 1 753 185 185 PRO C C 176.449 0.050 1 754 185 185 PRO CA C 61.180 0.050 1 755 185 185 PRO CB C 31.897 0.050 1 756 186 186 ILE H H 8.181 0.005 1 757 186 186 ILE C C 178.449 0.050 1 758 186 186 ILE CA C 61.441 0.050 1 759 186 186 ILE CB C 38.138 0.050 1 760 186 186 ILE N N 119.612 0.050 1 761 187 187 GLY H H 8.838 0.005 1 762 187 187 GLY C C 171.015 0.050 1 763 187 187 GLY CA C 44.920 0.050 1 764 187 187 GLY N N 116.075 0.050 1 765 188 188 VAL H H 7.812 0.005 1 766 188 188 VAL C C 173.955 0.050 1 767 188 188 VAL CA C 57.130 0.050 1 768 188 188 VAL CB C 31.986 0.050 1 769 188 188 VAL N N 118.992 0.050 1 770 189 189 GLY H H 8.265 0.005 1 771 189 189 GLY C C 171.058 0.050 1 772 189 189 GLY CA C 44.079 0.050 1 773 189 189 GLY N N 113.970 0.050 1 774 190 190 ARG H H 8.574 0.005 1 775 190 190 ARG C C 175.932 0.050 1 776 190 190 ARG CA C 52.523 0.050 1 777 190 190 ARG CB C 30.083 0.050 1 778 190 190 ARG N N 121.085 0.050 1 779 191 191 PRO C C 178.718 0.050 1 780 191 191 PRO CA C 64.433 0.050 1 781 191 191 PRO CB C 30.901 0.050 1 782 192 192 GLU H H 9.619 0.005 1 783 192 192 GLU C C 176.785 0.050 1 784 192 192 GLU CA C 59.327 0.050 1 785 192 192 GLU CB C 27.732 0.050 1 786 192 192 GLU N N 118.977 0.050 1 787 193 193 ASP H H 7.096 0.005 1 788 193 193 ASP C C 176.777 0.050 1 789 193 193 ASP CA C 54.874 0.050 1 790 193 193 ASP CB C 41.752 0.050 1 791 193 193 ASP N N 115.712 0.050 1 792 194 194 LEU H H 7.509 0.005 1 793 194 194 LEU C C 176.092 0.050 1 794 194 194 LEU CA C 55.773 0.050 1 795 194 194 LEU CB C 42.822 0.050 1 796 194 194 LEU N N 117.615 0.050 1 797 195 195 GLY H H 7.936 0.005 1 798 195 195 GLY C C 172.694 0.050 1 799 195 195 GLY CA C 43.638 0.050 1 800 195 195 GLY N N 107.452 0.050 1 801 196 196 ASP H H 7.896 0.005 1 802 196 196 ASP C C 176.899 0.050 1 803 196 196 ASP CA C 53.761 0.050 1 804 196 196 ASP CB C 41.181 0.050 1 805 196 196 ASP N N 117.201 0.050 1 806 197 197 ASP H H 8.761 0.005 1 807 197 197 ASP C C 175.256 0.050 1 808 197 197 ASP CA C 53.535 0.050 1 809 197 197 ASP CB C 39.539 0.050 1 810 197 197 ASP N N 117.531 0.050 1 811 198 198 ILE H H 6.821 0.005 1 812 198 198 ILE C C 175.340 0.050 1 813 198 198 ILE CA C 58.077 0.050 1 814 198 198 ILE CB C 40.362 0.050 1 815 198 198 ILE N N 114.503 0.050 1 816 199 199 VAL H H 8.940 0.005 1 817 199 199 VAL C C 174.303 0.050 1 818 199 199 VAL CA C 63.656 0.050 1 819 199 199 VAL CB C 30.311 0.050 1 820 199 199 VAL N N 126.231 0.050 1 821 200 200 ILE H H 7.922 0.005 1 822 200 200 ILE C C 176.043 0.050 1 823 200 200 ILE CA C 58.166 0.050 1 824 200 200 ILE CB C 41.184 0.050 1 825 200 200 ILE N N 126.075 0.050 1 826 201 201 VAL H H 8.667 0.005 1 827 201 201 VAL C C 174.346 0.050 1 828 201 201 VAL CA C 56.194 0.050 1 829 201 201 VAL CB C 31.662 0.050 1 830 201 201 VAL N N 119.921 0.050 1 831 202 202 PRO C C 177.137 0.050 1 832 202 202 PRO CA C 63.802 0.050 1 833 202 202 PRO CB C 31.192 0.050 1 834 203 203 ASP H H 6.755 0.005 1 835 203 203 ASP C C 175.753 0.050 1 836 203 203 ASP CA C 53.037 0.050 1 837 203 203 ASP CB C 41.502 0.050 1 838 203 203 ASP N N 110.324 0.050 1 839 204 204 THR H H 8.152 0.005 1 840 204 204 THR C C 176.498 0.050 1 841 204 204 THR CA C 65.228 0.050 1 842 204 204 THR CB C 68.839 0.050 1 843 204 204 THR N N 109.479 0.050 1 844 205 205 SER H H 8.753 0.005 1 845 205 205 SER C C 175.570 0.050 1 846 205 205 SER CA C 61.169 0.050 1 847 205 205 SER CB C 61.957 0.050 1 848 205 205 SER N N 119.616 0.050 1 849 206 206 HIS H H 7.164 0.005 1 850 206 206 HIS C C 176.611 0.050 1 851 206 206 HIS CA C 56.638 0.050 1 852 206 206 HIS CB C 30.073 0.050 1 853 206 206 HIS N N 118.278 0.050 1 854 207 207 TYR H H 7.718 0.005 1 855 207 207 TYR C C 173.474 0.050 1 856 207 207 TYR CA C 54.270 0.050 1 857 207 207 TYR CB C 35.380 0.050 1 858 207 207 TYR N N 120.477 0.050 1 859 208 208 THR H H 7.257 0.005 1 860 208 208 THR C C 174.652 0.050 1 861 208 208 THR CA C 57.859 0.050 1 862 208 208 THR CB C 71.095 0.050 1 863 208 208 THR N N 114.594 0.050 1 864 209 209 LEU H H 9.439 0.005 1 865 209 209 LEU C C 177.791 0.050 1 866 209 209 LEU CA C 58.245 0.050 1 867 209 209 LEU CB C 39.802 0.050 1 868 209 209 LEU N N 125.331 0.050 1 869 210 210 GLU H H 8.528 0.005 1 870 210 210 GLU C C 178.772 0.050 1 871 210 210 GLU CA C 59.453 0.050 1 872 210 210 GLU CB C 28.554 0.050 1 873 210 210 GLU N N 116.962 0.050 1 874 211 211 PHE H H 8.106 0.005 1 875 211 211 PHE C C 176.738 0.050 1 876 211 211 PHE CA C 60.831 0.050 1 877 211 211 PHE CB C 39.394 0.050 1 878 211 211 PHE N N 122.412 0.050 1 879 212 212 LEU H H 8.305 0.005 1 880 212 212 LEU C C 179.015 0.050 1 881 212 212 LEU CA C 58.858 0.050 1 882 212 212 LEU CB C 39.864 0.050 1 883 212 212 LEU N N 119.900 0.050 1 884 213 213 LYS H H 8.352 0.005 1 885 213 213 LYS C C 178.078 0.050 1 886 213 213 LYS CA C 60.496 0.050 1 887 213 213 LYS CB C 31.960 0.050 1 888 213 213 LYS N N 116.463 0.050 1 889 214 214 GLU H H 7.708 0.005 1 890 214 214 GLU C C 179.550 0.050 1 891 214 214 GLU CA C 59.045 0.050 1 892 214 214 GLU CB C 28.680 0.050 1 893 214 214 GLU N N 120.601 0.050 1 894 215 215 VAL H H 8.156 0.005 1 895 215 215 VAL C C 178.349 0.050 1 896 215 215 VAL CA C 65.663 0.050 1 897 215 215 VAL CB C 30.690 0.050 1 898 215 215 VAL N N 120.500 0.050 1 899 216 216 TRP H H 8.384 0.005 1 900 216 216 TRP C C 178.607 0.050 1 901 216 216 TRP CA C 60.518 0.050 1 902 216 216 TRP CB C 29.114 0.050 1 903 216 216 TRP N N 120.935 0.050 1 904 217 217 LEU H H 8.137 0.005 1 905 217 217 LEU C C 179.884 0.050 1 906 217 217 LEU CA C 57.020 0.050 1 907 217 217 LEU CB C 40.944 0.050 1 908 217 217 LEU N N 117.254 0.050 1 909 218 218 GLN H H 7.772 0.005 1 910 218 218 GLN C C 177.712 0.050 1 911 218 218 GLN CA C 57.144 0.050 1 912 218 218 GLN CB C 27.995 0.050 1 913 218 218 GLN N N 118.480 0.050 1 914 219 219 LYS H H 7.497 0.005 1 915 219 219 LYS C C 176.568 0.050 1 916 219 219 LYS CA C 55.353 0.050 1 917 219 219 LYS CB C 31.366 0.050 1 918 219 219 LYS N N 118.064 0.050 1 919 220 220 GLN H H 7.572 0.005 1 920 220 220 GLN C C 175.040 0.050 1 921 220 220 GLN CA C 55.096 0.050 1 922 220 220 GLN CB C 27.762 0.050 1 923 220 220 GLN N N 120.067 0.050 1 924 221 221 LYS H H 7.488 0.005 1 925 221 221 LYS C C 181.452 0.050 1 926 221 221 LYS CA C 57.213 0.050 1 927 221 221 LYS CB C 32.360 0.050 1 928 221 221 LYS N N 127.647 0.050 1 stop_ save_