data_6973 #Corrected using PDB structure: 1EJFB # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 12 R HA 4.79 2.00 # 49 H HA 3.64 5.58 # 56 F HA 3.35 4.23 # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 49 H CA 60.19 53.12 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 76 C CB 27.60 33.44 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 50 L N 111.48 123.26 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.01 -0.12 0.14 -0.04 -0.16 -0.01 # #bmr6973.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr6973.str file): #HA CA CB CO N HN #N/A +0.01 +0.01 -0.04 -0.16 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.12 +/-0.15 +/-0.15 +/-0.37 +/-0.06 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.698 0.946 0.993 0.663 0.818 0.785 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.154 0.640 0.782 0.696 1.907 0.286 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Human p23(1-119) ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Martinez-Yamout Maria A. . 2 Dyson H. Jane . stop_ _BMRB_accession_number 6973 _BMRB_flat_file_name bmr6973.str _Entry_type new _Submission_date 2006-02-07 _Accession_date 2006-02-08 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details "chemical shift assignments for p23(1-119) and p23(1-160)" loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 528 "13C chemical shifts" 373 "15N chemical shifts" 120 stop_ loop_ _Related_BMRB_accession_number _Relationship 6974 "human p23(1-160)" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Localization of sites of interaction between p23 and Hsp90 in solution ; _Citation_status published _Citation_type journal _PubMed_ID 16565516 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Martinez-Yamout Maria A. . 2 Venkitakrishnan Rani P. . 3 Preece Nicholas E. . 4 Kroon Gerard . . 5 Wright Peter E. . 6 Dyson H. Jane . stop_ _Journal_abbreviation "J. Biol. Chem." _Journal_volume ? _Journal_issue ? _Page_first ? _Page_last ? _Year 2006 save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name "human p23(1-119)" _Abbreviation_common "human p23(1-119)" loop_ _Mol_system_component_name _Mol_label "human p23(1-119)" $p23(1-119) stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state "all free" loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 "human p23(1-119)" stop_ loop_ _Biological_function co-chaperone stop_ save_ ######################## # Monomeric polymers # ######################## save_p23(1-119) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "p23 co-chaperone, structured domain" _Name_variant p23 _Abbreviation_common p23 _Mol_thiol_state "all free" loop_ _Biological_function co-chaperone stop_ ############################## # Polymer residue sequence # ############################## _Residue_count 119 _Mol_residue_sequence ; MQPASAKWYDRRDYVFIEFC VEDSKDVNVNFEKSKLTFSC LGGSDNFKHLNEIDLFHCID PNDSKHKRTDRSILCCLRKG ESGQSWPRLTKERAKLNWLS VDFNNWKDWEDDSDEDMSN ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLN 3 PRO 4 ALA 5 SER 6 ALA 7 LYS 8 TRP 9 TYR 10 ASP 11 ARG 12 ARG 13 ASP 14 TYR 15 VAL 16 PHE 17 ILE 18 GLU 19 PHE 20 CYS 21 VAL 22 GLU 23 ASP 24 SER 25 LYS 26 ASP 27 VAL 28 ASN 29 VAL 30 ASN 31 PHE 32 GLU 33 LYS 34 SER 35 LYS 36 LEU 37 THR 38 PHE 39 SER 40 CYS 41 LEU 42 GLY 43 GLY 44 SER 45 ASP 46 ASN 47 PHE 48 LYS 49 HIS 50 LEU 51 ASN 52 GLU 53 ILE 54 ASP 55 LEU 56 PHE 57 HIS 58 CYS 59 ILE 60 ASP 61 PRO 62 ASN 63 ASP 64 SER 65 LYS 66 HIS 67 LYS 68 ARG 69 THR 70 ASP 71 ARG 72 SER 73 ILE 74 LEU 75 CYS 76 CYS 77 LEU 78 ARG 79 LYS 80 GLY 81 GLU 82 SER 83 GLY 84 GLN 85 SER 86 TRP 87 PRO 88 ARG 89 LEU 90 THR 91 LYS 92 GLU 93 ARG 94 ALA 95 LYS 96 LEU 97 ASN 98 TRP 99 LEU 100 SER 101 VAL 102 ASP 103 PHE 104 ASN 105 ASN 106 TRP 107 LYS 108 ASP 109 TRP 110 GLU 111 ASP 112 ASP 113 SER 114 ASP 115 GLU 116 ASP 117 MET 118 SER 119 ASN stop_ _Sequence_homology_query_date 2006-06-22 _Sequence_homology_query_revised_last_date 2006-05-11 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 6974 "p23 co-chaperone, structured domain" 74.38 160 100 100 5e-69 PDB 1EJF "A Chain A, Crystal Structure Of The HumanCo-Chaperone P23" 95.20 125 100 100 5e-69 DBJ BAC36099.1 "unnamed protein product [Mus musculus]" 74.38 160 100 100 5e-69 DBJ BAC36854.1 "unnamed protein product [Mus musculus]" 74.38 160 100 100 5e-69 DBJ BAE40047.1 "unnamed protein product [Mus musculus]" 74.38 160 100 100 5e-69 DBJ BAE40169.1 "unnamed protein product [Mus musculus]" 74.38 160 100 100 5e-69 DBJ BAE40563.1 "unnamed protein product [Mus musculus]" 74.38 160 100 100 5e-69 EMBL CAI29639.1 "hypothetical protein [Pongo pygmaeus]" 74.38 160 100 100 5e-69 GenBank AAH03005.1 "Unactive progesterone receptor, 23 kD[Homo sapiens]" 74.38 160 100 100 5e-69 GenBank AAH03708.1 "Prostaglandin E synthase 3 (cytosolic)[Mus musculus]" 74.38 160 100 100 5e-69 GenBank AAH85264.1 "Prostaglandin E synthase 3 (cytosolic)[Mus musculus]" 74.38 160 100 100 5e-69 GenBank AAI03351.1 "Cytosolic prostaglandin E synthase [Bostaurus]" 74.38 160 100 100 5e-69 GenBank AAS89038.1 "cytosolic prostaglandin e synthase[Macaca fascicularis]" 74.38 160 100 100 5e-69 REF NP_001007807.2 "cytosolic prostaglandin E synthase[Bos taurus]" 74.38 160 100 100 5e-69 REF NP_006592.3 "unactive progesterone receptor, 23 kD[Homo sapiens]" 74.38 160 100 100 5e-69 REF NP_062740.1 "prostaglandin E synthase 3 (cytosolic)[Mus musculus]" 74.38 160 100 100 5e-69 REF XP_984731.1 "PREDICTED: similar to Prostaglandin Esynthase 3 (Cytosolic prostaglandin E2 synthase) (cPGES)(Telomerase-binding protein p23) (Hsp90 co-chaperone)(Progesterone receptor complex p23) (Sid 3177) [Musmusculus]" 74.38 160 100 100 5e-69 REF XP_848910.1 "PREDICTED: similar to unactiveprogesterone receptor, 23 kD [Canis familiaris]" 23.80 500 100 100 5e-69 SWISS-PROT Q15185 "TEBP_HUMAN Prostaglandin E synthase 3(Cytosolic prostaglandin E2 synthase) (cPGES)(Telomerase-binding protein p23) (Hsp90 co-chaperone)(Progesterone receptor complex p23)" 74.38 160 100 100 5e-69 SWISS-PROT Q9R0Q7 "TEBP_MOUSE Prostaglandin E synthase 3(Cytosolic prostaglandin E2 synthase) (cPGES)(Telomerase-binding protein p23) (Hsp90 co-chaperone)(Progesterone receptor complex p23) (Sid 3177)" 74.38 160 100 100 5e-69 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $p23(1-119) Human 9606 Eukaryota Metazoa Homo sapiens 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 $p23(1-119) "recombinant technology" "E. coli" Escherichia coli BL21(DE3) ? stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $p23(1-119) 3 mM 2.5 3.5 "[U-15N; U-13C]" Tris 10 mM 0.9 1.1 ? KCl 50 mM 45 55 ? MgCl2 8 mM 7 9 ? DTT 2 mM 1.5 2.5 ? stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 600 _Details ? save_ save_800MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 800 save_ save_900MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 900 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; HNCA HNCO CBCA(CO)NH HNCACB HCA(CO)CANH 3D 15N TOCSY 3D 15N NOESY 3D HCCH-COSY ; save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.1 pH temperature 293 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Saveframe_category chemical_shift_reference loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 "methyl protons" ppm 0.0 internal direct ? ? ? 1.0 DSS C 13 "methyl protons" ppm 0.0 . indirect ? ? ? 0.251449530 DSS N 15 "methyl protons" ppm 0.0 . indirect ? ? ? 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 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) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name "human p23(1-119)" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 MET HA H 3.74 0.05 . 2 1 MET HB2 H 1.89 0.05 . 3 1 MET HB3 H 1.85 0.05 . 4 1 MET HG2 H 2.45 0.05 . 5 1 MET HE H 2.04 0.05 . 6 1 MET CB C 34.01 0.05 . 7 1 MET CG C 31.48 0.05 . 8 1 MET CE C 17.26 0.05 . 9 2 GLN HA H 4.96 0.05 . 10 2 GLN HB2 H 2.17 0.05 . 11 2 GLN HB3 H 1.99 0.05 . 12 2 GLN CA C 53.59 0.05 . 13 2 GLN CB C 31.01 0.05 . 14 3 PRO HA H 4.29 0.05 . 15 3 PRO HB2 H 1.25 0.05 . 16 3 PRO HB3 H 0.76 0.05 . 17 3 PRO HG2 H 1.97 0.05 . 18 3 PRO HG3 H 2.03 0.05 . 19 3 PRO HD2 H 3.80 0.05 . 20 3 PRO HD3 H 3.77 0.05 . 21 3 PRO CA C 62.76 0.05 . 22 3 PRO CB C 31.22 0.05 . 23 3 PRO CG C 28.14 0.05 . 24 3 PRO CD C 50.60 0.05 . 25 4 ALA H H 9.61 0.05 . 26 4 ALA HA H 4.15 0.05 . 27 4 ALA HB H 1.02 0.05 . 28 4 ALA C C 177.70 0.05 . 29 4 ALA CA C 51.44 0.05 . 30 4 ALA CB C 19.62 0.05 . 31 4 ALA N N 127.52 0.05 . 32 5 SER H H 8.68 0.05 . 33 5 SER HA H 5.29 0.05 . 34 5 SER HB2 H 4.07 0.05 . 35 5 SER HB3 H 3.94 0.05 . 36 5 SER C C 173.76 0.05 . 37 5 SER CA C 59.58 0.05 . 38 5 SER CB C 63.82 0.05 . 39 5 SER N N 115.76 0.05 . 40 6 ALA H H 9.61 0.05 . 41 6 ALA HA H 5.82 0.05 . 42 6 ALA HB H 1.21 0.05 . 43 6 ALA C C 176.38 0.05 . 44 6 ALA CA C 50.49 0.05 . 45 6 ALA CB C 24.83 0.05 . 46 6 ALA N N 125.31 0.05 . 47 7 LYS H H 8.79 0.05 . 48 7 LYS HA H 6.17 0.05 . 49 7 LYS HB2 H 1.64 0.05 . 50 7 LYS HB3 H 1.71 0.05 . 51 7 LYS HG2 H 1.43 0.05 . 52 7 LYS HG3 H 1.39 0.05 . 53 7 LYS C C 175.58 0.05 . 54 7 LYS CA C 53.52 0.05 . 55 7 LYS CB C 36.38 0.05 . 56 7 LYS N N 119.33 0.05 . 57 8 TRP H H 8.41 0.05 . 58 8 TRP HA H 6.13 0.05 . 59 8 TRP HB2 H 4.00 0.05 . 60 8 TRP HB3 H 2.76 0.05 . 61 8 TRP HE1 H 10.27 0.05 . 62 8 TRP C C 173.51 0.05 . 63 8 TRP CA C 55.60 0.05 . 64 8 TRP CB C 33.61 0.05 . 65 8 TRP N N 119.01 0.05 . 66 8 TRP NE1 N 130.10 0.05 . 67 9 TYR H H 9.01 0.05 . 68 9 TYR HA H 4.29 0.05 . 69 9 TYR HB2 H 3.42 0.05 . 70 9 TYR HB3 H 2.82 0.05 . 71 9 TYR C C 171.77 0.05 . 72 9 TYR CA C 57.41 0.05 . 73 9 TYR CB C 37.77 0.05 . 74 9 TYR N N 113.45 0.05 . 75 10 ASP H H 7.65 0.05 . 76 10 ASP HA H 5.38 0.05 . 77 10 ASP HB2 H 2.96 0.05 . 78 10 ASP HB3 H 2.60 0.05 . 79 10 ASP C C 175.52 0.05 . 80 10 ASP CA C 53.26 0.05 . 81 10 ASP CB C 45.90 0.05 . 82 10 ASP N N 118.16 0.05 . 83 11 ARG H H 8.66 0.05 . 84 11 ARG HA H 4.10 0.05 . 85 11 ARG HB2 H 2.11 0.05 . 86 11 ARG HB3 H 1.86 0.05 . 87 11 ARG C C 174.14 0.05 . 88 11 ARG CA C 52.65 0.05 . 89 11 ARG CB C 33.96 0.05 . 90 11 ARG N N 124.11 0.05 . 91 12 ARG H H 7.95 0.05 . 92 12 ARG HA H 4.78 0.05 . 93 12 ARG HB2 H 1.39 0.05 . 94 12 ARG CA C 60.53 0.05 . 95 12 ARG CB C 30.43 0.05 . 96 12 ARG N N 121.60 0.05 . 97 13 ASP H H 8.44 0.05 . 98 13 ASP HA H 4.76 0.05 . 99 13 ASP HB2 H 2.28 0.05 . 100 13 ASP C C 175.20 0.05 . 101 13 ASP CA C 54.12 0.05 . 102 13 ASP CB C 42.79 0.05 . 103 13 ASP N N 110.67 0.05 . 104 14 TYR H H 6.54 0.05 . 105 14 TYR HA H 5.28 0.05 . 106 14 TYR HB2 H 2.06 0.05 . 107 14 TYR HD1 H 6.69 0.05 . 108 14 TYR C C 172.87 0.05 . 109 14 TYR CA C 56.46 0.05 . 110 14 TYR CB C 44.69 0.05 . 111 14 TYR N N 115.40 0.05 . 112 15 VAL H H 8.80 0.05 . 113 15 VAL HA H 4.14 0.05 . 114 15 VAL HB H 1.35 0.05 . 115 15 VAL HG1 H 0.73 0.05 . 116 15 VAL HG2 H -0.22 0.05 . 117 15 VAL C C 172.90 0.05 . 118 15 VAL CA C 61.31 0.05 . 119 15 VAL CB C 34.22 0.05 . 120 15 VAL CG1 C 21.46 0.05 . 121 15 VAL CG2 C 20.78 0.05 . 122 15 VAL N N 120.02 0.05 . 123 16 PHE H H 8.73 0.05 . 124 16 PHE HA H 5.25 0.05 . 125 16 PHE HB2 H 1.24 0.05 . 126 16 PHE HB3 H 2.36 0.05 . 127 16 PHE HD1 H 6.63 0.05 . 128 16 PHE C C 175.01 0.05 . 129 16 PHE CA C 56.55 0.05 . 130 16 PHE CB C 41.02 0.05 . 131 16 PHE N N 125.04 0.05 . 132 17 ILE H H 8.50 0.05 . 133 17 ILE HA H 4.88 0.05 . 134 17 ILE HB H 1.35 0.05 . 135 17 ILE HG12 H 1.51 0.05 . 136 17 ILE HG13 H 0.69 0.05 . 137 17 ILE HG2 H 0.26 0.05 . 138 17 ILE HD1 H 0.81 0.05 . 139 17 ILE C C 173.04 0.05 . 140 17 ILE CA C 59.92 0.05 . 141 17 ILE CB C 42.59 0.05 . 142 17 ILE CG1 C 27.35 0.05 . 143 17 ILE CG2 C 17.35 0.05 . 144 17 ILE CD1 C 17.08 0.05 . 145 17 ILE N N 117.75 0.05 . 146 18 GLU H H 9.55 0.05 . 147 18 GLU HA H 5.21 0.05 . 148 18 GLU HB2 H 2.16 0.05 . 149 18 GLU HB3 H 1.79 0.05 . 150 18 GLU HG2 H 2.28 0.05 . 151 18 GLU C C 175.34 0.05 . 152 18 GLU CA C 53.85 0.05 . 153 18 GLU CB C 32.42 0.05 . 154 18 GLU N N 130.29 0.05 . 155 19 PHE H H 9.47 0.05 . 156 19 PHE HA H 4.78 0.05 . 157 19 PHE HB2 H 2.45 0.05 . 158 19 PHE HB3 H 2.13 0.05 . 159 19 PHE C C 177.00 0.05 . 160 19 PHE CA C 57.76 0.05 . 161 19 PHE CB C 40.19 0.05 . 162 19 PHE N N 124.86 0.05 . 163 20 CYS H H 9.15 0.05 . 164 20 CYS HA H 4.31 0.05 . 165 20 CYS HB2 H 2.95 0.05 . 166 20 CYS HB3 H 2.83 0.05 . 167 20 CYS C C 173.79 0.05 . 168 20 CYS CA C 59.58 0.05 . 169 20 CYS CB C 25.39 0.05 . 170 20 CYS N N 126.76 0.05 . 171 21 VAL H H 7.20 0.05 . 172 21 VAL HA H 4.20 0.05 . 173 21 VAL HB H 1.77 0.05 . 174 21 VAL HG1 H 0.80 0.05 . 175 21 VAL C C 173.76 0.05 . 176 21 VAL CA C 60.96 0.05 . 177 21 VAL CB C 34.30 0.05 . 178 21 VAL CG1 C 21.57 0.05 . 179 21 VAL N N 123.47 0.05 . 180 22 GLU H H 8.73 0.05 . 181 22 GLU HA H 4.41 0.05 . 182 22 GLU HB2 H 2.05 0.05 . 183 22 GLU HB3 H 1.98 0.05 . 184 22 GLU HG2 H 2.38 0.05 . 185 22 GLU C C 176.54 0.05 . 186 22 GLU CA C 55.51 0.05 . 187 22 GLU CB C 30.41 0.05 . 188 22 GLU CG C 36.86 0.05 . 189 22 GLU N N 127.43 0.05 . 190 23 ASP H H 9.29 0.05 . 191 23 ASP HA H 4.24 0.05 . 192 23 ASP HB2 H 2.87 0.05 . 193 23 ASP HB3 H 2.50 0.05 . 194 23 ASP C C 175.79 0.05 . 195 23 ASP CA C 55.42 0.05 . 196 23 ASP CB C 39.32 0.05 . 197 23 ASP N N 120.43 0.05 . 198 24 SER H H 8.29 0.05 . 199 24 SER HA H 4.62 0.05 . 200 24 SER HB2 H 3.69 0.05 . 201 24 SER HB3 H 3.75 0.05 . 202 24 SER C C 175.82 0.05 . 203 24 SER CA C 59.58 0.05 . 204 24 SER CB C 65.29 0.05 . 205 24 SER N N 112.21 0.05 . 206 25 LYS H H 9.07 0.05 . 207 25 LYS HA H 4.70 0.05 . 208 25 LYS HB2 H 1.63 0.05 . 209 25 LYS HB3 H 1.86 0.05 . 210 25 LYS HG2 H 1.49 0.05 . 211 25 LYS HG3 H 1.71 0.05 . 212 25 LYS C C 174.30 0.05 . 213 25 LYS CA C 54.56 0.05 . 214 25 LYS CB C 36.01 0.05 . 215 25 LYS N N 119.17 0.05 . 216 26 ASP H H 8.91 0.05 . 217 26 ASP HA H 4.15 0.05 . 218 26 ASP HB2 H 2.79 0.05 . 219 26 ASP HB3 H 2.45 0.05 . 220 26 ASP C C 174.58 0.05 . 221 26 ASP CA C 54.73 0.05 . 222 26 ASP CB C 38.55 0.05 . 223 26 ASP N N 120.87 0.05 . 224 27 VAL H H 8.11 0.05 . 225 27 VAL HA H 3.75 0.05 . 226 27 VAL HB H 2.05 0.05 . 227 27 VAL HG1 H 0.92 0.05 . 228 27 VAL HG2 H 0.75 0.05 . 229 27 VAL C C 176.63 0.05 . 230 27 VAL CA C 63.65 0.05 . 231 27 VAL CB C 31.28 0.05 . 232 27 VAL CG1 C 22.88 0.05 . 233 27 VAL CG2 C 22.17 0.05 . 234 27 VAL N N 117.52 0.05 . 235 28 ASN H H 8.89 0.05 . 236 28 ASN HA H 4.79 0.05 . 237 28 ASN HB2 H 2.45 0.05 . 238 28 ASN HB3 H 2.39 0.05 . 239 28 ASN C C 172.92 0.05 . 240 28 ASN CA C 52.65 0.05 . 241 28 ASN CB C 41.49 0.05 . 242 28 ASN N N 128.36 0.05 . 243 29 VAL H H 8.24 0.05 . 244 29 VAL HA H 4.42 0.05 . 245 29 VAL HB H 1.17 0.05 . 246 29 VAL HG1 H 0.34 0.05 . 247 29 VAL HG2 H 0.16 0.05 . 248 29 VAL C C 173.71 0.05 . 249 29 VAL CA C 60.96 0.05 . 250 29 VAL CB C 33.35 0.05 . 251 29 VAL CG1 C 20.97 0.05 . 252 29 VAL CG2 C 22.67 0.05 . 253 29 VAL N N 123.91 0.05 . 254 30 ASN H H 8.76 0.05 . 255 30 ASN HA H 4.92 0.05 . 256 30 ASN HB2 H 2.76 0.05 . 257 30 ASN HB3 H 2.50 0.05 . 258 30 ASN C C 174.18 0.05 . 259 30 ASN CA C 51.79 0.05 . 260 30 ASN CB C 40.88 0.05 . 261 30 ASN N N 125.01 0.05 . 262 31 PHE H H 8.96 0.05 . 263 31 PHE HA H 5.02 0.05 . 264 31 PHE HB2 H 3.20 0.05 . 265 31 PHE HB3 H 2.92 0.05 . 266 31 PHE C C 174.13 0.05 . 267 31 PHE CA C 56.81 0.05 . 268 31 PHE CB C 40.36 0.05 . 269 31 PHE N N 124.71 0.05 . 270 32 GLU H H 8.77 0.05 . 271 32 GLU HA H 4.70 0.05 . 272 32 GLU HB2 H 2.09 0.05 . 273 32 GLU C C 174.88 0.05 . 274 32 GLU CA C 54.64 0.05 . 275 32 GLU CB C 33.18 0.05 . 276 32 GLU N N 122.70 0.05 . 277 33 LYS H H 8.59 0.05 . 278 33 LYS HA H 4.18 0.05 . 279 33 LYS HB2 H 2.00 0.05 . 280 33 LYS HB3 H 1.93 0.05 . 281 33 LYS C C 176.58 0.05 . 282 33 LYS CA C 59.58 0.05 . 283 33 LYS CB C 32.14 0.05 . 284 33 LYS N N 117.18 0.05 . 285 34 SER H H 8.11 0.05 . 286 34 SER HA H 4.90 0.05 . 287 34 SER HB2 H 3.88 0.05 . 288 34 SER HB3 H 3.95 0.05 . 289 34 SER C C 174.51 0.05 . 290 34 SER CA C 56.81 0.05 . 291 34 SER CB C 64.86 0.05 . 292 34 SER N N 105.51 0.05 . 293 35 LYS H H 7.48 0.05 . 294 35 LYS HA H 5.43 0.05 . 295 35 LYS HB2 H 1.75 0.05 . 296 35 LYS HB3 H 1.73 0.05 . 297 35 LYS HG2 H 1.30 0.05 . 298 35 LYS HG3 H 1.26 0.05 . 299 35 LYS C C 172.41 0.05 . 300 35 LYS CA C 55.77 0.05 . 301 35 LYS CB C 37.33 0.05 . 302 35 LYS N N 123.51 0.05 . 303 36 LEU H H 8.79 0.05 . 304 36 LEU HA H 5.28 0.05 . 305 36 LEU HB2 H 1.83 0.05 . 306 36 LEU HB3 H 1.66 0.05 . 307 36 LEU C C 172.40 0.05 . 308 36 LEU CA C 53.78 0.05 . 309 36 LEU CB C 46.85 0.05 . 310 36 LEU N N 124.53 0.05 . 311 37 THR H H 8.40 0.05 . 312 37 THR HA H 5.09 0.05 . 313 37 THR HB H 3.90 0.05 . 314 37 THR HG2 H 1.09 0.05 . 315 37 THR C C 174.86 0.05 . 316 37 THR CA C 62.39 0.05 . 317 37 THR CB C 70.40 0.05 . 318 37 THR CG2 C 21.42 0.05 . 319 37 THR N N 120.93 0.05 . 320 38 PHE H H 9.09 0.05 . 321 38 PHE HA H 5.02 0.05 . 322 38 PHE HB2 H 2.03 0.05 . 323 38 PHE HB3 H 2.29 0.05 . 324 38 PHE HD1 H 6.45 0.05 . 325 38 PHE C C 172.04 0.05 . 326 38 PHE CA C 55.34 0.05 . 327 38 PHE CB C 43.31 0.05 . 328 38 PHE N N 129.33 0.05 . 329 39 SER H H 8.07 0.05 . 330 39 SER HA H 4.58 0.05 . 331 39 SER HB2 H 3.83 0.05 . 332 39 SER HB3 H 3.64 0.05 . 333 39 SER C C 171.94 0.05 . 334 39 SER CA C 56.55 0.05 . 335 39 SER CB C 66.50 0.05 . 336 39 SER N N 119.66 0.05 . 337 40 CYS H H 7.90 0.05 . 338 40 CYS HA H 4.81 0.05 . 339 40 CYS HB2 H 2.82 0.05 . 340 40 CYS HB3 H 3.10 0.05 . 341 40 CYS C C 171.58 0.05 . 342 40 CYS CA C 56.72 0.05 . 343 40 CYS CB C 29.72 0.05 . 344 40 CYS N N 110.98 0.05 . 345 41 LEU H H 8.63 0.05 . 346 41 LEU HA H 5.32 0.05 . 347 41 LEU HB2 H 1.53 0.05 . 348 41 LEU HB3 H 1.24 0.05 . 349 41 LEU C C 177.81 0.05 . 350 41 LEU CA C 53.17 0.05 . 351 41 LEU CB C 44.26 0.05 . 352 41 LEU N N 118.40 0.05 . 353 42 GLY H H 9.39 0.05 . 354 42 GLY HA2 H 4.26 0.05 . 355 42 GLY HA3 H 3.95 0.05 . 356 42 GLY C C 173.89 0.05 . 357 42 GLY CA C 45.68 0.05 . 358 42 GLY N N 109.15 0.05 . 359 43 GLY H H 7.99 0.05 . 360 43 GLY HA2 H 4.34 0.05 . 361 43 GLY HA3 H 3.96 0.05 . 362 43 GLY C C 175.20 0.05 . 363 43 GLY CA C 46.18 0.05 . 364 43 GLY N N 108.58 0.05 . 365 44 SER H H 8.54 0.05 . 366 44 SER HA H 4.30 0.05 . 367 44 SER HB2 H 3.91 0.05 . 368 44 SER HB3 H 3.88 0.05 . 369 44 SER CA C 60.38 0.05 . 370 44 SER CB C 63.47 0.05 . 371 44 SER N N 114.75 0.05 . 372 45 ASP H H 8.17 0.05 . 373 45 ASP HA H 4.55 0.05 . 374 45 ASP HB2 H 2.45 0.05 . 375 45 ASP HB3 H 2.39 0.05 . 376 45 ASP C C 175.41 0.05 . 377 45 ASP CA C 53.78 0.05 . 378 45 ASP CB C 40.54 0.05 . 379 45 ASP N N 118.07 0.05 . 380 46 ASN H H 7.93 0.05 . 381 46 ASN HA H 4.16 0.05 . 382 46 ASN HB2 H 2.80 0.05 . 383 46 ASN HD21 H 7.98 0.05 . 384 46 ASN HD22 H 7.98 0.05 . 385 46 ASN C C 173.99 0.05 . 386 46 ASN CA C 54.12 0.05 . 387 46 ASN CB C 36.99 0.05 . 388 46 ASN N N 116.05 0.05 . 389 46 ASN ND2 N 118.73 0.05 . 390 47 PHE H H 8.09 0.05 . 391 47 PHE HA H 4.46 0.05 . 392 47 PHE HB2 H 2.86 0.05 . 393 47 PHE HB3 H 2.76 0.05 . 394 47 PHE C C 175.69 0.05 . 395 47 PHE CA C 57.76 0.05 . 396 47 PHE CB C 39.41 0.05 . 397 47 PHE N N 119.01 0.05 . 398 48 LYS H H 8.31 0.05 . 399 48 LYS HA H 4.53 0.05 . 400 48 LYS HB2 H 1.57 0.05 . 401 48 LYS HB3 H 1.73 0.05 . 402 48 LYS HG2 H 1.39 0.05 . 403 48 LYS HG3 H 1.24 0.05 . 404 48 LYS C C 175.93 0.05 . 405 48 LYS CA C 56.61 0.05 . 406 48 LYS CB C 33.37 0.05 . 407 48 LYS N N 123.41 0.05 . 408 49 HIS H H 8.87 0.05 . 409 49 HIS HA H 3.63 0.05 . 410 49 HIS HB2 H 3.15 0.05 . 411 49 HIS HB3 H 2.89 0.05 . 412 49 HIS C C 177.99 0.05 . 413 49 HIS CA C 60.32 0.05 . 414 49 HIS CB C 32.01 0.05 . 415 49 HIS N N 121.28 0.05 . 416 50 LEU H H 7.48 0.05 . 417 50 LEU HA H 5.03 0.05 . 418 50 LEU HB2 H 1.43 0.05 . 419 50 LEU HB3 H 1.35 0.05 . 420 50 LEU HG H 1.28 0.05 . 421 50 LEU HD1 H 0.80 0.05 . 422 50 LEU HD2 H 0.80 0.05 . 423 50 LEU C C 174.45 0.05 . 424 50 LEU CA C 54.81 0.05 . 425 50 LEU CB C 46.08 0.05 . 426 50 LEU CG C 28.59 0.05 . 427 50 LEU CD1 C 23.42 0.05 . 428 50 LEU CD2 C 26.00 0.05 . 429 50 LEU N N 111.48 0.05 . 430 51 ASN H H 9.58 0.05 . 431 51 ASN HA H 4.82 0.05 . 432 51 ASN HB2 H 2.34 0.05 . 433 51 ASN HB3 H 1.77 0.05 . 434 51 ASN C C 172.55 0.05 . 435 51 ASN CA C 52.31 0.05 . 436 51 ASN CB C 40.02 0.05 . 437 51 ASN N N 123.55 0.05 . 438 52 GLU H H 8.97 0.05 . 439 52 GLU HA H 5.04 0.05 . 440 52 GLU HB2 H 2.16 0.05 . 441 52 GLU HB3 H 1.99 0.05 . 442 52 GLU HG2 H 2.32 0.05 . 443 52 GLU C C 175.24 0.05 . 444 52 GLU CA C 55.42 0.05 . 445 52 GLU CB C 31.01 0.05 . 446 52 GLU N N 124.32 0.05 . 447 53 ILE H H 9.10 0.05 . 448 53 ILE HA H 4.52 0.05 . 449 53 ILE HB H 2.00 0.05 . 450 53 ILE HG12 H 1.79 0.05 . 451 53 ILE HG13 H 1.25 0.05 . 452 53 ILE HG2 H 0.87 0.05 . 453 53 ILE HD1 H 1.12 0.05 . 454 53 ILE C C 174.34 0.05 . 455 53 ILE CA C 60.62 0.05 . 456 53 ILE CB C 41.49 0.05 . 457 53 ILE CG1 C 27.19 0.05 . 458 53 ILE CG2 C 18.75 0.05 . 459 53 ILE CD1 C 14.92 0.05 . 460 53 ILE N N 122.78 0.05 . 461 54 ASP H H 9.05 0.05 . 462 54 ASP HA H 5.07 0.05 . 463 54 ASP HB2 H 2.73 0.05 . 464 54 ASP HB3 H 2.67 0.05 . 465 54 ASP C C 176.34 0.05 . 466 54 ASP CA C 54.12 0.05 . 467 54 ASP CB C 40.71 0.05 . 468 54 ASP N N 128.42 0.05 . 469 55 LEU H H 7.95 0.05 . 470 55 LEU HA H 4.56 0.05 . 471 55 LEU HB2 H 1.95 0.05 . 472 55 LEU HB3 H 1.80 0.05 . 473 55 LEU C C 177.44 0.05 . 474 55 LEU CA C 54.89 0.05 . 475 55 LEU CB C 44.04 0.05 . 476 55 LEU N N 126.13 0.05 . 477 56 PHE H H 7.98 0.05 . 478 56 PHE HA H 3.34 0.05 . 479 56 PHE HB2 H 1.49 0.05 . 480 56 PHE HB3 H 2.47 0.05 . 481 56 PHE C C 174.02 0.05 . 482 56 PHE CA C 60.95 0.05 . 483 56 PHE CB C 39.71 0.05 . 484 56 PHE N N 120.24 0.05 . 485 57 HIS H H 6.01 0.05 . 486 57 HIS HA H 4.45 0.05 . 487 57 HIS HB2 H 3.18 0.05 . 488 57 HIS HB3 H 2.18 0.05 . 489 57 HIS CA C 53.61 0.05 . 490 57 HIS CB C 34.13 0.05 . 491 57 HIS N N 113.52 0.05 . 492 58 CYS H H 7.81 0.05 . 493 58 CYS HA H 5.02 0.05 . 494 58 CYS HB2 H 3.10 0.05 . 495 58 CYS HB3 H 2.89 0.05 . 496 58 CYS CA C 58.19 0.05 . 497 58 CYS CB C 28.94 0.05 . 498 58 CYS N N 112.93 0.05 . 499 59 ILE H H 9.52 0.05 . 500 59 ILE HA H 5.05 0.05 . 501 59 ILE HB H 1.84 0.05 . 502 59 ILE HG12 H 1.26 0.05 . 503 59 ILE HG13 H 1.16 0.05 . 504 59 ILE HG2 H 1.01 0.05 . 505 59 ILE HD1 H 0.90 0.05 . 506 59 ILE C C 175.50 0.05 . 507 59 ILE CA C 59.58 0.05 . 508 59 ILE CB C 42.37 0.05 . 509 59 ILE CG1 C 26.29 0.05 . 510 59 ILE CG2 C 19.62 0.05 . 511 59 ILE CD1 C 14.92 0.05 . 512 59 ILE N N 116.66 0.05 . 513 60 ASP H H 8.58 0.05 . 514 60 ASP HA H 5.20 0.05 . 515 60 ASP HB2 H 2.58 0.05 . 516 60 ASP HB3 H 2.35 0.05 . 517 60 ASP C C 177.06 0.05 . 518 60 ASP CA C 49.71 0.05 . 519 60 ASP CB C 41.23 0.05 . 520 60 ASP N N 118.04 0.05 . 521 61 PRO HA H 3.78 0.05 . 522 61 PRO HB2 H 2.29 0.05 . 523 61 PRO HB3 H 2.07 0.05 . 524 61 PRO HG2 H 2.13 0.05 . 525 61 PRO HG3 H 1.58 0.05 . 526 61 PRO CA C 64.85 0.05 . 527 61 PRO CB C 33.17 0.05 . 528 61 PRO CG C 27.28 0.05 . 529 61 PRO CD C 51.82 0.05 . 530 62 ASN H H 8.08 0.05 . 531 62 ASN HA H 4.61 0.05 . 532 62 ASN HB2 H 2.93 0.05 . 533 62 ASN HB3 H 2.90 0.05 . 534 62 ASN CA C 55.27 0.05 . 535 62 ASN CB C 38.27 0.05 . 536 62 ASN N N 113.14 0.05 . 537 63 ASP H H 7.04 0.05 . 538 63 ASP HA H 5.09 0.05 . 539 63 ASP HB2 H 2.52 0.05 . 540 63 ASP HB3 H 2.24 0.05 . 541 63 ASP C C 174.50 0.05 . 542 63 ASP CA C 53.00 0.05 . 543 63 ASP CB C 42.18 0.05 . 544 63 ASP N N 117.87 0.05 . 545 64 SER H H 6.76 0.05 . 546 64 SER HA H 4.97 0.05 . 547 64 SER HB2 H 2.81 0.05 . 548 64 SER HG H 4.01 0.05 . 549 64 SER C C 171.96 0.05 . 550 64 SER CA C 58.34 0.05 . 551 64 SER CB C 63.56 0.05 . 552 64 SER N N 115.08 0.05 . 553 65 LYS H H 8.68 0.05 . 554 65 LYS HA H 5.08 0.05 . 555 65 LYS HB2 H 1.93 0.05 . 556 65 LYS HB3 H 1.76 0.05 . 557 65 LYS HG2 H 1.34 0.05 . 558 65 LYS HG3 H 1.29 0.05 . 559 65 LYS C C 174.37 0.05 . 560 65 LYS CA C 55.34 0.05 . 561 65 LYS CB C 36.38 0.05 . 562 65 LYS N N 120.71 0.05 . 563 66 HIS H H 9.14 0.05 . 564 66 HIS HA H 6.05 0.05 . 565 66 HIS CA C 54.68 0.05 . 566 66 HIS N N 122.03 0.05 . 567 67 LYS H H 9.11 0.05 . 568 67 LYS HA H 4.58 0.05 . 569 67 LYS HB2 H 1.81 0.05 . 570 67 LYS HB3 H 1.87 0.05 . 571 67 LYS HG2 H 1.41 0.05 . 572 67 LYS HG3 H 1.32 0.05 . 573 67 LYS CA C 55.39 0.05 . 574 67 LYS CB C 35.92 0.05 . 575 67 LYS N N 120.95 0.05 . 576 68 ARG H H 9.31 0.05 . 577 68 ARG HA H 5.12 0.05 . 578 68 ARG HB2 H 1.93 0.05 . 579 68 ARG HB3 H 1.89 0.05 . 580 68 ARG CA C 56.28 0.05 . 581 68 ARG CB C 31.37 0.05 . 582 68 ARG N N 129.59 0.05 . 583 69 THR H H 9.32 0.05 . 584 69 THR HA H 4.95 0.05 . 585 69 THR HB H 4.78 0.05 . 586 69 THR HG2 H 1.33 0.05 . 587 69 THR C C 174.13 0.05 . 588 69 THR CA C 60.62 0.05 . 589 69 THR CB C 72.30 0.05 . 590 69 THR CG2 C 20.84 0.05 . 591 69 THR N N 120.01 0.05 . 592 70 ASP H H 8.94 0.05 . 593 70 ASP HA H 4.56 0.05 . 594 70 ASP HB2 H 2.89 0.05 . 595 70 ASP HB3 H 2.77 0.05 . 596 70 ASP CA C 57.16 0.05 . 597 70 ASP CB C 40.35 0.05 . 598 70 ASP N N 118.09 0.05 . 599 71 ARG H H 8.16 0.05 . 600 71 ARG HA H 4.52 0.05 . 601 71 ARG HB2 H 1.81 0.05 . 602 71 ARG HB3 H 1.75 0.05 . 603 71 ARG HG2 H 1.65 0.05 . 604 71 ARG C C 174.73 0.05 . 605 71 ARG CA C 56.81 0.05 . 606 71 ARG CB C 32.11 0.05 . 607 71 ARG N N 116.90 0.05 . 608 72 SER H H 7.61 0.05 . 609 72 SER HA H 4.97 0.05 . 610 72 SER HB2 H 4.04 0.05 . 611 72 SER HB3 H 3.87 0.05 . 612 72 SER C C 171.75 0.05 . 613 72 SER CA C 57.93 0.05 . 614 72 SER CB C 64.86 0.05 . 615 72 SER N N 109.57 0.05 . 616 73 ILE H H 8.77 0.05 . 617 73 ILE HA H 5.12 0.05 . 618 73 ILE HB H 2.05 0.05 . 619 73 ILE HG12 H 1.66 0.05 . 620 73 ILE HG13 H 1.72 0.05 . 621 73 ILE HG2 H 1.02 0.05 . 622 73 ILE HD1 H 1.30 0.05 . 623 73 ILE C C 174.24 0.05 . 624 73 ILE CA C 62.09 0.05 . 625 73 ILE CB C 41.14 0.05 . 626 73 ILE CG2 C 21.40 0.05 . 627 73 ILE CD1 C 17.13 0.05 . 628 73 ILE N N 117.79 0.05 . 629 74 LEU H H 9.05 0.05 . 630 74 LEU HA H 5.14 0.05 . 631 74 LEU HB2 H 1.99 0.05 . 632 74 LEU HB3 H 1.61 0.05 . 633 74 LEU C C 176.90 0.05 . 634 74 LEU CA C 54.04 0.05 . 635 74 LEU CB C 44.34 0.05 . 636 74 LEU N N 128.87 0.05 . 637 75 CYS H H 9.96 0.05 . 638 75 CYS HA H 5.38 0.05 . 639 75 CYS HB2 H 3.32 0.05 . 640 75 CYS HB3 H 2.82 0.05 . 641 75 CYS C C 172.45 0.05 . 642 75 CYS CA C 58.37 0.05 . 643 75 CYS CB C 29.54 0.05 . 644 75 CYS N N 124.53 0.05 . 645 76 CYS H H 9.20 0.05 . 646 76 CYS HA H 4.48 0.05 . 647 76 CYS HB2 H 2.54 0.05 . 648 76 CYS HB3 H 2.41 0.05 . 649 76 CYS C C 172.65 0.05 . 650 76 CYS CA C 56.81 0.05 . 651 76 CYS CB C 27.47 0.05 . 652 76 CYS N N 123.99 0.05 . 653 77 LEU H H 9.48 0.05 . 654 77 LEU HA H 4.46 0.05 . 655 77 LEU HB2 H 1.67 0.05 . 656 77 LEU HB3 H 1.27 0.05 . 657 77 LEU C C 175.50 0.05 . 658 77 LEU CA C 53.26 0.05 . 659 77 LEU CB C 41.14 0.05 . 660 77 LEU N N 127.49 0.05 . 661 78 ARG H H 7.71 0.05 . 662 78 ARG HA H 3.97 0.05 . 663 78 ARG HB2 H 1.83 0.05 . 664 78 ARG HG2 H 1.27 0.05 . 665 78 ARG C C 175.53 0.05 . 666 78 ARG CA C 54.30 0.05 . 667 78 ARG CB C 29.63 0.05 . 668 78 ARG N N 124.68 0.05 . 669 79 LYS H H 8.23 0.05 . 670 79 LYS HA H 3.94 0.05 . 671 79 LYS HB2 H 1.71 0.05 . 672 79 LYS HB3 H 1.48 0.05 . 673 79 LYS C C 177.13 0.05 . 674 79 LYS CA C 58.72 0.05 . 675 79 LYS CB C 33.61 0.05 . 676 79 LYS N N 128.12 0.05 . 677 80 GLY H H 8.89 0.05 . 678 80 GLY HA2 H 3.66 0.05 . 679 80 GLY HA3 H 3.66 0.05 . 680 80 GLY CA C 46.16 0.05 . 681 80 GLY N N 111.07 0.05 . 682 81 GLU H H 7.64 0.05 . 683 81 GLU HA H 4.53 0.05 . 684 81 GLU HB2 H 2.31 0.05 . 685 81 GLU HB3 H 2.12 0.05 . 686 81 GLU HG2 H 2.42 0.05 . 687 81 GLU C C 176.42 0.05 . 688 81 GLU CA C 54.47 0.05 . 689 81 GLU CB C 30.24 0.05 . 690 81 GLU N N 118.65 0.05 . 691 82 SER H H 8.56 0.05 . 692 82 SER HA H 4.16 0.05 . 693 82 SER HB2 H 3.84 0.05 . 694 82 SER HB3 H 3.75 0.05 . 695 82 SER C C 176.51 0.05 . 696 82 SER CA C 59.78 0.05 . 697 82 SER CB C 63.32 0.05 . 698 82 SER N N 120.41 0.05 . 699 83 GLY H H 8.41 0.05 . 700 83 GLY HA2 H 4.22 0.05 . 701 83 GLY HA3 H 3.70 0.05 . 702 83 GLY C C 173.37 0.05 . 703 83 GLY CA C 46.42 0.05 . 704 83 GLY N N 111.79 0.05 . 705 84 GLN H H 7.21 0.05 . 706 84 GLN HA H 4.67 0.05 . 707 84 GLN HB2 H 2.10 0.05 . 708 84 GLN HB3 H 2.30 0.05 . 709 84 GLN HG2 H 2.45 0.05 . 710 84 GLN HG3 H 2.32 0.05 . 711 84 GLN CA C 54.82 0.05 . 712 84 GLN CB C 30.15 0.05 . 713 84 GLN CG C 33.58 0.05 . 714 84 GLN N N 118.36 0.05 . 715 85 SER H H 9.31 0.05 . 716 85 SER HA H 4.73 0.05 . 717 85 SER HB2 H 3.81 0.05 . 718 85 SER HB3 H 3.76 0.05 . 719 85 SER C C 174.65 0.05 . 720 85 SER CA C 59.27 0.05 . 721 85 SER CB C 63.27 0.05 . 722 85 SER N N 125.71 0.05 . 723 86 TRP H H 9.52 0.05 . 724 86 TRP HA H 5.25 0.05 . 725 86 TRP HB2 H 3.45 0.05 . 726 86 TRP HE1 H 10.57 0.05 . 727 86 TRP CA C 54.04 0.05 . 728 86 TRP CB C 27.47 0.05 . 729 86 TRP N N 128.75 0.05 . 730 86 TRP NE1 N 127.00 0.05 . 731 87 PRO HA H 4.66 0.05 . 732 87 PRO HB2 H 1.94 0.05 . 733 87 PRO HB3 H 2.26 0.05 . 734 87 PRO HG2 H 1.42 0.05 . 735 87 PRO HG3 H 1.97 0.05 . 736 87 PRO HD2 H 3.57 0.05 . 737 87 PRO HD3 H 2.93 0.05 . 738 87 PRO C C 175.82 0.05 . 739 87 PRO CA C 63.57 0.05 . 740 87 PRO CB C 31.72 0.05 . 741 87 PRO CG C 26.98 0.05 . 742 87 PRO CD C 50.54 0.05 . 743 88 ARG H H 7.16 0.05 . 744 88 ARG HA H 4.66 0.05 . 745 88 ARG HB2 H 1.91 0.05 . 746 88 ARG HB3 H 1.71 0.05 . 747 88 ARG HG2 H 1.65 0.05 . 748 88 ARG HG3 H 1.30 0.05 . 749 88 ARG C C 172.22 0.05 . 750 88 ARG CA C 53.78 0.05 . 751 88 ARG CB C 31.28 0.05 . 752 88 ARG N N 113.08 0.05 . 753 89 LEU H H 8.06 0.05 . 754 89 LEU HA H 3.92 0.05 . 755 89 LEU HB2 H 0.88 0.05 . 756 89 LEU HB3 H -0.67 0.05 . 757 89 LEU C C 177.60 0.05 . 758 89 LEU CA C 55.68 0.05 . 759 89 LEU CB C 42.27 0.05 . 760 89 LEU N N 117.76 0.05 . 761 90 THR H H 6.69 0.05 . 762 90 THR HA H 4.92 0.05 . 763 90 THR HB H 4.70 0.05 . 764 90 THR HG2 H 1.02 0.05 . 765 90 THR C C 174.89 0.05 . 766 90 THR CA C 58.71 0.05 . 767 90 THR CB C 70.92 0.05 . 768 90 THR CG2 C 21.40 0.05 . 769 90 THR N N 101.61 0.05 . 770 91 LYS H H 7.86 0.05 . 771 91 LYS HA H 3.86 0.05 . 772 91 LYS HB2 H 1.66 0.05 . 773 91 LYS HB3 H 1.63 0.05 . 774 91 LYS HG2 H 1.33 0.05 . 775 91 LYS HG3 H 1.25 0.05 . 776 91 LYS C C 178.66 0.05 . 777 91 LYS CA C 60.10 0.05 . 778 91 LYS CB C 32.57 0.05 . 779 91 LYS N N 121.97 0.05 . 780 92 GLU H H 8.82 0.05 . 781 92 GLU HA H 4.49 0.05 . 782 92 GLU HB2 H 1.97 0.05 . 783 92 GLU HB3 H 2.11 0.05 . 784 92 GLU HG2 H 2.11 0.05 . 785 92 GLU HG3 H 2.36 0.05 . 786 92 GLU C C 176.71 0.05 . 787 92 GLU CA C 54.99 0.05 . 788 92 GLU CB C 30.06 0.05 . 789 92 GLU N N 117.18 0.05 . 790 93 ARG H H 8.75 0.05 . 791 93 ARG HA H 4.03 0.05 . 792 93 ARG HB2 H 1.85 0.05 . 793 93 ARG HB3 H 1.62 0.05 . 794 93 ARG CA C 56.67 0.05 . 795 93 ARG CB C 29.74 0.05 . 796 93 ARG N N 122.14 0.05 . 797 94 ALA H H 7.49 0.05 . 798 94 ALA HA H 4.28 0.05 . 799 94 ALA HB H 1.31 0.05 . 800 94 ALA C C 176.39 0.05 . 801 94 ALA CA C 52.13 0.05 . 802 94 ALA CB C 20.22 0.05 . 803 94 ALA N N 124.68 0.05 . 804 95 LYS H H 8.47 0.05 . 805 95 LYS HA H 4.23 0.05 . 806 95 LYS HB2 H 1.92 0.05 . 807 95 LYS HB3 H 1.62 0.05 . 808 95 LYS HG2 H 1.41 0.05 . 809 95 LYS CA C 56.17 0.05 . 810 95 LYS CB C 36.01 0.05 . 811 95 LYS N N 122.86 0.05 . 812 96 LEU H H 8.48 0.05 . 813 96 LEU HA H 4.53 0.05 . 814 96 LEU HB2 H 1.19 0.05 . 815 96 LEU HB3 H 0.11 0.05 . 816 96 LEU CA C 53.07 0.05 . 817 96 LEU CB C 42.20 0.05 . 818 96 LEU N N 126.70 0.05 . 819 97 ASN H H 9.16 0.05 . 820 97 ASN HA H 4.40 0.05 . 821 97 ASN HB2 H 2.93 0.05 . 822 97 ASN HB3 H 2.99 0.05 . 823 97 ASN C C 175.34 0.05 . 824 97 ASN CA C 55.98 0.05 . 825 97 ASN N N 121.80 0.05 . 826 98 TRP H H 6.87 0.05 . 827 98 TRP HA H 4.79 0.05 . 828 98 TRP HB2 H 3.98 0.05 . 829 98 TRP HB3 H 3.03 0.05 . 830 98 TRP HE1 H 10.94 0.05 . 831 98 TRP C C 173.94 0.05 . 832 98 TRP CA C 54.12 0.05 . 833 98 TRP CB C 29.20 0.05 . 834 98 TRP N N 112.55 0.05 . 835 98 TRP NE1 N 132.30 0.05 . 836 99 LEU H H 6.92 0.05 . 837 99 LEU HA H 5.15 0.05 . 838 99 LEU HB2 H 1.39 0.05 . 839 99 LEU HB3 H 0.03 0.05 . 840 99 LEU HG H 1.34 0.05 . 841 99 LEU HD1 H 0.79 0.05 . 842 99 LEU HD2 H 0.50 0.05 . 843 99 LEU C C 175.28 0.05 . 844 99 LEU CA C 53.69 0.05 . 845 99 LEU CB C 44.34 0.05 . 846 99 LEU CG C 27.90 0.05 . 847 99 LEU CD1 C 22.69 0.05 . 848 99 LEU CD2 C 26.79 0.05 . 849 99 LEU N N 124.32 0.05 . 850 100 SER H H 8.78 0.05 . 851 100 SER HA H 4.99 0.05 . 852 100 SER HB2 H 3.89 0.05 . 853 100 SER C C 173.22 0.05 . 854 100 SER CA C 56.72 0.05 . 855 100 SER CB C 66.50 0.05 . 856 100 SER N N 120.75 0.05 . 857 101 VAL H H 8.37 0.05 . 858 101 VAL HA H 3.61 0.05 . 859 101 VAL HB H 1.22 0.05 . 860 101 VAL HG1 H 0.47 0.05 . 861 101 VAL HG2 H -0.06 0.05 . 862 101 VAL C C 176.39 0.05 . 863 101 VAL CA C 62.95 0.05 . 864 101 VAL CB C 32.31 0.05 . 865 101 VAL CG1 C 21.74 0.05 . 866 101 VAL CG2 C 20.97 0.05 . 867 101 VAL N N 122.29 0.05 . 868 102 ASP H H 8.80 0.05 . 869 102 ASP HA H 4.58 0.05 . 870 102 ASP HB2 H 2.29 0.05 . 871 102 ASP HB3 H 3.03 0.05 . 872 102 ASP C C 175.85 0.05 . 873 102 ASP CA C 51.96 0.05 . 874 102 ASP CB C 40.18 0.05 . 875 102 ASP N N 123.83 0.05 . 876 103 PHE H H 7.93 0.05 . 877 103 PHE HA H 4.21 0.05 . 878 103 PHE HB2 H 3.21 0.05 . 879 103 PHE HB3 H 2.95 0.05 . 880 103 PHE C C 175.55 0.05 . 881 103 PHE CA C 61.05 0.05 . 882 103 PHE CB C 38.37 0.05 . 883 103 PHE N N 124.92 0.05 . 884 104 ASN H H 8.10 0.05 . 885 104 ASN HA H 4.51 0.05 . 886 104 ASN HB2 H 2.77 0.05 . 887 104 ASN HB3 H 2.65 0.05 . 888 104 ASN C C 175.74 0.05 . 889 104 ASN CA C 55.24 0.05 . 890 104 ASN CB C 38.45 0.05 . 891 104 ASN N N 115.56 0.05 . 892 105 ASN H H 6.92 0.05 . 893 105 ASN HA H 4.54 0.05 . 894 105 ASN HB2 H 0.97 0.05 . 895 105 ASN HB3 H 1.02 0.05 . 896 105 ASN C C 173.92 0.05 . 897 105 ASN CA C 52.66 0.05 . 898 105 ASN CB C 39.41 0.05 . 899 105 ASN N N 114.34 0.05 . 900 106 TRP H H 7.87 0.05 . 901 106 TRP HA H 4.33 0.05 . 902 106 TRP HB2 H 3.09 0.05 . 903 106 TRP HB3 H 3.05 0.05 . 904 106 TRP HE1 H 10.05 0.05 . 905 106 TRP C C 175.55 0.05 . 906 106 TRP CA C 58.54 0.05 . 907 106 TRP CB C 28.25 0.05 . 908 106 TRP N N 123.79 0.05 . 909 106 TRP NE1 N 130.00 0.05 . 910 107 LYS H H 8.11 0.05 . 911 107 LYS HA H 4.35 0.05 . 912 107 LYS HB2 H 1.67 0.05 . 913 107 LYS HB3 H 1.53 0.05 . 914 107 LYS HG2 H 1.20 0.05 . 915 107 LYS C C 174.61 0.05 . 916 107 LYS CA C 55.34 0.05 . 917 107 LYS CB C 36.04 0.05 . 918 107 LYS N N 127.37 0.05 . 919 108 ASP H H 8.55 0.05 . 920 108 ASP HA H 4.56 0.05 . 921 108 ASP HB2 H 2.75 0.05 . 922 108 ASP HB3 H 2.55 0.05 . 923 108 ASP C C 176.07 0.05 . 924 108 ASP CA C 53.59 0.05 . 925 108 ASP CB C 39.73 0.05 . 926 108 ASP N N 123.14 0.05 . 927 109 TRP NE1 N 131.00 0.05 . 928 109 TRP H H 7.38 0.05 . 929 109 TRP HA H 4.47 0.05 . 930 109 TRP HB2 H 3.56 0.05 . 931 109 TRP HB3 H 2.93 0.05 . 932 109 TRP HE1 H 9.95 0.05 . 933 109 TRP C C 176.93 0.05 . 934 109 TRP CA C 56.81 0.05 . 935 109 TRP CB C 29.28 0.05 . 936 109 TRP N N 121.52 0.05 . 937 110 GLU H H 8.04 0.05 . 938 110 GLU HA H 3.94 0.05 . 939 110 GLU HB2 H 1.47 0.05 . 940 110 GLU HB3 H 1.72 0.05 . 941 110 GLU HG2 H 1.84 0.05 . 942 110 GLU C C 176.44 0.05 . 943 110 GLU CA C 58.19 0.05 . 944 110 GLU CB C 29.91 0.05 . 945 110 GLU N N 122.65 0.05 . 946 111 ASP H H 7.90 0.05 . 947 111 ASP HA H 4.61 0.05 . 948 111 ASP HB2 H 2.76 0.05 . 949 111 ASP HB3 H 2.56 0.05 . 950 111 ASP C C 175.83 0.05 . 951 111 ASP CA C 54.21 0.05 . 952 111 ASP CB C 41.32 0.05 . 953 111 ASP N N 119.29 0.05 . 954 112 ASP H H 8.03 0.05 . 955 112 ASP HA H 4.68 0.05 . 956 112 ASP HB2 H 2.75 0.05 . 957 112 ASP C C 176.35 0.05 . 958 112 ASP CA C 54.41 0.05 . 959 112 ASP CB C 41.46 0.05 . 960 112 ASP N N 120.99 0.05 . 961 113 SER H H 8.35 0.05 . 962 113 SER HA H 4.45 0.05 . 963 113 SER HB2 H 3.89 0.05 . 964 113 SER C C 174.59 0.05 . 965 113 SER CA C 58.70 0.05 . 966 113 SER CB C 64.23 0.05 . 967 113 SER N N 116.25 0.05 . 968 114 ASP H H 8.45 0.05 . 969 114 ASP HA H 4.64 0.05 . 970 114 ASP HB2 H 2.73 0.05 . 971 114 ASP HB3 H 2.66 0.05 . 972 114 ASP C C 176.42 0.05 . 973 114 ASP CA C 54.38 0.05 . 974 114 ASP CB C 41.14 0.05 . 975 114 ASP N N 122.61 0.05 . 976 115 GLU H H 8.33 0.05 . 977 115 GLU HA H 4.24 0.05 . 978 115 GLU HB2 H 1.93 0.05 . 979 115 GLU HB3 H 2.06 0.05 . 980 115 GLU HG2 H 2.26 0.05 . 981 115 GLU C C 176.31 0.05 . 982 115 GLU CA C 56.83 0.05 . 983 115 GLU CB C 30.15 0.05 . 984 115 GLU CG C 36.90 0.05 . 985 115 GLU N N 121.19 0.05 . 986 116 ASP H H 8.40 0.05 . 987 116 ASP HA H 4.59 0.05 . 988 116 ASP HB2 H 2.77 0.05 . 989 116 ASP HB3 H 2.64 0.05 . 990 116 ASP C C 176.35 0.05 . 991 116 ASP CA C 54.39 0.05 . 992 116 ASP CB C 40.98 0.05 . 993 116 ASP N N 121.20 0.05 . 994 117 MET H H 8.31 0.05 . 995 117 MET HA H 4.54 0.05 . 996 117 MET HB2 H 2.01 0.05 . 997 117 MET HB3 H 2.15 0.05 . 998 117 MET HG2 H 2.53 0.05 . 999 117 MET HG3 H 2.63 0.05 . 1000 117 MET HE H 17.06 0.05 . 1001 117 MET C C 176.33 0.05 . 1002 117 MET CA C 55.37 0.05 . 1003 117 MET CB C 32.42 0.05 . 1004 117 MET CG C 32.15 0.05 . 1005 117 MET CE C 17.07 0.05 . 1006 117 MET N N 121.19 0.05 . 1007 118 SER H H 8.34 0.05 . 1008 118 SER HA H 4.43 0.05 . 1009 118 SER HB2 H 3.87 0.05 . 1010 118 SER C C 173.48 0.05 . 1011 118 SER CA C 58.45 0.05 . 1012 118 SER CB C 63.90 0.05 . 1013 118 SER N N 117.18 0.05 . 1014 119 ASN H H 8.03 0.05 . 1015 119 ASN HA H 4.49 0.05 . 1016 119 ASN HB2 H 2.77 0.05 . 1017 119 ASN HB3 H 2.67 0.05 . 1018 119 ASN C C 179.55 0.05 . 1019 119 ASN CA C 54.90 0.05 . 1020 119 ASN CB C 40.27 0.05 . 1021 119 ASN N N 125.77 0.05 . stop_ save_