data_6822 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The Structure of the Hamp Domain Implies a Rotational Mechanism in Transmembrane Signalling ; _BMRB_accession_number 6822 _BMRB_flat_file_name bmr6822.str _Entry_type original _Submission_date 2005-09-09 _Accession_date 2005-09-29 _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 Coles M. . . 2 Truffault V. . . 3 Hulko M. . . 4 Martin J. . . 5 Lupas A. N. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 321 "13C chemical shifts" 229 "15N chemical shifts" 55 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-10-19 original author . stop_ _Original_release_date 2006-10-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The HAMP domain structure implies helix rotation in transmembrane signaling' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16959572 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hulko M. . . 2 Berndt F. . . 3 Gruber M. . . 4 Linder J. U. . 5 Truffault V. . . 6 Schultz A. . . 7 Martin J. . . 8 Schultz J. E. . 9 Lupas A. N. . 10 Coles M. . . stop_ _Journal_abbreviation Cell _Journal_volume 126 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 929 _Page_last 940 _Year 2006 _Details . loop_ _Keyword 'COMPLEMENTARY X-DA PACKING' HOMODIMER 'PARALLEL COILED-COIL' stop_ save_ ################################## # Molecular system description # ################################## save_system_AF1503 _Saveframe_category molecular_system _Mol_system_name 'hypothetical protein AF1503' _Abbreviation_common 'hypothetical protein AF1503' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'hypothetical protein AF1503 chain A' $AF1503 'hypothetical protein AF1503 chain B' $AF1503 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'hypothetical protein AF1503 chain A' 1 'hypothetical protein AF1503 chain B' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_AF1503 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'hypothetical protein AF1503' _Abbreviation_common 'hypothetical protein AF1503' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 56 _Mol_residue_sequence ; GSSTITRPIIELSNTADKIA EGNLEAEVPHQNRADEIGIL AKSIERLRRSLKVAME ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 276 GLY 2 277 SER 3 278 SER 4 279 THR 5 280 ILE 6 281 THR 7 282 ARG 8 283 PRO 9 284 ILE 10 285 ILE 11 286 GLU 12 287 LEU 13 288 SER 14 289 ASN 15 290 THR 16 291 ALA 17 292 ASP 18 293 LYS 19 294 ILE 20 295 ALA 21 296 GLU 22 297 GLY 23 298 ASN 24 299 LEU 25 300 GLU 26 301 ALA 27 302 GLU 28 303 VAL 29 304 PRO 30 305 HIS 31 306 GLN 32 307 ASN 33 308 ARG 34 309 ALA 35 310 ASP 36 311 GLU 37 312 ILE 38 313 GLY 39 314 ILE 40 315 LEU 41 316 ALA 42 317 LYS 43 318 SER 44 319 ILE 45 320 GLU 46 321 ARG 47 322 LEU 48 323 ARG 49 324 ARG 50 325 SER 51 326 LEU 52 327 LYS 53 328 VAL 54 329 ALA 55 330 MET 56 331 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 17775 HAMP-DHp 89.29 112 100.00 100.00 3.55e-25 BMRB 17776 HAMP-DHpF 89.29 112 98.00 98.00 2.08e-24 PDB 2ASW "The Solution Structure Of The Hamp Domain Of The Hypothetical Transmembrane Receptor Af1503" 100.00 56 100.00 100.00 5.25e-30 PDB 2ASX "The Solution Structure Of The Hamp Domain Of The Hypothetical Transmembrane Receptor Af1503" 100.00 56 100.00 100.00 5.25e-30 PDB 2L7H "The Solution Structure Of The Hamp Domain Of The Hypothetical Transmembrane Receptor Af1503" 96.43 58 100.00 100.00 1.95e-28 PDB 2L7I "The Solution Structure Of The Hamp Domain Of The Hypothetical Transmembrane Receptor Af1503 (A291f Variant)" 96.43 58 98.15 98.15 1.20e-27 PDB 2LFR "Solution Structure Of The Chimeric Af1503 Hamp- Envz Dhp Homodimer" 91.07 114 98.04 100.00 1.94e-25 PDB 2Y0Q "The Mechanisms Of Hamp-Mediated Signaling In Transmembrane Receptors - The A291c Mutant" 96.43 54 98.15 98.15 5.56e-28 PDB 2Y0T "The Mechanisms Of Hamp-Mediated Signaling In Transmembrane Receptors - The A291f Mutant" 96.43 54 98.15 98.15 1.10e-27 PDB 2Y20 "The Mechanisms Of Hamp-Mediated Signaling In Transmembrane Receptors - The A291i Mutant" 96.43 58 98.15 98.15 1.58e-27 PDB 2Y21 "The Mechanisms Of Hamp-Mediated Signaling In Transmembrane Receptors - The A291v Mutant" 96.43 56 98.15 98.15 8.40e-28 PDB 3ZCC "High Resolution Structure Of The Asymmetric R333g Hamp-Dhp Mutant" 89.29 114 100.00 100.00 3.66e-25 PDB 3ZRV "The High Resolution Structure Of A Dimeric Hamp-Dhp Fusion Displays Asymmetry - A291f Mutant" 89.29 116 98.00 98.00 2.30e-24 PDB 3ZRW "The Structure Of The Dimeric Hamp-Dhp Fusion A291v Mutant" 89.29 116 98.00 98.00 1.54e-24 PDB 3ZRX "The High Resolution Structure Of A Dimeric Hamp-Dhp Fusion Displays Strong Asymmetry" 89.29 115 98.00 98.00 2.39e-24 PDB 3ZX6 "Structure Of Hamp(af1503)-tsr Fusion - Hamp (a291v) Mutant" 87.50 341 97.96 97.96 2.18e-23 PDB 4CQ4 "C-terminal Fragment Of Af1503-sol: Transmembrane Receptor Af1503 From Archaeoglobus Fulgidus Engineered For Solubility" 98.21 309 98.18 100.00 3.60e-27 PDB 4CTI "Escherichia Coli Envz Histidine Kinase Catalytic Part Fused To Archaeoglobus Fulgidus Af1503 Hamp Domain" 89.29 273 98.00 98.00 6.12e-23 PDB 4GN0 "De Novo Phasing Of A Hamp-complex Using An Improved Arcimboldo Method" 98.21 105 98.18 100.00 1.10e-28 GB AAB89755 "predicted coding region AF_1503 [Archaeoglobus fulgidus DSM 4304]" 98.21 338 98.18 100.00 3.25e-27 GB AIG98513 "HAMP domain protein [Archaeoglobus fulgidus DSM 8774]" 98.21 337 98.18 100.00 2.28e-25 REF NP_070332 "hypothetical protein AF1503 [Archaeoglobus fulgidus DSM 4304]" 98.21 338 98.18 100.00 3.25e-27 REF WP_010879000 "hypothetical protein [Archaeoglobus fulgidus]" 98.21 338 98.18 100.00 3.25e-27 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $AF1503 'Archaeoglobus fulgidus' 2234 Archaea . Archaeoglobus fulgidus 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 $AF1503 'recombinant technology' 'E. Coli' . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AF1503 1.0 mM . 'phosphate buffer' 20 mM . NACL 150 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AF1503 1.0 mM [U-15N] 'phosphate buffer' 20 mM . NACL 150 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AF1503 1.0 mM '[U-13C; U-15N]' 'phosphate buffer' 20 mM . NACL 150 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version NIH-2.9.7 loop_ _Task refinement 'structure solution' stop_ _Details . save_ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 3.5 loop_ _Task processing stop_ _Details . save_ save_Sparky _Saveframe_category software _Name SPARKY _Version 3.110 loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_2D_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_HNHA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_2D_12C-FILTERED/13C-EDITED_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 12C-FILTERED/13C-EDITED NOESY' _Sample_label . save_ save_3D-NNH-NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-NNH-NOESY _Sample_label . save_ save_3D-CNH-NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-CNH-NOESY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 12C-FILTERED/13C-EDITED NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-NNH-NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-CNH-NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 150 . mM pH 7.2 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 2.61 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D 15N-separated NOESY' '2D NOESY' HNHA '2D 12C-FILTERED/13C-EDITED NOESY' 3D-NNH-NOESY 3D-CNH-NOESY stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'hypothetical protein AF1503 chain A' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 3 SER HA H 4.41 0.02 1 2 . 3 SER HB2 H 3.91 0.02 1 3 . 3 SER HB3 H 3.88 0.02 1 4 . 3 SER CA C 59.66 0.05 1 5 . 3 SER CB C 63.49 0.05 1 6 . 4 THR HA H 4.22 0.02 1 7 . 4 THR HB H 4.26 0.02 1 8 . 4 THR HG2 H 1.22 0.02 1 9 . 4 THR C C 175.07 0.05 1 10 . 4 THR CA C 63.11 0.05 1 11 . 4 THR CB C 69.12 0.05 1 12 . 4 THR CG2 C 21.92 0.05 1 13 . 5 ILE H H 7.81 0.02 1 14 . 5 ILE HA H 4.17 0.02 1 15 . 5 ILE HB H 1.86 0.02 1 16 . 5 ILE HG12 H 1.34 0.02 2 17 . 5 ILE HG13 H 1.13 0.02 2 18 . 5 ILE HG2 H 0.74 0.02 1 19 . 5 ILE HD1 H 0.69 0.02 1 20 . 5 ILE C C 175.85 0.05 1 21 . 5 ILE CA C 61.19 0.05 1 22 . 5 ILE CB C 38.79 0.05 1 23 . 5 ILE CG1 C 27.18 0.05 1 24 . 5 ILE CG2 C 17.83 0.05 1 25 . 5 ILE CD1 C 12.77 0.05 1 26 . 5 ILE N N 118.74 0.05 1 27 . 6 THR H H 7.77 0.02 1 28 . 6 THR HA H 3.81 0.02 1 29 . 6 THR HB H 4.08 0.02 1 30 . 6 THR HG2 H 1.14 0.02 1 31 . 6 THR C C 175.53 0.05 1 32 . 6 THR CA C 65.56 0.05 1 33 . 6 THR CB C 68.77 0.05 1 34 . 6 THR CG2 C 22.24 0.05 1 35 . 6 THR N N 114.25 0.05 1 36 . 7 ARG H H 8.25 0.02 1 37 . 7 ARG HA H 4.22 0.02 1 38 . 7 ARG HB2 H 1.93 0.02 1 39 . 7 ARG HB3 H 1.93 0.02 1 40 . 7 ARG HG2 H 1.55 0.02 1 41 . 7 ARG HG3 H 1.55 0.02 1 42 . 7 ARG HD2 H 3.17 0.02 1 43 . 7 ARG HD3 H 3.17 0.02 1 44 . 7 ARG CA C 59.92 0.05 1 45 . 7 ARG CB C 26.89 0.05 1 46 . 7 ARG CG C 27.58 0.05 1 47 . 7 ARG CD C 43.32 0.05 1 48 . 7 ARG N N 120.46 0.05 1 49 . 8 PRO HA H 4.23 0.02 1 50 . 8 PRO HB2 H 1.28 0.02 1 51 . 8 PRO HB3 H 1.11 0.02 1 52 . 8 PRO HG2 H 1.89 0.02 2 53 . 8 PRO HG3 H 1.60 0.02 2 54 . 8 PRO HD2 H 3.46 0.02 2 55 . 8 PRO HD3 H 3.43 0.02 2 56 . 8 PRO CA C 65.94 0.05 1 57 . 8 PRO CB C 30.51 0.05 1 58 . 8 PRO CG C 27.84 0.05 1 59 . 8 PRO CD C 49.47 0.05 1 60 . 9 ILE H H 7.28 0.02 1 61 . 9 ILE HA H 3.49 0.02 1 62 . 9 ILE HB H 2.00 0.02 1 63 . 9 ILE HG12 H 1.64 0.02 2 64 . 9 ILE HG13 H 0.94 0.02 2 65 . 9 ILE HG2 H 0.69 0.02 1 66 . 9 ILE HD1 H 0.62 0.02 1 67 . 9 ILE C C 177.82 0.05 1 68 . 9 ILE CA C 65.28 0.05 1 69 . 9 ILE CB C 36.54 0.05 1 70 . 9 ILE CG1 C 29.26 0.05 1 71 . 9 ILE CG2 C 18.76 0.05 1 72 . 9 ILE CD1 C 13.10 0.05 1 73 . 9 ILE N N 115.70 0.05 1 74 . 10 ILE H H 7.88 0.02 1 75 . 10 ILE HA H 3.77 0.02 1 76 . 10 ILE HB H 2.16 0.02 1 77 . 10 ILE HG12 H 1.54 0.02 2 78 . 10 ILE HG13 H 1.44 0.02 2 79 . 10 ILE HG2 H 0.89 0.02 1 80 . 10 ILE HD1 H 0.78 0.02 1 81 . 10 ILE C C 178.81 0.05 1 82 . 10 ILE CA C 62.70 0.05 1 83 . 10 ILE CB C 36.40 0.05 1 84 . 10 ILE CG1 C 27.56 0.05 1 85 . 10 ILE CG2 C 16.95 0.05 1 86 . 10 ILE CD1 C 10.77 0.05 1 87 . 10 ILE N N 121.88 0.05 1 88 . 11 GLU H H 8.52 0.02 1 89 . 11 GLU HA H 4.08 0.02 1 90 . 11 GLU HB2 H 2.00 0.02 1 91 . 11 GLU HB3 H 2.27 0.02 1 92 . 11 GLU HG2 H 2.50 0.02 1 93 . 11 GLU HG3 H 2.50 0.02 1 94 . 11 GLU C C 180.98 0.05 1 95 . 11 GLU CA C 59.63 0.05 1 96 . 11 GLU CB C 29.53 0.05 1 97 . 11 GLU CG C 36.86 0.05 1 98 . 11 GLU N N 120.42 0.05 1 99 . 12 LEU H H 8.53 0.02 1 100 . 12 LEU HA H 4.01 0.02 1 101 . 12 LEU HB2 H 2.05 0.02 1 102 . 12 LEU HB3 H 1.14 0.02 1 103 . 12 LEU HG H 1.81 0.02 1 104 . 12 LEU HD1 H 0.82 0.02 1 105 . 12 LEU HD2 H 0.99 0.02 1 106 . 12 LEU C C 178.03 0.05 1 107 . 12 LEU CA C 58.31 0.05 1 108 . 12 LEU CB C 41.50 0.05 1 109 . 12 LEU CG C 27.88 0.05 1 110 . 12 LEU CD1 C 25.87 0.05 1 111 . 12 LEU CD2 C 23.35 0.05 1 112 . 12 LEU N N 121.37 0.05 1 113 . 13 SER H H 8.35 0.02 1 114 . 13 SER HA H 4.17 0.02 1 115 . 13 SER HB2 H 3.91 0.02 1 116 . 13 SER HB3 H 3.91 0.02 1 117 . 13 SER HG H 5.15 0.02 1 118 . 13 SER C C 175.66 0.05 1 119 . 13 SER CA C 61.60 0.05 1 120 . 13 SER CB C 62.42 0.05 1 121 . 13 SER N N 117.28 0.05 1 122 . 14 ASN H H 8.67 0.02 1 123 . 14 ASN HA H 4.45 0.02 1 124 . 14 ASN HB2 H 2.97 0.02 1 125 . 14 ASN HB3 H 2.79 0.02 1 126 . 14 ASN HD21 H 7.69 0.02 1 127 . 14 ASN HD22 H 6.90 0.02 1 128 . 14 ASN C C 178.48 0.05 1 129 . 14 ASN CA C 55.87 0.05 1 130 . 14 ASN CB C 38.09 0.05 1 131 . 14 ASN N N 118.86 0.05 1 132 . 14 ASN ND2 N 111.91 0.05 1 133 . 15 THR H H 8.05 0.02 1 134 . 15 THR HA H 3.79 0.02 1 135 . 15 THR HB H 4.30 0.02 1 136 . 15 THR HG1 H 5.02 0.02 1 137 . 15 THR HG2 H 1.23 0.02 1 138 . 15 THR C C 175.03 0.05 1 139 . 15 THR CA C 67.79 0.05 1 140 . 15 THR CB C 68.42 0.05 1 141 . 15 THR CG2 C 22.11 0.05 1 142 . 15 THR N N 117.58 0.05 1 143 . 16 ALA H H 8.55 0.02 1 144 . 16 ALA HA H 3.83 0.02 1 145 . 16 ALA HB H 1.39 0.02 1 146 . 16 ALA C C 178.47 0.05 1 147 . 16 ALA CA C 55.74 0.05 1 148 . 16 ALA CB C 17.53 0.05 1 149 . 16 ALA N N 124.29 0.05 1 150 . 17 ASP H H 8.30 0.02 1 151 . 17 ASP HA H 4.33 0.02 1 152 . 17 ASP HB2 H 2.55 0.02 1 153 . 17 ASP HB3 H 2.84 0.02 1 154 . 17 ASP C C 178.42 0.05 1 155 . 17 ASP CA C 57.53 0.05 1 156 . 17 ASP CB C 40.13 0.05 1 157 . 17 ASP N N 117.62 0.05 1 158 . 18 LYS H H 7.66 0.02 1 159 . 18 LYS HA H 4.01 0.02 1 160 . 18 LYS HB2 H 2.10 0.02 1 161 . 18 LYS HB3 H 1.80 0.02 1 162 . 18 LYS HG2 H 1.66 0.02 2 163 . 18 LYS HG3 H 1.54 0.02 2 164 . 18 LYS HD2 H 1.65 0.02 2 165 . 18 LYS HD3 H 1.59 0.02 2 166 . 18 LYS HE2 H 2.89 0.02 1 167 . 18 LYS HE3 H 2.89 0.02 1 168 . 18 LYS C C 180.17 0.05 1 169 . 18 LYS CA C 59.02 0.05 1 170 . 18 LYS CB C 31.97 0.05 1 171 . 18 LYS CG C 25.12 0.05 1 172 . 18 LYS CD C 29.36 0.05 1 173 . 18 LYS CE C 41.98 0.05 1 174 . 18 LYS N N 118.88 0.05 1 175 . 19 ILE H H 8.22 0.02 1 176 . 19 ILE HA H 3.63 0.02 1 177 . 19 ILE HB H 1.82 0.02 1 178 . 19 ILE HG12 H 1.85 0.02 2 179 . 19 ILE HG13 H 0.94 0.02 2 180 . 19 ILE HG2 H 0.68 0.02 1 181 . 19 ILE HD1 H 0.56 0.02 1 182 . 19 ILE C C 178.92 0.05 1 183 . 19 ILE CA C 64.58 0.05 1 184 . 19 ILE CB C 38.26 0.05 1 185 . 19 ILE CG1 C 29.14 0.05 1 186 . 19 ILE CG2 C 18.73 0.05 1 187 . 19 ILE CD1 C 14.34 0.05 1 188 . 19 ILE N N 122.37 0.05 1 189 . 20 ALA H H 8.55 0.02 1 190 . 20 ALA HA H 3.79 0.02 1 191 . 20 ALA HB H 1.37 0.02 1 192 . 20 ALA C C 179.39 0.05 1 193 . 20 ALA CA C 54.87 0.05 1 194 . 20 ALA CB C 17.68 0.05 1 195 . 20 ALA N N 122.44 0.05 1 196 . 21 GLU H H 7.63 0.02 1 197 . 21 GLU HA H 4.16 0.02 1 198 . 21 GLU HB2 H 2.18 0.02 1 199 . 21 GLU HB3 H 1.99 0.02 1 200 . 21 GLU HG2 H 2.44 0.02 2 201 . 21 GLU HG3 H 2.30 0.02 2 202 . 21 GLU C C 176.56 0.05 1 203 . 21 GLU CA C 56.40 0.05 1 204 . 21 GLU CB C 29.75 0.05 1 205 . 21 GLU CG C 36.46 0.05 1 206 . 21 GLU N N 115.34 0.05 1 207 . 22 GLY H H 7.87 0.02 1 208 . 22 GLY HA2 H 3.51 0.02 1 209 . 22 GLY HA3 H 4.50 0.02 1 210 . 22 GLY C C 174.16 0.05 1 211 . 22 GLY CA C 44.86 0.05 1 212 . 22 GLY N N 105.98 0.05 1 213 . 23 ASN H H 8.04 0.02 1 214 . 23 ASN HA H 4.92 0.02 1 215 . 23 ASN HB2 H 2.54 0.02 1 216 . 23 ASN HB3 H 2.71 0.02 1 217 . 23 ASN HD21 H 7.43 0.02 1 218 . 23 ASN HD22 H 6.95 0.02 1 219 . 23 ASN C C 174.56 0.05 1 220 . 23 ASN CA C 51.39 0.05 1 221 . 23 ASN CB C 36.41 0.05 1 222 . 23 ASN N N 119.9 0.05 1 223 . 23 ASN ND2 N 110.97 0.05 1 224 . 24 LEU H H 7.86 0.02 1 225 . 24 LEU HA H 3.93 0.02 1 226 . 24 LEU HB2 H 1.78 0.02 1 227 . 24 LEU HB3 H 1.38 0.02 1 228 . 24 LEU HG H 1.65 0.02 1 229 . 24 LEU HD1 H 0.74 0.02 1 230 . 24 LEU HD2 H 0.89 0.02 1 231 . 24 LEU C C 176.39 0.05 1 232 . 24 LEU CA C 56.03 0.05 1 233 . 24 LEU CB C 41.24 0.05 1 234 . 24 LEU CG C 26.86 0.05 1 235 . 24 LEU CD1 C 23.21 0.05 1 236 . 24 LEU CD2 C 25.91 0.05 1 237 . 24 LEU N N 119.97 0.05 1 238 . 25 GLU H H 7.82 0.02 1 239 . 25 GLU HA H 4.23 0.02 1 240 . 25 GLU HB2 H 1.72 0.02 1 241 . 25 GLU HB3 H 2.21 0.02 1 242 . 25 GLU HG2 H 2.21 0.02 2 243 . 25 GLU HG3 H 2.09 0.02 2 244 . 25 GLU C C 176.05 0.05 1 245 . 25 GLU CA C 54.64 0.05 1 246 . 25 GLU CB C 28.94 0.05 1 247 . 25 GLU CG C 35.78 0.05 1 248 . 25 GLU N N 113.68 0.05 1 249 . 26 ALA H H 6.77 0.02 1 250 . 26 ALA HA H 3.85 0.02 1 251 . 26 ALA HB H 1.14 0.02 1 252 . 26 ALA C C 175.39 0.05 1 253 . 26 ALA CA C 52.68 0.05 1 254 . 26 ALA CB C 18.38 0.05 1 255 . 26 ALA N N 123.96 0.05 1 256 . 27 GLU H H 7.92 0.02 1 257 . 27 GLU HA H 4.08 0.02 1 258 . 27 GLU HB2 H 1.76 0.02 2 259 . 27 GLU HB3 H 1.74 0.02 2 260 . 27 GLU HG2 H 2.08 0.02 2 261 . 27 GLU HG3 H 1.90 0.02 2 262 . 27 GLU C C 176.51 0.05 1 263 . 27 GLU CA C 55.15 0.05 1 264 . 27 GLU CB C 30.16 0.05 1 265 . 27 GLU CG C 36.19 0.05 1 266 . 27 GLU N N 120.17 0.05 1 267 . 28 VAL H H 8.96 0.02 1 268 . 28 VAL HA H 4.22 0.02 1 269 . 28 VAL HB H 2.09 0.02 1 270 . 28 VAL HG1 H 1.09 0.02 1 271 . 28 VAL HG2 H 0.87 0.02 1 272 . 28 VAL CA C 60.30 0.05 1 273 . 28 VAL CB C 31.76 0.05 1 274 . 28 VAL CG1 C 20.93 0.05 1 275 . 28 VAL CG2 C 22.43 0.05 1 276 . 28 VAL N N 129.02 0.05 1 277 . 29 PRO HA H 4.40 0.02 1 278 . 29 PRO HB2 H 0.93 0.02 1 279 . 29 PRO HB3 H 1.88 0.02 1 280 . 29 PRO HG2 H 1.53 0.02 1 281 . 29 PRO HG3 H 1.81 0.02 1 282 . 29 PRO HD2 H 3.62 0.02 1 283 . 29 PRO HD3 H 4.00 0.02 1 284 . 29 PRO CA C 62.79 0.05 1 285 . 29 PRO CB C 32.06 0.05 1 286 . 29 PRO CG C 25.77 0.05 1 287 . 29 PRO CD C 51.27 0.05 1 288 . 30 HIS H H 7.80 0.02 1 289 . 30 HIS HA H 4.20 0.02 1 290 . 30 HIS HB2 H 3.30 0.02 1 291 . 30 HIS HB3 H 3.01 0.02 1 292 . 30 HIS HD2 H 6.46 0.02 1 293 . 30 HIS C C 175.59 0.05 1 294 . 30 HIS CA C 57.95 0.05 1 295 . 30 HIS CB C 27.86 0.05 1 296 . 30 HIS CD2 C 116.52 0.05 1 297 . 30 HIS N N 126.12 0.05 1 298 . 31 GLN H H 8.02 0.02 1 299 . 31 GLN HA H 3.99 0.02 1 300 . 31 GLN HB2 H 2.13 0.02 1 301 . 31 GLN HB3 H 1.79 0.02 1 302 . 31 GLN HG2 H 1.57 0.02 1 303 . 31 GLN HG3 H 2.17 0.02 1 304 . 31 GLN HE21 H 8.04 0.02 1 305 . 31 GLN HE22 H 6.37 0.02 1 306 . 31 GLN C C 176.29 0.05 1 307 . 31 GLN CA C 58.97 0.05 1 308 . 31 GLN CB C 30.61 0.05 1 309 . 31 GLN CG C 35.51 0.05 1 310 . 31 GLN N N 114.69 0.05 1 311 . 31 GLN NE2 N 113.27 0.05 1 312 . 32 ASN H H 8.38 0.02 1 313 . 32 ASN HA H 4.68 0.02 1 314 . 32 ASN HB2 H 2.75 0.02 1 315 . 32 ASN HB3 H 2.75 0.02 1 316 . 32 ASN HD21 H 7.49 0.02 1 317 . 32 ASN HD22 H 6.84 0.02 1 318 . 32 ASN C C 175.61 0.05 1 319 . 32 ASN CA C 52.68 0.05 1 320 . 32 ASN CB C 37.63 0.05 1 321 . 32 ASN N N 112.99 0.05 1 322 . 32 ASN ND2 N 113.16 0.05 1 323 . 33 ARG H H 7.15 0.02 1 324 . 33 ARG HA H 4.16 0.02 1 325 . 33 ARG HB2 H 1.52 0.02 1 326 . 33 ARG HB3 H 2.01 0.02 1 327 . 33 ARG HG2 H 1.58 0.02 2 328 . 33 ARG HG3 H 1.62 0.02 2 329 . 33 ARG HD2 H 3.47 0.02 1 330 . 33 ARG HD3 H 2.86 0.02 1 331 . 33 ARG HE H 8.37 0.02 1 332 . 33 ARG CA C 56.59 0.05 1 333 . 33 ARG CB C 33.00 0.05 1 334 . 33 ARG CG C 28.34 0.05 1 335 . 33 ARG CD C 44.23 0.05 1 336 . 33 ARG N N 119.62 0.05 1 337 . 33 ARG NE N 83.94 0.05 1 338 . 34 ALA HA H 4.50 0.02 1 339 . 34 ALA HB H 1.36 0.02 1 340 . 34 ALA C C 176.67 0.05 1 341 . 34 ALA CA C 51.70 0.05 1 342 . 34 ALA CB C 18.73 0.05 1 343 . 35 ASP H H 7.43 0.02 1 344 . 35 ASP HA H 4.66 0.02 1 345 . 35 ASP HB2 H 3.09 0.02 1 346 . 35 ASP HB3 H 2.78 0.02 1 347 . 35 ASP C C 176.74 0.05 1 348 . 35 ASP CA C 52.05 0.05 1 349 . 35 ASP CB C 41.51 0.05 1 350 . 35 ASP N N 117.49 0.05 1 351 . 36 GLU H H 10.15 0.02 1 352 . 36 GLU HA H 3.87 0.02 1 353 . 36 GLU HB2 H 1.90 0.02 1 354 . 36 GLU HB3 H 1.90 0.02 1 355 . 36 GLU HG2 H 2.38 0.02 1 356 . 36 GLU HG3 H 2.38 0.02 1 357 . 36 GLU C C 177.44 0.05 1 358 . 36 GLU CA C 60.46 0.05 1 359 . 36 GLU CB C 27.66 0.05 1 360 . 36 GLU CG C 36.88 0.05 1 361 . 36 GLU N N 118.17 0.05 1 362 . 37 ILE H H 7.40 0.02 1 363 . 37 ILE HA H 3.56 0.02 1 364 . 37 ILE HB H 1.99 0.02 1 365 . 37 ILE HG12 H 1.38 0.02 2 366 . 37 ILE HG13 H 1.22 0.02 2 367 . 37 ILE HG2 H 0.61 0.02 1 368 . 37 ILE HD1 H 0.67 0.02 1 369 . 37 ILE C C 177.46 0.05 1 370 . 37 ILE CA C 62.70 0.05 1 371 . 37 ILE CB C 35.45 0.05 1 372 . 37 ILE CG1 C 28.36 0.05 1 373 . 37 ILE CG2 C 17.97 0.05 1 374 . 37 ILE CD1 C 10.77 0.05 1 375 . 37 ILE N N 118.20 0.05 1 376 . 38 GLY H H 7.47 0.02 1 377 . 38 GLY HA2 H 4.41 0.02 1 378 . 38 GLY HA3 H 4.00 0.02 1 379 . 38 GLY C C 176.20 0.05 1 380 . 38 GLY CA C 46.94 0.05 1 381 . 38 GLY N N 108.16 0.05 1 382 . 39 ILE H H 7.38 0.02 1 383 . 39 ILE HA H 3.61 0.02 1 384 . 39 ILE HB H 1.92 0.02 1 385 . 39 ILE HG12 H 1.08 0.02 1 386 . 39 ILE HG13 H 1.60 0.02 1 387 . 39 ILE HG2 H 0.92 0.02 1 388 . 39 ILE HD1 H 0.77 0.02 1 389 . 39 ILE C C 179.07 0.05 1 390 . 39 ILE CA C 64.75 0.05 1 391 . 39 ILE CB C 37.74 0.05 1 392 . 39 ILE CG1 C 28.53 0.05 1 393 . 39 ILE CG2 C 16.64 0.05 1 394 . 39 ILE CD1 C 12.67 0.05 1 395 . 39 ILE N N 121.74 0.05 1 396 . 40 LEU H H 7.78 0.02 1 397 . 40 LEU HA H 4.09 0.02 1 398 . 40 LEU HB2 H 1.49 0.02 1 399 . 40 LEU HB3 H 1.94 0.02 1 400 . 40 LEU HG H 1.51 0.02 1 401 . 40 LEU HD1 H 0.85 0.02 1 402 . 40 LEU HD2 H 0.89 0.02 1 403 . 40 LEU C C 178.56 0.05 1 404 . 40 LEU CA C 57.62 0.05 1 405 . 40 LEU CB C 41.29 0.05 1 406 . 40 LEU CG C 27.33 0.05 1 407 . 40 LEU CD1 C 21.66 0.05 1 408 . 40 LEU CD2 C 27.89 0.05 1 409 . 40 LEU N N 121.15 0.05 1 410 . 41 ALA H H 9.01 0.02 1 411 . 41 ALA HA H 3.80 0.02 1 412 . 41 ALA HB H 1.56 0.02 1 413 . 41 ALA C C 179.70 0.05 1 414 . 41 ALA CA C 55.92 0.05 1 415 . 41 ALA CB C 19.76 0.05 1 416 . 41 ALA N N 123.31 0.05 1 417 . 42 LYS H H 8.28 0.02 1 418 . 42 LYS HA H 3.90 0.02 1 419 . 42 LYS HB2 H 2.09 0.02 1 420 . 42 LYS HB3 H 1.79 0.02 1 421 . 42 LYS HG2 H 1.94 0.02 2 422 . 42 LYS HG3 H 1.57 0.02 2 423 . 42 LYS HD2 H 1.76 0.02 1 424 . 42 LYS HD3 H 1.76 0.02 1 425 . 42 LYS HE2 H 3.03 0.02 2 426 . 42 LYS HE3 H 3.00 0.02 2 427 . 42 LYS C C 179.73 0.05 1 428 . 42 LYS CA C 60.43 0.05 1 429 . 42 LYS CB C 32.19 0.05 1 430 . 42 LYS CG C 26.44 0.05 1 431 . 42 LYS CD C 29.79 0.05 1 432 . 42 LYS CE C 42.02 0.05 1 433 . 42 LYS N N 116.56 0.05 1 434 . 43 SER H H 8.01 0.02 1 435 . 43 SER HA H 4.31 0.02 1 436 . 43 SER HB2 H 3.95 0.02 1 437 . 43 SER HB3 H 4.05 0.02 1 438 . 43 SER HG H 5.13 0.02 1 439 . 43 SER C C 177.43 0.05 1 440 . 43 SER CA C 62.54 0.05 1 441 . 43 SER CB C 62.69 0.05 1 442 . 43 SER N N 119.03 0.05 1 443 . 44 ILE H H 8.19 0.02 1 444 . 44 ILE HA H 3.60 0.02 1 445 . 44 ILE HB H 1.98 0.02 1 446 . 44 ILE HG12 H 1.67 0.02 2 447 . 44 ILE HG13 H 0.95 0.02 2 448 . 44 ILE HG2 H 0.76 0.02 1 449 . 44 ILE HD1 H 0.69 0.02 1 450 . 44 ILE CA C 64.93 0.05 1 451 . 44 ILE CB C 36.42 0.05 1 452 . 44 ILE CG1 C 29.24 0.05 1 453 . 44 ILE CG2 C 16.59 0.05 1 454 . 44 ILE CD1 C 12.94 0.05 1 455 . 44 ILE N N 123.90 0.05 1 456 . 45 GLU H H 8.33 0.02 1 457 . 45 GLU HA H 4.60 0.02 1 458 . 45 GLU HB2 H 1.89 0.02 1 459 . 45 GLU HB3 H 1.89 0.02 1 460 . 45 GLU HG2 H 2.02 0.02 1 461 . 45 GLU HG3 H 2.55 0.02 1 462 . 45 GLU C C 178.19 0.05 1 463 . 45 GLU CA C 58.43 0.05 1 464 . 45 GLU CB C 27.70 0.05 1 465 . 45 GLU CG C 33.71 0.05 1 466 . 45 GLU N N 122.80 0.05 1 467 . 46 ARG H H 7.91 0.02 1 468 . 46 ARG HA H 3.90 0.02 1 469 . 46 ARG HB2 H 2.06 0.02 1 470 . 46 ARG HB3 H 1.76 0.02 1 471 . 46 ARG HG2 H 1.90 0.02 2 472 . 46 ARG HG3 H 1.44 0.02 2 473 . 46 ARG HD2 H 3.17 0.02 1 474 . 46 ARG HD3 H 3.17 0.02 1 475 . 46 ARG C C 179.95 0.05 1 476 . 46 ARG CA C 60.27 0.05 1 477 . 46 ARG CB C 29.62 0.05 1 478 . 46 ARG CG C 28.69 0.05 1 479 . 46 ARG CD C 43.55 0.05 1 480 . 46 ARG N N 119.26 0.05 1 481 . 47 LEU H H 7.82 0.02 1 482 . 47 LEU HA H 4.00 0.02 1 483 . 47 LEU HB2 H 2.14 0.02 1 484 . 47 LEU HB3 H 1.45 0.02 1 485 . 47 LEU HG H 1.75 0.02 1 486 . 47 LEU HD1 H 0.81 0.02 1 487 . 47 LEU HD2 H 0.89 0.02 1 488 . 47 LEU C C 178.04 0.05 1 489 . 47 LEU CA C 58.36 0.05 1 490 . 47 LEU CB C 41.83 0.05 1 491 . 47 LEU CG C 26.96 0.05 1 492 . 47 LEU CD1 C 24.24 0.05 1 493 . 47 LEU CD2 C 25.91 0.05 1 494 . 47 LEU N N 121.29 0.05 1 495 . 48 ARG H H 8.67 0.02 1 496 . 48 ARG HA H 3.65 0.02 1 497 . 48 ARG HB2 H 1.63 0.02 1 498 . 48 ARG HB3 H 2.34 0.02 1 499 . 48 ARG HG2 H 1.46 0.02 2 500 . 48 ARG HG3 H 1.35 0.02 2 501 . 48 ARG HD2 H 3.47 0.02 1 502 . 48 ARG HD3 H 2.71 0.02 1 503 . 48 ARG HE H 8.74 0.02 1 504 . 48 ARG C C 178.12 0.05 1 505 . 48 ARG CA C 60.36 0.05 1 506 . 48 ARG CB C 30.53 0.05 1 507 . 48 ARG CG C 27.31 0.05 1 508 . 48 ARG CD C 42.97 0.05 1 509 . 48 ARG N N 121.3 0.05 1 510 . 48 ARG NE N 83.96 0.05 1 511 . 49 ARG H H 8.35 0.02 1 512 . 49 ARG HA H 3.80 0.02 1 513 . 49 ARG HB2 H 1.88 0.02 1 514 . 49 ARG HB3 H 1.88 0.02 1 515 . 49 ARG HG2 H 1.89 0.02 2 516 . 49 ARG HG3 H 1.50 0.02 2 517 . 49 ARG HD2 H 3.13 0.02 2 518 . 49 ARG HD3 H 3.03 0.02 2 519 . 49 ARG C C 179.06 0.05 1 520 . 49 ARG CA C 59.71 0.05 1 521 . 49 ARG CB C 29.54 0.05 1 522 . 49 ARG CG C 28.09 0.05 1 523 . 49 ARG CD C 43.42 0.05 1 524 . 49 ARG N N 116.39 0.05 1 525 . 50 SER H H 8.15 0.02 1 526 . 50 SER HA H 4.21 0.02 1 527 . 50 SER HB2 H 3.96 0.02 1 528 . 50 SER HB3 H 3.96 0.02 1 529 . 50 SER HG H 5.12 0.02 1 530 . 50 SER C C 176.05 0.05 1 531 . 50 SER CA C 62.16 0.05 1 532 . 50 SER CB C 62.55 0.05 1 533 . 50 SER N N 116.08 0.05 1 534 . 51 LEU H H 8.22 0.02 1 535 . 51 LEU HA H 3.93 0.02 1 536 . 51 LEU HB2 H 1.51 0.02 1 537 . 51 LEU HB3 H 1.65 0.02 1 538 . 51 LEU HG H 1.50 0.02 1 539 . 51 LEU HD1 H 0.70 0.02 1 540 . 51 LEU HD2 H 0.71 0.02 1 541 . 51 LEU C C 177.38 0.05 1 542 . 51 LEU CA C 57.68 0.05 1 543 . 51 LEU CB C 41.66 0.05 1 544 . 51 LEU CG C 27.33 0.05 1 545 . 51 LEU CD1 C 25.54 0.05 1 546 . 51 LEU CD2 C 24.41 0.05 1 547 . 51 LEU N N 124.76 0.05 1 548 . 52 LYS H H 8.21 0.02 1 549 . 52 LYS HA H 3.86 0.02 1 550 . 52 LYS HB2 H 1.90 0.02 1 551 . 52 LYS HB3 H 1.87 0.02 1 552 . 52 LYS HG2 H 1.46 0.02 1 553 . 52 LYS HG3 H 1.35 0.02 1 554 . 52 LYS HD2 H 1.60 0.02 1 555 . 52 LYS HD3 H 1.49 0.02 1 556 . 52 LYS HE2 H 2.90 0.02 1 557 . 52 LYS HE3 H 2.90 0.02 1 558 . 52 LYS C C 179.05 0.05 1 559 . 52 LYS CA C 59.70 0.05 1 560 . 52 LYS CB C 32.06 0.05 1 561 . 52 LYS CG C 25.13 0.05 1 562 . 52 LYS CD C 29.10 0.05 1 563 . 52 LYS CE C 41.43 0.05 1 564 . 52 LYS N N 118.52 0.05 1 565 . 53 VAL H H 7.78 0.02 1 566 . 53 VAL HA H 3.78 0.02 1 567 . 53 VAL HB H 2.08 0.02 1 568 . 53 VAL HG1 H 0.93 0.02 1 569 . 53 VAL HG2 H 1.05 0.02 1 570 . 53 VAL C C 178.20 0.05 1 571 . 53 VAL CA C 65.13 0.05 1 572 . 53 VAL CB C 31.83 0.05 1 573 . 53 VAL CG1 C 21.15 0.05 1 574 . 53 VAL CG2 C 22.57 0.05 1 575 . 53 VAL N N 116.91 0.05 1 576 . 54 ALA H H 7.64 0.02 1 577 . 54 ALA HA H 4.18 0.02 1 578 . 54 ALA HB H 1.41 0.02 1 579 . 54 ALA C C 178.44 0.05 1 580 . 54 ALA CA C 53.91 0.05 1 581 . 54 ALA CB C 19.09 0.05 1 582 . 54 ALA N N 121.39 0.05 1 583 . 55 MET H H 7.64 0.02 1 584 . 55 MET HA H 4.49 0.02 1 585 . 55 MET HB2 H 1.92 0.02 1 586 . 55 MET HB3 H 2.24 0.02 1 587 . 55 MET HG2 H 2.61 0.02 2 588 . 55 MET HG3 H 2.56 0.02 2 589 . 55 MET HE H 2.06 0.02 1 590 . 55 MET C C 175.99 0.05 1 591 . 55 MET CA C 55.59 0.05 1 592 . 55 MET CB C 32.99 0.05 1 593 . 55 MET CG C 32.57 0.05 1 594 . 55 MET CE C 16.57 0.05 1 595 . 55 MET N N 114.52 0.05 1 596 . 56 GLU H H 7.47 0.02 1 597 . 56 GLU HA H 4.00 0.02 1 598 . 56 GLU HB2 H 1.99 0.02 1 599 . 56 GLU HB3 H 1.99 0.02 1 600 . 56 GLU HG2 H 2.39 0.02 2 601 . 56 GLU HG3 H 2.24 0.02 2 602 . 56 GLU CA C 58.63 0.05 1 603 . 56 GLU CB C 30.60 0.05 1 604 . 56 GLU CG C 36.77 0.05 1 605 . 56 GLU N N 126.17 0.05 1 stop_ save_