data_6444 #Corrected using PDB structure: 1Y93A # #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 # 18 T HA 4.92 4.21 # 80 A HA 4.18 4.88 # 83 P HA 4.55 3.56 #102 H HA 4.18 4.94 #124 H HA 3.85 4.96 # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted #101 T CA 53.45 62.53 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 7 K CB 30.49 35.70 # 81 F CB 33.66 41.43 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 81 F N 131.08 118.92 # 97 E N 130.58 119.20 # 99 W N 116.69 127.34 #100 T N 125.89 113.28 #101 T N 122.67 110.86 #103 S N 123.44 111.08 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 81 F H 12.03 9.10 #131 V H 11.58 9.17 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.07 2.51 2.51 N/A -0.13 0.11 # #bmr6444.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr6444.str file): #HA CA CB CO N HN #N/A +2.51 +2.51 N/A -0.13 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.19 +/-0.20 N/A +/-0.34 +/-0.07 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.841 0.959 0.993 N/A 0.794 0.589 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.154 1.009 1.047 N/A 2.002 0.415 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N Chemical Shift Assignments for MMP12 ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bertini Ivano . . 2 Calderone Vito . . 3 Cosenza Marta . . 4 Fragai Marco . . 5 Lee Yong-Min . . 6 Luchinat Claudio . . 7 Mangani Stefano . . 8 Terni Beatrice . . 9 Turano Paola . . stop_ _BMRB_accession_number 6444 _BMRB_flat_file_name bmr6444.str _Entry_type new _Submission_date 2004-12-23 _Accession_date 2004-12-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 residual_dipolar_couplings 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 749 '15N chemical shifts' 157 '13C chemical shifts' 318 'residual dipolar couplings' 111 stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_title ; Conformational Variability of MMPs: Beyond a Single 3D Structure ; _Citation_status published _Citation_type journal _PubMed_ID . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bertini Ivano . . 2 Calderone Vito . . 3 Cosenza Marta . . 4 Fragai Marco . . 5 Lee Yong-Min . . 6 Luchinat Claudio . . 7 Mangani Stefano . . 8 Terni Beatrice . . 9 Turano Paola . . stop_ _Journal_abbreviation "Proc. Natl. Acad. Sci. U.S.A." _Journal_volume 102 _Journal_issue 15 _Page_first 5334 _Page_last 5339 _Year 2005 save_ ################################## # Molecular system description # ################################## save_assembly_MMP12 _Saveframe_category molecular_system _Mol_system_name MMP12 _Abbreviation_common MMP12 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "MMP12 catalytic domain" $MMP12 NNGH $NNGH stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state "not present" _Details ; The ligand NNGH is the hydroxamate-based N-Isobutyl-N-[4-methoxy-phenylsulfonyl]glycyl hydroxamic acid inhibitor. The interaction of the inhibitor with the active site is limited to the Zn1 ion and to the S1' subsite. In addition to the metal chelation, NNGH is held in the active site by H-bonds and hydrophobic interactions. The hydroxamic acid moiety (the protonated oxygen and carbonyl oxygen) chelates to the zinc ion and is further involved in two H-bonds. The protonated oxygen atom in addition to the zinc coordination, donates a H-bond to the carboxylate OE2 of Glu115. On the contrary the carbonyl hydroxamate oxygen is not involved in any H-bond while the hydroxamate NH has only a weak electrostatic interaction with the Ala78 carbonyl oxygen. The one of NNGH sulphonyl oxygen atoms makes important contributions to the inhibitor binding energy by establishing H-bonds with Leu77 N. ; save_ ######################## # Monomeric polymers # ######################## save_MMP12 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "matrix metalloelastase" _Name_variant . _Abbreviation_common MMP12 _Mol_thiol_state "not present" ############################## # Polymer residue sequence # ############################## _Residue_count 159 _Mol_residue_sequence ; MGPVWRKHYITYRINNYTPD MNREDVDYAIRKAFQVWSNV TPLKFSKINTGMADILVVFA RGAHGDDHAFDGKGGILAHA FGPGSGIGGDAHFDEDEFWT THSGGTNLFLTAVHEIGHSL GLGHSSDPKAVMFPTYKYVD INTFRLSADDIRGIQSLYG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLY 3 PRO 4 VAL 5 TRP 6 ARG 7 LYS 8 HIS 9 TYR 10 ILE 11 THR 12 TYR 13 ARG 14 ILE 15 ASN 16 ASN 17 TYR 18 THR 19 PRO 20 ASP 21 MET 22 ASN 23 ARG 24 GLU 25 ASP 26 VAL 27 ASP 28 TYR 29 ALA 30 ILE 31 ARG 32 LYS 33 ALA 34 PHE 35 GLN 36 VAL 37 TRP 38 SER 39 ASN 40 VAL 41 THR 42 PRO 43 LEU 44 LYS 45 PHE 46 SER 47 LYS 48 ILE 49 ASN 50 THR 51 GLY 52 MET 53 ALA 54 ASP 55 ILE 56 LEU 57 VAL 58 VAL 59 PHE 60 ALA 61 ARG 62 GLY 63 ALA 64 HIS 65 GLY 66 ASP 67 ASP 68 HIS 69 ALA 70 PHE 71 ASP 72 GLY 73 LYS 74 GLY 75 GLY 76 ILE 77 LEU 78 ALA 79 HIS 80 ALA 81 PHE 82 GLY 83 PRO 84 GLY 85 SER 86 GLY 87 ILE 88 GLY 89 GLY 90 ASP 91 ALA 92 HIS 93 PHE 94 ASP 95 GLU 96 ASP 97 GLU 98 PHE 99 TRP 100 THR 101 THR 102 HIS 103 SER 104 GLY 105 GLY 106 THR 107 ASN 108 LEU 109 PHE 110 LEU 111 THR 112 ALA 113 VAL 114 HIS 115 GLU 116 ILE 117 GLY 118 HIS 119 SER 120 LEU 121 GLY 122 LEU 123 GLY 124 HIS 125 SER 126 SER 127 ASP 128 PRO 129 LYS 130 ALA 131 VAL 132 MET 133 PHE 134 PRO 135 THR 136 TYR 137 LYS 138 TYR 139 VAL 140 ASP 141 ILE 142 ASN 143 THR 144 PHE 145 ARG 146 LEU 147 SER 148 ALA 149 ASP 150 ASP 151 ILE 152 ARG 153 GLY 154 ILE 155 GLN 156 SER 157 LEU 158 TYR 159 GLY stop_ _Sequence_homology_query_date 2005-09-22 _Sequence_homology_query_revised_last_date 2005-09-08 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1JK3 "A Chain A, Crystal Structure Of Human Mmp-12(Macrophage Elastase) At True Atomic Resolution" 100.63 158 99 99 8e-90 PDB 1RMZ "A Chain A, Crystal Structure Of The CatalyticDomain Of Human Mmp12 Complexed With The Inhibitor NnghAt 1.3 A Resolution" 100.00 159 100 100 4e-92 PDB 1Y93 "A Chain A, Crystal Structure Of The CatalyticDomain Of Human Mmp12 Complexed With AcetohydroxamicAcid At Atomic Resolution" 100.00 159 100 100 4e-92 PDB 1YCM "A Chain A, Solution Structure Of MatrixMetalloproteinase 12 (Mmp12) In The Presence OfN-Isobutyl-N-[4- Methoxyphenylsulfonyl]glycyl HydroxamicAcid (Nngh)" 100.00 159 100 100 4e-92 PDB 1Z3J "A Chain A, Solution Structure Of Mmp12 In ThePresence Of N-Isobutyl-N- 4-Methoxyphenylsulfonyl]glycylHydroxamic Acid (Nngh)" 100.00 159 100 100 4e-92 PDB 1UTT "A Chain A, Crystal Structure Of Mmp-12Complexed To 2-(1,3-Dioxo-1,3-Dihydro-2h-Isoindol-2-Yl)ethyl-4-(4-Ethoxy[1,1-Biphenyl]-4-Yl)-4-Oxobutanoic Acid" 100.00 159 99 99 2e-90 PDB 1UTZ "A Chain A, Crystal Structure Of Mmp-12Complexed To (2r)-3-({[4-[(PyriDin-4-Yl)phenyl]-Thien-2-Yl}carboxamido)(Phenyl)propanoic Acid" 100.00 159 99 99 2e-90 PDB 1ROS "A Chain A, Crystal Structure Of Mmp-12Complexed To 2-(1,3-Dioxo-1,3-Dihydro-2h-Isoindol-2-Yl)ethyl-4-(4-Ethoxy[1,1-Biphenyl]-4- Yl)-4-Oxobutanoic Acid" 97.55 163 99 99 2e-90 PDB 1OS2 "A Chain A, Ternary Enzyme-Product-InhibitorComplexes Of Human Mmp12" 96.36 165 100 100 4e-92 PDB 1OS9 "A Chain A, Binary Enzyme-Product Complexes OfHuman Mmp12" 96.36 165 100 100 4e-92 PDB 1JIZ "A Chain A, Crystal Structure Analysis Of HumanMacrophage Elastase Mmp- 12" 95.78 166 99 99 2e-90 GenBank AAA58658.1 metalloproteinase 33.83 470 99 99 2e-90 GenBank AAW29944.1 "matrix metalloproteinase 12 (macrophageelastase) [Homo sapiens]" 33.83 470 99 99 2e-90 REF XP_508724.1 "PREDICTED: matrix metalloproteinase 12[Pan troglodytes]" 34.34 463 99 99 2e-90 REF NP_002417.2 "matrix metalloproteinase 12preproprotein [Homo sapiens]" 33.83 470 99 99 2e-90 SWISS-PROT P39900 "MMP12_HUMAN Macrophage metalloelastaseprecursor (HME) (Matrix metalloproteinase-12) (MMP-12)(Macrophage elastase) (ME)" 33.83 470 99 99 2e-90 stop_ save_ ############# # Ligands # ############# save_NNGH _Saveframe_category ligand _Mol_type non-polymer _Name_common "N-Isobutyl-N-[4-methoxyphenylsulfonyl]glycyl hydroxamic acid" _Abbreviation_common NNGH _Name_IUPAC . _BMRB_code NNGH _PDB_code ? _Mol_empirical_formula ? _Mol_charge 0 _Mol_paramagnetic no _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C ? 0 ? ? C2 C2 C ? 0 ? ? C3 C3 C ? 0 ? ? C4 C4 C ? 0 ? ? C5 C5 C ? 0 ? ? C6 C6 C ? 0 ? ? O1 O1 O ? 0 ? ? C7 C7 C ? 0 ? ? S1 S1 S ? 0 ? ? O2 O2 O ? 0 ? ? O3 O3 O ? 0 ? ? N N N ? 0 ? ? C9 C9 C ? 0 ? ? C10 C10 C ? 0 ? ? C11 C11 C ? 0 ? ? N1 N1 N ? 0 ? ? O4 O4 O ? 0 ? ? O5 O5 O ? 0 ? ? C12 C12 C ? 0 ? ? C13 C13 C ? 0 ? ? C14 C14 C ? 0 ? ? 1H7 1H7 H ? 0 ? ? 2H7 2H7 H ? 0 ? ? 3H7 3H7 H ? 0 ? ? H4 H4 H ? 0 ? ? H5 H5 H ? 0 ? ? H1 H1 H ? 0 ? ? H2 H2 H ? 0 ? ? 1H9 1H9 H ? 0 ? ? 2H9 2H9 H ? 0 ? ? H12 H12 H ? 0 ? ? 1H13 1H13 H ? 0 ? ? 2H13 2H13 H ? 0 ? ? 3H13 3H13 H ? 0 ? ? 1H14 1H14 H ? 0 ? ? 2H14 2H14 H ? 0 ? ? 3H14 3H14 H ? 0 ? ? 1H10 1H10 H ? 0 ? ? 2H10 2H10 H ? 0 ? ? HN1 HN1 H ? 0 ? ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C1 H1 ? ? SING C1 C2 ? ? DOUB C1 C6 ? ? SING C2 H2 ? ? DOUB C2 C3 ? ? SING C3 O1 ? ? SING C3 C4 ? ? DOUB C4 C5 ? ? SING C4 H4 ? ? SING C5 H5 ? ? SING C5 C6 ? ? SING O1 C7 ? ? SING C7 1H7 ? ? SING C7 2H7 ? ? SING C7 3H7 ? ? SING C6 S1 ? ? DOUB S1 O2 ? ? DOUB S1 O3 ? ? SING S1 N ? ? SING N C9 ? ? SING C9 1H9 ? ? SING C9 2H9 ? ? SING C9 C12 ? ? SING C12 H12 ? ? SING C12 C13 ? ? SING C12 C14 ? ? SING C13 1H13 ? ? SING C13 2H13 ? ? SING C13 3H13 ? ? SING C14 1H14 ? ? SING C14 2H14 ? ? SING C14 3H14 ? ? SING N C10 ? ? SING C10 1H10 ? ? SING C10 2H10 ? ? SING C10 C11 ? ? DOUB C11 O5 ? ? SING C11 N1 ? ? SING N1 O4 ? ? SING N1 NH1 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MMP12 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 $MMP12 "recombinant technology" ? ? ? ? ? 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 _Isotopic_labeling $MMP12 0.9 mM "[U-13C; U-15N]" $NNGH 0.9 mM ? stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type bicelle loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MMP12 0.9 mM "[U-13C; U-15N]" $NNGH 0.9 mM ? stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_900MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 900 _Details "Isotope Filtered 2D NOESY" save_ save_800MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 800 _Details ; 3D 15N-separated NOESY 3D 13C-separated NOESY ; save_ save_700MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 700 _Details "Mobility measurements" save_ save_500MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details "other 3D NMR experiments" save_ ############################# # NMR applied experiments # ############################# save_3D_13N-separated_NOESY _Saveframe_category NMR_applied_experiment _Experiment_name "3D 13N-separated NOESY" _Sample_label $sample_1 save_ save_2D_NOESY _Saveframe_category NMR_applied_experiment _Experiment_name "2D NOESY" _Sample_label $sample_1 save_ save_one_bond_1H-15N_IPAP_HSQC _Saveframe_category NMR_applied_experiment _Experiment_name "one bond 1H-15N IPAP HSQC" _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.20 0.02 pH temperature 298.0 0.1 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 N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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 "MMP12 catalytic domain" 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 4 VAL HG1 H 0.39 0.004 . 2 5 TRP HB2 H 1.88 0.000 . 3 5 TRP NE1 N 125.62 0.000 . 4 5 TRP HD1 H 7.28 0.000 . 5 5 TRP HE1 H 9.32 0.016 . 6 6 ARG N N 115.80 0.000 . 7 6 ARG H H 7.50 0.001 . 8 6 ARG HA H 4.47 0.000 . 9 6 ARG HB2 H 1.80 0.000 . 10 6 ARG HG2 H 1.30 0.000 . 11 6 ARG HD2 H 3.33 0.000 . 12 7 LYS CB C 30.49 0.000 . 13 7 LYS HB2 H 2.03 0.000 . 14 7 LYS HB3 H 1.51 0.000 . 15 7 LYS HG2 H 1.33 0.000 . 16 7 LYS HG3 H 1.14 0.000 . 17 8 HIS H H 6.87 0.004 . 18 8 HIS HA H 4.08 0.001 . 19 8 HIS CB C 31.11 0.000 . 20 8 HIS HB2 H 3.25 0.000 . 21 8 HIS HB3 H 2.77 0.000 . 22 9 TYR N N 120.15 0.000 . 23 9 TYR H H 6.93 0.001 . 24 9 TYR CA C 56.44 0.000 . 25 9 TYR HA H 4.73 0.002 . 26 9 TYR CB C 38.03 0.000 . 27 9 TYR HB2 H 2.80 0.002 . 28 9 TYR HB3 H 2.67 0.000 . 29 10 ILE N N 128.44 0.000 . 30 10 ILE H H 8.26 0.000 . 31 10 ILE CA C 58.68 0.000 . 32 10 ILE HA H 4.08 0.005 . 33 10 ILE CB C 39.99 0.000 . 34 10 ILE HB H 1.31 0.002 . 35 10 ILE HG2 H 0.32 0.010 . 36 10 ILE CG2 C 16.89 0.000 . 37 10 ILE CG1 C 27.64 0.000 . 38 10 ILE HG12 H 0.69 0.002 . 39 10 ILE HG13 H 0.20 0.000 . 40 10 ILE HD1 H 0.07 0.012 . 41 10 ILE CD1 C 12.69 0.000 . 42 11 THR N N 117.23 0.000 . 43 11 THR H H 9.18 0.001 . 44 11 THR CA C 58.37 0.000 . 45 11 THR HA H 5.30 0.002 . 46 11 THR CB C 72.35 0.000 . 47 11 THR HB H 4.05 0.020 . 48 11 THR HG2 H 1.02 0.000 . 49 11 THR CG2 C 21.93 0.012 . 50 12 TYR N N 117.29 0.000 . 51 12 TYR H H 8.59 0.001 . 52 12 TYR CA C 54.85 0.000 . 53 12 TYR HA H 5.78 0.006 . 54 12 TYR CB C 43.04 0.000 . 55 12 TYR HB2 H 2.89 0.000 . 56 12 TYR HB3 H 2.29 0.003 . 57 12 TYR HD1 H 6.37 0.000 . 58 12 TYR HD2 H 6.37 0.000 . 59 12 TYR HE1 H 6.04 0.000 . 60 12 TYR HE2 H 6.04 0.000 . 61 12 TYR HH H 6.61 0.000 . 62 13 ARG N N 119.04 0.000 . 63 13 ARG H H 8.35 0.010 . 65 13 ARG HA H 4.61 0.007 . 66 13 ARG CB C 35.19 0.000 . 67 13 ARG HB2 H 1.52 0.000 . 68 13 ARG CG C 28.76 0.000 . 69 13 ARG HG2 H 1.47 0.020 . 70 13 ARG CD C 42.12 0.000 . 71 13 ARG HD2 H 2.90 0.008 . 72 14 ILE N N 127.12 0.000 . 73 14 ILE H H 9.12 0.002 . 74 14 ILE CA C 61.21 0.000 . 75 14 ILE HA H 4.24 0.009 . 76 14 ILE CB C 36.47 0.000 . 77 14 ILE HB H 1.70 0.004 . 78 14 ILE HG2 H 0.03 0.003 . 79 14 ILE CG2 C 16.68 0.000 . 80 14 ILE CG1 C 27.53 0.000 . 81 14 ILE HG12 H 1.68 0.011 . 82 14 ILE HG13 H 0.83 0.015 . 83 14 ILE HD1 H 0.93 0.001 . 84 14 ILE CD1 C 13.18 0.000 . 85 15 ASN N N 128.55 0.000 . 86 15 ASN H H 9.64 0.013 . 88 15 ASN HA H 4.26 0.001 . 90 15 ASN HB2 H 3.03 0.001 . 91 15 ASN HB3 H 2.48 0.038 . 92 15 ASN ND2 N 112.17 0.000 . 93 15 ASN HD21 H 7.41 0.001 . 94 15 ASN HD22 H 6.79 0.001 . 96 16 ASN H H 7.76 0.008 . 97 16 ASN HA H 4.63 0.007 . 98 16 ASN CB C 38.63 0.000 . 99 16 ASN HB2 H 2.98 0.000 . 100 16 ASN HB3 H 2.89 0.002 . 101 16 ASN ND2 N 115.18 0.000 . 102 16 ASN HD21 H 7.00 0.001 . 103 16 ASN HD22 H 7.93 0.000 . 104 17 TYR N N 114.96 0.000 . 105 17 TYR H H 8.56 0.000 . 106 17 TYR CA C 58.53 0.000 . 107 17 TYR HA H 4.00 0.000 . 108 17 TYR CB C 40.52 0.029 . 109 17 TYR HB2 H 2.83 0.000 . 110 17 TYR HB3 H 2.50 0.009 . 111 17 TYR HD1 H 7.33 0.000 . 112 17 TYR HD2 H 7.33 0.000 . 113 17 TYR HE1 H 7.22 0.010 . 114 17 TYR HE2 H 6.84 0.010 . 115 18 THR N N 115.65 0.000 . 116 18 THR H H 8.07 0.001 . 117 18 THR HA H 4.86 0.000 . 118 18 THR HB H 3.10 0.000 . 119 18 THR HG2 H 2.62 0.002 . 120 19 PRO CD C 50.12 0.000 . 121 19 PRO HA H 4.02 0.000 . 122 19 PRO CB C 31.47 0.000 . 123 19 PRO HB2 H 2.16 0.004 . 124 19 PRO HB3 H 2.00 0.000 . 125 19 PRO HG2 H 1.86 0.000 . 126 19 PRO HD2 H 3.81 0.000 . 127 19 PRO HD3 H 3.40 0.000 . 128 20 ASP N N 121.80 0.000 . 129 20 ASP H H 8.79 0.003 . 130 20 ASP CA C 54.86 0.000 . 131 20 ASP HA H 4.65 0.000 . 132 20 ASP CB C 41.62 0.000 . 133 20 ASP HB2 H 2.67 0.011 . 134 20 ASP HB3 H 2.48 0.000 . 135 21 MET N N 113.24 0.000 . 136 21 MET H H 6.90 0.001 . 137 21 MET CA C 53.24 0.000 . 138 21 MET HA H 4.54 0.000 . 139 21 MET CB C 39.13 0.000 . 140 21 MET HB2 H 2.18 0.000 . 141 21 MET HB3 H 1.32 0.009 . 142 21 MET CG C 32.08 0.000 . 143 21 MET HG2 H 2.24 0.000 . 144 21 MET HE H 0.34 0.003 . 145 22 ASN N N 118.66 0.000 . 146 22 ASN H H 8.85 0.002 . 148 22 ASN HA H 4.64 0.002 . 149 22 ASN CB C 38.15 0.000 . 150 22 ASN HB2 H 2.80 0.005 . 151 22 ASN HB3 H 2.77 0.008 . 152 22 ASN ND2 N 113.84 0.021 . 153 22 ASN HD21 H 7.60 0.001 . 154 22 ASN HD22 H 6.93 0.022 . 155 23 ARG N N 126.02 0.000 . 156 23 ARG H H 8.92 0.001 . 157 23 ARG CA C 60.20 0.000 . 158 23 ARG HA H 3.67 0.009 . 159 23 ARG CB C 29.79 0.000 . 160 23 ARG HB2 H 1.42 0.000 . 161 23 ARG HB3 H 1.31 0.007 . 162 23 ARG CG C 26.16 0.000 . 163 23 ARG HG2 H 0.96 0.000 . 164 23 ARG HG3 H 0.88 0.000 . 165 23 ARG CD C 43.14 0.000 . 166 23 ARG HD2 H 2.63 0.000 . 167 23 ARG HD3 H 2.54 0.000 . 168 24 GLU N N 116.08 0.000 . 169 24 GLU H H 9.08 0.013 . 170 24 GLU CA C 59.42 0.000 . 171 24 GLU HA H 4.06 0.008 . 172 24 GLU CB C 28.33 0.000 . 173 24 GLU HB2 H 1.92 0.011 . 174 24 GLU CG C 36.21 0.000 . 175 24 GLU HG2 H 2.25 0.002 . 176 25 ASP N N 119.76 0.000 . 177 25 ASP H H 7.43 0.003 . 178 25 ASP HA H 4.61 0.009 . 179 25 ASP CB C 40.50 0.034 . 180 25 ASP HB2 H 2.79 0.001 . 181 25 ASP HB3 H 2.59 0.002 . 182 26 VAL N N 123.92 0.000 . 183 26 VAL H H 7.73 0.003 . 184 26 VAL CA C 66.40 0.000 . 185 26 VAL HA H 3.39 0.006 . 186 26 VAL CB C 31.19 0.000 . 187 26 VAL HB H 2.59 0.017 . 188 26 VAL HG1 H 0.95 0.008 . 189 26 VAL HG2 H 0.86 0.000 . 190 26 VAL CG2 C 21.30 0.000 . 191 27 ASP N N 118.28 0.000 . 192 27 ASP H H 8.33 0.008 . 193 27 ASP CA C 57.80 0.000 . 194 27 ASP HA H 4.25 0.001 . 195 27 ASP CB C 40.20 0.000 . 196 27 ASP HB2 H 2.70 0.000 . 197 27 ASP HB3 H 2.63 0.007 . 198 28 TYR N N 119.61 0.000 . 199 28 TYR H H 8.12 0.000 . 200 28 TYR CA C 61.44 0.000 . 201 28 TYR HA H 4.16 0.003 . 202 28 TYR CB C 38.53 0.000 . 203 28 TYR HB2 H 3.20 0.001 . 204 28 TYR HB3 H 3.04 0.000 . 205 28 TYR HD1 H 7.12 0.009 . 206 28 TYR HD2 H 7.12 0.009 . 207 28 TYR HE1 H 6.67 0.008 . 208 28 TYR HE2 H 6.67 0.008 . 209 29 ALA N N 121.29 0.000 . 210 29 ALA H H 8.01 0.006 . 211 29 ALA CA C 55.34 0.000 . 212 29 ALA HA H 3.88 0.002 . 213 29 ALA HB H 1.47 0.001 . 214 29 ALA CB C 18.33 0.000 . 215 30 ILE N N 113.84 0.000 . 216 30 ILE H H 8.02 0.000 . 217 30 ILE CA C 61.83 0.000 . 218 30 ILE HA H 3.47 0.004 . 219 30 ILE CB C 35.55 0.000 . 220 30 ILE HB H 2.10 0.012 . 221 30 ILE HG2 H 0.72 0.001 . 222 30 ILE CG2 C 18.75 0.000 . 223 30 ILE HG12 H 1.57 0.018 . 224 30 ILE HG13 H 1.01 0.043 . 225 30 ILE HD1 H 0.23 0.000 . 226 30 ILE CD1 C 8.44 0.004 . 227 31 ARG N N 119.66 0.000 . 228 31 ARG H H 8.24 0.000 . 229 31 ARG CA C 59.61 0.000 . 230 31 ARG HA H 4.08 0.000 . 231 31 ARG CB C 29.81 0.015 . 232 31 ARG HB2 H 2.03 0.000 . 233 31 ARG HB3 H 1.96 0.000 . 234 31 ARG CG C 27.04 0.000 . 235 31 ARG HG2 H 1.72 0.015 . 236 31 ARG HG3 H 1.57 0.008 . 237 31 ARG CD C 43.80 0.000 . 238 31 ARG HD2 H 3.25 0.000 . 239 32 LYS N N 118.91 0.000 . 240 32 LYS H H 8.50 0.003 . 241 32 LYS CA C 58.13 0.000 . 242 32 LYS HA H 3.98 0.000 . 243 32 LYS CB C 30.88 0.000 . 244 32 LYS HB2 H 1.51 0.012 . 245 32 LYS CG C 23.98 0.000 . 246 32 LYS HG2 H 0.98 0.000 . 247 32 LYS HG3 H 0.86 0.000 . 248 32 LYS CD C 27.61 0.000 . 249 32 LYS HD2 H 1.23 0.010 . 250 32 LYS HD3 H 0.99 0.000 . 251 32 LYS CE C 41.60 0.025 . 252 32 LYS HE2 H 2.50 0.000 . 253 33 ALA N N 123.48 0.000 . 254 33 ALA H H 8.01 0.001 . 255 33 ALA CA C 55.32 0.000 . 256 33 ALA HA H 3.85 0.028 . 257 33 ALA HB H 1.05 0.005 . 258 33 ALA CB C 18.83 0.000 . 259 34 PHE N N 114.23 0.000 . 260 34 PHE H H 7.74 0.001 . 262 34 PHE HA H 3.69 0.000 . 263 34 PHE CB C 38.50 0.000 . 264 34 PHE HB2 H 2.52 0.038 . 265 34 PHE HD1 H 5.54 0.010 . 266 34 PHE HD2 H 5.54 0.010 . 267 34 PHE HE1 H 5.79 0.007 . 268 34 PHE HE2 H 5.79 0.007 . 269 35 GLN N N 118.97 0.000 . 270 35 GLN H H 8.04 0.007 . 271 35 GLN CA C 58.30 0.000 . 272 35 GLN HA H 4.13 0.000 . 273 35 GLN CB C 28.26 0.000 . 274 35 GLN HB2 H 2.23 0.013 . 275 35 GLN CG C 34.00 0.000 . 276 35 GLN HG2 H 2.56 0.000 . 277 35 GLN HG3 H 2.40 0.009 . 278 35 GLN NE2 N 112.72 0.000 . 279 35 GLN HE21 H 7.56 0.001 . 280 35 GLN HE22 H 6.93 0.002 . 281 36 VAL N N 117.18 0.000 . 282 36 VAL H H 7.60 0.000 . 284 36 VAL HA H 3.55 0.016 . 286 36 VAL HB H 2.09 0.003 . 287 36 VAL HG1 H 1.09 0.005 . 288 36 VAL HG2 H 0.41 0.001 . 289 36 VAL CG1 C 22.84 0.000 . 290 36 VAL CG2 C 20.96 0.000 . 291 37 TRP N N 116.76 0.000 . 292 37 TRP H H 6.70 0.014 . 293 37 TRP HA H 4.70 0.000 . 294 37 TRP CB C 30.21 0.000 . 295 37 TRP HB2 H 3.04 0.001 . 296 37 TRP HB3 H 3.02 0.000 . 297 37 TRP NE1 N 128.17 0.031 . 298 37 TRP HD1 H 6.84 0.003 . 299 37 TRP HE1 H 9.99 0.015 . 300 37 TRP HZ3 H 6.67 0.000 . 301 37 TRP HZ2 H 7.28 0.000 . 302 38 SER N N 118.44 0.020 . 303 38 SER H H 9.03 0.024 . 304 38 SER CA C 61.23 0.000 . 305 38 SER HA H 4.22 0.008 . 306 38 SER CB C 63.33 0.068 . 307 38 SER HB2 H 4.27 0.002 . 308 38 SER HB3 H 4.13 0.000 . 310 39 ASN H H 7.91 0.008 . 311 39 ASN HA H 4.66 0.000 . 312 39 ASN HB2 H 2.92 0.005 . 313 39 ASN ND2 N 111.75 0.000 . 314 39 ASN HD21 H 7.55 0.001 . 315 39 ASN HD22 H 6.94 0.001 . 316 40 VAL N N 106.37 0.000 . 317 40 VAL H H 7.12 0.003 . 319 40 VAL HA H 4.76 0.016 . 321 40 VAL HB H 2.60 0.005 . 322 40 VAL HG1 H 0.85 0.000 . 323 40 VAL HG2 H 1.06 0.012 . 324 40 VAL CG1 C 21.34 0.000 . 325 40 VAL CG2 C 19.10 0.000 . 326 41 THR N N 110.25 0.000 . 327 41 THR H H 7.42 0.003 . 328 41 THR CA C 59.69 0.000 . 329 41 THR HA H 5.15 0.000 . 330 41 THR CB C 72.09 0.042 . 331 41 THR HB H 3.92 0.000 . 332 41 THR HG2 H 1.39 0.003 . 333 41 THR CG2 C 24.34 0.000 . 334 42 PRO HA H 4.23 0.001 . 335 42 PRO HD2 H 3.47 0.000 . 336 43 LEU N N 110.53 0.000 . 337 43 LEU H H 7.21 0.001 . 338 43 LEU HA H 4.39 0.000 . 339 43 LEU HB2 H 2.02 0.000 . 340 43 LEU HB3 H 1.63 0.000 . 341 43 LEU HG H 1.43 0.000 . 342 43 LEU HD1 H 0.69 0.002 . 343 43 LEU HD2 H 0.57 0.001 . 344 44 LYS N N 122.30 0.000 . 345 44 LYS H H 8.12 0.001 . 346 44 LYS CA C 54.96 0.000 . 347 44 LYS HA H 4.23 0.000 . 348 44 LYS CB C 34.84 0.000 . 349 44 LYS HB2 H 1.57 0.001 . 350 44 LYS HB3 H 1.32 0.001 . 351 44 LYS HG2 H 1.50 0.000 . 352 44 LYS HE2 H 2.06 0.000 . 353 45 PHE N N 119.35 0.017 . 354 45 PHE H H 8.18 0.001 . 355 45 PHE CA C 55.32 0.000 . 356 45 PHE HA H 5.64 0.002 . 357 45 PHE CB C 41.53 0.000 . 358 45 PHE HB2 H 2.45 0.008 . 359 45 PHE HB3 H 2.12 0.000 . 360 45 PHE HD1 H 6.84 0.003 . 361 45 PHE HD2 H 6.84 0.003 . 362 46 SER N N 116.58 0.000 . 363 46 SER H H 8.03 0.002 . 365 46 SER HA H 4.58 0.006 . 367 46 SER HB2 H 3.47 0.000 . 368 46 SER HB3 H 3.37 0.000 . 369 47 LYS N N 127.61 0.000 . 370 47 LYS H H 8.09 0.001 . 371 47 LYS CA C 54.97 0.000 . 372 47 LYS HA H 3.39 0.002 . 373 47 LYS CB C 33.17 0.000 . 374 47 LYS HB2 H 1.35 0.000 . 375 47 LYS HB3 H 1.03 0.006 . 376 47 LYS CG C 25.38 0.000 . 377 47 LYS HG2 H 0.68 0.009 . 378 47 LYS HD2 H 2.97 0.007 . 379 48 ILE N N 123.76 0.000 . 380 48 ILE H H 8.71 0.006 . 381 48 ILE CA C 58.67 0.000 . 382 48 ILE HA H 4.65 0.000 . 384 48 ILE HB H 1.82 0.000 . 385 48 ILE HG2 H 0.70 0.006 . 386 48 ILE CG2 C 17.16 0.000 . 387 48 ILE CG1 C 25.85 0.000 . 388 48 ILE HG12 H 1.09 0.000 . 389 48 ILE HG13 H 0.84 0.001 . 390 48 ILE HD1 H 0.59 0.000 . 391 48 ILE CD1 C 12.64 0.000 . 392 49 ASN N N 119.34 0.000 . 393 49 ASN H H 8.77 0.001 . 394 49 ASN HA H 4.72 0.000 . 395 49 ASN HB2 H 2.78 0.000 . 396 49 ASN ND2 N 110.10 0.000 . 397 49 ASN HD21 H 7.85 0.001 . 398 49 ASN HD22 H 6.64 0.001 . 399 50 THR N N 111.62 0.000 . 400 50 THR H H 7.43 0.000 . 401 50 THR CA C 60.12 0.000 . 402 50 THR HA H 4.38 0.000 . 403 50 THR CB C 70.71 0.000 . 404 50 THR HB H 4.04 0.003 . 405 50 THR HG2 H 1.06 0.000 . 406 50 THR CG2 C 21.35 0.000 . 407 51 GLY N N 109.84 0.000 . 408 51 GLY H H 8.28 0.000 . 409 51 GLY CA C 43.98 0.000 . 410 51 GLY HA2 H 4.26 0.000 . 411 51 GLY HA3 H 3.46 0.000 . 412 52 MET N N 118.92 0.000 . 413 52 MET H H 8.18 0.001 . 414 52 MET CA C 54.99 0.000 . 415 52 MET HA H 4.20 0.000 . 416 52 MET HB2 H 1.90 0.004 . 417 52 MET HG2 H 2.46 0.004 . 418 53 ALA N N 127.03 0.000 . 419 53 ALA H H 7.92 0.000 . 420 53 ALA CA C 49.36 0.000 . 421 53 ALA HA H 4.40 0.000 . 422 53 ALA HB H 0.90 0.006 . 423 53 ALA CB C 22.25 0.000 . 424 54 ASP N N 121.35 0.000 . 425 54 ASP H H 7.99 0.001 . 426 54 ASP CA C 57.59 0.000 . 427 54 ASP HA H 4.48 0.003 . 428 54 ASP CB C 41.13 0.000 . 429 54 ASP HB2 H 2.94 0.028 . 430 54 ASP HB3 H 2.21 0.028 . 431 55 ILE N N 124.22 0.000 . 432 55 ILE H H 8.85 0.001 . 433 55 ILE CA C 61.40 0.000 . 434 55 ILE HA H 4.16 0.030 . 435 55 ILE CB C 40.02 0.000 . 436 55 ILE HB H 1.80 0.000 . 437 55 ILE HG2 H 0.89 0.007 . 438 55 ILE CG2 C 14.57 0.000 . 439 55 ILE CG1 C 26.34 0.000 . 440 55 ILE HG12 H 1.44 0.001 . 441 55 ILE HD1 H 1.04 0.001 . 442 55 ILE CD1 C 14.30 0.000 . 443 56 LEU N N 129.93 0.000 . 444 56 LEU H H 7.58 0.003 . 445 56 LEU CA C 53.06 0.000 . 446 56 LEU HA H 5.02 0.005 . 447 56 LEU CB C 43.33 0.000 . 448 56 LEU HB2 H 1.62 0.003 . 449 56 LEU HB3 H 1.41 0.001 . 450 56 LEU HD1 H 0.92 0.009 . 451 56 LEU HD2 H 0.83 0.002 . 452 56 LEU CD1 C 23.97 0.000 . 453 57 VAL N N 125.29 0.021 . 454 57 VAL H H 8.74 0.003 . 455 57 VAL CA C 61.61 0.000 . 456 57 VAL HA H 5.10 0.009 . 457 57 VAL CB C 32.68 0.000 . 458 57 VAL HB H 2.08 0.007 . 459 57 VAL HG1 H 0.91 0.001 . 460 57 VAL HG2 H 0.83 0.018 . 461 57 VAL CG1 C 20.22 0.000 . 462 57 VAL CG2 C 19.83 0.000 . 463 58 VAL N N 126.92 0.000 . 464 58 VAL H H 8.79 0.003 . 465 58 VAL CA C 60.66 0.000 . 466 58 VAL HA H 4.51 0.000 . 467 58 VAL CB C 37.05 0.000 . 468 58 VAL HB H 1.74 0.003 . 469 58 VAL HG1 H 0.71 0.001 . 470 58 VAL HG2 H 0.85 0.000 . 471 58 VAL CG1 C 20.60 0.000 . 472 58 VAL CG2 C 20.96 0.000 . 473 59 PHE N N 125.59 0.000 . 474 59 PHE H H 8.38 0.001 . 475 59 PHE CA C 56.71 0.000 . 476 59 PHE HA H 5.32 0.003 . 478 59 PHE HB2 H 2.69 0.011 . 479 59 PHE HB3 H 2.97 0.002 . 480 59 PHE HD1 H 6.88 0.016 . 481 59 PHE HD2 H 6.88 0.016 . 482 60 ALA N N 125.86 0.000 . 483 60 ALA H H 9.10 0.000 . 484 60 ALA CA C 50.94 0.000 . 485 60 ALA HA H 4.77 0.001 . 486 60 ALA HB H 0.94 0.007 . 487 60 ALA CB C 22.79 0.000 . 488 61 ARG N N 118.04 0.000 . 489 61 ARG H H 8.77 0.000 . 491 61 ARG HA H 5.21 0.003 . 493 61 ARG HB2 H 1.84 0.003 . 494 61 ARG HB3 H 1.60 0.001 . 495 61 ARG HG2 H 1.52 0.000 . 496 61 ARG HD2 H 3.19 0.000 . 498 62 GLY H H 9.43 0.002 . 500 62 GLY HA2 H 3.88 0.000 . 501 62 GLY HA3 H 3.77 0.000 . 503 63 ALA H H 9.15 0.000 . 505 63 ALA HA H 4.28 0.004 . 506 63 ALA HB H 1.44 0.009 . 508 64 HIS N N 121.81 0.000 . 509 64 HIS H H 9.34 0.001 . 510 64 HIS HB3 H 3.00 0.000 . 511 67 ASP N N 121.43 0.000 . 512 67 ASP H H 8.00 0.000 . 513 67 ASP HA H 4.38 0.003 . 514 67 ASP HB2 H 2.89 0.000 . 515 68 HIS N N 120.47 0.000 . 516 68 HIS H H 7.54 0.001 . 517 68 HIS CA C 53.44 0.000 . 518 68 HIS HA H 4.57 0.005 . 519 68 HIS CB C 29.84 0.000 . 520 68 HIS HB2 H 2.48 0.000 . 521 68 HIS HB3 H 2.06 0.000 . 522 68 HIS HD2 H 8.28 0.000 . 523 68 HIS HE1 H 6.54 0.000 . 524 69 ALA N N 123.19 0.000 . 525 69 ALA H H 7.95 0.000 . 526 69 ALA HA H 4.12 0.000 . 527 69 ALA HB H 1.25 0.000 . 529 70 PHE N N 119.85 0.000 . 530 70 PHE H H 7.94 0.001 . 531 70 PHE CA C 57.17 0.000 . 532 70 PHE HA H 4.86 0.000 . 533 70 PHE CB C 38.54 0.000 . 534 70 PHE HB2 H 3.75 0.000 . 535 70 PHE HB3 H 3.01 0.000 . 536 70 PHE HD1 H 6.73 0.013 . 537 70 PHE HD2 H 6.73 0.013 . 538 70 PHE HE1 H 7.14 0.000 . 539 70 PHE HE2 H 7.14 0.000 . 540 71 ASP N N 116.27 0.000 . 541 71 ASP H H 8.24 0.001 . 542 71 ASP CA C 53.47 0.000 . 543 71 ASP HA H 4.64 0.000 . 545 71 ASP HB2 H 3.04 0.000 . 546 71 ASP HB3 H 2.52 0.002 . 547 72 GLY N N 109.98 0.000 . 548 72 GLY H H 8.80 0.004 . 549 72 GLY CA C 43.52 0.000 . 550 72 GLY HA2 H 4.39 0.000 . 551 72 GLY HA3 H 4.23 0.002 . 552 73 LYS N N 123.95 0.000 . 553 73 LYS H H 8.70 0.000 . 554 73 LYS CA C 58.26 0.000 . 555 73 LYS HA H 3.40 0.000 . 556 73 LYS CB C 31.89 0.000 . 557 73 LYS HB2 H 1.52 0.002 . 558 73 LYS CG C 24.22 0.000 . 559 73 LYS HG2 H 1.23 0.000 . 560 73 LYS HG3 H 0.92 0.002 . 561 73 LYS CD C 28.66 0.015 . 562 73 LYS HD2 H 1.50 0.019 . 563 73 LYS CE C 42.15 0.000 . 564 73 LYS HE2 H 2.84 0.006 . 565 74 GLY N N 121.11 0.015 . 566 74 GLY H H 10.75 0.001 . 567 74 GLY CA C 42.74 0.000 . 568 74 GLY HA2 H 4.17 0.008 . 569 74 GLY HA3 H 3.50 0.002 . 570 75 GLY N N 110.59 0.000 . 571 75 GLY H H 8.44 0.000 . 573 75 GLY HA2 H 4.08 0.000 . 574 75 GLY HA3 H 3.36 0.000 . 575 76 ILE N N 129.64 0.000 . 576 76 ILE H H 10.61 0.004 . 577 76 ILE CA C 61.98 0.000 . 578 76 ILE HA H 3.88 0.000 . 579 76 ILE CB C 37.80 0.000 . 580 76 ILE HB H 2.07 0.000 . 581 76 ILE HG2 H 1.20 0.000 . 582 76 ILE CG2 C 18.37 0.000 . 583 76 ILE CG1 C 27.91 0.000 . 584 76 ILE HG12 H 1.67 0.000 . 585 76 ILE HG13 H 1.36 0.000 . 586 76 ILE HD1 H 0.98 0.000 . 587 76 ILE CD1 C 12.30 0.000 . 588 77 LEU N N 128.09 0.000 . 589 77 LEU H H 8.45 0.003 . 590 77 LEU CA C 55.32 0.000 . 591 77 LEU HA H 4.38 0.003 . 593 77 LEU HB2 H 1.34 0.005 . 594 77 LEU CG C 25.81 0.000 . 595 77 LEU HG H 1.55 0.000 . 596 77 LEU HD1 H 0.21 0.010 . 597 77 LEU HD2 H -0.04 0.011 . 598 77 LEU CD1 C 20.83 0.000 . 599 77 LEU CD2 C 24.28 0.000 . 600 78 ALA N N 114.40 0.000 . 601 78 ALA H H 7.40 0.006 . 602 78 ALA HA H 4.66 0.000 . 603 78 ALA HB H 1.02 0.009 . 604 78 ALA CB C 21.90 0.000 . 605 79 HIS N N 116.61 0.000 . 606 79 HIS H H 9.25 0.014 . 607 79 HIS CA C 54.12 0.000 . 608 79 HIS HA H 4.78 0.011 . 610 79 HIS HB2 H 3.27 0.000 . 611 79 HIS HB3 H 3.07 0.003 . 612 79 HIS HD2 H 6.43 0.005 . 613 79 HIS HE1 H 8.04 0.000 . 615 80 ALA H H 7.95 0.001 . 617 80 ALA HA H 4.11 0.000 . 618 80 ALA HB H 1.23 0.005 . 619 81 PHE N N 131.08 0.000 . 620 81 PHE H H 11.91 0.015 . 621 81 PHE CA C 54.36 0.000 . 622 81 PHE HA H 4.47 0.006 . 624 81 PHE HB2 H 1.90 0.006 . 625 81 PHE HD1 H 6.97 0.000 . 626 81 PHE HD2 H 6.97 0.000 . 627 82 GLY N N 105.26 0.000 . 628 82 GLY H H 8.18 0.004 . 630 82 GLY HA2 H 4.29 0.000 . 631 82 GLY HA3 H 3.46 0.000 . 632 83 PRO HA H 4.48 0.000 . 634 83 PRO HB2 H 0.59 0.000 . 635 83 PRO HB3 H -0.12 0.000 . 636 83 PRO HG2 H 1.63 0.000 . 637 83 PRO HG3 H 1.35 0.000 . 638 83 PRO HD2 H 3.01 0.006 . 639 83 PRO HD3 H 2.79 0.000 . 640 84 GLY N N 106.78 0.000 . 641 84 GLY H H 5.65 0.001 . 642 84 GLY CA C 43.99 0.000 . 643 84 GLY HA2 H 4.06 0.006 . 644 84 GLY HA3 H 3.59 0.000 . 645 85 SER N N 114.33 0.000 . 646 85 SER H H 8.33 0.002 . 647 85 SER HA H 4.55 0.001 . 648 86 GLY N N 112.22 0.000 . 649 86 GLY H H 8.91 0.000 . 650 86 GLY CA C 47.00 0.000 . 651 86 GLY HA2 H 3.92 0.003 . 652 86 GLY HA3 H 3.70 0.013 . 653 87 ILE N N 133.86 0.000 . 654 87 ILE H H 8.93 0.004 . 655 87 ILE CA C 61.70 0.000 . 656 87 ILE HA H 4.15 0.000 . 657 87 ILE CB C 37.79 0.000 . 658 87 ILE HB H 1.43 0.038 . 659 87 ILE HG2 H 0.42 0.001 . 660 87 ILE CG2 C 16.20 0.000 . 661 87 ILE CG1 C 27.91 0.000 . 662 87 ILE HG12 H 0.92 0.010 . 663 87 ILE HG13 H 0.49 0.007 . 664 87 ILE HD1 H 0.36 0.015 . 665 87 ILE CD1 C 14.27 0.000 . 666 88 GLY N N 105.96 0.000 . 667 88 GLY H H 7.60 0.001 . 668 88 GLY CA C 46.53 0.000 . 669 88 GLY HA2 H 3.72 0.007 . 670 88 GLY HA3 H 3.00 0.000 . 671 89 GLY N N 119.51 0.000 . 672 89 GLY H H 7.81 0.004 . 673 89 GLY CA C 46.39 0.000 . 674 89 GLY HA2 H 4.56 0.000 . 675 89 GLY HA3 H 4.12 0.000 . 676 90 ASP N N 122.47 0.000 . 677 90 ASP H H 8.28 0.002 . 678 90 ASP CA C 56.09 0.000 . 679 90 ASP HA H 4.63 0.002 . 680 90 ASP CB C 39.54 0.000 . 681 90 ASP HB2 H 2.90 0.015 . 682 91 ALA N N 119.67 0.000 . 683 91 ALA H H 8.61 0.022 . 685 91 ALA HA H 4.70 0.000 . 686 91 ALA HB H 0.94 0.029 . 688 92 HIS N N 121.69 0.000 . 689 92 HIS H H 9.34 0.001 . 691 92 HIS HA H 5.73 0.010 . 693 92 HIS HB2 H 3.20 0.000 . 694 92 HIS HB3 H 2.41 0.000 . 695 92 HIS HD2 H 6.88 0.006 . 696 92 HIS HE1 H 9.24 0.000 . 697 93 PHE N N 122.67 0.000 . 698 93 PHE H H 9.13 0.002 . 700 93 PHE HA H 4.16 0.002 . 702 93 PHE HB2 H 2.00 0.006 . 703 93 PHE HB3 H 1.65 0.012 . 704 93 PHE HD1 H 6.23 0.039 . 705 93 PHE HD2 H 6.23 0.039 . 706 94 ASP N N 120.87 0.000 . 707 94 ASP H H 8.01 0.000 . 708 94 ASP HA H 4.14 0.005 . 709 95 GLU N N 120.27 0.000 . 710 95 GLU H H 8.03 0.001 . 711 95 GLU HA H 4.84 0.000 . 712 95 GLU HB2 H 2.95 0.005 . 713 96 ASP N N 122.50 0.000 . 714 96 ASP H H 8.13 0.000 . 715 96 ASP HA H 4.33 0.002 . 716 96 ASP HB2 H 2.66 0.007 . 717 97 GLU N N 130.58 0.000 . 718 97 GLU H H 9.40 0.009 . 720 97 GLU HA H 4.27 0.000 . 722 97 GLU HB2 H 1.95 0.001 . 723 97 GLU HB3 H 1.64 0.003 . 724 98 PHE N N 119.28 0.000 . 725 98 PHE H H 9.02 0.014 . 726 98 PHE CA C 56.50 0.000 . 727 98 PHE HA H 4.72 0.004 . 728 98 PHE CB C 39.15 0.000 . 729 98 PHE HB2 H 2.50 0.016 . 730 99 TRP N N 116.69 0.000 . 731 99 TRP H H 7.37 0.006 . 733 99 TRP HA H 4.37 0.015 . 734 99 TRP CB C 25.76 0.000 . 735 99 TRP HB2 H 1.00 0.004 . 736 99 TRP HB3 H 0.55 0.010 . 737 99 TRP NE1 N 127.26 0.000 . 738 99 TRP HE3 H 7.12 0.000 . 739 99 TRP HE1 H 10.15 0.001 . 740 99 TRP HZ3 H 6.82 0.000 . 741 100 THR N N 125.89 0.000 . 742 100 THR H H 8.37 0.015 . 743 100 THR HA H 4.67 0.000 . 744 100 THR HB H 4.46 0.000 . 745 100 THR HG2 H 2.68 0.000 . 746 101 THR N N 122.67 0.000 . 747 101 THR H H 7.94 0.007 . 748 101 THR CA C 53.45 0.000 . 749 101 THR HA H 4.57 0.000 . 751 101 THR HB H 4.41 0.000 . 752 101 THR HG2 H 1.22 0.001 . 753 102 HIS N N 120.54 0.006 . 754 102 HIS H H 7.55 0.001 . 755 102 HIS HA H 4.11 0.005 . 757 102 HIS HB2 H 3.03 0.002 . 758 102 HIS HB3 H 2.79 0.000 . 759 102 HIS HD2 H 9.36 0.000 . 760 102 HIS HE1 H 6.92 0.000 . 761 103 SER N N 123.44 0.000 . 762 103 SER H H 7.50 0.003 . 763 103 SER CA C 58.14 0.000 . 764 103 SER HA H 3.58 0.001 . 765 103 SER CB C 63.17 0.000 . 766 103 SER HB2 H 3.30 0.000 . 767 103 SER HB3 H 2.65 0.002 . 768 104 GLY N N 115.17 0.000 . 769 104 GLY H H 9.51 0.006 . 770 104 GLY CA C 44.74 0.000 . 771 104 GLY HA2 H 4.08 0.000 . 772 104 GLY HA3 H 3.77 0.000 . 773 105 GLY N N 108.04 0.000 . 774 105 GLY H H 7.84 0.001 . 775 105 GLY CA C 45.64 0.000 . 776 105 GLY HA2 H 3.89 0.000 . 777 106 THR N N 125.04 0.000 . 778 106 THR H H 9.15 0.006 . 780 106 THR HA H 3.59 0.000 . 781 106 THR CB C 68.35 0.000 . 782 106 THR HB H 2.44 0.000 . 783 106 THR HG2 H 0.20 0.014 . 784 106 THR CG2 C 24.31 0.000 . 785 107 ASN N N 125.33 0.000 . 786 107 ASN H H 8.49 0.006 . 787 107 ASN CA C 55.27 0.000 . 788 107 ASN HA H 4.71 0.001 . 789 107 ASN CB C 41.52 0.000 . 790 107 ASN HB2 H 3.09 0.002 . 791 107 ASN ND2 N 111.06 0.000 . 792 107 ASN HD21 H 7.93 0.006 . 793 107 ASN HD22 H 6.31 0.007 . 794 108 LEU N N 131.67 0.000 . 795 108 LEU H H 8.54 0.011 . 796 108 LEU CA C 58.52 0.030 . 797 108 LEU HA H 4.36 0.003 . 798 108 LEU CB C 41.09 0.000 . 799 108 LEU HB2 H 1.80 0.002 . 800 108 LEU HB3 H 1.47 0.003 . 801 108 LEU CG C 27.53 0.000 . 802 108 LEU HG H 1.01 0.018 . 803 108 LEU HD1 H 0.75 0.032 . 804 108 LEU HD2 H -0.20 0.000 . 805 108 LEU CD1 C 27.57 0.000 . 806 108 LEU CD2 C 22.12 0.000 . 807 109 PHE N N 120.17 0.000 . 808 109 PHE H H 9.20 0.001 . 809 109 PHE HA H 3.85 0.002 . 810 109 PHE CB C 37.57 0.000 . 811 109 PHE HB2 H 3.36 0.001 . 812 109 PHE HB3 H 3.09 0.000 . 813 109 PHE HD1 H 7.16 0.000 . 814 109 PHE HD2 H 7.16 0.000 . 815 109 PHE HE1 H 6.47 0.007 . 816 109 PHE HE2 H 6.47 0.007 . 817 110 LEU N N 118.22 0.000 . 818 110 LEU H H 8.84 0.001 . 819 110 LEU CA C 57.73 0.000 . 820 110 LEU HA H 3.07 0.006 . 821 110 LEU CB C 42.83 0.000 . 822 110 LEU HB2 H 1.72 0.013 . 823 110 LEU HB3 H 1.51 0.001 . 824 110 LEU CG C 26.01 0.000 . 825 110 LEU HG H 0.95 0.018 . 826 110 LEU HD1 H 0.47 0.000 . 827 110 LEU CD1 C 23.66 0.000 . 828 111 THR N N 112.42 0.000 . 829 111 THR H H 7.35 0.014 . 830 111 THR CA C 66.51 0.000 . 831 111 THR HA H 4.08 0.000 . 832 111 THR CB C 68.07 0.000 . 833 111 THR HB H 4.31 0.003 . 834 111 THR HG2 H 1.34 0.002 . 835 111 THR CG2 C 22.13 0.000 . 836 112 ALA N N 124.02 0.000 . 837 112 ALA H H 9.37 0.003 . 838 112 ALA CA C 55.49 0.000 . 839 112 ALA HA H 3.92 0.003 . 840 112 ALA HB H 1.02 0.007 . 841 112 ALA CB C 17.11 0.000 . 842 113 VAL N N 118.44 0.000 . 843 113 VAL H H 8.35 0.002 . 844 113 VAL CA C 68.10 0.000 . 845 113 VAL HA H 3.13 0.025 . 846 113 VAL CB C 30.94 0.000 . 847 113 VAL HB H 1.68 0.003 . 848 113 VAL HG1 H 0.67 0.006 . 849 113 VAL HG2 H 0.08 0.001 . 850 113 VAL CG1 C 23.37 0.000 . 851 113 VAL CG2 C 23.10 0.000 . 852 114 HIS N N 118.02 0.000 . 853 114 HIS H H 6.99 0.000 . 854 114 HIS CA C 58.61 0.000 . 855 114 HIS HA H 4.35 0.000 . 857 114 HIS HB2 H 3.90 0.000 . 858 114 HIS HB3 H 3.07 0.000 . 859 114 HIS HD2 H 9.86 0.000 . 860 115 GLU N N 115.60 0.000 . 861 115 GLU H H 8.84 0.007 . 862 115 GLU CA C 58.64 0.000 . 863 115 GLU HA H 3.85 0.000 . 864 115 GLU CB C 28.42 0.024 . 865 115 GLU HB2 H 1.75 0.005 . 866 115 GLU CG C 33.15 0.000 . 867 115 GLU HG2 H 1.43 0.004 . 868 116 ILE N N 117.86 0.000 . 869 116 ILE H H 8.95 0.003 . 870 116 ILE CA C 63.37 0.000 . 871 116 ILE HA H 3.43 0.000 . 872 116 ILE CB C 37.05 0.000 . 873 116 ILE HB H 1.30 0.002 . 874 116 ILE HG2 H 0.13 0.002 . 875 116 ILE CG2 C 19.03 0.000 . 876 116 ILE CG1 C 28.94 0.000 . 877 116 ILE HG12 H 0.90 0.002 . 878 116 ILE HG13 H 0.20 0.014 . 879 116 ILE HD1 H -0.46 0.144 . 880 116 ILE CD1 C 12.02 0.000 . 881 117 GLY N N 108.06 0.000 . 882 117 GLY H H 7.53 0.010 . 884 117 GLY HA2 H 3.79 0.021 . 885 117 GLY HA3 H 2.29 0.002 . 886 118 HIS N N 119.58 0.000 . 887 118 HIS H H 7.12 0.004 . 889 118 HIS HA H 4.86 0.000 . 891 118 HIS HB2 H 3.73 0.000 . 892 118 HIS HB3 H 2.39 0.000 . 893 118 HIS HD2 H 6.70 0.000 . 894 118 HIS HE1 H 8.29 0.000 . 895 119 SER N N 122.34 0.005 . 896 119 SER H H 8.78 0.005 . 898 119 SER HA H 4.06 0.000 . 900 119 SER HB2 H 3.48 0.001 . 901 120 LEU N N 114.12 0.000 . 902 120 LEU H H 7.68 0.008 . 903 120 LEU HA H 4.48 0.001 . 904 120 LEU HB2 H 1.90 0.003 . 905 120 LEU HG H 1.55 0.000 . 906 120 LEU HD1 H 0.74 0.000 . 907 120 LEU HD2 H 0.23 0.000 . 908 121 GLY N N 106.54 0.000 . 909 121 GLY H H 8.13 0.000 . 910 121 GLY HA2 H 4.60 0.001 . 911 121 GLY HA3 H 3.33 0.007 . 912 122 LEU N N 120.82 0.000 . 913 122 LEU H H 8.37 0.000 . 914 122 LEU HA H 4.73 0.000 . 915 122 LEU HB2 H 1.41 0.002 . 916 122 LEU HG H 1.23 0.000 . 917 122 LEU HD1 H 0.69 0.001 . 918 122 LEU HD2 H 0.67 0.000 . 919 123 GLY N N 109.70 0.000 . 920 123 GLY H H 8.27 0.000 . 921 123 GLY HA2 H 4.60 0.000 . 922 123 GLY HA3 H 4.34 0.000 . 923 124 HIS N N 115.52 0.000 . 924 124 HIS H H 8.37 0.000 . 925 124 HIS HA H 3.78 0.000 . 926 124 HIS HB2 H 2.90 0.000 . 927 124 HIS HB3 H 2.72 0.000 . 928 124 HIS HD2 H 7.68 0.000 . 929 124 HIS HE1 H 8.49 0.000 . 931 125 SER H H 6.85 0.007 . 932 125 SER CA C 54.93 0.000 . 933 125 SER HA H 4.68 0.000 . 934 125 SER CB C 65.02 0.000 . 935 125 SER HB2 H 4.16 0.000 . 936 125 SER HB3 H 3.10 0.001 . 937 126 SER N N 119.78 0.000 . 938 126 SER H H 8.79 0.000 . 939 126 SER HA H 4.69 0.002 . 940 126 SER CB C 63.88 0.000 . 941 126 SER HB2 H 4.01 0.001 . 942 126 SER HB3 H 3.90 0.002 . 943 127 ASP N N 126.62 0.000 . 944 127 ASP H H 8.89 0.000 . 945 127 ASP HA H 4.70 0.000 . 946 127 ASP CB C 41.80 0.000 . 947 127 ASP HB2 H 2.96 0.013 . 948 127 ASP HB3 H 2.37 0.000 . 949 128 PRO CD C 50.46 0.000 . 950 128 PRO CA C 62.69 0.000 . 951 128 PRO HA H 2.43 0.006 . 952 128 PRO CB C 31.79 0.000 . 953 128 PRO HB2 H 1.44 0.009 . 954 128 PRO HD2 H 4.00 0.004 . 955 128 PRO HD3 H 3.66 0.001 . 956 129 LYS N N 116.58 0.000 . 957 129 LYS H H 8.18 0.000 . 958 129 LYS CA C 56.08 0.000 . 959 129 LYS HA H 4.05 0.002 . 960 129 LYS CB C 31.73 0.000 . 961 129 LYS HB2 H 1.70 0.004 . 962 129 LYS CG C 24.71 0.000 . 963 129 LYS HG2 H 1.35 0.008 . 964 129 LYS HG3 H 1.27 0.001 . 965 129 LYS HD2 H 2.42 0.000 . 966 129 LYS HE2 H 2.95 0.000 . 967 130 ALA N N 123.73 0.000 . 968 130 ALA H H 8.13 0.000 . 969 130 ALA CA C 51.61 0.000 . 970 130 ALA HA H 4.52 0.002 . 971 130 ALA HB H 1.72 0.012 . 972 130 ALA CB C 19.46 0.000 . 974 131 VAL H H 11.47 0.001 . 976 131 VAL HA H 4.35 0.000 . 978 131 VAL HB H 2.36 0.001 . 979 131 VAL HG1 H 0.02 0.000 . 980 131 VAL HG2 H 0.98 0.008 . 981 131 VAL CG1 C 22.40 0.000 . 982 131 VAL CG2 C 20.52 0.000 . 983 132 MET N N 115.33 0.000 . 984 132 MET H H 7.62 0.009 . 985 132 MET CA C 53.27 0.000 . 986 132 MET HA H 4.53 0.008 . 987 132 MET CB C 27.18 0.000 . 988 132 MET HB2 H 2.58 0.001 . 989 132 MET HB3 H 2.13 0.007 . 990 132 MET HG2 H 0.98 0.000 . 991 132 MET HE H 0.47 0.000 . 992 133 PHE N N 128.22 0.000 . 993 133 PHE H H 8.06 0.001 . 994 133 PHE CA C 56.38 0.000 . 995 133 PHE HA H 4.95 0.009 . 996 133 PHE CB C 39.77 0.000 . 997 133 PHE HB2 H 3.66 0.002 . 998 133 PHE HB3 H 3.17 0.000 . 999 133 PHE HD1 H 7.22 0.025 . 1000 133 PHE HD2 H 7.22 0.025 . 1001 133 PHE HE1 H 6.10 0.008 . 1002 133 PHE HE2 H 6.10 0.008 . 1003 134 PRO HA H 3.83 0.003 . 1004 135 THR N N 116.37 0.000 . 1005 135 THR H H 7.68 0.000 . 1006 135 THR CA C 61.77 0.000 . 1007 135 THR HA H 4.62 0.000 . 1008 135 THR CB C 71.65 0.000 . 1009 135 THR HB H 3.96 0.016 . 1010 135 THR HG2 H 1.20 0.001 . 1011 135 THR CG2 C 21.71 0.000 . 1012 136 TYR N N 127.86 0.000 . 1013 136 TYR H H 9.04 0.015 . 1014 136 TYR CA C 58.51 0.000 . 1015 136 TYR HA H 4.54 0.002 . 1016 136 TYR CB C 38.77 0.000 . 1017 136 TYR HB2 H 2.67 0.021 . 1018 136 TYR HB3 H 2.22 0.002 . 1019 136 TYR HD1 H 6.72 0.008 . 1020 136 TYR HD2 H 6.72 0.008 . 1021 136 TYR HE1 H 7.41 0.000 . 1022 136 TYR HE2 H 7.41 0.000 . 1023 136 TYR HH H 7.01 0.003 . 1024 137 LYS N N 129.81 0.000 . 1025 137 LYS H H 7.90 0.001 . 1026 137 LYS CA C 55.28 0.000 . 1027 137 LYS HA H 3.90 0.003 . 1028 137 LYS CB C 34.53 0.000 . 1029 137 LYS HB2 H 1.52 0.000 . 1030 137 LYS HB3 H 1.56 0.000 . 1031 137 LYS HG2 H 1.16 0.002 . 1032 137 LYS HD2 H 1.55 0.000 . 1033 137 LYS HE2 H 3.01 0.000 . 1034 138 TYR N N 123.97 0.000 . 1035 138 TYR H H 8.51 0.000 . 1036 138 TYR CA C 60.77 0.000 . 1037 138 TYR HA H 3.90 0.001 . 1038 138 TYR CB C 38.17 0.000 . 1039 138 TYR HB2 H 2.98 0.001 . 1040 138 TYR HB3 H 2.65 0.011 . 1041 138 TYR HD1 H 6.82 0.002 . 1042 138 TYR HD2 H 6.82 0.002 . 1043 138 TYR HE1 H 9.04 0.000 . 1044 138 TYR HE2 H 9.04 0.000 . 1045 139 VAL N N 124.25 0.000 . 1046 139 VAL H H 5.75 0.002 . 1047 139 VAL CA C 59.06 0.000 . 1048 139 VAL HA H 3.77 0.043 . 1049 139 VAL CB C 34.98 0.000 . 1050 139 VAL HB H 1.80 0.001 . 1051 139 VAL HG1 H 0.79 0.017 . 1052 139 VAL HG2 H 0.77 0.002 . 1053 139 VAL CG1 C 20.98 0.000 . 1054 139 VAL CG2 C 19.42 0.000 . 1055 140 ASP N N 118.96 0.000 . 1056 140 ASP H H 7.81 0.005 . 1057 140 ASP CA C 54.88 0.000 . 1058 140 ASP HA H 4.17 0.004 . 1059 140 ASP CB C 41.72 0.000 . 1060 140 ASP HB2 H 2.66 0.026 . 1061 141 ILE N N 124.28 0.000 . 1062 141 ILE H H 7.73 0.000 . 1063 141 ILE CA C 64.26 0.000 . 1064 141 ILE HA H 3.76 0.000 . 1065 141 ILE CB C 37.41 0.000 . 1066 141 ILE HB H 1.83 0.020 . 1067 141 ILE HG2 H 1.04 0.004 . 1068 141 ILE CG2 C 17.62 0.000 . 1069 141 ILE CG1 C 26.93 0.000 . 1070 141 ILE HG12 H 1.14 0.000 . 1071 141 ILE HD1 H 0.67 0.006 . 1072 141 ILE CD1 C 13.36 0.000 . 1073 142 ASN N N 118.34 0.000 . 1074 142 ASN H H 8.49 0.000 . 1075 142 ASN CA C 55.29 0.000 . 1076 142 ASN HA H 4.57 0.005 . 1077 142 ASN CB C 38.13 0.045 . 1078 142 ASN HB2 H 2.88 0.000 . 1079 142 ASN HB3 H 2.75 0.000 . 1080 142 ASN ND2 N 114.80 0.000 . 1081 142 ASN HD21 H 7.53 0.000 . 1082 142 ASN HD22 H 7.00 0.001 . 1083 143 THR N N 109.25 0.000 . 1084 143 THR H H 7.55 0.000 . 1085 143 THR CA C 60.77 0.000 . 1086 143 THR HA H 4.34 0.012 . 1087 143 THR CB C 69.22 0.000 . 1088 143 THR HB H 4.27 0.000 . 1089 143 THR HG2 H 1.05 0.012 . 1090 144 PHE N N 123.18 0.000 . 1091 144 PHE H H 7.18 0.000 . 1092 144 PHE CA C 59.62 0.048 . 1093 144 PHE HA H 4.10 0.002 . 1094 144 PHE CB C 39.77 0.000 . 1095 144 PHE HB2 H 3.02 0.001 . 1096 144 PHE HB3 H 2.81 0.018 . 1097 144 PHE HE1 H 6.48 0.000 . 1098 144 PHE HE2 H 6.48 0.000 . 1099 145 ARG N N 126.10 0.000 . 1100 145 ARG H H 7.12 0.000 . 1101 145 ARG CA C 53.91 0.000 . 1102 145 ARG HA H 3.92 0.013 . 1103 145 ARG CB C 33.20 0.000 . 1104 145 ARG HB2 H 1.60 0.000 . 1105 145 ARG HB3 H 1.39 0.001 . 1106 145 ARG CG C 25.82 0.000 . 1107 145 ARG HG2 H 1.42 0.000 . 1108 145 ARG HG3 H 1.35 0.000 . 1109 145 ARG CD C 43.29 0.000 . 1110 145 ARG HD2 H 3.08 0.001 . 1111 145 ARG HD3 H 2.99 0.000 . 1112 146 LEU N N 120.99 0.000 . 1113 146 LEU H H 8.09 0.000 . 1114 146 LEU CA C 54.58 0.000 . 1115 146 LEU HA H 3.82 0.000 . 1116 146 LEU CB C 42.82 0.000 . 1117 146 LEU HB2 H 1.40 0.003 . 1118 146 LEU HB3 H 1.31 0.000 . 1119 146 LEU HG H 1.32 0.000 . 1120 146 LEU HD1 H 0.70 0.007 . 1121 146 LEU HD2 H 0.15 0.063 . 1122 147 SER N N 118.14 0.000 . 1123 147 SER H H 8.89 0.012 . 1125 147 SER HA H 4.46 0.000 . 1126 147 SER CB C 65.72 0.000 . 1127 147 SER HB2 H 4.15 0.000 . 1128 147 SER HB3 H 3.82 0.000 . 1129 148 ALA N N 123.45 0.000 . 1130 148 ALA H H 8.78 0.001 . 1131 148 ALA CA C 55.34 0.000 . 1132 148 ALA HA H 4.00 0.005 . 1133 148 ALA HB H 1.40 0.009 . 1134 148 ALA CB C 17.63 0.000 . 1135 149 ASP N N 117.53 0.000 . 1136 149 ASP H H 8.21 0.001 . 1137 149 ASP CA C 57.94 0.000 . 1138 149 ASP HA H 4.25 0.017 . 1139 149 ASP CB C 43.75 0.000 . 1140 149 ASP HB2 H 2.77 0.000 . 1141 149 ASP HB3 H 2.43 0.004 . 1142 150 ASP N N 118.65 0.000 . 1143 150 ASP H H 7.40 0.009 . 1144 150 ASP HA H 4.67 0.000 . 1146 150 ASP HB2 H 3.01 0.012 . 1147 150 ASP HB3 H 2.71 0.000 . 1148 151 ILE N N 118.78 0.000 . 1149 151 ILE H H 7.91 0.008 . 1150 151 ILE CA C 65.36 0.000 . 1151 151 ILE HA H 3.66 0.010 . 1152 151 ILE CB C 38.15 0.000 . 1153 151 ILE HB H 1.67 0.000 . 1154 151 ILE HG2 H 0.89 0.005 . 1155 151 ILE CG2 C 16.84 0.000 . 1156 151 ILE CG1 C 30.40 0.000 . 1157 151 ILE HG12 H 1.71 0.009 . 1158 151 ILE HG13 H 0.74 0.000 . 1159 151 ILE HD1 H 0.68 0.009 . 1160 151 ILE CD1 C 12.83 0.000 . 1161 152 ARG N N 119.04 0.000 . 1162 152 ARG H H 8.50 0.015 . 1163 152 ARG CA C 59.03 0.000 . 1164 152 ARG HA H 3.98 0.000 . 1165 152 ARG CB C 29.85 0.000 . 1166 152 ARG HB2 H 1.87 0.037 . 1167 152 ARG HB3 H 1.82 0.015 . 1168 152 ARG CG C 26.92 0.000 . 1169 152 ARG HG2 H 1.73 0.000 . 1170 152 ARG HG3 H 1.55 0.000 . 1171 152 ARG CD C 43.19 0.000 . 1172 152 ARG HD2 H 3.16 0.000 . 1173 153 GLY N N 106.70 0.000 . 1174 153 GLY H H 8.26 0.000 . 1175 153 GLY CA C 47.32 0.000 . 1176 153 GLY HA2 H 3.74 0.000 . 1177 153 GLY HA3 H 3.96 0.000 . 1178 154 ILE N N 123.47 0.000 . 1179 154 ILE H H 8.62 0.000 . 1180 154 ILE CA C 60.71 0.000 . 1181 154 ILE HA H 4.43 0.004 . 1182 154 ILE CB C 38.51 0.000 . 1183 154 ILE HB H 2.11 0.000 . 1184 154 ILE HG2 H 1.52 0.000 . 1185 154 ILE CG2 C 20.53 0.000 . 1186 154 ILE HG12 H 1.72 0.035 . 1187 154 ILE HG13 H 1.50 0.000 . 1188 154 ILE HD1 H 0.85 0.000 . 1189 154 ILE CD1 C 14.74 0.000 . 1190 155 GLN N N 123.38 0.000 . 1191 155 GLN H H 8.63 0.006 . 1193 155 GLN HA H 4.42 0.000 . 1195 155 GLN HB2 H 2.20 0.000 . 1196 155 GLN HB3 H 1.98 0.000 . 1197 155 GLN CG C 34.86 0.000 . 1198 155 GLN HG2 H 2.89 0.010 . 1199 155 GLN HG3 H 2.73 0.107 . 1200 155 GLN NE2 N 117.74 0.000 . 1201 155 GLN HE21 H 8.29 0.001 . 1202 155 GLN HE22 H 7.69 0.000 . 1203 156 SER N N 115.37 0.000 . 1204 156 SER H H 7.89 0.010 . 1206 156 SER HA H 4.21 0.000 . 1207 156 SER HB3 H 3.96 0.000 . 1209 157 LEU H H 6.93 0.002 . 1211 157 LEU HA H 4.06 0.000 . 1213 157 LEU HB2 H 1.82 0.000 . 1214 157 LEU HB3 H 0.77 0.000 . 1215 157 LEU HG H 1.69 0.000 . 1216 157 LEU HD1 H 0.59 0.000 . 1217 157 LEU HD2 H 0.58 0.000 . 1218 157 LEU CD2 C 21.71 0.000 . 1220 158 TYR H H 8.16 0.000 . 1221 158 TYR HD1 H 7.24 0.000 . 1222 158 TYR HD2 H 7.24 0.000 . 1224 159 GLY H H 8.29 0.000 . stop_ save_ save_RDC_list_1 _Saveframe_category residual_dipolar_couplings loop_ _Sample_label $sample_2 stop_ _Sample_conditions_label $conditions_1 _Spectrometer_frequency_1H 800 _Mol_system_component_name "MMP12 catalytic domain" loop_ _Residual_dipolar_coupling_ID _Residual_dipolar_coupling_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name _Residual_dipolar_coupling_value _Residual_dipolar_coupling_error 1 1DHNN 6 ARG H 6 ARG N -6.10 1.00 2 1DHNN 9 TYR H 9 TYR N -3.66 1.00 3 1DHNN 10 ILE H 10 ILE N -2.44 1.00 4 1DHNN 11 THR H 11 THR N -2.04 1.00 5 1DHNN 12 TYR H 12 TYR N -6.52 1.00 6 1DHNN 13 ARG H 13 ARG N -10.18 1.00 7 1DHNN 14 ILE H 14 ILE N -10.18 1.00 8 1DHNN 15 ASN H 15 ASN N -0.82 1.00 9 1DHNN 16 ASN H 16 ASN N 6.10 1.00 10 1DHNN 17 TYR H 17 TYR N 10.17 1.00 11 1DHNN 20 ASP H 20 ASP N 0.81 1.00 12 1DHNN 21 MET H 21 MET N -2.44 1.00 13 1DHNN 22 ASN H 22 ASN N 1.63 1.00 14 1DHNN 23 ARG H 23 ARG N 16.68 1.00 15 1DHNN 24 GLU H 24 GLU N 9.77 1.00 16 1DHNN 25 ASP H 25 ASP N 14.65 1.00 17 1DHNN 26 VAL H 26 VAL N 12.61 1.00 18 1DHNN 28 TYR H 28 TYR N 11.40 1.00 19 1DHNN 30 ILE H 30 ILE N 15.47 1.00 20 1DHNN 31 ARG H 31 ARG N 12.21 1.00 21 1DHNN 33 ALA H 33 ALA N 17.91 1.00 22 1DHNN 34 PHE H 34 PHE N 13.33 1.00 23 1DHNN 35 GLN H 35 GLN N 13.02 1.00 24 1DHNN 36 VAL H 36 VAL N 13.02 1.00 25 1DHNN 37 TRP H 37 TRP N 15.87 1.00 26 1DHNN 38 SER H 38 SER N 13.84 1.00 27 1DHNN 40 VAL H 40 VAL N 13.02 1.00 28 1DHNN 41 THR H 41 THR N 2.85 1.00 29 1DHNN 43 LEU H 43 LEU N -5.29 1.00 30 1DHNN 45 PHE H 45 PHE N -2.03 1.00 31 1DHNN 46 SER H 46 SER N -1.22 1.00 32 1DHNN 47 LYS H 47 LYS N -2.44 1.00 33 1DHNN 50 THR H 50 THR N 8.55 1.00 34 1DHNN 53 ALA H 53 ALA N 2.85 1.00 35 1DHNN 55 ILE H 55 ILE N -6.10 1.00 36 1DHNN 56 LEU H 56 LEU N -3.25 1.00 37 1DHNN 57 VAL H 57 VAL N -8.14 1.00 38 1DHNN 58 VAL H 58 VAL N 4.07 1.00 39 1DHNN 59 PHE H 59 PHE N -2.44 1.00 40 1DHNN 60 ALA H 60 ALA N 5.69 1.00 41 1DHNN 61 ARG H 61 ARG N 2.44 1.00 42 1DHNN 62 GLY H 62 GLY N -2.85 1.00 43 1DHNN 63 ALA H 63 ALA N 13.02 1.00 44 1DHNN 67 ASP H 67 ASP N 9.36 1.00 45 1DHNN 69 ALA H 69 ALA N -4.07 1.00 46 1DHNN 72 GLY H 72 GLY N -14.25 1.00 47 1DHNN 74 GLY H 74 GLY N -13.42 1.00 48 1DHNN 75 GLY H 75 GLY N -7.73 1.00 49 1DHNN 76 ILE H 76 ILE N 7.32 1.00 50 1DHNN 77 LEU H 77 LEU N 15.47 1.00 51 1DHNN 78 ALA H 78 ALA N 0.00 1.00 52 1DHNN 79 HIS H 79 HIS N -2.85 1.00 53 1DHNN 82 GLY H 82 GLY N -7.74 1.00 54 1DHNN 84 GLY H 84 GLY N -1.62 1.00 55 1DHNN 85 SER H 85 SER N 0.81 1.00 56 1DHNN 86 GLY H 86 GLY N -12.61 1.00 57 1DHNN 87 ILE H 87 ILE N 1.63 1.00 58 1DHNN 88 GLY H 88 GLY N -7.73 1.00 59 1DHNN 89 GLY H 89 GLY N -7.74 1.00 60 1DHNN 90 ASP H 90 ASP N -3.25 1.00 61 1DHNN 91 ALA H 91 ALA N -5.29 1.00 62 1DHNN 92 HIS H 92 HIS N 2.44 1.00 63 1DHNN 93 PHE H 93 PHE N -3.25 1.00 64 1DHNN 95 GLU H 95 GLU N -3.26 1.00 65 1DHNN 97 GLU H 97 GLU N -2.85 1.00 66 1DHNN 98 PHE H 98 PHE N 1.62 1.00 67 1DHNN 99 TRP H 99 TRP N -10.58 1.00 68 1DHNN 100 THR H 100 THR N -2.85 1.00 69 1DHNN 101 THR H 101 THR N -1.62 1.00 70 1DHNN 105 GLY H 105 GLY N 0.41 1.00 71 1DHNN 106 THR H 106 THR N 7.53 1.00 72 1DHNN 107 ASN H 107 ASN N -2.44 1.00 73 1DHNN 108 LEU H 108 LEU N 7.32 1.00 74 1DHNN 109 PHE H 109 PHE N 2.44 1.00 75 1DHNN 111 THR H 111 THR N 7.32 1.00 76 1DHNN 112 ALA H 112 ALA N 0.00 1.00 77 1DHNN 113 VAL H 113 VAL N -2.85 1.00 78 1DHNN 114 HIS H 114 HIS N 5.29 1.00 79 1DHNN 115 GLU H 115 GLU N 3.46 1.00 80 1DHNN 116 ILE H 116 ILE N -2.45 1.00 81 1DHNN 117 GLY H 117 GLY N -3.66 1.00 82 1DHNN 118 HIS H 118 HIS N 5.69 1.00 83 1DHNN 119 SER H 119 SER N -1.63 1.00 84 1DHNN 120 LEU H 120 LEU N -11.80 1.00 85 1DHNN 122 LEU H 122 LEU N 4.88 1.00 86 1DHNN 124 HIS H 124 HIS N -0.61 1.00 87 1DHNN 125 SER H 125 SER N 10.17 1.00 88 1DHNN 126 SER H 126 SER N 4.88 1.00 89 1DHNN 129 LYS H 129 LYS N 12.40 1.00 90 1DHNN 131 VAL H 131 VAL N -3.25 1.00 91 1DHNN 132 MET H 132 MET N 13.42 1.00 92 1DHNN 133 PHE H 133 PHE N -2.45 1.00 93 1DHNN 135 THR H 135 THR N 2.04 1.00 94 1DHNN 136 TYR H 136 TYR N 1.63 1.00 95 1DHNN 137 LYS H 137 LYS N -8.58 1.00 96 1DHNN 138 TYR H 138 TYR N -6.51 1.00 97 1DHNN 139 VAL H 139 VAL N -2.85 1.00 98 1DHNN 140 ASP H 140 ASP N -2.85 1.00 99 1DHNN 141 ILE H 141 ILE N 12.61 1.00 100 1DHNN 142 ASN H 142 ASN N -2.85 1.00 101 1DHNN 143 THR H 143 THR N 4.07 1.00 102 1DHNN 144 PHE H 144 PHE N -2.03 1.00 103 1DHNN 147 SER H 147 SER N 0.41 1.00 104 1DHNN 148 ALA H 148 ALA N -5.29 1.00 105 1DHNN 149 ASP H 149 ASP N -8.96 1.00 106 1DHNN 150 ASP H 150 ASP N -4.07 1.00 107 1DHNN 151 ILE H 151 ILE N -6.51 1.00 108 1DHNN 153 GLY H 153 GLY N -4.47 1.00 109 1DHNN 155 GLN H 155 GLN N -3.26 1.00 110 1DHNN 156 SER H 156 SER N -6.92 1.00 111 1DHNN 157 LEU H 157 LEU N -4.88 1.00 stop_ save_