data_4214 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; N-terminal Domain of Tissue Inhibitor of Metalloproteinase-2 (N-TIMP-2) ; _BMRB_accession_number 4214 _BMRB_flat_file_name bmr4214.str _Entry_type original _Submission_date 1998-05-27 _Accession_date 1998-11-10 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Muskett F. W. . 2 Frenkiel T. A. . 3 Feeney J. . . 4 Freedman R. B. . 5 Carr M. D. . 6 Williamson R. A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 704 "13C chemical shifts" 372 "15N chemical shifts" 128 "coupling constants" 164 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-06-17 original author . stop_ _Original_release_date 2000-06-17 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; High resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98371010 _PubMed_ID 9705310 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Muskett F. W. . 2 Frenkiel T. A. . 3 Feeney J. . . 4 Freedman R. B. . 5 Carr M. D. . 6 Williamson R. A. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'Journal of Biological Chemistry' _Journal_volume 273 _Journal_issue 34 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 21736 _Page_last 21743 _Year 1998 _Details . loop_ _Keyword 'Matrix Metalloproteinase Inhibitor' 'MMP Inhibitor' OB-fold TIMP stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full 'Delaglio,F. et al (1995) J. Biomol NMR 6, 277-293' _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F . . 2 Grzesiek S . . 3 Vuister 'G W' W. . 4 Zhu G . . 5 Pfeifer J . . 6 Bax A . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ save_ref_2 _Saveframe_category citation _Citation_full 'Bartels, C. et al., (1995) J. Biomol NMR 6, 1-10' _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref_3 _Saveframe_category citation _Citation_full 'Guntert, P. et al., (1997) J. Mol. Biol. 273, 283-298' _Citation_title 'Torsion angle dynamics for NMR structure calculation with the new program DYANA.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9367762 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Guntert P. . . 2 Mumenthaler C. . . 3 Wuthrich K. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 273 _Journal_issue 1 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 283 _Page_last 298 _Year 1997 _Details ; The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the "bundle" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures. ; save_ ################################## # Molecular system description # ################################## save_system_N-TIMP-2 _Saveframe_category molecular_system _Mol_system_name 'Tissue Inhibitor of Metalloproteinases-2 (TIMP-2)' _Abbreviation_common N-TIMP-2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'N-TIMP-2 monomer' $N-TIMP-2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'matrix metalloproteinase (MMP) inhibitor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_N-TIMP-2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'tissue inhibitor of metalloproteinases-2 (TIMP-2)' _Name_variant 'A 21 T' _Abbreviation_common N-TIMP-2 _Molecular_mass 14084 _Mol_thiol_state 'all disulfide bound' _Details 'Recombinant material refolded from E.coli inclusion bodies' ############################## # Polymer residue sequence # ############################## _Residue_count 127 _Mol_residue_sequence ; CSCSPVHPQQAFCNADVVIR TKAVSEKEVDSGNDIYGNPI KRIQYEIKQIKMFKGPEKDI EFIYTAPSSAVCGVSLDVGG KKEYLIAGKAEGDGKMHITL CDFIVPWDTLSTTQKKSLNH RYQMGCE ; loop_ _Residue_seq_code _Residue_label 1 CYS 2 SER 3 CYS 4 SER 5 PRO 6 VAL 7 HIS 8 PRO 9 GLN 10 GLN 11 ALA 12 PHE 13 CYS 14 ASN 15 ALA 16 ASP 17 VAL 18 VAL 19 ILE 20 ARG 21 THR 22 LYS 23 ALA 24 VAL 25 SER 26 GLU 27 LYS 28 GLU 29 VAL 30 ASP 31 SER 32 GLY 33 ASN 34 ASP 35 ILE 36 TYR 37 GLY 38 ASN 39 PRO 40 ILE 41 LYS 42 ARG 43 ILE 44 GLN 45 TYR 46 GLU 47 ILE 48 LYS 49 GLN 50 ILE 51 LYS 52 MET 53 PHE 54 LYS 55 GLY 56 PRO 57 GLU 58 LYS 59 ASP 60 ILE 61 GLU 62 PHE 63 ILE 64 TYR 65 THR 66 ALA 67 PRO 68 SER 69 SER 70 ALA 71 VAL 72 CYS 73 GLY 74 VAL 75 SER 76 LEU 77 ASP 78 VAL 79 GLY 80 GLY 81 LYS 82 LYS 83 GLU 84 TYR 85 LEU 86 ILE 87 ALA 88 GLY 89 LYS 90 ALA 91 GLU 92 GLY 93 ASP 94 GLY 95 LYS 96 MET 97 HIS 98 ILE 99 THR 100 LEU 101 CYS 102 ASP 103 PHE 104 ILE 105 VAL 106 PRO 107 TRP 108 ASP 109 THR 110 LEU 111 SER 112 THR 113 THR 114 GLN 115 LYS 116 LYS 117 SER 118 LEU 119 ASN 120 HIS 121 ARG 122 TYR 123 GLN 124 MET 125 GLY 126 CYS 127 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-03-16 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 1BR9 "Human Tissue Inhibitor Of Metalloproteinase-2" 100.00 194 99.21 99.21 2.47e-86 PDB 1GXD "Prommp-2TIMP-2 Complex" 100.00 194 99.21 99.21 2.47e-86 PDB 2TMP "N-Terminal Domain Of Tissue Inhibitor Of Metalloproteinase- 2 (N-Timp-2), Nmr, 49 Structures" 99.21 127 100.00 100.00 7.90e-88 PDB 4ILW "Complex Of Matrix Metalloproteinase-10 Catalytic Domain (mmp-10cd) With Tissue Inhibitor Of Metalloproteinases-2 (timp-2)" 100.00 194 99.21 99.21 2.47e-86 DBJ BAG57573 "unnamed protein product [Homo sapiens]" 59.84 143 100.00 100.00 5.56e-47 EMBL CAA38400 "Tissue inhibitor of metalloproteinases, Type-2 [Homo sapiens]" 97.64 185 98.39 98.39 5.44e-83 EMBL CAA44491 "Tissue inhibitor of metalloproteinases, Type 2 [Mus musculus]" 100.00 220 97.64 98.43 2.36e-85 EMBL CAA53528 "tissue inhibitor of metaro proteinase [Cricetulus longicaudatus]" 100.00 196 98.43 99.21 8.48e-86 EMBL CAC35060 "tissue inhibitor of metalloproteinase type 2 [Rattus norvegicus]" 100.00 220 97.64 98.43 2.66e-85 GB AAA40445 "tissue inhibitor of metalloproteinases [Mus musculus domesticus]" 100.00 220 97.64 98.43 2.36e-85 GB AAA40446 "TIMP-2 [Mus musculus]" 100.00 220 97.64 98.43 3.39e-85 GB AAA59581 "metalloproteinase inhibitor precursor [Homo sapiens]" 100.00 220 99.21 99.21 1.13e-86 GB AAA61186 "metalloproteinase-2 inhibitor precursor [Homo sapiens]" 100.00 220 99.21 99.21 1.13e-86 GB AAA84581 "matrix metalloproteinase inhibitor [Rattus norvegicus]" 100.00 220 97.64 98.43 2.66e-85 PIR I53415 "tissue inhibitor of metalloproteinase type 2 - rat" 100.00 220 97.64 98.43 2.66e-85 REF NP_001166495 "metalloproteinase inhibitor 2 precursor [Cavia porcellus]" 100.00 220 99.21 99.21 1.89e-86 REF NP_003246 "metalloproteinase inhibitor 2 precursor [Homo sapiens]" 100.00 220 99.21 99.21 1.13e-86 REF NP_035724 "metalloproteinase inhibitor 2 precursor [Mus musculus]" 100.00 220 97.64 98.43 2.66e-85 REF NP_068824 "metalloproteinase inhibitor 2 precursor [Rattus norvegicus]" 100.00 220 97.64 98.43 2.66e-85 REF XP_001146829 "PREDICTED: metalloproteinase inhibitor 2 [Pan troglodytes]" 100.00 220 99.21 99.21 1.71e-86 SP P16035 "RecName: Full=Metalloproteinase inhibitor 2; AltName: Full=CSC-21K; AltName: Full=Tissue inhibitor of metalloproteinases 2; Sho" 100.00 220 99.21 99.21 1.13e-86 SP P25785 "RecName: Full=Metalloproteinase inhibitor 2; AltName: Full=Tissue inhibitor of metalloproteinases 2; Short=TIMP-2; Flags: Precu" 100.00 220 97.64 98.43 2.36e-85 SP P30121 "RecName: Full=Metalloproteinase inhibitor 2; AltName: Full=Tissue inhibitor of metalloproteinases 2; Short=TIMP-2; Flags: Precu" 100.00 220 97.64 98.43 2.66e-85 SP Q60453 "RecName: Full=Metalloproteinase inhibitor 2; AltName: Full=Tissue inhibitor of metalloproteinases 2; Short=TIMP-2; Flags: Precu" 100.00 196 98.43 99.21 8.48e-86 SP Q9WUC6 "RecName: Full=Metalloproteinase inhibitor 2; AltName: Full=Tissue inhibitor of metalloproteinases 2; Short=TIMP-2; Flags: Precu" 100.00 220 99.21 99.21 1.89e-86 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $N-TIMP-2 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 _Variant _Vector_type _Vector_name _Details $N-TIMP-2 'recombinant technology' 'Escherichia coli' Escherichia coli BL21 DE3 plasmid . 'protein refolded from inclusion bodies' 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 $N-TIMP-2 1.4 mM '[U-96% 13C; U-98% 15N]' 'Sodium Phosphate' 25 mM . 'potassium Chloride' 100 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 7/9/97 loop_ _Task 'NMR data processing' stop_ _Details . _Citation_label $ref_1 save_ save_xeasy _Saveframe_category software _Name XEASY _Version 1.13.11 loop_ _Task 'Spectral analysis' stop_ _Details . _Citation_label $ref_2 save_ save_Dyana _Saveframe_category software _Name DYANA _Version 1.4 loop_ _Task 'Structure Calculation' stop_ _Details . _Citation_label $ref_3 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 600 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ save_2D_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label $sample_1 save_ save_2D_COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D COSY' _Sample_label $sample_1 save_ save_3D_NOESY-TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NOESY-TOCSY' _Sample_label $sample_1 save_ save_2D_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D HSQC' _Sample_label $sample_1 save_ save_3D_15N_NOESY_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N NOESY HSQC' _Sample_label $sample_1 save_ save_3D_15N_HNHA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N HNHA' _Sample_label $sample_1 save_ save_3D_15N_HNHB_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N HNHB' _Sample_label $sample_1 save_ save_3D_HCCH_TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH TOCSY' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_CBCAHN_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCAHN' _Sample_label $sample_1 save_ save_3D_13C_HMQC_NOESY_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C HMQC NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details ; The sample was equilibrated for 2 hours under these condition before the spectra were collected ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 125 0.02 mM pH* 6.7 0.2 n/a pressure 1 . atm temperature 308 0.1 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 H2O C 13 proton ppm 0.0 internal indirect spherical internal parallel_to_Bo 0.251449530 H2O H 1 proton ppm 4.647 internal direct cylindrical internal parallel_to_Bo . H2O N 15 proton ppm 0.0 internal indirect cylindrical internal parallel_to_Bo 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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'N-TIMP-2 monomer' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 CYS CA C 56.902 . . 2 . 1 CYS HA H 3.886 . . 3 . 1 CYS CB C 44.363 . . 4 . 1 CYS HB2 H 3.110 . . 5 . 1 CYS HB3 H 3.069 . . 6 . 2 SER CA C 57.240 . . 7 . 2 SER HA H 4.687 . . 8 . 2 SER CB C 63.556 . . 9 . 2 SER HB2 H 3.868 . . 10 . 2 SER HB3 H 3.815 . . 11 . 3 CYS N N 121.646 . . 12 . 3 CYS H H 8.227 . . 13 . 3 CYS CA C 53.013 . . 14 . 3 CYS HA H 4.937 . . 15 . 3 CYS CB C 40.673 . . 16 . 3 CYS HB3 H 3.238 . . 17 . 3 CYS HB2 H 2.822 . . 18 . 4 SER N N 119.596 . . 19 . 4 SER H H 8.656 . . 20 . 4 SER CA C 56.450 . . 21 . 4 SER HA H 4.807 . . 22 . 4 SER CB C 63.103 . . 23 . 4 SER HB2 H 3.873 . . 24 . 4 SER HB3 H 3.756 . . 25 . 5 PRO CD C 50.803 . . 26 . 5 PRO CA C 63.426 . . 27 . 5 PRO HA H 4.424 . . 28 . 5 PRO CB C 31.875 . . 29 . 5 PRO HB2 H 2.260 . . 30 . 5 PRO HB3 H 1.850 . . 31 . 5 PRO CG C 27.459 . . 32 . 5 PRO HG2 H 2.079 . . 33 . 5 PRO HG3 H 1.997 . . 34 . 5 PRO HD2 H 3.884 . . 35 . 5 PRO HD3 H 3.692 . . 36 . 6 VAL N N 120.915 . . 37 . 6 VAL H H 8.135 . . 38 . 6 VAL CA C 60.820 . . 39 . 6 VAL HA H 4.205 . . 40 . 6 VAL CB C 33.991 . . 41 . 6 VAL HB H 2.016 . . 42 . 6 VAL HG1 H 0.896 . . 43 . 6 VAL HG2 H 0.866 . . 44 . 6 VAL CG1 C 20.313 . . 45 . 6 VAL CG2 C 19.090 . . 46 . 7 HIS N N 125.141 . . 47 . 7 HIS H H 8.441 . . 48 . 7 HIS CA C 54.639 . . 49 . 7 HIS HA H 4.754 . . 50 . 7 HIS CB C 30.634 . . 51 . 7 HIS HB3 H 3.188 . . 52 . 7 HIS HB2 H 3.086 . . 53 . 7 HIS HD2 H 7.188 . . 54 . 7 HIS HE1 H 8.026 . . 55 . 8 PRO CD C 50.268 . . 56 . 8 PRO CA C 65.830 . . 57 . 8 PRO HA H 3.395 . . 58 . 8 PRO CB C 31.663 . . 59 . 8 PRO HB2 H 1.785 . . 60 . 8 PRO HB3 H 1.653 . . 61 . 8 PRO CG C 27.353 . . 62 . 8 PRO HG2 H 1.959 . . 63 . 8 PRO HG3 H 1.835 . . 64 . 8 PRO HD2 H 3.721 . . 65 . 8 PRO HD3 H 3.198 . . 66 . 9 GLN N N 115.857 . . 67 . 9 GLN H H 8.905 . . 68 . 9 GLN CA C 58.781 . . 69 . 9 GLN HA H 3.782 . . 70 . 9 GLN CB C 28.231 . . 71 . 9 GLN HB2 H 2.010 . . 72 . 9 GLN HB3 H 2.010 . . 73 . 9 GLN CG C 34.074 . . 74 . 9 GLN HG2 H 2.335 . . 75 . 9 GLN HG3 H 2.335 . . 76 . 9 GLN NE2 N 112.460 . . 77 . 9 GLN HE21 H 7.304 . . 78 . 9 GLN HE22 H 7.000 . . 79 . 10 GLN N N 117.843 . . 80 . 10 GLN H H 7.299 . . 81 . 10 GLN CA C 57.624 . . 82 . 10 GLN HA H 4.062 . . 83 . 10 GLN CB C 28.502 . . 84 . 10 GLN HB2 H 2.034 . . 85 . 10 GLN HB3 H 2.034 . . 86 . 10 GLN CG C 33.972 . . 87 . 10 GLN HG2 H 2.310 . . 88 . 10 GLN HG3 H 2.310 . . 89 . 10 GLN NE2 N 112.273 . . 90 . 10 GLN HE21 H 7.434 . . 91 . 10 GLN HE22 H 6.792 . . 92 . 11 ALA N N 122.050 . . 93 . 11 ALA H H 7.893 . . 94 . 11 ALA CA C 54.722 . . 95 . 11 ALA HA H 3.957 . . 96 . 11 ALA HB H 1.112 . . 97 . 11 ALA CB C 18.135 . . 98 . 12 PHE N N 115.983 . . 99 . 12 PHE H H 8.089 . . 100 . 12 PHE CA C 59.549 . . 101 . 12 PHE HA H 4.031 . . 102 . 12 PHE CB C 38.345 . . 103 . 12 PHE HB2 H 3.108 . . 104 . 12 PHE HB3 H 2.876 . . 105 . 12 PHE HD1 H 6.870 . . 106 . 13 CYS N N 114.795 . . 107 . 13 CYS H H 7.779 . . 108 . 13 CYS CA C 57.303 . . 109 . 13 CYS HA H 4.378 . . 110 . 13 CYS CB C 38.761 . . 111 . 13 CYS HB3 H 3.205 . . 112 . 13 CYS HB2 H 3.007 . . 113 . 14 ASN N N 116.019 . . 114 . 14 ASN H H 8.005 . . 115 . 14 ASN CA C 53.900 . . 116 . 14 ASN HA H 4.612 . . 117 . 14 ASN CB C 39.105 . . 118 . 14 ASN HB2 H 2.819 . . 119 . 14 ASN HB3 H 2.693 . . 120 . 14 ASN ND2 N 111.631 . . 121 . 14 ASN HD21 H 7.521 . . 122 . 14 ASN HD22 H 6.913 . . 123 . 15 ALA N N 122.859 . . 124 . 15 ALA H H 7.411 . . 125 . 15 ALA CA C 52.047 . . 126 . 15 ALA HA H 4.214 . . 127 . 15 ALA HB H 1.465 . . 128 . 15 ALA CB C 20.516 . . 129 . 16 ASP N N 121.209 . . 130 . 16 ASP H H 7.900 . . 131 . 16 ASP CA C 55.791 . . 132 . 16 ASP HA H 4.614 . . 133 . 16 ASP HB2 H 3.028 . . 134 . 16 ASP HB3 H 2.866 . . 135 . 17 VAL N N 116.075 . . 136 . 17 VAL H H 7.881 . . 137 . 17 VAL CA C 59.991 . . 138 . 17 VAL HA H 4.733 . . 139 . 17 VAL CB C 35.626 . . 140 . 17 VAL HB H 1.860 . . 141 . 17 VAL HG1 H 1.094 . . 142 . 17 VAL HG2 H 0.999 . . 143 . 17 VAL CG1 C 23.480 . . 144 . 17 VAL CG2 C 21.638 . . 145 . 18 VAL N N 125.687 . . 146 . 18 VAL H H 8.963 . . 147 . 18 VAL CA C 62.134 . . 148 . 18 VAL HA H 5.234 . . 149 . 18 VAL CB C 34.102 . . 150 . 18 VAL HB H 1.920 . . 151 . 18 VAL HG1 H 0.803 . . 152 . 18 VAL HG2 H 0.710 . . 153 . 18 VAL CG1 C 21.724 . . 154 . 18 VAL CG2 C 20.752 . . 155 . 19 ILE N N 120.510 . . 156 . 19 ILE H H 9.293 . . 157 . 19 ILE CA C 59.143 . . 158 . 19 ILE HA H 5.403 . . 159 . 19 ILE CB C 43.547 . . 160 . 19 ILE HB H 1.674 . . 161 . 19 ILE HG2 H 0.915 . . 162 . 19 ILE CG2 C 18.076 . . 163 . 19 ILE CG1 C 23.212 . . 164 . 19 ILE HG13 H 1.463 . . 165 . 19 ILE HG12 H 0.965 . . 166 . 19 ILE HD1 H 0.682 . . 167 . 19 ILE CD1 C 14.308 . . 168 . 20 ARG N N 123.103 . . 169 . 20 ARG H H 8.853 . . 170 . 20 ARG CA C 54.145 . . 171 . 20 ARG HA H 5.685 . . 172 . 20 ARG CB C 44.798 . . 173 . 20 ARG HB2 H 1.536 . . 174 . 20 ARG HB3 H 1.377 . . 175 . 20 ARG HG2 H 1.504 . . 176 . 20 ARG HG3 H 0.789 . . 177 . 20 ARG NE N 108.320 . . 178 . 20 ARG HE H 5.525 . . 179 . 21 THR N N 123.058 . . 180 . 21 THR H H 9.524 . . 181 . 21 THR CA C 60.414 . . 182 . 21 THR HA H 5.028 . . 183 . 21 THR CB C 70.287 . . 184 . 21 THR HB H 3.683 . . 185 . 21 THR HG2 H 0.845 . . 186 . 21 THR CG2 C 18.437 . . 187 . 22 LYS N N 122.963 . . 188 . 22 LYS H H 7.890 . . 189 . 22 LYS CA C 81.826 . . 190 . 22 LYS HA H 4.922 . . 191 . 22 LYS CB C 36.256 . . 192 . 22 LYS HB2 H 1.602 . . 193 . 22 LYS HB3 H 1.602 . . 194 . 22 LYS CG C 24.177 . . 195 . 22 LYS HG2 H 1.237 . . 196 . 22 LYS HG3 H 1.237 . . 197 . 22 LYS CD C 29.681 . . 198 . 22 LYS HD2 H 1.558 . . 199 . 22 LYS HD3 H 1.558 . . 200 . 22 LYS CE C 41.771 . . 201 . 22 LYS HE2 H 2.758 . . 202 . 22 LYS HE3 H 2.758 . . 203 . 23 ALA N N 127.503 . . 204 . 23 ALA H H 9.908 . . 205 . 23 ALA CA C 51.415 . . 206 . 23 ALA HA H 4.765 . . 207 . 23 ALA HB H 1.129 . . 208 . 23 ALA CB C 20.167 . . 209 . 24 VAL N N 115.857 . . 210 . 24 VAL H H 8.953 . . 211 . 24 VAL CA C 62.417 . . 212 . 24 VAL HA H 4.325 . . 213 . 24 VAL CB C 33.268 . . 214 . 24 VAL HB H 2.056 . . 215 . 24 VAL HG1 H 0.799 . . 216 . 24 VAL HG2 H 0.663 . . 217 . 24 VAL CG1 C 21.239 . . 218 . 24 VAL CG2 C 19.099 . . 219 . 25 SER N N 113.235 . . 220 . 25 SER H H 7.844 . . 221 . 25 SER CA C 58.169 . . 222 . 25 SER HA H 4.629 . . 223 . 25 SER CB C 65.040 . . 224 . 25 SER HB2 H 3.945 . . 225 . 25 SER HB3 H 3.945 . . 226 . 26 GLU N N 121.113 . . 227 . 26 GLU H H 8.650 . . 228 . 26 GLU CA C 82.045 . . 229 . 26 GLU HA H 5.237 . . 230 . 26 GLU CB C 34.864 . . 231 . 26 GLU HB2 H 1.960 . . 232 . 26 GLU HB3 H 1.960 . . 233 . 26 GLU CG C 34.243 . . 234 . 26 GLU HG2 H 1.879 . . 235 . 26 GLU HG3 H 1.784 . . 236 . 27 LYS N N 121.755 . . 237 . 27 LYS H H 8.351 . . 238 . 27 LYS CA C 55.341 . . 239 . 27 LYS HA H 4.533 . . 240 . 27 LYS CB C 36.270 . . 241 . 27 LYS HB2 H 1.796 . . 242 . 27 LYS HB3 H 1.724 . . 243 . 27 LYS CG C 23.852 . . 244 . 27 LYS HG2 H 1.419 . . 245 . 27 LYS HG3 H 1.237 . . 246 . 27 LYS CD C 29.264 . . 247 . 27 LYS HD2 H 1.582 . . 248 . 27 LYS HD3 H 1.582 . . 249 . 27 LYS CE C 41.739 . . 250 . 27 LYS HE2 H 2.904 . . 251 . 27 LYS HE3 H 2.904 . . 252 . 28 GLU N N 123.388 . . 253 . 28 GLU H H 8.533 . . 254 . 28 GLU CA C 56.040 . . 255 . 28 GLU HA H 4.852 . . 256 . 28 GLU CB C 31.155 . . 257 . 28 GLU HB2 H 1.899 . . 258 . 28 GLU HB3 H 1.899 . . 259 . 28 GLU CG C 37.378 . . 260 . 28 GLU HG2 H 2.146 . . 261 . 28 GLU HG3 H 2.010 . . 262 . 29 VAL N N 120.088 . . 263 . 29 VAL H H 9.085 . . 264 . 29 VAL CA C 59.512 . . 265 . 29 VAL HA H 4.625 . . 266 . 29 VAL CB C 35.282 . . 267 . 29 VAL HB H 2.111 . . 268 . 29 VAL HG1 H 0.799 . . 269 . 29 VAL HG2 H 0.798 . . 270 . 29 VAL CG1 C 21.783 . . 271 . 29 VAL CG2 C 19.397 . . 272 . 30 ASP N N 122.629 . . 273 . 30 ASP H H 8.340 . . 274 . 30 ASP CA C 54.128 . . 275 . 30 ASP HA H 4.944 . . 276 . 30 ASP CB C 41.719 . . 277 . 30 ASP HB3 H 2.695 . . 278 . 30 ASP HB2 H 2.520 . . 279 . 31 SER N N 119.132 . . 280 . 31 SER H H 8.664 . . 281 . 31 SER CA C 56.710 . . 282 . 31 SER HA H 4.580 . . 283 . 31 SER CB C 63.980 . . 284 . 31 SER HB3 H 3.655 . . 285 . 31 SER HB2 H 3.377 . . 286 . 32 GLY N N 109.970 . . 287 . 32 GLY H H 8.032 . . 288 . 32 GLY CA C 44.117 . . 289 . 32 GLY HA2 H 4.154 . . 290 . 32 GLY HA3 H 3.668 . . 291 . 33 ASN N N 116.366 . . 292 . 33 ASN H H 8.204 . . 293 . 33 ASN CA C 51.692 . . 294 . 33 ASN HA H 5.445 . . 295 . 33 ASN CB C 41.771 . . 296 . 33 ASN HB2 H 2.449 . . 297 . 33 ASN HB3 H 2.285 . . 298 . 33 ASN ND2 N 111.092 . . 299 . 33 ASN HD21 H 7.116 . . 300 . 33 ASN HD22 H 6.614 . . 301 . 34 ASP N N 121.073 . . 302 . 34 ASP H H 8.943 . . 303 . 34 ASP CA C 52.396 . . 304 . 34 ASP HA H 4.573 . . 305 . 34 ASP CB C 41.184 . . 306 . 34 ASP HB3 H 3.348 . . 307 . 34 ASP HB2 H 2.627 . . 308 . 35 ILE N N 113.672 . . 309 . 35 ILE H H 7.738 . . 310 . 35 ILE CA C 63.402 . . 311 . 35 ILE HA H 3.901 . . 312 . 35 ILE CB C 38.073 . . 313 . 35 ILE HB H 1.649 . . 314 . 35 ILE HG2 H 0.533 . . 315 . 35 ILE CG2 C 16.664 . . 316 . 35 ILE CG1 C 26.317 . . 317 . 35 ILE HG12 H 0.826 . . 318 . 35 ILE HG13 H 0.528 . . 319 . 35 ILE HD1 H 0.611 . . 320 . 35 ILE CD1 C 13.639 . . 321 . 36 TYR N N 120.589 . . 322 . 36 TYR H H 7.826 . . 323 . 36 TYR CA C 57.158 . . 324 . 36 TYR HA H 4.556 . . 325 . 36 TYR CB C 37.918 . . 326 . 36 TYR HB2 H 3.313 . . 327 . 36 TYR HB3 H 2.882 . . 328 . 36 TYR HD1 H 7.073 . . 329 . 36 TYR HE1 H 6.786 . . 330 . 37 GLY N N 107.423 . . 331 . 37 GLY H H 8.070 . . 332 . 37 GLY CA C 44.792 . . 333 . 37 GLY HA3 H 4.252 . . 334 . 37 GLY HA2 H 3.510 . . 335 . 38 ASN N N 121.497 . . 336 . 38 ASN H H 8.608 . . 337 . 38 ASN CA C 51.180 . . 338 . 38 ASN HA H 5.023 . . 339 . 38 ASN CB C 38.120 . . 340 . 38 ASN HB2 H 2.927 . . 341 . 38 ASN HB3 H 2.628 . . 342 . 38 ASN ND2 N 117.505 . . 343 . 38 ASN HD21 H 8.495 . . 344 . 38 ASN HD22 H 7.053 . . 345 . 39 PRO CD C 50.563 . . 346 . 39 PRO CA C 63.171 . . 347 . 39 PRO HA H 4.776 . . 348 . 39 PRO CB C 32.220 . . 349 . 39 PRO HB2 H 2.262 . . 350 . 39 PRO HB3 H 1.716 . . 351 . 39 PRO CG C 27.434 . . 352 . 39 PRO HG3 H 3.667 . . 353 . 39 PRO HD2 H 3.948 . . 354 . 39 PRO HD3 H 3.700 . . 355 . 40 ILE N N 124.595 . . 356 . 40 ILE H H 8.513 . . 357 . 40 ILE CA C 60.536 . . 358 . 40 ILE HA H 4.158 . . 359 . 40 ILE CB C 38.951 . . 360 . 40 ILE HB H 1.530 . . 361 . 40 ILE HG2 H 0.761 . . 362 . 40 ILE CG2 C 17.340 . . 363 . 40 ILE CG1 C 27.134 . . 364 . 40 ILE HG13 H 1.409 . . 365 . 40 ILE HG12 H 0.921 . . 366 . 40 ILE HD1 H 0.624 . . 367 . 40 ILE CD1 C 13.112 . . 368 . 41 LYS N N 125.975 . . 369 . 41 LYS H H 8.211 . . 370 . 41 LYS CA C 82.045 . . 371 . 41 LYS HA H 5.089 . . 372 . 41 LYS CB C 34.321 . . 373 . 41 LYS HB2 H 1.713 . . 374 . 41 LYS HB3 H 1.661 . . 375 . 41 LYS CG C 24.705 . . 376 . 41 LYS HG2 H 1.347 . . 377 . 41 LYS HG3 H 1.347 . . 378 . 41 LYS CD C 28.533 . . 379 . 41 LYS HD2 H 1.468 . . 380 . 41 LYS HD3 H 1.468 . . 381 . 41 LYS CE C 41.778 . . 382 . 41 LYS HE3 H 2.886 . . 383 . 41 LYS HE2 H 2.837 . . 384 . 42 ARG N N 118.500 . . 385 . 42 ARG H H 8.725 . . 386 . 42 ARG CA C 54.799 . . 387 . 42 ARG HA H 4.651 . . 388 . 42 ARG CB C 35.422 . . 389 . 42 ARG HB2 H 1.668 . . 390 . 42 ARG HB3 H 1.630 . . 391 . 42 ARG CG C 27.077 . . 392 . 42 ARG HG2 H 1.608 . . 393 . 42 ARG HG3 H 1.608 . . 394 . 42 ARG CD C 44.166 . . 395 . 42 ARG HD2 H 2.960 . . 396 . 42 ARG HD3 H 2.960 . . 397 . 43 ILE N N 120.824 . . 398 . 43 ILE H H 8.800 . . 399 . 43 ILE CA C 59.446 . . 400 . 43 ILE HA H 4.373 . . 401 . 43 ILE CB C 37.055 . . 402 . 43 ILE HB H 1.586 . . 403 . 43 ILE HG2 H 0.150 . . 404 . 43 ILE CG2 C 16.445 . . 405 . 43 ILE CG1 C 27.375 . . 406 . 43 ILE HG12 H 1.319 . . 407 . 43 ILE HG13 H 1.053 . . 408 . 43 ILE HD1 H 0.683 . . 409 . 43 ILE CD1 C 10.308 . . 410 . 44 GLN N N 125.687 . . 411 . 44 GLN H H 8.998 . . 412 . 44 GLN CA C 53.721 . . 413 . 44 GLN HA H 4.385 . . 414 . 44 GLN CB C 34.187 . . 415 . 44 GLN HB2 H 1.987 . . 416 . 44 GLN HB3 H 1.987 . . 417 . 44 GLN CG C 35.291 . . 418 . 44 GLN HG2 H 1.705 . . 419 . 44 GLN HG3 H 1.280 . . 420 . 44 GLN NE2 N 111.943 . . 421 . 44 GLN HE21 H 7.314 . . 422 . 44 GLN HE22 H 6.667 . . 423 . 45 TYR N N 128.068 . . 424 . 45 TYR H H 9.776 . . 425 . 45 TYR CA C 56.872 . . 426 . 45 TYR HA H 5.455 . . 427 . 45 TYR CB C 38.928 . . 428 . 45 TYR HB2 H 2.740 . . 429 . 45 TYR HB3 H 2.570 . . 430 . 45 TYR HD1 H 6.799 . . 431 . 45 TYR HE1 H 6.631 . . 432 . 46 GLU N N 126.015 . . 433 . 46 GLU H H 8.167 . . 434 . 46 GLU CA C 56.130 . . 435 . 46 GLU HA H 4.631 . . 436 . 46 GLU CB C 30.374 . . 437 . 46 GLU HB3 H 2.029 . . 438 . 46 GLU HB2 H 1.980 . . 439 . 46 GLU HG2 H 2.270 . . 440 . 46 GLU HG3 H 2.270 . . 441 . 47 ILE N N 118.588 . . 442 . 47 ILE H H 7.687 . . 443 . 47 ILE CA C 58.799 . . 444 . 47 ILE HA H 5.148 . . 445 . 47 ILE CB C 40.700 . . 446 . 47 ILE HB H 1.949 . . 447 . 47 ILE HG2 H 0.514 . . 448 . 47 ILE CG2 C 17.668 . . 449 . 47 ILE CG1 C 25.598 . . 450 . 47 ILE HG12 H 0.929 . . 451 . 47 ILE HG13 H 0.426 . . 452 . 47 ILE HD1 H 0.418 . . 453 . 47 ILE CD1 C 14.378 . . 454 . 48 LYS N N 118.663 . . 455 . 48 LYS H H 8.314 . . 456 . 48 LYS CA C 53.934 . . 457 . 48 LYS HA H 4.517 . . 458 . 48 LYS CB C 33.221 . . 459 . 48 LYS HB2 H 1.613 . . 460 . 48 LYS HB3 H 1.211 . . 461 . 48 LYS CG C 24.248 . . 462 . 48 LYS HG2 H 1.156 . . 463 . 48 LYS CD C 28.279 . . 464 . 48 LYS HD2 H 1.583 . . 465 . 48 LYS HD3 H 1.583 . . 466 . 48 LYS CE C 41.868 . . 467 . 48 LYS HE2 H 2.859 . . 468 . 48 LYS HE3 H 2.859 . . 469 . 49 GLN N N 130.165 . . 470 . 49 GLN H H 9.261 . . 471 . 49 GLN CA C 56.874 . . 472 . 49 GLN HA H 3.887 . . 473 . 49 GLN HB2 H 1.942 . . 474 . 49 GLN HB3 H 1.713 . . 475 . 49 GLN CG C 13.427 . . 476 . 49 GLN HG2 H 1.719 . . 477 . 49 GLN HG3 H 1.611 . . 478 . 49 GLN NE2 N 110.756 . . 479 . 49 GLN HE22 H 7.189 . . 480 . 49 GLN HE21 H 6.543 . . 481 . 50 ILE N N 130.565 . . 482 . 50 ILE H H 8.587 . . 483 . 50 ILE CA C 62.707 . . 484 . 50 ILE HA H 3.839 . . 485 . 50 ILE CB C 38.268 . . 486 . 50 ILE HB H 0.994 . . 487 . 50 ILE HG2 H 0.543 . . 488 . 50 ILE CG2 C 15.954 . . 489 . 50 ILE CG1 C 27.524 . . 490 . 50 ILE HG12 H 1.416 . . 491 . 50 ILE HG13 H 1.017 . . 492 . 50 ILE HD1 H 0.533 . . 493 . 50 ILE CD1 C 12.484 . . 494 . 51 LYS N N 116.745 . . 495 . 51 LYS H H 7.303 . . 496 . 51 LYS CA C 55.706 . . 497 . 51 LYS HA H 4.115 . . 498 . 51 LYS CB C 36.084 . . 499 . 51 LYS HB3 H 1.487 . . 500 . 51 LYS HB2 H 0.983 . . 501 . 51 LYS CG C 24.785 . . 502 . 51 LYS HG2 H 0.535 . . 503 . 51 LYS HG3 H 0.421 . . 504 . 51 LYS CD C 28.336 . . 505 . 51 LYS HD2 H 1.404 . . 506 . 51 LYS HD3 H 1.404 . . 507 . 51 LYS CE C 42.017 . . 508 . 51 LYS HE2 H 2.768 . . 509 . 51 LYS HE3 H 2.633 . . 510 . 52 MET N N 126.787 . . 511 . 52 MET H H 8.779 . . 512 . 52 MET CA C 54.752 . . 513 . 52 MET HA H 4.636 . . 514 . 52 MET HB2 H 1.848 . . 515 . 52 MET HB3 H 1.848 . . 516 . 53 PHE N N 126.618 . . 517 . 53 PHE H H 8.664 . . 518 . 53 PHE CA C 59.339 . . 519 . 53 PHE HA H 4.484 . . 520 . 53 PHE CB C 39.859 . . 521 . 53 PHE HB3 H 3.378 . . 522 . 53 PHE HB2 H 2.444 . . 523 . 53 PHE HD1 H 7.038 . . 524 . 53 PHE HD2 H 7.038 . . 525 . 54 LYS N N 118.817 . . 526 . 54 LYS H H 7.700 . . 527 . 54 LYS CA C 56.089 . . 528 . 54 LYS HA H 4.479 . . 529 . 54 LYS CB C 36.309 . . 530 . 54 LYS HB2 H 1.470 . . 531 . 54 LYS HB3 H 1.409 . . 532 . 54 LYS HG2 H 1.828 . . 533 . 54 LYS HG3 H 1.204 . . 534 . 54 LYS HD2 H 1.343 . . 535 . 55 GLY N N 113.507 . . 536 . 55 GLY H H 8.445 . . 537 . 55 GLY CA C 45.785 . . 538 . 55 GLY HA2 H 5.058 . . 539 . 55 GLY HA3 H 4.210 . . 540 . 56 PRO CD C 49.948 . . 541 . 56 PRO CA C 62.001 . . 542 . 56 PRO HA H 4.635 . . 543 . 56 PRO CB C 33.064 . . 544 . 56 PRO HB3 H 2.312 . . 545 . 56 PRO HB2 H 2.249 . . 546 . 56 PRO CG C 26.120 . . 547 . 56 PRO HG3 H 2.106 . . 548 . 56 PRO HG2 H 2.086 . . 549 . 56 PRO HD2 H 3.456 . . 550 . 56 PRO HD3 H 3.456 . . 551 . 57 GLU N N 115.638 . . 552 . 57 GLU H H 8.146 . . 553 . 57 GLU CA C 58.084 . . 554 . 57 GLU HA H 3.994 . . 555 . 57 GLU CB C 29.324 . . 556 . 57 GLU HB2 H 2.045 . . 557 . 57 GLU HB3 H 1.953 . . 558 . 57 GLU CG C 36.498 . . 559 . 57 GLU HG2 H 2.297 . . 560 . 57 GLU HG3 H 2.250 . . 561 . 58 LYS N N 118.810 . . 562 . 58 LYS H H 7.260 . . 563 . 58 LYS CA C 55.323 . . 564 . 58 LYS HA H 4.334 . . 565 . 58 LYS CB C 32.752 . . 566 . 58 LYS HB3 H 1.746 . . 567 . 58 LYS HB2 H 1.659 . . 568 . 58 LYS CG C 24.936 . . 569 . 58 LYS HG2 H 1.387 . . 570 . 58 LYS HG3 H 1.387 . . 571 . 58 LYS HD3 H 2.915 . . 572 . 58 LYS CE C 42.091 . . 573 . 58 LYS HE2 H 2.997 . . 574 . 58 LYS HE3 H 2.912 . . 575 . 59 ASP N N 123.066 . . 576 . 59 ASP H H 8.017 . . 577 . 59 ASP CA C 54.447 . . 578 . 59 ASP HA H 4.325 . . 579 . 59 ASP CB C 40.789 . . 580 . 59 ASP HB3 H 2.313 . . 581 . 59 ASP HB2 H 2.251 . . 582 . 60 ILE N N 119.602 . . 583 . 60 ILE H H 8.304 . . 584 . 60 ILE CA C 59.104 . . 585 . 60 ILE HA H 3.555 . . 586 . 60 ILE CB C 34.712 . . 587 . 60 ILE HB H 1.965 . . 588 . 60 ILE HG2 H 0.693 . . 589 . 60 ILE CG2 C 18.570 . . 590 . 60 ILE CG1 C 26.641 . . 591 . 60 ILE HG12 H 1.778 . . 592 . 60 ILE HG13 H 1.287 . . 593 . 60 ILE HD1 H 0.625 . . 594 . 60 ILE CD1 C 30.209 . . 595 . 61 GLU N N 124.595 . . 596 . 61 GLU H H 8.824 . . 597 . 61 GLU CA C 56.676 . . 598 . 61 GLU HA H 4.127 . . 599 . 61 GLU CB C 33.533 . . 600 . 61 GLU HB2 H 1.660 . . 601 . 61 GLU HB3 H 1.509 . . 602 . 61 GLU CG C 36.576 . . 603 . 61 GLU HG2 H 2.000 . . 604 . 61 GLU HG3 H 1.814 . . 605 . 62 PHE N N 115.233 . . 606 . 62 PHE H H 7.742 . . 607 . 62 PHE CA C 55.831 . . 608 . 62 PHE HA H 5.629 . . 609 . 62 PHE CB C 45.215 . . 610 . 62 PHE HB2 H 2.606 . . 611 . 62 PHE HB3 H 2.544 . . 612 . 62 PHE HD1 H 7.009 . . 613 . 62 PHE HE1 H 7.222 . . 614 . 63 ILE N N 118.899 . . 615 . 63 ILE H H 8.741 . . 616 . 63 ILE CA C 59.883 . . 617 . 63 ILE HA H 4.696 . . 618 . 63 ILE CB C 41.218 . . 619 . 63 ILE HB H 1.456 . . 620 . 63 ILE HG2 H 0.807 . . 621 . 63 ILE CG2 C 18.321 . . 622 . 63 ILE HG12 H 1.498 . . 623 . 63 ILE HG13 H 0.919 . . 624 . 63 ILE HD1 H 0.614 . . 625 . 63 ILE CD1 C 14.967 . . 626 . 64 TYR N N 125.263 . . 627 . 64 TYR H H 9.171 . . 628 . 64 TYR CA C 56.178 . . 629 . 64 TYR HA H 5.943 . . 630 . 64 TYR CB C 42.611 . . 631 . 64 TYR HB3 H 2.874 . . 632 . 64 TYR HD1 H 6.969 . . 633 . 64 TYR HD2 H 6.969 . . 634 . 65 THR N N 113.672 . . 635 . 65 THR H H 8.858 . . 636 . 65 THR CA C 60.443 . . 637 . 65 THR HA H 4.792 . . 638 . 65 THR CB C 71.280 . . 639 . 65 THR HB H 4.139 . . 640 . 65 THR HG2 H 1.480 . . 641 . 66 ALA N N 127.328 . . 642 . 66 ALA H H 8.251 . . 643 . 66 ALA CA C 51.014 . . 644 . 66 ALA HA H 4.852 . . 645 . 66 ALA HB H 1.481 . . 646 . 66 ALA CB C 18.544 . . 647 . 67 PRO CD C 50.945 . . 648 . 67 PRO CA C 64.079 . . 649 . 67 PRO HA H 4.362 . . 650 . 67 PRO CB C 32.348 . . 651 . 67 PRO HB2 H 2.114 . . 652 . 67 PRO HB3 H 2.057 . . 653 . 67 PRO CG C 27.852 . . 654 . 67 PRO HG2 H 1.965 . . 655 . 67 PRO HG3 H 1.768 . . 656 . 67 PRO HD3 H 3.993 . . 657 . 67 PRO HD2 H 3.665 . . 658 . 68 SER CA C 57.428 . . 659 . 68 SER HA H 4.689 . . 660 . 68 SER CB C 65.109 . . 661 . 68 SER HB2 H 4.078 . . 662 . 68 SER HB3 H 3.786 . . 663 . 69 SER CA C 60.242 . . 664 . 69 SER HA H 4.487 . . 665 . 69 SER CB C 40.393 . . 666 . 69 SER HB2 H 3.996 . . 667 . 69 SER HB3 H 3.996 . . 668 . 70 ALA CA C 54.291 . . 669 . 70 ALA HA H 4.291 . . 670 . 70 ALA HB H 1.491 . . 671 . 70 ALA CB C 18.481 . . 672 . 71 VAL N N 109.303 . . 673 . 71 VAL H H 7.090 . . 674 . 71 VAL CA C 60.503 . . 675 . 71 VAL HA H 4.613 . . 676 . 71 VAL CB C 30.201 . . 677 . 71 VAL HB H 2.493 . . 678 . 71 VAL HG2 H 0.993 . . 679 . 71 VAL HG1 H 0.928 . . 680 . 71 VAL CG1 C 19.518 . . 681 . 71 VAL CG2 C 21.486 . . 682 . 72 CYS N N 111.706 . . 683 . 72 CYS H H 8.007 . . 684 . 72 CYS CA C 56.180 . . 685 . 72 CYS HA H 4.254 . . 686 . 72 CYS CB C 39.609 . . 687 . 72 CYS HB2 H 3.577 . . 688 . 72 CYS HB3 H 3.506 . . 689 . 73 GLY N N 109.988 . . 690 . 73 GLY H H 8.578 . . 691 . 73 GLY CA C 45.487 . . 692 . 73 GLY HA2 H 4.356 . . 693 . 73 GLY HA3 H 3.554 . . 694 . 74 VAL N N 118.806 . . 695 . 74 VAL H H 7.557 . . 696 . 74 VAL CA C 60.906 . . 697 . 74 VAL HA H 4.116 . . 698 . 74 VAL CB C 34.499 . . 699 . 74 VAL HB H 1.628 . . 700 . 74 VAL HG2 H 0.672 . . 701 . 74 VAL HG1 H 0.616 . . 702 . 74 VAL CG1 C 20.839 . . 703 . 74 VAL CG2 C 20.647 . . 704 . 75 SER N N 121.107 . . 705 . 75 SER H H 8.283 . . 706 . 75 SER CA C 56.778 . . 707 . 75 SER HA H 4.745 . . 708 . 75 SER CB C 63.721 . . 709 . 75 SER HB2 H 3.736 . . 710 . 75 SER HB3 H 3.692 . . 711 . 76 LEU N N 123.850 . . 712 . 76 LEU H H 7.332 . . 713 . 76 LEU CA C 52.416 . . 714 . 76 LEU HA H 4.154 . . 715 . 76 LEU CB C 42.652 . . 716 . 76 LEU HB3 H 0.528 . . 717 . 76 LEU HB2 H 0.435 . . 718 . 76 LEU CG C 25.943 . . 719 . 76 LEU HG H 0.590 . . 720 . 76 LEU CD1 C 24.045 . . 721 . 76 LEU CD2 C 20.608 . . 722 . 77 ASP N N 120.915 . . 723 . 77 ASP H H 8.147 . . 724 . 77 ASP CA C 54.299 . . 725 . 77 ASP HA H 4.577 . . 726 . 77 ASP CB C 41.463 . . 727 . 77 ASP HB2 H 2.818 . . 728 . 77 ASP HB3 H 2.595 . . 729 . 78 VAL N N 122.941 . . 730 . 78 VAL H H 8.184 . . 731 . 78 VAL CA C 61.788 . . 732 . 78 VAL HA H 4.297 . . 733 . 78 VAL CB C 32.027 . . 734 . 78 VAL HB H 2.064 . . 735 . 78 VAL HG1 H 0.933 . . 736 . 78 VAL HG2 H 0.814 . . 737 . 78 VAL CG1 C 20.675 . . 738 . 78 VAL CG2 C 21.566 . . 739 . 79 GLY N N 111.116 . . 740 . 79 GLY H H 8.612 . . 741 . 79 GLY CA C 46.221 . . 742 . 79 GLY HA2 H 4.058 . . 743 . 79 GLY HA3 H 3.920 . . 744 . 80 GLY N N 108.307 . . 745 . 80 GLY H H 8.439 . . 746 . 80 GLY CA C 45.243 . . 747 . 80 GLY HA2 H 3.971 . . 748 . 80 GLY HA3 H 3.887 . . 749 . 81 LYS N N 118.903 . . 750 . 81 LYS H H 8.170 . . 751 . 81 LYS CA C 56.157 . . 752 . 81 LYS HA H 4.309 . . 753 . 81 LYS CB C 32.172 . . 754 . 81 LYS HB2 H 1.780 . . 755 . 81 LYS HB3 H 1.780 . . 756 . 81 LYS CG C 24.802 . . 757 . 81 LYS HG2 H 1.361 . . 758 . 81 LYS HG3 H 1.361 . . 759 . 81 LYS CD C 28.907 . . 760 . 81 LYS HD2 H 1.719 . . 761 . 81 LYS HD3 H 1.635 . . 762 . 81 LYS CE C 41.955 . . 763 . 81 LYS HE2 H 3.003 . . 764 . 81 LYS HE3 H 3.003 . . 765 . 82 LYS N N 119.883 . . 766 . 82 LYS H H 7.672 . . 767 . 82 LYS CA C 56.542 . . 768 . 82 LYS HA H 4.117 . . 769 . 82 LYS CB C 33.478 . . 770 . 82 LYS HB2 H 1.661 . . 771 . 82 LYS HB3 H 1.583 . . 772 . 82 LYS CG C 24.440 . . 773 . 82 LYS HG2 H 1.202 . . 774 . 82 LYS HG3 H 1.041 . . 775 . 82 LYS HD2 H 1.673 . . 776 . 82 LYS HD3 H 1.673 . . 777 . 82 LYS CE C 41.371 . . 778 . 82 LYS HE2 H 2.873 . . 779 . 82 LYS HE3 H 2.873 . . 780 . 83 GLU N N 121.946 . . 781 . 83 GLU H H 8.185 . . 782 . 83 GLU CA C 82.045 . . 783 . 83 GLU HA H 4.917 . . 784 . 83 GLU CB C 32.585 . . 785 . 83 GLU HB2 H 1.884 . . 786 . 83 GLU HB3 H 1.595 . . 787 . 83 GLU CG C 36.588 . . 788 . 83 GLU HG2 H 2.210 . . 789 . 83 GLU HG3 H 2.210 . . 790 . 84 TYR N N 119.476 . . 791 . 84 TYR H H 9.454 . . 792 . 84 TYR CA C 57.793 . . 793 . 84 TYR HA H 5.182 . . 794 . 84 TYR CB C 43.708 . . 795 . 84 TYR HB2 H 2.767 . . 796 . 84 TYR HB3 H 2.284 . . 797 . 84 TYR HD1 H 6.700 . . 798 . 84 TYR HE1 H 6.748 . . 799 . 85 LEU N N 124.018 . . 800 . 85 LEU H H 9.484 . . 801 . 85 LEU CA C 54.263 . . 802 . 85 LEU HA H 5.353 . . 803 . 85 LEU CB C 44.118 . . 804 . 85 LEU HB2 H 2.257 . . 805 . 85 LEU HB3 H 2.257 . . 806 . 85 LEU CG C 44.193 . . 807 . 85 LEU HG H 1.624 . . 808 . 85 LEU HD2 H 1.001 . . 809 . 85 LEU HD1 H 1.001 . . 810 . 85 LEU CD1 C 27.037 . . 811 . 85 LEU CD2 C 24.502 . . 812 . 86 ILE N N 124.704 . . 813 . 86 ILE H H 9.104 . . 814 . 86 ILE CA C 60.743 . . 815 . 86 ILE HA H 4.878 . . 816 . 86 ILE CB C 41.704 . . 817 . 86 ILE HB H 1.497 . . 818 . 86 ILE HG2 H 0.725 . . 819 . 86 ILE CG2 C 18.025 . . 820 . 86 ILE CG1 C 28.168 . . 821 . 86 ILE HG12 H 1.506 . . 822 . 86 ILE HG13 H 0.977 . . 823 . 86 ILE HD1 H 0.362 . . 824 . 86 ILE CD1 C 13.366 . . 825 . 87 ALA N N 130.768 . . 826 . 87 ALA H H 8.643 . . 827 . 87 ALA CA C 49.003 . . 828 . 87 ALA HA H 5.844 . . 829 . 87 ALA HB H 1.506 . . 830 . 87 ALA CB C 22.298 . . 831 . 88 GLY N N 106.463 . . 832 . 88 GLY H H 8.509 . . 833 . 88 GLY CA C 45.775 . . 834 . 88 GLY HA3 H 4.597 . . 835 . 88 GLY HA2 H 3.706 . . 836 . 89 LYS N N 121.280 . . 837 . 89 LYS H H 8.028 . . 838 . 89 LYS CA C 54.728 . . 839 . 89 LYS HA H 4.908 . . 840 . 89 LYS CB C 34.772 . . 841 . 89 LYS HB2 H 1.893 . . 842 . 89 LYS HB3 H 1.782 . . 843 . 89 LYS CG C 24.517 . . 844 . 89 LYS HG2 H 1.605 . . 845 . 89 LYS CD C 28.787 . . 846 . 89 LYS HD2 H 1.785 . . 847 . 89 LYS CE C 41.980 . . 848 . 89 LYS HE2 H 3.084 . . 849 . 89 LYS HE3 H 3.084 . . 850 . 90 ALA N N 127.763 . . 851 . 90 ALA H H 10.111 . . 852 . 90 ALA CA C 52.289 . . 853 . 90 ALA HA H 4.490 . . 854 . 90 ALA HB H 1.479 . . 855 . 90 ALA CB C 19.638 . . 856 . 91 GLU N N 122.607 . . 857 . 91 GLU H H 8.125 . . 858 . 91 GLU CA C 54.777 . . 859 . 91 GLU HA H 4.597 . . 860 . 91 GLU CB C 31.327 . . 861 . 91 GLU HB2 H 1.942 . . 862 . 91 GLU HB3 H 1.765 . . 863 . 91 GLU CG C 36.902 . . 864 . 91 GLU HG2 H 2.111 . . 865 . 92 GLY N N 108.680 . . 866 . 92 GLY H H 7.874 . . 867 . 92 GLY CA C 44.135 . . 868 . 92 GLY HA2 H 4.219 . . 869 . 92 GLY HA3 H 3.836 . . 870 . 93 ASP N N 118.915 . . 871 . 93 ASP H H 8.448 . . 872 . 93 ASP CA C 55.481 . . 873 . 93 ASP HA H 4.362 . . 874 . 93 ASP CB C 40.470 . . 875 . 93 ASP HB2 H 2.605 . . 876 . 94 GLY N N 109.929 . . 877 . 94 GLY H H 9.327 . . 878 . 94 GLY CA C 45.924 . . 879 . 94 GLY HA2 H 4.338 . . 880 . 94 GLY HA3 H 4.338 . . 881 . 95 LYS N N 118.712 . . 882 . 95 LYS H H 7.892 . . 883 . 95 LYS CA C 55.599 . . 884 . 95 LYS HA H 5.786 . . 885 . 95 LYS CB C 36.993 . . 886 . 95 LYS HB2 H 1.915 . . 887 . 95 LYS HB3 H 1.842 . . 888 . 95 LYS CG C 29.315 . . 889 . 95 LYS HG2 H 1.729 . . 890 . 95 LYS HG3 H 1.729 . . 891 . 95 LYS CD C 29.315 . . 892 . 95 LYS HD2 H 1.595 . . 893 . 95 LYS HD3 H 1.595 . . 894 . 95 LYS CE C 41.987 . . 895 . 95 LYS HE2 H 2.973 . . 896 . 95 LYS HE3 H 2.973 . . 897 . 96 MET N N 119.352 . . 898 . 96 MET H H 8.417 . . 899 . 96 MET CA C 54.814 . . 900 . 96 MET HA H 5.324 . . 901 . 96 MET CB C 38.335 . . 902 . 96 MET HB2 H 2.122 . . 903 . 96 MET HB3 H 2.011 . . 904 . 96 MET CG C 31.755 . . 905 . 96 MET HG2 H 2.445 . . 906 . 96 MET HG3 H 2.304 . . 907 . 96 MET HE H 1.727 . . 908 . 97 HIS N N 120.335 . . 909 . 97 HIS H H 9.149 . . 910 . 97 HIS CA C 54.968 . . 911 . 97 HIS HA H 5.842 . . 912 . 97 HIS CB C 33.431 . . 913 . 97 HIS HB2 H 3.208 . . 914 . 97 HIS HB3 H 3.030 . . 915 . 97 HIS HD2 H 6.972 . . 916 . 98 ILE N N 114.874 . . 917 . 98 ILE H H 8.425 . . 918 . 98 ILE CA C 58.987 . . 919 . 98 ILE HA H 5.352 . . 920 . 98 ILE CB C 43.054 . . 921 . 98 ILE HB H 2.043 . . 922 . 98 ILE HG2 H 0.856 . . 923 . 98 ILE CG2 C 18.212 . . 924 . 98 ILE CG1 C 23.979 . . 925 . 98 ILE HG13 H 1.270 . . 926 . 98 ILE HG12 H 1.048 . . 927 . 98 ILE HD1 H 0.612 . . 928 . 98 ILE CD1 C 14.039 . . 929 . 99 THR N N 116.949 . . 930 . 99 THR H H 9.921 . . 931 . 99 THR CA C 59.850 . . 932 . 99 THR HA H 4.950 . . 933 . 99 THR CB C 73.853 . . 934 . 99 THR HB H 4.612 . . 935 . 99 THR HG2 H 1.276 . . 936 . 99 THR CG2 C 21.025 . . 937 . 100 LEU N N 118.190 . . 938 . 100 LEU H H 8.276 . . 939 . 100 LEU CA C 56.235 . . 940 . 100 LEU HA H 3.976 . . 941 . 100 LEU CB C 42.853 . . 942 . 100 LEU HB2 H 1.621 . . 943 . 100 LEU HB3 H 1.518 . . 944 . 100 LEU CG C 26.737 . . 945 . 100 LEU HG H 0.985 . . 946 . 100 LEU HD1 H 1.003 . . 947 . 100 LEU HD2 H 1.001 . . 948 . 100 LEU CD1 C 17.515 . . 949 . 100 LEU CD2 C 24.884 . . 950 . 101 CYS N N 114.209 . . 951 . 101 CYS H H 7.921 . . 952 . 101 CYS CA C 53.797 . . 953 . 101 CYS HA H 4.658 . . 954 . 101 CYS HB2 H 3.569 . . 955 . 101 CYS HB3 H 2.545 . . 956 . 102 ASP N N 121.349 . . 957 . 102 ASP H H 7.706 . . 958 . 102 ASP CA C 55.395 . . 959 . 102 ASP HA H 4.831 . . 960 . 102 ASP CB C 41.808 . . 961 . 102 ASP HB2 H 3.321 . . 962 . 102 ASP HB3 H 2.961 . . 963 . 103 PHE N N 120.885 . . 964 . 103 PHE H H 8.243 . . 965 . 103 PHE CA C 58.306 . . 966 . 103 PHE HA H 4.519 . . 967 . 103 PHE CB C 39.811 . . 968 . 103 PHE HB2 H 3.184 . . 969 . 103 PHE HB3 H 2.777 . . 970 . 104 ILE N N 128.436 . . 971 . 104 ILE H H 7.383 . . 972 . 104 ILE CA C 60.497 . . 973 . 104 ILE HA H 4.858 . . 974 . 104 ILE CB C 41.568 . . 975 . 104 ILE HB H 1.619 . . 976 . 104 ILE HG2 H 0.493 . . 977 . 104 ILE CG2 C 17.511 . . 978 . 104 ILE CG1 C 28.218 . . 979 . 104 ILE HG12 H 1.481 . . 980 . 104 ILE HG13 H 0.880 . . 981 . 104 ILE HD1 H 0.771 . . 982 . 104 ILE CD1 C 16.583 . . 983 . 105 VAL N N 122.120 . . 984 . 105 VAL H H 8.711 . . 985 . 105 VAL CA C 57.723 . . 986 . 105 VAL HA H 4.931 . . 987 . 105 VAL CB C 35.754 . . 988 . 105 VAL HB H 1.865 . . 989 . 105 VAL HG1 H 0.704 . . 990 . 105 VAL HG2 H 0.594 . . 991 . 105 VAL CG1 C 21.736 . . 992 . 105 VAL CG2 C 20.090 . . 993 . 106 PRO CD C 51.415 . . 994 . 106 PRO CA C 62.760 . . 995 . 106 PRO HA H 4.516 . . 996 . 106 PRO HB2 H 2.180 . . 997 . 106 PRO HB3 H 2.032 . . 998 . 106 PRO HG2 H 2.269 . . 999 . 106 PRO HG3 H 1.886 . . 1000 . 106 PRO HD2 H 4.061 . . 1001 . 106 PRO HD3 H 3.625 . . 1002 . 107 TRP N N 129.689 . . 1003 . 107 TRP H H 9.342 . . 1004 . 107 TRP CA C 59.950 . . 1005 . 107 TRP HA H 4.035 . . 1006 . 107 TRP CB C 30.815 . . 1007 . 107 TRP HB2 H 3.023 . . 1008 . 107 TRP HB3 H 2.847 . . 1009 . 107 TRP NE1 N 130.365 . . 1010 . 107 TRP HD1 H 7.150 . . 1011 . 107 TRP HE1 H 10.223 . . 1012 . 107 TRP HZ2 H 7.565 . . 1013 . 107 TRP HH2 H 7.206 . . 1014 . 108 ASP N N 112.497 . . 1015 . 108 ASP H H 8.619 . . 1016 . 108 ASP CA C 55.393 . . 1017 . 108 ASP HA H 4.294 . . 1018 . 108 ASP CB C 40.037 . . 1019 . 108 ASP HB2 H 2.691 . . 1020 . 108 ASP HB3 H 2.670 . . 1021 . 109 THR N N 108.757 . . 1022 . 109 THR H H 7.475 . . 1023 . 109 THR CA C 62.047 . . 1024 . 109 THR HA H 4.285 . . 1025 . 109 THR CB C 69.992 . . 1026 . 109 THR HB H 4.283 . . 1027 . 109 THR HG2 H 1.190 . . 1028 . 109 THR CG2 C 21.764 . . 1029 . 110 LEU N N 122.864 . . 1030 . 110 LEU H H 6.914 . . 1031 . 110 LEU CA C 54.488 . . 1032 . 110 LEU HA H 4.251 . . 1033 . 110 LEU CB C 43.070 . . 1034 . 110 LEU HB2 H 1.149 . . 1035 . 110 LEU HB3 H 0.960 . . 1036 . 110 LEU CG C 26.717 . . 1037 . 110 LEU HG H 1.433 . . 1038 . 110 LEU HD1 H 0.569 . . 1039 . 110 LEU HD2 H 0.288 . . 1040 . 110 LEU CD1 C 23.579 . . 1041 . 110 LEU CD2 C 26.722 . . 1042 . 111 SER N N 119.201 . . 1043 . 111 SER H H 8.865 . . 1044 . 111 SER CA C 60.420 . . 1045 . 111 SER HA H 4.453 . . 1046 . 111 SER CB C 62.513 . . 1047 . 111 SER HB2 H 4.366 . . 1048 . 111 SER HB3 H 3.992 . . 1049 . 112 THR N N 117.060 . . 1050 . 112 THR H H 8.901 . . 1051 . 112 THR CA C 66.755 . . 1052 . 112 THR HA H 3.739 . . 1053 . 112 THR CB C 68.376 . . 1054 . 112 THR HB H 4.165 . . 1055 . 112 THR HG2 H 1.243 . . 1056 . 112 THR CG2 C 22.120 . . 1057 . 113 THR N N 115.641 . . 1058 . 113 THR H H 7.961 . . 1059 . 113 THR CA C 66.510 . . 1060 . 113 THR HA H 3.839 . . 1061 . 113 THR CB C 68.374 . . 1062 . 113 THR HB H 3.986 . . 1063 . 113 THR HG2 H 1.178 . . 1064 . 113 THR CG2 C 21.710 . . 1065 . 114 GLN N N 122.963 . . 1066 . 114 GLN H H 7.719 . . 1067 . 114 GLN CA C 59.039 . . 1068 . 114 GLN HA H 3.923 . . 1069 . 114 GLN CB C 29.113 . . 1070 . 114 GLN HB2 H 2.239 . . 1071 . 114 GLN HB3 H 1.732 . . 1072 . 114 GLN CG C 34.658 . . 1073 . 114 GLN HG2 H 2.309 . . 1074 . 114 GLN NE2 N 110.942 . . 1075 . 114 GLN HE21 H 7.334 . . 1076 . 114 GLN HE22 H 6.811 . . 1077 . 115 LYS N N 118.260 . . 1078 . 115 LYS H H 8.126 . . 1079 . 115 LYS CA C 60.401 . . 1080 . 115 LYS HA H 3.534 . . 1081 . 115 LYS CB C 32.566 . . 1082 . 115 LYS HB2 H 1.708 . . 1083 . 115 LYS CG C 26.710 . . 1084 . 115 LYS HG2 H 1.102 . . 1085 . 115 LYS HG3 H 0.303 . . 1086 . 115 LYS CD C 29.972 . . 1087 . 115 LYS HD2 H 1.286 . . 1088 . 115 LYS CE C 41.522 . . 1089 . 115 LYS HE2 H 2.448 . . 1090 . 115 LYS HE3 H 1.875 . . 1091 . 116 LYS N N 118.255 . . 1092 . 116 LYS H H 7.902 . . 1093 . 116 LYS CA C 59.178 . . 1094 . 116 LYS HA H 4.055 . . 1095 . 116 LYS CB C 32.209 . . 1096 . 116 LYS HB2 H 1.852 . . 1097 . 116 LYS CG C 25.373 . . 1098 . 116 LYS HG2 H 1.657 . . 1099 . 116 LYS HG3 H 1.616 . . 1100 . 116 LYS CD C 25.314 . . 1101 . 116 LYS HD2 H 1.436 . . 1102 . 116 LYS HD3 H 1.436 . . 1103 . 116 LYS CE C 41.750 . . 1104 . 116 LYS HE2 H 2.910 . . 1105 . 116 LYS HE3 H 2.910 . . 1106 . 117 SER N N 114.765 . . 1107 . 117 SER H H 7.760 . . 1108 . 117 SER CA C 61.188 . . 1109 . 117 SER HA H 4.069 . . 1110 . 117 SER CB C 62.860 . . 1111 . 117 SER HB2 H 3.783 . . 1112 . 117 SER HB3 H 3.537 . . 1113 . 118 LEU N N 120.663 . . 1114 . 118 LEU H H 7.232 . . 1115 . 118 LEU CA C 56.880 . . 1116 . 118 LEU HA H 3.699 . . 1117 . 118 LEU CB C 41.543 . . 1118 . 118 LEU HB2 H 1.358 . . 1119 . 118 LEU HB3 H 0.631 . . 1120 . 118 LEU CG C 26.143 . . 1121 . 118 LEU HG H 1.488 . . 1122 . 118 LEU HD1 H 0.414 . . 1123 . 118 LEU HD2 H 0.303 . . 1124 . 118 LEU CD1 C 26.340 . . 1125 . 118 LEU CD2 C 22.912 . . 1126 . 119 ASN N N 113.747 . . 1127 . 119 ASN H H 7.452 . . 1128 . 119 ASN CA C 54.556 . . 1129 . 119 ASN HA H 4.706 . . 1130 . 119 ASN CB C 39.158 . . 1131 . 119 ASN HB2 H 2.782 . . 1132 . 119 ASN HB3 H 2.782 . . 1133 . 119 ASN ND2 N 113.345 . . 1134 . 119 ASN HD21 H 7.554 . . 1135 . 119 ASN HD22 H 6.932 . . 1136 . 120 HIS N N 117.204 . . 1137 . 120 HIS H H 7.792 . . 1138 . 120 HIS CA C 56.524 . . 1139 . 120 HIS HA H 4.719 . . 1140 . 120 HIS CB C 30.628 . . 1141 . 120 HIS HB2 H 3.117 . . 1142 . 120 HIS HB3 H 3.053 . . 1143 . 121 ARG N N 120.885 . . 1144 . 121 ARG H H 8.240 . . 1145 . 121 ARG CA C 58.078 . . 1146 . 121 ARG HA H 4.066 . . 1147 . 121 ARG CB C 29.754 . . 1148 . 121 ARG HB2 H 1.818 . . 1149 . 121 ARG HB3 H 1.731 . . 1150 . 121 ARG CG C 27.119 . . 1151 . 121 ARG HG2 H 1.526 . . 1152 . 121 ARG HG3 H 1.526 . . 1153 . 121 ARG CD C 43.101 . . 1154 . 121 ARG HD2 H 3.149 . . 1155 . 121 ARG HD3 H 3.149 . . 1156 . 122 TYR N N 118.815 . . 1157 . 122 TYR H H 8.194 . . 1158 . 122 TYR CA C 58.423 . . 1159 . 122 TYR HA H 4.532 . . 1160 . 122 TYR CB C 37.203 . . 1161 . 122 TYR HB2 H 2.856 . . 1162 . 122 TYR HB3 H 2.728 . . 1163 . 123 GLN N N 119.825 . . 1164 . 123 GLN H H 8.115 . . 1165 . 123 GLN CA C 56.844 . . 1166 . 123 GLN HA H 4.193 . . 1167 . 123 GLN CB C 28.262 . . 1168 . 123 GLN HB2 H 2.101 . . 1169 . 123 GLN HB3 H 2.029 . . 1170 . 123 GLN CG C 33.765 . . 1171 . 123 GLN HG2 H 2.273 . . 1172 . 123 GLN HG3 H 2.200 . . 1173 . 123 GLN NE2 N 111.212 . . 1174 . 123 GLN HE21 H 7.361 . . 1175 . 123 GLN HE22 H 6.762 . . 1176 . 124 MET N N 117.386 . . 1177 . 124 MET H H 7.808 . . 1178 . 124 MET CA C 55.913 . . 1179 . 124 MET HA H 4.375 . . 1180 . 124 MET CB C 32.407 . . 1181 . 124 MET HB2 H 2.060 . . 1182 . 124 MET HB3 H 1.998 . . 1183 . 124 MET CG C 32.103 . . 1184 . 124 MET HG2 H 2.439 . . 1185 . 124 MET HG3 H 2.349 . . 1186 . 125 GLY N N 107.556 . . 1187 . 125 GLY H H 8.042 . . 1188 . 126 CYS N N 118.211 . . 1189 . 126 CYS H H 8.040 . . 1190 . 126 CYS CA C 54.688 . . 1191 . 126 CYS HA H 4.727 . . 1192 . 126 CYS CB C 40.028 . . 1193 . 126 CYS HB2 H 3.377 . . 1194 . 126 CYS HB3 H 2.968 . . 1195 . 127 GLU N N 126.452 . . 1196 . 127 GLU H H 8.016 . . 1197 . 127 GLU CA C 58.193 . . 1198 . 127 GLU HA H 4.114 . . 1199 . 127 GLU CB C 31.068 . . 1200 . 127 GLU HB2 H 2.038 . . 1201 . 127 GLU HB3 H 1.885 . . 1202 . 127 GLU CG C 36.657 . . 1203 . 127 GLU HG2 H 2.205 . . 1204 . 127 GLU HG3 H 2.205 . . stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants_set_1 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name 'N-TIMP-2 monomer' _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 3 CYS HA 3 CYS H 5.10 . . 2.00 2 3JHNHA 4 SER HA 4 SER H 4.00 . . 0.50 3 3JHNHA 6 VAL HA 6 VAL H 8.76 . . 0.27 4 3JHNHA 7 HIS HA 7 HIS H 7.20 . . 0.50 5 3JHNHA 9 GLN HA 9 GLN H 4.10 . . 2.00 6 3JHNHA 10 GLN HA 10 GLN H 7.08 . . 0.55 7 3JHNHA 11 ALA HA 11 ALA H 8.83 . . 0.40 8 3JHNHA 12 PHE HA 12 PHE H 4.62 . . 0.59 9 3JHNHA 14 ASN HA 14 ASN H 6.60 . . 0.50 10 3JHNHA 14 ASN HB2 14 ASN H -6.00 . . 1.00 11 3JHNHA 14 ASN HB3 14 ASN H -1.00 . . 1.00 12 3JHNHA 15 ALA HA 15 ALA H 5.10 . . 0.50 13 3JHNHA 16 ASP HA 16 ASP H 6.18 . . 0.41 14 3JHNHA 16 ASP HB2 16 ASP H -1.00 . . 1.00 15 3JHNHA 16 ASP HB3 16 ASP H -6.00 . . 1.00 16 3JHNHA 17 VAL HA 17 VAL H 11.80 . . 2.00 17 3JHNHA 18 VAL HA 18 VAL H 8.52 . . 0.14 18 3JHNHA 19 ILE HA 19 ILE H 9.90 . . 0.50 19 3JHNHA 20 ARG HA 20 ARG H 10.90 . . 0.50 20 3JHNHA 21 THR HA 21 THR H 9.50 . . 0.50 21 3JHNHA 23 ALA HA 23 ALA H 9.10 . . 0.50 22 3JHNHA 24 VAL HA 24 VAL H 7.79 . . 0.16 23 3JHNHA 25 SER HA 25 SER H 6.3 . . 2.00 24 3JHNHA 26 GLU HA 26 GLU H 8.35 . . 0.25 25 3JHNHA 27 LYS HA 27 LYS H 8.21 . . 0.29 26 3JHNHA 28 GLU HA 28 GLU H 7.50 . . 0.50 27 3JHNHA 29 VAL HA 29 VAL H 8.70 . . 0.19 28 3JHNHA 30 ASP HA 30 ASP H 7.35 . . 0.22 29 3JHNHA 30 ASP HB2 30 ASP H -6.00 . . 1.00 30 3JHNHA 30 ASP HB3 30 ASP H -1.00 . . 1.00 31 3JHNHA 31 SER HA 31 SER H 9.10 . . 0.50 32 3JHNHA 33 ASN HA 33 ASN H 8.37 . . 0.17 33 3JHNHA 33 ASN HB2 33 ASN H -1.00 . . 1.00 34 3JHNHA 33 ASN HB3 33 ASN H -6.00 . . 1.00 35 3JHNHA 34 ASP HA 34 ASP H 8.30 . . 0.50 36 3JHNHA 34 ASP HB2 34 ASP H -6.00 . . 1.00 37 3JHNHA 34 ASP HB3 34 ASP H -1.00 . . 1.00 38 3JHNHA 35 ILE HA 35 ILE H 2.30 . . 0.50 39 3JHNHA 36 TYR HA 36 TYR H 8.84 . . 0.18 40 3JHNHA 36 TYR HB2 36 TYR H -6.00 . . 1.00 41 3JHNHA 36 TYR HB3 36 TYR H -1.00 . . 1.00 42 3JHNHA 38 ASN HA 38 ASN H 7.29 . . 0.17 43 3JHNHA 40 ILE HA 40 ILE H 9.80 . . 0.50 44 3JHNHA 41 LYS HA 41 LYS H 7.39 . . 0.10 45 3JHNHA 41 LYS HB2 41 LYS H -1.00 . . 1.00 46 3JHNHA 41 LYS HB3 41 LYS H -6.00 . . 1.00 47 3JHNHA 42 ARG HA 42 ARG H 7.97 . . 0.42 48 3JHNHA 42 ARG HB2 42 ARG H -6.00 . . 1.00 49 3JHNHA 42 ARG HB3 42 ARG H -1.00 . . 1.00 50 3JHNHA 43 ILE HA 43 ILE H 10.40 . . 0.50 51 3JHNHA 44 GLN HA 44 GLN H 7.79 . . 0.10 52 3JHNHA 45 TYR HA 45 TYR H 10.60 . . 0.50 53 3JHNHA 45 TYR HB2 45 TYR H -1.00 . . 1.00 54 3JHNHA 45 TYR HB3 45 TYR H -6.00 . . 1.00 55 3JHNHA 46 GLU HA 46 GLU H 7.18 . . 0.10 56 3JHNHA 46 GLU HB2 46 GLU H -6.00 . . 1.00 57 3JHNHA 46 GLU HB3 46 GLU H -1.00 . . 1.00 58 3JHNHA 47 ILE HA 47 ILE H 10.22 . . 0.39 59 3JHNHA 48 LYS HA 48 LYS H 9.30 . . 0.49 60 3JHNHA 48 LYS HB2 48 LYS H -6.00 . . 1.00 61 3JHNHA 48 LYS HB3 48 LYS H -1.00 . . 1.00 62 3JHNHA 49 GLN HA 49 GLN H 6.58 . . 0.56 63 3JHNHA 50 ILE HA 50 ILE H 6.50 . . 0.50 64 3JHNHA 51 LYS HA 51 LYS H 7.20 . . 0.50 65 3JHNHA 52 MET HA 52 MET H 9.40 . . 0.50 66 3JHNHA 53 PHE HA 53 PHE H 11.20 . . 0.50 67 3JHNHA 53 PHE HB2 53 PHE H -6.00 . . 1.00 68 3JHNHA 53 PHE HB3 53 PHE H -1.00 . . 1.00 69 3JHNHA 54 LYS HA 54 LYS H 7.50 . . 0.37 70 3JHNHA 54 LYS HB2 54 LYS H -6.00 . . 1.00 71 3JHNHA 54 LYS HB3 54 LYS H -1.00 . . 1.00 72 3JHNHA 57 GLU HA 57 GLU H 5.94 . . 0.24 73 3JHNHA 58 LYS HA 58 LYS H 7.30 . . 0.50 74 3JHNHA 58 LYS HB2 58 LYS H -6.00 . . 1.00 75 3JHNHA 58 LYS HB3 58 LYS H -1.00 . . 1.00 76 3JHNHA 59 ASP HA 59 ASP H 2.50 . . 0.50 77 3JHNHA 60 ILE HA 60 ILE H 6.00 . . 0.50 78 3JHNHA 61 GLU HA 61 GLU H 12.20 . . 0.50 79 3JHNHA 61 GLU HB2 61 GLU H -1.00 . . 1.00 80 3JHNHA 61 GLU HB3 61 GLU H -6.00 . . 1.00 81 3JHNHA 62 PHE HA 62 PHE H 2.70 . . 2.00 82 3JHNHA 62 PHE HB2 62 PHE H -1.00 . . 1.00 83 3JHNHA 62 PHE HB3 62 PHE H -6.00 . . 1.00 84 3JHNHA 63 ILE HA 63 ILE H 8.59 . . 0.38 85 3JHNHA 64 TYR HA 64 TYR H 10.31 . . 0.64 86 3JHNHA 65 THR HA 65 THR H 7.50 . . 0.50 87 3JHNHA 66 ALA HA 66 ALA H 5.40 . . 0.70 88 3JHNHA 71 VAL HA 71 VAL H 13.50 . . 0.50 89 3JHNHA 72 CYS HA 72 CYS H 12.00 . . 0.50 90 3JHNHA 74 VAL HA 74 VAL H 10.30 . . 0.50 91 3JHNHA 75 SER HA 75 SER H 6.71 . . 0.87 92 3JHNHA 76 LEU HA 76 LEU H 10.00 . . 0.50 93 3JHNHA 76 LEU HB2 76 LEU H -6.00 . . 1.00 94 3JHNHA 76 LEU HB3 76 LEU H -1.00 . . 1.00 95 3JHNHA 77 ASP HA 77 ASP H 8.80 . . 0.27 96 3JHNHA 77 ASP HB2 77 ASP H -6.00 . . 1.00 97 3JHNHA 77 ASP HB3 77 ASP H -1.00 . . 1.00 98 3JHNHA 78 VAL HA 78 VAL H 7.20 . . 0.50 99 3JHNHA 81 LYS HA 81 LYS H 7.17 . . 0.35 100 3JHNHA 82 LYS HA 82 LYS H 4.90 . . 0.50 101 3JHNHA 82 LYS HB2 82 LYS H -1.00 . . 1.00 102 3JHNHA 82 LYS HB3 82 LYS H -6.00 . . 1.00 103 3JHNHA 83 GLU HA 83 GLU H 8.19 . . 0.26 104 3JHNHA 84 TYR HA 84 TYR H 11.00 . . 0.50 105 3JHNHA 84 TYR HB2 84 TYR H -1.00 . . 1.00 106 3JHNHA 84 TYR HB3 84 TYR H -6.00 . . 1.00 107 3JHNHA 85 LEU HA 85 LEU H 9.90 . . 0.50 108 3JHNHA 86 ILE HA 86 ILE H 10.60 . . 0.50 109 3JHNHA 87 ALA HA 87 ALA H 9.88 . . 0.69 110 3JHNHA 90 ALA HA 90 ALA H 6.70 . . 0.50 111 3JHNHA 91 GLU HA 91 GLU H 7.98 . . 0.29 112 3JHNHA 91 GLU HB2 91 GLU H -6.00 . . 1.00 113 3JHNHA 91 GLU HB3 91 GLU H -1.00 . . 1.00 114 3JHNHA 93 ASP HA 93 ASP H 5.91 . . 0.30 115 3JHNHA 95 LYS HA 95 LYS H 9.17 . . 0.30 116 3JHNHA 95 LYS HB2 95 LYS H -1.00 . . 1.00 117 3JHNHA 95 LYS HB3 95 LYS H -6.00 . . 1.00 118 3JHNHA 96 MET HA 96 MET H 8.04 . . 0.54 119 3JHNHA 96 MET HB2 96 MET H -1.00 . . 1.00 120 3JHNHA 96 MET HB3 96 MET H -6.00 . . 1.00 121 3JHNHA 97 HIS HA 97 HIS H 8.70 . . 0.20 122 3JHNHA 97 HIS HB2 97 HIS H -6.00 . . 1.00 123 3JHNHA 97 HIS HB3 97 HIS H -1.00 . . 1.00 124 3JHNHA 98 ILE HA 98 ILE H 10.90 . . 0.50 125 3JHNHA 99 THR HA 99 THR H 11.60 . . 0.50 126 3JHNHA 100 LEU HA 100 LEU H 6.03 . . 0.37 127 3JHNHA 101 CYS HA 101 CYS H 8.02 . . 0.53 128 3JHNHA 101 CYS HB2 101 CYS H -6.00 . . 1.00 129 3JHNHA 101 CYS HB3 101 CYS H -1.00 . . 1.00 130 3JHNHA 102 ASP HA 102 ASP H 7.70 . . 0.50 131 3JHNHA 102 ASP HB2 102 ASP H -6.00 . . 1.00 132 3JHNHA 102 ASP HB3 102 ASP H -1.00 . . 1.00 133 3JHNHA 103 PHE HA 103 PHE H 7.35 . . 0.65 134 3JHNHA 104 ILE HA 104 ILE H 10.00 . . 0.50 135 3JHNHA 105 VAL HA 105 VAL H 9.10 . . 0.50 136 3JHNHA 107 TRP HA 107 TRP H 2.30 . . 0.50 137 3JHNHA 108 ASP HA 108 ASP H 4.10 . . 0.50 138 3JHNHA 109 THR HA 109 THR H 9.90 . . 0.50 139 3JHNHA 110 LEU HA 110 LEU H 5.50 . . 0.50 140 3JHNHA 110 LEU HB2 110 LEU H -1.00 . . 1.00 141 3JHNHA 110 LEU HB3 110 LEU H -6.00 . . 1.00 142 3JHNHA 111 SER HA 111 SER H 6.00 . . 0.50 143 3JHNHA 112 THR HA 112 THR H 2.70 . . 0.50 144 3JHNHA 113 THR HA 113 THR H 4.36 . . 1.25 145 3JHNHA 114 GLN HA 114 GLN H 5.10 . . 0.50 146 3JHNHA 114 GLN HB2 114 GLN H -1.00 . . 1.00 147 3JHNHA 114 GLN HB3 114 GLN H -6.00 . . 1.00 148 3JHNHA 115 LYS HA 115 LYS H 6.04 . . 0.43 149 3JHNHA 116 LYS HA 116 LYS H 6.02 . . 0.29 150 3JHNHA 118 LEU HA 118 LEU H 3.40 . . 0.50 151 3JHNHA 118 LEU HB2 118 LEU H -1.00 . . 1.00 152 3JHNHA 118 LEU HB3 118 LEU H -6.00 . . 1.00 153 3JHNHA 119 ASN HA 119 ASN H 6.82 . . 0.32 154 3JHNHA 120 HIS HA 120 HIS H 4.50 . . 2.10 155 3JHNHA 121 ARG HA 121 ARG H 4.30 . . 2.00 156 3JHNHA 121 ARG HB2 121 ARG H -6.00 . . 1.00 157 3JHNHA 121 ARG HB3 121 ARG H -1.00 . . 1.00 158 3JHNHA 122 TYR HA 122 TYR H 7.13 . . 0.34 159 3JHNHA 123 GLN HA 123 GLN H 6.58 . . 0.48 160 3JHNHA 124 MET HA 124 MET H 4.00 . . 0.50 161 3JHNHA 126 CYS HA 126 CYS H 7.70 . . 0.50 162 3JHNHA 126 CYS HB2 126 CYS H -6.00 . . 1.00 163 3JHNHA 126 CYS HB3 126 CYS H -1.00 . . 1.00 164 3JHNHA 127 GLU HA 127 GLU H 7.50 . . 0.50 stop_ save_