data_4374 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Mutational and structural analyses of the ribonucleotide reductase inhibitor sml1 define its rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethality ; _BMRB_accession_number 4374 _BMRB_flat_file_name bmr4374.str _Entry_type original _Submission_date 1999-08-05 _Accession_date 1999-08-05 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'NMR spectroscopy using uniformly U-[15N] and U-[15N,13C] labeled samples' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zao X. . . 2 Goergieva B. . . 3 Chabes Andrej A. . 4 Domkin Vladimir V. . 5 Ippel Hans J.H. . 6 Schleucher Juergen J. . 7 Wijmenga Sybren S.S. . 8 Thelander Lars L. . 9 Rothstein R. . . 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" 555 "13C chemical shifts" 389 "15N chemical shifts" 96 "coupling constants" 97 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-04-08 original author . stop_ _Original_release_date 2002-04-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Mutational and structural analyses of the ribonucleotide reductase inhibitor sml1 define its rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethality' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zao X. . . 2 Goergieva B. . . 3 Chabes Andrej A. . 4 Domkin Vladimir V. . 5 Ippel Hans J.H. . 6 Schleucher Juergen J. . 7 Wijmenga Sybren S.S. . 8 Thelander Lars L. . 9 Rothstein R. . . stop_ _Journal_abbreviation 'Mol. Cell. Biol.' _Journal_volume 20 _Journal_issue 23 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 9076 _Page_last 9083 _Year 2000 _Details . loop_ _Keyword 'carbon chemical shift' 'inhibitory complex' 'large subunit, RNR1' 'nitrogen chemical shift' 'NMR assignment' 'NMR spectroscopy' 'proton chemical shift' 'ribonucleotide reductase' 'Sml1 protein' structure stop_ save_ ################################## # Molecular system description # ################################## save_system_Sml1 _Saveframe_category molecular_system _Mol_system_name 'Sml1 protein' _Abbreviation_common Sml1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Sml1 protein' $Sml1 stop_ _System_molecular_weight 11834 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details ; Sml1 consists of 104 amino acids and binds specifically to the large R1 subunit of yeast and mouse ribonucleotide reductase, and thereby inhibit complex formation between the large R1 and small R2 subunit of ribonucleotide-diphosphate reductase ; save_ ######################## # Monomeric polymers # ######################## save_Sml1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Sml1 _Molecular_mass 11834.19 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 104 _Mol_residue_sequence ; MQNSQDYFYAQNRCQQQQAP STLRTVTMAEFRRVPLPPMA EVPMLSTQNSMGSSASASAS SLEMWEKDLEERLNSIDHDM NNNKFGSGELKSMFNQGKVE EMDF ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLN 3 ASN 4 SER 5 GLN 6 ASP 7 TYR 8 PHE 9 TYR 10 ALA 11 GLN 12 ASN 13 ARG 14 CYS 15 GLN 16 GLN 17 GLN 18 GLN 19 ALA 20 PRO 21 SER 22 THR 23 LEU 24 ARG 25 THR 26 VAL 27 THR 28 MET 29 ALA 30 GLU 31 PHE 32 ARG 33 ARG 34 VAL 35 PRO 36 LEU 37 PRO 38 PRO 39 MET 40 ALA 41 GLU 42 VAL 43 PRO 44 MET 45 LEU 46 SER 47 THR 48 GLN 49 ASN 50 SER 51 MET 52 GLY 53 SER 54 SER 55 ALA 56 SER 57 ALA 58 SER 59 ALA 60 SER 61 SER 62 LEU 63 GLU 64 MET 65 TRP 66 GLU 67 LYS 68 ASP 69 LEU 70 GLU 71 GLU 72 ARG 73 LEU 74 ASN 75 SER 76 ILE 77 ASP 78 HIS 79 ASP 80 MET 81 ASN 82 ASN 83 ASN 84 LYS 85 PHE 86 GLY 87 SER 88 GLY 89 GLU 90 LEU 91 LYS 92 SER 93 MET 94 PHE 95 ASN 96 GLN 97 GLY 98 LYS 99 VAL 100 GLU 101 GLU 102 MET 103 ASP 104 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 DBJ GAA25391 "K7_Sml1p [Saccharomyces cerevisiae Kyokai no. 7]" 100.00 104 98.08 98.08 2.24e-67 EMBL CAA86717 "unknown [Saccharomyces cerevisiae]" 100.00 104 100.00 100.00 4.04e-70 EMBL CAY81764 "Sml1p [Saccharomyces cerevisiae EC1118]" 100.00 104 100.00 100.00 4.04e-70 GB AAS56287 "YML058W [Saccharomyces cerevisiae]" 100.00 104 100.00 100.00 4.04e-70 GB AHY76409 "Sml1p [Saccharomyces cerevisiae YJM993]" 100.00 104 100.00 100.00 4.04e-70 GB AJP40654 "Sml1p [Saccharomyces cerevisiae YJM1078]" 100.00 104 100.00 100.00 4.04e-70 GB AJS61834 "Sml1p [Saccharomyces cerevisiae YJM189]" 100.00 104 100.00 100.00 4.04e-70 GB AJS62260 "Sml1p [Saccharomyces cerevisiae YJM193]" 100.00 104 100.00 100.00 4.04e-70 REF NP_013653 "ribonucleotide reductase inhibiting protein SML1 [Saccharomyces cerevisiae S288c]" 100.00 104 100.00 100.00 4.04e-70 SP Q04964 "RecName: Full=Ribonucleotide reductase inhibitor protein SML1" 100.00 104 100.00 100.00 4.04e-70 TPG DAA09840 "TPA: ribonucleotide reductase inhibiting protein SML1 [Saccharomyces cerevisiae S288c]" 100.00 104 100.00 100.00 4.04e-70 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic $Sml1 yeast 4932 Eukaryota . . . cerevisiae pET3a 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 $Sml1 'recombinant technology' yeast . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details 'Sml1 protein in 90% H2O / 10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Sml1 0.6 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details 'Sml1 protein in 90% H2O / 10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Sml1 0.4 mM [U-15N] H2O 90 % . D2O 10 % . 'sodium-phosphate buffer' 25 mM . NaCl 25 mM . Dithio-threitol 10 mM . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details 'Sml1 protein in 90% H2O / 10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Sml1 0.6 mM '[U-13C; U-15N]' H2O 90 % . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details ; Typical sample conditions, as used for the [U-15N] sample of Sml1: 25 mM sodium-phosphate buffer (pH 6.9) 25 mM NaCl 10 mM Dithio-threitol (DTT) in 90% H2O / 10% D2O mixture Temperature range used for NMR studies is 2 to 23 degrees Celsius. Triple-resonance and 15N-edited NOESY 3D spectra, dedicated to assignment of resonances, were recorded at a temperature of 2 degrees Celsius. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 50 . mM pH 6.9 0.2 pH pressure 1 . bar temperature 275 2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details ; Proton chemical shifts referenced directly to external DSS (concentration 10 mM) in D2O. Carbon and nitrogen chemical shifts are indirectly referenced to 0 ppm proton, based on the method by Wishart et al. Reference: Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D., "1H, 13C and 15N Chemical Shift Referencing in Biomolecular NMR," J. Biomol. NMR 6, 135-140 (1995). Note that the given indirectly referenced 13C and 15N chemical shifts are not corrected for temperature and pH, as recommended by the IUPAC-IUBMB-IUPAB Task Group. ; loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.000 external indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.000 external direct . 'external to the sample' . . $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.000 external indirect . . . 0.101329118 $entry_citation $entry_citation 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_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details ; # about the data. 1H, 13C, and 15N chemical shift assignments for the Sml1 protein. NMR experiments used for assignments (all recorded at 600 MHz, except stated otherwise): - triple resonance 3D spectra: HNCO, CTSL-HCANH (500 MHz), HNHA, CBCANH and CBCACONH - heteronuclear 2D spectra: 15N-1H HSQC and 13C-1H HSQC (500 MHz) - homonuclear spectra: 2D 1H-1H TOCSY (400 MHz) and 3D 15N-edited NOESY Backbone assigments (C,CA,CB,N,NH,HA) are virtually complete, except for residues Met1, Gln2, Tyr7, Tyr9, and Arg13 and residues followed by a proline. Sidechain assignments follow from a 3D 15N-edited NOESY spectrum and are mostly complete, except for proline resonances and amino protons of Asn and Gln residues. In the case of Met1 and Gln2, the increased solvent exchange prevent detection of their respective amide protons, and in doing so also preclude assignment of other resonances belonging to these residues. The one remaining cross peak in the 2D 15N-1H HSQC is ambiguously assigned to Arg13. Particularly resonances of Arg13, but also most resonances positioned between residue Asp6 and Arg13 are broad and have weak or missing cross peaks in the triple resonance spectra. The severe loss in peak intensity is probably caused by strong relaxation effects of resonances positioned in this part of the sequence. Amino signals of Asn and Gln residues could not be uniquely assigned, due to inefficient intraresidual NOE transfer between the amide proton and the amino protons. However the following amino peak positions (ppm) per residue have been resolved from a high resolution 15N-1H HSQC recorded for the [U-15N] labeled sample. Chemical shifts (ppm) are valid for a temperature of 2 degrees Celsius: Set Nr. 1H amino protons 15N amino Set 1. 7.801, 7.023 113.85 Set 2. 7.736, 7.035 113.41 Set 3. 7.700, 7.027 113.38 remark: weak intensity of crosspeaks Set 4. 7.604, 6.931 113.15 Set 5. 7.679, 6.973 113.11 Set 6. 7.707, (7.003 or 6.958) 113.05 Set 7. 7.763, (7.003 or 6.958) 113.04 Set 8. 7.677, 6.958 112.99 Set 9. 7.630, 6.947 112.98 Set 10. 7.692, 6.980 112.92 Set 11. 7.614, 6.958 112.88 Set 12. 7.628, 6.948 112.81 Set 13. 7.654, 6.92 112.73 Set 14. 7.578, 6.92 112.73 Set 15. 7.605, 6.937 112.69 Set 16. 7.485, 6.905 112.66 This accounts for 16 out of 17 expected resonance sets ( 8 Asn + 9 Gln) Absolute error limits of amino peak positions are estimated < 0.02 ppm in the 1H dimension and < 0.1 ppm in the 15N dimension. Aromatic proton resonances for the single Trp, four Phe, and two Tyr spin systems have been identified via a 2D 1H-1H TOCSY spectrum of an non-labeled Sml1 sample. Note that the Sml1 protein is highly unstructured, even at low temperature. As a result chemical shifts for the aromatic residues display a limited dispersion, in good agreement with published random coil chemical shift values. Reference random coil shifts: Wishart, D.S., Bigam, C.G., Holm, A., Hodges, R.S., & Sykes, B.D., "1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbour effects," J. Biomol. NMR 5, 67-81 (1995). Assignments of the aromatic protons are therefore based on analogy with known random coil chemical shifts determined for small peptides. Note that the TOCSY spectrum was recorded at higher temperature in comparison to the other spectra, so reported chemical shifts of aromatic base signals are only valid at a temperature of 23 degrees Celsius. 13C (and 1H) chemical shifts of given CD,CG, and CE sidechain carbons have been determined from a 2D 13C-1H HSQC, as many sidechain carbon shifts are invariant per residue type, and often overlap exactly into a well-defined crosspeak. The reported carbon (and proton) shifts correspond to the central position in the carbon dimension of the overlapping summed crosspeak. The coresponding error values in the table corresponds to the deviation or uncertainty of the position for an individual signal inside the broader distribution envelop of the overlapping crosspeak. The ambiguity code is set to 5 for these type of assignments. Assignment of the CA and HA proton of Pro37 follows from the presence of the remaining crosspeak in the 2D 13C-1H HSQC spectrum after assignment of all other HA-CA crosspeaks by means of CBCACONH and CBCANH triple-resonance spectra. The 2D 13C-1H HSQC is also used for accurate determination of 1H and 13C chemical shifts of CH2 and methyl resonances of the single Ile76 in the sequence. Proton and carbon shifts of methyl groups of Leu and Val residues are stereospecifically linked via the 2D 13C-1H HSQC spectrum and assigned via the carbon resonances, as the average carbon shift is very close to known random coil shifts determined for small peptides. However, the ambiguity code is here set to 2, because an absolute stereospecific assignment for Leu and Val methyl groups in unstructured peptides has not been determined as yet. Accurate chemical shifts for alpha, delta en gamma protons and carbons of the five prolines have also been extracted in this way, but delta resonances can not be assigned uniquely. Although the degenerate chemical shifts prevent listing of the chemical shifts in the final table, we give these chemical shifts below to make the list complete. Two different group of prolines can be distinguished based on the chemical shift dispersion of their respective delta resonances, and are denoted group I and II: Group I: HD2/HD3 3.80 and 3.61 (0.02) ppm CD 50.33 (0.2) ppm Group II: HD2/HD3 3.86 and 3.66 (0.02) ppm CD 50.84 (0.1) ppm Values given between brackets indicate the estimated error peak position in ppm. ; loop_ _Sample_label $sample_one $sample_2 $sample_3 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Sml1 protein' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 GLN C C 175.35 0.10 1 2 . 2 GLN CA C 55.72 0.10 1 3 . 2 GLN CB C 29.55 0.10 1 4 . 2 GLN CG C 33.66 0.50 5 5 . 2 GLN HA H 4.36 0.03 1 6 . 3 ASN C C 175.50 0.10 1 7 . 3 ASN CA C 53.05 0.10 1 8 . 3 ASN CB C 38.79 0.10 1 9 . 3 ASN HA H 4.70 0.03 1 10 . 3 ASN HB2 H 2.80 0.03 1 11 . 3 ASN HB3 H 2.80 0.03 1 12 . 3 ASN H H 8.83 0.01 1 13 . 3 ASN N N 121.21 0.10 1 14 . 4 SER C C 175.05 0.10 1 15 . 4 SER CA C 59.08 0.10 1 16 . 4 SER CB C 63.49 0.10 1 17 . 4 SER HA H 4.33 0.03 1 18 . 4 SER HB2 H 3.90 0.03 1 19 . 4 SER HB3 H 3.90 0.03 1 20 . 4 SER H H 8.56 0.01 1 21 . 4 SER N N 116.82 0.10 1 22 . 5 GLN C C 176.00 0.10 1 23 . 5 GLN CA C 56.58 0.10 1 24 . 5 GLN CB C 28.89 0.10 1 25 . 5 GLN CG C 33.66 0.50 5 26 . 5 GLN HA H 4.27 0.03 1 27 . 5 GLN HB2 H 2.02 0.03 1 28 . 5 GLN HB3 H 2.02 0.03 1 29 . 5 GLN HG2 H 2.29 0.03 1 30 . 5 GLN HG3 H 2.29 0.03 1 31 . 5 GLN H H 8.59 0.01 1 32 . 5 GLN N N 121.62 0.10 1 33 . 6 ASP C C 176.84 0.10 1 34 . 6 ASP CA C 54.96 0.10 1 35 . 6 ASP CB C 40.78 0.10 1 36 . 6 ASP HA H 4.53 0.03 1 37 . 6 ASP HB2 H 2.60 0.03 1 38 . 6 ASP HB3 H 2.60 0.03 1 39 . 6 ASP H H 8.25 0.01 1 40 . 6 ASP N N 120.52 0.10 1 41 . 7 TYR C C 177.72 0.10 1 42 . 7 TYR CA C 57.23 0.10 1 43 . 7 TYR HA H 4.34 0.03 1 44 . 7 TYR HB2 H 2.89 0.03 1 45 . 7 TYR HB3 H 2.89 0.03 1 46 . 7 TYR HD1 H 6.94 0.03 1 47 . 7 TYR HD2 H 6.94 0.02 1 48 . 7 TYR HE1 H 6.77 0.02 1 49 . 7 TYR HE2 H 6.77 0.02 1 50 . 7 TYR H H 8.10 0.01 1 51 . 7 TYR N N 120.92 0.10 1 52 . 8 PHE C C 176.90 0.10 1 53 . 8 PHE CA C 57.81 0.10 1 54 . 8 PHE CB C 39.43 0.10 1 55 . 8 PHE HA H 4.29 0.03 1 56 . 8 PHE HB2 H 2.99 0.03 1 57 . 8 PHE HB3 H 2.99 0.03 1 58 . 8 PHE HD1 H 7.27 0.03 1 59 . 8 PHE HD2 H 7.27 0.02 1 60 . 8 PHE HE1 H 7.36 0.02 1 61 . 8 PHE HE2 H 7.36 0.02 1 62 . 8 PHE H H 8.33 0.01 1 63 . 8 PHE HZ H 7.32 0.02 1 64 . 8 PHE N N 120.01 0.10 1 65 . 9 TYR C C 174.08 0.10 1 66 . 9 TYR CA C 59.02 0.10 1 67 . 9 TYR HA H 4.35 0.03 1 68 . 9 TYR HB2 H 2.97 0.03 1 69 . 9 TYR HB3 H 2.97 0.03 1 70 . 9 TYR HD1 H 7.15 0.03 1 71 . 9 TYR HD2 H 7.15 0.02 1 72 . 9 TYR HE1 H 6.86 0.02 1 73 . 9 TYR HE2 H 6.86 0.02 1 74 . 9 TYR H H 8.04 0.01 1 75 . 9 TYR N N 120.69 0.10 1 76 . 10 ALA C C 178.25 0.10 1 77 . 10 ALA CA C 52.97 0.10 1 78 . 10 ALA CB C 18.90 0.10 1 79 . 10 ALA HA H 4.12 0.03 1 80 . 10 ALA HB H 1.36 0.03 1 81 . 10 ALA H H 8.10 0.01 1 82 . 10 ALA N N 124.00 0.10 1 83 . 11 GLN C C 176.30 0.10 1 84 . 11 GLN CA C 56.30 0.10 1 85 . 11 GLN CB C 28.99 0.10 1 86 . 11 GLN CG C 33.60 0.50 5 87 . 11 GLN HA H 4.13 0.03 1 88 . 11 GLN HB2 H 1.92 0.03 1 89 . 11 GLN HB3 H 1.92 0.03 1 90 . 11 GLN HG2 H 2.26 0.03 1 91 . 11 GLN HG3 H 2.26 0.03 1 92 . 11 GLN H H 8.18 0.01 1 93 . 11 GLN N N 118.19 0.10 1 94 . 12 ASN CA C 53.58 0.10 1 95 . 12 ASN CB C 38.65 0.10 1 96 . 12 ASN HA H 4.60 0.03 1 97 . 12 ASN HB2 H 2.75 0.03 1 98 . 12 ASN HB3 H 2.75 0.03 1 99 . 12 ASN H H 8.30 0.01 1 100 . 12 ASN N N 118.36 0.10 1 101 . 13 ARG C C 176.54 0.10 1 102 . 13 ARG HA H 4.32 0.03 1 103 . 13 ARG CA C 56.60 0.30 1 104 . 14 CYS C C 174.96 0.10 1 105 . 14 CYS CA C 59.00 0.10 1 106 . 14 CYS CB C 27.71 0.10 1 107 . 14 CYS HA H 4.40 0.03 1 108 . 14 CYS HB2 H 2.92 0.03 1 109 . 14 CYS HB3 H 2.92 0.03 1 110 . 14 CYS H H 8.36 0.01 1 111 . 14 CYS N N 119.42 0.10 1 112 . 15 GLN C C 176.13 0.10 1 113 . 15 GLN CA C 56.04 0.10 1 114 . 15 GLN CB C 29.15 0.10 1 115 . 15 GLN CG C 33.66 0.50 1 116 . 15 GLN HA H 4.27 0.03 1 117 . 15 GLN HB2 H 1.96 0.03 1 118 . 15 GLN HB3 H 1.96 0.03 1 119 . 15 GLN HG2 H 2.35 0.03 1 120 . 15 GLN HG3 H 2.35 0.03 1 121 . 15 GLN H H 8.49 0.01 1 122 . 15 GLN N N 122.24 0.10 1 123 . 16 GLN C C 175.86 0.10 1 124 . 16 GLN CA C 55.88 0.10 1 125 . 16 GLN CB C 29.38 0.10 1 126 . 16 GLN CG C 33.66 0.50 1 127 . 16 GLN HA H 4.26 0.03 1 128 . 16 GLN HB2 H 2.02 0.03 1 129 . 16 GLN HB3 H 2.02 0.03 1 130 . 16 GLN HG2 H 2.35 0.03 1 131 . 16 GLN HG3 H 2.35 0.03 1 132 . 16 GLN H H 8.46 0.01 1 133 . 16 GLN N N 121.28 0.10 1 134 . 17 GLN C C 175.86 0.10 5 135 . 17 GLN CA C 55.38 0.10 5 136 . 17 GLN CB C 29.60 0.10 5 137 . 17 GLN CG C 33.66 0.50 5 138 . 17 GLN HA H 4.29 0.03 5 139 . 17 GLN HB2 H 2.05 0.03 5 140 . 17 GLN HB3 H 2.05 0.03 5 141 . 17 GLN HG2 H 2.35 0.03 5 142 . 17 GLN HG3 H 2.35 0.03 5 143 . 17 GLN H H 8.51 0.01 5 144 . 17 GLN N N 121.84 0.10 5 145 . 18 GLN C C 175.36 0.10 5 146 . 18 GLN CA C 55.38 0.10 5 147 . 18 GLN CB C 29.60 0.10 5 148 . 18 GLN CG C 33.66 0.50 5 149 . 18 GLN HA H 4.29 0.03 5 150 . 18 GLN HB2 H 2.05 0.03 5 151 . 18 GLN HB3 H 2.05 0.03 5 152 . 18 GLN HG2 H 2.35 0.03 5 153 . 18 GLN HG3 H 2.35 0.03 5 154 . 18 GLN H H 8.51 0.01 5 155 . 18 GLN N N 121.84 0.10 5 156 . 19 ALA CA C 50.57 0.10 1 157 . 19 ALA CB C 18.03 0.10 1 158 . 19 ALA HA H 4.54 0.03 1 159 . 19 ALA HB H 1.35 0.03 1 160 . 19 ALA H H 8.55 0.01 1 161 . 19 ALA N N 127.13 0.10 1 162 . 20 PRO C C 177.10 0.10 1 163 . 20 PRO CA C 63.06 0.10 1 164 . 20 PRO CB C 31.98 0.10 1 165 . 20 PRO CG C 27.33 0.40 5 166 . 20 PRO HA H 4.42 0.03 5 167 . 20 PRO HG2 H 2.02 0.05 5 168 . 20 PRO HG3 H 2.02 0.05 5 169 . 21 SER C C 175.15 0.10 1 170 . 21 SER CA C 58.40 0.10 1 171 . 21 SER CB C 63.56 0.10 1 172 . 21 SER HA H 4.43 0.03 1 173 . 21 SER HB2 H 3.86 0.03 1 174 . 21 SER HB3 H 3.86 0.03 1 175 . 21 SER H H 8.60 0.01 1 176 . 21 SER N N 115.98 0.10 1 177 . 22 THR C C 174.51 0.10 1 178 . 22 THR CA C 61.94 0.10 1 179 . 22 THR CB C 69.48 0.10 1 180 . 22 THR CG2 C 21.61 0.30 5 181 . 22 THR HA H 4.30 0.03 1 182 . 22 THR HB H 4.28 0.03 1 183 . 22 THR HG2 H 1.21 0.03 1 184 . 22 THR H H 8.29 0.01 1 185 . 22 THR N N 116.16 0.10 1 186 . 23 LEU C C 177.26 0.10 1 187 . 23 LEU CA C 55.16 0.10 1 188 . 23 LEU CB C 42.14 0.10 1 189 . 23 LEU CD1 C 24.80 0.30 2 190 . 23 LEU CD2 C 23.48 0.30 2 191 . 23 LEU CG C 27.00 0.30 5 192 . 23 LEU HA H 4.32 0.03 1 193 . 23 LEU HB2 H 1.60 0.03 1 194 . 23 LEU HB3 H 1.60 0.03 1 195 . 23 LEU HD1 H 0.91 0.03 2 196 . 23 LEU HD2 H 0.84 0.03 2 197 . 23 LEU HG H 1.60 0.05 5 198 . 23 LEU H H 8.24 0.01 1 199 . 23 LEU N N 124.31 0.10 1 200 . 24 ARG C C 176.37 0.10 1 201 . 24 ARG CA C 55.86 0.10 1 202 . 24 ARG CB C 30.71 0.10 1 203 . 24 ARG CD C 43.20 0.20 5 204 . 24 ARG CG C 27.00 0.40 5 205 . 24 ARG HA H 4.38 0.03 1 206 . 24 ARG HB2 H 1.80 0.03 1 207 . 24 ARG HB3 H 1.80 0.03 1 208 . 24 ARG HD2 H 3.16 0.03 5 209 . 24 ARG HD3 H 3.16 0.03 5 210 . 24 ARG HG2 H 1.59 0.03 1 211 . 24 ARG HG3 H 1.59 0.03 1 212 . 24 ARG H H 8.43 0.01 1 213 . 24 ARG N N 122.50 0.10 1 214 . 25 THR C C 174.60 0.10 1 215 . 25 THR CA C 62.02 0.10 1 216 . 25 THR CB C 69.64 0.10 1 217 . 25 THR CG2 C 21.61 0.30 5 218 . 25 THR HA H 4.31 0.03 1 219 . 25 THR HB H 4.16 0.03 1 220 . 25 THR HG2 H 1.18 0.03 1 221 . 25 THR H H 8.30 0.01 1 222 . 25 THR N N 116.62 0.10 1 223 . 26 VAL C C 176.31 0.10 1 224 . 26 VAL CA C 62.34 0.10 1 225 . 26 VAL CB C 32.76 0.10 1 226 . 26 VAL CG1 C 21.07 0.20 2 227 . 26 VAL CG2 C 20.41 0.20 2 228 . 26 VAL HA H 4.18 0.03 1 229 . 26 VAL HB H 2.09 0.03 1 230 . 26 VAL HG1 H 0.92 0.02 2 231 . 26 VAL HG2 H 0.93 0.02 2 232 . 26 VAL H H 8.36 0.01 1 233 . 26 VAL N N 123.08 0.10 1 234 . 27 THR C C 174.65 0.10 1 235 . 27 THR CA C 61.87 0.10 1 236 . 27 THR CB C 69.70 0.10 1 237 . 27 THR CG2 C 21.61 0.30 5 238 . 27 THR HA H 4.31 0.03 1 239 . 27 THR HB H 4.25 0.03 1 240 . 27 THR HG2 H 1.18 0.03 1 241 . 27 THR H H 8.38 0.01 1 242 . 27 THR N N 118.52 0.10 1 243 . 28 MET C C 176.29 0.10 1 244 . 28 MET CA C 55.71 0.10 1 245 . 28 MET CB C 32.43 0.10 1 246 . 28 MET CE C 16.85 0.30 5 247 . 28 MET CG C 31.93 0.30 5 248 . 28 MET HA H 4.42 0.03 1 249 . 28 MET HB2 H 2.06 0.03 1 250 . 28 MET HB3 H 2.06 0.03 1 251 . 28 MET HE H 2.07 0.03 5 252 . 28 MET HG2 H 2.58 0.03 1 253 . 28 MET HG3 H 2.58 0.03 1 254 . 28 MET H H 8.56 0.01 1 255 . 28 MET N N 123.06 0.10 1 256 . 29 ALA C C 177.99 0.10 1 257 . 29 ALA CA C 52.95 0.10 1 258 . 29 ALA CB C 19.19 0.10 1 259 . 29 ALA HA H 4.20 0.03 1 260 . 29 ALA HB H 1.34 0.03 1 261 . 29 ALA H H 8.40 0.01 1 262 . 29 ALA N N 124.83 0.10 1 263 . 30 GLU C C 177.85 0.10 1 264 . 30 GLU CA C 56.82 0.10 1 265 . 30 GLU CB C 30.25 0.10 1 266 . 30 GLU CG C 36.18 0.50 5 267 . 30 GLU HA H 4.15 0.03 1 268 . 30 GLU HB2 H 1.90 0.03 1 269 . 30 GLU HB3 H 1.90 0.03 1 270 . 30 GLU HG2 H 2.12 0.03 1 271 . 30 GLU HG3 H 2.12 0.03 1 272 . 30 GLU H H 8.36 0.01 1 273 . 30 GLU N N 119.49 0.10 1 274 . 31 PHE C C 175.54 0.10 1 275 . 31 PHE CA C 57.91 0.10 1 276 . 31 PHE CB C 39.37 0.10 1 277 . 31 PHE HA H 4.53 0.03 1 278 . 31 PHE HB2 H 3.08 0.03 1 279 . 31 PHE HB3 H 3.08 0.03 1 280 . 31 PHE HD1 H 7.27 0.03 1 281 . 31 PHE HD2 H 7.27 0.02 1 282 . 31 PHE HE1 H 7.36 0.02 1 283 . 31 PHE HE2 H 7.36 0.02 1 284 . 31 PHE H H 8.29 0.01 1 285 . 31 PHE HZ H 7.32 0.02 1 286 . 31 PHE N N 121.39 0.10 1 287 . 32 ARG C C 175.45 0.10 1 288 . 32 ARG CA C 55.66 0.10 1 289 . 32 ARG CB C 30.84 0.10 1 290 . 32 ARG CD C 43.20 0.20 5 291 . 32 ARG CG C 27.00 0.40 5 292 . 32 ARG HA H 4.23 0.03 1 293 . 32 ARG HB2 H 1.68 0.03 1 294 . 32 ARG HB3 H 1.68 0.03 1 295 . 32 ARG HD2 H 3.16 0.03 5 296 . 32 ARG HD3 H 3.16 0.03 5 297 . 32 ARG HG2 H 1.53 0.03 1 298 . 32 ARG HG3 H 1.53 0.03 1 299 . 32 ARG H H 8.15 0.01 1 300 . 32 ARG N N 122.90 0.10 1 301 . 33 ARG C C 176.11 0.10 1 302 . 33 ARG CA C 56.05 0.10 1 303 . 33 ARG CB C 30.59 0.10 1 304 . 33 ARG CD C 43.20 0.20 5 305 . 33 ARG CG C 27.00 0.40 5 306 . 33 ARG HA H 4.22 0.03 1 307 . 33 ARG HB2 H 1.74 0.03 1 308 . 33 ARG HB3 H 1.74 0.03 1 309 . 33 ARG HD2 H 3.16 0.03 5 310 . 33 ARG HD3 H 3.16 0.03 5 311 . 33 ARG HG2 H 1.61 0.03 1 312 . 33 ARG HG3 H 1.61 0.03 1 313 . 33 ARG H H 8.35 0.01 1 314 . 33 ARG N N 122.93 0.10 1 315 . 34 VAL CA C 59.68 0.10 1 316 . 34 VAL CB C 32.50 0.10 1 317 . 34 VAL CG1 C 20.90 0.20 2 318 . 34 VAL CG2 C 20.41 0.20 2 319 . 34 VAL HA H 4.38 0.03 1 320 . 34 VAL HB H 2.05 0.03 1 321 . 34 VAL HG1 H 0.96 0.02 2 322 . 34 VAL HG2 H 0.93 0.02 2 323 . 34 VAL H H 8.26 0.01 1 324 . 34 VAL N N 123.13 0.10 1 325 . 35 PRO C C 176.49 0.10 1 326 . 35 PRO CA C 62.75 0.10 1 327 . 35 PRO CB C 31.98 0.10 1 328 . 35 PRO CG C 27.35 0.20 5 329 . 35 PRO HA H 4.37 0.03 1 330 . 35 PRO HB2 H 2.23 0.03 4 331 . 35 PRO HB3 H 2.23 0.03 4 332 . 35 PRO HG2 H 1.83 0.03 4 333 . 35 PRO HG3 H 1.83 0.03 4 334 . 36 LEU CA C 52.91 0.10 1 335 . 36 LEU CB C 41.54 0.10 1 336 . 36 LEU CD1 C 24.80 0.30 2 337 . 36 LEU CD2 C 23.34 0.10 2 338 . 36 LEU CG C 27.00 0.30 5 339 . 36 LEU HA H 4.55 0.03 1 340 . 36 LEU HB2 H 1.55 0.03 1 341 . 36 LEU HB3 H 1.55 0.03 1 342 . 36 LEU HD1 H 0.95 0.03 2 343 . 36 LEU HD2 H 0.91 0.03 2 344 . 36 LEU HG H 1.60 0.05 5 345 . 36 LEU H H 8.42 0.01 1 346 . 36 LEU N N 123.82 0.10 1 347 . 37 PRO CA C 61.27 0.10 1 348 . 37 PRO CG C 27.33 0.40 5 349 . 37 PRO HA H 4.66 0.03 1 350 . 37 PRO HG2 H 2.02 0.05 5 351 . 37 PRO HG3 H 2.02 0.05 5 352 . 38 PRO C C 176.98 0.10 1 353 . 38 PRO CA C 62.77 0.10 1 354 . 38 PRO CB C 31.90 0.10 1 355 . 38 PRO CG C 27.33 0.40 5 356 . 38 PRO HA H 4.38 0.03 5 357 . 38 PRO HG2 H 2.02 0.05 5 358 . 38 PRO HG3 H 2.02 0.05 5 359 . 39 MET C C 175.92 0.10 1 360 . 39 MET CA C 55.29 0.10 1 361 . 39 MET CB C 32.91 0.10 1 362 . 39 MET CE C 16.85 0.30 5 363 . 39 MET CG C 32.01 0.10 5 364 . 39 MET HA H 4.39 0.03 1 365 . 39 MET HB2 H 2.02 0.03 1 366 . 39 MET HB3 H 2.02 0.03 1 367 . 39 MET HE H 2.01 0.02 5 368 . 39 MET HG2 H 2.29 0.03 1 369 . 39 MET HG3 H 2.29 0.03 1 370 . 39 MET H H 8.53 0.01 1 371 . 39 MET N N 120.69 0.10 1 372 . 40 ALA C C 177.50 0.10 1 373 . 40 ALA CA C 52.25 0.10 1 374 . 40 ALA CB C 19.43 0.10 1 375 . 40 ALA HA H 4.26 0.03 1 376 . 40 ALA HB H 1.36 0.03 1 377 . 40 ALA H H 8.41 0.01 1 378 . 40 ALA N N 125.50 0.10 1 379 . 41 GLU C C 176.29 0.10 1 380 . 41 GLU CA C 56.14 0.10 1 381 . 41 GLU CB C 30.29 0.10 1 382 . 41 GLU CG C 36.18 0.50 5 383 . 41 GLU HA H 4.25 0.03 1 384 . 41 GLU HB2 H 1.92 0.03 1 385 . 41 GLU HB3 H 1.92 0.03 1 386 . 41 GLU HG2 H 2.24 0.03 1 387 . 41 GLU HG3 H 2.24 0.03 1 388 . 41 GLU H H 8.49 0.01 1 389 . 41 GLU N N 120.61 0.10 1 390 . 42 VAL CA C 59.87 0.10 1 391 . 42 VAL CB C 32.43 0.10 1 392 . 42 VAL CG1 C 20.90 0.20 2 393 . 42 VAL CG2 C 20.41 0.20 2 394 . 42 VAL HA H 4.37 0.03 1 395 . 42 VAL HB H 2.06 0.03 1 396 . 42 VAL HG1 H 0.96 0.02 2 397 . 42 VAL HG2 H 0.93 0.02 2 398 . 42 VAL H H 8.38 0.01 1 399 . 42 VAL N N 123.68 0.10 1 400 . 43 PRO C C 176.77 0.10 1 401 . 43 PRO CA C 63.01 0.10 1 402 . 43 PRO CB C 32.06 0.10 1 403 . 43 PRO CG C 27.33 0.40 5 404 . 43 PRO HA H 4.40 0.03 1 405 . 43 PRO HG2 H 2.02 0.05 5 406 . 43 PRO HG3 H 2.02 0.05 5 407 . 44 MET C C 176.33 0.10 1 408 . 44 MET CA C 55.40 0.10 1 409 . 44 MET CB C 32.88 0.10 1 410 . 44 MET CE C 16.85 0.30 5 411 . 44 MET CG C 31.93 0.30 5 412 . 44 MET HA H 4.42 0.03 1 413 . 44 MET HB2 H 2.04 0.03 1 414 . 44 MET HB3 H 2.04 0.03 1 415 . 44 MET HE H 2.07 0.03 5 416 . 44 MET HG2 H 2.56 0.03 1 417 . 44 MET HG3 H 2.56 0.03 1 418 . 44 MET H H 8.58 0.01 1 419 . 44 MET N N 121.31 0.10 1 420 . 45 LEU C C 177.54 0.10 1 421 . 45 LEU CA C 55.12 0.10 1 422 . 45 LEU CB C 42.27 0.10 1 423 . 45 LEU CD1 C 24.80 0.30 2 424 . 45 LEU CD2 C 23.48 0.30 2 425 . 45 LEU CG C 27.00 0.30 5 426 . 45 LEU HA H 4.38 0.03 1 427 . 45 LEU HB2 H 1.61 0.03 1 428 . 45 LEU HB3 H 1.61 0.03 1 429 . 45 LEU HD1 H 0.91 0.03 2 430 . 45 LEU HD2 H 0.84 0.03 2 431 . 45 LEU HG H 1.60 0.05 5 432 . 45 LEU H H 8.44 0.01 1 433 . 45 LEU N N 124.02 0.10 1 434 . 46 SER C C 175.08 0.10 1 435 . 46 SER CA C 58.22 0.10 1 436 . 46 SER CB C 63.66 0.10 1 437 . 46 SER HA H 4.48 0.03 1 438 . 46 SER HB2 H 3.89 0.03 1 439 . 46 SER HB3 H 3.89 0.03 1 440 . 46 SER H H 8.51 0.01 1 441 . 46 SER N N 116.89 0.10 1 442 . 47 THR C C 174.85 0.10 1 443 . 47 THR CA C 61.92 0.10 1 444 . 47 THR CB C 69.41 0.10 1 445 . 47 THR CG2 C 21.61 0.30 5 446 . 47 THR HA H 4.35 0.03 1 447 . 47 THR HB H 4.30 0.03 1 448 . 47 THR HG2 H 1.19 0.03 1 449 . 47 THR H H 8.28 0.01 1 450 . 47 THR N N 115.51 0.10 1 451 . 48 GLN C C 175.86 0.10 1 452 . 48 GLN CA C 56.05 0.10 1 453 . 48 GLN CB C 29.25 0.10 1 454 . 48 GLN CG C 33.66 0.50 5 455 . 48 GLN HA H 4.30 0.03 1 456 . 48 GLN HB2 H 2.00 0.03 1 457 . 48 GLN HB3 H 2.00 0.03 1 458 . 48 GLN HG2 H 2.34 0.03 1 459 . 48 GLN HG3 H 2.34 0.03 1 460 . 48 GLN H H 8.42 0.01 1 461 . 48 GLN N N 122.11 0.10 1 462 . 49 ASN C C 175.49 0.10 1 463 . 49 ASN CA C 53.23 0.10 1 464 . 49 ASN CB C 38.75 0.10 1 465 . 49 ASN HA H 4.72 0.03 1 466 . 49 ASN HB2 H 2.78 0.03 1 467 . 49 ASN HB3 H 2.78 0.03 1 468 . 49 ASN H H 8.55 0.01 1 469 . 49 ASN N N 119.72 0.10 1 470 . 50 SER C C 174.90 0.10 1 471 . 50 SER CA C 58.67 0.10 1 472 . 50 SER CB C 63.53 0.10 1 473 . 50 SER HA H 4.42 0.03 1 474 . 50 SER HB2 H 3.88 0.03 1 475 . 50 SER HB3 H 3.88 0.03 1 476 . 50 SER H H 8.44 0.01 1 477 . 50 SER N N 116.48 0.10 1 478 . 51 MET C C 176.99 0.10 1 479 . 51 MET CA C 55.68 0.10 1 480 . 51 MET CB C 32.23 0.10 1 481 . 51 MET CE C 16.85 0.30 5 482 . 51 MET CG C 31.93 0.30 5 483 . 51 MET HA H 4.50 0.03 1 484 . 51 MET HB2 H 2.12 0.03 1 485 . 51 MET HB3 H 2.12 0.03 1 486 . 51 MET HE H 2.07 0.03 5 487 . 51 MET HG2 H 2.36 0.03 1 488 . 51 MET HG3 H 2.36 0.03 1 489 . 51 MET H H 8.51 0.01 1 490 . 51 MET N N 121.85 0.10 1 491 . 52 GLY C C 174.26 0.10 1 492 . 52 GLY CA C 45.21 0.10 1 493 . 52 GLY HA2 H 3.97 0.03 1 494 . 52 GLY HA3 H 3.97 0.03 1 495 . 52 GLY H H 8.45 0.01 1 496 . 52 GLY N N 109.80 0.10 1 497 . 53 SER C C 174.91 0.10 1 498 . 53 SER CA C 58.19 0.10 1 499 . 53 SER CB C 63.90 0.10 1 500 . 53 SER HA H 4.49 0.03 1 501 . 53 SER HB2 H 3.95 0.03 1 502 . 53 SER HB3 H 3.95 0.03 1 503 . 53 SER H H 8.36 0.01 1 504 . 53 SER N N 115.73 0.10 1 505 . 54 SER C C 174.54 0.10 1 506 . 54 SER CA C 58.43 0.10 1 507 . 54 SER CB C 63.67 0.10 1 508 . 54 SER HA H 4.46 0.03 1 509 . 54 SER HB2 H 3.90 0.03 1 510 . 54 SER HB3 H 3.90 0.03 1 511 . 54 SER H H 8.55 0.01 1 512 . 54 SER N N 118.09 0.10 1 513 . 55 ALA C C 178.07 0.10 1 514 . 55 ALA CA C 52.73 0.10 1 515 . 55 ALA CB C 19.18 0.10 1 516 . 55 ALA HA H 4.31 0.03 1 517 . 55 ALA HB H 1.39 0.03 1 518 . 55 ALA H H 8.45 0.01 1 519 . 55 ALA N N 125.98 0.10 1 520 . 56 SER C C 174.60 0.10 1 521 . 56 SER CA C 58.33 0.10 1 522 . 56 SER CB C 63.67 0.10 1 523 . 56 SER HA H 4.39 0.03 1 524 . 56 SER HB2 H 3.87 0.03 1 525 . 56 SER HB3 H 3.87 0.03 1 526 . 56 SER H H 8.32 0.01 1 527 . 56 SER N N 114.89 0.10 1 528 . 57 ALA C C 178.01 0.10 1 529 . 57 ALA CA C 52.70 0.10 1 530 . 57 ALA CB C 19.21 0.10 1 531 . 57 ALA HA H 4.33 0.03 1 532 . 57 ALA HB H 1.40 0.03 1 533 . 57 ALA H H 8.39 0.01 1 534 . 57 ALA N N 126.20 0.10 1 535 . 58 SER C C 174.59 0.10 1 536 . 58 SER CA C 58.28 0.10 1 537 . 58 SER CB C 63.74 0.10 1 538 . 58 SER HA H 4.40 0.03 1 539 . 58 SER HB2 H 3.88 0.03 1 540 . 58 SER HB3 H 3.88 0.03 1 541 . 58 SER H H 8.36 0.01 1 542 . 58 SER N N 115.00 0.10 1 543 . 59 ALA C C 178.26 0.10 1 544 . 59 ALA CA C 52.92 0.10 1 545 . 59 ALA CB C 19.17 0.10 1 546 . 59 ALA HA H 4.31 0.03 1 547 . 59 ALA HB H 1.41 0.03 1 548 . 59 ALA H H 8.43 0.01 1 549 . 59 ALA N N 125.96 0.10 1 550 . 60 SER C C 175.00 0.10 1 551 . 60 SER CA C 58.56 0.10 1 552 . 60 SER CB C 63.66 0.10 1 553 . 60 SER HA H 4.42 0.03 1 554 . 60 SER HB2 H 3.90 0.03 1 555 . 60 SER HB3 H 3.90 0.03 1 556 . 60 SER H H 8.41 0.01 1 557 . 60 SER N N 114.82 0.10 1 558 . 61 SER C C 175.04 0.10 1 559 . 61 SER CA C 58.90 0.10 1 560 . 61 SER CB C 63.49 0.10 1 561 . 61 SER HA H 4.41 0.03 1 562 . 61 SER HB2 H 3.90 0.03 1 563 . 61 SER HB3 H 3.90 0.03 1 564 . 61 SER H H 8.36 0.01 1 565 . 61 SER N N 118.03 0.10 1 566 . 62 LEU C C 177.98 0.10 1 567 . 62 LEU CA C 55.81 0.10 1 568 . 62 LEU CB C 42.00 0.10 1 569 . 62 LEU CD1 C 24.80 0.30 2 570 . 62 LEU CD2 C 23.48 0.30 2 571 . 62 LEU CG C 27.00 0.30 5 572 . 62 LEU HA H 4.28 0.03 1 573 . 62 LEU HB2 H 1.61 0.03 1 574 . 62 LEU HB3 H 1.61 0.03 1 575 . 62 LEU HD1 H 0.91 0.03 2 576 . 62 LEU HD2 H 0.84 0.03 2 577 . 62 LEU HG H 1.60 0.05 5 578 . 62 LEU H H 8.26 0.01 1 579 . 62 LEU N N 123.74 0.10 1 580 . 63 GLU C C 176.03 0.10 1 581 . 63 GLU CA C 55.85 0.10 1 582 . 63 GLU CB C 29.29 0.10 1 583 . 63 GLU CG C 36.18 0.50 5 584 . 63 GLU HA H 4.18 0.03 1 585 . 63 GLU HB2 H 1.99 0.03 1 586 . 63 GLU HB3 H 1.99 0.03 1 587 . 63 GLU H H 8.41 0.01 1 588 . 63 GLU N N 120.36 0.10 1 589 . 64 MET C C 176.97 0.10 1 590 . 64 MET CA C 56.55 0.10 1 591 . 64 MET CB C 32.11 0.10 1 592 . 64 MET CE C 16.85 0.30 5 593 . 64 MET CG C 31.93 0.30 5 594 . 64 MET HA H 4.28 0.03 1 595 . 64 MET HB2 H 2.04 0.03 1 596 . 64 MET HB3 H 2.04 0.03 1 597 . 64 MET HE H 2.07 0.03 5 598 . 64 MET HG2 H 2.36 0.03 1 599 . 64 MET HG3 H 2.36 0.03 1 600 . 64 MET H H 8.52 0.01 1 601 . 64 MET N N 121.60 0.10 1 602 . 65 TRP C C 177.24 0.10 1 603 . 65 TRP CA C 58.32 0.10 1 604 . 65 TRP CB C 29.04 0.10 1 605 . 65 TRP HA H 4.59 0.03 1 606 . 65 TRP HB2 H 3.35 0.03 1 607 . 65 TRP HB3 H 3.35 0.03 1 608 . 65 TRP HD1 H 7.25 0.03 1 609 . 65 TRP HE1 H 10.24 0.02 1 610 . 65 TRP HE3 H 7.62 0.02 1 611 . 65 TRP HH2 H 7.22 0.02 1 612 . 65 TRP H H 8.09 0.01 1 613 . 65 TRP HZ2 H 7.48 0.02 1 614 . 65 TRP HZ3 H 7.15 0.02 1 615 . 65 TRP N N 120.84 0.10 1 616 . 66 GLU C C 177.55 0.10 1 617 . 66 GLU CA C 57.58 0.10 1 618 . 66 GLU CB C 29.94 0.10 1 619 . 66 GLU CG C 36.18 0.50 5 620 . 66 GLU HA H 3.97 0.03 1 621 . 66 GLU HB2 H 1.92 0.03 1 622 . 66 GLU HB3 H 1.92 0.03 1 623 . 66 GLU HG2 H 2.04 0.03 1 624 . 66 GLU HG3 H 2.04 0.03 1 625 . 66 GLU H H 8.22 0.01 1 626 . 66 GLU N N 120.95 0.10 1 627 . 67 LYS C C 177.36 0.10 1 628 . 67 LYS CA C 57.54 0.10 1 629 . 67 LYS CB C 32.56 0.10 1 630 . 67 LYS CD C 28.99 0.20 5 631 . 67 LYS CE C 40.15 0.20 5 632 . 67 LYS CG C 24.64 0.30 5 633 . 67 LYS HA H 4.11 0.03 1 634 . 67 LYS HB2 H 1.81 0.03 1 635 . 67 LYS HB3 H 1.81 0.03 1 636 . 67 LYS HD2 H 1.64 0.03 1 637 . 67 LYS HD3 H 1.64 0.03 1 638 . 67 LYS HE2 H 3.10 0.05 5 639 . 67 LYS HE3 H 3.10 0.05 5 640 . 67 LYS HG2 H 1.44 0.03 1 641 . 67 LYS HG3 H 1.44 0.03 1 642 . 67 LYS H H 8.03 0.01 1 643 . 67 LYS N N 121.26 0.10 1 644 . 68 ASP C C 177.23 0.10 1 645 . 68 ASP CA C 55.49 0.10 1 646 . 68 ASP CB C 40.72 0.10 1 647 . 68 ASP HA H 4.47 0.03 1 648 . 68 ASP HB2 H 2.70 0.03 1 649 . 68 ASP HB3 H 2.70 0.03 1 650 . 68 ASP H H 8.30 0.01 1 651 . 68 ASP N N 120.33 0.10 1 652 . 69 LEU C C 178.24 0.10 1 653 . 69 LEU CA C 56.79 0.10 1 654 . 69 LEU CB C 41.81 0.10 1 655 . 69 LEU CD1 C 24.80 0.30 2 656 . 69 LEU CD2 C 23.48 0.30 2 657 . 69 LEU CG C 27.00 0.30 5 658 . 69 LEU HA H 4.06 0.03 1 659 . 69 LEU HB2 H 1.57 0.03 1 660 . 69 LEU HB3 H 1.57 0.03 1 661 . 69 LEU HD1 H 0.91 0.03 2 662 . 69 LEU HD2 H 0.84 0.03 2 663 . 69 LEU HG H 1.60 0.05 5 664 . 69 LEU H H 8.00 0.01 1 665 . 69 LEU N N 121.39 0.10 1 666 . 70 GLU C C 177.80 0.10 1 667 . 70 GLU CA C 57.98 0.10 1 668 . 70 GLU CB C 29.70 0.10 1 669 . 70 GLU CG C 36.18 0.50 5 670 . 70 GLU HA H 4.04 0.03 1 671 . 70 GLU HB2 H 2.03 0.03 1 672 . 70 GLU HB3 H 2.03 0.03 1 673 . 70 GLU HG2 H 2.26 0.03 1 674 . 70 GLU HG3 H 2.26 0.03 1 675 . 70 GLU H H 8.19 0.01 1 676 . 70 GLU N N 119.70 0.10 1 677 . 71 GLU C C 178.00 0.10 1 678 . 71 GLU CA C 57.78 0.10 1 679 . 71 GLU CB C 29.69 0.10 1 680 . 71 GLU CG C 36.18 0.50 5 681 . 71 GLU HA H 4.13 0.03 1 682 . 71 GLU HB2 H 2.03 0.03 1 683 . 71 GLU HB3 H 2.03 0.03 1 684 . 71 GLU HG2 H 2.33 0.03 1 685 . 71 GLU HG3 H 2.33 0.03 1 686 . 71 GLU H H 8.25 0.01 1 687 . 71 GLU N N 120.13 0.10 1 688 . 72 ARG C C 176.44 0.10 1 689 . 72 ARG CA C 57.31 0.10 1 690 . 72 ARG CB C 30.25 0.10 1 691 . 72 ARG CD C 43.20 0.20 5 692 . 72 ARG CG C 27.00 0.40 5 693 . 72 ARG HA H 4.20 0.03 1 694 . 72 ARG HB2 H 1.84 0.03 1 695 . 72 ARG HB3 H 1.84 0.03 1 696 . 72 ARG HD2 H 3.16 0.03 5 697 . 72 ARG HD3 H 3.16 0.03 5 698 . 72 ARG HG2 H 1.58 0.03 1 699 . 72 ARG HG3 H 1.58 0.03 1 700 . 72 ARG H H 8.24 0.01 1 701 . 72 ARG N N 120.84 0.10 1 702 . 73 LEU C C 178.09 0.10 1 703 . 73 LEU CA C 56.08 0.10 1 704 . 73 LEU CB C 41.78 0.10 1 705 . 73 LEU CD1 C 24.80 0.30 2 706 . 73 LEU CD2 C 23.48 0.30 2 707 . 73 LEU CG C 27.00 0.30 5 708 . 73 LEU HA H 4.20 0.03 1 709 . 73 LEU HB2 H 1.71 0.03 1 710 . 73 LEU HB3 H 1.71 0.03 1 711 . 73 LEU HD1 H 0.91 0.03 2 712 . 73 LEU HD2 H 0.84 0.03 2 713 . 73 LEU HG H 1.60 0.05 5 714 . 73 LEU H H 8.30 0.01 1 715 . 73 LEU N N 121.32 0.10 1 716 . 74 ASN C C 175.58 0.10 1 717 . 74 ASN CA C 53.62 0.10 1 718 . 74 ASN CB C 38.73 0.10 1 719 . 74 ASN HA H 4.70 0.03 1 720 . 74 ASN HB2 H 2.81 0.03 1 721 . 74 ASN HB3 H 2.81 0.03 1 722 . 74 ASN H H 8.28 0.01 1 723 . 74 ASN N N 117.95 0.10 1 724 . 75 SER C C 174.89 0.10 1 725 . 75 SER CA C 58.79 0.10 1 726 . 75 SER CB C 63.64 0.10 1 727 . 75 SER HA H 4.41 0.03 1 728 . 75 SER HB2 H 3.91 0.03 1 729 . 75 SER HB3 H 3.91 0.03 1 730 . 75 SER H H 8.11 0.01 1 731 . 75 SER N N 115.71 0.10 1 732 . 76 ILE C C 176.20 0.10 1 733 . 76 ILE CA C 61.76 0.10 1 734 . 76 ILE CB C 38.51 0.10 1 735 . 76 ILE CD1 C 13.17 0.10 1 736 . 76 ILE CG1 C 27.35 0.10 1 737 . 76 ILE CG2 C 17.27 0.10 1 738 . 76 ILE HA H 4.11 0.03 1 739 . 76 ILE HB H 1.85 0.03 1 740 . 76 ILE HD1 H 0.85 0.03 1 741 . 76 ILE HG12 H 1.47 0.02 2 742 . 76 ILE HG13 H 1.16 0.02 2 743 . 76 ILE HG2 H 0.84 0.03 1 744 . 76 ILE H H 8.09 0.01 1 745 . 76 ILE N N 122.07 0.10 1 746 . 77 ASP C C 176.39 0.10 1 747 . 77 ASP CA C 54.40 0.10 1 748 . 77 ASP CB C 40.90 0.10 1 749 . 77 ASP HA H 4.54 0.03 1 750 . 77 ASP HB2 H 2.63 0.03 1 751 . 77 ASP HB3 H 2.63 0.03 1 752 . 77 ASP H H 8.32 0.01 1 753 . 77 ASP N N 122.84 0.10 1 754 . 78 HIS C C 175.01 0.10 1 755 . 78 HIS CA C 56.40 0.10 1 756 . 78 HIS CB C 29.70 0.10 1 757 . 78 HIS HA H 4.55 0.03 1 758 . 78 HIS HB2 H 3.16 0.03 1 759 . 78 HIS HB3 H 3.16 0.03 1 760 . 78 HIS H H 8.33 0.01 1 761 . 78 HIS N N 119.44 0.10 1 762 . 79 ASP C C 176.95 0.10 1 763 . 79 ASP CA C 54.64 0.10 1 764 . 79 ASP CB C 40.85 0.10 1 765 . 79 ASP HA H 4.55 0.03 1 766 . 79 ASP HB2 H 2.69 0.03 1 767 . 79 ASP HB3 H 2.69 0.03 1 768 . 79 ASP H H 8.47 0.01 1 769 . 79 ASP N N 120.85 0.10 1 770 . 80 MET C C 176.77 0.10 1 771 . 80 MET CA C 56.05 0.10 1 772 . 80 MET CB C 31.97 0.10 1 773 . 80 MET CE C 16.85 0.30 5 774 . 80 MET CG C 31.93 0.30 5 775 . 80 MET HA H 4.37 0.03 1 776 . 80 MET HB2 H 2.06 0.03 1 777 . 80 MET HB3 H 2.06 0.03 1 778 . 80 MET HE H 2.07 0.03 5 779 . 80 MET HG2 H 2.53 0.03 1 780 . 80 MET HG3 H 2.53 0.03 1 781 . 80 MET H H 8.43 0.01 1 782 . 80 MET N N 120.86 0.10 1 783 . 81 ASN C C 175.21 0.10 1 784 . 81 ASN CA C 53.65 0.10 1 785 . 81 ASN CB C 38.62 0.10 1 786 . 81 ASN HA H 4.66 0.03 1 787 . 81 ASN HB2 H 2.78 0.03 1 788 . 81 ASN HB3 H 2.78 0.03 1 789 . 81 ASN H H 8.49 0.01 1 790 . 81 ASN N N 118.38 0.10 1 791 . 82 ASN C C 175.11 0.10 1 792 . 82 ASN CA C 53.44 0.10 1 793 . 82 ASN CB C 38.53 0.10 1 794 . 82 ASN HA H 4.65 0.03 1 795 . 82 ASN HB2 H 2.73 0.03 1 796 . 82 ASN HB3 H 2.73 0.03 1 797 . 82 ASN H H 8.29 0.01 1 798 . 82 ASN N N 118.61 0.10 1 799 . 83 ASN C C 175.44 0.10 1 800 . 83 ASN CA C 53.37 0.10 1 801 . 83 ASN CB C 38.47 0.10 1 802 . 83 ASN HA H 4.63 0.03 1 803 . 83 ASN HB2 H 2.75 0.03 1 804 . 83 ASN HB3 H 2.75 0.03 1 805 . 83 ASN H H 8.40 0.01 1 806 . 83 ASN N N 118.87 0.10 1 807 . 84 LYS C C 176.60 0.10 1 808 . 84 LYS CA C 56.55 0.10 1 809 . 84 LYS CB C 32.58 0.10 1 810 . 84 LYS CD C 28.92 0.20 5 811 . 84 LYS CE C 40.15 0.20 5 812 . 84 LYS CG C 24.64 0.30 5 813 . 84 LYS HA H 4.18 0.03 1 814 . 84 LYS HB2 H 1.60 0.03 1 815 . 84 LYS HB3 H 1.60 0.03 1 816 . 84 LYS HD2 H 1.57 0.03 1 817 . 84 LYS HD3 H 1.57 0.03 1 818 . 84 LYS HE2 H 3.10 0.05 5 819 . 84 LYS HE3 H 3.10 0.05 5 820 . 84 LYS HG2 H 1.19 0.03 1 821 . 84 LYS HG3 H 1.19 0.03 1 822 . 84 LYS H H 8.25 0.01 1 823 . 84 LYS N N 121.10 0.10 1 824 . 85 PHE C C 176.53 0.10 1 825 . 85 PHE CA C 57.70 0.10 1 826 . 85 PHE CB C 39.28 0.10 1 827 . 85 PHE HA H 4.61 0.03 1 828 . 85 PHE HB2 H 3.22 0.03 1 829 . 85 PHE HB3 H 3.22 0.03 1 830 . 85 PHE HD1 H 7.27 0.03 1 831 . 85 PHE HD2 H 7.27 0.02 1 832 . 85 PHE HE1 H 7.36 0.02 1 833 . 85 PHE HE2 H 7.36 0.02 1 834 . 85 PHE H H 8.32 0.01 1 835 . 85 PHE HZ H 7.32 0.02 1 836 . 85 PHE N N 120.21 0.10 1 837 . 86 GLY C C 174.32 0.10 1 838 . 86 GLY CA C 45.22 0.10 1 839 . 86 GLY HA2 H 3.94 0.03 1 840 . 86 GLY HA3 H 3.94 0.03 1 841 . 86 GLY H H 8.40 0.01 1 842 . 86 GLY N N 110.54 0.10 1 843 . 87 SER C C 175.40 0.10 1 844 . 87 SER CA C 58.60 0.10 1 845 . 87 SER CB C 63.78 0.10 1 846 . 87 SER HA H 4.43 0.03 1 847 . 87 SER HB2 H 3.94 0.03 1 848 . 87 SER HB3 H 3.94 0.03 1 849 . 87 SER H H 8.42 0.01 1 850 . 87 SER N N 115.70 0.10 1 851 . 88 GLY C C 174.26 0.10 1 852 . 88 GLY CA C 45.29 0.10 1 853 . 88 GLY HA2 H 3.94 0.03 1 854 . 88 GLY HA3 H 3.94 0.03 1 855 . 88 GLY H H 8.64 0.01 1 856 . 88 GLY N N 111.08 0.10 1 857 . 89 GLU C C 176.70 0.10 1 858 . 89 GLU CA C 56.50 0.10 1 859 . 89 GLU CB C 30.15 0.10 1 860 . 89 GLU CG C 36.18 0.50 5 861 . 89 GLU HA H 4.22 0.03 1 862 . 89 GLU HB2 H 1.97 0.03 1 863 . 89 GLU HB3 H 1.97 0.03 1 864 . 89 GLU HG2 H 2.23 0.03 1 865 . 89 GLU HG3 H 2.23 0.03 1 866 . 89 GLU H H 8.33 0.01 1 867 . 89 GLU N N 120.69 0.10 1 868 . 90 LEU C C 177.61 0.10 1 869 . 90 LEU CA C 55.33 0.10 1 870 . 90 LEU CB C 41.96 0.10 1 871 . 90 LEU CD1 C 24.80 0.30 2 872 . 90 LEU CD2 C 23.48 0.30 2 873 . 90 LEU CG C 27.00 0.30 5 874 . 90 LEU HA H 4.29 0.03 1 875 . 90 LEU HB2 H 1.62 0.03 1 876 . 90 LEU HB3 H 1.62 0.03 1 877 . 90 LEU HD1 H 0.91 0.03 2 878 . 90 LEU HD2 H 0.84 0.03 2 879 . 90 LEU HG H 1.60 0.05 5 880 . 90 LEU H H 8.39 0.01 1 881 . 90 LEU N N 123.26 0.10 1 882 . 91 LYS C C 176.74 0.10 1 883 . 91 LYS CA C 56.38 0.10 1 884 . 91 LYS CB C 32.78 0.10 1 885 . 91 LYS CD C 28.99 0.20 5 886 . 91 LYS CE C 40.15 0.20 5 887 . 91 LYS CG C 24.64 0.30 5 888 . 91 LYS HA H 4.26 0.03 1 889 . 91 LYS HB2 H 1.77 0.03 1 890 . 91 LYS HB3 H 1.77 0.03 1 891 . 91 LYS HD2 H 1.64 0.03 1 892 . 91 LYS HD3 H 1.64 0.03 1 893 . 91 LYS HE2 H 3.10 0.05 5 894 . 91 LYS HE3 H 3.10 0.05 5 895 . 91 LYS HG2 H 1.38 0.03 1 896 . 91 LYS HG3 H 1.38 0.03 1 897 . 91 LYS H H 8.39 0.01 1 898 . 91 LYS N N 122.10 0.10 1 899 . 92 SER C C 174.86 0.10 1 900 . 92 SER CA C 58.28 0.10 1 901 . 92 SER CB C 63.68 0.10 1 902 . 92 SER HA H 4.37 0.03 1 903 . 92 SER HB2 H 3.83 0.03 1 904 . 92 SER HB3 H 3.83 0.03 1 905 . 92 SER H H 8.35 0.01 1 906 . 92 SER N N 116.37 0.10 1 907 . 93 MET C C 176.19 0.10 1 908 . 93 MET CA C 55.59 0.10 1 909 . 93 MET CB C 32.32 0.10 1 910 . 93 MET CE C 16.85 0.30 5 911 . 93 MET CG C 31.93 0.30 5 912 . 93 MET HA H 4.39 0.03 1 913 . 93 MET HB2 H 1.95 0.03 1 914 . 93 MET HB3 H 1.95 0.03 1 915 . 93 MET HE H 2.07 0.03 5 916 . 93 MET HG2 H 2.36 0.03 1 917 . 93 MET HG3 H 2.36 0.03 1 918 . 93 MET H H 8.41 0.01 1 919 . 93 MET N N 121.87 0.10 1 920 . 94 PHE C C 175.61 0.10 1 921 . 94 PHE CA C 57.74 0.10 1 922 . 94 PHE CB C 39.39 0.10 1 923 . 94 PHE HA H 4.58 0.03 1 924 . 94 PHE HB2 H 3.12 0.03 1 925 . 94 PHE HB3 H 3.12 0.03 1 926 . 94 PHE HD1 H 7.27 0.03 1 927 . 94 PHE HD2 H 7.27 0.02 1 928 . 94 PHE HE1 H 7.36 0.02 1 929 . 94 PHE HE2 H 7.36 0.02 1 930 . 94 PHE H H 8.25 0.01 1 931 . 94 PHE HZ H 7.32 0.02 1 932 . 94 PHE N N 120.46 0.10 1 933 . 95 ASN C C 175.03 0.10 1 934 . 95 ASN CA C 53.06 0.10 1 935 . 95 ASN CB C 38.61 0.10 1 936 . 95 ASN HA H 4.60 0.03 1 937 . 95 ASN HB2 H 2.77 0.03 2 938 . 95 ASN HB3 H 2.67 0.03 2 939 . 95 ASN H H 8.43 0.01 1 940 . 95 ASN N N 120.46 0.10 1 941 . 96 GLN C C 176.38 0.10 1 942 . 96 GLN CA C 56.06 0.10 1 943 . 96 GLN CB C 29.11 0.10 1 944 . 96 GLN CG C 33.66 0.50 5 945 . 96 GLN HA H 4.21 0.03 1 946 . 96 GLN HB2 H 1.86 0.03 1 947 . 96 GLN HB3 H 1.86 0.03 1 948 . 96 GLN HG2 H 2.25 0.03 1 949 . 96 GLN HG3 H 2.25 0.03 1 950 . 96 GLN H H 8.41 0.01 1 951 . 96 GLN N N 120.30 0.10 1 952 . 97 GLY C C 173.70 0.10 1 953 . 97 GLY CA C 45.06 0.10 1 954 . 97 GLY HA2 H 3.91 0.03 1 955 . 97 GLY HA3 H 3.91 0.03 1 956 . 97 GLY H H 8.47 0.01 1 957 . 97 GLY N N 109.69 0.10 1 958 . 98 LYS C C 176.61 0.10 1 959 . 98 LYS CA C 55.94 0.10 1 960 . 98 LYS CB C 33.11 0.10 1 961 . 98 LYS CD C 28.99 0.20 5 962 . 98 LYS CE C 40.15 0.20 5 963 . 98 LYS CG C 24.64 0.30 5 964 . 98 LYS HA H 4.34 0.03 1 965 . 98 LYS HB2 H 1.74 0.03 1 966 . 98 LYS HB3 H 1.74 0.03 1 967 . 98 LYS HD2 H 1.64 0.03 1 968 . 98 LYS HD3 H 1.64 0.03 1 969 . 98 LYS HE2 H 3.10 0.05 5 970 . 98 LYS HE3 H 3.10 0.05 5 971 . 98 LYS HG2 H 1.36 0.03 1 972 . 98 LYS HG3 H 1.36 0.03 1 973 . 98 LYS H H 8.17 0.01 1 974 . 98 LYS N N 121.21 0.10 1 975 . 99 VAL C C 176.29 0.10 1 976 . 99 VAL CA C 62.46 0.10 1 977 . 99 VAL CB C 32.56 0.10 1 978 . 99 VAL CG1 C 21.07 0.20 2 979 . 99 VAL CG2 C 20.41 0.20 2 980 . 99 VAL HA H 4.07 0.03 1 981 . 99 VAL HB H 2.05 0.03 1 982 . 99 VAL HG1 H 0.92 0.02 2 983 . 99 VAL HG2 H 0.93 0.02 2 984 . 99 VAL H H 8.42 0.01 1 985 . 99 VAL N N 123.17 0.10 1 986 . 100 GLU C C 176.31 0.10 1 987 . 100 GLU CA C 56.36 0.10 1 988 . 100 GLU CB C 30.09 0.10 1 989 . 100 GLU CG C 36.18 0.50 5 990 . 100 GLU HA H 4.26 0.03 1 991 . 100 GLU HB2 H 2.02 0.03 2 992 . 100 GLU HB3 H 1.89 0.03 2 993 . 100 GLU HG2 H 2.24 0.03 1 994 . 100 GLU HG3 H 2.24 0.03 1 995 . 100 GLU H H 8.70 0.01 1 996 . 100 GLU N N 124.95 0.10 1 997 . 101 GLU C C 176.31 0.10 1 998 . 101 GLU CA C 56.41 0.10 1 999 . 101 GLU CB C 30.13 0.10 1 1000 . 101 GLU CG C 36.18 0.50 5 1001 . 101 GLU HA H 4.22 0.03 1 1002 . 101 GLU HB2 H 2.00 0.03 2 1003 . 101 GLU HB3 H 1.91 0.03 2 1004 . 101 GLU HG2 H 2.24 0.03 1 1005 . 101 GLU HG3 H 2.24 0.03 1 1006 . 101 GLU H H 8.53 0.01 1 1007 . 101 GLU N N 122.11 0.10 1 1008 . 102 MET C C 175.60 0.10 1 1009 . 102 MET CA C 55.09 0.10 1 1010 . 102 MET CB C 33.06 0.10 1 1011 . 102 MET CE C 16.85 0.30 5 1012 . 102 MET CG C 31.93 0.30 5 1013 . 102 MET HA H 4.45 0.03 1 1014 . 102 MET HB2 H 1.94 0.03 1 1015 . 102 MET HB3 H 1.94 0.03 1 1016 . 102 MET HE H 2.07 0.03 5 1017 . 102 MET HG2 H 2.48 0.03 1 1018 . 102 MET HG3 H 2.48 0.03 1 1019 . 102 MET H H 8.43 0.01 1 1020 . 102 MET N N 121.09 0.10 1 1021 . 103 ASP C C 174.72 0.10 1 1022 . 103 ASP CA C 54.11 0.10 1 1023 . 103 ASP CB C 41.00 0.10 1 1024 . 103 ASP HA H 4.59 0.03 1 1025 . 103 ASP HB2 H 2.54 0.03 1 1026 . 103 ASP HB3 H 2.54 0.03 1 1027 . 103 ASP H H 8.36 0.01 1 1028 . 103 ASP N N 121.77 0.10 1 1029 . 104 PHE CA C 58.90 0.10 1 1030 . 104 PHE CB C 40.21 0.10 1 1031 . 104 PHE HA H 4.40 0.03 1 1032 . 104 PHE HB2 H 3.14 0.03 2 1033 . 104 PHE HB3 H 3.00 0.03 2 1034 . 104 PHE HD1 H 7.11 0.02 1 1035 . 104 PHE HD2 H 7.11 0.02 1 1036 . 104 PHE HE1 H 7.32 0.02 1 1037 . 104 PHE HE2 H 7.32 0.02 1 1038 . 104 PHE H H 7.68 0.01 1 1039 . 104 PHE HZ H 7.32 0.02 1 1040 . 104 PHE N N 124.74 0.10 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 189 190 '195,195,195,196,196,196' '226,227' '230,230,230,231,231,231' '317,318' '321,321,321,322,322,322' '336,337' '342,342,342,343,343,343' '392,393' '396,396,396,397,397,397' '423,424' '429,429,429,430,430,430' '431,432' '569,570' '575,575,575,576,576,576' '655,656' '661,661,661,662,662,662' '705,706' '711,711,711,712,712,712' '741,742' '871,872' '877,877,877,878,878,878' '937,938' '978,979' '982,982,982,983,983,983' '991,992' '1032,1033' '4,25,86,115,126,137,148,454,944' '134,145' '135,146' '136,147' '138,149' '139,140,150,151' '141,142,152,153' '143,154' '144,155' '165,328,348,355,403' '166,356' '167,168,350,351,357,358,405,406' '180,217,237,445' '191,338,425,571,657,707,873' '197,344,431,577,663,713,879' '203,290,304,691' '204,291,305,692' '208,209,295,296,309,310,696,697' '246,362,410,481,592,773,910,1011' '247,363,411,482,593,774,911,1012' '251,251,251,367,367,367,415,415,415,486,486,486,597,597,597,778,778,778,915,915,915,1016,1016,1016' '266,382,583,619,669,680,860,989,1000' '330,331,332,333' '630,810,885,961' '631,811,886,962' '632,812,887,963' '638,639,818,819,893,894,969,970' stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants_label _Saveframe_category coupling_constants _Details ; # about the data. Quantitative coupling constants 3J(HNHalpha) (Hz) as measured by a 3D HNHA experiment on the [U-15N] labeled sample. Software used: UXNMR (processing), XEASY (analysis, peak integration) Remarks: - For Gly52,Gly86,Gly88 and Gly97 the average value 3JHNHA for both the overlapping HA2 and HA3 signals (indicated by HA*) is given. - Gln17 and Gln18 have near-identical HN, N and HA resonance frequencies. 3JHNHA of Gln17 and Gln18 are therefore indistinguishable from one another. The average value for both residues is listed instead. - 3JHNHA of residues Met1 and Gln2 are not given, because of missing amide proton signals in the proton dimension of the 3D HNHA spectrum. - In the case of overlapping diagonal peaks in the HNHA spectrum, an average intensity for the reference diagonal peak was taken as best approximation. - For residues 95,97-104 the 3J(HNHalpha) coupling constant was determined directly by taking slices through the amide proton signals from a high-resolution 15N-1H HSQC, recorded on the [U-15N]-labeled sample. - Comparison of the 3JHNHA values derived directly and calculated from the HNHA measurement show on average an absolute error of about 0.5 Hz in the determination of the 3JHNHA coupling constant. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $conditions_1 _Spectrometer_frequency_1H . _Mol_system_component_name 'Sml1 protein' _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 ASN H 3 ASN HA 6.53 . . 0.5 2 3JHNHA 4 SER H 4 SER HA 4.88 . . 0.5 3 3JHNHA 5 GLN H 5 GLN HA 6.79 . . 0.5 4 3JHNHA 6 ASP H 6 ASP HA 6.17 . . 0.5 5 3JHNHA 7 TYR H 7 TYR HA 6.22 . . 0.5 6 3JHNHA 8 PHE H 8 PHE HA 5.99 . . 0.5 7 3JHNHA 9 TYR H 9 TYR HA 6.21 . . 0.5 8 3JHNHA 10 ALA H 10 ALA HA 5.17 . . 0.5 9 3JHNHA 11 GLN H 11 GLN HA 5.94 . . 1.0 10 3JHNHA 12 ASN H 12 ASN HA 7.82 . . 1.0 11 3JHNHA 13 ARG H 13 ARG HA 6.87 . . 0.5 12 3JHNHA 14 CYS H 14 CYS HA 4.35 . . 0.5 13 3JHNHA 15 GLN H 15 GLN HA 6.01 . . 0.5 14 3JHNHA 16 GLN H 16 GLN HA 6.16 . . 0.5 15 3JHNHA 17 GLN H 17 GLN HA 7.23 . . 0.5 16 3JHNHA 18 GLN H 18 GLN HA 7.23 . . 0.5 17 3JHNHA 19 ALA H 19 ALA HA 5.01 . . 0.5 18 3JHNHA 21 SER H 21 SER HA 6.32 . . 0.5 19 3JHNHA 22 THR H 22 THR HA 8.00 . . 0.5 20 3JHNHA 23 LEU H 23 LEU HA 6.33 . . 0.5 21 3JHNHA 24 ARG H 24 ARG HA 6.39 . . 0.5 22 3JHNHA 25 THR H 25 THR HA 7.26 . . 0.5 23 3JHNHA 26 VAL H 26 VAL HA 6.85 . . 0.5 24 3JHNHA 27 THR H 27 THR HA 7.44 . . 0.5 25 3JHNHA 28 MET H 28 MET HA 5.67 . . 0.5 26 3JHNHA 29 ALA H 29 ALA HA 5.03 . . 0.5 27 3JHNHA 30 GLU H 30 GLU HA 5.17 . . 0.5 28 3JHNHA 31 PHE H 31 PHE HA 6.13 . . 0.5 29 3JHNHA 32 ARG H 32 ARG HA 7.37 . . 0.5 30 3JHNHA 33 ARG H 33 ARG HA 6.55 . . 0.5 31 3JHNHA 34 VAL H 34 VAL HA 7.38 . . 0.5 32 3JHNHA 36 LEU H 36 LEU HA 5.87 . . 0.5 33 3JHNHA 39 MET H 39 MET HA 5.94 . . 0.5 34 3JHNHA 40 ALA H 40 ALA HA 6.14 . . 0.5 35 3JHNHA 41 GLU H 41 GLU HA 6.36 . . 0.5 36 3JHNHA 42 VAL H 42 VAL HA 7.72 . . 0.5 37 3JHNHA 44 MET H 44 MET HA 6.37 . . 0.5 38 3JHNHA 45 LEU H 45 LEU HA 6.63 . . 0.5 39 3JHNHA 46 SER H 46 SER HA 5.97 . . 0.5 40 3JHNHA 47 THR H 47 THR HA 7.47 . . 0.5 41 3JHNHA 48 GLN H 48 GLN HA 5.96 . . 0.5 42 3JHNHA 49 ASN H 49 ASN HA 7.18 . . 0.5 43 3JHNHA 50 SER H 50 SER HA 6.31 . . 0.5 44 3JHNHA 51 MET H 51 MET HA 7.20 . . 0.5 45 3JHNHA 52 GLY H 52 GLY HA* 5.17 . . 0.5 46 3JHNHA 53 SER H 53 SER HA 6.55 . . 0.5 47 3JHNHA 54 SER H 54 SER HA 6.09 . . 0.5 48 3JHNHA 55 ALA H 55 ALA HA 5.48 . . 0.5 49 3JHNHA 56 SER H 56 SER HA 6.65 . . 0.5 50 3JHNHA 57 ALA H 57 ALA HA 5.94 . . 0.5 51 3JHNHA 58 SER H 58 SER HA 6.38 . . 0.5 52 3JHNHA 59 ALA H 59 ALA HA 5.71 . . 0.5 53 3JHNHA 60 SER H 60 SER HA 6.20 . . 0.5 54 3JHNHA 61 SER H 61 SER HA 6.29 . . 0.5 55 3JHNHA 62 LEU H 62 LEU HA 5.78 . . 0.5 56 3JHNHA 63 GLU H 63 GLU HA 5.84 . . 0.5 57 3JHNHA 64 MET H 64 MET HA 6.55 . . 0.5 58 3JHNHA 65 TRP H 65 TRP HA 5.20 . . 0.5 59 3JHNHA 66 GLU H 66 GLU HA 3.90 . . 0.5 60 3JHNHA 67 LYS H 67 LYS HA 5.25 . . 0.5 61 3JHNHA 68 ASP H 68 ASP HA 4.68 . . 0.5 62 3JHNHA 69 LEU H 69 LEU HA 4.60 . . 0.5 63 3JHNHA 70 GLU H 70 GLU HA 5.41 . . 0.5 64 3JHNHA 71 GLU H 71 GLU HA 5.37 . . 0.5 65 3JHNHA 72 ARG H 72 ARG HA 5.48 . . 0.5 66 3JHNHA 73 LEU H 73 LEU HA 6.00 . . 0.5 67 3JHNHA 74 ASN H 74 ASN HA 6.38 . . 0.5 68 3JHNHA 75 SER H 75 SER HA 6.31 . . 0.5 69 3JHNHA 76 ILE H 76 ILE HA 6.66 . . 0.5 70 3JHNHA 77 ASP H 77 ASP HA 6.60 . . 0.5 71 3JHNHA 78 HIS H 78 HIS HA 6.69 . . 0.5 72 3JHNHA 79 ASP H 79 ASP HA 6.17 . . 0.5 73 3JHNHA 80 MET H 80 MET HA 5.66 . . 0.5 74 3JHNHA 81 ASN H 81 ASN HA 7.14 . . 0.5 75 3JHNHA 82 ASN H 82 ASN HA 7.48 . . 0.5 76 3JHNHA 83 ASN H 83 ASN HA 7.19 . . 0.5 77 3JHNHA 84 LYS H 84 LYS HA 6.47 . . 0.5 78 3JHNHA 85 PHE H 85 PHE HA 6.32 . . 0.5 79 3JHNHA 86 GLY H 86 GLY HA* 7.36 . . 0.5 80 3JHNHA 87 SER H 87 SER HA 6.22 . . 0.5 81 3JHNHA 88 GLY H 88 GLY HA* 7.13 . . 0.5 82 3JHNHA 89 GLU H 89 GLU HA 6.36 . . 0.5 83 3JHNHA 90 LEU H 90 LEU HA 6.05 . . 0.5 84 3JHNHA 91 LYS H 91 LYS HA 7.45 . . 0.5 85 3JHNHA 92 SER H 92 SER HA 6.21 . . 0.5 86 3JHNHA 93 MET H 93 MET HA 6.00 . . 0.5 87 3JHNHA 94 PHE H 94 PHE HA 6.30 . . 0.5 88 3JHNHA 95 ASN H 95 ASN HA 5.74 . . 0.5 89 3JHNHA 96 GLN H 96 GLN HA 5.84 . . 0.5 90 3JHNHA 97 GLY H 97 GLY HA* 7.44 . . 0.5 91 3JHNHA 98 LYS H 98 LYS HA 6.80 . . 0.5 92 3JHNHA 99 VAL H 99 VAL HA 7.35 . . 0.5 93 3JHNHA 100 GLU H 100 GLU HA 6.30 . . 0.5 94 3JHNHA 101 GLU H 101 GLU HA 6.96 . . 0.5 95 3JHNHA 102 MET H 102 MET HA 7.48 . . 0.5 96 3JHNHA 103 ASP H 103 ASP HA 7.62 . . 0.5 97 3JHNHA 104 PHE H 104 PHE HA 7.93 . . 0.5 stop_ save_