data_4955 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Structure of Cysteinyl-phosphorylated Enzyme IIB of the N,N'-diacetylchitobiose-specific Phosphoenolpyruvate-dependent Phosphotransferase System of Escherichia coli ; _BMRB_accession_number 4955 _BMRB_flat_file_name bmr4955.str _Entry_type original _Submission_date 2001-02-07 _Accession_date 2001-02-07 _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 Ab Eiso . . 2 Schuurman-Wolters Gea K. . 3 Nijlant Dieter . . 4 Dijkstra Klaas . . 5 Saier Milton H. Jr. 6 Robillard George T. . 7 Scheek Ruud M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 623 "13C chemical shifts" 482 "15N chemical shifts" 114 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-28 update BMRB 'Updating non-standard residue' 2001-08-22 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Structure of Cysteinyl-phosphorylated Enzyme IIB of the N,N'-diacetylchitobiose-specific Phosphoenolpyruvate-dependent Phosphotransferase System of Escherichia coli ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21251097 _PubMed_ID 11352587 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ab Eiso . . 2 Schuurman-Wolters Gea K. . 3 Nijlant Dieter . . 4 Dijkstra Klaas . . 5 Saier Milton H. Jr. 6 Robillard George T. . 7 Scheek Ruud M. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 308 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 993 _Page_last 1009 _Year 2001 _Details . loop_ _Keyword 'ambiguous restraints' chitobiose cysteinyl-phosphate IIB-chitobiose phosphocysteine PTS stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Eiso AB and Gea K. Schuurman-Wolters and Saier, Jr., Milton H. and Jonathan Reizer and Michel Jacuinod and Peter Roepstorff. Enzyme IIB-cellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli: backbone assignment and secondary structure determined by three-dimensional NMR spectroscopy Protein Sci. 1994. 3(2):282-290 ; _Citation_title 'Enzyme IIBcellobiose of the phosphoenol-pyruvate-dependent phosphotransferase system of Escherichia coli: backbone assignment and secondary structure determined by three-dimensional NMR spectroscopy.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8003964 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ab E. . . 2 Schuurman-Wolters G.K. K. . 3 Saier M.H. H. . 4 Reizer J. . . 5 Jacuinod M. . . 6 Roepstorff P. . . 7 Dijkstra K. . . 8 Scheek R.M. M. . 9 Robillard G.T. T. . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein science : a publication of the Protein Society' _Journal_volume 3 _Journal_issue 2 _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 282 _Page_last 290 _Year 1994 _Details ; The assignment of backbone resonances and the secondary structure determination of the Cys 10 Ser mutant of enzyme IIBcellobiose of the Escherichia coli cellobiose-specific phosphoenol-pyruvate-dependent phosphotransferase system are presented. The backbone resonances were assigned using 4 triple resonance experiments, the HNCA and HN(CO)CA experiments, correlating backbone 1H, 15N, and 13C alpha resonances, and the HN(CA)CO and HNCO experiments, correlating backbone 1H,15N and 13CO resonances. Heteronuclear 1H-NOE 1H-15N single quantum coherence (15N-NOESY-HSQC) spectroscopy and heteronuclear 1H total correlation 1H-15N single quantum coherence (15N-TOCSY-HSQC) spectroscopy were used to resolve ambiguities arising from overlapping 13C alpha and 13CO frequencies and to check the assignments from the triple resonance experiments. This procedure, together with a 3-dimensional 1H alpha-13C alpha-13CO experiment (COCAH), yielded the assignment for all observed backbone resonances. The secondary structure was determined using information both from the deviation of observed 1H alpha and 13C alpha chemical shifts from their random coil values and 1H-NOE information from the 15N-NOESY-HSQC. These data show that enzyme IIBcellobiose consists of a 4-stranded parallel beta-sheet and 5 alpha-helices. In the wild-type enzyme IIBcellobiose, the catalytic residue appears to be located at the end of a beta-strand. ; save_ save_citation_two _Saveframe_category citation _Citation_full ; Eiso AB and Gea K. Schuurman-Wolters and Jonathan Reizer and Saier, Jr., Milton H. and Klaas Dijkstra and Ruud M. Scheek and George T. Robillard. The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli. Protein Sci. 1997. 6(2):304-314 ; _Citation_title 'The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9041631 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ab E. . . 2 Schuurman-Wolters G. . . 3 Reizer J. . . 4 Saier M.H. H. . 5 Dijkstra K. . . 6 Scheek R.M. M. . 7 Robillard G.T. T. . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein science : a publication of the Protein Society' _Journal_volume 6 _Journal_issue 2 _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 304 _Page_last 314 _Year 1997 _Details ; The assignment of the side-chain NMR resonances and the determination of the three-dimensional solution structure of the C10S mutant of enzyme IIBcellobiose (IIBcel) of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli are presented. The side-chain resonances were assigned nearly completely using a variety of mostly heteronuclear NMR experiments, including HCCH-TOCSY, HCCH-COSY, and COCCH-TOCSY experiments as well as CBCACOHA, CBCA(CO)NH, and HBHA(CBCA)(CO)NH experiments. In order to obtain the three-dimensional structure, NOE data were collected from 15N-NOESY-HSQC, 13C-HSQC-NOESY, and 2D NOE experiments. The distance restraints derived from these NOE data were used in distance geometry calculations followed by molecular dynamics and simulated annealing protocols. In an iterative procedure, additional NOE assignments were derived from the calculated structures and new structures were calculated. The final set of structures, calculated with approximately 2000 unambiguous and ambiguous distance restraints, has an rms deviation of 1.1 A on C alpha atoms. IIBcel consists of a four stranded parallel beta-sheet, in the order 2134. The sheet is flanked with two and three alpha-helices on either side. Residue 10, a cysteine in the wild-type enzyme, which is phosphorylated during the catalytic cycle, is located at the end of the first beta-strand. A loop that is proposed to be involved in the binding of the phosphoryl-group follows the cysteine. The loop appears to be disordered in the unphosphorylated state. ; save_ ################################## # Molecular system description # ################################## save_system_PIIBchb _Saveframe_category molecular_system _Mol_system_name 'Cysteinyl-phosphorylated enzyme IIB' _Abbreviation_common phospho-IIB-chitobiose _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label phospho-IIB-chitobiose $PIIBchb stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details 'IIB-chitobiose of E. coli phosphorylated at residue Cys10' save_ ######################## # Monomeric polymers # ######################## save_PIIBchb _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common phospho-IIB-chitobiose _Abbreviation_common IIBchb _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 106 _Mol_residue_sequence ; MEKKHIYLFXSAGMSTSLLV SKMRAQAEKYEVPVIIEAFP ETLAGEKGQNADVVLLGPQI AYMLPEIQRLLPNKPVEVID SLLYGKVDGLGVLKAAVAAI KKAAAN ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLU 3 LYS 4 LYS 5 HIS 6 ILE 7 TYR 8 LEU 9 PHE 10 CSP 11 SER 12 ALA 13 GLY 14 MET 15 SER 16 THR 17 SER 18 LEU 19 LEU 20 VAL 21 SER 22 LYS 23 MET 24 ARG 25 ALA 26 GLN 27 ALA 28 GLU 29 LYS 30 TYR 31 GLU 32 VAL 33 PRO 34 VAL 35 ILE 36 ILE 37 GLU 38 ALA 39 PHE 40 PRO 41 GLU 42 THR 43 LEU 44 ALA 45 GLY 46 GLU 47 LYS 48 GLY 49 GLN 50 ASN 51 ALA 52 ASP 53 VAL 54 VAL 55 LEU 56 LEU 57 GLY 58 PRO 59 GLN 60 ILE 61 ALA 62 TYR 63 MET 64 LEU 65 PRO 66 GLU 67 ILE 68 GLN 69 ARG 70 LEU 71 LEU 72 PRO 73 ASN 74 LYS 75 PRO 76 VAL 77 GLU 78 VAL 79 ILE 80 ASP 81 SER 82 LEU 83 LEU 84 TYR 85 GLY 86 LYS 87 VAL 88 ASP 89 GLY 90 LEU 91 GLY 92 VAL 93 LEU 94 LYS 95 ALA 96 ALA 97 VAL 98 ALA 99 ALA 100 ILE 101 LYS 102 LYS 103 ALA 104 ALA 105 ALA 106 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1E2B "Nmr Structure Of The C10s Mutant Of Enzyme Iib Cellobiose Of The Phosphoenol-Pyruvate Dependent Phosphotransferase System Of Es" 99.06 106 99.05 99.05 6.78e-66 PDB 1H9C "Nmr Structure Of Cysteinyl-Phosphorylated Enzyme Iib Of The N,N'-Diacetylchitobiose Specific Phosphoenolpyruvate-Dependent Phos" 100.00 106 100.00 100.00 1.38e-66 PDB 1IIB "Crystal Structure Of Iibcellobiose From Escherichia Coli" 100.00 106 99.06 99.06 6.64e-67 PDB 2WWV "Nmr Structure Of The Iiachitobiose-Iibchitobiose Complex Of The N,N'-Diacetylchitoboise Brance Of The E. Coli Phosphotransferas" 97.17 103 99.03 99.03 3.77e-64 PDB 2WY2 "Nmr Structure Of The Iiachitobiose-Iibchitobiose Phosphoryl Transition State Complex Of The N,N'-Diacetylchitoboise Brance Of T" 97.17 103 99.03 99.03 4.11e-64 DBJ BAA15519 "N,N'-diacetylchitobiose-specific enzyme IIB component of PTS [Escherichia coli str. K-12 substr. W3110]" 100.00 106 99.06 99.06 8.17e-67 DBJ BAB35867 "PEP-dependent phosphotransferase enzyme IV for cellobiose [Escherichia coli O157:H7 str. Sakai]" 100.00 106 99.06 99.06 8.17e-67 DBJ BAG77432 "PTS system cellobiose-specific IIB component [Escherichia coli SE11]" 100.00 106 99.06 99.06 8.17e-67 DBJ BAI25754 "N,N'-diacetylchitobiose-specific enzyme IIB component of PTS [Escherichia coli O26:H11 str. 11368]" 100.00 106 99.06 99.06 8.17e-67 DBJ BAI30732 "N,N'-diacetylchitobiose-specific enzyme IIB component of PTS [Escherichia coli O103:H2 str. 12009]" 100.00 106 99.06 99.06 8.17e-67 EMBL CAA37069 "unnamed protein product [Escherichia coli]" 100.00 106 99.06 99.06 8.17e-67 EMBL CAP76232 "N,N'-diacetylchitobiose-specific phosphotransferase [Escherichia coli LF82]" 100.00 106 99.06 99.06 8.17e-67 EMBL CAQ32212 "chbB, subunit of EIIChb [Escherichia coli BL21(DE3)]" 100.00 106 99.06 99.06 8.17e-67 EMBL CAQ98655 "N,N'-diacetylchitobiose-specific enzyme IIB component of PTS [Escherichia coli IAI1]" 100.00 106 99.06 99.06 8.17e-67 EMBL CAR03098 "N,N'-diacetylchitobiose-specific enzyme IIB component of PTS [Escherichia coli S88]" 100.00 106 99.06 99.06 8.17e-67 GB AAC74808 "N,N'-diacetylchitobiose-specific enzyme IIB component of PTS [Escherichia coli str. K-12 substr. MG1655]" 100.00 106 99.06 99.06 8.17e-67 GB AAG56724 "PEP-dependent phosphotransferase enzyme IV for cellobiose, arbutin, and salicin [Escherichia coli O157:H7 str. EDL933]" 100.00 106 99.06 99.06 8.17e-67 GB AAN43080 "PEP-dependent phosphotransferase enzyme IV for cellobiose, arbutin, and salicin [Shigella flexneri 2a str. 301]" 100.00 106 98.11 98.11 8.34e-66 GB AAN80596 "PTS system, cellobiose-specific IIB component [Escherichia coli CFT073]" 100.00 106 99.06 99.06 8.17e-67 GB AAP16973 "PEP-dependent phosphotransferase enzyme IV for cellobiose, arbutin, and salicin [Shigella flexneri 2a str. 2457T]" 100.00 106 98.11 98.11 8.34e-66 REF NP_288171 "PTS system N,N'-diacetylchitobiose-specific transporter subunit IIB [Escherichia coli O157:H7 str. EDL933]" 100.00 106 99.06 99.06 8.17e-67 REF NP_310471 "PTS system N,N'-diacetylchitobiose-specific transporter subunit IIB [Escherichia coli O157:H7 str. Sakai]" 100.00 106 99.06 99.06 8.17e-67 REF NP_416252 "N,N'-diacetylchitobiose-specific enzyme IIB component of PTS [Escherichia coli str. K-12 substr. MG1655]" 100.00 106 99.06 99.06 8.17e-67 REF NP_707373 "PTS system N,N'-diacetylchitobiose-specific transporter subunit IIB [Shigella flexneri 2a str. 301]" 100.00 106 98.11 98.11 8.34e-66 REF NP_754031 "PTS system N,N'-diacetylchitobiose-specific transporter subunit IIB [Escherichia coli CFT073]" 100.00 106 99.06 99.06 8.17e-67 SP P69795 "RecName: Full=N,N'-diacetylchitobiose-specific phosphotransferase enzyme IIB component; AltName: Full=PTS system N,N'-diacetylc" 100.00 106 99.06 99.06 8.17e-67 SP P69796 "RecName: Full=N,N'-diacetylchitobiose-specific phosphotransferase enzyme IIB component; AltName: Full=PTS system N,N'-diacetylc" 100.00 106 99.06 99.06 8.17e-67 SP P69830 "RecName: Full=N,N'-diacetylchitobiose-specific phosphotransferase enzyme IIB component; AltName: Full=PTS system N,N'-diacetylc" 100.00 106 99.06 99.06 8.17e-67 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_CSP _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common S-PHOSPHOCYSTEINE _BMRB_code . _PDB_code CSP _Standard_residue_derivative . _Molecular_mass 201.138 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jul 21 09:45:08 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? SG SG S . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HXT HXT H . 0 . ? HO2P HO2P H . 0 . ? HO3P HO3P H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H ? ? SING N H2 ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB SG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING SG P ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HO2P ? ? SING O3P HO3P ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PIIBchb E.coli 562 Bacteria . Escherichia coli 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 $PIIBchb 'recombinant technology' 'E. coli' Escherichia coli K12 W3110 plasmid pJR-BLIIB stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PIIBchb 4 mM '[U-15N; U-13C]' 'Enzyme I' 23 uM . HPr 34 uM . IIAchb 20 uM . PEP 100 mM . 'Tris-Acetate buffer' 100 mM . NaCl 100 mM . DTT 5 mM . MgCl2 4 mM . Glycerol 1.5 % [U-2H] 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_NMR_applied_experiment_1 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_Sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.2 n/a temperature 295 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 . indirect . . . 1.0 DSS N 15 'methyl protons' ppm 0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details ; The ppm-value is filled with the median of the observed values. the field Error-ppm is filled with the rms-value of the observed values. sample conditions are not very well defined as there is a reaction taking place causing pH shifts. most of the H/C chemical shift statistics however come from one spectrum. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $Sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name phospho-IIB-chitobiose _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 MET C C 175.751 0.044 1 2 . 1 MET H H 8.484 0.025 1 3 . 1 MET N N 128.449 0.055 1 4 . 1 MET CA C 54.168 0.060 1 5 . 1 MET CB C 33.367 0.032 1 6 . 1 MET CE C 17.018 0.162 1 7 . 1 MET HA H 4.541 0.005 1 8 . 1 MET HB2 H 2.100 0.010 2 9 . 1 MET HB3 H 2.021 0.025 2 10 . 1 MET HE H 2.120 0.007 1 11 . 2 GLU C C 176.145 0.028 1 12 . 2 GLU H H 8.605 0.004 1 13 . 2 GLU N N 122.673 0.023 1 14 . 2 GLU CA C 56.510 0.002 1 15 . 2 GLU CB C 30.010 0.1 1 16 . 2 GLU CD C 184.017 0.025 1 17 . 2 GLU CG C 36.210 0.147 1 18 . 2 GLU HA H 4.294 0.004 1 19 . 2 GLU HB2 H 2.012 0.025 1 20 . 2 GLU HB3 H 2.012 0.025 1 21 . 2 GLU HG2 H 2.303 0.025 1 22 . 2 GLU HG3 H 2.303 0.025 1 23 . 3 LYS C C 176.668 0.022 1 24 . 3 LYS H H 8.319 0.050 1 25 . 3 LYS N N 121.642 0.089 1 26 . 3 LYS CA C 56.041 0.033 1 27 . 3 LYS CB C 34.219 0.047 1 28 . 3 LYS CD C 29.639 0.018 1 29 . 3 LYS CE C 42.294 0.057 1 30 . 3 LYS CG C 26.019 0.031 1 31 . 3 LYS HA H 4.392 0.007 1 32 . 3 LYS HB2 H 1.610 0.006 2 33 . 3 LYS HB3 H 1.375 0.009 2 34 . 3 LYS HD2 H 1.467 0.004 1 35 . 3 LYS HD3 H 1.467 0.004 1 36 . 3 LYS HE2 H 2.933 0.025 1 37 . 3 LYS HE3 H 2.933 0.025 1 38 . 3 LYS HG2 H 1.476 0.010 2 39 . 3 LYS HG3 H 1.081 0.007 2 40 . 4 LYS C C 175.844 0.056 1 41 . 4 LYS H H 7.991 0.002 1 42 . 4 LYS N N 120.351 0.168 1 43 . 4 LYS CA C 54.061 0.070 1 44 . 4 LYS CB C 33.927 0.034 1 45 . 4 LYS CD C 24.913 0.036 1 46 . 4 LYS CE C 42.555 0.1 1 47 . 4 LYS CG C 28.566 0.022 1 48 . 4 LYS HA H 4.669 0.006 1 49 . 4 LYS HB2 H 1.787 0.013 1 50 . 4 LYS HB3 H 1.573 0.006 1 51 . 4 LYS HD2 H 1.596 0.025 1 52 . 4 LYS HD3 H 1.596 0.025 1 53 . 4 LYS HE2 H 2.928 0.003 2 54 . 4 LYS HE3 H 2.931 0.003 2 55 . 4 LYS HG2 H 1.652 0.001 2 56 . 4 LYS HG3 H 1.448 0.011 2 57 . 5 HIS C C 174.817 0.124 1 58 . 5 HIS H H 10.615 0.003 1 59 . 5 HIS N N 122.997 0.492 1 60 . 5 HIS CA C 55.881 0.013 1 61 . 5 HIS CB C 31.414 0.020 1 62 . 5 HIS HA H 5.092 0.003 1 63 . 5 HIS CD2 C 119.130 0.1 1 64 . 5 HIS HB2 H 3.035 0.003 1 65 . 5 HIS HB3 H 2.415 0.003 1 66 . 5 HIS HD2 H 7.120 0.025 1 67 . 6 ILE C C 173.495 0.025 1 68 . 6 ILE H H 9.492 0.001 1 69 . 6 ILE N N 127.007 0.060 1 70 . 6 ILE CA C 60.392 0.060 1 71 . 6 ILE CB C 39.203 0.016 1 72 . 6 ILE HA H 4.421 0.004 1 73 . 6 ILE HB H 1.930 0.004 1 74 . 6 ILE CG1 C 26.066 0.043 1 75 . 6 ILE CG2 C 17.340 0.027 1 76 . 6 ILE HD1 H 0.633 0.003 1 77 . 6 ILE HG12 H 1.418 0.009 2 78 . 6 ILE HG13 H 0.827 0.001 2 79 . 6 ILE HG2 H 0.718 0.010 1 80 . 7 TYR C C 173.724 0.060 1 81 . 7 TYR H H 8.037 0.003 1 82 . 7 TYR N N 125.049 0.085 1 83 . 7 TYR CA C 51.871 0.044 1 84 . 7 TYR CB C 40.571 0.046 1 85 . 7 TYR CD1 C 131.338 0.028 2 86 . 7 TYR CE1 C 119.400 0.082 2 87 . 7 TYR HA H 6.191 0.005 1 88 . 7 TYR HB2 H 3.069 0.005 2 89 . 7 TYR HB3 H 2.952 0.003 2 90 . 7 TYR HD1 H 7.054 0.021 2 91 . 7 TYR HE1 H 6.926 0.006 2 92 . 8 LEU C C 175.969 0.036 1 93 . 8 LEU H H 8.902 0.002 1 94 . 8 LEU N N 124.320 0.031 1 95 . 8 LEU CA C 54.466 0.054 1 96 . 8 LEU CB C 45.380 0.047 1 97 . 8 LEU CG C 30.769 0.082 1 98 . 8 LEU HA H 5.684 0.005 1 99 . 8 LEU HG H 1.784 0.006 1 100 . 8 LEU CD1 C 25.867 0.047 1 101 . 8 LEU CD2 C 27.773 0.076 1 102 . 8 LEU HB2 H 1.564 0.005 2 103 . 8 LEU HB3 H 1.300 0.007 2 104 . 8 LEU HD1 H 0.807 0.023 1 105 . 8 LEU HD2 H 0.798 0.010 1 106 . 9 PHE C C 175.673 0.030 1 107 . 9 PHE H H 8.670 0.002 1 108 . 9 PHE N N 114.781 0.050 1 109 . 9 PHE CA C 56.251 0.079 1 110 . 9 PHE CB C 43.193 0.021 1 111 . 9 PHE CD1 C 132.796 0.053 2 112 . 9 PHE CE1 C 131.090 0.070 2 113 . 9 PHE CZ C 127.603 0.050 1 114 . 9 PHE HA H 5.814 0.010 1 115 . 9 PHE HZ H 6.819 0.008 1 116 . 9 PHE HB2 H 2.662 0.002 2 117 . 9 PHE HB3 H 2.660 0.002 2 118 . 9 PHE HD1 H 7.200 0.006 2 119 . 9 PHE HE1 H 6.934 0.012 2 120 . 10 CSP C C 172.988 0.031 1 121 . 10 CSP H H 7.897 0.003 1 122 . 10 CSP N N 115.838 0.061 1 123 . 10 CSP CA C 57.023 0.049 1 124 . 10 CSP CB C 33.282 0.042 1 125 . 10 CSP HA H 4.709 0.008 1 126 . 10 CSP HB2 H 3.557 0.009 1 127 . 10 CSP HB3 H 3.283 0.007 1 128 . 11 SER C C 175.618 0.029 1 129 . 11 SER H H 9.567 0.003 1 130 . 11 SER N N 120.218 0.028 1 131 . 11 SER CA C 63.802 0.035 1 132 . 11 SER CB C 63.218 0.108 1 133 . 11 SER HA H 4.469 0.006 1 134 . 11 SER HB2 H 4.042 0.004 2 135 . 11 SER HB3 H 4.045 0.005 2 136 . 12 ALA C C 178.807 0.032 1 137 . 12 ALA H H 10.620 0.004 1 138 . 12 ALA N N 122.051 0.031 1 139 . 12 ALA CA C 52.248 0.036 1 140 . 12 ALA CB C 19.930 0.052 1 141 . 12 ALA HA H 4.701 0.011 1 142 . 12 ALA HB H 1.619 0.002 1 143 . 13 GLY C C 173.825 0.039 1 144 . 13 GLY H H 8.300 0.004 1 145 . 13 GLY N N 109.957 0.070 1 146 . 13 GLY CA C 45.157 0.046 1 147 . 13 GLY HA2 H 3.691 0.025 1 148 . 13 GLY HA3 H 3.691 0.025 1 149 . 14 MET C C 178.659 0.1 1 150 . 14 MET H H 8.676 0.001 1 151 . 14 MET N N 119.253 0.068 1 152 . 14 MET CA C 56.777 0.029 1 153 . 14 MET CB C 34.426 0.047 1 154 . 14 MET CE C 17.018 0.162 1 155 . 14 MET CG C 31.877 0.016 1 156 . 14 MET HA H 4.656 0.006 1 157 . 14 MET HB2 H 2.067 0.002 2 158 . 14 MET HB3 H 2.002 0.002 2 159 . 14 MET HG2 H 2.603 0.002 2 160 . 14 MET HG3 H 2.412 0.006 2 161 . 14 MET HE H 2.098 0.025 1 162 . 15 SER C C 176.025 0.013 1 163 . 15 SER H H 10.736 0.025 1 164 . 15 SER N N 121.902 0.1 1 165 . 15 SER CA C 62.241 0.1 1 166 . 15 SER CB C 62.131 0.090 1 167 . 15 SER HA H 4.315 0.025 1 168 . 15 SER HB2 H 4.290 0.025 2 169 . 15 SER HB3 H 4.079 0.007 2 170 . 16 THR C C 175.558 0.030 1 171 . 16 THR H H 7.557 0.001 1 172 . 16 THR N N 110.474 0.051 1 173 . 16 THR CA C 62.303 0.068 1 174 . 16 THR CB C 69.017 0.051 1 175 . 16 THR HA H 4.029 0.002 1 176 . 16 THR HB H 4.106 0.004 1 177 . 16 THR CG2 C 23.397 0.039 1 178 . 16 THR HG2 H 1.257 0.003 1 179 . 17 SER C C 176.396 0.032 1 180 . 17 SER H H 7.472 0.001 1 181 . 17 SER N N 117.997 0.028 1 182 . 17 SER CA C 62.461 0.054 1 183 . 17 SER CB C 62.563 0.1 1 184 . 17 SER HA H 3.966 0.010 1 185 . 18 LEU C C 178.917 0.008 1 186 . 18 LEU H H 7.986 0.001 1 187 . 18 LEU N N 123.935 0.040 1 188 . 18 LEU CA C 57.853 0.004 1 189 . 18 LEU CB C 41.011 0.032 1 190 . 18 LEU CG C 27.105 0.004 1 191 . 18 LEU HA H 4.213 0.001 1 192 . 18 LEU HG H 1.542 0.007 1 193 . 18 LEU CD1 C 23.580 0.016 2 194 . 18 LEU CD2 C 24.747 0.016 2 195 . 18 LEU HB2 H 1.701 0.025 1 196 . 18 LEU HB3 H 1.701 0.025 1 197 . 18 LEU HD1 H 0.985 0.025 2 198 . 18 LEU HD2 H 0.954 0.012 2 199 . 19 LEU C C 178.681 0.031 1 200 . 19 LEU H H 8.006 0.001 1 201 . 19 LEU N N 120.746 0.023 1 202 . 19 LEU CA C 58.017 0.048 1 203 . 19 LEU CB C 40.685 0.035 1 204 . 19 LEU CG C 27.084 0.1 1 205 . 19 LEU HA H 3.791 0.008 1 206 . 19 LEU HG H 1.468 0.025 1 207 . 19 LEU CD1 C 27.345 0.077 2 208 . 19 LEU CD2 C 22.524 0.061 2 209 . 19 LEU HB2 H 1.454 0.011 1 210 . 19 LEU HB3 H 1.641 0.013 1 211 . 19 LEU HD1 H 0.860 0.016 2 212 . 19 LEU HD2 H 0.653 0.007 2 213 . 20 VAL C C 177.936 0.034 1 214 . 20 VAL H H 8.538 0.001 1 215 . 20 VAL N N 119.194 0.022 1 216 . 20 VAL CA C 67.412 0.051 1 217 . 20 VAL CB C 31.267 0.045 1 218 . 20 VAL HA H 3.462 0.006 1 219 . 20 VAL HB H 2.109 0.008 1 220 . 20 VAL CG1 C 20.956 0.032 1 221 . 20 VAL CG2 C 24.761 0.030 1 222 . 20 VAL HG1 H 0.735 0.005 1 223 . 20 VAL HG2 H 0.897 0.007 1 224 . 21 SER C C 177.857 0.015 1 225 . 21 SER H H 7.939 0.002 1 226 . 21 SER N N 114.993 0.034 1 227 . 21 SER CA C 62.502 0.054 1 228 . 21 SER CB C 62.757 0.070 1 229 . 21 SER HA H 4.105 0.022 1 230 . 21 SER HB2 H 3.913 0.025 2 231 . 22 LYS C C 179.930 0.034 1 232 . 22 LYS H H 8.144 0.003 1 233 . 22 LYS N N 121.796 0.033 1 234 . 22 LYS CA C 59.031 0.028 1 235 . 22 LYS CB C 32.258 0.065 1 236 . 22 LYS CD C 28.759 0.040 1 237 . 22 LYS CE C 42.304 0.029 1 238 . 22 LYS CG C 25.301 0.030 1 239 . 22 LYS HA H 4.285 0.005 1 240 . 22 LYS HB2 H 2.102 0.017 2 241 . 22 LYS HB3 H 1.960 0.009 2 242 . 22 LYS HD2 H 1.830 0.007 2 243 . 22 LYS HD3 H 1.836 0.025 2 244 . 22 LYS HE2 H 3.039 0.025 2 245 . 22 LYS HE3 H 3.038 0.001 2 246 . 22 LYS HG2 H 1.776 0.012 2 247 . 22 LYS HG3 H 1.625 0.008 2 248 . 23 MET C C 178.210 0.022 1 249 . 23 MET H H 9.147 0.002 1 250 . 23 MET N N 120.240 0.062 1 251 . 23 MET CA C 60.316 0.047 1 252 . 23 MET CB C 35.570 0.062 1 253 . 23 MET CE C 16.066 0.016 1 254 . 23 MET CG C 32.660 0.070 1 255 . 23 MET HA H 3.693 0.006 1 256 . 23 MET HB2 H 2.255 0.003 2 257 . 23 MET HB3 H 2.142 0.001 2 258 . 23 MET HG2 H 2.871 0.014 2 259 . 23 MET HG3 H 2.804 0.010 2 260 . 23 MET HE H 1.791 0.003 1 261 . 24 ARG C C 179.072 0.034 1 262 . 24 ARG H H 8.847 0.001 1 263 . 24 ARG N N 118.448 0.049 1 264 . 24 ARG CA C 60.120 0.067 1 265 . 24 ARG CB C 30.650 0.098 1 266 . 24 ARG CD C 44.237 0.037 1 267 . 24 ARG CG C 28.539 0.018 1 268 . 24 ARG HA H 3.897 0.008 1 269 . 24 ARG HE H 6.749 0.027 1 270 . 24 ARG NE N 85.011 0.1 1 271 . 24 ARG HB2 H 1.953 0.008 1 272 . 24 ARG HB3 H 1.933 0.025 1 273 . 24 ARG HD2 H 3.175 0.030 2 274 . 24 ARG HD3 H 3.046 0.002 2 275 . 24 ARG HG2 H 1.981 0.008 2 276 . 24 ARG HG3 H 1.841 0.006 2 277 . 24 ARG HH21 H 6.678 0.001 2 278 . 24 ARG HH22 H 6.826 0.002 2 279 . 25 ALA C C 181.488 0.033 1 280 . 25 ALA H H 7.741 0.001 1 281 . 25 ALA N N 121.457 0.025 1 282 . 25 ALA CA C 55.179 0.069 1 283 . 25 ALA CB C 18.127 0.005 1 284 . 25 ALA HA H 4.270 0.009 1 285 . 25 ALA HB H 1.604 0.002 1 286 . 26 GLN C C 177.448 0.034 1 287 . 26 GLN H H 7.910 0.002 1 288 . 26 GLN N N 117.630 0.057 1 289 . 26 GLN CA C 57.726 0.107 1 290 . 26 GLN CB C 27.667 0.065 1 291 . 26 GLN CD C 177.704 0.002 1 292 . 26 GLN CG C 32.688 0.038 1 293 . 26 GLN HA H 4.249 0.013 1 294 . 26 GLN HB2 H 2.340 0.010 2 295 . 26 GLN HB3 H 1.953 0.008 2 296 . 26 GLN HG2 H 2.842 0.003 2 297 . 26 GLN HG3 H 2.152 0.004 2 298 . 26 GLN NE2 N 111.758 0.089 1 299 . 26 GLN HE21 H 7.537 0.003 1 300 . 26 GLN HE22 H 6.844 0.003 1 301 . 27 ALA C C 179.699 0.029 1 302 . 27 ALA H H 8.677 0.002 1 303 . 27 ALA N N 122.322 0.034 1 304 . 27 ALA CA C 55.300 0.049 1 305 . 27 ALA CB C 17.678 0.064 1 306 . 27 ALA HA H 3.953 0.007 1 307 . 27 ALA HB H 1.557 0.004 1 308 . 28 GLU C C 179.495 0.011 1 309 . 28 GLU H H 7.959 0.002 1 310 . 28 GLU N N 116.878 0.042 1 311 . 28 GLU CA C 58.959 0.063 1 312 . 28 GLU CB C 29.595 0.021 1 313 . 28 GLU CD C 183.529 0.025 1 314 . 28 GLU CG C 36.282 0.114 1 315 . 28 GLU HA H 4.130 0.005 1 316 . 28 GLU HB2 H 2.115 0.001 1 317 . 28 GLU HB3 H 2.120 0.003 1 318 . 28 GLU HG2 H 2.409 0.014 2 319 . 28 GLU HG3 H 2.254 0.013 2 320 . 29 LYS C C 177.701 0.021 1 321 . 29 LYS H H 7.690 0.002 1 322 . 29 LYS N N 121.087 0.103 1 323 . 29 LYS CA C 59.157 0.071 1 324 . 29 LYS CB C 32.599 0.031 1 325 . 29 LYS CD C 29.425 0.032 1 326 . 29 LYS CE C 42.114 0.081 1 327 . 29 LYS CG C 24.400 0.029 1 328 . 29 LYS HA H 3.911 0.006 1 329 . 29 LYS HB2 H 1.743 0.025 1 330 . 29 LYS HB3 H 1.743 0.025 1 331 . 29 LYS HD2 H 1.516 0.005 1 332 . 29 LYS HD3 H 1.516 0.005 1 333 . 29 LYS HE2 H 2.828 0.025 2 334 . 29 LYS HE3 H 2.825 0.003 2 335 . 29 LYS HG2 H 1.091 0.003 2 336 . 29 LYS HG3 H 0.494 0.006 2 337 . 30 TYR C C 173.618 0.044 1 338 . 30 TYR H H 7.768 0.003 1 339 . 30 TYR N N 113.678 0.060 1 340 . 30 TYR CA C 58.480 0.039 1 341 . 30 TYR CB C 38.127 0.064 1 342 . 30 TYR CD1 C 133.203 0.020 2 343 . 30 TYR CE1 C 118.459 0.1 2 344 . 30 TYR HA H 4.561 0.004 1 345 . 30 TYR HB2 H 3.374 0.008 1 346 . 30 TYR HB3 H 2.551 0.007 1 347 . 30 TYR HD1 H 7.319 0.008 2 348 . 30 TYR HE1 H 7.013 0.047 2 349 . 31 GLU C C 175.391 0.042 1 350 . 31 GLU H H 7.717 0.025 1 351 . 31 GLU N N 118.792 0.028 1 352 . 31 GLU CA C 57.156 0.009 1 353 . 31 GLU CB C 27.111 0.031 1 354 . 31 GLU CD C 184.950 0.028 1 355 . 31 GLU CG C 36.780 0.026 1 356 . 31 GLU HA H 3.899 0.006 1 357 . 31 GLU HB2 H 2.129 0.025 1 358 . 31 GLU HB3 H 2.200 0.025 1 359 . 31 GLU HG2 H 2.196 0.025 2 360 . 31 GLU HG3 H 2.129 0.025 2 361 . 32 VAL C C 176.288 0.1 1 362 . 32 VAL H H 8.883 0.004 1 363 . 32 VAL N N 122.289 0.019 1 364 . 32 VAL CA C 59.849 0.094 1 365 . 32 VAL CB C 32.775 0.051 1 366 . 32 VAL HA H 4.399 0.011 1 367 . 32 VAL HB H 2.035 0.009 1 368 . 32 VAL CG2 C 21.743 0.028 1 369 . 32 VAL HG1 H 0.931 0.001 1 370 . 32 VAL HG2 H 0.998 0.005 1 371 . 33 PRO C C 174.503 0.052 1 372 . 33 PRO N N 142.966 0.1 1 373 . 33 PRO CA C 62.293 0.024 1 374 . 33 PRO CB C 28.817 0.054 1 375 . 33 PRO CD C 50.971 0.023 1 376 . 33 PRO CG C 27.768 0.011 1 377 . 33 PRO HA H 4.752 0.003 1 378 . 33 PRO HB2 H 2.360 0.012 2 379 . 33 PRO HB3 H 1.954 0.004 2 380 . 33 PRO HD2 H 4.100 0.009 2 381 . 33 PRO HD3 H 3.708 0.001 2 382 . 33 PRO HG2 H 2.151 0.015 2 383 . 33 PRO HG3 H 2.126 0.010 2 384 . 34 VAL C C 174.429 0.022 1 385 . 34 VAL H H 8.163 0.002 1 386 . 34 VAL N N 116.868 0.044 1 387 . 34 VAL CA C 58.356 0.029 1 388 . 34 VAL CB C 36.359 0.011 1 389 . 34 VAL HA H 5.438 0.003 1 390 . 34 VAL HB H 1.872 0.003 1 391 . 34 VAL CG1 C 22.087 0.027 1 392 . 34 VAL CG2 C 18.818 0.030 1 393 . 34 VAL HG1 H 0.696 0.004 1 394 . 34 VAL HG2 H 0.671 0.002 1 395 . 35 ILE C C 174.118 0.037 1 396 . 35 ILE H H 8.860 0.002 1 397 . 35 ILE N N 125.464 0.109 1 398 . 35 ILE CA C 59.831 0.029 1 399 . 35 ILE CB C 40.260 0.010 1 400 . 35 ILE HA H 4.310 0.007 1 401 . 35 ILE HB H 1.214 0.004 1 402 . 35 ILE CG1 C 27.505 0.013 1 403 . 35 ILE CG2 C 17.622 0.036 1 404 . 35 ILE HD1 H 0.733 0.006 1 405 . 35 ILE HG12 H 1.039 0.006 1 406 . 35 ILE HG13 H 1.244 0.004 1 407 . 35 ILE HG2 H 0.929 0.003 1 408 . 36 ILE C C 175.115 0.037 1 409 . 36 ILE H H 9.371 0.002 1 410 . 36 ILE N N 128.133 0.167 1 411 . 36 ILE CA C 59.592 0.030 1 412 . 36 ILE CB C 40.603 0.034 1 413 . 36 ILE HA H 5.521 0.003 1 414 . 36 ILE HB H 1.591 0.008 1 415 . 36 ILE CG1 C 28.206 0.035 1 416 . 36 ILE CG2 C 20.037 0.030 1 417 . 36 ILE HD1 H 0.784 0.007 1 418 . 36 ILE HG12 H 1.480 0.006 2 419 . 36 ILE HG13 H 0.850 0.011 2 420 . 36 ILE HG2 H 0.942 0.002 1 421 . 37 GLU C C 172.822 0.030 1 422 . 37 GLU H H 8.430 0.001 1 423 . 37 GLU N N 124.105 0.056 1 424 . 37 GLU CA C 54.570 0.059 1 425 . 37 GLU CB C 35.618 0.012 1 426 . 37 GLU CD C 182.833 0.1 1 427 . 37 GLU CG C 35.749 0.025 1 428 . 37 GLU HA H 4.461 0.006 1 429 . 37 GLU HB2 H 1.363 0.004 1 430 . 37 GLU HB3 H 1.995 0.025 1 431 . 37 GLU HG2 H 1.959 0.020 2 432 . 37 GLU HG3 H 1.935 0.025 2 433 . 38 ALA C C 175.894 0.035 1 434 . 38 ALA H H 8.208 0.002 1 435 . 38 ALA N N 122.038 0.037 1 436 . 38 ALA CA C 49.435 0.043 1 437 . 38 ALA CB C 23.382 0.040 1 438 . 38 ALA HA H 5.232 0.008 1 439 . 38 ALA HB H 0.978 0.009 1 440 . 39 PHE C C 172.586 0.1 1 441 . 39 PHE H H 8.166 0.004 1 442 . 39 PHE N N 116.345 0.050 1 443 . 39 PHE CA C 55.410 0.016 1 444 . 39 PHE CB C 42.669 0.049 1 445 . 39 PHE CD1 C 131.799 0.031 2 446 . 39 PHE CE1 C 130.849 0.111 2 447 . 39 PHE CZ C 129.319 0.033 1 448 . 39 PHE HA H 5.006 0.005 1 449 . 39 PHE HZ H 6.699 0.010 1 450 . 39 PHE HB2 H 2.278 0.004 1 451 . 39 PHE HB3 H 3.136 0.005 1 452 . 39 PHE HD1 H 6.639 0.013 2 453 . 39 PHE HE1 H 6.267 0.008 2 454 . 40 PRO C C 179.626 0.013 1 455 . 40 PRO N N 130.932 0.1 1 456 . 40 PRO CA C 62.006 0.021 1 457 . 40 PRO CB C 32.911 0.054 1 458 . 40 PRO CD C 50.969 0.042 1 459 . 40 PRO CG C 27.314 0.074 1 460 . 40 PRO HA H 4.829 0.014 1 461 . 40 PRO HB2 H 2.188 0.005 1 462 . 40 PRO HB3 H 2.375 0.012 1 463 . 40 PRO HD2 H 3.923 0.004 1 464 . 40 PRO HD3 H 3.985 0.007 1 465 . 40 PRO HG2 H 2.101 0.003 1 466 . 40 PRO HG3 H 2.147 0.004 1 467 . 41 GLU C C 176.769 0.043 1 468 . 41 GLU H H 8.458 0.002 1 469 . 41 GLU N N 120.708 0.069 1 470 . 41 GLU CA C 59.597 0.027 1 471 . 41 GLU CB C 28.209 0.086 1 472 . 41 GLU CD C 180.099 0.1 1 473 . 41 GLU CG C 34.254 0.046 1 474 . 41 GLU HA H 3.991 0.003 1 475 . 41 GLU HB2 H 2.086 0.006 1 476 . 41 GLU HB3 H 1.961 0.015 1 477 . 41 GLU HG2 H 2.452 0.006 2 478 . 41 GLU HG3 H 2.313 0.010 2 479 . 42 THR C C 176.189 0.031 1 480 . 42 THR H H 7.794 0.003 1 481 . 42 THR N N 111.568 0.067 1 482 . 42 THR CA C 63.711 0.072 1 483 . 42 THR CB C 68.446 0.043 1 484 . 42 THR HA H 4.076 0.005 1 485 . 42 THR HB H 4.294 0.003 1 486 . 42 THR CG2 C 22.701 0.023 1 487 . 42 THR HG2 H 1.369 0.003 1 488 . 43 LEU C C 177.378 0.027 1 489 . 43 LEU H H 7.889 0.001 1 490 . 43 LEU N N 119.728 0.045 1 491 . 43 LEU CA C 54.340 0.099 1 492 . 43 LEU CB C 42.280 0.031 1 493 . 43 LEU CG C 27.496 0.058 1 494 . 43 LEU HA H 4.683 0.006 1 495 . 43 LEU HG H 1.702 0.013 1 496 . 43 LEU CD1 C 25.964 0.046 1 497 . 43 LEU CD2 C 23.071 0.023 1 498 . 43 LEU HB2 H 1.789 0.010 1 499 . 43 LEU HB3 H 1.675 0.004 1 500 . 43 LEU HD1 H 1.018 0.008 1 501 . 43 LEU HD2 H 0.869 0.007 1 502 . 44 ALA C C 179.104 0.028 1 503 . 44 ALA H H 8.017 0.002 1 504 . 44 ALA N N 124.716 0.074 1 505 . 44 ALA CA C 56.502 0.032 1 506 . 44 ALA CB C 16.576 0.042 1 507 . 44 ALA HA H 3.339 0.007 1 508 . 44 ALA HB H 0.668 0.004 1 509 . 45 GLY C C 174.458 0.040 1 510 . 45 GLY H H 8.666 0.002 1 511 . 45 GLY N N 103.252 0.039 1 512 . 45 GLY CA C 46.995 0.073 1 513 . 45 GLY HA2 H 3.792 0.008 1 514 . 45 GLY HA3 H 3.564 0.011 1 515 . 46 GLU C C 178.449 0.034 1 516 . 46 GLU H H 7.700 0.002 1 517 . 46 GLU N N 119.744 0.046 1 518 . 46 GLU CA C 58.150 0.048 1 519 . 46 GLU CB C 31.171 0.042 1 520 . 46 GLU CD C 182.596 0.020 1 521 . 46 GLU CG C 35.955 0.083 1 522 . 46 GLU HA H 4.247 0.009 1 523 . 46 GLU HB2 H 2.034 0.004 2 524 . 46 GLU HB3 H 1.840 0.004 2 525 . 46 GLU HG2 H 2.237 0.005 2 526 . 46 GLU HG3 H 2.040 0.005 2 527 . 47 LYS C C 179.464 0.032 1 528 . 47 LYS H H 8.602 0.002 1 529 . 47 LYS N N 115.568 0.024 1 530 . 47 LYS CA C 55.765 0.029 1 531 . 47 LYS CB C 31.757 0.053 1 532 . 47 LYS CD C 27.610 0.028 1 533 . 47 LYS CE C 41.982 0.032 1 534 . 47 LYS CG C 24.572 0.030 1 535 . 47 LYS HA H 4.237 0.006 1 536 . 47 LYS HB2 H 1.437 0.007 2 537 . 47 LYS HB3 H 1.209 0.012 2 538 . 47 LYS HD2 H 1.412 0.006 2 539 . 47 LYS HD3 H 0.958 0.005 2 540 . 47 LYS HE2 H 2.622 0.006 1 541 . 47 LYS HE3 H 2.622 0.006 1 542 . 47 LYS HG2 H 1.006 0.010 2 543 . 47 LYS HG3 H -0.006 0.004 2 544 . 48 GLY C C 174.512 0.038 1 545 . 48 GLY H H 8.258 0.002 1 546 . 48 GLY N N 106.447 0.103 1 547 . 48 GLY CA C 47.188 0.062 1 548 . 48 GLY HA2 H 3.679 0.003 1 549 . 48 GLY HA3 H 4.162 0.004 1 550 . 49 GLN C C 176.716 0.029 1 551 . 49 GLN H H 7.079 0.001 1 552 . 49 GLN N N 114.580 0.070 1 553 . 49 GLN CA C 58.049 0.092 1 554 . 49 GLN CB C 28.416 0.029 1 555 . 49 GLN CD C 179.986 0.042 1 556 . 49 GLN CG C 33.129 0.034 1 557 . 49 GLN HA H 4.018 0.006 1 558 . 49 GLN HB2 H 2.132 0.010 2 559 . 49 GLN HB3 H 1.962 0.007 2 560 . 49 GLN HG2 H 2.440 0.002 1 561 . 49 GLN HG3 H 2.440 0.002 1 562 . 49 GLN NE2 N 112.345 0.019 1 563 . 49 GLN HE21 H 7.635 0.001 1 564 . 49 GLN HE22 H 6.933 0.001 1 565 . 50 ASN C C 174.003 0.043 1 566 . 50 ASN H H 7.584 0.003 1 567 . 50 ASN N N 114.949 0.126 1 568 . 50 ASN CA C 52.250 0.045 1 569 . 50 ASN CB C 39.918 0.028 1 570 . 50 ASN CG C 177.098 0.1 1 571 . 50 ASN HA H 4.842 0.003 1 572 . 50 ASN HB2 H 2.952 0.001 2 573 . 50 ASN HB3 H 2.768 0.004 2 574 . 50 ASN ND2 N 112.201 0.049 1 575 . 50 ASN HD21 H 7.490 0.025 1 576 . 50 ASN HD22 H 6.941 0.003 1 577 . 51 ALA C C 176.092 0.023 1 578 . 51 ALA H H 7.201 0.001 1 579 . 51 ALA N N 121.280 0.017 1 580 . 51 ALA CA C 51.520 0.022 1 581 . 51 ALA CB C 20.749 0.021 1 582 . 51 ALA HA H 3.554 0.002 1 583 . 51 ALA HB H 1.250 0.002 1 584 . 52 ASP C C 175.437 0.042 1 585 . 52 ASP H H 9.355 0.025 1 586 . 52 ASP N N 119.149 0.097 1 587 . 52 ASP CA C 56.316 0.022 1 588 . 52 ASP CB C 43.178 0.018 1 589 . 52 ASP CG C 179.675 0.1 1 590 . 52 ASP HA H 4.886 0.003 1 591 . 52 ASP HB2 H 2.485 0.005 1 592 . 52 ASP HB3 H 2.661 0.005 1 593 . 53 VAL C C 170.981 0.037 1 594 . 53 VAL H H 7.548 0.003 1 595 . 53 VAL N N 113.786 0.110 1 596 . 53 VAL CA C 61.178 0.058 1 597 . 53 VAL CB C 33.933 0.088 1 598 . 53 VAL HA H 4.447 0.008 1 599 . 53 VAL HB H 2.128 0.014 1 600 . 53 VAL CG1 C 21.531 0.1 2 601 . 53 VAL CG2 C 21.556 0.1 2 602 . 53 VAL HG1 H 0.917 0.005 2 603 . 53 VAL HG2 H 0.887 0.001 2 604 . 54 VAL C C 173.419 0.042 1 605 . 54 VAL H H 8.408 0.002 1 606 . 54 VAL N N 128.898 0.042 1 607 . 54 VAL CA C 61.311 0.030 1 608 . 54 VAL CB C 33.316 0.067 1 609 . 54 VAL HA H 4.850 0.003 1 610 . 54 VAL HB H 2.154 0.003 1 611 . 54 VAL CG1 C 21.670 0.026 2 612 . 54 VAL CG2 C 21.683 0.013 2 613 . 54 VAL HG1 H 0.885 0.004 1 614 . 54 VAL HG2 H 0.885 0.004 1 615 . 55 LEU C C 175.890 0.037 1 616 . 55 LEU H H 9.375 0.001 1 617 . 55 LEU N N 125.494 0.041 1 618 . 55 LEU CA C 52.073 0.020 1 619 . 55 LEU CB C 44.361 0.049 1 620 . 55 LEU CG C 26.993 0.074 1 621 . 55 LEU HA H 5.604 0.006 1 622 . 55 LEU HG H 1.561 0.004 1 623 . 55 LEU CD1 C 25.928 0.021 1 624 . 55 LEU CD2 C 23.703 0.067 1 625 . 55 LEU HB2 H 1.901 0.004 1 626 . 55 LEU HB3 H 1.273 0.003 1 627 . 55 LEU HD1 H 0.711 0.013 1 628 . 55 LEU HD2 H 0.776 0.007 1 629 . 56 LEU C C 176.736 0.028 1 630 . 56 LEU H H 9.125 0.002 1 631 . 56 LEU N N 120.898 0.061 1 632 . 56 LEU CA C 52.532 0.041 1 633 . 56 LEU CB C 42.479 0.041 1 634 . 56 LEU CG C 27.465 0.045 1 635 . 56 LEU HA H 5.005 0.004 1 636 . 56 LEU HG H 1.555 0.026 1 637 . 56 LEU CD1 C 23.576 0.029 2 638 . 56 LEU CD2 C 25.240 0.022 2 639 . 56 LEU HB2 H 1.582 0.016 1 640 . 56 LEU HB3 H 1.364 0.005 1 641 . 56 LEU HD1 H 0.665 0.008 2 642 . 56 LEU HD2 H 0.617 0.003 2 643 . 57 GLY C C 171.428 0.1 1 644 . 57 GLY H H 8.486 0.002 1 645 . 57 GLY N N 107.506 0.077 1 646 . 57 GLY CA C 44.126 0.048 1 647 . 57 GLY HA2 H 3.780 0.010 1 648 . 57 GLY HA3 H 3.217 0.009 1 649 . 58 PRO C C 178.947 0.033 1 650 . 58 PRO N N 134.866 0.053 1 651 . 58 PRO CA C 65.078 0.031 1 652 . 58 PRO CB C 31.156 0.039 1 653 . 58 PRO CD C 49.381 0.046 1 654 . 58 PRO CG C 27.542 0.043 1 655 . 58 PRO HA H 3.991 0.008 1 656 . 58 PRO HB2 H 2.303 0.007 2 657 . 58 PRO HB3 H 1.906 0.003 2 658 . 58 PRO HD2 H 2.927 0.003 2 659 . 58 PRO HD3 H 2.333 0.005 2 660 . 58 PRO HG2 H 1.804 0.003 2 661 . 58 PRO HG3 H 1.700 0.003 2 662 . 59 GLN C C 177.671 0.030 1 663 . 59 GLN H H 9.969 0.001 1 664 . 59 GLN N N 118.055 0.025 1 665 . 59 GLN CA C 57.700 0.024 1 666 . 59 GLN CB C 27.737 0.048 1 667 . 59 GLN CD C 181.017 0.002 1 668 . 59 GLN CG C 33.817 0.082 1 669 . 59 GLN HA H 4.365 0.006 1 670 . 59 GLN HB2 H 2.259 0.004 1 671 . 59 GLN HB3 H 2.240 0.002 1 672 . 59 GLN HG2 H 2.900 0.003 2 673 . 59 GLN HG3 H 2.271 0.009 2 674 . 59 GLN NE2 N 113.163 0.022 1 675 . 59 GLN HE21 H 8.303 0.002 1 676 . 59 GLN HE22 H 6.619 0.002 1 677 . 60 ILE C C 175.851 0.032 1 678 . 60 ILE H H 7.770 0.003 1 679 . 60 ILE N N 112.403 0.013 1 680 . 60 ILE CA C 60.403 0.034 1 681 . 60 ILE CB C 37.421 0.027 1 682 . 60 ILE HA H 4.709 0.006 1 683 . 60 ILE HB H 1.925 0.002 1 684 . 60 ILE CG1 C 27.791 0.083 1 685 . 60 ILE CG2 C 18.489 0.054 1 686 . 60 ILE HD1 H 0.710 0.005 1 687 . 60 ILE HG12 H 0.801 0.006 1 688 . 60 ILE HG13 H 1.485 0.006 1 689 . 60 ILE HG2 H 0.909 0.004 1 690 . 61 ALA C C 179.891 0.036 1 691 . 61 ALA H H 7.547 0.001 1 692 . 61 ALA N N 124.714 0.024 1 693 . 61 ALA CA C 55.788 0.025 1 694 . 61 ALA CB C 19.044 0.034 1 695 . 61 ALA HA H 3.745 0.005 1 696 . 61 ALA HB H 1.591 0.005 1 697 . 62 TYR C C 176.140 0.023 1 698 . 62 TYR H H 7.703 0.002 1 699 . 62 TYR N N 113.290 0.034 1 700 . 62 TYR CA C 58.395 0.104 1 701 . 62 TYR CB C 36.504 0.023 1 702 . 62 TYR CD1 C 133.456 0.020 2 703 . 62 TYR CE1 C 118.731 0.1 2 704 . 62 TYR HA H 4.369 0.005 1 705 . 62 TYR HB2 H 3.212 0.008 1 706 . 62 TYR HB3 H 3.046 0.002 1 707 . 62 TYR HD1 H 7.137 0.005 2 708 . 62 TYR HE1 H 6.989 0.004 2 709 . 63 MET C C 176.049 0.026 1 710 . 63 MET H H 7.543 0.002 1 711 . 63 MET N N 119.546 0.105 1 712 . 63 MET CA C 55.547 0.081 1 713 . 63 MET CB C 32.307 0.508 1 714 . 63 MET CE C 16.757 0.017 1 715 . 63 MET CG C 32.905 0.562 1 716 . 63 MET HA H 4.333 0.009 1 717 . 63 MET HB2 H 1.955 0.002 2 718 . 63 MET HB3 H 1.787 0.010 2 719 . 63 MET HG2 H 1.880 0.025 2 720 . 63 MET HG3 H 1.764 0.025 2 721 . 63 MET HE H 1.960 0.004 1 722 . 64 LEU C C 173.351 0.1 1 723 . 64 LEU H H 7.582 0.001 1 724 . 64 LEU N N 120.523 0.050 1 725 . 64 LEU CA C 60.949 0.037 1 726 . 64 LEU CB C 39.406 0.021 1 727 . 64 LEU CG C 27.118 0.025 1 728 . 64 LEU HA H 3.842 0.004 1 729 . 64 LEU HG H 1.437 0.010 1 730 . 64 LEU CD1 C 24.593 0.074 1 731 . 64 LEU CD2 C 25.437 0.008 1 732 . 64 LEU HB2 H 1.961 0.004 1 733 . 64 LEU HB3 H 1.435 0.012 1 734 . 64 LEU HD1 H 0.801 0.008 1 735 . 64 LEU HD2 H 0.925 0.003 1 736 . 65 PRO C C 179.699 0.002 1 737 . 65 PRO N N 133.573 0.1 1 738 . 65 PRO CA C 65.972 0.030 1 739 . 65 PRO CB C 30.516 0.056 1 740 . 65 PRO CD C 49.162 0.022 1 741 . 65 PRO CG C 28.392 0.058 1 742 . 65 PRO HA H 4.427 0.003 1 743 . 65 PRO HB2 H 2.302 0.008 2 744 . 65 PRO HB3 H 1.905 0.003 2 745 . 65 PRO HD2 H 3.720 0.005 1 746 . 65 PRO HD3 H 3.620 0.002 1 747 . 65 PRO HG2 H 2.022 0.003 1 748 . 65 PRO HG3 H 2.150 0.006 1 749 . 66 GLU C C 178.716 0.005 1 750 . 66 GLU H H 7.283 0.002 1 751 . 66 GLU N N 117.563 0.021 1 752 . 66 GLU CA C 58.639 0.011 1 753 . 66 GLU CB C 29.445 0.050 1 754 . 66 GLU CD C 183.169 0.1 1 755 . 66 GLU CG C 35.754 0.063 1 756 . 66 GLU HA H 4.160 0.004 1 757 . 66 GLU HB2 H 2.140 0.025 2 758 . 66 GLU HB3 H 1.972 0.013 2 759 . 66 GLU HG2 H 2.297 0.016 2 760 . 66 GLU HG3 H 2.207 0.025 2 761 . 67 ILE C C 177.700 0.1 1 762 . 67 ILE H H 8.219 0.001 1 763 . 67 ILE N N 120.463 0.018 1 764 . 67 ILE CA C 64.066 0.015 1 765 . 67 ILE CB C 36.079 0.014 1 766 . 67 ILE HA H 3.604 0.003 1 767 . 67 ILE HB H 1.704 0.003 1 768 . 67 ILE CG1 C 28.869 0.034 1 769 . 67 ILE CG2 C 18.220 0.067 1 770 . 67 ILE HD1 H 0.458 0.004 1 771 . 67 ILE HG12 H 1.373 0.003 2 772 . 67 ILE HG13 H 1.086 0.006 2 773 . 67 ILE HG2 H 0.651 0.005 1 774 . 68 GLN C C 178.649 0.005 1 775 . 68 GLN H H 8.613 0.002 1 776 . 68 GLN N N 118.090 0.032 1 777 . 68 GLN CA C 58.891 0.032 1 778 . 68 GLN CB C 28.846 0.027 1 779 . 68 GLN CD C 179.757 0.1 1 780 . 68 GLN CG C 34.854 0.081 1 781 . 68 GLN HA H 3.990 0.003 1 782 . 68 GLN HB2 H 2.088 0.007 2 783 . 68 GLN HB3 H 1.949 0.003 2 784 . 68 GLN HG2 H 2.441 0.012 2 785 . 68 GLN HG3 H 2.320 0.002 2 786 . 68 GLN NE2 N 113.476 0.130 1 787 . 68 GLN HE21 H 7.315 0.001 1 788 . 68 GLN HE22 H 7.115 0.001 1 789 . 69 ARG C C 178.265 0.007 1 790 . 69 ARG H H 7.392 0.001 1 791 . 69 ARG N N 117.180 0.033 1 792 . 69 ARG CA C 58.727 0.130 1 793 . 69 ARG CB C 30.273 0.081 1 794 . 69 ARG CD C 43.377 0.021 1 795 . 69 ARG CG C 27.832 0.016 1 796 . 69 ARG HA H 3.977 0.016 1 797 . 69 ARG HE H 7.626 0.025 1 798 . 69 ARG HB2 H 1.917 0.025 1 799 . 69 ARG HB3 H 1.917 0.025 1 800 . 69 ARG HD2 H 3.236 0.008 2 801 . 69 ARG HD3 H 3.199 0.004 2 802 . 69 ARG HG2 H 1.760 0.003 2 803 . 69 ARG HG3 H 1.575 0.002 2 804 . 70 LEU C C 176.863 0.029 1 805 . 70 LEU H H 7.506 0.002 1 806 . 70 LEU N N 119.072 0.040 1 807 . 70 LEU CA C 56.739 0.014 1 808 . 70 LEU CB C 43.540 0.035 1 809 . 70 LEU CG C 26.359 0.008 1 810 . 70 LEU HA H 4.083 0.002 1 811 . 70 LEU HG H 1.756 0.001 1 812 . 70 LEU CD1 C 24.800 0.010 1 813 . 70 LEU CD2 C 23.503 0.097 1 814 . 70 LEU HB2 H 1.830 0.007 2 815 . 70 LEU HB3 H 1.552 0.002 2 816 . 70 LEU HD1 H 0.804 0.003 1 817 . 70 LEU HD2 H 0.788 0.003 1 818 . 71 LEU C C 173.279 0.1 1 819 . 71 LEU H H 7.402 0.001 1 820 . 71 LEU N N 118.189 0.016 1 821 . 71 LEU CA C 51.049 0.017 1 822 . 71 LEU CB C 42.179 0.033 1 823 . 71 LEU CG C 25.673 0.036 1 824 . 71 LEU HA H 4.758 0.004 1 825 . 71 LEU HG H 1.368 0.005 1 826 . 71 LEU CD1 C 26.822 0.032 1 827 . 71 LEU CD2 C 22.756 0.044 1 828 . 71 LEU HB2 H 1.737 0.002 2 829 . 71 LEU HB3 H 1.011 0.003 2 830 . 71 LEU HD1 H 0.656 0.004 1 831 . 71 LEU HD2 H 0.745 0.007 1 832 . 72 PRO C C 177.687 0.032 1 833 . 72 PRO N N 135.355 0.1 1 834 . 72 PRO CA C 64.647 0.027 1 835 . 72 PRO CB C 31.828 0.038 1 836 . 72 PRO CD C 50.027 0.022 1 837 . 72 PRO CG C 27.462 0.110 1 838 . 72 PRO HA H 4.474 0.003 1 839 . 72 PRO HB2 H 2.270 0.004 2 840 . 72 PRO HB3 H 1.932 0.006 2 841 . 72 PRO HD2 H 3.569 0.013 2 842 . 72 PRO HD3 H 3.426 0.008 2 843 . 72 PRO HG2 H 2.009 0.003 2 844 . 72 PRO HG3 H 1.918 0.025 2 845 . 73 ASN C C 174.442 0.034 1 846 . 73 ASN H H 8.628 0.001 1 847 . 73 ASN N N 114.056 0.058 1 848 . 73 ASN CA C 53.119 0.015 1 849 . 73 ASN CB C 38.038 0.047 1 850 . 73 ASN CG C 178.283 0.1 1 851 . 73 ASN HA H 4.698 0.001 1 852 . 73 ASN HB2 H 2.944 0.002 2 853 . 73 ASN HB3 H 2.943 0.001 2 854 . 73 ASN ND2 N 113.371 0.053 1 855 . 73 ASN HD21 H 7.640 0.001 1 856 . 73 ASN HD22 H 7.079 0.007 1 857 . 74 LYS C C 173.723 0.1 1 858 . 74 LYS H H 7.544 0.004 1 859 . 74 LYS N N 119.313 0.058 1 860 . 74 LYS CA C 51.602 0.073 1 861 . 74 LYS CB C 33.120 0.076 1 862 . 74 LYS CD C 28.012 0.141 1 863 . 74 LYS CE C 42.849 0.064 1 864 . 74 LYS CG C 23.950 0.089 1 865 . 74 LYS HA H 4.888 0.011 1 866 . 74 LYS HB2 H 1.724 0.006 2 867 . 74 LYS HB3 H 1.394 0.005 2 868 . 74 LYS HD2 H 1.642 0.003 2 869 . 74 LYS HD3 H 1.516 0.002 2 870 . 74 LYS HE2 H 3.286 0.004 2 871 . 74 LYS HE3 H 2.933 0.007 2 872 . 74 LYS HG2 H 1.306 0.007 2 873 . 74 LYS HG3 H 1.240 0.006 2 874 . 75 PRO C C 175.046 0.001 1 875 . 75 PRO N N 136.616 0.1 1 876 . 75 PRO CA C 62.880 0.051 1 877 . 75 PRO CB C 30.946 0.032 1 878 . 75 PRO CD C 50.723 0.031 1 879 . 75 PRO CG C 27.886 0.062 1 880 . 75 PRO HA H 4.669 0.011 1 881 . 75 PRO HB2 H 2.330 0.006 2 882 . 75 PRO HB3 H 1.998 0.004 2 883 . 75 PRO HD2 H 3.915 0.003 2 884 . 75 PRO HD3 H 3.669 0.006 2 885 . 75 PRO HG2 H 2.405 0.004 2 886 . 75 PRO HG3 H 1.994 0.008 2 887 . 76 VAL C C 175.180 0.010 1 888 . 76 VAL H H 7.986 0.002 1 889 . 76 VAL N N 126.685 0.022 1 890 . 76 VAL CA C 60.453 0.031 1 891 . 76 VAL CB C 33.814 0.027 1 892 . 76 VAL HA H 5.099 0.007 1 893 . 76 VAL HB H 1.861 0.007 1 894 . 76 VAL CG1 C 22.120 0.069 1 895 . 76 VAL CG2 C 20.756 0.038 1 896 . 76 VAL HG1 H 0.652 0.008 1 897 . 76 VAL HG2 H 0.774 0.005 1 898 . 77 GLU C C 174.839 0.006 1 899 . 77 GLU H H 8.810 0.002 1 900 . 77 GLU N N 123.338 0.044 1 901 . 77 GLU CA C 53.980 0.017 1 902 . 77 GLU CB C 34.225 0.069 1 903 . 77 GLU CD C 182.677 0.1 1 904 . 77 GLU CG C 35.275 0.062 1 905 . 77 GLU HA H 4.729 0.005 1 906 . 77 GLU HB2 H 2.021 0.005 2 907 . 77 GLU HB3 H 1.645 0.004 2 908 . 77 GLU HG2 H 2.077 0.001 2 909 . 77 GLU HG3 H 2.016 0.025 2 910 . 78 VAL C C 176.790 0.1 1 911 . 78 VAL H H 8.856 0.001 1 912 . 78 VAL N N 121.905 0.015 1 913 . 78 VAL CA C 61.352 0.013 1 914 . 78 VAL CB C 32.453 0.072 1 915 . 78 VAL HA H 4.349 0.002 1 916 . 78 VAL HB H 1.946 0.011 1 917 . 78 VAL CG1 C 21.528 0.011 1 918 . 78 VAL CG2 C 23.168 0.017 1 919 . 78 VAL HG1 H 0.943 0.004 1 920 . 78 VAL HG2 H 1.032 0.003 1 921 . 79 ILE C C 174.531 0.038 1 922 . 79 ILE H H 8.848 0.002 1 923 . 79 ILE N N 130.115 0.026 1 924 . 79 ILE CA C 62.745 0.090 1 925 . 79 ILE CB C 39.374 0.050 1 926 . 79 ILE HA H 3.742 0.006 1 927 . 79 ILE HB H 1.544 0.009 1 928 . 79 ILE CG1 C 29.861 0.046 1 929 . 79 ILE CG2 C 19.014 0.049 1 930 . 79 ILE HD1 H 0.894 0.004 1 931 . 79 ILE HG12 H 1.734 0.006 2 932 . 79 ILE HG13 H 0.917 0.005 2 933 . 79 ILE HG2 H 1.297 0.003 1 934 . 80 ASP C C 177.470 0.1 1 935 . 80 ASP H H 8.833 0.003 1 936 . 80 ASP N N 127.660 0.021 1 937 . 80 ASP CA C 55.681 0.107 1 938 . 80 ASP CB C 43.727 0.045 1 939 . 80 ASP CG C 179.648 0.003 1 940 . 80 ASP HA H 4.361 0.005 1 941 . 80 ASP HB2 H 2.866 0.005 2 942 . 80 ASP HB3 H 2.541 0.003 2 943 . 81 SER C C 176.935 0.016 1 944 . 81 SER H H 8.683 0.001 1 945 . 81 SER N N 122.139 0.034 1 946 . 81 SER CA C 62.767 0.050 1 947 . 81 SER HA H 4.004 0.009 1 948 . 81 SER HB2 H 3.994 0.025 1 949 . 81 SER HB3 H 3.994 0.025 1 950 . 82 LEU C C 179.855 0.027 1 951 . 82 LEU H H 8.396 0.001 1 952 . 82 LEU N N 125.793 0.028 1 953 . 82 LEU CA C 58.026 0.039 1 954 . 82 LEU CB C 41.057 0.010 1 955 . 82 LEU CG C 27.339 0.025 1 956 . 82 LEU HA H 4.335 0.005 1 957 . 82 LEU HG H 1.669 0.003 1 958 . 82 LEU CD1 C 24.013 0.1 1 959 . 82 LEU CD2 C 24.494 0.040 1 960 . 82 LEU HB2 H 1.881 0.010 2 961 . 82 LEU HB3 H 1.734 0.008 2 962 . 82 LEU HD1 H 0.917 0.008 1 963 . 82 LEU HD2 H 0.988 0.015 1 964 . 83 LEU C C 179.435 0.026 1 965 . 83 LEU H H 8.023 0.004 1 966 . 83 LEU N N 118.676 0.014 1 967 . 83 LEU CA C 58.027 0.030 1 968 . 83 LEU CB C 41.925 0.056 1 969 . 83 LEU CG C 26.899 0.102 1 970 . 83 LEU HA H 4.016 0.003 1 971 . 83 LEU HG H 1.967 0.008 1 972 . 83 LEU CD1 C 25.487 0.043 1 973 . 83 LEU CD2 C 22.812 0.113 1 974 . 83 LEU HB2 H 1.907 0.008 2 975 . 83 LEU HB3 H 1.462 0.006 2 976 . 83 LEU HD1 H 0.864 0.007 1 977 . 83 LEU HD2 H 0.927 0.012 1 978 . 84 TYR C C 179.888 0.1 1 979 . 84 TYR H H 8.680 0.002 1 980 . 84 TYR N N 117.917 0.044 1 981 . 84 TYR CA C 62.741 0.135 1 982 . 84 TYR CB C 39.513 0.061 1 983 . 84 TYR CD1 C 133.213 0.054 2 984 . 84 TYR CE1 C 118.347 0.076 2 985 . 84 TYR HA H 3.758 0.004 1 986 . 84 TYR HB2 H 3.072 0.006 2 987 . 84 TYR HB3 H 2.935 0.006 2 988 . 84 TYR HD1 H 6.986 0.011 2 989 . 84 TYR HE1 H 6.733 0.009 2 990 . 85 GLY C C 175.617 0.007 1 991 . 85 GLY H H 8.489 0.001 1 992 . 85 GLY N N 107.091 0.023 1 993 . 85 GLY CA C 46.952 0.064 1 994 . 85 GLY HA2 H 4.115 0.013 2 995 . 85 GLY HA3 H 3.970 0.013 2 996 . 86 LYS C C 175.481 0.037 1 997 . 86 LYS H H 7.633 0.001 1 998 . 86 LYS N N 117.719 0.028 1 999 . 86 LYS CA C 55.852 0.025 1 1000 . 86 LYS CB C 32.612 0.1 1 1001 . 86 LYS CD C 29.156 0.030 1 1002 . 86 LYS CE C 42.099 0.1 1 1003 . 86 LYS CG C 25.241 0.042 1 1004 . 86 LYS HA H 4.303 0.005 1 1005 . 86 LYS HB2 H 1.929 0.010 2 1006 . 86 LYS HB3 H 1.790 0.009 2 1007 . 86 LYS HD2 H 1.694 0.025 2 1008 . 86 LYS HD3 H 1.660 0.025 2 1009 . 86 LYS HE2 H 2.994 0.025 2 1010 . 86 LYS HE3 H 2.937 0.011 2 1011 . 86 LYS HG2 H 1.614 0.025 2 1012 . 86 LYS HG3 H 1.548 0.025 2 1013 . 87 VAL C C 174.734 0.047 1 1014 . 87 VAL H H 7.775 0.004 1 1015 . 87 VAL N N 121.317 0.027 1 1016 . 87 VAL CA C 62.550 0.053 1 1017 . 87 VAL CB C 28.870 0.023 1 1018 . 87 VAL HA H 2.956 0.006 1 1019 . 87 VAL HB H 2.454 0.004 1 1020 . 87 VAL CG1 C 24.163 0.027 2 1021 . 87 VAL CG2 C 20.767 0.012 2 1022 . 87 VAL HG1 H 0.811 0.003 2 1023 . 87 VAL HG2 H 0.742 0.005 2 1024 . 88 ASP C C 175.516 0.038 1 1025 . 88 ASP H H 7.815 0.004 1 1026 . 88 ASP N N 117.829 0.057 1 1027 . 88 ASP CA C 52.401 0.047 1 1028 . 88 ASP CB C 39.742 0.074 1 1029 . 88 ASP CG C 180.282 0.1 1 1030 . 88 ASP HA H 4.618 0.008 1 1031 . 88 ASP HB2 H 2.999 0.006 2 1032 . 88 ASP HB3 H 2.350 0.007 2 1033 . 89 GLY C C 174.737 0.040 1 1034 . 89 GLY H H 7.991 0.004 1 1035 . 89 GLY N N 111.305 0.103 1 1036 . 89 GLY CA C 47.384 0.058 1 1037 . 89 GLY HA2 H 3.579 0.009 1 1038 . 89 GLY HA3 H 3.326 0.005 1 1039 . 90 LEU C C 177.935 0.035 1 1040 . 90 LEU H H 8.477 0.004 1 1041 . 90 LEU N N 121.858 0.070 1 1042 . 90 LEU CA C 57.856 0.030 1 1043 . 90 LEU CB C 40.931 0.034 1 1044 . 90 LEU CG C 26.908 0.064 1 1045 . 90 LEU HA H 4.081 0.005 1 1046 . 90 LEU HG H 1.469 0.008 1 1047 . 90 LEU CD1 C 22.513 0.076 1 1048 . 90 LEU CD2 C 25.416 0.045 1 1049 . 90 LEU HB2 H 1.973 0.011 2 1050 . 90 LEU HB3 H 1.506 0.008 2 1051 . 90 LEU HD1 H 0.892 0.013 1 1052 . 90 LEU HD2 H 0.923 0.004 1 1053 . 91 GLY C C 177.365 0.030 1 1054 . 91 GLY H H 8.524 0.004 1 1055 . 91 GLY N N 107.430 0.033 1 1056 . 91 GLY CA C 47.977 0.086 1 1057 . 91 GLY HA2 H 3.723 0.001 1 1058 . 91 GLY HA3 H 3.617 0.002 1 1059 . 92 VAL C C 177.563 0.013 1 1060 . 92 VAL H H 8.323 0.004 1 1061 . 92 VAL N N 121.752 0.017 1 1062 . 92 VAL CA C 66.924 0.026 1 1063 . 92 VAL CB C 31.690 0.022 1 1064 . 92 VAL HA H 3.712 0.004 1 1065 . 92 VAL HB H 1.979 0.006 1 1066 . 92 VAL CG1 C 22.460 0.023 1 1067 . 92 VAL CG2 C 24.348 0.037 1 1068 . 92 VAL HG1 H 1.034 0.006 1 1069 . 92 VAL HG2 H 1.071 0.005 1 1070 . 93 LEU C C 178.001 0.037 1 1071 . 93 LEU H H 8.195 0.001 1 1072 . 93 LEU N N 121.672 0.086 1 1073 . 93 LEU CA C 58.817 0.057 1 1074 . 93 LEU CB C 42.245 0.061 1 1075 . 93 LEU CG C 26.752 0.025 1 1076 . 93 LEU HA H 3.915 0.007 1 1077 . 93 LEU HG H 1.549 0.003 1 1078 . 93 LEU CD1 C 25.928 0.055 2 1079 . 93 LEU CD2 C 24.101 0.001 2 1080 . 93 LEU HB2 H 2.237 0.005 2 1081 . 93 LEU HB3 H 1.479 0.004 2 1082 . 93 LEU HD1 H 0.868 0.007 2 1083 . 93 LEU HD2 H 0.827 0.003 2 1084 . 94 LYS C C 179.804 0.010 1 1085 . 94 LYS H H 8.840 0.002 1 1086 . 94 LYS N N 117.403 0.074 1 1087 . 94 LYS CA C 60.429 0.038 1 1088 . 94 LYS CB C 32.425 0.064 1 1089 . 94 LYS CD C 29.678 0.062 1 1090 . 94 LYS CE C 41.716 0.010 1 1091 . 94 LYS CG C 26.032 0.058 1 1092 . 94 LYS HA H 3.809 0.009 1 1093 . 94 LYS HB2 H 1.832 0.005 1 1094 . 94 LYS HB3 H 1.832 0.005 1 1095 . 94 LYS HD2 H 1.579 0.008 1 1096 . 94 LYS HD3 H 1.579 0.008 1 1097 . 94 LYS HE2 H 2.824 0.025 2 1098 . 94 LYS HE3 H 2.758 0.002 2 1099 . 94 LYS HG2 H 1.619 0.011 2 1100 . 94 LYS HG3 H 1.307 0.005 2 1101 . 95 ALA C C 180.620 0.033 1 1102 . 95 ALA H H 7.626 0.003 1 1103 . 95 ALA N N 122.171 0.028 1 1104 . 95 ALA CA C 54.930 0.033 1 1105 . 95 ALA CB C 17.698 0.079 1 1106 . 95 ALA HA H 4.193 0.002 1 1107 . 95 ALA HB H 1.552 0.010 1 1108 . 96 ALA C C 178.770 0.031 1 1109 . 96 ALA H H 8.487 0.002 1 1110 . 96 ALA N N 122.675 0.054 1 1111 . 96 ALA CA C 55.167 0.046 1 1112 . 96 ALA CB C 19.227 0.048 1 1113 . 96 ALA HA H 3.990 0.010 1 1114 . 96 ALA HB H 1.562 0.005 1 1115 . 97 VAL C C 178.345 0.043 1 1116 . 97 VAL H H 8.549 0.001 1 1117 . 97 VAL N N 116.687 0.090 1 1118 . 97 VAL CA C 66.550 0.085 1 1119 . 97 VAL CB C 31.653 0.074 1 1120 . 97 VAL HA H 3.516 0.004 1 1121 . 97 VAL HB H 2.093 0.004 1 1122 . 97 VAL CG1 C 22.489 0.042 1 1123 . 97 VAL CG2 C 21.276 0.004 1 1124 . 97 VAL HG1 H 0.948 0.006 1 1125 . 97 VAL HG2 H 0.919 0.002 1 1126 . 98 ALA C C 180.013 0.034 1 1127 . 98 ALA H H 8.050 0.004 1 1128 . 98 ALA N N 122.166 0.030 1 1129 . 98 ALA CA C 55.013 0.008 1 1130 . 98 ALA CB C 17.769 0.020 1 1131 . 98 ALA HA H 4.128 0.009 1 1132 . 98 ALA HB H 1.500 0.017 1 1133 . 99 ALA C C 180.309 0.030 1 1134 . 99 ALA H H 7.704 0.004 1 1135 . 99 ALA N N 120.891 0.016 1 1136 . 99 ALA CA C 54.805 0.024 1 1137 . 99 ALA CB C 18.336 0.1 1 1138 . 99 ALA HA H 4.181 0.007 1 1139 . 99 ALA HB H 1.504 0.005 1 1140 . 100 ILE C C 178.221 0.031 1 1141 . 100 ILE H H 7.749 0.001 1 1142 . 100 ILE N N 119.153 0.075 1 1143 . 100 ILE CA C 65.449 0.022 1 1144 . 100 ILE CB C 38.332 0.045 1 1145 . 100 ILE HA H 3.543 0.002 1 1146 . 100 ILE HB H 1.988 0.004 1 1147 . 100 ILE CG1 C 29.210 0.047 1 1148 . 100 ILE CG2 C 17.139 0.034 1 1149 . 100 ILE HD1 H 0.689 0.005 1 1150 . 100 ILE HG12 H 1.911 0.003 2 1151 . 100 ILE HG13 H 0.696 0.004 2 1152 . 100 ILE HG2 H 0.901 0.003 1 1153 . 101 LYS C C 178.891 0.032 1 1154 . 101 LYS H H 8.076 0.004 1 1155 . 101 LYS N N 120.139 0.079 1 1156 . 101 LYS CA C 59.055 0.1 1 1157 . 101 LYS CB C 32.492 0.020 1 1158 . 101 LYS CD C 29.333 0.036 1 1159 . 101 LYS CE C 42.298 0.1 1 1160 . 101 LYS CG C 25.440 0.009 1 1161 . 101 LYS HA H 4.069 0.004 1 1162 . 101 LYS HB2 H 1.885 0.002 1 1163 . 101 LYS HB3 H 1.885 0.002 1 1164 . 101 LYS HD2 H 1.653 0.014 1 1165 . 101 LYS HD3 H 1.653 0.014 1 1166 . 101 LYS HE2 H 2.940 0.025 1 1167 . 101 LYS HE3 H 2.940 0.025 1 1168 . 101 LYS HG2 H 1.445 0.007 2 1169 . 101 LYS HG3 H 1.436 0.011 2 1170 . 102 LYS C C 177.882 0.1 1 1171 . 102 LYS H H 8.106 0.005 1 1172 . 102 LYS N N 119.793 0.030 1 1173 . 102 LYS CA C 58.626 0.053 1 1174 . 102 LYS CB C 32.608 0.017 1 1175 . 102 LYS CD C 29.333 0.053 1 1176 . 102 LYS CE C 42.074 0.015 1 1177 . 102 LYS CG C 25.135 0.037 1 1178 . 102 LYS HA H 4.114 0.009 1 1179 . 102 LYS HB2 H 1.916 0.003 2 1180 . 102 LYS HB3 H 1.913 0.003 2 1181 . 102 LYS HD2 H 1.718 0.011 2 1182 . 102 LYS HD3 H 1.663 0.005 2 1183 . 102 LYS HE2 H 2.983 0.025 2 1184 . 102 LYS HE3 H 2.985 0.007 2 1185 . 102 LYS HG2 H 1.491 0.027 2 1186 . 102 LYS HG3 H 1.449 0.025 2 1187 . 103 ALA C C 178.026 0.1 1 1188 . 103 ALA H H 7.681 0.007 1 1189 . 103 ALA N N 121.213 0.102 1 1190 . 103 ALA CA C 53.217 0.046 1 1191 . 103 ALA CB C 18.742 0.037 1 1192 . 103 ALA HA H 4.278 0.004 1 1193 . 103 ALA HB H 1.524 0.010 1 1194 . 104 ALA C C 177.381 0.024 1 1195 . 104 ALA H H 7.715 0.002 1 1196 . 104 ALA N N 120.921 0.097 1 1197 . 104 ALA CA C 52.787 0.1 1 1198 . 104 ALA CB C 19.105 0.021 1 1199 . 104 ALA HA H 4.318 0.025 1 1200 . 104 ALA HB H 1.459 0.012 1 1201 . 105 ALA C C 176.601 0.024 1 1202 . 105 ALA H H 7.874 0.001 1 1203 . 105 ALA N N 122.526 0.062 1 1204 . 105 ALA CA C 52.591 0.1 1 1205 . 105 ALA CB C 19.200 0.005 1 1206 . 105 ALA HA H 4.343 0.002 1 1207 . 105 ALA HB H 1.453 0.005 1 1208 . 106 ASN C C 179.538 0.017 1 1209 . 106 ASN H H 7.878 0.025 1 1210 . 106 ASN N N 123.243 0.037 1 1211 . 106 ASN CA C 54.808 0.005 1 1212 . 106 ASN CB C 40.552 0.046 1 1213 . 106 ASN CG C 178.324 0.017 1 1214 . 106 ASN HA H 4.480 0.025 1 1215 . 106 ASN HB2 H 2.792 0.025 2 1216 . 106 ASN HB3 H 2.709 0.005 2 1217 . 106 ASN ND2 N 113.014 0.004 1 1218 . 106 ASN HD21 H 7.547 0.004 1 1219 . 106 ASN HD22 H 6.861 0.002 1 stop_ save_