data_5327 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural basis for Hif-1alpha/CBP recognition in the cellular hypoxic response ; _BMRB_accession_number 5327 _BMRB_flat_file_name bmr5327.str _Entry_type original _Submission_date 2002-03-19 _Accession_date 2002-03-19 _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 Dames Sonja . . 2 Martinez-Yamout Maria . . 3 'De Guzman' Roberto N. . 4 Dyson 'H. Jane' . . 5 Wright Peter E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 785 "13C chemical shifts" 467 "15N chemical shifts" 154 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-06-13 original BMRB . stop_ _Original_release_date 2002-03-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; From the Cover: Structural basis for Hif-1alpha/CBP Recognition in the Cellular Hypoxic Response ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21957241 _PubMed_ID 11959977 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Dames Sonja A. . 2 Martinez-Yamout Maria . . 3 'De Guzman' Roberto N. . 4 Dyson H. J. . 5 Wright Peter E. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 99 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5271 _Page_last 5276 _Year 2002 _Details . loop_ _Keyword CBP HIF-1alpha TAZ1 hypoxia stop_ save_ ################################## # Molecular system description # ################################## save_system_Hif-1alpha_CBP _Saveframe_category molecular_system _Mol_system_name 'Hif-1alpha/CBP complex' _Abbreviation_common 'Hif-1alpha CBP' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Hif-1alpha $Hif-1alpha CBP $CBP 'Zinc ion, I' $ZN 'Zinc ion, II' $ZN 'Zinc ion, III' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state complex _System_paramagnetic no _System_thiol_state 'other bound and free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Hif-1alpha _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'hypoxia induced factor 1 alpha' _Abbreviation_common Hif-1alpha _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 51 _Mol_residue_sequence ; SDLACRLLGQSMDESGLPQL TSYDCEVNAPIQGSRNLLQG EELLRALDQVN ; loop_ _Residue_seq_code _Residue_label 1 SER 2 ASP 3 LEU 4 ALA 5 CYS 6 ARG 7 LEU 8 LEU 9 GLY 10 GLN 11 SER 12 MET 13 ASP 14 GLU 15 SER 16 GLY 17 LEU 18 PRO 19 GLN 20 LEU 21 THR 22 SER 23 TYR 24 ASP 25 CYS 26 GLU 27 VAL 28 ASN 29 ALA 30 PRO 31 ILE 32 GLN 33 GLY 34 SER 35 ARG 36 ASN 37 LEU 38 LEU 39 GLN 40 GLY 41 GLU 42 GLU 43 LEU 44 LEU 45 ARG 46 ALA 47 LEU 48 ASP 49 GLN 50 VAL 51 ASN stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 5306 'C-terminal activation domain of hypoxia inducible factor-1alpha' 80.39 42 100.00 100.00 5.66e-15 PDB 1H2K 'Factor Inhibiting Hif-1 Alpha In Complex With Hif-1 Alpha Fragment Peptide' 80.39 41 100.00 100.00 5.39e-15 PDB 1H2L 'Factor Inhibiting Hif-1 Alpha In Complex With Hif-1 Alpha Fragment Peptide' 80.39 41 100.00 100.00 5.39e-15 PDB 1H2M 'Factor Inhibiting Hif-1 Alpha In Complex With Hif-1 Alpha Fragment Peptide' 100.00 52 100.00 100.00 1.53e-20 PDB 1L3E 'Nmr Structures Of The Hif-1alpha CtadP300 CH1 COMPLEX' 80.39 42 100.00 100.00 5.66e-15 PDB 1L8C 'Structural Basis For Hif-1alphaCBP RECOGNITION IN THE Cellular Hypoxic Response' 100.00 51 100.00 100.00 1.39e-20 PDB 2ILM 'Factor Inhibiting Hif-1 Alpha D201a Mutant In Complex With Fe(Ii), Alpha-Ketoglutarate And Hif-1 Alpha 35mer' 80.39 41 100.00 100.00 5.39e-15 DBJ BAA78675 'hypoxia-inducible factor-1 alpha [Bos taurus]' 100.00 823 100.00 100.00 9.24e-22 DBJ BAC28305 'unnamed protein product [Mus musculus]' 100.00 177 100.00 100.00 1.07e-21 DBJ BAC28578 'unnamed protein product [Mus musculus]' 100.00 837 100.00 100.00 8.36e-22 DBJ BAC36320 'unnamed protein product [Mus musculus]' 100.00 736 100.00 100.00 7.63e-22 DBJ BAE01417 'unnamed protein product [Macaca fascicularis]' 100.00 826 100.00 100.00 8.02e-22 EMBL CAA64833 'hypoxia-inducible factor one alpha [Mus musculus]' 100.00 810 98.04 98.04 5.89e-21 EMBL CAA70305 'hypoxia-inducible factor one alpha [Mus musculus]' 100.00 810 100.00 100.00 7.63e-22 EMBL CAA70306 'hypoxia-inducible factor one alpha [Mus musculus]' 100.00 822 100.00 100.00 7.50e-22 EMBL CAA70701 'hypoxia-inducible factor 1 [Rattus norvegicus]' 100.00 825 100.00 100.00 8.58e-22 EMBL CAG29396 'hypoxia inducible factor 1 alpha [Spalax judaei]' 100.00 824 98.04 98.04 7.89e-21 GenBank AAC50152 'hypoxia-inducible factor 1 alpha' 100.00 826 100.00 100.00 7.96e-22 GenBank AAC51210 'ARNT interacting protein' 100.00 826 100.00 100.00 7.96e-22 GenBank AAC52730 'hypoxia-inducible factor 1 alpha' 100.00 822 100.00 100.00 7.96e-22 GenBank AAC53455 'hypoxia-inducible factor 1 alpha [Mus musculus]' 100.00 836 100.00 100.00 8.36e-22 GenBank AAC53461 'hypoxia-inducible factor 1 alpha [Mus musculus]' 100.00 836 100.00 100.00 8.36e-22 PRF 2114407A 'hypoxia-inducible factor 1' 100.00 826 100.00 100.00 7.96e-22 REF NP_001076251 'hypoxia-inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor) [Oryctolagus cuniculus]' 100.00 819 100.00 100.00 9.40e-22 REF NP_001116596 'hypoxia-inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor) [Sus scrofa]' 100.00 824 100.00 100.00 8.16e-22 REF NP_001521 'hypoxia-inducible factor 1, alpha subunit isoform 1 [Homo sapiens]' 100.00 826 100.00 100.00 7.96e-22 REF NP_034561 'hypoxia inducible factor 1, alpha subunit [Mus musculus]' 100.00 836 100.00 100.00 8.36e-22 REF NP_077335 'hypoxia inducible factor 1, alpha subunit [Rattus norvegicus]' 100.00 823 100.00 100.00 8.29e-22 SWISS-PROT O35800 'Hypoxia-inducible factor 1 alpha (HIF-1 alpha) (HIF1 alpha)' 100.00 825 100.00 100.00 8.58e-22 SWISS-PROT Q0PGG7 'Hypoxia-inducible factor 1 alpha (HIF-1 alpha) (HIF1 alpha)' 100.00 823 98.04 98.04 2.97e-21 SWISS-PROT Q16665 ; Hypoxia-inducible factor 1 alpha (HIF-1 alpha) (HIF1 alpha) (ARNT-interacting protein) (Member of PAS protein 1) (Basic-helix-loop-helix-PAS protein MOP1) ; 100.00 826 100.00 100.00 7.96e-22 SWISS-PROT Q309Z6 'Hypoxia-inducible factor 1 alpha (HIF-1 alpha) (HIF1 alpha)' 100.00 819 98.04 98.04 7.57e-21 SWISS-PROT Q61221 'Hypoxia-inducible factor 1 alpha (HIF-1 alpha) (HIF1 alpha) (ARNT-interacting protein)' 100.00 836 100.00 100.00 8.58e-22 stop_ save_ save_CBP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'CREB-binding protein' _Abbreviation_common CBP _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . _Residue_count 95 _Mol_residue_sequence ; ADPEKRKLIQQQLVLLLHAH KCQRREQANGEVRACSLPHC RTMKNVLNHMTHCQAGKACQ VAHCASSRQIISHWKNCTRH DCPVCLPLKNASDKR ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ASP 3 PRO 4 GLU 5 LYS 6 ARG 7 LYS 8 LEU 9 ILE 10 GLN 11 GLN 12 GLN 13 LEU 14 VAL 15 LEU 16 LEU 17 LEU 18 HIS 19 ALA 20 HIS 21 LYS 22 CYS 23 GLN 24 ARG 25 ARG 26 GLU 27 GLN 28 ALA 29 ASN 30 GLY 31 GLU 32 VAL 33 ARG 34 ALA 35 CYS 36 SER 37 LEU 38 PRO 39 HIS 40 CYS 41 ARG 42 THR 43 MET 44 LYS 45 ASN 46 VAL 47 LEU 48 ASN 49 HIS 50 MET 51 THR 52 HIS 53 CYS 54 GLN 55 ALA 56 GLY 57 LYS 58 ALA 59 CYS 60 GLN 61 VAL 62 ALA 63 HIS 64 CYS 65 ALA 66 SER 67 SER 68 ARG 69 GLN 70 ILE 71 ILE 72 SER 73 HIS 74 TRP 75 LYS 76 ASN 77 CYS 78 THR 79 ARG 80 HIS 81 ASP 82 CYS 83 PRO 84 VAL 85 CYS 86 LEU 87 PRO 88 LEU 89 LYS 90 ASN 91 ALA 92 SER 93 ASP 94 LYS 95 ARG stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 5987 'CBP TAZ1 domain' 100.00 100 100.00 100.00 4.11e-48 BMRB 6268 'CBP TAZ1 domain' 100.00 100 100.00 100.00 4.11e-48 PDB 1L8C 'Structural Basis For Hif-1alphaCBP RECOGNITION IN THE Cellular Hypoxic Response' 98.95 95 100.00 100.00 2.11e-47 PDB 1R8U 'Nmr Structure Of Cbp Taz1CITED2 COMPLEX' 98.95 100 100.00 100.00 1.54e-47 PDB 1U2N 'Structure Cbp Taz1 Domain' 98.95 100 98.94 98.94 1.49e-46 DBJ BAE06125 'CREBBP variant protein [Homo sapiens]' 64.21 2472 98.36 98.36 4.43e-22 DBJ BAG65526 'unnamed protein product [Homo sapiens]' 55.79 1198 100.00 100.00 2.18e-25 GenBank AAB28651 'CREB-binding protein; CBP [Mus sp.]' 100.00 2441 98.95 98.95 4.55e-44 GenBank AAC08447 'CBP [Homo sapiens]' 100.00 555 100.00 100.00 2.33e-52 GenBank AAC51331 'CREB-binding protein [Homo sapiens]' 100.00 2442 100.00 100.00 4.02e-45 GenBank AAC51770 'CREB-binding protein' 100.00 2442 100.00 100.00 4.02e-45 GenBank AAH72594 'Crebbp protein [Mus musculus]' 100.00 1589 100.00 100.00 1.56e-51 PRF 1923401A 'protein CBP' 100.00 2441 98.95 98.95 4.37e-44 REF NP_001020603 'CREB binding protein [Mus musculus]' 100.00 2441 100.00 100.00 4.12e-45 REF NP_001073315 'CREB binding protein isoform b [Homo sapiens]' 64.21 2404 98.36 98.36 4.62e-22 REF NP_004371 'CREB binding protein isoform a [Homo sapiens]' 100.00 2442 100.00 100.00 4.02e-45 REF NP_596872 'CREB binding protein [Rattus norvegicus]' 100.00 2442 100.00 100.00 3.98e-45 REF XP_001095225 'PREDICTED: CREB binding protein [Macaca mulatta]' 100.00 2442 100.00 100.00 4.19e-45 SWISS-PROT P45481 'CREB-binding protein' 100.00 2441 98.95 98.95 4.55e-44 SWISS-PROT Q92793 'CREB-binding protein' 100.00 2442 100.00 100.00 4.02e-45 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Jun 10 14:23:33 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Hif-1alpha Human 9606 Eukaryota Metazoa Homo sapiens $CBP Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $Hif-1alpha 'recombinant technology' 'E. coli' . . BL21(DE3) . $CBP 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Hif-1alpha 2 mM . $CBP 1 mM '[U-13C; U-15N]' $ZN 3 mM . D-TRIS 10 mM . D-DTT 10 mM . NaN3 0.02 % . ZNSO4 0.5 mM . H2O 90 % . D2O 10 % . stop_ save_ save_Sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Hif-1alpha 2 mM . $CBP 1 mM '[U-13C; U-15N]' $ZN 3 mM . D-TRIS 10 mM . D-DTT 10 mM . NaN3 0.02 % . ZNSO4 0.5 mM . D2O 100 % . stop_ save_ save_Sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Hif-1alpha 2 mM . $CBP 1 mM [U-15N] $ZN 3 mM . D-TRIS 10 mM . D-DTT 10 mM . NaN3 0.02 % . ZNSO4 0.5 mM . H2O 90 % . D2O 10 % . stop_ save_ save_Sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Hif-1alpha 1 mM '[U-13C; U-15N]' $CBP 2 mM . $ZN 6 mM . D-TRIS 10 mM . D-DTT 10 mM . NaN3 0.02 % . ZNSO4 0.5 mM . H2O 90 % . D2O 10 % . stop_ save_ save_Sample_5 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Hif-1alpha 1 mM '[U-13C; U-15N]' $CBP 2 mM . $ZN 6 mM . D-TRIS 10 mM . D-DTT 10 mM . NaN3 0.02 % . ZNSO4 0.5 mM . D2O 100 % . stop_ save_ save_Sample_6 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Hif-1alpha 1 mM [U-15N] $CBP 2 mM . $ZN 6 mM . D-TRIS 10 mM . D-DTT 10 mM . NaN3 0.02 % . ZNSO4 0.5 mM . H2O 90 % . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DRX _Field_strength 800 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_1H-13C_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C NOESY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.15 0.02 M pH 6.1 0.2 n/a temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N NOESY' '1H-13C NOESY' stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Hif-1alpha _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 ASP N N 122.533 0.13 1 2 . 2 ASP H H 8.755 0.012 1 3 . 2 ASP CA C 54.573 0.06 1 4 . 2 ASP HA H 4.883 0.012 1 5 . 2 ASP CB C 41.611 0.06 1 6 . 2 ASP HB2 H 2.929 0.012 2 7 . 2 ASP HB3 H 2.849 0.012 2 8 . 3 LEU N N 123.232 0.13 1 9 . 3 LEU H H 8.547 0.012 1 10 . 3 LEU CA C 56.214 0.06 1 11 . 3 LEU HA H 4.410 0.012 1 12 . 3 LEU CB C 42.425 0.06 1 13 . 3 LEU HB2 H 1.811 0.012 1 14 . 3 LEU CG C 27.127 0.06 1 15 . 3 LEU HG H 1.820 0.012 1 16 . 3 LEU CD1 C 24.975 0.06 2 17 . 3 LEU HD1 H 1.104 0.012 1 18 . 3 LEU CD2 C 24.010 0.06 2 19 . 3 LEU HD2 H 1.041 0.012 1 20 . 4 ALA N N 123.475 0.13 1 21 . 4 ALA H H 8.486 0.012 1 22 . 4 ALA CA C 53.621 0.06 1 23 . 4 ALA HA H 4.381 0.012 1 24 . 4 ALA CB C 19.046 0.06 1 25 . 4 ALA HB H 1.586 0.012 1 26 . 5 CYS N N 117.306 0.13 1 27 . 5 CYS H H 8.287 0.012 1 28 . 5 CYS CA C 59.578 0.06 1 29 . 5 CYS HA H 4.540 0.012 1 30 . 5 CYS CB C 27.793 0.06 1 31 . 5 CYS HB2 H 3.132 0.012 1 32 . 6 ARG N N 122.776 0.13 1 33 . 6 ARG H H 8.386 0.012 1 34 . 6 ARG CA C 57.165 0.06 1 35 . 6 ARG HA H 4.488 0.012 1 36 . 6 ARG CB C 30.830 0.06 1 37 . 6 ARG HB2 H 2.043 0.012 2 38 . 6 ARG HB3 H 2.002 0.012 2 39 . 6 ARG CG C 27.505 0.06 1 40 . 6 ARG HG2 H 1.815 0.012 1 41 . 6 ARG CD C 43.600 0.06 1 42 . 6 ARG HD2 H 3.364 0.012 1 43 . 6 ARG NE N 84.706 0.13 1 44 . 6 ARG HE H 7.410 0.012 1 45 . 7 LEU N N 122.096 0.13 1 46 . 7 LEU H H 8.365 0.012 1 47 . 7 LEU CA C 55.650 0.06 1 48 . 7 LEU HA H 4.508 0.012 1 49 . 7 LEU CB C 42.450 0.06 1 50 . 7 LEU HB2 H 1.837 0.012 2 51 . 7 LEU HB3 H 1.722 0.012 2 52 . 7 LEU CG C 27.209 0.06 1 53 . 7 LEU HG H 1.822 0.012 1 54 . 7 LEU CD1 C 25.353 0.06 2 55 . 7 LEU HD1 H 1.077 0.012 1 56 . 7 LEU CD2 C 23.554 0.06 2 57 . 7 LEU HD2 H 1.016 0.012 1 58 . 8 LEU N N 121.898 0.13 1 59 . 8 LEU H H 8.298 0.012 1 60 . 8 LEU CA C 55.689 0.06 1 61 . 8 LEU HA H 4.492 0.012 1 62 . 8 LEU CB C 42.440 0.06 1 63 . 8 LEU HB2 H 1.880 0.012 2 64 . 8 LEU HB3 H 1.760 0.012 2 65 . 8 LEU CG C 27.181 0.06 1 66 . 8 LEU HG H 1.810 0.012 1 67 . 8 LEU CD1 C 25.310 0.06 2 68 . 8 LEU HD1 H 1.065 0.012 1 69 . 8 LEU CD2 C 23.589 0.06 2 70 . 8 LEU HD2 H 1.026 0.012 1 71 . 9 GLY N N 109.198 0.13 1 72 . 9 GLY H H 8.488 0.012 1 73 . 9 GLY CA C 45.759 0.06 1 74 . 9 GLY HA2 H 4.119 0.012 1 75 . 10 GLN N N 119.707 0.13 1 76 . 10 GLN H H 8.306 0.012 1 77 . 10 GLN CA C 55.988 0.06 1 78 . 10 GLN HA H 4.562 0.012 1 79 . 10 GLN CB C 29.869 0.06 1 80 . 10 GLN HB2 H 2.178 0.012 2 81 . 10 GLN HB3 H 2.320 0.012 2 82 . 10 GLN CG C 34.102 0.06 1 83 . 10 GLN HG2 H 2.528 0.012 1 84 . 10 GLN NE2 N 112.502 0.13 1 85 . 10 GLN HE21 H 7.731 0.012 2 86 . 10 GLN HE22 H 7.012 0.012 2 87 . 11 SER N N 117.196 0.13 1 88 . 11 SER H H 8.585 0.012 1 89 . 11 SER CA C 58.754 0.06 1 90 . 11 SER HA H 4.625 0.012 1 91 . 11 SER CB C 63.939 0.06 1 92 . 11 SER HB2 H 4.070 0.012 1 93 . 12 MET N N 122.351 0.13 1 94 . 12 MET H H 8.625 0.012 1 95 . 12 MET CA C 55.759 0.06 1 96 . 12 MET HA H 4.701 0.012 1 97 . 12 MET CB C 33.270 0.06 1 98 . 12 MET HB2 H 2.178 0.012 2 99 . 12 MET HB3 H 2.277 0.012 2 100 . 12 MET CG C 32.293 0.06 1 101 . 12 MET HG2 H 2.770 0.012 2 102 . 12 MET HG3 H 2.697 0.012 2 103 . 12 MET CE C 17.292 0.06 1 104 . 12 MET HE H 2.241 0.012 1 105 . 13 ASP N N 121.239 0.13 1 106 . 13 ASP H H 8.476 0.012 1 107 . 13 ASP CA C 54.576 0.06 1 108 . 13 ASP HA H 4.778 0.012 1 109 . 13 ASP CB C 41.516 0.06 1 110 . 13 ASP HB2 H 2.892 0.012 1 111 . 14 GLU N N 121.678 0.13 1 112 . 14 GLU H H 8.657 0.012 1 113 . 14 GLU CA C 57.131 0.06 1 114 . 14 GLU HA H 4.484 0.012 1 115 . 14 GLU CB C 30.226 0.06 1 116 . 14 GLU HB2 H 2.160 0.012 2 117 . 14 GLU HB3 H 2.319 0.012 2 118 . 14 GLU CG C 36.464 0.06 1 119 . 14 GLU HG2 H 2.455 0.012 1 120 . 15 SER N N 116.713 0.13 1 121 . 15 SER H H 8.597 0.012 1 122 . 15 SER CA C 59.187 0.06 1 123 . 15 SER HA H 4.636 0.012 1 124 . 15 SER CB C 64.127 0.06 1 125 . 15 SER HB2 H 4.158 0.012 2 126 . 15 SER HB3 H 4.122 0.012 2 127 . 16 GLY N N 110.263 0.13 1 128 . 16 GLY H H 8.524 0.012 1 129 . 16 GLY CA C 45.358 0.06 1 130 . 16 GLY HA2 H 4.172 0.012 1 131 . 17 LEU N N 124.353 0.13 1 132 . 17 LEU H H 8.209 0.012 1 133 . 17 LEU CA C 52.330 0.06 1 134 . 17 LEU HA H 4.473 0.012 1 135 . 17 LEU CB C 42.650 0.06 1 136 . 17 LEU HB2 H 1.567 0.012 2 137 . 17 LEU HB3 H 0.749 0.012 2 138 . 17 LEU CG C 26.303 0.06 1 139 . 17 LEU HG H 1.264 0.012 1 140 . 17 LEU CD1 C 24.921 0.06 2 141 . 17 LEU HD1 H 0.392 0.012 1 142 . 17 LEU CD2 C 24.399 0.06 2 143 . 17 LEU HD2 H 0.581 0.012 1 144 . 18 PRO CA C 63.228 0.06 1 145 . 18 PRO HA H 4.487 0.012 1 146 . 18 PRO CB C 32.188 0.06 1 147 . 18 PRO HB2 H 2.425 0.012 2 148 . 18 PRO HB3 H 1.890 0.012 2 149 . 18 PRO CG C 28.100 0.06 1 150 . 18 PRO HG2 H 2.250 0.012 2 151 . 18 PRO HG3 H 2.153 0.012 2 152 . 18 PRO CD C 50.907 0.06 1 153 . 18 PRO HD2 H 4.046 0.012 2 154 . 18 PRO HD3 H 3.586 0.012 2 155 . 19 GLN N N 121.741 0.13 1 156 . 19 GLN H H 8.708 0.012 1 157 . 19 GLN CA C 55.383 0.06 1 158 . 19 GLN HA H 4.668 0.012 1 159 . 19 GLN CB C 28.828 0.06 1 160 . 19 GLN HB2 H 2.082 0.012 2 161 . 19 GLN HB3 H 2.017 0.012 2 162 . 19 GLN CG C 34.552 0.06 1 163 . 19 GLN HG2 H 2.405 0.012 2 164 . 19 GLN HG3 H 2.045 0.012 2 165 . 19 GLN NE2 N 112.550 0.13 1 166 . 19 GLN HE21 H 7.789 0.012 2 167 . 19 GLN HE22 H 7.049 0.012 2 168 . 20 LEU N N 128.560 0.13 1 169 . 20 LEU H H 9.408 0.012 1 170 . 20 LEU CA C 53.702 0.06 1 171 . 20 LEU HA H 4.927 0.012 1 172 . 20 LEU CB C 44.072 0.06 1 173 . 20 LEU HB2 H 1.743 0.012 2 174 . 20 LEU HB3 H 1.535 0.012 2 175 . 20 LEU CG C 27.193 0.06 1 176 . 20 LEU HG H 1.906 0.012 1 177 . 20 LEU CD1 C 26.802 0.06 2 178 . 20 LEU HD1 H 0.927 0.012 1 179 . 20 LEU CD2 C 23.464 0.06 2 180 . 20 LEU HD2 H 1.013 0.012 1 181 . 21 THR N N 113.007 0.13 1 182 . 21 THR H H 9.441 0.012 1 183 . 21 THR CA C 60.353 0.06 1 184 . 21 THR HA H 4.789 0.012 1 185 . 21 THR CB C 72.010 0.06 1 186 . 21 THR HB H 4.935 0.012 1 187 . 21 THR CG2 C 22.137 0.06 1 188 . 21 THR HG2 H 1.559 0.012 1 189 . 22 SER N N 117.449 0.13 1 190 . 22 SER H H 9.316 0.012 1 191 . 22 SER CA C 62.329 0.06 1 192 . 22 SER HA H 4.111 0.012 1 193 . 22 SER CB C 62.369 0.06 1 194 . 22 SER HB2 H 4.114 0.012 1 195 . 23 TYR N N 122.071 0.13 1 196 . 23 TYR H H 8.351 0.012 1 197 . 23 TYR CA C 61.739 0.06 1 198 . 23 TYR HA H 4.374 0.012 1 199 . 23 TYR CB C 38.185 0.06 1 200 . 23 TYR HB2 H 3.346 0.012 2 201 . 23 TYR HB3 H 2.995 0.012 2 202 . 23 TYR HD1 H 7.258 0.012 1 203 . 23 TYR HE1 H 6.944 0.012 1 204 . 23 TYR CD1 C 133.363 0.06 2 205 . 23 TYR CE1 C 118.560 0.06 2 206 . 24 ASP N N 117.697 0.13 1 207 . 24 ASP H H 8.154 0.012 1 208 . 24 ASP CA C 57.791 0.06 1 209 . 24 ASP HA H 4.373 0.012 1 210 . 24 ASP CB C 41.807 0.06 1 211 . 24 ASP HB2 H 3.274 0.012 2 212 . 24 ASP HB3 H 2.403 0.012 2 213 . 25 CYS N N 118.030 0.13 1 214 . 25 CYS H H 7.804 0.012 1 215 . 25 CYS CA C 63.665 0.06 1 216 . 25 CYS HA H 4.152 0.012 1 217 . 25 CYS CB C 27.582 0.06 1 218 . 25 CYS HB2 H 3.255 0.012 2 219 . 25 CYS HB3 H 2.749 0.012 2 220 . 26 GLU N N 122.531 0.13 1 221 . 26 GLU H H 8.753 0.012 1 222 . 26 GLU CA C 59.545 0.06 1 223 . 26 GLU HA H 4.038 0.012 1 224 . 26 GLU CB C 29.540 0.06 1 225 . 26 GLU HB2 H 2.272 0.012 2 226 . 26 GLU HB3 H 2.055 0.012 2 227 . 26 GLU CG C 36.752 0.06 1 228 . 26 GLU HG2 H 2.514 0.012 2 229 . 26 GLU HG3 H 2.295 0.012 2 230 . 27 VAL N N 113.577 0.13 1 231 . 27 VAL H H 7.812 0.012 1 232 . 27 VAL CA C 65.004 0.06 1 233 . 27 VAL HA H 3.867 0.012 1 234 . 27 VAL CB C 32.571 0.06 1 235 . 27 VAL HB H 1.883 0.012 1 236 . 27 VAL CG2 C 21.078 0.06 2 237 . 27 VAL HG2 H 0.857 0.012 1 238 . 27 VAL CG1 C 21.825 0.06 2 239 . 27 VAL HG1 H 0.748 0.012 1 240 . 28 ASN N N 113.404 0.13 1 241 . 28 ASN H H 7.225 0.012 1 242 . 28 ASN CA C 55.582 0.06 1 243 . 28 ASN HA H 4.758 0.012 1 244 . 28 ASN CB C 41.673 0.06 1 245 . 28 ASN HB2 H 2.662 0.012 2 246 . 28 ASN HB3 H 2.391 0.012 2 247 . 28 ASN ND2 N 116.290 0.13 1 248 . 28 ASN HD21 H 8.130 0.012 2 249 . 28 ASN HD22 H 7.802 0.012 2 250 . 29 ALA N N 123.316 0.13 1 251 . 29 ALA H H 8.332 0.012 1 252 . 29 ALA CA C 50.032 0.06 1 253 . 29 ALA HA H 4.258 0.012 1 254 . 29 ALA CB C 17.752 0.06 1 255 . 29 ALA HB H 1.048 0.012 1 256 . 30 PRO CA C 63.558 0.06 1 257 . 30 PRO HA H 4.641 0.012 1 258 . 30 PRO CB C 32.773 0.06 1 259 . 30 PRO HB2 H 2.625 0.012 2 260 . 30 PRO HB3 H 2.069 0.012 2 261 . 30 PRO CG C 27.457 0.06 1 262 . 30 PRO HG2 H 2.174 0.012 1 263 . 30 PRO CD C 50.373 0.06 1 264 . 30 PRO HD2 H 3.513 0.012 2 265 . 30 PRO HD3 H 3.364 0.012 2 266 . 31 ILE N N 122.816 0.13 1 267 . 31 ILE H H 9.174 0.012 1 268 . 31 ILE CA C 61.560 0.06 1 269 . 31 ILE HA H 4.422 0.012 1 270 . 31 ILE CB C 39.702 0.06 1 271 . 31 ILE HB H 1.934 0.012 1 272 . 31 ILE CG1 C 27.580 0.06 2 273 . 31 ILE HG12 H 1.870 0.012 1 274 . 31 ILE HG13 H 0.974 0.012 1 275 . 31 ILE CD1 C 14.901 0.06 1 276 . 31 ILE HD1 H 1.020 0.012 1 277 . 31 ILE CG2 C 18.735 0.06 2 278 . 31 ILE HG2 H 1.006 0.012 1 279 . 32 GLN N N 127.096 0.13 1 280 . 32 GLN H H 8.770 0.012 1 281 . 32 GLN CA C 56.619 0.06 1 282 . 32 GLN HA H 4.474 0.012 1 283 . 32 GLN CB C 29.580 0.06 1 284 . 32 GLN HB2 H 2.228 0.012 1 285 . 32 GLN CG C 34.410 0.06 1 286 . 32 GLN HG2 H 2.559 0.012 2 287 . 32 GLN HG3 H 2.509 0.012 2 288 . 32 GLN NE2 N 113.523 0.13 1 289 . 32 GLN HE21 H 7.710 0.012 2 290 . 32 GLN HE22 H 7.289 0.012 2 291 . 33 GLY N N 110.620 0.13 1 292 . 33 GLY H H 8.677 0.012 1 293 . 33 GLY CA C 46.009 0.06 1 294 . 33 GLY HA2 H 4.258 0.012 2 295 . 33 GLY HA3 H 3.991 0.012 2 296 . 34 SER N N 116.100 0.13 1 297 . 34 SER H H 8.525 0.012 1 298 . 34 SER CA C 59.202 0.06 1 299 . 34 SER HA H 4.438 0.012 1 300 . 34 SER CB C 63.152 0.06 1 301 . 34 SER HB2 H 4.107 0.012 2 302 . 34 SER HB3 H 4.071 0.012 2 303 . 35 ARG N N 119.818 0.13 1 304 . 35 ARG H H 8.032 0.012 1 305 . 35 ARG CA C 56.486 0.06 1 306 . 35 ARG HA H 4.364 0.012 1 307 . 35 ARG CB C 30.097 0.06 1 308 . 35 ARG HB2 H 1.916 0.012 2 309 . 35 ARG HB3 H 2.100 0.012 2 310 . 35 ARG CG C 27.488 0.06 1 311 . 35 ARG HG2 H 1.784 0.012 1 312 . 35 ARG CD C 43.516 0.06 1 313 . 35 ARG HD2 H 3.342 0.012 1 314 . 35 ARG NE N 85.176 0.13 1 315 . 35 ARG HE H 7.321 0.012 1 316 . 36 ASN N N 117.282 0.13 1 317 . 36 ASN H H 8.228 0.012 1 318 . 36 ASN CA C 53.196 0.06 1 319 . 36 ASN HA H 4.857 0.012 1 320 . 36 ASN CB C 39.686 0.06 1 321 . 36 ASN HB2 H 2.984 0.012 2 322 . 36 ASN HB3 H 2.790 0.012 2 323 . 36 ASN ND2 N 113.080 0.13 1 324 . 36 ASN HD21 H 7.750 0.012 2 325 . 36 ASN HD22 H 7.129 0.012 2 326 . 37 LEU N N 121.100 0.13 1 327 . 37 LEU H H 8.253 0.012 1 328 . 37 LEU CA C 54.784 0.06 1 329 . 37 LEU HA H 4.381 0.012 1 330 . 37 LEU CB C 42.437 0.06 1 331 . 37 LEU HB2 H 1.782 0.012 2 332 . 37 LEU HB3 H 1.492 0.012 2 333 . 37 LEU CG C 27.225 0.06 1 334 . 37 LEU HG H 1.800 0.012 1 335 . 37 LEU CD1 C 25.337 0.06 2 336 . 37 LEU HD1 H 1.080 0.012 1 337 . 37 LEU CD2 C 24.537 0.06 2 338 . 37 LEU HD2 H 1.038 0.012 1 339 . 38 LEU N N 124.015 0.13 1 340 . 38 LEU H H 8.130 0.012 1 341 . 38 LEU CA C 55.317 0.06 1 342 . 38 LEU HA H 4.410 0.012 1 343 . 38 LEU CB C 43.378 0.06 1 344 . 38 LEU HB2 H 1.757 0.012 2 345 . 38 LEU HB3 H 1.221 0.012 2 346 . 38 LEU CG C 27.086 0.06 1 347 . 38 LEU HG H 2.028 0.012 1 348 . 38 LEU CD1 C 26.790 0.06 2 349 . 38 LEU HD1 H 1.013 0.012 1 350 . 38 LEU CD2 C 23.025 0.06 2 351 . 38 LEU HD2 H 1.018 0.012 1 352 . 39 GLN N N 116.111 0.13 1 353 . 39 GLN H H 8.712 0.012 1 354 . 39 GLN CA C 53.981 0.06 1 355 . 39 GLN HA H 4.515 0.012 1 356 . 39 GLN CB C 32.752 0.06 1 357 . 39 GLN HB2 H 2.075 0.012 2 358 . 39 GLN HB3 H 2.282 0.012 2 359 . 39 GLN CG C 33.016 0.06 1 360 . 39 GLN HG2 H 2.520 0.012 1 361 . 39 GLN NE2 N 111.885 0.13 1 362 . 39 GLN HE21 H 7.533 0.012 2 363 . 39 GLN HE22 H 6.935 0.012 2 364 . 40 GLY N N 109.939 0.13 1 365 . 40 GLY H H 9.126 0.012 1 366 . 40 GLY CA C 46.830 0.06 1 367 . 40 GLY HA2 H 4.292 0.012 2 368 . 40 GLY HA3 H 4.116 0.012 2 369 . 41 GLU N N 124.249 0.13 1 370 . 41 GLU H H 9.231 0.012 1 371 . 41 GLU CA C 59.247 0.06 1 372 . 41 GLU HA H 4.111 0.012 1 373 . 41 GLU CB C 29.552 0.06 1 374 . 41 GLU HB2 H 2.339 0.012 2 375 . 41 GLU HB3 H 2.266 0.012 2 376 . 41 GLU CG C 36.765 0.06 1 377 . 41 GLU HG2 H 2.589 0.012 2 378 . 41 GLU HG3 H 2.535 0.012 2 379 . 42 GLU N N 117.688 0.13 1 380 . 42 GLU H H 8.251 0.012 1 381 . 42 GLU CA C 59.312 0.06 1 382 . 42 GLU HA H 4.155 0.012 1 383 . 42 GLU CB C 30.226 0.06 1 384 . 42 GLU HB2 H 2.460 0.012 2 385 . 42 GLU HB3 H 2.291 0.012 2 386 . 42 GLU CG C 36.750 0.06 1 387 . 42 GLU HG2 H 2.697 0.012 2 388 . 42 GLU HG3 H 2.541 0.012 2 389 . 43 LEU N N 118.856 0.13 1 390 . 43 LEU H H 7.531 0.012 1 391 . 43 LEU CA C 58.189 0.06 1 392 . 43 LEU HA H 3.954 0.012 1 393 . 43 LEU CB C 42.625 0.06 1 394 . 43 LEU HB2 H 1.853 0.012 2 395 . 43 LEU HB3 H 1.557 0.012 2 396 . 43 LEU CG C 27.571 0.06 1 397 . 43 LEU HG H 1.456 0.012 1 398 . 43 LEU CD1 C 26.100 0.06 2 399 . 43 LEU HD1 H 1.023 0.012 1 400 . 43 LEU CD2 C 25.965 0.06 2 401 . 43 LEU HD2 H 1.092 0.012 1 402 . 44 LEU N N 115.146 0.13 1 403 . 44 LEU H H 6.843 0.012 1 404 . 44 LEU CA C 57.150 0.06 1 405 . 44 LEU HA H 3.870 0.012 1 406 . 44 LEU CB C 40.707 0.06 1 407 . 44 LEU HB2 H 2.115 0.012 2 408 . 44 LEU HB3 H 1.641 0.012 2 409 . 44 LEU CG C 27.177 0.06 1 410 . 44 LEU HG H 1.773 0.012 1 411 . 44 LEU CD1 C 25.593 0.06 2 412 . 44 LEU HD1 H 1.194 0.012 1 413 . 44 LEU CD2 C 22.394 0.06 2 414 . 44 LEU HD2 H 0.951 0.012 1 415 . 45 ARG N N 116.775 0.13 1 416 . 45 ARG H H 8.108 0.012 1 417 . 45 ARG CA C 58.885 0.06 1 418 . 45 ARG HA H 4.332 0.012 1 419 . 45 ARG CB C 30.559 0.06 1 420 . 45 ARG HB2 H 1.991 0.012 2 421 . 45 ARG HB3 H 2.073 0.012 2 422 . 45 ARG CG C 27.858 0.06 1 423 . 45 ARG HG2 H 1.978 0.012 2 424 . 45 ARG HG3 H 1.909 0.012 2 425 . 45 ARG CD C 43.715 0.06 1 426 . 45 ARG HD2 H 3.418 0.012 1 427 . 45 ARG NE N 84.890 0.13 1 428 . 45 ARG HE H 7.788 0.012 1 429 . 46 ALA N N 119.534 0.13 1 430 . 46 ALA H H 7.632 0.012 1 431 . 46 ALA CA C 54.582 0.06 1 432 . 46 ALA HA H 4.305 0.012 1 433 . 46 ALA CB C 19.271 0.06 1 434 . 46 ALA HB H 1.649 0.012 1 435 . 47 LEU N N 115.726 0.13 1 436 . 47 LEU H H 7.364 0.012 1 437 . 47 LEU CA C 55.798 0.06 1 438 . 47 LEU HA H 4.395 0.012 1 439 . 47 LEU CB C 41.377 0.06 1 440 . 47 LEU HB2 H 1.534 0.012 2 441 . 47 LEU HB3 H 1.256 0.012 2 442 . 47 LEU CG C 26.065 0.06 1 443 . 47 LEU HG H 1.949 0.012 1 444 . 47 LEU CD1 C 26.921 0.06 2 445 . 47 LEU HD1 H 0.786 0.012 1 446 . 47 LEU CD2 C 22.692 0.06 2 447 . 47 LEU HD2 H 0.702 0.012 1 448 . 48 ASP N N 118.631 0.13 1 449 . 48 ASP H H 7.771 0.012 1 450 . 48 ASP CA C 55.749 0.06 1 451 . 48 ASP HA H 4.947 0.012 1 452 . 48 ASP CB C 41.748 0.06 1 453 . 48 ASP HB2 H 3.015 0.012 1 454 . 49 GLN N N 119.712 0.13 1 455 . 49 GLN H H 8.101 0.012 1 456 . 49 GLN CA C 56.482 0.06 1 457 . 49 GLN HA H 4.598 0.012 1 458 . 49 GLN CB C 30.076 0.06 1 459 . 49 GLN HB2 H 2.424 0.012 2 460 . 49 GLN HB3 H 2.330 0.012 2 461 . 49 GLN CG C 34.555 0.06 1 462 . 49 GLN HG2 H 2.650 0.012 2 463 . 49 GLN HG3 H 2.608 0.012 2 464 . 49 GLN NE2 N 112.567 0.13 1 465 . 49 GLN HE21 H 7.762 0.012 2 466 . 49 GLN HE22 H 7.059 0.012 2 467 . 50 VAL N N 120.777 0.13 1 468 . 50 VAL H H 8.316 0.012 1 469 . 50 VAL CA C 62.569 0.06 1 470 . 50 VAL HA H 4.425 0.012 1 471 . 50 VAL CB C 32.995 0.06 1 472 . 50 VAL HB H 2.375 0.012 1 473 . 50 VAL CG2 C 20.840 0.06 2 474 . 50 VAL HG2 H 1.184 0.012 1 475 . 50 VAL CG1 C 21.630 0.06 2 476 . 50 VAL HG1 H 1.165 0.012 1 477 . 51 ASN N N 127.632 0.13 1 478 . 51 ASN H H 8.217 0.012 1 479 . 51 ASN CA C 55.005 0.06 1 480 . 51 ASN HA H 4.669 0.012 1 481 . 51 ASN CB C 40.648 0.06 1 482 . 51 ASN HB2 H 2.958 0.012 2 483 . 51 ASN HB3 H 2.855 0.012 2 484 . 51 ASN ND2 N 112.848 0.13 1 485 . 51 ASN HD21 H 7.571 0.012 2 486 . 51 ASN HD22 H 6.939 0.012 2 stop_ save_ save_shift_set_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N NOESY' '1H-13C NOESY' stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name CBP _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 ALA CA C 52.100 0.06 1 2 . 1 ALA HA H 4.111 0.012 1 3 . 1 ALA CB C 19.694 0.06 1 4 . 1 ALA HB H 1.666 0.012 1 5 . 2 ASP CA C 51.961 0.06 1 6 . 2 ASP HA H 5.260 0.012 1 7 . 2 ASP CB C 42.650 0.06 1 8 . 2 ASP HB2 H 2.959 0.012 2 9 . 2 ASP HB3 H 2.808 0.012 2 10 . 3 PRO CA C 64.849 0.06 1 11 . 3 PRO HA H 4.414 0.012 1 12 . 3 PRO CB C 32.510 0.06 1 13 . 3 PRO HB2 H 2.562 0.012 2 14 . 3 PRO HB3 H 2.180 0.012 2 15 . 3 PRO CG C 27.650 0.06 1 16 . 3 PRO HG2 H 2.324 0.012 2 17 . 3 PRO HG3 H 2.239 0.012 2 18 . 3 PRO CD C 51.307 0.06 1 19 . 3 PRO HD2 H 4.089 0.012 1 20 . 4 GLU N N 119.307 0.13 1 21 . 4 GLU H H 8.521 0.012 1 22 . 4 GLU CA C 58.847 0.06 1 23 . 4 GLU HA H 4.335 0.012 1 24 . 4 GLU CB C 29.347 0.06 1 25 . 4 GLU HB2 H 2.277 0.012 1 26 . 4 GLU CG C 36.496 0.06 1 27 . 4 GLU HG2 H 2.524 0.012 2 28 . 4 GLU HG3 H 2.452 0.012 2 29 . 5 LYS N N 119.372 0.13 1 30 . 5 LYS H H 8.036 0.012 1 31 . 5 LYS CA C 58.562 0.06 1 32 . 5 LYS HA H 4.157 0.012 1 33 . 5 LYS CB C 32.292 0.06 1 34 . 5 LYS HB2 H 2.117 0.012 2 35 . 5 LYS HB3 H 1.692 0.012 2 36 . 5 LYS CG C 25.643 0.06 1 37 . 5 LYS HG2 H 1.750 0.012 2 38 . 5 LYS HG3 H 1.599 0.012 2 39 . 5 LYS CD C 28.671 0.06 1 40 . 5 LYS HD2 H 1.730 0.012 2 41 . 5 LYS HD3 H 1.621 0.012 2 42 . 5 LYS CE C 42.095 0.06 1 43 . 5 LYS HE2 H 3.158 0.012 1 44 . 6 ARG N N 117.965 0.13 1 45 . 6 ARG H H 8.370 0.012 1 46 . 6 ARG CA C 60.950 0.06 1 47 . 6 ARG HA H 3.839 0.012 1 48 . 6 ARG CB C 30.270 0.06 1 49 . 6 ARG HB2 H 2.104 0.012 2 50 . 6 ARG HB3 H 1.974 0.012 2 51 . 6 ARG CG C 28.188 0.06 1 52 . 6 ARG HG2 H 1.874 0.012 2 53 . 6 ARG HG3 H 1.629 0.012 2 54 . 6 ARG CD C 44.141 0.06 1 55 . 6 ARG HD2 H 3.338 0.012 2 56 . 6 ARG HD3 H 3.302 0.012 2 57 . 7 LYS N N 118.854 0.13 1 58 . 7 LYS H H 7.676 0.012 1 59 . 7 LYS CA C 59.478 0.06 1 60 . 7 LYS HA H 4.341 0.012 1 61 . 7 LYS CB C 32.243 0.06 1 62 . 7 LYS HB2 H 2.102 0.012 1 63 . 7 LYS CG C 25.188 0.06 1 64 . 7 LYS HG2 H 1.747 0.012 2 65 . 7 LYS HG3 H 1.578 0.012 2 66 . 7 LYS CD C 29.465 0.06 1 67 . 7 LYS HD2 H 1.887 0.012 1 68 . 7 LYS CE C 42.390 0.06 1 69 . 7 LYS HE2 H 3.150 0.012 1 70 . 8 LEU N N 118.862 0.13 1 71 . 8 LEU H H 7.697 0.012 1 72 . 8 LEU CA C 58.020 0.06 1 73 . 8 LEU HA H 4.262 0.012 1 74 . 8 LEU CB C 41.976 0.06 1 75 . 8 LEU HB2 H 2.210 0.012 2 76 . 8 LEU HB3 H 1.713 0.012 2 77 . 8 LEU CG C 26.854 0.06 1 78 . 8 LEU HG H 2.100 0.012 1 79 . 8 LEU CD1 C 25.954 0.06 2 80 . 8 LEU HD1 H 1.039 0.012 1 81 . 8 LEU CD2 C 22.451 0.06 2 82 . 8 LEU HD2 H 1.045 0.012 1 83 . 9 ILE N N 122.184 0.13 1 84 . 9 ILE H H 8.442 0.012 1 85 . 9 ILE CA C 65.743 0.06 1 86 . 9 ILE HA H 3.565 0.012 1 87 . 9 ILE CB C 37.755 0.06 1 88 . 9 ILE HB H 2.119 0.012 1 89 . 9 ILE CG1 C 30.900 0.06 2 90 . 9 ILE HG12 H 1.950 0.012 1 91 . 9 ILE HG13 H 1.095 0.012 1 92 . 9 ILE CD1 C 16.074 0.06 1 93 . 9 ILE HD1 H 0.820 0.012 1 94 . 9 ILE CG2 C 17.482 0.06 2 95 . 9 ILE HG2 H 0.903 0.012 1 96 . 10 GLN N N 119.058 0.13 1 97 . 10 GLN H H 8.369 0.012 1 98 . 10 GLN CA C 59.826 0.06 1 99 . 10 GLN HA H 3.962 0.012 1 100 . 10 GLN CB C 29.870 0.06 1 101 . 10 GLN HB2 H 2.568 0.012 2 102 . 10 GLN HB3 H 2.344 0.012 2 103 . 10 GLN CG C 34.546 0.06 1 104 . 10 GLN HG2 H 2.887 0.012 2 105 . 10 GLN HG3 H 2.574 0.012 2 106 . 10 GLN NE2 N 111.120 0.13 1 107 . 10 GLN HE21 H 7.923 0.012 2 108 . 10 GLN HE22 H 6.782 0.012 2 109 . 11 GLN N N 116.856 0.13 1 110 . 11 GLN H H 8.413 0.012 1 111 . 11 GLN CA C 59.189 0.06 1 112 . 11 GLN HA H 4.095 0.012 1 113 . 11 GLN CB C 29.000 0.06 1 114 . 11 GLN HB2 H 2.338 0.012 2 115 . 11 GLN HB3 H 2.269 0.012 2 116 . 11 GLN CG C 35.052 0.06 1 117 . 11 GLN HG2 H 2.639 0.012 2 118 . 11 GLN HG3 H 2.545 0.012 2 119 . 11 GLN NE2 N 111.201 0.13 1 120 . 11 GLN HE21 H 8.028 0.012 2 121 . 11 GLN HE22 H 7.087 0.012 2 122 . 12 GLN N N 121.548 0.13 1 123 . 12 GLN H H 8.413 0.012 1 124 . 12 GLN CA C 60.564 0.06 1 125 . 12 GLN HA H 3.956 0.012 1 126 . 12 GLN CB C 27.914 0.06 1 127 . 12 GLN HB2 H 2.062 0.012 2 128 . 12 GLN HB3 H 2.432 0.012 2 129 . 12 GLN CG C 34.560 0.06 1 130 . 12 GLN HG2 H 2.306 0.012 2 131 . 12 GLN HG3 H 2.228 0.012 2 132 . 12 GLN NE2 N 111.560 0.13 1 133 . 12 GLN HE21 H 7.857 0.012 2 134 . 12 GLN HE22 H 6.964 0.012 2 135 . 13 LEU N N 120.516 0.13 1 136 . 13 LEU H H 8.558 0.012 1 137 . 13 LEU CA C 58.557 0.06 1 138 . 13 LEU HA H 4.129 0.012 1 139 . 13 LEU CB C 41.129 0.06 1 140 . 13 LEU HB2 H 1.438 0.012 2 141 . 13 LEU HB3 H 2.152 0.012 2 142 . 13 LEU CG C 26.871 0.06 1 143 . 13 LEU HG H 1.233 0.012 1 144 . 13 LEU CD1 C 26.449 0.06 2 145 . 13 LEU HD1 H 0.826 0.012 1 146 . 13 LEU CD2 C 20.911 0.06 2 147 . 13 LEU HD2 H 0.513 0.012 1 148 . 14 VAL N N 118.310 0.13 1 149 . 14 VAL H H 8.471 0.012 1 150 . 14 VAL CA C 67.222 0.06 1 151 . 14 VAL HA H 3.627 0.012 1 152 . 14 VAL CB C 31.854 0.06 1 153 . 14 VAL HB H 2.346 0.012 1 154 . 14 VAL CG2 C 23.973 0.06 2 155 . 14 VAL HG2 H 1.238 0.012 1 156 . 14 VAL CG1 C 21.396 0.06 2 157 . 14 VAL HG1 H 1.087 0.012 1 158 . 15 LEU N N 121.014 0.13 1 159 . 15 LEU H H 8.022 0.012 1 160 . 15 LEU CA C 58.210 0.06 1 161 . 15 LEU HA H 4.252 0.012 1 162 . 15 LEU CB C 43.142 0.06 1 163 . 15 LEU HB2 H 2.143 0.012 2 164 . 15 LEU HB3 H 1.582 0.012 2 165 . 15 LEU CG C 27.769 0.06 1 166 . 15 LEU HG H 1.871 0.012 1 167 . 15 LEU CD1 C 25.785 0.06 2 168 . 15 LEU HD1 H 0.995 0.012 1 169 . 15 LEU CD2 C 24.478 0.06 2 170 . 15 LEU HD2 H 1.033 0.012 1 171 . 16 LEU N N 122.814 0.13 1 172 . 16 LEU H H 8.652 0.012 1 173 . 16 LEU CA C 59.270 0.06 1 174 . 16 LEU HA H 4.044 0.012 1 175 . 16 LEU CB C 42.960 0.06 1 176 . 16 LEU HB2 H 2.283 0.012 2 177 . 16 LEU HB3 H 1.375 0.012 2 178 . 16 LEU CG C 27.641 0.06 1 179 . 16 LEU HG H 2.052 0.012 1 180 . 16 LEU CD1 C 23.632 0.06 2 181 . 16 LEU HD1 H 1.131 0.012 1 182 . 16 LEU CD2 C 25.232 0.06 2 183 . 16 LEU HD2 H 1.090 0.012 1 184 . 17 LEU N N 118.310 0.13 1 185 . 17 LEU H H 8.443 0.012 1 186 . 17 LEU CA C 58.598 0.06 1 187 . 17 LEU HA H 4.053 0.012 1 188 . 17 LEU CB C 41.957 0.06 1 189 . 17 LEU HB2 H 1.542 0.012 2 190 . 17 LEU HB3 H 1.971 0.012 2 191 . 17 LEU CG C 27.153 0.06 1 192 . 17 LEU HG H 1.494 0.012 1 193 . 17 LEU CD1 C 25.596 0.06 2 194 . 17 LEU HD1 H 0.458 0.012 1 195 . 17 LEU CD2 C 24.020 0.06 2 196 . 17 LEU HD2 H 0.786 0.012 1 197 . 18 HIS N N 117.340 0.13 1 198 . 18 HIS H H 8.465 0.012 1 199 . 18 HIS CA C 60.500 0.06 1 200 . 18 HIS HA H 4.282 0.012 1 201 . 18 HIS CB C 28.001 0.06 1 202 . 18 HIS HB2 H 3.415 0.012 2 203 . 18 HIS HB3 H 3.551 0.012 2 204 . 18 HIS CD2 C 128.297 0.06 1 205 . 18 HIS HD2 H 7.333 0.012 2 206 . 18 HIS CE1 C 138.833 0.06 1 207 . 18 HIS HE1 H 8.093 0.012 1 208 . 19 ALA N N 122.224 0.13 1 209 . 19 ALA H H 9.384 0.012 1 210 . 19 ALA CA C 55.489 0.06 1 211 . 19 ALA HA H 4.180 0.012 1 212 . 19 ALA CB C 19.207 0.06 1 213 . 19 ALA HB H 1.693 0.012 1 214 . 20 HIS N N 116.122 0.13 1 215 . 20 HIS H H 8.192 0.012 1 216 . 20 HIS CA C 59.230 0.06 1 217 . 20 HIS HA H 4.513 0.012 1 218 . 20 HIS CB C 31.436 0.06 1 219 . 20 HIS HB2 H 3.232 0.012 1 220 . 20 HIS CD2 C 118.975 0.06 1 221 . 20 HIS HD2 H 7.012 0.012 2 222 . 20 HIS CE1 C 138.644 0.06 1 223 . 20 HIS HE1 H 7.584 0.012 1 224 . 21 LYS N N 118.100 0.13 1 225 . 21 LYS H H 7.264 0.012 1 226 . 21 LYS CA C 58.604 0.06 1 227 . 21 LYS HA H 3.966 0.012 1 228 . 21 LYS CB C 32.849 0.06 1 229 . 21 LYS HB2 H 1.988 0.012 1 230 . 21 LYS CG C 25.315 0.06 1 231 . 21 LYS HG2 H 1.766 0.012 2 232 . 21 LYS HG3 H 1.603 0.012 2 233 . 21 LYS CD C 29.148 0.06 1 234 . 21 LYS HD2 H 1.852 0.012 1 235 . 21 LYS CE C 42.393 0.06 1 236 . 21 LYS HE2 H 3.215 0.012 1 237 . 22 CYS N N 124.105 0.13 1 238 . 22 CYS H H 8.870 0.012 1 239 . 22 CYS CA C 62.702 0.06 1 240 . 22 CYS HA H 3.873 0.012 1 241 . 22 CYS CB C 29.601 0.06 1 242 . 22 CYS HB2 H 2.716 0.012 2 243 . 22 CYS HB3 H 2.237 0.012 2 244 . 23 GLN N N 120.417 0.13 1 245 . 23 GLN H H 8.514 0.012 1 246 . 23 GLN CA C 57.978 0.06 1 247 . 23 GLN HA H 4.393 0.012 1 248 . 23 GLN CB C 29.190 0.06 1 249 . 23 GLN HB2 H 2.392 0.012 2 250 . 23 GLN HB3 H 2.220 0.012 2 251 . 23 GLN CG C 34.473 0.06 1 252 . 23 GLN HG2 H 2.576 0.012 1 253 . 23 GLN NE2 N 111.033 0.13 1 254 . 23 GLN HE21 H 7.657 0.012 2 255 . 23 GLN HE22 H 7.040 0.012 2 256 . 24 ARG N N 119.733 0.13 1 257 . 24 ARG H H 7.837 0.012 1 258 . 24 ARG CA C 58.223 0.06 1 259 . 24 ARG HA H 4.237 0.012 1 260 . 24 ARG CB C 30.016 0.06 1 261 . 24 ARG HB2 H 1.957 0.012 1 262 . 24 ARG CG C 27.242 0.06 1 263 . 24 ARG HG2 H 1.699 0.012 1 264 . 24 ARG CD C 43.490 0.06 1 265 . 24 ARG HD2 H 3.258 0.012 1 266 . 25 ARG N N 120.309 0.13 1 267 . 25 ARG H H 8.116 0.012 1 268 . 25 ARG CA C 57.934 0.06 1 269 . 25 ARG HA H 4.384 0.012 1 270 . 25 ARG CB C 30.622 0.06 1 271 . 25 ARG HB2 H 2.108 0.012 2 272 . 25 ARG HB3 H 2.027 0.012 2 273 . 25 ARG CG C 27.502 0.06 1 274 . 25 ARG HG2 H 1.875 0.012 2 275 . 25 ARG HG3 H 1.779 0.012 2 276 . 25 ARG CD C 43.644 0.06 1 277 . 25 ARG HD2 H 3.373 0.012 1 278 . 26 GLU N N 121.100 0.13 1 279 . 26 GLU H H 8.414 0.012 1 280 . 26 GLU CA C 58.151 0.06 1 281 . 26 GLU HA H 4.293 0.012 1 282 . 26 GLU CB C 30.223 0.06 1 283 . 26 GLU HB2 H 2.283 0.012 1 284 . 26 GLU CG C 36.657 0.06 1 285 . 26 GLU HG2 H 2.573 0.012 2 286 . 26 GLU HG3 H 2.435 0.012 2 287 . 27 GLN N N 118.982 0.13 1 288 . 27 GLN H H 8.242 0.012 1 289 . 27 GLN CA C 56.852 0.06 1 290 . 27 GLN HA H 4.413 0.012 1 291 . 27 GLN CB C 29.350 0.06 1 292 . 27 GLN HB2 H 2.274 0.012 1 293 . 27 GLN CG C 34.180 0.06 1 294 . 27 GLN HG2 H 2.647 0.012 2 295 . 27 GLN HG3 H 2.581 0.012 2 296 . 27 GLN NE2 N 111.913 0.13 1 297 . 27 GLN HE21 H 7.685 0.012 2 298 . 27 GLN HE22 H 6.996 0.012 2 299 . 28 ALA N N 123.858 0.13 1 300 . 28 ALA H H 8.055 0.012 1 301 . 28 ALA CA C 53.025 0.06 1 302 . 28 ALA HA H 4.487 0.012 1 303 . 28 ALA CB C 19.417 0.06 1 304 . 28 ALA HB H 1.585 0.012 1 305 . 29 ASN N N 122.373 0.13 1 306 . 29 ASN H H 8.077 0.012 1 307 . 29 ASN CA C 55.602 0.06 1 308 . 29 ASN HA H 4.504 0.012 1 309 . 29 ASN CB C 41.160 0.06 1 310 . 29 ASN HB2 H 3.139 0.012 2 311 . 29 ASN HB3 H 2.750 0.012 2 312 . 30 GLY N N 114.200 0.13 1 313 . 30 GLY H H 8.554 0.012 1 314 . 30 GLY CA C 45.886 0.06 1 315 . 30 GLY HA2 H 4.107 0.012 1 316 . 31 GLU N N 120.053 0.13 1 317 . 31 GLU H H 8.578 0.012 1 318 . 31 GLU CA C 56.751 0.06 1 319 . 31 GLU HA H 4.514 0.012 1 320 . 31 GLU CB C 30.491 0.06 1 321 . 31 GLU HB2 H 2.250 0.012 2 322 . 31 GLU HB3 H 2.108 0.012 2 323 . 31 GLU CG C 36.600 0.06 1 324 . 31 GLU HG2 H 2.446 0.012 2 325 . 31 GLU HG3 H 2.370 0.012 2 326 . 32 VAL N N 121.707 0.13 1 327 . 32 VAL H H 8.152 0.012 1 328 . 32 VAL CA C 62.444 0.06 1 329 . 32 VAL HA H 4.240 0.012 1 330 . 32 VAL CB C 33.072 0.06 1 331 . 32 VAL HB H 2.211 0.012 1 332 . 32 VAL CG1 C 21.511 0.06 2 333 . 32 VAL HG1 H 1.069 0.012 1 334 . 33 ARG N N 126.089 0.13 1 335 . 33 ARG H H 8.590 0.012 1 336 . 33 ARG CA C 55.580 0.06 1 337 . 33 ARG HA H 4.500 0.012 1 338 . 33 ARG CB C 31.086 0.06 1 339 . 33 ARG HB2 H 1.973 0.012 2 340 . 33 ARG HB3 H 1.899 0.012 2 341 . 33 ARG CG C 27.308 0.06 1 342 . 33 ARG HG2 H 1.804 0.012 1 343 . 33 ARG CD C 43.606 0.06 1 344 . 33 ARG HD2 H 3.364 0.012 1 345 . 34 ALA N N 126.314 0.13 1 346 . 34 ALA H H 8.552 0.012 1 347 . 34 ALA CA C 52.459 0.06 1 348 . 34 ALA HA H 4.360 0.012 1 349 . 34 ALA CB C 19.434 0.06 1 350 . 34 ALA HB H 1.486 0.012 1 351 . 35 CYS N N 124.864 0.13 1 352 . 35 CYS H H 8.723 0.012 1 353 . 35 CYS CA C 60.480 0.06 1 354 . 35 CYS HA H 4.411 0.012 1 355 . 35 CYS CB C 30.373 0.06 1 356 . 35 CYS HB2 H 2.978 0.012 1 357 . 36 SER CA C 57.932 0.06 1 358 . 36 SER HA H 4.751 0.012 1 359 . 36 SER CB C 64.122 0.06 1 360 . 36 SER HB2 H 4.210 0.012 2 361 . 36 SER HB3 H 3.997 0.012 2 362 . 37 LEU CA C 54.023 0.06 1 363 . 37 LEU HA H 4.569 0.012 1 364 . 37 LEU CB C 41.915 0.06 1 365 . 37 LEU HB2 H 1.566 0.012 1 366 . 37 LEU CG C 26.526 0.06 1 367 . 37 LEU HG H 1.625 0.012 1 368 . 37 LEU CD1 C 24.449 0.06 2 369 . 37 LEU HD1 H 0.729 0.012 1 370 . 37 LEU CD2 C 24.052 0.06 2 371 . 37 LEU HD2 H 0.453 0.012 1 372 . 38 PRO CA C 64.591 0.06 1 373 . 38 PRO HA H 4.212 0.012 1 374 . 38 PRO CB C 31.708 0.06 1 375 . 38 PRO HB2 H 2.030 0.012 2 376 . 38 PRO HB3 H 1.636 0.012 2 377 . 38 PRO CG C 27.968 0.06 1 378 . 38 PRO HG2 H 2.037 0.012 1 379 . 38 PRO CD C 51.282 0.06 1 380 . 38 PRO HD2 H 4.279 0.012 2 381 . 38 PRO HD3 H 3.742 0.012 2 382 . 39 HIS CA C 60.533 0.06 1 383 . 39 HIS HA H 4.416 0.012 1 384 . 39 HIS CD2 C 128.400 0.06 1 385 . 39 HIS HD2 H 7.415 0.012 2 386 . 40 CYS CA C 64.396 0.06 1 387 . 40 CYS HA H 4.164 0.012 1 388 . 40 CYS CB C 29.120 0.06 1 389 . 40 CYS HB2 H 3.271 0.012 2 390 . 40 CYS HB3 H 2.893 0.012 2 391 . 41 ARG CA C 59.403 0.06 1 392 . 41 ARG HA H 4.097 0.012 1 393 . 41 ARG CB C 28.880 0.06 1 394 . 41 ARG HB2 H 2.178 0.012 2 395 . 41 ARG HB3 H 2.143 0.012 2 396 . 41 ARG CG C 26.404 0.06 1 397 . 41 ARG HG2 H 1.959 0.012 2 398 . 41 ARG HG3 H 1.877 0.012 2 399 . 41 ARG CD C 42.870 0.06 1 400 . 41 ARG HD2 H 3.484 0.012 2 401 . 41 ARG HD3 H 3.433 0.012 2 402 . 42 THR N N 114.990 0.13 1 403 . 42 THR H H 7.886 0.012 1 404 . 42 THR CA C 66.564 0.06 1 405 . 42 THR HA H 4.132 0.012 1 406 . 42 THR CB C 68.971 0.06 1 407 . 42 THR HB H 4.442 0.012 1 408 . 42 THR CG2 C 22.023 0.06 1 409 . 42 THR HG2 H 1.416 0.012 1 410 . 43 MET N N 120.134 0.13 1 411 . 43 MET H H 8.241 0.012 1 412 . 43 MET CA C 57.129 0.06 1 413 . 43 MET HA H 4.689 0.012 1 414 . 43 MET CB C 32.168 0.06 1 415 . 43 MET HB2 H 2.419 0.012 2 416 . 43 MET HB3 H 2.016 0.012 2 417 . 43 MET CG C 33.924 0.06 1 418 . 43 MET HG2 H 2.737 0.012 2 419 . 43 MET HG3 H 2.703 0.012 2 420 . 43 MET CE C 18.235 0.06 1 421 . 43 MET HE H 1.832 0.012 1 422 . 44 LYS N N 122.808 0.13 1 423 . 44 LYS H H 9.366 0.012 1 424 . 44 LYS CA C 61.367 0.06 1 425 . 44 LYS HA H 4.076 0.012 1 426 . 44 LYS CB C 33.040 0.06 1 427 . 44 LYS HB2 H 2.250 0.012 2 428 . 44 LYS HB3 H 2.010 0.012 2 429 . 44 LYS CG C 27.668 0.06 1 430 . 44 LYS HG2 H 2.182 0.012 2 431 . 44 LYS HG3 H 1.396 0.012 2 432 . 44 LYS CD C 30.536 0.06 1 433 . 44 LYS HD2 H 1.808 0.012 2 434 . 44 LYS HD3 H 1.855 0.012 2 435 . 44 LYS CE C 42.660 0.06 1 436 . 44 LYS HE2 H 3.455 0.012 2 437 . 44 LYS HE3 H 2.899 0.012 2 438 . 45 ASN N N 117.603 0.13 1 439 . 45 ASN H H 8.162 0.012 1 440 . 45 ASN CA C 56.218 0.06 1 441 . 45 ASN HA H 4.745 0.012 1 442 . 45 ASN CB C 37.651 0.06 1 443 . 45 ASN HB2 H 3.378 0.012 2 444 . 45 ASN HB3 H 3.100 0.012 2 445 . 45 ASN ND2 N 112.453 0.13 1 446 . 45 ASN HD21 H 7.955 0.012 2 447 . 45 ASN HD22 H 7.143 0.012 2 448 . 46 VAL N N 123.794 0.13 1 449 . 46 VAL H H 8.355 0.012 1 450 . 46 VAL CA C 67.476 0.06 1 451 . 46 VAL HA H 3.930 0.012 1 452 . 46 VAL CB C 31.978 0.06 1 453 . 46 VAL HB H 2.575 0.012 1 454 . 46 VAL CG2 C 23.757 0.06 2 455 . 46 VAL HG2 H 1.422 0.012 1 456 . 46 VAL CG1 C 21.294 0.06 2 457 . 46 VAL HG1 H 1.148 0.012 1 458 . 47 LEU N N 121.847 0.13 1 459 . 47 LEU H H 8.859 0.012 1 460 . 47 LEU CA C 59.193 0.06 1 461 . 47 LEU HA H 4.089 0.012 1 462 . 47 LEU CB C 42.062 0.06 1 463 . 47 LEU HB2 H 1.685 0.012 2 464 . 47 LEU HB3 H 2.178 0.012 2 465 . 47 LEU CG C 27.319 0.06 1 466 . 47 LEU HG H 1.929 0.012 1 467 . 47 LEU CD1 C 25.780 0.06 2 468 . 47 LEU HD1 H 1.086 0.012 1 469 . 47 LEU CD2 C 24.155 0.06 2 470 . 47 LEU HD2 H 0.933 0.012 1 471 . 48 ASN N N 116.125 0.13 1 472 . 48 ASN H H 8.258 0.012 1 473 . 48 ASN CA C 56.175 0.06 1 474 . 48 ASN HA H 4.649 0.012 1 475 . 48 ASN CB C 38.452 0.06 1 476 . 48 ASN HB2 H 3.113 0.012 1 477 . 48 ASN ND2 N 112.768 0.13 1 478 . 48 ASN HD21 H 7.927 0.012 2 479 . 48 ASN HD22 H 7.389 0.012 2 480 . 49 HIS N N 118.880 0.13 1 481 . 49 HIS H H 8.051 0.012 1 482 . 49 HIS CA C 59.155 0.06 1 483 . 49 HIS HA H 4.574 0.012 1 484 . 49 HIS CB C 28.149 0.06 1 485 . 49 HIS HB2 H 3.576 0.012 2 486 . 49 HIS HB3 H 3.694 0.012 2 487 . 49 HIS CD2 C 128.384 0.06 1 488 . 49 HIS HD2 H 7.398 0.012 2 489 . 49 HIS CE1 C 139.241 0.06 1 490 . 49 HIS HE1 H 8.164 0.012 1 491 . 50 MET N N 119.893 0.13 1 492 . 50 MET H H 9.595 0.012 1 493 . 50 MET CA C 59.680 0.06 1 494 . 50 MET HA H 3.969 0.012 1 495 . 50 MET CB C 34.600 0.06 1 496 . 50 MET HB2 H 2.539 0.012 2 497 . 50 MET HB3 H 2.315 0.012 2 498 . 50 MET CG C 30.444 0.06 1 499 . 50 MET HG2 H 3.108 0.012 2 500 . 50 MET HG3 H 3.045 0.012 2 501 . 50 MET CE C 16.695 0.06 1 502 . 50 MET HE H 2.085 0.012 1 503 . 51 THR N N 110.037 0.13 1 504 . 51 THR H H 7.987 0.012 1 505 . 51 THR CA C 65.478 0.06 1 506 . 51 THR HA H 3.849 0.012 1 507 . 51 THR CB C 69.086 0.06 1 508 . 51 THR HB H 4.172 0.012 1 509 . 51 THR CG2 C 21.838 0.06 1 510 . 51 THR HG2 H 1.312 0.012 1 511 . 52 HIS N N 115.951 0.13 1 512 . 52 HIS H H 7.166 0.012 1 513 . 52 HIS CA C 55.299 0.06 1 514 . 52 HIS HA H 4.962 0.012 1 515 . 52 HIS CB C 30.089 0.06 1 516 . 52 HIS HB2 H 3.170 0.012 2 517 . 52 HIS HB3 H 3.618 0.012 2 518 . 52 HIS CD2 C 120.425 0.06 1 519 . 52 HIS HD2 H 7.499 0.012 2 520 . 52 HIS CE1 C 43.389 0.06 1 521 . 52 HIS HE1 H 8.510 0.012 1 522 . 53 CYS N N 123.965 0.13 1 523 . 53 CYS H H 7.186 0.012 1 524 . 53 CYS CA C 60.341 0.06 1 525 . 53 CYS HA H 4.255 0.012 1 526 . 53 CYS CB C 30.280 0.06 1 527 . 53 CYS HB2 H 2.138 0.012 2 528 . 53 CYS HB3 H 2.667 0.012 2 529 . 54 GLN N N 129.242 0.13 1 530 . 54 GLN H H 9.294 0.012 1 531 . 54 GLN CA C 55.529 0.06 1 532 . 54 GLN HA H 4.902 0.012 1 533 . 54 GLN CB C 34.177 0.06 1 534 . 54 GLN HB2 H 2.043 0.012 2 535 . 54 GLN HB3 H 2.639 0.012 2 536 . 54 GLN HG2 H 2.594 0.012 2 537 . 54 GLN HG3 H 2.541 0.012 2 538 . 54 GLN NE2 N 112.270 0.13 1 539 . 54 GLN HE21 H 7.621 0.012 2 540 . 54 GLN HE22 H 7.002 0.012 2 541 . 55 ALA N N 125.272 0.13 1 542 . 55 ALA H H 8.921 0.012 1 543 . 55 ALA CA C 53.321 0.06 1 544 . 55 ALA HA H 4.558 0.012 1 545 . 55 ALA CB C 19.925 0.06 1 546 . 55 ALA HB H 1.611 0.012 1 547 . 56 GLY N N 107.778 0.13 1 548 . 56 GLY H H 8.234 0.012 1 549 . 56 GLY CA C 46.488 0.06 1 550 . 56 GLY HA2 H 4.114 0.012 2 551 . 56 GLY HA3 H 3.688 0.012 2 552 . 57 LYS N N 125.941 0.13 1 553 . 57 LYS H H 9.272 0.012 1 554 . 57 LYS CA C 58.895 0.06 1 555 . 57 LYS HA H 4.276 0.012 1 556 . 57 LYS CB C 32.265 0.06 1 557 . 57 LYS HB2 H 2.040 0.012 2 558 . 57 LYS HB3 H 1.994 0.012 2 559 . 57 LYS CG C 25.570 0.06 1 560 . 57 LYS HG2 H 1.651 0.012 1 561 . 57 LYS CD C 29.839 0.06 1 562 . 57 LYS HD2 H 1.882 0.012 1 563 . 57 LYS CE C 42.141 0.06 1 564 . 57 LYS HE2 H 3.149 0.012 1 565 . 58 ALA N N 119.343 0.13 1 566 . 58 ALA H H 7.799 0.012 1 567 . 58 ALA CA C 51.776 0.06 1 568 . 58 ALA HA H 4.561 0.012 1 569 . 58 ALA CB C 19.160 0.06 1 570 . 58 ALA HB H 1.654 0.012 1 571 . 59 CYS N N 122.098 0.13 1 572 . 59 CYS H H 7.581 0.012 1 573 . 59 CYS CA C 62.633 0.06 1 574 . 59 CYS HA H 4.003 0.012 1 575 . 59 CYS CB C 29.924 0.06 1 576 . 59 CYS HB2 H 2.996 0.012 1 577 . 60 GLN N N 129.797 0.13 1 578 . 60 GLN H H 9.271 0.012 1 579 . 60 GLN CA C 55.828 0.06 1 580 . 60 GLN HA H 4.633 0.012 1 581 . 60 GLN CB C 29.578 0.06 1 582 . 60 GLN HB2 H 2.080 0.012 2 583 . 60 GLN HB3 H 2.583 0.012 2 584 . 60 GLN CG C 34.228 0.06 1 585 . 60 GLN HG2 H 2.656 0.012 2 586 . 60 GLN HG3 H 2.571 0.012 2 587 . 60 GLN NE2 N 113.432 0.13 1 588 . 60 GLN HE21 H 7.609 0.012 2 589 . 60 GLN HE22 H 7.015 0.012 2 590 . 61 VAL N N 127.947 0.13 1 591 . 61 VAL H H 9.466 0.012 1 592 . 61 VAL CA C 64.576 0.06 1 593 . 61 VAL HA H 3.774 0.012 1 594 . 61 VAL CB C 30.813 0.06 1 595 . 61 VAL HB H 2.064 0.012 1 596 . 61 VAL CG2 C 22.941 0.06 2 597 . 61 VAL HG2 H 0.742 0.012 1 598 . 61 VAL CG1 C 20.425 0.06 2 599 . 61 VAL HG1 H 0.606 0.012 1 600 . 62 ALA N N 134.534 0.13 1 601 . 62 ALA H H 8.829 0.012 1 602 . 62 ALA CA C 54.505 0.06 1 603 . 62 ALA HA H 3.862 0.012 1 604 . 62 ALA CB C 17.870 0.06 1 605 . 62 ALA HB H 1.056 0.012 1 606 . 63 HIS N N 110.451 0.13 1 607 . 63 HIS H H 8.161 0.012 1 608 . 63 HIS CA C 57.408 0.06 1 609 . 63 HIS HA H 4.604 0.012 1 610 . 63 HIS CB C 29.564 0.06 1 611 . 63 HIS HB2 H 3.844 0.012 2 612 . 63 HIS HB3 H 3.015 0.012 2 613 . 63 HIS CD2 C 117.522 0.06 1 614 . 63 HIS HD2 H 6.669 0.012 2 615 . 64 CYS N N 126.924 0.13 1 616 . 64 CYS H H 8.233 0.012 1 617 . 64 CYS CA C 64.209 0.06 1 618 . 64 CYS HA H 4.367 0.012 1 619 . 64 CYS CB C 30.170 0.06 1 620 . 64 CYS HB2 H 2.718 0.012 2 621 . 64 CYS HB3 H 3.502 0.012 2 622 . 65 ALA N N 119.360 0.13 1 623 . 65 ALA H H 9.002 0.012 1 624 . 65 ALA CA C 55.583 0.06 1 625 . 65 ALA HA H 4.510 0.012 1 626 . 65 ALA CB C 18.198 0.06 1 627 . 65 ALA HB H 1.694 0.012 1 628 . 66 SER N N 114.757 0.13 1 629 . 66 SER H H 9.253 0.012 1 630 . 66 SER CA C 60.462 0.06 1 631 . 66 SER HA H 4.264 0.012 1 632 . 66 SER CB C 62.191 0.06 1 633 . 66 SER HB2 H 4.027 0.012 2 634 . 66 SER HB3 H 3.961 0.012 2 635 . 67 SER N N 120.391 0.13 1 636 . 67 SER H H 7.945 0.012 1 637 . 67 SER CA C 64.331 0.06 1 638 . 67 SER HA H 4.164 0.012 1 639 . 67 SER CB C 62.701 0.06 1 640 . 67 SER HB2 H 3.722 0.012 2 641 . 67 SER HB3 H 4.820 0.012 2 642 . 68 ARG N N 124.093 0.13 1 643 . 68 ARG H H 9.197 0.012 1 644 . 68 ARG CA C 60.830 0.06 1 645 . 68 ARG HA H 3.871 0.012 1 646 . 68 ARG CB C 30.857 0.06 1 647 . 68 ARG HB2 H 2.324 0.012 2 648 . 68 ARG HB3 H 2.072 0.012 2 649 . 68 ARG CG C 28.240 0.06 1 650 . 68 ARG HG2 H 1.888 0.012 2 651 . 68 ARG HG3 H 1.629 0.012 2 652 . 68 ARG CD C 42.140 0.06 1 653 . 68 ARG HD2 H 3.150 0.012 1 654 . 69 GLN N N 122.178 0.13 1 655 . 69 GLN H H 8.403 0.012 1 656 . 69 GLN CA C 59.639 0.06 1 657 . 69 GLN HA H 4.038 0.012 1 658 . 69 GLN CB C 27.295 0.06 1 659 . 69 GLN HB2 H 2.600 0.012 2 660 . 69 GLN HB3 H 2.360 0.012 2 661 . 69 GLN CG C 34.156 0.06 1 662 . 69 GLN HG2 H 2.424 0.012 2 663 . 69 GLN HG3 H 2.367 0.012 2 664 . 69 GLN NE2 N 109.366 0.13 1 665 . 69 GLN HE21 H 7.075 0.012 2 666 . 69 GLN HE22 H 6.975 0.012 2 667 . 70 ILE N N 121.128 0.13 1 668 . 70 ILE H H 8.871 0.012 1 669 . 70 ILE CA C 67.040 0.06 1 670 . 70 ILE HA H 3.712 0.012 1 671 . 70 ILE CB C 38.957 0.06 1 672 . 70 ILE HB H 1.968 0.012 1 673 . 70 ILE CG1 C 29.347 0.06 2 674 . 70 ILE HG12 H 2.216 0.012 1 675 . 70 ILE HG13 H 0.976 0.012 1 676 . 70 ILE CD1 C 14.566 0.06 1 677 . 70 ILE HD1 H 0.968 0.012 1 678 . 70 ILE CG2 C 18.692 0.06 2 679 . 70 ILE HG2 H 1.004 0.012 1 680 . 71 ILE N N 119.998 0.13 1 681 . 71 ILE H H 9.150 0.012 1 682 . 71 ILE CA C 65.578 0.06 1 683 . 71 ILE HA H 3.847 0.012 1 684 . 71 ILE CB C 38.076 0.06 1 685 . 71 ILE HB H 1.855 0.012 1 686 . 71 ILE CG1 C 29.600 0.06 2 687 . 71 ILE HG12 H 2.120 0.012 1 688 . 71 ILE HG13 H 0.967 0.012 1 689 . 71 ILE CD1 C 14.918 0.06 1 690 . 71 ILE HD1 H 0.961 0.012 1 691 . 71 ILE CG2 C 19.144 0.06 2 692 . 71 ILE HG2 H 1.169 0.012 1 693 . 72 SER N N 114.980 0.13 1 694 . 72 SER H H 7.986 0.012 1 695 . 72 SER CA C 63.650 0.06 1 696 . 72 SER HA H 4.377 0.012 1 697 . 72 SER CB C 62.678 0.06 1 698 . 72 SER HB2 H 4.229 0.012 2 699 . 73 HIS N N 122.022 0.13 1 700 . 73 HIS H H 8.756 0.012 1 701 . 73 HIS CA C 60.918 0.06 1 702 . 73 HIS HA H 4.159 0.012 1 703 . 73 HIS CB C 27.395 0.06 1 704 . 73 HIS HB2 H 3.759 0.012 2 705 . 73 HIS HB3 H 3.394 0.012 2 706 . 73 HIS CD2 C 128.105 0.06 1 707 . 73 HIS HD2 H 6.825 0.012 2 708 . 74 TRP N N 121.785 0.13 1 709 . 74 TRP H H 8.693 0.012 1 710 . 74 TRP CA C 60.137 0.06 1 711 . 74 TRP HA H 4.633 0.012 1 712 . 74 TRP CB C 29.943 0.06 1 713 . 74 TRP HB2 H 3.782 0.012 2 714 . 74 TRP HB3 H 3.561 0.012 2 715 . 74 TRP CD1 C 124.153 0.06 2 716 . 74 TRP HD1 H 7.223 0.012 1 717 . 74 TRP NE1 N 128.626 0.13 1 718 . 74 TRP HE1 H 10.077 0.012 2 719 . 74 TRP CZ2 C 114.354 0.06 2 720 . 74 TRP HZ2 H 7.635 0.012 2 721 . 75 LYS N N 116.975 0.13 1 722 . 75 LYS H H 8.544 0.012 1 723 . 75 LYS CA C 57.973 0.06 1 724 . 75 LYS HA H 3.945 0.012 1 725 . 75 LYS CB C 33.215 0.06 1 726 . 75 LYS HB2 H 2.019 0.012 1 727 . 75 LYS CG C 24.573 0.06 1 728 . 75 LYS HG2 H 1.677 0.012 2 729 . 75 LYS HG3 H 1.531 0.012 2 730 . 75 LYS CD C 28.962 0.06 1 731 . 75 LYS HD2 H 1.888 0.012 2 732 . 75 LYS HD3 H 1.672 0.012 2 733 . 75 LYS CE C 42.590 0.06 1 734 . 75 LYS HE2 H 3.098 0.012 2 735 . 76 ASN N N 113.120 0.13 1 736 . 76 ASN H H 7.084 0.012 1 737 . 76 ASN CA C 53.868 0.06 1 738 . 76 ASN HA H 4.740 0.012 1 739 . 76 ASN CB C 41.835 0.06 1 740 . 76 ASN HB2 H 2.730 0.012 2 741 . 76 ASN HB3 H 2.976 0.012 2 742 . 76 ASN ND2 N 114.713 0.13 1 743 . 76 ASN HD21 H 7.722 0.012 2 744 . 76 ASN HD22 H 7.530 0.012 2 745 . 77 CYS N N 123.165 0.13 1 746 . 77 CYS H H 7.513 0.012 1 747 . 77 CYS CA C 61.266 0.06 1 748 . 77 CYS HA H 4.164 0.012 1 749 . 77 CYS CB C 28.711 0.06 1 750 . 77 CYS HB2 H 2.094 0.012 2 751 . 77 CYS HB3 H 2.985 0.012 2 752 . 78 THR N N 119.217 0.13 1 753 . 78 THR H H 8.641 0.012 1 754 . 78 THR CA C 60.752 0.06 1 755 . 78 THR HA H 4.704 0.012 1 756 . 78 THR CB C 69.507 0.06 1 757 . 78 THR HB H 4.718 0.012 1 758 . 78 THR CG2 C 21.378 0.06 1 759 . 78 THR HG2 H 1.257 0.012 1 760 . 79 ARG CA C 56.182 0.06 1 761 . 79 ARG HA H 4.583 0.012 1 762 . 79 ARG CB C 31.493 0.06 1 763 . 79 ARG HB2 H 2.127 0.012 2 764 . 79 ARG HB3 H 2.036 0.012 2 765 . 79 ARG CG C 27.137 0.06 1 766 . 79 ARG HG2 H 2.036 0.012 2 767 . 79 ARG HG3 H 1.824 0.012 2 768 . 79 ARG CD C 44.144 0.06 1 769 . 79 ARG HD2 H 3.506 0.012 2 770 . 79 ARG HD3 H 3.287 0.012 2 771 . 80 HIS CA C 58.494 0.06 1 772 . 80 HIS HA H 4.550 0.012 1 773 . 80 HIS CB C 29.517 0.06 1 774 . 80 HIS HB2 H 3.371 0.012 1 775 . 80 HIS CD2 C 119.293 0.06 1 776 . 80 HIS HD2 H 7.321 0.012 2 777 . 81 ASP N N 117.052 0.13 1 778 . 81 ASP H H 8.244 0.012 1 779 . 81 ASP CA C 52.041 0.06 1 780 . 81 ASP HA H 4.668 0.012 1 781 . 81 ASP CB C 39.721 0.06 1 782 . 81 ASP HB2 H 2.991 0.012 2 783 . 81 ASP HB3 H 2.413 0.012 2 784 . 82 CYS N N 122.739 0.13 1 785 . 82 CYS H H 7.213 0.012 1 786 . 82 CYS CA C 57.752 0.06 1 787 . 82 CYS HA H 4.454 0.012 1 788 . 82 CYS CB C 31.141 0.06 1 789 . 82 CYS HB2 H 3.144 0.012 1 790 . 83 PRO CA C 64.361 0.06 1 791 . 83 PRO HA H 4.622 0.012 1 792 . 83 PRO CB C 32.601 0.06 1 793 . 83 PRO HB2 H 2.530 0.012 2 794 . 83 PRO HB3 H 2.024 0.012 2 795 . 83 PRO CG C 27.510 0.06 1 796 . 83 PRO HG2 H 2.285 0.012 2 797 . 83 PRO HG3 H 2.144 0.012 2 798 . 83 PRO CD C 51.237 0.06 1 799 . 83 PRO HD2 H 4.225 0.012 2 800 . 83 PRO HD3 H 4.189 0.012 2 801 . 84 VAL N N 120.678 0.13 1 802 . 84 VAL H H 8.712 0.012 1 803 . 84 VAL CA C 66.448 0.06 1 804 . 84 VAL HA H 3.909 0.012 1 805 . 84 VAL CB C 33.215 0.06 1 806 . 84 VAL HB H 2.398 0.012 1 807 . 84 VAL CG1 C 21.931 0.06 2 808 . 84 VAL HG1 H 1.029 0.012 1 809 . 85 CYS N N 118.514 0.13 1 810 . 85 CYS H H 8.581 0.012 1 811 . 85 CYS CA C 63.425 0.06 1 812 . 85 CYS HA H 4.408 0.012 1 813 . 85 CYS CB C 31.467 0.06 1 814 . 85 CYS HB2 H 3.121 0.012 2 815 . 85 CYS HB3 H 3.349 0.012 2 816 . 86 LEU N N 119.400 0.13 1 817 . 86 LEU H H 8.042 0.012 1 818 . 86 LEU CA C 60.167 0.06 1 819 . 86 LEU HA H 4.386 0.012 1 820 . 86 LEU CB C 39.678 0.06 1 821 . 86 LEU HB2 H 2.007 0.012 2 822 . 86 LEU HB3 H 1.906 0.012 2 823 . 86 LEU CG C 27.647 0.06 1 824 . 86 LEU HG H 1.775 0.012 1 825 . 86 LEU CD1 C 25.234 0.06 2 826 . 86 LEU HD1 H 1.043 0.012 1 827 . 86 LEU CD2 C 24.293 0.06 2 828 . 86 LEU HD2 H 1.067 0.012 1 829 . 87 PRO CA C 65.333 0.06 1 830 . 87 PRO HA H 4.615 0.012 1 831 . 87 PRO CB C 31.442 0.06 1 832 . 87 PRO HB2 H 2.536 0.012 2 833 . 87 PRO HB3 H 1.832 0.012 2 834 . 87 PRO CG C 28.477 0.06 1 835 . 87 PRO HG2 H 2.120 0.012 2 836 . 87 PRO HG3 H 2.064 0.012 2 837 . 87 PRO CD C 50.229 0.06 1 838 . 87 PRO HD2 H 3.812 0.012 2 839 . 87 PRO HD3 H 3.622 0.012 2 840 . 88 LEU N N 116.633 0.13 1 841 . 88 LEU H H 7.772 0.012 1 842 . 88 LEU CA C 55.999 0.06 1 843 . 88 LEU HA H 4.508 0.012 1 844 . 88 LEU CB C 42.420 0.06 1 845 . 88 LEU HB2 H 2.266 0.012 2 846 . 88 LEU HB3 H 1.941 0.012 2 847 . 88 LEU CG C 28.378 0.06 1 848 . 88 LEU HG H 1.833 0.012 1 849 . 88 LEU CD1 C 25.737 0.06 2 850 . 88 LEU HD1 H 0.998 0.012 1 851 . 88 LEU CD2 C 24.080 0.06 2 852 . 88 LEU HD2 H 0.893 0.012 1 853 . 89 LYS N N 120.150 0.13 1 854 . 89 LYS H H 8.098 0.012 1 855 . 89 LYS CA C 57.411 0.06 1 856 . 89 LYS HA H 4.565 0.012 1 857 . 89 LYS CB C 33.335 0.06 1 858 . 89 LYS HB2 H 2.057 0.012 1 859 . 89 LYS CG C 25.707 0.06 1 860 . 89 LYS HG2 H 1.784 0.012 2 861 . 89 LYS HG3 H 1.622 0.012 2 862 . 89 LYS CD C 29.314 0.06 1 863 . 89 LYS HD2 H 1.749 0.012 1 864 . 89 LYS CE C 42.584 0.06 1 865 . 89 LYS HE2 H 2.943 0.012 2 866 . 89 LYS HE3 H 2.803 0.012 2 867 . 90 ASN N N 118.669 0.13 1 868 . 90 ASN H H 8.539 0.012 1 869 . 90 ASN CA C 53.638 0.06 1 870 . 90 ASN HA H 4.890 0.012 1 871 . 90 ASN CB C 39.093 0.06 1 872 . 90 ASN HB2 H 3.046 0.012 2 873 . 90 ASN HB3 H 2.945 0.012 2 874 . 90 ASN ND2 N 112.658 0.13 1 875 . 90 ASN HD21 H 7.787 0.012 2 876 . 90 ASN HD22 H 7.083 0.012 2 877 . 91 ALA N N 124.263 0.13 1 878 . 91 ALA H H 8.306 0.012 1 879 . 91 ALA CA C 53.193 0.06 1 880 . 91 ALA HA H 4.532 0.012 1 881 . 91 ALA CB C 19.400 0.06 1 882 . 91 ALA HB H 1.626 0.012 1 883 . 92 SER N N 114.581 0.13 1 884 . 92 SER H H 8.409 0.012 1 885 . 92 SER CA C 58.942 0.06 1 886 . 92 SER HA H 4.606 0.012 1 887 . 92 SER CB C 64.062 0.06 1 888 . 92 SER HB2 H 4.118 0.012 2 889 . 92 SER HB3 H 4.064 0.012 2 890 . 93 ASP N N 122.193 0.13 1 891 . 93 ASP H H 8.451 0.012 1 892 . 93 ASP CA C 54.530 0.06 1 893 . 93 ASP HA H 4.791 0.012 1 894 . 93 ASP CB C 41.229 0.06 1 895 . 93 ASP HB2 H 2.883 0.012 1 896 . 94 LYS N N 121.811 0.13 1 897 . 94 LYS H H 8.265 0.012 1 898 . 94 LYS CA C 56.385 0.06 1 899 . 94 LYS HA H 4.510 0.012 1 900 . 94 LYS CB C 32.949 0.06 1 901 . 94 LYS HB2 H 1.922 0.012 2 902 . 94 LYS HB3 H 2.050 0.012 2 903 . 94 LYS CG C 24.781 0.06 1 904 . 94 LYS HG2 H 1.625 0.012 2 905 . 94 LYS HG3 H 1.586 0.012 2 906 . 94 LYS CD C 29.136 0.06 1 907 . 94 LYS HD2 H 1.843 0.012 1 908 . 94 LYS CE C 42.392 0.06 1 909 . 94 LYS HE2 H 3.178 0.012 1 910 . 95 ARG N N 128.032 0.13 1 911 . 95 ARG H H 8.129 0.012 1 912 . 95 ARG CA C 57.635 0.06 1 913 . 95 ARG HA H 4.339 0.012 1 914 . 95 ARG CB C 31.710 0.06 1 915 . 95 ARG HB2 H 1.895 0.012 2 916 . 95 ARG HB3 H 2.023 0.012 2 917 . 95 ARG CG C 27.376 0.06 1 918 . 95 ARG HG2 H 1.769 0.012 1 919 . 95 ARG CD C 43.629 0.06 1 920 . 95 ARG HD2 H 3.388 0.012 1 stop_ save_