data_6095 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the KIX domain of CBP bound to the transactivation domain of c-Myb ; _BMRB_accession_number 6095 _BMRB_flat_file_name bmr6095.str _Entry_type original _Submission_date 2004-02-09 _Accession_date 2004-02-10 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zor Tsaffy . . 2 'De Guzman' Roberto N. . 3 Dyson 'H. Jane' . . 4 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" 634 "13C chemical shifts" 392 "15N chemical shifts" 118 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-05-15 original author . stop_ _Original_release_date 2004-05-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of the KIX domain of CBP bound to the transactivation domain of c-Myb ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15019774 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zor Tsaffy . . 2 'De Guzman' Roberto N. . 3 Dyson 'H. Jane' . . 4 Wright Peter E. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 337 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 521 _Page_last 534 _Year 2004 _Details . loop_ _Keyword 'CREB-binding protein' 'transcriptional coactivation' 'constitutive activation' 'LXXLL motif' stop_ save_ ################################## # Molecular system description # ################################## save_system_KIX _Saveframe_category molecular_system _Mol_system_name 'CBP KIX domain and c-Myb' _Abbreviation_common KIX _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CBP KIX domain' $KIX C-MYB $c-Myb stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_KIX _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'CBP KIX domain' _Abbreviation_common KIX _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 87 _Mol_residue_sequence ; GVRKGWHEHVTQDLRSHLVH KLVQAIFPTPDPAALKDRRM ENLVAYAKKVEGDMYESANS RDEYYHLLAEKIYKIQKELE EKRRSRL ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 VAL 3 ARG 4 LYS 5 GLY 6 TRP 7 HIS 8 GLU 9 HIS 10 VAL 11 THR 12 GLN 13 ASP 14 LEU 15 ARG 16 SER 17 HIS 18 LEU 19 VAL 20 HIS 21 LYS 22 LEU 23 VAL 24 GLN 25 ALA 26 ILE 27 PHE 28 PRO 29 THR 30 PRO 31 ASP 32 PRO 33 ALA 34 ALA 35 LEU 36 LYS 37 ASP 38 ARG 39 ARG 40 MET 41 GLU 42 ASN 43 LEU 44 VAL 45 ALA 46 TYR 47 ALA 48 LYS 49 LYS 50 VAL 51 GLU 52 GLY 53 ASP 54 MET 55 TYR 56 GLU 57 SER 58 ALA 59 ASN 60 SER 61 ARG 62 ASP 63 GLU 64 TYR 65 TYR 66 HIS 67 LEU 68 LEU 69 ALA 70 GLU 71 LYS 72 ILE 73 TYR 74 LYS 75 ILE 76 GLN 77 LYS 78 GLU 79 LEU 80 GLU 81 GLU 82 LYS 83 ARG 84 ARG 85 SER 86 ARG 87 LEU 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 1SB0 "Solution Structure Of The Kix Domain Of Cbp Bound To The Transactivation Domain Of C-Myb" 100.00 25 100.00 100.00 8.71e-06 PDB 2AGH "Structural Basis For Cooperative Transcription Factor Binding To The Cbp Coactivator" 100.00 25 100.00 100.00 8.71e-06 DBJ BAA05135 "cellular oncogene [Bos taurus]" 100.00 640 100.00 100.00 1.15e-04 DBJ BAA05136 "protooncogene c-myb [Bos taurus]" 100.00 555 100.00 100.00 2.55e-05 DBJ BAA05137 "protooncogene c-myb [Bos taurus]" 100.00 430 100.00 100.00 1.11e-05 DBJ BAC40133 "unnamed protein product [Mus musculus]" 100.00 755 100.00 100.00 6.15e-05 DBJ BAC40443 "unnamed protein product [Mus musculus]" 100.00 439 100.00 100.00 5.99e-05 EMBL CAA24979 "p153 protein [Avian leukemia virus]" 100.00 669 100.00 100.00 2.42e-06 EMBL CAA26551 "unnamed protein product [Mus musculus]" 100.00 648 100.00 100.00 4.56e-05 EMBL CAA26552 "unnamed protein product [Mus musculus]" 100.00 636 100.00 100.00 5.76e-05 EMBL CAA27197 "unnamed protein product [Gallus gallus]" 100.00 699 100.00 100.00 4.70e-05 EMBL CAA27724 "myb proto-oncogene [Mus musculus]" 100.00 330 100.00 100.00 4.88e-05 GB AAA39781 "myb protein [Mus musculus]" 100.00 715 100.00 100.00 3.17e-05 GB AAA39785 "tumor-specific myb protein [Mus musculus]" 100.00 593 100.00 100.00 3.26e-05 GB AAA42551 "transforming protein [Avian myeloblastosis virus]" 100.00 265 100.00 100.00 8.89e-07 GB AAA42553 "c-myb ORF startng at the first atg in the ORF [Avian myeloblastosis virus]" 100.00 265 100.00 100.00 8.89e-07 GB AAA48696 "c-myb oncogene product, partial [Gallus gallus]" 100.00 379 100.00 100.00 1.58e-05 PRF 0912261A "protein p135" 100.00 669 100.00 100.00 2.42e-06 PRF 1203379A "gene c-myb [Gallus gallus]" 100.00 699 100.00 100.00 4.70e-05 REF NP_001123644 "transcriptional activator Myb isoform 3 [Homo sapiens]" 92.00 637 100.00 100.00 1.19e-03 REF NP_001155128 "transcriptional activator Myb isoform 4 [Homo sapiens]" 92.00 758 100.00 100.00 7.18e-04 REF NP_001185843 "transcriptional activator Myb isoform 1 [Mus musculus]" 100.00 755 100.00 100.00 6.20e-05 REF NP_034978 "transcriptional activator Myb isoform 2 [Mus musculus]" 100.00 636 100.00 100.00 7.39e-05 REF NP_778220 "transcriptional activator Myb [Bos taurus]" 100.00 555 100.00 100.00 2.55e-05 SP P01103 "RecName: Full=Transcriptional activator Myb; AltName: Full=Proto-oncogene c-Myb [Gallus gallus]" 100.00 641 100.00 100.00 8.73e-05 SP P01104 "RecName: Full=Transforming protein Myb [Avian myeloblastosis virus]" 100.00 382 100.00 100.00 6.81e-06 SP P01105 "RecName: Full=p135Gag-Myb-Ets-transforming protein; Contains: RecName: Full=Transforming protein v-Myb; Contains: RecName: Full" 100.00 669 100.00 100.00 2.42e-06 SP P06876 "RecName: Full=Transcriptional activator Myb; AltName: Full=Proto-oncogene c-Myb [Mus musculus]" 100.00 636 100.00 100.00 7.39e-05 SP P46200 "RecName: Full=Transcriptional activator Myb; AltName: Full=Proto-oncogene c-Myb [Bos taurus]" 100.00 640 100.00 100.00 1.15e-04 TPG DAA26093 "TPA: myb proto-oncogene protein [Bos taurus]" 100.00 555 100.00 100.00 2.52e-05 stop_ save_ save_c-Myb _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common C-MYB _Abbreviation_common c-Myb _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 25 _Mol_residue_sequence ; KEKRIKELELLLMSTENELK GQQAL ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 GLU 3 LYS 4 ARG 5 ILE 6 LYS 7 GLU 8 LEU 9 GLU 10 LEU 11 LEU 12 LEU 13 MET 14 SER 15 THR 16 GLU 17 ASN 18 GLU 19 LEU 20 LYS 21 GLY 22 GLN 23 GLN 24 ALA 25 LEU 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 SWISS-PROT P06876 'Myb proto-oncogene protein (C-myb)' 100.00 636 100.00 100.00 3.08e-04 SWISS-PROT P46200 'Myb proto-oncogene protein (C-myb)' 100.00 640 100.00 100.00 4.64e-04 SWISS-PROT P01104 'Transforming protein Myb' 100.00 382 100.00 100.00 5.48e-05 SWISS-PROT P01105 'p135Gag-Myb-Ets-transforming protein [Contains: Transforming protein v-Myb; Transforming protein v-Ets]' 100.00 669 100.00 100.00 1.59e-05 REF XP_001061499 'PREDICTED: similar to Myb proto-oncogene protein (C-myb) [Rattus norvegicus]' 100.00 634 100.00 100.00 2.48e-04 SWISS-PROT P01103 'Myb proto-oncogene protein (C-myb)' 100.00 641 100.00 100.00 3.64e-04 REF NP_778220 'v-myb myeloblastosis viral oncogene homolog [Bos taurus]' 100.00 555 100.00 100.00 1.33e-04 REF NP_990637 'v-myb myeloblastosis viral oncogene homolog [Gallus gallus]' 100.00 699 100.00 100.00 2.07e-04 REF NP_001123644 'v-myb myeloblastosis viral oncogene homolog isoform 3 [Homo sapiens]' 92.00 637 100.00 100.00 3.55e-03 REF NP_034978 'myeloblastosis proto-oncogene product [Mus musculus]' 100.00 636 100.00 100.00 3.16e-04 PRF 0912261A 'protein p135' 100.00 669 100.00 100.00 1.59e-05 PRF 1203379A 'gene c-myb' 100.00 699 100.00 100.00 2.07e-04 GenBank AAA42553 'c-myb ORF startng at the first atg in the ORF' 100.00 265 100.00 100.00 1.59e-05 GenBank AAA48696 'c-myb oncogene product' 100.00 379 100.00 100.00 1.13e-04 GenBank AAA39785 'tumor-specific myb protein' 100.00 593 100.00 100.00 1.59e-04 GenBank AAA42551 'transforming protein' 100.00 265 100.00 100.00 1.59e-05 EMBL CAA27724 'myb proto-oncogene [Mus musculus]' 100.00 330 100.00 100.00 3.35e-04 GenBank AAA39781 'myb protein' 100.00 715 100.00 100.00 1.46e-04 EMBL CAA26552 'unnamed protein product [Mus musculus]' 100.00 636 100.00 100.00 2.54e-04 EMBL CAA27197 'unnamed protein product [Gallus gallus]' 100.00 699 100.00 100.00 2.07e-04 EMBL CAA24979 'p153 protein [Avian leukemia virus]' 100.00 669 100.00 100.00 1.59e-05 EMBL CAA26551 'unnamed protein product [Mus musculus]' 100.00 648 100.00 100.00 2.07e-04 DBJ BAC40133 'unnamed protein product [Mus musculus]' 100.00 755 100.00 100.00 2.54e-04 DBJ BAC40443 'unnamed protein product [Mus musculus]' 100.00 439 100.00 100.00 3.16e-04 DBJ BAA05136 'protooncogene c-myb [Bos taurus]' 100.00 555 100.00 100.00 1.33e-04 DBJ BAA05137 'protooncogene c-myb [Bos taurus]' 100.00 430 100.00 100.00 7.53e-05 PDB 2AGH 'Structural Basis For Cooperative Transcription Factor Binding To The Cbp Coactivator' 100.00 25 100.00 100.00 6.76e-04 DBJ BAA05135 'cellular oncogene [Bos taurus]' 100.00 640 100.00 100.00 4.64e-04 BMRB 6750 MYB 100.00 25 100.00 100.00 6.76e-04 PDB 1SB0 'Solution Structure Of The Kix Domain Of Cbp Bound To The Transactivation Domain Of C-Myb' 100.00 25 100.00 100.00 6.76e-04 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $KIX 'house mouse' 10090 Eukaryota Metazoa Mus musculus $c-Myb 'house mouse' 10090 Eukaryota Metazoa Mus musculus 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 $KIX 'recombinant technology' . . . . . $c-Myb '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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $KIX . mM 0.5 1 '[U-N15; U-C13]' $c-Myb . mM 0.5 1 '[U-N15; U-C13]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model AMX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DMX _Field_strength 750 _Details . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 0.1 n/a temperature 300 0.2 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.00 external direct . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.00 external direct . . . 0.251449530 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'CBP KIX domain' _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 GLY CA C 41.340 0.1 1 2 . 1 GLY HA3 H 3.883 0.02 2 3 . 2 VAL N N 119.186 0.1 1 4 . 2 VAL H H 8.506 0.02 1 5 . 2 VAL CA C 60.207 0.1 1 6 . 2 VAL HA H 4.172 0.02 1 7 . 2 VAL CB C 30.969 0.1 1 8 . 2 VAL HB H 2.041 0.02 1 9 . 2 VAL CG1 C 18.487 0.1 2 10 . 2 VAL HG1 H 0.928 0.02 4 11 . 3 ARG N N 125.412 0.1 1 12 . 3 ARG H H 8.541 0.02 1 13 . 3 ARG CA C 54.300 0.1 1 14 . 3 ARG HA H 4.345 0.02 1 15 . 3 ARG CB C 28.650 0.1 1 16 . 3 ARG HB3 H 1.820 0.02 2 17 . 3 ARG CG C 25.350 0.1 1 18 . 3 ARG HG2 H 1.675 0.02 2 19 . 3 ARG HG3 H 1.560 0.02 2 20 . 3 ARG CD C 41.400 0.1 1 21 . 3 ARG HD3 H 3.190 0.02 2 22 . 4 LYS N N 122.196 0.1 1 23 . 4 LYS H H 8.111 0.02 1 24 . 4 LYS CA C 53.057 0.1 1 25 . 4 LYS HA H 4.230 0.02 1 26 . 4 LYS CB C 31.141 0.1 1 27 . 4 LYS HB2 H 1.217 0.02 2 28 . 4 LYS HB3 H 0.637 0.02 2 29 . 4 LYS CG C 23.117 0.1 1 30 . 4 LYS HG2 H 1.287 0.02 2 31 . 4 LYS HG3 H 1.190 0.02 2 32 . 4 LYS CD C 27.501 0.1 1 33 . 4 LYS HD2 H 1.680 0.02 2 34 . 4 LYS HD3 H 1.468 0.02 2 35 . 4 LYS CE C 40.500 0.1 1 36 . 4 LYS HE2 H 2.990 0.02 2 37 . 4 LYS HE3 H 2.950 0.02 2 38 . 5 GLY N N 112.318 0.1 1 39 . 5 GLY H H 8.727 0.02 1 40 . 5 GLY CA C 45.379 0.1 1 41 . 5 GLY HA2 H 3.976 0.02 2 42 . 5 GLY HA3 H 3.766 0.02 2 43 . 6 TRP N N 119.021 0.1 1 44 . 6 TRP H H 8.037 0.02 1 45 . 6 TRP CA C 56.350 0.1 1 46 . 6 TRP HA H 4.530 0.02 1 47 . 6 TRP CB C 25.600 0.1 1 48 . 6 TRP HB2 H 3.600 0.02 2 49 . 6 TRP HB3 H 3.190 0.02 2 50 . 6 TRP CD1 C 123.701 0.1 3 51 . 6 TRP HD1 H 7.024 0.02 1 52 . 6 TRP NE1 N 128.886 0.1 1 53 . 6 TRP HE1 H 9.145 0.02 3 54 . 6 TRP CZ2 C 113.565 0.1 3 55 . 6 TRP HZ2 H 7.592 0.02 3 56 . 6 TRP CH2 C 123.892 0.1 1 57 . 6 TRP HH2 H 6.347 0.02 1 58 . 6 TRP CZ3 C 118.927 0.1 1 59 . 6 TRP HZ3 H 6.315 0.02 3 60 . 6 TRP CE3 C 117.796 0.1 3 61 . 6 TRP HE3 H 7.195 0.02 3 62 . 7 HIS N N 119.368 0.1 1 63 . 7 HIS H H 7.027 0.02 1 64 . 7 HIS CA C 54.331 0.1 1 65 . 7 HIS HA H 3.474 0.02 1 66 . 7 HIS CB C 26.900 0.1 1 67 . 7 HIS HB3 H 2.910 0.02 2 68 . 7 HIS CD2 C 117.900 0.1 1 69 . 7 HIS HD2 H 7.154 0.02 1 70 . 8 GLU N N 116.558 0.1 1 71 . 8 GLU H H 7.648 0.02 1 72 . 8 GLU CA C 56.350 0.1 1 73 . 8 GLU HA H 3.930 0.02 1 74 . 8 GLU CB C 27.450 0.1 1 75 . 8 GLU HB2 H 1.830 0.02 2 76 . 8 GLU HB3 H 1.750 0.02 2 77 . 8 GLU CG C 34.052 0.1 1 78 . 8 GLU HG3 H 2.094 0.02 2 79 . 9 HIS N N 112.676 0.1 1 80 . 9 HIS H H 7.443 0.02 1 81 . 9 HIS CA C 52.850 0.1 1 82 . 9 HIS HA H 4.900 0.02 1 83 . 9 HIS CB C 27.731 0.1 1 84 . 9 HIS HB2 H 3.694 0.02 2 85 . 9 HIS HB3 H 3.280 0.02 2 86 . 9 HIS CD2 C 117.900 0.1 1 87 . 9 HIS HD2 H 7.288 0.02 1 88 . 10 VAL N N 121.355 0.1 1 89 . 10 VAL H H 7.486 0.02 1 90 . 10 VAL CA C 60.165 0.1 1 91 . 10 VAL HA H 4.445 0.02 1 92 . 10 VAL CB C 30.969 0.1 1 93 . 10 VAL HB H 2.160 0.02 1 94 . 10 VAL CG1 C 19.950 0.1 2 95 . 10 VAL HG1 H 1.025 0.02 4 96 . 10 VAL CG2 C 19.050 0.1 2 97 . 10 VAL HG2 H 1.178 0.02 4 98 . 11 THR N N 115.006 0.1 1 99 . 11 THR H H 7.556 0.02 1 100 . 11 THR CA C 58.372 0.1 1 101 . 11 THR HA H 4.515 0.02 1 102 . 11 THR CB C 69.343 0.1 1 103 . 11 THR HB H 4.698 0.02 1 104 . 11 THR CG2 C 20.007 0.1 1 105 . 11 THR HG2 H 1.313 0.02 1 106 . 12 GLN N N 120.065 0.1 1 107 . 12 GLN H H 8.875 0.02 1 108 . 12 GLN CA C 57.050 0.1 1 109 . 12 GLN HA H 3.802 0.02 1 110 . 12 GLN CB C 26.123 0.1 1 111 . 12 GLN HB2 H 2.100 0.02 2 112 . 12 GLN HB3 H 2.040 0.02 2 113 . 12 GLN CG C 31.753 0.1 1 114 . 12 GLN HG3 H 2.374 0.02 2 115 . 12 GLN NE2 N 112.311 0.1 1 116 . 12 GLN HE21 H 6.660 0.02 2 117 . 12 GLN HE22 H 7.375 0.02 2 118 . 13 ASP N N 117.854 0.1 1 119 . 13 ASP H H 8.407 0.02 1 120 . 13 ASP CA C 55.250 0.1 1 121 . 13 ASP HA H 4.475 0.02 1 122 . 13 ASP CB C 38.650 0.1 1 123 . 13 ASP HB2 H 2.653 0.02 2 124 . 13 ASP HB3 H 2.562 0.02 2 125 . 14 LEU N N 122.534 0.1 1 126 . 14 LEU H H 7.694 0.02 1 127 . 14 LEU CA C 56.900 0.1 1 128 . 14 LEU HA H 4.090 0.02 1 129 . 14 LEU CB C 39.200 0.1 1 130 . 14 LEU HB2 H 2.150 0.02 2 131 . 14 LEU HB3 H 1.730 0.02 2 132 . 14 LEU CG C 25.800 0.1 1 133 . 14 LEU HG H 1.805 0.02 1 134 . 14 LEU CD1 C 21.250 0.1 2 135 . 14 LEU HD1 H 1.120 0.02 4 136 . 14 LEU CD2 C 24.287 0.1 2 137 . 14 LEU HD2 H 1.345 0.02 4 138 . 15 ARG N N 117.978 0.1 1 139 . 15 ARG H H 8.010 0.02 1 140 . 15 ARG CA C 58.700 0.1 1 141 . 15 ARG HA H 3.870 0.02 1 142 . 15 ARG CB C 28.800 0.1 1 143 . 15 ARG HB2 H 1.835 0.02 2 144 . 15 ARG HB3 H 1.560 0.02 2 145 . 15 ARG CG C 23.900 0.1 1 146 . 15 ARG HG2 H 1.740 0.02 2 147 . 15 ARG HG3 H 1.480 0.02 2 148 . 16 SER N N 112.699 0.1 1 149 . 16 SER H H 8.486 0.02 1 150 . 16 SER CA C 59.600 0.1 1 151 . 16 SER HA H 4.130 0.02 1 152 . 16 SER CB C 60.797 0.1 1 153 . 16 SER HB2 H 4.002 0.02 2 154 . 16 SER HB3 H 3.950 0.02 2 155 . 17 HIS N N 120.171 0.1 1 156 . 17 HIS H H 8.057 0.02 1 157 . 17 HIS CA C 57.900 0.1 1 158 . 17 HIS HA H 4.403 0.02 1 159 . 17 HIS CB C 26.750 0.1 1 160 . 17 HIS HB2 H 3.340 0.02 2 161 . 17 HIS HB3 H 3.240 0.02 2 162 . 17 HIS CD2 C 118.870 0.1 1 163 . 17 HIS HD2 H 7.500 0.02 1 164 . 18 LEU N N 123.194 0.1 1 165 . 18 LEU H H 8.834 0.02 1 166 . 18 LEU CA C 56.600 0.1 1 167 . 18 LEU HA H 4.173 0.02 1 168 . 18 LEU CB C 39.433 0.1 1 169 . 18 LEU HB2 H 2.312 0.02 2 170 . 18 LEU HB3 H 1.319 0.02 2 171 . 18 LEU CG C 25.500 0.1 1 172 . 18 LEU HG H 2.010 0.02 1 173 . 18 LEU CD1 C 22.749 0.1 2 174 . 18 LEU HD1 H 1.120 0.02 4 175 . 18 LEU CD2 C 25.210 0.1 2 176 . 18 LEU HD2 H 1.194 0.02 4 177 . 19 VAL N N 119.601 0.1 1 178 . 19 VAL H H 8.390 0.02 1 179 . 19 VAL CA C 65.900 0.1 1 180 . 19 VAL HA H 3.410 0.02 1 181 . 19 VAL CB C 29.400 0.1 1 182 . 19 VAL HB H 2.240 0.02 1 183 . 19 VAL CG1 C 19.550 0.1 2 184 . 19 VAL HG1 H 0.843 0.02 4 185 . 19 VAL CG2 C 22.000 0.1 2 186 . 19 VAL HG2 H 1.045 0.02 4 187 . 20 HIS N N 115.778 0.1 1 188 . 20 HIS H H 7.397 0.02 1 189 . 20 HIS CA C 57.500 0.1 1 190 . 20 HIS HA H 4.300 0.02 1 191 . 20 HIS CB C 26.900 0.1 1 192 . 20 HIS HB2 H 3.340 0.02 2 193 . 20 HIS HB3 H 3.260 0.02 2 194 . 20 HIS CD2 C 117.800 0.1 1 195 . 20 HIS HD2 H 7.155 0.02 1 196 . 21 LYS N N 119.065 0.1 1 197 . 21 LYS H H 7.950 0.02 1 198 . 21 LYS CA C 57.120 0.1 1 199 . 21 LYS HA H 4.065 0.02 1 200 . 21 LYS CB C 30.200 0.1 1 201 . 21 LYS HB2 H 2.110 0.02 2 202 . 21 LYS HB3 H 1.750 0.02 2 203 . 21 LYS CG C 23.550 0.1 1 204 . 21 LYS HG2 H 1.720 0.02 2 205 . 21 LYS HG3 H 1.563 0.02 2 206 . 22 LEU N N 120.997 0.1 1 207 . 22 LEU H H 8.495 0.02 1 208 . 22 LEU CA C 57.300 0.1 1 209 . 22 LEU HA H 3.840 0.02 1 210 . 22 LEU CB C 40.358 0.1 1 211 . 22 LEU HB2 H 2.050 0.02 2 212 . 22 LEU HB3 H 1.620 0.02 2 213 . 22 LEU CG C 25.950 0.1 1 214 . 22 LEU HG H 1.810 0.02 1 215 . 22 LEU CD1 C 24.250 0.1 2 216 . 22 LEU HD1 H 0.850 0.02 4 217 . 23 VAL N N 117.328 0.1 1 218 . 23 VAL H H 7.952 0.02 1 219 . 23 VAL CA C 65.500 0.1 1 220 . 23 VAL HA H 3.429 0.02 1 221 . 23 VAL CB C 29.750 0.1 1 222 . 23 VAL HB H 2.215 0.02 1 223 . 23 VAL CG1 C 19.927 0.1 2 224 . 23 VAL HG1 H 0.953 0.02 4 225 . 23 VAL CG2 C 22.250 0.1 2 226 . 23 VAL HG2 H 1.045 0.02 4 227 . 24 GLN N N 115.789 0.1 1 228 . 24 GLN H H 7.637 0.02 1 229 . 24 GLN CA C 56.050 0.1 1 230 . 24 GLN HA H 3.960 0.02 1 231 . 24 GLN CB C 26.800 0.1 1 232 . 24 GLN HB3 H 2.040 0.02 2 233 . 24 GLN CG C 32.150 0.1 1 234 . 24 GLN HG2 H 2.360 0.02 2 235 . 24 GLN HG3 H 2.280 0.02 2 236 . 24 GLN NE2 N 111.334 0.1 1 237 . 24 GLN HE21 H 6.820 0.02 2 238 . 24 GLN HE22 H 7.338 0.02 2 239 . 25 ALA N N 118.671 0.1 1 240 . 25 ALA H H 7.809 0.02 1 241 . 25 ALA CA C 51.850 0.1 1 242 . 25 ALA HA H 4.115 0.02 1 243 . 25 ALA CB C 16.700 0.1 1 244 . 25 ALA HB H 1.410 0.02 1 245 . 26 ILE N N 113.493 0.1 1 246 . 26 ILE H H 7.695 0.02 1 247 . 26 ILE CA C 61.000 0.1 1 248 . 26 ILE HA H 3.980 0.02 1 249 . 26 ILE CB C 37.000 0.1 1 250 . 26 ILE HB H 1.850 0.02 1 251 . 26 ILE CG2 C 16.237 0.1 2 252 . 26 ILE HG2 H 0.690 0.02 4 253 . 26 ILE CG1 C 25.500 0.1 2 254 . 26 ILE HG12 H 1.640 0.02 9 255 . 26 ILE HG13 H 1.270 0.02 9 256 . 26 ILE CD1 C 11.800 0.1 1 257 . 26 ILE HD1 H 0.820 0.02 1 258 . 27 PHE N N 119.992 0.1 1 259 . 27 PHE H H 7.940 0.02 1 260 . 27 PHE CA C 53.200 0.1 1 261 . 27 PHE HA H 4.880 0.02 1 262 . 27 PHE CB C 37.875 0.1 1 263 . 27 PHE HB2 H 3.143 0.02 2 264 . 27 PHE HB3 H 2.790 0.02 2 265 . 27 PHE CD1 C 130.258 0.1 3 266 . 27 PHE HD1 H 7.250 0.02 3 267 . 27 PHE CE1 C 129.023 0.1 3 268 . 27 PHE HE1 H 7.237 0.02 3 269 . 27 PHE CZ C 127.278 0.1 1 270 . 27 PHE HZ H 7.152 0.02 1 271 . 28 PRO CD C 48.150 0.1 1 272 . 28 PRO HD3 H 3.400 0.02 2 273 . 28 PRO CG C 25.400 0.1 1 274 . 28 PRO HG3 H 1.910 0.02 2 275 . 28 PRO CB C 29.850 0.1 1 276 . 28 PRO HB2 H 2.237 0.02 2 277 . 28 PRO HB3 H 1.875 0.02 2 278 . 28 PRO CA C 61.832 0.1 1 279 . 28 PRO HA H 4.493 0.02 1 280 . 29 THR N N 114.482 0.1 1 281 . 29 THR H H 7.962 0.02 1 282 . 29 THR CA C 56.900 0.1 1 283 . 29 THR HA H 4.550 0.02 1 284 . 29 THR CB C 68.056 0.1 1 285 . 29 THR HB H 4.099 0.02 1 286 . 29 THR CG2 C 19.350 0.1 1 287 . 29 THR HG2 H 1.130 0.02 1 288 . 30 PRO CD C 48.860 0.1 1 289 . 30 PRO HD3 H 3.665 0.02 2 290 . 30 PRO CG C 25.200 0.1 1 291 . 30 PRO HG3 H 1.900 0.02 2 292 . 30 PRO CB C 29.873 0.1 1 293 . 30 PRO HB2 H 2.095 0.02 2 294 . 30 PRO HB3 H 1.890 0.02 2 295 . 30 PRO CA C 61.435 0.1 1 296 . 30 PRO HA H 4.333 0.02 1 297 . 31 ASP N N 120.316 0.1 1 298 . 31 ASP H H 8.004 0.02 1 299 . 31 ASP CA C 49.593 0.1 1 300 . 31 ASP HA H 4.894 0.02 1 301 . 31 ASP CB C 39.818 0.1 1 302 . 31 ASP HB2 H 2.770 0.02 2 303 . 31 ASP HB3 H 2.610 0.02 2 304 . 32 PRO CD C 48.985 0.1 1 305 . 32 PRO HD3 H 3.877 0.02 2 306 . 32 PRO CG C 25.350 0.1 1 307 . 32 PRO HG2 H 2.030 0.02 2 308 . 32 PRO HG3 H 1.990 0.02 2 309 . 32 PRO CB C 29.994 0.1 1 310 . 32 PRO HB2 H 2.319 0.02 2 311 . 32 PRO HB3 H 1.950 0.02 2 312 . 32 PRO CA C 62.736 0.1 1 313 . 32 PRO HA H 4.248 0.02 1 314 . 33 ALA N N 120.356 0.1 1 315 . 33 ALA H H 8.230 0.02 1 316 . 33 ALA CA C 51.700 0.1 1 317 . 33 ALA HA H 4.170 0.02 1 318 . 33 ALA CB C 16.500 0.1 1 319 . 33 ALA HB H 1.390 0.02 1 320 . 34 ALA N N 120.848 0.1 1 321 . 34 ALA H H 7.743 0.02 1 322 . 34 ALA CA C 51.200 0.1 1 323 . 34 ALA HA H 4.250 0.02 1 324 . 34 ALA CB C 17.100 0.1 1 325 . 34 ALA HB H 1.461 0.02 1 326 . 35 LEU N N 117.984 0.1 1 327 . 35 LEU H H 7.661 0.02 1 328 . 35 LEU CA C 54.200 0.1 1 329 . 35 LEU HA H 4.170 0.02 1 330 . 35 LEU CB C 39.898 0.1 1 331 . 35 LEU HB2 H 1.690 0.02 2 332 . 35 LEU HB3 H 1.569 0.02 2 333 . 35 LEU CG C 25.250 0.1 1 334 . 35 LEU HG H 1.600 0.02 1 335 . 35 LEU CD1 C 21.500 0.1 2 336 . 35 LEU HD1 H 0.825 0.02 4 337 . 35 LEU CD2 C 23.237 0.1 2 338 . 35 LEU HD2 H 0.880 0.02 4 339 . 36 LYS N N 118.917 0.1 1 340 . 36 LYS H H 7.846 0.02 1 341 . 36 LYS CA C 54.550 0.1 1 342 . 36 LYS HA H 4.260 0.02 1 343 . 36 LYS CB C 30.640 0.1 1 344 . 36 LYS HB2 H 1.896 0.02 2 345 . 36 LYS HB3 H 1.780 0.02 2 346 . 36 LYS CG C 22.800 0.1 1 347 . 36 LYS HG2 H 1.445 0.02 2 348 . 36 LYS HG3 H 1.410 0.02 2 349 . 37 ASP N N 119.961 0.1 1 350 . 37 ASP H H 7.910 0.02 1 351 . 37 ASP CA C 52.375 0.1 1 352 . 37 ASP HA H 4.555 0.02 1 353 . 37 ASP CB C 40.000 0.1 1 354 . 37 ASP HB3 H 2.730 0.02 2 355 . 38 ARG N N 120.710 0.1 1 356 . 38 ARG H H 8.305 0.02 1 357 . 38 ARG CA C 55.800 0.1 1 358 . 38 ARG HA H 4.180 0.02 1 359 . 38 ARG CB C 27.900 0.1 1 360 . 38 ARG HB3 H 1.880 0.02 2 361 . 38 ARG CG C 25.500 0.1 1 362 . 38 ARG HG2 H 1.743 0.02 2 363 . 38 ARG HG3 H 1.642 0.02 2 364 . 38 ARG CD C 41.500 0.1 1 365 . 38 ARG HD3 H 3.155 0.02 2 366 . 38 ARG NE N 84.521 0.1 1 367 . 38 ARG HE H 7.235 0.02 1 368 . 39 ARG N N 119.764 0.1 1 369 . 39 ARG H H 8.390 0.02 1 370 . 39 ARG CA C 56.000 0.1 1 371 . 39 ARG HA H 4.160 0.02 1 372 . 39 ARG CB C 28.400 0.1 1 373 . 39 ARG HB3 H 1.900 0.02 2 374 . 39 ARG CG C 27.100 0.1 1 375 . 39 ARG HG3 H 1.660 0.02 2 376 . 39 ARG CD C 41.300 0.1 1 377 . 39 ARG HD3 H 3.210 0.02 2 378 . 40 MET N N 118.847 0.1 1 379 . 40 MET H H 8.250 0.02 1 380 . 40 MET CA C 54.650 0.1 1 381 . 40 MET HA H 4.380 0.02 1 382 . 40 MET CB C 29.350 0.1 1 383 . 40 MET HB2 H 2.130 0.02 2 384 . 40 MET HB3 H 2.050 0.02 2 385 . 40 MET CG C 30.400 0.1 1 386 . 40 MET HG2 H 2.565 0.02 2 387 . 40 MET HG3 H 2.485 0.02 2 388 . 40 MET CE C 14.971 0.1 1 389 . 40 MET HE H 1.892 0.02 1 390 . 41 GLU N N 119.056 0.1 1 391 . 41 GLU H H 8.374 0.02 1 392 . 41 GLU CA C 57.800 0.1 1 393 . 41 GLU HA H 3.967 0.02 1 394 . 41 GLU CB C 27.100 0.1 1 395 . 41 GLU HB3 H 2.020 0.02 2 396 . 41 GLU CG C 34.250 0.1 1 397 . 41 GLU HG3 H 2.307 0.02 2 398 . 42 ASN N N 117.533 0.1 1 399 . 42 ASN H H 8.177 0.02 1 400 . 42 ASN CA C 53.632 0.1 1 401 . 42 ASN HA H 4.564 0.02 1 402 . 42 ASN CB C 35.977 0.1 1 403 . 42 ASN HB2 H 2.882 0.02 2 404 . 42 ASN HB3 H 2.788 0.02 2 405 . 42 ASN ND2 N 112.063 0.1 1 406 . 42 ASN HD21 H 6.910 0.02 2 407 . 42 ASN HD22 H 7.618 0.02 2 408 . 43 LEU N N 123.162 0.1 1 409 . 43 LEU H H 7.851 0.02 1 410 . 43 LEU CA C 55.900 0.1 1 411 . 43 LEU HA H 4.180 0.02 1 412 . 43 LEU CB C 39.400 0.1 1 413 . 43 LEU HB3 H 1.875 0.02 2 414 . 43 LEU CG C 25.200 0.1 1 415 . 43 LEU HG H 1.670 0.02 1 416 . 43 LEU CD1 C 22.150 0.1 2 417 . 43 LEU HD1 H 0.708 0.02 4 418 . 43 LEU CD2 C 22.800 0.1 2 419 . 43 LEU HD2 H 0.826 0.02 4 420 . 44 VAL N N 119.607 0.1 1 421 . 44 VAL H H 8.320 0.02 1 422 . 44 VAL CA C 64.900 0.1 1 423 . 44 VAL HA H 3.478 0.02 1 424 . 44 VAL CB C 29.700 0.1 1 425 . 44 VAL HB H 2.090 0.02 1 426 . 44 VAL CG1 C 19.293 0.1 2 427 . 44 VAL HG1 H 0.903 0.02 4 428 . 44 VAL CG2 C 21.223 0.1 2 429 . 44 VAL HG2 H 1.072 0.02 4 430 . 45 ALA N N 120.273 0.1 1 431 . 45 ALA H H 7.751 0.02 1 432 . 45 ALA CA C 53.468 0.1 1 433 . 45 ALA HA H 4.046 0.02 1 434 . 45 ALA CB C 16.014 0.1 1 435 . 45 ALA HB H 1.528 0.02 1 436 . 46 TYR N N 120.091 0.1 1 437 . 46 TYR H H 7.900 0.02 1 438 . 46 TYR CA C 59.030 0.1 1 439 . 46 TYR HA H 4.305 0.02 1 440 . 46 TYR CB C 36.308 0.1 1 441 . 46 TYR HB3 H 3.250 0.02 2 442 . 46 TYR CD1 C 130.638 0.1 3 443 . 46 TYR HD1 H 7.051 0.02 3 444 . 46 TYR CE1 C 116.314 0.1 3 445 . 46 TYR HE1 H 6.705 0.02 3 446 . 47 ALA N N 121.826 0.1 1 447 . 47 ALA H H 8.601 0.02 1 448 . 47 ALA CA C 53.392 0.1 1 449 . 47 ALA HA H 3.740 0.02 1 450 . 47 ALA CB C 18.250 0.1 1 451 . 47 ALA HB H 1.540 0.02 1 452 . 48 LYS N N 116.156 0.1 1 453 . 48 LYS H H 8.617 0.02 1 454 . 48 LYS CA C 57.700 0.1 1 455 . 48 LYS HA H 3.982 0.02 1 456 . 48 LYS CB C 30.900 0.1 1 457 . 48 LYS HB3 H 1.880 0.02 2 458 . 48 LYS CG C 24.600 0.1 1 459 . 48 LYS HG2 H 1.670 0.02 2 460 . 48 LYS HG3 H 1.385 0.02 2 461 . 48 LYS CD C 27.800 0.1 1 462 . 48 LYS HD3 H 1.650 0.02 2 463 . 48 LYS CE C 40.100 0.1 1 464 . 48 LYS HE2 H 2.910 0.02 2 465 . 48 LYS HE3 H 2.840 0.02 2 466 . 49 LYS N N 122.851 0.1 1 467 . 49 LYS H H 7.703 0.02 1 468 . 49 LYS CA C 57.200 0.1 1 469 . 49 LYS HA H 4.065 0.02 1 470 . 49 LYS CB C 30.050 0.1 1 471 . 49 LYS HB2 H 2.090 0.02 2 472 . 49 LYS HB3 H 1.915 0.02 2 473 . 49 LYS CG C 23.000 0.1 1 474 . 49 LYS HG2 H 1.485 0.02 2 475 . 49 LYS HG3 H 1.405 0.02 2 476 . 49 LYS CD C 27.000 0.1 1 477 . 49 LYS HD2 H 1.700 0.02 2 478 . 49 LYS HD3 H 1.640 0.02 2 479 . 50 VAL N N 118.548 0.1 1 480 . 50 VAL H H 8.058 0.02 1 481 . 50 VAL CA C 64.011 0.1 1 482 . 50 VAL HA H 3.725 0.02 1 483 . 50 VAL CB C 29.800 0.1 1 484 . 50 VAL HB H 1.910 0.02 1 485 . 50 VAL CG1 C 20.143 0.1 2 486 . 50 VAL HG1 H 0.639 0.02 4 487 . 50 VAL CG2 C 19.801 0.1 2 488 . 50 VAL HG2 H 0.760 0.02 4 489 . 51 GLU N N 119.700 0.1 1 490 . 51 GLU H H 8.451 0.02 1 491 . 51 GLU CA C 59.728 0.1 1 492 . 51 GLU HA H 3.799 0.02 1 493 . 51 GLU CB C 26.800 0.1 1 494 . 51 GLU HB2 H 2.306 0.02 2 495 . 51 GLU HB3 H 1.620 0.02 2 496 . 51 GLU CG C 33.570 0.1 1 497 . 51 GLU HG2 H 2.400 0.02 2 498 . 51 GLU HG3 H 2.330 0.02 2 499 . 52 GLY N N 105.987 0.1 1 500 . 52 GLY H H 8.026 0.02 1 501 . 52 GLY CA C 45.484 0.1 1 502 . 52 GLY HA2 H 3.915 0.02 2 503 . 52 GLY HA3 H 3.583 0.02 2 504 . 53 ASP N N 122.305 0.1 1 505 . 53 ASP H H 8.280 0.02 1 506 . 53 ASP CA C 55.100 0.1 1 507 . 53 ASP HA H 4.526 0.02 1 508 . 53 ASP CB C 38.050 0.1 1 509 . 53 ASP HB2 H 2.960 0.02 2 510 . 53 ASP HB3 H 2.680 0.02 2 511 . 54 MET N N 120.317 0.1 1 512 . 54 MET H H 8.290 0.02 1 513 . 54 MET CA C 55.800 0.1 1 514 . 54 MET HA H 4.520 0.02 1 515 . 54 MET CB C 29.700 0.1 1 516 . 54 MET HB2 H 2.370 0.02 2 517 . 54 MET HB3 H 2.070 0.02 2 518 . 54 MET CG C 31.358 0.1 1 519 . 54 MET HG2 H 3.002 0.02 2 520 . 54 MET HG3 H 2.490 0.02 2 521 . 54 MET CE C 17.697 0.1 1 522 . 54 MET HE H 2.047 0.02 1 523 . 55 TYR N N 121.734 0.1 1 524 . 55 TYR H H 9.351 0.02 1 525 . 55 TYR CA C 60.346 0.1 1 526 . 55 TYR HA H 4.378 0.02 1 527 . 55 TYR CB C 36.965 0.1 1 528 . 55 TYR HB2 H 3.609 0.02 2 529 . 55 TYR HB3 H 3.090 0.02 2 530 . 55 TYR CD1 C 130.623 0.1 3 531 . 55 TYR HD1 H 6.601 0.02 3 532 . 55 TYR CE1 C 114.967 0.1 3 533 . 55 TYR HE1 H 5.986 0.02 3 534 . 56 GLU N N 114.225 0.1 1 535 . 56 GLU H H 7.880 0.02 1 536 . 56 GLU CA C 55.600 0.1 1 537 . 56 GLU HA H 4.358 0.02 1 538 . 56 GLU CB C 27.950 0.1 1 539 . 56 GLU HB2 H 2.246 0.02 2 540 . 56 GLU HB3 H 2.147 0.02 2 541 . 56 GLU CG C 33.800 0.1 1 542 . 56 GLU HG2 H 2.580 0.02 2 543 . 56 GLU HG3 H 2.520 0.02 2 544 . 57 SER N N 112.234 0.1 1 545 . 57 SER H H 7.878 0.02 1 546 . 57 SER CA C 58.164 0.1 1 547 . 57 SER HA H 4.424 0.02 1 548 . 57 SER CB C 62.700 0.1 1 549 . 57 SER HB3 H 3.940 0.02 2 550 . 58 ALA N N 123.584 0.1 1 551 . 58 ALA H H 8.192 0.02 1 552 . 58 ALA CA C 50.700 0.1 1 553 . 58 ALA HA H 4.185 0.02 1 554 . 58 ALA CB C 17.650 0.1 1 555 . 58 ALA HB H 1.560 0.02 1 556 . 59 ASN N N 117.074 0.1 1 557 . 59 ASN H H 9.195 0.02 1 558 . 59 ASN CA C 51.506 0.1 1 559 . 59 ASN HA H 5.104 0.02 1 560 . 59 ASN CB C 38.215 0.1 1 561 . 59 ASN HB2 H 2.950 0.02 2 562 . 59 ASN HB3 H 2.755 0.02 2 563 . 59 ASN ND2 N 116.145 0.1 1 564 . 59 ASN HD21 H 7.010 0.02 2 565 . 59 ASN HD22 H 8.064 0.02 2 566 . 60 SER N N 111.335 0.1 1 567 . 60 SER H H 6.872 0.02 1 568 . 60 SER CA C 54.632 0.1 1 569 . 60 SER HA H 3.718 0.02 1 570 . 60 SER CB C 63.000 0.1 1 571 . 60 SER HB3 H 3.890 0.02 2 572 . 61 ARG N N 121.716 0.1 1 573 . 61 ARG H H 8.704 0.02 1 574 . 61 ARG CA C 57.081 0.1 1 575 . 61 ARG HA H 3.221 0.02 1 576 . 61 ARG CB C 28.400 0.1 1 577 . 61 ARG HB2 H 2.020 0.02 2 578 . 61 ARG HB3 H 1.880 0.02 2 579 . 61 ARG CG C 25.850 0.1 1 580 . 61 ARG HG2 H 1.800 0.02 2 581 . 61 ARG HG3 H 1.760 0.02 2 582 . 61 ARG CD C 41.876 0.1 1 583 . 61 ARG HD2 H 3.446 0.02 2 584 . 61 ARG HD3 H 3.379 0.02 2 585 . 62 ASP N N 116.200 0.1 1 586 . 62 ASP H H 8.125 0.02 1 587 . 62 ASP CA C 55.400 0.1 1 588 . 62 ASP HA H 4.355 0.02 1 589 . 62 ASP CB C 38.200 0.1 1 590 . 62 ASP HB2 H 2.560 0.02 2 591 . 62 ASP HB3 H 2.445 0.02 2 592 . 63 GLU N N 120.351 0.1 1 593 . 63 GLU H H 7.713 0.02 1 594 . 63 GLU CA C 57.400 0.1 1 595 . 63 GLU HA H 4.000 0.02 1 596 . 63 GLU CB C 28.200 0.1 1 597 . 63 GLU HB3 H 1.880 0.02 2 598 . 63 GLU CG C 34.950 0.1 1 599 . 63 GLU HG2 H 2.328 0.02 2 600 . 63 GLU HG3 H 2.227 0.02 2 601 . 64 TYR N N 121.625 0.1 1 602 . 64 TYR H H 7.367 0.02 1 603 . 64 TYR CA C 58.850 0.1 1 604 . 64 TYR HA H 3.910 0.02 1 605 . 64 TYR CB C 36.500 0.1 1 606 . 64 TYR HB2 H 2.800 0.02 2 607 . 64 TYR HB3 H 2.436 0.02 2 608 . 64 TYR CD1 C 130.632 0.1 3 609 . 64 TYR HD1 H 6.705 0.02 3 610 . 64 TYR CE1 C 115.579 0.1 3 611 . 64 TYR HE1 H 7.053 0.02 3 612 . 64 TYR CE2 C 116.303 0.1 1 613 . 64 TYR HE2 H 7.049 0.02 3 614 . 65 TYR N N 114.571 0.1 1 615 . 65 TYR H H 7.684 0.02 1 616 . 65 TYR CA C 60.450 0.1 1 617 . 65 TYR HA H 4.010 0.02 1 618 . 65 TYR CB C 36.500 0.1 1 619 . 65 TYR HB2 H 2.990 0.02 2 620 . 65 TYR HB3 H 2.890 0.02 2 621 . 65 TYR CD1 C 130.639 0.1 3 622 . 65 TYR HD1 H 7.120 0.02 3 623 . 65 TYR CE1 C 116.060 0.1 3 624 . 65 TYR HE1 H 6.865 0.02 3 625 . 66 HIS N N 117.620 0.1 1 626 . 66 HIS H H 8.139 0.02 1 627 . 66 HIS CA C 58.000 0.1 1 628 . 66 HIS HA H 4.300 0.02 1 629 . 66 HIS CB C 26.700 0.1 1 630 . 66 HIS HB2 H 3.370 0.02 2 631 . 66 HIS HB3 H 3.280 0.02 2 632 . 66 HIS CD2 C 117.800 0.1 1 633 . 66 HIS HD2 H 7.155 0.02 1 634 . 67 LEU N N 118.845 0.1 1 635 . 67 LEU H H 9.139 0.02 1 636 . 67 LEU CA C 55.800 0.1 1 637 . 67 LEU HA H 3.935 0.02 1 638 . 67 LEU CB C 40.000 0.1 1 639 . 67 LEU HB2 H 1.970 0.02 2 640 . 67 LEU HB3 H 1.800 0.02 2 641 . 67 LEU CG C 25.150 0.1 1 642 . 67 LEU HG H 2.040 0.02 1 643 . 67 LEU CD1 C 20.150 0.1 2 644 . 67 LEU HD1 H 0.930 0.02 4 645 . 67 LEU CD2 C 23.854 0.1 2 646 . 67 LEU HD2 H 0.978 0.02 4 647 . 68 LEU N N 119.181 0.1 1 648 . 68 LEU H H 7.920 0.02 1 649 . 68 LEU CA C 56.165 0.1 1 650 . 68 LEU HA H 3.778 0.02 1 651 . 68 LEU CB C 41.329 0.1 1 652 . 68 LEU HB2 H 1.871 0.02 2 653 . 68 LEU HB3 H 1.073 0.02 2 654 . 68 LEU CG C 24.603 0.1 1 655 . 68 LEU HG H 1.500 0.02 1 656 . 68 LEU CD1 C 23.396 0.1 2 657 . 68 LEU HD1 H 0.330 0.02 4 658 . 68 LEU CD2 C 22.000 0.1 2 659 . 68 LEU HD2 H 0.694 0.02 4 660 . 69 ALA N N 121.057 0.1 1 661 . 69 ALA H H 8.103 0.02 1 662 . 69 ALA CA C 53.816 0.1 1 663 . 69 ALA HA H 3.798 0.02 1 664 . 69 ALA CB C 18.050 0.1 1 665 . 69 ALA HB H 1.515 0.02 1 666 . 70 GLU N N 116.201 0.1 1 667 . 70 GLU H H 8.410 0.02 1 668 . 70 GLU CA C 57.750 0.1 1 669 . 70 GLU HA H 3.770 0.02 1 670 . 70 GLU CB C 27.600 0.1 1 671 . 70 GLU HB2 H 2.030 0.02 2 672 . 70 GLU HB3 H 1.880 0.02 2 673 . 70 GLU CG C 34.270 0.1 1 674 . 70 GLU HG2 H 2.090 0.02 2 675 . 70 GLU HG3 H 1.975 0.02 2 676 . 71 LYS N N 119.610 0.1 1 677 . 71 LYS H H 7.871 0.02 1 678 . 71 LYS CA C 55.850 0.1 1 679 . 71 LYS HA H 4.183 0.02 1 680 . 71 LYS CB C 29.500 0.1 1 681 . 71 LYS HB2 H 2.030 0.02 2 682 . 71 LYS HB3 H 1.973 0.02 2 683 . 71 LYS CG C 22.350 0.1 1 684 . 71 LYS HG2 H 1.575 0.02 2 685 . 71 LYS HG3 H 1.425 0.02 2 686 . 71 LYS CD C 26.150 0.1 1 687 . 71 LYS HD2 H 1.857 0.02 2 688 . 71 LYS HD3 H 1.703 0.02 2 689 . 71 LYS CE C 40.000 0.1 1 690 . 71 LYS HE3 H 2.930 0.02 2 691 . 72 ILE N N 118.660 0.1 1 692 . 72 ILE H H 8.310 0.02 1 693 . 72 ILE CA C 63.640 0.1 1 694 . 72 ILE HA H 3.504 0.02 1 695 . 72 ILE CB C 35.598 0.1 1 696 . 72 ILE HB H 1.969 0.02 1 697 . 72 ILE CG2 C 17.057 0.1 2 698 . 72 ILE HG2 H 0.804 0.02 4 699 . 72 ILE CG1 C 27.048 0.1 2 700 . 72 ILE HG12 H 1.865 0.02 9 701 . 72 ILE HG13 H 0.968 0.02 9 702 . 72 ILE CD1 C 12.000 0.1 1 703 . 72 ILE HD1 H 0.820 0.02 1 704 . 73 TYR N N 119.778 0.1 1 705 . 73 TYR H H 8.304 0.02 1 706 . 73 TYR CA C 59.900 0.1 1 707 . 73 TYR HA H 3.975 0.02 1 708 . 73 TYR CB C 36.900 0.1 1 709 . 73 TYR HB2 H 3.145 0.02 2 710 . 73 TYR HB3 H 2.855 0.02 2 711 . 73 TYR CD1 C 131.194 0.1 3 712 . 73 TYR HD1 H 7.050 0.02 3 713 . 73 TYR CE1 C 115.590 0.1 3 714 . 73 TYR HE1 H 6.786 0.02 3 715 . 74 LYS N N 118.230 0.1 1 716 . 74 LYS H H 8.007 0.02 1 717 . 74 LYS CA C 57.900 0.1 1 718 . 74 LYS HA H 3.773 0.02 1 719 . 74 LYS CB C 30.950 0.1 1 720 . 74 LYS HB2 H 2.070 0.02 2 721 . 74 LYS HB3 H 2.015 0.02 2 722 . 74 LYS CG C 23.580 0.1 1 723 . 74 LYS HG2 H 1.718 0.02 2 724 . 74 LYS HG3 H 1.480 0.02 2 725 . 74 LYS CD C 27.750 0.1 1 726 . 74 LYS HD3 H 1.720 0.02 2 727 . 74 LYS CE C 40.100 0.1 1 728 . 74 LYS HE3 H 3.010 0.02 2 729 . 75 ILE N N 120.310 0.1 1 730 . 75 ILE H H 8.269 0.02 1 731 . 75 ILE CA C 62.900 0.1 1 732 . 75 ILE HA H 3.769 0.02 1 733 . 75 ILE CB C 36.300 0.1 1 734 . 75 ILE HB H 1.893 0.02 1 735 . 75 ILE CG2 C 15.875 0.1 2 736 . 75 ILE HG2 H 0.907 0.02 4 737 . 75 ILE CG1 C 26.871 0.1 2 738 . 75 ILE HG12 H 1.830 0.02 9 739 . 75 ILE HG13 H 1.181 0.02 9 740 . 75 ILE CD1 C 12.100 0.1 1 741 . 75 ILE HD1 H 0.830 0.02 1 742 . 76 GLN N N 118.581 0.1 1 743 . 76 GLN H H 8.685 0.02 1 744 . 76 GLN CA C 57.850 0.1 1 745 . 76 GLN HA H 3.865 0.02 1 746 . 76 GLN CB C 25.900 0.1 1 747 . 76 GLN HB2 H 2.170 0.02 2 748 . 76 GLN HB3 H 1.870 0.02 2 749 . 76 GLN CG C 32.452 0.1 1 750 . 76 GLN HG2 H 2.680 0.02 2 751 . 76 GLN HG3 H 2.288 0.02 2 752 . 76 GLN NE2 N 109.351 0.1 1 753 . 76 GLN HE21 H 6.561 0.02 2 754 . 76 GLN HE22 H 7.301 0.02 2 755 . 77 LYS N N 119.730 0.1 1 756 . 77 LYS H H 8.132 0.02 1 757 . 77 LYS CA C 56.300 0.1 1 758 . 77 LYS HA H 3.935 0.02 1 759 . 77 LYS CB C 29.470 0.1 1 760 . 77 LYS HB2 H 1.710 0.02 2 761 . 77 LYS HB3 H 1.535 0.02 2 762 . 77 LYS CG C 22.000 0.1 1 763 . 77 LYS HG2 H 1.209 0.02 2 764 . 77 LYS HG3 H 1.172 0.02 2 765 . 77 LYS CD C 26.350 0.1 1 766 . 77 LYS HD2 H 1.570 0.02 2 767 . 77 LYS HD3 H 1.510 0.02 2 768 . 77 LYS CE C 39.800 0.1 1 769 . 77 LYS HE2 H 2.950 0.02 2 770 . 77 LYS HE3 H 2.860 0.02 2 771 . 78 GLU N N 120.226 0.1 1 772 . 78 GLU H H 7.934 0.02 1 773 . 78 GLU CA C 57.500 0.1 1 774 . 78 GLU HA H 4.045 0.02 1 775 . 78 GLU CB C 27.350 0.1 1 776 . 78 GLU HB2 H 2.200 0.02 2 777 . 78 GLU HB3 H 2.070 0.02 2 778 . 78 GLU CG C 34.400 0.1 1 779 . 78 GLU HG2 H 2.460 0.02 2 780 . 78 GLU HG3 H 2.220 0.02 2 781 . 79 LEU N N 119.571 0.1 1 782 . 79 LEU H H 8.231 0.02 1 783 . 79 LEU CA C 55.700 0.1 1 784 . 79 LEU HA H 4.040 0.02 1 785 . 79 LEU CB C 39.700 0.1 1 786 . 79 LEU HB2 H 1.890 0.02 2 787 . 79 LEU HB3 H 1.520 0.02 2 788 . 79 LEU CG C 24.900 0.1 1 789 . 79 LEU HG H 1.831 0.02 1 790 . 79 LEU CD1 C 21.250 0.1 2 791 . 79 LEU HD1 H 0.847 0.02 4 792 . 79 LEU CD2 C 23.750 0.1 2 793 . 79 LEU HD2 H 0.860 0.02 4 794 . 80 GLU N N 119.884 0.1 1 795 . 80 GLU H H 7.940 0.02 1 796 . 80 GLU HA H 4.020 0.02 1 797 . 80 GLU HB2 H 2.120 0.02 2 798 . 80 GLU HB3 H 2.244 0.02 2 799 . 80 GLU HG3 H 2.375 0.02 2 800 . 81 GLU N N 118.938 0.1 1 801 . 81 GLU H H 8.001 0.02 1 802 . 81 GLU CA C 56.700 0.1 1 803 . 81 GLU HA H 4.045 0.02 1 804 . 81 GLU CB C 27.500 0.1 1 805 . 81 GLU HB2 H 2.130 0.02 2 806 . 81 GLU HB3 H 2.090 0.02 2 807 . 81 GLU CG C 34.250 0.1 1 808 . 81 GLU HG2 H 2.422 0.02 2 809 . 81 GLU HG3 H 2.288 0.02 2 810 . 82 LYS N N 119.157 0.1 1 811 . 82 LYS H H 7.900 0.02 1 812 . 82 LYS CA C 56.000 0.1 1 813 . 82 LYS HA H 4.140 0.02 1 814 . 82 LYS CB C 30.350 0.1 1 815 . 82 LYS HB3 H 1.915 0.02 2 816 . 82 LYS CG C 23.250 0.1 1 817 . 82 LYS HG2 H 1.580 0.02 2 818 . 82 LYS HG3 H 1.485 0.02 2 819 . 82 LYS CD C 26.900 0.1 1 820 . 82 LYS HD3 H 1.660 0.02 2 821 . 82 LYS CE C 40.000 0.1 1 822 . 82 LYS HE3 H 2.970 0.02 2 823 . 83 ARG N N 118.960 0.1 1 824 . 83 ARG H H 8.260 0.02 1 825 . 83 ARG CA C 56.000 0.1 1 826 . 83 ARG HA H 4.160 0.02 1 827 . 83 ARG CB C 28.400 0.1 1 828 . 83 ARG HB3 H 1.900 0.02 2 829 . 83 ARG CG C 27.100 0.1 1 830 . 83 ARG HG3 H 1.660 0.02 2 831 . 83 ARG CD C 41.300 0.1 1 832 . 83 ARG HD3 H 3.210 0.02 2 833 . 84 ARG N N 119.040 0.1 1 834 . 84 ARG H H 7.891 0.02 1 835 . 84 ARG CA C 54.900 0.1 1 836 . 84 ARG HA H 4.250 0.02 1 837 . 84 ARG CB C 28.600 0.1 1 838 . 84 ARG HB2 H 1.915 0.02 2 839 . 84 ARG HB3 H 1.840 0.02 2 840 . 84 ARG CG C 25.500 0.1 1 841 . 84 ARG HG2 H 1.740 0.02 2 842 . 84 ARG HG3 H 1.660 0.02 2 843 . 84 ARG CD C 41.600 0.1 1 844 . 84 ARG HD3 H 3.205 0.02 2 845 . 84 ARG NE N 84.450 0.1 1 846 . 84 ARG HE H 7.364 0.02 1 847 . 85 SER N N 114.896 0.1 1 848 . 85 SER H H 7.986 0.02 1 849 . 85 SER CA C 56.967 0.1 1 850 . 85 SER HA H 4.407 0.02 1 851 . 85 SER CB C 61.891 0.1 1 852 . 85 SER HB3 H 3.917 0.02 2 853 . 86 ARG N N 122.115 0.1 1 854 . 86 ARG H H 8.020 0.02 1 855 . 86 ARG CA C 54.000 0.1 1 856 . 86 ARG HA H 4.360 0.02 1 857 . 86 ARG CB C 28.600 0.1 1 858 . 86 ARG HB2 H 1.930 0.02 2 859 . 86 ARG HB3 H 1.790 0.02 2 860 . 86 ARG CG C 25.200 0.1 1 861 . 86 ARG HG3 H 1.650 0.02 2 862 . 86 ARG CD C 41.400 0.1 1 863 . 86 ARG HD3 H 3.180 0.02 2 864 . 86 ARG NE N 84.745 0.1 1 865 . 86 ARG HE H 7.191 0.02 1 866 . 87 LEU N N 128.142 0.1 1 867 . 87 LEU H H 7.755 0.02 1 868 . 87 LEU CA C 54.700 0.1 1 869 . 87 LEU HA H 4.157 0.02 1 870 . 87 LEU CB C 41.364 0.1 1 871 . 87 LEU HB3 H 1.563 0.02 2 872 . 87 LEU CG C 25.250 0.1 1 873 . 87 LEU HG H 1.575 0.02 1 874 . 87 LEU CD1 C 23.500 0.1 2 875 . 87 LEU HD1 H 0.860 0.02 4 stop_ loop_ _Atom_shift_assign_ID_ambiguity 10 '10,10' '97,97,97,95,95,95' '137,137,137,135,135,135' '186,186,186,184,184,184' '216,216,216' '226,226,226,224,224,224' '252,252,252' '338,338,338,336,336,336' '419,419,419,417,417,417' '429,429,429,427,427,427' '646,646,646,644,644,644' '659,659,659,657,657,657' '698,698,698' '736,736,736' '793,793,793,791,791,791' '875,875,875' stop_ save_ save_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name C-MYB _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 LYS CA C 55.701 . 1 2 . 1 LYS HA H 3.987 . 1 3 . 1 LYS CB C 33.100 . 1 4 . 1 LYS HB3 H 1.866 . . 5 . 1 LYS CG C 24.092 . 1 6 . 1 LYS HG2 H 1.470 . . 7 . 1 LYS HG3 H 1.414 . . 8 . 1 LYS CD C 29.070 . 1 9 . 1 LYS HD3 H 1.688 . . 10 . 1 LYS CE C 41.550 . 1 11 . 1 LYS HE3 H 2.940 . . 12 . 2 GLU CA C 56.832 . 1 13 . 2 GLU HA H 4.280 . 1 14 . 2 GLU CB C 29.700 . 1 15 . 2 GLU HB2 H 2.040 . . 16 . 2 GLU HB3 H 1.918 . . 17 . 2 GLU CG C 36.140 . 1 18 . 2 GLU HG3 H 2.305 . . 19 . 3 LYS N N 125.105 . 1 20 . 3 LYS H H 8.761 . 1 21 . 3 LYS CA C 58.400 . 1 22 . 3 LYS HA H 4.143 . 1 23 . 3 LYS CB C 32.700 . 1 24 . 3 LYS HB3 H 1.860 . . 25 . 3 LYS CG C 24.800 . 1 26 . 3 LYS HG2 H 1.490 . . 27 . 3 LYS HG3 H 1.440 . . 28 . 3 LYS CD C 29.200 . 1 29 . 3 LYS HD3 H 1.700 . . 30 . 3 LYS CE C 41.900 . 1 31 . 3 LYS HE3 H 3.014 . . 32 . 4 ARG N N 119.324 . 1 33 . 4 ARG H H 8.582 . 1 34 . 4 ARG CA C 57.350 . 1 35 . 4 ARG HA H 4.230 . 1 36 . 4 ARG CB C 30.129 . 1 37 . 4 ARG HB2 H 1.890 . . 38 . 4 ARG HB3 H 1.840 . . 39 . 4 ARG CG C 27.186 . 1 40 . 4 ARG HG2 H 1.897 . . 41 . 4 ARG HG3 H 1.710 . . 42 . 4 ARG CD C 43.012 . 1 43 . 4 ARG HD2 H 3.466 . . 44 . 4 ARG HD3 H 3.240 . . 45 . 5 ILE N N 118.680 . 1 46 . 5 ILE H H 7.531 . 1 47 . 5 ILE CA C 64.660 . 1 48 . 5 ILE HA H 3.602 . 1 49 . 5 ILE CB C 36.826 . 1 50 . 5 ILE HB H 1.812 . 1 51 . 5 ILE CG2 C 17.441 . . 52 . 5 ILE HG2 H 0.811 . . 53 . 5 ILE CG1 C 29.140 . . 54 . 5 ILE HG12 H 1.181 . . 55 . 5 ILE HG13 H 0.790 . . 56 . 5 ILE CD1 C 12.479 . 1 57 . 5 ILE HD1 H 0.629 . . 58 . 6 LYS N N 119.986 . 1 59 . 6 LYS H H 7.703 . 1 60 . 6 LYS CA C 58.627 . 1 61 . 6 LYS HA H 4.117 . 1 62 . 6 LYS CB C 31.635 . 1 63 . 6 LYS HB2 H 1.939 . . 64 . 6 LYS HB3 H 1.844 . . 65 . 6 LYS CG C 24.700 . 1 66 . 6 LYS HG3 H 1.475 . . 67 . 6 LYS CD C 28.500 . 1 68 . 6 LYS HD2 H 1.726 . . 69 . 6 LYS HD3 H 1.680 . . 70 . 6 LYS CE C 41.800 . 1 71 . 6 LYS HE3 H 2.940 . . 72 . 7 GLU N N 117.730 . 1 73 . 7 GLU H H 7.936 . 1 74 . 7 GLU CA C 59.433 . 1 75 . 7 GLU HA H 3.975 . 1 76 . 7 GLU CB C 29.500 . 1 77 . 7 GLU HB2 H 2.236 . . 78 . 7 GLU HB3 H 2.091 . . 79 . 7 GLU CG C 36.500 . 1 80 . 7 GLU HG2 H 2.430 . . 81 . 7 GLU HG3 H 2.250 . . 82 . 8 LEU N N 121.253 . 1 83 . 8 LEU H H 8.048 . 1 84 . 8 LEU CA C 57.672 . 1 85 . 8 LEU HA H 4.134 . 1 86 . 8 LEU CB C 43.151 . 1 87 . 8 LEU HB2 H 2.186 . . 88 . 8 LEU HB3 H 1.255 . . 89 . 8 LEU CG C 27.400 . 1 90 . 8 LEU HG H 1.790 . 1 91 . 8 LEU CD1 C 23.400 . . 92 . 8 LEU HD1 H 0.927 . . 93 . 8 LEU CD2 C 25.780 . . 94 . 8 LEU HD2 H 0.998 . . 95 . 9 GLU N N 120.478 . 1 96 . 9 GLU H H 8.576 . 1 97 . 9 GLU CA C 60.740 . 1 98 . 9 GLU HA H 3.704 . 1 99 . 9 GLU CB C 29.689 . 1 100 . 9 GLU HB2 H 2.314 . . 101 . 9 GLU HB3 H 2.010 . . 102 . 9 GLU CG C 37.222 . 1 103 . 9 GLU HG2 H 2.484 . . 104 . 9 GLU HG3 H 2.109 . . 105 . 10 LEU N N 118.323 . 1 106 . 10 LEU H H 7.853 . 1 107 . 10 LEU CA C 57.916 . 1 108 . 10 LEU HA H 4.016 . 1 109 . 10 LEU CB C 41.507 . 1 110 . 10 LEU HB2 H 1.840 . . 111 . 10 LEU HB3 H 1.575 . . 112 . 10 LEU CG C 27.036 . 1 113 . 10 LEU HG H 1.780 . 1 114 . 10 LEU CD1 C 23.325 . . 115 . 10 LEU HD1 H 0.880 . . 116 . 10 LEU CD2 C 24.978 . . 117 . 10 LEU HD2 H 0.895 . . 118 . 11 LEU N N 122.227 . 1 119 . 11 LEU H H 7.923 . 1 120 . 11 LEU CA C 58.016 . 1 121 . 11 LEU HA H 4.111 . 1 122 . 11 LEU CB C 42.006 . 1 123 . 11 LEU HB2 H 1.969 . . 124 . 11 LEU HB3 H 1.825 . . 125 . 11 LEU CG C 27.050 . 1 126 . 11 LEU HG H 1.608 . 1 127 . 11 LEU CD1 C 24.800 . . 128 . 11 LEU HD1 H 0.910 . . 129 . 11 LEU CD2 C 24.500 . . 130 . 11 LEU HD2 H 0.936 . . 131 . 12 LEU N N 119.314 . 1 132 . 12 LEU H H 8.299 . 1 133 . 12 LEU CA C 57.935 . 1 134 . 12 LEU HA H 3.933 . 1 135 . 12 LEU CB C 41.655 . 1 136 . 12 LEU HB2 H 2.060 . . 137 . 12 LEU HB3 H 1.440 . . 138 . 12 LEU CG C 26.506 . 1 139 . 12 LEU HG H 2.052 . 1 140 . 12 LEU CD1 C 22.038 . . 141 . 12 LEU HD1 H 0.764 . . 142 . 12 LEU CD2 C 27.021 . . 143 . 12 LEU HD2 H 0.920 . . 144 . 13 MET N N 119.941 . 1 145 . 13 MET H H 8.483 . 1 146 . 13 MET CA C 59.082 . 1 147 . 13 MET HA H 3.593 . 1 148 . 13 MET CB C 32.865 . 1 149 . 13 MET HB2 H 1.820 . . 150 . 13 MET HB3 H 1.745 . . 151 . 13 MET CG C 31.989 . 1 152 . 13 MET HG3 H 2.225 . . 153 . 13 MET CE C 17.123 . 1 154 . 13 MET HE H 1.993 . . 155 . 14 SER N N 115.196 . 1 156 . 14 SER H H 7.958 . 1 157 . 14 SER CA C 61.053 . 1 158 . 14 SER HA H 4.314 . 1 159 . 14 SER CB C 63.001 . 1 160 . 14 SER HB3 H 4.057 . . 161 . 15 THR N N 118.059 . 1 162 . 15 THR H H 7.806 . 1 163 . 15 THR CA C 65.312 . 1 164 . 15 THR HA H 4.065 . 1 165 . 15 THR CB C 68.706 . 1 166 . 15 THR HB H 4.213 . 1 167 . 15 THR CG2 C 22.614 . 1 168 . 15 THR HG2 H 1.317 . . 169 . 16 GLU N N 118.684 . 1 170 . 16 GLU H H 7.915 . 1 171 . 16 GLU CA C 59.433 . 1 172 . 16 GLU HA H 3.975 . 1 173 . 16 GLU CB C 29.500 . 1 174 . 16 GLU HB2 H 2.236 . . 175 . 16 GLU HB3 H 2.090 . . 176 . 16 GLU CG C 36.700 . 1 177 . 16 GLU HG2 H 2.695 . . 178 . 16 GLU HG3 H 2.430 . . 179 . 17 ASN N N 116.423 . 1 180 . 17 ASN H H 7.823 . 1 181 . 17 ASN CA C 54.594 . 1 182 . 17 ASN HA H 4.650 . 1 183 . 17 ASN CB C 38.451 . 1 184 . 17 ASN HB2 H 2.895 . . 185 . 17 ASN HB3 H 2.935 . . 186 . 17 ASN ND2 N 112.900 . 1 187 . 17 ASN HD21 H 7.650 . . 188 . 17 ASN HD22 H 6.970 . . 189 . 18 GLU N N 119.930 . 1 190 . 18 GLU H H 7.881 . 1 191 . 18 GLU CA C 57.395 . 1 192 . 18 GLU HA H 4.225 . 1 193 . 18 GLU CB C 29.600 . 1 194 . 18 GLU HB3 H 2.140 . . 195 . 18 GLU CG C 36.000 . 1 196 . 18 GLU HG2 H 2.380 . . 197 . 19 LEU N N 119.313 . 1 198 . 19 LEU H H 7.595 . 1 199 . 19 LEU CA C 55.473 . 1 200 . 19 LEU HA H 4.200 . 1 201 . 19 LEU CB C 41.565 . 1 202 . 19 LEU HB2 H 1.670 . . 203 . 19 LEU HB3 H 1.610 . . 204 . 19 LEU CG C 26.722 . 1 205 . 19 LEU HG H 1.656 . 1 206 . 19 LEU CD1 C 22.500 . . 207 . 19 LEU HD1 H 0.470 . . 208 . 19 LEU CD2 C 25.220 . . 209 . 19 LEU HD2 H 0.732 . . 210 . 20 LYS N N 119.969 . 1 211 . 20 LYS H H 7.838 . 1 212 . 20 LYS CA C 56.808 . 1 213 . 20 LYS HA H 4.300 . 1 214 . 20 LYS CB C 32.900 . 1 215 . 20 LYS HB2 H 1.920 . . 216 . 20 LYS HB3 H 1.860 . . 217 . 20 LYS CG C 24.910 . 1 218 . 20 LYS HG2 H 1.551 . . 219 . 20 LYS HG3 H 1.472 . . 220 . 20 LYS CD C 29.015 . 1 221 . 20 LYS HD3 H 1.725 . . 222 . 20 LYS CE C 42.000 . 1 223 . 20 LYS HE3 H 3.020 . . 224 . 21 GLY N N 108.729 . 1 225 . 21 GLY H H 8.205 . 1 226 . 21 GLY CA C 45.384 . 1 227 . 21 GLY HA3 H 3.980 . . 228 . 22 GLN N N 119.656 . 1 229 . 22 GLN H H 8.135 . 1 230 . 22 GLN CA C 55.800 . 1 231 . 22 GLN HA H 4.350 . 1 232 . 22 GLN CB C 29.504 . 1 233 . 22 GLN HB2 H 2.150 . . 234 . 22 GLN HB3 H 2.013 . . 235 . 22 GLN CG C 33.819 . 1 236 . 22 GLN HG3 H 2.377 . . 237 . 22 GLN NE2 N 111.850 . 1 238 . 22 GLN HE21 H 7.540 . . 239 . 22 GLN HE22 H 6.850 . . 240 . 23 GLN N N 121.236 . 1 241 . 23 GLN H H 8.353 . 1 242 . 23 GLN CA C 55.700 . 1 243 . 23 GLN HA H 4.330 . 1 244 . 23 GLN CB C 29.600 . 1 245 . 23 GLN HB2 H 2.130 . . 246 . 23 GLN HB3 H 2.010 . . 247 . 23 GLN CG C 33.821 . 1 248 . 23 GLN HG3 H 2.380 . . 249 . 23 GLN NE2 N 112.500 . 1 250 . 23 GLN HE21 H 7.540 . . 251 . 23 GLN HE22 H 6.850 . . 252 . 24 ALA N N 126.070 . 1 253 . 24 ALA H H 8.282 . 1 254 . 24 ALA CA C 52.263 . 1 255 . 24 ALA HA H 4.360 . 1 256 . 24 ALA CB C 19.172 . 1 257 . 24 ALA HB H 1.386 . 1 258 . 25 LEU N N 127.568 . 1 259 . 25 LEU H H 7.822 . 1 260 . 25 LEU CA C 56.551 . 1 261 . 25 LEU HA H 4.182 . 1 262 . 25 LEU CB C 43.410 . 1 263 . 25 LEU HB3 H 1.586 . . 264 . 25 LEU CG C 27.251 . 1 265 . 25 LEU HG H 1.609 . 1 266 . 25 LEU CD1 C 23.613 . . 267 . 25 LEU HD1 H 0.865 . . 268 . 25 LEU CD2 C 25.274 . . 269 . 25 LEU HD2 H 0.903 . . stop_ save_