data_18063
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
NH chemical shift Assignments for AbpSH3 bound to mutant ArkA peptide (L(-7)A)
;
_BMRB_accession_number 18063
_BMRB_flat_file_name bmr18063.str
_Entry_type original
_Submission_date 2011-11-13
_Accession_date 2011-11-13
_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 Stollar Elliott J. .
2 Forman-Kay Julie D. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 64
"15N chemical shifts" 64
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2013-01-04 original author .
stop_
loop_
_Related_BMRB_accession_number
_Relationship
18054 'monomer (free AbpSH3)'
18055 AbpSH3-ArkA
18056 AbpSH3-ArkB
18057 AbpSH3-ArkA_H(-6)A
18058 AbpSH3-ArkA_SI
18059 AbpSH3-ArkA_K(-3)A
18060 AbpSH3-ArkA_K(-3)R
18061 AbpSH3-ArkA_K(-3)V
18062 AbpSH3-ArkA_K(3)A
18064 AbpSH3-ArkA_L(-7)V
18065 AbpSH3-ArkA12
18066 AbpSH3-ArkA_P(-4)A
18067 AbpSH3-ArkA_P(2)A
18068 AbpSH3-ArkA_P(2)V
18069 AbpSH3-ArkA_P(0)A
18070 AbpSH3-ArkA_P(-1)A
18071 AbpSH3-Prk17
18072 AbpSH3-ArkA15_H(-6)A_K(-8)A
18073 AbpSH3-PRR
18074 AbpSH3-Scp12
18075 AbpSH3-Scp17
18076 AbpSH3-Sjl17
18077 AbpSH3-Srv12
18078 AbpSH3-Srv17
stop_
_Original_release_date 2013-01-04
save_
#############################
# Citation for this entry #
#############################
save_Cite_1
_Saveframe_category entry_citation
_Citation_full .
_Citation_title 'Differential Dynamic Engagement within 24 SH3 Domain: Peptide Complexes Revealed by Co-Linear Chemical Shift Perturbation Analysis.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 23251481
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Stollar Elliott J. .
2 Lin Hong . .
3 Davidson Alan R. .
4 Forman-Kay Julie D. .
stop_
_Journal_abbreviation 'PLoS ONE'
_Journal_name_full 'PloS one'
_Journal_volume 7
_Journal_issue 12
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first e51282
_Page_last e51282
_Year 2012
_Details .
loop_
_Keyword
'Protein dynamics'
'Multi-state exchange'
'peptide flexibility'
'domain:peptide ensemble'
'local binding'
stop_
save_
##################################
# Molecular system description #
##################################
save_assembly
_Saveframe_category molecular_system
_Mol_system_name AbpSH3-ArkA_L(-7)A
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
AbpSH3 $AbpSH3
ArkA_L(-7)A $ArkA_L(-7)A
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state ?
_System_paramagnetic no
_System_thiol_state .
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_AbpSH3
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common AbpSH3
_Molecular_mass .
_Mol_thiol_state 'not present'
loop_
_Biological_function
'modular interaction domain'
stop_
_Details 'Abp1p SH3 domain from S.Cerevisiae'
##############################
# Polymer residue sequence #
##############################
_Residue_count 59
_Mol_residue_sequence
;
APWATAEYDYDAAEDNELTF
VENDKIINIEFVDDDWWLGE
LEKDGSKGLFPSNYVSLGN
;
loop_
_Residue_seq_code
_Residue_label
1 ALA 2 PRO 3 TRP 4 ALA 5 THR
6 ALA 7 GLU 8 TYR 9 ASP 10 TYR
11 ASP 12 ALA 13 ALA 14 GLU 15 ASP
16 ASN 17 GLU 18 LEU 19 THR 20 PHE
21 VAL 22 GLU 23 ASN 24 ASP 25 LYS
26 ILE 27 ILE 28 ASN 29 ILE 30 GLU
31 PHE 32 VAL 33 ASP 34 ASP 35 ASP
36 TRP 37 TRP 38 LEU 39 GLY 40 GLU
41 LEU 42 GLU 43 LYS 44 ASP 45 GLY
46 SER 47 LYS 48 GLY 49 LEU 50 PHE
51 PRO 52 SER 53 ASN 54 TYR 55 VAL
56 SER 57 LEU 58 GLY 59 ASN
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-09-30
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 16843 Abp1p 100.00 62 100.00 100.00 5.72e-33
BMRB 18054 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18055 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18056 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18057 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18058 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18059 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18060 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18061 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18062 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18064 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18065 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18066 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18067 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18068 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18069 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18070 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18071 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18072 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18073 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18074 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18075 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18076 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18077 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 18078 AbpSH3 100.00 59 100.00 100.00 8.58e-33
BMRB 25354 Abp1p_SH3 100.00 62 100.00 100.00 5.72e-33
BMRB 26519 Abp1p 100.00 59 100.00 100.00 8.58e-33
PDB 1JO8 "Structural Analysis Of The Yeast Actin Binding Protein Abp1 Sh3 Domain" 98.31 58 100.00 100.00 3.51e-32
PDB 2K3B "Seeing The Invisible: Structures Of Excited Protein States By Relaxation Dispersion Nmr" 100.00 62 100.00 100.00 5.72e-33
PDB 2RPN "A Crucial Role For High Intrinsic Specificity In The Function Of Yeast Sh3 Domains" 100.00 59 100.00 100.00 8.58e-33
DBJ GAA21988 "K7_Abp1p [Saccharomyces cerevisiae Kyokai no. 7]" 98.31 592 100.00 100.00 6.83e-32
EMBL CAA36075 "unnamed protein product [Saccharomyces cerevisiae]" 98.31 592 100.00 100.00 7.41e-32
EMBL CAA42253 "actin-binding protein [Saccharomyces cerevisiae]" 98.31 592 100.00 100.00 7.80e-32
EMBL CAY78291 "Abp1p [Saccharomyces cerevisiae EC1118]" 98.31 592 100.00 100.00 6.63e-32
GB AHN96147 "ABP1 [synthetic construct]" 98.31 592 100.00 100.00 7.80e-32
GB AHV79349 "ABP1 [synthetic construct]" 98.31 592 100.00 100.00 7.80e-32
GB AHY79755 "Abp1p [Saccharomyces cerevisiae YJM993]" 98.31 592 100.00 100.00 6.83e-32
GB AJP37506 "Abp1p [Saccharomyces cerevisiae YJM1078]" 98.31 592 100.00 100.00 6.83e-32
GB AJQ31991 "Abp1p [Saccharomyces cerevisiae YJM1356]" 98.31 592 100.00 100.00 7.26e-32
PRF 1603360A "actin binding protein" 98.31 592 100.00 100.00 7.57e-32
REF NP_010012 "Abp1p [Saccharomyces cerevisiae S288c]" 98.31 592 100.00 100.00 7.80e-32
SP P15891 "RecName: Full=Actin-binding protein" 98.31 592 100.00 100.00 7.80e-32
TPG DAA07557 "TPA: Abp1p [Saccharomyces cerevisiae S288c]" 98.31 592 100.00 100.00 7.80e-32
stop_
save_
save_ArkA_L(-7)A
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common ArkA_L(-7)A
_Molecular_mass .
_Mol_thiol_state 'not present'
_Details 'Sequence from Ark1p from S.Cerevisiae'
_Residue_count 17
_Mol_residue_sequence KKTKPTPPPKPSHAKPK
loop_
_Residue_seq_code
_Residue_label
1 LYS 2 LYS 3 THR 4 LYS 5 PRO
6 THR 7 PRO 8 PRO 9 PRO 10 LYS
11 PRO 12 SER 13 HIS 14 ALA 15 LYS
16 PRO 17 LYS
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date .
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$AbpSH3 'baker's yeast' 4932 Eukaryota Fungi Saccharomyces cerevisiae
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
$ArkA_L(-7)A 'chemical synthesis' . . . . .
$AbpSH3 'recombinant technology' . . . BL21* .
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_AbpSH3-ArkA_L(-7)A
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$AbpSH3 1900 uM '[U-100% 15N]'
'sodium phosphate' 50 mM 'natural abundance'
'sodium chloride' 100 mM 'natural abundance'
D2O 10 % 'natural abundance'
H2O 90 % 'natural abundance'
$ArkA_L(-7)A 4000 uM 'natural abundance'
stop_
save_
############################
# Computer software used #
############################
save_NMRPipe
_Saveframe_category software
_Name NMRPipe
_Version .
loop_
_Vendor
_Address
_Electronic_address
'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . .
'Johnson, One Moon Scientific' . .
Goddard . .
stop_
loop_
_Task
'data analysis'
'chemical shift assignment'
stop_
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model Unity
_Field_strength 500
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_2D_1H-15N_HSQC_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-15N HSQC'
_Sample_label $AbpSH3-ArkA_L(-7)A
save_
#######################
# Sample conditions #
#######################
save_sample_conditions_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
temperature 303 . K
pH 7 . pH
pressure 1 . atm
'ionic strength' 0.189 . M
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference_1
_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
water H 1 protons ppm 4.77 internal direct . . . 1.0
urea N 15 nitrogen ppm 110 na direct . . . 1.0
stop_
save_
###################################
# Assigned chemical shift lists #
###################################
###################################################################
# Chemical Shift Ambiguity Index Value Definitions #
# #
# The values other than 1 are used for those atoms with different #
# chemical shifts that cannot be assigned to stereospecific atoms #
# or to specific residues or chains. #
# #
# Index Value Definition #
# #
# 1 Unique (including isolated methyl protons, #
# geminal atoms, and geminal methyl #
# groups with identical chemical shifts) #
# (e.g. ILE HD11, HD12, HD13 protons) #
# 2 Ambiguity of geminal atoms or geminal methyl #
# proton groups (e.g. ASP HB2 and HB3 #
# protons, LEU CD1 and CD2 carbons, or #
# LEU HD11, HD12, HD13 and HD21, HD22, #
# HD23 methyl protons) #
# 3 Aromatic atoms on opposite sides of #
# symmetrical rings (e.g. TYR HE1 and HE2 #
# protons) #
# 4 Intraresidue ambiguities (e.g. LYS HG and #
# HD protons or TRP HZ2 and HZ3 protons) #
# 5 Interresidue ambiguities (LYS 12 vs. LYS 27) #
# 6 Intermolecular ambiguities (e.g. ASP 31 CA #
# in monomer 1 and ASP 31 CA in monomer 2 #
# of an asymmetrical homodimer, duplex #
# DNA assignments, or other assignments #
# that may apply to atoms in one or more #
# molecule in the molecular assembly) #
# 9 Ambiguous, specific ambiguity not defined #
# #
###################################################################
save_assigned_chem_shift_list_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'2D 1H-15N HSQC'
stop_
loop_
_Sample_label
$AbpSH3-ArkA_L(-7)A
stop_
_Sample_conditions_label $sample_conditions_1
_Chem_shift_reference_set_label $chemical_shift_reference_1
_Mol_system_component_name AbpSH3
_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 1 ALA H H 8.452 . 1
2 1 1 ALA N N 127.586 . 1
3 3 3 TRP H H 7.922 . 1
4 3 3 TRP HE1 H 10.210 . 1
5 3 3 TRP N N 116.843 . 1
6 3 3 TRP NE1 N 130.270 . 1
7 4 4 ALA H H 10.116 . 1
8 4 4 ALA N N 121.114 . 1
9 5 5 THR H H 8.285 . 1
10 5 5 THR N N 113.626 . 1
11 6 6 ALA H H 8.971 . 1
12 6 6 ALA N N 127.916 . 1
13 7 7 GLU H H 9.470 . 1
14 7 7 GLU N N 125.711 . 1
15 8 8 TYR H H 7.479 . 1
16 8 8 TYR N N 113.734 . 1
17 9 9 ASP H H 8.673 . 1
18 9 9 ASP N N 119.166 . 1
19 10 10 TYR H H 8.243 . 1
20 10 10 TYR N N 121.730 . 1
21 11 11 ASP H H 7.188 . 1
22 11 11 ASP N N 126.222 . 1
23 12 12 ALA H H 7.784 . 1
24 12 12 ALA N N 124.263 . 1
25 13 13 ALA H H 9.019 . 1
26 13 13 ALA N N 126.206 . 1
27 14 14 GLU H H 7.109 . 1
28 14 14 GLU N N 114.084 . 1
29 15 15 ASP H H 8.859 . 1
30 15 15 ASP N N 119.922 . 1
31 16 16 ASN H H 7.680 . 1
32 16 16 ASN HD21 H 6.805 . 2
33 16 16 ASN N N 114.426 . 1
34 16 16 ASN ND2 N 110.378 . 1
35 17 17 GLU H H 7.629 . 1
36 17 17 GLU N N 118.822 . 1
37 18 18 LEU H H 8.707 . 1
38 18 18 LEU N N 122.881 . 1
39 19 19 THR H H 7.421 . 1
40 19 19 THR N N 114.986 . 1
41 20 20 PHE H H 9.076 . 1
42 20 20 PHE N N 120.730 . 1
43 21 21 VAL H H 9.282 . 1
44 21 21 VAL N N 117.266 . 1
45 22 22 GLU H H 8.856 . 1
46 22 22 GLU N N 121.103 . 1
47 23 23 ASN H H 8.929 . 1
48 23 23 ASN HD21 H 7.014 . 2
49 23 23 ASN N N 117.702 . 1
50 23 23 ASN ND2 N 114.252 . 1
51 24 24 ASP H H 8.670 . 1
52 24 24 ASP N N 123.129 . 1
53 25 25 LYS H H 8.256 . 1
54 25 25 LYS N N 120.586 . 1
55 26 26 ILE H H 9.362 . 1
56 26 26 ILE N N 107.537 . 1
57 27 27 ILE H H 9.852 . 1
58 27 27 ILE N N 119.245 . 1
59 28 28 ASN H H 9.135 . 1
60 28 28 ASN HD21 H 7.115 . 2
61 28 28 ASN N N 115.915 . 1
62 28 28 ASN ND2 N 115.743 . 1
63 29 29 ILE H H 7.964 . 1
64 29 29 ILE N N 117.302 . 1
65 30 30 GLU H H 9.265 . 1
66 30 30 GLU N N 125.499 . 1
67 31 31 PHE H H 8.701 . 1
68 31 31 PHE N N 128.153 . 1
69 32 32 VAL H H 7.736 . 1
70 32 32 VAL N N 121.651 . 1
71 33 33 ASP H H 8.384 . 1
72 33 33 ASP N N 119.095 . 1
73 34 34 ASP H H 8.268 . 1
74 34 34 ASP N N 116.405 . 1
75 35 35 ASP H H 8.829 . 1
76 35 35 ASP N N 117.651 . 1
77 36 36 TRP H H 8.196 . 1
78 36 36 TRP HE1 H 9.536 . 1
79 36 36 TRP N N 123.059 . 1
80 36 36 TRP NE1 N 130.016 . 1
81 37 37 TRP H H 8.027 . 1
82 37 37 TRP HE1 H 9.522 . 1
83 37 37 TRP N N 121.308 . 1
84 37 37 TRP NE1 N 128.455 . 1
85 38 38 LEU H H 8.553 . 1
86 38 38 LEU N N 121.399 . 1
87 39 39 GLY H H 8.799 . 1
88 39 39 GLY N N 109.537 . 1
89 40 40 GLU H H 8.574 . 1
90 40 40 GLU N N 120.341 . 1
91 41 41 LEU H H 9.567 . 1
92 41 41 LEU N N 126.557 . 1
93 42 42 GLU H H 8.228 . 1
94 42 42 GLU N N 129.781 . 1
95 43 43 LYS H H 9.373 . 1
96 43 43 LYS N N 113.969 . 1
97 44 44 ASP H H 6.806 . 1
98 44 44 ASP N N 114.548 . 1
99 45 45 GLY H H 8.408 . 1
100 45 45 GLY N N 110.072 . 1
101 46 46 SER H H 8.713 . 1
102 46 46 SER N N 118.550 . 1
103 47 47 LYS H H 8.468 . 1
104 47 47 LYS N N 119.545 . 1
105 48 48 GLY H H 8.705 . 1
106 48 48 GLY N N 108.798 . 1
107 49 49 LEU H H 9.045 . 1
108 49 49 LEU N N 120.448 . 1
109 50 50 PHE H H 9.324 . 1
110 50 50 PHE N N 115.976 . 1
111 52 52 SER H H 7.906 . 1
112 52 52 SER N N 121.774 . 1
113 53 53 ASN H H 8.050 . 1
114 53 53 ASN N N 116.422 . 1
115 54 54 TYR H H 7.837 . 1
116 54 54 TYR N N 119.552 . 1
117 55 55 VAL H H 7.441 . 1
118 55 55 VAL N N 109.544 . 1
119 56 56 SER H H 8.610 . 1
120 56 56 SER N N 114.178 . 1
121 57 57 LEU H H 9.303 . 1
122 57 57 LEU N N 129.833 . 1
123 58 58 GLY H H 8.586 . 1
124 58 58 GLY N N 112.192 . 1
125 59 59 ASN H H 7.525 . 1
126 59 59 ASN HD21 H 6.738 . 2
127 59 59 ASN N N 123.795 . 1
128 59 59 ASN ND2 N 112.014 . 1
stop_
save_