data_5183
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
BetaCore, a designed water soluble four-stranded antiparallel b-sheet protein
;
_BMRB_accession_number 5183
_BMRB_flat_file_name bmr5183.str
_Entry_type original
_Submission_date 2001-10-18
_Accession_date 2001-10-18
_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 Carulla Natalia . .
2 Woodward Clare . .
3 Barany George . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 2
coupling_constants 2
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 236
"15N chemical shifts" 17
"coupling constants" 17
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2008-07-16 update BMRB 'Updating non-standard residue'
stop_
_Original_release_date 2001-10-18
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
BetaCore, a Designed Water Soluble Four-stranded Antiparallel Beta-sheet Protein
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 22016650
_PubMed_ID 12021452
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Carulla Natalia . .
2 Woodward Clare . .
3 Barany George . .
stop_
_Journal_abbreviation 'Protein Sci.'
_Journal_volume 11
_Journal_issue 6
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 1539
_Page_last 1551
_Year 2002
_Details .
save_
#######################################
# Cited references within the entry #
#######################################
save_ref_1
_Saveframe_category citation
_Citation_full
;
Carulla, N.; Woodward, C.; Barany, G.
Synthesis and Characterization of a b-Hairpin Peptide That
Represents a 'Core Module' of Bovine Pancreatic Trypsin
Inhibitor (BPTI).
Biochemistry, 39, 7927-7937 (2000).
;
_Citation_title
;
Synthesis and characterization of a beta-hairpin peptide that represents a 'core module' of bovine pancreatic trypsin inhibitor (BPTI).
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 10891073
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Carulla N. . .
2 Woodward C. . .
3 Barany G. . .
stop_
_Journal_abbreviation Biochemistry
_Journal_name_full Biochemistry
_Journal_volume 39
_Journal_issue 27
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 7927
_Page_last 7937
_Year 2000
_Details
;
A new strategy for the design and construction of peptide fragments that can
achieve defined, nativelike secondary structure is presented. The strategy is
based upon the hypothesis that 'core elements' of a protein, synthesized in a
single polypeptide molecule, will favor nativelike structure, and that by
incorporating a cross-link, nativelike core structure will dominate the
ensemble as the more extended conformations are excluded. 'Core elements' are
the elements of packed secondary structure that contain the slowest exchanging
backbone amide protons in the native protein. The 'core elements' in bovine
pancreatic trypsin inhibitor (BPTI) are the two long strands of antiparallel
beta-sheet (residues 18-24 and 29-35) and the small beta-bridge (residues
43-44). To test the design strategy, we synthesized an 'oxidized core module',
which contains the antiparallel strands connected by a modified reverse turn
(A27 replaced by D), a natural disulfide cross-link at the open end of the
hairpin, and N- and C-termini blocking groups. A peptide with identical
sequence but lacking the disulfide cross-link at the open end was used as the
'reduced core module' control. The conformational behavior of both peptides was
examined using (1)H NMR spectroscopy. Chemical shift dispersion, chemical shift
deviation from random coil values, sequential and long-range NOEs, and H/D
amide exchange rates were compared for the two peptides. We conclude that the
ensemble of oxidized and reduced core module conformations samples both
nativelike 4:4 and non-native 3:5 beta-hairpin structure, and that the oxidized
module samples nativelike structure for a greater fraction of the time than the
reduced module.
;
save_
save_ref_2
_Saveframe_category citation
_Citation_full
;
Carulla, N.; Woodward, C.; Barany, G.
Toward New Designed Proteins Derived from Bovine Pancreatic
Trypsin Inhibitor (BPTI): Covalent Cross-Linking of Two
'Core Modules' by Oxime-Forming Ligation.
Bioconjugate Chemistry, 12, 726-741 (2001).
;
_Citation_title
;
Toward new designed proteins derived from bovine pancreatic trypsin inhibitor (BPTI): covalent cross-linking of two 'core modules' by oxime-forming ligation.
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 11562191
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Carulla N. . .
2 Woodward C. . .
3 Barany G. . .
stop_
_Journal_abbreviation 'Bioconjug. Chem.'
_Journal_name_full 'Bioconjugate chemistry'
_Journal_volume 12
_Journal_issue 5
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 726
_Page_last 741
_Year .
_Details
;
A 25-residue disulfide-cross-linked peptide, termed 'oxidized core module'
(OxCM), that includes essentially all of the secondary structural elements of
bovine pancreatic trypsin inhibitor (BPTI) most refractory to hydrogen
exchange, was shown previously to favor nativelike beta-sheet structure
[Carulla, N., Woodward, C., and Barany, G. (2000) Synthesis and
Characterization of a beta-Hairpin Peptide That Represents a 'Core Module' of
Bovine Pancreatic Trypsin Inhibitor (BPTI). Biochemistry 39, 7927-7937]. The
present work prepares to explore the hypothesis that the energies of nativelike
conformations, relative to other possible conformations, could be decreased
further by covalent linkage of two OxCMs. Optimized syntheses of six
approximately 50-residue OxCM dimers are reported herein, featuring appropriate
monomer modifications followed by oxime-forming ligation chemistry to create
covalent cross-links at various positions and with differing lengths. Several
side reactions were recognized through this work, and modified procedures to
lessen or mitigate their occurrence were developed. Particularly noteworthy,
guanidine or urea denaturants that were included as peptide-solubilizing
components for some reaction mixtures were proven to form adducts with
glyoxylyl moieties, thus affecting rates and outcomes. All six synthetic OxCM
dimers were characterized by 1D (1)H NMR; three of them showed considerable
chemical shift dispersion suggestive of self-association and mutual
stabilization between the monomer units.
;
save_
##################################
# Molecular system description #
##################################
save_system_BetaCore
_Saveframe_category molecular_system
_Mol_system_name BetaCore
_Abbreviation_common BetaCore
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'core module I' $CM_I
'core module II' $CM_II
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state dimer
_System_paramagnetic no
_System_thiol_state 'all disulfide bound'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_CM_I
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common BetaCore
_Abbreviation_common BetaCore
_Molecular_mass .
_Mol_thiol_state 'all disulfide bound'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 26
_Mol_residue_sequence
;
XKAXIIRYFYNAKDGLXQTF
VYGGCX
;
loop_
_Residue_seq_code
_Residue_label
1 MPT 2 LYS 3 ALA 4 CLG 5 ILE
6 ILE 7 ARG 8 TYR 9 PHE 10 TYR
11 ASN 12 ALA 13 LYS 14 ASP 15 GLY
16 LEU 17 ABA 18 GLN 19 THR 20 PHE
21 VAL 22 TYR 23 GLY 24 GLY 25 CYS
26 NH2
stop_
_Sequence_homology_query_date 2008-03-24
_Sequence_homology_query_revised_last_date 2008-02-11
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 1K09 'A Chain A, Solution Structure Of Betacore,A Designed Water Soluble Four-Stranded AntiparallelB-Sheet Protein' 100.00 25 100 100 4e-04
stop_
save_
save_CM_II
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common BetaCore
_Abbreviation_common BetaCore
_Molecular_mass .
_Mol_thiol_state 'all disulfide bound'
_Details .
_Residue_count 26
_Mol_residue_sequence
;
XKARIIRYFYNAKDGXXQTF
VYGGCX
;
loop_
_Residue_seq_code
_Residue_label
1 MPT 2 LYS 3 ALA 4 ARG 5 ILE
6 ILE 7 ARG 8 TYR 9 PHE 10 TYR
11 ASN 12 ALA 13 LYS 14 ASP 15 GLY
16 CLH 17 ABA 18 GLN 19 THR 20 PHE
21 VAL 22 TYR 23 GLY 24 GLY 25 CYS
26 NH2
stop_
_Sequence_homology_query_date 2008-03-24
_Sequence_homology_query_revised_last_date 2007-11-12
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 1K09 'B Chain B, Solution Structure Of Betacore,A Designed Water Soluble Four-Stranded AntiparallelB-Sheet Protein' 100.00 25 100 100 3e-04
stop_
save_
######################
# Polymer residues #
######################
save_chem_comp_CLG
_Saveframe_category polymer_residue
_Mol_type 'L-peptide linking'
_Name_common '2-AMINO-6-[2-(2-AMINOOXY-ACETYLAMINO)-ACETYLAMINO]-HEXANOIC ACID'
_BMRB_code .
_PDB_code CLG
_Standard_residue_derivative .
_Molecular_mass 276.290
_Mol_paramagnetic .
_Details
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Thu Jul 21 13:23:42 2011
;
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
N N N . 0 . ?
CA CA C . 0 . ?
CB CB C . 0 . ?
CG CG C . 0 . ?
CD CD C . 0 . ?
CE CE C . 0 . ?
NZ NZ N . 0 . ?
CH CH C . 0 . ?
OI OI O . 0 . ?
CI CI C . 0 . ?
NJ NJ N . 0 . ?
CK CK C . 0 . ?
OL OL O . 0 . ?
C C C . 0 . ?
O O O . 0 . ?
CL CL C . 0 . ?
OM OM O . 0 . ?
NM NM N . 0 . ?
OXT OXT O . 0 . ?
H H H . 0 . ?
H2 H2 H . 0 . ?
HA HA H . 0 . ?
HB2 HB2 H . 0 . ?
HB3 HB3 H . 0 . ?
HG2 HG2 H . 0 . ?
HG3 HG3 H . 0 . ?
HD2 HD2 H . 0 . ?
HD3 HD3 H . 0 . ?
HE2 HE2 H . 0 . ?
HE3 HE3 H . 0 . ?
HZ HZ H . 0 . ?
HI1 HI1 H . 0 . ?
HI2 HI2 H . 0 . ?
HNJ HNJ H . 0 . ?
HL1 HL1 H . 0 . ?
HL2 HL2 H . 0 . ?
HNM1 HNM1 H . 0 . ?
HNM2 HNM2 H . 0 . ?
HXT HXT H . 0 . ?
stop_
loop_
_Bond_order
_Bond_atom_one_atom_name
_Bond_atom_two_atom_name
_PDB_bond_atom_one_atom_name
_PDB_bond_atom_two_atom_name
SING N CA ? ?
SING N H ? ?
SING N H2 ? ?
SING CA CB ? ?
SING CA C ? ?
SING CA HA ? ?
SING CB CG ? ?
SING CB HB2 ? ?
SING CB HB3 ? ?
SING CG CD ? ?
SING CG HG2 ? ?
SING CG HG3 ? ?
SING CD CE ? ?
SING CD HD2 ? ?
SING CD HD3 ? ?
SING CE NZ ? ?
SING CE HE2 ? ?
SING CE HE3 ? ?
SING NZ CH ? ?
SING NZ HZ ? ?
DOUB CH OI ? ?
SING CH CI ? ?
SING CI NJ ? ?
SING CI HI1 ? ?
SING CI HI2 ? ?
SING NJ CK ? ?
SING NJ HNJ ? ?
DOUB CK OL ? ?
SING CK CL ? ?
DOUB C O ? ?
SING C OXT ? ?
SING CL OM ? ?
SING CL HL1 ? ?
SING CL HL2 ? ?
SING OM NM ? ?
SING NM HNM1 ? ?
SING NM HNM2 ? ?
SING OXT HXT ? ?
stop_
save_
save_chem_comp_CLH
_Saveframe_category polymer_residue
_Mol_type 'L-peptide linking'
_Name_common '2-AMINO-6-[2-(2-OXO-ACETYLAMINO)-ACETYLAMINO]-HEXANOIC ACID'
_BMRB_code .
_PDB_code CLH
_Standard_residue_derivative .
_Molecular_mass 259.259
_Mol_paramagnetic .
_Details
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Thu Jul 21 13:26:03 2011
;
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
N N N . 0 . ?
CA CA C . 0 . ?
CB CB C . 0 . ?
CG CG C . 0 . ?
CD CD C . 0 . ?
CE CE C . 0 . ?
NZ NZ N . 0 . ?
CH CH C . 0 . ?
OI OI O . 0 . ?
CI CI C . 0 . ?
NJ NJ N . 0 . ?
CK CK C . 0 . ?
OL OL O . 0 . ?
C C C . 0 . ?
O O O . 0 . ?
CL CL C . 0 . ?
OM OM O . 0 . ?
OXT OXT O . 0 . ?
H H H . 0 . ?
H2 H2 H . 0 . ?
HA HA H . 0 . ?
HB2 HB2 H . 0 . ?
HB3 HB3 H . 0 . ?
HG2 HG2 H . 0 . ?
HG3 HG3 H . 0 . ?
HD2 HD2 H . 0 . ?
HD3 HD3 H . 0 . ?
HE2 HE2 H . 0 . ?
HE3 HE3 H . 0 . ?
HZ HZ H . 0 . ?
HI1 HI1 H . 0 . ?
HI2 HI2 H . 0 . ?
HNJ HNJ H . 0 . ?
HL HL H . 0 . ?
HXT HXT H . 0 . ?
stop_
loop_
_Bond_order
_Bond_atom_one_atom_name
_Bond_atom_two_atom_name
_PDB_bond_atom_one_atom_name
_PDB_bond_atom_two_atom_name
SING N CA ? ?
SING N H ? ?
SING N H2 ? ?
SING CA CB ? ?
SING CA C ? ?
SING CA HA ? ?
SING CB CG ? ?
SING CB HB2 ? ?
SING CB HB3 ? ?
SING CG CD ? ?
SING CG HG2 ? ?
SING CG HG3 ? ?
SING CD CE ? ?
SING CD HD2 ? ?
SING CD HD3 ? ?
SING CE NZ ? ?
SING CE HE2 ? ?
SING CE HE3 ? ?
SING NZ CH ? ?
SING NZ HZ ? ?
DOUB CH OI ? ?
SING CH CI ? ?
SING CI NJ ? ?
SING CI HI1 ? ?
SING CI HI2 ? ?
SING NJ CK ? ?
SING NJ HNJ ? ?
DOUB CK OL ? ?
SING CK CL ? ?
DOUB C O ? ?
SING C OXT ? ?
DOUB CL OM ? ?
SING CL HL ? ?
SING OXT HXT ? ?
stop_
save_
save_chem_comp_MPT
_Saveframe_category polymer_residue
_Mol_type non-polymer
_Name_common 'BETA-MERCAPTOPROPIONIC ACID'
_BMRB_code .
_PDB_code MPT
_Standard_residue_derivative .
_Molecular_mass 106.144
_Mol_paramagnetic .
_Details
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Thu Jul 21 13:27:34 2011
;
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
CA CA C . 0 . ?
C C C . 0 . ?
O O O . 0 . ?
CB CB C . 0 . ?
SG SG S . 0 . ?
OXT OXT O . 0 . ?
HA1 HA1 H . 0 . ?
HA2 HA2 H . 0 . ?
HB1 HB1 H . 0 . ?
HB2 HB2 H . 0 . ?
HG HG H . 0 . ?
HXT HXT H . 0 . ?
stop_
loop_
_Bond_order
_Bond_atom_one_atom_name
_Bond_atom_two_atom_name
_PDB_bond_atom_one_atom_name
_PDB_bond_atom_two_atom_name
SING CA C ? ?
SING CA CB ? ?
SING CA HA1 ? ?
SING CA HA2 ? ?
DOUB C O ? ?
SING C OXT ? ?
SING CB SG ? ?
SING CB HB1 ? ?
SING CB HB2 ? ?
SING SG HG ? ?
SING OXT HXT ? ?
stop_
save_
save_chem_comp_ABA
_Saveframe_category polymer_residue
_Mol_type 'L-peptide linking'
_Name_common 'ALPHA-AMINOBUTYRIC ACID'
_BMRB_code .
_PDB_code ABA
_Standard_residue_derivative .
_Molecular_mass 103.120
_Mol_paramagnetic .
_Details
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Thu Jul 21 13:28:44 2011
;
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
N N N . 0 . ?
CA CA C . 0 . ?
C C C . 0 . ?
O O O . 0 . ?
CB CB C . 0 . ?
CG CG C . 0 . ?
OXT OXT O . 0 . ?
H H H . 0 . ?
HN2 HN2 H . 0 . ?
HA HA H . 0 . ?
HB3 HB3 H . 0 . ?
HB2 HB2 H . 0 . ?
HG1 HG1 H . 0 . ?
HG3 HG3 H . 0 . ?
HG2 HG2 H . 0 . ?
HXT HXT H . 0 . ?
stop_
loop_
_Bond_order
_Bond_atom_one_atom_name
_Bond_atom_two_atom_name
_PDB_bond_atom_one_atom_name
_PDB_bond_atom_two_atom_name
SING N CA ? ?
SING N H ? ?
SING N HN2 ? ?
SING CA C ? ?
SING CA CB ? ?
SING CA HA ? ?
DOUB C O ? ?
SING C OXT ? ?
SING CB CG ? ?
SING CB HB3 ? ?
SING CB HB2 ? ?
SING CG HG1 ? ?
SING CG HG3 ? ?
SING CG HG2 ? ?
SING OXT HXT ? ?
stop_
save_
save_chem_comp_NH2
_Saveframe_category polymer_residue
_Mol_type non-polymer
_Name_common 'AMINO GROUP'
_BMRB_code .
_PDB_code NH2
_Standard_residue_derivative .
_Molecular_mass 16.023
_Mol_paramagnetic .
_Details
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Thu Jul 21 10:41:13 2011
;
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
N N N . 0 . ?
HN1 HN1 H . 0 . ?
HN2 HN2 H . 0 . ?
stop_
loop_
_Bond_order
_Bond_atom_one_atom_name
_Bond_atom_two_atom_name
_PDB_bond_atom_one_atom_name
_PDB_bond_atom_two_atom_name
SING N HN1 ? ?
SING N HN2 ? ?
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$CM_I Bull 9913 Eukaryota Metazoa Bos taurus
$CM_II Bull 9913 Eukaryota Metazoa Bos taurus
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
$CM_I 'chemical synthesis' . . . . .
$CM_II 'chemical synthesis' . . . . .
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
$CM_I 0.4 mM '[38% selectively 15N]'
$CM_II 0.4 mM '[38% selectively 15N]'
stop_
save_
############################
# Computer software used #
############################
save_NMRPipe
_Saveframe_category software
_Name NMRPipe
_Version .
_Details .
save_
save_NMRView
_Saveframe_category software
_Name NMRView
_Version .
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model Inova
_Field_strength 600
_Details .
save_
save_NMR_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model Inova
_Field_strength 800
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_1H-1H_NOESY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-1H NOESY'
_Sample_label $sample_1
save_
save_1H-1H_TOCSY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-1H TOCSY'
_Sample_label $sample_1
save_
save_15N-1H_HSQC_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '15N-1H HSQC'
_Sample_label $sample_1
save_
save_15N-1H_HSQC-TOCSY_4
_Saveframe_category NMR_applied_experiment
_Experiment_name '15N-1H HSQC-TOCSY'
_Sample_label $sample_1
save_
save_15N-1H_HSQC-NOESY_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '15N-1H HSQC-NOESY'
_Sample_label $sample_1
save_
#######################
# Sample conditions #
#######################
save_cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 3 0.2 n/a
temperature 288 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 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_chemical_shifts_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'1H-1H NOESY'
'1H-1H TOCSY'
'15N-1H HSQC'
'15N-1H HSQC-TOCSY'
'15N-1H HSQC-NOESY'
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $cond_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'core module I'
_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 LYS H H 8.44 0.02 1
2 . 2 LYS HA H 4.19 0.02 1
3 . 2 LYS HB2 H 1.87 0.02 2
4 . 2 LYS HB3 H 1.79 0.02 2
5 . 2 LYS HG2 H 1.49 0.02 1
6 . 2 LYS HG3 H 1.49 0.02 1
7 . 2 LYS HD2 H 1.69 0.02 1
8 . 2 LYS HD3 H 1.69 0.02 1
9 . 2 LYS HE2 H 2.99 0.02 1
10 . 2 LYS HE3 H 2.99 0.02 1
11 . 3 ALA H H 8.00 0.02 1
12 . 3 ALA HA H 4.34 0.02 1
13 . 3 ALA HB H 1.39 0.02 1
14 . 3 ALA N N 122.01 0.02 1
15 . 4 CLG H H 7.76 0.02 1
16 . 4 CLG HA H 4.68 0.02 1
17 . 4 CLG HB2 H 2.07 0.02 2
18 . 4 CLG HB3 H 1.95 0.02 2
19 . 4 CLG HG2 H 1.47 0.02 1
20 . 4 CLG HG3 H 1.47 0.02 1
21 . 4 CLG HD2 H 1.67 0.02 1
22 . 4 CLG HD3 H 1.67 0.02 1
23 . 4 CLG HE2 H 2.30 0.02 2
24 . 4 CLG HE3 H 2.21 0.02 2
25 . 5 ILE H H 8.68 0.02 1
26 . 5 ILE HA H 4.38 0.02 1
27 . 5 ILE HB H 1.63 0.02 1
28 . 5 ILE HD1 H 0.548 0.02 1
29 . 7 ARG H H 9.34 0.02 1
30 . 7 ARG HA H 4.75 0.02 1
31 . 8 TYR H H 8.13 0.02 1
32 . 8 TYR HA H 5.93 0.02 1
33 . 8 TYR HB2 H 3.13 0.02 2
34 . 8 TYR HB3 H 2.85 0.02 2
35 . 8 TYR HD1 H 6.97 0.02 1
36 . 8 TYR HD2 H 6.97 0.02 1
37 . 8 TYR HE1 H 6.75 0.02 1
38 . 8 TYR HE2 H 6.75 0.02 1
39 . 9 PHE H H 9.28 0.02 1
40 . 9 PHE HA H 4.93 0.02 1
41 . 9 PHE HB2 H 3.30 0.02 2
42 . 9 PHE HB3 H 3.04 0.02 2
43 . 9 PHE HD1 H 7.27 0.02 1
44 . 9 PHE HD2 H 7.27 0.02 1
45 . 9 PHE HE1 H 7.22 0.02 1
46 . 9 PHE HE2 H 7.22 0.02 1
47 . 9 PHE N N 118.41 0.02 1
48 . 10 TYR H H 8.91 0.02 1
49 . 10 TYR HA H 5.11 0.02 1
50 . 10 TYR HB2 H 2.30 0.02 2
51 . 10 TYR HB3 H 2.06 0.02 2
52 . 10 TYR HD1 H 6.59 0.02 1
53 . 10 TYR HD2 H 6.59 0.02 1
54 . 10 TYR HE1 H 6.42 0.02 1
55 . 10 TYR HE2 H 6.42 0.02 1
56 . 11 ASN H H 8.09 0.02 1
57 . 11 ASN HA H 4.65 0.02 1
58 . 11 ASN HB2 H 3.02 0.02 2
59 . 11 ASN HB3 H 2.66 0.02 2
60 . 12 ALA H H 8.5 0.02 1
61 . 12 ALA HA H 3.76 0.02 1
62 . 12 ALA HB H 1.53 0.02 1
63 . 12 ALA N N 126.68 0.02 1
64 . 13 LYS H H 8.14 0.02 1
65 . 13 LYS HA H 4.05 0.02 1
66 . 14 ASP H H 7.27 0.02 1
67 . 14 ASP HA H 4.71 0.02 1
68 . 14 ASP HB2 H 2.68 0.02 2
69 . 14 ASP HB3 H 2.35 0.02 2
70 . 15 GLY H H 7.86 0.02 1
71 . 15 GLY HA2 H 3.50 0.02 2
72 . 15 GLY HA3 H 3.27 0.02 2
73 . 15 GLY N N 110.53 0.02 1
74 . 16 LEU H H 6.96 0.02 1
75 . 16 LEU HA H 5.15 0.02 1
76 . 16 LEU HB2 H 1.5 0.02 1
77 . 16 LEU HB3 H 1.5 0.02 1
78 . 16 LEU HG H 1.18 0.02 1
79 . 16 LEU HD1 H 0.79 0.02 2
80 . 16 LEU HD2 H 0.59 0.02 2
81 . 16 LEU N N 115.9 0.02 1
82 . 17 ABA H H 9.38 0.02 1
83 . 17 ABA HA H 5.24 0.02 1
84 . 17 ABA HB2 H 2.23 0.02 1
85 . 17 ABA HG2 H 1.05 0.02 1
86 . 18 GLN H H 9.29 0.02 1
87 . 18 GLN HA H 5.61 0.02 1
88 . 18 GLN HB2 H 2.04 0.02 2
89 . 18 GLN HB3 H 1.90 0.02 2
90 . 18 GLN HG2 H 2.29 0.02 1
91 . 18 GLN HG3 H 2.29 0.02 1
92 . 19 THR H H 8.99 0.02 1
93 . 19 THR HA H 5.43 0.02 1
94 . 19 THR HB H 4.23 0.02 1
95 . 19 THR HG2 H 1.36 0.02 1
96 . 20 PHE H H 9.77 0.02 1
97 . 20 PHE HA H 5.1 0.02 1
98 . 20 PHE HB2 H 3.03 0.02 2
99 . 20 PHE HB3 H 2.56 0.02 2
100 . 20 PHE HD1 H 7.16 0.02 1
101 . 20 PHE HD2 H 7.16 0.02 1
102 . 20 PHE HE1 H 6.68 0.02 1
103 . 20 PHE HE2 H 6.68 0.02 1
104 . 20 PHE N N 126.38 0.02 1
105 . 21 VAL H H 9.34 0.02 1
106 . 21 VAL HA H 4.75 0.02 1
107 . 21 VAL HB H 2.05 0.02 1
108 . 21 VAL HG1 H 0.88 0.02 1
109 . 21 VAL HG2 H 0.88 0.02 1
110 . 21 VAL N N 123.28 0.02 1
111 . 22 TYR H H 9.57 0.02 1
112 . 22 TYR HA H 4.97 0.02 1
113 . 22 TYR HB2 H 3.16 0.02 2
114 . 22 TYR HB3 H 3.04 0.02 2
115 . 22 TYR HE1 H 7.18 0.02 1
116 . 22 TYR HE2 H 7.18 0.02 1
117 . 23 GLY H H 8.82 0.02 1
118 . 23 GLY HA2 H 4.31 0.02 2
119 . 23 GLY HA3 H 3.98 0.02 2
120 . 23 GLY N N 110.47 0.02 1
121 . 24 GLY H H 8.07 0.02 1
122 . 24 GLY HA2 H 3.97 0.02 1
123 . 24 GLY HA3 H 3.97 0.02 1
124 . 24 GLY N N 106.23 0.02 1
125 . 25 CYS H H 8.49 0.02 1
126 . 25 CYS HA H 4.65 0.02 1
127 . 25 CYS HB2 H 3.23 0.02 2
128 . 25 CYS HB3 H 2.98 0.02 2
stop_
save_
save_chemical_shifts_2
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'1H-1H NOESY'
'1H-1H TOCSY'
'15N-1H HSQC'
'15N-1H HSQC-TOCSY'
'15N-1H HSQC-NOESY'
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $cond_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'core module II'
_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 LYS H H 8.36 0.02 1
2 . 2 LYS HA H 4.19 0.02 1
3 . 3 ALA H H 8.12 0.02 1
4 . 3 ALA HA H 4.34 0.02 1
5 . 3 ALA HB H 1.41 0.02 1
6 . 3 ALA N N 122.37 0.02 1
7 . 4 ARG H H 7.93 0.02 1
8 . 4 ARG HA H 4.62 0.02 1
9 . 4 ARG HB2 H 1.69 0.02 1
10 . 4 ARG HB3 H 1.69 0.02 1
11 . 4 ARG HG2 H 1.59 0.02 2
12 . 4 ARG HG3 H 1.50 0.02 2
13 . 5 ILE H H 8.68 0.02 1
14 . 5 ILE HA H 4.75 0.02 1
15 . 5 ILE HB H 1.78 0.02 1
16 . 5 ILE HG12 H 1.54 0.02 2
17 . 5 ILE HG13 H 0.96 0.02 2
18 . 5 ILE HG2 H 0.65 0.02 1
19 . 6 ILE H H 8.64 0.02 1
20 . 6 ILE HA H 4.7 0.02 1
21 . 6 ILE HG12 H 1.41 0.02 2
22 . 6 ILE HG13 H 0.97 0.02 2
23 . 6 ILE HG2 H 0.36 0.02 1
24 . 7 ARG H H 9.06 0.02 1
25 . 7 ARG HA H 5.33 0.02 1
26 . 7 ARG HB2 H 1.72 0.02 1
27 . 7 ARG HB3 H 1.72 0.02 1
28 . 7 ARG HG2 H 1.44 0.02 1
29 . 7 ARG HG3 H 1.44 0.02 1
30 . 8 TYR H H 8.79 0.02 1
31 . 8 TYR HA H 5.58 0.02 1
32 . 8 TYR HB2 H 3.15 0.02 2
33 . 8 TYR HB3 H 2.90 0.02 2
34 . 8 TYR HD1 H 6.94 0.02 1
35 . 8 TYR HD2 H 6.94 0.02 1
36 . 8 TYR HE1 H 6.51 0.02 1
37 . 8 TYR HE2 H 6.51 0.02 1
38 . 9 PHE H H 9.7 0.02 1
39 . 9 PHE HA H 5.28 0.02 1
40 . 9 PHE HB2 H 3.36 0.02 2
41 . 9 PHE HB3 H 2.97 0.02 2
42 . 9 PHE HD1 H 7.22 0.02 1
43 . 9 PHE HD2 H 7.22 0.02 1
44 . 9 PHE HE1 H 7.12 0.02 1
45 . 9 PHE HE2 H 7.12 0.02 1
46 . 9 PHE N N 126.63 0.02 1
47 . 10 TYR H H 9.28 0.02 1
48 . 10 TYR HA H 4.92 0.02 1
49 . 10 TYR HB2 H 3.30 0.02 2
50 . 10 TYR HB3 H 2.80 0.02 2
51 . 10 TYR HD1 H 6.75 0.02 1
52 . 10 TYR HD2 H 6.75 0.02 1
53 . 10 TYR HE1 H 6.42 0.02 1
54 . 10 TYR HE2 H 6.42 0.02 1
55 . 11 ASN H H 8.23 0.02 1
56 . 11 ASN HA H 4.49 0.02 1
57 . 11 ASN HB2 H 3.21 0.02 1
58 . 11 ASN HB3 H 3.21 0.02 1
59 . 12 ALA H H 8.42 0.02 1
60 . 12 ALA HA H 3.56 0.02 1
61 . 12 ALA HB H 1.3 0.02 1
62 . 12 ALA N N 124.64 0.02 1
63 . 13 LYS H H 7.95 0.02 1
64 . 13 LYS HA H 4.07 0.02 1
65 . 13 LYS HB2 H 1.87 0.02 2
66 . 13 LYS HB3 H 1.82 0.02 2
67 . 13 LYS HD2 H 1.69 0.02 1
68 . 13 LYS HD3 H 1.69 0.02 1
69 . 14 ASP H H 6.62 0.02 1
70 . 14 ASP HA H 4.65 0.02 1
71 . 15 GLY H H 7.44 0.02 1
72 . 15 GLY HA2 H 3.47 0.02 1
73 . 15 GLY HA3 H 3.47 0.02 1
74 . 15 GLY N N 108.01 0.02 1
75 . 16 CLH H H 6.78 0.02 1
76 . 16 CLH HA H 4.32 0.02 1
77 . 16 CLH HE2 H 1.56 0.02 1
78 . 16 CLH HE3 H 1.56 0.02 1
79 . 17 ABA H H 8.94 0.02 1
80 . 17 ABA HA H 5.1 0.02 1
81 . 17 ABA HB2 H 1.97 0.02 1
82 . 17 ABA HB3 H 1.97 0.02 1
83 . 17 ABA HG2 H 1.02 0.02 1
84 . 17 ABA HG3 H 1.02 0.02 1
85 . 18 GLN H H 9.34 0.02 1
86 . 18 GLN HA H 4.75 0.02 1
87 . 18 GLN HB2 H 1.95 0.02 1
88 . 18 GLN HB3 H 1.95 0.02 1
89 . 18 GLN HG2 H 2.05 0.02 1
90 . 18 GLN HG3 H 2.05 0.02 1
91 . 19 THR H H 8.55 0.02 1
92 . 19 THR HA H 5.19 0.02 1
93 . 19 THR HB H 3.85 0.02 1
94 . 19 THR HG2 H 1.06 0.02 1
95 . 20 PHE H H 9.34 0.02 1
96 . 20 PHE HA H 4.75 0.02 1
97 . 20 PHE HB2 H 2.76 0.02 1
98 . 20 PHE HB3 H 2.76 0.02 1
99 . 20 PHE N N 126.75 0.02 1
100 . 21 VAL H H 8.38 0.02 1
101 . 21 VAL HA H 4.64 0.02 1
102 . 21 VAL HB H 1.87 0.02 1
103 . 21 VAL HG1 H 0.83 0.02 1
104 . 21 VAL HG2 H 0.83 0.02 1
105 . 21 VAL N N 121.88 0.02 1
106 . 22 TYR H H 9.16 0.02 1
107 . 22 TYR HA H 4.88 0.02 1
108 . 22 TYR HB2 H 3.15 0.02 2
109 . 22 TYR HB3 H 2.91 0.02 2
110 . 22 TYR HD1 H 7.07 0.02 1
111 . 22 TYR HD2 H 7.07 0.02 1
112 . 22 TYR HE1 H 6.69 0.02 1
113 . 22 TYR HE2 H 6.69 0.02 1
114 . 23 GLY H H 8.67 0.02 1
115 . 23 GLY HA2 H 4.23 0.02 2
116 . 23 GLY HA3 H 3.80 0.02 2
117 . 23 GLY N N 110.18 0.02 1
118 . 24 GLY H H 7.99 0.02 1
119 . 24 GLY HA2 H 3.97 0.02 1
120 . 24 GLY HA3 H 3.97 0.02 1
121 . 24 GLY N N 107.17 0.02 1
122 . 25 CYS H H 8.56 0.02 1
123 . 25 CYS HA H 4.69 0.02 1
124 . 25 CYS HB2 H 3.27 0.02 1
125 . 25 CYS HB3 H 3.27 0.02 1
stop_
save_
########################
# Coupling constants #
########################
save_coupling_constants_1
_Saveframe_category coupling_constants
_Details .
loop_
_Experiment_label
'15N-1H HSQC'
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $cond_1
_Spectrometer_frequency_1H 600
_Mol_system_component_name 'core module I'
_Text_data_format .
_Text_data .
loop_
_Coupling_constant_ID
_Coupling_constant_code
_Atom_one_residue_seq_code
_Atom_one_residue_label
_Atom_one_name
_Atom_two_residue_seq_code
_Atom_two_residue_label
_Atom_two_name
_Coupling_constant_value
_Coupling_constant_min_value
_Coupling_constant_max_value
_Coupling_constant_value_error
1 3JHNHA 3 ALA H 3 ALA HA 5.8 . . 1.0
2 3JHNHA 9 PHE H 9 PHE HA 8.0 . . 1.0
3 3JHNHA 12 ALA H 12 ALA HA 4.4 . . 1.0
4 3JHNHA 15 GLY H 15 GLY HA2 5.2 . . 1.0
5 3JHNHA 15 GLY H 15 GLY HA3 4.7 . . 1.0
6 3JHNHA 16 LEU H 16 LEU HA 8.5 . . 1.0
7 3JHNHA 20 PHE H 20 PHE HA 8.5 . . 1.0
8 3JHNHA 21 VAL H 21 VAL HA 8.5 . . 1.0
9 3JHNHA 23 GLY H 23 GLY HA2 4.8 . . 1.0
10 3JHNHA 23 GLY H 23 GLY HA3 4.7 . . 1.0
stop_
save_
save_coupling_constants_2
_Saveframe_category coupling_constants
_Details .
loop_
_Experiment_label
'15N-1H HSQC'
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $cond_1
_Spectrometer_frequency_1H 600
_Mol_system_component_name 'core module II'
_Text_data_format .
_Text_data .
loop_
_Coupling_constant_ID
_Coupling_constant_code
_Atom_one_residue_seq_code
_Atom_one_residue_label
_Atom_one_name
_Atom_two_residue_seq_code
_Atom_two_residue_label
_Atom_two_name
_Coupling_constant_value
_Coupling_constant_min_value
_Coupling_constant_max_value
_Coupling_constant_value_error
1 3JHNHA 3 ALA H 3 ALA HA 5.9 . . 1.0
2 3JHNHA 9 PHE H 9 PHE HA 8.6 . . 1.0
3 3JHNHA 12 ALA H 12 ALA HA 5.1 . . 1.0
4 3JHNHA 20 PHE H 20 PHE HA 9.2 . . 1.0
5 3JHNHA 21 VAL H 21 VAL HA 8.0 . . 1.0
6 3JHNHA 23 GLY H 23 GLY HA2 5.2 . . 1.0
7 3JHNHA 23 GLY H 23 GLY HA3 4.6 . . 1.0
stop_
save_