data_6352
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Isolation and characterization of epilancin 15X, a novel lantibiotic from a
clinical strain of Staphylococcus epidermidis
;
_BMRB_accession_number 6352
_BMRB_flat_file_name bmr6352.str
_Entry_type original
_Submission_date 2004-10-14
_Accession_date 2004-10-14
_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 Ekkelenkamp Miquel . .
2 Hanssen Micha G.M. .
3 Hsu Shang-Te D. .
4 'de Jong' Ad . .
5 Milatovic Dana . .
6 Verhoef Jan . .
7 'van Nuland' Nico A.J. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 189
"13C chemical shifts" 140
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2008-07-16 update BMRB 'Updating non-standard residue'
stop_
_Original_release_date 2004-10-14
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Isolation and structural characterization of epilancin 15X, a novel lantibiotic
from a clinical strain of Staphylococcus epidermidis
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 15792796
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Ekkelenkamp Miquel B. .
2 Hanssen Micha G.M. .
3 Hsu Shang-Te D. .
4 'de Jong' Ad . .
5 Milatovic Dana . .
6 Verhoef Jan . .
7 'van Nuland' Nico A.J. .
stop_
_Journal_abbreviation 'FEBS Lett.'
_Journal_volume 579
_Journal_issue 9
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 1917
_Page_last 1922
_Year 2005
_Details .
save_
#######################################
# Cited references within the entry #
#######################################
save_ref_1
_Saveframe_category citation
_Citation_full
;
Hsu ST, Breukink E, de Kruijff B, Kaptein R, Bonvin AM, van Nuland NA.
Mapping the targeted membrane pore formation mechanism by solution NMR:
the nisin Z and lipid II interaction in SDS micelles.
Biochemistry. 2002 Jun 18;41(24):7670-6.
;
_Citation_title
;
Mapping the targeted membrane pore formation mechanism by solution NMR: the nisin Z and lipid II interaction in SDS micelles.
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 12056898
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Hsu Shang-Te T. .
2 Breukink Eefjan . .
3 'de Kruijff' Ben . .
4 Kaptein Robert . .
5 Bonvin 'Alexandre M. J. J.' M. .
6 'van Nuland' 'Nico A. J.' A. .
stop_
_Journal_abbreviation Biochemistry
_Journal_name_full Biochemistry
_Journal_volume 41
_Journal_issue 24
_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 7670
_Page_last 7676
_Year 2002
_Details
;
Nisin is an example of type-A lantibiotics that contain cyclic lanthionine rings
and unusual dehydrated amino acids. Among the numerous pore-forming
antimicrobial peptides, type-A lantibiotics form an unique family of
post-translationally modified peptides. Via the recognition of cell wall
precursor lipid II, nisin has the capacity to form pores against Gram-positive
bacteria with an extremely high activity in the nanomolar (nM) range. Here we
report a high-resolution NMR spectroscopy study of nisin/lipid II interactions
in SDS micelles as a model membrane system in order to elucidate the mechanism
of molecular recognition at residue level. The binding to lipid II was studied
through (15)N-(1)H HSQC titration, backbone amide proton temperature
coefficient analysis, and heteronuclear (15)N[(1)H]-NOE relaxation dynamics
experiments. Upon the addition of lipid II, significant changes were monitored
in the N-terminal part of nisin. An extremely low amide proton temperature
coefficient (Delta delta/Delta T) was found for the amide proton of Ala3 (>
-0.1 ppb/K) in the complex form. This suggests tight hydrogen bonding and/or
isolation from the bulk solvent for this residue. Large chemical shift
perturbations were also observed in the first two rings. In contrast, the
C-terminal part of nisin was almost unaffected. This part of the molecule
remains flexible and solvent-exposed. On the basis of our results, a multistep
pore-forming mechanism is proposed. The N-terminal part of nisin first binds to
lipid II, and a subsequent structural rearrangement takes place. The C-terminal
part of nisin is possibly responsible for the activation of the pore formation.
In light of the emerging antibiotic resistance problems, an understanding of
the specific recognition mechanism of nisin with lipid II at the residue
specific level may therefore aid in the development of novel antibiotics.
;
save_
save_ref_2
_Saveframe_category citation
_Citation_full
;
Hsu ST, Breukink E, Bierbaum G, Sahl HG, de Kruijff B, Kaptein R, van Nuland
NA, Bonvin AM.
Free Full Text NMR study of mersacidin and lipid II interaction in
dodecylphosphocholine micelles. Conformational changes are a key to
antimicrobial activity.
J Biol Chem. 2003 Apr 11;278(15):13110-7. Epub 2003 Jan 31.
;
_Citation_title
;
NMR study of mersacidin and lipid II interaction in dodecylphosphocholine micelles. Conformational changes are a key to antimicrobial activity.
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 12562773
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Hsu 'Shang-Te D.' T. .
2 Breukink Eefjan . .
3 Bierbaum Gabriele . .
4 Sahl Hans-Georg G. .
5 'de Kruijff' Ben . .
6 Kaptein Rob . .
7 'van Nuland' 'Nico A. J.' A. .
8 Bonvin 'Alexandre M. J. J.' M. .
stop_
_Journal_abbreviation 'J. Biol. Chem.'
_Journal_name_full 'The Journal of biological chemistry'
_Journal_volume 278
_Journal_issue 15
_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 13110
_Page_last 13117
_Year 2003
_Details
;
Mersacidin belongs to the type B lantibiotics (lanthionine-containing
antibiotics) that contain post-translationally modified amino acids and cyclic
ring structures. It targets the cell wall precursor lipid II and thereby
inhibits cell wall synthesis. In light of the emerging antibiotics resistance
problem, the understanding of the antibacterial activity on a structural basis
provides a key to circumvent this issue. Here we present solution NMR studies
of mersacidin-lipid II interaction in dodecylphosphocholine (DPC) micelles.
Distinct solution structures of mersacidin were determined in three different
states: in water/methanol solution and in DPC micelles with and without lipid
II. The structures in various sample conditions reveal remarkable
conformational changes in which the junction between Ala-12 and Abu-13 (where
Abu is aminobutyric acid) effectively serves as the hinge for the opening and
closure of the ring structures. The DPC micelle-bound form resembles the
previously determined NMR and x-ray crystal structures of mersacidin in pure
methanol but substantially deviates from the other two states in our current
report. The structural changes delineate the large chemical shift perturbations
observed during the course of a two-step (15)N-(1)H heteronuclear single
quantum coherence titration. They also modulate the surface charge distribution
of mersacidin suggesting that electrostatics play a central role in the
mersacidin-lipid II interaction. The observed conformational adaptability of
mersacidin might be a general feature of lipid II-interacting
antibiotics/peptides.
;
save_
save_ref_3
_Saveframe_category citation
_Citation_full
;
Hsu ST, Breukink E, Tischenko E, Lutters MA, De Kruijff B, Kaptein R, Bonvin
AM, Van Nuland NA.
The nisin-lipid II complex reveals a pyrophosphate cage that provides a
blueprint for novel antibiotics.
Nat Struct Mol Biol. 2004 Oct;11(10):963-7. Epub 2004 Sep 12.
;
_Citation_title
;
The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics.
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 15361862
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Hsu 'Shang-Te D.' T. .
2 Breukink Eefjan . .
3 Tischenko Eugene . .
4 Lutters 'Mandy A. G.' A. .
5 'de Kruijff' Ben . .
6 Kaptein Robert . .
7 Bonvin 'Alexandre M. J. J.' M. .
8 'van Nuland' 'Nico A. J.' A. .
stop_
_Journal_abbreviation 'Nat. Struct. Mol. Biol.'
_Journal_name_full 'Nature structural & molecular biology'
_Journal_volume 11
_Journal_issue 10
_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 963
_Page_last 967
_Year 2004
_Details
;
The emerging antibiotics-resistance problem has underlined the urgent need for
novel antimicrobial agents. Lantibiotics (lanthionine-containing antibiotics)
are promising candidates to alleviate this problem. Nisin, a member of this
family, has a unique pore-forming activity against bacteria. It binds to lipid
II, the essential precursor of cell wall synthesis. As a result, the membrane
permeabilization activity of nisin is increased by three orders of magnitude.
Here we report the solution structure of the complex of nisin and lipid II. The
structure shows a novel lipid II-binding motif in which the pyrophosphate
moiety of lipid II is primarily coordinated by the N-terminal backbone amides
of nisin via intermolecular hydrogen bonds. This cage structure provides a
rationale for the conservation of the lanthionine rings among several lipid
II-binding lantibiotics. The structure of the pyrophosphate cage offers a
template for structure-based design of novel antibiotics.
;
save_
##################################
# Molecular system description #
##################################
save_system_Epilancin_15X
_Saveframe_category molecular_system
_Mol_system_name 'Epilancin 15X'
_Abbreviation_common 'Epilancin 15X'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'Epilancin 15X' $Epilancin_15X
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'all other bound'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_Epilancin_15X
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'Epilancin 15X'
_Abbreviation_common 'Epilancin 15X'
_Molecular_mass 3175.2
_Mol_thiol_state 'all other bound'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 31
_Mol_residue_sequence
;
XAXIVKXXIKAXKKLCRGFX
LXCGCHFXGKK
;
loop_
_Residue_seq_code
_Residue_label
1 HOP 2 ALA 3 DHA 4 ILE 5 VAL
6 LYS 7 AA4 8 AA4 9 ILE 10 LYS
11 ALA 12 DAL 13 LYS 14 LYS 15 LEU
16 CYS 17 ARG 18 GLY 19 PHE 20 ABA
21 LEU 22 ABA 23 CYS 24 GLY 25 CYS
26 HIS 27 PHE 28 AA4 29 GLY 30 LYS
31 LYS
stop_
_Sequence_homology_query_date 2008-03-24
_Sequence_homology_query_revised_last_date 2007-05-31
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 1W9N 'A Chain A, Isolation And Characterization OfEpilancin 15x, A Novel Antibiotic From A ClinicalStrain Of Staphylococcus Ep' 100.00 31 100 100 2e-05
stop_
save_
######################
# Polymer residues #
######################
save_chem_comp_DHA
_Saveframe_category polymer_residue
_Mol_type 'PEPTIDE LINKING'
_Name_common '2-AMINO-ACRYLIC ACID'
_BMRB_code .
_PDB_code DHA
_Standard_residue_derivative .
_Molecular_mass 87.077
_Mol_paramagnetic .
_Details
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Mon Aug 1 12:11:43 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 . ?
C C C . 0 . ?
O O O . 0 . ?
OXT OXT O . 0 . ?
H H H . 0 . ?
H2 H2 H . 0 . ?
HB1 HB1 H . 0 . ?
HB2 HB2 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 ? ?
DOUB CA CB ? ?
SING CA C ? ?
SING CB HB1 ? ?
SING CB HB2 ? ?
DOUB C O ? ?
SING C OXT ? ?
SING OXT HXT ? ?
stop_
save_
save_chem_comp_DAL
_Saveframe_category polymer_residue
_Mol_type 'D-peptide linking'
_Name_common D-ALANINE
_BMRB_code .
_PDB_code DAL
_Standard_residue_derivative .
_Molecular_mass 89.093
_Mol_paramagnetic .
_Details
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Mon Aug 1 10:26:43 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 . ?
C C C . 0 . ?
O O O . 0 . ?
OXT OXT O . 0 . ?
H H H . 0 . ?
H2 H2 H . 0 . ?
HA HA H . 0 . ?
HB1 HB1 H . 0 . ?
HB2 HB2 H . 0 . ?
HB3 HB3 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 HB1 ? ?
SING CB HB2 ? ?
SING CB HB3 ? ?
DOUB C O ? ?
SING C OXT ? ?
SING OXT HXT ? ?
stop_
save_
save_chem_comp_HOP
_Saveframe_category polymer_residue
_Mol_type non-polymer
_Name_common (1S,2S,5S)2-(4-GLUTARIDYLBENZYL)-5-PHENYL-1-CYCLOHEXANOL
_BMRB_code .
_PDB_code HOP
_Standard_residue_derivative .
_Molecular_mass 381.465
_Mol_paramagnetic .
_Details
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Mon Aug 1 12:13:42 2011
;
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
C1 C1 C . 0 . ?
C2 C2 C . 0 . ?
C6 C6 C . 0 . ?
C5 C5 C . 0 . ?
C4 C4 C . 0 . ?
C3 C3 C . 0 . ?
C7 C7 C . 0 . ?
C12 C12 C . 0 . ?
C11 C11 C . 0 . ?
C10 C10 C . 0 . ?
C9 C9 C . 0 . ?
C8 C8 C . 0 . ?
C13 C13 C . 0 . ?
C14 C14 C . 0 . ?
C15 C15 C . 0 . ?
C16 C16 C . 0 . ?
C17 C17 C . 0 . ?
C18 C18 C . 0 . ?
O19 O19 O . 0 . ?
C20 C20 C . 0 . ?
O21 O21 O . 0 . ?
N22 N22 N . 0 . ?
C23 C23 C . 0 . ?
C24 C24 C . 0 . ?
C25 C25 C . 0 . ?
C26 C26 C . 0 . ?
O27 O27 O . 0 . ?
O28 O28 O . 0 . ?
H1 H1 H . 0 . ?
H2 H2 H . 0 . ?
H6 H6 H . 0 . ?
H5 H5 H . 0 . ?
H3 H3 H . 0 . ?
H7 H7 H . 0 . ?
H121 H121 H . 0 . ?
H122 H122 H . 0 . ?
H11 H11 H . 0 . ?
H10 H10 H . 0 . ?
H91 H91 H . 0 . ?
H92 H92 H . 0 . ?
H81 H81 H . 0 . ?
H82 H82 H . 0 . ?
H14 H14 H . 0 . ?
H15 H15 H . 0 . ?
H17 H17 H . 0 . ?
H18 H18 H . 0 . ?
HO9 HO9 H . 0 . ?
HN2 HN2 H . 0 . ?
H231 H231 H . 0 . ?
H232 H232 H . 0 . ?
H241 H241 H . 0 . ?
H242 H242 H . 0 . ?
H251 H251 H . 0 . ?
H252 H252 H . 0 . ?
HO8 HO8 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 C1 C2 ? ?
DOUB C1 C6 ? ?
SING C1 H1 ? ?
DOUB C2 C3 ? ?
SING C2 H2 ? ?
SING C6 C5 ? ?
SING C6 H6 ? ?
DOUB C5 C4 ? ?
SING C5 H5 ? ?
SING C4 C3 ? ?
SING C4 C7 ? ?
SING C3 H3 ? ?
SING C7 C12 ? ?
SING C7 C8 ? ?
SING C7 H7 ? ?
SING C12 C11 ? ?
SING C12 H121 ? ?
SING C12 H122 ? ?
SING C11 C10 ? ?
SING C11 O19 ? ?
SING C11 H11 ? ?
SING C10 C9 ? ?
SING C10 C13 ? ?
SING C10 H10 ? ?
SING C9 C8 ? ?
SING C9 H91 ? ?
SING C9 H92 ? ?
SING C8 H81 ? ?
SING C8 H82 ? ?
DOUB C13 C14 ? ?
SING C13 C18 ? ?
SING C14 C15 ? ?
SING C14 H14 ? ?
DOUB C15 C16 ? ?
SING C15 H15 ? ?
SING C16 C17 ? ?
SING C16 C20 ? ?
DOUB C17 C18 ? ?
SING C17 H17 ? ?
SING C18 H18 ? ?
SING O19 HO9 ? ?
DOUB C20 O21 ? ?
SING C20 N22 ? ?
SING N22 C23 ? ?
SING N22 HN2 ? ?
SING C23 C24 ? ?
SING C23 H231 ? ?
SING C23 H232 ? ?
SING C24 C25 ? ?
SING C24 H241 ? ?
SING C24 H242 ? ?
SING C25 C26 ? ?
SING C25 H251 ? ?
SING C25 H252 ? ?
DOUB C26 O27 ? ?
SING C26 O28 ? ?
SING O28 HO8 ? ?
stop_
save_
save_chem_comp_AA4
_Saveframe_category polymer_residue
_Mol_type 'L-PEPTIDE LINKING'
_Name_common '2-AMINO-5-HYDROXYPENTANOIC ACID'
_BMRB_code AA4
_PDB_code AA4
_Standard_residue_derivative .
_Molecular_mass 133.146
_Mol_paramagnetic .
_Details .
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 . ?
CD CD C . 0 . ?
OE OE 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 . ?
HE HE 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 C ? ?
SING CA CB ? ?
SING CA HA ? ?
DOUB C O ? ?
SING C OXT ? ?
SING CB CG ? ?
SING CB HB2 ? ?
SING CB HB3 ? ?
SING CG CD ? ?
SING CG HG2 ? ?
SING CG HG3 ? ?
SING CD OE ? ?
SING CD HD2 ? ?
SING CD HD3 ? ?
SING OE HE ? ?
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 ABA
_PDB_code ABA
_Standard_residue_derivative .
_Molecular_mass 103.120
_Mol_paramagnetic .
_Details .
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_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
_Strain
$Epilancin_15X 'Staphylococcus epidermidis' 1282 Eubacteria . Staphylococcus epidermidis 15X150
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
$Epilancin_15X 'purified from the natural source' . . . . .
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_water
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$Epilancin_15X 0.8 mM .
stop_
save_
save_sample_d2o
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$Epilancin_15X 3.1 mM .
stop_
save_
############################
# Computer software used #
############################
save_NMRPipe
_Saveframe_category software
_Name NMRPipe
_Version n/a
loop_
_Task
'data processing'
stop_
_Details .
save_
save_NMRView
_Saveframe_category software
_Name NMRView
_Version 4.0.5
loop_
_Task
Assignment
stop_
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 750
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_1H-1H_TOCSY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-1H TOCSY'
_Sample_label .
save_
save_1H-1H_NOESY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-1H NOESY'
_Sample_label .
save_
save_1H-13C_HSQC_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-13C HSQC'
_Sample_label .
save_
save_1H-13C_HMBC_4
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-13C HMBC'
_Sample_label .
save_
#######################
# Sample conditions #
#######################
save_Ex-cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH . . pH
temperature 305 . K
stop_
save_
save_Ex-cond_2
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH . . pH
temperature 283 . 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
_Reference_correction_type
water H 1 protons ppm 4.91 internal direct . internal parallel 1.0 temperature
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_shift_Epilancin_15X_283K
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'1H-1H TOCSY'
stop_
loop_
_Sample_label
$sample_water
stop_
_Sample_conditions_label $Ex-cond_2
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'Epilancin 15X'
_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 HOP CA C 69.006 0.0 .
2 . 1 HOP HA H 4.257 0.0 .
3 . 1 HOP CB C 21.217 0.0 .
4 . 1 HOP HB1 H 1.327 0.0 .
5 . 1 HOP C C 179.193 0.0 .
6 . 2 ALA H H 8.33 0.0 .
7 . 2 ALA CA C 51.147 0.0 .
8 . 2 ALA HA H 4.31 0.0 .
9 . 2 ALA CB C 17.907 0.0 .
10 . 2 ALA HB H 1.413 0.0 .
11 . 2 ALA C C 175.824 0.0 .
12 . 3 DHA H H 9.892 0.0 .
13 . 3 DHA CA C 137.099 0.0 .
14 . 3 DHA CB C 114.436 0.0 .
15 . 3 DHA HB2 H 5.488 0.0 .
16 . 3 DHA HB3 H 5.562 0.0 .
17 . 3 DHA C C 168.652 0.0 .
18 . 4 ILE H H 8.256 0.0 .
19 . 4 ILE CA C 60.396 0.0 .
20 . 4 ILE HA H 4.161 0.0 .
21 . 4 ILE CB C 37.237 0.0 .
22 . 4 ILE HB H 1.873 0.0 .
23 . 4 ILE CG1 C 26.384 0.0 .
24 . 4 ILE HG13 H 1.46 0.0 .
25 . 4 ILE HG12 H 1.18 0.0 .
26 . 4 ILE CD1 C 11.608 0.0 .
27 . 4 ILE HD1 H 0.846 0.0 .
28 . 4 ILE CG2 C 16.303 0.0 .
29 . 4 ILE HG2 H 0.868 0.0 .
30 . 4 ILE C C 175.344 0.0 .
31 . 5 VAL H H 8.283 0.0 .
32 . 5 VAL CA C 61.151 0.0 .
33 . 5 VAL HA H 4.082 0.0 .
34 . 5 VAL CB C 31.443 0.0 .
35 . 5 VAL HB H 2.019 0.0 .
36 . 5 VAL CG2 C 19.629 0.0 .
37 . 5 VAL HG2 H 0.9 0.0 .
38 . 5 VAL CG1 C 20.037 0.0 .
39 . 5 VAL HG1 H 0.851 0.0 .
40 . 5 VAL C C 175.348 0.0 .
41 . 6 LYS H H 8.516 0.0 .
42 . 6 LYS CA C 55.477 0.0 .
43 . 6 LYS HA H 4.36 0.0 .
44 . 6 LYS CB C 31.735 0.0 .
45 . 6 LYS HB3 H 1.89 0.0 .
46 . 6 LYS HB2 H 1.807 0.0 .
47 . 6 LYS CG C 23.644 0.0 .
48 . 6 LYS HG3 H 1.495 0.0 .
49 . 6 LYS HG2 H 1.415 0.0 .
50 . 6 LYS CD C 27.746 0.0 .
51 . 6 LYS HD3 H 1.67 0.0 .
52 . 6 LYS HD2 H 1.67 0.0 .
53 . 6 LYS CE C 39.455 0.0 .
54 . 6 LYS HE3 H 2.942 0.0 .
55 . 6 LYS HE2 H 2.942 0.0 .
56 . 6 LYS HZ H 7.59 0.0 .
57 . 6 LYS C C 175.457 0.0 .
58 . 7 AA4 H H 9.767 0.0 .
59 . 7 AA4 CA C 129.663 0.0 .
60 . 7 AA4 CB C 135.931 0.0 .
61 . 7 AA4 HB H 6.668 0.0 .
62 . 7 AA4 CG2 C 14.277 0.0 .
63 . 7 AA4 HG21 H 1.781 0.0 .
64 . 7 AA4 C C 167.962 0.0 .
65 . 8 AA4 H H 9.224 0.0 .
66 . 8 AA4 CA C 129.727 0.0 .
67 . 8 AA4 CB C 136.14 0.0 .
68 . 8 AA4 HB H 6.665 0.0 .
69 . 8 AA4 CG2 C 14.283 0.0 .
70 . 8 AA4 HG21 H 1.717 0.0 .
71 . 8 AA4 C C 168.814 0.0 .
72 . 9 ILE H H 7.898 0.0 .
73 . 9 ILE CA C 60.91 0.0 .
74 . 9 ILE HA H 4.103 0.0 .
75 . 9 ILE CB C 37.07 0.0 .
76 . 9 ILE HB H 1.895 0.0 .
77 . 9 ILE CG1 C 26.706 0.0 .
78 . 9 ILE HG13 H 1.456 0.0 .
79 . 9 ILE HG12 H 1.19 0.0 .
80 . 9 ILE CD1 C 11.608 0.0 .
81 . 9 ILE HD1 H 0.821 0.0 .
82 . 9 ILE CG2 C 16.597 0.0 .
83 . 9 ILE HG2 H 0.877 0.0 .
84 . 9 ILE C C 175.903 0.0 .
85 . 10 LYS H H 8.268 0.0 .
86 . 10 LYS CA C 55.526 0.0 .
87 . 10 LYS HA H 4.182 0.0 .
88 . 10 LYS CB C 31.838 0.0 .
89 . 10 LYS HB3 H 1.806 0.0 .
90 . 10 LYS HB2 H 1.755 0.0 .
91 . 10 LYS CG C 23.64 0.0 .
92 . 10 LYS HG3 H 1.456 0.0 .
93 . 10 LYS HG2 H 1.385 0.0 .
94 . 10 LYS CD C 27.844 0.0 .
95 . 10 LYS HD3 H 1.745 0.0 .
96 . 10 LYS HD2 H 1.745 0.0 .
97 . 10 LYS CE C 40.755 0.0 .
98 . 10 LYS HE3 H 2.943 0.0 .
99 . 10 LYS HE2 H 2.943 0.0 .
100 . 10 LYS HZ H 7.57 0.0 .
101 . 11 ALA H H 8.034 0.0 .
102 . 11 ALA CA C 51.525 0.0 .
103 . 11 ALA HA H 4.218 0.0 .
104 . 11 ALA CB C 17.946 0.0 .
105 . 11 ALA HB H 1.364 0.0 .
106 . 11 ALA C C 176.776 0.0 .
107 . 12 DAL H H 8.061 0.0 .
108 . 12 DAL CA C 55.762 0.0 .
109 . 12 DAL HA H 4.401 0.0 .
110 . 12 DAL CB C 35.694 0.0 .
111 . 12 DAL HB1 H 3.07 0.0 .
112 . 12 DAL HB2 H 3.025 0.0 .
113 . 12 DAL C C 179.654 0.0 .
114 . 13 LYS H H 8.392 0.0 .
115 . 13 LYS CA C 55.087 0.0 .
116 . 13 LYS HA H 4.104 0.0 .
117 . 13 LYS CB C 20.996 0.0 .
118 . 13 LYS HB3 H 1.766 0.0 .
119 . 13 LYS HB2 H 1.766 0.0 .
120 . 13 LYS HG3 H 1.395 0.0 .
121 . 13 LYS HG2 H 1.245 0.0 .
122 . 13 LYS HD3 H 1.632 0.0 .
123 . 13 LYS HD2 H 1.597 0.0 .
124 . 13 LYS HE3 H 2.957 0.0 .
125 . 13 LYS HE2 H 2.957 0.0 .
126 . 13 LYS HZ H 7.577 0.0 .
127 . 13 LYS C C 180.353 0.0 .
128 . 14 LYS H H 7.801 0.0 .
129 . 14 LYS CA C 55.814 0.0 .
130 . 14 LYS HA H 3.994 0.0 .
131 . 14 LYS CB C 31.723 0.0 .
132 . 14 LYS HB3 H 1.763 0.0 .
133 . 14 LYS HB2 H 1.763 0.0 .
134 . 14 LYS CG C 23.644 0.0 .
135 . 14 LYS HG3 H 1.315 0.0 .
136 . 14 LYS HG2 H 1.315 0.0 .
137 . 14 LYS CD C 27.746 0.0 .
138 . 14 LYS HD3 H 1.64 0.0 .
139 . 14 LYS HD2 H 1.64 0.0 .
140 . 14 LYS CE C 40.639 0.0 .
141 . 14 LYS HE3 H 2.943 0.0 .
142 . 14 LYS HE2 H 2.943 0.0 .
143 . 14 LYS HZ H 7.581 0.0 .
144 . 14 LYS C C 175.46 0.0 .
145 . 15 LEU H H 8.386 0.0 .
146 . 15 LEU CA C 54.283 0.0 .
147 . 15 LEU HA H 4.207 0.0 .
148 . 15 LEU CB C 39.55 0.0 .
149 . 15 LEU HB3 H 1.671 0.0 .
150 . 15 LEU HB2 H 1.626 0.0 .
151 . 15 LEU CG C 26.053 0.0 .
152 . 15 LEU HG H 1.538 0.0 .
153 . 15 LEU CD1 C 23.801 0.0 .
154 . 15 LEU HD1 H 0.809 0.0 .
155 . 15 LEU CD2 C 21.768 0.0 .
156 . 15 LEU HD2 H 0.858 0.0 .
157 . 15 LEU C C 177.654 0.0 .
158 . 16 CYS H H 8.018 0.0 .
159 . 16 CYS CA C 54.641 0.0 .
160 . 16 CYS HA H 4.477 0.0 .
161 . 16 CYS CB C 27.465 0.0 .
162 . 16 CYS HB3 H 3.067 0.0 .
163 . 16 CYS HB2 H 3.015 0.0 .
164 . 16 CYS C C 173.209 0.0 .
165 . 17 ARG H H 8.396 0.0 .
166 . 17 ARG CA C 55.605 0.0 .
167 . 17 ARG HA H 4.241 0.0 .
168 . 17 ARG CB C 29.122 0.0 .
169 . 17 ARG HB3 H 1.83 0.0 .
170 . 17 ARG HB2 H 1.775 0.0 .
171 . 17 ARG CG C 25.941 0.0 .
172 . 17 ARG HG3 H 1.644 0.0 .
173 . 17 ARG HG2 H 1.578 0.0 .
174 . 17 ARG CD C 42.045 0.0 .
175 . 17 ARG HD3 H 3.167 0.0 .
176 . 17 ARG HD2 H 3.167 0.0 .
177 . 17 ARG HE H 7.216 0.0 .
178 . 17 ARG CZ C 158.259 0.0 .
179 . 17 ARG HH21 H 6.913 0.0 .
180 . 17 ARG HH22 H 6.913 0.0 .
181 . 17 ARG HH11 H 6.483 0.0 .
182 . 17 ARG HH12 H 6.483 0.0 .
183 . 17 ARG C C 178.051 0.0 .
184 . 18 GLY H H 8.66 0.0 .
185 . 18 GLY CA C 44.029 0.0 .
186 . 18 GLY HA3 H 3.983 0.0 .
187 . 18 GLY HA2 H 3.819 0.0 .
188 . 18 GLY C C 173.444 0.0 .
189 . 19 PHE H H 8.046 0.0 .
190 . 19 PHE CA C 57.711 0.0 .
191 . 19 PHE HA H 4.561 0.0 .
192 . 19 PHE CB C 37.919 0.0 .
193 . 19 PHE HB3 H 3.196 0.0 .
194 . 19 PHE HB2 H 2.938 0.0 .
195 . 19 PHE CG C 137.172 0.0 .
196 . 19 PHE CD1 C 130.694 0.0 .
197 . 19 PHE HD1 H 7.213 0.0 .
198 . 19 PHE CE1 C 130.482 0.0 .
199 . 19 PHE HE1 H 7.316 0.0 .
200 . 19 PHE CZ C 128.973 0.0 .
201 . 19 PHE HZ H 7.256 0.0 .
202 . 19 PHE CE2 C 130.482 0.0 .
203 . 19 PHE HE2 H 7.316 0.0 .
204 . 19 PHE CD2 C 130.694 0.0 .
205 . 19 PHE HD2 H 7.213 0.0 .
206 . 19 PHE C C 177.07 0.0 .
207 . 20 ABA H H 8.758 0.0 .
208 . 20 ABA CA C 60.175 0.0 .
209 . 20 ABA HA H 4.685 0.0 .
210 . 20 ABA CB C 49.041 0.0 .
211 . 20 ABA HB H 3.296 0.0 .
212 . 20 ABA CG2 C 21.092 0.0 .
213 . 20 ABA HG2 H 0.55 0.0 .
214 . 20 ABA C C 176.762 0.0 .
215 . 21 LEU H H 7.991 0.0 .
216 . 21 LEU CA C 54.461 0.0 .
217 . 21 LEU HA H 4.56 0.0 .
218 . 21 LEU CB C 39.081 0.0 .
219 . 21 LEU HB3 H 1.771 0.0 .
220 . 21 LEU HB2 H 1.53 0.0 .
221 . 21 LEU CG C 26.185 0.0 .
222 . 21 LEU HG H 1.413 0.0 .
223 . 21 LEU CD1 C 22.479 0.0 .
224 . 21 LEU HD1 H 0.873 0.0 .
225 . 21 LEU CD2 C 22.719 0.0 .
226 . 21 LEU HD2 H 0.92 0.0 .
227 . 21 LEU C C 177.632 0.0 .
228 . 22 ABA H H 9.581 0.0 .
229 . 22 ABA CA C 60.932 0.0 .
230 . 22 ABA HA H 4.87 0.0 .
231 . 22 ABA CB C 46.744 0.0 .
232 . 22 ABA HB H 3.44 0.0 .
233 . 22 ABA CG2 C 21.173 0.0 .
234 . 22 ABA HG2 H 1.344 0.0 .
235 . 23 CYS H H 7.692 0.0 .
236 . 23 CYS CA C 57.21 0.0 .
237 . 23 CYS HA H 3.991 0.0 .
238 . 23 CYS CB C 37.945 0.0 .
239 . 23 CYS HB3 H 3.516 0.0 .
240 . 23 CYS HB2 H 2.736 0.0 .
241 . 23 CYS C C 172.718 0.0 .
242 . 24 GLY H H 9.118 0.0 .
243 . 24 GLY CA C 44.539 0.0 .
244 . 24 GLY HA3 H 3.989 0.0 .
245 . 24 GLY HA2 H 3.735 0.0 .
246 . 24 GLY C C 172.557 0.0 .
247 . 25 CYS H H 7.333 0.0 .
248 . 25 CYS CA C 54.744 0.0 .
249 . 25 CYS HA H 3.937 0.0 .
250 . 25 CYS CB C 38.533 0.0 .
251 . 25 CYS HB3 H 3.361 0.0 .
252 . 25 CYS HB2 H 2.499 0.0 .
253 . 25 CYS C C 173.156 0.0 .
254 . 26 HIS H H 8.734 0.0 .
255 . 26 HIS CA C 53.61 0.0 .
256 . 26 HIS HA H 4.695 0.0 .
257 . 26 HIS CB C 27.59 0.0 .
258 . 26 HIS HB3 H 3.189 0.0 .
259 . 26 HIS HB2 H 3.065 0.0 .
260 . 26 HIS CG C 129.924 0.0 .
261 . 26 HIS CD2 C 118.772 0.0 .
262 . 26 HIS HD2 H 7.203 0.0 .
263 . 26 HIS CE1 C 135.03 0.0 .
264 . 26 HIS HE1 H 8.572 0.0 .
265 . 26 HIS C C 173.053 0.0 .
266 . 27 PHE H H 8.605 0.0 .
267 . 27 PHE CA C 56.915 0.0 .
268 . 27 PHE HA H 4.676 0.0 .
269 . 27 PHE CB C 38.164 0.0 .
270 . 27 PHE HB3 H 3.112 0.0 .
271 . 27 PHE HB2 H 3.112 0.0 .
272 . 27 PHE CG C 137.403 0.0 .
273 . 27 PHE CD1 C 130.738 0.0 .
274 . 27 PHE HD1 H 7.275 0.0 .
275 . 27 PHE CE1 C 130.643 0.0 .
276 . 27 PHE HE1 H 7.351 0.0 .
277 . 27 PHE CZ C 128.959 0.0 .
278 . 27 PHE HZ H 7.294 0.0 .
279 . 27 PHE CE2 C 130.643 0.0 .
280 . 27 PHE HE2 H 7.351 0.0 .
281 . 27 PHE CD2 C 130.738 0.0 .
282 . 27 PHE HD2 H 7.275 0.0 .
283 . 27 PHE C C 174.791 0.0 .
284 . 28 AA4 H H 9.684 0.0 .
285 . 28 AA4 CA C 128.979 0.0 .
286 . 28 AA4 CB C 136.488 0.0 .
287 . 28 AA4 HB H 6.623 0.0 .
288 . 28 AA4 CG2 C 14.129 0.0 .
289 . 28 AA4 HG21 H 1.426 0.0 .
290 . 28 AA4 C C 168.367 0.0 .
291 . 29 GLY H H 7.829 0.0 .
292 . 29 GLY CA C 44.078 0.0 .
293 . 29 GLY HA3 H 3.891 0.0 .
294 . 29 GLY HA2 H 3.891 0.0 .
295 . 29 GLY C C 172.915 0.0 .
296 . 30 LYS H H 8.006 0.0 .
297 . 30 LYS CA C 55.007 0.0 .
298 . 30 LYS HA H 4.279 0.0 .
299 . 30 LYS CB C 32.055 0.0 .
300 . 30 LYS HB3 H 1.832 0.0 .
301 . 30 LYS HB2 H 1.752 0.0 .
302 . 30 LYS CG C 23.64 0.0 .
303 . 30 LYS HG3 H 1.419 0.0 .
304 . 30 LYS HG2 H 1.419 0.0 .
305 . 30 LYS CD C 27.746 0.0 .
306 . 30 LYS HD3 H 1.642 0.0 .
307 . 30 LYS HD2 H 1.642 0.0 .
308 . 30 LYS CE C 40.639 0.0 .
309 . 30 LYS HE3 H 2.94 0.0 .
310 . 30 LYS HE2 H 2.94 0.0 .
311 . 30 LYS HZ H 7.536 0.0 .
312 . 30 LYS C C 175.163 0.0 .
313 . 31 LYS H H 8.208 0.0 .
314 . 31 LYS CA C 54.87 0.0 .
315 . 31 LYS HA H 4.1 0.0 .
316 . 31 LYS CB C 31.842 0.0 .
317 . 31 LYS HB3 H 1.778 0.0 .
318 . 31 LYS HB2 H 1.682 0.0 .
319 . 31 LYS CG C 23.644 0.0 .
320 . 31 LYS HG3 H 1.371 0.0 .
321 . 31 LYS HG2 H 1.371 0.0 .
322 . 31 LYS CD C 27.746 0.0 .
323 . 31 LYS HD3 H 1.619 0.0 .
324 . 31 LYS HD2 H 1.619 0.0 .
325 . 31 LYS CE C 40.639 0.0 .
326 . 31 LYS HE3 H 2.941 0.0 .
327 . 31 LYS HE2 H 2.941 0.0 .
328 . 31 LYS HZ H 7.514 0.0 .
329 . 31 LYS C C 176.375 0.0 .
stop_
save_