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_