data_4988

#######################
#  Entry information  #
#######################

save_entry_information
   _Saveframe_category      entry_information

   _Entry_title
;
Three Dimensional Solution Structure of Huwentoxin-II BY 2D 1H-NMR
;
   _BMRB_accession_number   4988
   _BMRB_flat_file_name     bmr4988.str
   _Entry_type              original
   _Submission_date         2001-04-12
   _Accession_date          2001-04-17
   _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 Shu   Qin       . .
      2 Lu    Shan-yun  . .
      3 Gu    Xiao-chen . .
      4 Liang Song-ping . .

   stop_

   loop_
      _Saveframe_category_type
      _Saveframe_category_type_count

      assigned_chemical_shifts 1

   stop_

   loop_
      _Data_type
      _Data_type_count

      "1H chemical shifts" 249

   stop_

   loop_
      _Revision_date
      _Revision_keyword
      _Revision_author
      _Revision_detail

      2001-05-11 original BMRB .

   stop_

   _Original_release_date   2001-04-17

save_


#############################
#  Citation for this entry  #
#############################

save_entry_citation
   _Saveframe_category           entry_citation

   _Citation_full                .
   _Citation_title
;
Three-dimensional Solution Structure Determination of Huwentoxin-II by 2D 1H-NMR
;
   _Citation_status              submitted
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              .
   _PubMed_ID                    ?

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Shu   Q. .  .
      2 Lu    S. Y. .
      3 Gu    X. C. .
      4 Liang S. P. .

   stop_

   _Journal_abbreviation         .
   _Journal_volume               .
   _Journal_issue                .
   _Journal_CSD                  .
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_ISBN                    .
   _Conference_state_province    .
   _Conference_abstract_number   .
   _Page_first                   .
   _Page_last                    .
   _Year                         .
   _Details                      .

   loop_
      _Keyword

      'disulfide bonds'
      'insecticidal toxin'
       neurotoxin

   stop_

save_


#######################################
#  Cited references within the entry  #
#######################################

save_ref_1
   _Saveframe_category           citation

   _Citation_full
;
Q. SHU, S.Y. LU, X.C. GU, S.P. LIANG.
Sequence-specific assignment of 1H-NMR resonance and
determination of the secondary structure of HWTX-II.
Acta Biochim. et Biophys. Sinica  2001,33: 65
;
   _Citation_title
;
Sequence-specific Assignment of (1)H-NMR Resonance and Determination of the Secondary Structure of HWTX-II.
;
   _Citation_status              published
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              .
   _PubMed_ID                    12053191

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Shu   . .  .
      2 Lu    . Y. .
      3 Gu    . C. .
      4 Liang . P. .

   stop_

   _Journal_abbreviation        'Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao'
   _Journal_name_full           'Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica'
   _Journal_volume               33
   _Journal_issue                1
   _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                   65
   _Page_last                    70
   _Year                         2001
   _Details
;
Huwentoxin-II (HWTX-II)is an insecticidal peptide purified from the venom of
spider Selenocosmia huwena. The structure of this toxin in solution was
investigated using 2D-NMR. The complete sequence-specific assignments of proton
resonance in the (1)H-NMR spectra of HWTX-II were obtained by analyzing a
series of 2D spectrum, including COSY, DQF-COSY, TOCSY and NOESY. All the
backbone protons and side chain protons, except epsilonNH(2) protons of Lys
residues, were identified by d(alphaN), d(alpha&dgr);, d(NN) and d(betaN)
connectivities. The results provide a basis for further determination of the
solution conformation of HWTX-II. Furthermore the secondary structure of
HWTX-II was determined from NMR data. It contained mainly extended
conformation, especially a double-stranded anti-parallel beta-sheet with
Trp27--Cys29 and Cys34--Lys36 at the C terminal, and it lacked helix. These
characters of the secondary structure of HWTX-II were similar to those spider
toxins which structure in solution had been reported.
;

save_


save_ref_2
   _Saveframe_category           citation

   _Citation_full
;
Q.SHU,R.H.HUANG,S.P.LIANG
Assignment of disulfide bonds of huwentoxin-ii by Edman
degradation sequencing and stepwise thiol modification.
Eur. J. Biochem. 2001, 268(8):2301-2307
;
   _Citation_title
;
Assignment of the disulfide bonds of huwentoxin-II by Edman degradation sequencing and stepwise thiol modification.
;
   _Citation_status              published
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              .
   _PubMed_ID                    11298747

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Shu   Q . .
      2 Huang R . .
      3 Liang S . .

   stop_

   _Journal_abbreviation        'Eur. J. Biochem.'
   _Journal_name_full           'European journal of biochemistry / FEBS'
   _Journal_volume               268
   _Journal_issue                8
   _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                   2301
   _Page_last                    2307
   _Year                         2001
   _Details
;
A novel strategy combining Edman degradation and thiol modification was
developed to assign the three disulfides of huwentoxin-II (HWTX-II), an
insecticidal peptide purified from the venom of the spider Selenocosmia huwena.
Phenylthiohydantoin (Pth) derivatives of Cys and the elimination product,
dehydroalanine (DeltaSer), can be observed in the Cys cycles during Edman
degradation of native HWTX-II. The appearance of two products indicates that
the disulfides of HWTX-II were split and that the free thiol group of the
second half cystine has been generated. Information about the nature of the
disulfide bridges of HWTX-II could be obtained from the sequencing signal if
the nascent thiols were modified stepwise by 4-vinylpyridine. Using this method
the disulfide bridges of HWTX-II were assigned as Cys4-Cys18, Cys8-Cys29 and
Cys23-Cys34, which is different from that seen in HWTX-I, a neurotoxic peptide
from the same spider. Using this strategy, one can assign the disulfide bonds
of small proteins by sequencing and modification n - 1 times, where n is the
number of disulfide bonds in the protein. The above assignment of the disulfide
bonds of HWTX-II was confirmed by MALDI-TOF MS of tryptic fragments of HWTX-II.
Some disulfide interchanging during proteolysis was observed by monitoring the
kinetics of proteolysis of HWTX-II by MALDI-TOF MS.
;

save_


save_ref_3
   _Saveframe_category           citation

   _Citation_full
;
Purification and characterization of huwentoxin-II,
a neurotoxic peptide from the venom of the Chinese
bird spider Selenocosmia huwena.
J. Pept. Res. 1999 May;53(5):486-491
;
   _Citation_title
;
Purification and characterization of huwentoxin-II, a neurotoxic peptide from the venom of the Chinese bird spider Selenocosmia huwena.
;
   _Citation_status              published
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              .
   _PubMed_ID                    10424342

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Shu    Q    .  .
      2 Liang 'S P' P. .

   stop_

   _Journal_abbreviation        'J. Pept. Res.'
   _Journal_name_full           'The journal of peptide research : official journal of the American Peptide Society'
   _Journal_volume               53
   _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                   486
   _Page_last                    491
   _Year                         1999
   _Details
;
A neurotoxic peptide, huwentoxin-II (HWTX-II), was purified from the venom of
the Chinese bird spider Selenocosmia huwena by ion exchange chromatography and
reversed phase HPLC. The toxin can reversibly paralyse cockroaches for several
hours, with an ED50 of 127 +/- 54 microg/g. HWTX-II blocks neuromuscular
transmission in an isolated mouse phrenic nerve diaphragm preparation and acts
cooperatively to potentiate the activity of huwentoxin-I. The complete amino
sequence of HWTX-II was determined and found to consist of 37 amino acid
residues, including six Cys residues. There is microheterogeneity (Ile/Gln) in
position 10, and mass spectrometry indicated that the two isoproteins have a
tendency to dimerize. It was determined by mass spectrometry that the six Cys
residues are involved in three disulphide bonds. The sequence of HWTX-II is
highly homologous with ESTX, a toxin from the tarantula Eurypefina
californicum.
;

save_


##################################
#  Molecular system description  #
##################################

save_system_HWTX-II
   _Saveframe_category         molecular_system

   _Mol_system_name            HUWENTOXIN-II
   _Abbreviation_common        HWTX-II
   _Enzyme_commission_number   .

   loop_
      _Mol_system_component_name
      _Mol_label

      'HUWENTOXIN-II(Ile, 10)' $HUWENTOXIN-II

   stop_

   _System_molecular_weight    .
   _System_physical_state      native
   _System_oligomer_state      monomer
   _System_paramagnetic        no
   _System_thiol_state        'all disulfide bound'

   loop_
      _Biological_function

      neurotoxin

   stop_

   _Database_query_date        .
   _Details                    .

save_


    ########################
    #  Monomeric polymers  #
    ########################

save_HUWENTOXIN-II
   _Saveframe_category                          monomeric_polymer

   _Mol_type                                    polymer
   _Mol_polymer_class                           protein
   _Name_common                                 Huwentoxin-II
   _Abbreviation_common                         HWTX-II
   _Molecular_mass                              4284.3
   _Mol_thiol_state                            'all disulfide bound'
   _Details                                     .

   	##############################
   	#  Polymer residue sequence  #
   	##############################

      _Residue_count                               37
   _Mol_residue_sequence
;
LFECSFSCEIEKEGDKPCKK
KKCKGGWKCKFNMCVKV
;

   loop_
      _Residue_seq_code
      _Residue_label

       1 LEU   2 PHE   3 GLU   4 CYS   5 SER
       6 PHE   7 SER   8 CYS   9 GLU  10 ILE
      11 GLU  12 LYS  13 GLU  14 GLY  15 ASP
      16 LYS  17 PRO  18 CYS  19 LYS  20 LYS
      21 LYS  22 LYS  23 CYS  24 LYS  25 GLY
      26 GLY  27 TRP  28 LYS  29 CYS  30 LYS
      31 PHE  32 ASN  33 MET  34 CYS  35 VAL
      36 LYS  37 VAL

   stop_

   _Sequence_homology_query_date                2008-08-19
   _Sequence_homology_query_revised_last_date   2008-08-19

   loop_
      _Database_name
      _Database_accession_code
      _Database_entry_mol_name
      _Sequence_query_to_submitted_percentage
      _Sequence_subject_length
      _Sequence_identity
      _Sequence_positive
      _Sequence_homology_expectation_value

      PDB        1I25     'Three Dimensional Solution Structure Of Huwentoxin-Ii By 2d 1h-Nmr' 100.00 37 100.00 100.00 1.67e-11
      GenBank    AAP33076 'huwentoxin-II precursor [Ornithoctonus huwena]'                     100.00 85 100.00 100.00 4.89e-13
      GenBank    ABY77725 'HWTX-IIa precursor [Ornithoctonus huwena]'                           97.30 85 100.00 100.00 2.00e-12
      GenBank    ABY77726 'HWTX-IIb precursor [Ornithoctonus huwena]'                          100.00 85 100.00 100.00 4.89e-13
      GenBank    ABY77727 'HWTX-IIc precursor [Ornithoctonus huwena]'                           97.30 85 100.00 100.00 1.89e-12
      GenBank    ABY77732 'HWTX-VIIIa precursor [Ornithoctonus huwena]'                         97.30 84 100.00 100.00 2.23e-12
      SWISS-PROT P68421   'Huwentoxin-7 precursor (Huwentoxin-VII) (HwTx-VII)'                 100.00 84 100.00 100.00 5.78e-13
      SWISS-PROT P82959   'Huwentoxin-2 form 1 precursor (Huwentoxin-II) (HwTx-II)'            100.00 85 100.00 100.00 4.89e-13

   stop_

save_


    ####################
    #  Natural source  #
    ####################

save_natural_source
   _Saveframe_category   natural_source


   loop_
      _Mol_label
      _Organism_name_common
      _NCBI_taxonomy_ID
      _Superkingdom
      _Kingdom
      _Genus
      _Species
      _Organ

      $HUWENTOXIN-II 'Chinese bird spider' 29017 Eukaryota Metazoa Selenocosmia huwena 'venom gland'

   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

      $HUWENTOXIN-II 'purified from the natural source' . . . . .

   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

      $HUWENTOXIN-II      4 mM .
      'phosphate buffer' 20 mM .
       H2O               90 %  .
       D2O               10 %  .

   stop_

save_


save_sample_2
   _Saveframe_category   sample

   _Sample_type          solution
   _Details              .

   loop_
      _Mol_label
      _Concentration_value
      _Concentration_value_units
      _Isotopic_labeling

      $HUWENTOXIN-II       4 mM .
      'phosphate buffer'  20 mM .
       D2O               100 %  .

   stop_

save_


############################
#  Computer software used  #
############################

save_FELIX
   _Saveframe_category   software

   _Name                 FELIX
   _Version              98.0

   loop_
      _Task

      'data analysis'

   stop_

   _Details             'Molecular Simulations, Inc.'

save_


save_X-PLOR
   _Saveframe_category   software

   _Name                 X-PLOR
   _Version              3.851

   loop_
      _Task

      refinement

   stop_

   _Details              Brunger

save_


#########################
#  Experimental detail  #
#########################

    ##################################
    #  NMR Spectrometer definitions  #
    ##################################

save_NMR_spectrometer
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                DMX
   _Field_strength       500
   _Details              .

save_


    #############################
    #  NMR applied experiments  #
    #############################

save_NOESY_1
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      NOESY
   _Sample_label         .

save_


save_DQF-COSY_2
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      DQF-COSY
   _Sample_label         .

save_


save_TOCSY_3
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      TOCSY
   _Sample_label         .

save_


save_E-COSY_4
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      E-COSY
   _Sample_label         .

save_


#######################
#  Sample conditions  #
#######################

save_sample_cond_1
   _Saveframe_category   sample_conditions

   _Details              .

   loop_
      _Variable_type
      _Variable_value
      _Variable_value_error
      _Variable_value_units

      'ionic strength'  20   0.02 mM
       pH                5.4 0.2  n/a
       pressure          1    .   atm
       temperature     300   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

      TSP H 1 'methyl protons' ppm 0.00 internal direct cylindrical internal .

   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_shift_set_1
   _Saveframe_category               assigned_chemical_shifts

   _Details                          .

   loop_
      _Experiment_label

      NOESY

   stop_

   loop_
      _Sample_label

      $sample_1

   stop_

   _Sample_conditions_label         $sample_cond_1
   _Chem_shift_reference_set_label  $chemical_shift_reference
   _Mol_system_component_name       'HUWENTOXIN-II(Ile, 10)'
   _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 LEU HA   H  3.93 0.02 1
        2 .  1 LEU HB2  H  1.56 0.02 1
        3 .  1 LEU HB3  H  1.56 0.02 1
        4 .  1 LEU HG   H  1.59 0.02 1
        5 .  1 LEU HD1  H  0.78 0.02 2
        6 .  1 LEU HD2  H  0.80 0.02 2
        7 .  2 PHE H    H  8.48 0.02 1
        8 .  2 PHE HA   H  4.77 0.02 1
        9 .  2 PHE HB2  H  3.00 0.02 2
       10 .  2 PHE HB3  H  3.25 0.02 2
       11 .  2 PHE HD1  H  7.33 0.02 1
       12 .  2 PHE HD2  H  7.33 0.02 1
       13 .  2 PHE HE1  H  7.37 0.02 1
       14 .  2 PHE HE2  H  7.37 0.02 1
       15 .  2 PHE HZ   H  7.32 0.02 1
       16 .  3 GLU H    H  8.73 0.02 1
       17 .  3 GLU HA   H  4.54 0.02 1
       18 .  3 GLU HB2  H  1.96 0.02 1
       19 .  3 GLU HB3  H  1.96 0.02 1
       20 .  3 GLU HG2  H  2.25 0.02 2
       21 .  3 GLU HG3  H  2.57 0.02 2
       22 .  4 CYS H    H  9.60 0.02 1
       23 .  4 CYS HA   H  4.31 0.02 1
       24 .  4 CYS HB2  H  2.61 0.02 2
       25 .  4 CYS HB3  H  3.50 0.02 2
       26 .  5 SER H    H  9.95 0.02 1
       27 .  5 SER HA   H  4.06 0.02 1
       28 .  5 SER HB2  H  3.51 0.02 2
       29 .  5 SER HB3  H  3.81 0.02 2
       30 .  6 PHE H    H  9.75 0.02 1
       31 .  6 PHE HA   H  4.69 0.02 1
       32 .  6 PHE HB2  H  3.06 0.02 2
       33 .  6 PHE HB3  H  3.19 0.02 2
       34 .  6 PHE HD1  H  7.26 0.02 1
       35 .  6 PHE HD2  H  7.26 0.02 1
       36 .  6 PHE HE1  H  7.36 0.02 1
       37 .  6 PHE HE2  H  7.36 0.02 1
       38 .  6 PHE HZ   H  7.44 0.02 1
       39 .  7 SER H    H  7.96 0.02 1
       40 .  7 SER HA   H  4.48 0.02 1
       41 .  7 SER HB2  H  3.93 0.02 1
       42 .  7 SER HB3  H  3.93 0.02 1
       43 .  8 CYS H    H  7.48 0.02 1
       44 .  8 CYS HA   H  5.27 0.02 1
       45 .  8 CYS HB2  H  2.57 0.02 2
       46 .  8 CYS HB3  H  3.61 0.02 2
       47 .  9 GLU H    H  9.29 0.02 1
       48 .  9 GLU HA   H  4.57 0.02 1
       49 .  9 GLU HB2  H  2.20 0.02 1
       50 .  9 GLU HB3  H  2.20 0.02 1
       51 .  9 GLU HG2  H  2.31 0.02 1
       52 .  9 GLU HG3  H  2.31 0.02 1
       53 . 10 ILE H    H  8.09 0.02 1
       54 . 10 ILE HA   H  4.24 0.02 1
       55 . 10 ILE HB   H  2.01 0.02 1
       56 . 10 ILE HG12 H  1.22 0.02 2
       57 . 10 ILE HG13 H  1.55 0.02 2
       58 . 10 ILE HG2  H  1.03 0.02 1
       59 . 10 ILE HD1  H  0.91 0.02 1
       60 . 11 GLU H    H  8.44 0.02 1
       61 . 11 GLU HA   H  4.47 0.02 1
       62 . 11 GLU HB2  H  1.88 0.02 2
       63 . 11 GLU HB3  H  2.79 0.02 2
       64 . 11 GLU HG2  H  2.03 0.02 2
       65 . 11 GLU HG3  H  2.39 0.02 2
       66 . 12 LYS H    H  7.80 0.02 1
       67 . 12 LYS HA   H  4.92 0.02 1
       68 . 12 LYS HB2  H  1.55 0.02 2
       69 . 12 LYS HB3  H  1.64 0.02 2
       70 . 12 LYS HG2  H  1.09 0.02 2
       71 . 12 LYS HG3  H  1.18 0.02 2
       72 . 12 LYS HD2  H  1.56 0.02 1
       73 . 12 LYS HD3  H  1.56 0.02 1
       74 . 12 LYS HE2  H  2.84 0.02 1
       75 . 12 LYS HE3  H  2.84 0.02 1
       76 . 13 GLU H    H  8.45 0.02 1
       77 . 13 GLU HA   H  4.49 0.02 1
       78 . 13 GLU HB2  H  2.07 0.02 1
       79 . 13 GLU HB3  H  2.07 0.02 1
       80 . 13 GLU HG2  H  2.34 0.02 1
       81 . 13 GLU HG3  H  2.34 0.02 1
       82 . 14 GLY H    H  9.20 0.02 1
       83 . 14 GLY HA2  H  3.79 0.02 2
       84 . 14 GLY HA3  H  3.98 0.02 2
       85 . 15 ASP H    H  8.80 0.02 1
       86 . 15 ASP HA   H  4.52 0.02 1
       87 . 15 ASP HB2  H  2.76 0.02 2
       88 . 15 ASP HB3  H  2.87 0.02 2
       89 . 16 LYS H    H  7.88 0.02 1
       90 . 16 LYS HA   H  4.94 0.02 1
       91 . 16 LYS HB2  H  1.94 0.02 1
       92 . 16 LYS HB3  H  1.94 0.02 1
       93 . 16 LYS HG2  H  1.51 0.02 2
       94 . 16 LYS HG3  H  1.58 0.02 2
       95 . 16 LYS HD2  H  1.77 0.02 1
       96 . 16 LYS HD3  H  1.77 0.02 1
       97 . 16 LYS HE2  H  3.08 0.02 1
       98 . 16 LYS HE3  H  3.08 0.02 1
       99 . 17 PRO HA   H  4.92 0.02 1
      100 . 17 PRO HB2  H  1.90 0.02 2
      101 . 17 PRO HB3  H  2.40 0.02 2
      102 . 17 PRO HG2  H  2.00 0.02 2
      103 . 17 PRO HG3  H  2.12 0.02 2
      104 . 17 PRO HD2  H  3.77 0.02 2
      105 . 17 PRO HD3  H  3.98 0.02 2
      106 . 18 CYS H    H  7.96 0.02 1
      107 . 18 CYS HA   H  4.65 0.02 1
      108 . 18 CYS HB2  H  3.02 0.02 2
      109 . 18 CYS HB3  H  3.06 0.02 2
      110 . 19 LYS H    H  8.50 0.02 1
      111 . 19 LYS HA   H  4.46 0.02 1
      112 . 19 LYS HB2  H  1.49 0.02 2
      113 . 19 LYS HB3  H  1.61 0.02 2
      114 . 19 LYS HG2  H  1.38 0.02 2
      115 . 19 LYS HG3  H  1.68 0.02 2
      116 . 19 LYS HD2  H  1.49 0.02 1
      117 . 19 LYS HD3  H  1.49 0.02 1
      118 . 19 LYS HE2  H  2.95 0.02 1
      119 . 19 LYS HE3  H  2.95 0.02 1
      120 . 20 LYS H    H  8.93 0.02 1
      121 . 20 LYS HA   H  3.72 0.02 1
      122 . 20 LYS HB2  H  1.44 0.02 1
      123 . 20 LYS HB3  H  1.44 0.02 1
      124 . 20 LYS HG2  H  1.22 0.02 2
      125 . 20 LYS HG3  H  1.31 0.02 2
      126 . 20 LYS HD2  H  1.60 0.02 1
      127 . 20 LYS HD3  H  1.60 0.02 1
      128 . 20 LYS HE2  H  2.94 0.02 1
      129 . 20 LYS HE3  H  2.94 0.02 1
      130 . 21 LYS H    H  8.43 0.02 1
      131 . 21 LYS HA   H  4.06 0.02 1
      132 . 21 LYS HB2  H  1.26 0.02 2
      133 . 21 LYS HB3  H  1.41 0.02 2
      134 . 21 LYS HG2  H  1.01 0.02 2
      135 . 21 LYS HG3  H  1.08 0.02 2
      136 . 21 LYS HD2  H  1.30 0.02 2
      137 . 21 LYS HD3  H  1.38 0.02 2
      138 . 21 LYS HE2  H  2.88 0.02 1
      139 . 21 LYS HE3  H  2.88 0.02 1
      140 . 22 LYS H    H  8.24 0.02 1
      141 . 22 LYS HA   H  4.34 0.02 1
      142 . 22 LYS HB2  H  1.69 0.02 2
      143 . 22 LYS HB3  H  1.75 0.02 2
      144 . 22 LYS HG2  H  1.42 0.02 2
      145 . 22 LYS HG3  H  1.52 0.02 2
      146 . 22 LYS HD2  H  1.69 0.02 1
      147 . 22 LYS HD3  H  1.69 0.02 1
      148 . 22 LYS HE2  H  3.04 0.02 1
      149 . 22 LYS HE3  H  3.04 0.02 1
      150 . 23 CYS H    H  8.89 0.02 1
      151 . 23 CYS HA   H  4.66 0.02 1
      152 . 23 CYS HB2  H  2.55 0.02 2
      153 . 23 CYS HB3  H  3.10 0.02 2
      154 . 24 LYS H    H  8.56 0.02 1
      155 . 24 LYS HA   H  4.18 0.02 1
      156 . 24 LYS HB2  H  1.38 0.02 2
      157 . 24 LYS HB3  H  1.72 0.02 2
      158 . 24 LYS HG2  H  1.30 0.02 1
      159 . 24 LYS HG3  H  1.30 0.02 1
      160 . 24 LYS HD2  H  1.36 0.02 2
      161 . 24 LYS HD3  H  1.44 0.02 2
      162 . 24 LYS HE2  H  2.71 0.02 1
      163 . 24 LYS HE3  H  2.71 0.02 1
      164 . 25 GLY H    H  8.50 0.02 1
      165 . 25 GLY HA2  H  3.84 0.02 2
      166 . 25 GLY HA3  H  4.05 0.02 2
      167 . 26 GLY H    H  8.96 0.02 1
      168 . 26 GLY HA2  H  3.70 0.02 2
      169 . 26 GLY HA3  H  4.43 0.02 2
      170 . 27 TRP H    H  8.74 0.02 1
      171 . 27 TRP HA   H  5.27 0.02 1
      172 . 27 TRP HB2  H  2.96 0.02 2
      173 . 27 TRP HB3  H  3.55 0.02 2
      174 . 27 TRP HD1  H  7.13 0.02 1
      175 . 27 TRP HE1  H 10.38 0.02 1
      176 . 27 TRP HE3  H  7.15 0.02 1
      177 . 27 TRP HZ2  H  7.52 0.02 1
      178 . 27 TRP HZ3  H  7.17 0.02 1
      179 . 27 TRP HH2  H  7.27 0.02 1
      180 . 28 LYS H    H  9.69 0.02 1
      181 . 28 LYS HA   H  4.75 0.02 1
      182 . 28 LYS HB2  H  1.66 0.02 2
      183 . 28 LYS HB3  H  1.72 0.02 2
      184 . 28 LYS HG2  H  1.28 0.02 2
      185 . 28 LYS HG3  H  1.34 0.02 2
      186 . 28 LYS HD2  H  1.64 0.02 1
      187 . 28 LYS HD3  H  1.64 0.02 1
      188 . 28 LYS HE2  H  2.91 0.02 1
      189 . 28 LYS HE3  H  2.91 0.02 1
      190 . 29 CYS H    H  8.90 0.02 1
      191 . 29 CYS HA   H  5.07 0.02 1
      192 . 29 CYS HB2  H  3.01 0.02 2
      193 . 29 CYS HB3  H  3.10 0.02 2
      194 . 30 LYS H    H  9.68 0.02 1
      195 . 30 LYS HA   H  4.41 0.02 1
      196 . 30 LYS HB2  H  1.52 0.02 2
      197 . 30 LYS HB3  H  1.66 0.02 2
      198 . 30 LYS HG2  H  1.01 0.02 2
      199 . 30 LYS HG3  H  1.14 0.02 2
      200 . 30 LYS HD2  H  1.54 0.02 1
      201 . 30 LYS HD3  H  1.54 0.02 1
      202 . 30 LYS HE2  H  2.76 0.02 1
      203 . 30 LYS HE3  H  2.76 0.02 1
      204 . 31 PHE H    H  9.10 0.02 1
      205 . 31 PHE HA   H  4.34 0.02 1
      206 . 31 PHE HB2  H  3.26 0.02 2
      207 . 31 PHE HB3  H  3.32 0.02 2
      208 . 31 PHE HD1  H  7.30 0.02 1
      209 . 31 PHE HD2  H  7.30 0.02 1
      210 . 31 PHE HE1  H  7.41 0.02 1
      211 . 31 PHE HE2  H  7.41 0.02 1
      212 . 31 PHE HZ   H  7.35 0.02 1
      213 . 32 ASN H    H  8.76 0.02 1
      214 . 32 ASN HA   H  4.29 0.02 1
      215 . 32 ASN HB2  H  2.56 0.02 2
      216 . 32 ASN HB3  H  3.65 0.02 2
      217 . 32 ASN HD21 H  7.29 0.02 2
      218 . 32 ASN HD22 H  7.89 0.02 2
      219 . 33 MET H    H  7.90 0.02 1
      220 . 33 MET HA   H  5.06 0.02 1
      221 . 33 MET HB2  H  2.13 0.02 1
      222 . 33 MET HB3  H  2.13 0.02 1
      223 . 33 MET HG2  H  2.68 0.02 2
      224 . 33 MET HG3  H  2.76 0.02 2
      225 . 33 MET HE   H  2.16 0.02 1
      226 . 34 CYS H    H  9.27 0.02 1
      227 . 34 CYS HA   H  5.37 0.02 1
      228 . 34 CYS HB2  H  2.91 0.02 2
      229 . 34 CYS HB3  H  3.04 0.02 2
      230 . 35 VAL H    H  9.87 0.02 1
      231 . 35 VAL HA   H  4.80 0.02 1
      232 . 35 VAL HB   H  2.18 0.02 1
      233 . 35 VAL HG1  H  1.00 0.02 2
      234 . 35 VAL HG2  H  1.07 0.02 2
      235 . 36 LYS H    H  8.13 0.02 1
      236 . 36 LYS HA   H  3.30 0.02 1
      237 . 36 LYS HB2  H  0.40 0.02 2
      238 . 36 LYS HB3  H  1.23 0.02 2
      239 . 36 LYS HG2  H  0.54 0.02 2
      240 . 36 LYS HG3  H  0.74 0.02 2
      241 . 36 LYS HD2  H  1.15 0.02 1
      242 . 36 LYS HD3  H  1.15 0.02 1
      243 . 36 LYS HE2  H  2.79 0.02 1
      244 . 36 LYS HE3  H  2.79 0.02 1
      245 . 37 VAL H    H  7.58 0.02 1
      246 . 37 VAL HA   H  3.82 0.02 1
      247 . 37 VAL HB   H  1.96 0.02 1
      248 . 37 VAL HG1  H  0.76 0.02 2
      249 . 37 VAL HG2  H  0.85 0.02 2

   stop_

save_