data_5213

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

save_entry_information
   _Saveframe_category      entry_information

   _Entry_title
;
Copper Trafficking: The Solution Structure of Bacillus subtilis CopZ
;
   _BMRB_accession_number   5213
   _BMRB_flat_file_name     bmr5213.str
   _Entry_type              original
   _Submission_date         2001-11-20
   _Accession_date          2001-11-20
   _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  Banci       L. .  .
      2  Bertini     I. .  .
      3 'Del Conte'  R. .  .
      4  Markey      J. .  .
      5  Ruiz-Duenas J. F. .

   stop_

   loop_
      _Saveframe_category_type
      _Saveframe_category_type_count

      assigned_chemical_shifts 1

   stop_

   loop_
      _Data_type
      _Data_type_count

      "1H chemical shifts"  373
      "15N chemical shifts"  73

   stop_

   loop_
      _Revision_date
      _Revision_keyword
      _Revision_author
      _Revision_detail

      2002-02-14 original BMRB .

   stop_

   _Original_release_date   2001-11-20

save_


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

save_entry_citation
   _Saveframe_category           entry_citation

   _Citation_full                .
   _Citation_title
;
Copper Trafficking: The Solution Structure of Bacillus subtilis CopZ
;
   _Citation_status              published
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              21614397
   _PubMed_ID                    11747441

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1  Banci       L. .  .
      2  Bertini     I. .  .
      3 'Del Conte'  R. .  .
      4  Markey      J. .  .
      5  Ruiz-Duenas F. J. .

   stop_

   _Journal_abbreviation         Biochemistry
   _Journal_volume               40
   _Journal_issue                51
   _Journal_CSD                  .
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_ISBN                    .
   _Conference_state_province    .
   _Conference_abstract_number   .
   _Page_first                   15660
   _Page_last                    15668
   _Year                         2001
   _Details                      .

   loop_
      _Keyword

      beta-alpha-beta-beta-alpha-beta

   stop_

save_


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

save_system_CopZ
   _Saveframe_category         molecular_system

   _Mol_system_name           'CopZ from Bacillus subtilis'
   _Abbreviation_common        CopZ
   _Enzyme_commission_number   .

   loop_
      _Mol_system_component_name
      _Mol_label

      'CopZ from Bacillus subtilis' $CopZ
      'COPPER (I) ION'              $entity_CU1

   stop_

   _System_molecular_weight    .
   _System_physical_state      native
   _System_oligomer_state      ?
   _System_paramagnetic        no
   _System_thiol_state        'all other bound'

   loop_
      _Biological_function

      'copper-transport in Bacillus subtilis'

   stop_

   _Database_query_date        .
   _Details                    .

save_


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

save_CopZ
   _Saveframe_category                          monomeric_polymer

   _Mol_type                                    polymer
   _Mol_polymer_class                           protein
   _Name_common                                'CopZ from Bacillus subtilis'
   _Abbreviation_common                         CopZ
   _Molecular_mass                              7826
   _Mol_thiol_state                            'all other bound'
   _Details                                     .

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

      _Residue_count                               73
   _Mol_residue_sequence
;
MEQKTLQVEGMSCQHCVKAV
ETSVGELDGVSAVHVNLEAG
KVDVSFDADKVSVKDIADAI
EDQGYDVAKIEGR
;

   loop_
      _Residue_seq_code
      _Residue_label

       1 MET   2 GLU   3 GLN   4 LYS   5 THR
       6 LEU   7 GLN   8 VAL   9 GLU  10 GLY
      11 MET  12 SER  13 CYS  14 GLN  15 HIS
      16 CYS  17 VAL  18 LYS  19 ALA  20 VAL
      21 GLU  22 THR  23 SER  24 VAL  25 GLY
      26 GLU  27 LEU  28 ASP  29 GLY  30 VAL
      31 SER  32 ALA  33 VAL  34 HIS  35 VAL
      36 ASN  37 LEU  38 GLU  39 ALA  40 GLY
      41 LYS  42 VAL  43 ASP  44 VAL  45 SER
      46 PHE  47 ASP  48 ALA  49 ASP  50 LYS
      51 VAL  52 SER  53 VAL  54 LYS  55 ASP
      56 ILE  57 ALA  58 ASP  59 ALA  60 ILE
      61 GLU  62 ASP  63 GLN  64 GLY  65 TYR
      66 ASP  67 VAL  68 ALA  69 LYS  70 ILE
      71 GLU  72 GLY  73 ARG

   stop_

   _Sequence_homology_query_date                .
   _Sequence_homology_query_revised_last_date   .

save_


    #############
    #  Ligands  #
    #############

save_CU1
   _Saveframe_category             ligand

   _Mol_type                      "non-polymer (NON-POLYMER)"
   _Name_common                   'COPPER (I) ION'
   _BMRB_code                      CU1
   _PDB_code                       CU1
   _Molecular_mass                 63.546
   _Mol_charge                     1
   _Mol_paramagnetic               .
   _Mol_aromatic                   no
   _Details                        .

   loop_
      _Atom_name
      _PDB_atom_name
      _Atom_type
      _Atom_chirality
      _Atom_charge
      _Atom_oxidation_number
      _Atom_unpaired_electrons

      CU CU CU . 1 . ?

   stop_

   _Mol_thiol_state                .
   _Sequence_homology_query_date   .

save_


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

save_natural_source
   _Saveframe_category   natural_source


   loop_
      _Mol_label
      _Organism_name_common
      _NCBI_taxonomy_ID
      _Superkingdom
      _Kingdom
      _Genus
      _Species

      $CopZ 'Bacillus subtilis' 1423 Bacteria . Bacillus subtilis

   stop_

save_


    #########################
    #  Experimental source  #
    #########################

save_experimental_source
   _Saveframe_category   experimental_source


   loop_
      _Mol_label
      _Production_method
      _Host_organism_name_common
      _Genus
      _Species
      _Strain
      _Vector_type
      _Vector_name

      $CopZ 'recombinant technology' 'B. subtilis' Bacillus subtilis . plasmid pET21

   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

      $CopZ                  2 mM '[U-99% 15N]'
      $entity_CU1            2 mM  .
      'phosphate buffer'   100 mM  .
       DTT               trace  mM  .
       D2O                  10 %   .
       H2O                  90 %   .

   stop_

save_


save_sample_2
   _Saveframe_category   sample

   _Sample_type          solution
   _Details              .

   loop_
      _Mol_label
      _Concentration_value
      _Concentration_value_units
      _Isotopic_labeling

      $CopZ                  2 mM .
      $entity_CU1            2 mM .
      'phosphate buffer'   100 mM .
       DTT               trace  mM .
       D2O                  10 %  .
       H2O                  90 %  .

   stop_

save_


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

save_DYANA
   _Saveframe_category   software

   _Name                 DYANA
   _Version              1.5

   loop_
      _Task

      'solution structure calculation'

   stop_

   _Details             'Guenter et al. 1997'

save_


save_XWINNMR
   _Saveframe_category   software

   _Name                 xwinnmr
   _Version              2.6

   loop_
      _Task

      'NMR experiments collection'

   stop_

   _Details              .

save_


save_XEASY
   _Saveframe_category   software

   _Name                 XEASY
   _Version              1.3.13

   loop_
      _Task

      'data analysis'

   stop_

   _Details             'Eccles et al. 1991'

save_


save_AMBER
   _Saveframe_category   software

   _Name                 AMBER
   _Version              5.0

   loop_
      _Task

      'solution structure refinement'

   stop_

   _Details             'Pearlman et al. 1997'

save_


save_molmol
   _Saveframe_category   software

   _Name                 Molmol
   _Version              2.4

   loop_
      _Task

      'data analysis'

   stop_

   _Details             'Koradi et al. 1996'

save_


save_CORMA
   _Saveframe_category   software

   _Name                 CORMA
   _Version              .

   loop_
      _Task

      'data analysis'

   stop_

   _Details             'Borgias et al. 1989'

save_


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

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

save_NMR_spectrometer
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                AVANCE
   _Field_strength       700
   _Details              .

save_


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

save_3D_TOSCY-HMQC_1
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D TOSCY-HMQC'
   _Sample_label         .

save_


save_3D_NOESY-HSQC_2
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D NOESY-HSQC'
   _Sample_label         .

save_


save_3D_HNHA_3
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D HNHA'
   _Sample_label         .

save_


save_2D_TOSCY_4
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '2D TOSCY'
   _Sample_label         .

save_


save_2D_NOESY_5
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '2D NOESY'
   _Sample_label         .

save_


save_2D_HSQC_6
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '2D HSQC'
   _Sample_label         .

save_


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

save_sample_cond_1
   _Saveframe_category   sample_conditions

   _Details             'The samples were kept under reduction conditions with DTT in an inert atmophere.'

   loop_
      _Variable_type
      _Variable_value
      _Variable_value_error
      _Variable_value_units

      pH            7.0 0.01 na
      pressure      1    .   atm
      temperature 300   0.5  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

      TMS H  1 'methyl protons' ppm 0.0 . direct   . . . 1.000000000
      TMS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118

   stop_

save_


	###################################
	#  Assigned chemical shift lists  #
	###################################

###################################################################
#       Chemical Shift Ambiguity Index Value Definitions          #
#                                                                 #
# The values other than 1 are used for those atoms with different #
# chemical shifts that cannot be assigned to stereospecific atoms #
# or to specific residues or chains.                              #
#                                                                 #
#   Index Value            Definition                             #
#                                                                 #
#      1             Unique (including isolated methyl protons,   #
#                         geminal atoms, and geminal methyl       #
#                         groups with identical chemical shifts)  #
#                         (e.g. ILE HD11, HD12, HD13 protons)     #
#      2             Ambiguity of geminal atoms or geminal methyl #
#                         proton groups (e.g. ASP HB2 and HB3     #
#                         protons, LEU CD1 and CD2 carbons, or    #
#                         LEU HD11, HD12, HD13 and HD21, HD22,    #
#                         HD23 methyl protons)                    #
#      3             Aromatic atoms on opposite sides of          #
#                         symmetrical rings (e.g. TYR HE1 and HE2 #
#                         protons)                                #
#      4             Intraresidue ambiguities (e.g. LYS HG and    #
#                         HD protons or TRP HZ2 and HZ3 protons)  #
#      5             Interresidue ambiguities (LYS 12 vs. LYS 27) #
#      6             Intermolecular ambiguities (e.g. ASP 31 CA   #
#                         in monomer 1 and ASP 31 CA in monomer 2 #
#                         of an asymmetrical homodimer, duplex    #
#                         DNA assignments, or other assignments   #
#                         that may apply to atoms in one or more  #
#                         molecule in the molecular assembly)     #
#      9             Ambiguous, specific ambiguity not defined    #
#                                                                 #
###################################################################
save_chemical_shift_set_1
   _Saveframe_category               assigned_chemical_shifts

   _Details                          .

   loop_
      _Experiment_label

      '3D TOSCY-HMQC'
      '3D NOESY-HSQC'
      '3D HNHA'
      '2D TOSCY'
      '2D NOESY'
      '2D HSQC'

   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       'CopZ from Bacillus subtilis'
   _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 MET HA   H   4.047 0.05 1
        2 .  1 MET HB2  H   1.901 0.05 1
        3 .  1 MET HB3  H   1.910 0.05 1
        4 .  1 MET HG2  H   2.401 0.05 1
        5 .  1 MET HG3  H   2.410 0.05 1
        6 .  2 GLU N    N 124.775 0.05 1
        7 .  2 GLU H    H   8.774 0.05 1
        8 .  2 GLU HA   H   4.308 0.05 1
        9 .  2 GLU HB2  H   1.910 0.05 1
       10 .  2 GLU HB3  H   1.840 0.05 1
       11 .  2 GLU HG2  H   1.140 0.05 1
       12 .  2 GLU HG3  H   0.843 0.05 1
       13 .  3 GLN N    N 119.957 0.05 1
       14 .  3 GLN H    H   8.271 0.05 1
       15 .  3 GLN HA   H   5.462 0.05 1
       16 .  3 GLN HB2  H   1.889 0.05 1
       17 .  3 GLN HB3  H   1.785 0.05 1
       18 .  3 GLN HG2  H   2.120 0.05 1
       19 .  3 GLN HG3  H   2.208 0.05 1
       20 .  4 LYS N    N 122.366 0.05 1
       21 .  4 LYS H    H   8.845 0.05 1
       22 .  4 LYS HA   H   4.804 0.05 1
       23 .  4 LYS HB2  H   1.726 0.05 1
       24 .  4 LYS HB3  H   1.730 0.05 1
       25 .  4 LYS HG2  H   1.255 0.05 2
       26 .  4 LYS HG3  H   1.260 0.05 2
       27 .  4 LYS HD2  H   1.450 0.05 1
       28 .  5 THR N    N 118.925 0.05 1
       29 .  5 THR H    H   8.716 0.05 1
       30 .  5 THR HA   H   5.187 0.05 1
       31 .  5 THR HB   H   3.640 0.05 1
       32 .  5 THR HG2  H   1.070 0.05 1
       33 .  6 LEU N    N 126.496 0.05 1
       34 .  6 LEU H    H   9.696 0.05 1
       35 .  6 LEU HA   H   4.698 0.05 1
       36 .  6 LEU HB2  H   2.915 0.05 1
       37 .  6 LEU HB3  H   2.920 0.05 1
       38 .  6 LEU HG   H   2.513 0.05 1
       39 .  7 GLN N    N 125.808 0.05 1
       40 .  7 GLN H    H   9.159 0.05 1
       41 .  7 GLN HA   H   4.785 0.05 1
       42 .  7 GLN HB2  H   1.926 0.05 1
       43 .  7 GLN HB3  H   2.108 0.05 1
       44 .  7 GLN HG2  H   2.257 0.05 1
       45 .  7 GLN HG3  H   2.228 0.05 1
       46 .  8 VAL N    N 127.184 0.05 1
       47 .  8 VAL H    H   8.778 0.05 1
       48 .  8 VAL HA   H   4.966 0.05 1
       49 .  8 VAL HB   H   1.520 0.05 1
       50 .  8 VAL HG1  H   0.810 0.05 1
       51 .  8 VAL HG2  H   0.696 0.05 1
       52 .  9 GLU N    N 127.873 0.05 1
       53 .  9 GLU H    H   9.511 0.05 1
       54 .  9 GLU HA   H   4.688 0.05 1
       55 .  9 GLU HB2  H   2.206 0.05 1
       56 .  9 GLU HB3  H   2.112 0.05 1
       57 .  9 GLU HG2  H   1.901 0.05 1
       58 .  9 GLU HG3  H   1.910 0.05 1
       59 . 10 GLY N    N 108.257 0.05 1
       60 . 10 GLY H    H   8.499 0.05 1
       61 . 10 GLY HA2  H   3.697 0.05 1
       62 . 10 GLY HA3  H   3.700 0.05 1
       63 . 11 MET N    N 121.334 0.05 1
       64 . 11 MET H    H   8.926 0.05 1
       65 . 11 MET HA   H   4.716 0.05 1
       66 . 11 MET HB2  H   2.209 0.05 1
       67 . 11 MET HB3  H   2.156 0.05 1
       68 . 11 MET HG2  H   1.789 0.05 1
       69 . 11 MET HG3  H   1.205 0.05 1
       70 . 11 MET HE   H   3.163 0.05 1
       71 . 12 SER N    N 121.334 0.05 1
       72 . 12 SER H    H   8.040 0.05 1
       73 . 12 SER HA   H   5.133 0.05 1
       74 . 12 SER HB2  H   3.410 0.05 1
       75 . 12 SER HB3  H   3.391 0.05 1
       76 . 12 SER HG   H   4.201 0.05 1
       77 . 13 CYS N    N 118.925 0.05 1
       78 . 13 CYS H    H  10.196 0.05 1
       79 . 13 CYS HA   H   4.751 0.05 1
       80 . 13 CYS HB2  H   3.410 0.05 1
       81 . 13 CYS HB3  H   2.399 0.05 1
       82 . 14 GLN N    N 116.860 0.05 1
       83 . 14 GLN H    H   8.856 0.05 1
       84 . 14 GLN HA   H   3.934 0.05 1
       85 . 14 GLN HB2  H   1.854 0.05 1
       86 . 14 GLN HB3  H   1.861 0.05 1
       87 . 14 GLN HG2  H   2.108 0.05 1
       88 . 14 GLN HG3  H   2.120 0.05 1
       89 . 15 HIS N    N 123.399 0.05 1
       90 . 15 HIS H    H   9.444 0.05 1
       91 . 15 HIS HA   H   4.348 0.05 1
       92 . 15 HIS HB2  H   3.175 0.05 1
       93 . 15 HIS HB3  H   3.182 0.05 1
       94 . 15 HIS HD2  H   7.730 0.05 1
       95 . 15 HIS HE1  H   7.570 0.05 1
       96 . 16 CYS N    N 124.431 0.05 1
       97 . 16 CYS H    H   8.033 0.05 1
       98 . 16 CYS HA   H   4.197 0.05 1
       99 . 16 CYS HB2  H   3.411 0.05 1
      100 . 16 CYS HB3  H   2.715 0.05 1
      101 . 17 VAL N    N 116.516 0.05 1
      102 . 17 VAL H    H   7.040 0.05 1
      103 . 17 VAL HA   H   3.087 0.05 1
      104 . 17 VAL HB   H   2.117 0.05 1
      105 . 17 VAL HG1  H   0.848 0.05 2
      106 . 17 VAL HG2  H   0.716 0.05 2
      107 . 18 LYS N    N 116.860 0.05 1
      108 . 18 LYS H    H   7.583 0.05 1
      109 . 18 LYS HA   H   4.040 0.05 1
      110 . 18 LYS HB2  H   1.799 0.05 1
      111 . 18 LYS HB3  H   1.809 0.05 1
      112 . 18 LYS HG2  H   1.395 0.05 1
      113 . 18 LYS HG3  H   1.408 0.05 1
      114 . 18 LYS HD2  H   1.600 0.05 1
      115 . 18 LYS HD3  H   1.580 0.05 1
      116 . 18 LYS HE2  H   4.130 0.05 1
      117 . 18 LYS HE3  H   4.141 0.05 1
      118 . 18 LYS NZ   N 124.090 0.05 1
      119 . 18 LYS HZ   H   8.390 0.05 1
      120 . 19 ALA N    N 123.399 0.05 1
      121 . 19 ALA H    H   8.028 0.05 1
      122 . 19 ALA HA   H   4.016 0.05 1
      123 . 19 ALA HB   H   1.556 0.05 1
      124 . 20 VAL N    N 118.925 0.05 1
      125 . 20 VAL H    H   7.862 0.05 1
      126 . 20 VAL HA   H   3.335 0.05 1
      127 . 20 VAL HB   H   1.860 0.05 1
      128 . 20 VAL HG1  H   0.743 0.05 2
      129 . 20 VAL HG2  H   0.550 0.05 2
      130 . 21 GLU N    N 117.893 0.05 1
      131 . 21 GLU H    H   8.776 0.05 1
      132 . 21 GLU HA   H   3.488 0.05 1
      133 . 21 GLU HB2  H   2.075 0.05 1
      134 . 21 GLU HB3  H   2.080 0.05 1
      135 . 21 GLU HG2  H   2.374 0.05 1
      136 . 21 GLU HG3  H   2.381 0.05 1
      137 . 22 THR N    N 113.419 0.05 1
      138 . 22 THR H    H   8.395 0.05 1
      139 . 22 THR HA   H   3.819 0.05 1
      140 . 22 THR HB   H   4.097 0.05 1
      141 . 22 THR HG2  H   1.109 0.05 1
      142 . 23 SER N    N 115.484 0.05 1
      143 . 23 SER H    H   7.565 0.05 1
      144 . 23 SER HA   H   4.041 0.05 1
      145 . 23 SER HB2  H   3.739 0.05 1
      146 . 23 SER HB3  H   3.749 0.05 1
      147 . 24 VAL N    N 118.925 0.05 1
      148 . 24 VAL H    H   8.074 0.05 1
      149 . 24 VAL HA   H   3.454 0.05 1
      150 . 24 VAL HB   H   1.829 0.05 1
      151 . 24 VAL HG1  H   0.709 0.05 1
      152 . 24 VAL HG2  H   0.678 0.05 1
      153 . 25 GLY N    N 103.439 0.05 1
      154 . 25 GLY H    H   7.471 0.05 1
      155 . 25 GLY HA2  H   3.705 0.05 1
      156 . 25 GLY HA3  H   3.536 0.05 1
      157 . 26 GLU N    N 115.484 0.05 1
      158 . 26 GLU H    H   7.044 0.05 1
      159 . 26 GLU HA   H   4.087 0.05 1
      160 . 26 GLU HB2  H   1.992 0.05 1
      161 . 26 GLU HB3  H   1.909 0.05 1
      162 . 26 GLU HG2  H   2.386 0.05 2
      163 . 26 GLU HG3  H   2.247 0.05 2
      164 . 27 LEU N    N 120.907 0.05 1
      165 . 27 LEU H    H   7.278 0.05 1
      166 . 27 LEU HA   H   4.069 0.05 1
      167 . 27 LEU HB2  H   1.942 0.05 2
      168 . 27 LEU HB3  H   1.822 0.05 2
      169 . 27 LEU HG   H   1.080 0.05 1
      170 . 27 LEU HD1  H   0.710 0.05 1
      171 . 27 LEU HD2  H   0.648 0.05 1
      172 . 28 ASP N    N 125.119 0.05 1
      173 . 28 ASP H    H   8.445 0.05 1
      174 . 28 ASP HA   H   4.259 0.05 1
      175 . 28 ASP HB2  H   2.598 0.05 2
      176 . 28 ASP HB3  H   2.515 0.05 2
      177 . 29 GLY N    N 109.978 0.05 1
      178 . 29 GLY H    H   8.357 0.05 1
      179 . 29 GLY HA2  H   4.423 0.05 2
      180 . 29 GLY HA3  H   3.555 0.05 2
      181 . 30 VAL N    N 123.055 0.05 1
      182 . 30 VAL H    H   7.815 0.05 1
      183 . 30 VAL HA   H   4.031 0.05 1
      184 . 30 VAL HB   H   2.226 0.05 1
      185 . 30 VAL HG1  H   0.765 0.05 1
      186 . 30 VAL HG2  H   0.780 0.05 1
      187 . 31 SER N    N 123.399 0.05 1
      188 . 31 SER H    H   9.021 0.05 1
      189 . 31 SER HA   H   4.575 0.05 1
      190 . 31 SER HB2  H   3.737 0.05 2
      191 . 31 SER HB3  H   3.602 0.05 2
      192 . 32 ALA N    N 122.022 0.05 1
      193 . 32 ALA H    H   7.674 0.05 1
      194 . 32 ALA HA   H   4.543 0.05 1
      195 . 32 ALA HB   H   1.273 0.05 1
      196 . 33 VAL N    N 118.581 0.05 1
      197 . 33 VAL H    H   8.207 0.05 1
      198 . 33 VAL HA   H   4.789 0.05 1
      199 . 33 VAL HB   H   1.830 0.05 1
      200 . 33 VAL HG1  H   0.688 0.05 1
      201 . 33 VAL HG2  H   0.690 0.05 1
      202 . 34 HIS N    N 124.775 0.05 1
      203 . 34 HIS H    H   8.974 0.05 1
      204 . 34 HIS HA   H   4.965 0.05 1
      205 . 34 HIS HB2  H   2.996 0.05 1
      206 . 34 HIS HB3  H   3.010 0.05 1
      207 . 34 HIS HD2  H   6.990 0.05 1
      208 . 35 VAL N    N 127.528 0.05 1
      209 . 35 VAL H    H   9.333 0.05 1
      210 . 35 VAL HA   H   4.232 0.05 1
      211 . 35 VAL HB   H   1.947 0.05 1
      212 . 35 VAL HG1  H   0.808 0.05 2
      213 . 35 VAL HG2  H   0.663 0.05 2
      214 . 36 ASN N    N 125.808 0.05 1
      215 . 36 ASN H    H   8.816 0.05 1
      216 . 36 ASN HA   H   4.773 0.05 1
      217 . 36 ASN HB2  H   2.840 0.05 1
      218 . 36 ASN HB3  H   2.588 0.05 1
      219 . 37 LEU N    N 125.464 0.05 1
      220 . 37 LEU H    H   8.688 0.05 1
      221 . 37 LEU HA   H   3.615 0.05 1
      222 . 37 LEU HB2  H   1.571 0.05 1
      223 . 37 LEU HB3  H   1.534 0.05 1
      224 . 37 LEU HG   H   1.228 0.05 1
      225 . 37 LEU HD1  H   0.484 0.05 1
      226 . 37 LEU HD2  H   0.508 0.05 1
      227 . 38 GLU N    N 118.581 0.05 1
      228 . 38 GLU H    H   8.581 0.05 1
      229 . 38 GLU HA   H   3.811 0.05 1
      230 . 38 GLU HB2  H   2.009 0.05 2
      231 . 38 GLU HB3  H   1.923 0.05 2
      232 . 38 GLU HG2  H   2.240 0.05 1
      233 . 38 GLU HG3  H   2.178 0.05 1
      234 . 39 ALA N    N 116.860 0.05 1
      235 . 39 ALA H    H   7.391 0.05 1
      236 . 39 ALA HA   H   4.300 0.05 1
      237 . 39 ALA HB   H   1.176 0.05 1
      238 . 40 GLY N    N 108.945 0.05 1
      239 . 40 GLY H    H   7.794 0.05 1
      240 . 40 GLY HA2  H   3.969 0.05 2
      241 . 40 GLY HA3  H   3.429 0.05 2
      242 . 41 LYS N    N 114.795 0.05 1
      243 . 41 LYS H    H   7.398 0.05 1
      244 . 41 LYS HA   H   5.203 0.05 1
      245 . 41 LYS HB2  H   1.591 0.05 1
      246 . 41 LYS HB3  H   1.438 0.05 1
      247 . 41 LYS HG2  H   1.074 0.05 1
      248 . 41 LYS HG3  H   1.081 0.05 1
      249 . 41 LYS HD2  H   1.303 0.05 1
      250 . 41 LYS HD3  H   1.307 0.05 1
      251 . 42 VAL N    N 122.366 0.05 1
      252 . 42 VAL H    H   9.153 0.05 1
      253 . 42 VAL HA   H   4.575 0.05 1
      254 . 42 VAL HB   H   1.933 0.05 1
      255 . 42 VAL HG1  H   0.730 0.05 1
      256 . 42 VAL HG2  H   0.540 0.05 1
      257 . 43 ASP N    N 129.249 0.05 1
      258 . 43 ASP H    H   9.207 0.05 1
      259 . 43 ASP HA   H   5.482 0.05 1
      260 . 43 ASP HB2  H   2.581 0.05 1
      261 . 43 ASP HB3  H   2.593 0.05 1
      262 . 44 VAL N    N 123.399 0.05 1
      263 . 44 VAL H    H   9.211 0.05 1
      264 . 44 VAL HA   H   4.976 0.05 1
      265 . 44 VAL HB   H   2.094 0.05 1
      266 . 44 VAL HG1  H   0.986 0.05 1
      267 . 44 VAL HG2  H   0.834 0.05 1
      268 . 45 SER N    N 122.711 0.05 1
      269 . 45 SER H    H   8.779 0.05 1
      270 . 45 SER HA   H   5.784 0.05 1
      271 . 45 SER HB2  H   3.728 0.05 1
      272 . 45 SER HB3  H   3.761 0.05 1
      273 . 46 PHE N    N 122.022 0.05 1
      274 . 46 PHE H    H   9.148 0.05 1
      275 . 46 PHE HA   H   5.342 0.05 1
      276 . 46 PHE HB2  H   2.818 0.05 1
      277 . 46 PHE HB3  H   2.504 0.05 1
      278 . 46 PHE HD1  H   6.782 0.05 1
      279 . 46 PHE HE1  H   7.020 0.05 1
      280 . 46 PHE HZ   H   7.150 0.05 1
      281 . 47 ASP N    N 118.925 0.05 1
      282 . 47 ASP H    H   8.340 0.05 1
      283 . 47 ASP HA   H   4.658 0.05 1
      284 . 47 ASP HB2  H   2.868 0.05 1
      285 . 47 ASP HB3  H   2.542 0.05 1
      286 . 48 ALA N    N 129.593 0.05 1
      287 . 48 ALA H    H   8.626 0.05 1
      288 . 48 ALA HA   H   5.075 0.05 1
      289 . 48 ALA HB   H   1.417 0.05 1
      290 . 49 ASP N    N 115.828 0.05 1
      291 . 49 ASP H    H   8.486 0.05 1
      292 . 49 ASP HA   H   4.530 0.05 1
      293 . 49 ASP HB2  H   2.712 0.05 1
      294 . 49 ASP HB3  H   2.568 0.05 1
      295 . 50 LYS N    N 117.549 0.05 1
      296 . 50 LYS H    H   7.837 0.05 1
      297 . 50 LYS HA   H   4.318 0.05 1
      298 . 50 LYS HB2  H   1.787 0.05 1
      299 . 50 LYS HB3  H   1.698 0.05 1
      300 . 50 LYS HG2  H   1.247 0.05 1
      301 . 50 LYS HG3  H   1.256 0.05 1
      302 . 50 LYS HD2  H   1.474 0.05 1
      303 . 50 LYS HD3  H   1.464 0.05 1
      304 . 51 VAL N    N 120.302 0.05 1
      305 . 51 VAL H    H   8.142 0.05 1
      306 . 51 VAL HA   H   4.371 0.05 1
      307 . 51 VAL HB   H   2.292 0.05 1
      308 . 51 VAL HG1  H   0.964 0.05 1
      309 . 51 VAL HG2  H   0.720 0.05 1
      310 . 52 SER N    N 117.893 0.05 1
      311 . 52 SER H    H   8.291 0.05 1
      312 . 52 SER HA   H   5.112 0.05 1
      313 . 52 SER HB2  H   4.177 0.05 1
      314 . 52 SER HB3  H   3.833 0.05 1
      315 . 53 VAL N    N 116.860 0.05 1
      316 . 53 VAL H    H   8.597 0.05 1
      317 . 53 VAL HA   H   3.472 0.05 1
      318 . 53 VAL HB   H   2.091 0.05 1
      319 . 53 VAL HG1  H   1.057 0.05 2
      320 . 53 VAL HG2  H   1.001 0.05 2
      321 . 54 LYS N    N 119.613 0.05 1
      322 . 54 LYS H    H   7.714 0.05 1
      323 . 54 LYS HA   H   3.934 0.05 1
      324 . 54 LYS HB2  H   1.640 0.05 1
      325 . 54 LYS HB3  H   1.714 0.05 1
      326 . 54 LYS HG2  H   1.327 0.05 1
      327 . 54 LYS HG3  H   1.337 0.05 1
      328 . 54 LYS HD2  H   1.470 0.05 1
      329 . 54 LYS HD3  H   1.480 0.05 1
      330 . 55 ASP N    N 118.237 0.05 1
      331 . 55 ASP H    H   7.496 0.05 1
      332 . 55 ASP HA   H   4.080 0.05 1
      333 . 55 ASP HB2  H   2.940 0.05 1
      334 . 55 ASP HB3  H   2.441 0.05 1
      335 . 56 ILE N    N 119.613 0.05 1
      336 . 56 ILE H    H   7.321 0.05 1
      337 . 56 ILE HA   H   3.117 0.05 1
      338 . 56 ILE HB   H   1.396 0.05 1
      339 . 56 ILE HG2  H  -0.021 0.05 1
      340 . 56 ILE HG12 H   0.205 0.05 1
      341 . 56 ILE HG13 H   0.216 0.05 1
      342 . 56 ILE HD1  H  -0.238 0.05 1
      343 . 57 ALA N    N 120.990 0.05 1
      344 . 57 ALA H    H   8.229 0.05 1
      345 . 57 ALA HA   H   3.597 0.05 1
      346 . 57 ALA HB   H   1.446 0.05 1
      347 . 58 ASP N    N 116.860 0.05 1
      348 . 58 ASP H    H   8.753 0.05 1
      349 . 58 ASP HA   H   4.172 0.05 1
      350 . 58 ASP HB2  H   2.692 0.05 1
      351 . 58 ASP HB3  H   2.540 0.05 1
      352 . 59 ALA N    N 121.678 0.05 1
      353 . 59 ALA H    H   7.408 0.05 1
      354 . 59 ALA HA   H   4.070 0.05 1
      355 . 59 ALA HB   H   1.302 0.05 1
      356 . 60 ILE N    N 118.237 0.05 1
      357 . 60 ILE H    H   7.554 0.05 1
      358 . 60 ILE HA   H   3.330 0.05 1
      359 . 60 ILE HB   H   1.714 0.05 1
      360 . 60 ILE HG12 H   0.701 0.05 1
      361 . 60 ILE HG13 H   0.710 0.05 1
      362 . 60 ILE HG2  H   0.352 0.05 1
      363 . 60 ILE HD1  H   0.116 0.05 1
      364 . 61 GLU N    N 119.269 0.05 1
      365 . 61 GLU H    H   8.578 0.05 1
      366 . 61 GLU HA   H   4.607 0.05 1
      367 . 61 GLU HB2  H   2.012 0.05 1
      368 . 61 GLU HB3  H   2.021 0.05 1
      369 . 61 GLU HG2  H   2.699 0.05 1
      370 . 61 GLU HG3  H   2.508 0.05 1
      371 . 62 ASP N    N 121.334 0.05 1
      372 . 62 ASP H    H   8.596 0.05 1
      373 . 62 ASP HA   H   4.383 0.05 1
      374 . 62 ASP HB2  H   2.766 0.05 2
      375 . 62 ASP HB3  H   2.530 0.05 2
      376 . 63 GLN N    N 114.107 0.05 1
      377 . 63 GLN H    H   7.308 0.05 1
      378 . 63 GLN HA   H   4.124 0.05 1
      379 . 63 GLN HB2  H   2.194 0.05 1
      380 . 63 GLN HB3  H   2.183 0.05 1
      381 . 63 GLN HG2  H   2.680 0.05 1
      382 . 63 GLN HG3  H   2.690 0.05 1
      383 . 63 GLN HE21 H   6.690 0.05 1
      384 . 63 GLN HE22 H   6.810 0.05 1
      385 . 64 GLY N    N 104.816 0.05 1
      386 . 64 GLY H    H   7.819 0.05 1
      387 . 64 GLY HA2  H   3.785 0.05 1
      388 . 64 GLY HA3  H   3.433 0.05 1
      389 . 65 TYR N    N 119.269 0.05 1
      390 . 65 TYR H    H   6.451 0.05 1
      391 . 65 TYR HA   H   4.744 0.05 1
      392 . 65 TYR HB2  H   3.089 0.05 1
      393 . 65 TYR HB3  H   2.088 0.05 1
      394 . 65 TYR HE1  H   6.810 0.05 1
      395 . 65 TYR HD1  H   6.680 0.05 1
      396 . 66 ASP N    N 118.237 0.05 1
      397 . 66 ASP H    H   7.972 0.05 1
      398 . 66 ASP HA   H   4.957 0.05 1
      399 . 66 ASP HB2  H   2.516 0.05 1
      400 . 66 ASP HB3  H   2.391 0.05 1
      401 . 67 VAL N    N 124.431 0.05 1
      402 . 67 VAL H    H   9.475 0.05 1
      403 . 67 VAL HA   H   4.334 0.05 1
      404 . 67 VAL HB   H   2.118 0.05 1
      405 . 67 VAL HG1  H   0.998 0.05 1
      406 . 67 VAL HG2  H   0.959 0.05 1
      407 . 68 ALA N    N 132.002 0.05 1
      408 . 68 ALA H    H   8.797 0.05 1
      409 . 68 ALA HA   H   4.259 0.05 1
      410 . 68 ALA HB   H   1.277 0.05 1
      411 . 69 LYS N    N 115.828 0.05 1
      412 . 69 LYS H    H   7.720 0.05 1
      413 . 69 LYS HA   H   4.280 0.05 1
      414 . 69 LYS HB2  H   1.670 0.05 1
      415 . 69 LYS HB3  H   1.680 0.05 1
      416 . 69 LYS HG2  H   1.284 0.05 1
      417 . 69 LYS HG3  H   1.289 0.05 1
      418 . 69 LYS HD2  H   1.530 0.05 1
      419 . 69 LYS HD3  H   1.540 0.05 1
      420 . 70 ILE N    N 123.399 0.05 1
      421 . 70 ILE H    H   8.276 0.05 1
      422 . 70 ILE HA   H   4.202 0.05 1
      423 . 70 ILE HB   H   1.466 0.05 1
      424 . 70 ILE HG12 H   0.647 0.05 1
      425 . 70 ILE HG13 H   0.656 0.05 1
      426 . 70 ILE HG2  H   0.338 0.05 1
      427 . 71 GLU N    N 126.152 0.05 1
      428 . 71 GLU H    H   8.696 0.05 1
      429 . 71 GLU HA   H   4.359 0.05 1
      430 . 71 GLU HB2  H   1.945 0.05 2
      431 . 71 GLU HB3  H   1.848 0.05 2
      432 . 71 GLU HG2  H   2.093 0.05 1
      433 . 71 GLU HG3  H   2.085 0.05 1
      434 . 72 GLY N    N 109.978 0.05 1
      435 . 72 GLY H    H   8.469 0.05 1
      436 . 72 GLY HA2  H   4.012 0.05 2
      437 . 72 GLY HA3  H   3.942 0.05 2
      438 . 73 ARG N    N 125.808 0.05 1
      439 . 73 ARG H    H   7.885 0.05 1
      440 . 73 ARG HA   H   4.059 0.05 1
      441 . 73 ARG HB2  H   1.748 0.05 1
      442 . 73 ARG HB3  H   1.592 0.05 1
      443 . 73 ARG HG2  H   1.476 0.05 1
      444 . 73 ARG HG3  H   1.486 0.05 1
      445 . 73 ARG HD2  H   3.068 0.05 1
      446 . 73 ARG HD3  H   3.077 0.05 1

   stop_

save_