data_15045

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

save_entry_information
   _Saveframe_category      entry_information

   _Entry_title            
;
NMR SOLUTION STRUCTURE OF A MINIMAL TRANSMEMBRANE BETA-BARREL PLATFORM PROTEIN
;
   _BMRB_accession_number   15045
   _BMRB_flat_file_name     bmr15045.str
   _Entry_type              original
   _Submission_date         2006-11-20
   _Accession_date          2006-11-20
   _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 Johansson Maria      U. . 
      2 Alioth    Simon      .  . 
      3 Hu        Kaifeng    .  . 
      4 Walser    Reto       .  . 
      5 Koebnik   Ralf       .  . 
      6 Pervushin Konstantin .  . 

   stop_

   loop_
      _Saveframe_category_type
      _Saveframe_category_type_count

      assigned_chemical_shifts 1 

   stop_

   loop_
      _Data_type
      _Data_type_count

      "1H chemical shifts"  110 
      "13C chemical shifts" 308 
      "15N chemical shifts" 110 

   stop_

   loop_
      _Revision_date
      _Revision_keyword
      _Revision_author
      _Revision_detail

      2007-05-21 original author . 

   stop_

   _Original_release_date   2007-05-21

save_


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

save_entry_citation
   _Saveframe_category           entry_citation

   _Citation_full                .
   _Citation_title              
;
A Minimal Transmembrane Beta-Barrel Platform Protein   
Studied by NMR
;
   _Citation_status              published
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              .
   _PubMed_ID                    17260943

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Johansson Maria      U. . 
      2 Alioth    Simon      .  . 
      3 Hu        Kaifeng    .  . 
      4 Walser    Reto       .  . 
      5 Koebnik   Ralf       .  . 
      6 Pervushin Konstantin .  . 

   stop_

   _Journal_abbreviation         Biochemistry
   _Journal_volume               46
   _Journal_issue                5
   _Journal_CSD                  .
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_ISBN                    .
   _Conference_state_province    .
   _Conference_abstract_number   .
   _Page_first                   1128
   _Page_last                    1140
   _Year                         2007
   _Details                      .

save_


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

save_assembly
   _Saveframe_category         molecular_system

   _Mol_system_name           'BBP+EF in DHPC micelles'
   _Enzyme_commission_number   .

   loop_
      _Mol_system_component_name
      _Mol_label

      'BBP+EF in DHPC micelles' $BBP+EF 

   stop_

   _System_molecular_weight    .
   _System_physical_state      native
   _System_oligomer_state      ?
   _System_paramagnetic        ?
   _System_thiol_state         .
   _Database_query_date        .
   _Details                    .

save_


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

save_BBP+EF
   _Saveframe_category                          monomeric_polymer

   _Mol_type                                    polymer
   _Mol_polymer_class                           protein
   _Name_common                                 BBP+EF
   _Molecular_mass                              17206.318
   _Mol_thiol_state                            'not present'
   _Details                                     .

   	##############################
   	#  Polymer residue sequence  #
   	##############################
   
      _Residue_count                               156
   _Mol_residue_sequence                       
;
MPKDNTWYTGAKLGWSQYSR
ENQLGAGAFGGYQVNPYVGF
EMGYDWLGRMPRKAQGVQLT
AKLGYPKLGTDDLDIYTRLG
GMVWRADTSDKDGNGYISAA
EASVSPVFAGGVEYVIRRRI
TPEIATRLEYQWTNNASDNG
MLSLGVSYRFGQGEAA
;

   loop_
      _Residue_seq_code
      _Residue_label

        1 MET    2 PRO    3 LYS    4 ASP    5 ASN 
        6 THR    7 TRP    8 TYR    9 THR   10 GLY 
       11 ALA   12 LYS   13 LEU   14 GLY   15 TRP 
       16 SER   17 GLN   18 TYR   19 SER   20 ARG 
       21 GLU   22 ASN   23 GLN   24 LEU   25 GLY 
       26 ALA   27 GLY   28 ALA   29 PHE   30 GLY 
       31 GLY   32 TYR   33 GLN   34 VAL   35 ASN 
       36 PRO   37 TYR   38 VAL   39 GLY   40 PHE 
       41 GLU   42 MET   43 GLY   44 TYR   45 ASP 
       46 TRP   47 LEU   48 GLY   49 ARG   50 MET 
       51 PRO   52 ARG   53 LYS   54 ALA   55 GLN 
       56 GLY   57 VAL   58 GLN   59 LEU   60 THR 
       61 ALA   62 LYS   63 LEU   64 GLY   65 TYR 
       66 PRO   67 LYS   68 LEU   69 GLY   70 THR 
       71 ASP   72 ASP   73 LEU   74 ASP   75 ILE 
       76 TYR   77 THR   78 ARG   79 LEU   80 GLY 
       81 GLY   82 MET   83 VAL   84 TRP   85 ARG 
       86 ALA   87 ASP   88 THR   89 SER   90 ASP 
       91 LYS   92 ASP   93 GLY   94 ASN   95 GLY 
       96 TYR   97 ILE   98 SER   99 ALA  100 ALA 
      101 GLU  102 ALA  103 SER  104 VAL  105 SER 
      106 PRO  107 VAL  108 PHE  109 ALA  110 GLY 
      111 GLY  112 VAL  113 GLU  114 TYR  115 VAL 
      116 ILE  117 ARG  118 ARG  119 ARG  120 ILE 
      121 THR  122 PRO  123 GLU  124 ILE  125 ALA 
      126 THR  127 ARG  128 LEU  129 GLU  130 TYR 
      131 GLN  132 TRP  133 THR  134 ASN  135 ASN 
      136 ALA  137 SER  138 ASP  139 ASN  140 GLY 
      141 MET  142 LEU  143 SER  144 LEU  145 GLY 
      146 VAL  147 SER  148 TYR  149 ARG  150 PHE 
      151 GLY  152 GLN  153 GLY  154 GLU  155 ALA 
      156 ALA 

   stop_

   _Sequence_homology_query_date                .
   _Sequence_homology_query_revised_last_date   2014-05-12

   loop_
      _Database_name
      _Database_accession_code
      _Database_entry_mol_name
      _Sequence_query_to_submitted_percentage
      _Sequence_subject_length
      _Sequence_identity
      _Sequence_positive
      _Sequence_homology_expectation_value

      PDB 2JMM "Nmr Solution Structure Of A Minimal Transmembrane Beta- Barrel Platform Protein" 100.00 156 100.00 100.00 1.73e-108 

   stop_

save_


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

save_natural_source
   _Saveframe_category   natural_source


   loop_
      _Mol_label
      _Organism_name_common
      _NCBI_taxonomy_ID
      _Superkingdom
      _Kingdom
      _Genus
      _Species

      $BBP+EF 'E. coli' 562 Bacteria . Escherichia coli 

   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

      $BBP+EF 'recombinant technology' . Escherichia coli . pET-3b 

   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

      $BBP+EF  1 mM '[U-100% 13C; U-100% 15N; 80% 2H]' 
       H2O    90 %   .                                 
       D2O    10 %   .                                 

   stop_

save_


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

save_GROMACS
   _Saveframe_category   software

   _Name                 GROMACS
   _Version              .

   loop_
      _Vendor
      _Address
      _Electronic_address

      'Lindahl, Hess and van der Spoel' . . 

   stop_

   loop_
      _Task

      'structure solution' 

   stop_

   _Details              .

save_


save_CYANA
   _Saveframe_category   software

   _Name                 CYANA
   _Version              .

   loop_
      _Vendor
      _Address
      _Electronic_address

      'Guntert, Mumenthaler and Wuthrich' . . 

   stop_

   loop_
      _Task

      'structure solution' 

   stop_

   _Details              .

save_


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

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

save_spectrometer_1
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                Avance
   _Field_strength       600
   _Details              .

save_


save_spectrometer_2
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                Avance
   _Field_strength       900
   _Details              .

save_


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

save_2D_1H-15N_HSQC_1
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '2D 1H-15N HSQC'
   _Sample_label        $sample_1

save_


save_3D_HNCA_2
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D HNCA'
   _Sample_label        $sample_1

save_


save_3D_HN(CO)CA_3
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D HN(CO)CA'
   _Sample_label        $sample_1

save_


save_3D_HNCACB_4
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D HNCACB'
   _Sample_label        $sample_1

save_


save_3D_HNCO_5
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D HNCO'
   _Sample_label        $sample_1

save_


save_3D_HN(CA)CO_6
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D HN(CA)CO'
   _Sample_label        $sample_1

save_


save_3D_1H-15N_NOESY_7
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D 1H-15N NOESY'
   _Sample_label        $sample_1

save_


save_3D_1H-15N_NOESY_8
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D 1H-15N NOESY'
   _Sample_label        $sample_1

save_


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

save_sample_conditions_1
   _Saveframe_category   sample_conditions

   _Details              .

   loop_
      _Variable_type
      _Variable_value
      _Variable_value_error
      _Variable_value_units

      'ionic strength'  20 . mM  
       pH                6 . pH  
       pressure          1 . atm 
       temperature     303 . K   

   stop_

save_


####################
#  NMR parameters  #
####################

    ##############################
    #  Assigned chemical shifts  #
    ##############################

	################################
	#  Chemical shift referencing  #
	################################

save_chemical_shift_reference_1
   _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
      _Indirect_shift_ratio_citation_label
      _Correction_value_citation_label

      DSS C 13 'methyl protons' ppm 0.00 .        indirect . . . 0.251449530 $entry_citation $entry_citation 
      DSS H  1 'methyl protons' ppm 0.00 internal direct   . . . 1.000000000 $entry_citation $entry_citation 
      DSS N 15 'methyl protons' ppm 0.00 .        indirect . . . 0.101329118 $entry_citation $entry_citation 

   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_assigned_chem_shift_list_1
   _Saveframe_category               assigned_chemical_shifts

   _Details                          .

   loop_
      _Experiment_label

      '2D 1H-15N HSQC' 
      '3D HNCA'        
      '3D HN(CO)CA'    
      '3D HNCACB'      
      '3D HNCO'        
      '3D HN(CA)CO'    

   stop_

   loop_
      _Sample_label

      $sample_1 

   stop_

   _Sample_conditions_label         $sample_conditions_1
   _Chem_shift_reference_set_label  $chemical_shift_reference_1
   _Mol_system_component_name       'BBP+EF in DHPC micelles'
   _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   4   4 ASP H  H   8.23 . 1 
        2   4   4 ASP C  C 175.1  . 1 
        3   4   4 ASP CA C  53.7  . 1 
        4   4   4 ASP CB C  40.5  . 1 
        5   4   4 ASP N  N 119.6  . 1 
        6   5   5 ASN H  H   8.02 . 1 
        7   5   5 ASN C  C 174.2  . 1 
        8   5   5 ASN CA C  53.7  . 1 
        9   5   5 ASN CB C  37.2  . 1 
       10   5   5 ASN N  N 117.7  . 1 
       11   6   6 THR H  H   7.38 . 1 
       12   6   6 THR CA C  60.6  . 1 
       13   6   6 THR CB C  71.1  . 1 
       14   6   6 THR N  N 110.9  . 1 
       15   7   7 TRP H  H   8.58 . 1 
       16   7   7 TRP C  C 175.0  . 1 
       17   7   7 TRP CA C  55.68 . 1 
       18   7   7 TRP CB C  31.5  . 1 
       19   7   7 TRP N  N 123.1  . 1 
       20   8   8 TYR H  H   8.76 . 1 
       21   8   8 TYR C  C 174.0  . 1 
       22   8   8 TYR CA C  55.5  . 1 
       23   8   8 TYR CB C  40.7  . 1 
       24   8   8 TYR N  N 117.1  . 1 
       25   9   9 THR H  H   8.82 . 1 
       26   9   9 THR C  C 172.4  . 1 
       27   9   9 THR CA C  59.4  . 1 
       28   9   9 THR CB C  71.3  . 1 
       29   9   9 THR N  N 112.8  . 1 
       30  10  10 GLY H  H   8.55 . 1 
       31  10  10 GLY C  C 170.4  . 1 
       32  10  10 GLY CA C  45.7  . 1 
       33  10  10 GLY N  N 112.0  . 1 
       34  11  11 ALA H  H   8.17 . 1 
       35  11  11 ALA C  C 174.6  . 1 
       36  11  11 ALA CA C  49.8  . 1 
       37  11  11 ALA CB C  22.2  . 1 
       38  11  11 ALA N  N 118.8  . 1 
       39  12  12 LYS H  H   8.99 . 1 
       40  12  12 LYS C  C 172.9  . 1 
       41  12  12 LYS CA C  53.9  . 1 
       42  12  12 LYS CB C  36.3  . 1 
       43  12  12 LYS N  N 116.3  . 1 
       44  13  13 LEU H  H   8.68 . 1 
       45  13  13 LEU C  C 175.2  . 1 
       46  13  13 LEU CA C  53.1  . 1 
       47  13  13 LEU CB C  45.4  . 1 
       48  13  13 LEU N  N 120.2  . 1 
       49  14  14 GLY H  H   8.69 . 1 
       50  14  14 GLY C  C 170.9  . 1 
       51  14  14 GLY CA C  44.9  . 1 
       52  14  14 GLY N  N 108.8  . 1 
       53  15  15 TRP H  H   8.92 . 1 
       54  15  15 TRP C  C 174.3  . 1 
       55  15  15 TRP CA C  55.3  . 1 
       56  15  15 TRP CB C  31.5  . 1 
       57  15  15 TRP N  N 122.0  . 1 
       58  16  16 SER H  H   8.74 . 1 
       59  16  16 SER CA C  56.3  . 1 
       60  16  16 SER CB C  65.5  . 1 
       61  16  16 SER N  N 120.8  . 1 
       62  27  27 GLY H  H   8.25 . 1 
       63  27  27 GLY CA C  46.3  . 1 
       64  27  27 GLY N  N 104.6  . 1 
       65  28  28 ALA H  H   9.15 . 1 
       66  28  28 ALA C  C 176.3  . 1 
       67  28  28 ALA CA C  49.6  . 1 
       68  28  28 ALA CB C  22.3  . 1 
       69  28  28 ALA N  N 120.4  . 1 
       70  29  29 PHE H  H   8.54 . 1 
       71  29  29 PHE C  C 173.3  . 1 
       72  29  29 PHE CA C  55.7  . 1 
       73  29  29 PHE CB C  41.5  . 1 
       74  29  29 PHE N  N 119.3  . 1 
       75  30  30 GLY H  H   9.07 . 1 
       76  30  30 GLY C  C 170.5  . 1 
       77  30  30 GLY CA C  45.1  . 1 
       78  30  30 GLY N  N 106.9  . 1 
       79  31  31 GLY H  H   8.29 . 1 
       80  31  31 GLY C  C 169.6  . 1 
       81  31  31 GLY CA C  45.8  . 1 
       82  31  31 GLY N  N 109.4  . 1 
       83  32  32 TYR H  H   8.47 . 1 
       84  32  32 TYR C  C 173.4  . 1 
       85  32  32 TYR CA C  55.4  . 1 
       86  32  32 TYR CB C  41.8  . 1 
       87  32  32 TYR N  N 118.0  . 1 
       88  33  33 GLN H  H   8.76 . 1 
       89  33  33 GLN C  C 174.2  . 1 
       90  33  33 GLN CA C  53.9  . 1 
       91  33  33 GLN CB C  28.0  . 1 
       92  33  33 GLN N  N 129.0  . 1 
       93  34  34 VAL H  H   8.54 . 1 
       94  34  34 VAL CA C  64.5  . 1 
       95  34  34 VAL CB C  31.8  . 1 
       96  34  34 VAL N  N 127.8  . 1 
       97  35  35 ASN H  H   8.18 . 1 
       98  35  35 ASN C  C 172.6  . 1 
       99  35  35 ASN CA C  51.4  . 1 
      100  35  35 ASN CB C  37.3  . 1 
      101  35  35 ASN N  N 117.0  . 1 
      102  36  36 PRO C  C 175.3  . 1 
      103  36  36 PRO CA C  65.2  . 1 
      104  36  36 PRO CB C  30.5  . 1 
      105  37  37 TYR H  H   7.99 . 1 
      106  37  37 TYR C  C 175.3  . 1 
      107  37  37 TYR CA C  57.0  . 1 
      108  37  37 TYR CB C  39.1  . 1 
      109  37  37 TYR N  N 112.7  . 1 
      110  38  38 VAL H  H   7.37 . 1 
      111  38  38 VAL C  C 173.4  . 1 
      112  38  38 VAL CA C  60.5  . 1 
      113  38  38 VAL CB C  34.3  . 1 
      114  38  38 VAL N  N 117.9  . 1 
      115  39  39 GLY H  H   8.76 . 1 
      116  39  39 GLY C  C 170.7  . 1 
      117  39  39 GLY CA C  43.7  . 1 
      118  39  39 GLY N  N 115.1  . 1 
      119  40  40 PHE H  H   8.72 . 1 
      120  40  40 PHE C  C 173.1  . 1 
      121  40  40 PHE CA C  56.2  . 1 
      122  40  40 PHE CB C  42.1  . 1 
      123  40  40 PHE N  N 118.2  . 1 
      124  41  41 GLU H  H   9.17 . 1 
      125  41  41 GLU C  C 174.2  . 1 
      126  41  41 GLU CA C  54.8  . 1 
      127  41  41 GLU CB C  33.8  . 1 
      128  41  41 GLU N  N 121.9  . 1 
      129  42  42 MET H  H   9.45 . 1 
      130  42  42 MET C  C 174.1  . 1 
      131  42  42 MET CA C  53.1  . 1 
      132  42  42 MET CB C  35.9  . 1 
      133  42  42 MET N  N 125.6  . 1 
      134  43  43 GLY H  H   8.88 . 1 
      135  43  43 GLY C  C 170.8  . 1 
      136  43  43 GLY CA C  44.3  . 1 
      137  43  43 GLY N  N 110.0  . 1 
      138  44  44 TYR H  H   8.89 . 1 
      139  44  44 TYR C  C 172.9  . 1 
      140  44  44 TYR CA C  55.5  . 1 
      141  44  44 TYR CB C  41.4  . 1 
      142  44  44 TYR N  N 123.6  . 1 
      143  45  45 ASP H  H   8.65 . 1 
      144  45  45 ASP C  C 173.4  . 1 
      145  45  45 ASP CA C  52.7  . 1 
      146  45  45 ASP CB C  43.7  . 1 
      147  45  45 ASP N  N 126.6  . 1 
      148  46  46 TRP H  H   8.96 . 1 
      149  46  46 TRP C  C 173.6  . 1 
      150  46  46 TRP CA C  56.2  . 1 
      151  46  46 TRP N  N 119.9  . 1 
      152  47  47 LEU H  H   8.13 . 1 
      153  47  47 LEU C  C 176.5  . 1 
      154  47  47 LEU CA C  54.0  . 1 
      155  47  47 LEU CB C  40.5  . 1 
      156  47  47 LEU N  N 120.4  . 1 
      157  48  48 GLY H  H   8.27 . 1 
      158  48  48 GLY C  C 173.8  . 1 
      159  48  48 GLY CA C  44.8  . 1 
      160  48  48 GLY N  N 109.2  . 1 
      161  56  56 GLY H  H   8.86 . 1 
      162  56  56 GLY C  C 171.2  . 1 
      163  56  56 GLY CA C  45.2  . 1 
      164  56  56 GLY N  N 107.6  . 1 
      165  57  57 VAL H  H   8.92 . 1 
      166  57  57 VAL C  C 173.5  . 1 
      167  57  57 VAL CA C  59.1  . 1 
      168  57  57 VAL CB C  33.8  . 1 
      169  57  57 VAL N  N 119.9  . 1 
      170  58  58 GLN H  H   9.32 . 1 
      171  58  58 GLN C  C 174.0  . 1 
      172  58  58 GLN CA C  52.1  . 1 
      173  58  58 GLN CB C  33.1  . 1 
      174  58  58 GLN N  N 122.2  . 1 
      175  59  59 LEU H  H   8.47 . 1 
      176  59  59 LEU C  C 175.0  . 1 
      177  59  59 LEU CA C  53.6  . 1 
      178  59  59 LEU CB C  44.3  . 1 
      179  59  59 LEU N  N 123.9  . 1 
      180  60  60 THR H  H   9.06 . 1 
      181  60  60 THR C  C 173.1  . 1 
      182  60  60 THR CA C  58.8  . 1 
      183  60  60 THR CB C  73.1  . 1 
      184  60  60 THR N  N 112.7  . 1 
      185  61  61 ALA H  H   8.65 . 1 
      186  61  61 ALA C  C 175.0  . 1 
      187  61  61 ALA CA C  49.7  . 1 
      188  61  61 ALA CB C  18.9  . 1 
      189  61  61 ALA N  N 121.3  . 1 
      190  62  62 LYS H  H   8.86 . 1 
      191  62  62 LYS C  C 174.7  . 1 
      192  62  62 LYS CA C  54.0  . 1 
      193  62  62 LYS CB C  32.5  . 1 
      194  62  62 LYS N  N 125.0  . 1 
      195  63  63 LEU H  H   9.22 . 1 
      196  63  63 LEU C  C 175.1  . 1 
      197  63  63 LEU CA C  52.4  . 1 
      198  63  63 LEU CB C  42.3  . 1 
      199  63  63 LEU N  N 131.6  . 1 
      200  64  64 GLY H  H   8.98 . 1 
      201  64  64 GLY C  C 171.1  . 1 
      202  64  64 GLY CA C  44.3  . 1 
      203  64  64 GLY N  N 111.5  . 1 
      204  65  65 TYR H  H   8.20 . 1 
      205  65  65 TYR C  C 174.0  . 1 
      206  65  65 TYR CA C  54.4  . 1 
      207  65  65 TYR CB C  39.3  . 1 
      208  65  65 TYR N  N 116.7  . 1 
      209  70  70 THR H  H   8.21 . 1 
      210  70  70 THR C  C 174.1  . 1 
      211  70  70 THR CA C  59.8  . 1 
      212  70  70 THR CB C  69.9  . 1 
      213  70  70 THR N  N 113.4  . 1 
      214  71  71 ASP H  H   8.39 . 1 
      215  71  71 ASP C  C 176.3  . 1 
      216  71  71 ASP CA C  55.2  . 1 
      217  71  71 ASP CB C  40.2  . 1 
      218  71  71 ASP N  N 120.9  . 1 
      219  72  72 ASP H  H   8.04 . 1 
      220  72  72 ASP C  C 173.7  . 1 
      221  72  72 ASP CA C  54.2  . 1 
      222  72  72 ASP CB C  40.8  . 1 
      223  72  72 ASP N  N 116.7  . 1 
      224  73  73 LEU H  H   7.53 . 1 
      225  73  73 LEU C  C 174.1  . 1 
      226  73  73 LEU CA C  53.7  . 1 
      227  73  73 LEU CB C  44.0  . 1 
      228  73  73 LEU N  N 121.9  . 1 
      229  74  74 ASP H  H   9.11 . 1 
      230  74  74 ASP C  C 174.8  . 1 
      231  74  74 ASP CA C  52.5  . 1 
      232  74  74 ASP CB C  42.8  . 1 
      233  74  74 ASP N  N 126.2  . 1 
      234  75  75 ILE H  H   8.47 . 1 
      235  75  75 ILE C  C 174.5  . 1 
      236  75  75 ILE CA C  59.5  . 1 
      237  75  75 ILE CB C  38.1  . 1 
      238  75  75 ILE N  N 123.4  . 1 
      239  76  76 TYR H  H   8.60 . 1 
      240  76  76 TYR C  C 172.9  . 1 
      241  76  76 TYR CA C  56.0  . 1 
      242  76  76 TYR CB C  41.4  . 1 
      243  76  76 TYR N  N 123.1  . 1 
      244  77  77 THR H  H   9.08 . 1 
      245  77  77 THR C  C 174.1  . 1 
      246  77  77 THR CA C  58.4  . 1 
      247  77  77 THR CB C  71.9  . 1 
      248  77  77 THR N  N 110.5  . 1 
      249  78  78 ARG H  H   8.94 . 1 
      250  78  78 ARG C  C 174.9  . 1 
      251  78  78 ARG CA C  54.0  . 1 
      252  78  78 ARG CB C  32.2  . 1 
      253  78  78 ARG N  N 120.8  . 1 
      254  79  79 LEU H  H   8.44 . 1 
      255  79  79 LEU CA C  53.7  . 1 
      256  79  79 LEU CB C  44.6  . 1 
      257  79  79 LEU N  N 118.4  . 1 
      258  80  80 GLY H  H   8.11 . 1 
      259  80  80 GLY C  C 171.2  . 1 
      260  80  80 GLY CA C  46.1  . 1 
      261  80  80 GLY N  N 109.4  . 1 
      262  81  81 GLY H  H   8.33 . 1 
      263  81  81 GLY C  C 169.6  . 1 
      264  81  81 GLY CA C  43.7  . 1 
      265  81  81 GLY N  N 110.3  . 1 
      266  82  82 MET H  H   9.08 . 1 
      267  82  82 MET C  C 173.9  . 1 
      268  82  82 MET CA C  53.2  . 1 
      269  82  82 MET CB C  36.6  . 1 
      270  82  82 MET N  N 121.3  . 1 
      271  83  83 VAL H  H   9.11 . 1 
      272  83  83 VAL C  C 174.1  . 1 
      273  83  83 VAL CA C  59.2  . 1 
      274  83  83 VAL CB C  32.3  . 1 
      275  83  83 VAL N  N 127.0  . 1 
      276  84  84 TRP H  H   9.00 . 1 
      277  84  84 TRP C  C 173.8  . 1 
      278  84  84 TRP CA C  54.6  . 1 
      279  84  84 TRP CB C  32.5  . 1 
      280  84  84 TRP N  N 125.3  . 1 
      281  87  87 ASP H  H   8.44 . 1 
      282  87  87 ASP C  C 176.3  . 1 
      283  87  87 ASP CA C  53.7  . 1 
      284  87  87 ASP CB C  41.3  . 1 
      285  87  87 ASP N  N 120.7  . 1 
      286  88  88 THR H  H   8.24 . 1 
      287  88  88 THR C  C 174.4  . 1 
      288  88  88 THR CA C  60.7  . 1 
      289  88  88 THR CB C  69.3  . 1 
      290  88  88 THR N  N 114.7  . 1 
      291  89  89 SER H  H   8.38 . 1 
      292  89  89 SER C  C 174.2  . 1 
      293  89  89 SER CA C  58.1  . 1 
      294  89  89 SER CB C  63.3  . 1 
      295  89  89 SER N  N 118.4  . 1 
      296  90  90 ASP H  H   8.39 . 1 
      297  90  90 ASP C  C 176.0  . 1 
      298  90  90 ASP CA C  53.9  . 1 
      299  90  90 ASP CB C  40.2  . 1 
      300  90  90 ASP N  N 122.6  . 1 
      301  91  91 LYS H  H   8.07 . 1 
      302  91  91 LYS C  C 176.1  . 1 
      303  91  91 LYS CA C  55.7  . 1 
      304  91  91 LYS CB C  32.0  . 1 
      305  91  91 LYS N  N 121.0  . 1 
      306  92  92 ASP H  H   8.19 . 1 
      307  92  92 ASP C  C 176.3  . 1 
      308  92  92 ASP CA C  54.1  . 1 
      309  92  92 ASP CB C  40.5  . 1 
      310  92  92 ASP N  N 121.4  . 1 
      311  93  93 GLY H  H   8.14 . 1 
      312  93  93 GLY C  C 174.3  . 1 
      313  93  93 GLY CA C  45.2  . 1 
      314  93  93 GLY N  N 109.2  . 1 
      315  94  94 ASN H  H   8.33 . 1 
      316  94  94 ASN C  C 175.5  . 1 
      317  94  94 ASN CA C  52.9  . 1 
      318  94  94 ASN CB C  38.3  . 1 
      319  94  94 ASN N  N 119.1  . 1 
      320  95  95 GLY H  H   8.33 . 1 
      321  95  95 GLY C  C 173.6  . 1 
      322  95  95 GLY CA C  44.9  . 1 
      323  95  95 GLY N  N 109.3  . 1 
      324  96  96 TYR H  H   8.10 . 1 
      325  96  96 TYR C  C 175.7  . 1 
      326  96  96 TYR CA C  57.6  . 1 
      327  96  96 TYR CB C  37.8  . 1 
      328  96  96 TYR N  N 120.4  . 1 
      329  97  97 ILE H  H   7.99 . 1 
      330  97  97 ILE C  C 175.6  . 1 
      331  97  97 ILE CA C  60.4  . 1 
      332  97  97 ILE CB C  37.7  . 1 
      333  97  97 ILE N  N 122.6  . 1 
      334  98  98 SER H  H   8.17 . 1 
      335  98  98 SER C  C 174.3  . 1 
      336  98  98 SER CA C  57.5  . 1 
      337  98  98 SER CB C  63.2  . 1 
      338  98  98 SER N  N 119.9  . 1 
      339  99  99 ALA H  H   8.30 . 1 
      340  99  99 ALA C  C 177.1  . 1 
      341  99  99 ALA CA C  52.1  . 1 
      342  99  99 ALA CB C  18.1  . 1 
      343  99  99 ALA N  N 126.5  . 1 
      344 100 100 ALA H  H   8.07 . 1 
      345 100 100 ALA C  C 177.4  . 1 
      346 100 100 ALA CA C  52.0  . 1 
      347 100 100 ALA CB C  18.3  . 1 
      348 100 100 ALA N  N 122.8  . 1 
      349 101 101 GLU H  H   8.06 . 1 
      350 101 101 GLU C  C 175.4  . 1 
      351 101 101 GLU CA C  55.4  . 1 
      352 101 101 GLU CB C  29.6  . 1 
      353 101 101 GLU N  N 119.5  . 1 
      354 102 102 ALA H  H   8.16 . 1 
      355 102 102 ALA C  C 176.3  . 1 
      356 102 102 ALA CA C  51.1  . 1 
      357 102 102 ALA CB C  19.0  . 1 
      358 102 102 ALA N  N 124.7  . 1 
      359 103 103 SER H  H   8.15 . 1 
      360 103 103 SER C  C 171.9  . 1 
      361 103 103 SER CA C  57.0  . 1 
      362 103 103 SER CB C  64.5  . 1 
      363 103 103 SER N  N 116.5  . 1 
      364 107 107 VAL H  H   7.59 . 1 
      365 107 107 VAL C  C 170.3  . 1 
      366 107 107 VAL CA C  59.2  . 1 
      367 107 107 VAL CB C  33.9  . 1 
      368 107 107 VAL N  N 120.4  . 1 
      369 108 108 PHE H  H   7.94 . 1 
      370 108 108 PHE C  C 173.6  . 1 
      371 108 108 PHE CA C  53.9  . 1 
      372 108 108 PHE CB C  41.5  . 1 
      373 108 108 PHE N  N 123.6  . 1 
      374 109 109 ALA H  H   8.57 . 1 
      375 109 109 ALA C  C 176.6  . 1 
      376 109 109 ALA CA C  50.3  . 1 
      377 109 109 ALA CB C  21.9  . 1 
      378 109 109 ALA N  N 121.2  . 1 
      379 110 110 GLY H  H   8.78 . 1 
      380 110 110 GLY C  C 170.9  . 1 
      381 110 110 GLY CA C  43.9  . 1 
      382 110 110 GLY N  N 107.1  . 1 
      383 111 111 GLY H  H   8.03 . 1 
      384 111 111 GLY C  C 170.0  . 1 
      385 111 111 GLY CA C  45.5  . 1 
      386 111 111 GLY N  N 110.3  . 1 
      387 112 112 VAL H  H   8.48 . 1 
      388 112 112 VAL C  C 174.6  . 1 
      389 112 112 VAL CA C  57.6  . 1 
      390 112 112 VAL CB C  34.4  . 1 
      391 112 112 VAL N  N 111.7  . 1 
      392 113 113 GLU H  H   9.13 . 1 
      393 113 113 GLU C  C 174.3  . 1 
      394 113 113 GLU CA C  54.1  . 1 
      395 113 113 GLU CB C  32.8  . 1 
      396 113 113 GLU N  N 123.0  . 1 
      397 114 114 TYR H  H   9.04 . 1 
      398 114 114 TYR C  C 174.5  . 1 
      399 114 114 TYR CA C  54.7  . 1 
      400 114 114 TYR CB C  41.6  . 1 
      401 114 114 TYR N  N 126.4  . 1 
      402 115 115 VAL H  H   8.31 . 1 
      403 115 115 VAL C  C 174.2  . 1 
      404 115 115 VAL CA C  62.9  . 1 
      405 115 115 VAL CB C  33.7  . 1 
      406 115 115 VAL N  N 129.9  . 1 
      407 124 124 ILE H  H   7.27 . 1 
      408 124 124 ILE C  C 174.2  . 1 
      409 124 124 ILE CA C  59.4  . 1 
      410 124 124 ILE CB C  39.3  . 1 
      411 124 124 ILE N  N 117.9  . 1 
      412 125 125 ALA H  H   9.10 . 1 
      413 125 125 ALA C  C 176.4  . 1 
      414 125 125 ALA CA C  49.1  . 1 
      415 125 125 ALA CB C  21.3  . 1 
      416 125 125 ALA N  N 129.1  . 1 
      417 126 126 THR H  H   9.18 . 1 
      418 126 126 THR C  C 172.7  . 1 
      419 126 126 THR CA C  59.8  . 1 
      420 126 126 THR CB C  70.1  . 1 
      421 126 126 THR N  N 115.5  . 1 
      422 127 127 ARG H  H   8.82 . 1 
      423 127 127 ARG C  C 173.7  . 1 
      424 127 127 ARG CA C  53.4  . 1 
      425 127 127 ARG CB C  33.6  . 1 
      426 127 127 ARG N  N 124.4  . 1 
      427 128 128 LEU H  H   8.69 . 1 
      428 128 128 LEU C  C 174.1  . 1 
      429 128 128 LEU CA C  53.4  . 1 
      430 128 128 LEU CB C  44.1  . 1 
      431 128 128 LEU N  N 127.8  . 1 
      432 129 129 GLU H  H   8.75 . 1 
      433 129 129 GLU C  C 173.0  . 1 
      434 129 129 GLU CA C  54.2  . 1 
      435 129 129 GLU CB C  33.9  . 1 
      436 129 129 GLU N  N 123.4  . 1 
      437 130 130 TYR H  H   8.93 . 1 
      438 130 130 TYR C  C 173.0  . 1 
      439 130 130 TYR CA C  55.8  . 1 
      440 130 130 TYR CB C  41.0  . 1 
      441 130 130 TYR N  N 125.9  . 1 
      442 131 131 GLN H  H   8.53 . 1 
      443 131 131 GLN C  C 173.4  . 1 
      444 131 131 GLN CA C  53.1  . 1 
      445 131 131 GLN CB C  33.9  . 1 
      446 131 131 GLN N  N 128.1  . 1 
      447 132 132 TRP H  H   9.42 . 1 
      448 132 132 TRP C  C 173.1  . 1 
      449 132 132 TRP CA C  57.3  . 1 
      450 132 132 TRP CB C  31.6  . 1 
      451 132 132 TRP N  N 127.7  . 1 
      452 141 141 MET H  H   8.45 . 1 
      453 141 141 MET C  C 174.0  . 1 
      454 141 141 MET CA C  53.8  . 1 
      455 141 141 MET CB C  36.1  . 1 
      456 141 141 MET N  N 119.8  . 1 
      457 142 142 LEU H  H   8.67 . 1 
      458 142 142 LEU C  C 175.2  . 1 
      459 142 142 LEU CA C  52.9  . 1 
      460 142 142 LEU CB C  43.8  . 1 
      461 142 142 LEU N  N 131.2  . 1 
      462 143 143 SER H  H   9.58 . 1 
      463 143 143 SER C  C 171.3  . 1 
      464 143 143 SER CA C  56.5  . 1 
      465 143 143 SER CB C  66.4  . 1 
      466 143 143 SER N  N 119.3  . 1 
      467 144 144 LEU H  H   8.70 . 1 
      468 144 144 LEU C  C 175.2  . 1 
      469 144 144 LEU CA C  52.5  . 1 
      470 144 144 LEU CB C  45.0  . 1 
      471 144 144 LEU N  N 123.0  . 1 
      472 145 145 GLY H  H   9.42 . 1 
      473 145 145 GLY C  C 172.0  . 1 
      474 145 145 GLY CA C  43.9  . 1 
      475 145 145 GLY N  N 111.0  . 1 
      476 146 146 VAL H  H   8.88 . 1 
      477 146 146 VAL C  C 172.8  . 1 
      478 146 146 VAL CA C  59.3  . 1 
      479 146 146 VAL CB C  34.5  . 1 
      480 146 146 VAL N  N 119.0  . 1 
      481 147 147 SER H  H   9.04 . 1 
      482 147 147 SER C  C 172.6  . 1 
      483 147 147 SER CA C  55.7  . 1 
      484 147 147 SER CB C  66.1  . 1 
      485 147 147 SER N  N 117.9  . 1 
      486 148 148 TYR H  H   8.58 . 1 
      487 148 148 TYR C  C 175.0  . 1 
      488 148 148 TYR CA C  55.2  . 1 
      489 148 148 TYR CB C  41.4  . 1 
      490 148 148 TYR N  N 123.1  . 1 
      491 149 149 ARG H  H   8.68 . 1 
      492 149 149 ARG C  C 175.3  . 1 
      493 149 149 ARG CA C  54.3  . 1 
      494 149 149 ARG CB C  31.3  . 1 
      495 149 149 ARG N  N 120.9  . 1 
      496 150 150 PHE H  H   9.03 . 1 
      497 150 150 PHE C  C 175.2  . 1 
      498 150 150 PHE CA C  57.1  . 1 
      499 150 150 PHE CB C  39.6  . 1 
      500 150 150 PHE N  N 123.8  . 1 
      501 151 151 GLY H  H   8.49 . 1 
      502 151 151 GLY C  C 174.0  . 1 
      503 151 151 GLY CA C  44.5  . 1 
      504 151 151 GLY N  N 109.4  . 1 
      505 152 152 GLN H  H   8.55 . 1 
      506 152 152 GLN C  C 176.6  . 1 
      507 152 152 GLN CA C  55.6  . 1 
      508 152 152 GLN CB C  28.7  . 1 
      509 152 152 GLN N  N 120.4  . 1 
      510 153 153 GLY H  H   8.54 . 1 
      511 153 153 GLY C  C 173.9  . 1 
      512 153 153 GLY CA C  44.7  . 1 
      513 153 153 GLY N  N 110.9  . 1 
      514 154 154 GLU H  H   8.24 . 1 
      515 154 154 GLU C  C 175.9  . 1 
      516 154 154 GLU CA C  55.8  . 1 
      517 154 154 GLU CB C  29.4  . 1 
      518 154 154 GLU N  N 121.1  . 1 
      519 155 155 ALA H  H   8.24 . 1 
      520 155 155 ALA C  C 176.0  . 1 
      521 155 155 ALA CA C  51.7  . 1 
      522 155 155 ALA CB C  18.2  . 1 
      523 155 155 ALA N  N 125.7  . 1 
      524 156 156 ALA H  H   7.77 . 1 
      525 156 156 ALA C  C 182.0  . 1 
      526 156 156 ALA CA C  53.1  . 1 
      527 156 156 ALA CB C  19.2  . 1 
      528 156 156 ALA N  N 129.5  . 1 

   stop_

save_