data_4735

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

save_entry_information
   _Saveframe_category      entry_information

   _Entry_title            
;
Sequence-specific NMR resonance assignments for the backbone atoms of olfactory 
marker protein (OMP)
;
   _BMRB_accession_number   4735
   _BMRB_flat_file_name     bmr4735.str
   _Entry_type              original
   _Submission_date         2000-05-03
   _Accession_date          2000-05-03
   _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 Baldisseri Donna  M. . 
      2 Margolis   Joyce  W. . 
      3 Omotosho   Philip A. . 
      4 Volkman    Brian  F. . 
      5 Margolis   Frank  L. . 

   stop_

   loop_
      _Saveframe_category_type
      _Saveframe_category_type_count

      assigned_chemical_shifts 1 

   stop_

   loop_
      _Data_type
      _Data_type_count

      "1H chemical shifts"  317 
      "13C chemical shifts" 453 
      "15N chemical shifts" 150 

   stop_

   loop_
      _Revision_date
      _Revision_keyword
      _Revision_author
      _Revision_detail

      2000-09-25 original author . 

   stop_

   _Original_release_date   2000-09-25

save_


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

save_entry_citation
   _Saveframe_category           entry_citation

   _Citation_full                .
   _Citation_title              
;
Letter to the Editor:
Sequence-specific NMR resonance assignments of the backbone atoms for
the olfactory marker protein, OMP
;
   _Citation_status              published
   _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 Baldisseri Donna  M. . 
      2 Margolis   Joyce  W. . 
      3 Omotosho   Philip A. . 
      4 Volkman    Brian  F. . 
      5 Margolis   Frank  L. . 

   stop_

   _Journal_abbreviation        'J. Biomol. NMR'
   _Journal_volume               17
   _Journal_issue                4
   _Journal_CSD                  .
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_ISBN                    .
   _Conference_state_province    .
   _Conference_abstract_number   .
   _Page_first                   353
   _Page_last                    354
   _Year                         2000
   _Details                      .

save_


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

save_system_OMP
   _Saveframe_category         molecular_system

   _Mol_system_name           'olfactory marker protein'
   _Abbreviation_common        OMP
   _Enzyme_commission_number   .

   loop_
      _Mol_system_component_name
      _Mol_label

      OMP $OMP 

   stop_

   _System_molecular_weight    .
   _System_physical_state      native
   _System_oligomer_state      monomer
   _System_paramagnetic        no
   _System_thiol_state        'not present'
   _Database_query_date        .
   _Details                    .

save_


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

save_OMP
   _Saveframe_category                          monomeric_polymer

   _Mol_type                                    polymer
   _Mol_polymer_class                           protein
   _Name_common                                'olfactory marker protein'
   _Abbreviation_common                         OMP
   _Molecular_mass                              .
   _Mol_thiol_state                            'not present'
   _Details                                     .

   	##############################
   	#  Polymer residue sequence  #
   	##############################
   
      _Residue_count                               163
   _Mol_residue_sequence                       
;
MAEDGPQKQQLDMPLVLDQD
LTKQMRLRVESLKQRGEKKQ
DGEKLLRPAESVYRLDFIQQ
QKLQFDHWNVVLDKPGKVTI
TGTSQNWTPDLTNLMTRQLL
DPAAIFWRKEDSDAMDWNEA
DALEFGERLSDLAKIRKVMY
FLITFGEGVEPANLKASVVF
NQL
;

   loop_
      _Residue_seq_code
      _Residue_label

        1 MET    2 ALA    3 GLU    4 ASP    5 GLY 
        6 PRO    7 GLN    8 LYS    9 GLN   10 GLN 
       11 LEU   12 ASP   13 MET   14 PRO   15 LEU 
       16 VAL   17 LEU   18 ASP   19 GLN   20 ASP 
       21 LEU   22 THR   23 LYS   24 GLN   25 MET 
       26 ARG   27 LEU   28 ARG   29 VAL   30 GLU 
       31 SER   32 LEU   33 LYS   34 GLN   35 ARG 
       36 GLY   37 GLU   38 LYS   39 LYS   40 GLN 
       41 ASP   42 GLY   43 GLU   44 LYS   45 LEU 
       46 LEU   47 ARG   48 PRO   49 ALA   50 GLU 
       51 SER   52 VAL   53 TYR   54 ARG   55 LEU 
       56 ASP   57 PHE   58 ILE   59 GLN   60 GLN 
       61 GLN   62 LYS   63 LEU   64 GLN   65 PHE 
       66 ASP   67 HIS   68 TRP   69 ASN   70 VAL 
       71 VAL   72 LEU   73 ASP   74 LYS   75 PRO 
       76 GLY   77 LYS   78 VAL   79 THR   80 ILE 
       81 THR   82 GLY   83 THR   84 SER   85 GLN 
       86 ASN   87 TRP   88 THR   89 PRO   90 ASP 
       91 LEU   92 THR   93 ASN   94 LEU   95 MET 
       96 THR   97 ARG   98 GLN   99 LEU  100 LEU 
      101 ASP  102 PRO  103 ALA  104 ALA  105 ILE 
      106 PHE  107 TRP  108 ARG  109 LYS  110 GLU 
      111 ASP  112 SER  113 ASP  114 ALA  115 MET 
      116 ASP  117 TRP  118 ASN  119 GLU  120 ALA 
      121 ASP  122 ALA  123 LEU  124 GLU  125 PHE 
      126 GLY  127 GLU  128 ARG  129 LEU  130 SER 
      131 ASP  132 LEU  133 ALA  134 LYS  135 ILE 
      136 ARG  137 LYS  138 VAL  139 MET  140 TYR 
      141 PHE  142 LEU  143 ILE  144 THR  145 PHE 
      146 GLY  147 GLU  148 GLY  149 VAL  150 GLU 
      151 PRO  152 ALA  153 ASN  154 LEU  155 LYS 
      156 ALA  157 SER  158 VAL  159 VAL  160 PHE 
      161 ASN  162 GLN  163 LEU 

   stop_

   _Sequence_homology_query_date                .
   _Sequence_homology_query_revised_last_date   2015-07-28

   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 1JOB         "Crystal Structure Of Murine Olfactory Marker Protein In Spacegroup P3121"                             99.39 162  98.15 100.00 2.50e-111 
      PDB 1JYT         "Solution Structure Of Olfactory Marker Protein From Rat"                                             100.00 163 100.00 100.00 1.61e-113 
      PDB 1ZRI         "Noe-Based Solution Structure With Dipolar Coupling Restraints Of Rat Omp (Olfactory Marker Protein)" 100.00 163 100.00 100.00 1.61e-113 
      DBJ BAE21801     "unnamed protein product [Mus musculus]"                                                              100.00 163  97.55  99.39 3.76e-111 
      GB  AAA03054     "olfactory marker protein [Rattus norvegicus]"                                                        100.00 163 100.00 100.00 1.61e-113 
      GB  AAA18415     "olfactory marker protein [Mus musculus]"                                                             100.00 163  98.16 100.00 3.66e-112 
      GB  AAA20486     "olfactory marker protein [Mus musculus]"                                                             100.00 163  98.16 100.00 3.66e-112 
      GB  AAA41757     "olfactory neuronal specific protein, partial [Rattus norvegicus]"                                     99.39 162 100.00 100.00 9.97e-113 
      GB  AAH46600     "Olfactory marker protein [Mus musculus]"                                                             100.00 163  98.16 100.00 3.66e-112 
      REF NP_035140    "olfactory marker protein [Mus musculus]"                                                             100.00 163  98.16 100.00 3.66e-112 
      REF NP_036748    "olfactory marker protein [Rattus norvegicus]"                                                        100.00 163 100.00 100.00 1.61e-113 
      REF XP_005357594 "PREDICTED: olfactory marker protein [Microtus ochrogaster]"                                          100.00 163  96.93  98.16 2.73e-109 
      REF XP_006979947 "PREDICTED: olfactory marker protein [Peromyscus maniculatus bairdii]"                                100.00 163  98.16  99.39 5.63e-111 
      REF XP_007621284 "PREDICTED: olfactory marker protein [Cricetulus griseus]"                                            100.00 163  98.16  99.39 5.63e-111 
      SP  P08523       "RecName: Full=Olfactory marker protein; AltName: Full=Olfactory neuronal-specific protein"           100.00 163 100.00 100.00 1.61e-113 
      SP  Q64288       "RecName: Full=Olfactory marker protein"                                                              100.00 163  98.16 100.00 3.66e-112 

   stop_

save_


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

save_natural_source
   _Saveframe_category   natural_source


   loop_
      _Mol_label
      _Organism_name_common
      _NCBI_taxonomy_ID
      _Superkingdom
      _Kingdom
      _Genus
      _Species

      $OMP 'Norway rat' 10116 Eukaryota Metazoa rattus norvegicus 

   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

      $OMP 'recombinant technology' . . . . . 

   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

      $OMP 1.5 mM [U-15N] 

   stop_

save_


save_sample_2
   _Saveframe_category   sample

   _Sample_type          solution
   _Details              .

   loop_
      _Mol_label
      _Concentration_value
      _Concentration_value_units
      _Isotopic_labeling

      $OMP 1.8 mM [U-15N;U-13C] 

   stop_

save_


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

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

save_NMR_spectrometer1
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                DMX
   _Field_strength       600
   _Details              .

save_


save_NMR_spectrometer2
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                DMX
   _Field_strength       750
   _Details              .

save_


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

save_2D_1H-15N_HSQC_1
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '2D 1H-15N HSQC'
   _Sample_label         .

save_


save_3D_CBCA(CO)NH_2
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D CBCA(CO)NH'
   _Sample_label         .

save_


save_3D_HNCACB_3
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D HNCACB'
   _Sample_label         .

save_


save_3D_HNCO_4
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D HNCO'
   _Sample_label         .

save_


save_3D_HCACO_5
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D HCACO'
   _Sample_label         .

save_


save_3D_HCA(CO)N_6
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D HCA(CO)N'
   _Sample_label         .

save_


save_3D_HNHA_7
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D HNHA'
   _Sample_label         .

save_


save_3D_15N-NOESY-HSQC_8
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D 15N-NOESY-HSQC'
   _Sample_label         .

save_


save_3D_15N,15N-HMQC-NOESY-HSQC_9
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D 15N,15N-HMQC-NOESY-HSQC'
   _Sample_label         .

save_


save_4D_15N,13C-NOESY_10
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '4D 15N,13C-NOESY'
   _Sample_label         .

save_


save_NMR_spec_expt__0_1
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                       '2D 1H-15N HSQC'
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_2
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                       '3D CBCA(CO)NH'
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_3
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                       '3D HNCACB'
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_4
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                       '3D HNCO'
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_5
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                       '3D HCACO'
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_6
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                       '3D HCA(CO)N'
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_7
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                       '3D HNHA'
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_8
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                       '3D 15N-NOESY-HSQC'
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_9
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                       '3D 15N,15N-HMQC-NOESY-HSQC'
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_10
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                       '4D 15N,13C-NOESY'
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


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

save_cond_1
   _Saveframe_category   sample_conditions

   _Details              .

   loop_
      _Variable_type
      _Variable_value
      _Variable_value_error
      _Variable_value_units

      pH            6.6 0.1 n/a 
      temperature 310   0.1 K   

   stop_

save_


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

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

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

save_chem_shift_ref
   _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

      DSS H  1 'methyl protons' ppm 0.0 internal direct   . . . 1.0         
      DSS N 15 'methyl protons' ppm 0.0 .        indirect . . . 0.101329118 
      DSS C 13 'methyl protons' ppm 0.0 .        indirect . . . 0.251449530 

   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_nmr_parameters
   _Saveframe_category               assigned_chemical_shifts

   _Details                          .

   loop_
      _Sample_label

      $sample_1 

   stop_

   _Sample_conditions_label         $cond_1
   _Chem_shift_reference_set_label  $chem_shift_ref
   _Mol_system_component_name        OMP
   _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 .   2 ALA C   C 177.9  . 1 
        2 .   2 ALA CA  C  52.5  . 1 
        3 .   2 ALA CB  C  18.7  . 1 
        4 .   3 GLU N   N 120.89 . 1 
        5 .   3 GLU H   H   8.56 . 1 
        6 .   3 GLU C   C 177.9  . 1 
        7 .   3 GLU CA  C  56.6  . 1 
        8 .   3 GLU HA  H   4.28 . 1 
        9 .   3 GLU CB  C  29.9  . 1 
       10 .   4 ASP N   N 121.40 . 1 
       11 .   4 ASP H   H   8.27 . 1 
       12 .   4 ASP C   C 176.3  . 1 
       13 .   4 ASP CA  C  54.1  . 1 
       14 .   4 ASP HA  H   4.66 . 1 
       15 .   4 ASP CB  C  40.7  . 1 
       16 .   5 GLY N   N 109.38 . 1 
       17 .   5 GLY H   H   8.04 . 1 
       18 .   5 GLY CA  C  44.4  . 1 
       19 .   5 GLY HA2 H   4.06 . 2 
       20 .   5 GLY HA3 H   3.73 . 2 
       21 .   6 PRO C   C 182.3  . 1 
       22 .   6 PRO CA  C  62.8  . 1 
       23 .   6 PRO HA  H   4.37 . 1 
       24 .   6 PRO CB  C  31.9  . 1 
       25 .   7 GLN N   N 121.14 . 1 
       26 .   7 GLN H   H   8.40 . 1 
       27 .   7 GLN C   C 176.2  . 1 
       28 .   7 GLN CA  C  55.3  . 1 
       29 .   7 GLN HA  H   4.28 . 1 
       30 .   7 GLN CB  C  29.4  . 1 
       31 .   8 LYS N   N 123.21 . 1 
       32 .   8 LYS H   H   8.27 . 1 
       33 .   8 LYS C   C 178.7  . 1 
       34 .   8 LYS CA  C  55.6  . 1 
       35 .   8 LYS HA  H   4.33 . 1 
       36 .   8 LYS CB  C  32.6  . 1 
       37 .   9 GLN N   N 122.94 . 1 
       38 .   9 GLN H   H   8.55 . 1 
       39 .   9 GLN C   C 177.9  . 1 
       40 .   9 GLN CA  C  55.6  . 1 
       41 .   9 GLN HA  H   4.44 . 1 
       42 .   9 GLN CB  C  29.4  . 1 
       43 .  10 GLN N   N 121.55 . 1 
       44 .  10 GLN H   H   8.34 . 1 
       45 .  10 GLN C   C 175.8  . 1 
       46 .  10 GLN CA  C  55.3  . 1 
       47 .  10 GLN HA  H   5.04 . 1 
       48 .  10 GLN CB  C  31.3  . 1 
       49 .  11 LEU N   N 122.97 . 1 
       50 .  11 LEU H   H   9.07 . 1 
       51 .  11 LEU C   C 175.1  . 1 
       52 .  11 LEU CA  C  53.4  . 1 
       53 .  11 LEU HA  H   4.66 . 1 
       54 .  11 LEU CB  C  44.8  . 1 
       55 .  12 ASP N   N 126.46 . 1 
       56 .  12 ASP H   H   8.54 . 1 
       57 .  12 ASP C   C 177.3  . 1 
       58 .  12 ASP CA  C  53.1  . 1 
       59 .  12 ASP HA  H   4.88 . 1 
       60 .  12 ASP CB  C  41.6  . 1 
       61 .  13 MET N   N 125.38 . 1 
       62 .  13 MET H   H   9.06 . 1 
       63 .  13 MET CA  C  52.8  . 1 
       64 .  13 MET HA  H   5.10 . 1 
       65 .  13 MET CB  C  33.2  . 1 
       66 .  14 PRO C   C 175.7  . 1 
       67 .  14 PRO CA  C  62.2  . 1 
       68 .  14 PRO HA  H   4.31 . 1 
       69 .  14 PRO CB  C  32.2  . 1 
       70 .  15 LEU N   N 123.05 . 1 
       71 .  15 LEU H   H   8.43 . 1 
       72 .  15 LEU C   C 176.3  . 1 
       73 .  15 LEU CA  C  55.0  . 1 
       74 .  15 LEU HA  H   4.82 . 1 
       75 .  15 LEU CB  C  42.0  . 1 
       76 .  16 VAL N   N 122.06 . 1 
       77 .  16 VAL H   H   8.95 . 1 
       78 .  16 VAL C   C 175.1  . 1 
       79 .  16 VAL CA  C  59.7  . 1 
       80 .  16 VAL HA  H   4.60 . 1 
       81 .  16 VAL CB  C  34.5  . 1 
       82 .  17 LEU N   N 130.63 . 1 
       83 .  17 LEU H   H   8.32 . 1 
       84 .  17 LEU C   C 175.8  . 1 
       85 .  17 LEU CA  C  56.3  . 1 
       86 .  17 LEU HA  H   5.40 . 1 
       87 .  17 LEU CB  C  41.1  . 1 
       88 .  18 ASP N   N 130.90 . 1 
       89 .  18 ASP H   H   9.45 . 1 
       90 .  18 ASP CA  C  52.5  . 1 
       91 .  18 ASP HA  H   4.82 . 1 
       92 .  18 ASP CB  C  41.1  . 1 
       93 .  19 GLN N   N 127.97 . 1 
       94 .  19 GLN H   H   8.71 . 1 
       95 .  19 GLN C   C 178.7  . 1 
       96 .  19 GLN CA  C  59.4  . 1 
       97 .  19 GLN HA  H   4.00 . 1 
       98 .  19 GLN CB  C  28.6  . 1 
       99 .  20 ASP N   N 120.90 . 1 
      100 .  20 ASP H   H   8.29 . 1 
      101 .  20 ASP C   C 178.8  . 1 
      102 .  20 ASP CA  C  57.5  . 1 
      103 .  20 ASP HA  H   4.55 . 1 
      104 .  20 ASP CB  C  40.6  . 1 
      105 .  21 LEU N   N 123.58 . 1 
      106 .  21 LEU H   H   8.61 . 1 
      107 .  21 LEU C   C 179.4  . 1 
      108 .  21 LEU CA  C  57.2  . 1 
      109 .  21 LEU HA  H   4.22 . 1 
      110 .  21 LEU CB  C  41.6  . 1 
      111 .  22 THR N   N 116.24 . 1 
      112 .  22 THR H   H   8.17 . 1 
      113 .  22 THR C   C 175.5  . 1 
      114 .  22 THR CA  C  68.8  . 1 
      115 .  22 THR HA  H   3.84 . 1 
      116 .  22 THR CB  C  70.7  . 1 
      117 .  23 LYS N   N 120.89 . 1 
      118 .  23 LYS H   H   8.04 . 1 
      119 .  23 LYS C   C 179.0  . 1 
      120 .  23 LYS CA  C  60.0  . 1 
      121 .  23 LYS HA  H   4.06 . 1 
      122 .  23 LYS CB  C  31.4  . 1 
      123 .  24 GLN N   N 119.78 . 1 
      124 .  24 GLN H   H   8.18 . 1 
      125 .  24 GLN C   C 179.9  . 1 
      126 .  24 GLN CA  C  59.1  . 1 
      127 .  24 GLN HA  H   4.06 . 1 
      128 .  24 GLN CB  C  28.4  . 1 
      129 .  25 MET N   N 120.16 . 1 
      130 .  25 MET H   H   8.37 . 1 
      131 .  25 MET C   C 180.4  . 1 
      132 .  25 MET CA  C  60.0  . 1 
      133 .  25 MET HA  H   4.28 . 1 
      134 .  25 MET CB  C  34.1  . 1 
      135 .  26 ARG N   N 122.47 . 1 
      136 .  26 ARG H   H   8.74 . 1 
      137 .  26 ARG C   C 180.2  . 1 
      138 .  26 ARG CA  C  59.5  . 1 
      139 .  26 ARG HA  H   4.22 . 1 
      140 .  26 ARG CB  C  28.1  . 1 
      141 .  27 LEU N   N 121.84 . 1 
      142 .  27 LEU H   H   8.63 . 1 
      143 .  27 LEU C   C 180.1  . 1 
      144 .  27 LEU CA  C  57.2  . 1 
      145 .  27 LEU HA  H   4.17 . 1 
      146 .  27 LEU CB  C  41.3  . 1 
      147 .  28 ARG N   N 122.75 . 1 
      148 .  28 ARG H   H   7.73 . 1 
      149 .  28 ARG C   C 177.7  . 1 
      150 .  28 ARG CA  C  58.8  . 1 
      151 .  28 ARG HA  H   4.28 . 1 
      152 .  28 ARG CB  C  28.4  . 1 
      153 .  29 VAL N   N 118.48 . 1 
      154 .  29 VAL H   H   7.23 . 1 
      155 .  29 VAL C   C 178.8  . 1 
      156 .  29 VAL CA  C  66.9  . 1 
      157 .  29 VAL HA  H   3.62 . 1 
      158 .  29 VAL CB  C  31.7  . 1 
      159 .  30 GLU N   N 119.26 . 1 
      160 .  30 GLU H   H   7.85 . 1 
      161 .  30 GLU C   C 179.3  . 1 
      162 .  30 GLU CA  C  58.8  . 1 
      163 .  30 GLU HA  H   4.17 . 1 
      164 .  30 GLU CB  C  29.4  . 1 
      165 .  31 SER N   N 117.00 . 1 
      166 .  31 SER H   H   8.74 . 1 
      167 .  31 SER C   C 176.9  . 1 
      168 .  31 SER CA  C  61.6  . 1 
      169 .  31 SER HA  H   4.28 . 1 
      170 .  31 SER CB  C  62.7  . 1 
      171 .  32 LEU N   N 121.88 . 1 
      172 .  32 LEU H   H   7.86 . 1 
      173 .  32 LEU C   C 179.5  . 1 
      174 .  32 LEU CA  C  57.8  . 1 
      175 .  32 LEU HA  H   4.00 . 1 
      176 .  32 LEU CB  C  41.6  . 1 
      177 .  33 LYS N   N 118.64 . 1 
      178 .  33 LYS H   H   7.61 . 1 
      179 .  33 LYS C   C 175.1  . 1 
      180 .  33 LYS CA  C  58.8  . 1 
      181 .  33 LYS HA  H   4.11 . 1 
      182 .  33 LYS CB  C  32.2  . 1 
      183 .  34 GLN N   N 119.17 . 1 
      184 .  34 GLN H   H   8.38 . 1 
      185 .  34 GLN C   C 178.0  . 1 
      186 .  34 GLN CA  C  57.8  . 1 
      187 .  34 GLN HA  H   4.11 . 1 
      188 .  34 GLN CB  C  28.6  . 1 
      189 .  35 ARG N   N 116.16 . 1 
      190 .  35 ARG H   H   7.95 . 1 
      191 .  35 ARG C   C 176.9  . 1 
      192 .  35 ARG CA  C  56.3  . 1 
      193 .  35 ARG HA  H   4.38 . 1 
      194 .  35 ARG CB  C  30.8  . 1 
      195 .  36 GLY N   N 110.58 . 1 
      196 .  36 GLY H   H   7.95 . 1 
      197 .  36 GLY C   C 174.8  . 1 
      198 .  36 GLY CA  C  46.3  . 1 
      199 .  36 GLY HA2 H   3.89 . 2 
      200 .  36 GLY HA3 H   3.95 . 2 
      201 .  37 GLU N   N 120.59 . 1 
      202 .  37 GLU H   H   7.88 . 1 
      203 .  37 GLU CA  C  54.7  . 1 
      204 .  37 GLU HA  H   4.44 . 1 
      205 .  37 GLU CB  C  31.7  . 1 
      206 .  38 LYS N   N 122.24 . 1 
      207 .  38 LYS H   H   8.90 . 1 
      208 .  38 LYS CA  C  55.6  . 1 
      209 .  38 LYS HA  H   4.22 . 1 
      210 .  38 LYS CB  C  28.1  . 1 
      211 .  39 LYS N   N 123.73 . 1 
      212 .  39 LYS H   H   8.41 . 1 
      213 .  39 LYS CA  C  55.9  . 1 
      214 .  39 LYS HA  H   4.38 . 1 
      215 .  40 GLN N   N 123.11 . 1 
      216 .  40 GLN H   H   8.61 . 1 
      217 .  40 GLN CA  C  55.6  . 1 
      218 .  40 GLN HA  H   4.38 . 1 
      219 .  40 GLN CB  C  29.5  . 1 
      220 .  41 ASP N   N 124.59 . 1 
      221 .  41 ASP H   H   8.62 . 1 
      222 .  41 ASP C   C 175.8  . 1 
      223 .  41 ASP CA  C  55.9  . 1 
      224 .  41 ASP HA  H   4.66 . 1 
      225 .  41 ASP CB  C  40.7  . 1 
      226 .  42 GLY C   C 174.6  . 1 
      227 .  42 GLY CA  C  45.3  . 1 
      228 .  42 GLY HA2 H   3.77 . 2 
      229 .  42 GLY HA3 H   2.91 . 2 
      230 .  43 GLU N   N 124.23 . 1 
      231 .  43 GLU H   H   8.07 . 1 
      232 .  43 GLU C   C 175.5  . 1 
      233 .  43 GLU CA  C  57.2  . 1 
      234 .  43 GLU HA  H   4.49 . 1 
      235 .  43 GLU CB  C  31.3  . 1 
      236 .  44 LYS N   N 129.21 . 1 
      237 .  44 LYS H   H   9.06 . 1 
      238 .  44 LYS C   C 173.3  . 1 
      239 .  44 LYS CA  C  53.1  . 1 
      240 .  44 LYS HA  H   4.38 . 1 
      241 .  44 LYS CB  C  31.2  . 1 
      242 .  45 LEU N   N 128.27 . 1 
      243 .  45 LEU H   H   8.35 . 1 
      244 .  45 LEU C   C 177.1  . 1 
      245 .  45 LEU CA  C  52.2  . 1 
      246 .  45 LEU HA  H   4.66 . 1 
      247 .  45 LEU CB  C  41.1  . 1 
      248 .  46 LEU N   N 127.07 . 1 
      249 .  46 LEU H   H   8.78 . 1 
      250 .  46 LEU C   C 178.0  . 1 
      251 .  46 LEU CA  C  55.3  . 1 
      252 .  46 LEU HA  H   4.28 . 1 
      253 .  46 LEU CB  C  43.0  . 1 
      254 .  47 ARG N   N 130.23 . 1 
      255 .  47 ARG H   H   9.31 . 1 
      256 .  47 ARG CA  C  54.4  . 1 
      257 .  47 ARG HA  H   4.71 . 1 
      258 .  47 ARG CB  C  28.9  . 1 
      259 .  48 PRO C   C 177.7  . 1 
      260 .  49 ALA N   N 115.88 . 1 
      261 .  49 ALA H   H   7.52 . 1 
      262 .  49 ALA C   C 175.8  . 1 
      263 .  49 ALA CA  C  52.5  . 1 
      264 .  49 ALA HA  H   4.60 . 1 
      265 .  49 ALA CB  C  19.1  . 1 
      266 .  50 GLU N   N 118.20 . 1 
      267 .  50 GLU H   H   8.22 . 1 
      268 .  50 GLU C   C 177.3  . 1 
      269 .  50 GLU CA  C  54.1  . 1 
      270 .  50 GLU HA  H   5.86 . 1 
      271 .  50 GLU CB  C  32.7  . 1 
      272 .  51 SER N   N 115.47 . 1 
      273 .  51 SER H   H   8.98 . 1 
      274 .  51 SER C   C 171.5  . 1 
      275 .  51 SER CA  C  58.8  . 1 
      276 .  51 SER HA  H   5.04 . 1 
      277 .  51 SER CB  C  68.8  . 1 
      278 .  52 VAL N   N 124.56 . 1 
      279 .  52 VAL H   H   8.49 . 1 
      280 .  52 VAL C   C 174.9  . 1 
      281 .  52 VAL CA  C  62.5  . 1 
      282 .  52 VAL HA  H   5.15 . 1 
      283 .  52 VAL CB  C  31.7  . 1 
      284 .  53 TYR N   N 129.04 . 1 
      285 .  53 TYR H   H   9.94 . 1 
      286 .  53 TYR C   C 174.4  . 1 
      287 .  53 TYR CA  C  55.6  . 1 
      288 .  53 TYR HA  H   5.42 . 1 
      289 .  53 TYR CB  C  43.0  . 1 
      290 .  54 ARG N   N 122.03 . 1 
      291 .  54 ARG H   H  10.0  . 1 
      292 .  54 ARG C   C 173.2  . 1 
      293 .  54 ARG CA  C  54.1  . 1 
      294 .  54 ARG HA  H   5.53 . 1 
      295 .  54 ARG CB  C  35.5  . 1 
      296 .  55 LEU N   N 128.29 . 1 
      297 .  55 LEU H   H   8.98 . 1 
      298 .  55 LEU C   C 173.7  . 1 
      299 .  55 LEU CA  C  53.8  . 1 
      300 .  55 LEU HA  H   4.77 . 1 
      301 .  55 LEU CB  C  46.8  . 1 
      302 .  56 ASP N   N 126.39 . 1 
      303 .  56 ASP H   H   8.64 . 1 
      304 .  56 ASP C   C 175.1  . 1 
      305 .  56 ASP CA  C  52.8  . 1 
      306 .  56 ASP HA  H   4.99 . 1 
      307 .  56 ASP CB  C  40.7  . 1 
      308 .  57 PHE N   N 124.33 . 1 
      309 .  57 PHE H   H   8.57 . 1 
      310 .  57 PHE C   C 177.4  . 1 
      311 .  57 PHE CA  C  58.8  . 1 
      312 .  57 PHE HA  H   4.60 . 1 
      313 .  57 PHE CB  C  37.9  . 1 
      314 .  58 ILE N   N 123.67 . 1 
      315 .  58 ILE H   H   7.56 . 1 
      316 .  58 ILE C   C 175.7  . 1 
      317 .  58 ILE CA  C  62.8  . 1 
      318 .  58 ILE HA  H   3.95 . 1 
      319 .  58 ILE CB  C  38.1  . 1 
      320 .  59 GLN N   N 116.02 . 1 
      321 .  59 GLN H   H   7.30 . 1 
      322 .  59 GLN CA  C  54.4  . 1 
      323 .  59 GLN HA  H   4.44 . 1 
      324 .  59 GLN CB  C  31.7  . 1 
      325 .  60 GLN N   N 117.02 . 1 
      326 .  60 GLN H   H   8.28 . 1 
      327 .  60 GLN CA  C  56.3  . 1 
      328 .  60 GLN HA  H   4.06 . 1 
      329 .  61 GLN C   C 174.8  . 1 
      330 .  61 GLN CA  C  54.1  . 1 
      331 .  61 GLN CB  C  30.0  . 1 
      332 .  61 GLN HA  H   4.33 . 1 
      333 .  62 LYS N   N 115.79 . 1 
      334 .  62 LYS H   H   8.72 . 1 
      335 .  62 LYS C   C 174.8  . 1 
      336 .  62 LYS CA  C  56.9  . 1 
      337 .  62 LYS HA  H   3.73 . 1 
      338 .  62 LYS CB  C  29.4  . 1 
      339 .  63 LEU N   N 115.62 . 1 
      340 .  63 LEU H   H   7.51 . 1 
      341 .  63 LEU C   C 177.9  . 1 
      342 .  63 LEU CA  C  53.8  . 1 
      343 .  63 LEU HA  H   4.93 . 1 
      344 .  63 LEU CB  C  44.8  . 1 
      345 .  64 GLN N   N 121.06 . 1 
      346 .  64 GLN H   H   8.67 . 1 
      347 .  64 GLN C   C 175.4  . 1 
      348 .  64 GLN CA  C  53.8  . 1 
      349 .  64 GLN HA  H   4.82 . 1 
      350 .  64 GLN CB  C  33.1  . 1 
      351 .  65 PHE N   N 131.44 . 1 
      352 .  65 PHE H   H   9.51 . 1 
      353 .  65 PHE C   C 175.5  . 1 
      354 .  65 PHE CA  C  60.9  . 1 
      355 .  65 PHE HA  H   4.88 . 1 
      356 .  65 PHE CB  C  39.2  . 1 
      357 .  66 ASP N   N 128.00 . 1 
      358 .  66 ASP H   H   7.92 . 1 
      359 .  66 ASP C   C 174.1  . 1 
      360 .  66 ASP CA  C  55.6  . 1 
      361 .  66 ASP HA  H   4.60 . 1 
      362 .  66 ASP CB  C  44.8  . 1 
      363 .  67 HIS N   N 107.10 . 1 
      364 .  67 HIS H   H   6.81 . 1 
      365 .  67 HIS C   C 172.1  . 1 
      366 .  67 HIS CA  C  56.3  . 1 
      367 .  67 HIS HA  H   4.33 . 1 
      368 .  67 HIS CB  C  28.9  . 1 
      369 .  68 TRP N   N 121.34 . 1 
      370 .  68 TRP H   H   9.15 . 1 
      371 .  68 TRP C   C 176.0  . 1 
      372 .  68 TRP CA  C  57.2  . 1 
      373 .  68 TRP HA  H   4.38 . 1 
      374 .  68 TRP CB  C  31.3  . 1 
      375 .  69 ASN N   N 123.04 . 1 
      376 .  69 ASN H   H   8.74 . 1 
      377 .  69 ASN C   C 173.0  . 1 
      378 .  69 ASN CA  C  51.6  . 1 
      379 .  69 ASN HA  H   4.88 . 1 
      380 .  69 ASN CB  C  37.8  . 1 
      381 .  70 VAL N   N 125.03 . 1 
      382 .  70 VAL H   H   7.68 . 1 
      383 .  70 VAL C   C 174.1  . 1 
      384 .  70 VAL CA  C  61.3  . 1 
      385 .  70 VAL HA  H   4.44 . 1 
      386 .  70 VAL CB  C  32.7  . 1 
      387 .  71 VAL N   N 125.47 . 1 
      388 .  71 VAL H   H   8.68 . 1 
      389 .  71 VAL C   C 175.1  . 1 
      390 .  71 VAL CA  C  60.1  . 1 
      391 .  71 VAL HA  H   4.38 . 1 
      392 .  71 VAL CB  C  35.5  . 1 
      393 .  72 LEU N   N 126.84 . 1 
      394 .  72 LEU H   H   7.73 . 1 
      395 .  72 LEU C   C 177.6  . 1 
      396 .  72 LEU CA  C  51.9  . 1 
      397 .  72 LEU HA  H   5.53 . 1 
      398 .  72 LEU CB  C  45.8  . 1 
      399 .  73 ASP N   N 122.45 . 1 
      400 .  73 ASP H   H   8.78 . 1 
      401 .  73 ASP C   C 174.8  . 1 
      402 .  73 ASP CA  C  53.4  . 1 
      403 .  73 ASP HA  H   4.44 . 1 
      404 .  73 ASP CB  C  39.7  . 1 
      405 .  74 LYS N   N 117.55 . 1 
      406 .  74 LYS H   H   7.45 . 1 
      407 .  74 LYS CA  C  53.4  . 1 
      408 .  74 LYS HA  H   4.66 . 1 
      409 .  74 LYS CB  C  32.2  . 1 
      410 .  75 PRO C   C 175.5  . 1 
      411 .  75 PRO CA  C  63.0  . 1 
      412 .  75 PRO HA  H   4.11 . 1 
      413 .  75 PRO CB  C  31.9  . 1 
      414 .  76 GLY N   N 108.79 . 1 
      415 .  76 GLY H   H   8.31 . 1 
      416 .  76 GLY C   C 170.2  . 1 
      417 .  76 GLY CA  C  44.7  . 1 
      418 .  76 GLY HA2 H   4.28 . 2 
      419 .  76 GLY HA3 H   4.04 . 2 
      420 .  77 LYS N   N 120.62 . 1 
      421 .  77 LYS H   H   7.65 . 1 
      422 .  77 LYS C   C 174.4  . 1 
      423 .  77 LYS CA  C  54.7  . 1 
      424 .  77 LYS HA  H   5.42 . 1 
      425 .  77 LYS CB  C  36.6  . 1 
      426 .  78 VAL N   N 116.70 . 1 
      427 .  78 VAL H   H   9.13 . 1 
      428 .  78 VAL C   C 173.2  . 1 
      429 .  78 VAL CA  C  59.1  . 1 
      430 .  78 VAL HA  H   5.04 . 1 
      431 .  78 VAL CB  C  35.5  . 1 
      432 .  79 THR N   N 118.72 . 1 
      433 .  79 THR H   H   8.08 . 1 
      434 .  79 THR C   C 173.0  . 1 
      435 .  79 THR CA  C  61.6  . 1 
      436 .  79 THR HA  H   4.93 . 1 
      437 .  79 THR CB  C  70.6  . 1 
      438 .  80 ILE N   N 128.71 . 1 
      439 .  80 ILE H   H   9.92 . 1 
      440 .  80 ILE C   C 173.5  . 1 
      441 .  80 ILE CA  C  61.9  . 1 
      442 .  80 ILE HA  H   4.33 . 1 
      443 .  80 ILE CB  C  37.9  . 1 
      444 .  81 THR N   N 124.76 . 1 
      445 .  81 THR H   H   8.84 . 1 
      446 .  81 THR C   C 175.7  . 1 
      447 .  81 THR CA  C  60.9  . 1 
      448 .  81 THR HA  H   5.04 . 1 
      449 .  81 THR CB  C  69.7  . 1 
      450 .  82 GLY N   N 115.44 . 1 
      451 .  82 GLY H   H   9.83 . 1 
      452 .  82 GLY C   C 171.3  . 1 
      453 .  82 GLY CA  C  45.3  . 1 
      454 .  82 GLY HA2 H   4.24 . 2 
      455 .  82 GLY HA3 H   3.31 . 2 
      456 .  83 THR N   N 109.28 . 1 
      457 .  83 THR H   H   7.08 . 1 
      458 .  83 THR C   C 172.9  . 1 
      459 .  83 THR CA  C  59.1  . 1 
      460 .  83 THR HA  H   5.31 . 1 
      461 .  83 THR CB  C  72.0  . 1 
      462 .  84 SER N   N 110.73 . 1 
      463 .  84 SER H   H   8.54 . 1 
      464 .  84 SER CA  C  58.1  . 1 
      465 .  84 SER HA  H   4.28 . 1 
      466 .  84 SER CB  C  64.1  . 1 
      467 .  85 GLN C   C 175.1  . 1 
      468 .  85 GLN HA  H   5.3  . 1 
      469 .  85 GLN CB  C  29.7  . 1 
      470 .  86 ASN N   N 114.46 . 1 
      471 .  86 ASN H   H   8.15 . 1 
      472 .  86 ASN C   C 176.2  . 1 
      473 .  86 ASN CA  C  52.5  . 1 
      474 .  86 ASN HA  H   4.71 . 1 
      475 .  86 ASN CB  C  38.8  . 1 
      476 .  87 TRP N   N 121.89 . 1 
      477 .  87 TRP H   H   7.94 . 1 
      478 .  87 TRP C   C 176.0  . 1 
      479 .  87 TRP CA  C  56.6  . 1 
      480 .  87 TRP HA  H   4.99 . 1 
      481 .  87 TRP CB  C  27.5  . 1 
      482 .  88 THR N   N 126.82 . 1 
      483 .  88 THR H   H   8.38 . 1 
      484 .  88 THR CA  C  57.5  . 1 
      485 .  88 THR HA  H   4.49 . 1 
      486 .  88 THR CB  C  69.3  . 1 
      487 .  89 PRO C   C 176.3  . 1 
      488 .  89 PRO CA  C  64.7  . 1 
      489 .  89 PRO HA  H   3.77 . 1 
      490 .  89 PRO CB  C  32.2  . 1 
      491 .  90 ASP N   N 112.92 . 1 
      492 .  90 ASP H   H   8.36 . 1 
      493 .  90 ASP C   C 176.2  . 1 
      494 .  90 ASP CA  C  54.7  . 1 
      495 .  90 ASP HA  H   4.38 . 1 
      496 .  90 ASP CB  C  39.7  . 1 
      497 .  91 LEU N   N 118.31 . 1 
      498 .  91 LEU H   H   7.73 . 1 
      499 .  91 LEU C   C 177.4  . 1 
      500 .  91 LEU CA  C  55.6  . 1 
      501 .  91 LEU HA  H   4.60 . 1 
      502 .  91 LEU CB  C  45.2  . 1 
      503 .  92 THR N   N 109.16 . 1 
      504 .  92 THR H   H   7.82 . 1 
      505 .  92 THR CA  C  59.7  . 1 
      506 .  92 THR HA  H   4.77 . 1 
      507 .  92 THR CB  C  71.6  . 1 
      508 .  93 ASN C   C 174.8  . 1 
      509 .  93 ASN CA  C  53.1  . 1 
      510 .  93 ASN CB  C  38.7  . 1 
      511 .  94 LEU N   N 126.25 . 1 
      512 .  94 LEU H   H   8.82 . 1 
      513 .  94 LEU C   C 174.9  . 1 
      514 .  94 LEU CA  C  55.3  . 1 
      515 .  94 LEU HA  H   3.29 . 1 
      516 .  94 LEU CB  C  40.7  . 1 
      517 .  95 MET N   N 123.01 . 1 
      518 .  95 MET H   H   7.66 . 1 
      519 .  95 MET C   C 178.5  . 1 
      520 .  95 MET CA  C  52.2  . 1 
      521 .  95 MET HA  H   5.10 . 1 
      522 .  95 MET CB  C  33.6  . 1 
      523 .  96 THR N   N 119.49 . 1 
      524 .  96 THR H   H   8.99 . 1 
      525 .  96 THR C   C 175.1  . 1 
      526 .  96 THR CA  C  66.6  . 1 
      527 .  96 THR HA  H   3.62 . 1 
      528 .  96 THR CB  C  67.8  . 1 
      529 .  97 ARG N   N 122.07 . 1 
      530 .  97 ARG H   H   8.30 . 1 
      531 .  97 ARG C   C 176.5  . 1 
      532 .  97 ARG CA  C  55.0  . 1 
      533 .  97 ARG HA  H   4.44 . 1 
      534 .  97 ARG CB  C  35.4  . 1 
      535 .  98 GLN N   N 118.01 . 1 
      536 .  98 GLN H   H   7.86 . 1 
      537 .  98 GLN C   C 174.4  . 1 
      538 .  98 GLN CA  C  55.3  . 1 
      539 .  98 GLN HA  H   4.28 . 1 
      540 .  98 GLN CB  C  28.9  . 1 
      541 .  99 LEU N   N 120.72 . 1 
      542 .  99 LEU H   H   7.24 . 1 
      543 .  99 LEU C   C 176.6  . 1 
      544 .  99 LEU CA  C  54.4  . 1 
      545 .  99 LEU HA  H   4.60 . 1 
      546 .  99 LEU CB  C  40.2  . 1 
      547 . 100 LEU N   N 123.59 . 1 
      548 . 100 LEU H   H   8.13 . 1 
      549 . 100 LEU C   C 176.8  . 1 
      550 . 100 LEU CA  C  54.4  . 1 
      551 . 100 LEU HA  H   4.28 . 1 
      552 . 100 LEU CB  C  42.0  . 1 
      553 . 101 ASP N   N 124.72 . 1 
      554 . 101 ASP H   H   8.37 . 1 
      555 . 101 ASP CA  C  50.6  . 1 
      556 . 101 ASP HA  H   4.71 . 1 
      557 . 101 ASP CB  C  43.9  . 1 
      558 . 102 PRO C   C 174.9  . 1 
      559 . 102 PRO CA  C  62.5  . 1 
      560 . 102 PRO HA  H   4.77 . 1 
      561 . 102 PRO CB  C  34.4  . 1 
      562 . 103 ALA N   N 121.50 . 1 
      563 . 103 ALA H   H   7.94 . 1 
      564 . 103 ALA C   C 176.8  . 1 
      565 . 103 ALA CA  C  50.6  . 1 
      566 . 103 ALA HA  H   4.60 . 1 
      567 . 103 ALA CB  C  20.9  . 1 
      568 . 104 ALA N   N 122.90 . 1 
      569 . 104 ALA H   H   8.52 . 1 
      570 . 104 ALA C   C 173.8  . 1 
      571 . 104 ALA CA  C  50.3  . 1 
      572 . 104 ALA HA  H   4.71 . 1 
      573 . 104 ALA CB  C  20.5  . 1 
      574 . 105 ILE N   N 125.66 . 1 
      575 . 105 ILE H   H   8.66 . 1 
      576 . 105 ILE C   C 173.5  . 1 
      577 . 105 ILE CA  C  60.6  . 1 
      578 . 105 ILE HA  H   4.88 . 1 
      579 . 105 ILE CB  C  40.2  . 1 
      580 . 106 PHE N   N 122.68 . 1 
      581 . 106 PHE H   H   8.70 . 1 
      582 . 106 PHE C   C 174.9  . 1 
      583 . 106 PHE CA  C  55.4  . 1 
      584 . 106 PHE HA  H   5.31 . 1 
      585 . 106 PHE CB  C  43.1  . 1 
      586 . 107 TRP N   N 119.52 . 1 
      587 . 107 TRP H   H   9.10 . 1 
      588 . 107 TRP C   C 172.1  . 1 
      589 . 107 TRP CA  C  56.3  . 1 
      590 . 107 TRP HA  H   5.70 . 1 
      591 . 107 TRP CB  C  32.2  . 1 
      592 . 108 ARG N   N 121.95 . 1 
      593 . 108 ARG H   H   8.98 . 1 
      594 . 108 ARG C   C 176.6  . 1 
      595 . 108 ARG CA  C  54.4  . 1 
      596 . 108 ARG HA  H   5.15 . 1 
      597 . 108 ARG CB  C  33.6  . 1 
      598 . 109 LYS N   N 128.63 . 1 
      599 . 109 LYS H   H   9.40 . 1 
      600 . 109 LYS C   C 176.5  . 1 
      601 . 109 LYS CA  C  56.0  . 1 
      602 . 109 LYS HA  H   4.60 . 1 
      603 . 109 LYS CB  C  33.6  . 1 
      604 . 110 GLU N   N 119.40 . 1 
      605 . 110 GLU H   H   8.88 . 1 
      606 . 110 GLU C   C 176.9  . 1 
      607 . 110 GLU CA  C  58.4  . 1 
      608 . 110 GLU HA  H   4.06 . 1 
      609 . 110 GLU CB  C  29.8  . 1 
      610 . 111 ASP N   N 116.85 . 1 
      611 . 111 ASP H   H   8.48 . 1 
      612 . 111 ASP C   C 175.4  . 1 
      613 . 111 ASP CA  C  54.1  . 1 
      614 . 111 ASP HA  H   4.49 . 1 
      615 . 111 ASP CB  C  39.7  . 1 
      616 . 112 SER N   N 112.46 . 1 
      617 . 112 SER H   H   7.45 . 1 
      618 . 112 SER C   C 171.3  . 1 
      619 . 112 SER CA  C  56.9  . 1 
      620 . 112 SER HA  H   4.71 . 1 
      621 . 112 SER CB  C  64.5  . 1 
      622 . 113 ASP N   N 124.09 . 1 
      623 . 113 ASP H   H   8.50 . 1 
      624 . 113 ASP C   C 175.2  . 1 
      625 . 113 ASP CA  C  53.8  . 1 
      626 . 113 ASP HA  H   4.60 . 1 
      627 . 114 ALA N   N 123.19 . 1 
      628 . 114 ALA H   H   7.95 . 1 
      629 . 114 ALA C   C 177.3  . 1 
      630 . 114 ALA CA  C  51.3  . 1 
      631 . 114 ALA HA  H   4.49 . 1 
      632 . 114 ALA CB  C  20.5  . 1 
      633 . 115 MET N   N 119.29 . 1 
      634 . 115 MET H   H   8.30 . 1 
      635 . 115 MET C   C 175.8  . 1 
      636 . 115 MET CA  C  52.5  . 1 
      637 . 115 MET HA  H   5.15 . 1 
      638 . 115 MET CB  C  30.8  . 1 
      639 . 116 ASP N   N 124.40 . 1 
      640 . 116 ASP H   H   9.08 . 1 
      641 . 116 ASP C   C 173.7  . 1 
      642 . 116 ASP CA  C  52.5  . 1 
      643 . 116 ASP HA  H   4.71 . 1 
      644 . 116 ASP CB  C  42.5  . 1 
      645 . 117 TRP N   N 116.93 . 1 
      646 . 117 TRP H   H   8.19 . 1 
      647 . 117 TRP C   C 175.1  . 1 
      648 . 117 TRP CA  C  55.6  . 1 
      649 . 117 TRP HA  H   4.99 . 1 
      650 . 117 TRP CB  C  29.8  . 1 
      651 . 118 ASN N   N 119.20 . 1 
      652 . 118 ASN H   H   8.42 . 1 
      653 . 118 ASN C   C 174.9  . 1 
      654 . 118 ASN CA  C  51.4  . 1 
      655 . 118 ASN HA  H   4.88 . 1 
      656 . 118 ASN CB  C  36.1  . 1 
      657 . 119 GLU N   N 124.22 . 1 
      658 . 119 GLU H   H   7.39 . 1 
      659 . 119 GLU C   C 176.8  . 1 
      660 . 119 GLU CA  C  60.0  . 1 
      661 . 119 GLU HA  H   4.71 . 1 
      662 . 119 GLU CB  C  29.9  . 1 
      663 . 120 ALA N   N 121.10 . 1 
      664 . 120 ALA H   H   8.44 . 1 
      665 . 120 ALA C   C 181.0  . 1 
      666 . 120 ALA CA  C  55.6  . 1 
      667 . 120 ALA HA  H   4.11 . 1 
      668 . 120 ALA CB  C  18.2  . 1 
      669 . 121 ASP N   N 119.59 . 1 
      670 . 121 ASP H   H   7.86 . 1 
      671 . 121 ASP C   C 176.6  . 1 
      672 . 121 ASP CA  C  56.6  . 1 
      673 . 121 ASP HA  H   4.55 . 1 
      674 . 121 ASP CB  C  40.6  . 1 
      675 . 122 ALA N   N 121.71 . 1 
      676 . 122 ALA H   H   8.27 . 1 
      677 . 122 ALA C   C 176.5  . 1 
      678 . 122 ALA CA  C  55.3  . 1 
      679 . 122 ALA HA  H   4.66 . 1 
      680 . 122 ALA CB  C  17.6  . 1 
      681 . 123 LEU N   N 122.07 . 1 
      682 . 123 LEU H   H   8.53 . 1 
      683 . 123 LEU C   C 178.0  . 1 
      684 . 123 LEU CA  C  58.1  . 1 
      685 . 123 LEU HA  H   4.44 . 1 
      686 . 123 LEU CB  C  41.6  . 1 
      687 . 124 GLU N   N 121.19 . 1 
      688 . 124 GLU H   H   7.90 . 1 
      689 . 124 GLU C   C 179.4  . 1 
      690 . 124 GLU CA  C  59.4  . 1 
      691 . 124 GLU HA  H   4.11 . 1 
      692 . 124 GLU CB  C  28.9  . 1 
      693 . 125 PHE N   N 118.15 . 1 
      694 . 125 PHE H   H   8.28 . 1 
      695 . 125 PHE C   C 177.7  . 1 
      696 . 125 PHE CA  C  58.1  . 1 
      697 . 125 PHE HA  H   4.66 . 1 
      698 . 125 PHE CB  C  38.8  . 1 
      699 . 126 GLY N   N 106.51 . 1 
      700 . 126 GLY H   H   8.24 . 1 
      701 . 126 GLY C   C 175.4  . 1 
      702 . 126 GLY CA  C  45.6  . 1 
      703 . 126 GLY HA2 H   2.53 . 1 
      704 . 126 GLY HA3 H   1.76 . 1 
      705 . 127 GLU N   N 118.56 . 1 
      706 . 127 GLU H   H   8.05 . 1 
      707 . 127 GLU C   C 179.9  . 1 
      708 . 127 GLU CA  C  58.1  . 1 
      709 . 127 GLU HA  H   4.06 . 1 
      710 . 127 GLU CB  C  29.4  . 1 
      711 . 128 ARG N   N 118.46 . 1 
      712 . 128 ARG H   H   7.74 . 1 
      713 . 128 ARG C   C 179.4  . 1 
      714 . 128 ARG CA  C  57.8  . 1 
      715 . 128 ARG HA  H   4.38 . 1 
      716 . 128 ARG CB  C  30.8  . 1 
      717 . 129 LEU N   N 118.45 . 1 
      718 . 129 LEU H   H   8.04 . 1 
      719 . 129 LEU C   C 178.5  . 1 
      720 . 129 LEU CA  C  58.6  . 1 
      721 . 129 LEU HA  H   4.06 . 1 
      722 . 129 LEU CB  C  41.8  . 1 
      723 . 130 SER N   N 111.18 . 1 
      724 . 130 SER H   H   7.94 . 1 
      725 . 130 SER C   C 176.0  . 1 
      726 . 130 SER CA  C  61.6  . 1 
      727 . 130 SER HA  H   3.89 . 1 
      728 . 130 SER CB  C  62.2  . 1 
      729 . 131 ASP N   N 121.00 . 1 
      730 . 131 ASP H   H   7.50 . 1 
      731 . 131 ASP C   C 179.9  . 1 
      732 . 131 ASP CA  C  56.6  . 1 
      733 . 131 ASP HA  H   4.66 . 1 
      734 . 131 ASP CB  C  41.1  . 1 
      735 . 132 LEU N   N 123.25 . 1 
      736 . 132 LEU H   H   8.09 . 1 
      737 . 132 LEU C   C 180.4  . 1 
      738 . 132 LEU CA  C  57.8  . 1 
      739 . 132 LEU HA  H   4.22 . 1 
      740 . 132 LEU CB  C  39.7  . 1 
      741 . 133 ALA N   N 123.13 . 1 
      742 . 133 ALA H   H   7.78 . 1 
      743 . 133 ALA C   C 176.8  . 1 
      744 . 133 ALA CA  C  53.8  . 1 
      745 . 133 ALA HA  H   3.29 . 1 
      746 . 133 ALA CB  C  17.7  . 1 
      747 . 134 LYS N   N 111.18 . 1 
      748 . 134 LYS H   H   6.85 . 1 
      749 . 134 LYS C   C 178.3  . 1 
      750 . 134 LYS CA  C  57.8  . 1 
      751 . 134 LYS HA  H   3.84 . 1 
      752 . 134 LYS CB  C  32.7  . 1 
      753 . 135 ILE N   N 117.58 . 1 
      754 . 135 ILE H   H   7.35 . 1 
      755 . 135 ILE C   C 176.3  . 1 
      756 . 135 ILE CA  C  63.1  . 1 
      757 . 135 ILE HA  H   3.78 . 1 
      758 . 135 ILE CB  C  38.3  . 1 
      759 . 136 ARG N   N 113.29 . 1 
      760 . 136 ARG H   H   7.19 . 1 
      761 . 136 ARG C   C 173.8  . 1 
      762 . 136 ARG CA  C  55.3  . 1 
      763 . 136 ARG HA  H   4.66 . 1 
      764 . 136 ARG CB  C  31.3  . 1 
      765 . 137 LYS N   N 117.60 . 1 
      766 . 137 LYS H   H   8.21 . 1 
      767 . 137 LYS C   C 174.3  . 1 
      768 . 137 LYS CA  C  58.4  . 1 
      769 . 137 LYS HA  H   4.22 . 1 
      770 . 138 VAL N   N 118.54 . 1 
      771 . 138 VAL H   H   7.28 . 1 
      772 . 138 VAL C   C 173.4  . 1 
      773 . 138 VAL CA  C  58.4  . 1 
      774 . 138 VAL HA  H   5.37 . 1 
      775 . 138 VAL CB  C  35.0  . 1 
      776 . 139 MET N   N 125.08 . 1 
      777 . 139 MET H   H   8.39 . 1 
      778 . 139 MET C   C 172.9  . 1 
      779 . 139 MET CA  C  54.7  . 1 
      780 . 139 MET HA  H   4.82 . 1 
      781 . 139 MET CB  C  36.0  . 1 
      782 . 140 TYR N   N 124.02 . 1 
      783 . 140 TYR H   H   9.09 . 1 
      784 . 140 TYR C   C 176.3  . 1 
      785 . 140 TYR CA  C  57.2  . 1 
      786 . 140 TYR HA  H   5.70 . 1 
      787 . 140 TYR CB  C  40.2  . 1 
      788 . 141 PHE N   N 121.23 . 1 
      789 . 141 PHE H   H   9.86 . 1 
      790 . 141 PHE C   C 175.1  . 1 
      791 . 141 PHE CA  C  55.3  . 1 
      792 . 141 PHE HA  H   5.48 . 1 
      793 . 141 PHE CB  C  43.0  . 1 
      794 . 142 LEU N   N 122.34 . 1 
      795 . 142 LEU H   H   9.70 . 1 
      796 . 142 LEU C   C 177.3  . 1 
      797 . 142 LEU CA  C  54.1  . 1 
      798 . 142 LEU HA  H   5.31 . 1 
      799 . 142 LEU CB  C  43.0  . 1 
      800 . 143 ILE N   N 127.49 . 1 
      801 . 143 ILE H   H   9.28 . 1 
      802 . 143 ILE C   C 175.1  . 1 
      803 . 143 ILE CA  C  60.3  . 1 
      804 . 143 ILE HA  H   5.20 . 1 
      805 . 143 ILE CB  C  36.4  . 1 
      806 . 144 THR N   N 123.46 . 1 
      807 . 144 THR H   H   9.07 . 1 
      808 . 144 THR C   C 174.8  . 1 
      809 . 144 THR CA  C  61.6  . 1 
      810 . 144 THR HA  H   4.71 . 1 
      811 . 144 THR CB  C  68.7  . 1 
      812 . 145 PHE N   N 130.74 . 1 
      813 . 145 PHE H   H   9.55 . 1 
      814 . 145 PHE C   C 176.6  . 1 
      815 . 145 PHE CA  C  58.8  . 1 
      816 . 145 PHE HA  H   4.38 . 1 
      817 . 145 PHE CB  C  38.1  . 1 
      818 . 146 GLY N   N 112.63 . 1 
      819 . 146 GLY H   H   8.69 . 1 
      820 . 146 GLY C   C 172.1  . 1 
      821 . 146 GLY CA  C  44.1  . 1 
      822 . 146 GLY HA2 H   4.17 . 2 
      823 . 146 GLY HA3 H   4.0  . 2 
      824 . 147 GLU N   N 118.26 . 1 
      825 . 147 GLU H   H   8.25 . 1 
      826 . 147 GLU CA  C  58.1  . 1 
      827 . 147 GLU HA  H   4.06 . 1 
      828 . 147 GLU CB  C  28.9  . 1 
      829 . 148 GLY N   N 112.24 . 1 
      830 . 148 GLY H   H   8.81 . 1 
      831 . 148 GLY C   C 174.1  . 1 
      832 . 148 GLY CA  C  45.3  . 1 
      833 . 148 GLY HA2 H   3.78 . 1 
      834 . 148 GLY HA3 H   4.38 . 1 
      835 . 149 VAL N   N 114.98 . 1 
      836 . 149 VAL H   H   7.77 . 1 
      837 . 149 VAL C   C 173.3  . 1 
      838 . 149 VAL CA  C  60.0  . 1 
      839 . 149 VAL HA  H   4.71 . 1 
      840 . 149 VAL CB  C  35.0  . 1 
      841 . 150 GLU N   N 122.71 . 1 
      842 . 150 GLU H   H   8.73 . 1 
      843 . 150 GLU CA  C  53.8  . 1 
      844 . 150 GLU HA  H   4.17 . 1 
      845 . 150 GLU CB  C  28.4  . 1 
      846 . 151 PRO C   C 173.3  . 1 
      847 . 151 PRO CA  C  68.1  . 1 
      848 . 151 PRO HA  H   4.64 . 1 
      849 . 151 PRO CB  C  31.6  . 1 
      850 . 152 ALA N   N 117.04 . 1 
      851 . 152 ALA H   H   8.18 . 1 
      852 . 152 ALA C   C 179.4  . 1 
      853 . 152 ALA CA  C  54.1  . 1 
      854 . 152 ALA HA  H   4.17 . 1 
      855 . 152 ALA CB  C  18.6  . 1 
      856 . 153 ASN N   N 112.66 . 1 
      857 . 153 ASN H   H   8.48 . 1 
      858 . 153 ASN C   C 173.0  . 1 
      859 . 153 ASN CA  C  55.0  . 1 
      860 . 153 ASN HA  H   4.99 . 1 
      861 . 153 ASN CB  C  41.6  . 1 
      862 . 154 LEU N   N 121.55 . 1 
      863 . 154 LEU H   H   7.82 . 1 
      864 . 154 LEU C   C 175.1  . 1 
      865 . 154 LEU CA  C  53.8  . 1 
      866 . 154 LEU HA  H   5.10 . 1 
      867 . 154 LEU CB  C  45.8  . 1 
      868 . 155 LYS N   N 128.59 . 1 
      869 . 155 LYS H   H   8.56 . 1 
      870 . 155 LYS C   C 174.3  . 1 
      871 . 155 LYS CA  C  56.3  . 1 
      872 . 155 LYS HA  H   4.55 . 1 
      873 . 155 LYS CB  C  33.6  . 1 
      874 . 156 ALA N   N 127.88 . 1 
      875 . 156 ALA H   H   9.08 . 1 
      876 . 156 ALA C   C 174.9  . 1 
      877 . 156 ALA CA  C  50.0  . 1 
      878 . 156 ALA HA  H   5.48 . 1 
      879 . 156 ALA CB  C  21.4  . 1 
      880 . 157 SER N   N 118.94 . 1 
      881 . 157 SER H   H   8.87 . 1 
      882 . 157 SER C   C 171.3  . 1 
      883 . 157 SER CA  C  57.2  . 1 
      884 . 157 SER HA  H   4.77 . 1 
      885 . 157 SER CB  C  65.5  . 1 
      886 . 158 VAL N   N 118.60 . 1 
      887 . 158 VAL H   H   8.47 . 1 
      888 . 158 VAL C   C 172.7  . 1 
      889 . 158 VAL CA  C  60.6  . 1 
      890 . 158 VAL HA  H   3.95 . 1 
      891 . 158 VAL CB  C  33.6  . 1 
      892 . 159 VAL N   N 124.63 . 1 
      893 . 159 VAL H   H   7.82 . 1 
      894 . 159 VAL C   C 175.1  . 1 
      895 . 159 VAL CA  C  60.6  . 1 
      896 . 159 VAL HA  H   4.71 . 1 
      897 . 159 VAL CB  C  30.8  . 1 
      898 . 160 PHE N   N 125.19 . 1 
      899 . 160 PHE H   H   8.93 . 1 
      900 . 160 PHE C   C 175.7  . 1 
      901 . 160 PHE CA  C  55.9  . 1 
      902 . 160 PHE HA  H   4.88 . 1 
      903 . 160 PHE CB  C  43.0  . 1 
      904 . 161 ASN N   N 118.83 . 1 
      905 . 161 ASN H   H   9.71 . 1 
      906 . 161 ASN C   C 174.8  . 1 
      907 . 161 ASN CA  C  52.5  . 1 
      908 . 161 ASN HA  H   5.26 . 1 
      909 . 161 ASN CB  C  39.7  . 1 
      910 . 162 GLN N   N 121.82 . 1 
      911 . 162 GLN H   H   8.55 . 1 
      912 . 162 GLN C   C 175.2  . 1 
      913 . 162 GLN CA  C  55.3  . 1 
      914 . 162 GLN HA  H   4.77 . 1 
      915 . 162 GLN CB  C  30.8  . 1 
      916 . 163 LEU N   N 132.41 . 1 
      917 . 163 LEU H   H   8.42 . 1 
      918 . 163 LEU CA  C  55.3  . 1 
      919 . 163 LEU HA  H   4.22 . 1 
      920 . 163 LEU CB  C  42.1  . 1 

   stop_

save_