data_6338

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

save_entry_information
   _Saveframe_category      entry_information

   _Entry_title            
;
NMR solution structure of At1g77540 
;
   _BMRB_accession_number   6338
   _BMRB_flat_file_name     bmr6338.str
   _Entry_type              original
   _Submission_date         2004-10-05
   _Accession_date          2004-10-05
   _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 Tyler   Robert   C. . 
      2 Singh   Shanteri .  . 
      3 Tonelli Marco    .  . 
      4 Lee     Min      .  . 
      5 Markley John     L. . 

   stop_

   loop_
      _Saveframe_category_type
      _Saveframe_category_type_count

      assigned_chemical_shifts 1 

   stop_

   loop_
      _Data_type
      _Data_type_count

      "1H chemical shifts"  447 
      "13C chemical shifts" 367 
      "15N chemical shifts"  95 

   stop_

   loop_
      _Revision_date
      _Revision_keyword
      _Revision_author
      _Revision_detail

      2007-11-09 update   BMRB   'complete the entry citation' 
      2005-12-28 original author 'original release'            

   stop_

save_


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

save_entry_citation
   _Saveframe_category           entry_citation

   _Citation_full                .
   _Citation_title              'Structure of Arabidopsis thaliana At1g77540 Protein, a Minimal Acetyltransferase from the COG2388 Family'
   _Citation_status              published
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              .
   _PubMed_ID                    17128971

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

       1 Tyler     Robert      C. .   
       2 Bitto     Eduard      .  .   
       3 Berndsen  Christopher E. .   
       4 Bingman   Craig       A. .   
       5 Singh     Shanteri    .  .   
       6 Lee       Min         S. .   
       7 Wesenberg Gary        E. .   
       8 Denu      John        M. .   
       9 Phillips  George      N. Jr. 
      10 Markley   John        L. .   

   stop_

   _Journal_abbreviation         Biochemistry
   _Journal_volume               45
   _Journal_issue                48
   _Journal_CSD                  .
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_ISBN                    .
   _Conference_state_province    .
   _Conference_abstract_number   .
   _Page_first                   14325
   _Page_last                    14336
   _Year                         2006
   _Details                      .

save_


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

save_molecular_system_At1g77540
   _Saveframe_category         molecular_system

   _Mol_system_name            At1g77540
   _Abbreviation_common        At1g77540
   _Enzyme_commission_number   .

   loop_
      _Mol_system_component_name
      _Mol_label

      At1g77540 $At1g77540 

   stop_

   _System_molecular_weight    .
   _System_physical_state      native
   _System_oligomer_state      monomer
   _System_paramagnetic        no
   _System_thiol_state        'all free'
   _Database_query_date        .
   _Details                    .

save_


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

save_At1g77540
   _Saveframe_category                          monomeric_polymer

   _Mol_type                                    polymer
   _Mol_polymer_class                           protein
   _Name_common                                 At1g77540
   _Abbreviation_common                         At1g77540
   _Molecular_mass                              .
   _Mol_thiol_state                            'all free'
   _Details                                     .

   	##############################
   	#  Polymer residue sequence  #
   	##############################
   
      _Residue_count                               103
   _Mol_residue_sequence                       
;
MATEPPKIVWNEGKRRFETE
DHEAFIEYKMRNNGKVMDLV
HTYVPSFKRGLGLASHLCVA
AFEHASSHSISIIPSCSYVS
DTFLPRNPSWKPLIHSEVFK
SSI
;

   loop_
      _Residue_seq_code
      _Residue_label

        1 MET    2 ALA    3 THR    4 GLU    5 PRO 
        6 PRO    7 LYS    8 ILE    9 VAL   10 TRP 
       11 ASN   12 GLU   13 GLY   14 LYS   15 ARG 
       16 ARG   17 PHE   18 GLU   19 THR   20 GLU 
       21 ASP   22 HIS   23 GLU   24 ALA   25 PHE 
       26 ILE   27 GLU   28 TYR   29 LYS   30 MET 
       31 ARG   32 ASN   33 ASN   34 GLY   35 LYS 
       36 VAL   37 MET   38 ASP   39 LEU   40 VAL 
       41 HIS   42 THR   43 TYR   44 VAL   45 PRO 
       46 SER   47 PHE   48 LYS   49 ARG   50 GLY 
       51 LEU   52 GLY   53 LEU   54 ALA   55 SER 
       56 HIS   57 LEU   58 CYS   59 VAL   60 ALA 
       61 ALA   62 PHE   63 GLU   64 HIS   65 ALA 
       66 SER   67 SER   68 HIS   69 SER   70 ILE 
       71 SER   72 ILE   73 ILE   74 PRO   75 SER 
       76 CYS   77 SER   78 TYR   79 VAL   80 SER 
       81 ASP   82 THR   83 PHE   84 LEU   85 PRO 
       86 ARG   87 ASN   88 PRO   89 SER   90 TRP 
       91 LYS   92 PRO   93 LEU   94 ILE   95 HIS 
       96 SER   97 GLU   98 VAL   99 PHE  100 LYS 
      101 SER  102 SER  103 ILE 

   stop_

   _Sequence_homology_query_date                .
   _Sequence_homology_query_revised_last_date   2014-10-26

   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 1XMT      "X-ray Structure Of Gene Product From Arabidopsis Thaliana At1g77540"                                        99.03 103 100.00 100.00 1.01e-68 
      PDB 2EVN      "Nmr Solution Structures Of At1g77540"                                                                      100.00 103 100.00 100.00 1.06e-69 
      PDB 2IL4      "Crystal Structure Of At1g77540-Coenzyme A Complex"                                                         100.00 103 100.00 100.00 1.06e-69 
      PDB 2Q44      "Ensemble Refinement Of The Protein Crystal Structure Of Gene Product From Arabidopsis Thaliana At1g77540"   99.03 103 100.00 100.00 1.01e-68 
      PDB 2Q4Y      "Ensemble Refinement Of The Protein Crystal Structure Of At1g77540- Coenzyme A Complex"                     100.00 103 100.00 100.00 1.06e-69 
      GB  AAG51659  "unknown protein; 48670-48283 [Arabidopsis thaliana]"                                                       100.00 103 100.00 100.00 1.06e-69 
      GB  AAM62568  "unknown [Arabidopsis thaliana]"                                                                            100.00 114 100.00 100.00 3.23e-70 
      GB  ABD38887  "At1g77540 [Arabidopsis thaliana]"                                                                          100.00 114 100.00 100.00 3.23e-70 
      GB  AEE35991  "H3/H4 histone acetyltransferase [Arabidopsis thaliana]"                                                    100.00 114 100.00 100.00 3.23e-70 
      REF NP_565157 "H3/H4 histone acetyltransferase [Arabidopsis thaliana]"                                                    100.00 114 100.00 100.00 3.23e-70 
      SP  Q9CAQ2    "RecName: Full=Acetyltransferase At1g77540; AltName: Full=Minimal acetyltransferase [Arabidopsis thaliana]" 100.00 114 100.00 100.00 3.23e-70 

   stop_

save_


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

save_natural_source
   _Saveframe_category   natural_source


   loop_
      _Mol_label
      _Organism_name_common
      _NCBI_taxonomy_ID
      _Superkingdom
      _Kingdom
      _Genus
      _Species

      $At1g77540 'Arabidopsis thaliana' 3702 Eukaryota Viridiplantae Arabidopsis thaliana 

   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

      $At1g77540 'recombinant technology' . . . . . 

   stop_

save_


#####################################
#  Sample contents and methodology  #
#####################################
	 
    ########################
    #  Sample description  #
    ########################

save_sample_1
   _Saveframe_category   sample

   _Sample_type          solution
   _Details             '13C/15N labeled sample'

   loop_
      _Mol_label
      _Concentration_value
      _Concentration_value_units
      _Concentration_min_value
      _Concentration_max_value
      _Isotopic_labeling

      $At1g77540   . mM 0.9 1.1 '[U-13C; U-15N]' 
       KHPO4     10 mM  .   .   .               

   stop_

save_


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

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

save_NMR_spectrometer
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Varian
   _Model                Invoa
   _Field_strength       600
   _Details              .

save_


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

save_NHCO_1
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      NHCO
   _Sample_label         .

save_


save_CBCA(CO)NH_2
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      CBCA(CO)NH
   _Sample_label         .

save_


save_C(CO)NH_3
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      C(CO)NH
   _Sample_label         .

save_


save_HBHA(CO)NH_4
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HBHA(CO)NH
   _Sample_label         .

save_


save_HC(CO)NH_5
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HC(CO)NH
   _Sample_label         .

save_


save_CCH-TOCSY_6
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      CCH-TOCSY
   _Sample_label         .

save_


save_HCCH-TOCSY_7
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HCCH-TOCSY
   _Sample_label         .

save_


save_NMR_spec_expt__0_1
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        NHCO
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_2
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        CBCA(CO)NH
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_3
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        C(CO)NH
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_4
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        HBHA(CO)NH
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_5
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        HC(CO)NH
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_6
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        CCH-TOCSY
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_7
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        HCCH-TOCSY
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


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

save_sample_conditions
   _Saveframe_category   sample_conditions

   _Details              .

   loop_
      _Variable_type
      _Variable_value
      _Variable_value_error
      _Variable_value_units

       pH                6.0  0.1   pH 
       temperature     300    0.05  K  
      'ionic strength'   0.05 0.005 M  

   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

      DSS H  1 'methyl protons' ppm 0.0 internal direct   . . . 1.000000000 
      DSS C 13 'methyl protons' ppm 0.0 .        indirect . . . 0.251449530 
      DSS 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_assigned_chemical_shifts
   _Saveframe_category               assigned_chemical_shifts

   _Details                          .

   loop_
      _Experiment_label

      NHCO       
      CBCA(CO)NH 
      C(CO)NH    
      HBHA(CO)NH 
      HC(CO)NH   
      CCH-TOCSY  
      HCCH-TOCSY 

   stop_

   loop_
      _Sample_label

      $sample_1 

   stop_

   _Sample_conditions_label         $sample_conditions
   _Chem_shift_reference_set_label  $chemical_shift_reference
   _Mol_system_component_name        At1g77540
   _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 CA   C  53.247 . 1 
        2 .   2 ALA HA   H   4.448 . 1 
        3 .   2 ALA CB   C  19.760 . 1 
        4 .   2 ALA HB   H   1.441 . 1 
        5 .   2 ALA C    C 177.774 . 1 
        6 .   3 THR N    N 113.049 . 1 
        7 .   3 THR H    H   8.166 . 1 
        8 .   3 THR CA   C  61.990 . 1 
        9 .   3 THR HA   H   4.318 . 1 
       10 .   3 THR CB   C  70.145 . 1 
       11 .   3 THR HB   H   4.219 . 1 
       12 .   3 THR CG2  C  22.181 . 1 
       13 .   3 THR HG2  H   1.193 . 1 
       14 .   3 THR C    C 174.309 . 1 
       15 .   4 GLU N    N 124.960 . 1 
       16 .   4 GLU H    H   8.275 . 1 
       17 .   4 GLU CA   C  54.639 . 1 
       18 .   4 GLU CB   C  30.255 . 1 
       19 .   6 PRO CA   C  62.636 . 1 
       20 .   6 PRO HA   H   4.375 . 1 
       21 .   6 PRO CB   C  32.358 . 1 
       22 .   6 PRO HB3  H   1.688 . 2 
       23 .   6 PRO HB2  H   2.214 . 2 
       24 .   6 PRO CG   C  27.812 . 1 
       25 .   6 PRO HG2  H   1.894 . 2 
       26 .   6 PRO CD   C  49.979 . 1 
       27 .   6 PRO HD3  H   2.902 . 2 
       28 .   6 PRO HD2  H   3.553 . 2 
       29 .   7 LYS N    N 122.008 . 1 
       30 .   7 LYS H    H   8.347 . 1 
       31 .   7 LYS CA   C  57.028 . 1 
       32 .   7 LYS HA   H   4.165 . 1 
       33 .   7 LYS CB   C  32.943 . 1 
       34 .   7 LYS HB2  H   1.687 . 2 
       35 .   7 LYS CG   C  25.382 . 1 
       36 .   7 LYS HG2  H   1.238 . 2 
       37 .   7 LYS CD   C  29.332 . 1 
       38 .   7 LYS HD2  H   1.349 . 2 
       39 .   7 LYS CE   C  42.545 . 1 
       40 .   7 LYS HE3  H   2.701 . 2 
       41 .   7 LYS HE2  H   2.952 . 2 
       42 .   7 LYS C    C 175.340 . 1 
       43 .   8 ILE N    N 126.454 . 1 
       44 .   8 ILE H    H   8.373 . 1 
       45 .   8 ILE CA   C  58.628 . 1 
       46 .   8 ILE HA   H   4.621 . 1 
       47 .   8 ILE CB   C  38.550 . 1 
       48 .   8 ILE HB   H   1.829 . 1 
       49 .   8 ILE CG1  C  27.813 . 2 
       50 .   8 ILE HG12 H   1.240 . 1 
       51 .   8 ILE CD1  C  11.556 . 1 
       52 .   8 ILE HD1  H   0.573 . 1 
       53 .   8 ILE CG2  C  19.585 . 1 
       54 .   8 ILE HG2  H   0.894 . 1 
       55 .   8 ILE C    C 175.804 . 1 
       56 .   9 VAL N    N 124.416 . 1 
       57 .   9 VAL H    H   9.603 . 1 
       58 .   9 VAL CA   C  60.097 . 1 
       59 .   9 VAL HA   H   4.664 . 1 
       60 .   9 VAL CB   C  35.583 . 1 
       61 .   9 VAL HB   H   2.182 . 1 
       62 .   9 VAL CG2  C  21.976 . 1 
       63 .   9 VAL HG2  H   0.932 . 2 
       64 .   9 VAL CG1  C  20.135 . 1 
       65 .   9 VAL HG1  H   0.905 . 2 
       66 .   9 VAL C    C 174.778 . 1 
       67 .  10 TRP N    N 124.800 . 1 
       68 .  10 TRP H    H   8.906 . 1 
       69 .  10 TRP CA   C  55.571 . 1 
       70 .  10 TRP HA   H   4.630 . 1 
       71 .  10 TRP CB   C  29.264 . 1 
       72 .  10 TRP HB3  H   2.947 . 2 
       73 .  10 TRP HB2  H   3.433 . 2 
       74 .  10 TRP HD1  H   5.491 . 1 
       75 .  10 TRP NE1  N 126.588 . 1 
       76 .  10 TRP HE1  H   9.767 . 3 
       77 .  10 TRP C    C 174.621 . 1 
       78 .  11 ASN N    N 130.539 . 1 
       79 .  11 ASN H    H   8.985 . 1 
       80 .  11 ASN CA   C  50.763 . 1 
       81 .  11 ASN HA   H   4.505 . 1 
       82 .  11 ASN CB   C  37.859 . 1 
       83 .  11 ASN HB3  H   2.251 . 2 
       84 .  11 ASN HB2  H   2.807 . 2 
       85 .  11 ASN C    C 173.645 . 1 
       86 .  12 GLU N    N 124.956 . 1 
       87 .  12 GLU H    H   7.537 . 1 
       88 .  12 GLU CA   C  59.679 . 1 
       89 .  12 GLU HA   H   3.262 . 1 
       90 .  12 GLU CB   C  29.330 . 1 
       91 .  12 GLU HB3  H   0.339 . 2 
       92 .  12 GLU HB2  H   1.185 . 2 
       93 .  12 GLU CG   C  36.180 . 1 
       94 .  12 GLU HG2  H   1.783 . 2 
       95 .  12 GLU C    C 179.824 . 1 
       96 .  13 GLY N    N 106.735 . 1 
       97 .  13 GLY H    H   8.508 . 1 
       98 .  13 GLY CA   C  46.978 . 1 
       99 .  13 GLY HA3  H   3.746 . 2 
      100 .  13 GLY HA2  H   3.703 . 2 
      101 .  13 GLY C    C 175.296 . 1 
      102 .  14 LYS N    N 116.611 . 1 
      103 .  14 LYS H    H   6.853 . 1 
      104 .  14 LYS CA   C  54.659 . 1 
      105 .  14 LYS HA   H   4.165 . 1 
      106 .  14 LYS CB   C  32.996 . 1 
      107 .  14 LYS HB3  H   0.925 . 2 
      108 .  14 LYS HB2  H   1.546 . 2 
      109 .  14 LYS CG   C  25.309 . 1 
      110 .  14 LYS HG3  H   1.259 . 2 
      111 .  14 LYS HG2  H   1.093 . 2 
      112 .  14 LYS CD   C  28.881 . 1 
      113 .  14 LYS HD2  H   1.330 . 2 
      114 .  14 LYS CE   C  42.502 . 1 
      115 .  14 LYS HE2  H   2.700 . 2 
      116 .  14 LYS C    C 174.354 . 1 
      117 .  15 ARG N    N 118.568 . 1 
      118 .  15 ARG H    H   7.639 . 1 
      119 .  15 ARG CA   C  57.437 . 1 
      120 .  15 ARG HA   H   3.174 . 1 
      121 .  15 ARG CB   C  26.633 . 1 
      122 .  15 ARG HB3  H   1.091 . 2 
      123 .  15 ARG HB2  H   1.734 . 2 
      124 .  15 ARG CG   C  28.298 . 1 
      125 .  15 ARG HG2  H   1.372 . 2 
      126 .  15 ARG CD   C  44.342 . 1 
      127 .  15 ARG HD2  H   3.125 . 2 
      128 .  15 ARG C    C 173.150 . 1 
      129 .  16 ARG N    N 110.368 . 1 
      130 .  16 ARG H    H   7.511 . 1 
      131 .  16 ARG CA   C  54.402 . 1 
      132 .  16 ARG HA   H   3.887 . 1 
      133 .  16 ARG CB   C  35.824 . 1 
      134 .  16 ARG HB3  H   1.252 . 2 
      135 .  16 ARG HB2  H   1.817 . 2 
      136 .  16 ARG CG   C  26.362 . 1 
      137 .  16 ARG HG2  H   1.477 . 2 
      138 .  16 ARG CD   C  44.151 . 1 
      139 .  16 ARG HD2  H   2.407 . 2 
      140 .  16 ARG C    C 175.721 . 1 
      141 .  17 PHE N    N 120.007 . 1 
      142 .  17 PHE H    H   8.730 . 1 
      143 .  17 PHE CA   C  58.418 . 1 
      144 .  17 PHE HA   H   5.303 . 1 
      145 .  17 PHE CB   C  39.649 . 1 
      146 .  17 PHE HB3  H   2.688 . 2 
      147 .  17 PHE HB2  H   2.969 . 2 
      148 .  17 PHE HD1  H   7.020 . 3 
      149 .  17 PHE HE1  H   6.620 . 3 
      150 .  17 PHE C    C 174.905 . 1 
      151 .  18 GLU N    N 119.454 . 1 
      152 .  18 GLU H    H   9.554 . 1 
      153 .  18 GLU CA   C  54.231 . 1 
      154 .  18 GLU HA   H   5.946 . 1 
      155 .  18 GLU CB   C  35.752 . 1 
      156 .  18 GLU HB3  H   2.062 . 2 
      157 .  18 GLU HB2  H   2.367 . 2 
      158 .  18 GLU CG   C  34.481 . 1 
      159 .  18 GLU HG2  H   2.124 . 2 
      160 .  18 GLU C    C 176.036 . 1 
      161 .  19 THR N    N 109.626 . 1 
      162 .  19 THR H    H   8.536 . 1 
      163 .  19 THR CA   C  62.271 . 1 
      164 .  19 THR HA   H   4.721 . 1 
      165 .  19 THR CB   C  69.815 . 1 
      166 .  19 THR HB   H   4.721 . 1 
      167 .  19 THR CG2  C  26.148 . 1 
      168 .  19 THR HG2  H   1.283 . 1 
      169 .  19 THR C    C 177.932 . 1 
      170 .  20 GLU N    N 120.696 . 1 
      171 .  20 GLU H    H   8.817 . 1 
      172 .  20 GLU CA   C  60.052 . 1 
      173 .  20 GLU HA   H   3.753 . 1 
      174 .  20 GLU CB   C  30.625 . 1 
      175 .  20 GLU HB3  H   1.989 . 2 
      176 .  20 GLU HB2  H   2.082 . 2 
      177 .  20 GLU CG   C  38.159 . 1 
      178 .  20 GLU HG2  H   2.212 . 2 
      179 .  20 GLU C    C 176.657 . 1 
      180 .  21 ASP N    N 114.106 . 1 
      181 .  21 ASP H    H   7.590 . 1 
      182 .  21 ASP CA   C  53.534 . 1 
      183 .  21 ASP HA   H   4.182 . 1 
      184 .  21 ASP CB   C  40.564 . 1 
      185 .  21 ASP HB3  H   2.597 . 2 
      186 .  21 ASP HB2  H   3.161 . 2 
      187 .  21 ASP C    C 176.410 . 1 
      188 .  22 HIS N    N 111.204 . 1 
      189 .  22 HIS H    H   8.193 . 1 
      190 .  22 HIS CA   C  56.982 . 1 
      191 .  22 HIS HA   H   4.240 . 1 
      192 .  22 HIS CB   C  27.680 . 1 
      193 .  22 HIS HB3  H   3.282 . 2 
      194 .  22 HIS HB2  H   3.738 . 2 
      195 .  22 HIS HD2  H   7.100 . 3 
      196 .  22 HIS C    C 175.821 . 1 
      197 .  23 GLU N    N 118.506 . 1 
      198 .  23 GLU H    H   8.156 . 1 
      199 .  23 GLU CA   C  58.903 . 1 
      200 .  23 GLU HA   H   4.343 . 1 
      201 .  23 GLU CB   C  31.318 . 1 
      202 .  23 GLU HB2  H   2.114 . 2 
      203 .  23 GLU CG   C  35.889 . 1 
      204 .  23 GLU HG2  H   2.330 . 2 
      205 .  23 GLU C    C 175.424 . 1 
      206 .  24 ALA N    N 117.972 . 1 
      207 .  24 ALA H    H   7.553 . 1 
      208 .  24 ALA CA   C  50.199 . 1 
      209 .  24 ALA HA   H   5.128 . 1 
      210 .  24 ALA CB   C  23.269 . 1 
      211 .  24 ALA HB   H   1.363 . 1 
      212 .  24 ALA C    C 175.100 . 1 
      213 .  25 PHE N    N 115.582 . 1 
      214 .  25 PHE H    H   8.708 . 1 
      215 .  25 PHE CA   C  57.085 . 1 
      216 .  25 PHE HA   H   5.854 . 1 
      217 .  25 PHE CB   C  42.460 . 1 
      218 .  25 PHE HB3  H   2.891 . 2 
      219 .  25 PHE HB2  H   3.503 . 2 
      220 .  25 PHE HD1  H   6.870 . 3 
      221 .  25 PHE C    C 172.689 . 1 
      222 .  26 ILE N    N 118.225 . 1 
      223 .  26 ILE H    H   9.410 . 1 
      224 .  26 ILE CA   C  59.880 . 1 
      225 .  26 ILE HA   H   5.482 . 1 
      226 .  26 ILE CB   C  42.771 . 1 
      227 .  26 ILE HB   H   1.619 . 1 
      228 .  26 ILE CG1  C  28.545 . 2 
      229 .  26 ILE HG12 H   1.900 . 1 
      230 .  26 ILE CD1  C  16.800 . 1 
      231 .  26 ILE HD1  H   0.784 . 1 
      232 .  26 ILE CG2  C  17.940 . 1 
      233 .  26 ILE HG2  H   1.710 . 1 
      234 .  26 ILE C    C 174.113 . 1 
      235 .  27 GLU N    N 128.275 . 1 
      236 .  27 GLU H    H   9.252 . 1 
      237 .  27 GLU CA   C  54.881 . 1 
      238 .  27 GLU HA   H   5.374 . 1 
      239 .  27 GLU CB   C  34.151 . 1 
      240 .  27 GLU HB2  H   2.216 . 2 
      241 .  27 GLU CG   C  37.875 . 1 
      242 .  27 GLU HG2  H   2.536 . 2 
      243 .  27 GLU C    C 175.144 . 1 
      244 .  28 TYR N    N 120.383 . 1 
      245 .  28 TYR H    H   8.405 . 1 
      246 .  28 TYR CA   C  55.278 . 1 
      247 .  28 TYR HA   H   6.169 . 1 
      248 .  28 TYR CB   C  44.880 . 1 
      249 .  28 TYR HB3  H   2.662 . 2 
      250 .  28 TYR HB2  H   3.025 . 2 
      251 .  28 TYR HD1  H   6.660 . 3 
      252 .  28 TYR C    C 173.476 . 1 
      253 .  29 LYS N    N 117.619 . 1 
      254 .  29 LYS H    H   9.233 . 1 
      255 .  29 LYS CA   C  55.667 . 1 
      256 .  29 LYS HA   H   4.666 . 1 
      257 .  29 LYS CB   C  37.120 . 1 
      258 .  29 LYS HB3  H   1.651 . 2 
      259 .  29 LYS HB2  H   1.866 . 2 
      260 .  29 LYS CG   C  26.040 . 1 
      261 .  29 LYS HG2  H   1.443 . 2 
      262 .  29 LYS CD   C  29.810 . 1 
      263 .  29 LYS HD2  H   1.698 . 2 
      264 .  29 LYS CE   C  42.725 . 1 
      265 .  29 LYS HE2  H   2.967 . 2 
      266 .  29 LYS C    C 175.956 . 1 
      267 .  30 MET N    N 122.014 . 1 
      268 .  30 MET H    H   9.252 . 1 
      269 .  30 MET CA   C  53.494 . 1 
      270 .  30 MET HA   H   5.560 . 1 
      271 .  30 MET CB   C  31.366 . 1 
      272 .  30 MET HB3  H   1.924 . 2 
      273 .  30 MET HB2  H   2.244 . 2 
      274 .  30 MET HG3  H   2.713 . 2 
      275 .  30 MET HG2  H   3.042 . 2 
      276 .  30 MET C    C 176.782 . 1 
      277 .  31 ARG N    N 121.635 . 1 
      278 .  31 ARG H    H   9.467 . 1 
      279 .  31 ARG CA   C  54.048 . 1 
      280 .  31 ARG HA   H   4.782 . 1 
      281 .  31 ARG CB   C  34.117 . 1 
      282 .  31 ARG HB3  H   1.382 . 2 
      283 .  31 ARG HB2  H   1.923 . 2 
      284 .  31 ARG CG   C  27.856 . 1 
      285 .  31 ARG HG2  H   1.650 . 2 
      286 .  31 ARG CD   C  44.008 . 1 
      287 .  31 ARG HD3  H   2.993 . 2 
      288 .  31 ARG HD2  H   3.131 . 2 
      289 .  31 ARG C    C 175.407 . 1 
      290 .  32 ASN N    N 118.358 . 1 
      291 .  32 ASN H    H   9.046 . 1 
      292 .  32 ASN CA   C  54.215 . 1 
      293 .  32 ASN HA   H   4.270 . 1 
      294 .  32 ASN CB   C  36.557 . 1 
      295 .  32 ASN HB3  H   2.499 . 2 
      296 .  32 ASN HB2  H   2.946 . 2 
      297 .  32 ASN C    C 176.033 . 1 
      298 .  33 ASN N    N 115.786 . 1 
      299 .  33 ASN H    H   8.977 . 1 
      300 .  33 ASN CA   C  54.390 . 1 
      301 .  33 ASN HA   H   4.320 . 1 
      302 .  33 ASN CB   C  37.735 . 1 
      303 .  33 ASN HB3  H   2.749 . 2 
      304 .  33 ASN HB2  H   3.084 . 2 
      305 .  33 ASN C    C 175.274 . 1 
      306 .  34 GLY N    N 103.905 . 1 
      307 .  34 GLY H    H   7.831 . 1 
      308 .  34 GLY CA   C  45.964 . 1 
      309 .  34 GLY HA3  H   3.491 . 2 
      310 .  34 GLY HA2  H   4.240 . 2 
      311 .  34 GLY C    C 174.103 . 1 
      312 .  35 LYS N    N 117.011 . 1 
      313 .  35 LYS H    H   7.450 . 1 
      314 .  35 LYS CA   C  56.933 . 1 
      315 .  35 LYS HA   H   4.450 . 1 
      316 .  35 LYS CB   C  33.762 . 1 
      317 .  35 LYS HB3  H   1.941 . 2 
      318 .  35 LYS HB2  H   2.093 . 2 
      319 .  35 LYS CG   C  25.535 . 1 
      320 .  35 LYS HG3  H   1.641 . 2 
      321 .  35 LYS HG2  H   1.540 . 2 
      322 .  35 LYS CD   C  28.876 . 1 
      323 .  35 LYS HD2  H   1.759 . 2 
      324 .  35 LYS CE   C  42.502 . 1 
      325 .  35 LYS HE2  H   3.088 . 2 
      326 .  35 LYS C    C 175.745 . 1 
      327 .  36 VAL N    N 118.433 . 1 
      328 .  36 VAL H    H   7.758 . 1 
      329 .  36 VAL CA   C  60.661 . 1 
      330 .  36 VAL HA   H   4.527 . 1 
      331 .  36 VAL CB   C  35.916 . 1 
      332 .  36 VAL HB   H   1.377 . 1 
      333 .  36 VAL CG1  C  21.464 . 1 
      334 .  36 VAL HG1  H   0.383 . 2 
      335 .  36 VAL C    C 172.723 . 1 
      336 .  37 MET N    N 128.944 . 1 
      337 .  37 MET H    H   9.196 . 1 
      338 .  37 MET CA   C  54.993 . 1 
      339 .  37 MET HA   H   4.773 . 1 
      340 .  37 MET CB   C  36.933 . 1 
      341 .  37 MET HB3  H   1.511 . 2 
      342 .  37 MET HB2  H   1.840 . 2 
      343 .  37 MET C    C 172.670 . 1 
      344 .  38 ASP N    N 129.021 . 1 
      345 .  38 ASP H    H   9.328 . 1 
      346 .  38 ASP CA   C  52.773 . 1 
      347 .  38 ASP HA   H   5.185 . 1 
      348 .  38 ASP CB   C  42.648 . 1 
      349 .  38 ASP HB3  H   2.075 . 2 
      350 .  38 ASP HB2  H   3.250 . 2 
      351 .  38 ASP C    C 176.832 . 1 
      352 .  39 LEU N    N 125.502 . 1 
      353 .  39 LEU H    H   8.852 . 1 
      354 .  39 LEU CA   C  54.661 . 1 
      355 .  39 LEU HA   H   4.621 . 1 
      356 .  39 LEU CB   C  41.623 . 1 
      357 .  39 LEU HB3  H   1.279 . 2 
      358 .  39 LEU HB2  H   2.081 . 2 
      359 .  39 LEU CG   C  27.789 . 1 
      360 .  39 LEU HG   H   1.657 . 1 
      361 .  39 LEU CD1  C  23.047 . 1 
      362 .  39 LEU HD1  H   0.711 . 2 
      363 .  39 LEU C    C 175.134 . 1 
      364 .  40 VAL N    N 118.260 . 1 
      365 .  40 VAL H    H   8.400 . 1 
      366 .  40 VAL CA   C  63.916 . 1 
      367 .  40 VAL HA   H   4.249 . 1 
      368 .  40 VAL CB   C  33.973 . 1 
      369 .  40 VAL HB   H   2.135 . 1 
      370 .  40 VAL CG2  C  22.247 . 1 
      371 .  40 VAL HG2  H   0.884 . 2 
      372 .  40 VAL CG1  C  19.424 . 1 
      373 .  40 VAL HG1  H   0.852 . 2 
      374 .  40 VAL C    C 177.134 . 1 
      375 .  41 HIS N    N 117.776 . 1 
      376 .  41 HIS H    H   7.497 . 1 
      377 .  41 HIS CA   C  56.766 . 1 
      378 .  41 HIS HA   H   5.251 . 1 
      379 .  41 HIS CB   C  33.376 . 1 
      380 .  41 HIS HB3  H   3.164 . 2 
      381 .  41 HIS HB2  H   3.301 . 2 
      382 .  41 HIS HD2  H   7.120 . 3 
      383 .  41 HIS C    C 172.193 . 1 
      384 .  42 THR N    N 129.172 . 1 
      385 .  42 THR H    H   8.566 . 1 
      386 .  42 THR CA   C  63.573 . 1 
      387 .  42 THR HA   H   4.470 . 1 
      388 .  42 THR CB   C  67.959 . 1 
      389 .  42 THR HB   H   3.737 . 1 
      390 .  42 THR CG2  C  21.014 . 1 
      391 .  42 THR HG2  H   0.653 . 1 
      392 .  42 THR C    C 172.613 . 1 
      393 .  43 TYR N    N 128.345 . 1 
      394 .  43 TYR H    H   9.156 . 1 
      395 .  43 TYR CA   C  57.903 . 1 
      396 .  43 TYR HA   H   4.276 . 1 
      397 .  43 TYR CB   C  40.616 . 1 
      398 .  43 TYR HB3  H   1.296 . 2 
      399 .  43 TYR HB2  H   1.766 . 2 
      400 .  43 TYR HD1  H   6.932 . 3 
      401 .  43 TYR HE1  H   6.846 . 3 
      402 .  43 TYR C    C 172.023 . 1 
      403 .  44 VAL N    N 125.606 . 1 
      404 .  44 VAL H    H   7.375 . 1 
      405 .  44 VAL CA   C  58.016 . 1 
      406 .  44 VAL HA   H   3.947 . 1 
      407 .  44 VAL CB   C  34.949 . 1 
      408 .  44 VAL HB   H   1.560 . 1 
      409 .  44 VAL CG2  C  21.610 . 1 
      410 .  44 VAL HG2  H   0.623 . 2 
      411 .  44 VAL CG1  C  20.877 . 1 
      412 .  44 VAL HG1  H   0.454 . 2 
      413 .  45 PRO HD2  H   3.463 . 2 
      414 .  46 SER HA   H   3.905 . 1 
      415 .  47 PHE N    N 115.415 . 1 
      416 .  47 PHE H    H   7.312 . 1 
      417 .  47 PHE CA   C  57.957 . 1 
      418 .  47 PHE HA   H   4.704 . 1 
      419 .  47 PHE CB   C  37.892 . 1 
      420 .  47 PHE HB3  H   3.082 . 2 
      421 .  47 PHE HB2  H   3.435 . 2 
      422 .  47 PHE HD1  H   7.284 . 3 
      423 .  47 PHE HE1  H   7.410 . 3 
      424 .  47 PHE C    C 175.654 . 1 
      425 .  48 LYS N    N 120.012 . 1 
      426 .  48 LYS H    H   7.548 . 1 
      427 .  48 LYS CA   C  55.242 . 1 
      428 .  48 LYS HA   H   4.418 . 1 
      429 .  48 LYS CB   C  33.446 . 1 
      430 .  48 LYS HB3  H   1.050 . 2 
      431 .  48 LYS HB2  H   2.000 . 2 
      432 .  48 LYS CG   C  25.228 . 1 
      433 .  48 LYS HG3  H   1.011 . 2 
      434 .  48 LYS HG2  H   0.827 . 2 
      435 .  48 LYS CD   C  29.581 . 1 
      436 .  48 LYS HD2  H   1.420 . 2 
      437 .  48 LYS CE   C  41.827 . 1 
      438 .  48 LYS HE2  H   2.931 . 2 
      439 .  48 LYS C    C 175.199 . 1 
      440 .  49 ARG N    N 119.548 . 1 
      441 .  49 ARG H    H   7.217 . 1 
      442 .  49 ARG CA   C  57.677 . 1 
      443 .  49 ARG HA   H   4.092 . 1 
      444 .  49 ARG CB   C  30.817 . 1 
      445 .  49 ARG HB2  H   1.867 . 2 
      446 .  49 ARG CG   C  27.918 . 1 
      447 .  49 ARG HG2  H   1.632 . 2 
      448 .  49 ARG CD   C  43.383 . 1 
      449 .  49 ARG HD2  H   3.159 . 2 
      450 .  49 ARG C    C 176.850 . 1 
      451 .  50 GLY N    N 109.400 . 1 
      452 .  50 GLY H    H   8.990 . 1 
      453 .  50 GLY CA   C  46.424 . 1 
      454 .  50 GLY HA3  H   3.873 . 2 
      455 .  50 GLY HA2  H   4.114 . 2 
      456 .  50 GLY C    C 174.905 . 1 
      457 .  51 LEU N    N 120.198 . 1 
      458 .  51 LEU H    H   8.139 . 1 
      459 .  51 LEU CA   C  54.941 . 1 
      460 .  51 LEU HA   H   4.531 . 1 
      461 .  51 LEU CB   C  43.651 . 1 
      462 .  51 LEU HB2  H   1.653 . 2 
      463 .  51 LEU CG   C  25.512 . 1 
      464 .  51 LEU HG   H   1.420 . 1 
      465 .  51 LEU CD1  C  22.988 . 1 
      466 .  51 LEU HD1  H   0.871 . 2 
      467 .  51 LEU C    C 177.718 . 1 
      468 .  52 GLY N    N 110.748 . 1 
      469 .  52 GLY H    H   8.745 . 1 
      470 .  52 GLY CA   C  46.726 . 1 
      471 .  52 GLY HA2  H   3.954 . 2 
      472 .  52 GLY C    C 176.114 . 1 
      473 .  53 LEU N    N 118.922 . 1 
      474 .  53 LEU H    H   8.205 . 1 
      475 .  53 LEU CA   C  58.654 . 1 
      476 .  53 LEU HA   H   3.909 . 1 
      477 .  53 LEU CB   C  42.716 . 1 
      478 .  53 LEU HB3  H   1.191 . 2 
      479 .  53 LEU HB2  H   1.722 . 2 
      480 .  53 LEU CG   C  27.927 . 1 
      481 .  53 LEU HG   H   1.550 . 1 
      482 .  53 LEU CD1  C  24.846 . 1 
      483 .  53 LEU HD1  H   0.864 . 2 
      484 .  53 LEU C    C 177.684 . 1 
      485 .  54 ALA N    N 120.404 . 1 
      486 .  54 ALA H    H   8.540 . 1 
      487 .  54 ALA CA   C  56.410 . 1 
      488 .  54 ALA HA   H   3.458 . 1 
      489 .  54 ALA CB   C  16.517 . 1 
      490 .  54 ALA HB   H   0.553 . 1 
      491 .  54 ALA C    C 178.979 . 1 
      492 .  55 SER N    N 111.284 . 1 
      493 .  55 SER H    H   7.624 . 1 
      494 .  55 SER CA   C  62.932 . 1 
      495 .  55 SER HA   H   4.247 . 1 
      496 .  55 SER HB2  H   3.968 . 2 
      497 .  55 SER C    C 176.083 . 1 
      498 .  56 HIS N    N 119.227 . 1 
      499 .  56 HIS H    H   7.571 . 1 
      500 .  56 HIS CA   C  60.067 . 1 
      501 .  56 HIS HA   H   4.424 . 1 
      502 .  56 HIS CB   C  30.971 . 1 
      503 .  56 HIS HB2  H   3.007 . 2 
      504 .  56 HIS HD2  H   6.903 . 3 
      505 .  56 HIS C    C 179.179 . 1 
      506 .  57 LEU N    N 121.398 . 1 
      507 .  57 LEU H    H   8.533 . 1 
      508 .  57 LEU CA   C  59.032 . 1 
      509 .  57 LEU HA   H   3.812 . 1 
      510 .  57 LEU CB   C  41.932 . 1 
      511 .  57 LEU HB3  H   1.121 . 2 
      512 .  57 LEU HB2  H   1.954 . 2 
      513 .  57 LEU CG   C  26.678 . 1 
      514 .  57 LEU HG   H   1.541 . 1 
      515 .  57 LEU CD1  C  24.357 . 1 
      516 .  57 LEU HD1  H   0.851 . 2 
      517 .  57 LEU HD2  H   0.487 . 2 
      518 .  57 LEU C    C 177.331 . 1 
      519 .  58 CYS N    N 115.952 . 1 
      520 .  58 CYS H    H   7.275 . 1 
      521 .  58 CYS CA   C  64.855 . 1 
      522 .  58 CYS HA   H   3.569 . 1 
      523 .  58 CYS CB   C  25.286 . 1 
      524 .  58 CYS HB3  H   0.712 . 2 
      525 .  58 CYS HB2  H   2.299 . 2 
      526 .  58 CYS C    C 176.382 . 1 
      527 .  59 VAL N    N 119.617 . 1 
      528 .  59 VAL H    H   8.312 . 1 
      529 .  59 VAL CA   C  68.180 . 1 
      530 .  59 VAL HA   H   3.032 . 1 
      531 .  59 VAL CB   C  32.083 . 1 
      532 .  59 VAL HB   H   2.096 . 1 
      533 .  59 VAL CG2  C  24.484 . 1 
      534 .  59 VAL HG2  H   1.318 . 2 
      535 .  59 VAL CG1  C  22.197 . 1 
      536 .  59 VAL HG1  H   1.037 . 2 
      537 .  59 VAL C    C 176.722 . 1 
      538 .  60 ALA N    N 119.513 . 1 
      539 .  60 ALA H    H   7.342 . 1 
      540 .  60 ALA CA   C  55.324 . 1 
      541 .  60 ALA HA   H   3.915 . 1 
      542 .  60 ALA CB   C  18.617 . 1 
      543 .  60 ALA HB   H   1.304 . 1 
      544 .  60 ALA C    C 180.069 . 1 
      545 .  61 ALA N    N 120.981 . 1 
      546 .  61 ALA H    H   7.138 . 1 
      547 .  61 ALA CA   C  54.729 . 1 
      548 .  61 ALA HA   H   2.492 . 1 
      549 .  61 ALA CB   C  18.810 . 1 
      550 .  61 ALA HB   H   0.841 . 1 
      551 .  61 ALA C    C 178.665 . 1 
      552 .  62 PHE N    N 117.876 . 1 
      553 .  62 PHE H    H   8.122 . 1 
      554 .  62 PHE CA   C  62.535 . 1 
      555 .  62 PHE HA   H   3.376 . 1 
      556 .  62 PHE CB   C  35.772 . 1 
      557 .  62 PHE HB3  H   1.051 . 2 
      558 .  62 PHE HB2  H   1.706 . 2 
      559 .  62 PHE HD1  H   7.121 . 3 
      560 .  62 PHE HE1  H   6.891 . 3 
      561 .  62 PHE C    C 178.228 . 1 
      562 .  63 GLU N    N 119.595 . 1 
      563 .  63 GLU H    H   8.886 . 1 
      564 .  63 GLU CA   C  60.134 . 1 
      565 .  63 GLU HA   H   4.086 . 1 
      566 .  63 GLU CB   C  29.695 . 1 
      567 .  63 GLU HB2  H   2.027 . 2 
      568 .  63 GLU CG   C  37.703 . 1 
      569 .  63 GLU HG3  H   2.444 . 2 
      570 .  63 GLU HG2  H   2.667 . 2 
      571 .  63 GLU C    C 180.341 . 1 
      572 .  64 HIS N    N 120.903 . 1 
      573 .  64 HIS H    H   7.745 . 1 
      574 .  64 HIS CA   C  60.516 . 1 
      575 .  64 HIS HA   H   3.997 . 1 
      576 .  64 HIS CB   C  31.311 . 1 
      577 .  64 HIS HB3  H   2.779 . 2 
      578 .  64 HIS HB2  H   2.955 . 2 
      579 .  64 HIS C    C 178.475 . 1 
      580 .  65 ALA N    N 123.381 . 1 
      581 .  65 ALA H    H   8.357 . 1 
      582 .  65 ALA CA   C  56.235 . 1 
      583 .  65 ALA HA   H   3.733 . 1 
      584 .  65 ALA CB   C  17.950 . 1 
      585 .  65 ALA HB   H   1.339 . 1 
      586 .  65 ALA C    C 179.494 . 1 
      587 .  66 SER N    N 111.510 . 1 
      588 .  66 SER H    H   8.608 . 1 
      589 .  66 SER CA   C  61.426 . 1 
      590 .  66 SER HA   H   4.316 . 1 
      591 .  66 SER CB   C  63.732 . 1 
      592 .  66 SER C    C 178.575 . 1 
      593 .  67 SER N    N 114.548 . 1 
      594 .  67 SER H    H   8.223 . 1 
      595 .  67 SER CA   C  60.839 . 1 
      596 .  67 SER HA   H   4.292 . 1 
      597 .  67 SER CB   C  63.628 . 1 
      598 .  67 SER HB2  H   3.867 . 2 
      599 .  67 SER C    C 175.448 . 1 
      600 .  68 HIS N    N 117.149 . 1 
      601 .  68 HIS H    H   7.694 . 1 
      602 .  68 HIS CA   C  56.822 . 1 
      603 .  68 HIS HA   H   4.555 . 1 
      604 .  68 HIS CB   C  29.019 . 1 
      605 .  68 HIS HB3  H   2.338 . 2 
      606 .  68 HIS HB2  H   3.434 . 2 
      607 .  68 HIS HD1  H   6.826 . 3 
      608 .  68 HIS C    C 172.823 . 1 
      609 .  69 SER N    N 113.951 . 1 
      610 .  69 SER H    H   7.789 . 1 
      611 .  69 SER CA   C  59.404 . 1 
      612 .  69 SER HA   H   4.178 . 1 
      613 .  69 SER CB   C  61.456 . 1 
      614 .  69 SER C    C 173.636 . 1 
      615 .  70 ILE N    N 117.875 . 1 
      616 .  70 ILE H    H   8.153 . 1 
      617 .  70 ILE CA   C  60.100 . 1 
      618 .  70 ILE HA   H   4.583 . 1 
      619 .  70 ILE CB   C  42.106 . 1 
      620 .  70 ILE HB   H   1.643 . 1 
      621 .  70 ILE CG1  C  27.262 . 2 
      622 .  70 ILE HG12 H   1.409 . 1 
      623 .  70 ILE CD1  C  15.117 . 1 
      624 .  70 ILE HD1  H   0.894 . 1 
      625 .  70 ILE CG2  C  19.098 . 1 
      626 .  70 ILE C    C 174.758 . 1 
      627 .  71 SER N    N 116.374 . 1 
      628 .  71 SER H    H   7.683 . 1 
      629 .  71 SER CA   C  57.409 . 1 
      630 .  71 SER HA   H   5.661 . 1 
      631 .  71 SER CB   C  65.894 . 1 
      632 .  71 SER HB2  H   5.204 . 2 
      633 .  71 SER C    C 173.423 . 1 
      634 .  72 ILE N    N 120.053 . 1 
      635 .  72 ILE H    H   8.725 . 1 
      636 .  72 ILE CA   C  59.100 . 1 
      637 .  72 ILE HA   H   5.306 . 1 
      638 .  72 ILE CB   C  42.852 . 1 
      639 .  72 ILE HB   H   1.294 . 1 
      640 .  72 ILE CG1  C  28.019 . 2 
      641 .  72 ILE HG13 H   0.814 . 1 
      642 .  72 ILE HG12 H   0.743 . 1 
      643 .  72 ILE CD1  C  12.320 . 1 
      644 .  72 ILE HD1  H  -0.156 . 1 
      645 .  72 ILE CG2  C  17.403 . 1 
      646 .  72 ILE HG2  H   0.427 . 1 
      647 .  72 ILE C    C 176.989 . 1 
      648 .  73 ILE N    N 126.678 . 1 
      649 .  73 ILE H    H   8.636 . 1 
      650 .  73 ILE CA   C  58.005 . 1 
      651 .  73 ILE HA   H   4.892 . 1 
      652 .  73 ILE CB   C  41.237 . 1 
      653 .  73 ILE HB   H   1.612 . 1 
      654 .  74 PRO CA   C  60.328 . 1 
      655 .  74 PRO HA   H   4.850 . 1 
      656 .  74 PRO CB   C  30.204 . 1 
      657 .  74 PRO HB3  H   1.514 . 2 
      658 .  74 PRO HB2  H   2.253 . 2 
      659 .  74 PRO CG   C  27.122 . 1 
      660 .  74 PRO HG2  H   2.030 . 2 
      661 .  74 PRO CD   C  50.433 . 1 
      662 .  74 PRO HD2  H   4.050 . 2 
      663 .  75 SER N    N 121.447 . 1 
      664 .  75 SER H    H   7.759 . 1 
      665 .  75 SER CA   C  63.641 . 1 
      666 .  75 SER HA   H   4.156 . 1 
      667 .  75 SER CB   C  62.144 . 1 
      668 .  75 SER HB2  H   3.807 . 2 
      669 .  75 SER C    C 175.613 . 1 
      670 .  76 CYS N    N 124.611 . 1 
      671 .  76 CYS H    H   8.201 . 1 
      672 .  76 CYS CA   C  60.637 . 1 
      673 .  76 CYS HA   H   4.128 . 1 
      674 .  76 CYS CB   C  29.541 . 1 
      675 .  76 CYS HB3  H   2.565 . 2 
      676 .  76 CYS HB2  H   2.734 . 2 
      677 .  76 CYS C    C 176.635 . 1 
      678 .  77 SER N    N 125.258 . 1 
      679 .  77 SER H    H   8.674 . 1 
      680 .  77 SER CA   C  61.294 . 1 
      681 .  77 SER HA   H   4.460 . 1 
      682 .  77 SER CB   C  63.460 . 1 
      683 .  77 SER HB2  H   4.028 . 2 
      684 .  77 SER C    C 177.783 . 1 
      685 .  78 TYR N    N 130.081 . 1 
      686 .  78 TYR H    H  10.133 . 1 
      687 .  78 TYR CA   C  63.923 . 1 
      688 .  78 TYR HA   H   4.142 . 1 
      689 .  78 TYR CB   C  38.634 . 1 
      690 .  78 TYR HB3  H   3.238 . 2 
      691 .  78 TYR HB2  H   3.158 . 2 
      692 .  78 TYR HD1  H   6.890 . 3 
      693 .  78 TYR HE1  H   6.700 . 3 
      694 .  78 TYR C    C 178.876 . 1 
      695 .  79 VAL N    N 121.970 . 1 
      696 .  79 VAL H    H   8.066 . 1 
      697 .  79 VAL CA   C  66.766 . 1 
      698 .  79 VAL HA   H   3.663 . 1 
      699 .  79 VAL CB   C  32.680 . 1 
      700 .  79 VAL HB   H   2.279 . 1 
      701 .  79 VAL HG2  H   1.360 . 2 
      702 .  79 VAL CG1  C  23.504 . 1 
      703 .  79 VAL HG1  H   1.189 . 2 
      704 .  79 VAL C    C 177.571 . 1 
      705 .  80 SER N    N 111.020 . 1 
      706 .  80 SER H    H   8.549 . 1 
      707 .  80 SER CA   C  62.226 . 1 
      708 .  80 SER HA   H   4.123 . 1 
      709 .  80 SER CB   C  63.521 . 1 
      710 .  80 SER C    C 176.039 . 1 
      711 .  81 ASP N    N 117.814 . 1 
      712 .  81 ASP H    H   8.362 . 1 
      713 .  81 ASP CA   C  55.764 . 1 
      714 .  81 ASP HA   H   4.768 . 1 
      715 .  81 ASP CB   C  41.305 . 1 
      716 .  81 ASP HB3  H   2.651 . 2 
      717 .  81 ASP HB2  H   2.939 . 2 
      718 .  81 ASP C    C 176.969 . 1 
      719 .  82 THR N    N 115.189 . 1 
      720 .  82 THR H    H   7.409 . 1 
      721 .  82 THR CA   C  65.203 . 1 
      722 .  82 THR HA   H   4.271 . 1 
      723 .  82 THR CB   C  69.264 . 1 
      724 .  82 THR HB   H   3.248 . 1 
      725 .  82 THR CG2  C  22.600 . 1 
      726 .  82 THR HG2  H   0.959 . 1 
      727 .  82 THR C    C 173.922 . 1 
      728 .  83 PHE N    N 121.170 . 1 
      729 .  83 PHE H    H   8.206 . 1 
      730 .  83 PHE CA   C  63.173 . 1 
      731 .  83 PHE HA   H   3.989 . 1 
      732 .  83 PHE CB   C  41.112 . 1 
      733 .  83 PHE HB3  H   3.218 . 2 
      734 .  83 PHE HB2  H   3.177 . 2 
      735 .  83 PHE HD1  H   6.808 . 3 
      736 .  83 PHE C    C 177.930 . 1 
      737 .  84 LEU N    N 119.657 . 1 
      738 .  84 LEU H    H   8.583 . 1 
      739 .  84 LEU CA   C  59.647 . 1 
      740 .  84 LEU HA   H   3.882 . 1 
      741 .  84 LEU CB   C  40.242 . 1 
      742 .  84 LEU HB3  H   1.457 . 2 
      743 .  84 LEU HB2  H   2.054 . 2 
      744 .  84 LEU HG   H   1.776 . 1 
      745 .  84 LEU HD1  H   1.066 . 2 
      746 .  84 LEU HD2  H   0.875 . 2 
      747 .  85 PRO CA   C  66.031 . 1 
      748 .  85 PRO HA   H   4.135 . 1 
      749 .  85 PRO CB   C  31.628 . 1 
      750 .  85 PRO HB3  H   1.573 . 2 
      751 .  85 PRO HB2  H   2.289 . 2 
      752 .  85 PRO CG   C  28.889 . 1 
      753 .  85 PRO HG2  H   1.884 . 2 
      754 .  85 PRO CD   C  50.210 . 1 
      755 .  85 PRO HD3  H   2.906 . 2 
      756 .  85 PRO HD2  H   3.585 . 2 
      757 .  85 PRO C    C 178.127 . 1 
      758 .  86 ARG N    N 111.780 . 1 
      759 .  86 ARG H    H   6.599 . 1 
      760 .  86 ARG CA   C  56.523 . 1 
      761 .  86 ARG HA   H   4.177 . 1 
      762 .  86 ARG CB   C  31.735 . 1 
      763 .  86 ARG HB2  H   1.592 . 2 
      764 .  86 ARG CG   C  28.117 . 1 
      765 .  86 ARG CD   C  43.759 . 1 
      766 .  86 ARG HD2  H   3.085 . 2 
      767 .  86 ARG C    C 177.134 . 1 
      768 .  87 ASN N    N 118.040 . 1 
      769 .  87 ASN H    H   7.513 . 1 
      770 .  87 ASN CA   C  51.743 . 1 
      771 .  87 ASN HA   H   5.010 . 1 
      772 .  87 ASN CB   C  41.009 . 1 
      773 .  87 ASN HB3  H   1.706 . 2 
      774 .  87 ASN HB2  H   2.113 . 2 
      775 .  88 PRO CA   C  65.238 . 1 
      776 .  88 PRO CB   C  32.099 . 1 
      777 .  88 PRO HB3  H   2.222 . 2 
      778 .  88 PRO HB2  H   1.979 . 2 
      779 .  88 PRO CG   C  27.613 . 1 
      780 .  88 PRO CD   C  50.750 . 1 
      781 .  89 SER N    N 117.427 . 1 
      782 .  89 SER H    H   8.354 . 1 
      783 .  89 SER CA   C  61.103 . 1 
      784 .  89 SER HA   H   4.005 . 1 
      785 .  89 SER CB   C  62.297 . 1 
      786 .  89 SER HB2  H   3.503 . 2 
      787 .  89 SER C    C 175.071 . 1 
      788 .  90 TRP N    N 118.912 . 1 
      789 .  90 TRP H    H   7.344 . 1 
      790 .  90 TRP CA   C  56.952 . 1 
      791 .  90 TRP HA   H   4.982 . 1 
      792 .  90 TRP CB   C  31.308 . 1 
      793 .  90 TRP HB3  H   2.490 . 2 
      794 .  90 TRP HB2  H   3.465 . 2 
      795 .  90 TRP NE1  N 126.974 . 1 
      796 .  90 TRP HE1  H  10.326 . 3 
      797 .  90 TRP C    C 176.360 . 1 
      798 .  91 LYS N    N 120.111 . 1 
      799 .  91 LYS H    H   7.616 . 1 
      800 .  91 LYS CA   C  61.719 . 1 
      801 .  91 LYS HA   H   4.117 . 1 
      802 .  91 LYS CB   C  31.216 . 1 
      803 .  91 LYS HB2  H   1.979 . 2 
      804 .  92 PRO CA   C  66.074 . 1 
      805 .  92 PRO HA   H   4.489 . 1 
      806 .  92 PRO CB   C  31.778 . 1 
      807 .  92 PRO HB3  H   2.461 . 2 
      808 .  92 PRO HB2  H   1.780 . 2 
      809 .  92 PRO CG   C  28.611 . 1 
      810 .  92 PRO HG2  H   2.040 . 2 
      811 .  92 PRO CD   C  51.675 . 1 
      812 .  92 PRO HD2  H   3.565 . 2 
      813 .  92 PRO C    C 176.582 . 1 
      814 .  93 LEU N    N 116.946 . 1 
      815 .  93 LEU H    H   7.901 . 1 
      816 .  93 LEU CA   C  55.113 . 1 
      817 .  93 LEU HA   H   4.502 . 1 
      818 .  93 LEU CB   C  43.258 . 1 
      819 .  93 LEU HB3  H   2.066 . 2 
      820 .  93 LEU HB2  H   2.268 . 2 
      821 .  93 LEU CG   C  29.407 . 1 
      822 .  93 LEU HG   H   2.231 . 1 
      823 .  93 LEU CD1  C  25.902 . 1 
      824 .  93 LEU HD1  H   1.225 . 2 
      825 .  93 LEU C    C 176.601 . 1 
      826 .  94 ILE N    N 119.271 . 1 
      827 .  94 ILE H    H   7.900 . 1 
      828 .  94 ILE CA   C  59.589 . 1 
      829 .  94 ILE HA   H   4.618 . 1 
      830 .  94 ILE CB   C  36.216 . 1 
      831 .  94 ILE HB   H   2.313 . 1 
      832 .  94 ILE CG1  C  27.832 . 2 
      833 .  94 ILE HG12 H   1.892 . 1 
      834 .  94 ILE CD1  C  17.710 . 1 
      835 .  94 ILE HD1  H   1.059 . 1 
      836 .  94 ILE CG2  C  21.770 . 1 
      837 .  94 ILE HG2  H   1.653 . 1 
      838 .  94 ILE C    C 177.094 . 1 
      839 .  95 HIS N    N 129.375 . 1 
      840 .  95 HIS H    H   9.230 . 1 
      841 .  95 HIS CA   C  57.690 . 1 
      842 .  95 HIS HA   H   4.460 . 1 
      843 .  95 HIS CB   C  31.759 . 1 
      844 .  95 HIS HB2  H   2.856 . 2 
      845 .  95 HIS C    C 174.767 . 1 
      846 .  96 SER N    N 120.277 . 1 
      847 .  96 SER H    H   7.868 . 1 
      848 .  96 SER CA   C  58.063 . 1 
      849 .  96 SER HA   H   4.324 . 1 
      850 .  96 SER CB   C  64.291 . 1 
      851 .  96 SER HB2  H   3.727 . 2 
      852 .  96 SER C    C 173.782 . 1 
      853 .  97 GLU N    N 122.717 . 1 
      854 .  97 GLU H    H   8.047 . 1 
      855 .  97 GLU CA   C  56.703 . 1 
      856 .  97 GLU HA   H   4.200 . 1 
      857 .  97 GLU CB   C  30.912 . 1 
      858 .  97 GLU HB3  H   1.807 . 2 
      859 .  97 GLU HB2  H   1.976 . 2 
      860 .  97 GLU CG   C  36.562 . 1 
      861 .  97 GLU HG2  H   2.151 . 2 
      862 .  97 GLU C    C 176.075 . 1 
      863 .  98 VAL N    N 120.267 . 1 
      864 .  98 VAL H    H   7.980 . 1 
      865 .  98 VAL CA   C  62.835 . 1 
      866 .  98 VAL HA   H   3.985 . 1 
      867 .  98 VAL CB   C  33.097 . 1 
      868 .  98 VAL HB   H   1.936 . 1 
      869 .  98 VAL CG1  C  21.199 . 1 
      870 .  98 VAL HG1  H   0.818 . 2 
      871 .  98 VAL C    C 175.872 . 1 
      872 .  99 PHE N    N 123.827 . 1 
      873 .  99 PHE H    H   8.227 . 1 
      874 .  99 PHE CA   C  57.990 . 1 
      875 .  99 PHE CB   C  39.938 . 1 
      876 .  99 PHE HB2  H   3.037 . 2 
      877 .  99 PHE C    C 175.342 . 1 
      878 . 100 LYS N    N 124.073 . 1 
      879 . 100 LYS H    H   8.120 . 1 
      880 . 100 LYS CA   C  56.328 . 1 
      881 . 100 LYS HA   H   4.300 . 1 
      882 . 100 LYS CB   C  33.804 . 1 
      883 . 100 LYS HB3  H   1.778 . 2 
      884 . 100 LYS HB2  H   1.710 . 2 
      885 . 100 LYS CG   C  24.966 . 1 
      886 . 100 LYS HG2  H   1.365 . 2 
      887 . 100 LYS CD   C  29.448 . 1 
      888 . 100 LYS HD2  H   1.654 . 2 
      889 . 100 LYS CE   C  42.528 . 1 
      890 . 100 LYS HE2  H   2.968 . 2 
      891 . 100 LYS C    C 175.921 . 1 
      892 . 101 SER N    N 117.605 . 1 
      893 . 101 SER H    H   8.312 . 1 
      894 . 101 SER CA   C  58.581 . 1 
      895 . 101 SER HA   H   4.420 . 1 
      896 . 101 SER CB   C  64.172 . 1 
      897 . 101 SER HB2  H   3.875 . 2 
      898 . 101 SER C    C 174.471 . 1 
      899 . 102 SER N    N 118.600 . 1 
      900 . 102 SER H    H   8.374 . 1 
      901 . 102 SER CA   C  58.642 . 1 
      902 . 102 SER HA   H   4.502 . 1 
      903 . 102 SER CB   C  64.274 . 1 
      904 . 102 SER HB2  H   3.877 . 2 
      905 . 102 SER C    C 173.460 . 1 
      906 . 103 ILE N    N 126.011 . 1 
      907 . 103 ILE H    H   7.724 . 1 
      908 . 103 ILE CA   C  63.291 . 1 
      909 . 103 ILE CB   C  40.011 . 1 

   stop_

save_