data_6570

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

save_entry_information
   _Saveframe_category      entry_information

   _Entry_title            
;
NMR Assignments of the F-actin binding domain of human Bcr-Abl/c-Abl
;
   _BMRB_accession_number   6570
   _BMRB_flat_file_name     bmr6570.str
   _Entry_type              original
   _Submission_date         2005-03-24
   _Accession_date          2005-03-28
   _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 Wiesner       Silke   .  . 
      2 Hantschel     Oliver  .  . 
      3 Mackereth     Cameron D. . 
      4 Superti-Furga Giulio  .  . 
      5 Sattler       Michael .  . 

   stop_

   loop_
      _Saveframe_category_type
      _Saveframe_category_type_count

      assigned_chemical_shifts 1 

   stop_

   loop_
      _Data_type
      _Data_type_count

      "1H chemical shifts"  619 
      "13C chemical shifts" 499 
      "15N chemical shifts" 137 

   stop_

   loop_
      _Revision_date
      _Revision_keyword
      _Revision_author
      _Revision_detail

      2005-10-24 original author . 

   stop_

   _Original_release_date   2005-10-24

save_


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

save_entry_citation
   _Saveframe_category           entry_citation

   _Citation_full                .
   _Citation_title              
;
NMR Assignment Reveals an alpha-Helical Fold for the F-Actin Binding Domain of
Human Bcr-Abl/c-Abl
;
   _Citation_status              published
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              .
   _PubMed_ID                    16211486

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Wiesner       Silke   .  . 
      2 Hantschel     Oliver  .  . 
      3 Mackereth     Cameron D. . 
      4 Superti-Furga Giulio  .  . 
      5 Sattler       Michael .  . 

   stop_

   _Journal_abbreviation        'J. Biomol. NMR'
   _Journal_volume               32
   _Journal_issue                4
   _Journal_CSD                  .
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_ISBN                    .
   _Conference_state_province    .
   _Conference_abstract_number   .
   _Page_first                   335
   _Page_last                    335
   _Year                         2005
   _Details                      .

   loop_
      _Keyword

       Bcr-Abl                 
       c-Abl                   
      'tyrosine kinase'        
      'F-actin binding domain' 

   stop_

save_


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

save_system_FABD
   _Saveframe_category         molecular_system

   _Mol_system_name           'F-actin binding domain of human Bcr-Abl/c-Abl'
   _Abbreviation_common        FABD
   _Enzyme_commission_number   2.7.1.112

   loop_
      _Mol_system_component_name
      _Mol_label

      'c-Abl, FABD' $FABD 

   stop_

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

   loop_
      _Biological_function

      'non-recpetor tyrosin kinase' 
      'F-actin binding'             
      'cell adhesion'               

   stop_

   _Database_query_date        .
   _Details                    .

save_


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

save_FABD
   _Saveframe_category                          monomeric_polymer

   _Mol_type                                    polymer
   _Mol_polymer_class                           protein
   _Name_common                                'F-actin binding domain of cellular Abelson tyrosine kinase'
   _Abbreviation_common                         c-Abl
   _Molecular_mass                              10251
   _Mol_thiol_state                            'all free'
   _Details                                     .

   	##############################
   	#  Polymer residue sequence  #
   	##############################
   
      _Residue_count                               130
   _Mol_residue_sequence                       
;
GAMASTRVSLRKTRQPPERI
ASGAITKGVVLDSTEALCLA
ISRNSEQMASHSAVLEAGKN
LYSFCVSYVDSIQQMRNKFA
FREAINKLENNLRELQICPA
TAGSGPAATQDFSKLLSSVK
EISDIVQRLE
;

   loop_
      _Residue_seq_code
      _Residue_author_seq_code
      _Residue_label

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

   stop_

   _Sequence_homology_query_date                .
   _Sequence_homology_query_revised_last_date   2015-01-28

   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  1ZZP         "Solution Structure Of The F-Actin Binding Domain Of Bcr- AblC-Abl"                                                               100.00  130 100.00 100.00 1.12e-88 
      DBJ  BAD92693     "v-abl Abelson murine leukemia viral oncogene homolog 1 isoform b variant [Homo sapiens]"                                          96.92 1167  97.62  99.21 3.71e-76 
      DBJ  BAD92879     "Proto-oncogene tyrosine-protein kinase ABL1 variant [Homo sapiens]"                                                               96.92  949  97.62  99.21 1.27e-76 
      DBJ  BAG10808     "proto-oncogene tyrosine-protein kinase ABL1 [synthetic construct]"                                                                96.92 1149  97.62  99.21 2.73e-76 
      DBJ  BAG58052     "unnamed protein product [Homo sapiens]"                                                                                           95.38  581  97.58  99.19 3.56e-79 
      EMBL CAA34438     "unnamed protein product [Homo sapiens]"                                                                                           96.92 1130  97.62  99.21 3.92e-76 
      GB   AAB60393     "proto-oncogene tyrosine-protein kinase [Homo sapiens]"                                                                            96.92 1149  97.62  99.21 2.73e-76 
      GB   AAB60394     "proto-oncogene tyrosine-protein kinase [Homo sapiens]"                                                                            96.92 1130  97.62  99.21 3.92e-76 
      GB   AAI07070     "ABL1 protein, partial [Homo sapiens]"                                                                                             95.38  396  99.19 100.00 9.11e-83 
      GB   AAI07071     "ABL1 protein, partial [Homo sapiens]"                                                                                             95.38  396  99.19 100.00 6.31e-83 
      GB   AAI17452     "C-abl oncogene 1, receptor tyrosine kinase [Homo sapiens]"                                                                        96.92 1149  97.62  99.21 2.73e-76 
      REF  NP_005148    "tyrosine-protein kinase ABL1 isoform a [Homo sapiens]"                                                                            96.92 1130  97.62  99.21 3.92e-76 
      REF  NP_009297    "tyrosine-protein kinase ABL1 isoform b [Homo sapiens]"                                                                            96.92 1149  97.62  99.21 2.73e-76 
      REF  XP_001118598 "PREDICTED: tyrosine-protein kinase ABL1-like [Macaca mulatta]"                                                                    96.92  853  97.62  99.21 4.34e-77 
      REF  XP_001166213 "PREDICTED: tyrosine-protein kinase ABL1 [Pan troglodytes]"                                                                        96.92 1149  97.62  99.21 2.96e-76 
      REF  XP_003276793 "PREDICTED: LOW QUALITY PROTEIN: tyrosine-protein kinase ABL1 [Nomascus leucogenys]"                                               96.92 1058  97.62  99.21 3.70e-76 
      SP   P00519       "RecName: Full=Tyrosine-protein kinase ABL1; AltName: Full=Abelson murine leukemia viral oncogene homolog 1; AltName: Full=Abels"  96.92 1130  97.62  99.21 3.92e-76 

   stop_

save_


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

save_natural_source
   _Saveframe_category   natural_source


   loop_
      _Mol_label
      _Organism_name_common
      _NCBI_taxonomy_ID
      _Superkingdom
      _Kingdom
      _Genus
      _Species
      _Fraction
      _Gene_mnemonic

      $FABD Human 9606 Eukaryota Metazoa Homo sapiens nucleus/cytoplasm ABL1 

   stop_

save_


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

save_experimental_source
   _Saveframe_category   experimental_source


   loop_
      _Mol_label
      _Production_method
      _Host_organism_name_common
      _Genus
      _Species
      _Strain
      _Vector_type
      _Vector_name

      $FABD 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid 'pETM30 (modified pET24d)' 

   stop_

save_


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

save_15N-labeled_sample
   _Saveframe_category   sample

   _Sample_type          solution
   _Details              .

   loop_
      _Mol_label
      _Concentration_value
      _Concentration_value_units
      _Isotopic_labeling

      $FABD 1.0 mM '[U-100% 15N]' 

   stop_

save_


save_15N-13C-labeled_sample
   _Saveframe_category   sample

   _Sample_type          solution
   _Details              .

   loop_
      _Mol_label
      _Concentration_value
      _Concentration_value_units
      _Isotopic_labeling

      $FABD 1.0 mM '[U-100% 13C; U-100% 15N]' 

   stop_

save_


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

save_XEASY
   _Saveframe_category   software

   _Name                 XEASY
   _Version              .

   loop_
      _Task

      assignment 

   stop_

   _Details              .

save_


save_NMRPipe-NMRDraw
   _Saveframe_category   software

   _Name                 NMRPipe-NMRDraw
   _Version              .

   loop_
      _Task

      'data processing' 

   stop_

   _Details              .

save_


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

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

save_NMR_spectrometer_1
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                DRX
   _Field_strength       500
   _Details              .

save_


save_NMR_spectrometer_2
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                DRX
   _Field_strength       600
   _Details              .

save_


save_NMR_spectrometer_3
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                DRX
   _Field_strength       900
   _Details              .

save_


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

save_HN-HSQC_1
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HN-HSQC
   _Sample_label         .

save_


save_HNCA_2
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HNCA
   _Sample_label         .

save_


save_CBCANH_3
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      CBCANH
   _Sample_label         .

save_


save_CBCA(CO)NH_4
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      CBCA(CO)NH
   _Sample_label         .

save_


save_HNHA-J_5
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HNHA-J
   _Sample_label         .

save_


save_HNCO_6
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HNCO
   _Sample_label         .

save_


save_CBCACO(N)H_7
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      CBCACO(N)H
   _Sample_label         .

save_


save_HN-HSQC-NOESY-(H)C-HMQC_8
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HN-HSQC-NOESY-(H)C-HMQC
   _Sample_label         .

save_


save_HC-HSQC_9
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HC-HSQC
   _Sample_label         .

save_


save_H(CCO)NH_10
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      H(CCO)NH
   _Sample_label         .

save_


save_(H)C(CO)NH_11
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      (H)C(CO)NH
   _Sample_label         .

save_


save_HC(C)H-TOCSY_12
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HC(C)H-TOCSY
   _Sample_label         .

save_


save_13C-HMQC-NOESY_13
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      13C-HMQC-NOESY
   _Sample_label         .

save_


save_15N-HSQC-NOESY_14
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      15N-HSQC-NOESY
   _Sample_label         .

save_


save_NMR_spec_expt__0_1
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        HN-HSQC
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_2
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        HNCA
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_3
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        CBCANH
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_4
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        CBCA(CO)NH
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_5
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        HNHA-J
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_6
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        HNCO
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_7
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        CBCACO(N)H
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_8
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        HN-HSQC-NOESY-(H)C-HMQC
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_9
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        HC-HSQC
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_10
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        H(CCO)NH
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_11
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        (H)C(CO)NH
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_12
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        HC(C)H-TOCSY
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_13
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        13C-HMQC-NOESY
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_14
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        15N-HSQC-NOESY
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


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

save_ExpCondition
   _Saveframe_category   sample_conditions

   _Details              .

   loop_
      _Variable_type
      _Variable_value
      _Variable_value_error
      _Variable_value_units

      pH            6.3 0.1 pH 
      temperature 295   0.5 K  

   stop_

save_


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

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

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

save_chemical_shift_reference
   _Saveframe_category   chemical_shift_reference

   _Details              .

   loop_
      _Mol_common_name
      _Atom_type
      _Atom_isotope_number
      _Atom_group
      _Chem_shift_units
      _Chem_shift_value
      _Reference_method
      _Reference_type
      _External_reference_sample_geometry
      _External_reference_location
      _External_reference_axis
      _Indirect_shift_ratio
      _Reference_correction_type

      H2O H  1 protons ppm 4.79 internal direct   cylindrical internal parallel 1.0         'temperature, salt, pH' 
      H2O C 13 protons ppm 4.79 external indirect .           .        .        0.251449530  .                      
      H2O N 15 protons ppm 4.79 external 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_ChemShifts
   _Saveframe_category               assigned_chemical_shifts

   _Details                          .

   loop_
      _Sample_label

      $15N-labeled_sample     
      $15N-13C-labeled_sample 

   stop_

   _Sample_conditions_label         $ExpCondition
   _Chem_shift_reference_set_label  $chemical_shift_reference
   _Mol_system_component_name       'c-Abl, FABD'
   _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 .   5 SER H    H   8.425 0.030 1 
         2 .   5 SER N    N 115.528 0.100 1 
         3 .   5 SER CA   C  55.511 0.300 1 
         4 .   5 SER HA   H   4.218 0.030 1 
         5 .   5 SER C    C 172.119 0.300 1 
         6 .   6 THR H    H   8.115 0.030 1 
         7 .   6 THR N    N 116.426 0.100 1 
         8 .   6 THR HA   H   4.709 0.030 1 
         9 .   6 THR C    C 171.393 0.300 1 
        10 .   6 THR CG2  C  18.953 0.300 1 
        11 .   6 THR HG2  H   1.047 0.030 1 
        12 .   7 ARG H    H   8.265 0.030 1 
        13 .   7 ARG N    N 123.919 0.100 1 
        14 .   7 ARG C    C 173.401 0.300 1 
        15 .   8 VAL H    H   8.104 0.030 1 
        16 .   8 VAL N    N 121.990 0.100 1 
        17 .   8 VAL CA   C  59.686 0.300 1 
        18 .   8 VAL HA   H   4.001 0.034 1 
        19 .   8 VAL C    C 173.401 0.300 1 
        20 .   8 VAL CB   C  29.885 0.300 1 
        21 .   8 VAL HB   H   1.950 0.039 1 
        22 .   8 VAL CG2  C  17.888 0.300 1 
        23 .   8 VAL HG2  H   0.846 0.036 2 
        24 .   9 SER H    H   8.313 0.030 1 
        25 .   9 SER N    N 119.772 0.100 1 
        26 .   9 SER C    C 171.665 0.300 1 
        27 .  10 LEU H    H   8.245 0.030 1 
        28 .  10 LEU N    N 125.077 0.100 1 
        29 .  10 LEU CA   C  52.685 0.300 1 
        30 .  10 LEU HA   H   4.272 0.030 1 
        31 .  10 LEU C    C 174.540 0.300 1 
        32 .  10 LEU CB   C  40.270 0.300 1 
        33 .  10 LEU HB2  H   1.609 0.030 1 
        34 .  10 LEU HD1  H   0.805 0.030 2 
        35 .  11 ARG H    H   8.160 0.030 1 
        36 .  11 ARG N    N 121.894 0.100 1 
        37 .  11 ARG CA   C  53.615 0.300 1 
        38 .  11 ARG HA   H   4.218 0.030 1 
        39 .  11 ARG C    C 173.498 0.300 1 
        40 .  11 ARG HD2  H   3.021 0.030 1 
        41 .  12 LYS H    H   8.305 0.030 1 
        42 .  12 LYS N    N 123.244 0.100 1 
        43 .  12 LYS C    C 173.934 0.300 1 
        44 .  13 THR H    H   8.050 0.030 1 
        45 .  13 THR N    N 115.720 0.100 1 
        46 .  13 THR CA   C  59.146 0.300 1 
        47 .  13 THR HA   H   4.235 0.035 1 
        48 .  13 THR C    C 171.484 0.300 1 
        49 .  13 THR HB   H   4.119 0.030 1 
        50 .  13 THR CG2  C  18.953 0.300 1 
        51 .  13 THR HG2  H   1.102 0.038 1 
        52 .  14 ARG H    H   8.324 0.030 1 
        53 .  14 ARG N    N 123.630 0.100 1 
        54 .  14 ARG CA   C  53.214 0.300 1 
        55 .  14 ARG HA   H   4.229 0.034 1 
        56 .  14 ARG C    C 173.098 0.300 1 
        57 .  14 ARG CB   C  28.135 0.300 1 
        58 .  14 ARG HB2  H   1.697 0.033 1 
        59 .  14 ARG CG   C  23.820 0.300 1 
        60 .  14 ARG HG2  H   1.528 0.034 1 
        61 .  14 ARG CD   C  40.809 0.300 1 
        62 .  14 ARG HD2  H   3.094 0.033 1 
        63 .  15 GLN H    H   8.367 0.030 1 
        64 .  15 GLN N    N 123.556 0.100 1 
        65 .  15 GLN CA   C  50.787 0.300 1 
        66 .  15 GLN HA   H   4.516 0.038 1 
        67 .  15 GLN CB   C  25.977 0.300 1 
        68 .  15 GLN HB2  H   1.979 0.035 1 
        69 .  15 GLN CG   C  30.562 0.300 1 
        70 .  15 GLN HG2  H   2.280 0.034 1 
        71 .  15 GLN NE2  N 112.730 0.100 1 
        72 .  15 GLN HE21 H   7.469 0.030 1 
        73 .  15 GLN HE22 H   6.788 0.030 1 
        74 .  16 PRO CA   C  58.877 0.300 1 
        75 .  16 PRO HA   H   4.589 0.036 1 
        76 .  16 PRO CB   C  28.135 0.300 1 
        77 .  16 PRO HB2  H   2.268 0.032 2 
        78 .  16 PRO HB3  H   1.828 0.036 2 
        79 .  16 PRO CG   C  24.629 0.300 1 
        80 .  16 PRO HG2  H   1.920 0.032 2 
        81 .  16 PRO CD   C  47.820 0.300 1 
        82 .  16 PRO HD2  H   3.710 0.038 2 
        83 .  16 PRO HD3  H   3.549 0.037 2 
        84 .  17 PRO CA   C  60.225 0.300 1 
        85 .  17 PRO HA   H   4.299 0.033 1 
        86 .  17 PRO C    C 174.172 0.300 1 
        87 .  17 PRO CB   C  29.213 0.300 1 
        88 .  17 PRO HB2  H   2.193 0.033 2 
        89 .  17 PRO HB3  H   1.829 0.039 2 
        90 .  17 PRO CG   C  24.629 0.300 1 
        91 .  17 PRO HG2  H   1.906 0.030 1 
        92 .  17 PRO CD   C  47.551 0.300 1 
        93 .  17 PRO HD2  H   3.700 0.032 2 
        94 .  17 PRO HD3  H   3.541 0.035 2 
        95 .  18 GLU H    H   8.470 0.030 1 
        96 .  18 GLU N    N 120.796 0.100 1 
        97 .  18 GLU CA   C  54.091 0.300 1 
        98 .  18 GLU HA   H   4.102 0.036 1 
        99 .  18 GLU C    C 173.722 0.300 1 
       100 .  18 GLU CB   C  27.470 0.300 1 
       101 .  18 GLU HB2  H   1.853 0.035 1 
       102 .  18 GLU CG   C  33.528 0.300 1 
       103 .  18 GLU HG2  H   2.140 0.030 1 
       104 .  19 ARG H    H   8.231 0.030 1 
       105 .  19 ARG N    N 121.990 0.100 1 
       106 .  19 ARG CA   C  53.304 0.300 1 
       107 .  19 ARG HA   H   4.244 0.030 1 
       108 .  19 ARG C    C 173.355 0.300 1 
       109 .  19 ARG HB2  H   1.657 0.030 1 
       110 .  19 ARG HG2  H   1.503 0.030 1 
       111 .  19 ARG HD2  H   3.066 0.030 1 
       112 .  20 ILE H    H   8.060 0.030 1 
       113 .  20 ILE N    N 122.665 0.100 1 
       114 .  20 ILE CA   C  58.341 0.300 1 
       115 .  20 ILE HA   H   4.045 0.030 1 
       116 .  20 ILE C    C 173.220 0.300 1 
       117 .  20 ILE CB   C  35.986 0.300 1 
       118 .  20 ILE HB   H   1.755 0.030 1 
       119 .  20 ILE CG2  C  14.382 0.300 1 
       120 .  20 ILE HG2  H   0.823 0.032 1 
       121 .  20 ILE CG1  C  24.359 0.300 1 
       122 .  20 ILE HG12 H   1.398 0.038 2 
       123 .  20 ILE HG13 H   1.087 0.030 2 
       124 .  20 ILE CD1  C  10.067 0.300 1 
       125 .  20 ILE HD1  H   0.800 0.030 1 
       126 .  21 ALA H    H   8.351 0.030 1 
       127 .  21 ALA N    N 128.549 0.100 1 
       128 .  21 ALA CA   C  49.984 0.300 1 
       129 .  21 ALA HA   H   4.262 0.030 1 
       130 .  21 ALA C    C 174.945 0.300 1 
       131 .  21 ALA CB   C  16.449 0.300 1 
       132 .  21 ALA HB   H   1.306 0.030 1 
       133 .  22 SER H    H   8.208 0.030 1 
       134 .  22 SER N    N 115.528 0.100 1 
       135 .  22 SER CA   C  55.910 0.300 1 
       136 .  22 SER HA   H   4.295 0.032 1 
       137 .  22 SER C    C 172.392 0.300 1 
       138 .  22 SER CB   C  60.890 0.300 1 
       139 .  22 SER HB2  H   3.821 0.031 2 
       140 .  22 SER HB3  H   3.764 0.031 2 
       141 .  23 GLY H    H   8.306 0.030 1 
       142 .  23 GLY N    N 111.187 0.100 1 
       143 .  23 GLY CA   C  42.471 0.300 1 
       144 .  23 GLY HA2  H   3.843 0.030 1 
       145 .  23 GLY C    C 170.815 0.300 1 
       146 .  24 ALA H    H   7.923 0.030 1 
       147 .  24 ALA N    N 123.171 0.100 1 
       148 .  24 ALA CA   C  49.731 0.300 1 
       149 .  24 ALA HA   H   4.230 0.036 1 
       150 .  24 ALA C    C 174.795 0.300 1 
       151 .  24 ALA CB   C  16.592 0.300 1 
       152 .  24 ALA HB   H   1.248 0.030 1 
       153 .  25 ILE H    H   8.322 0.030 1 
       154 .  25 ILE N    N 121.315 0.100 1 
       155 .  25 ILE CA   C  57.598 0.300 1 
       156 .  25 ILE HA   H   3.928 0.034 1 
       157 .  25 ILE C    C 172.192 0.300 1 
       158 .  25 ILE CB   C  33.696 0.300 1 
       159 .  25 ILE HB   H   1.933 0.034 1 
       160 .  25 ILE CG2  C  15.461 0.300 1 
       161 .  25 ILE HG2  H   0.819 0.033 1 
       162 .  25 ILE CG1  C  24.629 0.300 1 
       163 .  25 ILE HG12 H   1.488 0.039 1 
       164 .  25 ILE CD1  C   8.989 0.300 1 
       165 .  25 ILE HD1  H   0.799 0.039 1 
       166 .  26 THR H    H   6.535 0.030 1 
       167 .  26 THR N    N 114.949 0.100 1 
       168 .  26 THR CA   C  56.667 0.300 1 
       169 .  26 THR HA   H   4.591 0.032 1 
       170 .  26 THR C    C 171.756 0.300 1 
       171 .  26 THR CB   C  69.334 0.300 1 
       172 .  26 THR HB   H   4.517 0.030 1 
       173 .  26 THR CG2  C  19.025 0.300 1 
       174 .  26 THR HG2  H   1.110 0.030 1 
       175 .  27 LYS H    H   8.721 0.030 1 
       176 .  27 LYS N    N 113.177 0.100 1 
       177 .  27 LYS CA   C  56.989 0.300 1 
       178 .  27 LYS HA   H   3.128 0.033 1 
       179 .  27 LYS C    C 174.903 0.300 1 
       180 .  27 LYS CB   C  29.213 0.300 1 
       181 .  27 LYS HB2  H   1.760 0.038 2 
       182 .  27 LYS HB3  H   1.547 0.030 2 
       183 .  27 LYS CG   C  21.663 0.300 1 
       184 .  27 LYS HG2  H   1.160 0.031 1 
       185 .  27 LYS CD   C  27.056 0.300 1 
       186 .  27 LYS HD2  H   1.581 0.033 1 
       187 .  27 LYS CE   C  39.191 0.300 1 
       188 .  27 LYS HE2  H   2.923 0.035 2 
       189 .  27 LYS HE3  H   2.861 0.038 2 
       190 .  28 GLY H    H   8.129 0.030 1 
       191 .  28 GLY N    N 105.014 0.100 1 
       192 .  28 GLY CA   C  44.045 0.300 1 
       193 .  28 GLY HA2  H   3.527 0.030 2 
       194 .  28 GLY HA3  H   3.644 0.030 2 
       195 .  28 GLY C    C 172.873 0.300 1 
       196 .  29 VAL H    H   7.147 0.030 1 
       197 .  29 VAL N    N 121.990 0.100 1 
       198 .  29 VAL CA   C  62.873 0.300 1 
       199 .  29 VAL HA   H   3.519 0.030 1 
       200 .  29 VAL C    C 176.504 0.300 1 
       201 .  29 VAL CB   C  28.885 0.300 1 
       202 .  29 VAL HB   H   1.829 0.031 1 
       203 .  29 VAL CG1  C  19.506 0.300 1 
       204 .  29 VAL HG1  H   0.871 0.036 2 
       205 .  29 VAL CG2  C  17.888 0.300 1 
       206 .  29 VAL HG2  H   0.130 0.035 2 
       207 .  30 VAL H    H   7.189 0.030 1 
       208 .  30 VAL N    N 120.640 0.100 1 
       209 .  30 VAL CA   C  64.539 0.300 1 
       210 .  30 VAL HA   H   3.176 0.038 1 
       211 .  30 VAL C    C 175.886 0.300 1 
       212 .  30 VAL CB   C  28.674 0.300 1 
       213 .  30 VAL HB   H   1.809 0.038 1 
       214 .  30 VAL CG1  C  19.655 0.334 1 
       215 .  30 VAL HG1  H   0.704 0.034 2 
       216 .  30 VAL CG2  C  19.775 0.300 1 
       217 .  30 VAL HG2  H   0.448 0.037 2 
       218 .  31 LEU H    H   8.414 0.030 1 
       219 .  31 LEU N    N 120.254 0.100 1 
       220 .  31 LEU CA   C  54.950 0.300 1 
       221 .  31 LEU HA   H   4.128 0.036 1 
       222 .  31 LEU C    C 178.093 0.300 1 
       223 .  31 LEU CB   C  37.843 0.300 1 
       224 .  31 LEU HB2  H   1.686 0.033 2 
       225 .  31 LEU HB3  H   1.429 0.030 2 
       226 .  31 LEU CG   C  24.090 0.300 1 
       227 .  31 LEU CD1  C  22.741 0.300 1 
       228 .  31 LEU HD1  H   0.697 0.034 2 
       229 .  31 LEU CD2  C  20.045 0.300 1 
       230 .  31 LEU HD2  H   0.749 0.032 2 
       231 .  31 LEU HG   H   1.545 0.033 1 
       232 .  32 ASP H    H   8.629 0.030 1 
       233 .  32 ASP N    N 122.448 0.100 1 
       234 .  32 ASP CA   C  54.880 0.300 1 
       235 .  32 ASP HA   H   4.311 0.031 1 
       236 .  32 ASP C    C 176.508 0.300 1 
       237 .  32 ASP CB   C  37.202 0.300 1 
       238 .  32 ASP HB2  H   2.689 0.032 2 
       239 .  32 ASP HB3  H   2.485 0.033 2 
       240 .  33 SER H    H   7.777 0.030 1 
       241 .  33 SER N    N 116.571 0.100 1 
       242 .  33 SER CA   C  59.101 0.300 1 
       243 .  33 SER HA   H   4.352 0.031 1 
       244 .  33 SER C    C 176.358 0.300 1 
       245 .  33 SER CB   C  60.185 0.300 1 
       246 .  33 SER HB2  H   4.098 0.036 1 
       247 .  34 THR H    H   8.657 0.030 1 
       248 .  34 THR N    N 116.781 0.100 1 
       249 .  34 THR CA   C  63.752 0.300 1 
       250 .  34 THR HA   H   3.948 0.030 1 
       251 .  34 THR C    C 173.850 0.300 1 
       252 .  34 THR CB   C  65.200 0.300 1 
       253 .  34 THR HB   H   4.127 0.031 1 
       254 .  34 THR CG2  C  20.814 0.300 1 
       255 .  34 THR HG2  H   1.240 0.031 1 
       256 .  35 GLU H    H   7.718 0.030 1 
       257 .  35 GLU N    N 124.305 0.100 1 
       258 .  35 GLU CA   C  56.811 0.300 1 
       259 .  35 GLU HA   H   3.984 0.037 1 
       260 .  35 GLU C    C 176.358 0.300 1 
       261 .  35 GLU CB   C  26.786 0.300 1 
       262 .  35 GLU HB2  H   2.027 0.034 2 
       263 .  35 GLU HB3  H   2.095 0.030 2 
       264 .  35 GLU CG   C  33.258 0.300 1 
       265 .  35 GLU HG2  H   2.289 0.033 2 
       266 .  35 GLU HG3  H   2.172 0.032 2 
       267 .  36 ALA H    H   8.079 0.030 1 
       268 .  36 ALA N    N 121.797 0.100 1 
       269 .  36 ALA CA   C  52.302 0.300 1 
       270 .  36 ALA HA   H   3.972 0.031 1 
       271 .  36 ALA C    C 178.371 0.300 1 
       272 .  36 ALA CB   C  15.110 0.300 1 
       273 .  36 ALA HB   H   1.483 0.030 1 
       274 .  37 LEU H    H   7.701 0.030 1 
       275 .  37 LEU N    N 120.543 0.100 1 
       276 .  37 LEU CA   C  55.133 0.300 1 
       277 .  37 LEU HA   H   4.069 0.031 1 
       278 .  37 LEU C    C 174.789 0.300 1 
       279 .  37 LEU CB   C  38.112 0.300 1 
       280 .  37 LEU HB2  H   2.037 0.039 2 
       281 .  37 LEU HB3  H   1.383 0.034 2 
       282 .  37 LEU CG   C  24.899 0.300 1 
       283 .  37 LEU CD1  C  21.663 0.300 1 
       284 .  37 LEU HD1  H   0.859 0.031 2 
       285 .  37 LEU CD2  C  25.438 0.300 1 
       286 .  37 LEU HD2  H   0.797 0.033 2 
       287 .  37 LEU HG   H   1.469 0.032 1 
       288 .  38 CYS H    H   8.111 0.030 1 
       289 .  38 CYS N    N 118.614 0.100 1 
       290 .  38 CYS CA   C  61.843 0.300 1 
       291 .  38 CYS HA   H   3.790 0.034 1 
       292 .  38 CYS C    C 174.840 0.300 1 
       293 .  38 CYS CB   C  23.250 0.300 1 
       294 .  38 CYS HB2  H   2.989 0.033 2 
       295 .  38 CYS HB3  H   2.828 0.031 2 
       296 .  39 LEU H    H   8.324 0.030 1 
       297 .  39 LEU N    N 121.315 0.100 1 
       298 .  39 LEU CA   C  55.101 0.300 1 
       299 .  39 LEU HA   H   4.077 0.033 1 
       300 .  39 LEU C    C 175.723 0.300 1 
       301 .  39 LEU CB   C  39.191 0.300 1 
       302 .  39 LEU HB2  H   1.585 0.032 1 
       303 .  39 LEU CG   C  24.090 0.300 1 
       304 .  39 LEU CD1  C  21.393 0.300 1 
       305 .  39 LEU HD1  H   0.786 0.031 2 
       306 .  39 LEU HG   H   1.467 0.033 1 
       307 .  40 ALA H    H   7.775 0.030 1 
       308 .  40 ALA N    N 121.966 0.100 1 
       309 .  40 ALA CA   C  52.601 0.300 1 
       310 .  40 ALA HA   H   3.888 0.033 1 
       311 .  40 ALA C    C 177.230 0.300 1 
       312 .  40 ALA CB   C  14.517 0.300 1 
       313 .  40 ALA HB   H   1.250 0.032 1 
       314 .  41 ILE H    H   8.002 0.030 1 
       315 .  41 ILE N    N 117.746 0.100 1 
       316 .  41 ILE CA   C  62.878 0.300 1 
       317 .  41 ILE HA   H   3.148 0.035 1 
       318 .  41 ILE C    C 175.474 0.300 1 
       319 .  41 ILE CB   C  35.685 0.300 1 
       320 .  41 ILE HB   H   1.751 0.037 1 
       321 .  41 ILE CG2  C  14.382 0.300 1 
       322 .  41 ILE HG2  H   0.772 0.034 1 
       323 .  41 ILE CG1  C  27.595 0.300 1 
       324 .  41 ILE HG12 H   1.590 0.034 2 
       325 .  41 ILE HG13 H   0.305 0.036 2 
       326 .  41 ILE CD1  C  11.416 0.300 1 
       327 .  41 ILE HD1  H   0.605 0.030 1 
       328 .  42 SER H    H   8.065 0.030 1 
       329 .  42 SER N    N 116.764 0.100 1 
       330 .  42 SER CA   C  58.628 0.330 1 
       331 .  42 SER HA   H   4.145 0.030 1 
       332 .  42 SER C    C 174.284 0.300 1 
       333 .  42 SER CB   C  60.225 0.300 1 
       334 .  42 SER HB2  H   3.938 0.030 2 
       335 .  42 SER HB3  H   3.896 0.030 2 
       336 .  43 ARG H    H   8.363 0.030 1 
       337 .  43 ARG N    N 120.736 0.100 1 
       338 .  43 ARG CA   C  55.371 0.300 1 
       339 .  43 ARG HA   H   4.160 0.036 1 
       340 .  43 ARG C    C 178.261 0.300 1 
       341 .  43 ARG CB   C  27.595 0.300 1 
       342 .  43 ARG HB2  H   1.739 0.036 1 
       343 .  43 ARG CG   C  25.168 0.300 1 
       344 .  43 ARG HG2  H   1.583 0.038 1 
       345 .  43 ARG CD   C  40.809 0.300 1 
       346 .  43 ARG HD2  H   3.018 0.037 1 
       347 .  43 ARG NE   N 109.161 0.100 1 
       348 .  43 ARG HE   H   7.112 0.030 1 
       349 .  44 ASN H    H   7.776 0.030 1 
       350 .  44 ASN N    N 120.447 0.100 1 
       351 .  44 ASN CA   C  53.708 0.300 1 
       352 .  44 ASN HA   H   4.658 0.030 1 
       353 .  44 ASN C    C 174.146 0.300 1 
       354 .  44 ASN CB   C  37.345 0.300 1 
       355 .  44 ASN HB2  H   2.750 0.032 2 
       356 .  44 ASN HB3  H   2.599 0.037 2 
       357 .  44 ASN ND2  N 112.441 0.100 1 
       358 .  44 ASN HD21 H   7.569 0.030 1 
       359 .  44 ASN HD22 H   7.224 0.030 1 
       360 .  45 SER H    H   8.151 0.030 1 
       361 .  45 SER N    N 107.816 0.100 1 
       362 .  45 SER CA   C  57.715 0.300 1 
       363 .  45 SER HA   H   4.401 0.037 1 
       364 .  45 SER C    C 171.838 0.300 1 
       365 .  45 SER CB   C  60.495 0.300 1 
       366 .  45 SER HB2  H   4.049 0.030 2 
       367 .  45 SER HB3  H   3.985 0.032 2 
       368 .  46 GLU H    H   7.720 0.030 1 
       369 .  46 GLU N    N 119.868 0.100 1 
       370 .  46 GLU CA   C  53.423 0.300 1 
       371 .  46 GLU HA   H   4.367 0.036 1 
       372 .  46 GLU C    C 173.217 0.300 1 
       373 .  46 GLU CB   C  27.326 0.300 1 
       374 .  46 GLU HB2  H   1.904 0.039 1 
       375 .  46 GLU CG   C  33.528 0.300 1 
       376 .  46 GLU HG2  H   2.166 0.034 1 
       377 .  47 GLN H    H   8.003 0.030 1 
       378 .  47 GLN N    N 115.431 0.100 1 
       379 .  47 GLN CA   C  54.020 0.300 1 
       380 .  47 GLN HA   H   4.155 0.030 1 
       381 .  47 GLN C    C 173.277 0.300 1 
       382 .  47 GLN CB   C  24.500 0.300 1 
       383 .  47 GLN HB2  H   2.169 0.030 1 
       384 .  47 GLN CG   C  31.549 0.300 1 
       385 .  47 GLN HG2  H   2.288 0.030 1 
       386 .  47 GLN NE2  N 112.634 0.100 1 
       387 .  47 GLN HE21 H   7.498 0.030 1 
       388 .  47 GLN HE22 H   6.741 0.030 1 
       389 .  48 MET H    H   8.282 0.030 1 
       390 .  48 MET N    N 117.360 0.100 1 
       391 .  48 MET CA   C  52.674 0.300 1 
       392 .  48 MET HA   H   4.481 0.033 1 
       393 .  48 MET C    C 173.217 0.300 1 
       394 .  48 MET CB   C  29.483 0.300 1 
       395 .  48 MET HB2  H   2.544 0.035 2 
       396 .  48 MET HB3  H   2.450 0.039 2 
       397 .  48 MET CG   C  30.292 0.300 1 
       398 .  48 MET HG2  H   2.120 0.035 2 
       399 .  48 MET HG3  H   1.851 0.034 2 
       400 .  49 ALA H    H   7.601 0.030 1 
       401 .  49 ALA N    N 121.604 0.100 1 
       402 .  49 ALA CA   C  49.646 0.300 1 
       403 .  49 ALA HA   H   4.390 0.035 1 
       404 .  49 ALA C    C 174.540 0.300 1 
       405 .  49 ALA CB   C  17.888 0.300 1 
       406 .  49 ALA HB   H   1.280 0.030 1 
       407 .  50 SER H    H   8.456 0.030 1 
       408 .  50 SER N    N 116.792 0.100 1 
       409 .  50 SER CA   C  55.087 0.300 1 
       410 .  50 SER HA   H   4.446 0.031 1 
       411 .  50 SER C    C 172.147 0.300 1 
       412 .  50 SER CB   C  61.965 0.300 1 
       413 .  50 SER HB2  H   4.129 0.033 2 
       414 .  50 SER HB3  H   3.881 0.035 2 
       415 .  51 HIS H    H   8.685 0.030 1 
       416 .  51 HIS N    N 122.314 0.100 1 
       417 .  51 HIS CA   C  56.723 0.300 1 
       418 .  51 HIS HA   H   4.340 0.036 1 
       419 .  51 HIS C    C 174.765 0.300 1 
       420 .  51 HIS CB   C  27.865 0.300 1 
       421 .  51 HIS HB2  H   3.315 0.031 2 
       422 .  51 HIS HB3  H   3.236 0.031 2 
       423 .  51 HIS CD2  C 115.474 0.300 1 
       424 .  51 HIS HD2  H   7.095 0.031 1 
       425 .  51 HIS CE1  C 134.586 0.300 1 
       426 .  51 HIS HE1  H   7.924 0.030 1 
       427 .  52 SER H    H   8.322 0.030 1 
       428 .  52 SER N    N 113.984 0.100 1 
       429 .  52 SER CA   C  58.607 0.300 1 
       430 .  52 SER HA   H   4.062 0.038 1 
       431 .  52 SER C    C 173.371 0.300 1 
       432 .  52 SER CB   C  58.607 0.300 1 
       433 .  52 SER HB2  H   3.873 0.031 1 
       434 .  53 ALA H    H   7.946 0.030 1 
       435 .  53 ALA N    N 125.077 0.100 1 
       436 .  53 ALA CA   C  52.365 0.300 1 
       437 .  53 ALA HA   H   4.093 0.030 1 
       438 .  53 ALA C    C 178.652 0.300 1 
       439 .  53 ALA CB   C  15.375 0.300 1 
       440 .  53 ALA HB   H   1.446 0.034 1 
       441 .  54 VAL H    H   7.513 0.030 1 
       442 .  54 VAL N    N 119.682 0.100 1 
       443 .  54 VAL CA   C  64.000 0.300 1 
       444 .  54 VAL HA   H   3.140 0.033 1 
       445 .  54 VAL C    C 174.453 0.300 1 
       446 .  54 VAL CB   C  28.505 0.300 1 
       447 .  54 VAL HB   H   1.831 0.036 1 
       448 .  54 VAL CG1  C  19.506 0.300 1 
       449 .  54 VAL HG1  H   0.457 0.031 2 
       450 .  54 VAL CG2  C  18.697 0.300 1 
       451 .  54 VAL HG2  H   0.092 0.035 2 
       452 .  55 LEU H    H   7.663 0.030 1 
       453 .  55 LEU N    N 119.193 0.100 1 
       454 .  55 LEU CA   C  55.363 0.312 1 
       455 .  55 LEU HA   H   3.709 0.030 1 
       456 .  55 LEU C    C 176.662 0.300 1 
       457 .  55 LEU CB   C  38.382 0.300 1 
       458 .  55 LEU HB2  H   1.643 0.030 2 
       459 .  55 LEU HB3  H   1.543 0.037 2 
       460 .  55 LEU CG   C  24.144 0.371 1 
       461 .  55 LEU CD1  C  20.584 0.300 1 
       462 .  55 LEU HD1  H   0.749 0.031 2 
       463 .  55 LEU CD2  C  22.202 0.300 1 
       464 .  55 LEU HD2  H   0.825 0.031 2 
       465 .  55 LEU HG   H   1.441 0.233 1 
       466 .  56 GLU H    H   8.289 0.030 1 
       467 .  56 GLU N    N 119.220 0.100 1 
       468 .  56 GLU CA   C  56.719 0.300 1 
       469 .  56 GLU HA   H   3.860 0.034 1 
       470 .  56 GLU C    C 175.734 0.300 1 
       471 .  56 GLU CB   C  26.769 0.300 1 
       472 .  56 GLU HB2  H   1.914 0.034 2 
       473 .  56 GLU HB3  H   1.838 0.030 2 
       474 .  56 GLU CG   C  33.258 0.300 1 
       475 .  56 GLU HG2  H   2.190 0.031 1 
       476 .  57 ALA H    H   7.694 0.000 1 
       477 .  57 ALA N    N 121.026 0.100 1 
       478 .  57 ALA CA   C  52.263 0.300 1 
       479 .  57 ALA HA   H   4.145 0.030 1 
       480 .  57 ALA C    C 179.272 0.300 1 
       481 .  57 ALA CB   C  14.691 0.300 1 
       482 .  57 ALA HB   H   1.385 0.032 1 
       483 .  58 GLY H    H   8.907 0.030 1 
       484 .  58 GLY N    N 110.212 0.100 1 
       485 .  58 GLY CA   C  45.124 0.300 1 
       486 .  58 GLY HA2  H   3.513 0.034 2 
       487 .  58 GLY HA3  H   3.695 0.032 2 
       488 .  58 GLY C    C 170.967 0.300 1 
       489 .  59 LYS H    H   8.579 0.030 1 
       490 .  59 LYS N    N 124.134 0.100 1 
       491 .  59 LYS CA   C  56.920 0.300 1 
       492 .  59 LYS HA   H   3.867 0.036 1 
       493 .  59 LYS C    C 176.635 0.300 1 
       494 .  59 LYS CB   C  28.944 0.300 1 
       495 .  59 LYS HB2  H   1.839 0.036 1 
       496 .  59 LYS CG   C  22.741 0.300 1 
       497 .  59 LYS HG2  H   1.543 0.030 2 
       498 .  59 LYS HG3  H   1.341 0.030 2 
       499 .  59 LYS CD   C  26.517 0.300 1 
       500 .  59 LYS HD2  H   1.547 0.030 1 
       501 .  59 LYS CE   C  38.921 0.300 1 
       502 .  59 LYS HE2  H   2.772 0.035 1 
       503 .  60 ASN H    H   8.064 0.030 1 
       504 .  60 ASN N    N 119.289 0.100 1 
       505 .  60 ASN CA   C  52.944 0.300 1 
       506 .  60 ASN HA   H   4.137 0.030 1 
       507 .  60 ASN C    C 173.710 0.300 1 
       508 .  60 ASN CB   C  34.704 0.300 1 
       509 .  60 ASN HB2  H   2.728 0.033 2 
       510 .  60 ASN HB3  H   2.453 0.035 2 
       511 .  60 ASN ND2  N 111.485 0.100 1 
       512 .  60 ASN HD21 H   7.524 0.030 1 
       513 .  60 ASN HD22 H   6.832 0.030 1 
       514 .  61 LEU H    H   7.602 0.030 1 
       515 .  61 LEU N    N 119.558 0.100 1 
       516 .  61 LEU CA   C  55.422 0.300 1 
       517 .  61 LEU HA   H   4.364 0.035 1 
       518 .  61 LEU C    C 175.968 0.300 1 
       519 .  61 LEU CB   C  38.112 0.300 1 
       520 .  61 LEU HB2  H   2.046 0.038 2 
       521 .  61 LEU HB3  H   1.465 0.030 2 
       522 .  61 LEU CG   C  24.899 0.300 1 
       523 .  61 LEU CD1  C  25.708 0.300 1 
       524 .  61 LEU HD1  H   0.828 0.034 2 
       525 .  61 LEU CD2  C  22.202 0.300 1 
       526 .  61 LEU HD2  H   0.939 0.035 2 
       527 .  61 LEU HG   H   1.469 0.038 1 
       528 .  62 TYR H    H   8.556 0.030 1 
       529 .  62 TYR N    N 120.377 0.100 1 
       530 .  62 TYR CA   C  60.495 0.300 1 
       531 .  62 TYR HA   H   3.679 0.034 1 
       532 .  62 TYR C    C 173.088 0.300 1 
       533 .  62 TYR CB   C  35.406 0.338 1 
       534 .  62 TYR HB2  H   3.084 0.034 2 
       535 .  62 TYR HB3  H   2.795 0.034 2 
       536 .  62 TYR CD1  C 128.822 0.300 3 
       537 .  62 TYR HD1  H   6.831 0.033 3 
       538 .  62 TYR CE1  C 115.777 0.300 3 
       539 .  62 TYR HE1  H   6.669 0.032 3 
       540 .  63 SER H    H   8.112 0.030 1 
       541 .  63 SER N    N 113.309 0.100 1 
       542 .  63 SER CA   C  58.877 0.300 1 
       543 .  63 SER HA   H   3.881 0.039 1 
       544 .  63 SER C    C 175.084 0.300 1 
       545 .  63 SER CB   C  59.692 0.300 1 
       546 .  63 SER HB2  H   3.807 0.031 1 
       547 .  64 PHE H    H   8.026 0.030 1 
       548 .  64 PHE N    N 120.158 0.100 1 
       549 .  64 PHE CA   C  56.315 0.300 1 
       550 .  64 PHE HA   H   4.605 0.032 1 
       551 .  64 PHE C    C 175.871 0.300 1 
       552 .  64 PHE CB   C  35.251 0.300 1 
       553 .  64 PHE HB2  H   3.205 0.030 2 
       554 .  64 PHE HB3  H   2.982 0.030 2 
       555 .  64 PHE CD1  C 127.608 0.300 3 
       556 .  64 PHE HD1  H   7.160 0.030 3 
       557 .  64 PHE HE1  H   7.185 0.031 3 
       558 .  64 PHE CZ   C 125.788 0.300 1 
       559 .  64 PHE HZ   H   6.997 0.030 1 
       560 .  65 CYS H    H   8.618 0.030 1 
       561 .  65 CYS N    N 117.746 0.100 1 
       562 .  65 CYS CA   C  63.322 0.300 1 
       563 .  65 CYS HA   H   4.106 0.034 1 
       564 .  65 CYS C    C 174.074 0.300 1 
       565 .  65 CYS CB   C  24.090 0.300 1 
       566 .  65 CYS HB2  H   3.028 0.035 2 
       567 .  65 CYS HB3  H   2.378 0.030 2 
       568 .  66 VAL H    H   8.117 0.030 1 
       569 .  66 VAL N    N 118.518 0.100 1 
       570 .  66 VAL CA   C  63.730 0.300 1 
       571 .  66 VAL HA   H   3.419 0.031 1 
       572 .  66 VAL C    C 175.594 0.300 1 
       573 .  66 VAL CB   C  28.686 0.300 1 
       574 .  66 VAL HB   H   1.832 0.032 1 
       575 .  66 VAL CG1  C  19.775 0.300 1 
       576 .  66 VAL HG1  H   0.479 0.032 2 
       577 .  66 VAL CG2  C  18.697 0.300 1 
       578 .  66 VAL HG2  H   0.698 0.003 2 
       579 .  67 SER H    H   7.318 0.000 1 
       580 .  67 SER N    N 114.177 0.100 1 
       581 .  67 SER CA   C  58.510 0.300 1 
       582 .  67 SER HA   H   4.347 0.031 1 
       583 .  67 SER C    C 172.633 0.300 1 
       584 .  67 SER CB   C  61.034 0.300 1 
       585 .  67 SER HB2  H   3.984 0.034 1 
       586 .  68 TYR H    H   8.286 0.030 1 
       587 .  68 TYR N    N 122.280 0.100 1 
       588 .  68 TYR CA   C  57.497 0.300 1 
       589 .  68 TYR HA   H   4.212 0.033 1 
       590 .  68 TYR C    C 174.305 0.300 1 
       591 .  68 TYR CB   C  37.574 0.300 1 
       592 .  68 TYR HB2  H   2.966 0.037 2 
       593 .  68 TYR HB3  H   2.828 0.036 2 
       594 .  68 TYR CD1  C 129.125 0.300 3 
       595 .  68 TYR HD1  H   6.564 0.032 3 
       596 .  68 TYR CE1  C 113.957 0.300 3 
       597 .  68 TYR HE1  H   6.344 0.036 3 
       598 .  69 VAL H    H   7.814 0.030 1 
       599 .  69 VAL N    N 117.843 0.100 1 
       600 .  69 VAL CA   C  62.800 0.300 1 
       601 .  69 VAL HA   H   3.499 0.034 1 
       602 .  69 VAL C    C 172.817 0.300 1 
       603 .  69 VAL CB   C  28.944 0.300 1 
       604 .  69 VAL HB   H   2.118 0.030 1 
       605 .  69 VAL CG1  C  20.854 0.300 1 
       606 .  69 VAL HG1  H   1.085 0.031 2 
       607 .  69 VAL CG2  C  17.348 0.300 1 
       608 .  69 VAL HG2  H   0.955 0.034 2 
       609 .  70 ASP H    H   7.302 0.030 1 
       610 .  70 ASP N    N 116.781 0.100 1 
       611 .  70 ASP CA   C  53.783 0.300 1 
       612 .  70 ASP HA   H   4.329 0.033 1 
       613 .  70 ASP C    C 174.203 0.300 1 
       614 .  70 ASP CB   C  37.846 0.300 1 
       615 .  70 ASP HB2  H   2.633 0.030 2 
       616 .  70 ASP HB3  H   2.474 0.030 2 
       617 .  71 SER H    H   7.959 0.030 1 
       618 .  71 SER N    N 114.981 0.100 1 
       619 .  71 SER CA   C  56.450 0.300 1 
       620 .  71 SER HA   H   4.176 0.030 1 
       621 .  71 SER C    C 171.299 0.300 1 
       622 .  71 SER CB   C  60.958 0.300 1 
       623 .  71 SER HB2  H   3.611 0.030 2 
       624 .  71 SER HB3  H   3.471 0.032 2 
       625 .  72 ILE H    H   7.039 0.030 1 
       626 .  72 ILE N    N 123.653 0.100 1 
       627 .  72 ILE CA   C  59.387 0.300 1 
       628 .  72 ILE HA   H   3.700 0.033 1 
       629 .  72 ILE C    C 173.536 0.300 1 
       630 .  72 ILE CB   C  35.126 0.300 1 
       631 .  72 ILE HB   H   1.640 0.032 1 
       632 .  72 ILE CG2  C  15.191 0.300 1 
       633 .  72 ILE HG2  H   0.768 0.037 1 
       634 .  72 ILE CG1  C  24.359 0.300 1 
       635 .  72 ILE HG12 H   1.106 0.030 2 
       636 .  72 ILE HG13 H   0.598 0.039 2 
       637 .  72 ILE CD1  C  11.416 0.300 1 
       638 .  72 ILE HD1  H   0.325 0.039 1 
       639 .  73 GLN H    H   8.798 0.030 1 
       640 .  73 GLN N    N 125.820 0.100 1 
       641 .  73 GLN CA   C  54.964 0.300 1 
       642 .  73 GLN HA   H   4.036 0.032 1 
       643 .  73 GLN C    C 173.927 0.300 1 
       644 .  73 GLN CB   C  27.326 0.300 1 
       645 .  73 GLN HB2  H   2.105 0.031 2 
       646 .  73 GLN HB3  H   1.876 0.031 2 
       647 .  73 GLN CG   C  31.101 0.300 1 
       648 .  73 GLN HG2  H   2.289 0.035 1 
       649 .  73 GLN NE2  N 112.537 0.100 1 
       650 .  73 GLN HE21 H   7.596 0.030 1 
       651 .  73 GLN HE22 H   6.836 0.030 1 
       652 .  74 GLN H    H   7.746 0.030 1 
       653 .  74 GLN N    N 118.498 0.100 1 
       654 .  74 GLN CA   C  53.192 0.300 1 
       655 .  74 GLN HA   H   4.393 0.032 1 
       656 .  74 GLN C    C 174.353 0.300 1 
       657 .  74 GLN CB   C  25.977 0.300 1 
       658 .  74 GLN HB2  H   2.083 0.032 2 
       659 .  74 GLN HB3  H   1.993 0.035 2 
       660 .  74 GLN CG   C  31.101 0.300 1 
       661 .  74 GLN HG2  H   2.407 0.039 1 
       662 .  74 GLN NE2  N 113.460 0.100 1 
       663 .  74 GLN HE21 H   7.781 0.030 1 
       664 .  74 GLN HE22 H   7.173 0.030 1 
       665 .  75 MET H    H   8.838 0.030 1 
       666 .  75 MET N    N 127.006 0.100 1 
       667 .  75 MET CA   C  55.371 0.300 1 
       668 .  75 MET HA   H   4.022 0.031 1 
       669 .  75 MET C    C 175.339 0.300 1 
       670 .  75 MET CB   C  29.483 0.300 1 
       671 .  75 MET HB2  H   2.561 0.030 2 
       672 .  75 MET HB3  H   2.474 0.035 2 
       673 .  75 MET CG   C  29.483 0.300 1 
       674 .  75 MET HG2  H   2.067 0.031 2 
       675 .  75 MET HG3  H   1.948 0.038 2 
       676 .  76 ARG H    H   8.879 0.030 1 
       677 .  76 ARG N    N 118.807 0.100 1 
       678 .  76 ARG CA   C  56.719 0.300 1 
       679 .  76 ARG HA   H   4.106 0.032 1 
       680 .  76 ARG C    C 176.503 0.300 1 
       681 .  76 ARG CG   C  23.820 0.300 1 
       682 .  76 ARG HG2  H   1.545 0.036 1 
       683 .  76 ARG HD2  H   3.116 0.030 1 
       684 .  77 ASN H    H   7.396 0.030 1 
       685 .  77 ASN N    N 117.360 0.100 1 
       686 .  77 ASN CA   C  52.135 0.300 1 
       687 .  77 ASN HA   H   4.679 0.033 1 
       688 .  77 ASN C    C 173.673 0.300 1 
       689 .  77 ASN CB   C  35.416 0.300 1 
       690 .  77 ASN HB2  H   2.707 0.032 2 
       691 .  77 ASN HB3  H   2.569 0.032 2 
       692 .  77 ASN ND2  N 113.984 0.100 1 
       693 .  77 ASN HD21 H   7.779 0.030 1 
       694 .  77 ASN HD22 H   7.176 0.030 1 
       695 .  78 LYS H    H   8.279 0.030 1 
       696 .  78 LYS N    N 123.823 0.100 1 
       697 .  78 LYS CA   C  58.068 0.300 1 
       698 .  78 LYS HA   H   3.799 0.031 1 
       699 .  78 LYS C    C 175.563 0.300 1 
       700 .  78 LYS CB   C  30.022 0.300 1 
       701 .  78 LYS HB2  H   1.741 0.030 1 
       702 .  78 LYS CG   C  22.472 0.300 1 
       703 .  78 LYS HG2  H   1.404 0.036 2 
       704 .  78 LYS HG3  H   1.273 0.034 2 
       705 .  78 LYS CD   C  27.056 0.300 1 
       706 .  78 LYS HD2  H   1.645 0.037 1 
       707 .  78 LYS CE   C  39.191 0.300 1 
       708 .  78 LYS HE2  H   2.868 0.034 1 
       709 .  79 PHE H    H   8.356 0.030 1 
       710 .  79 PHE N    N 118.460 0.100 1 
       711 .  79 PHE CA   C  56.512 0.300 1 
       712 .  79 PHE HA   H   4.104 0.030 1 
       713 .  79 PHE C    C 175.557 0.300 1 
       714 .  79 PHE CB   C  35.595 0.300 1 
       715 .  79 PHE HB2  H   3.162 0.030 1 
       716 .  79 PHE CD1  C 127.912 0.300 3 
       717 .  79 PHE HD1  H   7.197 0.030 3 
       718 .  79 PHE HE1  H   7.214 0.030 3 
       719 .  80 ALA H    H   7.772 0.030 1 
       720 .  80 ALA N    N 121.508 0.100 1 
       721 .  80 ALA CA   C  52.347 0.300 1 
       722 .  80 ALA HA   H   4.139 0.030 1 
       723 .  80 ALA C    C 178.107 0.300 1 
       724 .  80 ALA CB   C  15.215 0.300 1 
       725 .  80 ALA HB   H   1.555 0.036 1 
       726 .  81 PHE H    H   8.626 0.030 1 
       727 .  81 PHE N    N 120.833 0.100 1 
       728 .  81 PHE CA   C  58.257 0.300 1 
       729 .  81 PHE HA   H   4.270 0.030 1 
       730 .  81 PHE C    C 174.364 0.300 1 
       731 .  81 PHE CB   C  36.815 0.300 1 
       732 .  81 PHE HB2  H   3.257 0.034 2 
       733 .  81 PHE HB3  H   3.149 0.030 2 
       734 .  81 PHE CD1  C 127.912 0.300 3 
       735 .  81 PHE HD1  H   7.153 0.030 3 
       736 .  81 PHE CE1  C 127.912 0.300 3 
       737 .  81 PHE HE1  H   7.098 0.030 3 
       738 .  81 PHE CZ   C 125.485 0.300 1 
       739 .  81 PHE HZ   H   7.179 0.030 1 
       740 .  82 ARG H    H   8.630 0.030 1 
       741 .  82 ARG N    N 118.835 0.100 1 
       742 .  82 ARG CA   C  58.068 0.300 1 
       743 .  82 ARG HA   H   3.766 0.030 1 
       744 .  82 ARG C    C 176.020 0.300 1 
       745 .  82 ARG CB   C  27.056 0.300 1 
       746 .  82 ARG HB2  H   1.911 0.030 1 
       747 .  82 ARG CG   C  25.168 0.300 1 
       748 .  82 ARG HG2  H   1.706 0.030 2 
       749 .  82 ARG HG3  H   1.626 0.038 2 
       750 .  82 ARG CD   C  40.780 0.300 1 
       751 .  82 ARG HD2  H   3.108 0.036 1 
       752 .  83 GLU H    H   7.874 0.030 1 
       753 .  83 GLU N    N 118.518 0.100 1 
       754 .  83 GLU CA   C  56.667 0.300 1 
       755 .  83 GLU HA   H   3.951 0.036 1 
       756 .  83 GLU C    C 176.352 0.300 1 
       757 .  83 GLU CB   C  26.539 0.300 1 
       758 .  83 GLU HB2  H   1.882 0.030 1 
       759 .  83 GLU CG   C  33.839 0.300 1 
       760 .  83 GLU HG2  H   2.070 0.030 1 
       761 .  84 ALA H    H   7.692 0.030 1 
       762 .  84 ALA N    N 122.834 0.100 1 
       763 .  84 ALA CA   C  52.516 0.300 1 
       764 .  84 ALA HA   H   4.032 0.030 1 
       765 .  84 ALA C    C 178.077 0.300 1 
       766 .  84 ALA CB   C  15.373 0.300 1 
       767 .  84 ALA HB   H   1.323 0.034 1 
       768 .  85 ILE H    H   8.386 0.000 1 
       769 .  85 ILE N    N 119.482 0.100 1 
       770 .  85 ILE CA   C  62.900 0.300 1 
       771 .  85 ILE HA   H   3.488 0.036 1 
       772 .  85 ILE C    C 174.671 0.300 1 
       773 .  85 ILE CB   C  34.876 0.300 1 
       774 .  85 ILE HB   H   1.807 0.038 1 
       775 .  85 ILE CG2  C  15.461 0.300 1 
       776 .  85 ILE HG2  H   0.618 0.034 1 
       777 .  85 ILE CG1  C  25.708 0.300 1 
       778 .  85 ILE HG12 H   1.324 0.036 2 
       779 .  85 ILE HG13 H   0.477 0.038 2 
       780 .  85 ILE CD1  C  11.416 0.300 1 
       781 .  85 ILE HD1  H   0.323 0.030 1 
       782 .  86 ASN H    H   7.918 0.030 1 
       783 .  86 ASN N    N 120.521 0.100 1 
       784 .  86 ASN CA   C  52.944 0.300 1 
       785 .  86 ASN HA   H   4.498 0.033 1 
       786 .  86 ASN C    C 175.464 0.300 1 
       787 .  86 ASN CB   C  35.146 0.300 1 
       788 .  86 ASN HB2  H   2.869 0.031 2 
       789 .  86 ASN HB3  H   2.782 0.030 2 
       790 .  86 ASN ND2  N 111.573 0.100 1 
       791 .  86 ASN HD21 H   7.562 0.030 1 
       792 .  86 ASN HD22 H   6.750 0.030 1 
       793 .  87 LYS H    H   7.668 0.030 1 
       794 .  87 LYS N    N 120.736 0.100 1 
       795 .  87 LYS CA   C  56.989 0.300 1 
       796 .  87 LYS HA   H   4.017 0.030 1 
       797 .  87 LYS C    C 175.704 0.300 1 
       798 .  87 LYS CB   C  29.213 0.300 1 
       799 .  87 LYS HB2  H   1.836 0.035 1 
       800 .  87 LYS CG   C  22.741 0.300 1 
       801 .  87 LYS HG2  H   1.531 0.038 2 
       802 .  87 LYS HG3  H   1.333 0.039 2 
       803 .  87 LYS CD   C  26.517 0.300 1 
       804 .  87 LYS HD2  H   1.587 0.032 1 
       805 .  87 LYS CE   C  39.191 0.300 1 
       806 .  87 LYS HE2  H   2.889 0.035 1 
       807 .  88 LEU H    H   7.833 0.030 1 
       808 .  88 LEU N    N 121.017 0.100 1 
       809 .  88 LEU CA   C  56.009 0.300 1 
       810 .  88 LEU HA   H   3.983 0.030 1 
       811 .  88 LEU C    C 174.955 0.300 1 
       812 .  88 LEU CB   C  38.652 0.300 1 
       813 .  88 LEU HB2  H   2.292 0.031 2 
       814 .  88 LEU HB3  H   1.391 0.031 2 
       815 .  88 LEU CG   C  24.629 0.300 1 
       816 .  88 LEU CD1  C  20.854 0.300 1 
       817 .  88 LEU HD1  H   0.790 0.034 1 
       818 .  88 LEU CD2  C  23.550 0.300 1 
       819 .  88 LEU HD2  H   0.877 0.030 1 
       820 .  88 LEU HG   H   1.486 0.036 1 
       821 .  89 GLU H    H   8.588 0.030 1 
       822 .  89 GLU N    N 119.482 0.100 1 
       823 .  89 GLU CA   C  57.259 0.300 1 
       824 .  89 GLU HA   H   3.360 0.037 1 
       825 .  89 GLU C    C 176.019 0.300 1 
       826 .  89 GLU CB   C  26.517 0.300 1 
       827 .  89 GLU HB2  H   2.154 0.039 2 
       828 .  89 GLU HB3  H   1.999 0.037 2 
       829 .  89 GLU CG   C  32.989 0.300 1 
       830 .  89 GLU HG2  H   1.840 0.034 1 
       831 .  90 ASN H    H   7.836 0.030 1 
       832 .  90 ASN N    N 117.650 0.100 1 
       833 .  90 ASN CA   C  53.462 0.300 1 
       834 .  90 ASN HA   H   4.209 0.030 1 
       835 .  90 ASN C    C 174.828 0.300 1 
       836 .  90 ASN CB   C  35.481 0.300 1 
       837 .  90 ASN HB2  H   2.766 0.030 1 
       838 .  90 ASN ND2  N 113.309 0.100 1 
       839 .  90 ASN HD21 H   7.412 0.030 1 
       840 .  90 ASN HD22 H   6.800 0.030 1 
       841 .  91 ASN H    H   8.497 0.030 1 
       842 .  91 ASN N    N 119.193 0.100 1 
       843 .  91 ASN CA   C  52.610 0.300 1 
       844 .  91 ASN HA   H   4.416 0.030 1 
       845 .  91 ASN C    C 175.687 0.300 1 
       846 .  91 ASN CB   C  35.416 0.300 1 
       847 .  91 ASN HB2  H   2.784 0.034 2 
       848 .  91 ASN HB3  H   2.386 0.033 2 
       849 .  91 ASN ND2  N 110.705 0.100 1 
       850 .  91 ASN HD21 H   6.764 0.030 1 
       851 .  91 ASN HD22 H   6.658 0.030 1 
       852 .  92 LEU H    H   8.421 0.030 1 
       853 .  92 LEU N    N 120.640 0.100 1 
       854 .  92 LEU CA   C  55.236 0.300 1 
       855 .  92 LEU HA   H   3.930 0.038 1 
       856 .  92 LEU C    C 176.486 0.300 1 
       857 .  92 LEU CB   C  38.382 0.300 1 
       858 .  92 LEU HB2  H   1.783 0.034 2 
       859 .  92 LEU HB3  H   1.175 0.030 2 
       860 .  92 LEU CG   C  23.550 0.300 1 
       861 .  92 LEU CD1  C  22.741 0.300 1 
       862 .  92 LEU HD1  H   0.549 0.031 2 
       863 .  92 LEU CD2  C  19.775 0.300 1 
       864 .  92 LEU HD2  H   0.703 0.030 2 
       865 .  92 LEU HG   H   1.694 0.031 1 
       866 .  93 ARG H    H   7.934 0.030 1 
       867 .  93 ARG N    N 120.618 0.100 1 
       868 .  93 ARG CA   C  56.882 0.300 1 
       869 .  93 ARG HA   H   3.894 0.032 1 
       870 .  93 ARG C    C 176.685 0.300 1 
       871 .  93 ARG CB   C  27.056 0.300 1 
       872 .  93 ARG HB2  H   1.908 0.034 2 
       873 .  93 ARG HB3  H   1.828 0.037 2 
       874 .  93 ARG CG   C  24.899 0.300 1 
       875 .  93 ARG HG2  H   1.556 0.030 2 
       876 .  93 ARG HG3  H   1.478 0.034 2 
       877 .  93 ARG CD   C  40.539 0.300 1 
       878 .  93 ARG HD2  H   3.104 0.038 1 
       879 .  94 GLU H    H   7.626 0.030 1 
       880 .  94 GLU N    N 117.264 0.100 1 
       881 .  94 GLU CA   C  55.977 0.300 1 
       882 .  94 GLU HA   H   3.969 0.030 1 
       883 .  94 GLU C    C 175.306 0.300 1 
       884 .  94 GLU CB   C  27.255 0.300 1 
       885 .  94 GLU HB2  H   2.139 0.035 1 
       886 .  94 GLU CG   C  32.539 0.380 1 
       887 .  94 GLU HG2  H   2.373 0.034 2 
       888 .  94 GLU HG3  H   2.149 0.030 2 
       889 .  95 LEU H    H   7.215 0.030 1 
       890 .  95 LEU N    N 117.534 0.100 1 
       891 .  95 LEU CA   C  53.023 0.300 1 
       892 .  95 LEU HA   H   4.268 0.038 1 
       893 .  95 LEU C    C 174.617 0.300 1 
       894 .  95 LEU CB   C  40.270 0.300 1 
       895 .  95 LEU HB2  H   1.852 0.033 2 
       896 .  95 LEU HB3  H   1.608 0.036 2 
       897 .  95 LEU CG   C  24.359 0.300 1 
       898 .  95 LEU CD1  C  20.584 0.300 1 
       899 .  95 LEU HD1  H   0.789 0.034 2 
       900 .  95 LEU CD2  C  23.820 0.300 1 
       901 .  95 LEU HD2  H   0.943 0.036 2 
       902 .  95 LEU HG   H   1.614 0.035 1 
       903 .  96 GLN H    H   7.533 0.030 1 
       904 .  96 GLN N    N 117.872 0.100 1 
       905 .  96 GLN CA   C  54.205 0.300 1 
       906 .  96 GLN HA   H   4.044 0.031 1 
       907 .  96 GLN C    C 173.378 0.300 1 
       908 .  96 GLN CB   C  26.897 0.300 1 
       909 .  96 GLN HB2  H   2.020 0.031 1 
       910 .  96 GLN CG   C  31.620 0.300 1 
       911 .  96 GLN HG2  H   2.375 0.030 1 
       912 .  96 GLN NE2  N 111.766 0.100 1 
       913 .  96 GLN HE21 H   7.185 0.030 1 
       914 .  96 GLN HE22 H   6.795 0.030 1 
       915 .  97 ILE H    H   7.629 0.030 1 
       916 .  97 ILE N    N 118.807 0.100 1 
       917 .  97 ILE CA   C  58.512 0.300 1 
       918 .  97 ILE HA   H   4.050 0.030 1 
       919 .  97 ILE C    C 172.982 0.300 1 
       920 .  97 ILE CB   C  35.802 0.300 1 
       921 .  97 ILE HB   H   1.802 0.030 1 
       922 .  97 ILE CG2  C  14.652 0.300 1 
       923 .  97 ILE HG2  H   0.791 0.034 1 
       924 .  97 ILE CG1  C  24.359 0.300 1 
       925 .  97 ILE HG12 H   1.401 0.030 2 
       926 .  97 ILE HG13 H   1.104 0.030 2 
       927 .  97 ILE CD1  C  10.337 0.300 1 
       928 .  97 ILE HD1  H   0.737 0.030 1 
       929 .  98 CYS H    H   8.169 0.030 1 
       930 .  98 CYS N    N 124.788 0.100 1 
       931 .  98 CYS CA   C  53.753 0.300 1 
       932 .  98 CYS HA   H   4.640 0.032 1 
       933 .  98 CYS CB   C  24.502 0.300 1 
       934 .  98 CYS HB2  H   2.818 0.032 2 
       935 .  98 CYS HB3  H   2.756 0.030 2 
       936 .  99 PRO CA   C  60.764 0.300 1 
       937 .  99 PRO HA   H   4.297 0.033 1 
       938 .  99 PRO C    C 174.128 0.300 1 
       939 .  99 PRO CB   C  28.944 0.300 1 
       940 .  99 PRO HB2  H   2.197 0.036 2 
       941 .  99 PRO HB3  H   1.830 0.034 2 
       942 .  99 PRO CG   C  24.629 0.300 1 
       943 .  99 PRO HG2  H   1.922 0.034 2 
       944 .  99 PRO HG3  H   1.825 0.033 2 
       945 .  99 PRO CD   C  48.090 0.300 1 
       946 .  99 PRO HD2  H   3.692 0.039 2 
       947 .  99 PRO HD3  H   3.636 0.030 2 
       948 . 100 ALA H    H   8.264 0.030 1 
       949 . 100 ALA N    N 123.630 0.100 1 
       950 . 100 ALA CA   C  50.153 0.300 1 
       951 . 100 ALA HA   H   4.176 0.036 1 
       952 . 100 ALA C    C 175.392 0.300 1 
       953 . 100 ALA CB   C  16.520 0.300 1 
       954 . 100 ALA HB   H   1.291 0.033 1 
       955 . 101 THR H    H   7.897 0.030 1 
       956 . 101 THR N    N 112.441 0.100 1 
       957 . 101 THR CA   C  58.814 0.300 1 
       958 . 101 THR HA   H   4.220 0.033 1 
       959 . 101 THR C    C 171.637 0.300 1 
       960 . 101 THR CB   C  67.236 0.300 1 
       961 . 101 THR HB   H   4.130 0.035 1 
       962 . 101 THR CG2  C  18.799 0.325 1 
       963 . 101 THR HG2  H   1.109 0.030 1 
       964 . 102 ALA H    H   8.199 0.030 1 
       965 . 102 ALA N    N 126.331 0.100 1 
       966 . 102 ALA CA   C  50.153 0.300 1 
       967 . 102 ALA HA   H   4.233 0.030 1 
       968 . 102 ALA C    C 175.439 0.300 1 
       969 . 102 ALA CB   C  16.363 0.300 1 
       970 . 102 ALA HB   H   1.304 0.033 1 
       971 . 103 GLY H    H   8.303 0.030 1 
       972 . 103 GLY N    N 108.583 0.100 1 
       973 . 103 GLY CA   C  42.691 0.300 1 
       974 . 103 GLY HA2  H   3.875 0.036 1 
       975 . 103 GLY C    C 171.360 0.300 1 
       976 . 104 SER H    H   8.081 0.030 1 
       977 . 104 SER N    N 115.238 0.100 1 
       978 . 104 SER CA   C  55.522 0.300 1 
       979 . 104 SER HA   H   4.451 0.033 1 
       980 . 104 SER C    C 171.702 0.300 1 
       981 . 104 SER CB   C  61.391 0.300 1 
       982 . 104 SER HB2  H   3.809 0.032 2 
       983 . 104 SER HB3  H   3.770 0.031 2 
       984 . 105 GLY H    H   8.185 0.030 1 
       985 . 105 GLY N    N 110.801 0.100 1 
       986 . 105 GLY CA   C  41.825 0.300 1 
       987 . 105 GLY HA2  H   4.008 0.030 1 
       988 . 106 PRO CA   C  59.686 0.300 1 
       989 . 106 PRO HA   H   4.509 0.030 1 
       990 . 106 PRO C    C 173.393 0.300 1 
       991 . 106 PRO CB   C  31.957 0.346 1 
       992 . 106 PRO HB2  H   2.282 0.030 2 
       993 . 106 PRO HB3  H   2.038 0.030 2 
       994 . 106 PRO CG   C  22.202 0.300 1 
       995 . 106 PRO HG2  H   1.846 0.033 1 
       996 . 106 PRO CD   C  47.281 0.300 1 
       997 . 106 PRO HD2  H   3.488 0.030 2 
       998 . 106 PRO HD3  H   3.420 0.030 2 
       999 . 107 ALA H    H   8.463 0.030 1 
      1000 . 107 ALA N    N 125.077 0.100 1 
      1001 . 107 ALA CA   C  49.731 0.300 1 
      1002 . 107 ALA HA   H   4.221 0.030 1 
      1003 . 107 ALA C    C 174.762 0.300 1 
      1004 . 107 ALA CB   C  16.592 0.300 1 
      1005 . 107 ALA HB   H   1.294 0.030 1 
      1006 . 108 ALA H    H   8.076 0.030 1 
      1007 . 108 ALA N    N 123.283 0.100 1 
      1008 . 108 ALA CA   C  49.731 0.300 1 
      1009 . 108 ALA HA   H   4.218 0.030 1 
      1010 . 108 ALA C    C 175.078 0.300 1 
      1011 . 108 ALA CB   C  16.627 0.300 1 
      1012 . 108 ALA HB   H   1.279 0.035 1 
      1013 . 109 THR H    H   7.982 0.030 1 
      1014 . 109 THR N    N 113.984 0.100 1 
      1015 . 109 THR CA   C  59.101 0.300 1 
      1016 . 109 THR HA   H   4.201 0.034 1 
      1017 . 109 THR C    C 171.500 0.300 1 
      1018 . 109 THR CB   C  66.966 0.300 1 
      1019 . 109 THR HB   H   4.063 0.032 1 
      1020 . 109 THR CG2  C  19.025 0.300 1 
      1021 . 109 THR HG2  H   1.109 0.034 1 
      1022 . 110 GLN H    H   8.270 0.030 1 
      1023 . 110 GLN N    N 123.244 0.100 1 
      1024 . 110 GLN CA   C  52.643 0.300 1 
      1025 . 110 GLN HA   H   4.057 0.031 1 
      1026 . 110 GLN C    C 171.247 0.300 1 
      1027 . 110 GLN CB   C  27.326 0.300 1 
      1028 . 110 GLN HB2  H   1.559 0.039 2 
      1029 . 110 GLN HB3  H   1.558 0.030 2 
      1030 . 110 GLN CG   C  31.101 0.300 1 
      1031 . 110 GLN HG2  H   1.975 0.030 2 
      1032 . 110 GLN HG3  H   1.833 0.030 2 
      1033 . 110 GLN NE2  N 112.537 0.100 1 
      1034 . 110 GLN HE21 H   7.314 0.030 1 
      1035 . 110 GLN HE22 H   6.761 0.030 1 
      1036 . 111 ASP H    H   8.046 0.030 1 
      1037 . 111 ASP N    N 121.219 0.100 1 
      1038 . 111 ASP CA   C  50.517 0.300 1 
      1039 . 111 ASP HA   H   4.500 0.030 1 
      1040 . 111 ASP C    C 173.959 0.300 1 
      1041 . 111 ASP CB   C  38.382 0.300 1 
      1042 . 111 ASP HB2  H   2.648 0.030 2 
      1043 . 111 ASP HB3  H   2.529 0.033 2 
      1044 . 112 PHE H    H   8.777 0.030 1 
      1045 . 112 PHE N    N 123.244 0.100 1 
      1046 . 112 PHE CA   C  54.832 0.300 1 
      1047 . 112 PHE HA   H   4.878 0.036 1 
      1048 . 112 PHE C    C 173.379 0.300 1 
      1049 . 112 PHE CB   C  36.225 0.300 1 
      1050 . 112 PHE HB2  H   3.426 0.032 2 
      1051 . 112 PHE HB3  H   2.790 0.036 2 
      1052 . 112 PHE CD1  C 128.215 0.300 3 
      1053 . 112 PHE HD1  H   7.140 0.030 3 
      1054 . 112 PHE CE1  C 127.912 0.300 3 
      1055 . 112 PHE HE1  H   7.407 0.030 3 
      1056 . 112 PHE HZ   H   7.007 0.030 1 
      1057 . 113 SER H    H   8.596 0.030 1 
      1058 . 113 SER N    N 117.264 0.100 1 
      1059 . 113 SER CA   C  60.495 0.300 1 
      1060 . 113 SER HA   H   3.980 0.031 1 
      1061 . 113 SER C    C 174.651 0.300 1 
      1062 . 113 SER CB   C  59.955 0.300 1 
      1063 . 113 SER HB2  H   3.947 0.030 1 
      1064 . 114 LYS H    H   8.160 0.030 1 
      1065 . 114 LYS N    N 123.726 0.100 1 
      1066 . 114 LYS CA   C  57.259 0.300 1 
      1067 . 114 LYS HA   H   4.102 0.033 1 
      1068 . 114 LYS C    C 176.978 0.300 1 
      1069 . 114 LYS CB   C  28.674 0.300 1 
      1070 . 114 LYS HB2  H   1.717 0.030 1 
      1071 . 114 LYS CG   C  23.011 0.300 1 
      1072 . 114 LYS HG2  H   1.483 0.035 2 
      1073 . 114 LYS HG3  H   1.328 0.034 2 
      1074 . 114 LYS CD   C  26.786 0.300 1 
      1075 . 114 LYS HD2  H   1.619 0.031 1 
      1076 . 114 LYS CE   C  38.921 0.300 1 
      1077 . 114 LYS HE2  H   2.880 0.033 1 
      1078 . 115 LEU H    H   8.197 0.030 1 
      1079 . 115 LEU N    N 121.315 0.100 1 
      1080 . 115 LEU CA   C  55.371 0.300 1 
      1081 . 115 LEU HA   H   4.009 0.037 1 
      1082 . 115 LEU C    C 176.197 0.300 1 
      1083 . 115 LEU CB   C  38.921 0.300 1 
      1084 . 115 LEU HB2  H   1.758 0.036 2 
      1085 . 115 LEU HB3  H   1.586 0.032 2 
      1086 . 115 LEU CG   C  24.359 0.300 1 
      1087 . 115 LEU CD1  C  22.472 0.300 1 
      1088 . 115 LEU HD1  H   0.762 0.034 2 
      1089 . 115 LEU CD2  C  23.281 0.300 1 
      1090 . 115 LEU HD2  H   0.671 0.037 2 
      1091 . 115 LEU HG   H   1.466 0.033 1 
      1092 . 116 LEU H    H   8.542 0.030 1 
      1093 . 116 LEU N    N 119.289 0.100 1 
      1094 . 116 LEU CA   C  55.182 0.300 1 
      1095 . 116 LEU HA   H   3.872 0.036 1 
      1096 . 116 LEU C    C 176.581 0.300 1 
      1097 . 116 LEU CB   C  38.921 0.300 1 
      1098 . 116 LEU HB2  H   1.723 0.031 2 
      1099 . 116 LEU HB3  H   1.624 0.037 2 
      1100 . 116 LEU CG   C  24.629 0.300 1 
      1101 . 116 LEU CD1  C  21.932 0.300 1 
      1102 . 116 LEU HD1  H   0.870 0.035 2 
      1103 . 116 LEU CD2  C  22.741 0.300 1 
      1104 . 116 LEU HD2  H   0.606 0.032 2 
      1105 . 116 LEU HG   H   1.561 0.034 1 
      1106 . 117 SER H    H   7.881 0.030 1 
      1107 . 117 SER N    N 115.528 0.100 1 
      1108 . 117 SER CA   C  58.385 0.300 1 
      1109 . 117 SER HA   H   4.211 0.030 1 
      1110 . 117 SER C    C 174.994 0.300 1 
      1111 . 117 SER CB   C  59.686 0.300 1 
      1112 . 117 SER HB2  H   3.949 0.032 1 
      1113 . 118 SER H    H   8.002 0.030 1 
      1114 . 118 SER N    N 119.579 0.100 1 
      1115 . 118 SER CA   C  59.955 0.300 1 
      1116 . 118 SER HA   H   4.346 0.033 1 
      1117 . 118 SER C    C 172.096 0.300 1 
      1118 . 118 SER CB   C  61.034 0.300 1 
      1119 . 118 SER HB2  H   4.019 0.034 2 
      1120 . 118 SER HB3  H   3.743 0.032 2 
      1121 . 119 VAL H    H   8.111 0.030 1 
      1122 . 119 VAL N    N 122.280 0.100 1 
      1123 . 119 VAL CA   C  64.539 0.300 1 
      1124 . 119 VAL HA   H   3.358 0.030 1 
      1125 . 119 VAL C    C 174.575 0.300 1 
      1126 . 119 VAL CB   C  28.404 0.300 1 
      1127 . 119 VAL HB   H   2.182 0.033 1 
      1128 . 119 VAL CG1  C  21.393 0.300 1 
      1129 . 119 VAL HG1  H   0.903 0.030 2 
      1130 . 119 VAL CG2  C  19.775 0.300 1 
      1131 . 119 VAL HG2  H   0.874 0.030 2 
      1132 . 120 LYS H    H   7.851 0.030 1 
      1133 . 120 LYS N    N 121.026 0.100 1 
      1134 . 120 LYS CA   C  56.180 0.300 1 
      1135 . 120 LYS HA   H   3.944 0.030 1 
      1136 . 120 LYS C    C 175.231 0.300 1 
      1137 . 120 LYS CB   C  29.252 0.394 1 
      1138 . 120 LYS HB2  H   1.889 0.030 2 
      1139 . 120 LYS HB3  H   1.850 0.030 2 
      1140 . 120 LYS CG   C  22.202 0.300 1 
      1141 . 120 LYS HG2  H   1.407 0.030 1 
      1142 . 120 LYS CD   C  26.517 0.300 1 
      1143 . 120 LYS HD2  H   1.637 0.037 1 
      1144 . 120 LYS CE   C  38.921 0.300 1 
      1145 . 120 LYS HE2  H   2.870 0.030 1 
      1146 . 121 GLU H    H   7.819 0.030 1 
      1147 . 121 GLU N    N 119.579 0.100 1 
      1148 . 121 GLU CA   C  56.990 0.300 1 
      1149 . 121 GLU HA   H   4.049 0.030 1 
      1150 . 121 GLU C    C 176.494 0.300 1 
      1151 . 121 GLU CB   C  27.360 0.300 1 
      1152 . 121 GLU HB2  H   2.121 0.036 1 
      1153 . 121 GLU CG   C  33.798 0.300 1 
      1154 . 121 GLU HG2  H   2.352 0.030 1 
      1155 . 122 ILE H    H   8.052 0.030 1 
      1156 . 122 ILE N    N 118.518 0.100 1 
      1157 . 122 ILE CA   C  63.237 0.300 1 
      1158 . 122 ILE HA   H   3.480 0.030 1 
      1159 . 122 ILE C    C 174.448 0.300 1 
      1160 . 122 ILE CB   C  35.416 0.300 1 
      1161 . 122 ILE HB   H   1.942 0.034 1 
      1162 . 122 ILE CG2  C  15.461 0.300 1 
      1163 . 122 ILE HG2  H   1.333 0.030 1 
      1164 . 122 ILE CG1  C  28.135 0.300 1 
      1165 . 122 ILE HG12 H   1.774 0.030 2 
      1166 . 122 ILE HG13 H   0.778 0.038 2 
      1167 . 122 ILE CD1  C  12.225 0.300 1 
      1168 . 122 ILE HD1  H   0.702 0.034 1 
      1169 . 123 SER H    H   8.347 0.030 1 
      1170 . 123 SER N    N 113.791 0.100 1 
      1171 . 123 SER CA   C  59.028 0.300 1 
      1172 . 123 SER HA   H   3.848 0.035 1 
      1173 . 123 SER C    C 173.390 0.300 1 
      1174 . 123 SER CB   C  59.776 0.300 1 
      1175 . 123 SER HB2  H   3.841 0.033 1 
      1176 . 124 ASP H    H   8.314 0.030 1 
      1177 . 124 ASP N    N 119.965 0.100 1 
      1178 . 124 ASP CA   C  54.562 0.300 1 
      1179 . 124 ASP HA   H   4.255 0.035 1 
      1180 . 124 ASP C    C 176.376 0.300 1 
      1181 . 124 ASP CB   C  37.999 0.300 1 
      1182 . 124 ASP HB2  H   2.811 0.030 2 
      1183 . 124 ASP HB3  H   2.575 0.035 2 
      1184 . 125 ILE H    H   7.837 0.030 1 
      1185 . 125 ILE N    N 118.421 0.100 1 
      1186 . 125 ILE CA   C  62.731 0.300 1 
      1187 . 125 ILE HA   H   3.556 0.031 1 
      1188 . 125 ILE C    C 175.916 0.300 1 
      1189 . 125 ILE CB   C  35.955 0.300 1 
      1190 . 125 ILE HB   H   1.855 0.035 1 
      1191 . 125 ILE CG2  C  14.921 0.300 1 
      1192 . 125 ILE HG2  H   0.862 0.030 1 
      1193 . 125 ILE CG1  C  26.517 0.300 1 
      1194 . 125 ILE HG12 H   1.972 0.038 2 
      1195 . 125 ILE HG13 H   0.912 0.034 2 
      1196 . 125 ILE CD1  C  12.494 0.300 1 
      1197 . 125 ILE HD1  H   0.818 0.033 1 
      1198 . 126 VAL H    H   8.322 0.030 1 
      1199 . 126 VAL N    N 117.245 0.100 1 
      1200 . 126 VAL CA   C  63.009 0.300 1 
      1201 . 126 VAL HA   H   3.547 0.033 1 
      1202 . 126 VAL C    C 175.104 0.300 1 
      1203 . 126 VAL CB   C  28.686 0.300 1 
      1204 . 126 VAL HB   H   2.040 0.031 1 
      1205 . 126 VAL CG1  C  21.124 0.300 1 
      1206 . 126 VAL HG1  H   0.880 0.036 2 
      1207 . 126 VAL CG2  C  19.955 0.300 1 
      1208 . 126 VAL HG2  H   0.749 0.031 2 
      1209 . 127 GLN H    H   7.910 0.030 1 
      1210 . 127 GLN N    N 116.106 0.100 1 
      1211 . 127 GLN CA   C  55.305 0.300 1 
      1212 . 127 GLN HA   H   4.045 0.030 1 
      1213 . 127 GLN C    C 174.036 0.300 1 
      1214 . 127 GLN CB   C  26.825 0.300 1 
      1215 . 127 GLN HB2  H   2.132 0.031 2 
      1216 . 127 GLN HB3  H   2.053 0.033 2 
      1217 . 127 GLN CG   C  32.336 0.300 1 
      1218 . 127 GLN HG2  H   2.572 0.031 2 
      1219 . 127 GLN HG3  H   2.253 0.032 2 
      1220 . 127 GLN NE2  N 112.151 0.100 1 
      1221 . 127 GLN HE21 H   7.067 0.030 1 
      1222 . 127 GLN HE22 H   6.751 0.030 1 
      1223 . 128 ARG H    H   7.339 0.030 1 
      1224 . 128 ARG N    N 117.071 0.100 1 
      1225 . 128 ARG CA   C  53.783 0.300 1 
      1226 . 128 ARG HA   H   4.272 0.030 1 
      1227 . 128 ARG C    C 173.926 0.300 1 
      1228 . 128 ARG CB   C  28.135 0.300 1 
      1229 . 128 ARG HB2  H   1.795 0.030 1 
      1230 . 128 ARG CG   C  24.899 0.300 1 
      1231 . 128 ARG HG2  H   1.743 0.034 1 
      1232 . 128 ARG CD   C  41.079 0.300 1 
      1233 . 128 ARG HD2  H   3.026 0.035 1 
      1234 . 128 ARG NE   N 109.933 0.100 1 
      1235 . 128 ARG HE   H   7.080 0.030 1 
      1236 . 129 LEU H    H   7.652 0.030 1 
      1237 . 129 LEU N    N 121.990 0.100 1 
      1238 . 129 LEU CA   C  52.385 0.300 1 
      1239 . 129 LEU HA   H   4.257 0.036 1 
      1240 . 129 LEU C    C 173.569 0.300 1 
      1241 . 129 LEU CB   C  39.347 0.300 1 
      1242 . 129 LEU HB2  H   1.789 0.030 2 
      1243 . 129 LEU HB3  H   1.559 0.030 2 
      1244 . 129 LEU CG   C  23.281 0.300 1 
      1245 . 129 LEU CD1  C  23.281 0.300 1 
      1246 . 129 LEU HD1  H   0.818 0.032 2 
      1247 . 129 LEU CD2  C  20.315 0.300 1 
      1248 . 129 LEU HD2  H   0.754 0.034 2 
      1249 . 129 LEU HG   H   1.969 0.030 1 
      1250 . 130 GLU H    H   7.895 0.030 1 
      1251 . 130 GLU N    N 125.656 0.100 1 
      1252 . 130 GLU CA   C  55.391 0.300 1 
      1253 . 130 GLU HA   H   4.002 0.030 1 
      1254 . 130 GLU HB2  H   1.530 0.030 1 
      1255 . 130 GLU HG2  H   2.099 0.030 1 

   stop_

save_