data_5917

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

save_entry_information
   _Saveframe_category      entry_information

   _Entry_title            
;
Backbone 1HN, 13C, 15N Chemical Shift Assignments for human eIF2alpha 
;
   _BMRB_accession_number   5917
   _BMRB_flat_file_name     bmr5917.str
   _Entry_type              original
   _Submission_date         2003-08-21
   _Accession_date          2003-08-21
   _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 Ito Takuhiro . . 

   stop_

   loop_
      _Saveframe_category_type
      _Saveframe_category_type_count

      assigned_chemical_shifts 1 

   stop_

   loop_
      _Data_type
      _Data_type_count

      "1H chemical shifts"  278 
      "13C chemical shifts" 566 
      "15N chemical shifts" 278 

   stop_

   loop_
      _Revision_date
      _Revision_keyword
      _Revision_author
      _Revision_detail

      2004-02-13 original author . 

   stop_

   _Original_release_date   2004-02-13

save_


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

save_entry_citation
   _Saveframe_category           entry_citation

   _Citation_full                .
   _Citation_title              
;
Using condon optimization, chaperone co-expression, and rational mutagenesis for
 production and NMR assignments of Human eIF2a
;
   _Citation_status              published
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              .
   _PubMed_ID                    ?

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Ito    Takuhiro . . 
      2 Wagner Gerhard  . . 

   stop_

   _Journal_abbreviation        'J. Biomol. NMR'
   _Journal_volume               28
   _Journal_issue                4
   _Journal_CSD                  .
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_ISBN                    .
   _Conference_state_province    .
   _Conference_abstract_number   .
   _Page_first                   357
   _Page_last                    367
   _Year                         2004
   _Details                      .

save_


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

save_system_translation
   _Saveframe_category         molecular_system

   _Mol_system_name            translation
   _Abbreviation_common        translation
   _Enzyme_commission_number   .

   loop_
      _Mol_system_component_name
      _Mol_label

      'heIF2alpha monomer' $heIF2alpha_monomer 

   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_heIF2alpha_monomer
   _Saveframe_category                          monomeric_polymer

   _Mol_type                                    polymer
   _Mol_polymer_class                           protein
   _Name_common                                 eIF2alpha
   _Abbreviation_common                         eIF2a
   _Molecular_mass                              .
   _Mol_thiol_state                            'all free'
   _Details                                    
;
The expressed protein consists of a start Met and the residues from Ser4 to
Asp302 of heIF2alpha, followed by "LEHHHHHH".  
Three mutations are incorporated; A27Q, L46H, and V71K.  
;

   	##############################
   	#  Polymer residue sequence  #
   	##############################
   
      _Residue_count                               308
   _Mol_residue_sequence                       
;
MSCRFYQHKFPEVEDVVMVN
VRSIQEMGAYVSLLEYNNIE
GMIHLSELSRRRIRSINKLI
RIGRNECVKVIRVDKEKGYI
DLSKRRVSPEEAIKCEDKFT
KSKTVYSILRHVAEVLEYTK
DEQLESLFQRTAWVFDDKYK
RPGYGAYDAFKHAVSDPSIL
DSLDLNEDEREVLINNINRR
LTPQAVKIRADIEVACYGYE
GIDAVKEALRAGLNCSTENM
PIKINLIAPPRYVMTTTTLE
RTEGLSVLSQAMAVIKEKIE
EKRGVFNVQMEPKVVTDTDE
TELARQMERLERENAEVDGD
LEHHHHHH
;

   loop_
      _Residue_seq_code
      _Residue_author_seq_code
      _Residue_label

        1   3 MET    2   4 SER    3   5 CYS    4   6 ARG    5   7 PHE 
        6   8 TYR    7   9 GLN    8  10 HIS    9  11 LYS   10  12 PHE 
       11  13 PRO   12  14 GLU   13  15 VAL   14  16 GLU   15  17 ASP 
       16  18 VAL   17  19 VAL   18  20 MET   19  21 VAL   20  22 ASN 
       21  23 VAL   22  24 ARG   23  25 SER   24  26 ILE   25  27 GLN 
       26  28 GLU   27  29 MET   28  30 GLY   29  31 ALA   30  32 TYR 
       31  33 VAL   32  34 SER   33  35 LEU   34  36 LEU   35  37 GLU 
       36  38 TYR   37  39 ASN   38  40 ASN   39  41 ILE   40  42 GLU 
       41  43 GLY   42  44 MET   43  45 ILE   44  46 HIS   45  47 LEU 
       46  48 SER   47  49 GLU   48  50 LEU   49  51 SER   50  52 ARG 
       51  53 ARG   52  54 ARG   53  55 ILE   54  56 ARG   55  57 SER 
       56  58 ILE   57  59 ASN   58  60 LYS   59  61 LEU   60  62 ILE 
       61  63 ARG   62  64 ILE   63  65 GLY   64  66 ARG   65  67 ASN 
       66  68 GLU   67  69 CYS   68  70 VAL   69  71 LYS   70  72 VAL 
       71  73 ILE   72  74 ARG   73  75 VAL   74  76 ASP   75  77 LYS 
       76  78 GLU   77  79 LYS   78  80 GLY   79  81 TYR   80  82 ILE 
       81  83 ASP   82  84 LEU   83  85 SER   84  86 LYS   85  87 ARG 
       86  88 ARG   87  89 VAL   88  90 SER   89  91 PRO   90  92 GLU 
       91  93 GLU   92  94 ALA   93  95 ILE   94  96 LYS   95  97 CYS 
       96  98 GLU   97  99 ASP   98 100 LYS   99 101 PHE  100 102 THR 
      101 103 LYS  102 104 SER  103 105 LYS  104 106 THR  105 107 VAL 
      106 108 TYR  107 109 SER  108 110 ILE  109 111 LEU  110 112 ARG 
      111 113 HIS  112 114 VAL  113 115 ALA  114 116 GLU  115 117 VAL 
      116 118 LEU  117 119 GLU  118 120 TYR  119 121 THR  120 122 LYS 
      121 123 ASP  122 124 GLU  123 125 GLN  124 126 LEU  125 127 GLU 
      126 128 SER  127 129 LEU  128 130 PHE  129 131 GLN  130 132 ARG 
      131 133 THR  132 134 ALA  133 135 TRP  134 136 VAL  135 137 PHE 
      136 138 ASP  137 139 ASP  138 140 LYS  139 141 TYR  140 142 LYS 
      141 143 ARG  142 144 PRO  143 145 GLY  144 146 TYR  145 147 GLY 
      146 148 ALA  147 149 TYR  148 150 ASP  149 151 ALA  150 152 PHE 
      151 153 LYS  152 154 HIS  153 155 ALA  154 156 VAL  155 157 SER 
      156 158 ASP  157 159 PRO  158 160 SER  159 161 ILE  160 162 LEU 
      161 163 ASP  162 164 SER  163 165 LEU  164 166 ASP  165 167 LEU 
      166 168 ASN  167 169 GLU  168 170 ASP  169 171 GLU  170 172 ARG 
      171 173 GLU  172 174 VAL  173 175 LEU  174 176 ILE  175 177 ASN 
      176 178 ASN  177 179 ILE  178 180 ASN  179 181 ARG  180 182 ARG 
      181 183 LEU  182 184 THR  183 185 PRO  184 186 GLN  185 187 ALA 
      186 188 VAL  187 189 LYS  188 190 ILE  189 191 ARG  190 192 ALA 
      191 193 ASP  192 194 ILE  193 195 GLU  194 196 VAL  195 197 ALA 
      196 198 CYS  197 199 TYR  198 200 GLY  199 201 TYR  200 202 GLU 
      201 203 GLY  202 204 ILE  203 205 ASP  204 206 ALA  205 207 VAL 
      206 208 LYS  207 209 GLU  208 210 ALA  209 211 LEU  210 212 ARG 
      211 213 ALA  212 214 GLY  213 215 LEU  214 216 ASN  215 217 CYS 
      216 218 SER  217 219 THR  218 220 GLU  219 221 ASN  220 222 MET 
      221 223 PRO  222 224 ILE  223 225 LYS  224 226 ILE  225 227 ASN 
      226 228 LEU  227 229 ILE  228 230 ALA  229 231 PRO  230 232 PRO 
      231 233 ARG  232 234 TYR  233 235 VAL  234 236 MET  235 237 THR 
      236 238 THR  237 239 THR  238 240 THR  239 241 LEU  240 242 GLU 
      241 243 ARG  242 244 THR  243 245 GLU  244 246 GLY  245 247 LEU 
      246 248 SER  247 249 VAL  248 250 LEU  249 251 SER  250 252 GLN 
      251 253 ALA  252 254 MET  253 255 ALA  254 256 VAL  255 257 ILE 
      256 258 LYS  257 259 GLU  258 260 LYS  259 261 ILE  260 262 GLU 
      261 263 GLU  262 264 LYS  263 265 ARG  264 266 GLY  265 267 VAL 
      266 268 PHE  267 269 ASN  268 270 VAL  269 271 GLN  270 272 MET 
      271 273 GLU  272 274 PRO  273 275 LYS  274 276 VAL  275 277 VAL 
      276 278 THR  277 279 ASP  278 280 THR  279 281 ASP  280 282 GLU 
      281 283 THR  282 284 GLU  283 285 LEU  284 286 ALA  285 287 ARG 
      286 288 GLN  287 289 MET  288 290 GLU  289 291 ARG  290 292 LEU 
      291 293 GLU  292 294 ARG  293 295 GLU  294 296 ASN  295 297 ALA 
      296 298 GLU  297 299 VAL  298 300 ASP  299 301 GLY  300 302 ASP 
      301 303 LEU  302 304 GLU  303 305 HIS  304 306 HIS  305 307 HIS 
      306 308 HIS  307 309 HIS  308 310 HIS 

   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

      BMRB        10023  se-heIF2alpha                                                                                                                    100.00 308 100.00 100.00 0.00e+00 
      PDB  1Q8K          "Solution Structure Of Alpha Subunit Of Human Eif2"                                                                               100.00 308 100.00 100.00 0.00e+00 
      DBJ  BAB27049      "unnamed protein product [Mus musculus]"                                                                                           97.40 315  97.67  98.67 0.00e+00 
      DBJ  BAE25400      "unnamed protein product [Mus musculus]"                                                                                           97.40 315  97.67  98.67 0.00e+00 
      DBJ  BAE39796      "unnamed protein product [Mus musculus]"                                                                                           97.40 315  97.67  98.67 0.00e+00 
      DBJ  BAE89774      "unnamed protein product [Macaca fascicularis]"                                                                                    97.40 315  98.67  99.00 0.00e+00 
      DBJ  BAG35351      "unnamed protein product [Homo sapiens]"                                                                                           97.40 315  98.67  99.00 0.00e+00 
      EMBL CAA37728      "initiation factor 2 alpha [Bos taurus]"                                                                                           97.40 315  97.67  98.67 0.00e+00 
      EMBL CAD61953      "unnamed protein product [Homo sapiens]"                                                                                           97.40 315  98.67  99.00 0.00e+00 
      EMBL CAH93423      "hypothetical protein [Pongo abelii]"                                                                                              97.40 315  98.33  98.67 0.00e+00 
      GB   AAA41110      "translational initiation factor eIF-2, alpha subunit [Rattus norvegicus]"                                                         97.40 315  97.67  98.67 0.00e+00 
      GB   AAA52373      "translational initiation factor eIF-2, alpha subunit [Homo sapiens]"                                                              97.40 315  98.67  99.00 0.00e+00 
      GB   AAH02513      "EIF2S1 protein [Homo sapiens]"                                                                                                    97.40 315  98.67  99.00 0.00e+00 
      GB   AAH05463      "Eukaryotic translation initiation factor 2, subunit 1 alpha [Mus musculus]"                                                       97.40 315  97.67  98.67 0.00e+00 
      GB   AAH16448      "Eukaryotic translation initiation factor 2, subunit 1 alpha [Mus musculus]"                                                       97.40 315  97.67  98.67 0.00e+00 
      REF  NP_001127006  "eukaryotic translation initiation factor 2 subunit 1 [Pongo abelii]"                                                              97.40 315  98.33  98.67 0.00e+00 
      REF  NP_001244395  "eukaryotic translation initiation factor 2 subunit 1 [Macaca mulatta]"                                                            97.40 315  98.67  99.00 0.00e+00 
      REF  NP_001270066  "uncharacterized protein LOC101925386 [Macaca fascicularis]"                                                                       97.40 315  98.67  99.00 0.00e+00 
      REF  NP_004085     "eukaryotic translation initiation factor 2 subunit 1 [Homo sapiens]"                                                              97.40 315  98.67  99.00 0.00e+00 
      REF  NP_062229     "eukaryotic translation initiation factor 2 subunit 1 [Rattus norvegicus]"                                                         97.40 315  97.67  98.67 0.00e+00 
      SP   P05198        "RecName: Full=Eukaryotic translation initiation factor 2 subunit 1; AltName: Full=Eukaryotic translation initiation factor 2 su"  97.40 315  98.67  99.00 0.00e+00 
      SP   P68101        "RecName: Full=Eukaryotic translation initiation factor 2 subunit 1; AltName: Full=Eukaryotic translation initiation factor 2 su"  97.40 315  97.67  98.67 0.00e+00 
      SP   P68102        "RecName: Full=Eukaryotic translation initiation factor 2 subunit 1; AltName: Full=Eukaryotic translation initiation factor 2 su"  97.40 315  97.67  98.67 0.00e+00 
      SP   Q5R493        "RecName: Full=Eukaryotic translation initiation factor 2 subunit 1; AltName: Full=Eukaryotic translation initiation factor 2 su"  97.40 315  98.33  98.67 0.00e+00 
      SP   Q6ZWX6        "RecName: Full=Eukaryotic translation initiation factor 2 subunit 1; AltName: Full=Eukaryotic translation initiation factor 2 su"  97.40 315  97.67  98.67 0.00e+00 
      TPG  DAA25059      "TPA: eukaryotic translation initiation factor 2 subunit 1 [Bos taurus]"                                                           97.40 315  97.67  98.67 0.00e+00 

   stop_

save_


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

save_natural_source
   _Saveframe_category   natural_source


   loop_
      _Mol_label
      _Organism_name_common
      _NCBI_taxonomy_ID
      _Superkingdom
      _Kingdom
      _Genus
      _Species

      $heIF2alpha_monomer Human 9606 Eukaryota Metazoa Homo sapiens 

   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

      $heIF2alpha_monomer 'recombinant technology' . . . . . 

   stop_

save_


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

save_sample_1
   _Saveframe_category   sample

   _Sample_type          solution
   _Details              .

   loop_
      _Mol_label
      _Concentration_value
      _Concentration_value_units
      _Concentration_min_value
      _Concentration_max_value
      _Isotopic_labeling

      $heIF2alpha_monomer . mM 0.5 0.7 '[U-2H; U-13C; U-15N]' 

   stop_

save_


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

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

save_NMR_spectrometer_1
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Varian
   _Model                Inova
   _Field_strength       750
   _Details              .

save_


save_NMR_spectrometer_2
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                Avance
   _Field_strength       600
   _Details              .

save_


save_NMR_spectrometer_3
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                Avance
   _Field_strength       500
   _Details              .

save_


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

save_condition_1
   _Saveframe_category   sample_conditions

   _Details              .

   loop_
      _Variable_type
      _Variable_value
      _Variable_value_error
      _Variable_value_units

      pH            7.0 0.2 n/a 
      temperature 298   1   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

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

   stop_

save_


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

###################################################################
#       Chemical Shift Ambiguity Index Value Definitions          #
#                                                                 #
# The values other than 1 are used for those atoms with different #
# chemical shifts that cannot be assigned to stereospecific atoms #
# or to specific residues or chains.                              #
#                                                                 #
#   Index Value            Definition                             #
#                                                                 #
#      1             Unique (including isolated methyl protons,   #
#                         geminal atoms, and geminal methyl       #
#                         groups with identical chemical shifts)  #
#                         (e.g. ILE HD11, HD12, HD13 protons)     #
#      2             Ambiguity of geminal atoms or geminal methyl #
#                         proton groups (e.g. ASP HB2 and HB3     #
#                         protons, LEU CD1 and CD2 carbons, or    #
#                         LEU HD11, HD12, HD13 and HD21, HD22,    #
#                         HD23 methyl protons)                    #
#      3             Aromatic atoms on opposite sides of          #
#                         symmetrical rings (e.g. TYR HE1 and HE2 #
#                         protons)                                #
#      4             Intraresidue ambiguities (e.g. LYS HG and    #
#                         HD protons or TRP HZ2 and HZ3 protons)  #
#      5             Interresidue ambiguities (LYS 12 vs. LYS 27) #
#      6             Intermolecular ambiguities (e.g. ASP 31 CA   #
#                         in monomer 1 and ASP 31 CA in monomer 2 #
#                         of an asymmetrical homodimer, duplex    #
#                         DNA assignments, or other assignments   #
#                         that may apply to atoms in one or more  #
#                         molecule in the molecular assembly)     #
#      9             Ambiguous, specific ambiguity not defined    #
#                                                                 #
###################################################################
save_shift_set_1
   _Saveframe_category               assigned_chemical_shifts

   _Details                          .

   loop_
      _Sample_label

      $sample_1 

   stop_

   _Sample_conditions_label         $condition_1
   _Chem_shift_reference_set_label  $chemical_shift_reference
   _Mol_system_component_name       'heIF2alpha monomer'
   _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 .   3 CYS CA C  58.057 0.3  1 
         2 .   3 CYS C  C 171.626 0.2  1 
         3 .   4 ARG H  H   7.935 0.02 1 
         4 .   4 ARG N  N 123.470 0.1  1 
         5 .   4 ARG CA C  54.785 0.3  1 
         6 .   4 ARG C  C 172.400 0.2  1 
         7 .   5 PHE H  H   7.325 0.02 1 
         8 .   5 PHE N  N 113.664 0.1  1 
         9 .   5 PHE CA C  55.966 0.3  1 
        10 .   5 PHE C  C 177.824 0.2  1 
        11 .   6 TYR H  H   8.341 0.02 1 
        12 .   6 TYR N  N 119.318 0.1  1 
        13 .   6 TYR CA C  52.920 0.3  1 
        14 .   6 TYR C  C 172.662 0.2  1 
        15 .   7 GLN H  H   8.323 0.02 1 
        16 .   7 GLN N  N 117.217 0.1  1 
        17 .   7 GLN CA C  58.082 0.3  1 
        18 .   7 GLN C  C 178.579 0.2  1 
        19 .   8 HIS H  H   7.583 0.02 1 
        20 .   8 HIS N  N 115.075 0.1  1 
        21 .   8 HIS CA C  54.784 0.3  1 
        22 .   8 HIS C  C 174.420 0.2  1 
        23 .   9 LYS H  H   8.377 0.02 1 
        24 .   9 LYS N  N 118.730 0.1  1 
        25 .   9 LYS CA C  58.310 0.3  1 
        26 .   9 LYS C  C 175.444 0.2  1 
        27 .  10 PHE H  H   7.700 0.02 1 
        28 .  10 PHE N  N 113.402 0.1  1 
        29 .  10 PHE CA C  54.082 0.3  1 
        30 .  11 PRO CA C  61.116 0.3  1 
        31 .  11 PRO C  C 174.180 0.2  1 
        32 .  12 GLU H  H   8.077 0.02 1 
        33 .  12 GLU N  N 117.030 0.1  1 
        34 .  12 GLU CA C  53.860 0.3  1 
        35 .  12 GLU C  C 176.914 0.2  1 
        36 .  13 VAL H  H   8.491 0.02 1 
        37 .  13 VAL N  N 121.312 0.1  1 
        38 .  13 VAL CA C  65.336 0.3  1 
        39 .  13 VAL C  C 177.287 0.2  1 
        40 .  14 GLU H  H   8.837 0.02 1 
        41 .  14 GLU N  N 119.504 0.1  1 
        42 .  14 GLU CA C  59.710 0.3  1 
        43 .  14 GLU C  C 175.988 0.2  1 
        44 .  15 ASP H  H   8.169 0.02 1 
        45 .  15 ASP N  N 120.705 0.1  1 
        46 .  15 ASP CA C  54.795 0.3  1 
        47 .  15 ASP C  C 175.327 0.2  1 
        48 .  16 VAL H  H   8.498 0.02 1 
        49 .  16 VAL N  N 121.705 0.1  1 
        50 .  16 VAL CA C  61.349 0.3  1 
        51 .  16 VAL C  C 175.806 0.2  1 
        52 .  17 VAL H  H   9.447 0.02 1 
        53 .  17 VAL N  N 120.582 0.1  1 
        54 .  17 VAL CA C  58.073 0.3  1 
        55 .  17 VAL C  C 173.806 0.2  1 
        56 .  18 MET H  H   7.991 0.02 1 
        57 .  18 MET N  N 120.000 0.1  1 
        58 .  18 MET CA C  52.920 0.3  1 
        59 .  18 MET C  C 177.082 0.2  1 
        60 .  19 VAL H  H   9.376 0.02 1 
        61 .  19 VAL N  N 122.368 0.1  1 
        62 .  19 VAL CA C  57.360 0.3  1 
        63 .  19 VAL C  C 173.081 0.2  1 
        64 .  20 ASN H  H   8.528 0.02 1 
        65 .  20 ASN N  N 118.274 0.1  1 
        66 .  20 ASN CA C  52.210 0.3  1 
        67 .  20 ASN C  C 175.301 0.2  1 
        68 .  21 VAL H  H   8.105 0.02 1 
        69 .  21 VAL N  N 126.660 0.1  1 
        70 .  21 VAL CA C  64.156 0.3  1 
        71 .  21 VAL C  C 174.690 0.2  1 
        72 .  22 ARG H  H   9.037 0.02 1 
        73 .  22 ARG N  N 129.100 0.1  1 
        74 .  22 ARG CA C  56.646 0.3  1 
        75 .  22 ARG C  C 176.527 0.2  1 
        76 .  23 SER H  H   8.113 0.02 1 
        77 .  23 SER N  N 111.092 0.1  1 
        78 .  23 SER CA C  57.604 0.3  1 
        79 .  23 SER C  C 172.183 0.2  1 
        80 .  24 ILE H  H   8.663 0.02 1 
        81 .  24 ILE N  N 122.774 0.1  1 
        82 .  24 ILE CA C  61.344 0.3  1 
        83 .  24 ILE C  C 174.734 0.2  1 
        84 .  25 GLN H  H   8.704 0.02 1 
        85 .  25 GLN N  N 126.100 0.1  1 
        86 .  25 GLN CA C  53.609 0.3  1 
        87 .  25 GLN C  C 175.645 0.2  1 
        88 .  26 GLU H  H   8.774 0.02 1 
        89 .  26 GLU N  N 119.821 0.1  1 
        90 .  26 GLU CA C  59.714 0.3  1 
        91 .  26 GLU C  C 177.636 0.2  1 
        92 .  27 MET H  H   8.115 0.02 1 
        93 .  27 MET N  N 111.022 0.1  1 
        94 .  27 MET CA C  54.547 0.3  1 
        95 .  27 MET C  C 176.228 0.2  1 
        96 .  28 GLY H  H   7.385 0.02 1 
        97 .  28 GLY N  N 107.010 0.1  1 
        98 .  28 GLY CA C  45.182 0.3  1 
        99 .  28 GLY C  C 169.928 0.2  1 
       100 .  29 ALA H  H   8.603 0.02 1 
       101 .  29 ALA N  N 120.407 0.1  1 
       102 .  29 ALA CA C  49.415 0.3  1 
       103 .  29 ALA C  C 175.682 0.2  1 
       104 .  30 TYR H  H   8.825 0.02 1 
       105 .  30 TYR N  N 122.910 0.1  1 
       106 .  30 TYR CA C  57.602 0.3  1 
       107 .  30 TYR C  C 176.657 0.2  1 
       108 .  31 VAL H  H   8.813 0.02 1 
       109 .  31 VAL N  N 114.905 0.1  1 
       110 .  31 VAL CA C  57.596 0.3  1 
       111 .  31 VAL C  C 173.613 0.2  1 
       112 .  32 SER H  H   8.827 0.02 1 
       113 .  32 SER N  N 115.448 0.1  1 
       114 .  32 SER CA C  55.979 0.3  1 
       115 .  32 SER C  C 174.638 0.2  1 
       116 .  33 LEU H  H   9.300 0.02 1 
       117 .  33 LEU N  N 126.160 0.1  1 
       118 .  33 LEU CA C  57.144 0.3  1 
       119 .  33 LEU C  C 177.144 0.2  1 
       120 .  34 LEU H  H   7.506 0.02 1 
       121 .  34 LEU N  N 127.450 0.1  1 
       122 .  34 LEU CA C  56.661 0.3  1 
       123 .  35 GLU CA C  54.870 0.3  1 
       124 .  35 GLU C  C 175.289 0.2  1 
       125 .  36 TYR H  H   7.000 0.02 1 
       126 .  36 TYR N  N 116.200 0.1  1 
       127 .  36 TYR CA C  56.435 0.3  1 
       128 .  36 TYR C  C 176.242 0.2  1 
       129 .  37 ASN H  H   9.331 0.02 1 
       130 .  37 ASN N  N 120.802 0.1  1 
       131 .  37 ASN CA C  52.674 0.3  1 
       132 .  37 ASN C  C 174.294 0.2  1 
       133 .  38 ASN H  H   7.632 0.02 1 
       134 .  38 ASN N  N 107.620 0.1  1 
       135 .  38 ASN CA C  54.784 0.3  1 
       136 .  38 ASN C  C 174.914 0.2  1 
       137 .  39 ILE H  H   6.633 0.02 1 
       138 .  39 ILE N  N 111.705 0.1  1 
       139 .  39 ILE CA C  62.524 0.3  1 
       140 .  39 ILE C  C 174.845 0.2  1 
       141 .  40 GLU H  H   8.327 0.02 1 
       142 .  40 GLU N  N 121.837 0.1  1 
       143 .  40 GLU CA C  56.663 0.3  1 
       144 .  40 GLU C  C 176.783 0.2  1 
       145 .  41 GLY H  H   8.354 0.02 1 
       146 .  41 GLY N  N 108.152 0.1  1 
       147 .  41 GLY CA C  44.247 0.3  1 
       148 .  41 GLY C  C 171.506 0.2  1 
       149 .  42 MET H  H   8.400 0.02 1 
       150 .  42 MET N  N 119.990 0.1  1 
       151 .  42 MET CA C  54.087 0.3  1 
       152 .  42 MET C  C 174.259 0.2  1 
       153 .  43 ILE H  H   8.874 0.02 1 
       154 .  43 ILE N  N 123.406 0.1  1 
       155 .  43 ILE CA C  59.013 0.3  1 
       156 .  43 ILE C  C 175.151 0.2  1 
       157 .  44 HIS H  H   9.360 0.02 1 
       158 .  44 HIS N  N 127.897 0.1  1 
       159 .  44 HIS CA C  58.309 0.3  1 
       160 .  44 HIS C  C 176.963 0.2  1 
       161 .  45 LEU H  H   7.820 0.02 1 
       162 .  45 LEU N  N 125.600 0.1  1 
       163 .  45 LEU CA C  58.310 0.3  1 
       164 .  45 LEU C  C 178.971 0.2  1 
       165 .  46 SER H  H   9.540 0.02 1 
       166 .  46 SER N  N 114.988 0.1  1 
       167 .  46 SER CA C  60.411 0.3  1 
       168 .  46 SER C  C 175.479 0.2  1 
       169 .  47 GLU H  H   8.201 0.02 1 
       170 .  47 GLU N  N 118.056 0.1  1 
       171 .  47 GLU CA C  54.790 0.3  1 
       172 .  47 GLU C  C 177.280 0.2  1 
       173 .  48 LEU H  H   7.947 0.02 1 
       174 .  48 LEU N  N 123.452 0.1  1 
       175 .  48 LEU CA C  56.441 0.3  1 
       176 .  48 LEU C  C 175.621 0.2  1 
       177 .  49 SER H  H   7.813 0.02 1 
       178 .  49 SER N  N 110.397 0.1  1 
       179 .  49 SER CA C  56.659 0.3  1 
       180 .  50 ARG H  H   8.440 0.02 1 
       181 .  50 ARG N  N 124.274 0.1  1 
       182 .  50 ARG CA C  57.307 0.3  1 
       183 .  50 ARG C  C 176.962 0.2  1 
       184 .  51 ARG H  H   8.360 0.02 1 
       185 .  51 ARG N  N 119.250 0.1  1 
       186 .  51 ARG CA C  55.231 0.3  1 
       187 .  51 ARG C  C 176.019 0.2  1 
       188 .  52 ARG H  H   8.336 0.02 1 
       189 .  52 ARG N  N 120.350 0.1  1 
       190 .  52 ARG CA C  56.196 0.3  1 
       191 .  52 ARG C  C 176.240 0.2  1 
       192 .  53 ILE H  H   8.098 0.02 1 
       193 .  53 ILE N  N 122.546 0.1  1 
       194 .  53 ILE CA C  60.643 0.3  1 
       195 .  55 SER C  C 175.665 0.2  1 
       196 .  56 ILE H  H   8.704 0.02 1 
       197 .  56 ILE N  N 126.410 0.1  1 
       198 .  56 ILE CA C  64.166 0.3  1 
       199 .  56 ILE C  C 176.291 0.2  1 
       200 .  57 ASN H  H   8.160 0.02 1 
       201 .  57 ASN N  N 117.037 0.1  1 
       202 .  57 ASN CA C  55.050 0.3  1 
       203 .  57 ASN C  C 175.856 0.2  1 
       204 .  58 LYS H  H   7.676 0.02 1 
       205 .  58 LYS N  N 116.659 0.1  1 
       206 .  58 LYS CA C  56.212 0.3  1 
       207 .  58 LYS C  C 177.110 0.2  1 
       208 .  59 LEU H  H   7.760 0.02 1 
       209 .  59 LEU N  N 119.138 0.1  1 
       210 .  59 LEU CA C  55.491 0.3  1 
       211 .  59 LEU C  C 176.239 0.2  1 
       212 .  60 ILE H  H   7.664 0.02 1 
       213 .  60 ILE N  N 116.028 0.1  1 
       214 .  60 ILE CA C  59.013 0.3  1 
       215 .  60 ILE C  C 172.602 0.2  1 
       216 .  61 ARG H  H   8.581 0.02 1 
       217 .  61 ARG N  N 122.000 0.1  1 
       218 .  61 ARG CA C  54.084 0.3  1 
       219 .  61 ARG C  C 175.422 0.2  1 
       220 .  62 ILE H  H   8.485 0.02 1 
       221 .  62 ILE N  N 122.985 0.1  1 
       222 .  62 ILE CA C  62.524 0.3  1 
       223 .  62 ILE C  C 177.607 0.2  1 
       224 .  63 GLY H  H   9.132 0.02 1 
       225 .  63 GLY N  N 114.800 0.1  1 
       226 .  63 GLY CA C  45.184 0.3  1 
       227 .  63 GLY C  C 174.116 0.2  1 
       228 .  64 ARG H  H   7.566 0.02 1 
       229 .  64 ARG N  N 121.400 0.1  1 
       230 .  64 ARG CA C  54.321 0.3  1 
       231 .  64 ARG C  C 175.264 0.2  1 
       232 .  65 ASN H  H   8.519 0.02 1 
       233 .  65 ASN N  N 122.672 0.1  1 
       234 .  65 ASN CA C  51.497 0.3  1 
       235 .  65 ASN C  C 175.869 0.2  1 
       236 .  66 GLU H  H   8.860 0.02 1 
       237 .  66 GLU N  N 118.028 0.1  1 
       238 .  66 GLU CA C  53.634 0.3  1 
       239 .  66 GLU C  C 174.531 0.2  1 
       240 .  67 CYS H  H   8.839 0.02 1 
       241 .  67 CYS N  N 121.530 0.1  1 
       242 .  67 CYS CA C  57.139 0.3  1 
       243 .  67 CYS C  C 174.759 0.2  1 
       244 .  68 VAL H  H   8.906 0.02 1 
       245 .  68 VAL N  N 114.811 0.1  1 
       246 .  68 VAL CA C  58.545 0.3  1 
       247 .  68 VAL C  C 172.378 0.2  1 
       248 .  69 LYS H  H   9.004 0.02 1 
       249 .  69 LYS N  N 122.144 0.1  1 
       250 .  69 LYS CA C  54.087 0.3  1 
       251 .  69 LYS C  C 176.215 0.2  1 
       252 .  70 VAL H  H   9.182 0.02 1 
       253 .  70 VAL N  N 127.400 0.1  1 
       254 .  70 VAL CA C  62.761 0.3  1 
       255 .  70 VAL C  C 176.330 0.2  1 
       256 .  71 ILE H  H   8.860 0.02 1 
       257 .  71 ILE N  N 123.838 0.1  1 
       258 .  71 ILE CA C  61.077 0.3  1 
       259 .  71 ILE C  C 175.849 0.2  1 
       260 .  72 ARG H  H   7.555 0.02 1 
       261 .  72 ARG N  N 121.199 0.1  1 
       262 .  72 ARG CA C  56.896 0.3  1 
       263 .  72 ARG C  C 173.306 0.2  1 
       264 .  73 VAL H  H   8.675 0.02 1 
       265 .  73 VAL N  N 124.440 0.1  1 
       266 .  73 VAL CA C  60.888 0.3  1 
       267 .  73 VAL C  C 173.942 0.2  1 
       268 .  74 ASP H  H   8.767 0.02 1 
       269 .  74 ASP N  N 127.244 0.1  1 
       270 .  74 ASP CA C  52.205 0.3  1 
       271 .  74 ASP C  C 176.787 0.2  1 
       272 .  75 LYS H  H   8.702 0.02 1 
       273 .  75 LYS N  N 124.400 0.1  1 
       274 .  75 LYS CA C  58.305 0.3  1 
       275 .  75 LYS C  C 177.638 0.2  1 
       276 .  76 GLU H  H   8.127 0.02 1 
       277 .  76 GLU N  N 119.250 0.1  1 
       278 .  76 GLU CA C  58.305 0.3  1 
       279 .  76 GLU C  C 178.251 0.2  1 
       280 .  77 LYS H  H   7.721 0.02 1 
       281 .  77 LYS N  N 116.300 0.1  1 
       282 .  77 LYS CA C  55.727 0.3  1 
       283 .  77 LYS C  C 177.201 0.2  1 
       284 .  78 GLY H  H   7.743 0.02 1 
       285 .  78 GLY N  N 108.120 0.1  1 
       286 .  78 GLY CA C  46.118 0.3  1 
       287 .  78 GLY C  C 173.703 0.2  1 
       288 .  79 TYR H  H   7.305 0.02 1 
       289 .  79 TYR N  N 118.200 0.1  1 
       290 .  79 TYR CA C  55.498 0.3  1 
       291 .  79 TYR C  C 174.568 0.2  1 
       292 .  80 ILE H  H   8.410 0.02 1 
       293 .  80 ILE N  N 124.531 0.1  1 
       294 .  80 ILE CA C  60.185 0.3  1 
       295 .  80 ILE C  C 173.962 0.2  1 
       296 .  81 ASP H  H   8.691 0.02 1 
       297 .  81 ASP N  N 127.400 0.1  1 
       298 .  81 ASP CA C  53.612 0.3  1 
       299 .  81 ASP C  C 176.790 0.2  1 
       300 .  82 LEU H  H   8.670 0.02 1 
       301 .  82 LEU N  N 122.900 0.1  1 
       302 .  82 LEU CA C  53.373 0.3  1 
       303 .  82 LEU C  C 176.449 0.2  1 
       304 .  83 SER H  H   9.295 0.02 1 
       305 .  83 SER N  N 111.280 0.1  1 
       306 .  83 SER CA C  56.660 0.3  1 
       307 .  83 SER C  C 175.525 0.2  1 
       308 .  84 LYS H  H   7.986 0.02 1 
       309 .  84 LYS N  N 129.159 0.1  1 
       310 .  84 LYS CA C  57.834 0.3  1 
       311 .  84 LYS C  C 177.021 0.2  1 
       312 .  85 ARG H  H   8.031 0.02 1 
       313 .  85 ARG N  N 117.820 0.1  1 
       314 .  85 ARG CA C  57.816 0.3  1 
       315 .  85 ARG C  C 176.525 0.2  1 
       316 .  86 ARG H  H   7.134 0.02 1 
       317 .  86 ARG N  N 116.276 0.1  1 
       318 .  86 ARG CA C  55.955 0.3  1 
       319 .  86 ARG C  C 174.164 0.2  1 
       320 .  87 VAL H  H   7.087 0.02 1 
       321 .  87 VAL N  N 119.761 0.1  1 
       322 .  87 VAL CA C  61.821 0.3  1 
       323 .  87 VAL C  C 175.929 0.2  1 
       324 .  88 SER H  H   9.670 0.02 1 
       325 .  88 SER N  N 128.246 0.1  1 
       326 .  88 SER CA C  56.196 0.3  1 
       327 .  89 PRO CA C  65.572 0.3  1 
       328 .  89 PRO C  C 179.491 0.2  1 
       329 .  90 GLU H  H   8.685 0.02 1 
       330 .  90 GLU N  N 116.500 0.1  1 
       331 .  90 GLU CA C  59.708 0.3  1 
       332 .  90 GLU C  C 179.584 0.2  1 
       333 .  91 GLU H  H   7.889 0.02 1 
       334 .  91 GLU N  N 119.967 0.1  1 
       335 .  91 GLU CA C  58.535 0.3  1 
       336 .  91 GLU C  C 180.074 0.2  1 
       337 .  92 ALA H  H   8.276 0.02 1 
       338 .  92 ALA N  N 123.612 0.1  1 
       339 .  92 ALA CA C  55.259 0.3  1 
       340 .  92 ALA C  C 179.606 0.2  1 
       341 .  93 ILE H  H   7.866 0.02 1 
       342 .  93 ILE N  N 119.000 0.1  1 
       343 .  93 ILE CA C  64.644 0.3  1 
       344 .  93 ILE C  C 179.213 0.2  1 
       345 .  94 LYS H  H   7.660 0.02 1 
       346 .  94 LYS N  N 120.777 0.1  1 
       347 .  94 LYS CA C  59.221 0.3  1 
       348 .  94 LYS C  C 178.189 0.2  1 
       349 .  95 CYS H  H   8.128 0.02 1 
       350 .  95 CYS N  N 120.380 0.1  1 
       351 .  95 CYS CA C  61.554 0.3  1 
       352 .  95 CYS C  C 177.968 0.2  1 
       353 .  96 GLU H  H   8.357 0.02 1 
       354 .  96 GLU N  N 119.307 0.1  1 
       355 .  96 GLU CA C  59.936 0.3  1 
       356 .  96 GLU C  C 178.916 0.2  1 
       357 .  97 ASP H  H   7.981 0.02 1 
       358 .  97 ASP N  N 121.103 0.1  1 
       359 .  97 ASP CA C  57.825 0.3  1 
       360 .  97 ASP C  C 176.796 0.2  1 
       361 .  98 LYS H  H   8.393 0.02 1 
       362 .  98 LYS N  N 120.868 0.1  1 
       363 .  98 LYS CA C  59.723 0.3  1 
       364 .  98 LYS C  C 178.774 0.2  1 
       365 .  99 PHE H  H   9.182 0.02 1 
       366 .  99 PHE N  N 119.700 0.1  1 
       367 .  99 PHE CA C  61.385 0.3  1 
       368 .  99 PHE C  C 176.398 0.2  1 
       369 . 100 THR H  H   8.414 0.02 1 
       370 . 100 THR N  N 115.001 0.1  1 
       371 . 100 THR CA C  66.925 0.3  1 
       372 . 100 THR C  C 177.534 0.2  1 
       373 . 101 LYS H  H   7.750 0.02 1 
       374 . 101 LYS N  N 123.859 0.1  1 
       375 . 101 LYS CA C  60.179 0.3  1 
       376 . 101 LYS C  C 178.200 0.2  1 
       377 . 102 SER H  H   8.785 0.02 1 
       378 . 102 SER N  N 117.938 0.1  1 
       379 . 102 SER CA C  61.600 0.3  1 
       380 . 102 SER C  C 176.807 0.2  1 
       381 . 103 LYS H  H   8.835 0.02 1 
       382 . 103 LYS N  N 122.200 0.1  1 
       383 . 103 LYS CA C  58.087 0.3  1 
       384 . 103 LYS C  C 179.186 0.2  1 
       385 . 104 THR H  H   7.541 0.02 1 
       386 . 104 THR N  N 119.798 0.1  1 
       387 . 104 THR CA C  67.230 0.3  1 
       388 . 104 THR C  C 176.111 0.2  1 
       389 . 105 VAL H  H   7.437 0.02 1 
       390 . 105 VAL N  N 124.108 0.1  1 
       391 . 105 VAL CA C  67.453 0.3  1 
       392 . 105 VAL C  C 177.012 0.2  1 
       393 . 106 TYR H  H   8.426 0.02 1 
       394 . 106 TYR N  N 119.658 0.1  1 
       395 . 106 TYR CA C  61.586 0.3  1 
       396 . 106 TYR C  C 176.796 0.2  1 
       397 . 107 SER H  H   8.515 0.02 1 
       398 . 107 SER N  N 113.936 0.1  1 
       399 . 107 SER CA C  61.574 0.3  1 
       400 . 107 SER C  C 177.992 0.2  1 
       401 . 108 ILE H  H   7.983 0.02 1 
       402 . 108 ILE N  N 122.920 0.1  1 
       403 . 108 ILE CA C  65.572 0.3  1 
       404 . 108 ILE C  C 177.653 0.2  1 
       405 . 109 LEU H  H   8.006 0.02 1 
       406 . 109 LEU N  N 118.914 0.1  1 
       407 . 109 LEU CA C  57.367 0.3  1 
       408 . 109 LEU C  C 178.749 0.2  1 
       409 . 110 ARG H  H   9.180 0.02 1 
       410 . 110 ARG N  N 119.655 0.1  1 
       411 . 110 ARG CA C  58.551 0.3  1 
       412 . 110 ARG C  C 179.266 0.2  1 
       413 . 111 HIS H  H   7.800 0.02 1 
       414 . 111 HIS N  N 119.250 0.1  1 
       415 . 111 HIS CA C  59.560 0.3  1 
       416 . 111 HIS C  C 177.326 0.2  1 
       417 . 112 VAL H  H   8.147 0.02 1 
       418 . 112 VAL N  N 120.834 0.1  1 
       419 . 112 VAL CA C  65.571 0.3  1 
       420 . 112 VAL C  C 176.730 0.2  1 
       421 . 113 ALA H  H   8.106 0.02 1 
       422 . 113 ALA N  N 119.036 0.1  1 
       423 . 113 ALA CA C  54.554 0.3  1 
       424 . 113 ALA C  C 178.386 0.2  1 
       425 . 114 GLU H  H   7.743 0.02 1 
       426 . 114 GLU N  N 117.700 0.1  1 
       427 . 114 GLU CA C  58.769 0.3  1 
       428 . 114 GLU C  C 180.773 0.2  1 
       429 . 115 VAL H  H   8.010 0.02 1 
       430 . 115 VAL N  N 121.909 0.1  1 
       431 . 115 VAL CA C  65.568 0.3  1 
       432 . 115 VAL C  C 178.161 0.2  1 
       433 . 116 LEU H  H   7.570 0.02 1 
       434 . 116 LEU N  N 117.700 0.1  1 
       435 . 116 LEU CA C  54.325 0.3  1 
       436 . 116 LEU C  C 174.923 0.2  1 
       437 . 117 GLU H  H   7.535 0.02 1 
       438 . 117 GLU N  N 114.025 0.1  1 
       439 . 117 GLU CA C  56.902 0.3  1 
       440 . 117 GLU C  C 176.437 0.2  1 
       441 . 118 TYR H  H   8.640 0.02 1 
       442 . 118 TYR N  N 120.700 0.1  1 
       443 . 118 TYR CA C  53.154 0.3  1 
       444 . 118 TYR C  C 176.625 0.2  1 
       445 . 119 THR H  H   8.012 0.02 1 
       446 . 119 THR N  N 112.841 0.1  1 
       447 . 119 THR CA C  61.821 0.3  1 
       448 . 119 THR C  C 175.458 0.2  1 
       449 . 120 LYS H  H   8.311 0.02 1 
       450 . 120 LYS N  N 121.481 0.1  1 
       451 . 120 LYS CA C  54.784 0.3  1 
       452 . 122 GLU C  C 179.516 0.2  1 
       453 . 123 GLN H  H   7.361 0.02 1 
       454 . 123 GLN N  N 118.700 0.1  1 
       455 . 123 GLN CA C  57.601 0.3  1 
       456 . 123 GLN C  C 178.904 0.2  1 
       457 . 124 LEU H  H   7.356 0.02 1 
       458 . 124 LEU N  N 122.480 0.1  1 
       459 . 124 LEU CA C  57.596 0.3  1 
       460 . 124 LEU C  C 176.830 0.2  1 
       461 . 125 GLU H  H   8.340 0.02 1 
       462 . 125 GLU N  N 119.500 0.1  1 
       463 . 125 GLU CA C  59.706 0.3  1 
       464 . 125 GLU C  C 177.920 0.2  1 
       465 . 126 SER H  H   7.625 0.02 1 
       466 . 126 SER N  N 111.517 0.1  1 
       467 . 126 SER CA C  59.733 0.3  1 
       468 . 126 SER C  C 176.977 0.2  1 
       469 . 127 LEU H  H   7.500 0.02 1 
       470 . 127 LEU N  N 119.958 0.1  1 
       471 . 127 LEU CA C  58.060 0.3  1 
       472 . 127 LEU C  C 180.494 0.2  1 
       473 . 128 PHE H  H   8.110 0.02 1 
       474 . 128 PHE N  N 122.814 0.1  1 
       475 . 128 PHE CA C  62.762 0.3  1 
       476 . 128 PHE C  C 178.737 0.2  1 
       477 . 129 GLN H  H   8.490 0.02 1 
       478 . 129 GLN N  N 118.420 0.1  1 
       479 . 129 GLN CA C  58.535 0.3  1 
       480 . 129 GLN C  C 177.522 0.2  1 
       481 . 130 ARG H  H   7.520 0.02 1 
       482 . 130 ARG N  N 112.802 0.1  1 
       483 . 130 ARG CA C  56.430 0.3  1 
       484 . 130 ARG C  C 176.660 0.2  1 
       485 . 131 THR H  H   7.398 0.02 1 
       486 . 131 THR N  N 107.692 0.1  1 
       487 . 131 THR CA C  58.553 0.3  1 
       488 . 131 THR C  C 173.721 0.2  1 
       489 . 132 ALA H  H   9.355 0.02 1 
       490 . 132 ALA N  N 127.800 0.1  1 
       491 . 132 ALA CA C  55.018 0.3  1 
       492 . 132 ALA C  C 178.340 0.2  1 
       493 . 133 TRP H  H   8.394 0.02 1 
       494 . 133 TRP N  N 115.170 0.1  1 
       495 . 133 TRP CA C  57.602 0.3  1 
       496 . 133 TRP C  C 179.734 0.2  1 
       497 . 134 VAL H  H   7.267 0.02 1 
       498 . 134 VAL N  N 122.400 0.1  1 
       499 . 134 VAL CA C  65.598 0.3  1 
       500 . 134 VAL C  C 179.331 0.2  1 
       501 . 135 PHE H  H   7.183 0.02 1 
       502 . 135 PHE N  N 119.587 0.1  1 
       503 . 135 PHE CA C  60.647 0.3  1 
       504 . 135 PHE C  C 178.089 0.2  1 
       505 . 136 ASP H  H   8.970 0.02 1 
       506 . 136 ASP N  N 121.499 0.1  1 
       507 . 136 ASP CA C  58.046 0.3  1 
       508 . 136 ASP C  C 179.236 0.2  1 
       509 . 137 ASP H  H   7.485 0.02 1 
       510 . 137 ASP N  N 118.670 0.1  1 
       511 . 137 ASP CA C  56.893 0.3  1 
       512 . 137 ASP C  C 178.423 0.2  1 
       513 . 138 LYS H  H   8.333 0.02 1 
       514 . 138 LYS N  N 120.832 0.1  1 
       515 . 138 LYS CA C  59.015 0.3  1 
       516 . 138 LYS C  C 178.641 0.2  1 
       517 . 139 TYR H  H   8.220 0.02 1 
       518 . 139 TYR N  N 114.536 0.1  1 
       519 . 139 TYR CA C  57.596 0.3  1 
       520 . 139 TYR C  C 174.735 0.2  1 
       521 . 140 LYS H  H   7.814 0.02 1 
       522 . 140 LYS N  N 117.535 0.1  1 
       523 . 140 LYS CA C  56.426 0.3  1 
       524 . 140 LYS C  C 176.256 0.2  1 
       525 . 141 ARG H  H   7.722 0.02 1 
       526 . 141 ARG N  N 116.200 0.1  1 
       527 . 141 ARG CA C  53.153 0.3  1 
       528 . 142 PRO CA C  63.230 0.3  1 
       529 . 142 PRO C  C 178.366 0.2  1 
       530 . 143 GLY H  H   9.727 0.02 1 
       531 . 143 GLY N  N 116.686 0.1  1 
       532 . 143 GLY CA C  47.051 0.3  1 
       533 . 143 GLY C  C 175.551 0.2  1 
       534 . 144 TYR H  H   7.952 0.02 1 
       535 . 144 TYR N  N 120.179 0.1  1 
       536 . 144 TYR CA C  60.882 0.3  1 
       537 . 144 TYR C  C 177.688 0.2  1 
       538 . 145 GLY H  H   8.943 0.02 1 
       539 . 145 GLY N  N 107.700 0.1  1 
       540 . 145 GLY CA C  47.753 0.3  1 
       541 . 145 GLY C  C 175.239 0.2  1 
       542 . 146 ALA H  H   9.047 0.02 1 
       543 . 146 ALA N  N 123.780 0.1  1 
       544 . 146 ALA CA C  55.263 0.3  1 
       545 . 146 ALA C  C 177.995 0.2  1 
       546 . 147 TYR H  H   7.717 0.02 1 
       547 . 147 TYR N  N 116.499 0.1  1 
       548 . 147 TYR CA C  62.524 0.3  1 
       549 . 147 TYR C  C 176.086 0.2  1 
       550 . 148 ASP H  H   8.751 0.02 1 
       551 . 148 ASP N  N 118.410 0.1  1 
       552 . 148 ASP CA C  57.131 0.3  1 
       553 . 148 ASP C  C 179.783 0.2  1 
       554 . 149 ALA H  H   8.060 0.02 1 
       555 . 149 ALA N  N 123.351 0.1  1 
       556 . 149 ALA CA C  54.554 0.3  1 
       557 . 149 ALA C  C 179.125 0.2  1 
       558 . 150 PHE H  H   8.642 0.02 1 
       559 . 150 PHE N  N 118.679 0.1  1 
       560 . 150 PHE CA C  58.306 0.3  1 
       561 . 150 PHE C  C 177.216 0.2  1 
       562 . 151 LYS H  H   8.390 0.02 1 
       563 . 151 LYS N  N 117.500 0.1  1 
       564 . 151 LYS CA C  58.995 0.3  1 
       565 . 151 LYS C  C 180.587 0.2  1 
       566 . 152 HIS H  H   8.236 0.02 1 
       567 . 152 HIS N  N 121.400 0.1  1 
       568 . 152 HIS CA C  58.772 0.3  1 
       569 . 152 HIS C  C 177.328 0.2  1 
       570 . 153 ALA H  H   8.147 0.02 1 
       571 . 153 ALA N  N 121.726 0.1  1 
       572 . 153 ALA CA C  53.143 0.3  1 
       573 . 153 ALA C  C 177.197 0.2  1 
       574 . 154 VAL H  H   7.053 0.02 1 
       575 . 154 VAL N  N 115.877 0.1  1 
       576 . 154 VAL CA C  65.328 0.3  1 
       577 . 154 VAL C  C 177.440 0.2  1 
       578 . 155 SER H  H   7.138 0.02 1 
       579 . 155 SER N  N 111.300 0.1  1 
       580 . 155 SER CA C  58.782 0.3  1 
       581 . 155 SER C  C 174.712 0.2  1 
       582 . 156 ASP H  H   7.990 0.02 1 
       583 . 156 ASP N  N 118.700 0.1  1 
       584 . 156 ASP CA C  50.810 0.3  1 
       585 . 157 PRO CA C  64.039 0.3  1 
       586 . 157 PRO C  C 178.177 0.2  1 
       587 . 158 SER H  H   8.044 0.02 1 
       588 . 158 SER N  N 117.437 0.1  1 
       589 . 158 SER CA C  61.108 0.3  1 
       590 . 158 SER C  C 177.201 0.2  1 
       591 . 159 ILE H  H   7.350 0.02 1 
       592 . 159 ILE N  N 123.700 0.1  1 
       593 . 159 ILE CA C  63.226 0.3  1 
       594 . 159 ILE C  C 176.344 0.2  1 
       595 . 160 LEU H  H   7.780 0.02 1 
       596 . 160 LEU N  N 116.560 0.1  1 
       597 . 160 LEU CA C  54.319 0.3  1 
       598 . 160 LEU C  C 179.399 0.2  1 
       599 . 161 ASP H  H   8.061 0.02 1 
       600 . 161 ASP N  N 121.700 0.1  1 
       601 . 161 ASP CA C  57.598 0.3  1 
       602 . 162 SER CA C  58.769 0.3  1 
       603 . 162 SER C  C 174.402 0.2  1 
       604 . 163 LEU H  H   7.179 0.02 1 
       605 . 163 LEU N  N 120.213 0.1  1 
       606 . 163 LEU CA C  53.614 0.3  1 
       607 . 163 LEU C  C 177.191 0.2  1 
       608 . 164 ASP H  H   9.622 0.02 1 
       609 . 164 ASP N  N 124.600 0.1  1 
       610 . 164 ASP CA C  52.919 0.3  1 
       611 . 164 ASP C  C 174.040 0.2  1 
       612 . 165 LEU H  H   7.294 0.02 1 
       613 . 165 LEU N  N 121.910 0.1  1 
       614 . 165 LEU CA C  52.441 0.3  1 
       615 . 165 LEU C  C 177.417 0.2  1 
       616 . 166 ASN H  H   8.895 0.02 1 
       617 . 166 ASN N  N 120.768 0.1  1 
       618 . 166 ASN CA C  51.273 0.3  1 
       619 . 166 ASN C  C 175.449 0.2  1 
       620 . 167 GLU H  H   8.651 0.02 1 
       621 . 167 GLU N  N 117.700 0.1  1 
       622 . 167 GLU CA C  59.940 0.3  1 
       623 . 167 GLU C  C 178.780 0.2  1 
       624 . 168 ASP H  H   8.000 0.02 1 
       625 . 168 ASP N  N 119.900 0.1  1 
       626 . 168 ASP CA C  56.895 0.3  1 
       627 . 168 ASP C  C 177.876 0.2  1 
       628 . 169 GLU H  H   8.415 0.02 1 
       629 . 169 GLU N  N 118.442 0.1  1 
       630 . 169 GLU CA C  58.766 0.3  1 
       631 . 169 GLU C  C 178.033 0.2  1 
       632 . 170 ARG H  H   8.325 0.02 1 
       633 . 170 ARG N  N 116.776 0.1  1 
       634 . 170 ARG CA C  60.173 0.3  1 
       635 . 170 ARG C  C 177.133 0.2  1 
       636 . 171 GLU H  H   7.746 0.02 1 
       637 . 171 GLU N  N 118.050 0.1  1 
       638 . 171 GLU CA C  59.009 0.3  1 
       639 . 171 GLU C  C 178.975 0.2  1 
       640 . 172 VAL H  H   8.140 0.02 1 
       641 . 172 VAL N  N 118.853 0.1  1 
       642 . 172 VAL CA C  65.571 0.3  1 
       643 . 172 VAL C  C 179.698 0.2  1 
       644 . 173 LEU H  H   8.600 0.02 1 
       645 . 173 LEU N  N 123.626 0.1  1 
       646 . 173 LEU CA C  58.538 0.3  1 
       647 . 173 LEU C  C 177.901 0.2  1 
       648 . 174 ILE H  H   8.392 0.02 1 
       649 . 174 ILE N  N 119.700 0.1  1 
       650 . 174 ILE CA C  64.397 0.3  1 
       651 . 174 ILE C  C 177.803 0.2  1 
       652 . 175 ASN H  H   7.971 0.02 1 
       653 . 175 ASN N  N 118.194 0.1  1 
       654 . 175 ASN CA C  56.194 0.3  1 
       655 . 175 ASN C  C 178.182 0.2  1 
       656 . 176 ASN H  H   8.054 0.02 1 
       657 . 176 ASN N  N 118.200 0.1  1 
       658 . 176 ASN CA C  57.366 0.3  1 
       659 . 176 ASN C  C 177.383 0.2  1 
       660 . 177 ILE H  H   8.762 0.02 1 
       661 . 177 ILE N  N 123.400 0.1  1 
       662 . 177 ILE CA C  66.504 0.3  1 
       663 . 177 ILE C  C 177.470 0.2  1 
       664 . 178 ASN H  H   8.227 0.02 1 
       665 . 178 ASN N  N 117.700 0.1  1 
       666 . 178 ASN CA C  55.962 0.3  1 
       667 . 178 ASN C  C 178.603 0.2  1 
       668 . 179 ARG H  H   7.744 0.02 1 
       669 . 179 ARG N  N 117.795 0.1  1 
       670 . 179 ARG CA C  58.066 0.3  1 
       671 . 179 ARG C  C 177.543 0.2  1 
       672 . 180 ARG H  H   7.509 0.02 1 
       673 . 180 ARG N  N 114.705 0.1  1 
       674 . 180 ARG CA C  55.728 0.3  1 
       675 . 180 ARG C  C 177.216 0.2  1 
       676 . 181 LEU H  H   8.390 0.02 1 
       677 . 181 LEU N  N 117.500 0.1  1 
       678 . 181 LEU CA C  54.316 0.3  1 
       679 . 181 LEU C  C 176.655 0.2  1 
       680 . 182 THR H  H   7.392 0.02 1 
       681 . 182 THR N  N 116.656 0.1  1 
       682 . 182 THR CA C  61.116 0.3  1 
       683 . 183 PRO CA C  63.228 0.3  1 
       684 . 183 PRO C  C 176.225 0.2  1 
       685 . 184 GLN H  H   8.436 0.02 1 
       686 . 184 GLN N  N 121.211 0.1  1 
       687 . 184 GLN CA C  54.553 0.3  1 
       688 . 184 GLN C  C 174.881 0.2  1 
       689 . 185 ALA H  H   8.365 0.02 1 
       690 . 185 ALA N  N 125.628 0.1  1 
       691 . 185 ALA CA C  52.220 0.3  1 
       692 . 185 ALA C  C 177.405 0.2  1 
       693 . 186 VAL H  H   8.778 0.02 1 
       694 . 186 VAL N  N 117.420 0.1  1 
       695 . 186 VAL CA C  59.253 0.3  1 
       696 . 186 VAL C  C 173.579 0.2  1 
       697 . 187 LYS H  H   8.628 0.02 1 
       698 . 187 LYS N  N 124.326 0.1  1 
       699 . 187 LYS CA C  54.788 0.3  1 
       700 . 187 LYS C  C 174.420 0.2  1 
       701 . 188 ILE H  H   8.760 0.02 1 
       702 . 188 ILE N  N 125.600 0.1  1 
       703 . 188 ILE CA C  58.069 0.3  1 
       704 . 188 ILE C  C 174.134 0.2  1 
       705 . 189 ARG H  H   8.842 0.02 1 
       706 . 189 ARG N  N 127.400 0.1  1 
       707 . 189 ARG CA C  53.608 0.3  1 
       708 . 189 ARG C  C 172.942 0.2  1 
       709 . 190 ALA H  H   9.166 0.02 1 
       710 . 190 ALA N  N 125.912 0.1  1 
       711 . 190 ALA CA C  51.042 0.3  1 
       712 . 190 ALA C  C 174.645 0.2  1 
       713 . 191 ASP H  H   8.714 0.02 1 
       714 . 191 ASP N  N 119.200 0.1  1 
       715 . 191 ASP CA C  52.680 0.3  1 
       716 . 191 ASP C  C 176.420 0.2  1 
       717 . 192 ILE H  H   9.020 0.02 1 
       718 . 192 ILE N  N 116.773 0.1  1 
       719 . 192 ILE CA C  59.004 0.3  1 
       720 . 192 ILE C  C 173.131 0.2  1 
       721 . 193 GLU H  H   8.802 0.02 1 
       722 . 193 GLU N  N 121.400 0.1  1 
       723 . 193 GLU CA C  54.080 0.3  1 
       724 . 193 GLU C  C 175.402 0.2  1 
       725 . 194 VAL H  H   8.528 0.02 1 
       726 . 194 VAL N  N 120.162 0.1  1 
       727 . 194 VAL CA C  60.183 0.3  1 
       728 . 194 VAL C  C 173.371 0.2  1 
       729 . 195 ALA H  H   8.635 0.02 1 
       730 . 195 ALA N  N 125.611 0.1  1 
       731 . 195 ALA CA C  51.036 0.3  1 
       732 . 195 ALA C  C 175.230 0.2  1 
       733 . 196 CYS H  H   8.241 0.02 1 
       734 . 196 CYS N  N 119.200 0.1  1 
       735 . 196 CYS CA C  59.710 0.3  1 
       736 . 196 CYS C  C 172.754 0.2  1 
       737 . 197 TYR H  H   8.963 0.02 1 
       738 . 197 TYR N  N 127.736 0.1  1 
       739 . 197 TYR CA C  57.600 0.3  1 
       740 . 197 TYR C  C 176.302 0.2  1 
       741 . 198 GLY H  H   8.076 0.02 1 
       742 . 198 GLY N  N 109.224 0.1  1 
       743 . 198 GLY CA C  44.230 0.3  1 
       744 . 198 GLY C  C 174.686 0.2  1 
       745 . 199 TYR H  H   8.506 0.02 1 
       746 . 199 TYR N  N 121.065 0.1  1 
       747 . 199 TYR CA C  60.175 0.3  1 
       748 . 199 TYR C  C 177.541 0.2  1 
       749 . 200 GLU H  H   8.879 0.02 1 
       750 . 200 GLU N  N 119.827 0.1  1 
       751 . 200 GLU CA C  57.366 0.3  1 
       752 . 200 GLU C  C 177.975 0.2  1 
       753 . 201 GLY H  H   7.730 0.02 1 
       754 . 201 GLY N  N 107.653 0.1  1 
       755 . 201 GLY CA C  47.054 0.3  1 
       756 . 201 GLY C  C 175.396 0.2  1 
       757 . 202 ILE H  H   8.183 0.02 1 
       758 . 202 ILE N  N 122.379 0.1  1 
       759 . 202 ILE CA C  62.288 0.3  1 
       760 . 202 ILE C  C 177.605 0.2  1 
       761 . 203 ASP H  H   7.973 0.02 1 
       762 . 203 ASP N  N 121.682 0.1  1 
       763 . 203 ASP CA C  56.902 0.3  1 
       764 . 203 ASP C  C 178.459 0.2  1 
       765 . 204 ALA H  H   7.679 0.02 1 
       766 . 204 ALA N  N 122.900 0.1  1 
       767 . 204 ALA CA C  54.788 0.3  1 
       768 . 204 ALA C  C 180.101 0.2  1 
       769 . 205 VAL H  H   7.538 0.02 1 
       770 . 205 VAL N  N 119.000 0.1  1 
       771 . 205 VAL CA C  66.504 0.3  1 
       772 . 205 VAL C  C 177.426 0.2  1 
       773 . 206 LYS H  H   8.052 0.02 1 
       774 . 206 LYS N  N 118.151 0.1  1 
       775 . 206 LYS CA C  60.159 0.3  1 
       776 . 206 LYS C  C 179.384 0.2  1 
       777 . 207 GLU H  H   8.057 0.02 1 
       778 . 207 GLU N  N 118.227 0.1  1 
       779 . 207 GLU CA C  58.770 0.3  1 
       780 . 207 GLU C  C 179.140 0.2  1 
       781 . 208 ALA H  H   7.940 0.02 1 
       782 . 208 ALA N  N 123.631 0.1  1 
       783 . 208 ALA CA C  55.024 0.3  1 
       784 . 208 ALA C  C 178.726 0.2  1 
       785 . 209 LEU H  H   8.393 0.02 1 
       786 . 209 LEU N  N 116.101 0.1  1 
       787 . 209 LEU CA C  57.829 0.3  1 
       788 . 209 LEU C  C 179.307 0.2  1 
       789 . 210 ARG H  H   8.074 0.02 1 
       790 . 210 ARG N  N 118.267 0.1  1 
       791 . 210 ARG CA C  59.009 0.3  1 
       792 . 210 ARG C  C 178.490 0.2  1 
       793 . 211 ALA H  H   7.605 0.02 1 
       794 . 211 ALA N  N 121.432 0.1  1 
       795 . 211 ALA CA C  54.563 0.3  1 
       796 . 211 ALA C  C 181.082 0.2  1 
       797 . 212 GLY H  H   7.780 0.02 1 
       798 . 212 GLY N  N 105.998 0.1  1 
       799 . 212 GLY CA C  47.067 0.3  1 
       800 . 212 GLY C  C 175.463 0.2  1 
       801 . 213 LEU H  H   8.335 0.02 1 
       802 . 213 LEU N  N 121.300 0.1  1 
       803 . 213 LEU CA C  57.375 0.3  1 
       804 . 213 LEU C  C 179.924 0.2  1 
       805 . 214 ASN H  H   7.903 0.02 1 
       806 . 214 ASN N  N 118.075 0.1  1 
       807 . 214 ASN CA C  54.088 0.3  1 
       808 . 214 ASN C  C 175.898 0.2  1 
       809 . 215 CYS H  H   7.712 0.02 1 
       810 . 215 CYS N  N 116.699 0.1  1 
       811 . 215 CYS CA C  60.644 0.3  1 
       812 . 215 CYS C  C 173.931 0.2  1 
       813 . 216 SER H  H   7.680 0.02 1 
       814 . 216 SER N  N 114.532 0.1  1 
       815 . 216 SER CA C  59.701 0.3  1 
       816 . 216 SER C  C 173.600 0.2  1 
       817 . 217 THR H  H   7.735 0.02 1 
       818 . 217 THR N  N 114.329 0.1  1 
       819 . 217 THR CA C  59.476 0.3  1 
       820 . 221 PRO CA C  62.221 0.3  1 
       821 . 221 PRO C  C 178.448 0.2  1 
       822 . 222 ILE H  H   8.645 0.02 1 
       823 . 222 ILE N  N 128.214 0.1  1 
       824 . 222 ILE CA C  60.413 0.3  1 
       825 . 222 ILE C  C 174.407 0.2  1 
       826 . 223 LYS H  H   8.967 0.02 1 
       827 . 223 LYS N  N 126.400 0.1  1 
       828 . 223 LYS CA C  54.085 0.3  1 
       829 . 223 LYS C  C 175.539 0.2  1 
       830 . 224 ILE H  H   8.580 0.02 1 
       831 . 224 ILE N  N 121.886 0.1  1 
       832 . 224 ILE CA C  60.410 0.3  1 
       833 . 224 ILE C  C 174.657 0.2  1 
       834 . 225 ASN H  H   9.096 0.02 1 
       835 . 225 ASN N  N 124.660 0.1  1 
       836 . 225 ASN CA C  51.753 0.3  1 
       837 . 225 ASN C  C 174.890 0.2  1 
       838 . 226 LEU H  H   8.847 0.02 1 
       839 . 226 LEU N  N 126.001 0.1  1 
       840 . 226 LEU CA C  54.803 0.3  1 
       841 . 226 LEU C  C 176.491 0.2  1 
       842 . 227 ILE H  H   8.293 0.02 1 
       843 . 227 ILE N  N 127.300 0.1  1 
       844 . 227 ILE CA C  61.600 0.3  1 
       845 . 227 ILE C  C 174.230 0.2  1 
       846 . 228 ALA H  H   7.030 0.02 1 
       847 . 228 ALA N  N 119.761 0.1  1 
       848 . 230 PRO C  C 172.696 0.2  1 
       849 . 231 ARG H  H   9.166 0.02 1 
       850 . 231 ARG N  N 125.900 0.1  1 
       851 . 231 ARG CA C  56.250 0.3  1 
       852 . 231 ARG C  C 174.117 0.2  1 
       853 . 232 TYR H  H   9.313 0.02 1 
       854 . 232 TYR N  N 123.900 0.1  1 
       855 . 232 TYR CA C  62.280 0.3  1 
       856 . 232 TYR C  C 174.514 0.2  1 
       857 . 233 VAL H  H   9.083 0.02 1 
       858 . 233 VAL N  N 120.573 0.1  1 
       859 . 233 VAL CA C  60.211 0.3  1 
       860 . 233 VAL C  C 175.073 0.2  1 
       861 . 234 MET H  H   9.715 0.02 1 
       862 . 234 MET N  N 129.673 0.1  1 
       863 . 234 MET CA C  53.368 0.3  1 
       864 . 234 MET C  C 174.903 0.2  1 
       865 . 235 THR H  H   9.285 0.02 1 
       866 . 235 THR N  N 113.178 0.1  1 
       867 . 235 THR CA C  58.772 0.3  1 
       868 . 235 THR C  C 174.181 0.2  1 
       869 . 236 THR H  H   8.510 0.02 1 
       870 . 236 THR N  N 112.846 0.1  1 
       871 . 236 THR CA C  61.129 0.3  1 
       872 . 236 THR C  C 172.112 0.2  1 
       873 . 237 THR H  H   7.713 0.02 1 
       874 . 237 THR N  N 119.309 0.1  1 
       875 . 237 THR CA C  60.191 0.3  1 
       876 . 237 THR C  C 173.358 0.2  1 
       877 . 238 THR H  H   8.828 0.02 1 
       878 . 238 THR N  N 117.518 0.1  1 
       879 . 238 THR CA C  59.241 0.3  1 
       880 . 238 THR C  C 171.655 0.2  1 
       881 . 239 LEU H  H   8.405 0.02 1 
       882 . 239 LEU N  N 124.735 0.1  1 
       883 . 239 LEU CA C  55.737 0.3  1 
       884 . 239 LEU C  C 177.586 0.2  1 
       885 . 240 GLU H  H   8.501 0.02 1 
       886 . 240 GLU N  N 121.903 0.1  1 
       887 . 240 GLU CA C  54.319 0.3  1 
       888 . 241 ARG CA C  60.173 0.3  1 
       889 . 241 ARG C  C 176.913 0.2  1 
       890 . 242 THR H  H   8.645 0.02 1 
       891 . 242 THR N  N 112.513 0.1  1 
       892 . 242 THR CA C  66.044 0.3  1 
       893 . 242 THR C  C 177.379 0.2  1 
       894 . 243 GLU H  H   7.757 0.02 1 
       895 . 243 GLU N  N 122.700 0.1  1 
       896 . 243 GLU CA C  58.532 0.3  1 
       897 . 243 GLU C  C 178.928 0.2  1 
       898 . 244 GLY H  H   8.124 0.02 1 
       899 . 244 GLY N  N 107.598 0.1  1 
       900 . 244 GLY CA C  47.285 0.3  1 
       901 . 244 GLY C  C 174.849 0.2  1 
       902 . 245 LEU H  H   8.077 0.02 1 
       903 . 245 LEU N  N 121.275 0.1  1 
       904 . 245 LEU CA C  58.301 0.3  1 
       905 . 245 LEU C  C 179.558 0.2  1 
       906 . 246 SER H  H   7.644 0.02 1 
       907 . 246 SER N  N 113.827 0.1  1 
       908 . 246 SER CA C  61.104 0.3  1 
       909 . 246 SER C  C 177.535 0.2  1 
       910 . 247 VAL H  H   8.522 0.02 1 
       911 . 247 VAL N  N 122.700 0.1  1 
       912 . 247 VAL CA C  66.038 0.3  1 
       913 . 247 VAL C  C 178.169 0.2  1 
       914 . 248 LEU H  H   7.864 0.02 1 
       915 . 248 LEU N  N 119.078 0.1  1 
       916 . 248 LEU CA C  57.839 0.3  1 
       917 . 248 LEU C  C 179.393 0.2  1 
       918 . 249 SER H  H   7.952 0.02 1 
       919 . 249 SER N  N 115.129 0.1  1 
       920 . 249 SER CA C  62.747 0.3  1 
       921 . 249 SER C  C 177.457 0.2  1 
       922 . 250 GLN H  H   8.440 0.02 1 
       923 . 250 GLN N  N 124.007 0.1  1 
       924 . 250 GLN CA C  58.769 0.3  1 
       925 . 250 GLN C  C 178.042 0.2  1 
       926 . 251 ALA H  H   8.465 0.02 1 
       927 . 251 ALA N  N 122.384 0.1  1 
       928 . 251 ALA CA C  55.023 0.3  1 
       929 . 251 ALA C  C 179.941 0.2  1 
       930 . 252 MET H  H   8.460 0.02 1 
       931 . 252 MET N  N 116.080 0.1  1 
       932 . 252 MET CA C  59.947 0.3  1 
       933 . 252 MET C  C 176.499 0.2  1 
       934 . 253 ALA H  H   7.561 0.02 1 
       935 . 253 ALA N  N 120.244 0.1  1 
       936 . 253 ALA CA C  54.788 0.3  1 
       937 . 253 ALA C  C 180.664 0.2  1 
       938 . 254 VAL H  H   7.793 0.02 1 
       939 . 254 VAL N  N 119.285 0.1  1 
       940 . 254 VAL CA C  65.335 0.3  1 
       941 . 254 VAL C  C 177.803 0.2  1 
       942 . 255 ILE H  H   7.972 0.02 1 
       943 . 255 ILE N  N 121.746 0.1  1 
       944 . 255 ILE CA C  65.335 0.3  1 
       945 . 255 ILE C  C 177.073 0.2  1 
       946 . 256 LYS H  H   7.722 0.02 1 
       947 . 256 LYS N  N 119.138 0.1  1 
       948 . 256 LYS CA C  59.473 0.3  1 
       949 . 256 LYS C  C 177.285 0.2  1 
       950 . 257 GLU H  H   7.632 0.02 1 
       951 . 257 GLU N  N 116.864 0.1  1 
       952 . 257 GLU CA C  58.773 0.3  1 
       953 . 257 GLU C  C 179.777 0.2  1 
       954 . 258 LYS H  H   8.030 0.02 1 
       955 . 258 LYS N  N 117.537 0.1  1 
       956 . 258 LYS CA C  56.910 0.3  1 
       957 . 258 LYS C  C 179.431 0.2  1 
       958 . 259 ILE H  H   8.739 0.02 1 
       959 . 259 ILE N  N 119.500 0.1  1 
       960 . 259 ILE CA C  59.707 0.3  1 
       961 . 259 ILE C  C 178.554 0.2  1 
       962 . 260 GLU H  H   8.464 0.02 1 
       963 . 260 GLU N  N 123.603 0.1  1 
       964 . 260 GLU CA C  59.473 0.3  1 
       965 . 260 GLU C  C 181.314 0.2  1 
       966 . 261 GLU H  H   7.905 0.02 1 
       967 . 261 GLU N  N 122.595 0.1  1 
       968 . 261 GLU CA C  58.773 0.3  1 
       969 . 261 GLU C  C 177.972 0.2  1 
       970 . 262 LYS H  H   6.942 0.02 1 
       971 . 262 LYS N  N 116.873 0.1  1 
       972 . 262 LYS CA C  54.085 0.3  1 
       973 . 262 LYS C  C 174.400 0.2  1 
       974 . 263 ARG H  H   7.832 0.02 1 
       975 . 263 ARG N  N 112.300 0.1  1 
       976 . 263 ARG CA C  56.898 0.3  1 
       977 . 263 ARG C  C 176.626 0.2  1 
       978 . 264 GLY H  H   8.237 0.02 1 
       979 . 264 GLY N  N 106.153 0.1  1 
       980 . 264 GLY CA C  44.004 0.3  1 
       981 . 264 GLY C  C 172.058 0.2  1 
       982 . 265 VAL H  H   8.802 0.02 1 
       983 . 265 VAL N  N 117.789 0.1  1 
       984 . 265 VAL CA C  60.885 0.3  1 
       985 . 265 VAL C  C 173.233 0.2  1 
       986 . 266 PHE H  H   8.704 0.02 1 
       987 . 266 PHE N  N 126.155 0.1  1 
       988 . 266 PHE CA C  55.957 0.3  1 
       989 . 266 PHE C  C 174.418 0.2  1 
       990 . 267 ASN H  H   8.369 0.02 1 
       991 . 267 ASN N  N 123.822 0.1  1 
       992 . 267 ASN CA C  52.208 0.3  1 
       993 . 267 ASN C  C 172.799 0.2  1 
       994 . 268 VAL H  H   8.581 0.02 1 
       995 . 268 VAL N  N 122.553 0.1  1 
       996 . 268 VAL CA C  62.520 0.3  1 
       997 . 268 VAL C  C 175.676 0.2  1 
       998 . 269 GLN H  H   8.335 0.02 1 
       999 . 269 GLN N  N 127.100 0.1  1 
      1000 . 269 GLN CA C  55.949 0.3  1 
      1001 . 269 GLN C  C 176.042 0.2  1 
      1002 . 270 MET H  H   8.290 0.02 1 
      1003 . 270 MET N  N 121.230 0.1  1 
      1004 . 270 MET CA C  56.160 0.3  1 
      1005 . 270 MET C  C 174.411 0.2  1 
      1006 . 271 GLU H  H   8.640 0.02 1 
      1007 . 271 GLU N  N 127.400 0.1  1 
      1008 . 271 GLU CA C  55.481 0.3  1 
      1009 . 272 PRO CA C  62.986 0.3  1 
      1010 . 272 PRO C  C 176.126 0.2  1 
      1011 . 273 LYS H  H   8.906 0.02 1 
      1012 . 273 LYS N  N 122.392 0.1  1 
      1013 . 273 LYS CA C  54.553 0.3  1 
      1014 . 273 LYS C  C 174.884 0.2  1 
      1015 . 274 VAL H  H   8.553 0.02 1 
      1016 . 274 VAL N  N 123.446 0.1  1 
      1017 . 274 VAL CA C  62.758 0.3  1 
      1018 . 274 VAL C  C 176.802 0.2  1 
      1019 . 275 VAL H  H   8.766 0.02 1 
      1020 . 275 VAL N  N 123.781 0.1  1 
      1021 . 275 VAL CA C  59.946 0.3  1 
      1022 . 275 VAL C  C 175.987 0.2  1 
      1023 . 276 THR H  H   8.710 0.02 1 
      1024 . 276 THR N  N 116.000 0.1  1 
      1025 . 276 THR CA C  60.410 0.3  1 
      1026 . 276 THR C  C 175.238 0.2  1 
      1027 . 277 ASP H  H   8.669 0.02 1 
      1028 . 277 ASP N  N 121.614 0.1  1 
      1029 . 277 ASP CA C  55.968 0.3  1 
      1030 . 277 ASP C  C 177.822 0.2  1 
      1031 . 278 THR H  H   8.115 0.02 1 
      1032 . 278 THR N  N 114.580 0.1  1 
      1033 . 278 THR CA C  63.695 0.3  1 
      1034 . 278 THR C  C 175.691 0.2  1 
      1035 . 279 ASP H  H   7.966 0.02 1 
      1036 . 279 ASP N  N 122.717 0.1  1 
      1037 . 279 ASP CA C  55.960 0.3  1 
      1038 . 279 ASP C  C 178.077 0.2  1 
      1039 . 280 GLU H  H   8.343 0.02 1 
      1040 . 280 GLU N  N 120.242 0.1  1 
      1041 . 280 GLU CA C  59.239 0.3  1 
      1042 . 280 GLU C  C 178.612 0.2  1 
      1043 . 281 THR H  H   8.274 0.02 1 
      1044 . 281 THR N  N 117.200 0.1  1 
      1045 . 281 THR CA C  64.866 0.3  1 
      1046 . 281 THR C  C 176.208 0.2  1 
      1047 . 282 GLU H  H   8.040 0.02 1 
      1048 . 282 GLU N  N 122.904 0.1  1 
      1049 . 282 GLU CA C  58.304 0.3  1 
      1050 . 282 GLU C  C 178.594 0.2  1 
      1051 . 283 LEU H  H   8.104 0.02 1 
      1052 . 283 LEU N  N 121.073 0.1  1 
      1053 . 283 LEU CA C  57.123 0.3  1 
      1054 . 283 LEU C  C 178.788 0.2  1 
      1055 . 284 ALA H  H   7.948 0.02 1 
      1056 . 284 ALA N  N 121.500 0.1  1 
      1057 . 284 ALA CA C  54.316 0.3  1 
      1058 . 284 ALA C  C 180.089 0.2  1 
      1059 . 285 ARG H  H   7.932 0.02 1 
      1060 . 285 ARG N  N 118.874 0.1  1 
      1061 . 285 ARG CA C  58.070 0.3  1 
      1062 . 285 ARG C  C 178.789 0.2  1 
      1063 . 286 GLN H  H   8.108 0.02 1 
      1064 . 286 GLN N  N 119.592 0.1  1 
      1065 . 286 GLN CA C  57.603 0.3  1 
      1066 . 286 GLN C  C 178.066 0.2  1 
      1067 . 287 MET H  H   8.170 0.02 1 
      1068 . 287 MET N  N 118.905 0.1  1 
      1069 . 287 MET CA C  56.900 0.3  1 
      1070 . 287 MET C  C 177.833 0.2  1 
      1071 . 288 GLU H  H   8.022 0.02 1 
      1072 . 288 GLU N  N 120.602 0.1  1 
      1073 . 288 GLU CA C  57.841 0.3  1 
      1074 . 288 GLU C  C 177.859 0.2  1 
      1075 . 289 ARG H  H   7.907 0.02 1 
      1076 . 289 ARG N  N 119.903 0.1  1 
      1077 . 289 ARG CA C  57.592 0.3  1 
      1078 . 289 ARG C  C 177.471 0.2  1 
      1079 . 290 LEU H  H   7.944 0.02 1 
      1080 . 290 LEU N  N 121.147 0.1  1 
      1081 . 290 LEU CA C  56.194 0.3  1 
      1082 . 290 LEU C  C 178.364 0.2  1 
      1083 . 291 GLU H  H   8.102 0.02 1 
      1084 . 291 GLU N  N 120.153 0.1  1 
      1085 . 291 GLU CA C  57.361 0.3  1 
      1086 . 291 GLU C  C 177.641 0.2  1 
      1087 . 292 ARG H  H   8.020 0.02 1 
      1088 . 292 ARG N  N 120.393 0.1  1 
      1089 . 292 ARG CA C  56.891 0.3  1 
      1090 . 292 ARG C  C 177.290 0.2  1 
      1091 . 293 GLU H  H   8.313 0.02 1 
      1092 . 293 GLU N  N 120.788 0.1  1 
      1093 . 293 GLU CA C  57.129 0.3  1 
      1094 . 293 GLU C  C 176.989 0.2  1 
      1095 . 294 ASN H  H   8.280 0.02 1 
      1096 . 294 ASN N  N 118.833 0.1  1 
      1097 . 294 ASN CA C  53.382 0.3  1 
      1098 . 294 ASN C  C 175.128 0.2  1 
      1099 . 295 ALA H  H   8.066 0.02 1 
      1100 . 295 ALA N  N 123.857 0.1  1 
      1101 . 295 ALA CA C  52.673 0.3  1 
      1102 . 295 ALA C  C 177.874 0.2  1 
      1103 . 296 GLU H  H   8.257 0.02 1 
      1104 . 296 GLU N  N 119.838 0.1  1 
      1105 . 296 GLU CA C  56.424 0.3  1 
      1106 . 296 GLU C  C 176.763 0.2  1 
      1107 . 297 VAL H  H   8.040 0.02 1 
      1108 . 297 VAL N  N 120.429 0.1  1 
      1109 . 297 VAL CA C  61.823 0.3  1 
      1110 . 297 VAL C  C 176.006 0.2  1 
      1111 . 298 ASP H  H   8.366 0.02 1 
      1112 . 298 ASP N  N 123.786 0.1  1 
      1113 . 298 ASP CA C  54.318 0.3  1 
      1114 . 298 ASP C  C 176.822 0.2  1 
      1115 . 299 GLY H  H   8.285 0.02 1 
      1116 . 299 GLY N  N 109.785 0.1  1 
      1117 . 299 GLY CA C  45.410 0.3  1 
      1118 . 299 GLY C  C 174.070 0.2  1 
      1119 . 300 ASP H  H   8.277 0.02 1 
      1120 . 300 ASP N  N 120.627 0.1  1 
      1121 . 300 ASP CA C  54.089 0.3  1 
      1122 . 300 ASP C  C 176.526 0.2  1 

   stop_

save_