data_4117

#######################
#  Entry information  #
#######################
save_entry_information
   _Saveframe_category      entry_information

   _Entry_title            
;
1H, 15N and 13C Chemical Shift Assignment of the Guanine Nucleotide 
Exchange Domain of Human Elongation Factor-one Beta
;

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

       1   Perez     Janice  M.J.  . 
       2   Kriek     Jan     .     . 
       3   Dijk      Jan     .     . 
       4   Moller    Wim     .     . 
       5   Siegal    Gregg   .     . 
       6   Hard      Karl    .     . 
       7   Kalverda  Arnout  P.    . 
       8   Canters   Gerard  W.    . 

   stop_

   _BMRB_accession_number   4117
   _BMRB_flat_file_name     bmr4117.str
   _Entry_type              new
   _Submission_date         1998-03-05
   _Accession_date          1998-03-05
   _Entry_origination       author
   _NMR_STAR_version        2.1
   _Experimental_method     NMR

   loop_
      _Saveframe_category_type
      _Saveframe_category_type_count

       assigned_chemical_shifts  1  

   stop_

   loop_
      _Data_type
      _Data_type_count

      '1H chemical shifts'   522  
      '13C chemical shifts'  370  
      '15N chemical shifts'   95  

   stop_

save_


#############################
#  Citation for this entry  #
#############################
save_entry_citation
   _Saveframe_category     entry_citation

   _Citation_full         
;
   
Perez, J. M. J., Kriek, J., Dijk, J., Moller, W., Siegal, G., 
Hard, K., Kalverda, A. P., and Canters, G. W., "1H, 15N and 
13C Chemical Shift Assignment of the Guanine Nucleotide Exchange
Domain of Human Elongation Factor-one Beta," J. Biomol. NMR 12,
467-468 (1998).
;
   _Citation_title        
;
1H, 15N and 13C Chemical Shift Assignment of the Guanine Nucleotide 
Exchange Domain of Human Elongation Factor-one Beta
;
   _Citation_status        published
   _Citation_type          journal
   _MEDLINE_UI_code        99052123

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

       1   Perez     Janice  M.J.  . 
       2   Kriek     Jan     .     . 
       3   Dijk      Jan     .     . 
       4   Moller    Wim     .     . 
       5   Siegal    Gregg   .     . 
       6   Hard      Karl    .     . 
       7   Kalverda  Arnout  P.    . 
       8   Canters   Gerard  W.    . 

   stop_

   _Journal_abbreviation  'J. Biomol. NMR'
   _Journal_volume         12
   _Journal_issue          .
   _Page_first             467
   _Page_last              468
   _Year                   1998

   loop_
      _Keyword

      'protein synthesis'           
      'G proteins'                  
      'Guanine nucleotide exchange' 

   stop_

save_


##################################
#  Molecular system description  #
##################################
save_system_hEF-1beta
   _Saveframe_category      molecular_system

   _Mol_system_name        'human Elongation Factor-1beta'
   _Abbreviation_common     hEF-1beta

   loop_
      _Mol_system_component_name
      _Mol_label

       hEF-1beta $b91 

   stop_

   _System_physical_state   native
   _System_oligomer_state   monomer
   _System_type             simple
   _System_paramagnetic     no
   _Details                
;
GDP:GTP exchange factor for Elongation Factor-1alpha
;

   loop_
      _Database_name
      _Database_accession_code
      _Database_entry_mol_name
      _Database_entry_details

       PDB  1B64 "Solution Structure Of The Guanine Nucleotide Exchange Factor Domain From Human Elongation Factor-One Beta, Nmr, 20 Structures"  . 

   stop_

save_


    ########################
    #  Monomeric polymers  #
    ########################
save_b91
   _Saveframe_category                          monomeric_polymer

   _Mol_type                                    polymer
   _Mol_polymer_class                           protein
   _Name_common                                'human Elongation Factor-1beta'
   _Name_variant                                .
   _Abbreviation_common                         hEF-1beta
   _Molecular_mass                              10079
   	##############################
   	#  Polymer residue sequence  #
   	##############################
   _Residue_count                               91
   _Mol_residue_sequence                       
;
MLVAKSSILLDVKPWDDETD
MAKLEECVRSIQADGLVWGS
SKLVPVGYGIKKLQIQCVVE
DDKVGTDMLEEQITAFEDYV
QSMDVAAFNKI
;

   loop_
      _Residue_seq_code
      _Residue_author_seq_code
      _Residue_label

        1     1   MET    2   135   LEU    3   136   VAL    4   137   ALA    5   138   LYS 
        6   139   SER    7   140   SER    8   141   ILE    9   142   LEU   10   143   LEU 
       11   144   ASP   12   145   VAL   13   146   LYS   14   147   PRO   15   148   TRP 
       16   149   ASP   17   150   ASP   18   151   GLU   19   152   THR   20   153   ASP 
       21   154   MET   22   155   ALA   23   156   LYS   24   157   LEU   25   158   GLU 
       26   159   GLU   27   160   CYS   28   161   VAL   29   162   ARG   30   163   SER 
       31   164   ILE   32   165   GLN   33   166   ALA   34   167   ASP   35   168   GLY 
       36   169   LEU   37   170   VAL   38   171   TRP   39   172   GLY   40   173   SER 
       41   174   SER   42   175   LYS   43   176   LEU   44   177   VAL   45   178   PRO 
       46   179   VAL   47   180   GLY   48   181   TYR   49   182   GLY   50   183   ILE 
       51   184   LYS   52   185   LYS   53   186   LEU   54   187   GLN   55   188   ILE 
       56   189   GLN   57   190   CYS   58   191   VAL   59   192   VAL   60   193   GLU 
       61   194   ASP   62   195   ASP   63   196   LYS   64   197   VAL   65   198   GLY 
       66   299   THR   67   200   ASP   68   201   MET   69   202   LEU   70   203   GLU 
       71   204   GLU   72   205   GLN   73   206   ILE   74   207   THR   75   208   ALA 
       76   209   PHE   77   210   GLU   78   211   ASP   79   212   TYR   80   213   VAL 
       81   214   GLN   82   215   SER   83   216   MET   84   217   ASP   85   218   VAL 
       86   219   ALA   87   220   ALA   88   221   PHE   89   222   ASN   90   223   LYS 
       91   224   ILE 

   stop_

   _Sequence_homology_query_date                2001-09-08
   _Sequence_homology_query_revised_last_date   2001-09-08

   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         1B64        "Solution Structure Of The Guanine Nucleotide Exchange Factor Domain From Human Elongation Factor-One Beta, Nmr, 20 Structures"    100%     91     100%    100%    5e-46 
       EMBL        CAA43019.1  "(X60489) elongation factor-1-beta [Homo sapiens]"                                                                                  98%    225     100%    100%    2e-45 
       EMBL        CAA43063.1  "(X60656) elongation factor 1-beta [Homo sapiens]"                                                                                  98%    225     100%    100%    2e-45 
       EMBL        CAA52741.1  "(X74728) elongation factor 1 beta [Oryctolagus cuniculus]"                                                                         98%    225      98%     98%    6e-45 
       GenBank     AAD16874.1  "(AF103726) peptide elongation factor 1-beta [Gallus gallus]"                                                                       98%    225     100%    100%    2e-45 
       GenBank     AAH00211.1  "AAH00211 (BC000211) eukaryotic translation elongation factor 1 beta 2 [Homo sapiens]"                                              98%    225     100%    100%    2e-45 
       GenBank     AAH04931.1  "AAH04931 (BC004931) eukaryotic translation elongation factor 1 beta 2 [Homo sapiens]"                                              98%    225     100%    100%    2e-45 
       PIR         ?           "S25432 translation elongation factor eEF-1 beta chain - human"                                                                     98%    225     100%    100%    2e-45 
       REF         NP_001950.1 "eukaryotic translation elongation factor 1 beta 2 [Homo sapiens]"                                                                  98%    225     100%    100%    2e-45 
       REF         NP_066944.1 "eukaryotic translation elongation factor 1 beta 1 [Homo sapiens]"                                                                  98%    225     100%    100%    2e-45 
       REF         XP_002668.1 "eukaryotic translation elongation factor 1 beta 2 [Homo sapiens]"                                                                  98%    225     100%    100%    2e-45 
       REF         XP_010882.1 "eukaryotic translation elongation factor 1 beta 2 [Homo sapiens]"                                                                  98%    225     100%    100%    2e-45 
       REF         XP_027740.1 "eukaryotic translation elongation factor 1 beta 2 [Homo sapiens]"                                                                  98%    225     100%    100%    2e-45 
       SWISS-PROT  P24534      "EF1B_HUMAN ELONGATION FACTOR 1-BETA (EF-1-BETA)"                                                                                   98%    225     100%    100%    2e-45 
       SWISS-PROT  P34826      "EF1B_RABIT ELONGATION FACTOR 1-BETA (EF-1-BETA)"                                                                                   98%    225      98%     98%    6e-45 

   stop_

save_


    ####################
    #  Natural source  #
    ####################
save_natural_source
   _Saveframe_category   natural_source


   loop_
      _Mol_label
      _Organism_name_common
      _NCBI_taxonomy_ID
      _Superkingdom
      _Kingdom
      _Genus
      _Species
      _Details

      $b91  Human  9606   Eukaryota  Metazoa  Homo  sapiens 
;
cloned from cDNA library made from human fibroblast mRNA
; 

   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
      _Details

      $b91 'recombinant technology' 'E. coli'  Escherichia  coli  BL21(DE3)  plasmid  pET11a 
;
pET11a operating under T7 promoter and lac control
; 

   stop_

save_


#####################################
#  Sample contents and methodology  #
#####################################
	 
    ########################
    #  Sample description  #
    ########################
save_sample_one
   _Saveframe_category   sample

   _Sample_type          solution

   loop_
      _Mol_label
      _Concentration_value
      _Concentration_value_units
      _Isotopic_labeling

      $b91      1     mM '[U-13C; U-15N]' 
       NaCl   100     mM  .               
       NaPO4   10     mM  .               
       DTT      1     mM  .               
       NaN3     0.02  %   .               
       H2O     95     %   .               
       D2O      5     %   .               

   stop_

save_


#######################
#  Sample conditions  #
#######################
save_sample_conditions_one
   _Saveframe_category   sample_conditions


   loop_
      _Variable_type
      _Variable_value
      _Variable_value_error
      _Variable_value_units

       pH                 6.9  ?  n/a 
       temperature      303    ?  K   
      'ionic strength'    0.1  ?  M   

   stop_

save_


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

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

	################################
	#  Chemical shift referencing  #
	################################
save_chemical_shift_reference_one
   _Saveframe_category   chemical_shift_reference

   _Details             
;
   Method of Wishart and Sykes, Meth. Enzymol. 239, 363-392, (1994).
;

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

       DSS  H   1  'methyl protons'  ppm  0.0  external  direct    cylindrical 'external to the sample'  parallel   .           .            
       DSS  N  15  'methyl protons'  ppm  0.0  .         indirect  .            .                        .         0.101329122 $citation_one 
       DSS  C  13  'methyl carbons'  ppm  0.0  external  direct    cylindrical 'external to the sample'  parallel   .           .            

   stop_

save_


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

###################################################################
#       Chemical Shift Ambiguity Index Value Definitions          #
#                                                                 #
#   Index Value            Definition                             #
#                                                                 #
#      1             Unique                                       #
#      2             Ambiguity of geminal atoms or geminal methyl #
#                         proton groups                           #
#      3             Aromatic atoms on opposite sides of the ring #
#                        (e.g. Tyr HE1 and HE2 protons)           #
#      4             Intraresidue ambiguities (e.g. Lys HG and    #
#                         HD protons)                             #
#      5             Interresidue ambiguities (Lys 12 vs. Lys 27) #
#      9             Ambiguous, specific ambiguity not defined    #
#                                                                 #
###################################################################
save_assigned_chemical_shifts_one
   _Saveframe_category               assigned_chemical_shifts


   loop_
      _Sample_label

      $sample_one 

   stop_

   _Sample_conditions_label         $sample_conditions_one
   _Chem_shift_reference_set_label  $chemical_shift_reference_one
   _Mol_system_component_name        hEF-1beta

   loop_
      _Atom_shift_assign_ID
      _Residue_seq_code
      _Residue_label
      _Atom_name
      _Atom_type
      _Chem_shift_value
      _Chem_shift_value_error
      _Chem_shift_ambiguity_code

         1    2   LEU  C     C  176.4   .  1  
         2    3   VAL  H     H    8.13  .  1  
         3    3   VAL  HA    H    4.06  .  1  
         4    3   VAL  HB    H    1.94  .  1  
         5    3   VAL  HG1   H    0.83  .  1  
         6    3   VAL  HG2   H    0.83  .  1  
         7    3   VAL  C     C  175.0   .  1  
         8    3   VAL  CA    C   61.3   .  1  
         9    3   VAL  CB    C   32.5   .  1  
        10    3   VAL  CG1   C   20.5   .  1  
        11    3   VAL  CG2   C   20.5   .  1  
        12    3   VAL  N     N  122.4   .  1  
        13    4   ALA  H     H    8.37  .  1  
        14    4   ALA  HA    H    4.34  .  1  
        15    4   ALA  HB    H    1.37  .  1  
        16    4   ALA  C     C  176.8   .  1  
        17    4   ALA  CA    C   52.0   .  1  
        18    4   ALA  CB    C   18.8   .  1  
        19    4   ALA  N     N  129.5   .  1  
        20    5   LYS  H     H    8.48  .  1  
        21    5   LYS  HA    H    5.34  .  1  
        22    5   LYS  HB2   H    1.62  .  2  
        23    5   LYS  HB3   H    1.49  .  2  
        24    5   LYS  HG2   H    1.19  .  2  
        25    5   LYS  HG3   H    1.38  .  2  
        26    5   LYS  HD2   H    1.49  .  1  
        27    5   LYS  HD3   H    1.49  .  1  
        28    5   LYS  HE2   H    2.72  .  1  
        29    5   LYS  HE3   H    2.72  .  1  
        30    5   LYS  C     C  176.2   .  1  
        31    5   LYS  CA    C   54.9   .  1  
        32    5   LYS  CB    C   37.2   .  1  
        33    5   LYS  CG    C   25.4   .  1  
        34    5   LYS  CD    C   29.1   .  1  
        35    5   LYS  CE    C   41.7   .  1  
        36    5   LYS  N     N  122.8   .  1  
        37    6   SER  H     H    8.78  .  1  
        38    6   SER  HA    H    5.02  .  1  
        39    6   SER  HB2   H    3.17  .  2  
        40    6   SER  HB3   H    3.29  .  2  
        41    6   SER  C     C  171.9   .  1  
        42    6   SER  CA    C   57.7   .  1  
        43    6   SER  CB    C   65.2   .  1  
        44    6   SER  N     N  115.6   .  1  
        45    7   SER  H     H    8.99  .  1  
        46    7   SER  HA    H    5.11  .  1  
        47    7   SER  HB2   H    3.58  .  2  
        48    7   SER  HB3   H    3.68  .  2  
        49    7   SER  C     C  174.1   .  1  
        50    7   SER  CA    C   55.6   .  1  
        51    7   SER  CB    C   63.7   .  1  
        52    7   SER  N     N  117.8   .  1  
        53    8   ILE  H     H    9.07  .  1  
        54    8   ILE  HA    H    5.11  .  1  
        55    8   ILE  HB    H    1.74  .  1  
        56    8   ILE  HG12  H    1.22  .  2  
        57    8   ILE  HG13  H    0.62  .  2  
        58    8   ILE  HG2   H    0.81  .  2  
        59    8   ILE  HD1   H    0.50  .  2  
        60    8   ILE  C     C  174.0   .  1  
        61    8   ILE  CA    C   59.8   .  1  
        62    8   ILE  CB    C   40.3   .  1  
        63    8   ILE  CG1   C   26.4   .  1  
        64    8   ILE  CG2   C   18.8   .  1  
        65    8   ILE  CD1   C   13.8   .  1  
        66    8   ILE  N     N  127.8   .  1  
        67    9   LEU  H     H    8.69  .  1  
        68    9   LEU  HA    H    4.92  .  1  
        69    9   LEU  HB2   H    1.72  .  2  
        70    9   LEU  HB3   H    1.30  .  2  
        71    9   LEU  HG    H    1.24  .  1  
        72    9   LEU  HD1   H    0.72  .  2  
        73    9   LEU  HD2   H    0.65  .  2  
        74    9   LEU  C     C  175.1   .  1  
        75    9   LEU  CA    C   53.0   .  1  
        76    9   LEU  CB    C   44.9   .  1  
        77    9   LEU  CG    C   26.4   .  1  
        78    9   LEU  CD1   C   23.5   .  2  
        79    9   LEU  CD2   C   24.8   .  2  
        80    9   LEU  N     N  128.2   .  1  
        81   10   LEU  H     H    9.31  .  1  
        82   10   LEU  HA    H    5.01  .  1  
        83   10   LEU  HB2   H    1.15  .  2  
        84   10   LEU  HB3   H    2.01  .  2  
        85   10   LEU  HG    H    0.82  .  1  
        86   10   LEU  HD1   H    0.98  .  2  
        87   10   LEU  HD2   H    1.76  .  2  
        88   10   LEU  C     C  174.8   .  1  
        89   10   LEU  CA    C   53.0   .  1  
        90   10   LEU  CB    C   43.8   .  1  
        91   10   LEU  CG    C   24.2   .  1  
        92   10   LEU  CD1   C   26.2   .  1  
        93   10   LEU  CD2   C   26.2   .  1  
        94   10   LEU  N     N  126.4   .  1  
        95   11   ASP  H     H    8.89  .  1  
        96   11   ASP  HA    H    5.50  .  1  
        97   11   ASP  HB2   H    2.56  .  2  
        98   11   ASP  HB3   H    2.14  .  2  
        99   11   ASP  C     C  176.0   .  1  
       100   11   ASP  CA    C   52.2   .  1  
       101   11   ASP  CB    C   43.2   .  1  
       102   11   ASP  N     N  121.2   .  1  
       103   12   VAL  H     H    9.73  .  1  
       104   12   VAL  HA    H    4.44  .  1  
       105   12   VAL  HB    H    2.08  .  1  
       106   12   VAL  HG1   H    0.78  .  1  
       107   12   VAL  HG2   H    0.78  .  1  
       108   12   VAL  C     C  174.5   .  1  
       109   12   VAL  CA    C   61.7   .  1  
       110   12   VAL  CB    C   32.5   .  1  
       111   12   VAL  CG1   C   24.2   .  2  
       112   12   VAL  CG2   C   20.2   .  2  
       113   12   VAL  N     N  124.5   .  1  
       114   13   LYS  H     H    8.56  .  1  
       115   13   LYS  HA    H    4.76  .  1  
       116   13   LYS  HB2   H    1.76  .  2  
       117   13   LYS  HB3   H    1.61  .  2  
       118   13   LYS  HG2   H    1.20  .  2  
       119   13   LYS  HG3   H    1.29  .  2  
       120   13   LYS  HD2   H    1.56  .  1  
       121   13   LYS  HD3   H    1.56  .  1  
       122   13   LYS  HE2   H    2.72  .  1  
       123   13   LYS  HE3   H    2.72  .  1  
       124   13   LYS  C     C  174.1   .  1  
       125   13   LYS  CA    C   53.2   .  1  
       126   13   LYS  CB    C   32.9   .  1  
       127   13   LYS  CG    C   25.6   .  1  
       128   13   LYS  CD    C   34.7   .  1  
       129   13   LYS  CE    C   41.7   .  1  
       130   13   LYS  N     N  127.6   .  1  
       131   14   PRO  HA    H    5.42  .  1  
       132   14   PRO  HB2   H    2.17  .  2  
       133   14   PRO  HB3   H    2.46  .  2  
       134   14   PRO  HG2   H    1.75  .  2  
       135   14   PRO  HG3   H    2.60  .  2  
       136   14   PRO  HD2   H    3.57  .  2  
       137   14   PRO  HD3   H    3.73  .  2  
       138   14   PRO  C     C  176.4   .  1  
       139   14   PRO  CA    C   61.0   .  1  
       140   14   PRO  CB    C   33.4   .  1  
       141   14   PRO  CG    C   26.2   .  1  
       142   14   PRO  CD    C   50.9   .  1  
       143   15   TRP  H     H    6.71  .  1  
       144   15   TRP  HA    H    4.22  .  1  
       145   15   TRP  HB2   H    2.76  .  1  
       146   15   TRP  HB3   H    3.27  .  1  
       147   15   TRP  HD1   H    6.78  .  1  
       148   15   TRP  HE1   H    9.42  .  1  
       149   15   TRP  HE3   H    7.56  .  1  
       150   15   TRP  HZ2   H    7.54  .  1  
       151   15   TRP  HZ3   H    7.29  .  1  
       152   15   TRP  HH2   H    7.16  .  1  
       153   15   TRP  C     C  176.5   .  1  
       154   15   TRP  CA    C   60.3   .  1  
       155   15   TRP  CB    C   30.0   .  1  
       156   15   TRP  N     N  116.4   .  1  
       157   15   TRP  NE1   N  129.1   .  1  
       158   16   ASP  H     H    8.06  .  1  
       159   16   ASP  HA    H    4.53  .  1  
       160   16   ASP  HB2   H    3.03  .  1  
       161   16   ASP  HB3   H    3.03  .  1  
       162   16   ASP  C     C  175.4   .  1  
       163   16   ASP  CA    C   53.5   .  1  
       164   16   ASP  CB    C   40.9   .  1  
       165   16   ASP  N     N  112.7   .  1  
       166   17   ASP  H     H    8.77  .  1  
       167   17   ASP  HA    H    4.30  .  1  
       168   17   ASP  HB2   H    2.52  .  2  
       169   17   ASP  HB3   H    2.89  .  2  
       170   17   ASP  C     C  176.1   .  1  
       171   17   ASP  CA    C   54.9   .  1  
       172   17   ASP  CB    C   39.5   .  1  
       173   17   ASP  N     N  115.1   .  1  
       174   18   GLU  H     H    8.70  .  1  
       175   18   GLU  HA    H    4.38  .  1  
       176   18   GLU  HB2   H    2.12  .  2  
       177   18   GLU  HB3   H    1.90  .  2  
       178   18   GLU  HG2   H    2.10  .  2  
       179   18   GLU  HG3   H    2.25  .  2  
       180   18   GLU  C     C  177.2   .  1  
       181   18   GLU  CA    C   55.4   .  1  
       182   18   GLU  CB    C   30.0   .  1  
       183   18   GLU  CG    C   36.4   .  1  
       184   18   GLU  N     N  119.7   .  1  
       185   19   THR  H     H    7.64  .  1  
       186   19   THR  HA    H    4.07  .  1  
       187   19   THR  HB    H    4.66  .  1  
       188   19   THR  HG1   H    5.62  .  1  
       189   19   THR  HG2   H    1.66  .  1  
       190   19   THR  C     C  174.2   .  1  
       191   19   THR  CA    C   64.5   .  1  
       192   19   THR  CB    C   69.6   .  1  
       193   19   THR  CG2   C   23.3   .  1  
       194   19   THR  N     N  119.9   .  1  
       195   20   ASP  H     H    8.89  .  1  
       196   20   ASP  HA    H    4.45  .  1  
       197   20   ASP  HB2   H    2.97  .  2  
       198   20   ASP  HB3   H    2.67  .  2  
       199   20   ASP  C     C  176.1   .  1  
       200   20   ASP  CA    C   53.9   .  1  
       201   20   ASP  CB    C   40.5   .  1  
       202   20   ASP  N     N  126.8   .  1  
       203   21   MET  H     H    8.70  .  1  
       204   21   MET  HA    H    4.49  .  1  
       205   21   MET  HB2   H    2.02  .  2  
       206   21   MET  HB3   H    1.94  .  2  
       207   21   MET  HG2   H    2.63  .  2  
       208   21   MET  HG3   H    2.73  .  2  
       209   21   MET  HE    H    1.81  .  2  
       210   21   MET  C     C  180.3   .  1  
       211   21   MET  CA    C   54.9   .  1  
       212   21   MET  CB    C   28.9   .  1  
       213   21   MET  CG    C   32.0   .  1  
       214   21   MET  CE    C   16.3   .  1  
       215   21   MET  N     N  125.7   .  1  
       216   22   ALA  H     H    8.30  .  1  
       217   22   ALA  HA    H    4.18  .  1  
       218   22   ALA  HB    H    1.42  .  1  
       219   22   ALA  C     C  180.6   .  1  
       220   22   ALA  CA    C   54.6   .  1  
       221   22   ALA  CB    C   17.1   .  1  
       222   22   ALA  N     N  126.1   .  1  
       223   23   LYS  H     H    7.54  .  1  
       224   23   LYS  HA    H    3.79  .  1  
       225   23   LYS  HB2   H    1.44  .  2  
       226   23   LYS  HB3   H    1.30  .  2  
       227   23   LYS  HG2   H    1.53  .  1  
       228   23   LYS  HG3   H    1.53  .  1  
       229   23   LYS  HD2   H    1.03  .  2  
       230   23   LYS  HD3   H    1.18  .  2  
       231   23   LYS  HE2   H    2.82  .  1  
       232   23   LYS  HE3   H    2.82  .  1  
       233   23   LYS  C     C  178.4   .  1  
       234   23   LYS  CA    C   57.4   .  1  
       235   23   LYS  CB    C   31.2   .  1  
       236   23   LYS  CG    C   27.9   .  1  
       237   23   LYS  CD    C   24.6   .  1  
       238   23   LYS  CE    C   41.7   .  1  
       239   23   LYS  N     N  120.7   .  1  
       240   24   LEU  H     H    7.88  .  1  
       241   24   LEU  HA    H    3.22  .  1  
       242   24   LEU  HB2   H    1.72  .  1  
       243   24   LEU  HB3   H    1.53  .  1  
       244   24   LEU  HG    H    1.29  .  1  
       245   24   LEU  HD1   H    0.62  .  2  
       246   24   LEU  HD2   H    0.81  .  2  
       247   24   LEU  C     C  177.6   .  1  
       248   24   LEU  CA    C   60.0   .  1  
       249   24   LEU  CB    C   42.2   .  1  
       250   24   LEU  CG    C   27.3   .  1  
       251   24   LEU  CD1   C   25.7   .  2  
       252   24   LEU  CD2   C   26.4   .  2  
       253   24   LEU  N     N  120.6   .  1  
       254   25   GLU  H     H    7.71  .  1  
       255   25   GLU  HA    H    3.23  .  1  
       256   25   GLU  HB2   H    1.88  .  2  
       257   25   GLU  HB3   H    1.78  .  2  
       258   25   GLU  HG2   H    1.78  .  2  
       259   25   GLU  HG3   H    2.06  .  2  
       260   25   GLU  C     C  176.5   .  1  
       261   25   GLU  CA    C   59.6   .  1  
       262   25   GLU  CB    C   28.1   .  1  
       263   25   GLU  CG    C   35.3   .  1  
       264   25   GLU  N     N  118.7   .  1  
       265   26   GLU  H     H    7.76  .  1  
       266   26   GLU  HA    H    3.61  .  1  
       267   26   GLU  HB2   H    1.88  .  2  
       268   26   GLU  HB3   H    1.78  .  2  
       269   26   GLU  HG2   H    1.94  .  2  
       270   26   GLU  HG3   H    2.16  .  2  
       271   26   GLU  C     C  179.3   .  1  
       272   26   GLU  CA    C   59.0   .  1  
       273   26   GLU  CB    C   29.1   .  1  
       274   26   GLU  CG    C   35.8   .  1  
       275   26   GLU  N     N  119.3   .  1  
       276   27   CYS  H     H    7.73  .  1  
       277   27   CYS  HA    H    3.34  .  1  
       278   27   CYS  HB2   H    0.42  .  2  
       279   27   CYS  HB3   H    2.39  .  2  
       280   27   CYS  C     C  177.3   .  1  
       281   27   CYS  CA    C   63.3   .  1  
       282   27   CYS  CB    C   23.8   .  1  
       283   27   CYS  N     N  116.6   .  1  
       284   28   VAL  H     H    7.42  .  1  
       285   28   VAL  HA    H    3.08  .  1  
       286   28   VAL  HB    H    1.50  .  1  
       287   28   VAL  HG1   H   -0.03  .  2  
       288   28   VAL  HG2   H    0.71  .  2  
       289   28   VAL  C     C  175.5   .  1  
       290   28   VAL  CA    C   67.0   .  1  
       291   28   VAL  CB    C   30.8   .  1  
       292   28   VAL  CG1   C   21.3   .  2  
       293   28   VAL  CG2   C   22.7   .  2  
       294   28   VAL  N     N  120.8   .  1  
       295   29   ARG  H     H    7.70  .  1  
       296   29   ARG  HA    H    2.62  .  1  
       297   29   ARG  HB2   H    1.24  .  2  
       298   29   ARG  HB3   H    1.51  .  2  
       299   29   ARG  HG2   H    0.88  .  2  
       300   29   ARG  HG3   H    1.11  .  2  
       301   29   ARG  HE    H    9.08  .  1  
       302   29   ARG  C     C  176.3   .  1  
       303   29   ARG  CA    C   57.5   .  1  
       304   29   ARG  CB    C   28.9   .  1  
       305   29   ARG  CG    C   29.1   .  1  
       306   29   ARG  N     N  111.8   .  1  
       307   29   ARG  NE    N   86.7   .  1  
       308   30   SER  H     H    7.41  .  1  
       309   30   SER  HA    H    4.26  .  1  
       310   30   SER  HB2   H    3.96  .  2  
       311   30   SER  HB3   H    4.01  .  2  
       312   30   SER  HG    H    6.58  .  1  
       313   30   SER  C     C  174.9   .  1  
       314   30   SER  CA    C   59.2   .  1  
       315   30   SER  CB    C   62.9   .  1  
       316   30   SER  N     N  114.1   .  1  
       317   31   ILE  H     H    7.64  .  1  
       318   31   ILE  HA    H    3.95  .  1  
       319   31   ILE  HB    H    2.44  .  1  
       320   31   ILE  HG12  H    2.11  .  2  
       321   31   ILE  HG13  H    1.28  .  2  
       322   31   ILE  HG2   H    0.86  .  1  
       323   31   ILE  HD1   H    1.14  .  1  
       324   31   ILE  C     C  175.5   .  1  
       325   31   ILE  CA    C   62.8   .  1  
       326   31   ILE  CB    C   37.2   .  1  
       327   31   ILE  CG1   C   27.7   .  1  
       328   31   ILE  CG2   C   15.5   .  1  
       329   31   ILE  CD1   C   15.7   .  1  
       330   31   ILE  N     N  125.7   .  1  
       331   32   GLN  H     H    8.48  .  1  
       332   32   GLN  HA    H    4.86  .  1  
       333   32   GLN  HB2   H    1.91  .  2  
       334   32   GLN  HB3   H    2.05  .  2  
       335   32   GLN  HG2   H    2.35  .  2  
       336   32   GLN  HG3   H    2.42  .  2  
       337   32   GLN  HE21  H    6.61  .  2  
       338   32   GLN  HE22  H    7.13  .  2  
       339   32   GLN  C     C  174.7   .  1  
       340   32   GLN  CA    C   53.5   .  1  
       341   32   GLN  CB    C   31.2   .  1  
       342   32   GLN  CG    C   33.5   .  1  
       343   32   GLN  N     N  128.0   .  1  
       344   32   GLN  NE2   N  110.4   .  1  
       345   33   ALA  H     H    8.67  .  1  
       346   33   ALA  HA    H    4.35  .  1  
       347   33   ALA  HB    H    1.14  .  1  
       348   33   ALA  C     C  175.8   .  1  
       349   33   ALA  CA    C   51.3   .  1  
       350   33   ALA  CB    C   21.1   .  1  
       351   33   ALA  N     N  125.1   .  1  
       352   34   ASP  H     H    8.39  .  1  
       353   34   ASP  HA    H    4.32  .  1  
       354   34   ASP  HB2   H    2.48  .  2  
       355   34   ASP  HB3   H    2.56  .  2  
       356   34   ASP  C     C  176.3   .  1  
       357   34   ASP  CA    C   55.2   .  1  
       358   34   ASP  CB    C   39.9   .  1  
       359   34   ASP  N     N  121.8   .  1  
       360   35   GLY  H     H    8.40  .  1  
       361   35   GLY  HA2   H    3.54  .  2  
       362   35   GLY  HA3   H    4.04  .  2  
       363   35   GLY  C     C  172.3   .  1  
       364   35   GLY  CA    C   45.1   .  1  
       365   35   GLY  N     N  111.4   .  1  
       366   36   LEU  H     H    7.55  .  1  
       367   36   LEU  HA    H    4.80  .  1  
       368   36   LEU  HB2   H    1.85  .  1  
       369   36   LEU  HB3   H    0.88  .  1  
       370   36   LEU  HG    H    0.57  .  1  
       371   36   LEU  HD1   H    0.31  .  2  
       372   36   LEU  HD2   H   -0.14  .  2  
       373   36   LEU  C     C  175.3   .  1  
       374   36   LEU  CA    C   53.5   .  1  
       375   36   LEU  CB    C   44.9   .  1  
       376   36   LEU  CG    C   27.8   .  1  
       377   36   LEU  CD1   C   25.4   .  2  
       378   36   LEU  CD2   C   23.8   .  2  
       379   36   LEU  N     N  120.5   .  1  
       380   37   VAL  H     H    8.39  .  1  
       381   37   VAL  HA    H    4.29  .  1  
       382   37   VAL  HB    H    1.82  .  1  
       383   37   VAL  HG1   H    0.85  .  1  
       384   37   VAL  HG2   H    0.85  .  1  
       385   37   VAL  C     C  175.6   .  1  
       386   37   VAL  CA    C   60.8   .  1  
       387   37   VAL  CB    C   34.7   .  1  
       388   37   VAL  CG1   C   18.5   .  2  
       389   37   VAL  CG2   C   20.6   .  2  
       390   37   VAL  N     N  126.8   .  1  
       391   38   TRP  H     H    8.77  .  1  
       392   38   TRP  HA    H    4.70  .  1  
       393   38   TRP  HB2   H    3.21  .  2  
       394   38   TRP  HB3   H    3.34  .  2  
       395   38   TRP  HD1   H    7.38  .  1  
       396   38   TRP  HE1   H   10.15  .  1  
       397   38   TRP  HE3   H    7.52  .  1  
       398   38   TRP  HZ2   H    7.12  .  1  
       399   38   TRP  HZ3   H    6.59  .  1  
       400   38   TRP  HH2   H    6.69  .  1  
       401   38   TRP  C     C  177.1   .  1  
       402   38   TRP  CA    C   57.9   .  1  
       403   38   TRP  CB    C   30.8   .  1  
       404   38   TRP  N     N  128.2   .  1  
       405   38   TRP  NE1   N  129.1   .  1  
       406   39   GLY  H     H    9.24  .  1  
       407   39   GLY  HA2   H    4.58  .  2  
       408   39   GLY  HA3   H    3.68  .  2  
       409   39   GLY  C     C  173.9   .  1  
       410   39   GLY  CA    C   43.6   .  1  
       411   39   GLY  N     N  113.7   .  1  
       412   40   SER  H     H    8.45  .  1  
       413   40   SER  HA    H    4.47  .  1  
       414   40   SER  HB2   H    3.88  .  1  
       415   40   SER  HB3   H    3.88  .  1  
       416   40   SER  C     C  172.7   .  1  
       417   40   SER  CA    C   58.1   .  1  
       418   40   SER  CB    C   64.2   .  1  
       419   40   SER  N     N  119.5   .  1  
       420   41   SER  H     H    8.59  .  1  
       421   41   SER  HA    H    5.49  .  1  
       422   41   SER  HB2   H    3.76  .  2  
       423   41   SER  HB3   H    3.43  .  2  
       424   41   SER  C     C  173.4   .  1  
       425   41   SER  CA    C   55.9   .  1  
       426   41   SER  CB    C   66.8   .  1  
       427   41   SER  N     N  113.3   .  1  
       428   42   LYS  H     H    8.75  .  1  
       429   42   LYS  HA    H    4.51  .  1  
       430   42   LYS  HB2   H    1.85  .  2  
       431   42   LYS  HB3   H    1.66  .  2  
       432   42   LYS  HG2   H    1.19  .  2  
       433   42   LYS  HG3   H    1.38  .  2  
       434   42   LYS  HD2   H    1.52  .  1  
       435   42   LYS  HD3   H    1.52  .  1  
       436   42   LYS  HE2   H    2.85  .  1  
       437   42   LYS  HE3   H    2.85  .  1  
       438   42   LYS  C     C  174.0   .  1  
       439   42   LYS  CA    C   54.9   .  1  
       440   42   LYS  CB    C   35.8   .  1  
       441   42   LYS  CG    C   23.3   .  1  
       442   42   LYS  CD    C   28.9   .  1  
       443   42   LYS  CE    C   41.7   .  1  
       444   42   LYS  N     N  116.8   .  1  
       445   43   LEU  H     H    8.43  .  1  
       446   43   LEU  HA    H    5.28  .  1  
       447   43   LEU  HB2   H    1.02  .  2  
       448   43   LEU  HB3   H    1.75  .  2  
       449   43   LEU  HG    H    1.62  .  1  
       450   43   LEU  HD1   H    0.72  .  2  
       451   43   LEU  HD2   H    0.80  .  2  
       452   43   LEU  C     C  177.3   .  1  
       453   43   LEU  CA    C   53.0   .  1  
       454   43   LEU  CB    C   42.6   .  1  
       455   43   LEU  CG    C   26.4   .  1  
       456   43   LEU  CD1   C   23.8   .  2  
       457   43   LEU  CD2   C   25.2   .  2  
       458   43   LEU  N     N  120.8   .  1  
       459   44   VAL  H     H    8.90  .  1  
       460   44   VAL  HA    H    4.57  .  1  
       461   44   VAL  HB    H    1.71  .  1  
       462   44   VAL  HG1   H    0.86  .  2  
       463   44   VAL  HG2   H    0.74  .  2  
       464   44   VAL  C     C  173.8   .  1  
       465   44   VAL  CA    C   58.6   .  1  
       466   44   VAL  CB    C   35.0   .  1  
       467   44   VAL  CG1   C   19.8   .  2  
       468   44   VAL  CG2   C   20.5   .  2  
       469   44   VAL  N     N  123.9   .  1  
       470   45   PRO  HA    H    4.55  .  1  
       471   45   PRO  HB2   H    1.96  .  2  
       472   45   PRO  HB3   H    2.30  .  2  
       473   45   PRO  HG2   H    1.85  .  2  
       474   45   PRO  HG3   H    2.15  .  2  
       475   45   PRO  HD2   H    3.76  .  2  
       476   45   PRO  HD3   H    3.81  .  2  
       477   45   PRO  C     C  176.9   .  1  
       478   45   PRO  CA    C   63.3   .  1  
       479   45   PRO  CB    C   32.0   .  1  
       480   45   PRO  CG    C   27.3   .  1  
       481   45   PRO  CD    C   51.1   .  1  
       482   46   VAL  H     H    8.49  .  1  
       483   46   VAL  HA    H    4.36  .  1  
       484   46   VAL  HB    H    2.13  .  1  
       485   46   VAL  HG1   H    0.74  .  2  
       486   46   VAL  HG2   H    0.83  .  2  
       487   46   VAL  C     C  175.5   .  1  
       488   46   VAL  CA    C   60.8   .  1  
       489   46   VAL  CB    C   32.5   .  1  
       490   46   VAL  CG1   C   19.8   .  2  
       491   46   VAL  CG2   C   21.0   .  2  
       492   46   VAL  N     N  118.1   .  1  
       493   47   GLY  H     H    7.67  .  1  
       494   47   GLY  HA2   H    4.05  .  2  
       495   47   GLY  HA3   H    3.68  .  2  
       496   47   GLY  CA    C   44.9   .  1  
       497   47   GLY  N     N  109.7   .  1  
       498   48   TYR  HA    H    4.18  .  1  
       499   48   TYR  HB2   H    3.15  .  1  
       500   48   TYR  HB3   H    3.01  .  1  
       501   48   TYR  HD1   H    7.04  .  1  
       502   48   TYR  HD2   H    7.04  .  1  
       503   48   TYR  HE1   H    6.80  .  1  
       504   48   TYR  HE2   H    6.80  .  1  
       505   48   TYR  C     C  175.9   .  1  
       506   48   TYR  CA    C   59.0   .  1  
       507   48   TYR  CB    C   35.4   .  1  
       508   49   GLY  H     H    8.28  .  1  
       509   49   GLY  HA2   H    4.07  .  1  
       510   49   GLY  HA3   H    3.57  .  1  
       511   49   GLY  C     C  173.7   .  1  
       512   49   GLY  CA    C   45.3   .  1  
       513   49   GLY  N     N  107.7   .  1  
       514   50   ILE  H     H    7.62  .  1  
       515   50   ILE  HA    H    4.11  .  1  
       516   50   ILE  HB    H    1.80  .  1  
       517   50   ILE  HG12  H    0.87  .  2  
       518   50   ILE  HG13  H    1.52  .  2  
       519   50   ILE  HG2   H    0.66  .  1  
       520   50   ILE  HD1   H    0.74  .  1  
       521   50   ILE  C     C  175.4   .  1  
       522   50   ILE  CA    C   60.4   .  1  
       523   50   ILE  CB    C   38.8   .  1  
       524   50   ILE  CG1   C   27.5   .  1  
       525   50   ILE  CG2   C   17.1   .  1  
       526   50   ILE  CD1   C   12.4   .  1  
       527   50   ILE  N     N  119.5   .  1  
       528   51   LYS  H     H    8.76  .  1  
       529   51   LYS  HA    H    4.93  .  1  
       530   51   LYS  HB2   H    1.51  .  1  
       531   51   LYS  HB3   H    1.51  .  1  
       532   51   LYS  HG2   H    1.11  .  2  
       533   51   LYS  HG3   H    1.38  .  2  
       534   51   LYS  HD2   H    1.51  .  1  
       535   51   LYS  HD3   H    1.51  .  1  
       536   51   LYS  HE2   H    2.89  .  1  
       537   51   LYS  HE3   H    2.89  .  1  
       538   51   LYS  C     C  174.4   .  1  
       539   51   LYS  CA    C   54.4   .  1  
       540   51   LYS  CB    C   34.9   .  1  
       541   51   LYS  CG    C   25.0   .  1  
       542   51   LYS  CD    C   29.6   .  1  
       543   51   LYS  CE    C   41.7   .  1  
       544   51   LYS  N     N  126.4   .  1  
       545   52   LYS  H     H    8.65  .  1  
       546   52   LYS  HA    H    4.78  .  1  
       547   52   LYS  HB2   H    1.51  .  2  
       548   52   LYS  HB3   H    1.35  .  2  
       549   52   LYS  HG2   H    1.44  .  2  
       550   52   LYS  HG3   H    0.88  .  2  
       551   52   LYS  HD2   H    1.33  .  1  
       552   52   LYS  HD3   H    1.33  .  1  
       553   52   LYS  HE2   H    2.49  .  2  
       554   52   LYS  HE3   H    2.55  .  2  
       555   52   LYS  C     C  174.4   .  1  
       556   52   LYS  CA    C   53.0   .  1  
       557   52   LYS  CB    C   34.7   .  1  
       558   52   LYS  CG    C   24.2   .  1  
       559   52   LYS  CD    C   29.8   .  1  
       560   52   LYS  CE    C   42.2   .  1  
       561   52   LYS  N     N  115.1   .  1  
       562   53   LEU  H     H    8.56  .  1  
       563   53   LEU  HA    H    4.65  .  1  
       564   53   LEU  HB2   H    1.81  .  2  
       565   53   LEU  HB3   H    0.95  .  2  
       566   53   LEU  HG    H    1.16  .  1  
       567   53   LEU  HD1   H    0.47  .  2  
       568   53   LEU  HD2   H    0.70  .  2  
       569   53   LEU  C     C  174.5   .  1  
       570   53   LEU  CA    C   53.5   .  1  
       571   53   LEU  CB    C   43.7   .  1  
       572   53   LEU  CG    C   26.9   .  1  
       573   53   LEU  CD1   C   26.0   .  2  
       574   53   LEU  CD2   C   24.0   .  2  
       575   53   LEU  N     N  122.6   .  1  
       576   54   GLN  H     H    9.13  .  1  
       577   54   GLN  HA    H    5.91  .  1  
       578   54   GLN  HB2   H    1.96  .  2  
       579   54   GLN  HB3   H    1.63  .  2  
       580   54   GLN  HG2   H    1.92  .  2  
       581   54   GLN  HG3   H    2.31  .  2  
       582   54   GLN  HE21  H    6.60  .  2  
       583   54   GLN  HE22  H    9.02  .  2  
       584   54   GLN  C     C  175.1   .  1  
       585   54   GLN  CA    C   54.4   .  1  
       586   54   GLN  CB    C   31.9   .  1  
       587   54   GLN  CG    C   35.0   .  1  
       588   54   GLN  N     N  128.8   .  1  
       589   54   GLN  NE2   N  112.1   .  1  
       590   55   ILE  H     H    9.43  .  1  
       591   55   ILE  HA    H    5.02  .  1  
       592   55   ILE  HB    H    1.22  .  1  
       593   55   ILE  HG12  H    1.41  .  2  
       594   55   ILE  HG13  H    1.57  .  2  
       595   55   ILE  HG2   H    0.38  .  1  
       596   55   ILE  HD1   H    0.88  .  1  
       597   55   ILE  C     C  171.7   .  1  
       598   55   ILE  CA    C   58.1   .  1  
       599   55   ILE  CB    C   42.2   .  1  
       600   55   ILE  CG1   C   28.9   .  1  
       601   55   ILE  CG2   C   14.4   .  1  
       602   55   ILE  CD1   C   14.3   .  1  
       603   55   ILE  N     N  125.7   .  1  
       604   56   GLN  H     H    8.36  .  1  
       605   56   GLN  HA    H    5.39  .  1  
       606   56   GLN  HB2   H    2.25  .  2  
       607   56   GLN  HB3   H    1.96  .  2  
       608   56   GLN  HG2   H    2.25  .  2  
       609   56   GLN  HG3   H    2.32  .  2  
       610   56   GLN  HE21  H    6.76  .  2  
       611   56   GLN  HE22  H    7.48  .  2  
       612   56   GLN  C     C  175.5   .  1  
       613   56   GLN  CA    C   53.9   .  1  
       614   56   GLN  CB    C   31.0   .  1  
       615   56   GLN  CG    C   33.5   .  1  
       616   56   GLN  N     N  127.8   .  1  
       617   56   GLN  NE2   N  111.6   .  1  
       618   57   CYS  H     H    9.26  .  1  
       619   57   CYS  HA    H    5.06  .  1  
       620   57   CYS  HB2   H    1.96  .  2  
       621   57   CYS  HB3   H    2.80  .  2  
       622   57   CYS  C     C  172.3   .  1  
       623   57   CYS  CA    C   55.6   .  1  
       624   57   CYS  CB    C   31.4   .  1  
       625   57   CYS  N     N  118.1   .  1  
       626   58   VAL  H     H    8.48  .  1  
       627   58   VAL  HA    H    4.94  .  1  
       628   58   VAL  HB    H    1.66  .  1  
       629   58   VAL  HG1   H    0.75  .  2  
       630   58   VAL  HG2   H    0.82  .  2  
       631   58   VAL  C     C  176.1   .  1  
       632   58   VAL  CA    C   60.8   .  1  
       633   58   VAL  CB    C   33.7   .  1  
       634   58   VAL  CG1   C   21.3   .  1  
       635   58   VAL  CG2   C   21.3   .  1  
       636   58   VAL  N     N  121.4   .  1  
       637   59   VAL  H     H    8.81  .  1  
       638   59   VAL  HA    H    5.53  .  1  
       639   59   VAL  HB    H    1.96  .  1  
       640   59   VAL  HG1   H    0.61  .  2  
       641   59   VAL  HG2   H    0.71  .  2  
       642   59   VAL  C     C  175.7   .  1  
       643   59   VAL  CA    C   56.9   .  1  
       644   59   VAL  CB    C   34.9   .  1  
       645   59   VAL  CG1   C   22.6   .  2  
       646   59   VAL  CG2   C   19.0   .  2  
       647   59   VAL  N     N  119.3   .  1  
       648   60   GLU  H     H    8.23  .  1  
       649   60   GLU  HA    H    4.66  .  1  
       650   60   GLU  HB2   H    1.79  .  2  
       651   60   GLU  HB3   H    2.11  .  2  
       652   60   GLU  HG2   H    2.01  .  2  
       653   60   GLU  HG3   H    2.29  .  2  
       654   60   GLU  C     C  176.6   .  1  
       655   60   GLU  CA    C   55.0   .  1  
       656   60   GLU  CB    C   29.6   .  1  
       657   60   GLU  CG    C   36.6   .  1  
       658   60   GLU  N     N  120.8   .  1  
       659   61   ASP  H     H    8.31  .  1  
       660   61   ASP  HA    H    4.28  .  1  
       661   61   ASP  HB2   H    2.39  .  2  
       662   61   ASP  HB3   H    2.63  .  2  
       663   61   ASP  C     C  176.4   .  1  
       664   61   ASP  CA    C   56.7   .  1  
       665   61   ASP  CB    C   40.3   .  1  
       666   61   ASP  N     N  126.6   .  1  
       667   62   ASP  H     H    8.92  .  1  
       668   62   ASP  HA    H    4.32  .  1  
       669   62   ASP  HB2   H    2.65  .  2  
       670   62   ASP  HB3   H    2.56  .  2  
       671   62   ASP  C     C  176.3   .  1  
       672   62   ASP  CA    C   55.0   .  1  
       673   62   ASP  CB    C   39.9   .  1  
       674   62   ASP  N     N  114.9   .  1  
       675   63   LYS  H     H    7.92  .  1  
       676   63   LYS  HA    H    4.34  .  1  
       677   63   LYS  HB2   H    1.97  .  2  
       678   63   LYS  HB3   H    1.68  .  2  
       679   63   LYS  HE2   H    2.82  .  1  
       680   63   LYS  HE3   H    2.82  .  1  
       681   63   LYS  C     C  176.3   .  1  
       682   63   LYS  CA    C   57.5   .  1  
       683   63   LYS  CB    C   35.8   .  1  
       684   63   LYS  CE    C   41.7   .  1  
       685   63   LYS  N     N  117.0   .  1  
       686   64   VAL  H     H    7.62  .  1  
       687   64   VAL  HA    H    4.24  .  1  
       688   64   VAL  HB    H    1.74  .  1  
       689   64   VAL  HG1   H    0.67  .  1  
       690   64   VAL  HG2   H    0.67  .  1  
       691   64   VAL  C     C  173.6   .  1  
       692   64   VAL  CA    C   61.4   .  1  
       693   64   VAL  CB    C   34.7   .  1  
       694   64   VAL  CG1   C   21.3   .  2  
       695   64   VAL  CG2   C   23.6   .  2  
       696   64   VAL  N     N  118.9   .  1  
       697   65   GLY  H     H    7.41  .  1  
       698   65   GLY  HA2   H    4.45  .  2  
       699   65   GLY  HA3   H    3.80  .  2  
       700   65   GLY  C     C  174.8   .  1  
       701   65   GLY  CA    C   43.0   .  1  
       702   65   GLY  N     N  111.2   .  1  
       703   66   THR  H     H    8.70  .  1  
       704   66   THR  HA    H    3.69  .  1  
       705   66   THR  HB    H    4.07  .  1  
       706   66   THR  HG2   H    1.17  .  1  
       707   66   THR  C     C  176.4   .  1  
       708   66   THR  CA    C   65.4   .  1  
       709   66   THR  CB    C   67.2   .  1  
       710   66   THR  CG2   C   22.7   .  1  
       711   66   THR  N     N  111.0   .  1  
       712   67   ASP  H     H    8.66  .  1  
       713   67   ASP  HA    H    4.34  .  1  
       714   67   ASP  HB2   H    2.70  .  2  
       715   67   ASP  HB3   H    2.56  .  2  
       716   67   ASP  C     C  178.2   .  1  
       717   67   ASP  CA    C   56.5   .  1  
       718   67   ASP  CB    C   38.7   .  1  
       719   67   ASP  N     N  121.6   .  1  
       720   68   MET  H     H    7.61  .  1  
       721   68   MET  HA    H    4.16  .  1  
       722   68   MET  HB2   H    2.26  .  2  
       723   68   MET  HB3   H    2.11  .  2  
       724   68   MET  HG2   H    2.70  .  2  
       725   68   MET  HG3   H    2.45  .  2  
       726   68   MET  HE    H    1.99  .  1  
       727   68   MET  C     C  178.2   .  1  
       728   68   MET  CA    C   58.1   .  1  
       729   68   MET  CB    C   32.7   .  1  
       730   68   MET  CG    C   31.8   .  1  
       731   68   MET  CE    C   17.3   .  1  
       732   68   MET  N     N  121.8   .  1  
       733   69   LEU  H     H    7.39  .  1  
       734   69   LEU  HA    H    3.91  .  1  
       735   69   LEU  HB2   H    1.75  .  2  
       736   69   LEU  HB3   H    1.29  .  2  
       737   69   LEU  HG    H    1.60  .  1  
       738   69   LEU  HD1   H    0.69  .  2  
       739   69   LEU  HD2   H    0.62  .  2  
       740   69   LEU  C     C  177.6   .  1  
       741   69   LEU  CA    C   57.7   .  1  
       742   69   LEU  CB    C   41.4   .  1  
       743   69   LEU  CG    C   26.0   .  1  
       744   69   LEU  CD1   C   22.6   .  2  
       745   69   LEU  CD2   C   25.7   .  2  
       746   69   LEU  N     N  118.0   .  1  
       747   70   GLU  H     H    8.33  .  1  
       748   70   GLU  HA    H    4.14  .  1  
       749   70   GLU  HB2   H    2.10  .  2  
       750   70   GLU  HB3   H    2.04  .  2  
       751   70   GLU  HG2   H    2.17  .  2  
       752   70   GLU  HG3   H    2.23  .  2  
       753   70   GLU  C     C  179.4   .  1  
       754   70   GLU  CA    C   60.3   .  1  
       755   70   GLU  CB    C   29.1   .  1  
       756   70   GLU  CG    C   36.1   .  1  
       757   70   GLU  N     N  118.7   .  1  
       758   71   GLU  H     H    7.95  .  1  
       759   71   GLU  HA    H    3.80  .  1  
       760   71   GLU  HB2   H    2.11  .  1  
       761   71   GLU  HB3   H    2.11  .  1  
       762   71   GLU  HG2   H    2.12  .  2  
       763   71   GLU  HG3   H    2.29  .  2  
       764   71   GLU  C     C  178.3   .  1  
       765   71   GLU  CA    C   59.3   .  1  
       766   71   GLU  CB    C   29.3   .  1  
       767   71   GLU  CG    C   35.6   .  1  
       768   71   GLU  N     N  120.8   .  1  
       769   72   GLN  H     H    8.03  .  1  
       770   72   GLN  HA    H    3.95  .  1  
       771   72   GLN  HB2   H    1.99  .  2  
       772   72   GLN  HB3   H    2.17  .  2  
       773   72   GLN  HG2   H    2.47  .  1  
       774   72   GLN  HG3   H    2.47  .  1  
       775   72   GLN  HE21  H    6.69  .  2  
       776   72   GLN  HE22  H    7.36  .  2  
       777   72   GLN  C     C  177.9   .  1  
       778   72   GLN  CA    C   58.3   .  1  
       779   72   GLN  CB    C   28.5   .  1  
       780   72   GLN  CG    C   34.3   .  1  
       781   72   GLN  N     N  114.9   .  1  
       782   72   GLN  NE2   N  110.8   .  1  
       783   73   ILE  H     H    8.68  .  1  
       784   73   ILE  HA    H    3.91  .  1  
       785   73   ILE  HB    H    2.00  .  1  
       786   73   ILE  HG12  H    2.09  .  1  
       787   73   ILE  HG13  H    2.09  .  1  
       788   73   ILE  HG2   H    0.83  .  1  
       789   73   ILE  HD1   H    0.91  .  1  
       790   73   ILE  C     C  177.7   .  1  
       791   73   ILE  CA    C   65.6   .  1  
       792   73   ILE  CB    C   37.8   .  1  
       793   73   ILE  CG1   C   31.4   .  1  
       794   73   ILE  CG2   C   18.4   .  1  
       795   73   ILE  CD1   C   14.6   .  1  
       796   73   ILE  N     N  118.0   .  1  
       797   74   THR  H     H    8.04  .  1  
       798   74   THR  HA    H    3.75  .  1  
       799   74   THR  HB    H    4.32  .  1  
       800   74   THR  HG2   H    1.2   .  1  
       801   74   THR  C     C  175.6   .  1  
       802   74   THR  CA    C   64.0   .  1  
       803   74   THR  CB    C   68.7   .  1  
       804   74   THR  CG2   C   21.6   .  1  
       805   74   THR  N     N  106.0   .  1  
       806   75   ALA  H     H    6.87  .  1  
       807   75   ALA  HA    H    4.23  .  1  
       808   75   ALA  HB    H    1.26  .  1  
       809   75   ALA  C     C  179.6   .  1  
       810   75   ALA  CA    C   53.2   .  1  
       811   75   ALA  CB    C   17.7   .  1  
       812   75   ALA  N     N  121.4   .  1  
       813   76   PHE  H     H    7.22  .  1  
       814   76   PHE  HA    H    5.07  .  1  
       815   76   PHE  HB2   H    3.34  .  2  
       816   76   PHE  HB3   H    3.17  .  2  
       817   76   PHE  HD1   H    7.55  .  1  
       818   76   PHE  HD2   H    7.55  .  1  
       819   76   PHE  HE1   H    7.19  .  1  
       820   76   PHE  HE2   H    7.19  .  1  
       821   76   PHE  HZ    H    7.10  .  1  
       822   76   PHE  C     C  177.8   .  1  
       823   76   PHE  CA    C   56.9   .  1  
       824   76   PHE  CB    C   35.6   .  1  
       825   76   PHE  N     N  118.9   .  1  
       826   77   GLU  H     H    8.02  .  1  
       827   77   GLU  HA    H    4.43  .  1  
       828   77   GLU  HB2   H    2.18  .  1  
       829   77   GLU  HB3   H    2.18  .  1  
       830   77   GLU  HG2   H    2.38  .  1  
       831   77   GLU  HG3   H    2.38  .  1  
       832   77   GLU  C     C  177.3   .  1  
       833   77   GLU  CA    C   58.8   .  1  
       834   77   GLU  CB    C   30.0   .  1  
       835   77   GLU  CG    C   36.1   .  1  
       836   77   GLU  N     N  122.6   .  1  
       837   78   ASP  H     H    8.82  .  1  
       838   78   ASP  HA    H    4.26  .  1  
       839   78   ASP  HB2   H    2.03  .  2  
       840   78   ASP  HB3   H    1.83  .  2  
       841   78   ASP  C     C  176.3   .  1  
       842   78   ASP  CA    C   56.1   .  1  
       843   78   ASP  CB    C   39.5   .  1  
       844   78   ASP  N     N  117.6   .  1  
       845   79   TYR  H     H    7.64  .  1  
       846   79   TYR  HA    H    4.87  .  1  
       847   79   TYR  HB2   H    3.09  .  2  
       848   79   TYR  HB3   H    2.55  .  2  
       849   79   TYR  HD1   H    6.97  .  1  
       850   79   TYR  HD2   H    6.97  .  1  
       851   79   TYR  HE1   H    6.85  .  1  
       852   79   TYR  HE2   H    6.85  .  1  
       853   79   TYR  C     C  173.6   .  1  
       854   79   TYR  CA    C   58.8   .  1  
       855   79   TYR  CB    C   42.4   .  1  
       856   79   TYR  N     N  113.1   .  1  
       857   80   VAL  H     H    7.97  .  1  
       858   80   VAL  HA    H    3.56  .  1  
       859   80   VAL  HB    H    1.83  .  1  
       860   80   VAL  HG1   H    0.88  .  2  
       861   80   VAL  HG2   H    0.49  .  2  
       862   80   VAL  C     C  173.3   .  1  
       863   80   VAL  CA    C   62.3   .  1  
       864   80   VAL  CB    C   33.4   .  1  
       865   80   VAL  CG1   C   20.9   .  2  
       866   80   VAL  CG2   C   21.6   .  2  
       867   80   VAL  N     N  116.6   .  1  
       868   81   GLN  H     H    8.44  .  1  
       869   81   GLN  HA    H    2.66  .  1  
       870   81   GLN  HB2   H    0.97  .  2  
       871   81   GLN  HB3   H    0.19  .  2  
       872   81   GLN  HG2   H    1.59  .  2  
       873   81   GLN  HG3   H    1.71  .  2  
       874   81   GLN  HE21  H    6.91  .  2  
       875   81   GLN  HE22  H    7.17  .  2  
       876   81   GLN  C     C  175.6   .  1  
       877   81   GLN  CA    C   55.8   .  1  
       878   81   GLN  CB    C   28.8   .  1  
       879   81   GLN  CG    C   33.5   .  1  
       880   81   GLN  N     N  125.9   .  1  
       881   81   GLN  NE2   N  111.5   .  1  
       882   82   SER  H     H    7.24  .  1  
       883   82   SER  HA    H    4.19  .  1  
       884   82   SER  HB2   H    3.65  .  1  
       885   82   SER  HB3   H    3.65  .  1  
       886   82   SER  C     C  171.2   .  1  
       887   82   SER  CA    C   57.1   .  1  
       888   82   SER  CB    C   64.7   .  1  
       889   82   SER  N     N  108.3   .  1  
       890   83   MET  H     H    8.68  .  1  
       891   83   MET  HA    H    5.21  .  1  
       892   83   MET  HB2   H    1.94  .  2  
       893   83   MET  HB3   H    1.86  .  2  
       894   83   MET  HG2   H    2.18  .  2  
       895   83   MET  HG3   H    2.37  .  2  
       896   83   MET  HE    H    1.8   .  1  
       897   83   MET  C     C  173.4   .  1  
       898   83   MET  CA    C   54.0   .  1  
       899   83   MET  CB    C   38.3   .  1  
       900   83   MET  CG    C   30.6   .  1  
       901   83   MET  CE    C   17.7   .  1  
       902   83   MET  N     N  118.7   .  1  
       903   84   ASP  H     H    9.05  .  1  
       904   84   ASP  HA    H    4.99  .  1  
       905   84   ASP  HB2   H    2.39  .  1  
       906   84   ASP  HB3   H    2.52  .  1  
       907   84   ASP  C     C  174.9   .  1  
       908   84   ASP  CA    C   52.5   .  1  
       909   84   ASP  CB    C   45.1   .  1  
       910   84   ASP  N     N  122.6   .  1  
       911   85   VAL  H     H    8.83  .  1  
       912   85   VAL  HA    H    4.03  .  1  
       913   85   VAL  HB    H    2.03  .  1  
       914   85   VAL  HG1   H    0.84  .  1  
       915   85   VAL  HG2   H    0.84  .  1  
       916   85   VAL  C     C  175.2   .  1  
       917   85   VAL  CA    C   62.9   .  1  
       918   85   VAL  CB    C   30.9   .  1  
       919   85   VAL  CG1   C   21.1   .  2  
       920   85   VAL  N     N  123.0   .  1  
       921   86   ALA  H     H    9.04  .  1  
       922   86   ALA  HA    H    4.21  .  1  
       923   86   ALA  HB    H    1.11  .  1  
       924   86   ALA  C     C  177.8   .  1  
       925   86   ALA  CA    C   53.0   .  1  
       926   86   ALA  CB    C   19.0   .  1  
       927   86   ALA  N     N  130.6   .  1  
       928   87   ALA  H     H    7.88  .  1  
       929   87   ALA  HA    H    4.43  .  1  
       930   87   ALA  HB    H    1.33  .  1  
       931   87   ALA  C     C  174.8   .  1  
       932   87   ALA  CA    C   52.3   .  1  
       933   87   ALA  CB    C   21.5   .  1  
       934   87   ALA  N     N  117.8   .  1  
       935   88   PHE  H     H    8.33  .  1  
       936   88   PHE  HA    H    5.03  .  1  
       937   88   PHE  HB2   H    3.09  .  2  
       938   88   PHE  HB3   H    2.72  .  2  
       939   88   PHE  HD1   H    7.07  .  1  
       940   88   PHE  HD2   H    7.07  .  1  
       941   88   PHE  HZ    H    7.32  .  1  
       942   88   PHE  C     C  174.1   .  1  
       943   88   PHE  CA    C   56.9   .  1  
       944   88   PHE  CB    C   41.2   .  1  
       945   88   PHE  N     N  121.4   .  1  
       946   89   ASN  H     H    8.68  .  1  
       947   89   ASN  HA    H    4.96  .  1  
       948   89   ASN  HB2   H    2.64  .  2  
       949   89   ASN  HB3   H    2.51  .  2  
       950   89   ASN  HD21  H    6.82  .  2  
       951   89   ASN  HD22  H    7.50  .  2  
       952   89   ASN  C     C  173.5   .  1  
       953   89   ASN  CA    C   52.3   .  1  
       954   89   ASN  CB    C   41.9   .  1  
       955   89   ASN  N     N  122.7   .  1  
       956   89   ASN  ND2   N  112.9   .  1  
       957   90   LYS  H     H    8.55  .  1  
       958   90   LYS  HA    H    4.50  .  1  
       959   90   LYS  HB2   H    1.75  .  2  
       960   90   LYS  HB3   H    1.82  .  2  
       961   90   LYS  HG2   H    1.54  .  1  
       962   90   LYS  HG3   H    1.54  .  1  
       963   90   LYS  HD2   H    1.67  .  1  
       964   90   LYS  HD3   H    1.67  .  1  
       965   90   LYS  HE2   H    2.95  .  1  
       966   90   LYS  HE3   H    2.95  .  1  
       967   90   LYS  C     C  176.2   .  1  
       968   90   LYS  CA    C   56.3   .  1  
       969   90   LYS  CB    C   32.2   .  1  
       970   90   LYS  CG    C   30.8   .  1  
       971   90   LYS  CD    C   28.5   .  1  
       972   90   LYS  CE    C   41.8   .  1  
       973   90   LYS  N     N  123.4   .  1  
       974   91   ILE  H     H    7.96  .  1  
       975   91   ILE  HA    H    4.04  .  1  
       976   91   ILE  HB    H    1.69  .  1  
       977   91   ILE  HG12  H    1.26  .  2  
       978   91   ILE  HG13  H    0.83  .  2  
       979   91   ILE  HG2   H    0.76  .  1  
       980   91   ILE  HD1   H    0.70  .  1  
       981   91   ILE  C     C  176.3   .  1  
       982   91   ILE  CA    C   63.0   .  1  
       983   91   ILE  CB    C   39.2   .  1  
       984   91   ILE  CG1   C   27.3   .  1  
       985   91   ILE  CG2   C   17.7   .  1  
       986   91   ILE  CD1   C   13.8   .  1  
       987   91   ILE  N     N  127.8   .  1  

   stop_

save_


#######################################
#  Cited references within the entry  #
#######################################
save_citation_one
   _Saveframe_category   citation

   _Citation_full       
;
Wishart and Sykes, Meth. Enzymol. 239, 363-392 (1994).
;

save_

