data_5148

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

save_entry_information
   _Saveframe_category      entry_information

   _Entry_title            
;
NMR Structure of the [2Fe-2S] Ferredoxin Domain from Soluble Methane 
Monooxygenase Reductase and Interaction with its Hydroxylase 
;
   _BMRB_accession_number   5148
   _BMRB_flat_file_name     bmr5148.str
   _Entry_type              original
   _Submission_date         2001-09-12
   _Accession_date          2001-09-13
   _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 Muller    J. .  . 
      2 Lugovskoy A. A. . 
      3 Wagner    G. .  . 
      4 Lippard   S. J. . 

   stop_

   loop_
      _Saveframe_category_type
      _Saveframe_category_type_count

      assigned_chemical_shifts 1 

   stop_

   loop_
      _Data_type
      _Data_type_count

      "1H chemical shifts"  406 
      "13C chemical shifts" 312 
      "15N chemical shifts"  79 

   stop_

   loop_
      _Revision_date
      _Revision_keyword
      _Revision_author
      _Revision_detail

      2002-01-23 original author . 

   stop_

   _Original_release_date   2002-01-23

save_


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

save_entry_citation
   _Saveframe_category           entry_citation

   _Citation_full                .
   _Citation_title              
;
NMR Structure of the [2Fe-2S] Ferredoxin Domain from Soluble Methane 
Monooxygenase Reductase and Interaction with its Hydroxylase
;
   _Citation_status              published
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              21633978
   _PubMed_ID                    11772001

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Muller    J. .  . 
      2 Lugovskoy A. A. . 
      3 Wagner    G. .  . 
      4 Lippard   S. J. . 

   stop_

   _Journal_abbreviation         Biochemistry
   _Journal_volume               41
   _Journal_issue                1
   _Journal_CSD                  .
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_ISBN                    .
   _Conference_state_province    .
   _Conference_abstract_number   .
   _Page_first                   42
   _Page_last                    51
   _Year                         2002
   _Details                      .

   loop_
      _Keyword

      '[2Fe-2S] ferredoxin' 

   stop_

save_


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

save_system_MMOR
   _Saveframe_category         molecular_system

   _Mol_system_name           'METHANE MONOOXYGENASE COMPONENT C'
   _Abbreviation_common        MMOR
   _Enzyme_commission_number   1.14.13.25

   loop_
      _Mol_system_component_name
      _Mol_label

      'methane monooxygenase component C' $MMOR 
      'FE2/S2 CLUSTER'                    $FES  

   stop_

   _System_molecular_weight    .
   _System_physical_state      native
   _System_oligomer_state      monomer
   _System_paramagnetic        yes
   _System_thiol_state        'other bound, and free'
   _Database_query_date        .
   _Details                    .

save_


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

save_MMOR
   _Saveframe_category                          monomeric_polymer

   _Mol_type                                    polymer
   _Mol_polymer_class                           protein
   _Name_common                                '[2Fe-2S] domain of Methane Monooxygenase Reductase'
   _Abbreviation_common                         MMOR-Fd
   _Molecular_mass                              .
   _Mol_thiol_state                            'other bound, and free'
   _Details                                     .

   	##############################
   	#  Polymer residue sequence  #
   	##############################
   
      _Residue_count                               98
   _Mol_residue_sequence                       
;
MQRVHTITAVTEDGESLRFE
CRSDEDVITAALRQNIFLMS
SCREGGCATCKALCSEGDYD
LKGCSVQALPPEEEEEGLVL
LCRTYPKTDLEIELPYTH
;

   loop_
      _Residue_seq_code
      _Residue_label

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

   stop_

   _Sequence_homology_query_date                .
   _Sequence_homology_query_revised_last_date   2014-03-02

   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 1JQ4         "[2fe-2s] Domain Of Methane Monooxygenase Reductase From Methylococcus Capsulatus (Bath)"                                         100.00  98 100.00 100.00 3.75e-64 
      GB  AAB62391     "methane monooxygenase component C [Methylococcus capsulatus]"                                                                    100.00 348 100.00 100.00 4.42e-62 
      GB  AAU92722     "methane monooxygenase, C subunit [Methylococcus capsulatus str. Bath]"                                                           100.00 348 100.00 100.00 4.42e-62 
      REF WP_010960487 "methane monooxygenase [Methylococcus capsulatus]"                                                                                100.00 348 100.00 100.00 4.42e-62 
      REF YP_113665    "methane monooxygenase subunit C [Methylococcus capsulatus str. Bath]"                                                            100.00 348 100.00 100.00 4.42e-62 
      SP  P22868       "RecName: Full=Methane monooxygenase component C; AltName: Full=Methane hydroxylase; AltName: Full=Methane monooxygenase reducta" 100.00 348 100.00 100.00 4.42e-62 

   stop_

save_


    #############
    #  Ligands  #
    #############

save_FES
   _Saveframe_category             ligand

   _Mol_type                       non-polymer
   _Name_common                   "FES (FE2/S2 (INORGANIC) CLUSTER)"
   _BMRB_code                      .
   _PDB_code                       FES
   _Molecular_mass                 175.820
   _Mol_charge                     0
   _Mol_paramagnetic               .
   _Mol_aromatic                   no
   _Details                       
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Mon Jun 13 14:37:28 2011
;

   loop_
      _Atom_name
      _PDB_atom_name
      _Atom_type
      _Atom_chirality
      _Atom_charge
      _Atom_oxidation_number
      _Atom_unpaired_electrons

      FE1 FE1 FE . 0 . ? 
      FE2 FE2 FE . 0 . ? 
      S1  S1  S  . 0 . ? 
      S2  S2  S  . 0 . ? 

   stop_

   loop_
      _Bond_order
      _Bond_atom_one_atom_name
      _Bond_atom_two_atom_name
      _PDB_bond_atom_one_atom_name
      _PDB_bond_atom_two_atom_name

      SING FE1 S1 ? ? 
      SING FE1 S2 ? ? 
      SING FE2 S1 ? ? 
      SING FE2 S2 ? ? 

   stop_

   _Mol_thiol_state                .
   _Sequence_homology_query_date   .

save_


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

save_natural_source
   _Saveframe_category   natural_source


   loop_
      _Mol_label
      _Organism_name_common
      _NCBI_taxonomy_ID
      _Superkingdom
      _Kingdom
      _Genus
      _Species
      _Strain

      $MMOR 'Methylococcus capsulatus' 414 Bacteria . Methylococcus capsulatus (Bath) 

   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

      $MMOR 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pRED-Fd 

   stop_

save_


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

save_sample_1
   _Saveframe_category   sample

   _Sample_type          solution
   _Details             
;
A proprietary protease inhibitor tablet has been used 
("Complete Mini EDTA free" from Roche Diagnostics, Germany).
;

   loop_
      _Mol_label
      _Concentration_value
      _Concentration_value_units
      _Isotopic_labeling

      $MMOR                      0.5 mM '[U-13C; U-15N; U-70% 2H]' 
      'sodium phosphate buffer' 50   mM  .                         
       DTT                       1   mM  .                         
      'sodium dithionite'        1.5 mM  .                         
       NaN3                      0.1 %   .                         
      'protease inhibitor'       1   x   .                         

   stop_

save_


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

save_FELIX
   _Saveframe_category   software

   _Name                 FELIX
   _Version              97.0

   loop_
      _Task

      processing 

   stop_

   _Details              MSI

save_


save_DYANA
   _Saveframe_category   software

   _Name                 DYANA
   _Version              1.5

   loop_
      _Task

      'structure solution' 

   stop_

   _Details              Guentert

save_


save_X-PLOR
   _Saveframe_category   software

   _Name                 X-PLOR
   _Version              3.84

   loop_
      _Task

      refinement 

   stop_

   _Details              Brunger

save_


save_XEasy
   _Saveframe_category   software

   _Name                 XEasy
   _Version              1.3.9

   loop_
      _Task

      'data analysis' 

   stop_

   _Details             'Xia, Bartels'

save_


save_VNMR
   _Saveframe_category   software

   _Name                 VNMR
   _Version              5.1A

   loop_
      _Task

      collection 

   stop_

   _Details              Varian

save_


save_XWINNMR
   _Saveframe_category   software

   _Name                 XWINNMR
   _Version              2.5

   loop_
      _Task

      collection 

   stop_

   _Details              Bruker

save_


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

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

save_NMR_spectrometer_1
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Varian
   _Model                UNITY-INOVA
   _Field_strength       750
   _Details              .

save_


save_NMR_spectrometer_2
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Varian
   _Model                INOVA
   _Field_strength       500
   _Details              .

save_


save_NMR_spectrometer_3
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Varian
   _Model                Unity
   _Field_strength       500
   _Details              .

save_


save_NMR_spectrometer_4
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Varian
   _Model                Unity-Plus
   _Field_strength       400
   _Details              .

save_


save_NMR_spectrometer_5
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                DRX
   _Field_strength       600
   _Details              .

save_


save_NMR_spectrometer_6
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                DRX
   _Field_strength       500
   _Details              .

save_


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

save_HNCA_1
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HNCA
   _Sample_label        $sample_1

save_


save_HN(CO)CA_2
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HN(CO)CA
   _Sample_label        $sample_1

save_


save_HN(CA)CB_3
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HN(CA)CB
   _Sample_label        $sample_1

save_


save_HN(COCA)CB_4
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HN(COCA)CB
   _Sample_label        $sample_1

save_


save_HNCO_5
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HNCO
   _Sample_label        $sample_1

save_


save_HCCH-TOCSY_6
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HCCH-TOCSY
   _Sample_label        $sample_1

save_


save_15N_NOESY-HSQC_7
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '15N NOESY-HSQC'
   _Sample_label        $sample_1

save_


save_13C_NOESY-HSQC_8
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '13C NOESY-HSQC'
   _Sample_label        $sample_1

save_


save_NOESY_9
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      NOESY
   _Sample_label        $sample_1

save_


save_15N_TOCSY-HSQC_10
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '15N TOCSY-HSQC'
   _Sample_label        $sample_1

save_


save_15N_HSQC_11
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '15N HSQC'
   _Sample_label        $sample_1

save_


save_H(C-CO)NH-TOCSY_12
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      H(C-CO)NH-TOCSY
   _Sample_label        $sample_1

save_


save_(H)C(CO)NH-TOCSY_13
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      (H)C(CO)NH-TOCSY
   _Sample_label        $sample_1

save_


save_NMR_spec_expt__0_1
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        HNCA
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_2
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        HN(CO)CA
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_3
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        HN(CA)CB
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_4
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        HN(COCA)CB
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_5
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        HNCO
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_6
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        HCCH-TOCSY
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_7
   _Saveframe_category                     NMR_applied_experiment

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

save_


save_NMR_spec_expt__0_8
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                       '13C NOESY-HSQC'
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_9
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        NOESY
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_10
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                       '15N TOCSY-HSQC'
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_11
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                       '15N HSQC'
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_12
   _Saveframe_category                     NMR_applied_experiment

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

save_


save_NMR_spec_expt__0_13
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        (H)C(CO)NH-TOCSY
   _BMRB_pulse_sequence_accession_number   .
   _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 0.1 na  
       temperature     298   1   K   
      'ionic strength'  50    .  mM  
       pressure          1    .  atm 

   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
      _Indirect_shift_ratio_citation_label
      _Correction_value_citation_label

      DSS H  1 'methyl protons' ppm 0.0 internal direct   . . . 1.000000000 $entry_citation $entry_citation 
      DSS N 15 'methyl protons' ppm 0.0 .        indirect . . . 0.101329118 $entry_citation $entry_citation 
      DSS C 13 'methyl protons' ppm 0.0 .        indirect . . . 0.251449530 $entry_citation $entry_citation 

   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_cs_MMOR
   _Saveframe_category               assigned_chemical_shifts

   _Details                          .

   loop_
      _Experiment_label

       HNCA             
       HN(CO)CA         
       HN(CA)CB         
       HN(COCA)CB       
       HNCO             
       HCCH-TOCSY       
      '15N NOESY-HSQC'  
      '13C NOESY-HSQC'  
       NOESY            
      '15N TOCSY-HSQC'  
      '15N HSQC'        
       H(C-CO)NH-TOCSY  
       (H)C(CO)NH-TOCSY 

   stop_

   loop_
      _Sample_label

      $sample_1 

   stop_

   _Sample_conditions_label         $condition_1
   _Chem_shift_reference_set_label  $chemical_shift_reference
   _Mol_system_component_name       'methane monooxygenase component C'
   _Text_data_format                 .
   _Text_data                        .

   loop_
      _Atom_shift_assign_ID
      _Residue_author_seq_code
      _Residue_seq_code
      _Residue_label
      _Atom_name
      _Atom_type
      _Chem_shift_value
      _Chem_shift_value_error
      _Chem_shift_ambiguity_code

        1 .  2 GLN CA   C  55.172 . 1 
        2 .  2 GLN HA   H   4.66  . 1 
        3 .  2 GLN CB   C  28.825 . 1 
        4 .  2 GLN C    C 175.033 . 1 
        5 .  3 ARG N    N 123.131 . 1 
        6 .  3 ARG H    H   8.32  . 1 
        7 .  3 ARG CA   C  55.201 . 1 
        8 .  3 ARG HA   H   4.21  . 1 
        9 .  3 ARG CB   C  30.763 . 1 
       10 .  3 ARG HB2  H   1.547 . 1 
       11 .  3 ARG CG   C  26.913 . 1 
       12 .  3 ARG HG2  H   1.424 . 2 
       13 .  3 ARG HG3  H   1.39  . 2 
       14 .  3 ARG CD   C  43.041 . 1 
       15 .  3 ARG HD2  H   3.117 . 1 
       16 .  3 ARG C    C 174.511 . 1 
       17 .  4 VAL N    N 119.862 . 1 
       18 .  4 VAL H    H   7.768 . 1 
       19 .  4 VAL CA   C  60.918 . 1 
       20 .  4 VAL HA   H   3.906 . 1 
       21 .  4 VAL CB   C  32.702 . 1 
       22 .  4 VAL HB   H   1.689 . 1 
       23 .  4 VAL HG1  H   0.676 . 1 
       24 .  4 VAL HG2  H   0.68  . 1 
       25 .  4 VAL CG1  C  20.804 . 1 
       26 .  4 VAL CG2  C  20.747 . 1 
       27 .  4 VAL C    C 173.685 . 1 
       28 .  5 HIS N    N 125.934 . 1 
       29 .  5 HIS H    H   8.128 . 1 
       30 .  5 HIS CA   C  54.206 . 1 
       31 .  5 HIS HA   H   4.748 . 1 
       32 .  5 HIS CB   C  32.218 . 1 
       33 .  5 HIS HB2  H   2.874 . 2 
       34 .  5 HIS HB3  H   2.47  . 2 
       35 .  5 HIS HD2  H   6.389 . 1 
       36 .  5 HIS C    C 173.989 . 1 
       37 .  6 THR N    N 117.95  . 1 
       38 .  6 THR H    H   9.016 . 1 
       39 .  6 THR CA   C  62.409 . 1 
       40 .  6 THR HA   H   4.326 . 1 
       41 .  6 THR CB   C  68.815 . 1 
       42 .  6 THR HB   H   3.653 . 1 
       43 .  6 THR HG2  H   0.853 . 1 
       44 .  6 THR CG2  C  21.591 . 1 
       45 .  6 THR C    C 173.076 . 1 
       46 .  7 ILE N    N 129.224 . 1 
       47 .  7 ILE H    H   9.137 . 1 
       48 .  7 ILE CA   C  56.78  . 1 
       49 .  7 ILE HA   H   4.189 . 1 
       50 .  7 ILE CB   C  34.399 . 1 
       51 .  7 ILE HB   H   0.361 . 1 
       52 .  7 ILE HG2  H   0.247 . 1 
       53 .  7 ILE CG2  C  17.885 . 1 
       54 .  7 ILE CG1  C  17.885 . 1 
       55 .  7 ILE HG12 H   1.098 . 2 
       56 .  7 ILE HG13 H   0.559 . 2 
       57 .  7 ILE HD1  H   0.37  . 1 
       58 .  7 ILE CD1  C   9.257 . 1 
       59 .  8 THR N    N 122.134 . 1 
       60 .  8 THR H    H   8.264 . 1 
       61 .  8 THR CA   C  61.166 . 1 
       62 .  8 THR HA   H   4.75  . 1 
       63 .  8 THR CB   C  68.815 . 1 
       64 .  8 THR HB   H   3.951 . 1 
       65 .  8 THR HG2  H   0.975 . 1 
       66 .  8 THR CG2  C  20.794 . 1 
       67 .  8 THR C    C 172.684 . 1 
       68 .  9 ALA N    N 130.097 . 1 
       69 .  9 ALA H    H   9.387 . 1 
       70 .  9 ALA CA   C  48.957 . 1 
       71 .  9 ALA HA   H   5.352 . 1 
       72 .  9 ALA HB   H   1.127 . 1 
       73 .  9 ALA CB   C  19.857 . 1 
       74 .  9 ALA C    C 175.121 . 1 
       75 . 10 VAL N    N 122.291 . 1 
       76 . 10 VAL H    H   8.653 . 1 
       77 . 10 VAL CA   C  59.675 . 1 
       78 . 10 VAL HA   H   5.124 . 1 
       79 . 10 VAL CB   C  33.187 . 1 
       80 . 10 VAL HB   H   1.914 . 1 
       81 . 10 VAL HG1  H   0.901 . 1 
       82 . 10 VAL HG2  H   0.804 . 1 
       83 . 10 VAL CG1  C  20.539 . 1 
       84 . 10 VAL CG2  C  20.779 . 1 
       85 . 10 VAL C    C 177.077 . 1 
       86 . 11 THR N    N 116.682 . 1 
       87 . 11 THR H    H   8.712 . 1 
       88 . 11 THR CA   C  60.698 . 1 
       89 . 11 THR HA   H   4.515 . 1 
       90 . 11 THR CB   C  70.269 . 1 
       91 . 11 THR HB   H   4.889 . 1 
       92 . 11 THR HG2  H   1.076 . 1 
       93 . 11 THR CG2  C  22.388 . 1 
       94 . 11 THR C    C 177.512 . 1 
       95 . 12 GLU N    N 120.267 . 1 
       96 . 12 GLU H    H   8.244 . 1 
       97 . 12 GLU CA   C  58.432 . 1 
       98 . 12 GLU HA   H   3.995 . 1 
       99 . 12 GLU CB   C  29.067 . 1 
      100 . 12 GLU HB2  H   1.796 . 1 
      101 . 12 GLU HG2  H   2.111 . 1 
      102 . 12 GLU C    C 176.599 . 1 
      103 . 13 ASP N    N 112.933 . 1 
      104 . 13 ASP H    H   8.07  . 1 
      105 . 13 ASP CA   C  52.715 . 1 
      106 . 13 ASP HA   H   4.579 . 1 
      107 . 13 ASP CB   C  39.489 . 1 
      108 . 13 ASP HB2  H   2.902 . 2 
      109 . 13 ASP HB3  H   2.631 . 2 
      110 . 13 ASP C    C 176.599 . 1 
      111 . 14 GLY N    N 107.893 . 1 
      112 . 14 GLY H    H   7.94  . 1 
      113 . 14 GLY CA   C  45.305 . 1 
      114 . 14 GLY HA2  H   3.439 . 2 
      115 . 14 GLY HA3  H   4.038 . 2 
      116 . 14 GLY C    C 174.511 . 1 
      117 . 15 GLU N    N 121.793 . 1 
      118 . 15 GLU H    H   7.492 . 1 
      119 . 15 GLU CA   C  55.573 . 1 
      120 . 15 GLU HA   H   4.234 . 1 
      121 . 15 GLU CB   C  29.067 . 1 
      122 . 15 GLU HB2  H   2.027 . 2 
      123 . 15 GLU HB3  H   1.837 . 2 
      124 . 15 GLU CG   C  35.652 . 1 
      125 . 15 GLU HG2  H   2.062 . 2 
      126 . 15 GLU HG3  H   1.904 . 2 
      127 . 15 GLU C    C 176.251 . 1 
      128 . 16 SER N    N 117.275 . 1 
      129 . 16 SER H    H   8.426 . 1 
      130 . 16 SER CA   C  56.941 . 1 
      131 . 16 SER HA   H   5.172 . 1 
      132 . 16 SER CB   C  64.452 . 1 
      133 . 16 SER HB2  H   3.588 . 1 
      134 . 16 SER C    C 173.815 . 1 
      135 . 17 LEU N    N 127.408 . 1 
      136 . 17 LEU H    H   9.288 . 1 
      137 . 17 LEU CA   C  53.585 . 1 
      138 . 17 LEU HA   H   4.648 . 1 
      139 . 17 LEU CB   C  43.124 . 1 
      140 . 17 LEU HB2  H   1.885 . 2 
      141 . 17 LEU HB3  H   1.455 . 2 
      142 . 17 LEU CG   C  26.775 . 1 
      143 . 17 LEU HG   H   1.633 . 1 
      144 . 17 LEU HD1  H   0.711 . 1 
      145 . 17 LEU HD2  H   0.758 . 1 
      146 . 17 LEU CD1  C  23.994 . 1 
      147 . 17 LEU CD2  C  23.988 . 1 
      148 . 18 ARG N    N 121.77  . 1 
      149 . 18 ARG H    H   8.31  . 1 
      150 . 18 ARG CA   C  54.082 . 1 
      151 . 18 ARG HA   H   5.687 . 1 
      152 . 18 ARG CB   C  32.218 . 1 
      153 . 18 ARG HB2  H   1.566 . 2 
      154 . 18 ARG HB3  H   1.534 . 2 
      155 . 18 ARG CG   C  27.431 . 1 
      156 . 18 ARG HG2  H   1.447 . 1 
      157 . 18 ARG CD   C  43.379 . 1 
      158 . 18 ARG HD2  H   3.014 . 1 
      159 . 18 ARG C    C 175.468 . 1 
      160 . 19 PHE N    N 119.884 . 1 
      161 . 19 PHE H    H   8.511 . 1 
      162 . 19 PHE CA   C  55.325 . 1 
      163 . 19 PHE HA   H   4.747 . 1 
      164 . 19 PHE CB   C  37.792 . 1 
      165 . 19 PHE HB2  H   3.095 . 2 
      166 . 19 PHE HB3  H   2.793 . 2 
      167 . 19 PHE HD1  H   6.797 . 1 
      168 . 19 PHE HE1  H   6.911 . 1 
      169 . 19 PHE C    C 172.336 . 1 
      170 . 20 GLU N    N 119.168 . 1 
      171 . 20 GLU H    H   8.632 . 1 
      172 . 20 GLU CA   C  54.703 . 1 
      173 . 20 GLU HA   H   4.895 . 1 
      174 . 20 GLU CB   C  31.248 . 1 
      175 . 20 GLU HB2  H   1.878 . 2 
      176 . 20 GLU HB3  H   1.736 . 2 
      177 . 20 GLU CG   C  36.435 . 1 
      178 . 20 GLU HG2  H   2.123 . 1 
      179 . 20 GLU C    C 176.599 . 1 
      180 . 21 CYS N    N 120.457 . 1 
      181 . 21 CYS H    H   8.923 . 1 
      182 . 21 CYS CA   C  58.308 . 1 
      183 . 21 CYS HA   H   4.514 . 1 
      184 . 21 CYS CB   C  30.036 . 1 
      185 . 21 CYS HB2  H   2.436 . 2 
      186 . 21 CYS HB3  H   1.988 . 2 
      187 . 21 CYS C    C 174.25  . 1 
      188 . 22 ARG N    N 129.721 . 1 
      189 . 22 ARG H    H  10.383 . 1 
      190 . 22 ARG CA   C  56.443 . 1 
      191 . 22 ARG HA   H   4.725 . 1 
      192 . 22 ARG CB   C  31.975 . 1 
      193 . 22 ARG HB2  H   2.023 . 2 
      194 . 22 ARG HB3  H   1.891 . 2 
      195 . 22 ARG CG   C  28.333 . 1 
      196 . 22 ARG HG2  H   1.681 . 2 
      197 . 22 ARG HG3  H   1.444 . 2 
      198 . 22 ARG CD   C  43.373 . 1 
      199 . 22 ARG HD2  H   3.154 . 2 
      200 . 22 ARG HD3  H   3.067 . 2 
      201 . 22 ARG C    C 178.034 . 1 
      202 . 23 SER N    N 112.461 . 1 
      203 . 23 SER H    H   8.57  . 1 
      204 . 23 SER CA   C  60.669 . 1 
      205 . 23 SER HA   H   4.562 . 1 
      206 . 23 SER CB   C  63.725 . 1 
      207 . 23 SER HB2  H   4.17  . 2 
      208 . 23 SER HB3  H   4.027 . 2 
      209 . 23 SER C    C 174.424 . 1 
      210 . 24 ASP N    N 116.104 . 1 
      211 . 24 ASP H    H   8.038 . 1 
      212 . 24 ASP CA   C  52.218 . 1 
      213 . 24 ASP HA   H   4.699 . 1 
      214 . 24 ASP CB   C  39.489 . 1 
      215 . 24 ASP HB2  H   3.002 . 2 
      216 . 24 ASP HB3  H   2.444 . 2 
      217 . 24 ASP C    C 174.772 . 1 
      218 . 25 GLU N    N 122.526 . 1 
      219 . 25 GLU H    H   7.853 . 1 
      220 . 25 GLU CA   C  54.206 . 1 
      221 . 25 GLU HA   H   4.699 . 1 
      222 . 25 GLU CB   C  33.187 . 1 
      223 . 25 GLU HB2  H   1.993 . 1 
      224 . 25 GLU CG   C  36.359 . 1 
      225 . 25 GLU HG2  H   2.336 . 1 
      226 . 25 GLU C    C 171.466 . 1 
      227 . 26 ASP N    N 114.196 . 1 
      228 . 26 ASP H    H   6.745 . 1 
      229 . 26 ASP CA   C  50.718 . 1 
      230 . 26 ASP HA   H   4.629 . 1 
      231 . 26 ASP CB   C  42.397 . 1 
      232 . 26 ASP HB2  H   2.298 . 2 
      233 . 26 ASP HB3  H   1.573 . 2 
      234 . 26 ASP C    C 176.207 . 1 
      235 . 27 VAL N    N 117.145 . 1 
      236 . 27 VAL H    H   6.971 . 1 
      237 . 27 VAL CA   C  66.526 . 1 
      238 . 27 VAL HA   H   3.401 . 1 
      239 . 27 VAL CB   C  30.594 . 1 
      240 . 27 VAL HB   H   1.749 . 1 
      241 . 27 VAL HG1  H   0.797 . 1 
      242 . 27 VAL HG2  H   0.657 . 1 
      243 . 27 VAL CG1  C  22.553 . 1 
      244 . 27 VAL CG2  C  22.543 . 1 
      245 . 27 VAL C    C 176.251 . 1 
      246 . 28 ILE N    N 117.231 . 1 
      247 . 28 ILE H    H   7.196 . 1 
      248 . 28 ILE CA   C  61.539 . 1 
      249 . 28 ILE HA   H   3.688 . 1 
      250 . 28 ILE CB   C  33.914 . 1 
      251 . 28 ILE HB   H   2.287 . 1 
      252 . 28 ILE C    C 177.643 . 1 
      253 . 29 THR N    N 121.692 . 1 
      254 . 29 THR H    H   8.749 . 1 
      255 . 29 THR CA   C  67.015 . 1 
      256 . 29 THR HA   H   3.519 . 1 
      257 . 29 THR CB   C  67.361 . 1 
      258 . 29 THR HB   H   4.019 . 1 
      259 . 29 THR HG2  H   1.275 . 1 
      260 . 29 THR CG2  C  22.388 . 1 
      261 . 29 THR C    C 177.382 . 1 
      262 . 30 ALA N    N 123.968 . 1 
      263 . 30 ALA H    H   8.14  . 1 
      264 . 30 ALA CA   C  54.952 . 1 
      265 . 30 ALA HA   H   3.968 . 1 
      266 . 30 ALA HB   H   1.855 . 1 
      267 . 30 ALA CB   C  19.034 . 1 
      268 . 30 ALA C    C 179.905 . 1 
      269 . 31 ALA N    N 122.464 . 1 
      270 . 31 ALA H    H   8.163 . 1 
      271 . 31 ALA CA   C  55.449 . 1 
      272 . 31 ALA HA   H   2.824 . 1 
      273 . 31 ALA HB   H   0.848 . 1 
      274 . 31 ALA CB   C  15.979 . 1 
      275 . 31 ALA C    C 174.946 . 1 
      276 . 32 LEU N    N 117.665 . 1 
      277 . 32 LEU H    H   8.374 . 1 
      278 . 32 LEU CA   C  57.416 . 1 
      279 . 32 LEU HA   H   3.714 . 1 
      280 . 32 LEU CB   C  40.913 . 1 
      281 . 32 LEU HB2  H   1.749 . 2 
      282 . 32 LEU HB3  H   1.351 . 2 
      283 . 32 LEU CG   C  26.869 . 1 
      284 . 32 LEU HG   H   1.78  . 1 
      285 . 32 LEU HD1  H   0.78  . 1 
      286 . 32 LEU HD2  H   0.775 . 1 
      287 . 32 LEU CD1  C  25.322 . 1 
      288 . 32 LEU CD2  C  25.281 . 1 
      289 . 32 LEU C    C 176.891 . 1 
      290 . 33 ARG N    N 117.231 . 1 
      291 . 33 ARG H    H   7.705 . 1 
      292 . 33 ARG CA   C  57.686 . 1 
      293 . 33 ARG HA   H   4.285 . 1 
      294 . 33 ARG CB   C  27.855 . 1 
      295 . 33 ARG HB2  H   2.017 . 2 
      296 . 33 ARG HB3  H   1.943 . 2 
      297 . 33 ARG CG   C  27.701 . 1 
      298 . 33 ARG HG2  H   1.583 . 1 
      299 . 33 ARG CD   C  42.969 . 1 
      300 . 33 ARG HD2  H   3.181 . 2 
      301 . 33 ARG HD3  H   2.962 . 2 
      302 . 33 ARG C    C 177.208 . 1 
      303 . 34 GLN N    N 119.675 . 1 
      304 . 34 GLN H    H   7.384 . 1 
      305 . 34 GLN CA   C  55.076 . 1 
      306 . 34 GLN HA   H   4.28  . 1 
      307 . 34 GLN CB   C  29.794 . 1 
      308 . 34 GLN HB2  H   2.625 . 2 
      309 . 34 GLN HB3  H   1.548 . 2 
      310 . 34 GLN CG   C  36.466 . 1 
      311 . 34 GLN HG2  H   2.252 . 2 
      312 . 34 GLN HG3  H   2.12  . 2 
      313 . 34 GLN NE2  N 115.701 . 1 
      314 . 34 GLN HE21 H   9.018 . 1 
      315 . 34 GLN HE22 H   7.504 . 1 
      316 . 34 GLN C    C 173.511 . 1 
      317 . 35 ASN N    N 113.761 . 1 
      318 . 35 ASN H    H   7.735 . 1 
      319 . 35 ASN CA   C  54.082 . 1 
      320 . 35 ASN HA   H   3.927 . 1 
      321 . 35 ASN CB   C  36.407 . 1 
      322 . 35 ASN HB2  H   2.977 . 2 
      323 . 35 ASN HB3  H   2.748 . 2 
      324 . 35 ASN C    C 172.902 . 1 
      325 . 36 ILE N    N 120.006 . 1 
      326 . 36 ILE H    H   7.804 . 1 
      327 . 36 ILE CA   C  59.258 . 1 
      328 . 36 ILE HA   H   3.822 . 1 
      329 . 36 ILE CB   C  37.307 . 1 
      330 . 36 ILE HB   H   1.084 . 1 
      331 . 36 ILE HG2  H   0.344 . 1 
      332 . 36 ILE CG2  C  17.036 . 1 
      333 . 36 ILE CG1  C  26.115 . 1 
      334 . 36 ILE HG12 H   1.094 . 2 
      335 . 36 ILE HG13 H   0.834 . 2 
      336 . 36 ILE HD1  H   0.55  . 1 
      337 . 36 ILE CD1  C  12.919 . 1 
      338 . 36 ILE C    C 174.381 . 1 
      339 . 37 PHE N    N 126.945 . 1 
      340 . 37 PHE H    H   8.422 . 1 
      341 . 37 PHE CA   C  56.813 . 1 
      342 . 37 PHE HA   H   4.281 . 1 
      343 . 37 PHE CB   C  37.307 . 1 
      344 . 37 PHE HB2  H   2.822 . 1 
      345 . 37 PHE HD1  H   7.051 . 1 
      346 . 37 PHE HE1  H   7.166 . 1 
      347 . 37 PHE C    C 175.12  . 1 
      348 . 38 LEU N    N 124.17  . 1 
      349 . 38 LEU H    H   7.401 . 1 
      350 . 38 LEU CA   C  52.928 . 1 
      351 . 38 LEU HA   H   4.242 . 1 
      352 . 38 LEU CB   C  41.428 . 1 
      353 . 38 LEU HB2  H   1.441 . 2 
      354 . 38 LEU HB3  H   1.255 . 2 
      355 . 38 LEU CG   C  26.596 . 1 
      356 . 38 LEU HG   H   0.592 . 1 
      357 . 38 LEU HD1  H   0.698 . 1 
      358 . 38 LEU HD2  H   0.699 . 1 
      359 . 38 LEU CD1  C  22.9   . 1 
      360 . 38 LEU CD2  C  23.025 . 1 
      361 . 38 LEU C    C 176.512 . 1 
      362 . 39 MET N    N 119.804 . 1 
      363 . 39 MET H    H   7.693 . 1 
      364 . 39 MET CA   C  56.512 . 1 
      365 . 39 MET HA   H   4.154 . 1 
      366 . 39 MET CB   C  31.43  . 1 
      367 . 39 MET HB2  H   1.956 . 2 
      368 . 39 MET HB3  H   1.884 . 2 
      369 . 39 MET CG   C  31.43  . 1 
      370 . 39 MET HG2  H   1.763 . 1 
      371 . 40 SER N    N 115.061 . 1 
      372 . 40 SER H    H   8.141 . 1 
      373 . 40 SER CA   C  51.341 . 1 
      374 . 40 SER HA   H   4.687 . 1 
      375 . 40 SER HB2  H   3.779 . 1 
      376 . 51 LYS N    N 118.889 . 1 
      377 . 51 LYS H    H   8.935 . 1 
      378 . 51 LYS CA   C  56.397 . 1 
      379 . 51 LYS HA   H   4.167 . 1 
      380 . 51 LYS CB   C  31.952 . 1 
      381 . 51 LYS HB2  H   1.758 . 1 
      382 . 51 LYS C    C 175.789 . 1 
      383 . 52 ALA N    N 125.992 . 1 
      384 . 52 ALA H    H   8.556 . 1 
      385 . 52 ALA CA   C  50.602 . 1 
      386 . 52 ALA HA   H   4.548 . 1 
      387 . 52 ALA HB   H   1.158 . 1 
      388 . 52 ALA CB   C  21.796 . 1 
      389 . 52 ALA C    C 173.25  . 1 
      390 . 53 LEU N    N 119.689 . 1 
      391 . 53 LEU H    H   7.582 . 1 
      392 . 53 LEU CA   C  53.833 . 1 
      393 . 53 LEU HA   H   4.542 . 1 
      394 . 53 LEU CB   C  44.094 . 1 
      395 . 53 LEU HB2  H   1.766 . 2 
      396 . 53 LEU HB3  H   1.354 . 2 
      397 . 53 LEU CG   C  25.044 . 1 
      398 . 53 LEU HG   H   1.159 . 1 
      399 . 53 LEU HD1  H   0.748 . 1 
      400 . 53 LEU HD2  H   0.768 . 1 
      401 . 53 LEU CD1  C  23.451 . 1 
      402 . 53 LEU CD2  C  22.897 . 1 
      403 . 53 LEU C    C 175.512 . 1 
      404 . 54 CYS N    N 127.379 . 1 
      405 . 54 CYS H    H   8.882 . 1 
      406 . 54 CYS CA   C  57.189 . 1 
      407 . 54 CYS HA   H   4.936 . 1 
      408 . 54 CYS CB   C  25.916 . 1 
      409 . 54 CYS HB2  H   2.582 . 2 
      410 . 54 CYS HB3  H   1.887 . 2 
      411 . 54 CYS C    C 173.815 . 1 
      412 . 55 SER N    N 124.951 . 1 
      413 . 55 SER H    H   8.522 . 1 
      414 . 55 SER CA   C  58.784 . 1 
      415 . 55 SER HA   H   4.234 . 1 
      416 . 55 SER CB   C  63.483 . 1 
      417 . 55 SER HB2  H   3.825 . 2 
      418 . 55 SER HB3  H   3.543 . 2 
      419 . 55 SER C    C 174.816 . 1 
      420 . 56 GLU N    N 121.134 . 1 
      421 . 56 GLU H    H   7.648 . 1 
      422 . 56 GLU CA   C  56.443 . 1 
      423 . 56 GLU HA   H   4.42  . 1 
      424 . 56 GLU CB   C  32.702 . 1 
      425 . 56 GLU HB2  H   1.842 . 2 
      426 . 56 GLU HB3  H   1.74  . 2 
      427 . 56 GLU CG   C  36.172 . 1 
      428 . 56 GLU HG2  H   2.135 . 1 
      429 . 56 GLU C    C 174.337 . 1 
      430 . 57 GLY N    N 111.998 . 1 
      431 . 57 GLY H    H   8.197 . 1 
      432 . 57 GLY CA   C  43.124 . 1 
      433 . 57 GLY HA2  H   4.736 . 2 
      434 . 57 GLY HA3  H   3.517 . 2 
      435 . 58 ASP N    N 117.501 . 1 
      436 . 58 ASP H    H   8.12  . 1 
      437 . 58 ASP CA   C  52.342 . 1 
      438 . 58 ASP HA   H   4.818 . 1 
      439 . 58 ASP CB   C  43.367 . 1 
      440 . 58 ASP HB2  H   2.32  . 1 
      441 . 58 ASP C    C 174.337 . 1 
      442 . 59 TYR N    N 117.087 . 1 
      443 . 59 TYR H    H   7.385 . 1 
      444 . 59 TYR CA   C  55.176 . 1 
      445 . 59 TYR HA   H   4.887 . 1 
      446 . 59 TYR CB   C  40.458 . 1 
      447 . 59 TYR HB2  H   2.725 . 2 
      448 . 59 TYR HB3  H   2.577 . 2 
      449 . 59 TYR HD1  H   6.618 . 1 
      450 . 59 TYR HE1  H   6.442 . 1 
      451 . 59 TYR C    C 172.858 . 1 
      452 . 60 ASP N    N 118.937 . 1 
      453 . 60 ASP H    H   9.146 . 1 
      454 . 60 ASP CA   C  52.839 . 1 
      455 . 60 ASP HA   H   5.055 . 1 
      456 . 60 ASP CB   C  43.367 . 1 
      457 . 60 ASP HB2  H   2.507 . 1 
      458 . 60 ASP C    C 174.99  . 1 
      459 . 61 LEU N    N 123.216 . 1 
      460 . 61 LEU H    H   8.683 . 1 
      461 . 61 LEU CA   C  53.062 . 1 
      462 . 61 LEU HA   H   5.5   . 1 
      463 . 61 LEU CB   C  42.397 . 1 
      464 . 61 LEU HB2  H   1.828 . 2 
      465 . 61 LEU HB3  H   1.726 . 2 
      466 . 61 LEU CG   C  26.597 . 1 
      467 . 61 LEU HG   H   1.111 . 1 
      468 . 61 LEU HD1  H   0.901 . 1 
      469 . 61 LEU HD2  H   0.892 . 1 
      470 . 61 LEU CD1  C  25.315 . 1 
      471 . 61 LEU CD2  C  25.548 . 1 
      472 . 61 LEU C    C 177.686 . 1 
      473 . 62 LYS N    N 123.158 . 1 
      474 . 62 LYS H    H   8.288 . 1 
      475 . 62 LYS CA   C  54.703 . 1 
      476 . 62 LYS HA   H   4.797 . 1 
      477 . 62 LYS CB   C  33.429 . 1 
      478 . 62 LYS HB2  H   1.826 . 1 
      479 . 62 LYS CG   C  24.834 . 1 
      480 . 62 LYS HG2  H   1.277 . 2 
      481 . 62 LYS HG3  H   1.201 . 2 
      482 . 62 LYS CD   C  28.763 . 1 
      483 . 62 LYS HD2  H   1.12  . 1 
      484 . 62 LYS CE   C  41.503 . 1 
      485 . 62 LYS HE2  H   2.4   . 1 
      486 . 62 LYS C    C 175.99  . 1 
      487 . 63 GLY N    N 110.61  . 1 
      488 . 63 GLY H    H   8.708 . 1 
      489 . 63 GLY CA   C  46.76  . 1 
      490 . 63 GLY HA2  H   3.957 . 2 
      491 . 63 GLY HA3  H   3.857 . 2 
      492 . 63 GLY C    C 175.946 . 1 
      493 . 64 CYS N    N 118.9   . 1 
      494 . 64 CYS H    H   8.801 . 1 
      495 . 64 CYS CA   C  59.124 . 1 
      496 . 64 CYS HA   H   4.836 . 1 
      497 . 64 CYS CB   C  28.569 . 1 
      498 . 64 CYS HB2  H   3.342 . 2 
      499 . 64 CYS HB3  H   2.9   . 2 
      500 . 64 CYS C    C 175.531 . 1 
      501 . 65 SER N    N 120.891 . 1 
      502 . 65 SER H    H   8.56  . 1 
      503 . 65 SER CA   C  57.065 . 1 
      504 . 65 SER HA   H   4.42  . 1 
      505 . 65 SER CB   C  63.483 . 1 
      506 . 65 SER HB2  H   3.911 . 2 
      507 . 65 SER HB3  H   3.761 . 2 
      508 . 65 SER C    C 176.251 . 1 
      509 . 66 VAL N    N 124.893 . 1 
      510 . 66 VAL H    H   8.677 . 1 
      511 . 66 VAL CA   C  63.606 . 1 
      512 . 66 VAL HA   H   3.869 . 1 
      513 . 66 VAL CB   C  30.763 . 1 
      514 . 66 VAL HB   H   2.112 . 1 
      515 . 66 VAL HG1  H   0.97  . 1 
      516 . 66 VAL HG2  H   0.976 . 1 
      517 . 66 VAL CG1  C  20.806 . 1 
      518 . 66 VAL CG2  C  20.668 . 1 
      519 . 66 VAL C    C 176.879 . 1 
      520 . 67 GLN N    N 117.231 . 1 
      521 . 67 GLN H    H   7.702 . 1 
      522 . 67 GLN CA   C  57.182 . 1 
      523 . 67 GLN HA   H   3.924 . 1 
      524 . 67 GLN CB   C  27.37  . 1 
      525 . 67 GLN HB2  H   1.827 . 1 
      526 . 67 GLN CG   C  33.905 . 1 
      527 . 67 GLN HG2  H   2.241 . 1 
      528 . 68 ALA N    N 120.903 . 1 
      529 . 68 ALA H    H   6.937 . 1 
      530 . 68 ALA CA   C  53.096 . 1 
      531 . 68 ALA HA   H   3.925 . 1 
      532 . 68 ALA HB   H   0.96  . 1 
      533 . 68 ALA CB   C  22.038 . 1 
      534 . 68 ALA C    C 176.12  . 1 
      535 . 69 LEU N    N 116.3   . 1 
      536 . 69 LEU H    H   7.803 . 1 
      537 . 69 LEU CA   C  51.053 . 1 
      538 . 69 LEU HA   H   4.81  . 1 
      539 . 69 LEU CB   C  40.195 . 1 
      540 . 69 LEU HB2  H   2.014 . 2 
      541 . 69 LEU HB3  H   1.018 . 2 
      542 . 70 PRO CD   C  50.262 . 1 
      543 . 70 PRO CA   C  61.703 . 1 
      544 . 70 PRO HA   H   4.826 . 1 
      545 . 70 PRO CB   C  31.392 . 1 
      546 . 70 PRO HB2  H   2.487 . 2 
      547 . 70 PRO HB3  H   1.991 . 2 
      548 . 70 PRO CG   C  27.572 . 1 
      549 . 70 PRO HG2  H   2.117 . 1 
      550 . 70 PRO HD2  H   3.822 . 2 
      551 . 70 PRO HD3  H   3.693 . 2 
      552 . 71 PRO CD   C  50.279 . 1 
      553 . 71 PRO CA   C  65.268 . 1 
      554 . 71 PRO HA   H   4.413 . 1 
      555 . 71 PRO CB   C  30.763 . 1 
      556 . 71 PRO HB2  H   2.359 . 2 
      557 . 71 PRO HB3  H   1.93  . 2 
      558 . 71 PRO CG   C  27.537 . 1 
      559 . 71 PRO HG2  H   2.137 . 2 
      560 . 71 PRO HG3  H   2.09  . 2 
      561 . 71 PRO HD2  H   3.829 . 2 
      562 . 71 PRO HD3  H   3.685 . 2 
      563 . 71 PRO C    C 178.73  . 1 
      564 . 72 GLU N    N 116.097 . 1 
      565 . 72 GLU H    H   9.499 . 1 
      566 . 72 GLU CA   C  59.053 . 1 
      567 . 72 GLU HA   H   4.045 . 1 
      568 . 72 GLU CB   C  27.181 . 1 
      569 . 72 GLU HB2  H   1.988 . 2 
      570 . 72 GLU HB3  H   1.911 . 2 
      571 . 72 GLU CG   C  36.132 . 1 
      572 . 72 GLU HG2  H   2.288 . 1 
      573 . 72 GLU C    C 179.165 . 1 
      574 . 73 GLU N    N 118.925 . 1 
      575 . 73 GLU H    H   7.296 . 1 
      576 . 73 GLU CA   C  58.183 . 1 
      577 . 73 GLU HA   H   4.071 . 1 
      578 . 73 GLU CB   C  28.34  . 1 
      579 . 73 GLU HB2  H   2.086 . 2 
      580 . 73 GLU HB3  H   1.949 . 2 
      581 . 73 GLU CG   C  36.998 . 1 
      582 . 73 GLU HG2  H   2.222 . 2 
      583 . 73 GLU HG3  H   2.099 . 2 
      584 . 73 GLU C    C 178.687 . 1 
      585 . 74 GLU N    N 122.319 . 1 
      586 . 74 GLU H    H   7.905 . 1 
      587 . 74 GLU CA   C  58.556 . 1 
      588 . 74 GLU HA   H   4.185 . 1 
      589 . 74 GLU CB   C  28.825 . 1 
      590 . 74 GLU HB2  H   2.104 . 1 
      591 . 74 GLU CG   C  35.935 . 1 
      592 . 74 GLU HG2  H   2.379 . 2 
      593 . 74 GLU HG3  H   2.135 . 2 
      594 . 75 GLU N    N 118.3   . 1 
      595 . 75 GLU H    H   8.248 . 1 
      596 . 75 GLU CA   C  58.059 . 1 
      597 . 75 GLU HA   H   4.049 . 1 
      598 . 75 GLU CB   C  28.825 . 1 
      599 . 75 GLU HB2  H   2.028 . 1 
      600 . 75 GLU CG   C  36.05  . 1 
      601 . 75 GLU HG2  H   2.31  . 1 
      602 . 75 GLU C    C 177.208 . 1 
      603 . 76 GLU N    N 116.74  . 1 
      604 . 76 GLU H    H   7.103 . 1 
      605 . 76 GLU CA   C  55.698 . 1 
      606 . 76 GLU HA   H   4.284 . 1 
      607 . 76 GLU CB   C  29.067 . 1 
      608 . 76 GLU HB2  H   2.225 . 2 
      609 . 76 GLU HB3  H   2.031 . 2 
      610 . 76 GLU CG   C  35.864 . 1 
      611 . 76 GLU HG2  H   2.41  . 2 
      612 . 76 GLU HG3  H   2.303 . 2 
      613 . 76 GLU C    C 175.99  . 1 
      614 . 77 GLY N    N 105.348 . 1 
      615 . 77 GLY H    H   7.534 . 1 
      616 . 77 GLY CA   C  45.063 . 1 
      617 . 77 GLY HA2  H   4.28  . 2 
      618 . 77 GLY HA3  H   3.629 . 2 
      619 . 77 GLY C    C 173.598 . 1 
      620 . 78 LEU N    N 120.237 . 1 
      621 . 78 LEU H    H   7.397 . 1 
      622 . 78 LEU CA   C  54.828 . 1 
      623 . 78 LEU HA   H   4.795 . 1 
      624 . 78 LEU CB   C  40.216 . 1 
      625 . 78 LEU HB2  H   1.561 . 2 
      626 . 78 LEU HB3  H   1.037 . 2 
      627 . 78 LEU CG   C  28.5   . 1 
      628 . 78 LEU HG   H   1.557 . 1 
      629 . 78 LEU HD1  H   0.805 . 1 
      630 . 78 LEU HD2  H   0.726 . 1 
      631 . 78 LEU CD1  C  25.099 . 1 
      632 . 78 LEU CD2  C  23.907 . 1 
      633 . 78 LEU C    C 176.381 . 1 
      634 . 79 VAL N    N 111.062 . 1 
      635 . 79 VAL H    H   8.739 . 1 
      636 . 79 VAL CA   C  57.99  . 1 
      637 . 79 VAL HA   H   4.316 . 1 
      638 . 79 VAL CB   C  33.663 . 1 
      639 . 79 VAL HB   H   1.749 . 1 
      640 . 79 VAL HG1  H   0.172 . 1 
      641 . 79 VAL HG2  H  -0.006 . 1 
      642 . 79 VAL CG1  C  22.919 . 1 
      643 . 79 VAL CG2  C  18.358 . 1 
      644 . 83 ARG CA   C  52.593 . 1 
      645 . 83 ARG CB   C  32.161 . 1 
      646 . 84 THR N    N 116.624 . 1 
      647 . 84 THR H    H   6.503 . 1 
      648 . 84 THR CA   C  62.658 . 1 
      649 . 84 THR HA   H   4.335 . 1 
      650 . 84 THR CB   C  67.846 . 1 
      651 . 84 THR HB   H   3.451 . 1 
      652 . 84 THR HG2  H   0.339 . 1 
      653 . 84 THR CG2  C  20.083 . 1 
      654 . 84 THR C    C 172.249 . 1 
      655 . 85 TYR N    N 125.876 . 1 
      656 . 85 TYR H    H   8.816 . 1 
      657 . 85 TYR CA   C  53.263 . 1 
      658 . 85 TYR HA   H   5.047 . 1 
      659 . 85 TYR CB   C  37.843 . 1 
      660 . 85 TYR HB2  H   2.998 . 2 
      661 . 85 TYR HB3  H   2.875 . 2 
      662 . 85 TYR HD1  H   6.996 . 1 
      663 . 85 TYR HE1  H   6.614 . 1 
      664 . 86 PRO CD   C  52.138 . 1 
      665 . 86 PRO CA   C  63.403 . 1 
      666 . 86 PRO HA   H   4.359 . 1 
      667 . 86 PRO CB   C  30.763 . 1 
      668 . 86 PRO HB2  H   1.991 . 1 
      669 . 86 PRO CG   C  28.232 . 1 
      670 . 86 PRO HG2  H   1.815 . 1 
      671 . 86 PRO HD2  H   4.338 . 2 
      672 . 86 PRO HD3  H   3.69  . 2 
      673 . 86 PRO C    C 175.772 . 1 
      674 . 87 LYS N    N 116.978 . 1 
      675 . 87 LYS H    H   8.565 . 1 
      676 . 87 LYS CA   C  55.325 . 1 
      677 . 87 LYS HA   H   4.193 . 1 
      678 . 87 LYS CB   C  33.187 . 1 
      679 . 87 LYS HB2  H   1.865 . 2 
      680 . 87 LYS HB3  H   0.977 . 2 
      681 . 87 LYS CG   C  25.463 . 1 
      682 . 87 LYS HG2  H   1.275 . 2 
      683 . 87 LYS HG3  H   1.164 . 2 
      684 . 87 LYS CD   C  29.795 . 1 
      685 . 87 LYS HD2  H   1.976 . 2 
      686 . 87 LYS HD3  H   1.875 . 2 
      687 . 87 LYS CE   C  41.405 . 1 
      688 . 87 LYS HE2  H   2.668 . 2 
      689 . 87 LYS HE3  H   2.502 . 2 
      690 . 87 LYS C    C 174.816 . 1 
      691 . 88 THR N    N 110.884 . 1 
      692 . 88 THR H    H   7.398 . 1 
      693 . 88 THR CA   C  59.426 . 1 
      694 . 88 THR HA   H   4.047 . 1 
      695 . 88 THR CB   C  73.373 . 1 
      696 . 88 THR HB   H   4.554 . 1 
      697 . 88 THR HG2  H   1.034 . 1 
      698 . 88 THR CG2  C  21.566 . 1 
      699 . 88 THR C    C 172.162 . 1 
      700 . 89 ASP N    N 117.021 . 1 
      701 . 89 ASP H    H   8.092 . 1 
      702 . 89 ASP CA   C  55.946 . 1 
      703 . 89 ASP HA   H   4.76  . 1 
      704 . 89 ASP CB   C  39.731 . 1 
      705 . 89 ASP HB2  H   2.742 . 2 
      706 . 89 ASP HB3  H   2.451 . 2 
      707 . 89 ASP C    C 176.381 . 1 
      708 . 90 LEU N    N 119.825 . 1 
      709 . 90 LEU H    H   7.98  . 1 
      710 . 90 LEU CA   C  53.129 . 1 
      711 . 90 LEU HA   H   5.22  . 1 
      712 . 90 LEU CB   C  45.305 . 1 
      713 . 90 LEU HB2  H   1.528 . 2 
      714 . 90 LEU HB3  H   1.234 . 2 
      715 . 90 LEU HG   H   0.816 . 1 
      716 . 90 LEU HD1  H   0.431 . 1 
      717 . 90 LEU HD2  H   0.295 . 1 
      718 . 91 GLU N    N 122.002 . 1 
      719 . 91 GLU H    H   8.304 . 1 
      720 . 91 GLU CA   C  54.828 . 1 
      721 . 91 GLU HA   H   3.849 . 1 
      722 . 91 GLU CB   C  30.279 . 1 
      723 . 91 GLU HB2  H   1.979 . 2 
      724 . 91 GLU HB3  H   1.759 . 2 
      725 . 91 GLU CG   C  34.352 . 1 
      726 . 91 GLU HG2  H   2.042 . 2 
      727 . 91 GLU HG3  H   1.971 . 2 
      728 . 91 GLU C    C 174.99  . 1 
      729 . 92 ILE N    N 123.158 . 1 
      730 . 92 ILE H    H   9.007 . 1 
      731 . 92 ILE CA   C  57.065 . 1 
      732 . 92 ILE HA   H   5.055 . 1 
      733 . 92 ILE CB   C  40.701 . 1 
      734 . 92 ILE HB   H   1.535 . 1 
      735 . 92 ILE HG2  H   0.558 . 1 
      736 . 92 ILE CG2  C  18.03  . 1 
      737 . 92 ILE CG1  C  26.756 . 1 
      738 . 92 ILE HG12 H   0.957 . 1 
      739 . 92 ILE HD1  H   0.465 . 1 
      740 . 92 ILE CD1  C  12.505 . 1 
      741 . 92 ILE C    C 174.555 . 1 
      742 . 93 GLU N    N 125.558 . 1 
      743 . 93 GLU H    H   9.312 . 1 
      744 . 93 GLU CA   C  54.234 . 1 
      745 . 93 GLU HA   H   4.78  . 1 
      746 . 93 GLU CB   C  29.794 . 1 
      747 . 93 GLU HB2  H   1.968 . 2 
      748 . 93 GLU HB3  H   1.826 . 2 
      749 . 93 GLU CG   C  35.38  . 1 
      750 . 93 GLU HG2  H   2.15  . 2 
      751 . 93 GLU HG3  H   2.02  . 2 
      752 . 93 GLU C    C 176.033 . 1 
      753 . 94 LEU N    N 126.223 . 1 
      754 . 94 LEU H    H   8.775 . 1 
      755 . 94 LEU CA   C  50.751 . 1 
      756 . 94 LEU HA   H   4.51  . 1 
      757 . 94 LEU CB   C  40.195 . 1 
      758 . 94 LEU HB2  H   1.341 . 2 
      759 . 94 LEU HB3  H   0.33  . 2 
      760 . 94 LEU CG   C  27.412 . 1 
      761 . 94 LEU HG   H   1.148 . 1 
      762 . 94 LEU HD1  H   0.733 . 1 
      763 . 94 LEU HD2  H   0.592 . 1 
      764 . 94 LEU CD1  C  25.316 . 1 
      765 . 94 LEU CD2  C  22.388 . 1 
      766 . 95 PRO CD   C  49.584 . 1 
      767 . 95 PRO CA   C  62.272 . 1 
      768 . 95 PRO HA   H   4.81  . 1 
      769 . 95 PRO CB   C  28.097 . 1 
      770 . 95 PRO HB2  H   2.339 . 2 
      771 . 95 PRO HB3  H   1.919 . 2 
      772 . 95 PRO CG   C  27.569 . 1 
      773 . 95 PRO HG2  H   1.991 . 2 
      774 . 95 PRO HG3  H   1.765 . 2 
      775 . 95 PRO HD2  H   3.636 . 2 
      776 . 95 PRO HD3  H   3.14  . 2 
      777 . 95 PRO C    C 174.946 . 1 
      778 . 96 TYR N    N 116.019 . 1 
      779 . 96 TYR H    H   7.467 . 1 
      780 . 96 TYR CA   C  55.591 . 1 
      781 . 96 TYR HA   H   4.776 . 1 
      782 . 96 TYR CB   C  38.277 . 1 
      783 . 96 TYR HB2  H   3.255 . 2 
      784 . 96 TYR HB3  H   3.178 . 2 
      785 . 96 TYR HD1  H   6.913 . 1 
      786 . 96 TYR HE1  H   6.698 . 1 
      787 . 96 TYR C    C 175.251 . 1 
      788 . 97 THR N    N 111.825 . 1 
      789 . 97 THR H    H   8.359 . 1 
      790 . 97 THR CA   C  61.134 . 1 
      791 . 97 THR HA   H   4.421 . 1 
      792 . 97 THR CB   C  69.911 . 1 
      793 . 97 THR HB   H   4.312 . 1 
      794 . 97 THR HG2  H   1.174 . 1 
      795 . 97 THR CG2  C  22.123 . 1 
      796 . 98 HIS N    N 120.37  . 1 
      797 . 98 HIS H    H   8.336 . 1 

   stop_

save_