data_4566
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# Entry information #
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save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Assignment of 1H,13C and 15N signals of Bovine Adrenodoxin
;
_BMRB_accession_number 4566
_BMRB_flat_file_name bmr4566.str
_Entry_type original
_Submission_date 1999-12-14
_Accession_date 1999-12-15
_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 Weiss Roland . .
2 Brachais Laurent . .
3 Loehr Frank . .
4 Hartleib Judith . .
5 Bernhardt Rita . .
6 Rueterjans Heinz . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 470
"13C chemical shifts" 415
"15N chemical shifts" 106
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2000-09-25 original author .
stop_
_Original_release_date 2000-09-25
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Letter to the Editor:
Assignment of 1H, 13C and 15N signals of bovine adrenodoxin
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID ?
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Weiss Roland . .
2 Brachais Laurent . .
3 Lohr Frank . .
4 Hartleib Judith . .
5 Bernhardt Rita . .
6 Rueterjans Heinz . .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_volume 17
_Journal_issue 4
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 355
_Page_last 356
_Year 2000
_Details .
save_
#######################################
# Cited references within the entry #
#######################################
save_ref_1
_Saveframe_category citation
_Citation_full 'Kimura, T. and Suzuki (1965), Biochem. Biophys. Res. Comm. 19, S. 340-345'
_Citation_title 'AN IRON PROTEIN AS A COMPONENT OF STEROID 11-BETA-HYDROXYLASE COMPLEX.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 14317399
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 SUZUKI K. . .
2 KIMURA T. . .
stop_
_Journal_abbreviation 'Biochem. Biophys. Res. Commun.'
_Journal_name_full 'Biochemical and biophysical research communications'
_Journal_volume 19
_Journal_issue .
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
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_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 340
_Page_last 345
_Year 1965
_Details .
save_
save_ref_4
_Saveframe_category citation
_Citation_full 'Stormer, F.C., Pedersen, J.I. and Oftebro, H. (1979), JBC 254, S. 4331-4334'
_Citation_title 'The presence of an adrenodoxin-like ferredoxin and cytochrome P-450 in brain mitochondria.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 438190
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Oftebro H. . .
2 Stormer F.C. C. .
3 Pedersen J.L. L. .
stop_
_Journal_abbreviation 'J. Biol. Chem.'
_Journal_name_full 'The Journal of biological chemistry'
_Journal_volume 254
_Journal_issue 11
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 4331
_Page_last 4334
_Year 1979
_Details
;
An iron-sulfur protein has been isolated from bovine brain mitochondria and
purified 200-fold. The optical spectrum (peaks at 412 and 455 nm which
disappear upon reduction) and the EPR spectrum (g values at 1.94 and 2.02) were
typical for a ferredoxin. In reconstitution experiments, the protein could
replace adrenodoxin in the cholesterol side chain cleavage reaction. The
additional detection of cytochrome P-450 in brain mitochondria indicates that
the isolated ferredoxin is part of a cytochrome P-450-dependent hydroxylation
system.
;
save_
save_ref_5
_Saveframe_category citation
_Citation_full
;
Saarem, K., Bjorkhem, I., Pedersen, J.I. and Oftebro, H. (1981), J.Lipid. Res.
22, S. 1254-1264
;
_Citation_title 'Side chain hydroxylation of C27-steroids and vitamin D3 by a cytochrome P-450 enzyme system isolated from human liver mitochondria.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 6274987
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Oftebro H. . .
2 Saarem K. . .
3 Borkhem I. . .
4 Pedersen J.I. I. .
stop_
_Journal_abbreviation 'J. Lipid Res.'
_Journal_name_full 'Journal of lipid research'
_Journal_volume 22
_Journal_issue 8
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 1254
_Page_last 1264
_Year 1981
_Details
;
The present study was undertaken to obtain information on the involvement of
cytochrome P-450 in the 26-hydroxylation on bile acid intermediates and in the
25-hydroxylation of vitamin D3 in human liver mitochondria. Cytochrome P-450
was solubilized from human liver mitochondria and purified two times to a
specific content of 0.125 nmol per mg protein. Furthermore, a ferredoxin was
isolated from the mitochondria and partly purified. This iron-sulfur protein
had properties similar to bovine adrenal ferredoxin. A mitochondrial
NADPH-ferredoxin reductase was also isolated and purified to homogeneity. This
enzyme was a flavoprotein with properties very similar to the bovine adrenal
NADPH-ferredoxin reductase. The cytochrome P-450 preparation catalyzed
26-hydroxylation of C27-steroids and 25-hydroxylation of vitamin D3 when
reconstructed with NADPH, the ferredoxin and the ferredoxin reductase. With
different substrates the following turnover numbers (nmol product X nmol
P-450(-1) X min-1) were found: cholesterol, 8; 5-cholestene-3 beta, 7
alpha-diol, 10; 7 alpha-hydroxy-4-cholesten-3-one, 23; 7 alpha, 12
alpha-dihydroxy-4-cholesten-3-one, 27; 5 beta-cholestane-3 alpha, 7 alpha-diol,
28; 5 beta-cholestane-3 alpha, 7 alpha, 12 alpha-triol, 41; and vitamin D3,
0.16. The hydroxylation reactions were inhibited by CO and metyrapone. The
human liver mitochondrial ferredoxin and ferredoxin reductase could be replaced
by adrenal ferredoxin and adrenal ferredoxin reductase without reduction of
activity, but they could not be replaced by microsomal NADPH-cytochrome P-450
reductase. It is concluded that human liver mitochondria contain cytochrome
P-450 involved in the oxidation of the side chain of C27-steroids and vitamin
D3.
;
save_
save_ref_6
_Saveframe_category citation
_Citation_full 'Okuda, K. and Atsuta, Y. (1978), JBC 253, S. 4653-4658'
_Citation_title 'Isolation of rat liver mitochondrial ferredoxin and its reductase active in the 5beta-cholestane-3alpha, 7alpha, 12alpha-triol 26-hydroxylase.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 207706
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Atsuta Y. . .
2 Okuda K. . .
stop_
_Journal_abbreviation 'J. Biol. Chem.'
_Journal_name_full 'The Journal of biological chemistry'
_Journal_volume 253
_Journal_issue 13
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 4653
_Page_last 4658
_Year 1978
_Details .
save_
save_ref_7
_Saveframe_category citation
_Citation_full 'Hiwatashi, A., Ichikawa, Y. and Waki, N. (1986), FEBS Lett. 195, S. 87-91'
_Citation_title 'Purification and biochemical characterization of hepatic ferredoxin (hepatoredoxin) from bovine liver mitochondria.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 3080335
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Waki N. . .
2 Hiwatashi A. . .
3 Ichikawa Y. . .
stop_
_Journal_abbreviation 'FEBS Lett.'
_Journal_name_full 'FEBS letters'
_Journal_volume 195
_Journal_issue 1-2
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 87
_Page_last 91
_Year 1986
_Details
;
Hepatic ferredoxin (hepatoredoxin) was purified from bovine liver mitochondria.
The monomeric molecular mass of the hepatoredoxin was larger than that of
adrenocortical ferredoxin (adrenodoxin) from bovine adrenocortical mitochondria
at 14 kDa. We studied the amino acid residues and NH2-terminal sequence of this
protein. The hepatoredoxin was organ-specific protein. The optical absorption
spectrum of oxidized hepatoredoxin had two peaks, at 414 and 455 nm in the
visible region. Hepatoredoxin formed an immunoprecipitin line against
anti-adrenodoxin immunoglobulin in Ouchterlony double diffusion, and an
immunochemical staining band in Western blotting.
;
save_
save_ref_3
_Saveframe_category citation
_Citation_full 'Kimura, T. (1968), Struct. Bonding 5, S. 1-40'
_Citation_title .
_Citation_status .
_Citation_type .
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID ?
_Journal_abbreviation .
_Journal_name_full .
_Journal_volume .
_Journal_issue .
_Journal_CSD .
_Book_title .
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_Book_series .
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_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
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_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first .
_Page_last .
_Year .
_Details .
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save_ref_2
_Saveframe_category citation
_Citation_full
;
Cupp, J.R., Vickery, L.E. and Coghlan, V.M. (1988), Arch.Biochem.Biophys. 264,
S. 376-382
;
_Citation_title 'Purification and characterization of human placental ferredoxin.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 3401007
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Coghlan V.M. M. .
2 Cupp J.R. R. .
3 Vickery L.E. E. .
stop_
_Journal_abbreviation 'Arch. Biochem. Biophys.'
_Journal_name_full 'Archives of biochemistry and biophysics'
_Journal_volume 264
_Journal_issue 2
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 376
_Page_last 382
_Year 1988
_Details
;
A ferredoxin-type iron-sulfur protein was isolated from human placenta
mitochondria. The properties of the purified protein were very similar to those
of adrenal ferredoxin (adrenodoxin), and immunological cross-reactivity with
polyclonal antibodies to bovine adrenodoxin was observed. The N-terminal amino
acid sequence and the visible absorption spectrum were identical to bovine
adrenodoxin. The molecular mass as determined by sodium dodecyl
sulfate-polyacrylamide gel electrophoresis (Mr approximately 13,500), however,
is slightly smaller than that of adrenodoxin, and the C-terminal sequence is
different. Human placental ferredoxin can substitute for bovine adrenodoxin in
reactions reconstituted with bovine adrenal enzymes which catalyze the side
chain cleavage of cholesterol to pregnenolone and the 11 beta-hydroxylation of
deoxycorticosterone to corticosterone.
;
save_
save_ref_8
_Saveframe_category citation
_Citation_full
;
Uhlmann, H., Beckert, V., Schwarz, D. and Bernhardt, R. (1992), Biochem.
Biophys. Res. Commun. 188, S. 1131-1138
;
_Citation_title 'Expression of bovine adrenodoxin in E. coli and site-directed mutagenesis of /2 Fe-2S/ cluster ligands.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 1332711
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Uhlmann H. . .
2 Beckert V. . .
3 Schwarz D. . .
4 Bernhardt R. . .
stop_
_Journal_abbreviation 'Biochem. Biophys. Res. Commun.'
_Journal_name_full 'Biochemical and biophysical research communications'
_Journal_volume 188
_Journal_issue 3
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 1131
_Page_last 1138
_Year 1992
_Details
;
Expression systems for adrenodoxin into the periplasm and the cytoplasm of E.
coli have been developed as a prerequisite for site-directed mutagenesis
studies. In both systems the /2Fe-2S/ cluster of the protein was correctly
assembled, the cytoplasmic one gives, however, a tenfold higher expression
level. To determine which of the five cysteines at positions 46, 52, 55, 92,
and 95 coordinate the /2Fe-2S/ center, they have been individually mutated into
serines. From these mutants, only C95S forms a functionally active holoprotein.
Thus, residues 46, 52, 55, and 92 are the cysteines that coordinate the
/2Fe-2S/ cluster in adrenodoxin.
;
save_
save_ref_9
_Saveframe_category citation
_Citation_full
;
Muller, A., Muller, J.J., Muller, Y.A., Uhlmann, H., Bernhardt, R. and
Heinemann, U. (1998), Structure 6, S. 269-280
;
_Citation_title 'New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108).'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 9551550
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Muller A. . .
2 Muller J.J. J. .
3 Muller Y.A. A. .
4 Uhlmann H. . .
5 Bernhardt R. . .
6 Heinemann U. . .
stop_
_Journal_abbreviation Structure
_Journal_name_full 'Structure (London, England : 1993)'
_Journal_volume 6
_Journal_issue 3
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
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_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 269
_Page_last 280
_Year 1998
_Details
;
BACKGROUND: Adrenodoxin (Adx) is a [2Fe-2S] ferredoxin involved in steroid
hormone biosynthesis in the adrenal gland mitochondrial matrix of mammals. Adx
is a small soluble protein that transfers electrons from adrenodoxin reductase
(AR) to different cytochrome P450 isoforms where they are consumed in
hydroxylation reactions. A crystallographic study of Adx is expected to reveal
the structural basis for an important electron transfer reaction mediated by a
vertebrate [2Fe-2S] ferredoxin. RESULTS: The crystal structure of a truncated
bovine adrenodoxin, Adx(4-108), was determined at 1.85 A resolution and refined
to a crystallographic R value of 0.195. The structure was determined using
multiple wavelength anomalous dispersion phasing techniques, making use of the
iron atoms in the [2Fe-2S] cluster of the protein. The protein displays the
compact (alpha + beta) fold typical for [2Fe-2S] ferredoxins. The polypeptide
chain is organized into a large core domain and a smaller interaction domain
which comprises 35 residues, including all those previously determined to be
involved in binding to AR and cytochrome P450. A small interdomain motion is
observed as a structural difference between the two independent molecules in
the asymmetric unit of the crystal. Charged residues of Adx(4-108) are
clustered to yield a strikingly asymmetric electric potential of the protein
molecule. CONCLUSIONS: The crystal structure of Adx(4-108) provides the first
detailed description of a vertebrate [2Fe-2S] ferredoxin and serves to explain
a large body of biochemical studies in terms of a three-dimensional structure.
The structure suggests how a change in the redox state of the [2Fe-2S] cluster
may be coupled to a domain motion of the protein. It seems likely that the
clearly asymmetric charge distribution on the surface of Adx(4-108) and the
resulting strong molecular dipole are involved in electrostatic steering of the
interactions with AR and cytochrome P450.
;
save_
save_ref_10
_Saveframe_category citation
_Citation_full
;
Wishart,David S., Bigam,Colin G., Yo,Jian, Abildgaard,Frits ,H. Dyson,
H. Jane , Eric Oldfield, Markley,John L., and Sykes,Brian D. (1995), J.
of. Biomolecular NMR 6, 135-140
;
_Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 8589602
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Wishart D.S. S. .
2 Bigam C.G. G. .
3 Yao J. . .
4 Abildgaard F. . .
5 Dyson H.J. J. .
6 Oldfield E. . .
7 Markley J.L. L. .
8 Sykes B.D. D. .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_name_full 'Journal of biomolecular NMR'
_Journal_volume 6
_Journal_issue 2
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
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_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 135
_Page_last 140
_Year 1995
_Details
;
A considerable degree of variability exists in the way that 1H, 13C and 15N
chemical shifts are reported and referenced for biomolecules. In this article
we explore some of the reasons for this situation and propose guidelines for
future chemical shift referencing and for conversion from many common 1H, 13C
and 15N chemical shift standards, now used in biomolecular NMR, to those
proposed here.
;
save_
##################################
# Molecular system description #
##################################
save_system_bAdx
_Saveframe_category molecular_system
_Mol_system_name 'bovine adrenodoxin'
_Abbreviation_common bAdx
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'bovine adrenodoxin' $bAdx
2[FeS] $FES
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic yes
_System_thiol_state 'free and other bound'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_bAdx
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'bovine adrenodoxin'
_Abbreviation_common bAdx
_Molecular_mass .
_Mol_thiol_state 'free and other bound'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 128
_Mol_residue_sequence
;
SSSEDKITVHFINRDGETLT
TKGKIGDSLLDVVVQNNLDI
DGFGACEGTLACSTCHLIFE
QHIFEKLEAITDEENDMLDL
AYGLTDRSRLGCQICLTKAM
DNMTVRVPDAVSDARESIDM
GMNSSKIE
;
loop_
_Residue_seq_code
_Residue_label
1 SER 2 SER 3 SER 4 GLU 5 ASP
6 LYS 7 ILE 8 THR 9 VAL 10 HIS
11 PHE 12 ILE 13 ASN 14 ARG 15 ASP
16 GLY 17 GLU 18 THR 19 LEU 20 THR
21 THR 22 LYS 23 GLY 24 LYS 25 ILE
26 GLY 27 ASP 28 SER 29 LEU 30 LEU
31 ASP 32 VAL 33 VAL 34 VAL 35 GLN
36 ASN 37 ASN 38 LEU 39 ASP 40 ILE
41 ASP 42 GLY 43 PHE 44 GLY 45 ALA
46 CYS 47 GLU 48 GLY 49 THR 50 LEU
51 ALA 52 CYS 53 SER 54 THR 55 CYS
56 HIS 57 LEU 58 ILE 59 PHE 60 GLU
61 GLN 62 HIS 63 ILE 64 PHE 65 GLU
66 LYS 67 LEU 68 GLU 69 ALA 70 ILE
71 THR 72 ASP 73 GLU 74 GLU 75 ASN
76 ASP 77 MET 78 LEU 79 ASP 80 LEU
81 ALA 82 TYR 83 GLY 84 LEU 85 THR
86 ASP 87 ARG 88 SER 89 ARG 90 LEU
91 GLY 92 CYS 93 GLN 94 ILE 95 CYS
96 LEU 97 THR 98 LYS 99 ALA 100 MET
101 ASP 102 ASN 103 MET 104 THR 105 VAL
106 ARG 107 VAL 108 PRO 109 ASP 110 ALA
111 VAL 112 SER 113 ASP 114 ALA 115 ARG
116 GLU 117 SER 118 ILE 119 ASP 120 MET
121 GLY 122 MET 123 ASN 124 SER 125 SER
126 LYS 127 ILE 128 GLU
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-11-10
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 1AYF "Bovine Adrenodoxin (oxidized)" 82.03 105 100.00 100.00 1.02e-69
PDB 1CJE "Adrenodoxin From Bovine" 99.22 127 100.00 100.00 6.02e-86
PDB 1E6E "Adrenodoxin Reductase/adrenodoxin Complex Of Mitochondrial P450 Systems" 99.22 128 100.00 100.00 6.94e-86
PDB 1L6U "Nmr Structure Of Oxidized Adrenodoxin" 99.22 128 100.00 100.00 6.22e-86
PDB 1L6V "Structure Of Reduced Bovine Adrenodoxin" 100.00 128 100.00 100.00 1.02e-86
PDB 2BT6 "Ru(Bpy)2(Mbpy)-Modified Bovine Adrenodoxin" 83.59 108 99.07 99.07 6.53e-70
PDB 2JQR "Solution Model Of Crosslinked Complex Of Cytochrome C And Adrenodoxin" 82.03 105 98.10 98.10 1.97e-67
DBJ BAA00362 "adrenodoxin [Bos taurus]" 100.00 186 100.00 100.00 3.42e-87
DBJ BAA00363 "adrenodoxin [Bos taurus]" 100.00 186 100.00 100.00 3.42e-87
GB AAA30357 "adrenodoxin precursor, partial [Bos taurus]" 100.00 186 100.00 100.00 4.25e-87
GB AAA30358 "adrenodoxin precursor [Bos taurus]" 98.44 186 100.00 100.00 1.75e-85
GB AAB21264 "hepato-ferredoxin [Bos taurus]" 100.00 186 100.00 100.00 3.42e-87
GB AAI09850 "FDX1 protein [Bos taurus]" 100.00 186 100.00 100.00 3.35e-87
GB ABQ13041 "ferredoxin 1 precursor [Bos taurus]" 100.00 186 100.00 100.00 3.42e-87
REF NP_851354 "adrenodoxin, mitochondrial precursor [Bos taurus]" 98.44 186 100.00 100.00 1.75e-85
REF XP_004329468 "PREDICTED: adrenodoxin, mitochondrial-like [Tursiops truncatus]" 66.41 91 97.65 98.82 1.16e-52
REF XP_005889885 "PREDICTED: adrenodoxin, mitochondrial [Bos mutus]" 100.00 204 100.00 100.00 1.02e-86
REF XP_006072637 "PREDICTED: adrenodoxin, mitochondrial [Bubalus bubalis]" 100.00 186 98.44 100.00 3.23e-86
REF XP_010861227 "PREDICTED: adrenodoxin, mitochondrial [Bison bison bison]" 100.00 158 100.00 100.00 6.38e-87
SP P00257 "RecName: Full=Adrenodoxin, mitochondrial; AltName: Full=Adrenal ferredoxin; AltName: Full=Ferredoxin-1; AltName: Full=Hepato-fe" 100.00 186 100.00 100.00 3.42e-87
TPG DAA22428 "TPA: adrenodoxin, mitochondrial precursor [Bos taurus]" 72.66 153 100.00 100.00 2.69e-60
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 Jul 18 10:07:38 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
_Plasmid
$bAdx 'E. coli' 562 Bacteria . Escherichia coli pkkAdx
stop_
save_
#########################
# Experimental source #
#########################
save_experimental_source
_Saveframe_category experimental_source
loop_
_Mol_label
_Production_method
_Host_organism_name_common
_Genus
_Species
_Strain
_Vector_name
$bAdx 'recombinant technology' . . . . .
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Saveframe_category sample
_Sample_type solution
_Details
;
Every sample was fully 15N,13C labeled, only for definite experiments we used a
only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB).
For each NMR experiment a new sample was neccessary. So we did approximatly 17
samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained
from E. coli and purified as described elsewhere [8]. For 15N-labelled samples,
15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and
13C3-glycerol were introduced into the growth medium. Purity of the protein was
checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.
;
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Concentration_min_value
_Concentration_max_value
_Isotopic_labeling
$bAdx . mM 1.0 4.0 '[U-100% 13C; U-100% 15N]'
D2O 5 % . . .
stop_
save_
save_sample_2
_Saveframe_category sample
_Sample_type solution
_Details
;
Every sample was fully 15N,13C labeled, only for definite experiments we used a
only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB).
For each NMR experiment a new sample was neccessary. So we did approximatly 17
samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained
from E. coli and purified as described elsewhere [8]. For 15N-labelled samples,
15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and
13C3-glycerol were introduced into the growth medium. Purity of the protein was
checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer.
;
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Concentration_min_value
_Concentration_max_value
_Isotopic_labeling
$bAdx . mM 1.0 4.0 '[U-100% 15N]'
D2O 5 % . . .
stop_
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DMX
_Field_strength 500
_Details .
save_
save_NMR_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model 'DMX Avance'
_Field_strength 600
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_3D-TOCSY-(15N,1H)HSQC_1
_Saveframe_category NMR_applied_experiment
_Experiment_name 3D-TOCSY-(15N,1H)HSQC
_Sample_label .
save_
save_3D-NOESY-(15N,1H)HSQC_2
_Saveframe_category NMR_applied_experiment
_Experiment_name 3D-NOESY-(15N,1H)HSQC
_Sample_label .
save_
save_3D-HNHB_3
_Saveframe_category NMR_applied_experiment
_Experiment_name 3D-HNHB
_Sample_label .
save_
save_HNCA_4
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCA
_Sample_label .
save_
save_HN(CO)CA_5
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CO)CA
_Sample_label .
save_
save_H(N)CA,CO_6
_Saveframe_category NMR_applied_experiment
_Experiment_name H(N)CA,CO
_Sample_label .
save_
save_HNCACB_7
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_Sample_label .
save_
save_HCACO_8
_Saveframe_category NMR_applied_experiment
_Experiment_name HCACO
_Sample_label .
save_
save_HNCO_9
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCO
_Sample_label .
save_
save_(HCA)CO(CA)NH_10
_Saveframe_category NMR_applied_experiment
_Experiment_name (HCA)CO(CA)NH
_Sample_label .
save_
save_HBHA(CO)NH_11
_Saveframe_category NMR_applied_experiment
_Experiment_name HBHA(CO)NH
_Sample_label .
save_
save_HCCH-TOCSY_12
_Saveframe_category NMR_applied_experiment
_Experiment_name HCCH-TOCSY
_Sample_label .
save_
save_HCCC(O)NH_13
_Saveframe_category NMR_applied_experiment
_Experiment_name HCCC(O)NH
_Sample_label .
save_
save_NMR_spec_expt__0_1
_Saveframe_category NMR_applied_experiment
_Experiment_name 3D-TOCSY-(15N,1H)HSQC
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_2
_Saveframe_category NMR_applied_experiment
_Experiment_name 3D-NOESY-(15N,1H)HSQC
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_3
_Saveframe_category NMR_applied_experiment
_Experiment_name 3D-HNHB
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_4
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCA
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_5
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CO)CA
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_6
_Saveframe_category NMR_applied_experiment
_Experiment_name H(N)CA,CO
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_7
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_8
_Saveframe_category NMR_applied_experiment
_Experiment_name HCACO
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_9
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCO
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_10
_Saveframe_category NMR_applied_experiment
_Experiment_name (HCA)CO(CA)NH
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_11
_Saveframe_category NMR_applied_experiment
_Experiment_name HBHA(CO)NH
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_12
_Saveframe_category NMR_applied_experiment
_Experiment_name HCCH-TOCSY
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_13
_Saveframe_category NMR_applied_experiment
_Experiment_name HCCC(O)NH
_BMRB_pulse_sequence_accession_number .
_Details .
save_
#######################
# Sample conditions #
#######################
save_cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 7.4 0.2 n/a
temperature 300 1 K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference
_Saveframe_category chemical_shift_reference
_Details .
loop_
_Mol_common_name
_Atom_type
_Atom_isotope_number
_Atom_group
_Chem_shift_units
_Chem_shift_value
_Reference_method
_Reference_type
_External_reference_sample_geometry
_External_reference_location
_External_reference_axis
_Indirect_shift_ratio
DSS H 1 'methyl protons' ppm 0.00 internal direct spherical internal parallel 1.0
DSS C 13 'methyl protons' ppm 0.00 internal indirect spherical internal parallel 0.251449530
DSS N 15 'methyl protons' ppm 0.00 internal indirect spherical internal parallel 0.101329118
stop_
save_
###################################
# Assigned chemical shift lists #
###################################
###################################################################
# Chemical Shift Ambiguity Index Value Definitions #
# #
# The values other than 1 are used for those atoms with different #
# chemical shifts that cannot be assigned to stereospecific atoms #
# or to specific residues or chains. #
# #
# Index Value Definition #
# #
# 1 Unique (including isolated methyl protons, #
# geminal atoms, and geminal methyl #
# groups with identical chemical shifts) #
# (e.g. ILE HD11, HD12, HD13 protons) #
# 2 Ambiguity of geminal atoms or geminal methyl #
# proton groups (e.g. ASP HB2 and HB3 #
# protons, LEU CD1 and CD2 carbons, or #
# LEU HD11, HD12, HD13 and HD21, HD22, #
# HD23 methyl protons) #
# 3 Aromatic atoms on opposite sides of #
# symmetrical rings (e.g. TYR HE1 and HE2 #
# protons) #
# 4 Intraresidue ambiguities (e.g. LYS HG and #
# HD protons or TRP HZ2 and HZ3 protons) #
# 5 Interresidue ambiguities (LYS 12 vs. LYS 27) #
# 6 Intermolecular ambiguities (e.g. ASP 31 CA #
# in monomer 1 and ASP 31 CA in monomer 2 #
# of an asymmetrical homodimer, duplex #
# DNA assignments, or other assignments #
# that may apply to atoms in one or more #
# molecule in the molecular assembly) #
# 9 Ambiguous, specific ambiguity not defined #
# #
###################################################################
save_bAdx1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
3D-TOCSY-(15N,1H)HSQC
3D-NOESY-(15N,1H)HSQC
3D-HNHB
HNCA
HN(CO)CA
H(N)CA,CO
HNCACB
HCACO
HNCO
(HCA)CO(CA)NH
HBHA(CO)NH
HCCH-TOCSY
HCCC(O)NH
stop_
_Sample_conditions_label $cond_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'bovine adrenodoxin'
_Text_data_format .
_Text_data .
loop_
_Atom_shift_assign_ID
_Residue_author_seq_code
_Residue_seq_code
_Residue_label
_Atom_name
_Atom_type
_Chem_shift_value
_Chem_shift_value_error
_Chem_shift_ambiguity_code
1 . 3 SER CA C 58.05 0.03 4
2 . 3 SER CB C 62.81 0.03 4
3 . 4 GLU H H 8.39 0.022 1
4 . 4 GLU HA H 4.24 0.022 1
5 . 4 GLU HB2 H 2.01 0.022 2
6 . 4 GLU HB3 H 1.86 0.022 2
7 . 4 GLU HG2 H 2.37 0.022 2
8 . 4 GLU HG3 H 2.22 0.022 2
9 . 4 GLU C C 175.95 0.03 1
10 . 4 GLU CA C 56.25 0.03 1
11 . 4 GLU CB C 29.35 0.03 1
12 . 4 GLU CG C 35.91 0.03 1
13 . 4 GLU N N 121.2 0.04 1
14 . 5 ASP H H 8.25 0.022 1
15 . 5 ASP HA H 4.54 0.022 1
16 . 5 ASP HB2 H 3.03 0.022 2
17 . 5 ASP HB3 H 2.59 0.022 2
18 . 5 ASP C C 175.15 0.03 1
19 . 5 ASP CA C 53.76 0.03 1
20 . 5 ASP CB C 40.11 0.03 1
21 . 5 ASP N N 120.73 0.04 1
22 . 6 LYS H H 7.88 0.022 1
23 . 6 LYS HA H 4.89 0.022 1
24 . 6 LYS HB2 H 1.59 0.022 2
25 . 6 LYS HG2 H 1.45 0.022 2
26 . 6 LYS HG3 H 1.17 0.022 2
27 . 6 LYS HD2 H 1.66 0.022 4
28 . 6 LYS HE2 H 2.8 0.022 4
29 . 6 LYS C C 175.95 0.03 1
30 . 6 LYS CA C 54.72 0.03 1
31 . 6 LYS CB C 34.71 0.03 1
32 . 6 LYS CG C 24.81 0.03 1
33 . 6 LYS CD C 28.78 0.03 1
34 . 6 LYS CE C 41.72 0.03 1
35 . 6 LYS N N 118.92 0.04 1
36 . 7 ILE H H 8.92 0.022 1
37 . 7 ILE HA H 4.43 0.022 1
38 . 7 ILE HB H 1.85 0.022 1
39 . 7 ILE HG12 H 0.73 0.022 2
40 . 7 ILE HG13 H 0.61 0.022 2
41 . 7 ILE HG2 H 1.04 0.022 1
42 . 7 ILE HD1 H 0.64 0.022 1
43 . 7 ILE C C 174.58 0.03 1
44 . 7 ILE CA C 58.36 0.03 1
45 . 7 ILE CB C 40.11 0.03 1
46 . 7 ILE CG1 C 25.08 0.03 1
47 . 7 ILE CG2 C 17.68 0.03 1
48 . 7 ILE CD1 C 13.46 0.03 1
49 . 7 ILE N N 117.69 0.04 1
50 . 8 THR H H 8.76 0.022 1
51 . 8 THR HA H 4.73 0.022 1
52 . 8 THR HB H 3.83 0.022 1
53 . 8 THR HG2 H 0.78 0.022 1
54 . 8 THR C C 173.78 0.03 1
55 . 8 THR CA C 62.58 0.03 1
56 . 8 THR CB C 68.42 0.03 1
57 . 8 THR CG2 C 21.12 0.03 1
58 . 8 THR N N 121.32 0.04 1
59 . 9 VAL H H 8.53 0.022 1
60 . 9 VAL HA H 4.16 0.022 1
61 . 9 VAL HB H 1.52 0.022 1
62 . 9 VAL HG1 H 0.67 0.022 2
63 . 9 VAL HG2 H 0.35 0.022 2
64 . 9 VAL C C 173.21 0.03 1
65 . 9 VAL CA C 60.47 0.03 1
66 . 9 VAL CB C 34.71 0.03 1
67 . 9 VAL CG1 C 22.6 0.03 2
68 . 9 VAL CG2 C 21.65 0.03 2
69 . 9 VAL N N 124.54 0.04 1
70 . 10 HIS H H 8.57 0.022 1
71 . 10 HIS HA H 5.4 0.022 1
72 . 10 HIS HB2 H 3.24 0.022 2
73 . 10 HIS HB3 H 2.59 0.022 2
74 . 10 HIS C C 174.34 0.03 1
75 . 10 HIS CA C 53.76 0.03 1
76 . 10 HIS CB C 30.82 0.03 1
77 . 10 HIS N N 125.48 0.04 1
78 . 11 PHE H H 9.56 0.022 1
79 . 11 PHE HA H 5.08 0.022 1
80 . 11 PHE HB2 H 3.01 0.022 2
81 . 11 PHE HB3 H 2.21 0.022 2
82 . 11 PHE C C 175.27 0.03 1
83 . 11 PHE CA C 55.1 0.03 1
84 . 11 PHE CB C 40.95 0.03 1
85 . 11 PHE N N 122.32 0.04 1
86 . 12 ILE H H 9.02 0.022 1
87 . 12 ILE HA H 4.66 0.022 1
88 . 12 ILE HB H 1.67 0.022 1
89 . 12 ILE HG12 H 1.28 0.022 2
90 . 12 ILE HG13 H 1.06 0.022 2
91 . 12 ILE HG2 H 0.89 0.022 1
92 . 12 ILE HD1 H 0.66 0.022 1
93 . 12 ILE C C 175.84 0.03 1
94 . 12 ILE CA C 59.9 0.03 1
95 . 12 ILE CB C 36.63 0.03 1
96 . 12 ILE CG1 C 26.14 0.03 1
97 . 12 ILE CG2 C 16.36 0.03 1
98 . 12 ILE CD1 C 12.14 0.03 1
99 . 12 ILE N N 122.9 0.04 1
100 . 13 ASN H H 8.85 0.022 1
101 . 13 ASN HA H 4.69 0.022 1
102 . 13 ASN HB2 H 3.35 0.022 2
103 . 13 ASN HB3 H 2.97 0.022 2
104 . 13 ASN HD21 H 7.83 0.022 2
105 . 13 ASN HD22 H 7.3 0.022 2
106 . 13 ASN C C 176.75 0.03 1
107 . 13 ASN CA C 50.69 0.03 1
108 . 13 ASN CB C 38.07 0.03 1
109 . 13 ASN N N 125.07 0.04 1
110 . 13 ASN ND2 N 112.04 0.04 1
111 . 14 ARG H H 8.55 0.022 1
112 . 14 ARG HA H 4.01 0.022 1
113 . 14 ARG HB2 H 1.78 0.022 2
114 . 14 ARG HG2 H 1.57 0.022 2
115 . 14 ARG HD2 H 3.28 0.022 2
116 . 14 ARG C C 176.07 0.03 1
117 . 14 ARG CA C 58.56 0.03 1
118 . 14 ARG CB C 29.03 0.03 1
119 . 14 ARG CG C 28.2 0.03 1
120 . 14 ARG CD C 43.57 0.03 1
121 . 14 ARG N N 118.92 0.04 1
122 . 15 ASP H H 7.67 0.022 1
123 . 15 ASP HA H 4.54 0.022 1
124 . 15 ASP HB2 H 2.82 0.022 2
125 . 15 ASP HB3 H 2.67 0.022 2
126 . 15 ASP C C 176.46 0.03 1
127 . 15 ASP CA C 52.99 0.03 1
128 . 15 ASP CB C 39.9 0.03 1
129 . 15 ASP N N 116.04 0.04 1
130 . 16 GLY H H 8.17 0.022 1
131 . 16 GLY HA2 H 4.16 0.022 2
132 . 16 GLY HA3 H 3.43 0.022 2
133 . 16 GLY C C 175.81 0.03 1
134 . 16 GLY CA C 44.74 0.03 1
135 . 16 GLY N N 108.31 0.04 1
136 . 17 GLU H H 7.97 0.022 1
137 . 17 GLU HA H 4.26 0.022 1
138 . 17 GLU HB2 H 1.94 0.022 2
139 . 17 GLU HG2 H 2.27 0.022 2
140 . 17 GLU C C 175.38 0.03 1
141 . 17 GLU CA C 55.49 0.03 1
142 . 17 GLU CB C 29.52 0.03 1
143 . 17 GLU CG C 35.64 0.03 1
144 . 17 GLU N N 122.32 0.04 1
145 . 18 THR H H 8.63 0.022 1
146 . 18 THR HA H 4.89 0.022 1
147 . 18 THR HB H 3.97 0.022 1
148 . 18 THR HG2 H 1.06 0.022 1
149 . 18 THR C C 174.13 0.03 1
150 . 18 THR CA C 62.39 0.03 1
151 . 18 THR CB C 68.21 0.03 1
152 . 18 THR CG2 C 21.12 0.03 1
153 . 18 THR N N 119.09 0.04 1
154 . 19 LEU H H 10.02 0.022 1
155 . 19 LEU HA H 4.76 0.022 1
156 . 19 LEU HB2 H 1.9 0.022 2
157 . 19 LEU HB3 H 1.43 0.022 2
158 . 19 LEU HG H 1.7 0.022 1
159 . 19 LEU HD1 H 0.83 0.022 2
160 . 19 LEU C C 175.38 0.03 1
161 . 19 LEU CA C 52.8 0.03 1
162 . 19 LEU CB C 42.05 0.03 1
163 . 19 LEU CG C 25.34 0.03 1
164 . 19 LEU CD1 C 22.7 0.03 2
165 . 19 LEU N N 131.28 0.04 1
166 . 20 THR H H 8.8 0.022 1
167 . 20 THR HA H 4.89 0.022 1
168 . 20 THR HB H 3.78 0.022 1
169 . 20 THR HG2 H 1.17 0.022 1
170 . 20 THR C C 173.9 0.03 1
171 . 20 THR CA C 63.35 0.03 1
172 . 20 THR CB C 69.51 0.03 1
173 . 20 THR CG2 C 22.17 0.03 1
174 . 20 THR N N 122.96 0.04 1
175 . 21 THR H H 8.82 0.022 1
176 . 21 THR HA H 4.71 0.022 1
177 . 21 THR HB H 3.74 0.022 1
178 . 21 THR HG2 H 0.9 0.022 1
179 . 21 THR C C 171.61 0.03 1
180 . 21 THR CA C 59.52 0.03 1
181 . 21 THR CB C 69.51 0.03 1
182 . 21 THR CG2 C 19.53 0.03 1
183 . 21 THR N N 122.49 0.04 1
184 . 22 LYS H H 7.97 0.022 1
185 . 22 LYS HA H 5.54 0.022 1
186 . 22 LYS HB2 H 1.67 0.022 2
187 . 22 LYS HB3 H 1.44 0.022 2
188 . 22 LYS HE2 H 2.76 0.022 2
189 . 22 LYS C C 176.18 0.03 1
190 . 22 LYS CA C 53.38 0.03 1
191 . 22 LYS CB C 35.12 0.03 1
192 . 22 LYS CG C 24.02 0.03 1
193 . 22 LYS CD C 28.78 0.03 1
194 . 22 LYS CE C 41.72 0.03 1
195 . 22 LYS N N 118.33 0.04 1
196 . 23 GLY H H 8.81 0.022 1
197 . 23 GLY HA2 H 4.58 0.022 2
198 . 23 GLY HA3 H 3.2 0.022 2
199 . 23 GLY C C 170.73 0.03 1
200 . 23 GLY CA C 43.4 0.03 1
201 . 23 GLY N N 107.14 0.04 1
202 . 24 LYS H H 8.85 0.022 1
203 . 24 LYS HA H 4.62 0.022 1
204 . 24 LYS HB2 H 1.59 0.022 2
205 . 24 LYS HG2 H 1.38 0.022 2
206 . 24 LYS HE2 H 2.95 0.022 2
207 . 24 LYS C C 175.95 0.03 1
208 . 24 LYS CA C 54.53 0.03 1
209 . 24 LYS CB C 32.98 0.03 1
210 . 24 LYS CG C 24.02 0.03 1
211 . 24 LYS CD C 28.51 0.03 1
212 . 24 LYS CE C 41.57 0.03 1
213 . 24 LYS N N 121.91 0.04 1
214 . 25 ILE H H 8.3 0.022 1
215 . 25 ILE HA H 3.28 0.022 1
216 . 25 ILE HB H 1.7 0.022 1
217 . 25 ILE HG12 H 1.52 0.022 2
218 . 25 ILE HG2 H 0.9 0.022 1
219 . 25 ILE HD1 H 0.71 0.022 1
220 . 25 ILE C C 177.35 0.03 1
221 . 25 ILE CA C 62.78 0.03 1
222 . 25 ILE CB C 36.14 0.03 1
223 . 25 ILE CG1 C 28.25 0.03 1
224 . 25 ILE CG2 C 16.63 0.03 1
225 . 25 ILE CD1 C 11.87 0.03 1
226 . 25 ILE N N 122.49 0.04 1
227 . 26 GLY H H 8.84 0.022 1
228 . 26 GLY HA2 H 4.49 0.022 2
229 . 26 GLY HA3 H 3.56 0.022 2
230 . 26 GLY C C 173.94 0.03 1
231 . 26 GLY CA C 44.55 0.03 1
232 . 26 GLY N N 117.04 0.04 1
233 . 27 ASP H H 8.09 0.022 1
234 . 27 ASP HA H 4.84 0.022 1
235 . 27 ASP HB2 H 2.9 0.022 2
236 . 27 ASP HB3 H 2.82 0.022 2
237 . 27 ASP C C 176.18 0.03 1
238 . 27 ASP CA C 53.95 0.03 1
239 . 27 ASP CB C 40.55 0.03 1
240 . 27 ASP N N 122.32 0.04 1
241 . 28 SER H H 9.68 0.022 1
242 . 28 SER HA H 5.77 0.022 1
243 . 28 SER HB2 H 4.21 0.022 2
244 . 28 SER HB3 H 3.99 0.022 2
245 . 28 SER C C 176.41 0.03 1
246 . 28 SER CA C 56.64 0.03 1
247 . 28 SER CB C 65.62 0.03 1
248 . 28 SER N N 118.04 0.04 1
249 . 29 LEU H H 8.16 0.022 1
250 . 29 LEU HA H 4.21 0.022 1
251 . 29 LEU HB2 H 2.33 0.022 2
252 . 29 LEU HB3 H 1.47 0.022 2
253 . 29 LEU HG H 1.8 0.022 1
254 . 29 LEU HD1 H 1.04 0.022 2
255 . 29 LEU HD2 H 0.85 0.022 2
256 . 29 LEU C C 179.04 0.03 1
257 . 29 LEU CA C 57.4 0.03 1
258 . 29 LEU CB C 40.36 0.03 1
259 . 29 LEU CG C 25.87 0.03 1
260 . 29 LEU CD1 C 23.76 0.03 2
261 . 29 LEU N N 118.68 0.04 1
262 . 30 LEU H H 7.26 0.022 1
263 . 30 LEU HA H 4.49 0.022 1
264 . 30 LEU HB2 H 2.23 0.022 2
265 . 30 LEU HB3 H 1.32 0.022 2
266 . 30 LEU HG H 1.85 0.022 1
267 . 30 LEU HD1 H 0.78 0.022 2
268 . 30 LEU HD2 H 0.66 0.022 2
269 . 30 LEU C C 176.42 0.03 1
270 . 30 LEU CA C 57.79 0.03 1
271 . 30 LEU CB C 42.09 0.03 1
272 . 30 LEU CG C 27.12 0.03 1
273 . 30 LEU CD1 C 22.44 0.03 4
274 . 30 LEU N N 116.75 0.04 1
275 . 31 ASP H H 7.87 0.022 1
276 . 31 ASP HA H 4.31 0.022 1
277 . 31 ASP HB2 H 2.76 0.022 2
278 . 31 ASP HB3 H 2.49 0.022 2
279 . 31 ASP C C 178.01 0.03 1
280 . 31 ASP CA C 57.4 0.03 1
281 . 31 ASP CB C 39.45 0.03 1
282 . 31 ASP N N 120.73 0.04 1
283 . 32 VAL H H 7.75 0.022 1
284 . 32 VAL HA H 3.58 0.022 1
285 . 32 VAL HB H 2.28 0.022 1
286 . 32 VAL HG1 H 1.18 0.022 2
287 . 32 VAL HG2 H 0.85 0.022 2
288 . 32 VAL C C 178.13 0.03 1
289 . 32 VAL CA C 65.85 0.03 1
290 . 32 VAL CB C 31.39 0.03 1
291 . 32 VAL CG1 C 22.7 0.03 1
292 . 32 VAL CG2 C 23.49 0.03 1
293 . 32 VAL N N 117.16 0.04 1
294 . 33 VAL H H 7.42 0.022 1
295 . 33 VAL HA H 3.04 0.022 1
296 . 33 VAL HB H 2.11 0.022 1
297 . 33 VAL HG1 H 0.18 0.022 2
298 . 33 VAL HG2 H 0.56 0.022 2
299 . 33 VAL C C 177.78 0.03 1
300 . 33 VAL CA C 66.61 0.03 1
301 . 33 VAL CB C 31.25 0.03 1
302 . 33 VAL CG1 C 22.97 0.03 4
303 . 33 VAL CG2 C 20.32 0.03 4
304 . 33 VAL N N 120.97 0.04 1
305 . 34 VAL H H 8.46 0.022 1
306 . 34 VAL HA H 3.7 0.022 1
307 . 34 VAL HB H 2.13 0.022 1
308 . 34 VAL HG1 H 0.9 0.022 2
309 . 34 VAL HG2 H 1.09 0.022 2
310 . 34 VAL C C 180.87 0.03 1
311 . 34 VAL CA C 65.65 0.03 1
312 . 34 VAL CB C 31.9 0.03 1
313 . 34 VAL CG1 C 21.65 0.03 4
314 . 34 VAL CG2 C 20.59 0.03 4
315 . 34 VAL N N 118.33 0.04 1
316 . 35 GLN H H 9.14 0.022 1
317 . 35 GLN HA H 4.01 0.022 1
318 . 35 GLN HB2 H 2.01 0.022 2
319 . 35 GLN HG2 H 2.57 0.022 2
320 . 35 GLN HG3 H 2.46 0.022 2
321 . 35 GLN HE21 H 7.42 0.022 2
322 . 35 GLN HE22 H 6.97 0.022 2
323 . 35 GLN C C 177.33 0.03 1
324 . 35 GLN CA C 57.98 0.03 1
325 . 35 GLN CB C 27.36 0.03 1
326 . 35 GLN CG C 34.06 0.03 1
327 . 35 GLN N N 118.68 0.04 1
328 . 35 GLN NE2 N 110.82 0.04 1
329 . 36 ASN H H 7.17 0.022 1
330 . 36 ASN HA H 4.77 0.022 1
331 . 36 ASN HB2 H 2.7 0.022 2
332 . 36 ASN HB3 H 2.51 0.022 2
333 . 36 ASN HD21 H 7.63 0.022 2
334 . 36 ASN HD22 H 6.95 0.022 2
335 . 36 ASN C C 172.87 0.03 1
336 . 36 ASN CA C 52.8 0.03 1
337 . 36 ASN CB C 38.6 0.03 1
338 . 36 ASN N N 112.29 0.04 1
339 . 36 ASN ND2 N 113.05 0.04 1
340 . 37 ASN H H 7.83 0.022 1
341 . 37 ASN HA H 4.31 0.022 1
342 . 37 ASN HB2 H 2.93 0.022 2
343 . 37 ASN HB3 H 2.59 0.022 2
344 . 37 ASN HD21 H 7.51 0.022 2
345 . 37 ASN HD22 H 6.74 0.022 2
346 . 37 ASN C C 174.47 0.03 1
347 . 37 ASN CA C 53.57 0.03 1
348 . 37 ASN CB C 36.44 0.03 1
349 . 37 ASN N N 117.16 0.04 1
350 . 37 ASN ND2 N 112.24 0.04 1
351 . 38 LEU H H 7.78 0.022 1
352 . 38 LEU HA H 4.9 0.022 1
353 . 38 LEU HB2 H 1.29 0.022 2
354 . 38 LEU C C 177.67 0.03 1
355 . 38 LEU CA C 54.91 0.03 1
356 . 38 LEU CB C 41.19 0.03 1
357 . 38 LEU CG C 26.14 0.03 1
358 . 38 LEU CD1 C 25.08 0.03 2
359 . 38 LEU CD2 C 21.91 0.03 2
360 . 38 LEU N N 115.52 0.04 1
361 . 39 ASP H H 8.55 0.022 1
362 . 39 ASP HA H 4.46 0.022 1
363 . 39 ASP HB2 H 2.74 0.022 2
364 . 39 ASP HB3 H 2.43 0.022 2
365 . 39 ASP C C 174.47 0.03 1
366 . 39 ASP CA C 52.99 0.03 1
367 . 39 ASP CB C 38.6 0.03 1
368 . 39 ASP N N 122.84 0.04 1
369 . 40 ILE H H 7.59 0.022 1
370 . 40 ILE HA H 4.12 0.022 1
371 . 40 ILE HB H 1.29 0.022 1
372 . 40 ILE HG12 H 0.9 0.022 2
373 . 40 ILE HG2 H 0.63 0.022 1
374 . 40 ILE HD1 H 0.01 0.022 1
375 . 40 ILE C C 175.61 0.03 1
376 . 40 ILE CA C 59.52 0.03 1
377 . 40 ILE CB C 37.74 0.03 1
378 . 40 ILE CG1 C 25.34 0.03 1
379 . 40 ILE CG2 C 18.48 0.03 1
380 . 40 ILE CD1 C 12.66 0.03 1
381 . 40 ILE N N 123.78 0.04 1
382 . 41 ASP H H 8.53 0.022 1
383 . 41 ASP HA H 4.35 0.022 1
384 . 41 ASP HB2 H 2.64 0.022 2
385 . 41 ASP C C 177.9 0.03 1
386 . 41 ASP CA C 56.25 0.03 1
387 . 41 ASP CB C 40.76 0.03 1
388 . 41 ASP N N 127.77 0.04 1
389 . 42 GLY H H 8.99 0.022 1
390 . 42 GLY HA2 H 4.01 0.022 2
391 . 42 GLY HA3 H 3.73 0.022 2
392 . 42 GLY C C 173.78 0.03 1
393 . 42 GLY CA C 45.7 0.03 1
394 . 42 GLY N N 113.7 0.04 1
395 . 43 PHE H H 7.64 0.022 1
396 . 43 PHE HA H 4.06 0.022 1
397 . 43 PHE HB2 H 3.01 0.022 2
398 . 43 PHE HB3 H 2.01 0.022 2
399 . 43 PHE C C 178.01 0.03 1
400 . 43 PHE CA C 58.75 0.03 1
401 . 43 PHE CB C 40.33 0.03 1
402 . 57 LEU H H 9.39 0.022 1
403 . 57 LEU HA H 4.82 0.022 1
404 . 57 LEU HB2 H 1.66 0.022 2
405 . 57 LEU HG H 0.9 0.022 1
406 . 57 LEU C C 173.56 0.03 1
407 . 57 LEU CA C 53.18 0.03 1
408 . 57 LEU CB C 48.54 0.03 1
409 . 57 LEU CG C 27.98 0.03 1
410 . 57 LEU CD1 C 25.51 0.03 2
411 . 57 LEU CD2 C 23.49 0.03 2
412 . 57 LEU N N 128.35 0.04 1
413 . 58 ILE H H 8.46 0.022 1
414 . 58 ILE HA H 4.46 0.022 1
415 . 58 ILE HB H 1.4 0.022 1
416 . 58 ILE HG12 H 1.23 0.022 2
417 . 58 ILE HG13 H 0.99 0.022 2
418 . 58 ILE HG2 H 0.86 0.022 1
419 . 58 ILE HD1 H 0.61 0.022 1
420 . 58 ILE C C 176.75 0.03 1
421 . 58 ILE CA C 60.86 0.03 1
422 . 58 ILE CB C 39.46 0.03 1
423 . 58 ILE CG1 C 27.46 0.03 1
424 . 58 ILE CG2 C 17.15 0.03 1
425 . 58 ILE CD1 C 13.98 0.03 1
426 . 58 ILE N N 119.5 0.04 1
427 . 59 PHE H H 8.66 0.022 1
428 . 59 PHE HA H 4.51 0.022 1
429 . 59 PHE HB2 H 3.15 0.022 2
430 . 59 PHE HB3 H 3.12 0.022 2
431 . 59 PHE C C 175.5 0.03 1
432 . 59 PHE CA C 57.79 0.03 1
433 . 59 PHE CB C 42.06 0.03 1
434 . 59 PHE N N 127.88 0.04 1
435 . 60 GLU H H 9.18 0.022 1
436 . 60 GLU HA H 4.34 0.022 1
437 . 60 GLU HB2 H 2.05 0.022 2
438 . 60 GLU HB3 H 1.88 0.022 2
439 . 60 GLU HG2 H 2.23 0.022 2
440 . 60 GLU C C 178.78 0.03 1
441 . 60 GLU CA C 56.25 0.03 1
442 . 60 GLU CB C 31.04 0.03 1
443 . 60 GLU CG C 37.49 0.03 1
444 . 60 GLU N N 119.39 0.04 1
445 . 61 GLN H H 9.58 0.022 1
446 . 61 GLN HA H 3.74 0.022 1
447 . 61 GLN HB2 H 2.22 0.022 2
448 . 61 GLN HB3 H 2.12 0.022 2
449 . 61 GLN HG2 H 2.47 0.022 2
450 . 61 GLN HG3 H 2.33 0.022 2
451 . 61 GLN HE21 H 7.97 0.022 2
452 . 61 GLN HE22 H 6.95 0.022 2
453 . 61 GLN C C 176.39 0.03 1
454 . 61 GLN CA C 59.71 0.03 1
455 . 61 GLN CB C 28.44 0.03 1
456 . 61 GLN CG C 31.95 0.03 1
457 . 61 GLN N N 125.3 0.04 1
458 . 61 GLN NE2 N 112.44 0.04 1
459 . 62 HIS H H 8.42 0.022 1
460 . 62 HIS HA H 4.43 0.022 1
461 . 62 HIS HB2 H 3.19 0.022 2
462 . 62 HIS HB3 H 3.09 0.022 2
463 . 62 HIS C C 176.64 0.03 1
464 . 62 HIS CA C 58.36 0.03 1
465 . 62 HIS CB C 28.86 0.03 1
466 . 62 HIS N N 112.82 0.04 1
467 . 63 ILE H H 6.3 0.022 1
468 . 63 ILE HA H 3.81 0.022 1
469 . 63 ILE HB H 2.16 0.022 1
470 . 63 ILE HG12 H 1.38 0.022 2
471 . 63 ILE HG13 H 1.06 0.022 2
472 . 63 ILE HG2 H 0.97 0.022 1
473 . 63 ILE C C 177.44 0.03 1
474 . 63 ILE CA C 59.32 0.03 1
475 . 63 ILE CB C 35.57 0.03 1
476 . 63 ILE CG1 C 25.34 0.03 1
477 . 63 ILE CG2 C 17.15 0.03 1
478 . 63 ILE CD1 C 8.44 0.03 1
479 . 63 ILE N N 119.56 0.04 1
480 . 64 PHE H H 8.7 0.022 1
481 . 64 PHE HA H 3.51 0.022 1
482 . 64 PHE HB2 H 3.09 0.022 2
483 . 64 PHE HB3 H 2.86 0.022 2
484 . 64 PHE C C 177.21 0.03 1
485 . 64 PHE CA C 61.05 0.03 1
486 . 64 PHE CB C 39.68 0.03 1
487 . 64 PHE N N 120.26 0.04 1
488 . 65 GLU H H 7.97 0.022 1
489 . 65 GLU HA H 4.01 0.022 1
490 . 65 GLU HB2 H 2.05 0.022 2
491 . 65 GLU HG2 H 2.5 0.022 2
492 . 65 GLU C C 176.3 0.03 1
493 . 65 GLU CA C 57.4 0.03 1
494 . 65 GLU CB C 29.09 0.03 1
495 . 65 GLU CG C 35.38 0.03 1
496 . 65 GLU N N 113.23 0.04 1
497 . 66 LYS H H 7.43 0.022 1
498 . 66 LYS HA H 4.35 0.022 1
499 . 66 LYS HB2 H 1.98 0.022 2
500 . 66 LYS HB3 H 1.67 0.022 2
501 . 66 LYS HG2 H 1.6 0.022 2
502 . 66 LYS HG3 H 1.37 0.022 2
503 . 66 LYS HD2 H 1.66 0.022 2
504 . 66 LYS HE2 H 3.03 0.022 2
505 . 66 LYS C C 176.3 0.03 1
506 . 66 LYS CA C 54.34 0.03 1
507 . 66 LYS CB C 32.52 0.03 1
508 . 66 LYS CG C 24.29 0.03 1
509 . 66 LYS CD C 28.25 0.03 1
510 . 66 LYS CE C 41.72 0.03 1
511 . 66 LYS N N 116.92 0.04 1
512 . 67 LEU H H 6.76 0.022 1
513 . 67 LEU HA H 4.01 0.022 1
514 . 67 LEU HB2 H 1.21 0.022 2
515 . 67 LEU HG H 1.71 0.022 1
516 . 67 LEU HD1 H 0.42 0.022 1
517 . 67 LEU HD2 H 0.01 0.022 1
518 . 67 LEU C C 177.1 0.03 1
519 . 67 LEU CA C 53.95 0.03 1
520 . 67 LEU CB C 40.55 0.03 1
521 . 67 LEU CG C 24.55 0.03 1
522 . 67 LEU CD1 C 24.99 0.03 2
523 . 67 LEU CD2 C 21.38 0.03 2
524 . 67 LEU N N 119.27 0.04 1
525 . 68 GLU H H 9.05 0.022 1
526 . 68 GLU HA H 3.89 0.022 1
527 . 68 GLU HB2 H 1.96 0.022 2
528 . 68 GLU HB3 H 1.84 0.022 2
529 . 68 GLU HG2 H 2.34 0.022 2
530 . 68 GLU HG3 H 2.26 0.022 2
531 . 68 GLU C C 175.73 0.03 1
532 . 68 GLU CA C 56.25 0.03 1
533 . 68 GLU CB C 29.09 0.03 1
534 . 68 GLU CG C 36.17 0.03 1
535 . 68 GLU N N 121.96 0.04 1
536 . 69 ALA H H 8.21 0.022 1
537 . 69 ALA HA H 3.89 0.022 1
538 . 69 ALA HB H 1.25 0.022 1
539 . 69 ALA C C 178.13 0.03 1
540 . 69 ALA CA C 52.23 0.03 1
541 . 69 ALA CB C 18.06 0.03 1
542 . 69 ALA N N 123.9 0.04 1
543 . 70 ILE H H 8.37 0.022 1
544 . 70 ILE HA H 3.91 0.022 1
545 . 70 ILE HB H 1.44 0.022 1
546 . 70 ILE HG12 H 1.29 0.022 2
547 . 70 ILE HG2 H 0.86 0.022 1
548 . 70 ILE C C 175.84 0.03 1
549 . 70 ILE CA C 62.39 0.03 1
550 . 70 ILE CB C 38.6 0.03 1
551 . 70 ILE CG1 C 28.51 0.03 1
552 . 70 ILE CG2 C 15.83 0.03 1
553 . 70 ILE CD1 C 14.25 0.03 1
554 . 70 ILE N N 124.43 0.04 1
555 . 71 THR H H 7.91 0.022 1
556 . 71 THR HA H 4.46 0.022 1
557 . 71 THR HB H 4.62 0.022 1
558 . 71 THR HG2 H 1.18 0.022 1
559 . 71 THR C C 175.5 0.03 1
560 . 71 THR CA C 60.28 0.03 1
561 . 71 THR CB C 71.45 0.03 1
562 . 71 THR CG2 C 21.12 0.03 1
563 . 71 THR N N 118.27 0.04 1
564 . 72 ASP H H 8.96 0.022 1
565 . 72 ASP HA H 4.24 0.022 1
566 . 72 ASP HB2 H 2.74 0.022 2
567 . 72 ASP HB3 H 2.7 0.022 2
568 . 72 ASP C C 177.55 0.03 1
569 . 72 ASP CA C 57.21 0.03 1
570 . 72 ASP CB C 39.25 0.03 1
571 . 72 ASP N N 122.49 0.04 1
572 . 73 GLU H H 8.95 0.022 1
573 . 73 GLU HA H 3.97 0.022 1
574 . 73 GLU HB2 H 1.94 0.022 2
575 . 73 GLU HG2 H 2.47 0.022 2
576 . 73 GLU HG3 H 2.28 0.022 2
577 . 73 GLU C C 179.04 0.03 1
578 . 73 GLU CA C 60.09 0.03 1
579 . 73 GLU CB C 28.44 0.03 1
580 . 73 GLU CG C 36.97 0.03 1
581 . 73 GLU N N 117.39 0.04 1
582 . 74 GLU H H 7.52 0.022 1
583 . 74 GLU HA H 3.89 0.022 1
584 . 74 GLU HB2 H 2.01 0.022 2
585 . 74 GLU HG2 H 2.96 0.022 2
586 . 74 GLU C C 177.76 0.03 1
587 . 74 GLU CA C 58.75 0.03 1
588 . 74 GLU CB C 28.23 0.03 1
589 . 74 GLU CG C 35.64 0.03 1
590 . 74 GLU N N 119.5 0.04 1
591 . 75 ASN H H 8.56 0.022 1
592 . 75 ASN HA H 4.3 0.022 1
593 . 75 ASN HB2 H 2.93 0.022 2
594 . 75 ASN HB3 H 2.63 0.022 2
595 . 75 ASN HD21 H 7.63 0.022 2
596 . 75 ASN HD22 H 6.72 0.022 2
597 . 75 ASN C C 176.87 0.03 1
598 . 75 ASN CA C 56.64 0.03 1
599 . 75 ASN CB C 38.38 0.03 1
600 . 75 ASN N N 119.56 0.04 1
601 . 75 ASN ND2 N 113.46 0.04 1
602 . 76 ASP H H 8.32 0.022 1
603 . 76 ASP HA H 4.23 0.022 1
604 . 76 ASP HB2 H 2.67 0.022 2
605 . 76 ASP HB3 H 2.51 0.022 2
606 . 76 ASP C C 178.35 0.03 1
607 . 76 ASP CA C 56.64 0.03 1
608 . 76 ASP CB C 39.8 0.03 1
609 . 76 ASP N N 117.33 0.04 1
610 . 77 MET H H 7.06 0.022 1
611 . 77 MET HA H 4.5 0.022 1
612 . 77 MET C C 179.61 0.03 1
613 . 77 MET CA C 55.1 0.03 1
614 . 77 MET CB C 33.2 0.03 1
615 . 77 MET CG C 32.49 0.03 1
616 . 77 MET CE C 19.63 0.03 1
617 . 77 MET N N 116.1 0.04 1
618 . 78 LEU H H 8.79 0.022 1
619 . 78 LEU HA H 3.78 0.022 1
620 . 78 LEU HB2 H 1.75 0.022 2
621 . 78 LEU HG H 1.61 0.022 1
622 . 78 LEU HD1 H 0.76 0.022 2
623 . 78 LEU HD2 H 0.52 0.022 2
624 . 78 LEU C C 178.13 0.03 1
625 . 78 LEU CA C 57.21 0.03 1
626 . 78 LEU CB C 40.92 0.03 1
627 . 78 LEU CG C 26.14 0.03 1
628 . 78 LEU CD1 C 24.55 0.03 2
629 . 78 LEU CD2 C 22.97 0.03 2
630 . 78 LEU N N 123.55 0.04 1
631 . 79 ASP H H 7.85 0.022 1
632 . 79 ASP HA H 4.38 0.022 1
633 . 79 ASP HB2 H 2.67 0.022 2
634 . 79 ASP HB3 H 2.44 0.022 2
635 . 79 ASP C C 177.21 0.03 1
636 . 79 ASP CA C 56.25 0.03 1
637 . 79 ASP CB C 40.55 0.03 1
638 . 79 ASP N N 115.87 0.04 1
639 . 80 LEU H H 7.1 0.022 1
640 . 80 LEU HA H 4.33 0.022 1
641 . 80 LEU HB2 H 1.76 0.022 2
642 . 80 LEU HB3 H 1.63 0.022 2
643 . 80 LEU HG H 1.38 0.022 1
644 . 80 LEU HD1 H 0.85 0.022 2
645 . 80 LEU HD2 H 0.47 0.022 2
646 . 80 LEU C C 177.1 0.03 1
647 . 80 LEU CA C 53.38 0.03 1
648 . 80 LEU CB C 41.41 0.03 1
649 . 80 LEU CG C 26.14 0.03 1
650 . 80 LEU CD1 C 25.08 0.03 2
651 . 80 LEU CD2 C 21.91 0.03 2
652 . 80 LEU N N 116.63 0.04 1
653 . 81 ALA H H 7.85 0.022 1
654 . 81 ALA HA H 4.16 0.022 1
655 . 81 ALA HB H 1.21 0.022 1
656 . 81 ALA C C 176.66 0.03 1
657 . 81 ALA CA C 51.84 0.03 1
658 . 81 ALA CB C 18.75 0.03 1
659 . 81 ALA N N 124.02 0.04 1
660 . 82 TYR H H 8.25 0.022 1
661 . 82 TYR HA H 4.43 0.022 1
662 . 82 TYR HB2 H 2.97 0.022 2
663 . 82 TYR HB3 H 2.82 0.022 2
664 . 82 TYR C C 176.56 0.03 1
665 . 82 TYR CA C 57.4 0.03 1
666 . 82 TYR CB C 38.47 0.03 1
667 . 82 TYR N N 122.43 0.04 1
668 . 83 GLY H H 8.34 0.022 1
669 . 83 GLY HA2 H 4.05 0.022 2
670 . 83 GLY HA3 H 3.58 0.022 2
671 . 83 GLY C C 174.56 0.03 1
672 . 83 GLY CA C 45.89 0.03 1
673 . 83 GLY N N 112.65 0.04 1
674 . 84 LEU H H 7.32 0.022 1
675 . 84 LEU HA H 3.81 0.022 1
676 . 84 LEU HB2 H 1.52 0.022 2
677 . 84 LEU HG H 1.52 0.022 1
678 . 84 LEU HD1 H 0.8 0.022 2
679 . 84 LEU C C 176.41 0.03 1
680 . 84 LEU CA C 56.31 0.03 1
681 . 84 LEU CB C 42.06 0.03 1
682 . 84 LEU CG C 25.87 0.03 1
683 . 84 LEU CD1 C 24.02 0.03 2
684 . 84 LEU CD2 C 23.49 0.03 2
685 . 84 LEU N N 118.51 0.04 1
686 . 85 THR H H 8.77 0.022 1
687 . 85 THR HA H 4.3 0.022 1
688 . 85 THR HB H 4.85 0.022 1
689 . 85 THR HG2 H 1.18 0.022 1
690 . 85 THR C C 174.47 0.03 1
691 . 85 THR CA C 59.52 0.03 1
692 . 85 THR CB C 73.1 0.03 1
693 . 85 THR CG2 C 21.38 0.03 1
694 . 85 THR N N 116.69 0.04 1
695 . 86 ASP H H 8.56 0.022 1
696 . 86 ASP HA H 4.39 0.022 1
697 . 86 ASP HB2 H 2.67 0.022 2
698 . 86 ASP HB3 H 2.63 0.022 2
699 . 86 ASP C C 175.61 0.03 1
700 . 86 ASP CA C 54.14 0.03 1
701 . 86 ASP CB C 38.91 0.03 1
702 . 86 ASP N N 117.74 0.04 1
703 . 87 ARG H H 8.07 0.022 1
704 . 87 ARG HA H 2.87 0.022 1
705 . 87 ARG HB2 H 2.05 0.022 2
706 . 87 ARG HB3 H 1.95 0.022 2
707 . 87 ARG HG2 H 1.18 0.022 2
708 . 87 ARG HG3 H 0.8 0.022 2
709 . 87 ARG HD2 H 3.14 0.022 2
710 . 87 ARG HD3 H 3.04 0.022 2
711 . 87 ARG C C 175 0.03 1
712 . 87 ARG CA C 54.3 0.03 1
713 . 87 ARG CB C 29.64 0.03 1
714 . 87 ARG CG C 27.19 0.03 1
715 . 87 ARG CD C 42.78 0.03 1
716 . 87 ARG N N 119.57 0.04 1
717 . 88 SER H H 6.88 0.022 1
718 . 88 SER HA H 5.38 0.022 1
719 . 88 SER HB2 H 3.85 0.022 2
720 . 88 SER HB3 H 3.78 0.022 2
721 . 88 SER C C 174.01 0.03 1
722 . 88 SER CA C 60.28 0.03 1
723 . 88 SER CB C 64.32 0.03 1
724 . 88 SER N N 119.56 0.04 1
725 . 89 ARG H H 9.17 0.022 1
726 . 89 ARG HA H 4.84 0.022 1
727 . 89 ARG HB2 H 2.02 0.022 2
728 . 89 ARG HB3 H 1.68 0.022 2
729 . 89 ARG C C 175.5 0.03 1
730 . 89 ARG CA C 52.23 0.03 1
731 . 89 ARG CB C 33.63 0.03 1
732 . 89 ARG N N 117.28 0.04 1
733 . 94 ILE C C 176.41 0.03 1
734 . 94 ILE CA C 57.19 0.03 1
735 . 94 ILE CB C 36.01 0.03 1
736 . 94 ILE CG1 C 25.08 0.03 1
737 . 94 ILE CG2 C 17.42 0.03 1
738 . 94 ILE CD1 C 8.44 0.03 1
739 . 95 CYS H H 7.97 0.022 1
740 . 95 CYS HA H 4.61 0.022 1
741 . 95 CYS HB2 H 1.98 0.022 2
742 . 95 CYS HB3 H 1.06 0.022 2
743 . 95 CYS C C 174.65 0.03 1
744 . 95 CYS CA C 52.99 0.03 1
745 . 95 CYS CB C 40.14 0.03 1
746 . 95 CYS N N 124.54 0.04 1
747 . 96 LEU H H 9.03 0.022 1
748 . 96 LEU HA H 4.62 0.022 1
749 . 96 LEU HB2 H 1.98 0.022 2
750 . 96 LEU HB3 H 1.06 0.022 2
751 . 96 LEU HG H 1.77 0.022 1
752 . 96 LEU HD1 H 0.72 0.022 2
753 . 96 LEU HD2 H 0.66 0.022 2
754 . 96 LEU C C 178.3 0.03 1
755 . 96 LEU CA C 55.49 0.03 1
756 . 96 LEU CB C 41.57 0.03 1
757 . 96 LEU CG C 26.4 0.03 1
758 . 96 LEU CD1 C 24.29 0.03 2
759 . 96 LEU N N 121.55 0.04 1
760 . 97 THR H H 7.72 0.022 1
761 . 97 THR HA H 4.65 0.022 1
762 . 97 THR HB H 4.54 0.022 1
763 . 97 THR HG2 H 1.16 0.022 1
764 . 97 THR C C 174.81 0.03 1
765 . 97 THR CA C 58.56 0.03 1
766 . 97 THR CB C 71.02 0.03 1
767 . 97 THR CG2 C 21.12 0.03 1
768 . 97 THR N N 113.47 0.04 1
769 . 98 LYS H H 9.04 0.022 1
770 . 98 LYS HA H 3.81 0.022 1
771 . 98 LYS HB2 H 1.88 0.022 2
772 . 98 LYS HG2 H 1.47 0.022 2
773 . 98 LYS HG3 H 1.37 0.022 2
774 . 98 LYS HD2 H 1.64 0.022 2
775 . 98 LYS HE2 H 2.95 0.022 2
776 . 98 LYS C C 178.13 0.03 1
777 . 98 LYS CA C 58.88 0.03 1
778 . 98 LYS CB C 31.25 0.03 1
779 . 98 LYS CG C 24.55 0.03 1
780 . 98 LYS CD C 28.51 0.03 1
781 . 98 LYS CE C 41.46 0.03 1
782 . 98 LYS N N 120.56 0.04 1
783 . 99 ALA H H 7.86 0.022 1
784 . 99 ALA HA H 4.12 0.022 1
785 . 99 ALA HB H 1.33 0.022 1
786 . 99 ALA C C 177.67 0.03 1
787 . 99 ALA CA C 53.18 0.03 1
788 . 99 ALA CB C 17.89 0.03 1
789 . 99 ALA N N 119.91 0.04 1
790 . 100 MET H H 7.62 0.022 1
791 . 100 MET HA H 4.01 0.022 1
792 . 100 MET HB2 H 2.44 0.022 2
793 . 100 MET HB3 H 1.99 0.022 2
794 . 100 MET C C 173.9 0.03 1
795 . 100 MET CA C 56.06 0.03 1
796 . 100 MET CB C 31.47 0.03 1
797 . 100 MET CG C 33.53 0.03 1
798 . 100 MET N N 115.58 0.04 1
799 . 101 ASP H H 7.27 0.022 1
800 . 101 ASP HA H 4.39 0.022 1
801 . 101 ASP HB2 H 2.66 0.022 2
802 . 101 ASP HB3 H 2.47 0.022 2
803 . 101 ASP C C 177.55 0.03 1
804 . 101 ASP CA C 56.25 0.03 1
805 . 101 ASP CB C 40.34 0.03 1
806 . 101 ASP N N 118.27 0.04 1
807 . 102 ASN H H 10.04 0.022 1
808 . 102 ASN HA H 3.81 0.022 1
809 . 102 ASN HB2 H 3.16 0.022 2
810 . 102 ASN HB3 H 2.97 0.022 2
811 . 102 ASN HD21 H 7.61 0.022 2
812 . 102 ASN HD22 H 6.85 0.022 2
813 . 102 ASN C C 174.01 0.03 1
814 . 102 ASN CA C 55.29 0.03 1
815 . 102 ASN CB C 37.3 0.03 1
816 . 102 ASN N N 122.96 0.04 1
817 . 102 ASN ND2 N 114.48 0.04 1
818 . 103 MET H H 8.43 0.022 1
819 . 103 MET HA H 4.62 0.022 1
820 . 103 MET HB2 H 2.17 0.022 2
821 . 103 MET HG2 H 2.95 0.022 2
822 . 103 MET HE H 2.01 0.022 1
823 . 103 MET C C 172.87 0.03 1
824 . 103 MET CA C 56.06 0.03 1
825 . 103 MET CB C 30.82 0.03 1
826 . 103 MET CG C 32.48 0.03 1
827 . 103 MET CE C 20.4 0.03 1
828 . 103 MET N N 118.1 0.04 1
829 . 104 THR H H 8.57 0.022 1
830 . 104 THR HA H 5.35 0.022 1
831 . 104 THR HB H 3.66 0.022 1
832 . 104 THR HG2 H 0.98 0.022 1
833 . 104 THR C C 175.5 0.03 1
834 . 104 THR CA C 61.24 0.03 1
835 . 104 THR CB C 69.72 0.03 1
836 . 104 THR CG2 C 21.12 0.03 1
837 . 104 THR N N 116.69 0.04 1
838 . 105 VAL H H 9.11 0.022 1
839 . 105 VAL HA H 4.5 0.022 1
840 . 105 VAL HB H 1.25 0.022 1
841 . 105 VAL HG1 H 0.04 0.022 2
842 . 105 VAL HG2 H 0 0.022 2
843 . 105 VAL C C 172.98 0.03 1
844 . 105 VAL CA C 57.79 0.03 1
845 . 105 VAL CB C 33.63 0.03 1
846 . 105 VAL CG1 C 22.7 0.03 2
847 . 105 VAL CG2 C 19 0.03 2
848 . 105 VAL N N 122.73 0.04 1
849 . 106 ARG H H 8.44 0.022 1
850 . 106 ARG HA H 4.81 0.022 1
851 . 106 ARG HB2 H 1.63 0.022 2
852 . 106 ARG HB3 H 1.45 0.022 2
853 . 106 ARG HG2 H 1.29 0.022 2
854 . 106 ARG HD2 H 2.99 0.022 2
855 . 106 ARG C C 174.47 0.03 1
856 . 106 ARG CA C 53.95 0.03 1
857 . 106 ARG CB C 32.98 0.03 1
858 . 106 ARG CG C 27.48 0.03 1
859 . 106 ARG CD C 43.04 0.03 1
860 . 106 ARG N N 121.14 0.04 1
861 . 107 VAL H H 8.35 0.022 1
862 . 107 VAL HA H 4.45 0.022 1
863 . 107 VAL HB H 2.23 0.022 1
864 . 107 VAL HG1 H 1.18 0.022 2
865 . 107 VAL HG2 H 0.9 0.022 2
866 . 107 VAL C C 177.56 0.03 1
867 . 107 VAL CA C 59.32 0.03 1
868 . 107 VAL CB C 31.59 0.03 1
869 . 107 VAL N N 124.6 0.04 1
870 . 108 PRO HA H 4.24 0.022 1
871 . 108 PRO HB2 H 1.98 0.022 2
872 . 108 PRO HB3 H 1.9 0.022 2
873 . 108 PRO HD2 H 3.65 0.022 2
874 . 108 PRO C C 175.69 0.03 1
875 . 108 PRO CA C 62.2 0.03 1
876 . 108 PRO CB C 31.68 0.03 1
877 . 108 PRO CG C 26.14 0.03 1
878 . 108 PRO CD C 50.7 0.03 1
879 . 109 ASP H H 8.47 0.022 1
880 . 109 ASP HA H 4.39 0.022 1
881 . 109 ASP HB2 H 2.74 0.022 2
882 . 109 ASP HB3 H 2.67 0.022 2
883 . 109 ASP C C 175.15 0.03 1
884 . 109 ASP CA C 54.34 0.03 1
885 . 109 ASP CB C 40.76 0.03 1
886 . 109 ASP N N 120.03 0.04 1
887 . 110 ALA H H 8.16 0.022 1
888 . 110 ALA HA H 4.3 0.022 1
889 . 110 ALA HB H 1.17 0.022 1
890 . 110 ALA C C 176.75 0.03 1
891 . 110 ALA CA C 51.07 0.03 1
892 . 110 ALA CB C 19.37 0.03 1
893 . 110 ALA N N 122.28 0.04 1
894 . 111 VAL H H 7.85 0.022 1
895 . 111 VAL HA H 3.85 0.022 1
896 . 111 VAL HB H 1.82 0.022 1
897 . 111 VAL HG1 H 0.78 0.022 2
898 . 111 VAL C C 174.81 0.03 1
899 . 111 VAL CA C 61.43 0.03 1
900 . 111 VAL CB C 32.11 0.03 1
901 . 111 VAL CG1 C 20.06 0.03 2
902 . 111 VAL CG2 C 19.8 0.03 2
903 . 111 VAL N N 118.11 0.04 1
904 . 112 SER H H 8.12 0.022 1
905 . 112 SER HA H 4.14 0.022 1
906 . 112 SER HB2 H 3.83 0.022 2
907 . 112 SER HB3 H 3.79 0.022 2
908 . 112 SER C C 178.24 0.03 1
909 . 112 SER CA C 57.4 0.03 1
910 . 112 SER CB C 63.24 0.03 1
911 . 112 SER N N 118.68 0.04 1
912 . 113 ASP H H 8.2 0.022 1
913 . 113 ASP HA H 4.18 0.022 1
914 . 113 ASP HB2 H 2.97 0.022 2
915 . 113 ASP HB3 H 2.81 0.022 2
916 . 113 ASP C C 175.73 0.03 1
917 . 113 ASP CA C 53.51 0.03 1
918 . 113 ASP CB C 40.55 0.03 1
919 . 113 ASP N N 123.19 0.04 1
920 . 114 ALA H H 8.23 0.022 1
921 . 114 ALA HA H 4.26 0.022 1
922 . 114 ALA HB H 1.34 0.022 1
923 . 114 ALA CA C 52 0.03 1
924 . 114 ALA CB C 18.5 0.03 1
925 . 114 ALA N N 124.84 0.04 1
926 . 115 ARG H H 8.28 0.022 1
927 . 115 ARG HA H 4.26 0.022 1
928 . 115 ARG HB2 H 1.8 0.022 2
929 . 115 ARG HB3 H 1.64 0.022 2
930 . 115 ARG CA C 55.67 0.03 1
931 . 115 ARG CB C 29.96 0.03 1
932 . 115 ARG CG C 26.4 0.03 1
933 . 115 ARG CD C 42.78 0.03 1
934 . 115 ARG N N 119.97 0.04 1
935 . 116 GLU H H 8.37 0.022 1
936 . 116 GLU HA H 4.26 0.022 1
937 . 116 GLU HB2 H 2.03 0.022 2
938 . 116 GLU HB3 H 1.92 0.022 2
939 . 116 GLU HG2 H 2.23 0.022 2
940 . 116 GLU CA C 55.89 0.03 1
941 . 116 GLU CB C 29.52 0.03 1
942 . 116 GLU CG C 35.64 0.03 1
943 . 116 GLU N N 121.85 0.04 1
944 . 117 SER H H 8.28 0.022 1
945 . 117 SER HA H 4.8 0.022 1
946 . 117 SER HB2 H 3.79 0.022 2
947 . 117 SER CA C 57.62 0.03 1
948 . 117 SER CB C 63.02 0.03 1
949 . 117 SER N N 116.69 0.04 1
950 . 118 ILE H H 8.05 0.022 1
951 . 118 ILE HA H 4.18 0.022 1
952 . 118 ILE HB H 1.88 0.022 1
953 . 118 ILE HG12 H 0.9 0.022 2
954 . 118 ILE CA C 60.64 0.03 1
955 . 118 ILE CB C 38.17 0.03 1
956 . 118 ILE CG1 C 26.66 0.03 1
957 . 118 ILE CG2 C 16.89 0.03 1
958 . 118 ILE CD1 C 12.66 0.03 1
959 . 118 ILE N N 122.28 0.04 1
960 . 119 ASP H H 8.35 0.022 1
961 . 119 ASP HA H 4.61 0.022 1
962 . 119 ASP HB2 H 2.74 0.022 1
963 . 119 ASP HB3 H 2.58 0.022 1
964 . 119 ASP CA C 53.73 0.03 1
965 . 119 ASP CB C 40.55 0.03 1
966 . 119 ASP N N 123.84 0.04 1
967 . 120 MET CA C 55.19 0.03 1
968 . 120 MET CB C 31.68 0.03 1
969 . 120 MET CG C 28.25 0.03 1
970 . 120 MET CE C 19.53 0.03 1
971 . 121 GLY H H 8.49 0.022 1
972 . 121 GLY HA2 H 4.5 0.022 2
973 . 121 GLY C C 173.95 0.03 1
974 . 121 GLY CA C 45.13 0.03 1
975 . 121 GLY N N 109.36 0.04 1
976 . 122 MET H H 8.11 0.022 1
977 . 122 MET HA H 4.24 0.022 1
978 . 122 MET HB2 H 2.01 0.022 2
979 . 122 MET HB3 H 1.86 0.022 2
980 . 122 MET HG2 H 2.18 0.022 2
981 . 122 MET C C 175.05 0.03 1
982 . 122 MET CA C 54.85 0.03 1
983 . 122 MET CB C 29.31 0.03 1
984 . 122 MET CG C 31.42 0.03 1
985 . 122 MET CE C 19.75 0.03 1
986 . 122 MET N N 119.62 0.04 1
987 . 123 ASN H H 8.03 0.022 1
988 . 123 ASN C C 179.27 0.03 1
989 . 123 ASN CA C 54.34 0.03 1
990 . 123 ASN CB C 39.9 0.03 1
991 . 123 ASN N N 125.07 0.04 1
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