data_5466
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Structural model for an alkaline form of ferricytochrome c
;
_BMRB_accession_number 5466
_BMRB_flat_file_name bmr5466.str
_Entry_type original
_Submission_date 2002-07-16
_Accession_date 2002-07-16
_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 Assfalg M. . .
2 Bertini I. . .
3 Dolfi A. . .
4 Turano P. . .
5 Mauk A. G. .
6 Rosell F. I. .
7 Gray H. B. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 348
"15N chemical shifts" 72
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2003-04-23 original author .
stop_
_Original_release_date 2003-04-23
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title 'Structural Model for an Alkaline form of Ferricytochrome C'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 22505586
_PubMed_ID 12617658
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Assfalg M. . .
2 Bertini I. . .
3 Dolfi A. . .
4 Turano P. . .
5 Mauk A. G. .
6 Rosell F. I. .
7 Gray H. B. .
stop_
_Journal_abbreviation 'J. Am. Chem. Soc.'
_Journal_volume 125
_Journal_issue 10
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 2913
_Page_last 2922
_Year 2003
_Details .
loop_
_Keyword
'alkaline transition'
'cytochrome c; NMR structure'
stop_
save_
##################################
# Molecular system description #
##################################
save_system_cytochrome_c
_Saveframe_category molecular_system
_Mol_system_name 'Cytochrome c, iso-1'
_Abbreviation_common 'cyt c'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'Cytochrome c, iso-1' $cyt_c_iso1
'HEME C reduced' $HEM
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'not reported'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_cyt_c_iso1
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'Cytochrome c, iso-1'
_Abbreviation_common 'Cyt c'
_Molecular_mass .
_Mol_thiol_state 'not reported'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 95
_Mol_residue_sequence
;
LFKTRCLQCHTVEKGGPHKV
GPNLHGIFGRHSGQAEGYSY
TDANIKKNVLWDENNMSEYL
TNPAKYIPGTAMAFGGLKKE
KDRNDLITYLKKATE
;
loop_
_Residue_seq_code
_Residue_author_seq_code
_Residue_label
1 9 LEU 2 10 PHE 3 11 LYS 4 12 THR 5 13 ARG
6 14 CYS 7 15 LEU 8 16 GLN 9 17 CYS 10 18 HIS
11 19 THR 12 20 VAL 13 21 GLU 14 22 LYS 15 23 GLY
16 24 GLY 17 25 PRO 18 26 HIS 19 27 LYS 20 28 VAL
21 29 GLY 22 30 PRO 23 31 ASN 24 32 LEU 25 33 HIS
26 34 GLY 27 35 ILE 28 36 PHE 29 37 GLY 30 38 ARG
31 39 HIS 32 40 SER 33 41 GLY 34 42 GLN 35 43 ALA
36 44 GLU 37 45 GLY 38 46 TYR 39 47 SER 40 48 TYR
41 49 THR 42 50 ASP 43 51 ALA 44 52 ASN 45 53 ILE
46 54 LYS 47 55 LYS 48 56 ASN 49 57 VAL 50 58 LEU
51 59 TRP 52 60 ASP 53 61 GLU 54 62 ASN 55 63 ASN
56 64 MET 57 65 SER 58 66 GLU 59 67 TYR 60 68 LEU
61 69 THR 62 70 ASN 63 71 PRO 64 72 ALA 65 73 LYS
66 74 TYR 67 75 ILE 68 76 PRO 69 77 GLY 70 78 THR
71 79 ALA 72 80 MET 73 81 ALA 74 82 PHE 75 83 GLY
76 84 GLY 77 85 LEU 78 86 LYS 79 87 LYS 80 88 GLU
81 89 LYS 82 90 ASP 83 91 ARG 84 92 ASN 85 93 ASP
86 94 LEU 87 95 ILE 88 96 THR 89 97 TYR 90 98 LEU
91 99 LYS 92 100 LYS 93 101 ALA 94 102 THR 95 103 GLU
stop_
_Sequence_homology_query_date 2008-08-19
_Sequence_homology_query_revised_last_date 2008-08-19
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 1LMS 'Structural Model For An Alkaline Form Of Ferricytochrome C' 100.00 108 100.00 100.00 1.20e-50
stop_
save_
#############
# Ligands #
#############
save_HEM
_Saveframe_category ligand
_Mol_type non-polymer
_Name_common "HEM (PROTOPORPHYRIN IX CONTAINING FE)"
_BMRB_code .
_PDB_code HEM
_Molecular_mass 616.487
_Mol_charge 0
_Mol_paramagnetic .
_Mol_aromatic yes
_Details
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Fri Jun 10 14:42:48 2011
;
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
CHA CHA C . 0 . ?
CHB CHB C . 0 . ?
CHC CHC C . 0 . ?
CHD CHD C . 0 . ?
C1A C1A C . 0 . ?
C2A C2A C . 0 . ?
C3A C3A C . 0 . ?
C4A C4A C . 0 . ?
CMA CMA C . 0 . ?
CAA CAA C . 0 . ?
CBA CBA C . 0 . ?
CGA CGA C . 0 . ?
O1A O1A O . 0 . ?
O2A O2A O . 0 . ?
C1B C1B C . 0 . ?
C2B C2B C . 0 . ?
C3B C3B C . 0 . ?
C4B C4B C . 0 . ?
CMB CMB C . 0 . ?
CAB CAB C . 0 . ?
CBB CBB C . 0 . ?
C1C C1C C . 0 . ?
C2C C2C C . 0 . ?
C3C C3C C . 0 . ?
C4C C4C C . 0 . ?
CMC CMC C . 0 . ?
CAC CAC C . 0 . ?
CBC CBC C . 0 . ?
C1D C1D C . 0 . ?
C2D C2D C . 0 . ?
C3D C3D C . 0 . ?
C4D C4D C . 0 . ?
CMD CMD C . 0 . ?
CAD CAD C . 0 . ?
CBD CBD C . 0 . ?
CGD CGD C . 0 . ?
O1D O1D O . 0 . ?
O2D O2D O . 0 . ?
NA NA N . 0 . ?
NB NB N . 0 . ?
NC NC N . 0 . ?
ND ND N . 0 . ?
FE FE FE . 0 . ?
HHB HHB H . 0 . ?
HHC HHC H . 0 . ?
HHD HHD H . 0 . ?
HMA HMA H . 0 . ?
HMAA HMAA H . 0 . ?
HMAB HMAB H . 0 . ?
HAA HAA H . 0 . ?
HAAA HAAA H . 0 . ?
HBA HBA H . 0 . ?
HBAA HBAA H . 0 . ?
HMB HMB H . 0 . ?
HMBA HMBA H . 0 . ?
HMBB HMBB H . 0 . ?
HAB HAB H . 0 . ?
HBB HBB H . 0 . ?
HBBA HBBA H . 0 . ?
HMC HMC H . 0 . ?
HMCA HMCA H . 0 . ?
HMCB HMCB H . 0 . ?
HAC HAC H . 0 . ?
HBC HBC H . 0 . ?
HBCA HBCA H . 0 . ?
HMD HMD H . 0 . ?
HMDA HMDA H . 0 . ?
HMDB HMDB H . 0 . ?
HAD HAD H . 0 . ?
HADA HADA H . 0 . ?
HBD HBD H . 0 . ?
HBDA HBDA H . 0 . ?
H2A H2A H . 0 . ?
H2D H2D H . 0 . ?
HHA HHA H . 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 CHA C1A ? ?
DOUB CHA C4D ? ?
SING CHA HHA ? ?
SING CHB C4A ? ?
DOUB CHB C1B ? ?
SING CHB HHB ? ?
SING CHC C4B ? ?
DOUB CHC C1C ? ?
SING CHC HHC ? ?
DOUB CHD C4C ? ?
SING CHD C1D ? ?
SING CHD HHD ? ?
DOUB C1A C2A ? ?
SING C1A NA ? ?
SING C2A C3A ? ?
SING C2A CAA ? ?
DOUB C3A C4A ? ?
SING C3A CMA ? ?
SING C4A NA ? ?
SING CMA HMA ? ?
SING CMA HMAA ? ?
SING CMA HMAB ? ?
SING CAA CBA ? ?
SING CAA HAA ? ?
SING CAA HAAA ? ?
SING CBA CGA ? ?
SING CBA HBA ? ?
SING CBA HBAA ? ?
DOUB CGA O1A ? ?
SING CGA O2A ? ?
SING C1B C2B ? ?
SING C1B NB ? ?
DOUB C2B C3B ? ?
SING C2B CMB ? ?
SING C3B C4B ? ?
SING C3B CAB ? ?
DOUB C4B NB ? ?
SING CMB HMB ? ?
SING CMB HMBA ? ?
SING CMB HMBB ? ?
DOUB CAB CBB ? ?
SING CAB HAB ? ?
SING CBB HBB ? ?
SING CBB HBBA ? ?
SING C1C C2C ? ?
SING C1C NC ? ?
DOUB C2C C3C ? ?
SING C2C CMC ? ?
SING C3C C4C ? ?
SING C3C CAC ? ?
SING C4C NC ? ?
SING CMC HMC ? ?
SING CMC HMCA ? ?
SING CMC HMCB ? ?
DOUB CAC CBC ? ?
SING CAC HAC ? ?
SING CBC HBC ? ?
SING CBC HBCA ? ?
SING C1D C2D ? ?
DOUB C1D ND ? ?
DOUB C2D C3D ? ?
SING C2D CMD ? ?
SING C3D C4D ? ?
SING C3D CAD ? ?
SING C4D ND ? ?
SING CMD HMD ? ?
SING CMD HMDA ? ?
SING CMD HMDB ? ?
SING CAD CBD ? ?
SING CAD HAD ? ?
SING CAD HADA ? ?
SING CBD CGD ? ?
SING CBD HBD ? ?
SING CBD HBDA ? ?
DOUB CGD O1D ? ?
SING CGD O2D ? ?
SING O2A H2A ? ?
SING O2D H2D ? ?
SING FE NA ? ?
SING FE NB ? ?
SING FE NC ? ?
SING FE ND ? ?
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
$cyt_c_iso1 'baker's yeast' 4932 Eukaryota Fungi Saccharomyces cerevisiae
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
$cyt_c_iso1 'recombinant technology' 'E. coli' Escherichia coli . .
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$cyt_c_iso1 2 mM .
$HEM . mM .
'phosphate buffer' 50 mM .
H2O 90 % .
D2O 10 % .
stop_
save_
############################
# Computer software used #
############################
save_DYANA
_Saveframe_category software
_Name DYANA
_Version 1.5
loop_
_Task
'structure solution'
stop_
_Details Guentert
save_
save_CORMA
_Saveframe_category software
_Name CORMA
_Version .
loop_
_Task
'iterative matrix relaxation'
stop_
_Details .
save_
save_AMBER
_Saveframe_category software
_Name AMBER
_Version 6.0
loop_
_Task
refinement
stop_
_Details 'CASE AND KOLLMAN'
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 800
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_2D_NOESY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D NOESY'
_Sample_label $sample_1
save_
save_2D_TOCSY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D TOCSY'
_Sample_label $sample_1
save_
save_3D_15N-separated_NOESY_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 15N-separated NOESY'
_Sample_label $sample_1
save_
save_NMR_spec_expt__0_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D TOCSY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 15N-separated NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
#######################
# Sample conditions #
#######################
save_sample_cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
'ionic strength' 50 . mM
pH 11.1 . pH
pressure 1 . atm
temperature 298 . 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_citation_label
_Correction_value_citation_label
. H 1 . ppm . . . . . . $entry_citation $entry_citation
. N 15 . ppm . . . . . . $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_chemical_shift_set_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_cond_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'Cytochrome c, iso-1'
_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 . 1 LEU N N 124.09 . .
2 . 1 LEU H H 7.92 . .
3 . 1 LEU HB2 H 2.16 . .
4 . 1 LEU HB3 H 1.71 . .
5 . 1 LEU HA H 4.02 . .
6 . 1 LEU HG H 1.30 . .
7 . 1 LEU HD1 H 1.10 . .
8 . 1 LEU HD2 H 0.87 . .
9 . 2 PHE N N 120.3 . .
10 . 2 PHE H H 8.8 . .
11 . 2 PHE HB2 H 2.89 . .
12 . 2 PHE HA H 3.93 . .
13 . 2 PHE HD1 H 7.03 . .
14 . 2 PHE HE1 H 6.12 . .
15 . 2 PHE HZ H 8.62 . .
16 . 3 LYS N N 120.3 . .
17 . 3 LYS H H 8.24 . .
18 . 3 LYS HB2 H 1.92 . .
19 . 3 LYS HA H 3.1 . .
20 . 3 LYS HG2 H 1.20 . .
21 . 3 LYS HG3 H 1.07 . .
22 . 3 LYS HD2 H 0.73 . .
23 . 3 LYS HD3 H 0.54 . .
24 . 4 THR N N 107.22 . .
25 . 4 THR H H 7.93 . .
26 . 4 THR HA H 4.27 . .
27 . 4 THR HB H 3.95 . .
28 . 4 THR HG2 H 1.29 . .
29 . 5 ARG N N 116.83 . .
30 . 5 ARG H H 8.55 . .
31 . 5 ARG HA H 5.06 . .
32 . 5 ARG HB2 H 2.2 . .
33 . 5 ARG HB3 H 2.09 . .
34 . 5 ARG HG2 H 2.50 . .
35 . 6 CYS N N 115.18 . .
36 . 6 CYS H H 7.99 . .
37 . 6 CYS HA H 5.18 . .
38 . 6 CYS HB2 H 1.73 . .
39 . 6 CYS HB3 H 0.84 . .
40 . 7 LEU N N 121.37 . .
41 . 7 LEU H H 7.18 . .
42 . 7 LEU HA H 3.95 . .
43 . 7 LEU HD1 H 1.72 . .
44 . 7 LEU HD2 H 1.28 . .
45 . 8 GLN N N 124.18 . .
46 . 8 GLN H H 10.71 . .
47 . 8 GLN HA H 3.87 . .
48 . 8 GLN HB2 H 2.02 . .
49 . 8 GLN HB3 H 1.84 . .
50 . 8 GLN HG2 H 3.06 . .
51 . 8 GLN HG3 H 2.72 . .
52 . 8 GLN HE21 H 7.71 . .
53 . 8 GLN HE22 H 7.36 . .
54 . 8 GLN NE2 N 114.80 . .
55 . 9 CYS N N 113.08 . .
56 . 9 CYS H H 8.98 . .
57 . 9 CYS HA H 5.79 . .
58 . 9 CYS HB2 H 2.01 . .
59 . 10 HIS N N 120.66 . .
60 . 10 HIS H H 11.4 . .
61 . 10 HIS HA H 10.8 . .
62 . 10 HIS HB2 H 15.37 . .
63 . 10 HIS HB3 H 9.74 . .
64 . 10 HIS HD1 H 13.8 . .
65 . 10 HIS HD2 H 21.0 . .
66 . 10 HIS HE1 H -10 . .
67 . 11 THR N N 111.7 . .
68 . 11 THR H H 11.13 . .
69 . 11 THR HA H 6.51 . .
70 . 11 THR HB H 5.63 . .
71 . 11 THR HG2 H 2.39 . .
72 . 12 VAL H H 8.29 . .
73 . 12 VAL HA H 5 . .
74 . 16 GLY N N 108.26 . .
75 . 16 GLY H H 8.19 . .
76 . 16 GLY HA2 H 4.5 . .
77 . 16 GLY HA3 H 3.81 . .
78 . 21 GLY N N 104.13 . .
79 . 21 GLY H H 8.7 . .
80 . 21 GLY HA2 H -1.25 . .
81 . 21 GLY HA3 H 0.79 . .
82 . 22 PRO HA H 5.78 . .
83 . 22 PRO HG2 H 0.40 . .
84 . 22 PRO HG3 H -0.051 . .
85 . 22 PRO HD2 H 4.37 . .
86 . 22 PRO HD3 H -1.76 . .
87 . 23 ASN HA H 5.78 . .
88 . 23 ASN HD21 H 9.08 . .
89 . 23 ASN HD22 H 8.27 . .
90 . 23 ASN ND2 N 115.31 . .
91 . 24 LEU N N 123.05 . .
92 . 24 LEU H H 10.11 . .
93 . 24 LEU HB2 H 2.42 . .
94 . 24 LEU HB3 H 1.64 . .
95 . 24 LEU HA H 4.84 . .
96 . 24 LEU HD1 H 0.84 . .
97 . 24 LEU HD2 H -0.45 . .
98 . 25 HIS N N 119.96 . .
99 . 25 HIS H H 8.3 . .
100 . 25 HIS HA H 3.93 . .
101 . 25 HIS HB2 H 3.27 . .
102 . 25 HIS HB3 H 3.12 . .
103 . 26 GLY HA2 H 3.81 . .
104 . 26 GLY HA3 H 3.68 . .
105 . 27 ILE N N 116.82 . .
106 . 27 ILE H H 7.14 . .
107 . 27 ILE HB H 1.56 . .
108 . 27 ILE HA H 3.59 . .
109 . 27 ILE HG12 H 0.75 . .
110 . 27 ILE HG13 H 0.64 . .
111 . 27 ILE HG2 H 0.13 . .
112 . 27 ILE HD1 H 0.17 . .
113 . 28 PHE N N 115.56 . .
114 . 28 PHE H H 7.84 . .
115 . 28 PHE HA H 4.15 . .
116 . 28 PHE HB2 H 2.86 . .
117 . 28 PHE HD1 H 7.12 . .
118 . 28 PHE HE1 H 6.68 . .
119 . 28 PHE HZ H 7.00 . .
120 . 29 GLY N N 109.7 . .
121 . 29 GLY H H 8.69 . .
122 . 29 GLY HA2 H 4.15 . .
123 . 29 GLY HA3 H 3.63 . .
124 . 30 ARG N N 121.37 . .
125 . 30 ARG H H 8.03 . .
126 . 30 ARG HA H 4.53 . .
127 . 30 ARG HB2 H 2.1 . .
128 . 30 ARG HB3 H 1.84 . .
129 . 30 ARG HG2 H 1.69 . .
130 . 30 ARG HD2 H 1.92 . .
131 . 31 HIS N N 118.25 . .
132 . 31 HIS H H 7.76 . .
133 . 31 HIS HA H 5.35 . .
134 . 31 HIS HB2 H 2.74 . .
135 . 31 HIS HB3 H 2.58 . .
136 . 31 HIS HD1 H 6.50 . .
137 . 32 SER N N 115.49 . .
138 . 32 SER H H 8.63 . .
139 . 32 SER HA H 4.82 . .
140 . 32 SER HB2 H 4.24 . .
141 . 32 SER HB3 H 4.22 . .
142 . 33 GLY N N 112.75 . .
143 . 33 GLY H H 8.13 . .
144 . 33 GLY HA2 H 1.22 . .
145 . 33 GLY HA3 H 3.33 . .
146 . 34 GLN N N 113.38 . .
147 . 34 GLN H H 7.65 . .
148 . 34 GLN HA H 3.82 . .
149 . 35 ALA N N 127.87 . .
150 . 35 ALA H H 7.85 . .
151 . 35 ALA HA H 4.34 . .
152 . 35 ALA HB H 1.67 . .
153 . 36 GLU H H 8.44 . .
154 . 36 GLU HA H 4.61 . .
155 . 37 GLY N N 112.43 . .
156 . 37 GLY H H 9.99 . .
157 . 37 GLY HA2 H 4.34 . .
158 . 37 GLY HA3 H 4.9 . .
159 . 38 TYR H H 6.62 . .
160 . 38 TYR HB2 H 1.71 . .
161 . 38 TYR HA H 3.75 . .
162 . 38 TYR HD1 H 7.04 . .
163 . 38 TYR HD2 H 7.31 . .
164 . 38 TYR HE1 H 6.93 . .
165 . 38 TYR HE2 H 6.24 . .
166 . 40 TYR HB2 H 2.08 . .
167 . 40 TYR HD1 H 6.15 . .
168 . 40 TYR HE1 H 6.73 . .
169 . 41 THR H H 9.42 . .
170 . 41 THR HG2 H 1.35 . .
171 . 44 ASN N N 118.63 . .
172 . 44 ASN H H 8.16 . .
173 . 44 ASN HB2 H 2.97 . .
174 . 44 ASN HB3 H 2.89 . .
175 . 44 ASN HA H 4.03 . .
176 . 44 ASN HD21 H 8.70 . .
177 . 44 ASN HD22 H 7.19 . .
178 . 44 ASN ND2 N 106.55 . .
179 . 45 ILE N N 119.95 . .
180 . 45 ILE H H 7.59 . .
181 . 45 ILE HA H 3.27 . .
182 . 45 ILE HB H 1.76 . .
183 . 45 ILE HG12 H 0.95 . .
184 . 45 ILE HG13 H 1.05 . .
185 . 45 ILE HD1 H 0.82 . .
186 . 46 LYS N N 118.66 . .
187 . 46 LYS H H 8.95 . .
188 . 46 LYS HA H 3.79 . .
189 . 46 LYS HB2 H 1.73 . .
190 . 46 LYS HB3 H 1.62 . .
191 . 46 LYS HG2 H 1.35 . .
192 . 47 LYS N N 119.22 . .
193 . 47 LYS H H 7.33 . .
194 . 47 LYS HA H 3.72 . .
195 . 47 LYS HB2 H 1.65 . .
196 . 47 LYS HG2 H 1.20 . .
197 . 47 LYS HD2 H 0.93 . .
198 . 48 ASN N N 114.45 . .
199 . 48 ASN H H 8.16 . .
200 . 48 ASN HA H 4.36 . .
201 . 49 VAL N N 115.14 . .
202 . 49 VAL H H 7.23 . .
203 . 49 VAL HA H 3.66 . .
204 . 49 VAL HB H 0.97 . .
205 . 49 VAL HG1 H -0.35 . .
206 . 49 VAL HG2 H 0.28 . .
207 . 50 LEU N N 127.87 . .
208 . 50 LEU H H 8.12 . .
209 . 50 LEU HB2 H 1.48 . .
210 . 50 LEU HB3 H 0.71 . .
211 . 50 LEU HA H 3.66 . .
212 . 50 LEU HG H 0.94 . .
213 . 50 LEU HD1 H 0.57 . .
214 . 50 LEU HD2 H 0.13 . .
215 . 51 TRP N N 128.9 . .
216 . 51 TRP H H 7.93 . .
217 . 51 TRP HB2 H 3.66 . .
218 . 51 TRP HB3 H 2.53 . .
219 . 51 TRP HA H 4.89 . .
220 . 51 TRP HD1 H 6.93 . .
221 . 51 TRP HE1 H 8.88 . .
222 . 51 TRP HE3 H 7.50 . .
223 . 51 TRP HZ2 H 6.55 . .
224 . 51 TRP HZ3 H 7.02 . .
225 . 51 TRP HH2 H 5.60 . .
226 . 51 TRP NE1 N 121.00 . .
227 . 52 ASP N N 125.12 . .
228 . 52 ASP H H 9.65 . .
229 . 54 ASN N N 126.15 . .
230 . 54 ASN H H 7.63 . .
231 . 54 ASN HA H 4.47 . .
232 . 54 ASN HB2 H 2.94 . .
233 . 54 ASN HB3 H 1.85 . .
234 . 55 ASN N N 122.71 . .
235 . 55 ASN H H 9.4 . .
236 . 55 ASN HA H 4.43 . .
237 . 55 ASN HB2 H 3 . .
238 . 55 ASN HB3 H 2.77 . .
239 . 55 ASN HD21 H 6.86 . .
240 . 55 ASN HD22 H 6.64 . .
241 . 56 MET N N 123.4 . .
242 . 56 MET H H 8.58 . .
243 . 56 MET HA H 4.02 . .
244 . 56 MET HB2 H 1.6 . .
245 . 56 MET HB3 H 1.32 . .
246 . 56 MET HE H -0.89 . .
247 . 57 SER N N 114.11 . .
248 . 57 SER H H 7.32 . .
249 . 57 SER HA H 3.44 . .
250 . 57 SER HB2 H 3.99 . .
251 . 57 SER HB3 H 3.74 . .
252 . 58 GLU N N 120.3 . .
253 . 58 GLU H H 7.68 . .
254 . 58 GLU HA H 3.69 . .
255 . 58 GLU HB2 H 1.85 . .
256 . 58 GLU HB3 H 1.67 . .
257 . 58 GLU HG2 H 2.17 . .
258 . 59 TYR N N 121.04 . .
259 . 59 TYR H H 8.3 . .
260 . 59 TYR HA H 3.43 . .
261 . 59 TYR HB2 H 2.98 . .
262 . 59 TYR HB3 H 2.9 . .
263 . 60 LEU N N 111.33 . .
264 . 60 LEU H H 8.22 . .
265 . 60 LEU HA H 2.9 . .
266 . 60 LEU HB2 H 1.92 . .
267 . 60 LEU HB3 H 1.64 . .
268 . 60 LEU HG H 1.02 . .
269 . 60 LEU HD1 H 0.03 . .
270 . 61 THR N N 115.56 . .
271 . 61 THR H H 7.25 . .
272 . 61 THR HA H 3.77 . .
273 . 61 THR HB H 4.05 . .
274 . 61 THR HG2 H 1.09 . .
275 . 62 ASN N N 107.22 . .
276 . 62 ASN H H 6.09 . .
277 . 62 ASN HA H 4.06 . .
278 . 62 ASN HB2 H 2.93 . .
279 . 62 ASN HB3 H 2.64 . .
280 . 63 PRO HB2 H 0.08 . .
281 . 63 PRO HG2 H 0.60 . .
282 . 63 PRO HD2 H 1.09 . .
283 . 64 ALA N N 112.83 . .
284 . 64 ALA H H 7.82 . .
285 . 65 LYS N N 122.29 . .
286 . 65 LYS H H 8.19 . .
287 . 65 LYS HB2 H 10.94 . .
288 . 65 LYS HB3 H 9.43 . .
289 . 65 LYS HA H 5.06 . .
290 . 65 LYS HG2 H 6.7 . .
291 . 65 LYS HD2 H 24.5 . .
292 . 67 ILE N N 121.35 . .
293 . 67 ILE H H 7.68 . .
294 . 67 ILE HB H 2.22 . .
295 . 67 ILE HA H 3.86 . .
296 . 67 ILE HG12 H 1.15 . .
297 . 67 ILE HG13 H 0.28 . .
298 . 67 ILE HG2 H -0.73 . .
299 . 67 ILE HD1 H -0.99 . .
300 . 69 GLY H H 8.27 . .
301 . 70 THR H H 8.63 . .
302 . 71 ALA N N 125.12 . .
303 . 71 ALA H H 7.97 . .
304 . 71 ALA HA H 2.36 . .
305 . 71 ALA HB H 1.12 . .
306 . 72 MET N N 112.39 . .
307 . 72 MET H H 6.92 . .
308 . 72 MET HA H 4.15 . .
309 . 72 MET HG2 H 1.89 . .
310 . 72 MET HG3 H 1.41 . .
311 . 73 ALA N N 115.48 . .
312 . 73 ALA H H 6.44 . .
313 . 73 ALA HA H 3.51 . .
314 . 73 ALA HB H 0.67 . .
315 . 74 PHE HB2 H 1.93 . .
316 . 74 PHE HD1 H 6.87 . .
317 . 74 PHE HE1 H 7.02 . .
318 . 74 PHE HZ H 6.86 . .
319 . 75 GLY N N 108.26 . .
320 . 75 GLY H H 9.53 . .
321 . 76 GLY N N 105.5 . .
322 . 76 GLY H H 7.54 . .
323 . 76 GLY HA2 H 3.51 . .
324 . 77 LEU N N 116.46 . .
325 . 77 LEU H H 7.8 . .
326 . 77 LEU HA H 4.08 . .
327 . 77 LEU HB2 H 1.52 . .
328 . 77 LEU HB3 H 0.97 . .
329 . 77 LEU HG H 1.08 . .
330 . 77 LEU HD1 H 0.00 . .
331 . 78 LYS N N 119.15 . .
332 . 78 LYS H H 8.39 . .
333 . 78 LYS HA H 4.21 . .
334 . 78 LYS HG2 H 1.10 . .
335 . 78 LYS HD2 H 0.27 . .
336 . 78 LYS HD3 H -0.03 . .
337 . 79 LYS N N 120.3 . .
338 . 79 LYS H H 7.99 . .
339 . 79 LYS HA H 3.59 . .
340 . 79 LYS HB2 H 2.39 . .
341 . 79 LYS HB3 H 2.27 . .
342 . 79 LYS HG2 H 1.04 . .
343 . 79 LYS HD2 H 1.17 . .
344 . 82 ASP N N 115.55 . .
345 . 82 ASP H H 6.37 . .
346 . 82 ASP HA H 4.28 . .
347 . 82 ASP HB2 H 2.86 . .
348 . 82 ASP HB3 H 2.52 . .
349 . 83 ARG N N 117.9 . .
350 . 83 ARG H H 7.48 . .
351 . 83 ARG HA H 3.78 . .
352 . 83 ARG HB2 H 1.8 . .
353 . 83 ARG HB3 H 1.59 . .
354 . 83 ARG HG2 H 1.04 . .
355 . 84 ASN N N 117.56 . .
356 . 84 ASN H H 8.7 . .
357 . 84 ASN HA H 4.62 . .
358 . 84 ASN HB2 H 2.71 . .
359 . 85 ASP N N 125.09 . .
360 . 85 ASP H H 8.67 . .
361 . 85 ASP HA H 4.19 . .
362 . 85 ASP HB2 H 2.65 . .
363 . 86 LEU N N 120.3 . .
364 . 86 LEU H H 8.55 . .
365 . 86 LEU HA H 4.21 . .
366 . 86 LEU HB2 H 2.12 . .
367 . 86 LEU HB3 H 1.9 . .
368 . 86 LEU HG H 1.08 . .
369 . 86 LEU HD1 H 1.04 . .
370 . 87 ILE N N 119.95 . .
371 . 87 ILE H H 9.12 . .
372 . 87 ILE HB H 2.07 . .
373 . 87 ILE HA H 3.6 . .
374 . 87 ILE HG12 H 0.08 . .
375 . 87 ILE HG2 H 0.98 . .
376 . 87 ILE HD1 H 0.53 . .
377 . 88 THR N N 117.2 . .
378 . 88 THR H H 8.15 . .
379 . 88 THR HA H 3.78 . .
380 . 88 THR HB H 4.39 . .
381 . 88 THR HG2 H 1.18 . .
382 . 89 TYR N N 119.55 . .
383 . 89 TYR H H 7.81 . .
384 . 89 TYR HA H 4.08 . .
385 . 89 TYR HB2 H 3.54 . .
386 . 89 TYR HB3 H 3.09 . .
387 . 90 LEU N N 119.94 . .
388 . 90 LEU H H 9.34 . .
389 . 90 LEU HB2 H 1.95 . .
390 . 90 LEU HB3 H 1.89 . .
391 . 90 LEU HA H 3.33 . .
392 . 90 LEU HG H 1.61 . .
393 . 90 LEU HD1 H 0.79 . .
394 . 90 LEU HD2 H -0.11 . .
395 . 91 LYS N N 120.66 . .
396 . 91 LYS H H 8.67 . .
397 . 91 LYS HA H 3.41 . .
398 . 91 LYS HB2 H 1.9 . .
399 . 91 LYS HB3 H 1.43 . .
400 . 91 LYS HG2 H 0.47 . .
401 . 91 LYS HD2 H 0.83 . .
402 . 92 LYS N N 115.83 . .
403 . 92 LYS H H 6.56 . .
404 . 92 LYS HA H 4.06 . .
405 . 92 LYS HB2 H 1.7 . .
406 . 92 LYS HG2 H 1.30 . .
407 . 93 ALA N N 119.61 . .
408 . 93 ALA H H 8.33 . .
409 . 93 ALA HA H 3.8 . .
410 . 93 ALA HB H 0.46 . .
411 . 94 THR N N 102.41 . .
412 . 94 THR H H 7.26 . .
413 . 94 THR HA H 4.3 . .
414 . 94 THR HG2 H 0.81 . .
415 . 95 GLU N N 125.8 . .
416 . 95 GLU H H 6.65 . .
417 . 95 GLU HA H 3.93 . .
418 . 95 GLU HB2 H 2.16 . .
419 . 95 GLU HB3 H 1.87 . .
420 . 95 GLU HG2 H 2.71 . .
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