data_4997
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
1H, 13C Chemical Shift Assignment of PT-insulin in H2O and 35% TFE
;
_BMRB_accession_number 4997
_BMRB_flat_file_name bmr4997.str
_Entry_type original
_Submission_date 2001-04-23
_Accession_date 2001-04-23
_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 Keller Danielle . .
2 Clausen R. . .
3 Josefsen Knud . .
4 Led Jens J. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 4
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 456
"13C chemical shifts" 109
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2001-05-21 original BMRB .
stop_
_Original_release_date 2001-04-23
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Flexibility and Bioactivity of Insulin: an NMR Investigation of the Solution
Structure and Folding of an Unusually Flexible Human Insulin Mutant with
Increased Biological Activity
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 21415430
_PubMed_ID 11524020
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Keller Danielle . .
2 Clausen R. . .
3 Josefsen Knud . .
4 Led Jens J. .
stop_
_Journal_abbreviation Biochemistry
_Journal_volume 40
_Journal_issue 35
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 10732
_Page_last 10740
_Year 2001
_Details .
loop_
_Keyword
Insulin
stop_
save_
##################################
# Molecular system description #
##################################
save_system_PT-insulin
_Saveframe_category molecular_system
_Mol_system_name [Thr(B27)->Pro,Pro(B28)->Thr]-insulin
_Abbreviation_common PT-insulin
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'PT-insulin A chain' $PT-insulin_A_chain
'PT-insulin B chain' $PT-insulin_B_chain
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'all disulfide bound'
loop_
_Biological_function
'Peptide hormone'
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_PT-insulin_A_chain
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common Insulin
_Abbreviation_common Insulin
_Molecular_mass .
_Mol_thiol_state 'all disulfide bound'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 21
_Mol_residue_sequence
;
GIVEQCCTSICSLYQLENYC
N
;
loop_
_Residue_seq_code
_Residue_author_seq_code
_Residue_label
1 1 GLY 2 2 ILE 3 3 VAL 4 4 GLU 5 5 GLN
6 6 CYS 7 7 CYS 8 8 THR 9 9 SER 10 10 ILE
11 11 CYS 12 12 SER 13 13 LEU 14 14 TYR 15 15 GLN
16 16 LEU 17 17 GLU 18 18 ASN 19 19 TYR 20 20 CYS
21 21 ASN
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
BMRB 1000 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 1002 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 1004 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 1006 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 1008 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 1010 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 1012 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 1014 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 1016 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 1018 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 1020 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 1022 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 1023 'insulin B chain' 95.24 42 100.00 100.00 1.97e-02
BMRB 11016 'Chain A' 100.00 21 100.00 100.00 4.53e-03
BMRB 1344 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 15464 entity_1 100.00 21 100.00 100.00 4.53e-03
BMRB 1585 'insulin A chain' 95.24 20 100.00 100.00 2.46e-02
BMRB 1587 'insulin A chain' 95.24 20 100.00 100.00 2.46e-02
BMRB 1632 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 1761 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 4266 [D-AlaB26]destetra(B27-B30)insulin-B26-amide 100.00 47 100.00 100.00 3.04e-03
BMRB 554 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 556 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 6203 'ThrB12-DKP-insulin, chain A' 100.00 21 100.00 100.00 4.53e-03
BMRB 6204 'AlaB12-DKP-insulin, chain A' 100.00 21 100.00 100.00 4.53e-03
BMRB 6205 'AbaB12-DKP-insulin, chain A' 100.00 21 100.00 100.00 4.53e-03
BMRB 936 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 994 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 996 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
BMRB 998 'insulin A chain' 100.00 21 100.00 100.00 4.53e-03
PDB 1A7F 'Insulin Mutant B16 Glu, B24 Gly, Des-B30, Nmr, 20 Structures' 100.00 21 100.00 100.00 4.53e-03
PDB 1AI0 'R6 Human Insulin Hexamer (Non-Symmetric), Nmr, 10 Structures' 100.00 21 100.00 100.00 4.53e-03
PDB 1AIY 'R6 Human Insulin Hexamer (Symmetric), Nmr, 10 Structures' 100.00 21 100.00 100.00 4.53e-03
PDB 1B17 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 5.00 Coordinates)' 100.00 21 100.00 100.00 4.53e-03
PDB 1B18 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 5.53 Coordinates)' 100.00 21 100.00 100.00 4.53e-03
PDB 1B19 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 5.80 Coordinates)' 100.00 21 100.00 100.00 4.53e-03
PDB 1B2A 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 6.00 Coordinates)' 100.00 21 100.00 100.00 4.53e-03
PDB 1B2B 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 6.16 Coordinates)' 100.00 21 100.00 100.00 4.53e-03
PDB 1B2C 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 6.26 Coordinates)' 100.00 21 100.00 100.00 4.53e-03
PDB 1B2D 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 6.35 Coordinates)' 100.00 21 100.00 100.00 4.53e-03
PDB 1B2E 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 6.50 Coordinates)' 100.00 21 100.00 100.00 4.53e-03
PDB 1B2F 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 6.98 Coordinates)' 100.00 21 100.00 100.00 4.53e-03
PDB 1B2G 'Ph Affects Glu B13 Switching And Sulfate Binding In Cubic Insulin Crystals (Ph 9.00 Coordinates)' 100.00 21 100.00 100.00 4.53e-03
PDB 1B9E 'Human Insulin Mutant Serb9glu' 100.00 21 100.00 100.00 4.53e-03
PDB 1BEN 'Insulin Complexed With 4-Hydroxybenzamide' 95.24 21 100.00 100.00 2.46e-02
PDB 1BZV '[d-Alab26]-Des(B27-B30)-Insulin-B26-Amide A Superpotent Single-Replacement Insulin Analogue, Nmr, Minimized Average Structure' 100.00 21 100.00 100.00 4.53e-03
PDB 1DEI 'Desheptapeptide (B24-B30) Insulin' 100.00 21 100.00 100.00 4.53e-03
PDB 1EFE 'An Active Mini-Proinsulin, M2pi' 100.00 60 100.00 100.00 2.27e-03
PDB 1EV3 'Structure Of The Rhombohedral Form Of The M-CresolINSULIN R6 Hexamer' 100.00 21 100.00 100.00 4.53e-03
PDB 1EV6 'Structure Of The Monoclinic Form Of The M-CresolINSULIN R6 Hexamer' 100.00 21 100.00 100.00 4.53e-03
PDB 1EVR 'The Structure Of The ResorcinolINSULIN R6 HEXAMER' 100.00 21 100.00 100.00 4.53e-03
PDB 1FU2 'First Protein Structure Determined From X-Ray Powder Diffraction Data' 100.00 21 100.00 100.00 4.53e-03
PDB 1FUB 'First Protein Structure Determined From X-Ray Powder Diffraction Data' 100.00 21 100.00 100.00 4.53e-03
PDB 1G7A '1.2 A Structure Of T3r3 Human Insulin At 100 K' 95.24 21 100.00 100.00 2.46e-02
PDB 1GUJ 'Insulin At Ph 2: Structural Analysis Of The Conditions Promoting Insulin Fibre Formation.' 100.00 21 100.00 100.00 4.53e-03
PDB 1HIQ 'Paradoxical Structure And Function In A Mutant Human Insulin Associated With Diabetes Mellitus' 100.00 21 100.00 100.00 4.53e-03
PDB 1HIS 'Structure And Dynamics Of Des-Pentapeptide-Insulin In Solution: The Molten-Globule Hypothesis' 100.00 21 100.00 100.00 4.53e-03
PDB 1HIT 'Receptor Binding Redefined By A Structural Switch In A Mutant Human Insulin' 100.00 21 100.00 100.00 4.53e-03
PDB 1HLS 'Nmr Structure Of The Human Insulin-His(B16)' 100.00 21 100.00 100.00 4.53e-03
PDB 1HTV 'Crystal Structure Of Destripeptide (B28-B30) Insulin' 100.00 21 100.00 100.00 4.53e-03
PDB 1HUI 'Insulin Mutant (B1, B10, B16, B27)glu, Des-B30, Nmr, 25 Structures' 100.00 21 100.00 100.00 4.53e-03
PDB 1IZA 'Role Of B13 Glu In Insulin Assembly: The Hexamer Structure Of Recombinant Mutant (B13 Glu-> Gln) Insulin' 100.00 21 100.00 100.00 4.53e-03
PDB 1IZB 'Role Of B13 Glu In Insulin Assembly: The Hexamer Structure Of Recombinant Mutant (B13 Glu-> Gln) Insulin' 100.00 21 100.00 100.00 4.53e-03
PDB 1JCO 'Solution Structure Of The Monomeric [thr(B27)->pro,Pro(B28)- >thr] Insulin Mutant (Pt Insulin)' 100.00 21 100.00 100.00 4.53e-03
PDB 1LPH 'Lys(B28)pro(B29)-Human Insulin' 100.00 21 100.00 100.00 4.53e-03
PDB 1M5A 'Crystal Structure Of 2-Co(2+)-Insulin At 1.2a Resolution' 100.00 21 100.00 100.00 4.53e-03
PDB 1MHJ
;
Solution Structure Of The Superactive Monomeric Des- [phe(B25)] Human Insulin Mutant. Elucidation Of The Structural Basis For The Monomerization Of The Des- [phe(B25)] Insulin And The Dimerization Of Native Insulin
; 100.00 21 100.00 100.00 4.53e-03
PDB 1MPJ
;
X-Ray Crystallographic Studies On Hexameric Insulins In The Presence Of Helix-Stabilizing Agents, Thiocyanate, Methylparaben And Phenol
; 100.00 21 100.00 100.00 4.53e-03
PDB 1OS3 'Dehydrated T6 Human Insulin At 100 K' 100.00 21 100.00 100.00 4.53e-03
PDB 1OS4 'Dehydrated T6 Human Insulin At 295 K' 100.00 21 100.00 100.00 4.53e-03
PDB 1QIY 'Human Insulin Hexamers With Chain B His Mutated To Tyr Complexed With Phenol' 100.00 21 100.00 100.00 4.53e-03
PDB 1QIZ 'Human Insulin Hexamers With Chain B His Mutated To Tyr Complexed With Resorcinol' 100.00 21 100.00 100.00 4.53e-03
PDB 1QJ0 'Human Insulin Hexamers With Chain B His Mutated To Tyr' 100.00 21 100.00 100.00 4.53e-03
PDB 1SDB 'Porcine Desb1-2 Despentapeptide(B26-B30) Insulin' 100.00 21 100.00 100.00 4.53e-03
PDB 1SF1 'Nmr Structure Of Human Insulin Under Amyloidogenic Condition, 15 Structures' 100.00 21 100.00 100.00 4.53e-03
PDB 1SJT 'Mini-Proinsulin, Two Chain Insulin Analog Mutant: Des B30, His(B 10)asp, Pro(B 28)asp, Nmr, 20 Structures' 100.00 21 100.00 100.00 4.53e-03
PDB 1SJU
;
Mini-Proinsulin, Single Chain Insulin Analog Mutant: Des B30, His(B 10)asp, Pro(B 28)asp And Peptide Bond Between Lys B 29 And Gly A 1, Nmr, 20 Structures
; 100.00 50 100.00 100.00 3.11e-03
PDB 1T1K 'Nmr Structure Of Human Insulin Mutant His-B10-Asp, Val-B12- Ala, Pro-B28-Lys, Lys-B29-Pro, 15 Structures' 100.00 21 100.00 100.00 4.53e-03
PDB 1T1P 'Nmr Structure Of Human Insulin Mutant His-B10-Asp, Val-B12- Thr, Pro-B28-Lys, Lys-B29-Pro, 15 Structures' 100.00 21 100.00 100.00 4.53e-03
PDB 1T1Q 'Nmr Structure Of Human Insulin Mutant His-B10-Asp, Val-B12- Aba, Pro-B28-Lys, Lys-B29-Pro, 15 Structures' 100.00 21 100.00 100.00 4.53e-03
PDB 1TRZ 'Crystallographic Evidence For Dual Coordination Around Zinc In The T3r3 Human Insulin Hexamer' 100.00 21 100.00 100.00 4.53e-03
PDB 1TYL "The Structure Of A Complex Of Hexameric Insulin And 4'- Hydroxyacetanilide" 100.00 21 100.00 100.00 4.53e-03
PDB 1TYM "The Structure Of A Complex Of Hexameric Insulin And 4'- Hydroxyacetanilide" 100.00 21 100.00 100.00 4.53e-03
PDB 1UZ9 'Crystallographic And Solution Studies Of N-Lithocholyl Insulin: A New Generation Of Prolonged-Acting Insulins.' 100.00 21 100.00 100.00 4.53e-03
PDB 1W8P 'Structural Properties Of The B25tyr-Nme-B26phe Insulin Mutant.' 100.00 21 100.00 100.00 4.53e-03
PDB 1WAV 'Crystal Structure Of Form B Monoclinic Crystal Of Insulin' 100.00 21 100.00 100.00 4.53e-03
PDB 1XDA 'Structure Of Insulin' 100.00 21 100.00 100.00 4.53e-03
PDB 1XGL 'Human Insulin Disulfide Isomer, Nmr, 10 Structures' 100.00 21 100.00 100.00 4.53e-03
PDB 1ZEG 'Structure Of B28 Asp Insulin In Complex With Phenol' 100.00 21 100.00 100.00 4.53e-03
PDB 1ZEH 'Structure Of Insulin' 100.00 21 100.00 100.00 4.53e-03
PDB 1ZEI 'Cross-Linked B28 Asp Insulin' 100.00 53 100.00 100.00 2.36e-03
PDB 1ZNI Insulin 100.00 21 100.00 100.00 4.53e-03
PDB 1ZNJ 'Insulin, Monoclinic Crystal Form' 100.00 21 100.00 100.00 4.53e-03
PDB 2AIY 'R6 Human Insulin Hexamer (Symmetric), Nmr, 20 Structures' 100.00 21 100.00 100.00 4.53e-03
PDB 2C8Q 'Insuline(1sec) And Uv Laser Excited Fluorescence' 100.00 21 100.00 100.00 4.53e-03
PDB 2C8R 'Insuline(60sec) And Uv Laser Excited Fluorescence' 100.00 21 100.00 100.00 4.53e-03
PDB 2CEU 'Despentapeptide Insulin In Acetic Acid (Ph 2)' 100.00 21 100.00 100.00 4.53e-03
PDB 2G4M 'Insulin Collected At 2.0 A Wavelength' 100.00 21 100.00 100.00 4.53e-03
PDB 2H67 'Nmr Structure Of Human Insulin Mutant His-B5-Ala, His-B10- Asp Pro-B28-Lys, Lys-B29-Pro, 20 Structures' 100.00 21 100.00 100.00 4.53e-03
PDB 2HH4 'Nmr Structure Of Human Insulin Mutant Gly-B8-D-Ser, His-B10- Asp Pro-B28-Lys, Lys-B29-Pro, 20 Structures' 100.00 21 100.00 100.00 4.53e-03
PDB 2HHO 'Nmr Structure Of Human Insulin Mutant Gly-B8-Ser, His-B10- Asp Pro-B28-Lys, Lys-B29-Pro, 20 Structures' 100.00 21 100.00 100.00 4.53e-03
PDB 2HIU 'Nmr Structure Of Human Insulin In 20% Acetic Acid, Zinc- Free, 10 Structures' 100.00 21 100.00 100.00 4.53e-03
PDB 2JMN 'Nmr Structure Of Human Insulin Mutant His-B10-Asp, Pro-B28- Lys, Lys-B29-Pro, 20 Structures' 100.00 21 100.00 100.00 4.53e-03
PDB 2JV1 'Nmr Structure Of Human Insulin Monomer In 35% Cd3cn Zinc Free, 50 Structures' 100.00 21 100.00 100.00 4.53e-03
PDB 2OLY 'Structure Of Human Insulin In Presence Of Urea At Ph 7.0' 100.00 21 100.00 100.00 4.53e-03
PDB 2OLZ 'Structure Of Human Insulin In Presence Of Thiocyanate At Ph 7.0' 100.00 21 100.00 100.00 4.53e-03
PDB 2OM0 'Structure Of Human Insulin In Presence Of Urea At Ph 6.5' 100.00 21 100.00 100.00 4.53e-03
PDB 2OM1 'Structure Of Human Insulin In Presence Of Thiocyanate At Ph 6.5' 100.00 21 100.00 100.00 4.53e-03
PDB 2OMG 'Structure Of Human Insulin Cocrystallized With Protamine And Urea' 100.00 21 100.00 100.00 4.53e-03
PDB 2OMH 'Structure Of Human Insulin Cocrystallized With Arg-12 Peptide In Presence Of Urea' 100.00 21 100.00 100.00 4.53e-03
PDB 2OMI 'Structure Of Human Insulin Cocrystallized With Protamine' 100.00 21 100.00 100.00 4.53e-03
PDB 2QIU 'Structure Of Human Arg-Insulin' 100.00 22 100.00 100.00 4.10e-03
PDB 2TCI
;
X-Ray Crystallographic Studies On Hexameric Insulins In The Presence Of Helix-Stabilizing Agents, Thiocyanate, Methylparaben And Phenol
; 100.00 21 100.00 100.00 4.53e-03
PDB 3AIY 'R6 Human Insulin Hexamer (Symmetric), Nmr, Refined Average Structure' 100.00 21 100.00 100.00 4.53e-03
PDB 3BXQ 'The Structure Of A Mutant Insulin Uncouples Receptor Binding From Protein Allostery. An Electrostatic Block To The Tr Transition' 100.00 21 100.00 100.00 4.53e-03
PDB 3MTH
;
X-Ray Crystallographic Studies On Hexameric Insulins In The Presence Of Helix-Stabilizing Agents, Thiocyanate, Methylparaben And Phenol
; 100.00 21 100.00 100.00 4.53e-03
PDB 4AIY "R6 Human Insulin Hexamer (Symmetric), Nmr, 'green' Substate, Average Structure" 100.00 21 100.00 100.00 4.53e-03
PDB 4INS 'The Structure Of 2zn Pig Insulin Crystals At 1.5 Angstroms Resolution' 100.00 21 100.00 100.00 4.53e-03
PDB 5AIY "R6 Human Insulin Hexamer (Symmetric), Nmr, 'red' Substate, Average Structure" 100.00 21 100.00 100.00 4.53e-03
PDB 6INS 'X-Ray Analysis Of The Single Chain B29-A1 Peptide-Linked Insulin Molecule. A Completely Inactive Analogue' 100.00 50 100.00 100.00 3.11e-03
PDB 7INS 'Structure Of Porcine Insulin Cocrystallized With Clupeine Z' 100.00 21 100.00 100.00 4.53e-03
PDB 9INS 'Monovalent Cation Binding In Cubic Insulin Crystals' 100.00 21 100.00 100.00 4.53e-03
EMBL CAA23424 'unnamed protein product [synthetic construct]' 100.00 87 100.00 100.00 1.29e-03
EMBL CAA23475 'preproinsulin [Canis sp.]' 100.00 110 100.00 100.00 8.40e-04
EMBL CAA23828 'preproinsulin [Homo sapiens]' 100.00 110 100.00 100.00 1.16e-03
EMBL CAA43403 'Preproinsulin [Pan troglodytes]' 100.00 110 100.00 100.00 7.79e-04
EMBL CAA43405 'Preproinsulin [Chlorocebus aethiops]' 100.00 110 100.00 100.00 8.40e-04
GenBank AAA17540 insulin 100.00 55 100.00 100.00 1.35e-03
GenBank AAA19033 insulin 100.00 110 100.00 100.00 8.33e-04
GenBank AAA36849 preproinsulin 100.00 110 100.00 100.00 7.99e-04
GenBank AAA59172 'insulin [Homo sapiens]' 100.00 110 100.00 100.00 1.16e-03
GenBank AAA59173 'insulin [Homo sapiens]' 100.00 110 100.00 100.00 1.16e-03
PRF 0601246A insulin,prepro 100.00 110 100.00 100.00 1.16e-03
PRF 1006230A insulin,pro- 100.00 86 100.00 100.00 1.29e-03
PRF 550086A insulin 100.00 51 100.00 100.00 2.86e-03
PRF 560164B insulin 100.00 21 100.00 100.00 4.53e-03
PRF 580107B insulin 100.00 50 100.00 100.00 2.77e-03
REF NP_000198 'proinsulin precursor [Homo sapiens]' 100.00 110 100.00 100.00 1.16e-03
REF NP_001008996 'proinsulin precursor [Pan troglodytes]' 100.00 110 100.00 100.00 7.79e-04
REF NP_001075804 'insulin [Oryctolagus cuniculus]' 100.00 110 100.00 100.00 8.33e-04
REF NP_001103242 'insulin [Sus scrofa]' 100.00 108 100.00 100.00 1.13e-03
REF NP_001123565 'proinsulin [Canis lupus familiaris]' 100.00 110 100.00 100.00 8.40e-04
SWISS-PROT P01308 'Insulin precursor [Contains: Insulin B chain; Insulin A chain]' 100.00 110 100.00 100.00 1.16e-03
SWISS-PROT P01311 'Insulin precursor [Contains: Insulin B chain; Insulin A chain]' 100.00 110 100.00 100.00 8.33e-04
SWISS-PROT P01315 'Insulin precursor [Contains: Insulin B chain; Insulin A chain]' 100.00 108 100.00 100.00 1.13e-03
SWISS-PROT P01321 'Insulin precursor [Contains: Insulin B chain; Insulin A chain]' 100.00 110 100.00 100.00 8.40e-04
SWISS-PROT P30406 'Insulin precursor [Contains: Insulin B chain; Insulin A chain]' 100.00 110 100.00 100.00 7.99e-04
stop_
save_
save_PT-insulin_B_chain
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common Insulin
_Abbreviation_common Insulin
_Molecular_mass .
_Mol_thiol_state 'all disulfide bound'
_Details .
_Residue_count 30
_Mol_residue_sequence
;
FVNQHLCGSHLVEALYLVCG
ERGFFYPTKT
;
loop_
_Residue_seq_code
_Residue_author_seq_code
_Residue_label
1 22 PHE 2 23 VAL 3 24 ASN 4 25 GLN 5 26 HIS
6 27 LEU 7 28 CYS 8 29 GLY 9 30 SER 10 31 HIS
11 32 LEU 12 33 VAL 13 34 GLU 14 35 ALA 15 36 LEU
16 37 TYR 17 38 LEU 18 39 VAL 19 40 CYS 20 41 GLY
21 42 GLU 22 43 ARG 23 44 GLY 24 45 PHE 25 46 PHE
26 47 TYR 27 48 PRO 28 49 THR 29 50 LYS 30 51 THR
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 1JCO 'Solution Structure Of The Monomeric [thr(B27)->pro,Pro(B28)- >thr] Insulin Mutant (Pt Insulin)' 100.00 30 100.00 100.00 2.23e-09
PRF 640291A insulin 86.67 51 100.00 100.00 8.54e-07
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
_Secretion
$PT-insulin_A_chain human 9606 Eukaryota Metazoa Homo sapiens pancreas
$PT-insulin_B_chain human 9606 Eukaryota Metazoa Homo sapiens pancreas
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
$PT-insulin_A_chain 'recombinant technology' 'Pichia pastoris' Pichia pastoris . plasmid pPIC9
$PT-insulin_B_chain 'recombinant technology' 'Pichia pastoris' Pichia pastoris . plasmid pPIC9
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
$PT-insulin_A_chain 2.8 mM .
$PT-insulin_B_chain 2.8 mM .
H2O 90 % .
D2O 10 % .
stop_
save_
save_sample_2
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$PT-insulin_A_chain 2.8 mM .
$PT-insulin_B_chain 2.8 mM .
H2O 65 % .
TFE 35 % .
stop_
save_
############################
# Computer software used #
############################
save_NMRPipe
_Saveframe_category software
_Name NMRPipe
_Version .
loop_
_Task
'Fourier Transformation'
stop_
_Details .
save_
save_XEASY
_Saveframe_category software
_Name XEASY
_Version .
loop_
_Task
'Cross peak integration'
'Resonance assignment'
stop_
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model INOVA
_Field_strength 500
_Details .
save_
save_NMR_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model INOVA
_Field_strength 750
_Details .
save_
save_NMR_spectrometer_3
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model INOVA
_Field_strength 800
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_COSY_with_DQF_1
_Saveframe_category NMR_applied_experiment
_Experiment_name 'COSY with DQF'
_Sample_label .
save_
save_TOCSY/NOESY_with_WaterGate_2
_Saveframe_category NMR_applied_experiment
_Experiment_name 'TOCSY/NOESY with WaterGate'
_Sample_label .
save_
save_HSQC:_Gradient_enhanced_3
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HSQC: Gradient enhanced'
_Sample_label .
save_
#######################
# Sample conditions #
#######################
save_cond_H2O
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 3.13 0.1 n/a
temperature 298 0.1 K
stop_
save_
save_cond_TFE
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 3.23 0.1 n/a
temperature 298 0.1 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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530
DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0
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_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'COSY with DQF'
'TOCSY/NOESY with WaterGate'
'HSQC: Gradient enhanced'
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $cond_H2O
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'PT-insulin A chain'
_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 ILE H H 8.58 0.02 1
2 . 2 ILE HA H 3.95 0.02 1
3 . 2 ILE HB H 1.42 0.02 1
4 . 2 ILE HG12 H 1.17 0.02 2
5 . 2 ILE HG13 H 0.87 0.02 2
6 . 2 ILE HG2 H 0.63 0.02 1
7 . 2 ILE HD1 H 0.52 0.02 1
8 . 3 VAL H H 8.21 0.02 1
9 . 3 VAL HA H 3.69 0.02 1
10 . 3 VAL HB H 1.95 0.02 1
11 . 3 VAL HG1 H 1.00 0.02 2
12 . 3 VAL HG2 H 0.92 0.02 2
13 . 4 GLU H H 8.32 0.02 1
14 . 4 GLU HA H 4.01 0.02 1
15 . 5 GLN HB2 H 2.01 0.02 2
16 . 5 GLN HB3 H 2.08 0.02 2
17 . 5 GLN HG2 H 2.34 0.02 2
18 . 5 GLN HG3 H 2.43 0.02 2
19 . 5 GLN HE21 H 7.45 0.02 2
20 . 5 GLN HE22 H 6.84 0.02 2
21 . 6 CYS H H 8.32 0.02 1
22 . 6 CYS HA H 4.85 0.02 1
23 . 6 CYS HB2 H 3.35 0.02 2
24 . 7 CYS HA H 4.82 0.02 1
25 . 8 THR H H 8.36 0.02 1
26 . 8 THR HA H 3.96 0.02 1
27 . 8 THR HB H 4.34 0.02 1
28 . 8 THR HG2 H 1.24 0.02 1
29 . 9 SER HA H 4.09 0.02 1
30 . 9 SER HB2 H 4.03 0.02 2
31 . 9 SER HB3 H 3.87 0.02 2
32 . 10 ILE H H 7.87 0.02 1
33 . 10 ILE HA H 4.36 0.02 1
34 . 10 ILE HB H 1.55 0.02 1
35 . 10 ILE HG12 H 1.05 0.02 2
36 . 10 ILE HG13 H 1.23 0.02 2
37 . 10 ILE HG2 H 0.61 0.02 1
38 . 10 ILE HD1 H 0.43 0.02 1
39 . 11 CYS H H 9.79 0.02 1
40 . 11 CYS HA H 4.95 0.02 1
41 . 12 SER H H 8.73 0.02 1
42 . 12 SER HA H 4.57 0.02 1
43 . 12 SER HB2 H 4.25 0.02 2
44 . 12 SER HB3 H 3.98 0.02 2
45 . 13 LEU H H 8.62 0.02 1
46 . 13 LEU HA H 3.73 0.02 1
47 . 13 LEU HB2 H 1.33 0.02 2
48 . 13 LEU HB3 H 1.21 0.02 2
49 . 13 LEU HG H 0.93 0.02 1
50 . 13 LEU HD1 H 0.78 0.02 1
51 . 13 LEU HD2 H 0.71 0.02 1
52 . 14 TYR H H 7.56 0.02 1
53 . 14 TYR HA H 4.11 0.02 1
54 . 14 TYR HB2 H 2.99 0.02 2
55 . 14 TYR HB3 H 2.94 0.02 2
56 . 14 TYR HD1 H 6.89 0.02 3
57 . 14 TYR HE1 H 7.05 0.02 3
58 . 15 GLN H H 7.51 0.02 1
59 . 15 GLN HA H 3.94 0.02 1
60 . 15 GLN HB2 H 2.01 0.02 2
61 . 15 GLN HG2 H 2.33 0.02 2
62 . 15 GLN HG3 H 2.38 0.02 2
63 . 15 GLN HE21 H 6.84 0.02 2
64 . 15 GLN HE22 H 7.05 0.02 2
65 . 16 LEU H H 7.90 0.02 1
66 . 16 LEU HA H 4.11 0.02 1
67 . 16 LEU HB2 H 1.71 0.02 2
68 . 17 GLU H H 8.07 0.02 1
69 . 17 GLU HA H 4.28 0.02 1
70 . 17 GLU HB2 H 2.06 0.02 2
71 . 17 GLU HG2 H 2.29 0.02 2
72 . 17 GLU HG3 H 2.54 0.02 2
73 . 18 ASN H H 7.36 0.02 1
74 . 18 ASN HA H 4.48 0.02 1
75 . 18 ASN HB2 H 2.62 0.02 2
76 . 18 ASN HB3 H 2.53 0.02 2
77 . 18 ASN HD21 H 6.58 0.02 2
78 . 18 ASN HD22 H 7.15 0.02 2
79 . 19 TYR H H 7.90 0.02 1
80 . 19 TYR HA H 4.38 0.02 1
81 . 19 TYR HB2 H 2.93 0.02 2
82 . 19 TYR HB3 H 3.51 0.02 2
83 . 19 TYR HD1 H 6.74 0.02 3
84 . 19 TYR HE1 H 7.23 0.02 3
85 . 20 CYS H H 7.29 0.02 1
86 . 20 CYS HA H 5.23 0.02 1
87 . 20 CYS HB2 H 3.32 0.02 2
88 . 20 CYS HB3 H 2.18 0.02 2
89 . 21 ASN HD21 H 6.27 0.02 2
90 . 21 ASN HD22 H 7.48 0.02 2
stop_
save_
save_CS_2
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'COSY with DQF'
'TOCSY/NOESY with WaterGate'
'HSQC: Gradient enhanced'
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $cond_H2O
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'PT-insulin B chain'
_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 PHE HA H 4.19 0.02 1
2 . 1 PHE HB2 H 3.13 0.02 1
3 . 1 PHE HB3 H 3.08 0.02 2
4 . 1 PHE HD1 H 7.18 0.02 2
5 . 1 PHE HE1 H 7.3 0.02 3
6 . 1 PHE HZ H 7.21 0.02 1
7 . 2 VAL H H 7.99 0.02 1
8 . 2 VAL HA H 4.01 0.02 1
9 . 2 VAL HB H 1.99 0.02 1
10 . 2 VAL HG1 H 0.78 0.02 2
11 . 3 ASN H H 8.45 0.02 1
12 . 3 ASN HA H 4.64 0.02 1
13 . 3 ASN HB2 H 2.66 0.02 2
14 . 3 ASN HD21 H 6.82 0.02 2
15 . 3 ASN HD22 H 7.49 0.02 2
16 . 4 GLN H H 8.36 0.02 1
17 . 4 GLN HA H 4.43 0.02 1
18 . 4 GLN HB2 H 2.04 0.02 2
19 . 4 GLN HB3 H 1.87 0.02 2
20 . 4 GLN HG2 H 2.21 0.02 2
21 . 4 GLN HE21 H 7.37 0.02 2
22 . 4 GLN HE22 H 6.76 0.02 2
23 . 5 HIS H H 8.69 0.02 1
24 . 5 HIS HA H 4.43 0.02 1
25 . 5 HIS HB2 H 3.55 0.02 2
26 . 5 HIS HB3 H 3.24 0.02 2
27 . 5 HIS HD2 H 7.34 0.02 1
28 . 5 HIS HE1 H 8.56 0.02 1
29 . 6 LEU H H 9.08 0.02 1
30 . 6 LEU HA H 4.47 0.02 1
31 . 6 LEU HB2 H 1.75 0.02 2
32 . 6 LEU HB3 H 1.56 0.02 2
33 . 6 LEU HG H 0.87 0.02 1
34 . 6 LEU HD1 H 0.73 0.02 2
35 . 6 LEU HD2 H 0.66 0.02 2
36 . 7 CYS H H 8.52 0.02 1
37 . 7 CYS HA H 4.97 0.02 1
38 . 7 CYS HB2 H 3.23 0.02 2
39 . 7 CYS HB3 H 2.94 0.02 2
40 . 8 GLY H H 9.43 0.02 1
41 . 8 GLY HA2 H 3.95 0.02 2
42 . 8 GLY HA3 H 3.85 0.02 2
43 . 9 SER H H 9.15 0.02 1
44 . 9 SER HA H 3.72 0.02 1
45 . 10 HIS H H 7.92 0.02 1
46 . 10 HIS HA H 4.38 0.02 1
47 . 10 HIS HB2 H 3.51 0.02 2
48 . 10 HIS HB3 H 3.23 0.02 2
49 . 10 HIS HD2 H 7.44 0.02 1
50 . 10 HIS HE1 H 8.58 0.02 1
51 . 12 VAL HA H 3.55 0.02 1
52 . 12 VAL HB H 1.9 0.02 1
53 . 12 VAL HG1 H 0.86 0.02 2
54 . 14 ALA HA H 4.05 0.02 1
55 . 14 ALA HB H 1.42 0.02 1
56 . 15 LEU H H 7.83 0.02 1
57 . 15 LEU HA H 3.61 0.02 1
58 . 15 LEU HB2 H 1.98 0.02 2
59 . 15 LEU HG H 1.28 0.02 1
60 . 15 LEU HD1 H 0.48 0.02 2
61 . 15 LEU HD2 H 0.02 0.02 2
62 . 17 LEU H H 7.74 0.02 1
63 . 17 LEU HA H 3.9 0.02 1
64 . 17 LEU HB2 H 1.85 0.02 2
65 . 17 LEU HB3 H 1.56 0.02 2
66 . 18 VAL H H 8.51 0.02 1
67 . 18 VAL HA H 3.74 0.02 1
68 . 18 VAL HB H 1.99 0.02 1
69 . 18 VAL HG1 H 0.78 0.02 2
70 . 18 VAL HG2 H 0.93 0.02 2
71 . 19 CYS H H 8.7 0.02 1
72 . 19 CYS HA H 4.76 0.02 1
73 . 19 CYS HB2 H 2.92 0.02 2
74 . 19 CYS HB3 H 3.35 0.02 2
75 . 20 GLY H H 7.74 0.02 1
76 . 20 GLY HA2 H 3.77 0.02 2
77 . 20 GLY HA3 H 3.91 0.02 2
78 . 21 GLU H H 8.98 0.02 1
79 . 21 GLU HA H 4.19 0.02 1
80 . 21 GLU HB2 H 2.25 0.02 2
81 . 21 GLU HB3 H 1.99 0.02 2
82 . 21 GLU HG2 H 2.54 0.02 2
83 . 21 GLU HG3 H 2.11 0.02 2
84 . 22 ARG H H 8.13 0.02 1
85 . 22 ARG HA H 4.15 0.02 1
86 . 22 ARG HG2 H 1.84 0.02 4
87 . 22 ARG HE H 7.15 0.02 1
88 . 23 GLY HA2 H 4.38 0.02 2
89 . 23 GLY HA3 H 4.1 0.02 2
90 . 24 PHE H H 8.39 0.02 1
91 . 24 PHE HA H 4.99 0.02 1
92 . 24 PHE HB2 H 2.93 0.02 2
93 . 24 PHE HB3 H 3.22 0.02 2
94 . 24 PHE HD1 H 6.89 0.02 3
95 . 25 PHE H H 9.58 0.02 1
96 . 25 PHE HB2 H 3.92 0.02 2
97 . 25 PHE HB3 H 3.8 0.02 2
98 . 28 THR H H 8.13 0.02 1
99 . 28 THR HA H 4.15 0.02 1
100 . 28 THR HG2 H 1.24 0.02 1
101 . 29 LYS H H 8.29 0.02 1
102 . 29 LYS HA H 4.38 0.02 1
103 . 29 LYS HB2 H 1.88 0.02 2
104 . 29 LYS HG2 H 1.46 0.02 2
105 . 29 LYS HD2 H 1.68 0.02 4
106 . 29 LYS HE2 H 3 0.02 2
107 . 29 LYS HZ H 7.52 0.02 1
108 . 30 THR HA H 4.28 0.02 1
109 . 30 THR HB H 4.23 0.02 1
110 . 30 THR HG2 H 1.15 0.02 1
stop_
save_
save_CS_3
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'COSY with DQF'
'TOCSY/NOESY with WaterGate'
'HSQC: Gradient enhanced'
stop_
loop_
_Sample_label
$sample_2
stop_
_Sample_conditions_label $cond_TFE
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'PT-insulin A chain'
_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 GLY HA2 H 4.09 0.02 2
2 . 1 GLY HA3 H 4.01 0.02 2
3 . 1 GLY CA C 43.75 0.02 1
4 . 2 ILE H H 8.52 0.02 1
5 . 2 ILE HA H 3.95 0.02 1
6 . 2 ILE HB H 0.95 0.02 1
7 . 2 ILE HG12 H 1.30 0.02 2
8 . 2 ILE HG13 H 1.23 0.02 2
9 . 2 ILE HG2 H 0.76 0.02 1
10 . 2 ILE HD1 H 0.68 0.02 1
11 . 2 ILE CA C 63.31 0.02 1
12 . 2 ILE CG2 C 17.08 0.02 1
13 . 2 ILE CD1 C 12.59 0.02 1
14 . 3 VAL H H 8.11 0.02 1
15 . 3 VAL HA H 3.38 0.02 1
16 . 3 VAL HB H 1.95 0.02 1
17 . 3 VAL HG1 H 0.95 0.02 2
18 . 3 VAL HG2 H 0.91 0.02 2
19 . 3 VAL CA C 66.15 0.02 1
20 . 3 VAL CB C 27.34 0.02 1
21 . 4 GLU H H 8.19 0.02 1
22 . 4 GLU HA H 4.11 0.02 1
23 . 4 GLU HB2 H 2.18 0.02 2
24 . 4 GLU HB3 H 2.07 0.02 2
25 . 4 GLU HG2 H 2.58 0.02 2
26 . 4 GLU HG3 H 2.40 0.02 2
27 . 4 GLU CA C 61.49 0.02 1
28 . 4 GLU CG C 34.94 0.02 1
29 . 5 GLN H H 8.26 0.02 1
30 . 5 GLN HA H 4.05 0.02 1
31 . 5 GLN HB2 H 2.88 0.02 2
32 . 5 GLN HB3 H 2.10 0.02 2
33 . 5 GLN HG2 H 2.49 0.02 2
34 . 5 GLN HG3 H 2.42 0.02 2
35 . 5 GLN HE21 H 7.54 0.02 2
36 . 5 GLN CA C 59.08 0.02 1
37 . 5 GLN CG C 33.17 0.02 1
38 . 6 CYS H H 8.38 0.02 1
39 . 6 CYS HA H 4.95 0.02 1
40 . 6 CYS HB2 H 3.37 0.02 2
41 . 6 CYS HB3 H 2.96 0.02 2
42 . 6 CYS CA C 55.37 0.02 1
43 . 7 CYS H H 8.29 0.02 1
44 . 7 CYS HA H 4.89 0.02 1
45 . 7 CYS HB2 H 3.73 0.02 2
46 . 7 CYS HB3 H 3.32 0.02 2
47 . 7 CYS CA C 57.41 0.02 1
48 . 8 THR HA H 4.20 0.02 1
49 . 8 THR HB H 4.44 0.02 1
50 . 8 THR HG2 H 1.27 0.02 1
51 . 8 THR CA C 60.47 0.02 1
52 . 8 THR CB C 69.45 0.02 1
53 . 8 THR CG2 C 21.99 0.02 1
54 . 9 SER HA H 4.76 0.02 1
55 . 9 SER HB2 H 4.08 0.02 2
56 . 9 SER HB3 H 3.92 0.02 2
57 . 9 SER CA C 53.44 0.02 1
58 . 10 ILE H H 7.92 0.02 1
59 . 10 ILE HA H 4.53 0.02 1
60 . 10 ILE HB H 1.69 0.02 1
61 . 10 ILE HG12 H 1.30 0.02 2
62 . 10 ILE HG2 H 0.77 0.02 1
63 . 10 ILE HD1 H 0.66 0.02 1
64 . 10 ILE CA C 56.59 0.02 1
65 . 10 ILE CB C 39.46 0.02 1
66 . 10 ILE CG2 C 17.48 0.02 1
67 . 10 ILE CD1 C 14.19 0.02 1
68 . 11 CYS H H 9.37 0.02 1
69 . 11 CYS HA H 5.08 0.02 1
70 . 11 CYS CA C 53.62 0.02 1
71 . 12 SER H H 8.71 0.02 1
72 . 12 SER HA H 4.66 0.02 1
73 . 12 SER HB2 H 4.29 0.02 2
74 . 12 SER HB3 H 4.03 0.02 2
75 . 12 SER CB C 66.11 0.02 1
76 . 13 LEU H H 8.59 0.02 1
77 . 13 LEU HA H 4.08 0.02 1
78 . 13 LEU HB2 H 1.51 0.02 2
79 . 13 LEU HB3 H 1.46 0.02 2
80 . 13 LEU HG H 1.57 0.02 1
81 . 13 LEU HD1 H 0.90 0.02 2
82 . 13 LEU HD2 H 0.82 0.02 2
83 . 13 LEU CA C 59.37 0.02 1
84 . 13 LEU CB C 41.88 0.02 1
85 . 14 TYR H H 7.42 0.02 1
86 . 14 TYR HA H 4.19 0.02 1
87 . 14 TYR HB2 H 3.03 0.02 2
88 . 14 TYR HB3 H 2.96 0.02 2
89 . 14 TYR HD1 H 7.12 0.02 3
90 . 14 TYR HE1 H 6.89 0.02 .
91 . 14 TYR CA C 60.47 0.02 1
92 . 14 TYR CB C 37.89 0.02 1
93 . 14 TYR CD1 C 132.90 0.02 3
94 . 14 TYR CE1 C 118.59 0.02 3
95 . 15 GLN H H 7.57 0.02 1
96 . 15 GLN HA H 4.01 0.02 1
97 . 15 GLN HG2 H 2.48 0.02 2
98 . 15 GLN HG3 H 2.41 0.02 2
99 . 15 GLN HE21 H 7.49 0.02 2
100 . 15 GLN HE22 H 6.95 0.02 2
101 . 15 GLN CA C 58.65 0.02 1
102 . 15 GLN CB C 28.00 0.02 1
103 . 16 LEU H H 7.98 0.02 1
104 . 16 LEU HA H 4.18 0.02 1
105 . 16 LEU HB2 H 1.98 0.02 2
106 . 16 LEU HB3 H 1.79 0.02 2
107 . 16 LEU HG H 1.59 0.02 1
108 . 16 LEU HD1 H 0.88 0.02 2
109 . 16 LEU HD2 H 0.83 0.02 2
110 . 16 LEU CA C 58.48 0.02 1
111 . 17 GLU H H 8.21 0.02 1
112 . 17 GLU HA H 4.20 0.02 1
113 . 17 GLU HB2 H 2.14 0.02 2
114 . 17 GLU HB3 H 2.08 0.02 2
115 . 17 GLU HG2 H 2.57 0.02 2
116 . 17 GLU HG3 H 2.43 0.02 2
117 . 17 GLU CA C 58.43 0.02 1
118 . 17 GLU CG C 33.41 0.02 1
119 . 18 ASN H H 7.48 0.02 1
120 . 18 ASN HA H 4.47 0.02 1
121 . 18 ASN HB2 H 2.65 0.02 2
122 . 18 ASN HB3 H 2.57 0.02 2
123 . 18 ASN HD21 H 7.20 0.02 2
124 . 18 ASN CA C 60.49 0.02 1
125 . 18 ASN CB C 39.06 0.02 1
126 . 19 TYR H H 8.01 0.02 1
127 . 19 TYR HA H 4.51 0.02 1
128 . 19 TYR HB2 H 3.39 0.02 2
129 . 19 TYR HB3 H 3.06 0.02 2
130 . 19 TYR HD1 H 7.34 0.02 3
131 . 19 TYR HE1 H 6.83 0.02 3
132 . 19 TYR CA C 55.42 0.02 1
133 . 19 TYR CB C 38.52 0.02 1
134 . 19 TYR CD1 C 130.76 0.02 3
135 . 19 TYR CE1 C 118.27 0.02 3
136 . 20 CYS H H 7.46 0.02 1
137 . 20 CYS HA H 4.87 0.02 1
138 . 20 CYS HB2 H 3.28 0.02 2
139 . 20 CYS HB3 H 2.89 0.02 2
140 . 20 CYS CA C 54.93 0.02 1
141 . 21 ASN H H 8.13 0.02 1
142 . 21 ASN HA H 4.66 0.02 1
143 . 21 ASN HB2 H 2.87 0.02 2
144 . 21 ASN HB3 H 2.76 0.02 2
145 . 21 ASN HD21 H 7.48 0.02 2
146 . 21 ASN CA C 56.82 0.02 1
147 . 21 ASN CB C 39.27 0.02 1
stop_
save_
save_CS_4
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'COSY with DQF'
'TOCSY/NOESY with WaterGate'
'HSQC: Gradient enhanced'
stop_
loop_
_Sample_label
$sample_2
stop_
_Sample_conditions_label $cond_TFE
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'PT-insulin B chain'
_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 PHE HA H 4.33 0.02 1
2 . 1 PHE HB2 H 3.27 0.02 2
3 . 1 PHE HB3 H 3.2 0.02 2
4 . 1 PHE HD1 H 7.32 0.02 3
5 . 1 PHE HE1 H 7.38 0.02 3
6 . 1 PHE HZ H 7.42 0.02 1
7 . 1 PHE CA C 57.41 0.02 1
8 . 1 PHE CB C 39.85 0.02 1
9 . 1 PHE CD1 C 132.24 0.02 3
10 . 1 PHE CE1 C 131.97 0.02 3
11 . 2 VAL H H 8.17 0.02 1
12 . 2 VAL HA H 4.14 0.02 1
13 . 2 VAL HB H 2.01 0.02 1
14 . 2 VAL HG1 H 0.92 0.02 2
15 . 2 VAL CA C 62.51 0.02 1
16 . 3 ASN H H 8.37 0.02 1
17 . 3 ASN HA H 4.73 0.02 1
18 . 3 ASN HB2 H 2.83 0.02 2
19 . 3 ASN HB3 H 2.78 0.02 2
20 . 3 ASN HD21 H 7.57 0.02 2
21 . 3 ASN HD22 H 6.88 0.02 2
22 . 3 ASN CA C 56.63 0.02 1
23 . 3 ASN CB C 39.03 0.02 1
24 . 4 GLN H H 8.39 0.02 1
25 . 4 GLN HA H 4.41 0.02 1
26 . 4 GLN HB2 H 2.15 0.02 2
27 . 4 GLN HB3 H 1.92 0.02 2
28 . 4 GLN HG2 H 2.32 0.02 2
29 . 4 GLN HG3 H 2.26 0.02 2
30 . 4 GLN HE21 H 7.27 0.02 2
31 . 4 GLN HE22 H 6.69 0.02 2
32 . 4 GLN CA C 56.5 0.02 1
33 . 4 GLN CB C 31.86 0.02 1
34 . 5 HIS H H 8.57 0.02 1
35 . 5 HIS HA H 4.58 0.02 1
36 . 5 HIS HB2 H 3.58 0.02 2
37 . 5 HIS HB3 H 3.32 0.02 2
38 . 5 HIS HD2 H 7.42 0.02 1
39 . 5 HIS HE1 H 8.56 0.02 1
40 . 5 HIS CA C 57.7 0.02 1
41 . 5 HIS CB C 28.57 0.02 1
42 . 5 HIS CD2 C 120.72 0.02 1
43 . 5 HIS CE1 C 136.23 0.02 1
44 . 6 LEU H H 8.76 0.02 1
45 . 6 LEU HA H 4.48 0.02 1
46 . 6 LEU HB2 H 1.78 0.02 2
47 . 6 LEU HB3 H 1.62 0.02 2
48 . 6 LEU HG H 1.2 0.02 1
49 . 6 LEU HD1 H 0.83 0.02 2
50 . 6 LEU HD2 H 0.93 0.02 2
51 . 6 LEU CA C 59.42 0.02 1
52 . 7 CYS H H 8.25 0.02 1
53 . 7 CYS HA H 4.46 0.02 1
54 . 7 CYS HB2 H 3.18 0.02 2
55 . 7 CYS HB3 H 3.07 0.02 2
56 . 7 CYS CA C 56.01 0.02 1
57 . 8 GLY H H 8.92 0.02 1
58 . 8 GLY HA2 H 3.99 0.02 2
59 . 8 GLY HA3 H 3.79 0.02 2
60 . 8 GLY CA C 45.41 0.02 1
61 . 9 SER H H 8.75 0.02 1
62 . 9 SER HA H 4.08 0.02 1
63 . 9 SER HB2 H 3.92 0.02 2
64 . 9 SER CA C 59.64 0.02 1
65 . 9 SER CB C 64.33 0.02 1
66 . 10 HIS H H 7.93 0.02 1
67 . 10 HIS HA H 4.55 0.02 1
68 . 10 HIS HB2 H 3.53 0.02 2
69 . 10 HIS HB3 H 3.33 0.02 2
70 . 10 HIS HD2 H 7.77 0.02 1
71 . 10 HIS HE1 H 8.66 0.02 1
72 . 10 HIS CA C 58.06 0.02 1
73 . 10 HIS CB C 28.19 0.02 1
74 . 10 HIS CD2 C 119.93 0.02 1
75 . 10 HIS CE1 C 136.53 0.02 1
76 . 11 LEU HA H 3.94 0.02 1
77 . 11 LEU CA C 58.25 0.02 1
78 . 12 VAL H H 7.16 0.02 1
79 . 12 VAL HA H 3.41 0.02 1
80 . 12 VAL HB H 2.07 0.02 1
81 . 12 VAL HG1 H 0.96 0.02 2
82 . 12 VAL CA C 67.17 0.02 1
83 . 12 VAL CB C 28.21 0.02 1
84 . 13 GLU H H 7.88 0.02 1
85 . 13 GLU HA H 4.01 0.02 1
86 . 13 GLU HB2 H 2.24 0.02 2
87 . 13 GLU HB3 H 2.11 0.02 2
88 . 13 GLU HG2 H 2.6 0.02 2
89 . 13 GLU HG3 H 2.44 0.02 2
90 . 13 GLU CA C 59.01 0.02 1
91 . 13 GLU CB C 29.45 0.02 1
92 . 14 ALA H H 7.86 0.02 1
93 . 14 ALA HA H 4.09 0.02 1
94 . 14 ALA HB H 1.52 0.02 1
95 . 14 ALA CA C 55.66 0.02 1
96 . 14 ALA CB C 18.52 0.02 1
97 . 15 LEU H H 8.23 0.02 1
98 . 15 LEU HA H 3.94 0.02 1
99 . 15 LEU HB2 H 1.54 0.02 2
100 . 15 LEU HB3 H 1.5 0.02 2
101 . 15 LEU HG H 1.6 0.02 1
102 . 15 LEU HD1 H 0.76 0.02 2
103 . 15 LEU HD2 H 0.61 0.02 2
104 . 15 LEU CA C 62.8 0.02 1
105 . 15 LEU CD1 C 24.34 0.02 2
106 . 15 LEU CD2 C 25.58 0.02 2
107 . 16 TYR H H 8.36 0.02 1
108 . 16 TYR HA H 4.2 0.02 1
109 . 16 TYR HB2 H 3.19 0.02 2
110 . 16 TYR HD1 H 7.14 0.02 3
111 . 16 TYR HE1 H 6.9 0.02 3
112 . 16 TYR CA C 61.85 0.02 1
113 . 16 TYR CB C 38.09 0.02 1
114 . 16 TYR CD1 C 133 0.02 3
115 . 16 TYR CE1 C 118.14 0.02 3
116 . 17 LEU H H 8.12 0.02 1
117 . 17 LEU HA H 4.07 0.02 1
118 . 17 LEU HB2 H 1.98 0.02 2
119 . 17 LEU HB3 H 1.92 0.02 2
120 . 17 LEU HG H 1.63 0.02 1
121 . 17 LEU HD1 H 0.93 0.02 2
122 . 17 LEU CA C 58.14 0.02 1
123 . 18 VAL H H 8.82 0.02 1
124 . 18 VAL HA H 3.77 0.02 1
125 . 18 VAL HB H 2.13 0.02 1
126 . 18 VAL HG1 H 1.06 0.02 2
127 . 18 VAL HG2 H 0.91 0.02 2
128 . 18 VAL CA C 66 0.02 1
129 . 18 VAL CB C 32.65 0.02 1
130 . 19 CYS H H 8.82 0.02 1
131 . 19 CYS HA H 4.83 0.02 1
132 . 19 CYS HB2 H 3.26 0.02 2
133 . 19 CYS HB3 H 3.03 0.02 2
134 . 19 CYS CA C 54.27 0.02 1
135 . 20 GLY H H 7.82 0.02 1
136 . 20 GLY HA2 H 3.94 0.02 2
137 . 20 GLY CA C 46.76 0.02 1
138 . 21 GLU H H 8.43 0.02 1
139 . 21 GLU HA H 4.23 0.02 1
140 . 21 GLU HB2 H 2.24 0.02 2
141 . 21 GLU HB3 H 2.13 0.02 2
142 . 21 GLU HG2 H 2.56 0.02 2
143 . 21 GLU HG3 H 2.51 0.02 2
144 . 21 GLU CA C 57.17 0.02 1
145 . 21 GLU CB C 28.23 0.02 1
146 . 22 ARG H H 7.96 0.02 1
147 . 22 ARG HA H 4.22 0.02 1
148 . 22 ARG HB2 H 2.06 0.02 2
149 . 22 ARG HB3 H 2.03 0.02 2
150 . 22 ARG HG2 H 1.84 0.02 2
151 . 22 ARG HG3 H 1.78 0.02 2
152 . 22 ARG HD2 H 3.29 0.02 2
153 . 22 ARG HE H 7.32 0.02 1
154 . 22 ARG CA C 57.58 0.02 1
155 . 22 ARG CD C 43.82 0.02 1
156 . 23 GLY H H 7.75 0.02 1
157 . 23 GLY HA2 H 3.99 0.02 2
158 . 23 GLY HA3 H 3.87 0.02 2
159 . 23 GLY CA C 47.05 0.02 1
160 . 24 PHE H H 7.68 0.02 1
161 . 24 PHE HA H 4.77 0.02 1
162 . 24 PHE HB2 H 3.15 0.02 2
163 . 24 PHE HB3 H 2.99 0.02 2
164 . 24 PHE HD1 H 7.16 0.02 3
165 . 24 PHE HE1 H 7 0.02 3
166 . 24 PHE CB C 40.46 0.02 1
167 . 24 PHE CD1 C 132.21 0.02 3
168 . 24 PHE CE1 C 131.21 0.02 3
169 . 25 PHE H H 8.13 0.02 1
170 . 25 PHE HA H 4.63 0.02 1
171 . 25 PHE HB2 H 3.07 0.02 2
172 . 25 PHE HB3 H 3.02 0.02 2
173 . 25 PHE HD1 H 7.23 0.02 3
174 . 25 PHE HE1 H 7.32 0.02 3
175 . 25 PHE HZ H 7.27 0.02 1
176 . 25 PHE CA C 56.97 0.02 1
177 . 25 PHE CB C 40.1 0.02 1
178 . 25 PHE CD1 C 131.97 0.02 3
179 . 25 PHE CE1 C 133.58 0.02 3
180 . 26 TYR H H 7.86 0.02 1
181 . 26 TYR HA H 4.76 0.02 1
182 . 26 TYR HB2 H 3.02 0.02 2
183 . 26 TYR HB3 H 2.86 0.02 2
184 . 26 TYR CA C 56.01 0.02 1
185 . 26 TYR CB C 39.2 0.02 1
186 . 26 TYR CE1 C 118.08 0.02 3
187 . 27 PRO HA H 4.45 0.02 1
188 . 27 PRO HB2 H 2.22 0.02 2
189 . 27 PRO HG2 H 1.97 0.02 2
190 . 27 PRO HG3 H 1.92 0.02 2
191 . 27 PRO HD2 H 3.51 0.02 2
192 . 27 PRO HD3 H 3.26 0.02 2
193 . 27 PRO CA C 55.44 0.02 1
194 . 27 PRO CD C 50.54 0.02 1
195 . 28 THR H H 7.89 0.02 1
196 . 28 THR HA H 4.4 0.02 1
197 . 28 THR HB H 4.29 0.02 1
198 . 28 THR HG2 H 1.27 0.02 1
199 . 28 THR CA C 61.86 0.02 1
200 . 28 THR CB C 70.14 0.02 1
201 . 28 THR CG2 C 21.64 0.02 1
202 . 29 LYS H H 8.16 0.02 1
203 . 29 LYS HA H 4.49 0.02 1
204 . 29 LYS HB2 H 1.95 0.02 2
205 . 29 LYS HB3 H 1.82 0.02 2
206 . 29 LYS HG2 H 1.51 0.02 2
207 . 29 LYS HD2 H 1.74 0.02 2
208 . 29 LYS HE2 H 3.01 0.02 2
209 . 29 LYS HZ H 7.57 0.02 1
210 . 29 LYS CA C 55.44 0.02 1
211 . 29 LYS CB C 33.53 0.02 1
212 . 29 LYS CE C 42.38 0.02 1
213 . 30 THR H H 7.98 0.02 1
214 . 30 THR HA H 4.38 0.02 1
215 . 30 THR HG2 H 1.22 0.02 1
216 . 30 THR CA C 61.85 0.02 1
217 . 30 THR CB C 70.52 0.02 1
218 . 30 THR CG2 C 21.85 0.02 1
stop_
save_