HEADER HORMONE 27-FEB-14 2MLI
TITLE NMR STRUCTURE OF B25-(ALPHA, BETA)-DEHYDRO-PHENYLALANINE INSULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: A CHAIN (UNP RESIDUES 90-110);
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: INSULIN;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: B CHAIN (UNP RESIDUES 25-54);
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: INS;
SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: PICHIA PASTORIS;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPICZALPHA;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606
KEYWDS INSULIN ANALOG, HORMONE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Y.YANG,M.WEISS
REVDAT 3 14-JUN-23 2MLI 1 REMARK SEQADV LINK
REVDAT 2 03-SEP-14 2MLI 1 JRNL
REVDAT 1 20-AUG-14 2MLI 0
JRNL AUTH J.G.MENTING,Y.YANG,S.J.CHAN,N.B.PHILLIPS,B.J.SMITH,
JRNL AUTH 2 J.WHITTAKER,N.P.WICKRAMASINGHE,L.J.WHITTAKER,V.PANDYARAJAN,
JRNL AUTH 3 Z.L.WAN,S.P.YADAV,J.M.CARROLL,N.STROKES,C.T.ROBERTS,
JRNL AUTH 4 F.ISMAIL-BEIGI,W.MILEWSKI,D.F.STEINER,V.S.CHAUHAN,C.W.WARD,
JRNL AUTH 5 M.A.WEISS,M.C.LAWRENCE
JRNL TITL PROTECTIVE HINGE IN INSULIN OPENS TO ENABLE ITS RECEPTOR
JRNL TITL 2 ENGAGEMENT.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 E3395 2014
JRNL REFN ISSN 0027-8424
JRNL PMID 25092300
JRNL DOI 10.1073/PNAS.1412897111
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, X-PLOR NIH
REMARK 3 AUTHORS : DELAGLIO, GRZESIEK, VUISTER, ZHU, PFEIFER AND BAX
REMARK 3 (NMRPIPE), SCHWIETERS, KUSZEWSKI, TJANDRA AND
REMARK 3 CLORE (X-PLOR NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2MLI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000103759.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298
REMARK 210 PH : 7; 7
REMARK 210 IONIC STRENGTH : 0.01; 0.01
REMARK 210 PRESSURE : AMBIENT; NULL
REMARK 210 SAMPLE CONTENTS : 0.5 MM [U-13C; U-15N] INSULIN,
REMARK 210 90% H2O/10% D2O; 0.5 MM INSULIN,
REMARK 210 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 3D HNCACB; 3D CBCA(CO)NH; 3D
REMARK 210 HCCH-TOCSY; 3D 1H-13C NOESY; 3D
REMARK 210 C(CO)NH; 4D 13C, 13C-NOESY; 4D
REMARK 210 15N, 13C-NOESY; 2D 1H-1H NOESY;
REMARK 210 2D 1H-1H TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PIPP, X-PLOR NIH, INSIGHT II,
REMARK 210 PROCHECK
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLY B 29 H VAL B 33 1.57
REMARK 500 O VAL A 3 H CYS A 7 1.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 ARG B 43 -17.33 -47.02
REMARK 500 1 TYR B 47 -83.52 -176.97
REMARK 500 1 THR B 48 106.57 -176.07
REMARK 500 1 PRO B 50 -72.07 -51.28
REMARK 500 2 ARG B 43 -19.35 -48.41
REMARK 500 2 TYR B 47 118.67 -177.82
REMARK 500 2 THR B 48 -132.12 -89.93
REMARK 500 3 ARG B 43 -18.28 -47.02
REMARK 500 3 TYR B 47 103.93 -176.65
REMARK 500 4 ARG B 43 -17.01 -47.58
REMARK 500 4 TYR B 47 -87.92 -179.95
REMARK 500 4 THR B 48 -134.97 40.54
REMARK 500 4 PRO B 50 -75.55 -56.17
REMARK 500 5 ARG B 43 -17.48 -48.20
REMARK 500 5 TYR B 47 82.59 -176.76
REMARK 500 6 ARG B 43 -18.72 -49.06
REMARK 500 6 TYR B 47 94.82 -176.49
REMARK 500 6 LYS B 49 71.14 47.09
REMARK 500 7 ARG B 43 -18.38 -48.81
REMARK 500 7 TYR B 47 91.20 -179.33
REMARK 500 7 THR B 48 -28.20 -160.46
REMARK 500 8 ARG B 43 -18.39 -48.30
REMARK 500 8 TYR B 47 101.63 -179.54
REMARK 500 8 THR B 48 -60.08 -166.37
REMARK 500 9 ARG B 43 -18.99 -48.31
REMARK 500 9 TYR B 47 135.97 -176.50
REMARK 500 9 PRO B 50 -72.22 -56.06
REMARK 500 10 ARG B 43 -18.66 -46.51
REMARK 500 10 TYR B 47 104.19 -176.86
REMARK 500 10 LYS B 49 72.27 45.88
REMARK 500 10 PRO B 50 -70.41 -58.18
REMARK 500 11 ARG B 43 -16.27 -49.38
REMARK 500 11 TYR B 47 -64.39 -169.92
REMARK 500 11 THR B 48 99.36 97.00
REMARK 500 12 ARG B 43 -14.69 -49.22
REMARK 500 12 TYR B 47 97.78 -170.58
REMARK 500 13 ARG B 43 -15.49 -49.72
REMARK 500 13 TYR B 47 84.11 -175.86
REMARK 500 13 THR B 48 -144.92 -147.55
REMARK 500 13 LYS B 49 158.00 58.27
REMARK 500 14 ARG B 43 -18.05 -46.77
REMARK 500 14 TYR B 47 92.12 -175.91
REMARK 500 14 THR B 48 -117.88 -80.95
REMARK 500 15 ARG B 43 -15.78 -49.45
REMARK 500 15 TYR B 47 -84.88 -176.39
REMARK 500 15 THR B 48 -140.37 43.67
REMARK 500 15 LYS B 49 72.42 46.82
REMARK 500 16 ARG B 43 -17.75 -48.24
REMARK 500 16 TYR B 47 134.06 179.48
REMARK 500 16 PRO B 50 -71.32 -50.38
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 19822 RELATED DB: BMRB
DBREF 2MLI A 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 2MLI B 22 51 UNP P01308 INS_HUMAN 25 54
SEQADV 2MLI ASP B 31 UNP P01308 HIS 34 CONFLICT
SEQADV 2MLI LYS B 49 UNP P01308 PRO 52 CONFLICT
SEQADV 2MLI PRO B 50 UNP P01308 LYS 53 CONFLICT
SEQRES 1 A 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 A 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 B 30 PHE VAL ASN GLN HIS LEU CYS GLY SER ASP LEU VAL GLU
SEQRES 2 B 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE 23F TYR
SEQRES 3 B 30 THR LYS PRO THR
MODRES 2MLI 23F B 46 PHE (2Z)-2-AMINO-3-PHENYLACRYLIC ACID
HET 23F B 46 18
HETNAM 23F (2Z)-2-AMINO-3-PHENYLACRYLIC ACID
HETSYN 23F DEHYDROPHENYLALANINE
FORMUL 2 23F C9 H9 N O2
HELIX 1 1 GLY A 1 CYS A 7 1 7
HELIX 2 2 SER A 12 TYR A 19 1 8
HELIX 3 3 GLY B 29 CYS B 40 1 12
HELIX 4 4 GLY B 41 GLY B 44 5 4
SSBOND 1 CYS A 6 CYS A 11 1555 1555 2.01
SSBOND 2 CYS A 7 CYS B 28 1555 1555 2.02
SSBOND 3 CYS A 20 CYS B 40 1555 1555 2.01
LINK C PHE B 45 N 23F B 46 1555 1555 1.42
LINK C 23F B 46 N TYR B 47 1555 1555 1.40
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
