HEADER HORMONE 29-DEC-12 2M2O
TITLE STRUCTURE OF [D-HISB24] INSULIN ANALOGUE AT PH 1.9
CAVEAT 2M2O CHIRALITY ERROR AT CA ATOM OF SER B9 IN MODEL 21
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN A CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: INSULIN B CHAIN;
COMPND 7 CHAIN: B;
COMPND 8 FRAGMENT: F24(D-HIS);
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606;
SOURCE 6 MOL_ID: 2;
SOURCE 7 SYNTHETIC: YES;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606
KEYWDS INSULIN, HORMONE
EXPDTA SOLUTION NMR
NUMMDL 29
AUTHOR L.ZAKOVA,V.VEVERKA,J.JIRACEK
REVDAT 2 05-JUN-13 2M2O 1 JRNL
REVDAT 1 06-MAR-13 2M2O 0
JRNL AUTH E.KLETVIKOVA,V.VEVERKA,M.LEPSIK,C.J.WATSON,J.P.TURKENBURG,
JRNL AUTH 2 J.JIRACEK,A.M.BRZOZOWSKI
JRNL TITL STRUCTURAL INTEGRITY OF THE B24 SITE IN HUMAN INSULIN IS
JRNL TITL 2 IMPORTANT FOR HORMONE FUNCTIONALITY.
JRNL REF J.BIOL.CHEM. V. 288 10230 2013
JRNL REFN ISSN 0021-9258
JRNL PMID 23447530
JRNL DOI 10.1074/JBC.M112.448050
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : CASE, DARDEN, CHEATHAM, III, SIMMERLING, WANG,
REMARK 3 DUKE, LUO, KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2M2O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-13.
REMARK 100 THE RCSB ID CODE IS RCSB103132.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 1.9
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.250 MM CHAIN_A, 0.250 MM
REMARK 210 CHAIN_B, 20% [U-2H] ACETIC ACID,
REMARK 210 95% H2O/5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-1H TOCSY; 2D 1H-1H NOESY;
REMARK 210 2D DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 29
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 17 ARG B 22 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 23 ARG B 22 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 28 ARG B 22 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
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 THR B 27 80.05 51.88
REMARK 500 2 ARG B 22 35.49 -80.48
REMARK 500 2 PHE B 25 117.61 53.48
REMARK 500 2 LYS B 29 147.01 61.51
REMARK 500 3 GLU A 4 5.77 -69.16
REMARK 500 4 THR A 8 -33.08 60.65
REMARK 500 8 GLN B 4 -167.90 -161.89
REMARK 500 8 LYS B 29 28.30 48.94
REMARK 500 12 GLU B 21 -32.03 68.51
REMARK 500 13 CYS A 11 122.18 58.34
REMARK 500 13 GLU B 21 36.72 -140.97
REMARK 500 13 DHI B 24 -18.57 -55.96
REMARK 500 14 GLU A 4 13.26 58.44
REMARK 500 14 LYS B 29 165.17 59.09
REMARK 500 15 ARG B 22 46.17 -79.65
REMARK 500 15 DHI B 24 30.99 -63.92
REMARK 500 15 THR B 27 54.47 39.02
REMARK 500 16 LEU B 6 179.62 56.29
REMARK 500 16 SER B 9 -35.86 59.03
REMARK 500 16 LYS B 29 -46.98 -150.15
REMARK 500 17 GLN B 4 -157.56 -154.44
REMARK 500 17 GLU B 21 -150.77 -99.68
REMARK 500 17 DHI B 24 -19.01 -52.40
REMARK 500 17 LYS B 29 -47.48 -148.84
REMARK 500 18 THR B 27 -58.20 -123.00
REMARK 500 19 CYS B 7 -93.64 -131.99
REMARK 500 19 SER B 9 -35.13 57.27
REMARK 500 19 LYS B 29 15.36 -141.58
REMARK 500 20 GLU A 4 15.11 58.74
REMARK 500 20 GLN A 5 -73.47 -90.11
REMARK 500 22 ILE A 2 -57.39 45.73
REMARK 500 23 ASN B 3 -132.78 47.75
REMARK 500 23 GLN B 4 162.31 59.55
REMARK 500 23 LYS B 29 -46.05 -145.45
REMARK 500 24 GLU A 4 16.88 59.10
REMARK 500 24 GLN A 5 -69.74 -102.56
REMARK 500 24 GLU B 21 -178.18 56.68
REMARK 500 24 TYR B 26 112.73 -33.84
REMARK 500 24 LYS B 29 -39.85 62.55
REMARK 500 25 GLU B 21 -40.39 66.78
REMARK 500 25 DHI B 24 74.87 80.44
REMARK 500 26 GLU A 4 24.07 48.75
REMARK 500 26 DHI B 24 11.74 -58.88
REMARK 500 27 LYS B 29 149.33 62.23
REMARK 500 28 GLU A 4 -60.31 66.07
REMARK 500 28 HIS B 5 77.76 -69.58
REMARK 500 28 SER B 9 -8.82 70.22
REMARK 500 28 THR B 27 72.35 45.94
REMARK 500 29 GLU B 21 -164.96 52.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 CYS A 6 CYS A 7 16 146.09
REMARK 500 GLU A 4 GLN A 5 24 145.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DHI B 24
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 18924 RELATED DB: BMRB
REMARK 900 RELATED ID: 2M2N RELATED DB: PDB
REMARK 900 RELATED ID: 2M2M RELATED DB: PDB
REMARK 900 RELATED ID: 2M2P RELATED DB: PDB
DBREF 2M2O A 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 2M2O B 1 30 UNP P01308 INS_HUMAN 25 54
SEQADV 2M2O DHI B 24 UNP P01308 PHE 48 ENGINEERED MUTATION
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 HIS LEU VAL GLU
SEQRES 2 B 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY DHI PHE TYR
SEQRES 3 B 30 THR PRO LYS THR
HET DHI B 24 17
HETNAM DHI D-HISTIDINE
FORMUL 2 DHI C6 H10 N3 O2 1+
HELIX 1 1 GLY A 1 SER A 9 1 9
HELIX 2 2 SER A 12 GLU A 17 1 6
HELIX 3 3 ASN A 18 ASN A 21 5 4
HELIX 4 4 CYS B 7 GLY B 20 1 14
SSBOND 1 CYS A 6 CYS A 11 1555 1555 2.04
SSBOND 2 CYS A 7 CYS B 7 1555 1555 2.04
SSBOND 3 CYS A 20 CYS B 19 1555 1555 2.03
LINK C GLY B 23 N DHI B 24 1555 1555 1.34
LINK C DHI B 24 N PHE B 25 1555 1555 1.33
CISPEP 1 LYS B 29 THR B 30 3 -4.67
CISPEP 2 GLU B 21 ARG B 22 4 -0.49
CISPEP 3 THR B 27 PRO B 28 14 -1.52
CISPEP 4 LYS B 29 THR B 30 17 -9.01
CISPEP 5 LYS B 29 THR B 30 22 -4.05
SITE 1 AC1 5 ARG B 22 GLY B 23 PHE B 25 LYS B 29
SITE 2 AC1 5 THR B 30
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
