HEADER HORMONE 21-NOV-08 2KB8
TITLE THE DYNAMIC ALPHA-HELIX STRUCTURE OF MICELLE-BOUND HUMAN AMYLIN.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISLET AMYLOID POLYPEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AMYLIN, DIABETES-ASSOCIATED PEPTIDE, DAP, INSULINOMA AMYLOID
COMPND 5 PEPTIDE;
COMPND 6 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: IAPP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 OTHER_DETAILS: RECOMBINANT 15N-LABELED AMYLIN WAS PURCHASED FROM
SOURCE 9 RPEPTIDE
KEYWDS IAPP, AMYLOID, MICELLE-BOUND, TYPE II DIABETES, HORMONE, AMIDATION,
KEYWDS 2 CLEAVAGE ON PAIR OF BASIC RESIDUES, POLYMORPHISM, SECRETED
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR S.M.PATIL,S.XU,S.R.SHEFTIC,A.T.ALEXANDRESCU
REVDAT 3 16-MAR-22 2KB8 1 REMARK
REVDAT 2 09-JUN-09 2KB8 1 JRNL
REVDAT 1 24-FEB-09 2KB8 0
JRNL AUTH S.M.PATIL,S.XU,S.R.SHEFTIC,A.T.ALEXANDRESCU
JRNL TITL DYNAMIC ALPHA-HELIX STRUCTURE OF MICELLE-BOUND HUMAN AMYLIN.
JRNL REF J.BIOL.CHEM. V. 284 11982 2009
JRNL REFN ISSN 0021-9258
JRNL PMID 19244249
JRNL DOI 10.1074/JBC.M809085200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2KB8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-NOV-08.
REMARK 100 THE DEPOSITION ID IS D_1000100905.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310; 310
REMARK 210 PH : 4.6; NULL
REMARK 210 IONIC STRENGTH : 60; 60
REMARK 210 PRESSURE : AMBIENT; NULL
REMARK 210 SAMPLE CONTENTS : 0.5 MM [U-100% 15N] AMYLIN, 100
REMARK 210 MM [U-99% 2H] SODIUM DODECYL
REMARK 210 SULFATE, 60 MM [U-99% 2H] ACETIC
REMARK 210 ACID, 100% D2O; 0.5 MM [U-99%
REMARK 210 15N] AMYLIN, 100 MM [U-2H] SDS,
REMARK 210 60 MM ACETIC ACID, 90% H2O/10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 1H-15N NOESY; 3D HNCA; 3D
REMARK 210 HNHB; 2D 1H-1H NOESY; 3D TROSY;
REMARK 210 3D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DGSA-DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 ILE A 26 H SER A 29 1.51
REMARK 500 O ALA A 8 H LEU A 12 1.56
REMARK 500 O GLY A 33 H ASN A 35 1.57
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 CYS A 2 -82.48 -86.69
REMARK 500 1 ASN A 3 17.65 -154.64
REMARK 500 1 THR A 4 -86.64 75.88
REMARK 500 1 ALA A 5 -18.50 -49.54
REMARK 500 1 THR A 6 -71.42 -92.44
REMARK 500 1 THR A 30 -73.97 -121.13
REMARK 500 1 SER A 34 -61.16 67.28
REMARK 500 1 ASN A 35 -170.68 -67.93
REMARK 500 2 CYS A 2 -101.56 -156.68
REMARK 500 2 ASN A 3 34.85 175.50
REMARK 500 2 THR A 4 105.17 -169.48
REMARK 500 2 ALA A 5 -25.99 -34.98
REMARK 500 2 ASN A 22 -75.70 -57.31
REMARK 500 2 THR A 30 -35.13 81.59
REMARK 500 2 SER A 34 -86.59 -121.01
REMARK 500 2 THR A 36 77.18 43.15
REMARK 500 3 THR A 4 -71.00 63.01
REMARK 500 3 THR A 6 -76.79 -92.71
REMARK 500 3 ASN A 31 27.79 41.96
REMARK 500 3 VAL A 32 -54.20 -174.31
REMARK 500 3 ASN A 35 74.89 47.63
REMARK 500 4 CYS A 2 -73.25 -52.01
REMARK 500 4 ASN A 3 -34.80 178.53
REMARK 500 4 ASN A 22 -63.82 -92.36
REMARK 500 4 SER A 29 63.66 -165.08
REMARK 500 4 ASN A 31 -21.78 168.66
REMARK 500 4 ASN A 35 -163.89 55.36
REMARK 500 4 THR A 36 98.46 -37.79
REMARK 500 5 CYS A 2 -116.56 -112.89
REMARK 500 5 ASN A 3 17.64 -162.44
REMARK 500 5 THR A 4 -83.51 72.88
REMARK 500 5 THR A 6 -75.29 -91.40
REMARK 500 5 THR A 30 -48.51 64.58
REMARK 500 5 SER A 34 -83.21 -158.11
REMARK 500 5 THR A 36 96.08 44.56
REMARK 500 6 CYS A 2 -85.48 -69.91
REMARK 500 6 ASN A 3 -26.75 170.08
REMARK 500 6 ASN A 31 13.68 -148.97
REMARK 500 6 ASN A 35 157.61 61.90
REMARK 500 6 THR A 36 79.46 -61.10
REMARK 500 7 CYS A 2 -76.09 -179.49
REMARK 500 7 ASN A 3 -33.57 177.03
REMARK 500 7 ALA A 5 -25.94 -39.88
REMARK 500 7 ASN A 31 27.33 176.30
REMARK 500 7 THR A 36 105.46 54.69
REMARK 500 8 CYS A 2 -78.20 -45.66
REMARK 500 8 ASN A 3 -35.16 178.52
REMARK 500 8 ALA A 5 -24.21 -39.53
REMARK 500 8 SER A 29 66.72 -167.62
REMARK 500 8 ASN A 31 -30.19 -164.54
REMARK 500
REMARK 500 THIS ENTRY HAS 200 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 11 0.25 SIDE CHAIN
REMARK 500 3 ARG A 11 0.22 SIDE CHAIN
REMARK 500 4 ARG A 11 0.08 SIDE CHAIN
REMARK 500 5 ARG A 11 0.28 SIDE CHAIN
REMARK 500 6 ARG A 11 0.31 SIDE CHAIN
REMARK 500 7 ARG A 11 0.21 SIDE CHAIN
REMARK 500 8 ARG A 11 0.31 SIDE CHAIN
REMARK 500 9 ARG A 11 0.27 SIDE CHAIN
REMARK 500 11 ARG A 11 0.29 SIDE CHAIN
REMARK 500 12 ARG A 11 0.14 SIDE CHAIN
REMARK 500 13 ARG A 11 0.31 SIDE CHAIN
REMARK 500 14 ARG A 11 0.26 SIDE CHAIN
REMARK 500 15 ARG A 11 0.18 SIDE CHAIN
REMARK 500 16 ARG A 11 0.31 SIDE CHAIN
REMARK 500 17 ARG A 11 0.23 SIDE CHAIN
REMARK 500 18 ARG A 11 0.16 SIDE CHAIN
REMARK 500 19 ARG A 11 0.23 SIDE CHAIN
REMARK 500 21 ARG A 11 0.31 SIDE CHAIN
REMARK 500 23 ARG A 11 0.28 SIDE CHAIN
REMARK 500 24 ARG A 11 0.30 SIDE CHAIN
REMARK 500 25 ARG A 11 0.21 SIDE CHAIN
REMARK 500 26 ARG A 11 0.17 SIDE CHAIN
REMARK 500 27 ARG A 11 0.17 SIDE CHAIN
REMARK 500 28 ARG A 11 0.16 SIDE CHAIN
REMARK 500 30 ARG A 11 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2KB8 A 1 37 UNP P10997 IAPP_HUMAN 34 70
SEQRES 1 A 37 LYS CYS ASN THR ALA THR CYS ALA THR GLN ARG LEU ALA
SEQRES 2 A 37 ASN PHE LEU VAL HIS SER SER ASN ASN PHE GLY ALA ILE
SEQRES 3 A 37 LEU SER SER THR ASN VAL GLY SER ASN THR TYR
HELIX 1 1 THR A 6 SER A 28 1 23
SSBOND 1 CYS A 2 CYS A 7 1555 1555 2.03
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
