HEADER LIPID BINDING PROTEIN 28-MAY-07 2JQ3
TITLE STRUCTURE AND DYNAMICS OF HUMAN APOLIPOPROTEIN C-III
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOLIPOPROTEIN C-III;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: APO-CIII, APOC-III;
COMPND 5 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: APOC3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET23B
KEYWDS APOCIII, DYNAMICS, APOLIPOPROTEIN, RECEPTOR, LIPID BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR C.S.GANGABADAGE,J.ZDUNEK,M.TESSARI,S.NILSSON,G.OLIVECRONA,S.WIJMENGA
REVDAT 4 19-FEB-20 2JQ3 1 REMARK
REVDAT 3 24-FEB-09 2JQ3 1 VERSN
REVDAT 2 01-JUL-08 2JQ3 1 JRNL
REVDAT 1 29-APR-08 2JQ3 0
JRNL AUTH C.S.GANGABADAGE,J.ZDUNEK,M.TESSARI,S.NILSSON,G.OLIVECRONA,
JRNL AUTH 2 S.S.WIJMENGA
JRNL TITL STRUCTURE AND DYNAMICS OF HUMAN APOLIPOPROTEIN CIII
JRNL REF J.BIOL.CHEM. V. 283 17416 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18408013
JRNL DOI 10.1074/JBC.M800756200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE
REMARK 3 AUTHORS : DELAGLIO, GRZESIEK, VUISTER, ZHU, PFEIFER AND BAX
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SIMULATED ANNEALING USING IVM ALGORITHM
REMARK 3 AVAILABLE WITHIN XPLOR-NIH (2.10) FOLLOWED BY ENERGY
REMARK 3 MINIMIZATION. IVM DYNAMICS (XPLOR-NIH) WITH RESTRAINING TERMS:
REMARK 3 NOE, CDIH, JCOUP, RDC AND 7 POSITIONAL RESTRAINTS (APPR. ONE CA
REMARK 3 ATOM PER HELIX NEAR THE MIDDLE OF EACH HELIX).
REMARK 4
REMARK 4 2JQ3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000100147.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 315.7
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 0.3
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM [U-13C; U-15N]
REMARK 210 APOLIPOPROTEIN CIII, 180 MM [U-
REMARK 210 2H] SDS, 92% H2O/8% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : CBCA(CO)NH; HNCACB; HNCO; HNHA;
REMARK 210 15N NOESY HSQC; 15N HSQC NOESY
REMARK 210 HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY, TALOS, X-PLOR NIH 2.10,
REMARK 210 MONTE_CARLO_SCRIPT, PROTEIN
REMARK 210 CONSTRUCTOR
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 LYS A 51 H SER A 55 1.42
REMARK 500 O ALA A 23 H LEU A 27 1.44
REMARK 500 O THR A 56 H LYS A 60 1.44
REMARK 500 O VAL A 30 H SER A 33 1.52
REMARK 500 O LEU A 50 H TRP A 54 1.53
REMARK 500 OD1 ASP A 52 H TYR A 53 1.54
REMARK 500 O TYR A 15 H ALA A 19 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 LEU A 8 -1.11 -55.15
REMARK 500 1 LYS A 24 -74.11 -50.90
REMARK 500 1 VAL A 30 0.89 -56.03
REMARK 500 1 GLN A 31 -13.21 -43.91
REMARK 500 1 VAL A 35 -7.73 -46.71
REMARK 500 1 GLN A 37 -38.45 -39.99
REMARK 500 1 ARG A 40 -5.44 -58.03
REMARK 500 1 TRP A 42 -18.17 -43.56
REMARK 500 1 SER A 49 -9.30 -53.33
REMARK 500 1 LYS A 51 -70.89 -55.78
REMARK 500 1 THR A 56 -76.31 -75.68
REMARK 500 1 PHE A 64 -4.95 -58.64
REMARK 500 1 PRO A 69 -11.63 -46.19
REMARK 500 2 ALA A 6 107.05 -54.08
REMARK 500 2 LEU A 8 -0.07 -58.55
REMARK 500 2 LYS A 24 -75.52 -50.87
REMARK 500 2 VAL A 30 1.45 -54.14
REMARK 500 2 GLN A 31 -16.66 -43.29
REMARK 500 2 VAL A 35 -14.52 -41.43
REMARK 500 2 ARG A 40 -4.37 -56.67
REMARK 500 2 TRP A 42 -18.77 -42.11
REMARK 500 2 SER A 49 -15.15 -47.66
REMARK 500 2 THR A 56 -75.86 -78.10
REMARK 500 2 PHE A 64 -7.67 -54.49
REMARK 500 2 PRO A 69 -10.52 -46.60
REMARK 500 3 LEU A 8 0.15 -56.69
REMARK 500 3 LYS A 24 -75.30 -50.23
REMARK 500 3 VAL A 30 0.37 -55.57
REMARK 500 3 GLN A 31 -16.28 -43.07
REMARK 500 3 VAL A 35 -11.65 -43.67
REMARK 500 3 GLN A 37 -39.83 -39.97
REMARK 500 3 ARG A 40 -7.83 -58.22
REMARK 500 3 TRP A 42 -17.68 -46.41
REMARK 500 3 ASP A 45 22.76 -69.40
REMARK 500 3 THR A 56 -77.26 -73.21
REMARK 500 3 PHE A 64 -1.40 -58.41
REMARK 500 3 PRO A 69 -13.24 -45.44
REMARK 500 4 ALA A 3 107.43 -55.34
REMARK 500 4 LEU A 8 -0.18 -57.38
REMARK 500 4 LYS A 24 -74.47 -51.67
REMARK 500 4 VAL A 30 1.75 -54.64
REMARK 500 4 GLN A 31 -16.08 -43.22
REMARK 500 4 VAL A 35 -6.92 -45.94
REMARK 500 4 GLN A 37 -39.23 -39.60
REMARK 500 4 ARG A 40 -5.28 -56.37
REMARK 500 4 PHE A 47 -16.89 -45.42
REMARK 500 4 THR A 56 -75.58 -76.50
REMARK 500 4 PHE A 64 -7.11 -57.84
REMARK 500 4 PRO A 69 -9.96 -45.64
REMARK 500 5 LEU A 8 0.19 -56.93
REMARK 500
REMARK 500 THIS ENTRY HAS 120 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 15268 RELATED DB: BMRB
DBREF 2JQ3 A 1 79 UNP P02656 APOC3_HUMAN 21 99
SEQRES 1 A 79 SER GLU ALA GLU ASP ALA SER LEU LEU SER PHE MET GLN
SEQRES 2 A 79 GLY TYR MET LYS HIS ALA THR LYS THR ALA LYS ASP ALA
SEQRES 3 A 79 LEU SER SER VAL GLN GLU SER GLN VAL ALA GLN GLN ALA
SEQRES 4 A 79 ARG GLY TRP VAL THR ASP GLY PHE SER SER LEU LYS ASP
SEQRES 5 A 79 TYR TRP SER THR VAL LYS ASP LYS PHE SER GLU PHE TRP
SEQRES 6 A 79 ASP LEU ASP PRO GLU VAL ARG PRO THR SER ALA VAL ALA
SEQRES 7 A 79 ALA
HELIX 1 1 LEU A 8 THR A 20 1 13
HELIX 2 2 THR A 22 SER A 29 1 8
HELIX 3 3 VAL A 30 GLN A 34 5 5
HELIX 4 4 VAL A 35 VAL A 43 1 9
HELIX 5 5 SER A 48 PHE A 61 1 14
HELIX 6 6 SER A 62 ASP A 66 5 5
HELIX 7 7 ARG A 72 ALA A 79 1 8
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
