HEADER LIPID BINDING PROTEIN 11-OCT-04 1XQ8
TITLE HUMAN MICELLE-BOUND ALPHA-SYNUCLEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-SYNUCLEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NON-A BETA COMPONENT OF AD AMYLOID, NON-A4 COMPONENT OF
COMPND 5 AMYLOID, NACP;
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: SNCA, NACP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET-41
KEYWDS MICELLE-BOUND HELIX, LIPID BINDING PROTEIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR T.S.ULMER,A.BAX,N.B.COLE,R.L.NUSSBAUM
REVDAT 7 02-MAR-22 1XQ8 1 REMARK
REVDAT 6 24-FEB-09 1XQ8 1 VERSN
REVDAT 5 26-APR-05 1XQ8 1 HEADER
REVDAT 4 12-APR-05 1XQ8 1 JRNL
REVDAT 3 22-FEB-05 1XQ8 1 JRNL
REVDAT 2 08-FEB-05 1XQ8 1 JRNL
REVDAT 1 11-JAN-05 1XQ8 0
JRNL AUTH T.S.ULMER,A.BAX,N.B.COLE,R.L.NUSSBAUM
JRNL TITL STRUCTURE AND DYNAMICS OF MICELLE-BOUND HUMAN
JRNL TITL 2 ALPHA-SYNUCLEIN
JRNL REF J.BIOL.CHEM. V. 280 9595 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15615727
JRNL DOI 10.1074/JBC.M411805200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 2.9.5
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: PLEASE NOTE THAT LARGE AMPLITUDE
REMARK 3 DYNAMICS ARE PRESENT IN THIS SYSTEM, DESCRIBED IN THE PRIMARY
REMARK 3 CITATION, AND THE REPORTED STRUCTURE MERELY REPRESENTS THE
REMARK 3 EFFECTIVE AVERAGE CONFORMATION OF THE MOLECULE.
REMARK 4
REMARK 4 1XQ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000030638.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.2
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 115
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.5 MM ALPHA-SYNUCLEIN 2H, 13C,
REMARK 210 15N
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCO-QJ; HN(CO)CA-QJ; HNCO-JNH
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 2.9.5
REMARK 210 METHOD USED : MOLECULAR FRAGMENT REPLACEMENT,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : AVERAGE STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 ASN A 122 H ALA A 124 1.52
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 VAL A 95 101.52 -52.18
REMARK 500 LYS A 96 163.31 -46.73
REMARK 500 GLN A 99 -30.10 -175.72
REMARK 500 LYS A 102 90.03 48.10
REMARK 500 GLU A 105 120.48 168.47
REMARK 500 GLN A 109 -109.53 -57.01
REMARK 500 GLU A 110 -17.46 -171.13
REMARK 500 GLU A 114 -3.87 -54.43
REMARK 500 ASN A 122 30.68 -170.31
REMARK 500 GLU A 123 -52.52 66.99
REMARK 500 ALA A 124 -139.70 -156.57
REMARK 500 TYR A 125 -72.31 -53.41
REMARK 500 GLU A 126 88.83 -151.08
REMARK 500 MET A 127 -171.21 52.67
REMARK 500 GLU A 130 -149.52 35.41
REMARK 500 TYR A 133 -77.99 56.83
REMARK 500 ASP A 135 -17.92 -163.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 THE SECONDARY STRUCTURE OF THIS PROTEIN WAS
REMARK 650 AUTHOR DETERMINED
DBREF 1XQ8 A 1 140 UNP P37840 SYUA_HUMAN 1 140
SEQRES 1 A 140 MET ASP VAL PHE MET LYS GLY LEU SER LYS ALA LYS GLU
SEQRES 2 A 140 GLY VAL VAL ALA ALA ALA GLU LYS THR LYS GLN GLY VAL
SEQRES 3 A 140 ALA GLU ALA ALA GLY LYS THR LYS GLU GLY VAL LEU TYR
SEQRES 4 A 140 VAL GLY SER LYS THR LYS GLU GLY VAL VAL HIS GLY VAL
SEQRES 5 A 140 ALA THR VAL ALA GLU LYS THR LYS GLU GLN VAL THR ASN
SEQRES 6 A 140 VAL GLY GLY ALA VAL VAL THR GLY VAL THR ALA VAL ALA
SEQRES 7 A 140 GLN LYS THR VAL GLU GLY ALA GLY SER ILE ALA ALA ALA
SEQRES 8 A 140 THR GLY PHE VAL LYS LYS ASP GLN LEU GLY LYS ASN GLU
SEQRES 9 A 140 GLU GLY ALA PRO GLN GLU GLY ILE LEU GLU ASP MET PRO
SEQRES 10 A 140 VAL ASP PRO ASP ASN GLU ALA TYR GLU MET PRO SER GLU
SEQRES 11 A 140 GLU GLY TYR GLN ASP TYR GLU PRO GLU ALA
HELIX 1 1 VAL A 3 VAL A 37 1 35
HELIX 2 2 LYS A 45 THR A 92 1 48
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
(ATOM LINES ARE NOT SHOWN.)
END
