Header list of 2bp4.pdb file
Complete list - 25 20 Bytes
HEADER AMYLOID PEPTIDE 18-APR-05 2BP4
TITLE ZINC-BINDING DOMAIN OF ALZHEIMER'S DISEASE AMYLOID BETA-
TITLE 2 PEPTIDE IN TFE-WATER (80-20) SOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMYLOID BETA A4 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: 16-MER FRAGMENT BETWEEN THE BETA AND ALPHA
COMPND 5 SECRETASES CLEAVAGE SITES OF ALZHEIMER'S DISEASE AMYLOID
COMPND 6 A4 PROTEIN, RESIDUES 672-687;
COMPND 7 SYNONYM: APP, ABPP, ALZHEIMER'S DISEASE AMYLOID A4
COMPND 8 PROTEIN, CEREBRAL VASCULAR AMYLOID PEPTIDE, CVAP,
COMPND 9 PROTEASE NEXIN-II, PN-II, APPI, PREA4
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606
KEYWDS 3D-STRUCTURE, HELIX, ALZHEIMER'S DISEASE, AMYLOID, AMYLOID
KEYWDS 2 PEPTIDE, BETA-AMYLOID PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.ZIRAH,S.A.KOZIN,A.K.MAZUR,A.BLOND,M.CHEMINANT,
AUTHOR 2 I.SEGALAS-MILAZZO,P.DEBEY,S.REBUFFAT
REVDAT 3 24-FEB-09 2BP4 1 VERSN
REVDAT 2 25-JAN-06 2BP4 1 JRNL
REVDAT 1 21-APR-05 2BP4 0
SPRSDE 21-APR-05 2BP4 1O6N
JRNL AUTH S.ZIRAH,S.A.KOZIN,A.K.MAZUR,A.BLOND,M.CHEMINANT,
JRNL AUTH 2 I.SEGALAS-MILAZZO,P.DEBEY,S.REBUFFAT
JRNL TITL STRUCTURAL CHANGES OF REGION 1-16 OF THE ALZHEIMER
JRNL TITL 2 DISEASE AMYLOID BETA-PEPTIDE UPON ZINC BINDING AND
JRNL TITL 3 IN VITRO AGING.
JRNL REF J.BIOL.CHEM. V. 281 2151 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16301322
JRNL DOI 10.1074/JBC.M504454200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ICMD
REMARK 3 AUTHORS : ALEXEY K. MAZUR
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN
REMARK 3 THE JRNL CITATION ABOVE
REMARK 4
REMARK 4 2BP4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-APR-05.
REMARK 100 THE PDBE ID CODE IS EBI-23670.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0
REMARK 210 PH : 3.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1.0
REMARK 210 SAMPLE CONTENTS : 80 % TFE-D2OH / 20 % H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY, 2D TOCSY
REMARK 210 2D NOESY, HSQC, HMBC
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 ; 600
REMARK 210 SPECTROMETER MODEL : AVANCE ; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ICMD 2.7
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMAL TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES
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 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 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 5 GLN A 15 45.11 -91.10
REMARK 500 8 HIS A 14 59.17 -104.97
REMARK 500 11 GLN A 15 45.36 -84.46
REMARK 500 12 GLN A 15 46.35 -87.59
REMARK 500 14 HIS A 14 53.09 -95.48
REMARK 500 17 HIS A 14 60.45 -110.68
REMARK 500 18 HIS A 14 53.24 -101.43
REMARK 500 19 HIS A 14 46.56 -95.78
REMARK 500 20 HIS A 14 -71.08 -92.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AAP RELATED DB: PDB
REMARK 900
REMARK 900 RELATED ID: 1AMB RELATED DB: PDB
REMARK 900 ALZHEIMER'S DISEASE AMYLOID BETA-PEPTIDE (
REMARK 900 RESIDUES 1 - 28) (NMR, MINIMIZED AVERAGE
REMARK 900 STRUCTURE)
REMARK 900 RELATED ID: 1AMC RELATED DB: PDB
REMARK 900 ALZHEIMER'S DISEASE AMYLOID BETA-PEPTIDE (
REMARK 900 RESIDUES 1 - 28) (NMR, 5 STRUCTURES)
REMARK 900 RELATED ID: 1AML RELATED DB: PDB
REMARK 900 THE ALZHEIMER`S DISEASE AMYLOID A4 PEPTIDE
REMARK 900 (RESIDUES 1-40)
REMARK 900 RELATED ID: 1BA4 RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF AMYLOID BETA-
REMARK 900 PEPTIDE (1-40) IN A WATER-MICELLE
REMARK 900 ENVIRONMENT. IS THE MEMBRANE-SPANNING DOMAIN
REMARK 900 WHERE WE THINK IT IS? NMR, 10 STRUCTURES
REMARK 900 RELATED ID: 1BA6 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE METHIONINE-OXIDIZED
REMARK 900 AMYLOID BETA-PEPTIDE (1-40). DOES
REMARK 900 OXIDATION AFFECT CONFORMATIONAL SWITCHING? NMR
REMARK 900 , 10 STRUCTURES
REMARK 900 RELATED ID: 1BJB RELATED DB: PDB
REMARK 900 SOLUTION NMR STRUCTURE OF AMYLOID BETA[E16
REMARK 900 ], RESIDUES 1-28, 14 STRUCTURES
REMARK 900 RELATED ID: 1BJC RELATED DB: PDB
REMARK 900 SOLUTION NMR STRUCTURE OF AMYLOID BETA[F16
REMARK 900 ], RESIDUES 1-28, 15 STRUCTURES
REMARK 900 RELATED ID: 1BRC RELATED DB: PDB
REMARK 900
REMARK 900 RELATED ID: 1CA0 RELATED DB: PDB
REMARK 900 BOVINE CHYMOTRYPSIN COMPLEXED TO APPI
REMARK 900 RELATED ID: 1HZ3 RELATED DB: PDB
REMARK 900 ALZHEIMER'S DISEASE AMYLOID-BETA PEPTIDE (
REMARK 900 RESIDUES 10-35)
REMARK 900 RELATED ID: 1IYT RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE ALZHEIMER'S
REMARK 900 DISEASE AMYLOID BETA-PEPTIDE (1-42)
REMARK 900 RELATED ID: 1MWP RELATED DB: PDB
REMARK 900 N-TERMINAL DOMAIN OF THE AMYLOID PRECURSOR
REMARK 900 PROTEIN
REMARK 900 RELATED ID: 1O6N RELATED DB: PDB
REMARK 900 ABETA(1-16) FRAGMENT OF THE AMYLOID
REMARK 900 PEPTIDE
REMARK 900 RELATED ID: 1OWT RELATED DB: PDB
REMARK 900 STRUCTURE OF THE ALZHEIMER'S DISEASE AMYLOID
REMARK 900 PRECURSORPROTEIN COPPER BINDING DOMAIN
REMARK 900 RELATED ID: 1QCM RELATED DB: PDB
REMARK 900 AMYLOID BETA PEPTIDE (25-35), NMR, 20
REMARK 900 STRUCTURES
REMARK 900 RELATED ID: 1QWP RELATED DB: PDB
REMARK 900 NMR ANALYSIS OF 25-35 FRAGMENT OF BETA
REMARK 900 AMYLOID PEPTIDE
REMARK 900 RELATED ID: 1QXC RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE FRAGMENT 25-35 OF
REMARK 900 BETA AMYLOID PEPTIDEIN 20/80 V:V
REMARK 900 HEXAFLUOROISOPROPANOL/WATER MIXTURE
REMARK 900 RELATED ID: 1QYT RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF FRAGMENT (25-35) OF
REMARK 900 BETA AMYLOIDPEPTIDE IN SDS MICELLAR SOLUTION
REMARK 900 RELATED ID: 1TAW RELATED DB: PDB
REMARK 900 BOVINE TRYPSIN COMPLEXED TO APPI
REMARK 900 RELATED ID: 1TKN RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF CAPPD*, AN INDEPENDENTLY
REMARK 900 FOLDEDEXTRACELLULAR DOMAIN OF HUMAN AMYLOID-
REMARK 900 BETA PRECURSORPROTEIN
REMARK 900 RELATED ID: 1UO7 RELATED DB: PDB
REMARK 900 MOLECULAR DYNAMICS SIMULATION OF AMYLOID BETA
REMARK 900 1-42 (PDB: 1IYT) IN WATER
REMARK 900 RELATED ID: 1UO8 RELATED DB: PDB
REMARK 900 AFTER 2NS
REMARK 900 RELATED ID: 1UOA RELATED DB: PDB
REMARK 900 AFTER 3NS
REMARK 900 RELATED ID: 1UOI RELATED DB: PDB
REMARK 900 AFTER 4NS
REMARK 900 RELATED ID: 2BOM RELATED DB: PDB
REMARK 900 MODEL OF ALZHEIMER'S DISEASE AMYLOID-SS
REMARK 900 PEPTIDE BASED ON A RNA BINDING PROTEIN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 PEPTIDE FRAGMENT 672-687
DBREF 2BP4 A 1 16 UNP P05067 A4_HUMAN 672 687
SEQRES 1 A 16 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 A 16 HIS GLN LYS
HELIX 1 1 ASP A 1 GLN A 15 1 15
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
Complete list - 25 20 Bytes