HEADER PROTEIN FIBRIL 03-JAN-12 2LNQ
TITLE 40-RESIDUE D23N BETA AMYLOID FIBRIL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: P3(40);
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 SYNONYM: AMYLOID BETA A4 PROTEIN, ABPP, APPI, APP, ALZHEIMER DISEASE
COMPND 5 AMYLOID PROTEIN, CEREBRAL VASCULAR AMYLOID PEPTIDE, CVAP, PREA4,
COMPND 6 PROTEASE NEXIN-II, PN-II;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: 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
KEYWDS IOWA MUTANT, ANTIPARALLEL BETA SHEET, PROTEIN FIBRIL
EXPDTA SOLID-STATE NMR
NUMMDL 10
AUTHOR W.QIANG,W.YAU,Y.LUO,M.P.MATTSON,R.TYCKO
REVDAT 1 08-FEB-12 2LNQ 0
JRNL AUTH W.QIANG,W.-M.YAU,Y.LUO,M.P.MATTSON,R.TYCKO
JRNL TITL ANTIPARALLEL BETA-SHEET ARCHITECTURE IN IOWA-MUTANT
JRNL TITL 2 BETA-AMYLOID FIBRILS
JRNL REF PROC.NATL.ACAD.SCI.USA 2012
JRNL REFN ESSN 1091-6490
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH 2.28.1
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2LNQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-12.
REMARK 100 THE RCSB ID CODE IS RCSB102608.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 279
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 25 UM [U-13C] PROTEIN, H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 13C-13C FPRFDR; 2D 13C-13C
REMARK 210 RAD; 2D 13C-13C CHHC; 1D 13C
REMARK 210 PITHIRDS-CT
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ
REMARK 210 SPECTROMETER MODEL : INFINITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 12
REMARK 210
REMARK 210 REMARK: NULL
REMARK 217
REMARK 217 SOLID STATE NMR STUDY
REMARK 217 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLID
REMARK 217 STATE NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 217 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 217 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: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-10
REMARK 465 RES C SSSEQI
REMARK 465 ASP A 1
REMARK 465 ALA A 2
REMARK 465 GLU A 3
REMARK 465 PHE A 4
REMARK 465 ARG A 5
REMARK 465 HIS A 6
REMARK 465 ASP A 7
REMARK 465 SER A 8
REMARK 465 GLY A 9
REMARK 465 TYR A 10
REMARK 465 GLU A 11
REMARK 465 VAL A 12
REMARK 465 HIS A 13
REMARK 465 HIS A 14
REMARK 465 ASP B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 PHE B 4
REMARK 465 ARG B 5
REMARK 465 HIS B 6
REMARK 465 ASP B 7
REMARK 465 SER B 8
REMARK 465 GLY B 9
REMARK 465 TYR B 10
REMARK 465 GLU B 11
REMARK 465 VAL B 12
REMARK 465 HIS B 13
REMARK 465 HIS B 14
REMARK 465 ASP C 1
REMARK 465 ALA C 2
REMARK 465 GLU C 3
REMARK 465 PHE C 4
REMARK 465 ARG C 5
REMARK 465 HIS C 6
REMARK 465 ASP C 7
REMARK 465 SER C 8
REMARK 465 GLY C 9
REMARK 465 TYR C 10
REMARK 465 GLU C 11
REMARK 465 VAL C 12
REMARK 465 HIS C 13
REMARK 465 HIS C 14
REMARK 465 ASP D 1
REMARK 465 ALA D 2
REMARK 465 GLU D 3
REMARK 465 PHE D 4
REMARK 465 ARG D 5
REMARK 465 HIS D 6
REMARK 465 ASP D 7
REMARK 465 SER D 8
REMARK 465 GLY D 9
REMARK 465 TYR D 10
REMARK 465 GLU D 11
REMARK 465 VAL D 12
REMARK 465 HIS D 13
REMARK 465 HIS D 14
REMARK 465 ASP E 1
REMARK 465 ALA E 2
REMARK 465 GLU E 3
REMARK 465 PHE E 4
REMARK 465 ARG E 5
REMARK 465 HIS E 6
REMARK 465 ASP E 7
REMARK 465 SER E 8
REMARK 465 GLY E 9
REMARK 465 TYR E 10
REMARK 465 GLU E 11
REMARK 465 VAL E 12
REMARK 465 HIS E 13
REMARK 465 HIS E 14
REMARK 465 ASP F 1
REMARK 465 ALA F 2
REMARK 465 GLU F 3
REMARK 465 PHE F 4
REMARK 465 ARG F 5
REMARK 465 HIS F 6
REMARK 465 ASP F 7
REMARK 465 SER F 8
REMARK 465 GLY F 9
REMARK 465 TYR F 10
REMARK 465 GLU F 11
REMARK 465 VAL F 12
REMARK 465 HIS F 13
REMARK 465 HIS F 14
REMARK 465 ASP G 1
REMARK 465 ALA G 2
REMARK 465 GLU G 3
REMARK 465 PHE G 4
REMARK 465 ARG G 5
REMARK 465 HIS G 6
REMARK 465 ASP G 7
REMARK 465 SER G 8
REMARK 465 GLY G 9
REMARK 465 TYR G 10
REMARK 465 GLU G 11
REMARK 465 VAL G 12
REMARK 465 HIS G 13
REMARK 465 HIS G 14
REMARK 465 ASP H 1
REMARK 465 ALA H 2
REMARK 465 GLU H 3
REMARK 465 PHE H 4
REMARK 465 ARG H 5
REMARK 465 HIS H 6
REMARK 465 ASP H 7
REMARK 465 SER H 8
REMARK 465 GLY H 9
REMARK 465 TYR H 10
REMARK 465 GLU H 11
REMARK 465 VAL H 12
REMARK 465 HIS H 13
REMARK 465 HIS H 14
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 HD21 ASN C 23 H GLN D 15 1.32
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 SER A 26 -51.48 -163.22
REMARK 500 1 LYS A 28 -7.40 -165.93
REMARK 500 1 ASN D 27 -169.87 -123.28
REMARK 500 1 LYS D 28 -48.15 -163.52
REMARK 500 1 SER E 26 -168.24 -115.00
REMARK 500 1 LYS G 28 -61.44 -99.09
REMARK 500 1 VAL H 24 -33.48 -160.73
REMARK 500 1 SER H 26 -175.10 53.03
REMARK 500 1 ASN H 27 153.80 -47.88
REMARK 500 2 VAL A 24 -166.20 -77.11
REMARK 500 2 SER A 26 -107.68 -168.43
REMARK 500 2 ASN A 27 61.90 -168.48
REMARK 500 2 LYS A 28 -111.71 45.51
REMARK 500 2 VAL B 24 -37.22 -149.11
REMARK 500 2 SER B 26 82.81 -170.33
REMARK 500 2 ASN B 27 -162.98 -76.30
REMARK 500 2 LYS B 28 -8.25 -142.07
REMARK 500 2 SER C 26 -109.06 -161.08
REMARK 500 2 ASN C 27 -162.71 -79.77
REMARK 500 2 SER D 26 139.58 -177.84
REMARK 500 2 ASN D 27 110.49 -176.77
REMARK 500 2 VAL F 24 37.44 -143.89
REMARK 500 2 SER F 26 71.59 48.61
REMARK 500 2 LYS F 28 -147.18 -144.98
REMARK 500 2 ASN G 27 171.67 56.01
REMARK 500 3 LYS B 28 -27.61 -153.16
REMARK 500 3 VAL C 24 -77.21 -99.27
REMARK 500 3 LYS C 28 44.82 -158.63
REMARK 500 3 ASN D 27 -46.80 -136.25
REMARK 500 3 LYS D 28 -85.93 54.05
REMARK 500 3 LYS E 28 -132.81 -132.13
REMARK 500 3 VAL G 24 33.54 -149.53
REMARK 500 3 SER G 26 -73.08 -172.64
REMARK 500 3 ASN G 27 -178.61 59.52
REMARK 500 3 LYS G 28 117.26 -168.86
REMARK 500 4 VAL A 24 -12.78 -48.31
REMARK 500 4 SER A 26 -141.37 -61.55
REMARK 500 4 LYS A 28 66.79 -157.60
REMARK 500 4 ASN B 27 55.99 -155.95
REMARK 500 4 SER C 26 90.47 -162.94
REMARK 500 4 LYS C 28 34.01 -172.28
REMARK 500 4 ASN D 27 102.98 -173.28
REMARK 500 4 VAL E 24 -73.94 -93.23
REMARK 500 4 SER F 26 173.14 174.68
REMARK 500 4 ASN F 27 155.53 56.65
REMARK 500 4 LYS F 28 84.83 -165.75
REMARK 500 4 SER G 26 100.24 48.92
REMARK 500 4 LYS G 28 157.00 -47.42
REMARK 500 5 VAL A 24 -30.95 -144.47
REMARK 500 5 SER A 26 -175.11 -63.53
REMARK 500
REMARK 500 THIS ENTRY HAS 138 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 18175 RELATED DB: BMRB
DBREF 2LNQ A 1 40 UNP P05067 A4_HUMAN 672 711
DBREF 2LNQ B 1 40 UNP P05067 A4_HUMAN 672 711
DBREF 2LNQ C 1 40 UNP P05067 A4_HUMAN 672 711
DBREF 2LNQ D 1 40 UNP P05067 A4_HUMAN 672 711
DBREF 2LNQ E 1 40 UNP P05067 A4_HUMAN 672 711
DBREF 2LNQ F 1 40 UNP P05067 A4_HUMAN 672 711
DBREF 2LNQ G 1 40 UNP P05067 A4_HUMAN 672 711
DBREF 2LNQ H 1 40 UNP P05067 A4_HUMAN 672 711
SEQADV 2LNQ ASN A 23 UNP P05067 ASP 694 VARIANT
SEQADV 2LNQ ASN B 23 UNP P05067 ASP 694 VARIANT
SEQADV 2LNQ ASN C 23 UNP P05067 ASP 694 VARIANT
SEQADV 2LNQ ASN D 23 UNP P05067 ASP 694 VARIANT
SEQADV 2LNQ ASN E 23 UNP P05067 ASP 694 VARIANT
SEQADV 2LNQ ASN F 23 UNP P05067 ASP 694 VARIANT
SEQADV 2LNQ ASN G 23 UNP P05067 ASP 694 VARIANT
SEQADV 2LNQ ASN H 23 UNP P05067 ASP 694 VARIANT
SEQRES 1 A 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 A 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER
SEQRES 3 A 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 A 40 VAL
SEQRES 1 B 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 B 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER
SEQRES 3 B 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 B 40 VAL
SEQRES 1 C 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 C 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER
SEQRES 3 C 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 C 40 VAL
SEQRES 1 D 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 D 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER
SEQRES 3 D 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 D 40 VAL
SEQRES 1 E 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 E 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER
SEQRES 3 E 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 E 40 VAL
SEQRES 1 F 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 F 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER
SEQRES 3 F 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 F 40 VAL
SEQRES 1 G 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 G 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER
SEQRES 3 G 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 G 40 VAL
SEQRES 1 H 40 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 H 40 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASN VAL GLY SER
SEQRES 3 H 40 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 H 40 VAL
SHEET 1 A 8 LYS A 16 ALA A 21 0
SHEET 2 A 8 LEU B 17 GLU B 22 -1 O GLU B 22 N LYS A 16
SHEET 3 A 8 LYS C 16 GLU C 22 -1 O LEU C 17 N ALA B 21
SHEET 4 A 8 LYS D 16 GLU D 22 -1 O LYS D 16 N GLU C 22
SHEET 5 A 8 LYS E 16 GLU E 22 -1 O LEU E 17 N ALA D 21
SHEET 6 A 8 LYS F 16 GLU F 22 -1 O LYS F 16 N GLU E 22
SHEET 7 A 8 LEU G 17 GLU G 22 -1 O PHE G 19 N PHE F 19
SHEET 8 A 8 LYS H 16 ALA H 21 -1 O VAL H 18 N PHE G 20
SHEET 1 B 8 ILE A 31 MET A 35 0
SHEET 2 B 8 ALA B 30 VAL B 36 -1 O ILE B 31 N MET A 35
SHEET 3 B 8 ALA C 30 VAL C 36 -1 O ILE C 32 N LEU B 34
SHEET 4 B 8 ALA D 30 MET D 35 -1 O MET D 35 N ILE C 31
SHEET 5 B 8 ILE E 31 VAL E 36 -1 O ILE E 32 N LEU D 34
SHEET 6 B 8 ILE F 31 MET F 35 -1 O MET F 35 N ILE E 31
SHEET 7 B 8 ILE G 31 VAL G 36 -1 O ILE G 32 N LEU F 34
SHEET 8 B 8 ALA H 30 MET H 35 -1 O ILE H 31 N MET G 35
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
