Header list of 1z0q.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 02-MAR-05 1Z0Q
TITLE AQUEOUS SOLUTION STRUCTURE OF THE ALZHEIMER'S DISEASE ABETA PEPTIDE
TITLE 2 (1-42)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALZHEIMER'S DISEASE AMYLOID;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BETA-PEPTIDE;
COMPND 5 SYNONYM: AMYLOID BETA A4 PROTEIN, BETA-APP, BETA-AMYLOID PROTEIN,
COMPND 6 BETA-APP42;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS PREPARED BY SOLID-PHASE SYNTHESIS.
SOURCE 4 THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS
SOURCE 5 (HUMAN).
KEYWDS AMYLOID BETA PEPTIDE, HELIX-KINK-HELIX, ALZHEIMER'S DISEASE, 30
KEYWDS 2 STRUCTURES, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR S.TOMASELLI,V.ESPOSITO,P.VANGONE,N.A.VAN NULAND,A.M.BONVIN,
AUTHOR 2 R.GUERRINI,T.TANCREDI,P.A.TEMUSSI,D.PICONE
REVDAT 3 02-MAR-22 1Z0Q 1 REMARK
REVDAT 2 24-FEB-09 1Z0Q 1 VERSN
REVDAT 1 23-MAY-06 1Z0Q 0
JRNL AUTH S.TOMASELLI,V.ESPOSITO,P.VANGONE,N.A.VAN NULAND,A.M.BONVIN,
JRNL AUTH 2 R.GUERRINI,T.TANCREDI,P.A.TEMUSSI,D.PICONE
JRNL TITL THE ALPHA-TO-BETA CONFORMATIONAL TRANSITION OF ALZHEIMER'S
JRNL TITL 2 ABETA-(1-42) PEPTIDE IN AQUEOUS MEDIA IS REVERSIBLE: A STEP
JRNL TITL 3 BY STEP CONFORMATIONAL ANALYSIS SUGGESTS THE LOCATION OF
JRNL TITL 4 BETA CONFORMATION SEEDING
JRNL REF CHEMBIOCHEM V. 7 257 2006
JRNL REFN ISSN 1439-4227
JRNL PMID 16444756
JRNL DOI 10.1002/CBIC.200500223
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : GUNTERT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Z0Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032151.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM BETA PEPTIDE (TFA
REMARK 210 PRETREATED); 70% H2O, 30%
REMARK 210 HEXAFLUOROISOPROPANOL-D2
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ; 500 MHZ; 600 MHZ; 750
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.5, XWINNMR 3.0,
REMARK 210 NMRVIEW 5.0.4, DYANA 1.5
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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 : 25
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 HIS A 13 H LYS A 16 1.12
REMARK 500 O LEU A 17 H PHE A 20 1.24
REMARK 500 O VAL A 18 H GLU A 22 1.37
REMARK 500 O TYR A 10 H HIS A 14 1.41
REMARK 500 O ASP A 7 H GLU A 11 1.55
REMARK 500 O LYS A 28 H ILE A 31 1.58
REMARK 500 O HIS A 13 N LYS A 16 2.07
REMARK 500 O LEU A 17 N PHE A 20 2.19
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 ALA A 2 -138.39 -133.84
REMARK 500 1 GLU A 3 -45.45 -131.18
REMARK 500 1 HIS A 6 -71.73 -102.11
REMARK 500 1 ASP A 7 -28.26 -37.04
REMARK 500 1 TYR A 10 -44.59 -138.35
REMARK 500 1 GLU A 11 -73.33 -45.93
REMARK 500 1 HIS A 13 -72.17 -79.73
REMARK 500 1 HIS A 14 -58.02 -18.98
REMARK 500 1 GLN A 15 -17.41 -42.05
REMARK 500 1 LYS A 16 -49.11 -26.41
REMARK 500 1 PHE A 20 -68.11 -98.10
REMARK 500 1 ASN A 27 -58.05 -159.36
REMARK 500 1 LEU A 34 -31.87 -37.39
REMARK 500 1 VAL A 36 -14.95 65.69
REMARK 500 1 VAL A 40 -173.87 47.46
REMARK 500 1 ILE A 41 164.50 -42.98
REMARK 500 2 ALA A 2 117.41 78.79
REMARK 500 2 PHE A 4 -31.46 70.61
REMARK 500 2 HIS A 6 -74.66 -77.95
REMARK 500 2 TYR A 10 -61.67 -97.52
REMARK 500 2 HIS A 14 -52.60 -22.43
REMARK 500 2 GLN A 15 -19.12 -44.48
REMARK 500 2 LYS A 16 -48.95 -29.10
REMARK 500 2 LEU A 17 -18.79 -141.41
REMARK 500 2 PHE A 19 -16.34 -46.16
REMARK 500 2 PHE A 20 -70.48 -99.79
REMARK 500 2 VAL A 24 -65.53 -100.78
REMARK 500 2 SER A 26 -96.88 -88.13
REMARK 500 2 ASN A 27 -84.13 172.87
REMARK 500 2 LYS A 28 -78.22 -146.08
REMARK 500 2 ALA A 30 -7.39 -58.81
REMARK 500 2 ILE A 32 -90.96 -135.05
REMARK 500 2 VAL A 36 -13.52 66.24
REMARK 500 2 VAL A 39 -25.52 79.63
REMARK 500 2 VAL A 40 102.43 -32.90
REMARK 500 2 ILE A 41 162.44 -44.65
REMARK 500 3 ALA A 2 -138.55 -128.69
REMARK 500 3 GLU A 3 -50.16 80.62
REMARK 500 3 HIS A 6 -94.11 -63.62
REMARK 500 3 TYR A 10 -60.84 -98.19
REMARK 500 3 HIS A 13 -72.02 -85.64
REMARK 500 3 HIS A 14 -58.24 -23.50
REMARK 500 3 GLN A 15 -9.04 -48.46
REMARK 500 3 LYS A 16 -36.42 -29.96
REMARK 500 3 LEU A 17 -15.07 -154.30
REMARK 500 3 PHE A 19 -16.99 -48.72
REMARK 500 3 PHE A 20 -65.45 -94.70
REMARK 500 3 ASN A 27 -72.43 -173.59
REMARK 500 3 ALA A 30 11.50 89.26
REMARK 500 3 ILE A 32 -52.05 80.83
REMARK 500
REMARK 500 THIS ENTRY HAS 421 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1Z0Q A 1 42 UNP P05067 A4_HUMAN 672 713
SEQRES 1 A 42 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 A 42 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER
SEQRES 3 A 42 ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL
SEQRES 4 A 42 VAL ILE ALA
HELIX 1 1 TYR A 10 GLU A 22 1 13
HELIX 2 2 LYS A 28 ILE A 32 5 5
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 - r 2 2 Bytes