Header list of 1qwp.pdb file
Complete list - 2 20 Bytes
HEADER PROTEIN BINDING 03-SEP-03 1QWP
TITLE NMR ANALYSIS OF 25-35 FRAGMENT OF BETA AMYLOID PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 11-MER PEPTIDE FROM AMYLOID BETA A4 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.
KEYWDS AMYLOID BETA PEPTIDE- KINK STRUCTURE, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.M.D'URSI,M.R.ARMENANTE,R.GUERRINI,S.SALVADORI,G.SORRENTINO,D.PICONE
REVDAT 3 02-MAR-22 1QWP 1 REMARK
REVDAT 2 24-FEB-09 1QWP 1 VERSN
REVDAT 1 14-SEP-04 1QWP 0
JRNL AUTH A.M.D'URSI,M.R.ARMENANTE,R.GUERRINI,S.SALVADORI,
JRNL AUTH 2 G.SORRENTINO,D.PICONE
JRNL TITL SOLUTION STRUCTURE OF AMYLOID BETA-PEPTIDE (25-35) IN
JRNL TITL 2 DIFFERENT MEDIA
JRNL REF J.MED.CHEM. V. 47 4231 2004
JRNL REFN ISSN 0022-2623
JRNL PMID 15293994
JRNL DOI 10.1021/JM040773O
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QWP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-SEP-03.
REMARK 100 THE DEPOSITION ID IS D_1000020159.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM ABETA(25-35) PEPTIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 1.3, SPARKY 1.2, DYANA
REMARK 210 1.5
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM
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 ALA A 30 H GLY A 33 1.59
REMARK 500 O ILE A 31 H LEU A 34 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 SER A 26 39.94 -89.01
REMARK 500 1 LEU A 34 46.04 178.21
REMARK 500 2 LEU A 34 45.50 179.98
REMARK 500 3 SER A 26 -151.64 -74.48
REMARK 500 3 LEU A 34 48.25 179.69
REMARK 500 4 SER A 26 -151.11 -73.80
REMARK 500 4 LEU A 34 48.58 179.42
REMARK 500 5 SER A 26 -151.16 -74.93
REMARK 500 5 LEU A 34 44.23 -161.83
REMARK 500 6 LEU A 34 44.19 -161.82
REMARK 500 7 SER A 26 -151.71 -75.57
REMARK 500 7 ASN A 27 49.35 175.28
REMARK 500 7 LEU A 34 44.05 -161.96
REMARK 500 8 SER A 26 -150.76 -71.81
REMARK 500 8 LEU A 34 44.34 -163.03
REMARK 500 9 SER A 26 -151.41 -74.39
REMARK 500 9 LEU A 34 43.97 -160.45
REMARK 500 10 SER A 26 -150.87 -71.71
REMARK 500 10 LEU A 34 44.10 -162.48
REMARK 500 11 ASN A 27 -25.33 156.15
REMARK 500 11 LEU A 34 44.32 -162.97
REMARK 500 12 SER A 26 -151.92 -76.12
REMARK 500 12 LEU A 34 44.89 -157.46
REMARK 500 13 ASN A 27 -25.27 156.05
REMARK 500 13 LEU A 34 44.01 -161.41
REMARK 500 14 SER A 26 -151.43 -75.61
REMARK 500 14 LEU A 34 44.11 -163.34
REMARK 500 15 SER A 26 -152.00 -76.46
REMARK 500 15 ASN A 27 47.96 -144.76
REMARK 500 15 LEU A 34 44.72 -158.44
REMARK 500 16 SER A 26 -151.48 -75.27
REMARK 500 16 LEU A 34 44.53 -156.34
REMARK 500 17 SER A 26 40.39 -88.99
REMARK 500 17 LEU A 34 44.17 -162.02
REMARK 500 18 SER A 26 40.45 -88.88
REMARK 500 18 LEU A 34 44.19 -161.92
REMARK 500 19 ASN A 27 60.64 -116.02
REMARK 500 19 LEU A 34 44.30 -162.40
REMARK 500 20 SER A 26 98.04 -46.59
REMARK 500 20 LEU A 34 44.17 -162.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IYT RELATED DB: PDB
REMARK 900 THE PARENT PEPTIDE BETA AMYLOID 1-42
DBREF 1QWP A 25 35 UNP P05067 A4_HUMAN 696 706
SEQRES 1 A 11 GLY SER ASN LYS GLY ALA ILE ILE GLY LEU MET
HELIX 1 1 ASN A 27 ILE A 32 1 6
HELIX 2 2 GLY A 33 MET A 35 5 3
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 - 2 20 Bytes