Header list of 1amb.pdb file
Complete list - 16 202 Bytes
HEADER PROTEINASE INHIBITOR(TRYPSIN) 21-OCT-94 1AMB
TITLE SOLUTION STRUCTURE OF RESIDUES 1-28 OF THE AMYLOID BETA-PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMYLOID BETA-PEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS PROTEINASE INHIBITOR(TRYPSIN)
EXPDTA SOLUTION NMR
AUTHOR J.TALAFOUS,K.J.MARCINOWSKI,G.KLOPMAN,M.G.ZAGORSKI
REVDAT 3 16-FEB-22 1AMB 1 REMARK
REVDAT 2 24-FEB-09 1AMB 1 VERSN
REVDAT 1 20-DEC-94 1AMB 0
JRNL AUTH J.TALAFOUS,K.J.MARCINOWSKI,G.KLOPMAN,M.G.ZAGORSKI
JRNL TITL SOLUTION STRUCTURE OF RESIDUES 1-28 OF THE AMYLOID
JRNL TITL 2 BETA-PEPTIDE.
JRNL REF BIOCHEMISTRY V. 33 7788 1994
JRNL REFN ISSN 0006-2960
JRNL PMID 7516706
JRNL DOI 10.1021/BI00191A006
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.G.ZAGORSKI,C.J.BARROW
REMARK 1 TITL NMR STUDIES OF AMYLOID BETA-PEPTIDES: PROTON ASSIGNMENTS
REMARK 1 TITL 2 SECONDARY STRUCTURE, AND MECHANISM OF AN ALPHA-HELIX TO
REMARK 1 TITL 3 BETA-SHEET CONVERSION FOR A HOMOLOGOUS, 28-RESIDUE
REMARK 1 TITL 4 N-TERMINAL FRAGMENT
REMARK 1 REF BIOCHEMISTRY V. 31 5621 1992
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.J.BARROW,M.G.ZAGORSKI
REMARK 1 TITL SOLUTION STRUCTURES OF BETA-PEPTIDE AND ITS CONSTITUENT
REMARK 1 TITL 2 FRAGMENTS: RELATION TO AMYLOID DEPOSITION
REMARK 1 REF SCIENCE V. 253 179 1991
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.0
REMARK 3 AUTHORS : BRUNGER (X-PLOR),
REMARK 3 NILGES,GRONENBORN,BRUNGER,CLORE,KUSZEWSKI
REMARK 3 (GENERATE,DGSA,ACCEPT,AVERAGE,AND REFINE PROTOCOLS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AMB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170993.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
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 : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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: 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 HIS A 6 -70.06 -76.41
REMARK 500 ASN A 27 51.47 -108.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AMC RELATED DB: PDB
DBREF 1AMB A 1 28 UNP P05067 A4_HUMAN 672 699
SEQRES 1 A 28 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS
SEQRES 2 A 28 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER
SEQRES 3 A 28 ASN LYS
HELIX 1 H1 PHE A 4 GLY A 25 1MOST DEFINED HELICAL REGION 22
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
Complete list - 16 202 Bytes