Header list of 1ze9.pdb file
Complete list - 12 20 Bytes
HEADER METAL BINDING PROTEIN 18-APR-05 1ZE9
TITLE ZINC-BINDING DOMAIN OF ALZHEIMER'S DISEASE AMYLOID BETA-PEPTIDE
TITLE 2 COMPLEXED WITH A ZINC (II) CATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 16-MER FROM ALZHEIMER'S DISEASE AMYLOID PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALZHEIMER'S DISEASE AMYLOID A4 PROTEIN, AMYLOID BETA A4
COMPND 5 PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.
KEYWDS PEPTIDE-ZINC COMPLEX, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.ZIRAH,S.A.KOZIN,A.K.MAZUR,A.BLOND,M.CHEMINANT,I.SEGALAS-MILAZZO,
AUTHOR 2 P.DEBEY,S.REBUFFAT
REVDAT 3 09-OCT-13 1ZE9 1 JRNL VERSN
REVDAT 2 24-FEB-09 1ZE9 1 VERSN
REVDAT 1 03-MAY-05 1ZE9 0
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 DISEASE
JRNL TITL 2 AMYLOID BETA-PEPTIDE UPON ZINC BINDING AND 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 2.7
REMARK 3 AUTHORS : ALEXEY K.MAZUR
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 305 RESTRAINTS, 282 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 6
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, AND 17 ZINC TETRAHEDRAL COORDINATION
REMARK 3 CONSTRAINTS.
REMARK 4
REMARK 4 1ZE9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-APR-05.
REMARK 100 THE RCSB ID CODE IS RCSB032622.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 278
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 0.1
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.8MM IN 50MM SODIUM PHOSPHATE
REMARK 210 BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY;
REMARK 210 HSQC; HMBC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.1, AURELIA 1.6, ICMD
REMARK 210 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 : 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 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 2 SER A 8 41.58 -85.94
REMARK 500 3 ALA A 2 -163.04 -100.03
REMARK 500 3 GLU A 11 -166.57 -129.49
REMARK 500 4 PHE A 4 47.12 -95.52
REMARK 500 5 PHE A 4 43.41 -142.33
REMARK 500 6 PHE A 4 50.06 -144.32
REMARK 500 6 SER A 8 42.90 -84.36
REMARK 500 8 SER A 8 34.70 -85.62
REMARK 500 12 SER A 8 31.82 -87.39
REMARK 500 14 PHE A 4 49.97 -85.81
REMARK 500 15 PHE A 4 39.00 -145.93
REMARK 500 15 SER A 8 32.05 -85.42
REMARK 500 16 PHE A 4 41.66 -148.90
REMARK 500 16 HIS A 6 58.61 -119.52
REMARK 500 16 SER A 8 39.67 -85.01
REMARK 500 17 SER A 8 30.82 -85.90
REMARK 500 18 SER A 8 36.47 -83.09
REMARK 500 19 HIS A 6 46.56 -97.05
REMARK 500 19 SER A 8 30.07 -87.52
REMARK 500 20 PHE A 4 81.37 -155.00
REMARK 500 20 SER A 8 37.05 -88.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 19 ARG A 5 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 ZN A 18 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 6 ND1
REMARK 620 2 GLU A 11 OE1 123.0
REMARK 620 3 GLU A 11 OE2 88.3 63.8
REMARK 620 4 HIS A 13 NE2 120.7 103.6 81.0
REMARK 620 5 HIS A 14 ND1 103.8 88.2 151.5 112.8
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 18
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BP4 RELATED DB: PDB
REMARK 900 THE SAME PEPTIDE IN TFE/WATER 80/20 SOLUTION
REMARK 900 RELATED ID: 1ZE7 RELATED DB: PDB
REMARK 900 THE SAME PEPTIDE IN WATER SOLUTION AT PH 6.5
DBREF 1ZE9 A 1 16 UNP P05067 A4_HUMAN 672 687
SEQADV 1ZE9 ACE A 0 UNP P05067 ACETYLATION
SEQADV 1ZE9 NH2 A 17 UNP P05067 AMIDATION
SEQRES 1 A 18 ACE ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL
SEQRES 2 A 18 HIS HIS GLN LYS NH2
HET ACE A 0 6
HET NH2 A 17 3
HET ZN A 18 1
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
HETNAM ZN ZINC ION
FORMUL 1 ACE C2 H4 O
FORMUL 1 NH2 H2 N
FORMUL 2 ZN ZN 2+
HELIX 1 1 GLU A 11 GLN A 15 5 5
LINK ZN ZN A 18 ND1 HIS A 6 1555 1555 2.11
LINK ZN ZN A 18 OE1 GLU A 11 1555 1555 2.11
LINK ZN ZN A 18 OE2 GLU A 11 1555 1555 2.11
LINK ZN ZN A 18 NE2 HIS A 13 1555 1555 2.15
LINK ZN ZN A 18 ND1 HIS A 14 1555 1555 2.29
LINK C ACE A 0 N ASP A 1 1555 1555 1.33
LINK C LYS A 16 N NH2 A 17 1555 1555 1.33
SITE 1 AC1 4 HIS A 6 GLU A 11 HIS A 13 HIS A 14
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 - 12 20 Bytes