Header list of 1i17.pdb file
Complete list - b 23 2 Bytes
HEADER UNKNOWN FUNCTION 31-JAN-01 1I17
TITLE NMR STRUCTURE OF MOUSE DOPPEL 51-157
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRION-LIKE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GLOBULAR DOMAIN (RESIDUES 51-157);
COMPND 5 SYNONYM: MOUSE DOPPEL;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21A(+)
KEYWDS MOUSE DOPPEL, DOPPEL, DPL, PRION, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.MO,R.C.MOORE,F.E.COHEN,D.WESTAWAY,S.B.PRUSINER,P.E.WRIGHT,H.J.DYSON
REVDAT 3 23-FEB-22 1I17 1 REMARK
REVDAT 2 24-FEB-09 1I17 1 VERSN
REVDAT 1 07-MAR-01 1I17 0
JRNL AUTH H.MO,R.C.MOORE,F.E.COHEN,D.WESTAWAY,S.B.PRUSINER,P.E.WRIGHT,
JRNL AUTH 2 H.J.DYSON
JRNL TITL TWO DIFFERENT NEURODEGENERATIVE DISEASES CAUSED BY PROTEINS
JRNL TITL 2 WITH SIMILAR STRUCTURES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 98 2352 2001
JRNL REFN ISSN 0027-8424
JRNL PMID 11226243
JRNL DOI 10.1073/PNAS.051627998
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.C.MOORE,I.Y.LEE,G.L.SILVERMAN,P.M.HARRISON,R.STROME,
REMARK 1 AUTH 2 C.HEINRICH,A.KARUNARATNE,S.H.PASTERNAK,M.A.CHISHTI,Y.LIANG,
REMARK 1 AUTH 3 P.MASTRANGELO,K.WANG,A.F.SMIT,S.KATAMINE,G.A.CARLSON,
REMARK 1 AUTH 4 F.E.COHEN,S.B.PRUSINER,D.W.MELTON,P.TREMBLAY,L.E.HOOD,
REMARK 1 AUTH 5 D.WESTAWAY
REMARK 1 TITL ATAXIA IN PRION PROTEIN (PRP)-DEFICIENT MICE IS ASSOCIATED
REMARK 1 TITL 2 WITH UPREGULATION OF THE NOVEL PRP-LIKE PROTEIN DOPPEL
REMARK 1 REF J.MOL.BIOL. V. 292 797 1999
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1999.3108
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, AMBER 7
REMARK 3 AUTHORS : GUENTERT (DYANA), CASE (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BASED ON 1311 DISTANCE RESTRAINTS
REMARK 4
REMARK 4 1I17 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-FEB-01.
REMARK 100 THE DEPOSITION ID IS D_1000012777.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 299
REMARK 210 PH : 5.2
REMARK 210 IONIC STRENGTH : 0.02M
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 4MM 15N OR 2MM 15N/13C PROTEIN
REMARK 210 20MM D3-NAOAC, PH5.2
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY MOLECULAR
REMARK 210 DYNAMICS SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 16
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 ARG A 104 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 3 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 4 ARG A 1 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 4 ARG A 73 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 5 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 7 ARG A 1 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 8 ARG A 1 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 8 ARG A 83 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 9 ARG A 1 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 10 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 10 ARG A 73 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 12 ARG A 1 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 13 ARG A 83 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 14 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 14 ARG A 83 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 15 ARG A 73 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 16 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 18 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 19 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 20 ARG A 1 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
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 3 37.30 -75.33
REMARK 500 1 SER A 46 -58.71 -141.70
REMARK 500 1 ASP A 77 -45.33 -130.32
REMARK 500 2 SER A 46 -58.72 -137.84
REMARK 500 2 GLU A 74 47.23 -79.92
REMARK 500 2 LYS A 75 -33.55 -147.29
REMARK 500 2 LYS A 79 -59.59 -124.57
REMARK 500 3 VAL A 2 -82.40 -91.65
REMARK 500 3 ALA A 3 -159.70 -153.92
REMARK 500 3 SER A 46 -57.27 -131.83
REMARK 500 3 GLU A 74 46.80 -79.84
REMARK 500 3 LYS A 75 -61.46 -155.31
REMARK 500 3 LYS A 96 49.80 -72.99
REMARK 500 4 CYS A 45 109.23 -55.54
REMARK 500 4 SER A 46 -56.25 -125.81
REMARK 500 4 ASP A 77 -39.91 -136.72
REMARK 500 5 SER A 46 -58.40 -139.31
REMARK 500 6 ASP A 77 -37.21 -138.10
REMARK 500 7 SER A 46 -61.09 -144.68
REMARK 500 7 ASP A 77 -40.22 -135.10
REMARK 500 8 SER A 46 -50.81 -145.91
REMARK 500 8 LYS A 75 -53.68 -142.37
REMARK 500 8 SER A 78 37.17 -143.84
REMARK 500 9 SER A 46 -58.61 -139.06
REMARK 500 9 LEU A 102 -162.77 -124.18
REMARK 500 9 ALA A 106 92.64 -67.18
REMARK 500 10 SER A 46 -51.40 -148.02
REMARK 500 10 TRP A 101 84.31 -67.32
REMARK 500 11 LYS A 12 73.52 -101.77
REMARK 500 11 SER A 46 -61.90 -132.26
REMARK 500 11 ASP A 77 -40.92 -132.93
REMARK 500 11 LYS A 79 -67.69 -120.73
REMARK 500 12 SER A 46 -52.52 -146.55
REMARK 500 12 ASP A 77 -35.04 -135.49
REMARK 500 12 GLU A 103 -74.21 -139.49
REMARK 500 13 LYS A 16 105.77 -46.26
REMARK 500 13 SER A 46 -59.32 -136.87
REMARK 500 13 GLU A 74 43.67 -74.49
REMARK 500 13 LYS A 75 -62.47 -155.31
REMARK 500 13 ARG A 104 -59.31 -141.90
REMARK 500 14 SER A 46 -60.19 -140.76
REMARK 500 14 ASP A 77 -36.78 -136.72
REMARK 500 15 SER A 46 -47.23 -147.30
REMARK 500 15 ASP A 77 -40.31 -135.76
REMARK 500 16 SER A 46 -59.47 -139.94
REMARK 500 16 LYS A 79 -77.76 -121.33
REMARK 500 17 SER A 46 -52.61 -145.52
REMARK 500 17 ASP A 77 -44.27 -135.25
REMARK 500 17 LYS A 79 -76.38 -120.40
REMARK 500 17 GLU A 103 -65.48 -140.09
REMARK 500
REMARK 500 THIS ENTRY HAS 57 RAMACHANDRAN OUTLIERS.
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 3 TYR A 41 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1I17 A 1 107 UNP Q9QUG3 PRND_MOUSE 51 157
SEQRES 1 A 107 ARG VAL ALA GLU ASN ARG PRO GLY ALA PHE ILE LYS GLN
SEQRES 2 A 107 GLY ARG LYS LEU ASP ILE ASP PHE GLY ALA GLU GLY ASN
SEQRES 3 A 107 ARG TYR TYR ALA ALA ASN TYR TRP GLN PHE PRO ASP GLY
SEQRES 4 A 107 ILE TYR TYR GLU GLY CYS SER GLU ALA ASN VAL THR LYS
SEQRES 5 A 107 GLU MET LEU VAL THR SER CYS VAL ASN ALA THR GLN ALA
SEQRES 6 A 107 ALA ASN GLN ALA GLU PHE SER ARG GLU LYS GLN ASP SER
SEQRES 7 A 107 LYS LEU HIS GLN ARG VAL LEU TRP ARG LEU ILE LYS GLU
SEQRES 8 A 107 ILE CYS SER ALA LYS HIS CYS ASP PHE TRP LEU GLU ARG
SEQRES 9 A 107 GLY ALA ALA
HELIX 1 1 GLY A 22 TYR A 33 1 12
HELIX 2 2 TRP A 34 PHE A 36 5 3
HELIX 3 3 THR A 51 ASN A 67 1 17
HELIX 4 4 ASN A 67 GLN A 76 1 10
HELIX 5 5 SER A 78 LYS A 96 1 19
SHEET 1 A 2 ALA A 9 ILE A 11 0
SHEET 2 A 2 GLY A 39 TYR A 41 -1 O GLY A 39 N ILE A 11
SSBOND 1 CYS A 45 CYS A 98 1555 1555 2.04
SSBOND 2 CYS A 59 CYS A 93 1555 1555 2.04
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 - b 23 2 Bytes