Header list of 1dwy.pdb file
Complete list - 25 20 Bytes
HEADER PRION PROTEIN 15-DEC-99 1DWY
TITLE BOVINE PRION PROTEIN FRAGMENT 121-230
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 121-230;
COMPND 5 SYNONYM: PRP, MAJOR PRION PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 CELLULAR_LOCATION: EXTRACELLULAR;
SOURCE 7 GENE: PRNP;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PRSET A
KEYWDS PRION PROTEIN, PRION, BRAIN, REPEAT
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR F.LOPEZ-GARCIA,R.ZAHN,R.RIEK,M.BILLETER,K.WUTHRICH
REVDAT 5 24-FEB-09 1DWY 1 VERSN
REVDAT 4 04-APR-05 1DWY 1 ATOM
REVDAT 3 27-FEB-04 1DWY 1 SSBOND ATOM CONECT
REVDAT 2 26-FEB-02 1DWY 1 JRNL REMARK
REVDAT 1 20-JUL-00 1DWY 0
JRNL AUTH F.LOPEZ-GARCIA,R.ZAHN,R.RIEK,K.WUTHRICH
JRNL TITL NMR STRUCTURE OF THE BOVINE PRION PROTEIN
JRNL REF PROC.NATL.ACAD.SCI.USA V. 97 8334 2000
JRNL REFN ISSN 0027-8424
JRNL PMID 10899999
JRNL DOI 10.1073/PNAS.97.15.8334
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPALP
REMARK 3 AUTHORS : KORADI, BILLETER,GUNTERT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DWY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-DEC-99.
REMARK 100 THE PDBE ID CODE IS EBI-4446.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : 0.01
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750
REMARK 210 SPECTROMETER MODEL : DRX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: CLOSEST TO THE MEAN
REMARK 210 (BACKBONE HEAVY ATOMS OF RESIDUES 125-227). THE STRUCTURE
REMARK 210 WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON
REMARK 210 13C, 15N-LABELED PROTEIN
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 400
REMARK 400 COMPOUND
REMARK 400 THE PDB ENTRIES 1DWY, 1DWZ, 1DX0 AND 1DX1 FORM
REMARK 400 A SET OF STRUCTURE DETERMINATIONS AS:
REMARK 400 1DWY THE MINIMIZED CONFORMER CLOSEST TO THE MEAN
REMARK 400 OF THE FRAGMENT BPRP(121-230) (ONLY SUBMITTED
REMARK 400 RESIDUES 124-227)
REMARK 400 1DWZ 20 MINIMIZED CONFORMERS OF THE FRAGMENT BPRP(121-230)
REMARK 400 (ONLY SUBMITTED RESIDUES 124-227)
REMARK 400 1DX0 THE MINIMIZED CONFORMER CLOSEST TO THE MEAN OF
REMARK 400 THE FULL LENGTH BPRP(23-230) (ONLY SUBMITTED RESIDUES
REMARK 400 124-227)
REMARK 400 1DX1 20 MINIMIZED CONFORMERS OF THE FULL LENGTH BPRP(23-230)
REMARK 400 (ONLY SUBMITTED RESIDUES 124-227)
REMARK 400
REMARK 400 THE SEQUENCE NUMBERING GIVEN IN THESE ENTRIES IS THAT
REMARK 400 FOR HUMAN PRION PROTEIN (RATHER THAN SEQUENTIAL) BASED
REMARK 400 ON SEQUENCE ALIGNMENT.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 119
REMARK 465 SER A 120
REMARK 465 VAL A 121
REMARK 465 VAL A 122
REMARK 465 GLY A 123
REMARK 465 ARG A 228
REMARK 465 GLY A 229
REMARK 465 ALA A 230
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 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 GLN A 168 -20.26 71.41
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 ARG A 151 0.10 SIDE CHAIN
REMARK 500 TYR A 163 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DWZ RELATED DB: PDB
REMARK 900 BOVINE PRION PROTEIN FRAGMENT 121-230 NMR, 20 STRUCTURES
REMARK 900 MINIMIZED STRUCTURE
REMARK 900 RELATED ID: 1DX0 RELATED DB: PDB
REMARK 900 BOVINE PRION PROTEIN NMR, REPRESENTATIVE MINIMIZED STRUCTURE
REMARK 900 RELATED ID: 1DX1 RELATED DB: PDB
REMARK 900 BOVINE PRION PROTEIN NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 1AG2 RELATED DB: PDB
REMARK 900 PRION PROTEIN DOMAIN PRP(121-231) FROM MOUSE, NMR,
REMARK 900 MINIMIZED AVERAGE STRUCTURE
REMARK 900 RELATED ID: 1B10 RELATED DB: PDB
REMARK 900 SOLUTION NMR STRUCTURE OF RECOMBINANT SYRIAN HAMSTER PRION
REMARK 900 PROTEIN RPRP(90-231), 25 STRUCTURES
REMARK 900 RELATED ID: 1QLX RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN RESIDUES 23-230 NMR,
REMARK 900 REPRESENTATIVE STRUCTURE
REMARK 900 RELATED ID: 1QM0 RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN FRAGMENT 90-230 NMR,
REMARK 900 REPRESENTATIVE STRUCTURE
REMARK 900 RELATED ID: 1QM1 RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN FRAGMENT 90-230 NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 1QM2 RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN FRAGMENT 121-230 NMR,
REMARK 900 REPRESENTATIVE STRUCTURE
REMARK 900 RELATED ID: 1QM3 RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN FRAGMENT 121-230 NMR, 20 STRUCTURES
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES (GLY SER) INSERTED AT THE N-TERMINUS
REMARK 999 GLY A 119 CLONING ARTIFACT
REMARK 999 SER A 120 CLONING ARTIFACT
DBREF 1DWY A 119 120 PDB 1DWY 1DWY 119 120
DBREF 1DWY A 121 230 UNP P10279 PRIO_BOVIN 132 241
SEQRES 1 A 112 GLY SER VAL VAL GLY GLY LEU GLY GLY TYR MET LEU GLY
SEQRES 2 A 112 SER ALA MET SER ARG PRO LEU ILE HIS PHE GLY SER ASP
SEQRES 3 A 112 TYR GLU ASP ARG TYR TYR ARG GLU ASN MET HIS ARG TYR
SEQRES 4 A 112 PRO ASN GLN VAL TYR TYR ARG PRO VAL ASP GLN TYR SER
SEQRES 5 A 112 ASN GLN ASN ASN PHE VAL HIS ASP CYS VAL ASN ILE THR
SEQRES 6 A 112 VAL LYS GLU HIS THR VAL THR THR THR THR LYS GLY GLU
SEQRES 7 A 112 ASN PHE THR GLU THR ASP ILE LYS MET MET GLU ARG VAL
SEQRES 8 A 112 VAL GLU GLN MET CYS ILE THR GLN TYR GLN ARG GLU SER
SEQRES 9 A 112 GLN ALA TYR TYR GLN ARG GLY ALA
HELIX 1 H1 ASP A 144 GLU A 152 1 9
HELIX 2 H2 ASN A 173 THR A 192 1 20
HELIX 3 H3 GLU A 200 TYR A 225 1 26
SHEET 1 A 2 TYR A 128 GLY A 131 0
SHEET 2 A 2 VAL A 161 ARG A 164 -1 O TYR A 163 N MET A 129
SSBOND 1 CYS A 179 CYS A 214 1555 1555 2.01
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 - 25 20 Bytes