Header list of 1oei.pdb file
Complete list - 25 20 Bytes
HEADER PRION PROTEIN 27-MAR-03 1OEI
TITLE HUMAN PRION PROTEIN 61-84
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR PRION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 61-84;
COMPND 5 SYNONYM: PRP, PRION PROTEIN, PRP27-30, PRP33-35C;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRSET A
KEYWDS PRION PROTEIN, OCTAPEPTIDE REPEATS, NMR STRUCTURE, PROTEIN
KEYWDS 2 AGGREGATION, PH-DEPENDENT CONFORMATION, BRAIN, DISEASE
KEYWDS 3 MUTATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.ZAHN
REVDAT 2 24-FEB-09 1OEI 1 VERSN
REVDAT 1 06-MAY-04 1OEI 0
JRNL AUTH R.ZAHN
JRNL TITL THE OCTAPEPTIDE REPEATS IN MAMMALIAN PRION PROTEIN
JRNL TITL 2 CONSTITUTE A PH-DEPENDENT FOLDING AND AGGREGATION
JRNL TITL 3 SITE
JRNL REF J.MOL.BIOL. V. 334 477 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 14623188
JRNL DOI 10.1016/J.JMB.2003.09.048
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 1OEI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-MAR-03.
REMARK 100 THE PDBE ID CODE IS EBI-12471.
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 : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800
REMARK 210 SPECTROMETER MODEL : DRX800
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 : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 5
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED ON 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 PHYSIOLOGICAL FUNCTION OF PRP IS UNKNOWN
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 1 PRO A 76 -94.32 -67.01
REMARK 500 2 PRO A 68 -153.47 -75.97
REMARK 500 3 PRO A 68 -178.27 -68.89
REMARK 500 4 PRO A 76 -126.42 -77.31
REMARK 500 6 PRO A 76 78.96 -69.66
REMARK 500 7 PRO A 76 -71.04 -80.28
REMARK 500 10 PRO A 68 -168.97 -76.16
REMARK 500 11 GLN A 83 -58.00 -121.54
REMARK 500 12 PRO A 76 42.30 -77.87
REMARK 500 13 PRO A 76 -164.88 -75.77
REMARK 500 13 GLN A 83 -55.85 -128.49
REMARK 500 14 PRO A 68 83.65 -64.99
REMARK 500 16 PRO A 68 -75.30 -75.75
REMARK 500 17 GLN A 67 -71.00 -71.20
REMARK 500 17 PRO A 68 88.64 -62.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN A 75 PRO A 76 2 148.21
REMARK 500 HIS A 69 GLY A 70 8 -149.14
REMARK 500 HIS A 77 GLY A 78 20 -147.68
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 1 TRP A 73 0.06 SIDE CHAIN
REMARK 500 18 TRP A 65 0.06 SIDE CHAIN
REMARK 500 19 TRP A 65 0.06 SIDE CHAIN
REMARK 500 19 TRP A 73 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E1G RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT M166V
REMARK 900 RELATED ID: 1E1J RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT M166V
REMARK 900 RELATED ID: 1E1P RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT S170N
REMARK 900 RELATED ID: 1E1S RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT S170N
REMARK 900 RELATED ID: 1E1U RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT R220K
REMARK 900 RELATED ID: 1E1W RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT R220K
REMARK 900 RELATED ID: 1FKC RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN (MUTANT E200K) FRAGMENT 90-231
REMARK 900 RELATED ID: 1FO7 RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN (MUTANT E200K) FRAGMENT 90-231
REMARK 900 RELATED ID: 1H0L RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN 121-230 M166C/E221C
REMARK 900 RELATED ID: 1HJM RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN AT PH 7.0
REMARK 900 RELATED ID: 1HJN RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN AT PH 7.0
REMARK 900 RELATED ID: 1I4M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN PRION PROTEIN
REMARK 900 REVEALS A MECHANISM FOR OLIGOMERIZATION
REMARK 900 RELATED ID: 1OEH RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN 61-68
REMARK 900 RELATED ID: 1QLX RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN
REMARK 900 RELATED ID: 1QLZ RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN
REMARK 900 RELATED ID: 1QM0 RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN FRAGMENT 90-230
REMARK 900 RELATED ID: 1QM1 RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN FRAGMENT 90-230
REMARK 900 RELATED ID: 1QM2 RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN FRAGMENT 121-230
REMARK 900 RELATED ID: 1QM3 RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN FRAGMENT 121-230
DBREF 1OEI A 61 84 UNP P04156 PRIO_HUMAN 61 84
SEQRES 1 A 24 HIS GLY GLY GLY TRP GLY GLN PRO HIS GLY GLY GLY TRP
SEQRES 2 A 24 GLY GLN PRO HIS GLY GLY GLY TRP GLY GLN PRO
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 - 25 20 Bytes