Header list of 1dx0.pdb file
Complete list - 25 20 Bytes
HEADER PRION PROTEIN 15-DEC-99 1DX0
TITLE BOVINE PRION PROTEIN RESIDUES 23-230
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 23-230;
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 1DX0 1 VERSN
REVDAT 4 04-APR-05 1DX0 1 ATOM
REVDAT 3 27-FEB-04 1DX0 1 SSBOND ATOM CONECT
REVDAT 2 26-FEB-02 1DX0 1 TITLE JRNL REMARK
REVDAT 1 20-JUL-00 1DX0 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 1DX0 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-4472.
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 21
REMARK 465 SER A 22
REMARK 465 LYS A 23
REMARK 465 LYS A 24
REMARK 465 ARG A 25
REMARK 465 PRO A 26
REMARK 465 LYS A 27
REMARK 465 PRO A 28
REMARK 465 GLY A 281
REMARK 465 GLY A 29
REMARK 465 GLY A 30
REMARK 465 TRP A 31
REMARK 465 ASN A 32
REMARK 465 THR A 33
REMARK 465 GLY A 34
REMARK 465 GLY A 35
REMARK 465 SER A 36
REMARK 465 ARG A 37
REMARK 465 TYR A 38
REMARK 465 PRO A 39
REMARK 465 GLY A 40
REMARK 465 GLN A 41
REMARK 465 GLY A 42
REMARK 465 SER A 43
REMARK 465 PRO A 44
REMARK 465 GLY A 45
REMARK 465 GLY A 46
REMARK 465 ASN A 47
REMARK 465 ARG A 48
REMARK 465 TYR A 49
REMARK 465 PRO A 50
REMARK 465 PRO A 51
REMARK 465 GLN A 52
REMARK 465 GLY A 53
REMARK 465 GLY A 54
REMARK 465 GLY A 55
REMARK 465 GLY A 56
REMARK 465 TRP A 57
REMARK 465 GLY A 58
REMARK 465 GLN A 59
REMARK 465 PRO A 60
REMARK 465 HIS A 61
REMARK 465 GLY A 62
REMARK 465 GLY A 63
REMARK 465 GLY A 64
REMARK 465 TRP A 65
REMARK 465 GLY A 66
REMARK 465 GLN A 67
REMARK 465 PRO A 671
REMARK 465 HIS A 672
REMARK 465 GLY A 673
REMARK 465 GLY A 674
REMARK 465 GLY A 675
REMARK 465 TRP A 676
REMARK 465 GLY A 677
REMARK 465 GLN A 678
REMARK 465 PRO A 68
REMARK 465 HIS A 69
REMARK 465 GLY A 70
REMARK 465 GLY A 71
REMARK 465 GLY A 72
REMARK 465 TRP A 73
REMARK 465 GLY A 74
REMARK 465 GLN A 75
REMARK 465 PRO A 76
REMARK 465 HIS A 77
REMARK 465 GLY A 78
REMARK 465 GLY A 79
REMARK 465 GLY A 80
REMARK 465 TRP A 81
REMARK 465 GLY A 82
REMARK 465 GLN A 83
REMARK 465 PRO A 84
REMARK 465 HIS A 85
REMARK 465 GLY A 86
REMARK 465 GLY A 87
REMARK 465 GLY A 871
REMARK 465 GLY A 88
REMARK 465 TRP A 89
REMARK 465 GLY A 90
REMARK 465 GLN A 91
REMARK 465 GLY A 92
REMARK 465 GLY A 93
REMARK 465 THR A 95
REMARK 465 HIS A 96
REMARK 465 GLY A 97
REMARK 465 GLN A 98
REMARK 465 TRP A 99
REMARK 465 ASN A 100
REMARK 465 LYS A 101
REMARK 465 PRO A 102
REMARK 465 SER A 103
REMARK 465 LYS A 104
REMARK 465 PRO A 105
REMARK 465 LYS A 106
REMARK 465 THR A 107
REMARK 465 ASN A 108
REMARK 465 MET A 109
REMARK 465 LYS A 110
REMARK 465 HIS A 111
REMARK 465 VAL A 112
REMARK 465 ALA A 113
REMARK 465 GLY A 114
REMARK 465 ALA A 115
REMARK 465 ALA A 116
REMARK 465 ALA A 117
REMARK 465 ALA A 118
REMARK 465 GLY A 119
REMARK 465 ALA 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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HH TYR A 157 - OD1 ASP A 202 1.60
REMARK 500 O THR A 188 - HG1 THR A 192 1.59
REMARK 500
REMARK 500 REMARK: NULL
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 TYR A 128 CB - CG - CD1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 156 CD - NE - CZ ANGL. DEV. = 9.5 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 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 TYR A 128 -159.55 42.22
REMARK 500 GLN A 168 133.84 95.57
REMARK 500 GLN A 172 -75.58 -91.76
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 TYR A 128 0.10 SIDE CHAIN
REMARK 500 TYR A 149 0.09 SIDE CHAIN
REMARK 500 TYR A 157 0.10 SIDE CHAIN
REMARK 500 TYR A 162 0.07 SIDE CHAIN
REMARK 500 TYR A 225 0.09 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 RELATED ID: 1DWY RELATED DB: PDB
REMARK 900 BOVINE PRION PROTEIN FRAGMENT 121-230 NMR,REPRESENTATIVE
REMARK 900 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 21 CLONING ARTIFACT
REMARK 999 SER A 22 CLONING ARTIFACT
DBREF 1DX0 A 21 22 PDB 1DX0 1DX0 21 22
DBREF 1DX0 A 23 230 UNP P10279 PRIO_BOVIN 25 241
SEQRES 1 A 219 GLY SER LYS LYS ARG PRO LYS PRO GLY GLY GLY TRP ASN
SEQRES 2 A 219 THR GLY GLY SER ARG TYR PRO GLY GLN GLY SER PRO GLY
SEQRES 3 A 219 GLY ASN ARG TYR PRO PRO GLN GLY GLY GLY GLY TRP GLY
SEQRES 4 A 219 GLN PRO HIS GLY GLY GLY TRP GLY GLN PRO HIS GLY GLY
SEQRES 5 A 219 GLY TRP GLY GLN PRO HIS GLY GLY GLY TRP GLY GLN PRO
SEQRES 6 A 219 HIS GLY GLY GLY TRP GLY GLN PRO HIS GLY GLY GLY GLY
SEQRES 7 A 219 TRP GLY GLN GLY GLY THR HIS GLY GLN TRP ASN LYS PRO
SEQRES 8 A 219 SER LYS PRO LYS THR ASN MET LYS HIS VAL ALA GLY ALA
SEQRES 9 A 219 ALA ALA ALA GLY ALA VAL VAL GLY GLY LEU GLY GLY TYR
SEQRES 10 A 219 MET LEU GLY SER ALA MET SER ARG PRO LEU ILE HIS PHE
SEQRES 11 A 219 GLY SER ASP TYR GLU ASP ARG TYR TYR ARG GLU ASN MET
SEQRES 12 A 219 HIS ARG TYR PRO ASN GLN VAL TYR TYR ARG PRO VAL ASP
SEQRES 13 A 219 GLN TYR SER ASN GLN ASN ASN PHE VAL HIS ASP CYS VAL
SEQRES 14 A 219 ASN ILE THR VAL LYS GLU HIS THR VAL THR THR THR THR
SEQRES 15 A 219 LYS GLY GLU ASN PHE THR GLU THR ASP ILE LYS MET MET
SEQRES 16 A 219 GLU ARG VAL VAL GLU GLN MET CYS ILE THR GLN TYR GLN
SEQRES 17 A 219 ARG GLU SER 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 2.05
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