Header list of 1lg4.pdb file
Complete list - b 23 2 Bytes
HEADER PRION PROTEIN 15-APR-02 1LG4
TITLE NMR STRUCTURE OF THE HUMAN DOPPEL PROTEIN FRAGMENT 24-152
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRION-LIKE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HDPL(24-152);
COMPND 5 SYNONYM: DOPPEL PROTEIN;
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 GENE: PRND;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21/DE3;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRSETA
KEYWDS PRION, DOPPEL, SCRAPIE, PRION PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.LUHRS,R.RIEK,P.GUNTERT,K.WUTHRICH
REVDAT 3 23-FEB-22 1LG4 1 REMARK
REVDAT 2 24-FEB-09 1LG4 1 VERSN
REVDAT 1 25-FEB-03 1LG4 0
JRNL AUTH T.LUHRS,R.RIEK,P.GUNTERT,K.WUTHRICH
JRNL TITL NMR STRUCTURE OF THE HUMAN DOPPEL PROTEIN
JRNL REF J.MOL.BIOL. V. 326 1549 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12595265
JRNL DOI 10.1016/S0022-2836(02)01471-7
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPALP 1.3
REMARK 3 AUTHORS : LUGINBUHL, P., GUNTERT, P., BILLETER, M., AND
REMARK 3 WUTHRICH, K.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LG4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015919.
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 : 10 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 13C,15N LABELED HDPL(24-152);
REMARK 210 15N LABELED HDPL(24-152); 13C,
REMARK 210 15N LABELED HDPL(24-152)
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.5, DYANA 1.65
REMARK 210 METHOD USED : NULL
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 : 1
REMARK 210
REMARK 210 REMARK: NULL
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 VAL A 24
REMARK 465 GLN A 25
REMARK 465 THR A 26
REMARK 465 ARG A 27
REMARK 465 GLY A 28
REMARK 465 ILE A 29
REMARK 465 LYS A 30
REMARK 465 HIS A 31
REMARK 465 ARG A 32
REMARK 465 ILE A 33
REMARK 465 LYS A 34
REMARK 465 TRP A 35
REMARK 465 ASN A 36
REMARK 465 ARG A 37
REMARK 465 LYS A 38
REMARK 465 ALA A 39
REMARK 465 LEU A 40
REMARK 465 PRO A 41
REMARK 465 SER A 42
REMARK 465 THR A 43
REMARK 465 ALA A 44
REMARK 465 GLN A 45
REMARK 465 ILE A 46
REMARK 465 THR A 47
REMARK 465 GLU A 48
REMARK 465 ALA A 49
REMARK 465 GLN A 50
REMARK 465 VAL A 51
REMARK 465 ARG A 151
REMARK 465 GLY A 152
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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
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 1 ARG A 134 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 2 TYR A 91 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 3 TYR A 78 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 6 VAL A 105 CA - CB - CG1 ANGL. DEV. = 9.0 DEGREES
REMARK 500 8 TYR A 78 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 13 CYS A 108 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 14 CYS A 108 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 19 CYS A 145 CB - CA - C ANGL. DEV. = 7.3 DEGREES
REMARK 500 19 CYS A 145 CA - CB - SG ANGL. DEV. = 8.4 DEGREES
REMARK 500 20 ARG A 76 NE - CZ - NH2 ANGL. DEV. = -3.4 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 ASN A 54 34.87 -80.08
REMARK 500 1 PRO A 56 24.50 -74.59
REMARK 500 1 LEU A 66 -167.11 48.36
REMARK 500 1 ALA A 72 -76.08 -49.28
REMARK 500 1 ASN A 81 41.22 -150.90
REMARK 500 1 TYR A 91 47.54 -80.43
REMARK 500 1 CYS A 94 110.50 125.95
REMARK 500 1 ASN A 98 69.91 -166.72
REMARK 500 1 PHE A 120 31.42 -68.99
REMARK 500 1 ASP A 124 -106.60 -143.21
REMARK 500 1 LYS A 126 -65.75 -26.25
REMARK 500 1 SER A 141 -66.06 -102.58
REMARK 500 1 LEU A 142 -163.91 45.91
REMARK 500 1 LYS A 143 -80.97 -29.02
REMARK 500 1 CYS A 145 -89.68 -86.82
REMARK 500 1 GLU A 146 -69.49 -144.45
REMARK 500 2 LYS A 61 70.64 27.29
REMARK 500 2 ASP A 67 77.04 -106.53
REMARK 500 2 PHE A 70 -10.25 -146.97
REMARK 500 2 HIS A 90 -101.40 -77.53
REMARK 500 2 TYR A 91 -9.18 72.15
REMARK 500 2 ASN A 92 151.76 68.61
REMARK 500 2 CYS A 94 166.66 72.95
REMARK 500 2 SER A 95 -30.33 -164.82
REMARK 500 2 ASN A 116 55.34 -110.62
REMARK 500 2 ASP A 124 -56.82 -134.43
REMARK 500 2 ASN A 125 93.04 36.86
REMARK 500 2 LYS A 126 -87.46 -104.02
REMARK 500 2 CYS A 145 -86.27 -73.25
REMARK 500 2 GLU A 146 -70.62 -142.73
REMARK 500 2 TRP A 148 39.44 -95.47
REMARK 500 3 GLN A 62 5.14 -61.11
REMARK 500 3 ASP A 67 44.38 -85.30
REMARK 500 3 ALA A 72 -86.05 -120.16
REMARK 500 3 ASN A 81 30.78 -154.52
REMARK 500 3 ASP A 87 -45.28 -135.62
REMARK 500 3 ALA A 103 -63.04 -101.44
REMARK 500 3 ASN A 125 44.43 -99.71
REMARK 500 3 LYS A 126 -98.66 -100.90
REMARK 500 3 SER A 141 -91.27 -62.35
REMARK 500 3 LEU A 142 31.97 26.04
REMARK 500 3 LYS A 143 -49.74 179.75
REMARK 500 3 HIS A 144 -175.02 58.65
REMARK 500 3 CYS A 145 -8.28 -147.50
REMARK 500 3 GLU A 146 -90.14 -109.49
REMARK 500 3 TRP A 148 42.56 -86.47
REMARK 500 4 ALA A 58 -156.05 45.46
REMARK 500 4 LYS A 61 85.72 26.36
REMARK 500 4 ASP A 67 76.95 -106.32
REMARK 500 4 ALA A 72 -74.69 -107.60
REMARK 500
REMARK 500 THIS ENTRY HAS 322 RAMACHANDRAN OUTLIERS.
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 121 LYS A 122 2 148.36
REMARK 500 ASN A 92 GLY A 93 6 143.25
REMARK 500 TRP A 148 LEU A 149 6 149.95
REMARK 500 LEU A 66 ASP A 67 11 149.82
REMARK 500 ASP A 124 ASN A 125 11 -148.65
REMARK 500 ASP A 87 GLY A 88 15 149.38
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 ARG A 55 0.09 SIDE CHAIN
REMARK 500 3 ARG A 134 0.11 SIDE CHAIN
REMARK 500 4 TYR A 82 0.07 SIDE CHAIN
REMARK 500 5 ARG A 76 0.11 SIDE CHAIN
REMARK 500 5 TYR A 78 0.08 SIDE CHAIN
REMARK 500 6 ARG A 134 0.12 SIDE CHAIN
REMARK 500 7 TYR A 78 0.09 SIDE CHAIN
REMARK 500 8 TYR A 78 0.08 SIDE CHAIN
REMARK 500 10 TYR A 78 0.10 SIDE CHAIN
REMARK 500 12 ARG A 64 0.12 SIDE CHAIN
REMARK 500 12 TYR A 78 0.08 SIDE CHAIN
REMARK 500 13 ARG A 76 0.10 SIDE CHAIN
REMARK 500 16 ARG A 76 0.08 SIDE CHAIN
REMARK 500 17 ARG A 55 0.09 SIDE CHAIN
REMARK 500 18 ARG A 55 0.10 SIDE CHAIN
REMARK 500 18 ARG A 76 0.08 SIDE CHAIN
REMARK 500 19 TYR A 82 0.07 SIDE CHAIN
REMARK 500 20 ARG A 55 0.08 SIDE CHAIN
REMARK 500 20 ARG A 76 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1I17 RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE MURINE DOPPEL PROTEIN
DBREF 1LG4 A 24 152 UNP Q9UKY0 PRND_HUMAN 24 152
SEQRES 1 A 129 VAL GLN THR ARG GLY ILE LYS HIS ARG ILE LYS TRP ASN
SEQRES 2 A 129 ARG LYS ALA LEU PRO SER THR ALA GLN ILE THR GLU ALA
SEQRES 3 A 129 GLN VAL ALA GLU ASN ARG PRO GLY ALA PHE ILE LYS GLN
SEQRES 4 A 129 GLY ARG LYS LEU ASP ILE ASP PHE GLY ALA GLU GLY ASN
SEQRES 5 A 129 ARG TYR TYR GLU ALA ASN TYR TRP GLN PHE PRO ASP GLY
SEQRES 6 A 129 ILE HIS TYR ASN GLY CYS SER GLU ALA ASN VAL THR LYS
SEQRES 7 A 129 GLU ALA PHE VAL THR GLY CYS ILE ASN ALA THR GLN ALA
SEQRES 8 A 129 ALA ASN GLN GLY GLU PHE GLN LYS PRO ASP ASN LYS LEU
SEQRES 9 A 129 HIS GLN GLN VAL LEU TRP ARG LEU VAL GLN GLU LEU CYS
SEQRES 10 A 129 SER LEU LYS HIS CYS GLU PHE TRP LEU GLU ARG GLY
HELIX 1 1 GLY A 71 TYR A 82 1 12
HELIX 2 2 TRP A 83 PHE A 85 5 3
HELIX 3 3 THR A 100 ASN A 116 1 17
HELIX 4 4 ASN A 125 LEU A 142 1 18
SSBOND 1 CYS A 94 CYS A 145 1555 1555 2.02
SSBOND 2 CYS A 108 CYS A 140 1555 1555 2.02
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