Header list of 1h0l.pdb file
Complete list - n 12 2 Bytes
HEADER CELL CYCLE 24-JUN-02 1H0L
TITLE HUMAN PRION PROTEIN 121-230 M166C/E221C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR PRION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 121-230;
COMPND 5 SYNONYM: PRP, PRION PROTEIN, PRP27-30, PRP33-35C;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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 CELL CYCLE, BRAIN, GLYCOPROTEIN, GPI-ANCHOR, REPEAT,
KEYWDS 2 POLYMORPHISM, DISEASE MUTATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.ZAHN,P.GUNTERT,K.WUTHRICH
REVDAT 3 15-MAY-13 1H0L 1 HEADER KEYWDS AUTHOR REMARK
REVDAT 3 2 VERSN ATOM TER
REVDAT 2 24-FEB-09 1H0L 1 VERSN
REVDAT 1 30-JAN-03 1H0L 0
JRNL AUTH R.ZAHN,P.GUNTERT,C.VON SCHROETTER,K.WUTHRICH
JRNL TITL NMR STRUCTURE OF A VARIANT HUMAN PRION PROTEIN
JRNL TITL 2 WITH TWO DISULFIDE BRIDGES
JRNL REF J.MOL.BIOL. V. 326 225 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12547204
JRNL DOI 10.1016/S0022-2836(02)01332-3
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 1H0L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUN-02.
REMARK 100 THE PDBE ID CODE IS EBI-9859.
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 M
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
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 : 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 : 2
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE
REMARK 210 SPECTROSCOPY ON 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 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 400
REMARK 400 COMPOUND
REMARK 400 DISULFIDE BOND BETWEEN C166 AND C221
REMARK 400
REMARK 400 ENGINEERED MUTATION MET 166 CYS AND GLU 221 CYS CHAIN A
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 3 ARG A 164 CD - NE - CZ ANGL. DEV. = 8.7 DEGREES
REMARK 500 3 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 4 ARG A 164 CD - NE - CZ ANGL. DEV. = 9.1 DEGREES
REMARK 500 4 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 5 CYS A 166 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 6 TYR A 226 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 7 ARG A 208 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 8 CYS A 166 CA - CB - SG ANGL. DEV. = 9.1 DEGREES
REMARK 500 8 CYS A 214 CA - CB - SG ANGL. DEV. = -6.9 DEGREES
REMARK 500 8 ARG A 228 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 9 TYR A 226 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 12 ARG A 148 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 13 CYS A 214 CA - CB - SG ANGL. DEV. = -7.0 DEGREES
REMARK 500 14 ARG A 164 CD - NE - CZ ANGL. DEV. = 8.8 DEGREES
REMARK 500 18 TYR A 169 CB - CG - CD2 ANGL. DEV. = -3.9 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 SER A 120 112.92 86.52
REMARK 500 1 VAL A 122 152.69 70.25
REMARK 500 1 TYR A 128 172.18 44.17
REMARK 500 1 ARG A 148 0.99 -66.99
REMARK 500 1 TYR A 149 -62.86 -93.28
REMARK 500 1 ASN A 171 174.11 63.83
REMARK 500 2 MET A 134 -154.27 -138.22
REMARK 500 2 ILE A 138 79.72 52.46
REMARK 500 2 PRO A 165 -174.84 -63.82
REMARK 500 2 TYR A 169 90.51 -56.95
REMARK 500 2 SER A 170 39.27 -140.28
REMARK 500 2 ASN A 171 162.32 62.32
REMARK 500 2 CYS A 221 -73.09 -50.90
REMARK 500 2 ARG A 228 -80.40 -80.42
REMARK 500 3 SER A 120 161.94 67.35
REMARK 500 3 ILE A 138 73.02 53.44
REMARK 500 3 ASP A 147 -62.21 -93.65
REMARK 500 3 TYR A 169 98.08 -31.19
REMARK 500 3 ASN A 171 -171.63 52.30
REMARK 500 3 PHE A 198 178.65 -53.77
REMARK 500 4 SER A 132 178.40 49.26
REMARK 500 4 ILE A 138 73.74 49.32
REMARK 500 4 CYS A 166 17.96 -67.71
REMARK 500 4 TYR A 169 24.83 43.65
REMARK 500 4 SER A 170 46.70 -80.98
REMARK 500 4 ASN A 171 162.25 70.42
REMARK 500 5 VAL A 122 152.40 62.06
REMARK 500 5 LEU A 125 -88.62 -89.19
REMARK 500 5 PRO A 137 6.40 -69.88
REMARK 500 5 ILE A 138 72.29 37.06
REMARK 500 5 GLU A 168 39.26 -99.51
REMARK 500 5 SER A 170 -46.36 -157.14
REMARK 500 5 ARG A 228 -68.62 -130.25
REMARK 500 6 SER A 120 148.65 67.49
REMARK 500 6 TYR A 128 -169.48 41.43
REMARK 500 6 ILE A 138 77.20 50.02
REMARK 500 6 GLU A 168 62.80 -106.77
REMARK 500 6 SER A 170 52.14 -171.12
REMARK 500 6 ASN A 171 -179.96 60.05
REMARK 500 7 VAL A 121 175.59 58.23
REMARK 500 7 VAL A 122 152.44 67.06
REMARK 500 7 MET A 129 -160.41 -112.99
REMARK 500 7 ILE A 138 74.37 47.74
REMARK 500 7 PRO A 165 -173.32 -67.27
REMARK 500 7 GLU A 168 -74.64 -69.50
REMARK 500 7 TYR A 169 171.44 65.72
REMARK 500 7 SER A 170 -80.01 66.60
REMARK 500 7 ASN A 171 165.90 178.37
REMARK 500 8 SER A 120 23.62 47.42
REMARK 500 8 ILE A 138 72.15 44.49
REMARK 500
REMARK 500 THIS ENTRY HAS 133 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 GLY A 119 SER A 120 1 145.44
REMARK 500 GLY A 127 TYR A 128 7 144.75
REMARK 500 GLY A 229 SER A 230 14 147.62
REMARK 500 GLY A 142 SER A 143 17 149.29
REMARK 500 GLY A 229 SER A 230 17 142.39
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 ARG A 148 0.09 SIDE CHAIN
REMARK 500 1 ARG A 151 0.08 SIDE CHAIN
REMARK 500 1 ARG A 164 0.10 SIDE CHAIN
REMARK 500 1 TYR A 218 0.09 SIDE CHAIN
REMARK 500 1 TYR A 225 0.06 SIDE CHAIN
REMARK 500 1 ARG A 228 0.12 SIDE CHAIN
REMARK 500 2 TYR A 128 0.06 SIDE CHAIN
REMARK 500 2 TYR A 163 0.09 SIDE CHAIN
REMARK 500 2 ARG A 164 0.12 SIDE CHAIN
REMARK 500 2 TYR A 226 0.07 SIDE CHAIN
REMARK 500 3 ARG A 148 0.13 SIDE CHAIN
REMARK 500 3 ARG A 156 0.08 SIDE CHAIN
REMARK 500 3 TYR A 163 0.08 SIDE CHAIN
REMARK 500 3 ARG A 220 0.08 SIDE CHAIN
REMARK 500 3 ARG A 228 0.10 SIDE CHAIN
REMARK 500 4 ARG A 151 0.08 SIDE CHAIN
REMARK 500 4 PHE A 175 0.10 SIDE CHAIN
REMARK 500 4 ARG A 208 0.17 SIDE CHAIN
REMARK 500 5 TYR A 150 0.09 SIDE CHAIN
REMARK 500 5 ARG A 164 0.18 SIDE CHAIN
REMARK 500 5 PHE A 175 0.08 SIDE CHAIN
REMARK 500 5 ARG A 208 0.10 SIDE CHAIN
REMARK 500 6 ARG A 148 0.10 SIDE CHAIN
REMARK 500 7 ARG A 148 0.08 SIDE CHAIN
REMARK 500 7 ARG A 156 0.11 SIDE CHAIN
REMARK 500 7 TYR A 218 0.15 SIDE CHAIN
REMARK 500 8 ARG A 148 0.10 SIDE CHAIN
REMARK 500 8 TYR A 150 0.12 SIDE CHAIN
REMARK 500 8 TYR A 169 0.08 SIDE CHAIN
REMARK 500 8 PHE A 175 0.09 SIDE CHAIN
REMARK 500 10 ARG A 148 0.09 SIDE CHAIN
REMARK 500 11 TYR A 163 0.07 SIDE CHAIN
REMARK 500 11 ARG A 164 0.11 SIDE CHAIN
REMARK 500 12 TYR A 128 0.07 SIDE CHAIN
REMARK 500 12 ARG A 151 0.14 SIDE CHAIN
REMARK 500 12 TYR A 163 0.10 SIDE CHAIN
REMARK 500 12 TYR A 218 0.09 SIDE CHAIN
REMARK 500 13 ARG A 148 0.10 SIDE CHAIN
REMARK 500 13 TYR A 149 0.08 SIDE CHAIN
REMARK 500 13 TYR A 150 0.12 SIDE CHAIN
REMARK 500 13 ARG A 164 0.08 SIDE CHAIN
REMARK 500 14 ARG A 136 0.08 SIDE CHAIN
REMARK 500 14 ARG A 148 0.12 SIDE CHAIN
REMARK 500 14 TYR A 149 0.08 SIDE CHAIN
REMARK 500 14 TYR A 162 0.07 SIDE CHAIN
REMARK 500 14 TYR A 169 0.07 SIDE CHAIN
REMARK 500 14 ARG A 208 0.22 SIDE CHAIN
REMARK 500 15 ARG A 148 0.12 SIDE CHAIN
REMARK 500 15 TYR A 226 0.07 SIDE CHAIN
REMARK 500 17 TYR A 163 0.11 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 61 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FKC RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN (MUTANT E200K) FRAGMENT
REMARK 900 90-231
REMARK 900 RELATED ID: 1FO7 RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN MUTANT E200K FRAGMENT 90
REMARK 900 -231
REMARK 900 RELATED ID: 1I4M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN PRION PROTEIN
REMARK 900 REVEALS AMECHANISM FOR OLIGOMERIZATION
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
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 2 RESIDUES (GLY SER) INSERTED AT THE N-TERMINUS
REMARK 999 MET166 AND GLU221 REPLACED AGAINST CYS
DBREF 1H0L A 119 120 PDB 1H0L 1H0L 119 120
DBREF 1H0L A 121 230 UNP P04156 PRIO_HUMAN 121 230
SEQADV 1H0L CYS A 166 UNP P04156 MET 166 ENGINEERED MUTATION
SEQADV 1H0L CYS A 221 UNP P04156 GLU 221 ENGINEERED MUTATION
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 ILE 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 CYS ASP GLU TYR SER
SEQRES 5 A 112 ASN GLN ASN ASN PHE VAL HIS ASP CYS VAL ASN ILE THR
SEQRES 6 A 112 ILE LYS GLN HIS THR VAL THR THR THR THR LYS GLY GLU
SEQRES 7 A 112 ASN PHE THR GLU THR ASP VAL LYS MET MET GLU ARG VAL
SEQRES 8 A 112 VAL GLU GLN MET CYS ILE THR GLN TYR GLU ARG CYS SER
SEQRES 9 A 112 GLN ALA TYR TYR GLN ARG GLY SER
HELIX 1 H1 ASP A 144 MET A 154 1 11
HELIX 2 H2 ASN A 173 LYS A 194 1 22
HELIX 3 H3 GLU A 200 ARG A 228 1 29
SHEET 1 S1 2 TYR A 128 GLY A 131 0
SHEET 2 S1 2 VAL A 161 ARG A 164 -1 N TYR A 128 O VAL A 161
SSBOND 1 CYS A 166 CYS A 221 1555 1555 2.04
SSBOND 2 CYS A 179 CYS A 214 1555 1555 2.03
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 - n 12 2 Bytes