Header list of 1fkc.pdb file
Complete list - 14 20 Bytes
HEADER MEMBRANE PROTEIN 09-AUG-00 1FKC
TITLE HUMAN PRION PROTEIN (MUTANT E200K) FRAGMENT 90-231
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PRP(90-231);
COMPND 5 ENGINEERED: YES;
COMPND 6 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: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3;
SOURCE 10 OTHER_DETAILS: BRAIN
KEYWDS THREE HELIX, CREUTZFELDT-JAKOB DISEASE, PRION, AGGREGATION, MEMBRANE
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
AUTHOR Y.ZHANG,W.SWIETNICKI,M.G.ZAGORSKI,W.K.SUREWICZ,F.D.SOENNICHSEN
REVDAT 6 14-MAR-18 1FKC 1 REMARK SEQADV
REVDAT 5 24-FEB-09 1FKC 1 VERSN
REVDAT 4 01-APR-03 1FKC 1 JRNL
REVDAT 3 25-APR-01 1FKC 1 KEYWDS AUTHOR JRNL
REVDAT 2 22-SEP-00 1FKC 3 AUTHOR JRNL ATOM
REVDAT 1 21-SEP-00 1FKC 0
JRNL AUTH Y.ZHANG,W.SWIETNICKI,M.G.ZAGORSKI,W.K.SUREWICZ,
JRNL AUTH 2 F.D.SONNICHSEN
JRNL TITL SOLUTION STRUCTURE OF THE E200K VARIANT OF HUMAN PRION
JRNL TITL 2 PROTEIN. IMPLICATIONS FOR THE MECHANISM OF PATHOGENESIS IN
JRNL TITL 3 FAMILIAL PRION DISEASES.
JRNL REF J.BIOL.CHEM. V. 275 33650 2000
JRNL REFN ISSN 0021-9258
JRNL PMID 10954699
JRNL DOI 10.1074/JBC.C000483200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9, CNS 0.9
REMARK 3 AUTHORS : BRUNGER (CNS), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FKC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-SEP-00.
REMARK 100 THE DEPOSITION ID IS D_1000011668.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 299
REMARK 210 PH : 4.6
REMARK 210 IONIC STRENGTH : 0.00001
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.8 MM E200K(90-231)PRP U
REMARK 210 -15N,13C; 10MM ACETATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ARIA 0.9
REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 11
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 RES C SSSEQI
REMARK 465 GLY A 90
REMARK 465 GLN A 91
REMARK 465 GLY A 92
REMARK 465 GLY A 93
REMARK 465 GLY A 94
REMARK 465 THR A 95
REMARK 465 HIS A 96
REMARK 465 SER 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 MET 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 GLY A 124
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 SER A 132 172.00 -52.92
REMARK 500 MET A 134 -71.03 -130.63
REMARK 500 PHE A 141 -93.00 -99.71
REMARK 500 SER A 143 -154.30 -148.65
REMARK 500 ASP A 167 -157.65 -105.55
REMARK 500 TYR A 169 74.06 55.24
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FKC A 90 231 UNP P04156 PRIO_HUMAN 90 231
SEQADV 1FKC LYS A 200 UNP P04156 GLU 200 ENGINEERED MUTATION
SEQRES 1 A 142 GLY GLN GLY GLY GLY THR HIS SER GLN TRP ASN LYS PRO
SEQRES 2 A 142 SER LYS PRO LYS THR ASN MET LYS HIS MET ALA GLY ALA
SEQRES 3 A 142 ALA ALA ALA GLY ALA VAL VAL GLY GLY LEU GLY GLY TYR
SEQRES 4 A 142 MET LEU GLY SER ALA MET SER ARG PRO ILE ILE HIS PHE
SEQRES 5 A 142 GLY SER ASP TYR GLU ASP ARG TYR TYR ARG GLU ASN MET
SEQRES 6 A 142 HIS ARG TYR PRO ASN GLN VAL TYR TYR ARG PRO MET ASP
SEQRES 7 A 142 GLU TYR SER ASN GLN ASN ASN PHE VAL HIS ASP CYS VAL
SEQRES 8 A 142 ASN ILE THR ILE LYS GLN HIS THR VAL THR THR THR THR
SEQRES 9 A 142 LYS GLY GLU ASN PHE THR LYS THR ASP VAL LYS MET MET
SEQRES 10 A 142 GLU ARG VAL VAL GLU GLN MET CYS ILE THR GLN TYR GLU
SEQRES 11 A 142 ARG GLU SER GLN ALA TYR TYR GLN ARG GLY SER SER
HELIX 1 1 SER A 143 MET A 154 1 12
HELIX 2 2 HIS A 155 TYR A 157 5 3
HELIX 3 3 ASN A 171 GLY A 195 1 25
HELIX 4 4 THR A 199 GLY A 229 1 31
SHEET 1 A 2 MET A 129 GLY A 131 0
SHEET 2 A 2 VAL A 161 TYR A 163 -1 O VAL A 161 N GLY A 131
SSBOND 1 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
Complete list - 14 20 Bytes