Header list of 1ag2.pdb file
Complete list - 24 20 Bytes
HEADER PRION PROTEIN 31-MAR-97 1AG2
TITLE PRION PROTEIN DOMAIN PRP(121-231) FROM MOUSE, NMR, 2 MINIMIZED AVERAGE
TITLE 2 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR PRION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOMAIN 121 - 231;
COMPND 5 SYNONYM: PRP(121-231);
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 CELL_LINE: BL21 (DE3);
SOURCE 6 GENE: T7;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: BL21 (DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: T7;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: T7 PPRP-C6;
SOURCE 12 EXPRESSION_SYSTEM_GENE: T7
KEYWDS PRION PROTEIN, BRAIN, GLYCOPROTEIN, GPI-ANCHOR
EXPDTA SOLUTION NMR
AUTHOR M.BILLETER,R.RIEK,G.WIDER,K.WUTHRICH,S.HORNEMANN,R.GLOCKSHUBER
REVDAT 3 24-FEB-16 1AG2 1 JRNL VERSN
REVDAT 2 24-FEB-09 1AG2 1 VERSN
REVDAT 1 08-OCT-97 1AG2 0
JRNL AUTH R.RIEK,S.HORNEMANN,G.WIDER,M.BILLETER,R.GLOCKSHUBER,
JRNL AUTH 2 K.WUTHRICH
JRNL TITL NMR STRUCTURE OF THE MOUSE PRION PROTEIN DOMAIN
JRNL TITL 2 PRP(121-231).
JRNL REF NATURE V. 382 180 1996
JRNL REFN ISSN 0028-0836
JRNL PMID 8700211
JRNL DOI 10.1038/382180A0
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPAL
REMARK 3 AUTHORS : LUGINBUHL,GUNTERT,BILLETER,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AG2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
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 : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; UNITY+
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : BEST 20
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 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 HH TYR A 128 OD2 ASP A 178 1.59
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 ALA A 133 160.92 175.40
REMARK 500 GLN A 168 -33.82 -143.41
REMARK 500 SER A 170 -102.62 117.29
REMARK 500 ASN A 181 -83.16 -77.94
REMARK 500 THR A 188 -69.39 -99.32
REMARK 500 GLN A 217 -78.42 -61.87
REMARK 500 SER A 222 1.36 -64.21
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 ARG A 208 0.11 SIDE CHAIN
REMARK 500 TYR A 218 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AG2 A 124 226 UNP P04925 PRIO_MOUSE 123 225
SEQRES 1 A 103 GLY LEU GLY GLY TYR MET LEU GLY SER ALA MET SER ARG
SEQRES 2 A 103 PRO MET ILE HIS PHE GLY ASN ASP TRP GLU ASP ARG TYR
SEQRES 3 A 103 TYR ARG GLU ASN MET TYR ARG TYR PRO ASN GLN VAL TYR
SEQRES 4 A 103 TYR ARG PRO VAL ASP GLN TYR SER ASN GLN ASN ASN PHE
SEQRES 5 A 103 VAL HIS ASP CYS VAL ASN ILE THR ILE LYS GLN HIS THR
SEQRES 6 A 103 VAL THR THR THR THR LYS GLY GLU ASN PHE THR GLU THR
SEQRES 7 A 103 ASP VAL LYS MET MET GLU ARG VAL VAL GLU GLN MET CYS
SEQRES 8 A 103 VAL THR GLN TYR GLN LYS GLU SER GLN ALA TYR TYR
HELIX 1 1 ASP A 144 ASN A 153 1 10
HELIX 2 2 GLN A 172 LYS A 194 1 23
HELIX 3 3 GLU A 200 ALA A 224 1 25
SHEET 1 S1 2 TYR A 128 GLY A 131 0
SHEET 2 S1 2 VAL A 161 ARG A 164 -1
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 - 24 20 Bytes