HEADER TRANSFERASE 11-MAY-09 2KIT
TITLE THE SOLUTION STRUCTURE OF THE REDUCED YEAST TOR1 FATC DOMAIN BOUND TO
TITLE 2 DPC MICELLES AT 298K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE TOR1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: YEAST TOR1 FATC DOMAIN;
COMPND 5 SYNONYM: PHOSPHATIDYLINOSITOL KINASE HOMOLOG TOR1, TARGET OF
COMPND 6 RAPAMYCIN KINASE 1, DOMINANT RAPAMYCIN RESISTANCE PROTEIN 1;
COMPND 7 EC: 2.7.11.1;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: DRR1, J1803, TOR1, YJR066W;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: ROSETTA (DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PGEV2
KEYWDS PROTEIN, DPC MICELLE, MEMBRANE-MIMETIC, ATP-BINDING, CELL CYCLE, CELL
KEYWDS 2 MEMBRANE, KINASE, MEMBRANE, NUCLEOTIDE-BINDING, SERINE/THREONINE-
KEYWDS 3 PROTEIN KINASE, TRANSFERASE, VACUOLE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.A.DAMES
REVDAT 3 14-DEC-16 2KIT 1 TITLE VERSN
REVDAT 2 16-MAR-10 2KIT 1 JRNL
REVDAT 1 19-JAN-10 2KIT 0
JRNL AUTH S.A.DAMES
JRNL TITL STRUCTURAL BASIS FOR THE ASSOCIATION OF THE REDOX-SENSITIVE
JRNL TITL 2 TARGET OF RAPAMYCIN FATC DOMAIN WITH MEMBRANE-MIMETIC
JRNL TITL 3 MICELLES.
JRNL REF J.BIOL.CHEM. V. 285 7766 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20042596
JRNL DOI 10.1074/JBC.M109.058404
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR_NIH 2.16.0
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2KIT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-09.
REMARK 100 THE RCSB ID CODE IS RCSB101172.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 150
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM [U-13C; U-15N] Y1FATC-1,
REMARK 210 95% H2O/5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 3D HNCA; 3D HCCH-TOCSY; 3D 1H-15N
REMARK 210 NOESY; 3D 1H-13C NOESY; 3D HACAHB
REMARK 210 -COSY; 3D HNHB; {15N} SED 1H-13C
REMARK 210 HSQC; {13C'} SED 1H-13C HSQC; 15N
REMARK 210 T1; 15N T2; {1H}-15N-NOE
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR_NIH 2.16.0, NMRVIEW
REMARK 210 5.2.2_01, NMRPIPE, NMRDRAW,
REMARK 210 PROCHECKNMR, MOLMOL, XWINNMR 3.5,
REMARK 210 TENSOR2 2
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY
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 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 O GLN A 8 H LEU A 12 1.46
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 LEU A 3 164.38 -47.37
REMARK 500 1 ASP A 4 -177.68 -68.31
REMARK 500 1 PRO A 6 30.31 -87.33
REMARK 500 1 VAL A 9 -70.99 -46.60
REMARK 500 1 HIS A 25 -63.36 -95.86
REMARK 500 1 TYR A 26 -70.07 -55.64
REMARK 500 1 TRP A 29 -168.92 -127.28
REMARK 500 1 PHE A 32 -70.19 -81.47
REMARK 500 2 LEU A 3 171.82 -58.83
REMARK 500 2 ASP A 4 -177.86 -61.54
REMARK 500 2 VAL A 9 -71.19 -46.30
REMARK 500 2 HIS A 25 -65.13 -95.73
REMARK 500 2 TYR A 26 -70.14 -44.03
REMARK 500 3 GLU A 2 -118.18 -76.19
REMARK 500 3 VAL A 9 -71.21 -48.50
REMARK 500 3 HIS A 25 -60.38 -95.35
REMARK 500 3 TYR A 26 -70.21 -53.07
REMARK 500 3 TRP A 29 -162.59 -125.92
REMARK 500 4 ASP A 4 -178.95 -66.65
REMARK 500 4 VAL A 9 -70.70 -49.11
REMARK 500 4 HIS A 25 -68.30 -96.83
REMARK 500 4 TYR A 26 -70.86 -43.22
REMARK 500 4 TRP A 29 -162.55 -123.90
REMARK 500 4 PHE A 32 -71.22 -82.88
REMARK 500 5 GLU A 2 -77.31 -74.36
REMARK 500 5 VAL A 9 -70.75 -44.71
REMARK 500 5 HIS A 25 -65.56 -95.43
REMARK 500 5 PHE A 32 -71.71 -83.56
REMARK 500 6 ASP A 4 -175.43 -60.46
REMARK 500 6 PRO A 6 44.16 -88.64
REMARK 500 6 VAL A 9 -70.76 -44.90
REMARK 500 6 LEU A 22 -70.44 -66.06
REMARK 500 6 HIS A 25 -64.98 -96.19
REMARK 500 6 TRP A 29 -162.48 -125.00
REMARK 500 6 PHE A 32 -70.47 -81.09
REMARK 500 7 LEU A 3 154.65 -45.42
REMARK 500 7 VAL A 9 -71.04 -52.96
REMARK 500 7 HIS A 25 -65.52 -96.07
REMARK 500 7 TYR A 26 -70.76 -51.62
REMARK 500 7 TRP A 29 -164.20 -129.90
REMARK 500 7 PHE A 32 -70.46 -84.41
REMARK 500 8 GLU A 2 -166.38 -58.54
REMARK 500 8 VAL A 9 -71.11 -50.16
REMARK 500 8 HIS A 25 -60.75 -96.34
REMARK 500 8 TYR A 26 -70.34 -52.03
REMARK 500 8 TRP A 29 -167.81 -119.18
REMARK 500 8 PHE A 32 -73.26 -86.82
REMARK 500 9 GLU A 2 -76.31 -72.04
REMARK 500 9 VAL A 9 -71.12 -45.62
REMARK 500 9 HIS A 25 -64.99 -95.63
REMARK 500
REMARK 500 THIS ENTRY HAS 108 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6228 RELATED DB: BMRB
REMARK 900 OXIDIZED YEAST TOR1 FATC DOMAIN IN SOLUTION, 298K
REMARK 900 RELATED ID: 1W1N RELATED DB: PDB
REMARK 900 OXIDIZED YEAST TOR1 FATC DOMAIN IN SOLUTION, 298K
REMARK 900 RELATED ID: 16284 RELATED DB: BMRB
REMARK 900 OXIDIZED YEAST TOR1 FATC DOMAIN BOUND TO DPC MICELLES, 318K
REMARK 900 RELATED ID: 2KIO RELATED DB: PDB
REMARK 900 OXIDIZED YEAST TOR1 FATC DOMAIN BOUND TO DPC MICELLES, 318K
REMARK 900 RELATED ID: 16295 RELATED DB: BMRB
REMARK 900 REDUCED YEAST TOR1 FATC DOMAIN BOUND TO DPC MICELLES AT 298K
DBREF 2KIT A 1 33 UNP P35169 TOR1_YEAST 2438 2470
SEQRES 1 A 33 ASN GLU LEU ASP VAL PRO GLU GLN VAL ASP LYS LEU ILE
SEQRES 2 A 33 GLN GLN ALA THR SER ILE GLU ARG LEU CYS GLN HIS TYR
SEQRES 3 A 33 ILE GLY TRP CYS PRO PHE TRP
HELIX 1 1 PRO A 6 ILE A 27 1 22
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
(ATOM LINES ARE NOT SHOWN.)
END