HEADER SIGNALING PROTEIN 14-MAY-01 1IPG
TITLE SOLUTION STRUCTURE OF THE PB1 DOMAIN OF BEM1P
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BEM1 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PB1 DOMAIN(RESIDUES 472-551);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPROEX-HTA
KEYWDS UBIQUITIN ALPHA/BETA ROLL, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR H.TERASAWA,Y.NODA,T.ITO,H.HATANAKA,S.ICHIKAWA,K.OGURA,H.SUMIMOTO,
AUTHOR 2 F.INAGAKI
REVDAT 5 27-DEC-23 1IPG 1 REMARK
REVDAT 4 23-FEB-22 1IPG 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1IPG 1 VERSN
REVDAT 2 14-JAN-03 1IPG 1 REMARK
REVDAT 1 15-AUG-01 1IPG 0
JRNL AUTH H.TERASAWA,Y.NODA,T.ITO,H.HATANAKA,S.ICHIKAWA,K.OGURA,
JRNL AUTH 2 H.SUMIMOTO,F.INAGAKI
JRNL TITL STRUCTURE AND LIGAND RECOGNITION OF THE PB1 DOMAIN: A NOVEL
JRNL TITL 2 PROTEIN MODULE BINDING TO THE PC MOTIF.
JRNL REF EMBO J. V. 20 3947 2001
JRNL REFN ISSN 0261-4189
JRNL PMID 11483498
JRNL DOI 10.1093/EMBOJ/20.15.3947
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.ITO,Y.MATSUI,T.AGO,K.OTA,H.SUMIMOTO
REMARK 1 TITL NOVEL MODULAR DOMAIN PB1 RECOGNIZES PC MOTIF TO MEDIATE
REMARK 1 TITL 2 FUNCTIONAL PROTEIN-PROTEIN INTERACTIONS
REMARK 1 REF EMBO J. V. 20 3938 2001
REMARK 1 REFN ISSN 0261-4189
REMARK 1 DOI 10.1093/EMBOJ/20.15.3938
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1, X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1334 RESTRAINTS, 1269 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 65
REMARK 3 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1IPG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAY-01.
REMARK 100 THE DEPOSITION ID IS D_1000005149.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : 50MM POTASSIUM PHOSPHATE; 150MM
REMARK 210 SODIUM CHLORIDE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM BEM PB1 U-15N, 13C; 50MM
REMARK 210 POTASSIUM PHOSPHATE PH 6.3;
REMARK 210 150MM SODIUM CHLORIDE; 1MM
REMARK 210 SODIUM AZIDE; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA; HNHB;
REMARK 210 HN(CO)HB
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DYNAMICAL SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 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 2 104.84 58.10
REMARK 500 MET A 3 61.68 -157.75
REMARK 500 SER A 5 -58.49 -175.64
REMARK 500 SER A 6 76.36 44.03
REMARK 500 THR A 7 72.42 54.42
REMARK 500 LEU A 10 -146.15 35.09
REMARK 500 LYS A 20 -135.74 52.86
REMARK 500 ASP A 46 8.33 91.71
REMARK 500 LYS A 55 106.52 -35.25
REMARK 500 LEU A 56 -85.15 -92.99
REMARK 500 PHE A 57 -37.94 -160.46
REMARK 500 LYS A 65 13.65 -148.47
REMARK 500 LYS A 77 81.51 45.04
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 38 0.25 SIDE CHAIN
REMARK 500 ARG A 44 0.18 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IP9 RELATED DB: PDB
REMARK 900 1IP9 IS THE ENSEMBLES OF 20 STRUCTURES.
DBREF 1IPG A 6 85 UNP P29366 BEM1_YEAST 472 551
SEQADV 1IPG GLY A 1 UNP P29366 CLONING ARTIFACT
SEQADV 1IPG ALA A 2 UNP P29366 CLONING ARTIFACT
SEQADV 1IPG MET A 3 UNP P29366 CLONING ARTIFACT
SEQADV 1IPG GLY A 4 UNP P29366 CLONING ARTIFACT
SEQADV 1IPG SER A 5 UNP P29366 CLONING ARTIFACT
SEQRES 1 A 85 GLY ALA MET GLY SER SER THR SER GLY LEU LYS THR THR
SEQRES 2 A 85 LYS ILE LYS PHE TYR TYR LYS ASP ASP ILE PHE ALA LEU
SEQRES 3 A 85 MET LEU LYS GLY ASP THR THR TYR LYS GLU LEU ARG SER
SEQRES 4 A 85 LYS ILE ALA PRO ARG ILE ASP THR ASP ASN PHE LYS LEU
SEQRES 5 A 85 GLN THR LYS LEU PHE ASP GLY SER GLY GLU GLU ILE LYS
SEQRES 6 A 85 THR ASP SER GLN VAL SER ASN ILE ILE GLN ALA LYS LEU
SEQRES 7 A 85 LYS ILE SER VAL HIS ASP ILE
HELIX 1 1 THR A 33 ASP A 46 1 14
HELIX 2 2 THR A 66 ALA A 76 1 11
SHEET 1 A 4 PHE A 24 LEU A 28 0
SHEET 2 A 4 THR A 13 TYR A 19 -1 N THR A 13 O LEU A 28
SHEET 3 A 4 ILE A 80 ASP A 84 1 N ILE A 80 O LYS A 16
SHEET 4 A 4 PHE A 50 THR A 54 -1 O LYS A 51 N HIS A 83
CRYST1 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
(ATOM LINES ARE NOT SHOWN.)
END