HEADER SIGNALING PROTEIN 27-MAY-08 2K42
TITLE SOLUTION STRUCTURE OF THE GTPASE BINDING DOMAIN OF WASP IN COMPLEX
TITLE 2 WITH ESPFU, AN EHEC EFFECTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: WISKOTT-ALDRICH SYNDROME PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CRIB DOMAIN, UNP RESIDUES 242-310;
COMPND 5 SYNONYM: WASP;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ESPFU;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UNP RESIDUES 268-300;
COMPND 11 SYNONYM: TIR-CYTOSKELETON COUPLING PROTEIN;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: WAS, IMD2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PGEX;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI O157:H7;
SOURCE 11 ORGANISM_TAXID: 83334;
SOURCE 12 GENE: TCCP, ECS2715;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 15 EXPRESSION_SYSTEM_VECTOR: PGEX
KEYWDS WASP, ESPFU, GBD, AUTOINHIBITION, CYTOPLASM, CYTOSKELETON, DISEASE
KEYWDS 2 MUTATION, PHOSPHOPROTEIN, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.-C.CHENG,B.M.SKEHAN,K.G.CAMPELLONE,J.M.LEONG,M.K.ROSEN
REVDAT 4 16-MAR-22 2K42 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2K42 1 VERSN
REVDAT 2 09-SEP-08 2K42 1 JRNL
REVDAT 1 22-JUL-08 2K42 0
JRNL AUTH H.C.CHENG,B.M.SKEHAN,K.G.CAMPELLONE,J.M.LEONG,M.K.ROSEN
JRNL TITL STRUCTURAL MECHANISM OF WASP ACTIVATION BY THE
JRNL TITL 2 ENTEROHAEMORRHAGIC E. COLI EFFECTOR ESPF(U).
JRNL REF NATURE V. 454 1009 2008
JRNL REFN ISSN 0028-0836
JRNL PMID 18650809
JRNL DOI 10.1038/NATURE07160
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 2.1, ARIA 2.1, CNS
REMARK 3 AUTHORS : LINGE, O'DONOGHUE AND NILGES (ARIA), LINGE,
REMARK 3 O'DONOGHUE AND NILGES (ARIA), BRUNGER, ADAMS,
REMARK 3 CLORE, GROS, NILGES AND READ (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2K42 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-08.
REMARK 100 THE DEPOSITION ID IS D_1000100649.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.15
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1~1.5 MM [U-100% 13C; U-100%
REMARK 210 15N] GBD/R33 COMPLEX, 90% H2O/10%
REMARK 210 D2O; 1~1.5 MM [U-100% 13C; U-
REMARK 210 100% 15N] GBD/R33 COMPLEX, 100%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D HNCACB; 3D CBCA(CO)NH; 3D
REMARK 210 HCCH-TOCSY; 2D 1H-15N HSQC; 3D
REMARK 210 1H-15N NOESY; 3D HNCO; 4D 13C-
REMARK 210 13C NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW, NMRPIPE
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 5 PHE A 33 CE1 PHE A 33 CZ 0.120
REMARK 500 11 TYR A 53 CE1 TYR A 53 CZ 0.080
REMARK 500 11 TYR A 53 CZ TYR A 53 CE2 -0.080
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 HIS A 2 39.76 -147.60
REMARK 500 1 HIS A 8 96.84 -178.62
REMARK 500 1 VAL A 12 36.81 35.75
REMARK 500 1 ARG A 71 -63.03 -140.86
REMARK 500 1 HIS B 90 -64.19 -122.21
REMARK 500 1 ARG B 96 -79.75 -156.81
REMARK 500 1 ASN B 97 -171.68 -174.01
REMARK 500 2 SER A 4 -32.77 -149.01
REMARK 500 2 HIS A 8 71.58 45.52
REMARK 500 2 VAL A 12 -35.52 72.27
REMARK 500 2 ARG A 71 -58.72 -120.65
REMARK 500 2 ASP B 78 -166.92 -102.68
REMARK 500 2 HIS B 90 -73.48 -117.13
REMARK 500 2 ASN B 97 45.46 -77.42
REMARK 500 2 MET B 98 -46.47 -150.96
REMARK 500 2 ALA B 99 55.65 -95.85
REMARK 500 3 SER A 10 -42.03 64.81
REMARK 500 3 ASN A 24 42.09 -102.65
REMARK 500 3 ARG A 71 -104.74 -104.78
REMARK 500 3 MET B 75 72.40 -155.98
REMARK 500 3 PRO B 77 32.21 -94.46
REMARK 500 3 ASP B 78 -166.85 -164.31
REMARK 500 3 PRO B 94 172.26 -57.95
REMARK 500 3 ALA B 95 28.65 -69.72
REMARK 500 3 GLU B 100 -130.38 -173.37
REMARK 500 3 HIS B 101 144.51 73.87
REMARK 500 3 ASN B 107 54.92 -115.33
REMARK 500 4 PHE A 6 69.32 -106.89
REMARK 500 4 VAL A 9 18.97 -164.28
REMARK 500 4 SER A 10 21.68 -77.16
REMARK 500 4 HIS A 11 13.94 58.37
REMARK 500 4 VAL A 12 25.10 43.88
REMARK 500 4 MET B 75 76.09 -155.59
REMARK 500 4 PRO B 77 34.47 -81.41
REMARK 500 4 ASP B 78 -168.66 -165.33
REMARK 500 4 ARG B 96 12.15 -157.24
REMARK 500 4 MET B 98 85.64 43.91
REMARK 500 4 ASN B 107 -7.66 73.43
REMARK 500 5 HIS A 8 91.82 20.57
REMARK 500 5 VAL A 9 -22.19 -163.77
REMARK 500 5 VAL A 12 19.02 50.27
REMARK 500 5 ARG A 71 -81.57 -112.92
REMARK 500 5 PRO B 77 32.57 -93.67
REMARK 500 5 ASP B 78 -168.38 -164.93
REMARK 500 5 ALA B 95 16.91 50.94
REMARK 500 6 MET A 3 93.57 64.02
REMARK 500 6 SER A 4 85.58 -154.27
REMARK 500 6 HIS A 11 -14.47 71.21
REMARK 500 6 VAL A 12 -68.91 62.18
REMARK 500 6 ASN A 18 -82.58 -87.20
REMARK 500
REMARK 500 THIS ENTRY HAS 159 RAMACHANDRAN OUTLIERS.
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 13 TYR A 53 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2K42 A 4 72 UNP P42768 WASP_HUMAN 242 310
DBREF 2K42 B 76 108 UNP Q8X2D5 Q8X2D5_ECO57 268 300
SEQADV 2K42 GLY A 1 UNP P42768 EXPRESSION TAG
SEQADV 2K42 HIS A 2 UNP P42768 EXPRESSION TAG
SEQADV 2K42 MET A 3 UNP P42768 EXPRESSION TAG
SEQADV 2K42 GLY B 73 UNP Q8X2D5 EXPRESSION TAG
SEQADV 2K42 HIS B 74 UNP Q8X2D5 EXPRESSION TAG
SEQADV 2K42 MET B 75 UNP Q8X2D5 EXPRESSION TAG
SEQRES 1 A 72 GLY HIS MET SER GLY PHE LYS HIS VAL SER HIS VAL GLY
SEQRES 2 A 72 TRP ASP PRO GLN ASN GLY PHE ASP VAL ASN ASN LEU ASP
SEQRES 3 A 72 PRO ASP LEU ARG SER LEU PHE SER ARG ALA GLY ILE SER
SEQRES 4 A 72 GLU ALA GLN LEU THR ASP ALA GLU THR SER LYS LEU ILE
SEQRES 5 A 72 TYR ASP PHE ILE GLU ASP GLN GLY GLY LEU GLU ALA VAL
SEQRES 6 A 72 ARG GLN GLU MET ARG ARG GLN
SEQRES 1 B 36 GLY HIS MET LEU PRO ASP VAL ALA GLN ARG LEU MET GLN
SEQRES 2 B 36 HIS LEU ALA GLU HIS GLY ILE GLN PRO ALA ARG ASN MET
SEQRES 3 B 36 ALA GLU HIS ILE PRO PRO ALA PRO ASN TRP
HELIX 1 1 ASP A 26 GLY A 37 1 12
HELIX 2 2 SER A 39 THR A 44 1 6
HELIX 3 3 ASP A 45 GLN A 59 1 15
HELIX 4 4 GLY A 61 ARG A 70 1 10
HELIX 5 5 ASP B 78 GLU B 89 1 12
SHEET 1 A 2 TRP A 14 ASP A 15 0
SHEET 2 A 2 GLY A 19 PHE A 20 -1 O GLY A 19 N ASP A 15
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
