HEADER PROTEIN BINDING 27-JUN-02 1M3A
TITLE SOLUTION STRUCTURE OF A CIRCULAR FORM OF THE TRUNCATED N-TERMINAL SH3
TITLE 2 DOMAIN FROM ONCOGENE PROTEIN C-CRK.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTO-ONCOGENE C-CRK;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL SH3 DOMAIN (RESIDUES 135-191);
COMPND 5 SYNONYM: P38, ADAPTER MOLECULE CRK;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: CRK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1
KEYWDS SH3, SH3 DOMAIN, CIRCULAR PROTEIN, CYCLIZED PROTEIN, ADAPTOR PROTEIN,
KEYWDS 2 PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.H.SCHUMANN,R.VARADAN,P.P.TAYAKUNIYIL,J.B.HALL,J.A.CAMARERO,
AUTHOR 2 D.FUSHMAN
REVDAT 3 27-OCT-21 1M3A 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1M3A 1 VERSN
REVDAT 1 05-AUG-03 1M3A 0
JRNL AUTH F.H.SCHUMANN,R.VARADAN,P.P.TAYAKUNIYIL,J.B.HALL,
JRNL AUTH 2 J.A.CAMARERO,D.FUSHMAN
JRNL TITL CHANGING PROTEIN BACKBONE TOPOLOGY: STRUCTURAL AND DYNAMIC
JRNL TITL 2 CONSEQUENCES OF THE BACKBONE CYCLIZATION IN SH3 DOMAIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.A.CAMARERO,D.FUSHMAN,S.SATO,I.GIRIAT,D.COWBURN,
REMARK 1 AUTH 2 D.P.RALEIGH,T.W.MUIR
REMARK 1 TITL RESCUING A DESTABILIZED PROTEIN FOLD THROUGH BACKBONE
REMARK 1 TITL 2 CYCLIZATION
REMARK 1 REF J.MOL.BIOL. V. 308 1045 2001
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.2001.4631
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, 3.0, DYANA
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, WUETHRICH (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1090
REMARK 3 RESTRAINTS, 993 ARE NOE-DERIVED DISTANCE CONTRAINTS, 25 DIHEDRAL
REMARK 3 ANGLE CONSTRAINTS, AND 72 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS. STRUCTURES WERE CALCULATED USING PROGRAM DYANA. NO
REMARK 3 FURTHER REFINEMENT WAS PERFORMED.
REMARK 4
REMARK 4 1M3A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-02.
REMARK 100 THE DEPOSITION ID IS D_1000016543.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 307
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM SH3 NA, 20MM SODIUM
REMARK 210 PHOSPHATE, 20 MM DTT-D10, 100 MM
REMARK 210 NACL, 0.1% (W/V) NAN3; 1MM SH3 U-
REMARK 210 15N, 20MM SODIUM PHOSPHATE, 20
REMARK 210 MM DTT-D10, 100 MM NACL, 0.1% (W/
REMARK 210 V) NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY; 2D
REMARK 210 HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.1.3, DYANA 1.6
REMARK 210 METHOD USED : SIMULATED ANNEALING COMBINED
REMARK 210 WITH TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES COMBINED WITH 2D 1H-15N HSQC DATA.
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 168 H VAL A 184 1.56
REMARK 500 O ALA A 139 H GLY A 156 1.59
REMARK 500 O PHE A 143 H PHE A 153 1.60
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 PHE A 143 102.85 -177.16
REMARK 500 1 ASN A 146 84.65 171.32
REMARK 500 1 ASP A 147 -75.08 -109.77
REMARK 500 1 PHE A 153 -175.59 -173.83
REMARK 500 1 LYS A 155 110.88 -37.54
REMARK 500 1 GLN A 168 -40.17 -172.35
REMARK 500 2 GLU A 149 38.31 171.37
REMARK 500 2 GLN A 168 -43.19 -157.84
REMARK 500 3 PHE A 143 102.30 -178.55
REMARK 500 3 ASN A 146 -72.41 172.64
REMARK 500 3 ASP A 147 -81.70 62.73
REMARK 500 3 ASP A 150 143.53 170.38
REMARK 500 3 LYS A 155 107.51 -32.58
REMARK 500 3 LYS A 164 65.29 -165.13
REMARK 500 3 GLN A 168 -32.12 173.64
REMARK 500 4 ASN A 146 36.86 -178.20
REMARK 500 4 ASP A 147 -72.58 -135.51
REMARK 500 4 GLU A 148 39.31 -140.54
REMARK 500 4 ASP A 150 163.44 -45.27
REMARK 500 4 LYS A 164 71.14 -165.85
REMARK 500 4 GLN A 168 -40.05 -152.13
REMARK 500 5 GLU A 148 -22.56 88.84
REMARK 500 5 LYS A 155 108.07 -42.90
REMARK 500 5 GLN A 168 -33.84 174.41
REMARK 500 5 ASP A 174 -157.03 -95.85
REMARK 500 5 LYS A 178 108.28 -49.62
REMARK 500 5 TYR A 190 -64.70 -96.42
REMARK 500 6 ASN A 146 -56.04 -151.65
REMARK 500 6 GLU A 148 40.37 -79.48
REMARK 500 6 GLU A 149 -31.05 -146.76
REMARK 500 6 LYS A 155 135.49 -38.32
REMARK 500 6 LYS A 164 76.14 -155.19
REMARK 500 6 GLN A 168 -45.73 -155.31
REMARK 500 7 ASN A 146 74.85 160.48
REMARK 500 7 GLU A 148 25.19 -77.65
REMARK 500 7 GLU A 149 18.71 -153.64
REMARK 500 7 LYS A 178 109.04 -46.74
REMARK 500 8 ASN A 146 82.89 154.12
REMARK 500 8 GLU A 149 49.09 -141.27
REMARK 500 9 PHE A 143 139.57 -177.50
REMARK 500 9 ASN A 146 -17.07 152.76
REMARK 500 9 ASP A 147 -162.89 86.67
REMARK 500 9 GLU A 148 38.56 35.20
REMARK 500 9 GLU A 149 -25.68 168.30
REMARK 500 9 LYS A 164 66.63 -160.15
REMARK 500 9 GLN A 168 -37.99 -175.66
REMARK 500 10 ASN A 146 -52.56 -179.40
REMARK 500 10 LYS A 155 128.21 -39.27
REMARK 500 10 GLN A 168 -42.59 -146.55
REMARK 500 11 PHE A 143 98.05 -173.78
REMARK 500
REMARK 500 THIS ENTRY HAS 102 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1M30 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF N-TERMINAL SH3 DOMAIN FROM ONCOGENE PROTEIN C-
REMARK 900 CRK
REMARK 900 RELATED ID: 1M3B RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF A CIRCULAR FORM OF THE N-TERMINAL SH3 DOMAIN
REMARK 900 (A134C,E135G MUTANT) FROM ONCOGENE PROTEIN C-CRK.
REMARK 900 RELATED ID: 1M3C RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF A CIRCULAR FORM OF THE N-TERMINAL SH3 DOMAIN
REMARK 900 FROM ONCOGENE PROTEIN C-CRK
DBREF 1M3A A 135 191 UNP Q64010 CRK_MOUSE 135 191
SEQADV 1M3A CYS A 135 UNP Q64010 GLU 135 ENGINEERED MUTATION
SEQADV 1M3A GLY A 191 UNP Q64010 ARG 191 ENGINEERED MUTATION
SEQRES 1 A 57 CYS TYR VAL ARG ALA LEU PHE ASP PHE ASN GLY ASN ASP
SEQRES 2 A 57 GLU GLU ASP LEU PRO PHE LYS LYS GLY ASP ILE LEU ARG
SEQRES 3 A 57 ILE ARG ASP LYS PRO GLU GLU GLN TRP TRP ASN ALA GLU
SEQRES 4 A 57 ASP SER GLU GLY LYS ARG GLY MET ILE PRO VAL PRO TYR
SEQRES 5 A 57 VAL GLU LYS TYR GLY
SHEET 1 A 5 ARG A 179 PRO A 183 0
SHEET 2 A 5 TRP A 169 GLU A 173 -1 N TRP A 170 O ILE A 182
SHEET 3 A 5 ASP A 157 ASP A 163 -1 N ARG A 160 O GLU A 173
SHEET 4 A 5 TYR A 136 ALA A 139 -1 N VAL A 137 O LEU A 159
SHEET 5 A 5 VAL A 187 GLY A 191 -1 O TYR A 190 N TYR A 136
LINK N CYS A 135 C GLY A 191 1555 1555 1.52
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
