HEADER LIGASE/SIGNALING PROTEIN 06-APR-06 2DJY
TITLE SOLUTION STRUCTURE OF SMURF2 WW3 DOMAIN-SMAD7 PY PEPTIDE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SMAD UBIQUITINATION REGULATORY FACTOR 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: WW3 DOMAIN;
COMPND 5 SYNONYM: UBIQUITIN--PROTEIN LIGASE SMURF2, SMAD-SPECIFIC E3 UBIQUITIN
COMPND 6 LIGASE 2, HSMURF2;
COMPND 7 EC: 6.3.2.-;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: MOTHERS AGAINST DECAPENTAPLEGIC HOMOLOG 7;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: PY MOTIF REGION;
COMPND 13 SYNONYM: SMAD 7, MOTHERS AGAINST DPP HOMOLOG 7, SMAD7, HSMAD7;
COMPND 14 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: SMURF2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX6P1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: SMAD7, MADH7, MADH8;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PGEX6P1
KEYWDS BETA SHEET, POLYPROLINE TYPE II HELIX, PPII, LIGASE-SIGNALING PROTEIN
KEYWDS 2 COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR P.A.CHONG,H LIN,J.L.WRANA,J.D.FORMAN-KAY
REVDAT 4 09-MAR-22 2DJY 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2DJY 1 VERSN
REVDAT 2 04-JUL-06 2DJY 1 JRNL
REVDAT 1 02-MAY-06 2DJY 0
JRNL AUTH P.A.CHONG,H.LIN,J.L.WRANA,J.D.FORMAN-KAY
JRNL TITL AN EXPANDED WW DOMAIN RECOGNITION MOTIF REVEALED BY THE
JRNL TITL 2 INTERACTION BETWEEN SMAD7 AND THE E3 UBIQUITIN LIGASE
JRNL TITL 3 SMURF2.
JRNL REF J.BIOL.CHEM. V. 281 17069 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16641086
JRNL DOI 10.1074/JBC.M601493200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 1.2
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DJY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000025503.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.3, NMRVIEW 5.2.2
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 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: 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: 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 PRO A 293 62.66 -67.48
REMARK 500 1 LEU A 294 -170.38 -61.51
REMARK 500 1 SER A 296 91.20 -65.11
REMARK 500 1 PRO A 300 -172.62 -52.03
REMARK 500 1 THR A 308 38.16 -91.22
REMARK 500 1 ALA A 309 -63.06 68.95
REMARK 500 1 ARG A 321 58.10 70.77
REMARK 500 1 GLN A 324 123.55 172.44
REMARK 500 1 LEU B 200 90.85 -65.09
REMARK 500 1 LEU B 204 -158.58 60.25
REMARK 500 1 SER B 206 -42.94 169.68
REMARK 500 1 PRO B 208 116.53 -39.98
REMARK 500 1 PRO B 209 -171.24 -46.88
REMARK 500 1 TYR B 211 -83.46 -58.32
REMARK 500 1 SER B 212 -80.49 61.41
REMARK 500 1 ARG B 213 -47.39 159.34
REMARK 500 2 PRO A 293 -173.54 -67.48
REMARK 500 2 LEU A 294 -43.87 -177.33
REMARK 500 2 PRO A 300 -179.76 -51.40
REMARK 500 2 THR A 308 45.48 -88.46
REMARK 500 2 ALA A 309 -68.68 66.36
REMARK 500 2 GLN A 324 151.58 177.82
REMARK 500 2 PHE A 325 40.49 -91.64
REMARK 500 2 LEU A 330 -80.01 -68.40
REMARK 500 2 SER B 202 -49.49 -136.86
REMARK 500 2 GLU B 203 -41.50 -169.30
REMARK 500 2 SER B 206 -46.93 177.08
REMARK 500 2 PRO B 208 117.25 -38.46
REMARK 500 2 PRO B 209 -171.91 -45.26
REMARK 500 2 TYR B 211 -80.23 -59.87
REMARK 500 2 SER B 212 -83.04 58.34
REMARK 500 2 ARG B 213 -35.82 162.79
REMARK 500 3 SER A 296 -67.51 -126.51
REMARK 500 3 PRO A 300 -178.05 -62.93
REMARK 500 3 ALA A 309 -65.86 175.72
REMARK 500 3 ARG A 321 64.21 66.55
REMARK 500 3 ALA A 332 39.26 -175.31
REMARK 500 3 SER B 202 63.05 -168.93
REMARK 500 3 GLU B 203 -47.52 -161.44
REMARK 500 3 PRO B 208 115.88 -37.48
REMARK 500 3 PRO B 209 -172.08 -45.00
REMARK 500 3 TYR B 211 -87.05 -47.43
REMARK 500 3 SER B 212 -161.87 49.52
REMARK 500 4 SER A 296 91.69 -49.85
REMARK 500 4 PRO A 298 -169.91 -52.04
REMARK 500 4 PRO A 300 177.90 -55.37
REMARK 500 4 THR A 308 41.73 -89.00
REMARK 500 4 ALA A 309 -68.18 68.14
REMARK 500 4 GLN A 324 140.55 174.44
REMARK 500 4 GLU B 203 -80.11 61.73
REMARK 500
REMARK 500 THIS ENTRY HAS 454 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2DJY A 297 333 UNP Q9HAU4 SMUF2_HUMAN 297 333
DBREF 2DJY B 203 217 UNP O15105 SMAD7_HUMAN 203 217
SEQADV 2DJY GLY A 292 UNP Q9HAU4 CLONING ARTIFACT
SEQADV 2DJY PRO A 293 UNP Q9HAU4 CLONING ARTIFACT
SEQADV 2DJY LEU A 294 UNP Q9HAU4 CLONING ARTIFACT
SEQADV 2DJY GLY A 295 UNP Q9HAU4 CLONING ARTIFACT
SEQADV 2DJY SER A 296 UNP Q9HAU4 CLONING ARTIFACT
SEQADV 2DJY GLY B 198 UNP O15105 CLONING ARTIFACT
SEQADV 2DJY PRO B 199 UNP O15105 CLONING ARTIFACT
SEQADV 2DJY LEU B 200 UNP O15105 CLONING ARTIFACT
SEQADV 2DJY GLY B 201 UNP O15105 CLONING ARTIFACT
SEQADV 2DJY SER B 202 UNP O15105 CLONING ARTIFACT
SEQRES 1 A 42 GLY PRO LEU GLY SER GLY PRO LEU PRO PRO GLY TRP GLU
SEQRES 2 A 42 ILE ARG ASN THR ALA THR GLY ARG VAL TYR PHE VAL ASP
SEQRES 3 A 42 HIS ASN ASN ARG THR THR GLN PHE THR ASP PRO ARG LEU
SEQRES 4 A 42 SER ALA ASN
SEQRES 1 B 20 GLY PRO LEU GLY SER GLU LEU GLU SER PRO PRO PRO PRO
SEQRES 2 B 20 TYR SER ARG TYR PRO MET ASP
SHEET 1 A 3 TRP A 303 ASN A 307 0
SHEET 2 A 3 VAL A 313 ASP A 317 -1 O VAL A 316 N GLU A 304
SHEET 3 A 3 THR A 322 GLN A 324 -1 O GLN A 324 N PHE A 315
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
