HEADER SIGNALING PROTEIN/TRANSCRIPTION 22-MAR-11 2LAY
TITLE STRUCTURE OF THE FIRST WW DOMAIN OF HUMAN YAP IN COMPLEX WITH A
TITLE 2 PHOSPHORYLATED HUMAN SMAD1 DERIVED PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: YORKIE HOMOLOG;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 170-205;
COMPND 5 SYNONYM: 65 KDA YES-ASSOCIATED PROTEIN, YAP65;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: MOTHERS AGAINST DECAPENTAPLEGIC HOMOLOG 1;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: RESIDUES 201-209;
COMPND 11 SYNONYM: MAD HOMOLOG 1, MOTHERS AGAINST DPP HOMOLOG 1, JV4-1, MAD-
COMPND 12 RELATED PROTEIN 1, SMAD FAMILY MEMBER 1, SMAD 1, SMAD1, HSMAD1,
COMPND 13 TRANSFORMING GROWTH FACTOR-BETA-SIGNALING PROTEIN 1, BSP-1;
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: YAP1, YAP65;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PETM11;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS YAP, SMAD, CDK, SIGNAL TRANSDUCTION, SIGNALING PROTEIN-TRANSCRIPTION
KEYWDS 2 COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.J.MACIAS,E.ARAGON,N.GOERNER,A.ZAROMYTIDOU,Q.XI,A.ESCOBEDO,
AUTHOR 2 J.MASSAGUE
REVDAT 1 06-JUL-11 2LAY 0
JRNL AUTH E.ARAGON,N.GOERNER,A.I.ZAROMYTIDOU,Q.XI,A.ESCOBEDO,
JRNL AUTH 2 J.MASSAGUE,M.J.MACIAS
JRNL TITL A SMAD ACTION TURNOVER SWITCH OPERATED BY WW DOMAIN READERS
JRNL TITL 2 OF A PHOSPHOSERINE CODE.
JRNL REF GENES DEV. V. 25 1275 2011
JRNL REFN ISSN 0890-9369
JRNL PMID 21685363
JRNL DOI 10.1101/GAD.2060811
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,
REMARK 3 JIANG,KUSZEWSKI,NILGES,PANNU,READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2LAY COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-11.
REMARK 100 THE RCSB ID CODE IS RCSB102174.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 285
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 0.420
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM NEDD4LWW3, 3 MM SMAD3, 20
REMARK 210 MM SODIUM PHOSPHATE, 100 MM
REMARK 210 SODIUM CHLORIDE, 2 MM SODIUM
REMARK 210 AZIDE, 90% H2O/10% D2O; 1 MM [U-
REMARK 210 100% 15N] NEDD4LWW3, 3 MM SMAD3,
REMARK 210 20 MM SODIUM PHOSPHATE, 100 MM
REMARK 210 SODIUM CHLORIDE, 2 MM SODIUM
REMARK 210 AZIDE, 90% H2O/10% D2O; 1 MM [U-
REMARK 210 100% 13C; U-100% 15N] NEDD4LWW3,
REMARK 210 3 MM SMAD3, 20 MM SODIUM
REMARK 210 PHOSPHATE, 100 MM SODIUM
REMARK 210 CHLORIDE, 2 MM SODIUM AZIDE, 90%
REMARK 210 H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-1H NOESY; 2D 1H-1H TOCSY;
REMARK 210 3D CBCA(CO)NH; 3D HNCACB; 2D 1H-
REMARK 210 15N HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.3, XEASY, TOPSPIN, NMRPIPE
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY
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 HZ2 TRP A 177 HB2 PHE A 189 1.48
REMARK 500 HB3 GLU A 178 HB2 LEU A 190 1.50
REMARK 500 HG22 THR A 198 H GLN A 200 1.52
REMARK 500 HE1 TRP A 199 HG2 PRO B 207 1.53
REMARK 500 HH2 TRP A 177 HB THR A 198 1.55
REMARK 500 HE2 TYR A 188 HG2 PRO B 204 1.56
REMARK 500 HB2 PRO B 204 H HIS B 205 1.57
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 B 204 -141.41 -90.19
REMARK 500 2 THR B 202 15.81 -140.88
REMARK 500 2 PRO B 204 -125.79 -79.01
REMARK 500 2 HIS B 205 25.29 -150.03
REMARK 500 2 SEP B 206 150.29 54.59
REMARK 500 3 PRO B 204 -135.79 -85.44
REMARK 500 4 PRO B 204 -133.42 -83.10
REMARK 500 4 SEP B 206 159.39 54.61
REMARK 500 5 PRO B 204 -111.02 -84.92
REMARK 500 6 LEU A 173 -72.68 -98.45
REMARK 500 6 PRO B 204 -126.64 -69.70
REMARK 500 6 SEP B 206 140.02 60.28
REMARK 500 7 THR B 202 20.93 -150.02
REMARK 500 7 PRO B 204 -156.61 -84.53
REMARK 500 7 PRO B 207 -71.96 -46.13
REMARK 500 7 THR B 208 -158.05 -132.70
REMARK 500 8 PRO B 204 -133.47 -76.62
REMARK 500 8 HIS B 205 43.37 -148.48
REMARK 500 8 SEP B 206 145.15 61.87
REMARK 500 9 PRO B 204 -108.56 -91.46
REMARK 500 10 PRO B 204 -145.68 -91.11
REMARK 500 11 TRP A 177 -167.73 -169.61
REMARK 500 11 ASP A 201 103.92 58.46
REMARK 500 11 PRO B 204 -114.60 -84.88
REMARK 500 12 PRO B 204 -145.85 -84.32
REMARK 500 12 SEP B 206 141.86 64.90
REMARK 500 13 PRO B 204 -144.12 -74.94
REMARK 500 14 PRO A 172 -9.92 -58.84
REMARK 500 14 HIS A 192 3.58 -69.36
REMARK 500 14 ASP A 201 99.61 62.57
REMARK 500 14 PRO B 204 -158.54 -82.79
REMARK 500 15 GLN A 195 74.59 55.54
REMARK 500 15 PRO B 204 -139.43 -81.52
REMARK 500 16 TRP A 177 -169.11 -160.24
REMARK 500 16 PRO B 204 -131.62 -84.93
REMARK 500 16 HIS B 205 27.15 -143.24
REMARK 500 16 SEP B 206 132.32 53.45
REMARK 500 17 GLN A 195 32.58 70.18
REMARK 500 17 LYS A 204 -72.91 -74.23
REMARK 500 17 PRO B 204 -154.75 -90.71
REMARK 500 18 PRO B 204 -124.15 -85.58
REMARK 500 18 HIS B 205 20.08 -149.88
REMARK 500 18 SEP B 206 144.54 56.49
REMARK 500 18 PRO B 207 -75.14 -64.44
REMARK 500 18 THR B 208 84.45 -150.23
REMARK 500 19 HIS A 192 1.63 -68.40
REMARK 500 19 PRO B 204 -121.03 -83.56
REMARK 500 20 THR B 202 -44.34 -150.02
REMARK 500 20 PRO B 204 -110.65 -62.20
REMARK 500 20 HIS B 205 3.11 -150.06
REMARK 500
REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 17540 RELATED DB: BMRB
REMARK 900 RELATED ID: 2LAW RELATED DB: PDB
REMARK 900 RELATED ID: 2LAX RELATED DB: PDB
REMARK 900 RELATED ID: 2LAZ RELATED DB: PDB
REMARK 900 RELATED ID: 2LB0 RELATED DB: PDB
REMARK 900 RELATED ID: 2LB1 RELATED DB: PDB
REMARK 900 RELATED ID: 2LB2 RELATED DB: PDB
REMARK 900 RELATED ID: 2LB3 RELATED DB: PDB
DBREF 2LAY A 170 205 UNP P46937 YAP1_HUMAN 170 205
DBREF 2LAY B 201 209 UNP Q15797 SMAD1_HUMAN 201 209
SEQRES 1 A 36 ASP VAL PRO LEU PRO ALA GLY TRP GLU MET ALA LYS THR
SEQRES 2 A 36 SER SER GLY GLN ARG TYR PHE LEU ASN HIS ILE ASP GLN
SEQRES 3 A 36 THR THR THR TRP GLN ASP PRO ARG LYS ALA
SEQRES 1 B 9 SER THR TYR PRO HIS SEP PRO THR SER
MODRES 2LAY SEP B 206 SER PHOSPHOSERINE
HET SEP B 206 14
HETNAM SEP PHOSPHOSERINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 2 SEP C3 H8 N O6 P
SHEET 1 A 3 TRP A 177 THR A 182 0
SHEET 2 A 3 GLN A 186 ASN A 191 -1 O LEU A 190 N GLU A 178
SHEET 3 A 3 THR A 196 THR A 198 -1 O THR A 196 N ASN A 191
LINK C HIS B 205 N SEP B 206 1555 1555 1.33
LINK C SEP B 206 N PRO B 207 1555 1555 1.35
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
