HEADER TRANSLATION REGULATOR 07-FEB-14 2MKJ
TITLE SOLUTION STRUCTURE OF TANDEM RRM DOMAINS OF CYTOPLASMIC
TITLE 2 POLYADENYLATION ELEMENT BINDING PROTEIN 4 (CPEB4) IN FREE STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOPLASMIC POLYADENYLATION ELEMENT-BINDING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 53-254;
COMPND 5 SYNONYM: CPE-BP4, CPE-BINDING PROTEIN 4, HCPEB-4;
COMPND 6 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: CPEB4, KIAA1673;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET28A(+)
KEYWDS CPEB4, RNA RECOGNITION MOTIF (RRM), CYTOPLASMIC POLYADENYLATION,
KEYWDS 2 TRANSLATIONAL REGULATION, TRANSLATION REGULATOR
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.AFROZ,L.SKRISOVSKA,E.BELLOC,J.G.BOIXET,R.MENDEZ,F.H.-T.ALLAIN
REVDAT 3 14-JUN-23 2MKJ 1 REMARK
REVDAT 2 27-APR-16 2MKJ 1 DBREF SEQRES
REVDAT 1 23-JUL-14 2MKJ 0
JRNL AUTH T.AFROZ,L.SKRISOVSKA,E.BELLOC,J.GUILLEN-BOIXET,R.MENDEZ,
JRNL AUTH 2 F.H.-T.ALLAIN
JRNL TITL A FLY TRAP MECHANISM PROVIDES SEQUENCE-SPECIFIC RNA
JRNL TITL 2 RECOGNITION BY CPEB PROTEINS
JRNL REF GENES DEV. V. 28 1498 2014
JRNL REFN ISSN 0890-9369
JRNL PMID 24990967
JRNL DOI 10.1101/GAD.241133.114
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : CASE, DARDEN, CHEATHAM, III, SIMMERLING, WANG,
REMARK 3 DUKE, LUO, ... AND KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2MKJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000103724.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 0.15
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.4-0.6 MM [U-100% 13C; U-100%
REMARK 210 15N] CPEB4RRM12-1, 100 MM SODIUM
REMARK 210 CHLORIDE-2, 50 MM SODIUM
REMARK 210 PHOSPHATE-3, 1 MM DTT-4, 90% H2O/
REMARK 210 10% D2O; 0.4-0.6 MM [U-100% 13C;
REMARK 210 U-100% 15N; U-80% 2H] CPEB4RRM12-
REMARK 210 5, 100 MM SODIUM CHLORIDE-6, 50
REMARK 210 MM SODIUM PHOSPHATE-7, 1 MM DTT-
REMARK 210 8, 90% H2O/10% D2O; 0.4-0.6 MM
REMARK 210 [U-100% 15N] CPEB4RRM12-9, 100
REMARK 210 MM SODIUM CHLORIDE-10, 50 MM
REMARK 210 SODIUM PHOSPHATE-11, 1 MM DTT-12,
REMARK 210 90% H2O/10% D2O; 0.4-0.6 MM [U-
REMARK 210 100% 15N] CPEB4RRM12-13, 100 MM
REMARK 210 SODIUM CHLORIDE-14, 50 MM SODIUM
REMARK 210 PHOSPHATE-15, 1 MM DTT-16, 100%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D TROSY; 2D 1H
REMARK 210 -13C HSQC; 2D 1H-13C HSQC
REMARK 210 ALIPHATIC; 2D 1H-13C HSQC
REMARK 210 AROMATIC; 2D 1H-1H TOCSY; 2D 1H-
REMARK 210 1H NOESY; 3D CBCA(CO)NH; 3D
REMARK 210 TRHNCACB; 3D TRHN(CO)CA; 3D
REMARK 210 TRHNCO; 3D TRHCACO; 3D HCCH-
REMARK 210 TOCSY; 3D 1H-15N NOESY; 3D 1H-
REMARK 210 13C NOESY ALIPHATIC; 3D 1H-13C
REMARK 210 NOESY AROMATIC
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 700 MHZ; 600 MHZ; 500
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA, SPARKY, TOPSPIN
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 LEU A 255
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 GLN A 55 -32.64 -151.84
REMARK 500 1 ARG A 87 -17.22 60.65
REMARK 500 1 LYS A 98 12.19 -156.20
REMARK 500 1 LYS A 102 -54.24 -151.11
REMARK 500 1 CYS A 138 39.70 -90.77
REMARK 500 1 SER A 140 109.55 -54.17
REMARK 500 1 SER A 141 -44.88 -167.25
REMARK 500 1 PRO A 142 -145.75 -75.08
REMARK 500 1 THR A 143 9.95 -66.11
REMARK 500 1 ASP A 146 12.57 54.20
REMARK 500 1 SER A 159 -3.18 -50.17
REMARK 500 1 MET A 163 -30.29 -134.87
REMARK 500 1 ALA A 186 13.24 -69.85
REMARK 500 1 TYR A 197 42.28 -140.91
REMARK 500 1 ALA A 217 -165.06 -55.95
REMARK 500 1 SER A 223 26.00 -148.92
REMARK 500 1 ASP A 245 -32.27 -131.51
REMARK 500 2 ARG A 59 172.18 60.56
REMARK 500 2 PRO A 73 155.71 -49.82
REMARK 500 2 ARG A 87 -1.81 -141.84
REMARK 500 2 PRO A 90 10.31 -64.95
REMARK 500 2 LYS A 98 11.87 -144.48
REMARK 500 2 LYS A 108 13.16 51.91
REMARK 500 2 PRO A 142 -5.05 -54.85
REMARK 500 2 ILE A 144 -25.47 -143.28
REMARK 500 2 LYS A 147 161.36 62.04
REMARK 500 2 LEU A 156 6.88 -69.73
REMARK 500 2 SER A 159 -18.26 -43.82
REMARK 500 2 MET A 163 -0.19 -140.02
REMARK 500 2 ASP A 164 169.62 59.54
REMARK 500 2 ARG A 185 46.80 -93.82
REMARK 500 2 LEU A 196 -72.88 -103.77
REMARK 500 2 CYS A 201 -50.93 -153.37
REMARK 500 2 ALA A 217 176.48 59.39
REMARK 500 2 PHE A 222 28.35 -158.90
REMARK 500 2 ASN A 224 -3.53 -147.51
REMARK 500 2 GLN A 238 -77.76 -84.20
REMARK 500 2 LEU A 239 163.81 59.62
REMARK 500 2 ARG A 247 117.60 56.01
REMARK 500 3 ARG A 59 18.49 56.03
REMARK 500 3 PHE A 85 63.90 -106.29
REMARK 500 3 ARG A 86 1.55 -68.93
REMARK 500 3 SER A 103 165.96 56.39
REMARK 500 3 TYR A 104 15.12 -142.64
REMARK 500 3 LYS A 108 18.54 -155.29
REMARK 500 3 SER A 141 -45.95 -158.02
REMARK 500 3 ASP A 146 -92.82 -151.87
REMARK 500 3 ASN A 155 56.50 -91.34
REMARK 500 3 PRO A 181 176.87 -57.03
REMARK 500 3 ALA A 186 8.96 -68.40
REMARK 500
REMARK 500 THIS ENTRY HAS 371 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 19777 RELATED DB: BMRB
REMARK 900 RELATED ID: 2MKE RELATED DB: PDB
REMARK 900 RELATED ID: 2MKH RELATED DB: PDB
REMARK 900 RELATED ID: 2MKI RELATED DB: PDB
REMARK 900 RELATED ID: 2MKK RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS PROTEIN SEQUENCE IS ISOFORM 3 OF CPEB4_HUMAN.
DBREF 2MKJ A 53 255 UNP Q17RY0 CPEB4_HUMAN 53 255
SEQRES 1 A 203 SER HIS GLN ASN GLY GLU ARG VAL GLU ARG TYR SER ARG
SEQRES 2 A 203 LYS VAL PHE VAL GLY GLY LEU PRO PRO ASP ILE ASP GLU
SEQRES 3 A 203 ASP GLU ILE THR ALA SER PHE ARG ARG PHE GLY PRO LEU
SEQRES 4 A 203 ILE VAL ASP TRP PRO HIS LYS ALA GLU SER LYS SER TYR
SEQRES 5 A 203 PHE PRO PRO LYS GLY TYR ALA PHE LEU LEU PHE GLN ASP
SEQRES 6 A 203 GLU SER SER VAL GLN ALA LEU ILE ASP ALA CYS ILE GLU
SEQRES 7 A 203 GLU ASP GLY LYS LEU TYR LEU CYS VAL SER SER PRO THR
SEQRES 8 A 203 ILE LYS ASP LYS PRO VAL GLN ILE ARG PRO TRP ASN LEU
SEQRES 9 A 203 SER ASP SER ASP PHE VAL MET ASP GLY SER GLN PRO LEU
SEQRES 10 A 203 ASP PRO ARG LYS THR ILE PHE VAL GLY GLY VAL PRO ARG
SEQRES 11 A 203 PRO LEU ARG ALA VAL GLU LEU ALA MET ILE MET ASP ARG
SEQRES 12 A 203 LEU TYR GLY GLY VAL CYS TYR ALA GLY ILE ASP THR ASP
SEQRES 13 A 203 PRO GLU LEU LYS TYR PRO LYS GLY ALA GLY ARG VAL ALA
SEQRES 14 A 203 PHE SER ASN GLN GLN SER TYR ILE ALA ALA ILE SER ALA
SEQRES 15 A 203 ARG PHE VAL GLN LEU GLN HIS GLY GLU ILE ASP LYS ARG
SEQRES 16 A 203 VAL GLU VAL LYS PRO TYR VAL LEU
HELIX 1 1 ASP A 77 PHE A 85 1 9
HELIX 2 2 SER A 119 ALA A 127 1 9
HELIX 3 3 ALA A 186 TYR A 197 1 12
HELIX 4 4 GLN A 225 SER A 233 1 9
SHEET 1 A 6 LEU A 91 ASP A 94 0
SHEET 2 A 6 ALA A 111 PHE A 115 -1 O LEU A 114 N ILE A 92
SHEET 3 A 6 SER A 64 VAL A 69 -1 N VAL A 69 O ALA A 111
SHEET 4 A 6 VAL A 149 TRP A 154 -1 O TRP A 154 N SER A 64
SHEET 5 A 6 LEU A 135 LEU A 137 -1 N LEU A 135 O ILE A 151
SHEET 6 A 6 ILE A 129 GLU A 130 -1 N ILE A 129 O TYR A 136
SHEET 1 B 5 ASP A 160 VAL A 162 0
SHEET 2 B 5 TYR A 202 ASP A 208 -1 O ALA A 203 N PHE A 161
SHEET 3 B 5 TYR A 213 ALA A 221 -1 O ALA A 217 N ASP A 206
SHEET 4 B 5 THR A 174 GLY A 178 -1 N ILE A 175 O VAL A 220
SHEET 5 B 5 GLU A 249 PRO A 252 -1 O LYS A 251 N PHE A 176
SHEET 1 C 2 GLN A 238 HIS A 241 0
SHEET 2 C 2 ILE A 244 LYS A 246 -1 O ASP A 245 N LEU A 239
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