HEADER TRANSLATION REGULATOR 06-FEB-14 2MKE
TITLE SOLUTION STRUCTURE OF CPEB1 ZZ DOMAIN IN THE FREE STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOPLASMIC POLYADENYLATION ELEMENT-BINDING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 426-486;
COMPND 5 SYNONYM: CPE-BP1, CPE-BINDING PROTEIN 1, H-CEBP, HCPEB-1;
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: CPEB1, CPEB;
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 CPEB1, CPEB4, RRM, CYTOPLASMIC POLYADENYLATION ELEMENT, TRANSLATION
KEYWDS 2 REGULATION, TRANSLATION REGULATOR
EXPDTA SOLUTION NMR
NUMMDL 26
AUTHOR T.AFROZ,L.SKRISOVSKA,E.BELLOC,J.G.BOIXET,R.MENDEZ,F.H.-T.ALLAIN
REVDAT 1 23-JUL-14 2MKE 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 2MKE 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 RCSB ID CODE IS RCSB103719.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
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] CPEB1ZZ-1, 0.4-0.6 MM [U-
REMARK 210 100% 15N] CPEB1ZZ-2, 90% H2O/10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 2D 1H-13C HSQC ALIPHATIC; 2D 1H-
REMARK 210 13C HSQC AROMATIC; 2D 1H-1H
REMARK 210 TOCSY; 3D CBCA(CO)NH; 3D HNCO; 3D
REMARK 210 HNCA; 3D HNCACB; 3D HCCH-TOCSY;
REMARK 210 3D 1H-15N NOESY; 3D 1H-13C NOESY
REMARK 210 ALIPHATIC; 3D 1H-13C NOESY
REMARK 210 AROMATIC; 2D 1H-1H NOESY
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 : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 26
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST 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 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 SER A 439 33.80 39.89
REMARK 500 2 SER A 439 35.43 39.65
REMARK 500 2 PRO A 442 5.39 -63.82
REMARK 500 2 PHE A 453 27.82 -157.14
REMARK 500 2 ARG A 478 12.78 55.72
REMARK 500 3 SER A 439 41.89 39.95
REMARK 500 3 PHE A 453 18.22 -150.98
REMARK 500 4 PRO A 442 18.93 -69.85
REMARK 500 4 PHE A 453 20.71 -150.79
REMARK 500 4 ARG A 483 11.08 -145.70
REMARK 500 5 SER A 433 23.28 -144.42
REMARK 500 5 SER A 439 26.95 40.49
REMARK 500 5 CYS A 452 43.04 -148.89
REMARK 500 5 PHE A 453 43.02 -73.84
REMARK 500 6 SER A 439 21.56 45.87
REMARK 500 6 ARG A 448 75.43 -111.77
REMARK 500 6 PHE A 453 23.86 -147.93
REMARK 500 7 SER A 439 28.15 42.57
REMARK 500 7 CYS A 452 40.89 -150.66
REMARK 500 8 TYR A 429 17.32 56.39
REMARK 500 8 SER A 439 26.27 46.22
REMARK 500 8 PRO A 442 5.53 -57.56
REMARK 500 8 PHE A 453 27.27 46.28
REMARK 500 9 CYS A 438 -17.39 -144.73
REMARK 500 9 PRO A 442 28.93 -67.71
REMARK 500 9 PHE A 453 28.79 -156.45
REMARK 500 10 CYS A 438 -17.60 -142.24
REMARK 500 10 PRO A 442 8.78 -56.96
REMARK 500 10 CYS A 452 40.17 -146.76
REMARK 500 10 PHE A 453 47.64 -75.15
REMARK 500 11 PRO A 428 -8.35 -59.42
REMARK 500 11 SER A 439 27.41 41.61
REMARK 500 11 PRO A 442 -9.45 -56.11
REMARK 500 11 CYS A 452 -69.94 -120.72
REMARK 500 11 ARG A 471 0.60 -68.96
REMARK 500 12 PRO A 442 24.00 -69.42
REMARK 500 12 CYS A 452 35.94 -149.04
REMARK 500 12 PHE A 453 22.62 -68.84
REMARK 500 12 SER A 485 11.26 -141.53
REMARK 500 13 CYS A 452 36.31 -146.93
REMARK 500 13 PHE A 453 34.61 -73.72
REMARK 500 14 ASP A 432 32.93 -77.24
REMARK 500 14 SER A 439 48.14 35.96
REMARK 500 14 PHE A 453 25.71 47.93
REMARK 500 14 ARG A 478 16.53 55.58
REMARK 500 15 PRO A 442 6.94 -62.45
REMARK 500 15 CYS A 452 32.28 -146.19
REMARK 500 15 PHE A 453 38.14 -75.37
REMARK 500 15 ARG A 478 19.99 54.07
REMARK 500 16 PRO A 442 29.82 -71.55
REMARK 500
REMARK 500 THIS ENTRY HAS 97 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 ZN A 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 447 SG
REMARK 620 2 HIS A 465 NE2 117.1
REMARK 620 3 CYS A 452 SG 114.6 110.1
REMARK 620 4 HIS A 473 ND1 111.1 91.6 110.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 ZN A 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 438 SG
REMARK 620 2 CYS A 460 SG 111.7
REMARK 620 3 CYS A 457 SG 109.2 103.2
REMARK 620 4 CYS A 435 SG 111.5 110.2 110.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 19771 RELATED DB: BMRB
REMARK 900 RELATED ID: 2MKH RELATED DB: PDB
REMARK 900 RELATED ID: 2MKI RELATED DB: PDB
REMARK 900 RELATED ID: 2MKJ RELATED DB: PDB
REMARK 900 RELATED ID: 2MKK RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE RESIDUE NUMBERS ARE BASED ON ISOFORM 4 OF CPEB1_HUMAN.
DBREF 2MKE A 426 486 UNP Q9BZB8 CPEB1_HUMAN 426 486
SEQRES 1 A 61 ILE ASP PRO TYR LEU GLU ASP SER LEU CYS HIS ILE CYS
SEQRES 2 A 61 SER SER GLN PRO GLY PRO PHE PHE CYS ARG ASP GLN VAL
SEQRES 3 A 61 CYS PHE LYS TYR PHE CYS ARG SER CYS TRP HIS TRP ARG
SEQRES 4 A 61 HIS SER MET GLU GLY LEU ARG HIS HIS SER PRO LEU MET
SEQRES 5 A 61 ARG ASN GLN LYS ASN ARG ASP SER SER
HET ZN A 501 1
HET ZN A 502 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 CYS A 457 HIS A 465 1 9
HELIX 2 2 MET A 467 ARG A 471 5 5
SHEET 1 A 3 TYR A 455 PHE A 456 0
SHEET 2 A 3 PHE A 445 CYS A 447 -1 N PHE A 445 O PHE A 456
SHEET 3 A 3 PRO A 475 LEU A 476 -1 O LEU A 476 N PHE A 446
LINK SG CYS A 447 ZN ZN A 502 1555 1555 1.96
LINK NE2 HIS A 465 ZN ZN A 502 1555 1555 1.97
LINK SG CYS A 452 ZN ZN A 502 1555 1555 1.96
LINK ND1 HIS A 473 ZN ZN A 502 1555 1555 1.99
LINK SG CYS A 438 ZN ZN A 501 1555 1555 2.01
LINK SG CYS A 460 ZN ZN A 501 1555 1555 2.00
LINK SG CYS A 457 ZN ZN A 501 1555 1555 1.98
LINK SG CYS A 435 ZN ZN A 501 1555 1555 2.00
SITE 1 AC1 4 CYS A 435 CYS A 438 CYS A 457 CYS A 460
SITE 1 AC2 4 CYS A 447 CYS A 452 HIS A 465 HIS A 473
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
