HEADER RNA BINDING PROTEIN 26-JUN-01 1JGN
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL PABC DOMAIN OF HUMAN POLY(A)-
TITLE 2 BINDING PROTEIN IN COMPLEX WITH THE PEPTIDE FROM PAIP2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYADENYLATE-BINDING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 SYNONYM: PABP1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: POLYADENYLATE-BINDING PROTEIN-INTERACTING PROTEIN 2;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: C-TERMINAL 22 RESIDUES;
COMPND 11 SYNONYM: PAIP2;
COMPND 12 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: PABPC1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1
KEYWDS ALL-HELICAL DOMAIN, PROTEIN-PEPTIDE COMPLEX, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR G.KOZLOV,N.SIDDIQUI,S.COILLET-MATILLON,I.EKIEL,K.GEHRING
REVDAT 4 23-FEB-22 1JGN 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1JGN 1 VERSN
REVDAT 2 01-MAR-05 1JGN 1 JRNL
REVDAT 1 24-JUN-03 1JGN 0
JRNL AUTH G.KOZLOV,G.DE CRESCENZO,N.S.LIM,N.SIDDIQUI,D.FANTUS,
JRNL AUTH 2 A.KAHVEJIAN,J.F.TREMPE,D.ELIAS,I.EKIEL,N.SONENBERG,
JRNL AUTH 3 M.O'CONNOR-MCCOURT,K.GEHRING
JRNL TITL STRUCTURAL BASIS OF LIGAND RECOGNITION BY PABC, A HIGHLY
JRNL TITL 2 SPECIFIC PEPTIDE-BINDING DOMAIN FOUND IN POLY(A)-BINDING
JRNL TITL 3 PROTEIN AND A HECT UBIQUITIN LIGASE
JRNL REF EMBO J. V. 23 272 2004
JRNL REFN ISSN 0261-4189
JRNL PMID 14685257
JRNL DOI 10.1038/SJ.EMBOJ.7600048
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.KOZLOV,J.F.TREMPE,K.KHALEGHPOUR,A.KAHVEJIAN,I.EKIEL,
REMARK 1 AUTH 2 K.GEHRING
REMARK 1 TITL STRUCTURE AND FUNCTION OF THE C-TERMINAL PABC DOMAIN OF
REMARK 1 TITL 2 HUMAN POLY(A)-BINDING PROTEIN
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 98 4409 2001
REMARK 1 REFN ISSN 0027-8424
REMARK 1 DOI 10.1073/PNAS.071024998
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, CNS 0.9
REMARK 3 AUTHORS : BRUKER SPECTROSPIN (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 2058 NON
REMARK 3 -REDUNDANT NOE-DERIVED DISTANCE CONSTRAINTS, 106 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS, AND 35 HYDROGEN BONDS.
REMARK 4
REMARK 4 1JGN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000013748.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : 0.1M NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 3MM 15N-LABELED PABC; 4MM
REMARK 210 UNLABELED PEPTIDE; 50MM
REMARK 210 PHOSPHATE BUFFER; 0.1M NACL; 1MM
REMARK 210 NAN3; PH 6.3; 3MM 15N,13C-
REMARK 210 LABELED PABC; 4MM UNLABELED
REMARK 210 PEPTIDE; 50MM PHOSPHATE BUFFER;
REMARK 210 0.1M NACL; 1MM NAN3; PH 6.3;
REMARK 210 2.5MM 15N-LABELED PEPTIDE; 3MM
REMARK 210 UNLABELED PABC; 50MM PHOSPHATE
REMARK 210 BUFFER; 0.1M NACL; 1MM NAN3; PH
REMARK 210 6.3; 2MM 15N,13C-LABELED PEPTIDE;
REMARK 210 3MM UNLABELED PABC; 50MM
REMARK 210 PHOSPHATE BUFFER; 0.1M NACL; 1MM
REMARK 210 NAN3; PH 6.3; 3MM UNLABELED PABC;
REMARK 210 3MM UNLABELED PEPTIDE; 50MM
REMARK 210 PHOSPHATE BUFFER; 0.1M NACL; 1MM
REMARK 210 NAN3; PH 6.3; 3MM UNLABELED PABC;
REMARK 210 3MM UNLABELED PEPTIDE; 50MM
REMARK 210 PHOSPHATE BUFFER; 0.1M NACL; 1MM
REMARK 210 NAN3; PH 6.3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS; DRX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : GIFA 4.31, XEASY 1.3.13, ARIA
REMARK 210 0.9
REMARK 210 METHOD USED : SIMULATED ANNEALING
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: THE STRUCTURE WAS DETERMINED USING STANDARD TRIPLE
REMARK 210 -RESONANCE AND HOMONUCLEAR TECHNIQUES
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 LEU A 3 45.28 -86.18
REMARK 500 1 PRO A 6 -158.73 -68.06
REMARK 500 1 GLN A 22 -80.48 -73.61
REMARK 500 1 MET A 23 -95.24 -69.80
REMARK 500 1 ARG A 27 9.99 -160.06
REMARK 500 1 LEU A 28 -74.88 -59.41
REMARK 500 1 PRO A 37 -28.57 -38.24
REMARK 500 1 THR A 38 -86.54 -78.08
REMARK 500 1 LEU A 39 49.70 -171.46
REMARK 500 1 GLU A 49 21.72 -74.63
REMARK 500 1 ALA A 85 30.69 -84.11
REMARK 500 1 GLN A 86 -78.07 -81.10
REMARK 500 1 LEU B 6 -76.53 -68.94
REMARK 500 1 ALA B 10 93.69 -60.23
REMARK 500 1 PRO B 15 -167.67 -55.82
REMARK 500 2 PRO A 17 -162.08 -68.76
REMARK 500 2 GLN A 22 -77.04 -73.26
REMARK 500 2 MET A 23 -95.91 -68.99
REMARK 500 2 ARG A 27 13.52 -159.96
REMARK 500 2 LEU A 28 -78.85 -57.30
REMARK 500 2 PRO A 37 -32.94 -36.00
REMARK 500 2 THR A 38 -88.38 -78.18
REMARK 500 2 LEU A 39 61.06 -171.31
REMARK 500 2 GLU A 49 20.49 -79.59
REMARK 500 2 PRO A 96 -175.67 -68.52
REMARK 500 2 LEU B 6 -74.78 -68.66
REMARK 500 2 ALA B 10 96.06 -60.96
REMARK 500 2 PRO B 15 -169.86 -55.34
REMARK 500 3 PRO A 6 -159.89 -71.39
REMARK 500 3 PRO A 17 -160.95 -70.31
REMARK 500 3 GLN A 22 -76.75 -72.47
REMARK 500 3 MET A 23 -96.24 -69.16
REMARK 500 3 ARG A 27 13.22 -159.70
REMARK 500 3 LEU A 28 -76.46 -57.32
REMARK 500 3 PRO A 37 -30.39 -37.11
REMARK 500 3 THR A 38 -85.17 -78.28
REMARK 500 3 LEU A 39 51.29 -171.11
REMARK 500 3 ALA A 40 -38.18 -39.83
REMARK 500 3 GLU A 49 22.38 -74.59
REMARK 500 3 ASN B 5 -66.70 -104.32
REMARK 500 3 LEU B 6 -87.44 -64.85
REMARK 500 3 ALA B 10 98.13 -60.57
REMARK 500 3 PRO B 15 -172.83 -55.42
REMARK 500 3 LYS B 18 98.99 -67.19
REMARK 500 4 PRO A 6 -154.95 -70.05
REMARK 500 4 PRO A 17 -157.34 -69.11
REMARK 500 4 GLN A 18 47.44 -74.64
REMARK 500 4 GLN A 22 -79.82 -73.60
REMARK 500 4 MET A 23 -96.09 -69.57
REMARK 500 4 LEU A 24 0.43 -61.04
REMARK 500
REMARK 500 THIS ENTRY HAS 494 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G9L RELATED DB: PDB
REMARK 900 1G9L CONTAINS THE UNCOMPLEXED C-TERMINAL DOMAIN OF HUMAN POLY(A)-
REMARK 900 BINDING PROTEIN
DBREF 1JGN A 6 98 UNP P11940 PABP1_HUMAN 544 636
DBREF 1JGN B 1 22 UNP Q9BPZ3 PAIP2_HUMAN 106 127
SEQADV 1JGN GLY A 1 UNP P11940 CLONING ARTIFACT
SEQADV 1JGN PRO A 2 UNP P11940 CLONING ARTIFACT
SEQADV 1JGN LEU A 3 UNP P11940 CLONING ARTIFACT
SEQADV 1JGN GLY A 4 UNP P11940 CLONING ARTIFACT
SEQADV 1JGN SER A 5 UNP P11940 CLONING ARTIFACT
SEQRES 1 A 98 GLY PRO LEU GLY SER PRO LEU THR ALA SER MET LEU ALA
SEQRES 2 A 98 SER ALA PRO PRO GLN GLU GLN LYS GLN MET LEU GLY GLU
SEQRES 3 A 98 ARG LEU PHE PRO LEU ILE GLN ALA MET HIS PRO THR LEU
SEQRES 4 A 98 ALA GLY LYS ILE THR GLY MET LEU LEU GLU ILE ASP ASN
SEQRES 5 A 98 SER GLU LEU LEU HIS MET LEU GLU SER PRO GLU SER LEU
SEQRES 6 A 98 ARG SER LYS VAL ASP GLU ALA VAL ALA VAL LEU GLN ALA
SEQRES 7 A 98 HIS GLN ALA LYS GLU ALA ALA GLN LYS ALA VAL ASN SER
SEQRES 8 A 98 ALA THR GLY VAL PRO THR VAL
SEQRES 1 B 22 VAL VAL LYS SER ASN LEU ASN PRO ASN ALA LYS GLU PHE
SEQRES 2 B 22 VAL PRO GLY VAL LYS TYR GLY ASN ILE
HELIX 1 1 LEU A 7 SER A 14 1 8
HELIX 2 2 PRO A 16 GLN A 20 5 5
HELIX 3 3 ARG A 27 MET A 35 1 9
HELIX 4 4 LEU A 39 LEU A 47 1 9
HELIX 5 5 LEU A 48 ILE A 50 5 3
HELIX 6 6 ASP A 51 SER A 61 1 11
HELIX 7 7 SER A 61 GLN A 80 1 20
HELIX 8 8 GLN A 80 ALA A 85 1 6
CISPEP 1 SER A 5 PRO A 6 3 -1.64
CISPEP 2 PRO A 16 PRO A 17 5 3.22
CISPEP 3 SER A 5 PRO A 6 9 -0.99
CISPEP 4 PRO A 16 PRO A 17 10 2.22
CISPEP 5 GLY A 1 PRO A 2 11 0.34
CISPEP 6 VAL A 95 PRO A 96 12 0.78
CISPEP 7 PRO A 16 PRO A 17 13 3.90
CISPEP 8 SER A 5 PRO A 6 16 -1.79
CISPEP 9 GLY A 1 PRO A 2 18 0.38
CISPEP 10 SER A 5 PRO A 6 20 -0.04
CISPEP 11 GLY A 1 PRO A 2 24 0.49
CISPEP 12 VAL A 95 PRO A 96 24 0.77
CISPEP 13 GLY A 1 PRO A 2 25 0.45
CISPEP 14 HIS A 36 PRO A 37 28 4.08
CISPEP 15 HIS A 36 PRO A 37 29 5.16
CISPEP 16 GLY A 1 PRO A 2 30 0.18
CRYST1 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
