HEADER TRANSCRIPTION 06-MAR-12 2LQH
TITLE NMR STRUCTURE OF FOXO3A TRANSACTIVATION DOMAINS (CR2C-CR3) IN COMPLEX
TITLE 2 WITH CBP KIX DOMAIN (2B3L CONFORMATION)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CREB-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KIX DOMAIN;
COMPND 5 EC: 2.3.1.48;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: FORKHEAD BOX O3;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: TRANSACTIVATION DOMAINS (CR2C-CR3);
COMPND 11 SYNONYM: FOXO3A;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: CREBBP, CBP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET21B;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR: PGEX4T-1
KEYWDS PROMISCUOUS BINDING, INTRINSIC DISORDER, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.WANG,C.B.MARSHALL,K.YAMAMOTO,G.B.LI,G.M.C.GASMI-SEABROOK,H.OKADA,
AUTHOR 2 T.W.MAK,M.IKURA
REVDAT 2 14-JUN-23 2LQH 1 REMARK
REVDAT 1 16-MAY-12 2LQH 0
JRNL AUTH F.WANG,C.B.MARSHALL,K.YAMAMOTO,G.Y.LI,G.M.GASMI-SEABROOK,
JRNL AUTH 2 H.OKADA,T.W.MAK,M.IKURA
JRNL TITL STRUCTURES OF KIX DOMAIN OF CBP IN COMPLEX WITH TWO FOXO3A
JRNL TITL 2 TRANSACTIVATION DOMAINS REVEAL PROMISCUITY AND PLASTICITY IN
JRNL TITL 3 COACTIVATOR RECRUITMENT.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 6078 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22474372
JRNL DOI 10.1073/PNAS.1119073109
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RECOORD WATER REFINEMENT
REMARK 4
REMARK 4 2LQH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000102705.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6
REMARK 210 IONIC STRENGTH : 0.05
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6 MM [U-100% 13C; U-100% 15N]
REMARK 210 KIX, 0.6 MM CR2C-CR3, 20 MM MES,
REMARK 210 50 MM SODIUM CHLORIDE, 1 MM DTT,
REMARK 210 90% H2O/10% D2O; 0.6 MM [U-100%
REMARK 210 13C; U-100% 15N] KIX, 0.6 MM
REMARK 210 CR2C-CR3, 20 MM MES, 50 MM
REMARK 210 SODIUM CHLORIDE, 1 MM DTT, 100%
REMARK 210 D2O; 0.6 MM [U-100% 13C; U-100%
REMARK 210 15N] CR2C-CR3, 0.6 MM KIX, 20 MM
REMARK 210 MES, 50 MM SODIUM CHLORIDE, 1 MM
REMARK 210 DTT, 90% H2O/10% D2O; 0.6 MM [U-
REMARK 210 100% 13C; U-100% 15N] CR2C-CR3,
REMARK 210 0.6 MM KIX, 20 MM MES, 50 MM
REMARK 210 SODIUM CHLORIDE, 1 MM DTT, 100%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D HNCO; 3D
REMARK 210 CBCA(CO)NH; 3D HNCACB; 3D 1H-15N
REMARK 210 NOESY; 2D 1H-13C HSQC; 3D HCCH-
REMARK 210 TOCSY; 3D 1H-13C NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA, TALOS
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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: 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 28 76.50 -67.57
REMARK 500 1 SER B 102 -67.73 -124.85
REMARK 500 1 MET B 103 73.22 42.35
REMARK 500 1 SER B 123 -59.15 71.67
REMARK 500 1 SER B 136 32.81 -155.79
REMARK 500 1 CYS B 139 -85.18 48.35
REMARK 500 2 LYS A 4 102.62 -161.82
REMARK 500 2 PRO A 28 91.93 -63.74
REMARK 500 2 SER A 85 73.45 77.72
REMARK 500 2 MET B 103 -67.07 -108.66
REMARK 500 2 ASP B 124 -79.41 68.13
REMARK 500 2 SER B 132 -60.17 -161.97
REMARK 500 2 CYS B 139 -101.34 45.61
REMARK 500 3 PRO A 28 78.84 -62.12
REMARK 500 3 SER A 85 87.24 170.58
REMARK 500 3 TYR B 106 58.72 -116.91
REMARK 500 3 ASP B 124 -54.23 -126.78
REMARK 500 3 SER B 132 152.71 69.28
REMARK 500 3 ASP B 151 -50.55 75.55
REMARK 500 4 PRO A 28 77.30 -68.06
REMARK 500 4 SER A 85 118.82 162.58
REMARK 500 4 MET B 103 77.68 57.64
REMARK 500 4 SER B 136 80.01 61.34
REMARK 500 5 PRO A 28 96.42 -66.86
REMARK 500 5 SER A 85 90.37 168.96
REMARK 500 5 SER B 123 -84.59 63.70
REMARK 500 5 SER B 132 31.87 -150.48
REMARK 500 6 ARG A 3 71.47 -111.00
REMARK 500 6 LYS A 4 101.28 -162.41
REMARK 500 6 PRO A 28 94.44 -61.60
REMARK 500 6 SER A 85 91.70 153.78
REMARK 500 6 ASP B 124 -53.12 -127.15
REMARK 500 6 SER B 132 -49.20 -130.81
REMARK 500 7 PRO A 28 98.49 -59.76
REMARK 500 7 SER A 85 85.41 76.77
REMARK 500 7 SER B 123 -51.84 73.03
REMARK 500 8 ARG A 86 -34.56 -160.27
REMARK 500 8 SER B 102 82.30 57.76
REMARK 500 8 SER B 123 -90.98 56.71
REMARK 500 8 ASP B 124 20.10 -142.56
REMARK 500 8 SER B 132 145.84 -174.45
REMARK 500 8 CYS B 139 -83.23 23.57
REMARK 500 9 VAL A 2 120.78 78.96
REMARK 500 9 SER A 85 85.14 79.50
REMARK 500 9 SER B 102 -74.71 67.33
REMARK 500 9 HIS B 105 -80.43 66.14
REMARK 500 9 SER B 136 -76.36 -149.95
REMARK 500 10 SER A 85 -64.42 -128.09
REMARK 500 10 TYR B 106 49.23 -103.76
REMARK 500 10 SER B 136 35.63 -84.51
REMARK 500
REMARK 500 THIS ENTRY HAS 100 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 5 ARG A 86 0.09 SIDE CHAIN
REMARK 500 10 ARG A 61 0.07 SIDE CHAIN
REMARK 500 14 ARG A 61 0.09 SIDE CHAIN
REMARK 500 16 ARG A 38 0.07 SIDE CHAIN
REMARK 500 16 ARG A 39 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 18314 RELATED DB: BMRB
REMARK 900 RELATED ID: 2LQI RELATED DB: PDB
DBREF 2LQH A 1 87 UNP P45481 CBP_MOUSE 586 672
DBREF 2LQH B 101 152 PDB 2LQH 2LQH 101 152
SEQRES 1 A 87 GLY VAL ARG LYS GLY TRP HIS GLU HIS VAL THR GLN ASP
SEQRES 2 A 87 LEU ARG SER HIS LEU VAL HIS LYS LEU VAL GLN ALA ILE
SEQRES 3 A 87 PHE PRO THR PRO ASP PRO ALA ALA LEU LYS ASP ARG ARG
SEQRES 4 A 87 MET GLU ASN LEU VAL ALA TYR ALA LYS LYS VAL GLU GLY
SEQRES 5 A 87 ASP MET TYR GLU SER ALA ASN SER ARG ASP GLU TYR TYR
SEQRES 6 A 87 HIS LEU LEU ALA GLU LYS ILE TYR LYS ILE GLN LYS GLU
SEQRES 7 A 87 LEU GLU GLU LYS ARG ARG SER ARG LEU
SEQRES 1 B 52 GLY SER MET SER HIS TYR GLY ASN GLN THR LEU GLN ASP
SEQRES 2 B 52 LEU LEU THR SER ASP SER LEU SER HIS SER ASP GLY GLY
SEQRES 3 B 52 GLY SER GLY GLY GLY SER GLY GLY GLY SER LEU GLU CYS
SEQRES 4 B 52 ASP MET GLU SER ILE ILE ARG SER GLU LEU MET ASP ALA
HELIX 1 1 LYS A 4 VAL A 10 5 7
HELIX 2 2 THR A 11 PHE A 27 1 17
HELIX 3 3 ASP A 31 LYS A 36 5 6
HELIX 4 4 ASP A 37 ALA A 58 1 22
HELIX 5 5 SER A 60 SER A 85 1 26
HELIX 6 6 ASN B 108 SER B 119 1 12
HELIX 7 7 ASP B 140 ASP B 151 1 12
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
