Header list of 2c52.pdb file
Complete list - y 2 2 Bytes
HEADER TRANSFERASE 25-OCT-05 2C52
TITLE STRUCTURAL DIVERSITY IN CBP P160 COMPLEXES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CREB-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SID, RESIDUES 2059-2117;
COMPND 5 EC: 2.3.1.48;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR 1;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: AD1, RESIDUES 920-970;
COMPND 11 SYNONYM: STEROID RECEPTOR COACTIVATOR 1, NCOA-1, SRC-1, RIP160, HIN-2
COMPND 12 PROTEIN;
COMPND 13 EC: 2.3.1.48;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: B834;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS TRANSFERASE, ACTIVATOR, BROMODOMAIN, METAL-BINDING, METHYLATION,
KEYWDS 2 NUCLEAR PROTEIN, TRANSCRIPTION, TRANSCRIPTION REGULATION, ZINC,
KEYWDS 3 ZINC-FINGER, ACYLTRANSFERASE, ALTERNATIVE SPLICING, CHROMOSOMAL
KEYWDS 4 TRANSLOCATION, POLYMORPHISM, PROTO-ONCOGENE, UBL CONJUGATION
EXPDTA SOLUTION NMR
NUMMDL 37
AUTHOR L.C.WATERS,B.YUE,V.VEVERKA,P.S.RENSHAW,J.BRAMHAM,S.MATSUDA,
AUTHOR 2 T.FRENKIEL,G.KELLY,F.W.MUSKETT,M.D.CARR,D.M.HEERY
REVDAT 4 02-MAY-18 2C52 1 JRNL REMARK
REVDAT 3 24-FEB-09 2C52 1 VERSN
REVDAT 2 24-MAY-06 2C52 1 JRNL
REVDAT 1 15-MAR-06 2C52 0
JRNL AUTH L.WATERS,B.YUE,V.VEVERKA,P.RENSHAW,J.BRAMHAM,S.MATSUDA,
JRNL AUTH 2 T.FRENKIEL,G.KELLY,F.MUSKETT,M.CARR,D.M.HEERY
JRNL TITL STRUCTURAL DIVERSITY IN P160/CREB-BINDING PROTEIN
JRNL TITL 2 COACTIVATOR COMPLEXES.
JRNL REF J. BIOL. CHEM. V. 281 14787 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16540468
JRNL DOI 10.1074/JBC.M600237200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA
REMARK 3 AUTHORS : GUNTERT,MUMENTHALER,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 2C52 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1290023743.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0; 298.0; 298.0; 298.0
REMARK 210 PH : 7.0; 7.0; 7.0; 7.0
REMARK 210 IONIC STRENGTH : 100; 100; 100; 100
REMARK 210 PRESSURE : NULL; NULL; NULL; NULL
REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O; 90% WATER/10%
REMARK 210 D2O; 100% D2O; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-1H HSQC 15N-13C-1H HNCACB
REMARK 210 15N-13C-1H CBCACONH 15N-1H TOCSY-
REMARK 210 HSQC; 15N-1H NOESYHSQC; 13C-1H
REMARK 210 HMQCNOESY; 13C-1H HCCHTOCSY
REMARK 210 NOESY TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA
REMARK 210 METHOD USED : CANDID
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 37
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED CBP-SID SRC1-AD1.
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 400
REMARK 400 COMPOUND
REMARK 400 ACETYLATES HISTONES, GIVING A SPECIFIC TAG FOR TRANSCRIPTIONAL
REMARK 400 ACTIVATION AND NUCLEAR RECEPTOR COACTIVATOR THAT DIRECTLY BINDS
REMARK 400 NUCLEAR RECEPTORS AND STIMULATES THE TRANSCRIPTIONAL ACTIVITIES
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 1-37
REMARK 465 RES C SSSEQI
REMARK 465 GLN A 60
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 O MET A 41 H ILE A 45 1.47
REMARK 500 O THR A 49 H VAL A 53 1.50
REMARK 500 O GLU B 328 H ALA B 332 1.51
REMARK 500 O ILE B 340 H LEU B 343 1.51
REMARK 500 O TYR A 52 H GLN A 56 1.51
REMARK 500 O THR B 329 HE ARG B 336 1.52
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 SER A 5 -92.14 -58.77
REMARK 500 1 SER A 20 -174.19 -51.70
REMARK 500 1 SER A 22 85.33 86.12
REMARK 500 1 SER A 23 -62.67 160.79
REMARK 500 1 PRO A 24 -96.64 -75.08
REMARK 500 1 GLN A 26 -61.68 -29.90
REMARK 500 1 VAL A 53 -32.12 -39.79
REMARK 500 1 THR B 305 36.07 -140.90
REMARK 500 1 VAL B 306 32.36 -147.24
REMARK 500 1 ARG B 309 -64.14 -137.43
REMARK 500 1 ASN B 310 134.08 61.20
REMARK 500 1 ASP B 311 167.74 156.31
REMARK 500 1 GLN B 345 -45.79 -28.96
REMARK 500 1 LEU B 349 32.30 -166.48
REMARK 500 1 ASP B 350 170.69 162.87
REMARK 500 1 VAL B 351 -79.48 -156.01
REMARK 500 1 LEU B 352 -92.87 -144.38
REMARK 500 1 SER B 353 48.36 154.94
REMARK 500 1 LEU B 355 93.95 55.10
REMARK 500 1 VAL B 356 95.47 -34.55
REMARK 500 1 ARG B 358 -41.46 -132.46
REMARK 500 2 ASN A 3 -54.56 -159.36
REMARK 500 2 SER A 5 -71.15 67.45
REMARK 500 2 ILE A 6 144.45 176.41
REMARK 500 2 SER A 20 -173.77 -57.39
REMARK 500 2 SER A 22 88.94 87.68
REMARK 500 2 SER A 23 -61.18 157.33
REMARK 500 2 PRO A 24 -98.98 -75.00
REMARK 500 2 ASN A 37 105.01 -163.41
REMARK 500 2 THR B 304 -160.15 45.76
REMARK 500 2 THR B 305 30.69 -168.44
REMARK 500 2 VAL B 306 36.75 -153.81
REMARK 500 2 ARG B 309 -64.11 -138.43
REMARK 500 2 ASN B 310 137.50 61.49
REMARK 500 2 ASP B 311 166.54 155.08
REMARK 500 2 ARG B 336 -30.45 -37.88
REMARK 500 2 LEU B 349 -89.66 -79.52
REMARK 500 2 ASP B 350 -155.65 -136.88
REMARK 500 2 LEU B 352 -99.72 39.75
REMARK 500 2 SER B 353 -47.30 155.36
REMARK 500 2 LEU B 355 75.52 66.71
REMARK 500 2 VAL B 356 102.29 -43.11
REMARK 500 2 SER B 360 -53.04 -131.46
REMARK 500 3 ASN A 3 137.29 62.77
REMARK 500 3 ARG A 4 163.99 -46.40
REMARK 500 3 SER A 9 -39.09 -37.19
REMARK 500 3 SER A 20 -177.04 -51.27
REMARK 500 3 SER A 22 83.57 91.59
REMARK 500 3 SER A 23 -60.91 163.12
REMARK 500 3 PRO A 24 -102.85 -75.03
REMARK 500
REMARK 500 THIS ENTRY HAS 771 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F81 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE TAZ2 DOMAIN OF THE TRANSCRIPTIONAL
REMARK 900 ADAPTOR PROTEIN CBP
REMARK 900 RELATED ID: 1JJS RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF IBID, A DOMAIN OF CBP/P300
REMARK 900 RELATED ID: 1KBH RELATED DB: PDB
REMARK 900 MUTUAL SYNERGISTIC FOLDING IN THE INTERACTION BETWEEN NUCLEAR
REMARK 900 RECEPTOR COACTIVATORS CBP AND ACTR
REMARK 900 RELATED ID: 1KDX RELATED DB: PDB
REMARK 900 KIX DOMAIN OF MOUSE CBP (CREB BINDING PROTEIN) IN COMPLEXWITH
REMARK 900 PHOSPHORYLATED KINASE INDUCIBLE DOMAIN (PKID) OF RATCREB (CYCLIC
REMARK 900 AMP RESPONSE ELEMENT BINDING PROTEIN), NMR17 STRUCTURES
REMARK 900 RELATED ID: 1L8C RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR HIF-1ALPHA/CBP RECOGNITION IN THECELLULAR
REMARK 900 HYPOXIC RESPONSE
REMARK 900 RELATED ID: 1R8U RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF CBP TAZ1/CITED2 COMPLEX
REMARK 900 RELATED ID: 1SB0 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE KIX DOMAIN OF CBP BOUND TO
REMARK 900 THETRANSACTIVATION DOMAIN OF C C-MYB
REMARK 900 RELATED ID: 1TOT RELATED DB: PDB
REMARK 900 ZZ DOMAIN OF CBP- A NOVEL FOLD FOR A PROTEIN INTERACTIONMODULE
REMARK 900 RELATED ID: 1U2N RELATED DB: PDB
REMARK 900 STRUCTURE CBP TAZ1 DOMAIN
REMARK 900 RELATED ID: 1XIU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE AGONIST-BOUND LIGAND-BINDING DOMAIN OF
REMARK 900 BIOMPHALARIA GLABRATA RXR
REMARK 900 RELATED ID: 2A3I RELATED DB: PDB
REMARK 900 STRUCTURAL AND BIOCHEMICAL MECHANISMS FOR THE SPECIFICITY OF
REMARK 900 HORMONE BINDING AND COACTIVATOR ASSEMBLY BY MINERALOCORTICOID
REMARK 900 RECEPTOR
REMARK 900 RELATED ID: 6874 RELATED DB: BMRB
REMARK 900 SHIFTS HAVE BEEN DEPOSITED AT BMRB UNDER ACCESSION NUMBER BMRB-6874
DBREF 2C52 A 2 60 UNP P45481 CBP_MOUSE 2059 2117
DBREF 2C52 B 303 353 UNP Q15788 NCOA1_HUMAN 920 970
DBREF 2C52 B 354 361 PDB 2C52 2C52 354 361
SEQRES 1 A 59 PRO ASN ARG SER ILE SER PRO SER ALA LEU GLN ASP LEU
SEQRES 2 A 59 LEU ARG THR LEU LYS SER PRO SER SER PRO GLN GLN GLN
SEQRES 3 A 59 GLN GLN VAL LEU ASN ILE LEU LYS SER ASN PRO GLN LEU
SEQRES 4 A 59 MET ALA ALA PHE ILE LYS GLN ARG THR ALA LYS TYR VAL
SEQRES 5 A 59 ALA ASN GLN PRO GLY MET GLN
SEQRES 1 B 59 PRO THR THR VAL GLU GLY ARG ASN ASP GLU LYS ALA LEU
SEQRES 2 B 59 LEU GLU GLN LEU VAL SER PHE LEU SER GLY LYS ASP GLU
SEQRES 3 B 59 THR GLU LEU ALA GLU LEU ASP ARG ALA LEU GLY ILE ASP
SEQRES 4 B 59 LYS LEU VAL GLN GLY GLY GLY LEU ASP VAL LEU SER LYS
SEQRES 5 B 59 LEU VAL PRO ARG GLY SER LEU
HELIX 1 1 SER A 9 LYS A 19 1 11
HELIX 2 2 GLN A 25 SER A 36 1 12
HELIX 3 3 PRO A 38 THR A 49 1 12
HELIX 4 4 TYR A 52 ASN A 55 1 4
HELIX 5 5 GLU B 312 SER B 324 1 13
HELIX 6 6 GLU B 328 LEU B 331 1 4
HELIX 7 7 GLU B 333 LEU B 338 5 6
HELIX 8 8 ILE B 340 GLN B 345 1 6
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
Complete list - y 2 2 Bytes