HEADER TRANSCRIPTION 21-JUN-05 2A24
TITLE HADDOCK STRUCTURE OF HIF-2A/ARNT PAS-B HETERODIMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOTHELIAL PAS DOMAIN PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL PAS DOMAIN (PAS-B);
COMPND 5 SYNONYM: EPAS-1, MEMBER OF PAS PROTEIN 2, MOP2, HYPOXIA-INDUCIBLE
COMPND 6 FACTOR 2 ALPHA, HIF-2 ALPHA, HIF2 ALPHA, HIF-1 ALPHA-LIKE FACTOR,
COMPND 7 HLF;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: ARYL HYDROCARBON RECEPTOR NUCLEAR TRANSLOCATOR;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: C-TERMINAL PAS DOMAIN (PAS-B);
COMPND 12 SYNONYM: ARNT PROTEIN, DIOXIN RECEPTOR, NUCLEAR TRANSLOCATOR,
COMPND 13 HYPOXIA-INDUCIBLE FACTOR 1 BETA, HIF-1 BETA
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606
KEYWDS ARNT, HIF, HYPOXIA, TRANSCRIPTION, PAS
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.B.CARD,P.J.ERBEL,K.H.GARDNER
REVDAT 4 09-MAR-22 2A24 1 REMARK
REVDAT 3 24-FEB-09 2A24 1 VERSN
REVDAT 2 22-AUG-06 2A24 1 EXPDTA REMARK
REVDAT 1 17-JAN-06 2A24 0
JRNL AUTH P.B.CARD,P.J.ERBEL,K.H.GARDNER
JRNL TITL STRUCTURAL BASIS OF ARNT PAS-B DIMERIZATION: USE OF A COMMON
JRNL TITL 2 BETA-SHEET INTERFACE FOR HETERO- AND HOMODIMERIZATION.
JRNL REF J.MOL.BIOL. V. 353 664 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 16181639
JRNL DOI 10.1016/J.JMB.2005.08.043
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : HADDOCK 1.2, CNS 1.1
REMARK 3 AUTHORS : BONVIN (HADDOCK),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2A24 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000033396.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 50MM TRIS, 17MM NACL, 5MM DTT
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 250 MICRO M (15N)HIF-2ALPHA PAS
REMARK 210 -B (240-350) + 1MM ARNT PAS-B
REMARK 210 (356-470), 50MM TRIS (PH=7.5),
REMARK 210 17MM NACL, 5MM DTT; 250 MICRO M
REMARK 210 (15N)ARNT PAS-B (356-470) + 1MM
REMARK 210 HIF-2ALPHA PAS-B (240-350), 50MM
REMARK 210 TRIS (PH=7.5), 17MM NACL, 5MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N/1H HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.3, CNS 1.1, NMRVIEW
REMARK 210 5.2.2
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: 15N/1H HSQC WAS USED TO MONITOR CHEMICAL SHIFT
REMARK 210 PERTURBATION UPON COMPLEX FORMATION TO IDENTIFY
REMARK 210 INTERACTION INTERFACE.
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 MET A 14 -102.84 60.51
REMARK 500 1 LEU A 28 -57.26 -123.67
REMARK 500 1 HIS A 46 -173.25 65.65
REMARK 500 1 LEU A 96 72.57 56.55
REMARK 500 1 GLN A 99 -77.09 -89.86
REMARK 500 1 LEU A 108 -65.89 -125.41
REMARK 500 1 GLU A 110 -159.53 -91.38
REMARK 500 1 THR B 32 -64.01 -90.81
REMARK 500 1 LYS B 68 83.70 56.69
REMARK 500 1 TYR B 99 -73.72 -81.02
REMARK 500 1 GLU B 102 129.08 -171.43
REMARK 500 1 VAL B 113 -90.23 -85.74
REMARK 500 2 MET A 14 -102.15 54.68
REMARK 500 2 ASP A 15 32.36 -87.27
REMARK 500 2 PHE A 44 34.17 -148.48
REMARK 500 2 HIS A 46 170.05 70.71
REMARK 500 2 ALA A 47 -64.48 -99.28
REMARK 500 2 LYS A 63 -53.01 -132.17
REMARK 500 2 HIS A 77 30.39 -176.65
REMARK 500 2 LEU A 108 -80.89 -120.92
REMARK 500 2 THR B 10 47.55 -86.33
REMARK 500 2 ARG B 28 19.61 -147.83
REMARK 500 2 LYS B 68 119.42 65.69
REMARK 500 2 TYR B 99 -76.28 -106.06
REMARK 500 3 MET A 14 -102.51 58.73
REMARK 500 3 HIS A 46 149.89 68.80
REMARK 500 3 LYS A 63 -47.52 -140.03
REMARK 500 3 LYS A 76 37.48 -81.76
REMARK 500 3 HIS A 77 27.26 -166.00
REMARK 500 3 GLN A 99 -84.93 -98.91
REMARK 500 3 THR B 10 48.81 -86.99
REMARK 500 3 ARG B 28 -18.16 -148.66
REMARK 500 3 THR B 32 -67.16 -94.44
REMARK 500 3 LYS B 68 125.72 67.57
REMARK 500 3 PRO B 98 39.75 -81.70
REMARK 500 3 TYR B 99 -71.65 -119.52
REMARK 500 4 LEU A 28 -68.63 -91.54
REMARK 500 4 PHE A 44 20.87 -145.02
REMARK 500 4 HIS A 46 121.90 67.00
REMARK 500 4 ASP A 49 49.08 -87.37
REMARK 500 4 ARG B 28 10.55 -151.92
REMARK 500 4 THR B 32 -71.93 -102.84
REMARK 500 4 LYS B 68 101.55 61.06
REMARK 500 4 PRO B 98 47.05 -87.36
REMARK 500 4 TYR B 99 -60.83 -127.17
REMARK 500 5 MET A 14 -98.09 55.98
REMARK 500 5 PHE A 44 29.30 -140.41
REMARK 500 5 HIS A 46 151.87 67.87
REMARK 500 5 GLN A 70 112.35 -36.06
REMARK 500 5 HIS A 77 26.99 178.98
REMARK 500
REMARK 500 THIS ENTRY HAS 210 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2A24 A 6 112 UNP Q99814 EPAS1_HUMAN 242 348
DBREF 2A24 B 7 114 UNP P27540 ARNT_HUMAN 358 465
SEQRES 1 A 107 LYS THR PHE LEU SER ARG HIS SER MET ASP MET LYS PHE
SEQRES 2 A 107 THR TYR CYS ASP ASP ARG ILE THR GLU LEU ILE GLY TYR
SEQRES 3 A 107 HIS PRO GLU GLU LEU LEU GLY ARG SER ALA TYR GLU PHE
SEQRES 4 A 107 TYR HIS ALA LEU ASP SER GLU ASN MET THR LYS SER HIS
SEQRES 5 A 107 GLN ASN LEU CYS THR LYS GLY GLN VAL VAL SER GLY GLN
SEQRES 6 A 107 TYR ARG MET LEU ALA LYS HIS GLY GLY TYR VAL TRP LEU
SEQRES 7 A 107 GLU THR GLN GLY THR VAL ILE TYR ASN PRO ARG ASN LEU
SEQRES 8 A 107 GLN PRO GLN CYS ILE MET CYS VAL ASN TYR VAL LEU SER
SEQRES 9 A 107 GLU ILE GLU
SEQRES 1 B 108 CYS GLN PRO THR GLU PHE ILE SER ARG HIS ASN ILE GLU
SEQRES 2 B 108 GLY ILE PHE THR PHE VAL ASP HIS ARG CYS VAL ALA THR
SEQRES 3 B 108 VAL GLY TYR GLN PRO GLN GLU LEU LEU GLY LYS ASN ILE
SEQRES 4 B 108 VAL GLU PHE CYS HIS PRO GLU ASP GLN GLN LEU LEU ARG
SEQRES 5 B 108 ASP SER PHE GLN GLN VAL VAL LYS LEU LYS GLY GLN VAL
SEQRES 6 B 108 LEU SER VAL MET PHE ARG PHE ARG SER LYS ASN GLN GLU
SEQRES 7 B 108 TRP LEU TRP MET ARG THR SER SER PHE THR PHE GLN ASN
SEQRES 8 B 108 PRO TYR SER ASP GLU ILE GLU TYR ILE ILE CYS THR ASN
SEQRES 9 B 108 THR ASN VAL LYS
HELIX 1 1 ASP A 23 GLU A 27 5 5
HELIX 2 2 HIS A 32 LEU A 37 1 6
HELIX 3 3 SER A 40 TYR A 45 5 6
HELIX 4 4 ASP A 49 THR A 62 1 14
HELIX 5 5 ARG B 28 VAL B 33 1 6
HELIX 6 6 GLN B 36 LEU B 41 1 6
HELIX 7 7 ASN B 44 CYS B 49 5 6
HELIX 8 8 HIS B 50 GLU B 52 5 3
HELIX 9 9 ASP B 53 LYS B 68 1 16
SHEET 1 A 5 LYS A 17 CYS A 21 0
SHEET 2 A 5 THR A 7 SER A 13 -1 N ARG A 11 O TYR A 20
SHEET 3 A 5 GLN A 97 GLU A 112 -1 O ILE A 101 N HIS A 12
SHEET 4 A 5 TYR A 80 ASN A 92 -1 N GLU A 84 O TYR A 106
SHEET 5 A 5 GLN A 65 LEU A 74 -1 N SER A 68 O THR A 85
SHEET 1 B 4 GLU B 11 PHE B 12 0
SHEET 2 B 4 THR B 109 ASN B 112 -1 O ASN B 110 N PHE B 12
SHEET 3 B 4 TRP B 85 GLN B 96 -1 N SER B 91 O THR B 109
SHEET 4 B 4 VAL B 71 ARG B 79 -1 N PHE B 76 O MET B 88
SHEET 1 C 4 GLU B 11 PHE B 12 0
SHEET 2 C 4 THR B 109 ASN B 112 -1 O ASN B 110 N PHE B 12
SHEET 3 C 4 TRP B 85 GLN B 96 -1 N SER B 91 O THR B 109
SHEET 4 C 4 ILE B 103 ILE B 106 -1 O TYR B 105 N PHE B 95
SHEET 1 D 2 SER B 14 HIS B 16 0
SHEET 2 D 2 PHE B 22 VAL B 25 -1 O PHE B 24 N ARG B 15
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