HEADER APOPTOSIS 25-JUN-10 2KZU
TITLE DAXX HELICAL BUNDLE (DHB) DOMAIN / RASSF1C COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEATH-ASSOCIATED PROTEIN 6;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 55 TO 144;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: RAS ASSOCIATION (RALGDS/AF-6) DOMAIN FAMILY 1;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: UNP RESIDUES 23 TO 38;
COMPND 10 SYNONYM: RAS ASSOCIATION (RALGDS/AF-6) DOMAIN FAMILY 1, ISOFORM
COMPND 11 CRA_A;
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: DAXX, DADB-159G18.9-007, DAMC-227D19.15-007, DAQB-126H3.2-007,
SOURCE 6 XXBAC-BCX165D10.3-007, XXBAC-BPG185D15.6-007;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PGEX-2T;
SOURCE 11 OTHER_DETAILS: CLONED WITH BAMHI ECORI;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 GENE: RASSF1, HCG_17462;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FAS DEATH-DOMAIN ASSOCIATED PROTEIN, DAXX HELICAL BUNDLE DOMAIN, RAS-
KEYWDS 2 ASSOCIATION DOMAIN FAMILY 1C PROTEIN, APOPTOSIS, TUMOR SUPPRESSOR
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR E.ESCOBAR-CABRERA,D.K.W.LAU,S.GIOVINAZZI,A.M.ISHOV,L.P.MCINTOSH
REVDAT 3 14-JUN-23 2KZU 1 REMARK
REVDAT 2 05-FEB-20 2KZU 1 SEQADV
REVDAT 1 15-DEC-10 2KZU 0
JRNL AUTH E.ESCOBAR-CABRERA,D.K.LAU,S.GIOVINAZZI,A.M.ISHOV,
JRNL AUTH 2 L.P.MCINTOSH
JRNL TITL STRUCTURAL CHARACTERIZATION OF THE DAXX N-TERMINAL HELICAL
JRNL TITL 2 BUNDLE DOMAIN AND ITS COMPLEX WITH RASSF1C.
JRNL REF STRUCTURE V. 18 1642 2010
JRNL REFN ISSN 0969-2126
JRNL PMID 21134643
JRNL DOI 10.1016/J.STR.2010.09.016
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 2.2, ARIA 2.2
REMARK 3 AUTHORS : LINGE, O'DONOGHUE AND NILGES (ARIA), LINGE,
REMARK 3 O'DONOGHUE AND NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2KZU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000101779.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.1 MM [U-100% 13C; U-100% 15N]
REMARK 210 DAXX-1, 1.65 MM RASSF1C-2, 95%
REMARK 210 H2O/5% D2O; 1.8 MM DAXX-3, 1.2
REMARK 210 MM [U-100% 13C; U-100% 15N]
REMARK 210 RASSF1C-4, 95% H2O/5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D CBCA(CO)NH;
REMARK 210 3D HNCACB; 3D HCCH-TOCSY; 2D 1H-
REMARK 210 13C HSQC; (H)CC(CO)NH-TOCSY;
REMARK 210 HCC(CO)NH-TOCSY; (HB)CB(CGCD)HD;
REMARK 210 (HB)CB(CGCDCE)HE; 3D 1H-15N
REMARK 210 NOESY; 3D 1H-13C NOESY; 13C/15N
REMARK 210 ISOTOPE-FILTERED NOESY-HSQC; (HB)
REMARK 210 CB(CGCD)HD-TOCSY; 3D 1H-15N TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ARIA 2.2
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 120
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
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 O GLU A 129 H VAL A 133 1.57
REMARK 500 HZ2 LYS A 141 O ASN A 144 1.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 5 TYR A 59 CE1 TYR A 59 CZ -0.142
REMARK 500 5 TYR A 59 CZ TYR A 59 CE2 0.132
REMARK 500 8 PHE A 99 CE1 PHE A 99 CZ 0.130
REMARK 500 8 PHE A 99 CZ PHE A 99 CE2 -0.132
REMARK 500 10 TYR A 59 CE1 TYR A 59 CZ -0.083
REMARK 500 10 TYR A 59 CZ TYR A 59 CE2 0.078
REMARK 500 11 TYR A 59 CE1 TYR A 59 CZ -0.081
REMARK 500 20 TYR A 59 CE1 TYR A 59 CZ -0.119
REMARK 500 20 TYR A 59 CZ TYR A 59 CE2 0.101
REMARK 500 25 TYR A 59 CE1 TYR A 59 CZ -0.121
REMARK 500 25 TYR A 59 CZ TYR A 59 CE2 0.117
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 52 -66.31 -130.12
REMARK 500 1 HIS A 53 -91.30 -158.32
REMARK 500 1 THR A 78 45.66 -87.19
REMARK 500 1 PRO A 82 21.63 -76.02
REMARK 500 1 ARG A 119 75.39 -118.99
REMARK 500 1 LYS A 140 22.93 -174.92
REMARK 500 1 SER B 27 -108.34 59.62
REMARK 500 1 ALA B 37 -158.04 -101.58
REMARK 500 2 LYS A 56 100.57 50.59
REMARK 500 2 THR A 78 42.71 -90.41
REMARK 500 2 ALA A 101 41.12 -108.09
REMARK 500 2 LYS A 140 -29.26 -143.90
REMARK 500 2 SER B 27 -82.65 -99.54
REMARK 500 2 THR B 36 -175.41 -171.71
REMARK 500 2 ALA B 37 -157.88 -113.59
REMARK 500 3 THR A 78 38.28 -85.89
REMARK 500 3 ALA A 101 41.36 -76.97
REMARK 500 3 GLU B 25 78.05 48.28
REMARK 500 3 SER B 27 -120.99 -90.95
REMARK 500 3 THR B 36 -164.11 179.55
REMARK 500 3 ALA B 37 -165.80 -125.27
REMARK 500 4 THR A 78 49.44 -88.30
REMARK 500 4 PRO A 82 28.06 -72.34
REMARK 500 4 ALA A 101 48.74 -79.25
REMARK 500 4 ALA A 139 81.38 41.49
REMARK 500 4 SER B 23 72.06 58.87
REMARK 500 4 SER B 27 -76.45 -90.12
REMARK 500 4 ALA B 37 -169.35 -117.15
REMARK 500 5 MET A 54 11.67 -157.79
REMARK 500 5 THR A 78 44.98 -86.53
REMARK 500 5 PRO A 82 25.79 -70.50
REMARK 500 5 ALA A 101 41.80 -79.21
REMARK 500 5 ALA A 139 70.51 60.27
REMARK 500 5 GLU B 25 -166.70 50.62
REMARK 500 5 SER B 27 -92.32 -92.58
REMARK 500 5 ALA B 37 -166.98 -125.47
REMARK 500 6 HIS A 53 -72.27 -89.24
REMARK 500 6 MET A 54 -97.04 -142.26
REMARK 500 6 THR A 78 41.57 -87.61
REMARK 500 6 PRO A 82 17.90 -69.13
REMARK 500 6 ALA A 139 87.68 20.22
REMARK 500 6 LYS A 140 -17.10 110.31
REMARK 500 6 LYS A 141 -73.42 -40.22
REMARK 500 6 SER B 23 54.71 -98.09
REMARK 500 6 GLU B 25 -157.16 68.05
REMARK 500 6 ASP B 26 -92.97 -95.13
REMARK 500 6 SER B 27 -124.87 169.90
REMARK 500 6 THR B 36 -165.72 -165.60
REMARK 500 6 ALA B 37 -161.15 -116.35
REMARK 500 7 THR A 78 42.18 -87.98
REMARK 500
REMARK 500 THIS ENTRY HAS 196 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2KZS RELATED DB: PDB
REMARK 900 RELATED ID: 17019 RELATED DB: BMRB
DBREF 2KZU A 55 144 UNP Q4VX54 Q4VX54_HUMAN 55 144
DBREF 2KZU B 23 38 UNP Q5TZT2 Q5TZT2_HUMAN 23 38
SEQADV 2KZU GLY A 51 UNP Q4VX54 EXPRESSION TAG
SEQADV 2KZU SER A 52 UNP Q4VX54 EXPRESSION TAG
SEQADV 2KZU HIS A 53 UNP Q4VX54 EXPRESSION TAG
SEQADV 2KZU MET A 54 UNP Q4VX54 EXPRESSION TAG
SEQADV 2KZU GLY B 22 UNP Q5TZT2 EXPRESSION TAG
SEQADV 2KZU TRP B 39 UNP Q5TZT2 EXPRESSION TAG
SEQRES 1 A 94 GLY SER HIS MET GLY LYS LYS CYS TYR LYS LEU GLU ASN
SEQRES 2 A 94 GLU LYS LEU PHE GLU GLU PHE LEU GLU LEU CYS LYS MET
SEQRES 3 A 94 GLN THR ALA ASP HIS PRO GLU VAL VAL PRO PHE LEU TYR
SEQRES 4 A 94 ASN ARG GLN GLN ARG ALA HIS SER LEU PHE LEU ALA SER
SEQRES 5 A 94 ALA GLU PHE CYS ASN ILE LEU SER ARG VAL LEU SER ARG
SEQRES 6 A 94 ALA ARG SER ARG PRO ALA LYS LEU TYR VAL TYR ILE ASN
SEQRES 7 A 94 GLU LEU CYS THR VAL LEU LYS ALA HIS SER ALA LYS LYS
SEQRES 8 A 94 LYS LEU ASN
SEQRES 1 B 18 GLY SER GLN GLU ASP SER ASP SER GLU LEU GLU GLN TYR
SEQRES 2 B 18 PHE THR ALA ARG TRP
HELIX 1 1 TYR A 59 THR A 78 1 20
HELIX 2 2 GLU A 83 ARG A 94 1 12
HELIX 3 3 LEU A 98 ALA A 101 5 4
HELIX 4 4 SER A 102 ARG A 119 1 18
HELIX 5 5 LYS A 122 SER A 138 1 17
HELIX 6 6 ASP B 28 GLN B 33 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
(ATOM LINES ARE NOT SHOWN.)
END