HEADER DNA BINDING PROTEIN 15-DEC-03 1RW2
TITLE THREE-DIMENSIONAL STRUCTURE OF KU80 CTD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP-DEPENDENT DNA HELICASE II, 80 KDA SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KU80 C-TERMINAL DOMAIN;
COMPND 5 SYNONYM: LUPUS KU AUTOANTIGEN PROTEIN P86, KU86, KU80, 86 KDA SUBUNIT
COMPND 6 OF KU ANTIGEN, THYROID- LUPUS AUTOANTIGEN, TLAA, CTC BOX BINDING
COMPND 7 FACTOR 85 KDA SUBUNIT, CTCBF, CTC85, NUCLEAR FACTOR IV, DNA-REPAIR
COMPND 8 PROTEIN XRCC5;
COMPND 9 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: KU80 (566-710);
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS KU80, NHEJ, DNA-PK, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR Z.ZHANG,W.HU,L.CANO,T.D.LEE,D.J.CHEN,Y.CHEN
REVDAT 4 02-MAR-22 1RW2 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1RW2 1 VERSN
REVDAT 2 18-MAY-04 1RW2 1 AUTHOR JRNL
REVDAT 1 30-DEC-03 1RW2 0
JRNL AUTH Z.ZHANG,W.HU,L.CANO,T.D.LEE,D.J.CHEN,Y.CHEN
JRNL TITL SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF KU80 SUGGESTS
JRNL TITL 2 IMPORTANT SITES FOR PROTEIN-PROTEIN INTERACTIONS.
JRNL REF STRUCTURE V. 12 495 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15016365
JRNL DOI 10.1016/J.STR.2004.02.007
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1, ARIA 1.2
REMARK 3 AUTHORS : VARIAN (VNMR), JENS LINGE, MICHAEL NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2449 RESTRAINTS, 2180 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 201 DIHEDRAL ANGLE RESTRAINTS,68 RESIDUE
REMARK 3 DIPOLAR COUPLING
REMARK 4
REMARK 4 1RW2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000021079.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 100 MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : 1 ATMOSPHERE
REMARK 210 SAMPLE CONTENTS : APPROXIMATELY 1 MM N-15/C-13
REMARK 210 LABELED PROTEIN IN 100 MM
REMARK 210 PHOSPHATE BUFFER, PH 6.0, AND 5
REMARK 210 MM DTT; APPROXIMATELY 1 MM N-15/
REMARK 210 C-13 LABELED PROTEIN IN 100 MM
REMARK 210 PHOSPHATE BUFFER, PH 6.0, AND 5
REMARK 210 MM DTT; APPROXIMATELY 1 MM N-15
REMARK 210 LABELED PROTEIN IN 100 MM
REMARK 210 PHOSPHATE BUFFER, PH 6.0, AN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; HCCH
REMARK 210 -TOCSY; HNCACB, C(CO)NH, HNCO,
REMARK 210 HN(CA)CO, H(CCO)NH, HBHA(CO)NH;
REMARK 210 3D_15N-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98, 2000, DIANA 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: 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 2 PHE A 74 CE1 PHE A 74 CZ 0.193
REMARK 500 2 PHE A 74 CZ PHE A 74 CE2 -0.166
REMARK 500 2 PHE A 100 CE1 PHE A 100 CZ 0.180
REMARK 500 2 PHE A 100 CZ PHE A 100 CE2 -0.164
REMARK 500 3 PHE A 74 CE1 PHE A 74 CZ 0.198
REMARK 500 3 PHE A 74 CZ PHE A 74 CE2 -0.172
REMARK 500 3 PHE A 84 CE1 PHE A 84 CZ 0.118
REMARK 500 4 PHE A 74 CE1 PHE A 74 CZ 0.208
REMARK 500 4 PHE A 74 CZ PHE A 74 CE2 -0.180
REMARK 500 6 PHE A 100 CZ PHE A 100 CE2 0.127
REMARK 500 7 PHE A 74 CE1 PHE A 74 CZ 0.238
REMARK 500 7 PHE A 74 CZ PHE A 74 CE2 -0.208
REMARK 500 8 PHE A 74 CE1 PHE A 74 CZ 0.200
REMARK 500 8 PHE A 74 CZ PHE A 74 CE2 -0.173
REMARK 500 9 PHE A 74 CE1 PHE A 74 CZ 0.194
REMARK 500 9 PHE A 74 CZ PHE A 74 CE2 -0.166
REMARK 500 9 PHE A 100 CE1 PHE A 100 CZ 0.171
REMARK 500 9 PHE A 100 CZ PHE A 100 CE2 -0.146
REMARK 500 9 PHE A 146 CE1 PHE A 146 CZ 0.187
REMARK 500 9 PHE A 146 CZ PHE A 146 CE2 -0.168
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 HIS A 5 -170.29 59.05
REMARK 500 1 LYS A 8 98.75 58.93
REMARK 500 1 GLN A 13 -87.72 58.41
REMARK 500 1 PHE A 18 -165.07 -170.04
REMARK 500 1 SER A 21 -85.16 60.90
REMARK 500 1 LEU A 23 -67.86 -92.76
REMARK 500 1 GLU A 25 -73.99 -97.29
REMARK 500 1 SER A 27 -78.65 -71.62
REMARK 500 1 VAL A 28 -92.47 50.92
REMARK 500 1 VAL A 31 130.38 65.36
REMARK 500 1 VAL A 34 172.10 50.74
REMARK 500 1 ASN A 35 107.84 61.34
REMARK 500 1 LYS A 48 -72.66 -46.10
REMARK 500 1 THR A 68 -177.60 -66.59
REMARK 500 1 LYS A 111 -157.62 -107.59
REMARK 500 1 GLN A 112 -122.68 -91.66
REMARK 500 1 ILE A 125 50.82 -104.35
REMARK 500 1 LEU A 127 167.15 53.80
REMARK 500 1 GLU A 131 53.13 170.66
REMARK 500 1 LYS A 150 -160.03 -121.75
REMARK 500 1 ASP A 151 -166.05 47.59
REMARK 500 2 HIS A 2 -158.71 -80.65
REMARK 500 2 LYS A 10 -39.17 -145.30
REMARK 500 2 GLU A 12 30.61 -145.47
REMARK 500 2 GLN A 13 148.39 65.31
REMARK 500 2 HIS A 17 107.84 64.77
REMARK 500 2 SER A 21 -58.49 -125.70
REMARK 500 2 SER A 22 13.97 59.60
REMARK 500 2 SER A 33 -1.97 -161.70
REMARK 500 2 LYS A 48 -156.32 -64.11
REMARK 500 2 ALA A 49 167.62 -48.55
REMARK 500 2 THR A 68 -178.71 -65.38
REMARK 500 2 SER A 92 77.51 45.02
REMARK 500 2 LYS A 111 -164.36 -108.48
REMARK 500 2 GLN A 112 51.47 -101.72
REMARK 500 2 ILE A 125 61.14 -115.18
REMARK 500 2 LEU A 127 -166.03 35.54
REMARK 500 2 LYS A 130 -56.16 168.23
REMARK 500 2 GLU A 131 -80.05 176.88
REMARK 500 2 ALA A 133 -152.69 -85.24
REMARK 500 2 SER A 136 -179.30 57.38
REMARK 500 3 HIS A 7 -14.71 -164.87
REMARK 500 3 LYS A 8 106.13 63.16
REMARK 500 3 HIS A 17 -11.88 -140.46
REMARK 500 3 GLU A 25 -36.37 -152.61
REMARK 500 3 SER A 27 -71.45 -150.61
REMARK 500 3 VAL A 28 176.84 52.99
REMARK 500 3 SER A 33 -173.65 -172.26
REMARK 500 3 VAL A 34 -152.56 40.36
REMARK 500 3 LYS A 48 -82.05 -46.34
REMARK 500
REMARK 500 THIS ENTRY HAS 204 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1RW2 A 8 152 UNP P13010 KU86_HUMAN 565 709
SEQADV 1RW2 MET A 1 UNP P13010 CLONING ARTIFACT
SEQADV 1RW2 HIS A 2 UNP P13010 EXPRESSION TAG
SEQADV 1RW2 HIS A 3 UNP P13010 EXPRESSION TAG
SEQADV 1RW2 HIS A 4 UNP P13010 EXPRESSION TAG
SEQADV 1RW2 HIS A 5 UNP P13010 EXPRESSION TAG
SEQADV 1RW2 HIS A 6 UNP P13010 EXPRESSION TAG
SEQADV 1RW2 HIS A 7 UNP P13010 EXPRESSION TAG
SEQRES 1 A 152 MET HIS HIS HIS HIS HIS HIS LYS LEU LYS THR GLU GLN
SEQRES 2 A 152 GLY GLY ALA HIS PHE SER VAL SER SER LEU ALA GLU GLY
SEQRES 3 A 152 SER VAL THR SER VAL GLY SER VAL ASN PRO ALA GLU ASN
SEQRES 4 A 152 PHE ARG VAL LEU VAL LYS GLN LYS LYS ALA SER PHE GLU
SEQRES 5 A 152 GLU ALA SER ASN GLN LEU ILE ASN HIS ILE GLU GLN PHE
SEQRES 6 A 152 LEU ASP THR ASN GLU THR PRO TYR PHE MET LYS SER ILE
SEQRES 7 A 152 ASP CYS ILE ARG ALA PHE ARG GLU GLU ALA ILE LYS PHE
SEQRES 8 A 152 SER GLU GLU GLN ARG PHE ASN ASN PHE LEU LYS ALA LEU
SEQRES 9 A 152 GLN GLU LYS VAL GLU ILE LYS GLN LEU ASN HIS PHE TRP
SEQRES 10 A 152 GLU ILE VAL VAL GLN ASP GLY ILE THR LEU ILE THR LYS
SEQRES 11 A 152 GLU GLU ALA SER GLY SER SER VAL THR ALA GLU GLU ALA
SEQRES 12 A 152 LYS LYS PHE LEU ALA PRO LYS ASP LYS
HELIX 1 1 ALA A 37 GLN A 46 1 10
HELIX 2 2 SER A 50 THR A 68 1 19
HELIX 3 3 THR A 71 SER A 92 1 22
HELIX 4 4 GLU A 94 LYS A 111 1 18
HELIX 5 5 LEU A 113 GLY A 124 1 12
HELIX 6 6 ALA A 140 LEU A 147 1 8
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
