Header list of 1q2z.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 28-JUL-03 1Q2Z
TITLE THE 3D SOLUTION STRUCTURE OF THE C-TERMINAL REGION OF KU86
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP-DEPENDENT DNA HELICASE II, 80 KDA SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KU86CTR (591-709);
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: XRCC5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21STAR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSET-B
KEYWDS KU, DNA REPAIR, PROTEIN STRUCTURE, NMR SPECTROSCOPY, DNA-PK, KU86,
KEYWDS 2 KU80, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.HARRIS,D.ESPOSITO,A.SANKAR,J.D.MAMAN,J.A.HINKS,L.H.PEARL,
AUTHOR 2 P.C.DRISCOLL
REVDAT 3 02-MAR-22 1Q2Z 1 REMARK
REVDAT 2 24-FEB-09 1Q2Z 1 VERSN
REVDAT 1 13-JAN-04 1Q2Z 0
JRNL AUTH R.HARRIS,D.ESPOSITO,A.SANKAR,J.D.MAMAN,J.A.HINKS,L.H.PEARL,
JRNL AUTH 2 P.C.DRISCOLL
JRNL TITL THE 3D SOLUTION STRUCTURE OF THE C-TERMINAL REGION OF KU86
JRNL TITL 2 (KU86CTR)
JRNL REF J.MOL.BIOL. V. 335 573 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 14672664
JRNL DOI 10.1016/J.JMB.2003.10.047
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ANSIG 1.0.3, CNS 1.1
REMARK 3 AUTHORS : KRAULIS, P.J. (ANSIG), BRUNGER, A.T. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1959 RESTRAINTS, 1863 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 174 DIHEDRAL ANGLE RESTRAINTS,96 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS, 96 RESIDUAL DIPOLAR COUPLINGS
REMARK 4
REMARK 4 1Q2Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000019850.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 293
REMARK 210 PH : 7.0; 7.0
REMARK 210 IONIC STRENGTH : 100 MM NACL; 100 MM NACL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM U-15N; 20MM PHOSPHATE; 100MM
REMARK 210 NACL; 1MM NAN3; 1MM U-13C,15N;
REMARK 210 20MM PHOSPHATE; 100MM NACL; 1MM
REMARK 210 NAN3; 1MM U-15N; 20MM PHOSPHATE;
REMARK 210 100MM NACL; 1MM NAN3; 5% N-OCTYL-
REMARK 210 PENTA(ETHYLENE GLYCOL):OCTANOL
REMARK 210 0.96:1
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; IPAP
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1, VNMR 6.1B
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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: 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 LYS A 16 -40.62 -175.87
REMARK 500 1 ALA A 18 -31.94 -169.49
REMARK 500 1 SER A 19 -21.75 70.45
REMARK 500 1 GLU A 21 -57.78 -141.39
REMARK 500 1 ASN A 38 59.99 92.35
REMARK 500 1 PHE A 60 77.77 -179.20
REMARK 500 1 SER A 61 -99.97 -158.82
REMARK 500 1 ILE A 79 53.01 -92.89
REMARK 500 1 LYS A 80 -82.70 -155.75
REMARK 500 1 GLN A 81 -35.94 -176.95
REMARK 500 1 LEU A 82 37.53 -74.08
REMARK 500 1 LEU A 96 -177.60 -62.36
REMARK 500 1 ALA A 102 -164.05 -117.86
REMARK 500 1 SER A 103 79.62 -113.07
REMARK 500 1 VAL A 107 131.73 -173.99
REMARK 500 2 PRO A 2 -179.42 -59.24
REMARK 500 2 VAL A 3 60.46 33.31
REMARK 500 2 LYS A 16 120.83 -175.77
REMARK 500 2 SER A 19 117.46 74.97
REMARK 500 2 PHE A 60 86.95 -172.27
REMARK 500 2 SER A 61 -98.08 -174.40
REMARK 500 2 ILE A 79 -89.50 -62.95
REMARK 500 2 GLN A 81 118.28 66.96
REMARK 500 2 LEU A 82 11.15 80.91
REMARK 500 2 ALA A 102 -95.15 -95.63
REMARK 500 2 VAL A 107 146.60 174.41
REMARK 500 2 LEU A 116 37.56 -91.27
REMARK 500 2 PRO A 118 -176.00 -69.82
REMARK 500 3 LYS A 16 132.02 -179.64
REMARK 500 3 LYS A 17 91.80 -66.99
REMARK 500 3 SER A 19 -29.20 -174.07
REMARK 500 3 PHE A 20 -56.41 75.82
REMARK 500 3 ASN A 38 45.81 -77.20
REMARK 500 3 PHE A 60 88.52 -176.44
REMARK 500 3 SER A 61 -96.77 -173.56
REMARK 500 3 ILE A 79 54.13 -69.95
REMARK 500 3 GLN A 81 -77.27 -122.44
REMARK 500 3 ILE A 97 121.17 84.72
REMARK 500 3 ALA A 102 -94.48 -95.87
REMARK 500 3 SER A 103 -16.24 -142.90
REMARK 500 3 VAL A 107 139.68 170.50
REMARK 500 3 LYS A 119 -60.59 -94.56
REMARK 500 4 PRO A 2 -179.78 -58.99
REMARK 500 4 ASN A 4 113.20 64.69
REMARK 500 4 LYS A 16 -52.09 179.59
REMARK 500 4 LYS A 17 61.86 -176.38
REMARK 500 4 SER A 19 127.47 68.64
REMARK 500 4 PHE A 60 90.39 -178.59
REMARK 500 4 SER A 61 -99.76 -172.75
REMARK 500 4 ILE A 79 -6.45 -59.02
REMARK 500
REMARK 500 THIS ENTRY HAS 285 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5221 RELATED DB: BMRB
REMARK 900 RESONANCE ASSIGNMENT FOR C-TERMINAL REGION OF KU86
DBREF 1Q2Z A 1 120 UNP P13010 KU86_HUMAN 591 708
SEQADV 1Q2Z GLY A 1 UNP P13010 SEE REMARK 999
SEQADV 1Q2Z PRO A 2 UNP P13010 SEE REMARK 999
SEQRES 1 A 120 GLY PRO VAL ASN PRO ALA GLU ASN PHE ARG VAL LEU VAL
SEQRES 2 A 120 LYS GLN LYS LYS ALA SER PHE GLU GLU ALA SER ASN GLN
SEQRES 3 A 120 LEU ILE ASN HIS ILE GLU GLN PHE LEU ASP THR ASN GLU
SEQRES 4 A 120 THR PRO TYR PHE MET LYS SER ILE ASP CYS ILE ARG ALA
SEQRES 5 A 120 PHE ARG GLU GLU ALA ILE LYS PHE SER GLU GLU GLN ARG
SEQRES 6 A 120 PHE ASN ASN PHE LEU LYS ALA LEU GLN GLU LYS VAL GLU
SEQRES 7 A 120 ILE LYS GLN LEU ASN HIS PHE TRP GLU ILE VAL VAL GLN
SEQRES 8 A 120 ASP GLY ILE THR LEU ILE THR LYS GLU GLU ALA SER GLY
SEQRES 9 A 120 SER SER VAL THR ALA GLU GLU ALA LYS LYS PHE LEU ALA
SEQRES 10 A 120 PRO LYS ASP
HELIX 1 1 ASN A 4 VAL A 13 1 10
HELIX 2 2 GLU A 21 ASN A 38 1 18
HELIX 3 3 GLU A 39 SER A 61 1 23
HELIX 4 4 GLU A 62 ILE A 79 1 18
HELIX 5 5 ASN A 83 ASP A 92 1 10
HELIX 6 6 THR A 108 LYS A 113 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 - r 2 2 Bytes