Header list of 1dpu.pdb file
Complete list - b 16 2 Bytes
HEADER DNA BINDING PROTEIN 27-DEC-99 1DPU
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF HUMAN RPA32 COMPLEXED
TITLE 2 WITH UNG2(73-88)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REPLICATION PROTEIN A (RPA32) C-TERMINAL DOMAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (RESIDUES 172-270);
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: URACIL DNA GLYCOSYLASE (UNG2);
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: RESIDUES 73-88;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: CHEMICALLY SYNTHESIZED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 OTHER_DETAILS: THIS PEPTIDE SEQUENCE IS FOUND IN THE NUCLEAR
SOURCE 12 [UNG2(73-88)] AND MITOCHONDRIAL [UNG1(64-79)] FORMS OF HUMAN URACIL-
SOURCE 13 DNA GLYCOSYLASE
KEYWDS PROTEIN-PEPTIDE COMPLEX, DNA REPAIR, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR G.MER,A.M.EDWARDS,W.J.CHAZIN
REVDAT 3 16-FEB-22 1DPU 1 REMARK
REVDAT 2 24-FEB-09 1DPU 1 VERSN
REVDAT 1 10-NOV-00 1DPU 0
JRNL AUTH G.MER,A.BOCHKAREV,R.GUPTA,E.BOCHKAREVA,L.FRAPPIER,
JRNL AUTH 2 C.J.INGLES,A.M.EDWARDS,W.J.CHAZIN
JRNL TITL STRUCTURAL BASIS FOR THE RECOGNITION OF DNA REPAIR PROTEINS
JRNL TITL 2 UNG2, XPA, AND RAD52 BY REPLICATION FACTOR RPA.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 103 449 2000
JRNL REFN ISSN 0092-8674
JRNL PMID 11081631
JRNL DOI 10.1016/S0092-8674(00)00136-7
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA 2.8
REMARK 3 AUTHORS : GUNTERT PROGRAM 2 : AMBER 4.1 AUTHORS 2 :
REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM, FERGUSON,
REMARK 3 SEIBEL,SINGH,WEINER,KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DPU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JAN-00.
REMARK 100 THE DEPOSITION ID IS D_1000010272.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.00
REMARK 210 PH : 7.00
REMARK 210 IONIC STRENGTH : 25MM PHOSPHATE, 50MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM RPA32(172-270) U- 15N,13C;
REMARK 210 1.2 MM UNG2(73- 88) NA; 25MM
REMARK 210 PHOSPHATE BUFFER NA; 50MM NACL;
REMARK 210 5 MM DTT NA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; DQF- COSY; HNHA;
REMARK 210 HNHB; HACAHB -COSY; FILTER-
REMARK 210 EDITED NOESY; DOUBLE-HALF
REMARK 210 FILTERED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ; 800
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : MSI FELIX97 SOFTWARE USED 2 :
REMARK 210 DIANA 2.8 SOFTWARE USED 3 :
REMARK 210 AMBER 4.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING DOUBLE- AND TRIPLE
REMARK 210 -RESONANCE NMR 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: 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: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 19 ARG B 88 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 21 ARG B 84 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
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 GLU A 223 43.40 -73.55
REMARK 500 1 THR A 258 -96.89 -122.28
REMARK 500 1 ASP A 268 55.27 -176.07
REMARK 500 1 GLN B 75 -117.89 -148.54
REMARK 500 1 ARG B 76 49.53 -82.65
REMARK 500 2 CYS A 219 100.79 -27.67
REMARK 500 2 THR A 258 -90.51 -132.43
REMARK 500 2 ASP A 261 36.18 -80.98
REMARK 500 2 ASP A 268 141.86 167.18
REMARK 500 2 ALA A 269 -178.35 175.61
REMARK 500 2 ARG B 76 -58.58 71.63
REMARK 500 2 ASN B 77 -80.12 44.04
REMARK 500 3 PRO A 220 -171.27 -68.35
REMARK 500 3 PRO A 222 -117.96 -84.31
REMARK 500 3 THR A 258 -87.63 -125.10
REMARK 500 3 ASP A 268 40.46 -109.29
REMARK 500 3 ILE B 74 -109.82 46.27
REMARK 500 3 ALA B 87 -50.97 75.27
REMARK 500 4 ASN A 203 47.82 -80.51
REMARK 500 4 CYS A 219 111.15 -36.18
REMARK 500 4 THR A 258 -94.43 -120.28
REMARK 500 4 ILE B 74 -36.94 73.70
REMARK 500 5 LEU A 205 -139.48 -89.34
REMARK 500 5 CYS A 219 110.21 -29.31
REMARK 500 5 THR A 258 -82.09 -89.29
REMARK 500 5 ASP A 268 -49.78 -165.78
REMARK 500 5 ALA A 269 -72.87 64.79
REMARK 500 5 ARG B 76 -63.32 73.73
REMARK 500 5 ASN B 77 -71.67 62.81
REMARK 500 6 ASN A 203 62.96 64.69
REMARK 500 6 VAL A 207 -69.57 -26.66
REMARK 500 6 CYS A 219 106.49 -50.42
REMARK 500 6 HIS A 236 -32.56 -162.77
REMARK 500 6 THR A 258 -86.42 -144.03
REMARK 500 6 ASP A 262 46.48 -88.16
REMARK 500 6 ILE B 74 -69.87 62.43
REMARK 500 6 GLN B 75 -69.40 67.06
REMARK 500 7 ASN A 203 -40.15 178.04
REMARK 500 7 CYS A 219 101.36 -29.24
REMARK 500 7 THR A 258 -85.94 -94.54
REMARK 500 7 HIS A 263 88.56 -150.63
REMARK 500 7 THR A 267 -128.41 -81.80
REMARK 500 7 ASP A 268 -56.09 60.65
REMARK 500 7 GLN B 75 -148.22 54.49
REMARK 500 8 CYS A 219 107.63 -44.61
REMARK 500 8 THR A 258 -102.73 -104.20
REMARK 500 8 ASP A 261 2.42 -67.14
REMARK 500 9 HIS A 236 -28.66 -164.09
REMARK 500 9 THR A 258 -96.73 -123.29
REMARK 500 9 ASP A 268 57.23 -95.28
REMARK 500
REMARK 500 THIS ENTRY HAS 171 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 4 TYR A 256 0.08 SIDE CHAIN
REMARK 500 7 TYR A 256 0.13 SIDE CHAIN
REMARK 500 8 ARG A 221 0.10 SIDE CHAIN
REMARK 500 8 TYR A 256 0.09 SIDE CHAIN
REMARK 500 9 ARG A 221 0.08 SIDE CHAIN
REMARK 500 9 TYR A 256 0.10 SIDE CHAIN
REMARK 500 10 ARG B 84 0.07 SIDE CHAIN
REMARK 500 11 TYR A 256 0.12 SIDE CHAIN
REMARK 500 12 ARG A 221 0.09 SIDE CHAIN
REMARK 500 14 TYR A 256 0.11 SIDE CHAIN
REMARK 500 18 TYR A 256 0.12 SIDE CHAIN
REMARK 500 20 ARG A 221 0.09 SIDE CHAIN
REMARK 500 20 TYR A 256 0.13 SIDE CHAIN
REMARK 500 22 ARG A 221 0.12 SIDE CHAIN
REMARK 500 23 ARG B 88 0.08 SIDE CHAIN
REMARK 500 26 ARG A 221 0.08 SIDE CHAIN
REMARK 500 26 TYR A 256 0.09 SIDE CHAIN
REMARK 500 29 HIS A 263 0.08 SIDE CHAIN
REMARK 500 30 TYR A 256 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1DPU A 172 270 UNP P15927 RFA2_HUMAN 202 270
DBREF 1DPU B 73 88 UNP P13051 UNG_HUMAN 73 88
SEQRES 1 A 99 ALA ASN SER GLN PRO SER ALA GLY ARG ALA PRO ILE SER
SEQRES 2 A 99 ASN PRO GLY MET SER GLU ALA GLY ASN PHE GLY GLY ASN
SEQRES 3 A 99 SER PHE MET PRO ALA ASN GLY LEU THR VAL ALA GLN ASN
SEQRES 4 A 99 GLN VAL LEU ASN LEU ILE LYS ALA CYS PRO ARG PRO GLU
SEQRES 5 A 99 GLY LEU ASN PHE GLN ASP LEU LYS ASN GLN LEU LYS HIS
SEQRES 6 A 99 MET SER VAL SER SER ILE LYS GLN ALA VAL ASP PHE LEU
SEQRES 7 A 99 SER ASN GLU GLY HIS ILE TYR SER THR VAL ASP ASP ASP
SEQRES 8 A 99 HIS PHE LYS SER THR ASP ALA GLU
SEQRES 1 B 16 ARG ILE GLN ARG ASN LYS ALA ALA ALA LEU LEU ARG LEU
SEQRES 2 B 16 ALA ALA ARG
HELIX 1 1 THR A 206 CYS A 219 1 14
HELIX 2 2 PHE A 227 LEU A 234 1 8
HELIX 3 3 SER A 238 GLU A 252 1 15
HELIX 4 4 ARG B 76 ALA B 87 1 12
SHEET 1 A 3 LEU A 225 ASN A 226 0
SHEET 2 A 3 HIS A 263 SER A 266 -1 O PHE A 264 N LEU A 225
SHEET 3 A 3 ILE A 255 SER A 257 -1 N TYR A 256 O LYS A 265
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 - b 16 2 Bytes