HEADER DNA EXCISION REPAIR 14-JUL-00 1E52
TITLE SOLUTION STRUCTURE OF ESCHERICHIA COLI UVRB C-TERMINAL DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXCINUCLEASE ABC SUBUNIT;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN RESIDUES 618-673;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: PP3398;
SOURCE 5 GENE: UVRB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET-HIS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PNP118;
SOURCE 12 EXPRESSION_SYSTEM_GENE: UVRB(DOMAIN)
KEYWDS DNA EXCISION REPAIR, UVRB, DNA REPAIR, UVRC BINDING DOMAIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.A.ALEXANDROVICH,G.G.KELLY,T.A.FRENKIEL,G.F.MOOLENAAR,N.N.GOOSEN,
AUTHOR 2 M.R.SANDERSON,A.N.LANE
REVDAT 6 14-JUN-23 1E52 1 REMARK
REVDAT 5 15-JAN-20 1E52 1 REMARK
REVDAT 4 17-JAN-18 1E52 1 JRNL
REVDAT 3 24-FEB-09 1E52 1 VERSN
REVDAT 2 17-JAN-02 1E52 1 JRNL
REVDAT 1 12-JUL-01 1E52 0
JRNL AUTH A.A.ALEXANDROVICH,M.M.CZISCH,T.T.FRENKIEL,G.G.KELLY,
JRNL AUTH 2 N.N.GOOSEN,G.G.MOOLENAAR,B.B.CHOWDHRY,M.M.SANDERSON,A.A.LANE
JRNL TITL SOLUTION STRUCTURE, HYDRODYNAMICS AND THERMODYNAMICS OF THE
JRNL TITL 2 UVRB C-TERMINAL DOMAIN.
JRNL REF J.BIOMOL.STRUCT.DYN. V. 19 219 2001
JRNL REFN ISSN 0739-1102
JRNL PMID 11697728
JRNL DOI 10.1080/07391102.2001.10506734
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SIMULATED ANNEALING PROTOCOL WITH NON
REMARK 3 -CRYSTALLOGRAPHIC SYMMETRY RESTRAINTS
REMARK 4
REMARK 4 1E52 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1290005162.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 0.2
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1 MM PROTEIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-EDITED HSQC-NOESY; 13C
REMARK 210 -EDITED HSQC-NOESY; 13C/12C-
REMARK 210 FILTERED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
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 : MINIMAL ENERGY/VIOLATIONS
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 ON 13C, 15N-LABELED PROTEIN. INTERMOLECULAR
REMARK 210 DISTANCE RESTRAINTS WERE OBTAINED
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 400
REMARK 400 COMPOUND
REMARK 400 CHAIN A, B ARE THE UVRC-BINDING DOMAIN OF UVRB
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 MET B 1
REMARK 465 HIS B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
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 PRO A 14 -82.81 -82.31
REMARK 500 1 MET A 15 -172.02 -176.33
REMARK 500 1 ASP A 16 38.22 -159.29
REMARK 500 1 LYS A 20 -70.31 63.79
REMARK 500 1 GLN A 35 -74.83 -52.07
REMARK 500 1 ALA A 62 -74.64 -84.67
REMARK 500 1 PRO B 14 -82.96 -82.35
REMARK 500 1 MET B 15 -172.09 -176.18
REMARK 500 1 ASP B 16 38.09 -159.17
REMARK 500 1 LYS B 20 -70.38 63.73
REMARK 500 1 GLN B 35 -75.01 -51.85
REMARK 500 1 ALA B 62 -74.64 -84.62
REMARK 500 2 GLU A 9 70.87 53.05
REMARK 500 2 ASP A 11 -82.52 59.80
REMARK 500 2 ASN A 12 18.93 -152.34
REMARK 500 2 MET A 15 -163.64 53.80
REMARK 500 2 LYS A 20 -67.55 64.18
REMARK 500 2 ALA A 62 -67.97 -98.56
REMARK 500 2 GLU B 9 70.83 53.12
REMARK 500 2 ASP B 11 -82.54 59.76
REMARK 500 2 ASN B 12 18.90 -152.31
REMARK 500 2 MET B 15 -163.69 53.84
REMARK 500 2 LYS B 20 -67.55 64.21
REMARK 500 2 ALA B 62 -67.84 -98.54
REMARK 500 3 GLU A 9 87.38 53.12
REMARK 500 3 ASP A 11 -80.67 60.60
REMARK 500 3 ASN A 12 28.23 -143.95
REMARK 500 3 PRO A 14 -74.94 -81.87
REMARK 500 3 MET A 15 122.78 -176.74
REMARK 500 3 ASP A 16 34.21 -97.28
REMARK 500 3 LYS A 20 -69.44 61.49
REMARK 500 3 GLN A 35 -78.44 -49.00
REMARK 500 3 PHE A 42 -9.92 -59.95
REMARK 500 3 ALA A 62 -64.52 -96.71
REMARK 500 3 GLU B 9 87.35 52.99
REMARK 500 3 ASP B 11 -80.73 60.58
REMARK 500 3 ASN B 12 28.32 -143.92
REMARK 500 3 PRO B 14 -74.95 -81.81
REMARK 500 3 MET B 15 122.79 -176.74
REMARK 500 3 ASP B 16 34.13 -97.26
REMARK 500 3 LYS B 20 -69.42 61.44
REMARK 500 3 GLN B 35 -78.49 -49.02
REMARK 500 3 ALA B 62 -64.46 -96.75
REMARK 500 4 GLU A 9 81.01 53.07
REMARK 500 4 ASP A 11 -79.63 61.30
REMARK 500 4 MET A 15 -150.81 52.78
REMARK 500 4 LYS A 20 -67.43 64.65
REMARK 500 4 GLN A 35 -74.92 -60.77
REMARK 500 4 PHE A 42 -57.14 62.21
REMARK 500 4 ALA A 62 -65.99 -103.13
REMARK 500
REMARK 500 THIS ENTRY HAS 333 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 1 ARG A 49 0.24 SIDE CHAIN
REMARK 500 1 ARG A 56 0.18 SIDE CHAIN
REMARK 500 1 ARG B 49 0.24 SIDE CHAIN
REMARK 500 1 ARG B 56 0.18 SIDE CHAIN
REMARK 500 2 ARG A 49 0.25 SIDE CHAIN
REMARK 500 2 ARG A 56 0.27 SIDE CHAIN
REMARK 500 2 ARG B 49 0.25 SIDE CHAIN
REMARK 500 2 ARG B 56 0.27 SIDE CHAIN
REMARK 500 3 ARG A 49 0.17 SIDE CHAIN
REMARK 500 3 ARG A 56 0.30 SIDE CHAIN
REMARK 500 3 ARG B 49 0.17 SIDE CHAIN
REMARK 500 3 ARG B 56 0.30 SIDE CHAIN
REMARK 500 4 ARG A 49 0.15 SIDE CHAIN
REMARK 500 4 ARG A 56 0.29 SIDE CHAIN
REMARK 500 4 ARG B 49 0.15 SIDE CHAIN
REMARK 500 4 ARG B 56 0.29 SIDE CHAIN
REMARK 500 5 ARG A 49 0.19 SIDE CHAIN
REMARK 500 5 ARG A 56 0.31 SIDE CHAIN
REMARK 500 5 ARG B 49 0.19 SIDE CHAIN
REMARK 500 5 ARG B 56 0.31 SIDE CHAIN
REMARK 500 6 ARG A 49 0.15 SIDE CHAIN
REMARK 500 6 ARG A 56 0.23 SIDE CHAIN
REMARK 500 6 ARG B 49 0.15 SIDE CHAIN
REMARK 500 6 ARG B 56 0.23 SIDE CHAIN
REMARK 500 7 ARG A 49 0.23 SIDE CHAIN
REMARK 500 7 ARG A 56 0.18 SIDE CHAIN
REMARK 500 7 ARG B 49 0.23 SIDE CHAIN
REMARK 500 7 ARG B 56 0.18 SIDE CHAIN
REMARK 500 8 ARG A 49 0.21 SIDE CHAIN
REMARK 500 8 ARG A 56 0.27 SIDE CHAIN
REMARK 500 8 ARG B 49 0.21 SIDE CHAIN
REMARK 500 8 ARG B 56 0.27 SIDE CHAIN
REMARK 500 9 ARG A 49 0.17 SIDE CHAIN
REMARK 500 9 ARG A 56 0.28 SIDE CHAIN
REMARK 500 9 ARG B 49 0.17 SIDE CHAIN
REMARK 500 9 ARG B 56 0.28 SIDE CHAIN
REMARK 500 10 ARG A 49 0.30 SIDE CHAIN
REMARK 500 10 ARG A 56 0.30 SIDE CHAIN
REMARK 500 10 ARG B 49 0.30 SIDE CHAIN
REMARK 500 10 ARG B 56 0.30 SIDE CHAIN
REMARK 500 11 ARG A 49 0.25 SIDE CHAIN
REMARK 500 11 ARG A 56 0.31 SIDE CHAIN
REMARK 500 11 ARG B 49 0.25 SIDE CHAIN
REMARK 500 11 ARG B 56 0.31 SIDE CHAIN
REMARK 500 12 ARG A 49 0.24 SIDE CHAIN
REMARK 500 12 ARG A 56 0.32 SIDE CHAIN
REMARK 500 12 ARG B 49 0.24 SIDE CHAIN
REMARK 500 12 ARG B 56 0.32 SIDE CHAIN
REMARK 500 13 ARG A 49 0.23 SIDE CHAIN
REMARK 500 13 ARG A 56 0.24 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 80 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QOJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E.COLI UVRB C-TERMINAL DOMAIN, AND A MODEL FOR
REMARK 900 UVRB-UVRC INTERACTION.
REMARK 900 RELATED ID: 4622 RELATED DB: BMRB
DBREF 1E52 A 1 7 PDB 1E52 1E52 1 7
DBREF 1E52 A 8 63 UNP P07025 UVRB_ECOLI 618 673
DBREF 1E52 B 1 7 PDB 1E52 1E52 1 7
DBREF 1E52 B 8 63 UNP P07025 UVRB_ECOLI 618 673
SEQADV 1E52 LEU A 8 UNP P07025 VAL 618 CONFLICT
SEQADV 1E52 LEU B 8 UNP P07025 VAL 618 CONFLICT
SEQRES 1 A 63 MET HIS HIS HIS HIS HIS HIS LEU GLU PRO ASP ASN VAL
SEQRES 2 A 63 PRO MET ASP MET SER PRO LYS ALA LEU GLN GLN LYS ILE
SEQRES 3 A 63 HIS GLU LEU GLU GLY LEU MET MET GLN HIS ALA GLN ASN
SEQRES 4 A 63 LEU GLU PHE GLU GLU ALA ALA GLN ILE ARG ASP GLN LEU
SEQRES 5 A 63 HIS GLN LEU ARG GLU LEU PHE ILE ALA ALA SER
SEQRES 1 B 63 MET HIS HIS HIS HIS HIS HIS LEU GLU PRO ASP ASN VAL
SEQRES 2 B 63 PRO MET ASP MET SER PRO LYS ALA LEU GLN GLN LYS ILE
SEQRES 3 B 63 HIS GLU LEU GLU GLY LEU MET MET GLN HIS ALA GLN ASN
SEQRES 4 B 63 LEU GLU PHE GLU GLU ALA ALA GLN ILE ARG ASP GLN LEU
SEQRES 5 B 63 HIS GLN LEU ARG GLU LEU PHE ILE ALA ALA SER
HELIX 1 1 LYS A 20 ASN A 39 1 20
HELIX 2 2 GLU A 41 ALA A 46 1 6
HELIX 3 3 GLN A 47 SER A 63 1 17
HELIX 4 4 LYS B 20 ASN B 39 1 20
HELIX 5 5 GLU B 41 ALA B 46 1 6
HELIX 6 6 GLN B 47 SER B 63 1 17
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
