HEADER DNA REPAIR 15-JUN-04 1TP4
TITLE SOLUTION STRUCTURE OF THE XPC BINDING DOMAIN OF HHR23A PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UV EXCISION REPAIR PROTEIN RAD23 HOMOLOG A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: XPC BINDING DOMAIN;
COMPND 5 SYNONYM: HHR23A;
COMPND 6 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: RAD23A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX2T
KEYWDS DNA REPAIR, NER, XPC, RAD23
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR M.KAMIONKA,J.FEIGON
REVDAT 3 02-MAR-22 1TP4 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1TP4 1 VERSN
REVDAT 1 28-SEP-04 1TP4 0
JRNL AUTH M.KAMIONKA,J.FEIGON
JRNL TITL STRUCTURE OF THE XPC BINDING DOMAIN OF HHR23A REVEALS
JRNL TITL 2 HYDROPHOBIC PATCHES FOR PROTEIN INTERACTION
JRNL REF PROTEIN SCI. V. 13 2370 2004
JRNL REFN ISSN 0961-8368
JRNL PMID 15322280
JRNL DOI 10.1110/PS.04824304
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 917 NON-REDUNDANT NOE-DERIVED DISTANCE CONSTRAINTS, 82 DIHEDRAL
REMARK 3 ANGLE RESTRAINTS AND 42 DISTANCE RESTRAINTS FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1TP4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022810.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.3
REMARK 210 IONIC STRENGTH : 20MM SODIUM PHOSPHATE, 122MM
REMARK 210 SODIUM CHLORIDE, 0.05% SODIUM
REMARK 210 AZIDE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM XPCB U-15N,13C, 20MM SODIUM
REMARK 210 PHOSPHATE, 122MM SODIUM CHLORIDE,
REMARK 210 0.05% SODIUM AZIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2000, X-PLOR 3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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: 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 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 1-25
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 221
REMARK 465 SER A 222
REMARK 465 ALA A 223
REMARK 465 THR A 224
REMARK 465 GLU A 225
REMARK 465 ALA A 226
REMARK 465 ALA A 227
REMARK 465 GLY A 228
REMARK 465 GLU A 229
REMARK 465 GLY A 289
REMARK 465 GLU A 290
REMARK 465 LEU A 291
REMARK 465 ALA A 292
REMARK 465 ASP A 293
REMARK 465 ILE A 294
REMARK 465 SER A 295
REMARK 465 ASP A 296
REMARK 465 VAL A 297
REMARK 465 GLU A 298
REMARK 465 GLY A 299
REMARK 465 GLU A 300
REMARK 465 VAL A 301
REMARK 465 GLY A 302
REMARK 465 ALA A 303
REMARK 465 ILE A 304
REMARK 465 GLY A 305
REMARK 465 GLU A 306
REMARK 465 GLU A 307
REMARK 465 ALA A 308
REMARK 465 PRO A 309
REMARK 465 GLN A 310
REMARK 465 MET A 311
REMARK 465 ASN A 312
REMARK 465 TYR A 313
REMARK 465 ILE A 314
REMARK 465 GLN A 315
REMARK 465 VAL A 316
REMARK 465 THR A 317
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 ILE A 273 H HIS A 276 1.44
REMARK 500 O PHE A 234 H GLN A 238 1.54
REMARK 500 O PRO A 239 H ASN A 243 1.59
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 ASN A 251 71.40 -101.70
REMARK 500 1 PRO A 252 36.90 -73.80
REMARK 500 1 LEU A 255 171.34 50.65
REMARK 500 1 LEU A 258 -37.56 -36.76
REMARK 500 1 GLU A 265 -70.09 -38.12
REMARK 500 1 SER A 274 -37.70 -39.03
REMARK 500 1 HIS A 276 -144.02 -76.84
REMARK 500 1 GLN A 277 -67.19 86.57
REMARK 500 1 GLU A 286 121.74 -34.50
REMARK 500 2 PRO A 252 30.52 -76.88
REMARK 500 2 LEU A 255 171.65 50.84
REMARK 500 2 HIS A 276 37.65 -92.78
REMARK 500 2 ASN A 285 35.41 -90.31
REMARK 500 2 GLU A 286 91.59 -30.81
REMARK 500 3 PRO A 252 29.88 -77.48
REMARK 500 3 LEU A 255 177.02 49.22
REMARK 500 3 PRO A 256 55.71 -67.64
REMARK 500 3 GLU A 265 -71.33 -38.24
REMARK 500 3 ARG A 275 -85.45 -53.67
REMARK 500 3 HIS A 276 48.89 -82.32
REMARK 500 3 ASN A 285 37.11 -89.14
REMARK 500 3 GLU A 286 89.19 -30.63
REMARK 500 4 PRO A 252 33.50 -75.98
REMARK 500 4 LEU A 255 128.78 60.62
REMARK 500 4 PRO A 256 82.74 -38.08
REMARK 500 4 SER A 274 -31.17 -36.87
REMARK 500 4 LEU A 284 -36.85 -38.63
REMARK 500 4 ASN A 285 36.31 -89.74
REMARK 500 5 PRO A 252 30.85 -76.48
REMARK 500 5 LEU A 255 174.26 50.06
REMARK 500 5 GLU A 265 -71.64 -42.97
REMARK 500 5 ARG A 275 -71.52 -53.69
REMARK 500 5 ASN A 285 38.30 -90.99
REMARK 500 5 GLU A 286 -55.95 -26.79
REMARK 500 6 ARG A 245 -28.72 -38.62
REMARK 500 6 PRO A 252 28.24 -76.37
REMARK 500 6 LEU A 255 133.92 61.24
REMARK 500 6 PRO A 256 57.40 -61.52
REMARK 500 6 ASN A 285 32.64 -89.94
REMARK 500 7 PRO A 252 32.58 -75.51
REMARK 500 7 LEU A 255 170.10 51.86
REMARK 500 7 ASN A 285 32.24 -89.79
REMARK 500 7 GLU A 286 102.46 -32.60
REMARK 500 8 PRO A 252 34.01 -75.62
REMARK 500 8 LEU A 255 171.01 51.47
REMARK 500 8 LEU A 284 -37.43 -39.92
REMARK 500 8 ASN A 285 35.46 -89.02
REMARK 500 8 GLU A 286 106.64 -33.15
REMARK 500 9 PRO A 231 30.82 -86.62
REMARK 500 9 PRO A 252 30.68 -76.59
REMARK 500
REMARK 500 THIS ENTRY HAS 153 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1TP4 A 223 317 UNP P54725 RD23A_HUMAN 223 317
SEQADV 1TP4 GLY A 221 UNP P54725 CLONING ARTIFACT
SEQADV 1TP4 SER A 222 UNP P54725 CLONING ARTIFACT
SEQRES 1 A 97 GLY SER ALA THR GLU ALA ALA GLY GLU ASN PRO LEU GLU
SEQRES 2 A 97 PHE LEU ARG ASP GLN PRO GLN PHE GLN ASN MET ARG GLN
SEQRES 3 A 97 VAL ILE GLN GLN ASN PRO ALA LEU LEU PRO ALA LEU LEU
SEQRES 4 A 97 GLN GLN LEU GLY GLN GLU ASN PRO GLN LEU LEU GLN GLN
SEQRES 5 A 97 ILE SER ARG HIS GLN GLU GLN PHE ILE GLN MET LEU ASN
SEQRES 6 A 97 GLU PRO PRO GLY GLU LEU ALA ASP ILE SER ASP VAL GLU
SEQRES 7 A 97 GLY GLU VAL GLY ALA ILE GLY GLU GLU ALA PRO GLN MET
SEQRES 8 A 97 ASN TYR ILE GLN VAL THR
HELIX 1 1 PRO A 231 GLN A 238 1 8
HELIX 2 2 GLN A 238 ASN A 251 1 14
HELIX 3 3 ALA A 257 ASN A 266 1 10
HELIX 4 4 GLN A 268 SER A 274 1 7
HELIX 5 5 GLN A 277 ASN A 285 1 9
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
