Header list of 1qze.pdb file
Complete list - 2 20 Bytes
HEADER REPLICATION 16-SEP-03 1QZE
TITLE HHR23A PROTEIN STRUCTURE BASED ON RESIDUAL DIPOLAR COUPLING DATA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UV EXCISION REPAIR PROTEIN RAD23 HOMOLOG A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HHR23A;
COMPND 5 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;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DNA REPAIR, PROTEASOME-MEDIATED DEGRADATION, PROTEIN-PROTEIN
KEYWDS 2 INTERACTION, REPLICATION
EXPDTA SOLUTION NMR
AUTHOR K.J.WALTERS,P.J.LECH,A.M.GOH,Q.WANG,P.M.HOWLEY
REVDAT 3 02-MAR-22 1QZE 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1QZE 1 VERSN
REVDAT 1 21-OCT-03 1QZE 0
JRNL AUTH K.J.WALTERS,P.J.LECH,A.M.GOH,Q.WANG,P.M.HOWLEY
JRNL TITL DNA-REPAIR PROTEIN HHR23A ALTERS ITS PROTEIN STRUCTURE UPON
JRNL TITL 2 BINDING PROTEASOMAL SUBUNIT S5A
JRNL REF PROC.NATL.ACAD.SCI.USA V. 100 12694 2003
JRNL REFN ISSN 0027-8424
JRNL PMID 14557549
JRNL DOI 10.1073/PNAS.1634989100
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : MODULE 1.0
REMARK 3 AUTHORS : DOSSET, HUS, MARION, BLACKLEDGE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QZE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000020255.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.55 MM 15N, HHR23A; 20MM NAPO4
REMARK 210 PH 6.5; 100 MM NACL;7.5 MG/ML
REMARK 210 PF1 PHAGE; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : IPAP [1H,15N] HSQC
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 : MODULE 1.0
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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 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 RES C SSSEQI
REMARK 465 GLY A -4
REMARK 465 PRO A -3
REMARK 465 LEU A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 LYS A 78
REMARK 465 THR A 79
REMARK 465 LYS A 80
REMARK 465 ALA A 81
REMARK 465 GLY A 82
REMARK 465 GLN A 83
REMARK 465 GLY A 84
REMARK 465 THR A 85
REMARK 465 SER A 86
REMARK 465 ALA A 87
REMARK 465 PRO A 88
REMARK 465 PRO A 89
REMARK 465 GLU A 90
REMARK 465 ALA A 91
REMARK 465 SER A 92
REMARK 465 PRO A 93
REMARK 465 THR A 94
REMARK 465 ALA A 95
REMARK 465 ALA A 96
REMARK 465 PRO A 97
REMARK 465 GLU A 98
REMARK 465 SER A 99
REMARK 465 SER A 100
REMARK 465 THR A 101
REMARK 465 SER A 102
REMARK 465 PHE A 103
REMARK 465 PRO A 104
REMARK 465 PRO A 105
REMARK 465 ALA A 106
REMARK 465 PRO A 107
REMARK 465 THR A 108
REMARK 465 SER A 109
REMARK 465 GLY A 110
REMARK 465 MET A 111
REMARK 465 SER A 112
REMARK 465 HIS A 113
REMARK 465 PRO A 114
REMARK 465 PRO A 115
REMARK 465 PRO A 116
REMARK 465 ALA A 117
REMARK 465 ALA A 118
REMARK 465 ARG A 119
REMARK 465 GLU A 120
REMARK 465 ASP A 121
REMARK 465 LYS A 122
REMARK 465 SER A 123
REMARK 465 PRO A 124
REMARK 465 SER A 125
REMARK 465 GLU A 126
REMARK 465 GLU A 127
REMARK 465 SER A 128
REMARK 465 ALA A 129
REMARK 465 PRO A 130
REMARK 465 THR A 131
REMARK 465 THR A 132
REMARK 465 SER A 133
REMARK 465 PRO A 134
REMARK 465 GLU A 135
REMARK 465 SER A 136
REMARK 465 VAL A 137
REMARK 465 SER A 138
REMARK 465 GLY A 139
REMARK 465 SER A 140
REMARK 465 VAL A 141
REMARK 465 PRO A 142
REMARK 465 SER A 143
REMARK 465 SER A 144
REMARK 465 GLY A 145
REMARK 465 SER A 146
REMARK 465 SER A 147
REMARK 465 GLY A 148
REMARK 465 ARG A 149
REMARK 465 GLU A 150
REMARK 465 GLU A 151
REMARK 465 ASP A 152
REMARK 465 ALA A 153
REMARK 465 ALA A 154
REMARK 465 SER A 155
REMARK 465 THR A 156
REMARK 465 LEU A 157
REMARK 465 VAL A 158
REMARK 465 THR A 159
REMARK 465 GLY A 201
REMARK 465 ILE A 202
REMARK 465 PRO A 203
REMARK 465 GLY A 204
REMARK 465 SER A 205
REMARK 465 PRO A 206
REMARK 465 GLU A 207
REMARK 465 PRO A 208
REMARK 465 GLU A 209
REMARK 465 HIS A 210
REMARK 465 GLY A 211
REMARK 465 SER A 212
REMARK 465 VAL A 213
REMARK 465 GLN A 214
REMARK 465 GLU A 215
REMARK 465 SER A 216
REMARK 465 GLN A 217
REMARK 465 VAL A 218
REMARK 465 SER A 219
REMARK 465 GLU A 220
REMARK 465 GLN A 221
REMARK 465 PRO 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 ASN A 230
REMARK 465 PRO A 231
REMARK 465 LEU A 284
REMARK 465 ASN A 285
REMARK 465 GLU A 286
REMARK 465 PRO A 287
REMARK 465 PRO A 288
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 ASP A 361
REMARK 465 ASP A 362
REMARK 465 GLU A 363
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 H VAL A 25 O VAL A 59 1.49
REMARK 500 O ARG A 193 H TYR A 197 1.54
REMARK 500 HZ2 LYS A 29 O GLN A 46 1.54
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 VAL A 3 122.25 -175.45
REMARK 500 GLN A 12 35.52 77.79
REMARK 500 PHE A 15 -153.66 -164.06
REMARK 500 ARG A 18 -46.71 -143.51
REMARK 500 MET A 19 -148.97 36.25
REMARK 500 ASP A 22 -28.06 -177.59
REMARK 500 ALA A 40 22.92 -152.00
REMARK 500 PRO A 42 -162.98 -79.15
REMARK 500 ALA A 51 57.96 -155.96
REMARK 500 SER A 56 -172.64 -65.50
REMARK 500 SER A 172 -31.88 -38.62
REMARK 500 TYR A 175 174.60 -59.44
REMARK 500 GLU A 176 -152.29 -83.03
REMARK 500 ARG A 177 -61.35 -107.53
REMARK 500 ASN A 189 34.55 37.67
REMARK 500 HIS A 192 -83.08 -69.55
REMARK 500 GLN A 261 -71.99 -108.16
REMARK 500 PRO A 333 -159.15 -70.08
REMARK 500 GLU A 334 -71.18 -117.00
REMARK 500 VAL A 337 -61.54 -90.44
REMARK 500 ALA A 343 -72.29 -79.91
REMARK 500 CYS A 344 -65.07 -125.14
REMARK 500 ASN A 359 -64.47 -95.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 1 ALA A 2 -145.87
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 ARG A 18 0.32 SIDE CHAIN
REMARK 500 ARG A 38 0.23 SIDE CHAIN
REMARK 500 ARG A 62 0.30 SIDE CHAIN
REMARK 500 ARG A 65 0.23 SIDE CHAIN
REMARK 500 ARG A 177 0.23 SIDE CHAIN
REMARK 500 ARG A 179 0.31 SIDE CHAIN
REMARK 500 ARG A 185 0.24 SIDE CHAIN
REMARK 500 ARG A 193 0.29 SIDE CHAIN
REMARK 500 ARG A 236 0.32 SIDE CHAIN
REMARK 500 ARG A 245 0.30 SIDE CHAIN
REMARK 500 ARG A 275 0.22 SIDE CHAIN
REMARK 500 ARG A 326 0.27 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OQY RELATED DB: PDB
REMARK 900 BUNDLE OF STRUCTURES FOR THIS PROTEIN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 IN THIS ANALYSIS THE LINKER REGIONS WERE
REMARK 999 IGNORED. ALTHOUGH THEY DO STILL EXIST IN
REMARK 999 THE SAMPLE, THOSE REGIONS WERE OMITTED
REMARK 999 FROM THE CALCULATION.
DBREF 1QZE A 2 363 UNP P54725 RD23A_HUMAN 2 363
SEQADV 1QZE GLY A -4 UNP P54725 CLONING ARTIFACT
SEQADV 1QZE PRO A -3 UNP P54725 CLONING ARTIFACT
SEQADV 1QZE LEU A -2 UNP P54725 CLONING ARTIFACT
SEQADV 1QZE GLY A -1 UNP P54725 CLONING ARTIFACT
SEQADV 1QZE SER A 0 UNP P54725 CLONING ARTIFACT
SEQADV 1QZE SER A 1 UNP P54725 CLONING ARTIFACT
SEQRES 1 A 368 GLY PRO LEU GLY SER SER ALA VAL THR ILE THR LEU LYS
SEQRES 2 A 368 THR LEU GLN GLN GLN THR PHE LYS ILE ARG MET GLU PRO
SEQRES 3 A 368 ASP GLU THR VAL LYS VAL LEU LYS GLU LYS ILE GLU ALA
SEQRES 4 A 368 GLU LYS GLY ARG ASP ALA PHE PRO VAL ALA GLY GLN LYS
SEQRES 5 A 368 LEU ILE TYR ALA GLY LYS ILE LEU SER ASP ASP VAL PRO
SEQRES 6 A 368 ILE ARG ASP TYR ARG ILE ASP GLU LYS ASN PHE VAL VAL
SEQRES 7 A 368 VAL MET VAL THR LYS THR LYS ALA GLY GLN GLY THR SER
SEQRES 8 A 368 ALA PRO PRO GLU ALA SER PRO THR ALA ALA PRO GLU SER
SEQRES 9 A 368 SER THR SER PHE PRO PRO ALA PRO THR SER GLY MET SER
SEQRES 10 A 368 HIS PRO PRO PRO ALA ALA ARG GLU ASP LYS SER PRO SER
SEQRES 11 A 368 GLU GLU SER ALA PRO THR THR SER PRO GLU SER VAL SER
SEQRES 12 A 368 GLY SER VAL PRO SER SER GLY SER SER GLY ARG GLU GLU
SEQRES 13 A 368 ASP ALA ALA SER THR LEU VAL THR GLY SER GLU TYR GLU
SEQRES 14 A 368 THR MET LEU THR GLU ILE MET SER MET GLY TYR GLU ARG
SEQRES 15 A 368 GLU ARG VAL VAL ALA ALA LEU ARG ALA SER TYR ASN ASN
SEQRES 16 A 368 PRO HIS ARG ALA VAL GLU TYR LEU LEU THR GLY ILE PRO
SEQRES 17 A 368 GLY SER PRO GLU PRO GLU HIS GLY SER VAL GLN GLU SER
SEQRES 18 A 368 GLN VAL SER GLU GLN PRO ALA THR GLU ALA ALA GLY GLU
SEQRES 19 A 368 ASN PRO LEU GLU PHE LEU ARG ASP GLN PRO GLN PHE GLN
SEQRES 20 A 368 ASN MET ARG GLN VAL ILE GLN GLN ASN PRO ALA LEU LEU
SEQRES 21 A 368 PRO ALA LEU LEU GLN GLN LEU GLY GLN GLU ASN PRO GLN
SEQRES 22 A 368 LEU LEU GLN GLN ILE SER ARG HIS GLN GLU GLN PHE ILE
SEQRES 23 A 368 GLN MET LEU ASN GLU PRO PRO GLY GLU LEU ALA ASP ILE
SEQRES 24 A 368 SER ASP VAL GLU GLY GLU VAL GLY ALA ILE GLY GLU GLU
SEQRES 25 A 368 ALA PRO GLN MET ASN TYR ILE GLN VAL THR PRO GLN GLU
SEQRES 26 A 368 LYS GLU ALA ILE GLU ARG LEU LYS ALA LEU GLY PHE PRO
SEQRES 27 A 368 GLU SER LEU VAL ILE GLN ALA TYR PHE ALA CYS GLU LYS
SEQRES 28 A 368 ASN GLU ASN LEU ALA ALA ASN PHE LEU LEU SER GLN ASN
SEQRES 29 A 368 PHE ASP ASP GLU
HELIX 1 1 THR A 24 LYS A 36 1 13
HELIX 2 2 GLY A 160 SER A 172 1 13
HELIX 3 3 ARG A 177 SER A 187 1 11
HELIX 4 4 ASN A 190 THR A 200 1 11
HELIX 5 5 LEU A 232 ASP A 237 1 6
HELIX 6 6 GLN A 238 VAL A 247 1 10
HELIX 7 7 ILE A 248 ASN A 251 5 4
HELIX 8 8 ALA A 253 GLN A 261 1 9
HELIX 9 9 ASN A 266 MET A 283 1 18
HELIX 10 10 GLU A 320 GLY A 331 1 12
HELIX 11 11 GLU A 334 TYR A 341 1 8
HELIX 12 12 ASN A 349 ASN A 359 1 11
SHEET 1 A 5 PHE A 15 ILE A 17 0
SHEET 2 A 5 ILE A 5 THR A 9 -1 N ILE A 5 O ILE A 17
SHEET 3 A 5 VAL A 72 THR A 77 1 O VAL A 74 N LYS A 8
SHEET 4 A 5 GLY A 45 ILE A 49 -1 N LYS A 47 O MET A 75
SHEET 5 A 5 ILE A 54 LEU A 55 -1 O LEU A 55 N LEU A 48
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
Complete list - 2 20 Bytes