Header list of 1v06.pdb file
Complete list - r 25 2 Bytes
HEADER DNA-BINDING PROTEIN 24-MAR-04 1V06
TITLE AXH DOMAIN OF THE TRANSCRIPTION FACTOR HBP1 FROM M.MUSCULUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HMG BOX-CONTAINING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: AXH DOMAIN, RESIDUES 208-345;
COMPND 5 SYNONYM: HBP1, HMG-BOX CONTAINING PROTEIN-1, HMG BOX
COMPND 6 TRANSCRIPTION FACTOR 1, HIGH MOBILITY GROUP BOX
COMPND 7 TRANSCRIPTION FACTOR 1;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET24D
KEYWDS DNA-BINDING PROTEIN, TRANSCRIPTION FACTOR, PROTEIN-PROTEIN
KEYWDS 2 INTERACTION, NUCLEIC ACID BINDING, OB-FOLD, ATAXIN-1
KEYWDS 3 HOMOLOGOUS, REPRESSOR, TRANSCRIPTION, TRANSCRIPTION
KEYWDS 4 REGULATION, WNT SIGNALING PATHWAY
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.DE CHIARA,G.KELLY,A.PASTORE
REVDAT 2 24-FEB-09 1V06 1 VERSN
REVDAT 1 21-APR-05 1V06 0
JRNL AUTH C.DE CHIARA,R.P.MENON,S.ADINOLFI,J.DE BOER,
JRNL AUTH 2 E.KTISTAKI,G.KELLY,L.CALDER,D.KIOUSSIS,A.PASTORE
JRNL TITL THE AXH DOMAIN ADOPTS ALTERNATIVE FOLDS THE
JRNL TITL 2 SOLUTION STRUCTURE OF HBP1 AXH.
JRNL REF STRUCTURE V. 13 743 2005
JRNL REFN ISSN 0969-2126
JRNL PMID 15893665
JRNL DOI 10.1016/J.STR.2005.02.016
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.DE CHIARA,G.KELLY,T.A.FRANKIEL,A.PASTORE
REMARK 1 TITL ASSIGNMENT OF THE 1H,13C, AND 15N RESONANCES OF
REMARK 1 TITL 2 THE AXH DOMAIN OF THE TRANSCRIPTION FACTOR HBP1
REMARK 1 REF J.BIOMOL.NMR V. 28 411 2004
REMARK 1 REFN ISSN 0925-2738
REMARK 1 PMID 14872137
REMARK 1 DOI 10.1023/B:JNMR.0000015367.92295.0F
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.DE CHIARA,C.GIANNINI,S.ADINOLFI,J.DEBOER,S.GUIDA,
REMARK 1 AUTH 2 A.RAMOS,C.JODICE,D.KIOUSSIS,A.PASTORE
REMARK 1 TITL THE AXH MODULE:AN INDEPENDENTLY FOLDED DOMAIN
REMARK 1 TITL 2 COMMON TO ATAXIN-1 AND HBP1
REMARK 1 REF FEBS LETT. V. 551 107 2003
REMARK 1 REFN ISSN 0014-5793
REMARK 1 PMID 12965213
REMARK 1 DOI 10.1016/S0014-5793(03)00818-4
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 1.2, CNS 1.1
REMARK 3 AUTHORS : NILGES, BRUNGER ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE EXPERIMENTALLY DETERMINED
REMARK 3 DISTANCE AND DIHEDRAL ANGLE RESTRAINTS WERE APPLIED IN A MIXED
REMARK 3 TORSION AND CARTESIAN DYNAMICS SIMULATED ANNEALING PROTOCOL.
REMARK 3 THE FINAL STRUCTURE ENSEMBLE WAS REFINED IN A SHELL OF WATER
REMARK 3 MOLECULES
REMARK 4
REMARK 4 1V06 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-MAR-04.
REMARK 100 THE PDBE ID CODE IS EBI-14821.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 10 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.7 MM 15N- OR 15N,
REMARK 210 13C-LABELED PROTEIN,
REMARK 210 20 MM TRIS-HCL, 10 MM NACL,
REMARK 210 2 MM BETA-MERCAPTOETHANOL,
REMARK 210 10% WATER/90% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TRIPLE RESONANCE, NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 ; 800
REMARK 210 SPECTROMETER MODEL : INOVA ; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN ; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.7, XEASY 1.2,
REMARK 210 ARIA 1.2
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 : LOWEST ENERGIES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: STRUCTURAL RESTRAINTS WERE DERIVED FROM 13C- AND
REMARK 210 15N-EDITED NOESY EXPERIMENTS AND J-COUPLINGS
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 204
REMARK 465 ALA A 205
REMARK 465 MET A 206
REMARK 465 ALA A 207
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 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 HIS A 213 -138.43 58.62
REMARK 500 1 CYS A 214 37.18 -98.61
REMARK 500 1 ASN A 245 124.30 -179.12
REMARK 500 1 ILE A 249 -62.51 -121.99
REMARK 500 1 HIS A 254 147.56 -173.23
REMARK 500 1 ASN A 306 -17.13 78.95
REMARK 500 2 HIS A 213 -136.53 54.54
REMARK 500 2 ASP A 244 -169.18 -106.86
REMARK 500 2 ASN A 245 72.83 -68.12
REMARK 500 2 GLU A 246 51.51 -93.99
REMARK 500 2 GLN A 250 81.41 -66.54
REMARK 500 2 ASN A 306 -1.45 77.95
REMARK 500 2 ASN A 344 52.80 -117.54
REMARK 500 3 HIS A 213 -144.99 55.68
REMARK 500 3 CYS A 214 44.74 -94.79
REMARK 500 3 GLU A 226 -95.05 -145.27
REMARK 500 3 ASN A 245 42.14 -170.14
REMARK 500 3 GLU A 246 45.49 -86.68
REMARK 500 3 GLN A 250 -64.91 -93.35
REMARK 500 3 LEU A 264 97.75 -65.36
REMARK 500 3 ASN A 306 -33.36 76.27
REMARK 500 3 ASN A 344 73.93 -114.41
REMARK 500 4 HIS A 213 -135.01 55.15
REMARK 500 4 GLN A 250 -51.42 177.76
REMARK 500 4 LEU A 264 95.35 -65.97
REMARK 500 4 ASN A 306 -23.08 77.64
REMARK 500 4 ASN A 344 42.52 -107.04
REMARK 500 5 HIS A 213 -139.46 57.19
REMARK 500 5 CYS A 214 36.74 -97.50
REMARK 500 5 THR A 253 -80.14 -66.74
REMARK 500 5 HIS A 254 93.05 64.10
REMARK 500 5 ASN A 306 -5.21 76.81
REMARK 500 6 HIS A 213 -142.42 57.50
REMARK 500 6 CYS A 214 37.29 -96.98
REMARK 500 6 SER A 227 32.09 -84.65
REMARK 500 6 ASN A 245 47.84 -176.37
REMARK 500 6 GLU A 246 38.72 -81.15
REMARK 500 6 ASN A 306 -6.45 76.61
REMARK 500 7 HIS A 213 -136.09 55.53
REMARK 500 7 ILE A 249 -62.22 -101.21
REMARK 500 7 GLN A 250 -68.00 -145.24
REMARK 500 7 THR A 253 30.18 -99.02
REMARK 500 7 LEU A 264 107.57 -58.69
REMARK 500 8 HIS A 213 -139.15 56.86
REMARK 500 8 CYS A 214 40.05 -98.96
REMARK 500 8 SER A 227 30.07 -88.75
REMARK 500 8 ASN A 228 67.99 -104.02
REMARK 500 8 SER A 242 -70.81 -38.54
REMARK 500 8 ASP A 244 -31.25 178.57
REMARK 500 8 GLN A 250 -47.95 -139.08
REMARK 500 8 ASP A 299 31.34 -87.37
REMARK 500 8 ASN A 344 43.74 -109.65
REMARK 500 9 HIS A 213 -135.75 55.23
REMARK 500 9 ASP A 244 36.21 -82.87
REMARK 500 9 ASN A 245 -36.26 -139.66
REMARK 500 9 HIS A 254 130.38 176.27
REMARK 500 9 ASN A 306 -8.68 77.10
REMARK 500 9 ASN A 344 31.57 -99.57
REMARK 500 10 HIS A 213 -146.56 59.06
REMARK 500 10 CYS A 214 39.82 -94.64
REMARK 500 10 ASP A 244 -160.92 178.52
REMARK 500 10 GLU A 246 30.06 -140.50
REMARK 500 10 THR A 253 -79.83 -95.52
REMARK 500 10 HIS A 254 141.64 74.22
REMARK 500 10 TYR A 313 74.22 -119.67
REMARK 500 11 HIS A 213 -139.26 55.83
REMARK 500 11 CYS A 214 42.69 -100.40
REMARK 500 11 GLU A 226 -156.50 -105.78
REMARK 500 11 CYS A 243 -80.65 -76.43
REMARK 500 11 ASP A 244 -33.71 177.05
REMARK 500 11 ASN A 245 128.59 177.54
REMARK 500 11 GLU A 246 50.09 -95.12
REMARK 500 11 GLN A 250 -62.46 -150.01
REMARK 500 11 THR A 253 38.36 -160.47
REMARK 500 11 ALA A 342 91.73 -69.00
REMARK 500 12 HIS A 213 -139.22 55.94
REMARK 500 12 CYS A 214 40.09 -99.80
REMARK 500 12 GLU A 246 44.90 -89.13
REMARK 500 12 GLN A 250 -56.31 -178.76
REMARK 500 12 ASN A 306 -26.39 81.45
REMARK 500 13 HIS A 213 -137.40 56.43
REMARK 500 13 GLU A 226 -165.06 -101.62
REMARK 500 13 ASN A 228 43.57 -82.03
REMARK 500 13 GLU A 246 47.32 -83.22
REMARK 500 13 GLN A 250 -56.91 -166.42
REMARK 500 13 LEU A 264 107.21 -59.46
REMARK 500 13 ASN A 344 62.51 -114.56
REMARK 500 14 HIS A 213 -151.51 57.83
REMARK 500 14 CYS A 214 46.36 -88.37
REMARK 500 14 SER A 227 49.51 -93.74
REMARK 500 14 GLN A 250 -61.73 -133.72
REMARK 500 14 THR A 253 -66.56 -98.98
REMARK 500 14 HIS A 254 91.07 53.64
REMARK 500 14 ASN A 344 53.43 -110.56
REMARK 500 15 HIS A 213 -141.04 53.53
REMARK 500 15 CYS A 214 38.68 -98.40
REMARK 500 15 GLU A 226 -101.92 -126.85
REMARK 500 15 ASN A 228 38.76 -80.80
REMARK 500 15 ASN A 306 -2.79 76.85
REMARK 500 16 HIS A 213 -149.59 59.74
REMARK 500 16 CYS A 214 36.15 -90.68
REMARK 500 16 SER A 227 41.03 -88.47
REMARK 500 16 ASN A 245 133.72 176.03
REMARK 500 16 GLU A 246 43.41 -105.80
REMARK 500 16 GLN A 250 -58.09 -174.80
REMARK 500 16 THR A 253 -92.25 -80.56
REMARK 500 16 HIS A 254 109.17 69.12
REMARK 500 17 HIS A 213 -138.54 60.94
REMARK 500 17 CYS A 214 32.38 -95.40
REMARK 500 17 SER A 242 -177.98 178.76
REMARK 500 17 ASP A 244 -28.90 179.52
REMARK 500 17 ASN A 245 91.48 -165.98
REMARK 500 17 GLN A 250 -85.05 -131.99
REMARK 500 17 ASN A 306 -6.84 75.72
REMARK 500 17 ASN A 344 74.02 -107.97
REMARK 500 18 HIS A 213 -149.67 57.63
REMARK 500 18 CYS A 214 43.75 -88.61
REMARK 500 18 GLU A 226 -168.21 -110.69
REMARK 500 18 SER A 227 42.45 -82.67
REMARK 500 18 ASN A 245 -68.67 -136.11
REMARK 500 18 GLU A 246 18.61 -154.68
REMARK 500 18 GLN A 250 164.66 179.49
REMARK 500 18 THR A 253 -77.51 -153.03
REMARK 500 18 HIS A 254 114.64 65.12
REMARK 500 18 ASN A 306 -1.95 78.08
REMARK 500 19 HIS A 213 -137.54 53.10
REMARK 500 19 SER A 227 31.08 -82.18
REMARK 500 19 ASP A 244 -177.73 178.52
REMARK 500 19 ASN A 245 70.46 -106.44
REMARK 500 19 GLN A 250 74.58 -64.22
REMARK 500 19 HIS A 254 -164.25 59.85
REMARK 500 20 HIS A 213 -133.54 56.04
REMARK 500 20 SER A 242 -145.84 178.18
REMARK 500 20 GLU A 246 40.34 -76.05
REMARK 500 20 GLN A 250 -61.45 -168.17
REMARK 500 20 HIS A 254 76.90 -68.79
REMARK 500 20 ASN A 306 -20.04 78.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FOLLOWING N-TERMINAL RESIDUES FROM THE EXPRESSION SYSTEM
REMARK 999 TAG WERE NOT LOCATED IN THE EXPERIMENT: GLY ALA MET ALA
DBREF 1V06 A 204 207 PDB 1V06 1V06 204 207
DBREF 1V06 A 208 345 UNP Q8R316 Q8R316 208 345
SEQRES 1 A 142 GLY ALA MET ALA PRO SER THR ILE TRP HIS CYS PHE LEU
SEQRES 2 A 142 LYS GLY THR ARG LEU CYS PHE HIS LYS GLU SER ASN LYS
SEQRES 3 A 142 GLU TRP GLN ASP VAL GLU ASP PHE ALA ARG ALA ALA SER
SEQRES 4 A 142 CYS ASP ASN GLU GLU GLU ILE GLN MET GLY THR HIS LYS
SEQRES 5 A 142 GLY TYR GLY SER ASP GLY LEU LYS LEU LEU SER HIS GLU
SEQRES 6 A 142 GLU SER VAL SER PHE GLY GLU SER VAL LEU LYS LEU THR
SEQRES 7 A 142 PHE ASP PRO GLY THR VAL GLU ASP GLY LEU LEU THR VAL
SEQRES 8 A 142 GLU CYS LYS LEU ASP HIS PRO PHE TYR VAL LYS ASN LYS
SEQRES 9 A 142 GLY TRP SER SER PHE TYR PRO SER LEU THR VAL VAL GLN
SEQRES 10 A 142 HIS GLY ILE PRO CYS CYS GLU ILE HIS ILE GLY ASP VAL
SEQRES 11 A 142 CYS LEU PRO PRO GLY HIS PRO ASP ALA ILE ASN PHE
HELIX 1 1 VAL A 234 ALA A 241 1 8
HELIX 2 2 THR A 286 GLY A 290 5 5
HELIX 3 3 TYR A 313 GLY A 322 1 10
SHEET 1 AA 6 GLN A 232 ASP A 233 0
SHEET 2 AA 6 ARG A 220 PHE A 223 -1 O LEU A 221 N GLN A 232
SHEET 3 AA 6 LEU A 292 CYS A 296 -1 O THR A 293 N CYS A 222
SHEET 4 AA 6 GLU A 275 ASP A 283 -1 O LEU A 278 N CYS A 296
SHEET 5 AA 6 LEU A 262 SER A 272 -1 O LYS A 263 N ASP A 283
SHEET 6 AA 6 VAL A 333 CYS A 334 -1 O CYS A 334 N LEU A 262
SHEET 1 AB 3 PHE A 302 VAL A 304 0
SHEET 2 AB 3 GLY A 308 SER A 311 -1 O GLY A 308 N VAL A 304
SHEET 3 AB 3 CYS A 326 GLU A 327 1 O CYS A 326 N SER A 311
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 25 2 Bytes