Header list of 2aga.pdb file
Complete list - g 9 2 Bytes
HEADER TRANSCRIPTION 26-JUL-05 2AGA
TITLE DE-UBIQUITINATING FUNCTION OF ATAXIN-3: INSIGHTS FROM THE SOLUTION
TITLE 2 STRUCTURE OF THE JOSEPHIN DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MACHADO-JOSEPH DISEASE PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: JOSEPHIN DOMAIN;
COMPND 5 SYNONYM: ATAXIN-3, SPINOCEREBELLAR ATAXIA TYPE 3 PROTEIN;
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: ATXN3, ATX3, MJD, MJD1, SCA3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX6P-1
KEYWDS POLYGLUTAMINE, UBIQUITIN, UIM, ATAXIA, VCP/P97, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Y.MAO,F.SENIC-MATUGLIA,P.DI FIORE,S.POLO,M.E.HODSDON,P.DE CAMILLI
REVDAT 4 14-JUN-23 2AGA 1 REMARK
REVDAT 3 05-FEB-20 2AGA 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2AGA 1 VERSN
REVDAT 1 30-AUG-05 2AGA 0
JRNL AUTH Y.MAO,F.SENIC-MATUGLIA,P.P.DI FIORE,S.POLO,M.E.HODSDON,
JRNL AUTH 2 P.DE CAMILLI
JRNL TITL DEUBIQUITINATING FUNCTION OF ATAXIN-3: INSIGHTS FROM THE
JRNL TITL 2 SOLUTION STRUCTURE OF THE JOSEPHIN DOMAIN.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 12700 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 16118278
JRNL DOI 10.1073/PNAS.0506344102
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 1.0.5, CYANA 1.0.5
REMARK 3 AUTHORS : GUENTERT (CYANA), GUENTERT (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2960 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 224 DIHEDRAL ANGLE RESTRAINTS,122 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 2AGA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-AUG-05.
REMARK 100 THE DEPOSITION ID IS D_1000033857.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.4
REMARK 210 IONIC STRENGTH : 20 MM KPO4
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2MM JOSEPHIN DOMAIN U-15N,13C;
REMARK 210 20MM PHOSPHATE BUFFER PH 6.4; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_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 : NMRPIPE 2.3, SPARKY 3.106
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: THIS 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 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 LEU A 45 H GLU A 49 1.36
REMARK 500 O PHE A 66 H GLN A 69 1.41
REMARK 500 O GLU A 37 H ILE A 41 1.43
REMARK 500 O MET A 51 H GLU A 55 1.44
REMARK 500 O THR A 59 H GLU A 61 1.44
REMARK 500 O GLU A 48 H ARG A 52 1.47
REMARK 500 O TYR A 152 H PHE A 156 1.48
REMARK 500 O GLN A 44 H GLU A 48 1.50
REMARK 500 O TRP A 135 H ILE A 148 1.51
REMARK 500 HD1 HIS A 11 OE1 GLN A 14 1.53
REMARK 500 H GLU A 95 O LYS A 171 1.54
REMARK 500 O CYS A 119 H PHE A 126 1.58
REMARK 500 O TYR A 63 H LEU A 67 1.60
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 LEU A 3 -47.90 86.12
REMARK 500 1 SER A 8 58.19 -155.07
REMARK 500 1 PHE A 10 -163.44 156.52
REMARK 500 1 GLU A 12 -103.99 -49.26
REMARK 500 1 LEU A 18 -50.69 -175.04
REMARK 500 1 GLN A 29 -5.35 78.94
REMARK 500 1 GLU A 31 -108.24 -56.19
REMARK 500 1 VAL A 58 7.47 49.65
REMARK 500 1 THR A 59 20.75 35.92
REMARK 500 1 SER A 60 -50.88 65.64
REMARK 500 1 SER A 71 -151.95 -84.85
REMARK 500 1 ASN A 73 -72.41 62.80
REMARK 500 1 MET A 74 165.53 177.55
REMARK 500 1 ASP A 76 21.12 -148.43
REMARK 500 1 SER A 101 106.32 -21.65
REMARK 500 1 ARG A 108 64.22 127.78
REMARK 500 1 LYS A 122 -84.44 53.95
REMARK 500 1 GLU A 123 -68.68 -109.11
REMARK 500 1 ASN A 139 -74.39 176.68
REMARK 500 1 SER A 140 -29.21 172.03
REMARK 500 1 THR A 143 25.35 46.82
REMARK 500 1 TYR A 165 106.96 158.26
REMARK 500 1 SER A 166 70.62 -167.72
REMARK 500 1 GLN A 184 -68.11 -161.80
REMARK 500 1 MET A 185 107.66 -42.85
REMARK 500 1 GLN A 189 -56.69 -177.53
REMARK 500 2 SER A 8 59.30 -151.67
REMARK 500 2 PHE A 10 -161.90 160.63
REMARK 500 2 GLU A 12 -101.44 -47.65
REMARK 500 2 SER A 17 37.54 33.64
REMARK 500 2 LEU A 18 -52.02 -121.14
REMARK 500 2 GLN A 29 112.57 68.00
REMARK 500 2 GLU A 31 101.26 -58.22
REMARK 500 2 THR A 59 14.74 52.72
REMARK 500 2 SER A 60 -49.17 77.13
REMARK 500 2 LEU A 67 -32.54 -35.26
REMARK 500 2 SER A 71 -157.93 -102.59
REMARK 500 2 ASN A 73 -73.76 64.76
REMARK 500 2 MET A 74 176.89 174.02
REMARK 500 2 ASN A 100 -64.25 -23.74
REMARK 500 2 SER A 101 110.91 -8.36
REMARK 500 2 ARG A 108 57.93 133.28
REMARK 500 2 ASN A 113 98.62 -20.35
REMARK 500 2 GLU A 114 97.58 -30.34
REMARK 500 2 ARG A 115 -149.34 -175.84
REMARK 500 2 LYS A 122 -90.55 35.24
REMARK 500 2 HIS A 124 139.38 97.24
REMARK 500 2 ASN A 139 -73.80 -174.83
REMARK 500 2 SER A 140 -27.95 169.55
REMARK 500 2 THR A 143 25.29 49.76
REMARK 500
REMARK 500 THIS ENTRY HAS 612 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6742 RELATED DB: BMRB
REMARK 900 NMR CHIMICAL SHIFTS
DBREF 2AGA A 6 190 UNP P54252 MJD1_HUMAN 1 185
SEQADV 2AGA GLY A 1 UNP P54252 CLONING ARTIFACT
SEQADV 2AGA PRO A 2 UNP P54252 CLONING ARTIFACT
SEQADV 2AGA LEU A 3 UNP P54252 CLONING ARTIFACT
SEQADV 2AGA GLY A 4 UNP P54252 CLONING ARTIFACT
SEQADV 2AGA SER A 5 UNP P54252 CLONING ARTIFACT
SEQRES 1 A 190 GLY PRO LEU GLY SER MET GLU SER ILE PHE HIS GLU LYS
SEQRES 2 A 190 GLN GLU GLY SER LEU CYS ALA GLN HIS CYS LEU ASN ASN
SEQRES 3 A 190 LEU LEU GLN GLY GLU TYR PHE SER PRO VAL GLU LEU SER
SEQRES 4 A 190 SER ILE ALA HIS GLN LEU ASP GLU GLU GLU ARG MET ARG
SEQRES 5 A 190 MET ALA GLU GLY GLY VAL THR SER GLU ASP TYR ARG THR
SEQRES 6 A 190 PHE LEU GLN GLN PRO SER GLY ASN MET ASP ASP SER GLY
SEQRES 7 A 190 PHE PHE SER ILE GLN VAL ILE SER ASN ALA LEU LYS VAL
SEQRES 8 A 190 TRP GLY LEU GLU LEU ILE LEU PHE ASN SER PRO GLU TYR
SEQRES 9 A 190 GLN ARG LEU ARG ILE ASP PRO ILE ASN GLU ARG SER PHE
SEQRES 10 A 190 ILE CYS ASN TYR LYS GLU HIS TRP PHE THR VAL ARG LYS
SEQRES 11 A 190 LEU GLY LYS GLN TRP PHE ASN LEU ASN SER LEU LEU THR
SEQRES 12 A 190 GLY PRO GLU LEU ILE SER ASP THR TYR LEU ALA LEU PHE
SEQRES 13 A 190 LEU ALA GLN LEU GLN GLN GLU GLY TYR SER ILE PHE VAL
SEQRES 14 A 190 VAL LYS GLY ASP LEU PRO ASP CYS GLU ALA ASP GLN LEU
SEQRES 15 A 190 LEU GLN MET ILE ARG VAL GLN GLN
HELIX 1 1 GLY A 4 ILE A 9 5 6
HELIX 2 2 ALA A 20 LEU A 28 1 9
HELIX 3 3 SER A 34 GLY A 57 1 24
HELIX 4 4 SER A 60 GLN A 68 1 9
HELIX 5 5 ILE A 82 GLY A 93 1 12
HELIX 6 6 SER A 101 ILE A 109 1 9
HELIX 7 7 SER A 149 GLY A 164 1 16
HELIX 8 8 CYS A 177 GLN A 184 1 8
SHEET 1 A 6 GLU A 95 LEU A 98 0
SHEET 2 A 6 ILE A 167 LYS A 171 -1 O LYS A 171 N GLU A 95
SHEET 3 A 6 SER A 116 ASN A 120 -1 N SER A 116 O VAL A 170
SHEET 4 A 6 TRP A 125 LEU A 131 -1 O PHE A 126 N CYS A 119
SHEET 5 A 6 GLN A 134 LEU A 138 -1 O PHE A 136 N ARG A 129
SHEET 6 A 6 GLU A 146 ILE A 148 -1 O ILE A 148 N TRP A 135
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 - g 9 2 Bytes