Header list of 1yzb.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSCRIPTION 28-FEB-05 1YZB
TITLE SOLUTION STRUCTURE OF THE JOSEPHIN DOMAIN OF ATAXIN-3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MACHADO-JOSEPH DISEASE PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN OF ATAXIN-3;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS PAPAIN-LIKE FOLD, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR G.NICASTRO,L.MASINO,R.P.MENON,P.P.KNOWLES,N.Q.MCDONALD,A.PASTORE
REVDAT 4 02-MAR-22 1YZB 1 REMARK
REVDAT 3 24-FEB-09 1YZB 1 VERSN
REVDAT 2 09-AUG-05 1YZB 1 JRNL
REVDAT 1 05-JUL-05 1YZB 0
JRNL AUTH G.NICASTRO,R.P.MENON,L.MASINO,P.P.KNOWLES,N.Q.MCDONALD,
JRNL AUTH 2 A.PASTORE
JRNL TITL THE SOLUTION STRUCTURE OF THE JOSEPHIN DOMAIN OF ATAXIN-3:
JRNL TITL 2 STRUCTURAL DETERMINANTS FOR MOLECULAR RECOGNITION
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 10493 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 16020535
JRNL DOI 10.1073/PNAS.0501732102
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.NICASTRO,L.MASINO,T.A.FRENKIEL,G.KELLY,J.MCCORMICK,
REMARK 1 AUTH 2 R.P.MENON,A.PASTORE
REMARK 1 TITL ASSIGNMENT OF THE 1H, 13C, AND 15N RESONANCES OF THE
REMARK 1 TITL 2 JOSEPHIN DOMAIN OF HUMAN ATAXIN-3
REMARK 1 REF J.BIOMOL.NMR V. 30 457 2004
REMARK 1 REFN ISSN 0925-2738
REMARK 1 PMID 15630566
REMARK 1 DOI 10.1007/S10858-004-4343-3
REMARK 1 REFERENCE 2
REMARK 1 AUTH L.MASINO,G.NICASTRO,R.P.MENON,F.DAL PIAZ,L.CALDER,A.PASTORE
REMARK 1 TITL CHARACTERIZATION OF THE STRUCTURE AND THE AMYLOIDOGENIC
REMARK 1 TITL 2 PROPERTIES OF THE JOSEPHIN DOMAIN OF THE
REMARK 1 TITL 3 POLYGLUTAMINE-CONTAINING PROTEIN ATAXIN-3
REMARK 1 REF J.MOL.BIOL. V. 344 1021 2004
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 15544810
REMARK 1 DOI 10.1016/J.JMB.2004.09.065
REMARK 1 REFERENCE 3
REMARK 1 AUTH L.MASINO,V.MUSI,R.P.MENON,P.FUSI,G.KELLY,T.A.FRENKIEL,
REMARK 1 AUTH 2 Y.TROTTIER,A.PASTORE
REMARK 1 TITL DOMAIN ARCHITECTURE OF THE POLYGLUTAMINE PROTEIN ATAXIN-3: A
REMARK 1 TITL 2 GLOBULAR DOMAIN FOLLOWED BY A FLEXIBLE TAIL
REMARK 1 REF FEBS LETT. V. 549 21 2003
REMARK 1 REFN ISSN 0014-5793
REMARK 1 PMID 12914917
REMARK 1 DOI 10.1016/S0014-5793(03)00748-8
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2000, ARIA 1.2
REMARK 3 AUTHORS : DELAGLIO F. (NMRPIPE), NILGES M. (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 5532 UNAMBIGUOUS AND 927 AMBIGUOUS RESTRAINTS, 114 DIHEDRAL
REMARK 3 ANGLE RESTRAINTS, 44 DISTANCE RESTRAINTS FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1YZB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032100.
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 : 20MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.4MM OF JOSEPHIN 15N, 13C; 20MM
REMARK 210 SODIUM PHOSPHATE BUFFER (PH 6.5);
REMARK 210 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ARIA 1.2
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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 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 HG LEU A 93 H ASN A 95 1.25
REMARK 500 O ARG A 110 HG SER A 111 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 LEU A 13 75.61 -67.02
REMARK 500 1 THR A 54 -76.05 -70.60
REMARK 500 1 SER A 55 -65.19 -158.98
REMARK 500 1 GLN A 63 22.46 -76.47
REMARK 500 1 ASP A 70 -66.35 -124.22
REMARK 500 1 ARG A 103 64.48 73.36
REMARK 500 1 LYS A 117 -76.33 66.92
REMARK 500 1 PRO A 170 90.52 -69.43
REMARK 500 2 GLU A 7 -93.39 -82.53
REMARK 500 2 LYS A 8 122.36 -176.72
REMARK 500 2 GLN A 24 19.85 82.64
REMARK 500 2 TYR A 27 -32.84 -130.37
REMARK 500 2 SER A 55 -58.97 73.72
REMARK 500 2 SER A 66 -149.89 -127.30
REMARK 500 2 ASP A 71 45.36 -75.66
REMARK 500 2 ARG A 103 63.59 70.59
REMARK 500 2 GLU A 109 -156.01 -84.16
REMARK 500 2 ARG A 110 -41.08 -130.43
REMARK 500 2 LYS A 117 -80.68 64.84
REMARK 500 2 PRO A 170 94.55 -64.74
REMARK 500 2 LEU A 177 54.58 -108.83
REMARK 500 2 ILE A 181 151.82 -46.93
REMARK 500 3 GLU A 2 -67.82 -98.03
REMARK 500 3 PHE A 5 97.91 -64.12
REMARK 500 3 LYS A 8 122.91 69.58
REMARK 500 3 THR A 54 43.77 -90.29
REMARK 500 3 SER A 55 -60.07 71.84
REMARK 500 3 ARG A 103 74.18 43.22
REMARK 500 3 ARG A 110 -60.86 -91.20
REMARK 500 3 LYS A 117 -86.07 67.46
REMARK 500 4 THR A 54 -75.21 -73.29
REMARK 500 4 SER A 55 -63.55 -169.65
REMARK 500 4 PRO A 65 45.81 -73.97
REMARK 500 4 SER A 66 -159.58 -130.85
REMARK 500 4 ASP A 70 -51.93 -123.08
REMARK 500 4 SER A 72 20.65 -75.31
REMARK 500 4 ASN A 95 52.37 -95.94
REMARK 500 4 ARG A 103 60.96 64.16
REMARK 500 4 GLU A 109 -160.90 -76.02
REMARK 500 4 LYS A 117 -75.25 69.00
REMARK 500 4 LEU A 133 73.02 -114.43
REMARK 500 4 CYS A 172 -165.94 -114.19
REMARK 500 5 GLU A 7 -158.80 -76.68
REMARK 500 5 SER A 12 -102.41 -98.82
REMARK 500 5 GLN A 24 30.17 71.27
REMARK 500 5 THR A 54 39.64 -89.94
REMARK 500 5 SER A 55 -62.46 72.94
REMARK 500 5 GLN A 63 22.83 -76.02
REMARK 500 5 SER A 66 -70.79 -86.73
REMARK 500 5 ARG A 103 89.13 63.98
REMARK 500
REMARK 500 THIS ENTRY HAS 100 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1YZB A 1 182 UNP P54252 MJD1_HUMAN 1 182
SEQRES 1 A 182 MET GLU SER ILE PHE HIS GLU LYS GLN GLU GLY SER LEU
SEQRES 2 A 182 CYS ALA GLN HIS CYS LEU ASN ASN LEU LEU GLN GLY GLU
SEQRES 3 A 182 TYR PHE SER PRO VAL GLU LEU SER SER ILE ALA HIS GLN
SEQRES 4 A 182 LEU ASP GLU GLU GLU ARG MET ARG MET ALA GLU GLY GLY
SEQRES 5 A 182 VAL THR SER GLU ASP TYR ARG THR PHE LEU GLN GLN PRO
SEQRES 6 A 182 SER GLY ASN MET ASP ASP SER GLY PHE PHE SER ILE GLN
SEQRES 7 A 182 VAL ILE SER ASN ALA LEU LYS VAL TRP GLY LEU GLU LEU
SEQRES 8 A 182 ILE LEU PHE ASN SER PRO GLU TYR GLN ARG LEU ARG ILE
SEQRES 9 A 182 ASP PRO ILE ASN GLU ARG SER PHE ILE CYS ASN TYR LYS
SEQRES 10 A 182 GLU HIS TRP PHE THR VAL ARG LYS LEU GLY LYS GLN TRP
SEQRES 11 A 182 PHE ASN LEU ASN SER LEU LEU THR GLY PRO GLU LEU ILE
SEQRES 12 A 182 SER ASP THR TYR LEU ALA LEU PHE LEU ALA GLN LEU GLN
SEQRES 13 A 182 GLN GLU GLY TYR SER ILE PHE VAL VAL LYS GLY ASP LEU
SEQRES 14 A 182 PRO ASP CYS GLU ALA ASP GLN LEU LEU GLN MET ILE ARG
HELIX 1 1 LEU A 13 LEU A 23 1 11
HELIX 2 2 SER A 29 GLU A 50 1 22
HELIX 3 3 SER A 55 GLN A 63 1 9
HELIX 4 4 ILE A 77 VAL A 86 1 10
HELIX 5 5 ASP A 105 GLU A 109 5 5
HELIX 6 6 SER A 144 GLY A 159 1 16
HELIX 7 7 CYS A 172 LEU A 177 1 6
SHEET 1 A 6 GLU A 90 LEU A 93 0
SHEET 2 A 6 SER A 161 LYS A 166 -1 O LYS A 166 N GLU A 90
SHEET 3 A 6 SER A 111 TYR A 116 -1 N ASN A 115 O SER A 161
SHEET 4 A 6 HIS A 119 LEU A 126 -1 O VAL A 123 N PHE A 112
SHEET 5 A 6 GLN A 129 ASN A 134 -1 O LEU A 133 N THR A 122
SHEET 6 A 6 GLU A 141 ILE A 143 -1 O GLU A 141 N ASN A 132
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 2 2 Bytes