Header list of 1v66.pdb file
Complete list - r 2 2 Bytes
HEADER LIGASE 27-NOV-03 1V66
TITLE SOLUTION STRUCTURE OF HUMAN P53 BINDING DOMAIN OF PIAS-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN INHIBITOR OF ACTIVATED STAT PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-65;
COMPND 5 SYNONYM: PROTEIN INHIBITOR OF ACTIVATED STAT-1, PIAS-1, GU BINDING
COMPND 6 PROTEIN, GBP, RNA HELICASE II BINDING PROTEIN, DEAD/H BOX-BINDING
COMPND 7 PROTEIN 1;
COMPND 8 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;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS FOUR HELIX BUNDLE, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE,
KEYWDS 2 RSGI, STRUCTURAL GENOMICS, LIGASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.OKUBO,F.HARA,Y.TSUCHIDA,S.SHIMOTAKAHARA,S.SUZUKI,H.HATANAKA,
AUTHOR 2 S.YOKOYAMA,H.TANAKA,H.YASUDA,H.SHINDO,RIKEN STRUCTURAL
AUTHOR 3 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1V66 1 REMARK
REVDAT 2 24-FEB-09 1V66 1 VERSN
REVDAT 1 07-DEC-04 1V66 0
JRNL AUTH S.OKUBO,F.HARA,Y.TSUCHIDA,S.SHIMOTAKAHARA,S.SUZUKI,
JRNL AUTH 2 H.HATANAKA,S.YOKOYAMA,H.TANAKA,H.YASUDA,H.SHINDO
JRNL TITL NMR STRUCTURE OF THE N-TERMINAL DOMAIN OF SUMO LIGASE PIAS1
JRNL TITL 2 AND ITS INTERACTION WITH TUMOR SUPPRESSOR P53 AND A/T-RICH
JRNL TITL 3 DNA OLIGOMERS
JRNL REF J.BIOL.CHEM. V. 279 31455 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15133049
JRNL DOI 10.1074/JBC.M403561200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA
REMARK 3 AUTHORS : GUENTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V66 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000006255.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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 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 LYS A 34 H LEU A 38 1.50
REMARK 500 H ARG A 15 OE1 GLU A 18 1.55
REMARK 500 O VAL A 21 H TYR A 25 1.57
REMARK 500 O ARG A 62 H PHE A 65 1.58
REMARK 500 O GLN A 20 H GLY A 24 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 ALA A 2 -166.04 -173.86
REMARK 500 1 SER A 4 32.77 -94.85
REMARK 500 1 ARG A 28 155.88 -44.99
REMARK 500 1 HIS A 31 105.98 -173.47
REMARK 500 1 SER A 50 163.75 -42.60
REMARK 500 2 ALA A 2 128.27 -176.35
REMARK 500 2 SER A 4 -58.87 79.02
REMARK 500 2 ARG A 28 142.50 -38.82
REMARK 500 2 LYS A 30 -151.59 -109.73
REMARK 500 2 HIS A 31 105.97 64.71
REMARK 500 3 ALA A 2 139.35 74.13
REMARK 500 3 ASP A 3 -45.50 -158.04
REMARK 500 3 SER A 4 -56.71 174.36
REMARK 500 3 LYS A 30 -147.69 -95.33
REMARK 500 3 HIS A 31 115.01 69.95
REMARK 500 3 SER A 50 160.70 -41.05
REMARK 500 4 ASP A 3 -43.97 -163.65
REMARK 500 4 SER A 4 -55.75 172.42
REMARK 500 4 HIS A 31 87.84 -178.86
REMARK 500 4 SER A 50 160.34 -48.46
REMARK 500 5 ASP A 3 -45.64 -156.73
REMARK 500 5 SER A 4 -58.74 176.80
REMARK 500 5 ARG A 28 155.97 -44.42
REMARK 500 5 LYS A 30 -152.94 -121.62
REMARK 500 5 HIS A 31 116.03 72.59
REMARK 500 5 SER A 50 163.24 -44.43
REMARK 500 5 ARG A 63 -35.82 -39.40
REMARK 500 6 ASP A 3 -46.65 -150.79
REMARK 500 6 SER A 4 -46.65 173.90
REMARK 500 6 LEU A 14 153.74 -43.26
REMARK 500 6 HIS A 31 92.98 -165.97
REMARK 500 6 SER A 50 165.46 -46.16
REMARK 500 7 SER A 4 -58.94 84.61
REMARK 500 7 LEU A 14 157.36 -40.96
REMARK 500 7 HIS A 31 82.80 -176.32
REMARK 500 7 SER A 50 171.54 -59.53
REMARK 500 8 ALA A 2 108.09 72.06
REMARK 500 8 SER A 4 -59.11 84.68
REMARK 500 8 LEU A 14 154.43 -40.35
REMARK 500 8 HIS A 31 94.28 -171.15
REMARK 500 8 CYS A 49 141.32 62.88
REMARK 500 9 ASP A 3 -45.64 -130.17
REMARK 500 9 SER A 4 -59.36 164.61
REMARK 500 9 LYS A 30 -153.98 -129.00
REMARK 500 9 HIS A 31 112.22 62.41
REMARK 500 10 ASP A 3 -44.13 -163.38
REMARK 500 10 SER A 4 -55.22 171.43
REMARK 500 10 LEU A 14 152.37 -41.69
REMARK 500 11 ALA A 2 146.37 -176.79
REMARK 500 11 ASP A 3 -43.04 -166.86
REMARK 500
REMARK 500 THIS ENTRY HAS 103 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: AR_001000243.1 RELATED DB: TARGETDB
DBREF 1V66 A 1 65 UNP O75925 PIAS1_HUMAN 1 65
SEQRES 1 A 65 MET ALA ASP SER ALA GLU LEU LYS GLN MET VAL MET SER
SEQRES 2 A 65 LEU ARG VAL SER GLU LEU GLN VAL LEU LEU GLY TYR ALA
SEQRES 3 A 65 GLY ARG ASN LYS HIS GLY ARG LYS HIS GLU LEU LEU THR
SEQRES 4 A 65 LYS ALA LEU HIS LEU LEU LYS ALA GLY CYS SER PRO ALA
SEQRES 5 A 65 VAL GLN MET LYS ILE LYS GLU LEU TYR ARG ARG ARG PHE
HELIX 1 1 ALA A 5 MET A 12 1 8
HELIX 2 2 ARG A 15 TYR A 25 1 11
HELIX 3 3 ARG A 33 ALA A 47 1 15
HELIX 4 4 SER A 50 ARG A 64 1 15
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