Header list of 1pqn.pdb file
Complete list - r 2 2 Bytes
HEADER CELL CYCLE 18-JUN-03 1PQN
TITLE DOMINANT NEGATIVE HUMAN HDIM1 (HDIM1 1-128)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SPLICEOSOMAL U5 SNRNP-SPECIFIC 15 KDA PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOMINANT NEGATIVE HUMAN HDIM1;
COMPND 5 SYNONYM: DIM1 PROTEIN HOMOLOG, THIOREDOXIN-LIKE U5 SNRNP PROTEIN U5-
COMPND 6 15KD;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DIM1;
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: PET29B
KEYWDS DIM1, DOMINANT NEGATIVE, CELL CYCLE, PRE-MRNA SPLICING, SNRNP, U5-15K
KEYWDS 2 SPLICEOSOMAL PROTEIN, THIOREDOXIN, TRANSCRIPTION, CLEAVAGE
EXPDTA SOLUTION NMR
NUMMDL 20
MDLTYP MINIMIZED AVERAGE
AUTHOR Y.Z.ZHANG,H.CHENG,K.L.GOULD,E.A.GOLEMIS,H.RODER
REVDAT 3 02-MAR-22 1PQN 1 REMARK
REVDAT 2 24-FEB-09 1PQN 1 VERSN
REVDAT 1 26-AUG-03 1PQN 0
JRNL AUTH Y.Z.ZHANG,H.CHENG,K.L.GOULD,E.A.GOLEMIS,H.RODER
JRNL TITL STRUCTURE, STABILITY AND FUNCTION OF HDIM1 INVESTIGATED BY
JRNL TITL 2 NMR, CIRCULAR DICHROISM AND MUTATIONAL ANALYSIS
JRNL REF BIOCHEMISTRY V. 42 9609 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12911302
JRNL DOI 10.1021/BI034486I
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.Z.ZHANG,K.L.GOULD,R.L.DUNBRACK JR.,H.CHENG,H.RODER,
REMARK 1 AUTH 2 E.A.GOLEMIS
REMARK 1 TITL THE EVOLUTIONARILY CONSERVED DIM1 PROTEIN DEFINES A NOVEL
REMARK 1 TITL 2 BRANCH OF THE THIOREDOXIN FOLD SUPERFAMILY
REMARK 1 REF PHYSIOL.GENOMICS V. 1 109 1999
REMARK 1 REFN ISSN 1094-8341
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.0, CNS 1.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1445 RESTRAINTS, 1294 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 67 DIHEDRAL ANGLE RESTRAINTS,84 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1PQN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000019508.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 7.65
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM HDIM1 1-128,U-15N; 10MM
REMARK 210 PHOSPHATE BUFFER; 95% H2O, 5% D2O, 0.2% 2,2-DIMETHYL-2-
REMARK 210 SILAPENTANE-5-SULFONATE (DSS), 0.04% NAN3; 1MM HDIM1 1-128,U-15N,
REMARK 210 13C; 10MM PHOSPHATE BUFFER; 95% H2O, 5% D2O, 0.2% 2,2-DIMETHYL-2-
REMARK 210 SILAPENTANE-5-SULFONATE (DSS), 0.04% NAN3; 1MM HDIM1 1-128,U-13C;
REMARK 210 10MM PHOSPHATE BUFFER; 100% D2O, 0.2% 2,2-DIMETHYL-2-
REMARK 210 SILAPENTANE-5-SULFONATE (DSS), 0.04% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98, CNS 1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 120
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: 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: 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 TYR A 3 -175.68 60.38
REMARK 500 1 LEU A 5 105.25 -49.87
REMARK 500 1 HIS A 7 -169.33 -110.02
REMARK 500 1 LEU A 8 134.06 -175.84
REMARK 500 1 ASN A 10 135.83 -177.96
REMARK 500 1 SER A 20 40.59 -90.21
REMARK 500 1 ASP A 23 -74.52 -155.89
REMARK 500 1 ARG A 24 -77.67 -165.12
REMARK 500 1 VAL A 25 -166.55 -118.46
REMARK 500 1 ALA A 49 -82.21 -103.32
REMARK 500 1 VAL A 52 20.69 -148.99
REMARK 500 1 THR A 64 -44.98 -159.13
REMARK 500 1 ASP A 68 54.04 -90.06
REMARK 500 1 PHE A 69 98.11 60.63
REMARK 500 1 LYS A 71 -69.24 67.95
REMARK 500 1 MET A 72 -40.24 -176.62
REMARK 500 1 TYR A 73 30.96 -144.13
REMARK 500 1 TYR A 76 -39.84 -177.15
REMARK 500 1 ASN A 98 -51.84 -139.74
REMARK 500 1 ASN A 100 146.90 62.70
REMARK 500 1 LYS A 101 176.00 -50.00
REMARK 500 1 ALA A 105 115.42 67.06
REMARK 500 1 MET A 106 102.67 -177.73
REMARK 500 1 GLU A 107 -35.17 179.50
REMARK 500 1 ASP A 108 -157.06 62.47
REMARK 500 1 GLN A 110 -75.10 -90.16
REMARK 500 1 LYS A 125 80.10 60.98
REMARK 500 1 ARG A 127 32.68 -166.22
REMARK 500 2 TYR A 3 -66.04 -105.94
REMARK 500 2 LEU A 5 106.20 -49.95
REMARK 500 2 GLU A 22 -66.95 -103.47
REMARK 500 2 ILE A 48 33.95 -144.62
REMARK 500 2 ALA A 49 -63.70 -108.57
REMARK 500 2 TYR A 59 122.13 -175.89
REMARK 500 2 PRO A 67 83.37 -69.21
REMARK 500 2 PHE A 69 -56.40 -155.68
REMARK 500 2 ASN A 70 -79.09 64.13
REMARK 500 2 LYS A 71 -69.39 68.35
REMARK 500 2 MET A 72 -46.04 -157.12
REMARK 500 2 TYR A 73 36.39 -156.40
REMARK 500 2 TYR A 76 -66.33 -160.35
REMARK 500 2 LYS A 88 -168.33 -106.65
REMARK 500 2 MET A 91 -86.35 -110.02
REMARK 500 2 ILE A 92 136.99 62.66
REMARK 500 2 THR A 96 -62.47 -163.97
REMARK 500 2 ASN A 100 95.79 -176.20
REMARK 500 2 ALA A 105 121.60 65.51
REMARK 500 2 MET A 106 103.34 -179.40
REMARK 500 2 GLU A 107 -32.46 179.92
REMARK 500 2 ASP A 108 -154.75 61.62
REMARK 500
REMARK 500 THIS ENTRY HAS 501 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QGV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF OXIDIZED FULL LENGTH HDIM1 PROTEIN
DBREF 1PQN A 2 128 UNP P83876 TXN4A_HUMAN 2 128
SEQRES 1 A 127 SER TYR MET LEU PRO HIS LEU HIS ASN GLY TRP GLN VAL
SEQRES 2 A 127 ASP GLN ALA ILE LEU SER GLU GLU ASP ARG VAL VAL VAL
SEQRES 3 A 127 ILE ARG PHE GLY HIS ASP TRP ASP PRO THR CYS MET LYS
SEQRES 4 A 127 MET ASP GLU VAL LEU TYR SER ILE ALA GLU LYS VAL LYS
SEQRES 5 A 127 ASN PHE ALA VAL ILE TYR LEU VAL ASP ILE THR GLU VAL
SEQRES 6 A 127 PRO ASP PHE ASN LYS MET TYR GLU LEU TYR ASP PRO CYS
SEQRES 7 A 127 THR VAL MET PHE PHE PHE ARG ASN LYS HIS ILE MET ILE
SEQRES 8 A 127 ASP LEU GLY THR GLY ASN ASN ASN LYS ILE ASN TRP ALA
SEQRES 9 A 127 MET GLU ASP LYS GLN GLU MET VAL ASP ILE ILE GLU THR
SEQRES 10 A 127 VAL TYR ARG GLY ALA ARG LYS GLY ARG GLY
HELIX 1 1 ASN A 10 SER A 20 1 11
HELIX 2 2 ASP A 35 ILE A 48 1 14
HELIX 3 3 GLU A 107 ALA A 123 1 17
SHEET 1 A 4 TYR A 59 ASP A 62 0
SHEET 2 A 4 VAL A 26 GLY A 31 1 N ARG A 29 O TYR A 59
SHEET 3 A 4 THR A 80 PHE A 85 -1 O PHE A 84 N VAL A 26
SHEET 4 A 4 LYS A 88 ILE A 90 -1 O ILE A 90 N PHE A 83
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