Header list of 1srk.pdb file
Complete list - 27 20 Bytes
HEADER TRANSCRIPTION 22-MAR-04 1SRK
TITLE SOLUTION STRUCTURE OF THE THIRD ZINC FINGER DOMAIN OF FOG-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZINC FINGER PROTEIN ZFPM1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 328-360;
COMPND 5 SYNONYM: ZINC FINGER PROTEIN MULTITYPE 1, FRIEND OF GATA PROTEIN 1,
COMPND 6 FRIEND OF GATA-1, FOG-1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ZFPM1, FOG1, FOG;
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: PGEX-2T
KEYWDS CLASSICAL ZINC FINGER, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.J.Y.SIMPSON,S.H.Y.LEE,N.BARTLE,J.M.MATTHEWS,J.P.MACKAY,M.CROSSLEY
REVDAT 3 27-OCT-21 1SRK 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1SRK 1 VERSN
REVDAT 1 21-SEP-04 1SRK 0
JRNL AUTH R.J.Y.SIMPSON,S.H.Y.LEE,N.BARTLE,E.Y.SUM,J.E.VISVADER,
JRNL AUTH 2 J.M.MATTHEWS,J.P.MACKAY,M.CROSSLEY
JRNL TITL A CLASSIC ZINC FINGER FROM FRIEND OF GATA MEDIATES AN
JRNL TITL 2 INTERACTION WITH THE COILED-COIL OF TRANSFORMING ACIDIC
JRNL TITL 3 COILED-COIL 3.
JRNL REF J.BIOL.CHEM. V. 279 39789 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15234987
JRNL DOI 10.1074/JBC.M404130200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, DYANA 1.5
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT ET AL (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: FINAL STRUCTURES WERE BASED ON 859
REMARK 3 UNAMBIGUOUS NOE-DERIVED DISTANCE CONSTRAINTS, 20 AMBIGUOUS
REMARK 3 CONSTRAINTS AND 31 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1SRK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021946.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 275; 275
REMARK 210 PH : 5.6; 5.6
REMARK 210 IONIC STRENGTH : 0 MM; 0 MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.27 MM FOG-F3, 2MM TCEP, 1 MM
REMARK 210 ZNSO4, 95% H2O, 5% D2O; 0.245 MM
REMARK 210 15N-FOG-F3, 2MM TCEP, 1 MM ZNSO4,
REMARK 210 95% H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY;
REMARK 210 HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, ARIA 1.2
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS, TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000
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: STRUCTURE WAS DETERMINED USING STANDARD 2D HOMONUCLEAR 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
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 SER A 2 -42.07 -174.81
REMARK 500 1 SER A 3 -152.93 -162.38
REMARK 500 1 PRO A 7 28.17 -72.29
REMARK 500 1 PHE A 8 53.18 -94.29
REMARK 500 1 CYS A 13 -128.52 -95.16
REMARK 500 1 LEU A 14 36.17 -153.66
REMARK 500 1 HIS A 30 42.20 -77.74
REMARK 500 1 THR A 31 -45.18 175.94
REMARK 500 2 LYS A 5 133.71 -173.30
REMARK 500 2 PRO A 7 4.30 -60.10
REMARK 500 2 CYS A 13 -123.38 -101.70
REMARK 500 2 LEU A 14 36.20 -157.26
REMARK 500 2 THR A 31 31.78 -176.39
REMARK 500 2 ASP A 32 130.61 -179.29
REMARK 500 3 LYS A 5 -145.85 -72.04
REMARK 500 3 ARG A 6 65.74 -159.07
REMARK 500 3 CYS A 13 -124.38 -96.24
REMARK 500 3 LEU A 14 37.46 -159.96
REMARK 500 3 HIS A 30 25.12 -79.82
REMARK 500 3 THR A 31 34.97 -179.95
REMARK 500 3 LEU A 34 43.62 -79.67
REMARK 500 4 SER A 3 -139.93 61.51
REMARK 500 4 CYS A 13 -122.53 -102.82
REMARK 500 4 LEU A 14 34.92 -159.54
REMARK 500 4 HIS A 30 43.10 -78.26
REMARK 500 4 THR A 31 -45.76 -177.93
REMARK 500 4 LEU A 34 -42.98 -161.08
REMARK 500 5 SER A 3 134.29 73.24
REMARK 500 5 PRO A 7 13.03 -65.87
REMARK 500 5 PHE A 8 48.31 -85.02
REMARK 500 5 CYS A 13 -124.89 -96.42
REMARK 500 5 LEU A 14 39.66 -160.09
REMARK 500 5 HIS A 30 47.56 -77.16
REMARK 500 5 THR A 31 -39.86 179.06
REMARK 500 5 LEU A 34 54.98 -151.78
REMARK 500 6 SER A 3 139.71 71.81
REMARK 500 6 CYS A 13 -121.87 -100.20
REMARK 500 6 LEU A 14 34.03 -159.84
REMARK 500 6 HIS A 30 34.30 -77.74
REMARK 500 6 THR A 31 -45.11 -162.28
REMARK 500 6 LEU A 34 44.93 -144.09
REMARK 500 7 SER A 3 136.35 -174.35
REMARK 500 7 ARG A 6 33.19 -98.78
REMARK 500 7 CYS A 13 -123.92 -104.52
REMARK 500 7 LEU A 14 39.48 -160.02
REMARK 500 7 THR A 31 32.29 -176.09
REMARK 500 7 ASP A 32 132.60 -170.92
REMARK 500 8 PRO A 7 24.83 -71.42
REMARK 500 8 PHE A 8 49.66 -91.50
REMARK 500 8 CYS A 13 -124.54 -99.15
REMARK 500
REMARK 500 THIS ENTRY HAS 137 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 36 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 10 SG
REMARK 620 2 CYS A 13 SG 105.6
REMARK 620 3 HIS A 26 NE2 107.9 112.7
REMARK 620 4 HIS A 30 NE2 109.2 112.4 108.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 36
DBREF 1SRK A 3 35 UNP O35615 FOG1_MOUSE 328 360
SEQADV 1SRK GLY A 1 UNP O35615 EXPRESSION TAG
SEQADV 1SRK SER A 2 UNP O35615 EXPRESSION TAG
SEQADV 1SRK LYS A 5 UNP O35615 GLU 330 ENGINEERED MUTATION
SEQADV 1SRK ARG A 11 UNP O35615 LEU 336 ENGINEERED MUTATION
SEQADV 1SRK ALA A 24 UNP O35615 GLU 349 ENGINEERED MUTATION
SEQRES 1 A 35 GLY SER SER GLY LYS ARG PRO PHE VAL CYS ARG ILE CYS
SEQRES 2 A 35 LEU SER ALA PHE THR THR LYS ALA ASN CYS ALA ARG HIS
SEQRES 3 A 35 LEU LYS VAL HIS THR ASP THR LEU SER
HET ZN A 36 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 THR A 19 LYS A 28 1 10
HELIX 2 2 VAL A 29 THR A 31 5 3
SHEET 1 A 2 PHE A 8 VAL A 9 0
SHEET 2 A 2 ALA A 16 PHE A 17 -1 O PHE A 17 N PHE A 8
LINK SG CYS A 10 ZN ZN A 36 1555 1555 2.24
LINK SG CYS A 13 ZN ZN A 36 1555 1555 2.31
LINK NE2 HIS A 26 ZN ZN A 36 1555 1555 1.95
LINK NE2 HIS A 30 ZN ZN A 36 1555 1555 1.95
SITE 1 AC1 4 CYS A 10 CYS A 13 HIS A 26 HIS A 30
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 - 27 20 Bytes