Header list of 1lpv.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION 08-MAY-02 1LPV
TITLE DROSOPHILA MELANOGASTER DOUBLESEX (DSX), NMR, 18 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DOUBLESEX PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE SEQUENCE NATURALLY OCCURS IN DROSOPHILA
SOURCE 4 MELANOGASTER (FRUIT FLY).
KEYWDS TRANSCRIPTION, DROSOPHILA MELANOGASTER, DNA BINDING, GENE REGULATION
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR L.ZHU,J.WILKEN,N.PHILLIPS,U.NARENDRA,G.CHAN,S.STRATTON,S.KENT,
AUTHOR 2 M.A.WEISS
REVDAT 4 23-FEB-22 1LPV 1 REMARK LINK
REVDAT 3 24-FEB-09 1LPV 1 VERSN
REVDAT 2 01-APR-03 1LPV 1 JRNL
REVDAT 1 02-OCT-02 1LPV 0
JRNL AUTH L.ZHU,J.WILKEN,N.B.PHILLIPS,U.NARENDRA,G.CHAN,S.M.STRATTON,
JRNL AUTH 2 S.B.KENT,M.A.WEISS
JRNL TITL SEXUAL DIMORPHISM IN DIVERSE METAZOANS IS REGULATED BY A
JRNL TITL 2 NOVEL CLASS OF INTERTWINED ZINC FINGERS.
JRNL REF GENES DEV. V. 14 1750 2000
JRNL REFN ISSN 0890-9369
JRNL PMID 10898790
JRNL DOI 10.1101/GAD.189500
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.E.ERDMAN,K.C.BURTIS
REMARK 1 TITL THE DROSOPHILA DOUBLESEX PROTEINS SHARE A NOVEL ZIN FINGER
REMARK 1 TITL 2 RELATED DNA-BINDING DOMAIN
REMARK 1 REF EMBO J. V. 12 527 1993
REMARK 1 REFN ISSN 0261-4189
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.S.RAYMOND,C.E.SHAMU,M.M.SHEN,K.J.SEIFERT,B.HIRSCH,
REMARK 1 AUTH 2 J.HODGKIN,D.ZARKOWER
REMARK 1 TITL EVIDENCE FOR EVOLUTIONARY CONSERVATION OF SEX-DETERMINING
REMARK 1 TITL 2 GENES
REMARK 1 REF NATURE V. 391 691 1998
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/35618
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 MOLECULAR MODELS WERE OBTAINED BY DGII IMPLEMENTED IN INSIGHT II
REMARK 3 (BIOSYM INC., SAN DIEGO, CA), FOLLOWED BY REFINEMENT WITH
REMARK 3 SIMULATED ANNEALING IN X-PLOR (T.F.HAVEL, A.T.BRUNGER). RESIDUE 1
REMARK 3 IN RESTRAINTS CORRESPONDS TO RESIDUE 35 IN DSX.
REMARK 3 TWO ZINC BINDING SITES ARE: C44,C47,H59,C63 AND H50,C68 C70, C73
REMARK 3 EACH IN A TETRAHEDRAL PATTERN.
REMARK 3 (I.E., 10,13,25,29 AND 16,34,36,39 IN THE COORDINATES). RESIDUE 35-
REMARK 3 40 AND 82-105 IN DEX ARE DISORDERED. STRUCTURES ARE GIVING FOR
REMARK 3 RESIDUES 35 TO 86, CORRESPONDING TO 1 TO 52 NUMBERED IN THE
REMARK 3 COORDINATES.
REMARK 3 NO MINOR CONFORMERS WERE DETECTED.
REMARK 4
REMARK 4 1LPV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-02.
REMARK 100 THE DEPOSITION ID IS D_1000016166.
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 : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; NOESY; COSY
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 : VNMR 5.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NMR EXPERIMENTS WERE CONDUCTED ON VARIAN INOVA 600 MHZ
REMARK 210 SPECTROMETERS. SOFTWARE VNMR5.1 AND FELIX WERE USED TO PROCESS
REMARK 210 NMR DATA. STRUCTURE DETERMINATION WAS PERFORMED ON A SILICON
REMARK 210 GRAPHICS WORK STATION. IN 50 MM DEUTERATED TRIS, 10 MM
REMARK 210 DEUTERATED DTT.
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-18
REMARK 470 RES CSSEQI ATOMS
REMARK 470 SER A 1 CA
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 26 H CYS A 29 1.47
REMARK 500 O CYS A 29 H ARG A 32 1.48
REMARK 500 O THR A 35 HH11 ARG A 40 1.50
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 ASN A 9 162.78 51.14
REMARK 500 1 THR A 21 -2.98 80.55
REMARK 500 1 LEU A 22 13.78 54.37
REMARK 500 1 HIS A 25 -101.49 -127.49
REMARK 500 1 LYS A 26 -91.90 41.11
REMARK 500 1 CYS A 34 169.66 -46.40
REMARK 500 1 CYS A 36 171.15 -46.22
REMARK 500 2 LEU A 22 25.77 47.58
REMARK 500 2 HIS A 25 -99.05 -109.19
REMARK 500 2 LYS A 26 -92.92 44.46
REMARK 500 2 CYS A 34 169.55 -46.91
REMARK 500 2 CYS A 36 168.57 -46.32
REMARK 500 2 GLN A 46 56.85 -113.52
REMARK 500 3 SER A 3 -64.12 -160.45
REMARK 500 3 LEU A 22 22.79 48.69
REMARK 500 3 HIS A 25 -101.01 -125.65
REMARK 500 3 LYS A 26 -93.60 43.15
REMARK 500 3 CYS A 34 168.93 -47.16
REMARK 500 3 CYS A 36 173.22 -48.92
REMARK 500 3 THR A 42 -70.89 -76.59
REMARK 500 3 VAL A 48 56.22 -93.40
REMARK 500 3 ALA A 50 -73.90 -151.49
REMARK 500 4 LEU A 22 18.68 50.40
REMARK 500 4 HIS A 25 -101.76 -132.76
REMARK 500 4 LYS A 26 -89.59 43.85
REMARK 500 4 CYS A 34 169.11 -44.79
REMARK 500 4 THR A 35 12.24 -145.09
REMARK 500 4 CYS A 36 -174.57 -54.69
REMARK 500 5 ILE A 2 160.27 58.81
REMARK 500 5 LEU A 22 20.98 46.51
REMARK 500 5 HIS A 25 -103.27 -119.51
REMARK 500 5 LYS A 26 -82.09 48.54
REMARK 500 5 PHE A 31 11.93 -142.48
REMARK 500 5 CYS A 34 170.04 -45.63
REMARK 500 5 CYS A 36 -177.46 -52.09
REMARK 500 5 ARG A 47 167.96 -48.43
REMARK 500 6 LEU A 22 23.80 47.26
REMARK 500 6 HIS A 25 -100.52 -124.66
REMARK 500 6 LYS A 26 -93.90 45.06
REMARK 500 6 CYS A 36 176.18 -49.33
REMARK 500 6 ARG A 45 -28.55 -37.71
REMARK 500 6 ARG A 47 84.26 -59.27
REMARK 500 7 PRO A 4 -159.68 -73.88
REMARK 500 7 THR A 21 5.88 82.52
REMARK 500 7 LEU A 22 26.03 42.04
REMARK 500 7 HIS A 25 -100.02 -117.45
REMARK 500 7 LYS A 26 -93.58 43.37
REMARK 500 7 CYS A 36 171.88 -48.08
REMARK 500 8 SER A 3 61.91 -158.51
REMARK 500 8 ARG A 5 40.15 -87.16
REMARK 500
REMARK 500 THIS ENTRY HAS 155 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 5 0.24 SIDE CHAIN
REMARK 500 1 ARG A 12 0.32 SIDE CHAIN
REMARK 500 1 ARG A 14 0.24 SIDE CHAIN
REMARK 500 1 ARG A 27 0.31 SIDE CHAIN
REMARK 500 1 ARG A 32 0.23 SIDE CHAIN
REMARK 500 1 ARG A 40 0.23 SIDE CHAIN
REMARK 500 1 ARG A 45 0.20 SIDE CHAIN
REMARK 500 1 ARG A 47 0.18 SIDE CHAIN
REMARK 500 2 ARG A 5 0.27 SIDE CHAIN
REMARK 500 2 ARG A 27 0.21 SIDE CHAIN
REMARK 500 2 ARG A 32 0.19 SIDE CHAIN
REMARK 500 2 ARG A 40 0.30 SIDE CHAIN
REMARK 500 2 ARG A 45 0.28 SIDE CHAIN
REMARK 500 2 ARG A 47 0.30 SIDE CHAIN
REMARK 500 3 ARG A 5 0.31 SIDE CHAIN
REMARK 500 3 ARG A 12 0.23 SIDE CHAIN
REMARK 500 3 ARG A 14 0.32 SIDE CHAIN
REMARK 500 3 ARG A 27 0.21 SIDE CHAIN
REMARK 500 3 ARG A 32 0.15 SIDE CHAIN
REMARK 500 3 ARG A 40 0.30 SIDE CHAIN
REMARK 500 3 ARG A 47 0.27 SIDE CHAIN
REMARK 500 4 ARG A 5 0.32 SIDE CHAIN
REMARK 500 4 ARG A 12 0.23 SIDE CHAIN
REMARK 500 4 ARG A 14 0.32 SIDE CHAIN
REMARK 500 4 ARG A 27 0.32 SIDE CHAIN
REMARK 500 4 ARG A 40 0.23 SIDE CHAIN
REMARK 500 4 ARG A 45 0.30 SIDE CHAIN
REMARK 500 4 ARG A 47 0.20 SIDE CHAIN
REMARK 500 5 ARG A 5 0.32 SIDE CHAIN
REMARK 500 5 ARG A 12 0.30 SIDE CHAIN
REMARK 500 5 ARG A 14 0.31 SIDE CHAIN
REMARK 500 5 ARG A 27 0.28 SIDE CHAIN
REMARK 500 5 ARG A 32 0.23 SIDE CHAIN
REMARK 500 5 ARG A 40 0.28 SIDE CHAIN
REMARK 500 5 ARG A 45 0.32 SIDE CHAIN
REMARK 500 5 ARG A 47 0.32 SIDE CHAIN
REMARK 500 6 ARG A 5 0.31 SIDE CHAIN
REMARK 500 6 ARG A 12 0.29 SIDE CHAIN
REMARK 500 6 ARG A 14 0.14 SIDE CHAIN
REMARK 500 6 ARG A 27 0.23 SIDE CHAIN
REMARK 500 6 ARG A 32 0.15 SIDE CHAIN
REMARK 500 6 ARG A 40 0.23 SIDE CHAIN
REMARK 500 6 ARG A 47 0.23 SIDE CHAIN
REMARK 500 7 ARG A 5 0.21 SIDE CHAIN
REMARK 500 7 ARG A 12 0.20 SIDE CHAIN
REMARK 500 7 ARG A 14 0.16 SIDE CHAIN
REMARK 500 7 ARG A 27 0.28 SIDE CHAIN
REMARK 500 7 ARG A 32 0.32 SIDE CHAIN
REMARK 500 7 ARG A 40 0.30 SIDE CHAIN
REMARK 500 7 ARG A 45 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 137 PLANE DEVIATIONS.
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 54 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 10 SG
REMARK 620 2 CYS A 13 SG 103.7
REMARK 620 3 HIS A 25 NE2 107.6 113.4
REMARK 620 4 CYS A 29 SG 105.9 122.6 102.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 53 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 16 NE2
REMARK 620 2 CYS A 34 SG 100.9
REMARK 620 3 CYS A 36 SG 100.5 112.9
REMARK 620 4 CYS A 39 SG 124.6 110.4 107.3
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 53
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 54
DBREF 1LPV A 1 52 UNP P23023 DSX_DROME 35 86
SEQRES 1 A 52 SER ILE SER PRO ARG THR PRO PRO ASN CYS ALA ARG CYS
SEQRES 2 A 52 ARG ASN HIS GLY LEU LYS ILE THR LEU LYS GLY HIS LYS
SEQRES 3 A 52 ARG TYR CYS LYS PHE ARG TYR CYS THR CYS GLU LYS CYS
SEQRES 4 A 52 ARG LEU THR ALA ASP ARG GLN ARG VAL MET ALA LEU GLN
HET ZN A 53 1
HET ZN A 54 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 CYS A 10 ASN A 15 1 6
HELIX 2 2 HIS A 25 CYS A 29 5 5
HELIX 3 3 CYS A 36 ARG A 47 1 12
LINK SG CYS A 10 ZN ZN A 54 1555 1555 2.21
LINK SG CYS A 13 ZN ZN A 54 1555 1555 2.31
LINK NE2 HIS A 16 ZN ZN A 53 1555 1555 2.03
LINK NE2 HIS A 25 ZN ZN A 54 1555 1555 2.07
LINK SG CYS A 29 ZN ZN A 54 1555 1555 2.27
LINK SG CYS A 34 ZN ZN A 53 1555 1555 2.27
LINK SG CYS A 36 ZN ZN A 53 1555 1555 2.27
LINK SG CYS A 39 ZN ZN A 53 1555 1555 2.27
SITE 1 AC1 4 HIS A 16 CYS A 34 CYS A 36 CYS A 39
SITE 1 AC2 5 CYS A 10 CYS A 13 ILE A 20 HIS A 25
SITE 2 AC2 5 CYS A 29
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 - b 23 2 Bytes