HEADER DNA BINDING PROTEIN 28-APR-15 2N25
TITLE SOLUTION STRUCTURE OF MIZ-1 ZINC FINGER 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZINC FINGER AND BTB DOMAIN-CONTAINING PROTEIN 17;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 304-414;
COMPND 5 SYNONYM: MYC-INTERACTING ZINC FINGER PROTEIN 1, MIZ-1, ZINC FINGER
COMPND 6 PROTEIN 151, ZINC FINGER PROTEIN 60;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MIZ1, ZBTB17, ZNF151, ZNF60;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 STAR (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET-3A
KEYWDS MIZ-1, ZBTB17, C2H2 ZINC FINGER, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.BEDARD,P.LAVIGNE
REVDAT 3 14-JUN-23 2N25 1 REMARK SEQADV LINK
REVDAT 2 10-AUG-16 2N25 1 JRNL
REVDAT 1 17-JUN-15 2N25 0
JRNL AUTH C.TREMBLAY,M.BEDARD,M.A.BONIN,P.LAVIGNE
JRNL TITL SOLUTION STRUCTURE OF THE 13TH C2H2 ZINC FINGER OF MIZ-1.
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 473 471 2016
JRNL REFN ISSN 0006-291X
JRNL PMID 26972249
JRNL DOI 10.1016/J.BBRC.2016.03.034
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 2.2, ARIA 2.2, CNS 1.21
REMARK 3 AUTHORS : NILGES, RIEPING, HABECK, BARDIAUX, BERNARD AND
REMARK 3 MALLIAVIN (ARIA), NILGES, RIEPING, HABECK,
REMARK 3 BARDIAUX, BERNARD AND MALLIAVIN (ARIA), BRUNGER,
REMARK 3 ADAMS, CLORE, GROS, NILGES AND READ (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2N25 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000104326.
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 : 0.05
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.75 MM [U-13C; U-15N] MIZ1, 90%
REMARK 210 H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : CBCACONH (H[N[CO[{CA|CA[C]}]]]);
REMARK 210 3D HNCO; HNHA (H{[N]+[HA]}); 3D
REMARK 210 1H-15N NOESY; 2D 1H-15N HSQC/
REMARK 210 HMQC; 3D HNCACB; CCCONH (HNCO);
REMARK 210 3D 1H-13C NOESY; 3D HCCH-TOCSY;
REMARK 210 2D 1H-13C HSQC/HMQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYINOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.21, CCPNMR ANALYSIS 2.1,
REMARK 210 DANGLE 1.1, NMRPIPE 7.4
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 VAL A 2
REMARK 465 ILE A 3
REMARK 465 HIS A 4
REMARK 465 LYS A 5
REMARK 465 CYS A 6
REMARK 465 GLU A 7
REMARK 465 ASP A 8
REMARK 465 CYS A 9
REMARK 465 GLY A 10
REMARK 465 LYS A 11
REMARK 465 GLU A 12
REMARK 465 PHE A 13
REMARK 465 THR A 14
REMARK 465 HIS A 15
REMARK 465 THR A 16
REMARK 465 GLY A 17
REMARK 465 ASN A 18
REMARK 465 PHE A 19
REMARK 465 LYS A 20
REMARK 465 ARG A 21
REMARK 465 HIS A 22
REMARK 465 ILE A 23
REMARK 465 ARG A 24
REMARK 465 ILE A 25
REMARK 465 HIS A 26
REMARK 465 THR A 27
REMARK 465 GLY A 28
REMARK 465 GLU A 29
REMARK 465 PRO A 59
REMARK 465 TYR A 60
REMARK 465 GLY A 61
REMARK 465 CYS A 62
REMARK 465 GLU A 63
REMARK 465 GLU A 64
REMARK 465 CYS A 65
REMARK 465 GLY A 66
REMARK 465 LYS A 67
REMARK 465 SER A 68
REMARK 465 TYR A 69
REMARK 465 ARG A 70
REMARK 465 LEU A 71
REMARK 465 ILE A 72
REMARK 465 SER A 73
REMARK 465 LEU A 74
REMARK 465 LEU A 75
REMARK 465 ASN A 76
REMARK 465 LEU A 77
REMARK 465 HIS A 78
REMARK 465 LYS A 79
REMARK 465 LYS A 80
REMARK 465 ARG A 81
REMARK 465 HIS A 82
REMARK 465 SER A 83
REMARK 465 GLY A 84
REMARK 465 GLU A 85
REMARK 465 ALA A 86
REMARK 465 ARG A 87
REMARK 465 TYR A 88
REMARK 465 ARG A 89
REMARK 465 CYS A 90
REMARK 465 GLU A 91
REMARK 465 ASP A 92
REMARK 465 CYS A 93
REMARK 465 GLY A 94
REMARK 465 LYS A 95
REMARK 465 LEU A 96
REMARK 465 PHE A 97
REMARK 465 THR A 98
REMARK 465 THR A 99
REMARK 465 SER A 100
REMARK 465 GLY A 101
REMARK 465 ASN A 102
REMARK 465 LEU A 103
REMARK 465 LYS A 104
REMARK 465 ARG A 105
REMARK 465 HIS A 106
REMARK 465 GLN A 107
REMARK 465 LEU A 108
REMARK 465 VAL A 109
REMARK 465 HIS A 110
REMARK 465 SER A 111
REMARK 465 GLY A 112
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 3 SER A 55 79.00 -115.05
REMARK 500 12 PHE A 32 72.52 -119.14
REMARK 500 12 SER A 55 78.07 -113.44
REMARK 500 13 SER A 55 76.19 -118.61
REMARK 500 14 SER A 55 79.72 -115.85
REMARK 500 16 SER A 38 28.06 48.54
REMARK 500 17 PRO A 56 120.71 -34.40
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 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 34 SG
REMARK 620 2 CYS A 37 SG 106.5
REMARK 620 3 HIS A 50 NE2 96.8 108.3
REMARK 620 4 HIS A 54 NE2 107.0 112.9 123.0
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 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 25587 RELATED DB: BMRB
DBREF 2N25 A 2 112 UNP Q13105 ZBT17_HUMAN 304 414
SEQADV 2N25 MET A 1 UNP Q13105 INITIATING METHIONINE
SEQRES 1 A 112 MET VAL ILE HIS LYS CYS GLU ASP CYS GLY LYS GLU PHE
SEQRES 2 A 112 THR HIS THR GLY ASN PHE LYS ARG HIS ILE ARG ILE HIS
SEQRES 3 A 112 THR GLY GLU LYS PRO PHE SER CYS ARG GLU CYS SER LYS
SEQRES 4 A 112 ALA PHE SER ASP PRO ALA ALA CYS LYS ALA HIS GLU LYS
SEQRES 5 A 112 THR HIS SER PRO LEU LYS PRO TYR GLY CYS GLU GLU CYS
SEQRES 6 A 112 GLY LYS SER TYR ARG LEU ILE SER LEU LEU ASN LEU HIS
SEQRES 7 A 112 LYS LYS ARG HIS SER GLY GLU ALA ARG TYR ARG CYS GLU
SEQRES 8 A 112 ASP CYS GLY LYS LEU PHE THR THR SER GLY ASN LEU LYS
SEQRES 9 A 112 ARG HIS GLN LEU VAL HIS SER GLY
HET ZN A 201 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 ALA A 45 SER A 55 1 11
SHEET 1 A 2 PHE A 32 SER A 33 0
SHEET 2 A 2 ALA A 40 PHE A 41 -1 O PHE A 41 N PHE A 32
LINK SG CYS A 34 ZN ZN A 201 1555 1555 2.30
LINK SG CYS A 37 ZN ZN A 201 1555 1555 2.31
LINK NE2 HIS A 50 ZN ZN A 201 1555 1555 2.08
LINK NE2 HIS A 54 ZN ZN A 201 1555 1555 2.00
SITE 1 AC1 4 CYS A 34 CYS A 37 HIS A 50 HIS A 54
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
(ATOM LINES ARE NOT SHOWN.)
END