HEADER TRANSCRIPTION 20-JUN-13 2M9W
TITLE SOLUTION NMR STRUCTURE OF TRANSCRIPTION FACTOR GATA-4 FROM HOMO
TITLE 2 SAPIENS, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET
TITLE 3 HR4783B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION FACTOR GATA-4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GATA-TYPE 2 ZINC FINGER RESIDUES 262-321;
COMPND 5 SYNONYM: GATA-BINDING FACTOR 4;
COMPND 6 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: GATA4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PMGK;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET15NANO6HT_NESG
KEYWDS STRUCTURAL GENOMICS, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG),
KEYWDS 2 PSI-BIOLOGY, PROTEIN STRUCTURE INITIATIVE, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR X.XU,A.ELETSKY,D.LEE,E.KOHN,H.JANJUA,R.XIAO,T.B.ACTON,J.K.EVERETT,
AUTHOR 2 G.T.MONTELIONE,T.SZYPERSKI,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 3 (NESG)
REVDAT 2 14-JUN-23 2M9W 1 REMARK SEQADV LINK
REVDAT 1 10-JUL-13 2M9W 0
JRNL AUTH X.XU,A.ELETSKY,D.LEE,E.KOHN,H.JANJUA,R.XIAO,T.ACTON,
JRNL AUTH 2 J.K.EVERETT,G.T.MONTELIONE,T.SZYPERSKI
JRNL TITL SOLUTION NMR STRUCTURE OF A TRANSCRIPTION FACTOR GATA-4 FROM
JRNL TITL 2 HOMO SAPIENS, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM
JRNL TITL 3 (NESG) TARGET HR4783B
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.3, CYANA 3.0, AUTOSTRUCTURE 2.1
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ
REMARK 3 (CNS), GUNTERT, MUMENTHALER AND WUTHRICH (CYANA),
REMARK 3 HUANG, TEJERO, POWERS AND MONTELIONE
REMARK 3 (AUTOSTRUCTURE)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURE DETERMINATION WAS PERFORMED
REMARK 3 BY RUNNNING CYANA AND ASDP IN PARALLEL USING NOE-BASED
REMARK 3 CONSTRAINTS AND PHI AND PSI DIHEDRAL ANGLE CONSTRAINTS FROM
REMARK 3 TALOS+. CONSENSUS PEAK ASSIGNMENTS WERE SELECTED AND USED IN
REMARK 3 ITERATIVE REFINEMENT WITH CYANA. THE 20 CONFORMERS OUT OF 100
REMARK 3 WITH THE LOWEST TARGET FUNCTION WERE FURTHER REFINED BY
REMARK 3 SIMULATED ANNEALING IN EXPLICIT WATER BATH USING THE PROGRAM CNS
REMARK 3 WITH PARAM19 FORCE FIELD.
REMARK 4
REMARK 4 2M9W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1000103392.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.378 MM [U-100% 13C; U-100%
REMARK 210 15N] HR4783B.009, 100 MM SODIUM
REMARK 210 CHLORIDE, 5 MM DTT, 10 MM TRIS-
REMARK 210 HCL, 50 UM DSS, 0.02 % SODIUM
REMARK 210 AZIDE, 50 UM ZINC ION, 90% H2O/
REMARK 210 10% D2O; 0.156 MM [U-5% 13C; U-
REMARK 210 100% 15N] HR4783B.009, 100 MM
REMARK 210 SODIUM CHLORIDE, 5 MM DTT, 10 MM
REMARK 210 TRIS-HCL, 50 UM DSS, 0.02 %
REMARK 210 SODIUM AZIDE, 50 UM ZINC ION, 90%
REMARK 210 H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D CT 1H-13C
REMARK 210 HSQC ALI; 3D HNCO; 3D CBCA(CO)NH;
REMARK 210 3D HNCACB; 2D CT 1H-13C HSQC
REMARK 210 ARO; 3D SIMUTANEOUS 13C-AROMATIC,
REMARK 210 13C-ALIPHATIC,15N EDITED 1H-1H
REMARK 210 NOESY; 3D CCH-TOCSY; 3D HBHA(CO)
REMARK 210 NH; 2D 1H-15N HSQC_HIS; 2D 1H-
REMARK 210 15N HSQC_WIDE; 3D (H)CCH-COSY
REMARK 210 ALI; 2D 1H-13C HSQC_METHYL
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.3, CYANA 3.0,
REMARK 210 AUTOSTRUCTURE 2.1, AUTOASSIGN
REMARK 210 2.3.1, XEASY, VNMRJ 2.3.1, TALOS+
REMARK 210 , PSVS 1.4, PROSA, CSI, CARA
REMARK 210 1.8.4
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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 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 ARG A 7 99.72 -53.26
REMARK 500 1 LEU A 11 -172.91 65.14
REMARK 500 1 ASN A 15 -68.13 -171.59
REMARK 500 1 GLN A 17 -1.95 68.73
REMARK 500 1 HIS A 44 -71.51 -124.83
REMARK 500 1 LEU A 50 -71.21 -113.38
REMARK 500 1 ALA A 51 35.81 -94.00
REMARK 500 1 MET A 52 173.47 69.08
REMARK 500 1 ARG A 53 44.66 -80.53
REMARK 500 1 GLU A 55 44.09 -91.71
REMARK 500 2 ASN A 15 -51.06 -172.34
REMARK 500 2 ASN A 27 -168.95 -76.97
REMARK 500 2 LEU A 50 -60.79 -91.23
REMARK 500 2 ALA A 51 -50.36 -139.27
REMARK 500 2 MET A 52 96.85 -68.51
REMARK 500 2 LYS A 54 83.83 -163.40
REMARK 500 2 GLN A 58 -44.76 79.97
REMARK 500 2 ARG A 62 40.75 -97.26
REMARK 500 3 ALA A 5 52.56 -90.43
REMARK 500 3 SER A 6 94.07 -67.01
REMARK 500 3 ASN A 15 -56.45 -171.35
REMARK 500 3 ARG A 53 97.70 -48.99
REMARK 500 3 ARG A 60 110.79 67.45
REMARK 500 4 LEU A 11 170.73 69.26
REMARK 500 4 GLU A 55 -172.60 60.50
REMARK 500 4 ILE A 57 94.68 48.46
REMARK 500 4 GLN A 58 99.22 -61.34
REMARK 500 4 ARG A 62 -54.35 74.45
REMARK 500 5 ASN A 15 -72.18 -103.03
REMARK 500 5 THR A 21 141.98 -170.87
REMARK 500 6 HIS A 2 53.47 -164.75
REMARK 500 6 CYS A 13 103.63 -55.14
REMARK 500 6 ASN A 15 -75.39 -94.16
REMARK 500 6 GLN A 17 69.95 61.66
REMARK 500 6 ARG A 48 109.47 -59.34
REMARK 500 6 LYS A 54 83.14 -69.14
REMARK 500 6 THR A 59 94.79 -63.78
REMARK 500 6 ARG A 62 100.92 63.69
REMARK 500 7 ARG A 7 72.21 55.60
REMARK 500 7 ASN A 27 -169.13 -71.17
REMARK 500 7 ILE A 57 75.97 56.48
REMARK 500 8 VAL A 9 88.07 63.43
REMARK 500 8 THR A 19 -47.20 67.63
REMARK 500 8 HIS A 44 -71.20 -129.14
REMARK 500 8 LEU A 50 -69.98 -100.07
REMARK 500 8 LYS A 61 24.74 -154.82
REMARK 500 9 HIS A 2 84.89 -68.09
REMARK 500 9 MET A 3 114.96 -161.49
REMARK 500 9 SER A 6 94.58 -66.91
REMARK 500 9 ASN A 15 -67.41 -175.38
REMARK 500
REMARK 500 THIS ENTRY HAS 136 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 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 13 SG
REMARK 620 2 CYS A 16 SG 100.2
REMARK 620 3 CYS A 34 SG 124.1 111.4
REMARK 620 4 CYS A 37 SG 109.8 106.7 103.7
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 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 19312 RELATED DB: BMRB
REMARK 900 RELATED ID: NESG-HR4783B RELATED DB: TARGETTRACK
DBREF 2M9W A 4 63 UNP P43694 GATA4_HUMAN 262 321
SEQADV 2M9W SER A 1 UNP P43694 EXPRESSION TAG
SEQADV 2M9W HIS A 2 UNP P43694 EXPRESSION TAG
SEQADV 2M9W MET A 3 UNP P43694 EXPRESSION TAG
SEQRES 1 A 63 SER HIS MET SER ALA SER ARG ARG VAL GLY LEU SER CYS
SEQRES 2 A 63 ALA ASN CYS GLN THR THR THR THR THR LEU TRP ARG ARG
SEQRES 3 A 63 ASN ALA GLU GLY GLU PRO VAL CYS ASN ALA CYS GLY LEU
SEQRES 4 A 63 TYR MET LYS LEU HIS GLY VAL PRO ARG PRO LEU ALA MET
SEQRES 5 A 63 ARG LYS GLU GLY ILE GLN THR ARG LYS ARG LYS
HET ZN A 101 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 ASN A 35 HIS A 44 1 10
SHEET 1 A 2 TRP A 24 ARG A 26 0
SHEET 2 A 2 PRO A 32 CYS A 34 -1 O VAL A 33 N ARG A 25
LINK SG CYS A 13 ZN ZN A 101 1555 1555 1.93
LINK SG CYS A 16 ZN ZN A 101 1555 1555 1.86
LINK SG CYS A 34 ZN ZN A 101 1555 1555 1.82
LINK SG CYS A 37 ZN ZN A 101 1555 1555 1.92
SITE 1 AC1 4 CYS A 13 CYS A 16 CYS A 34 CYS A 37
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