Header list of 1jn7.pdb file
Complete list - 27 20 Bytes
HEADER TRANSCRIPTION 23-JUL-01 1JN7
TITLE SOLUTION STRUCTURE OF A CCHH MUTANT OF THE NINTH CCHC ZINC FINGER OF
TITLE 2 U-SHAPED
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: U-SHAPED TRANSCRIPTIONAL COFACTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: NINTH ZINC-FINGER DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 GENE: U-SHAPED;
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 ZINC FINGER, PROTEIN-PROTEIN INTERACTION, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.KOWALSKI,J.P.MACKAY
REVDAT 3 27-OCT-21 1JN7 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1JN7 1 VERSN
REVDAT 1 25-SEP-02 1JN7 0
JRNL AUTH K.KOWALSKI,C.K.LIEW,J.M.MATTHEWS,D.A.GELL,M.CROSSLEY,
JRNL AUTH 2 J.P.MACKAY
JRNL TITL CHARACTERIZATION OF THE CONSERVED INTERACTION BETWEEN GATA
JRNL TITL 2 AND FOG FAMILY PROTEINS
JRNL REF J.BIOL.CHEM. V. 277 35720 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 12110675
JRNL DOI 10.1074/JBC.M204663200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 0.5
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER ET AL (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JN7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000013962.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293; 293
REMARK 210 PH : 5.0; 5.0
REMARK 210 IONIC STRENGTH : 1.5MM ZNSO4; 0.75MM ZNSO4
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM PROTEIN; 1.5MM ZNSO4; 1.5MM
REMARK 210 TCEP; 95% H2O, 5% D2O; 0.5MM
REMARK 210 PROTEIN U-15N; 0.75MM ZNSO4;
REMARK 210 0.75MM TCEP; 95% H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; E-COSY; 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 : DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 500
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 STANDARD 2D HOMONUCLEAR
REMARK 210 TECHNIQUES
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 SER A 2 -169.40 -170.42
REMARK 500 1 ALA A 4 -70.41 -175.08
REMARK 500 1 GLU A 5 64.85 165.51
REMARK 500 1 MET A 7 171.99 64.26
REMARK 500 1 LYS A 8 -76.64 -147.25
REMARK 500 1 HIS A 32 39.17 -97.34
REMARK 500 1 LYS A 33 74.10 -177.74
REMARK 500 1 LYS A 35 56.49 -176.77
REMARK 500 2 ALA A 4 100.11 58.96
REMARK 500 2 GLU A 5 64.85 165.51
REMARK 500 2 MET A 7 79.98 -173.83
REMARK 500 2 LYS A 8 -85.23 -151.52
REMARK 500 2 LYS A 9 45.88 -147.00
REMARK 500 2 THR A 13 -34.87 -134.38
REMARK 500 2 HIS A 32 42.73 -96.12
REMARK 500 2 LYS A 33 44.34 -172.51
REMARK 500 2 ASN A 34 36.60 -174.24
REMARK 500 2 LYS A 35 84.46 59.92
REMARK 500 3 SER A 2 33.70 -166.65
REMARK 500 3 GLU A 5 64.96 165.45
REMARK 500 3 MET A 7 89.36 60.35
REMARK 500 3 THR A 13 -35.14 -134.42
REMARK 500 3 HIS A 32 42.43 -95.77
REMARK 500 3 LYS A 33 44.31 -168.89
REMARK 500 3 ASN A 34 36.94 -175.00
REMARK 500 3 LYS A 35 87.62 -174.97
REMARK 500 4 SER A 2 85.79 60.37
REMARK 500 4 ALA A 3 40.01 -109.69
REMARK 500 4 GLU A 5 64.80 165.48
REMARK 500 4 VAL A 6 57.08 -92.52
REMARK 500 4 MET A 7 82.13 -162.40
REMARK 500 4 LYS A 8 87.22 -178.48
REMARK 500 4 THR A 13 -34.96 -134.35
REMARK 500 4 HIS A 32 51.28 -113.16
REMARK 500 4 LYS A 33 54.76 -144.96
REMARK 500 5 ALA A 3 95.35 59.97
REMARK 500 5 GLU A 5 64.96 165.49
REMARK 500 5 MET A 7 83.96 61.62
REMARK 500 5 LYS A 8 -38.17 -179.15
REMARK 500 5 THR A 13 -35.07 -134.38
REMARK 500 5 HIS A 32 43.84 -98.06
REMARK 500 5 LYS A 33 44.60 -145.25
REMARK 500 5 ASN A 34 39.56 -160.52
REMARK 500 5 LYS A 35 153.31 61.31
REMARK 500 6 SER A 2 171.84 58.60
REMARK 500 6 ALA A 4 70.72 60.61
REMARK 500 6 GLU A 5 64.90 165.40
REMARK 500 6 MET A 7 62.44 -162.08
REMARK 500 6 THR A 13 -34.99 -134.47
REMARK 500 6 HIS A 32 39.68 -97.02
REMARK 500
REMARK 500 THIS ENTRY HAS 158 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 37 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 11 SG
REMARK 620 2 CYS A 14 SG 113.3
REMARK 620 3 HIS A 27 NE2 112.8 112.3
REMARK 620 4 HIS A 32 NE2 109.7 109.9 97.7
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 37
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FU9 RELATED DB: PDB
REMARK 900 1FU9 IS THE SOLUTION STRUCTURE OF THE NINTH ZINC-FINGER DOMAIN OF
REMARK 900 THE U-SHAPED TRANSCRIPTION FACTOR
REMARK 900 RELATED ID: 1FV5 RELATED DB: PDB
REMARK 900 1FV5 IS THE SOLUTION STRUCTURE OF THE FIRST ZINC FINGER FROM THE
REMARK 900 DROSOPHILA U-SHAPED TRANSCRIPTION FACTOR
DBREF 1JN7 A 3 36 UNP Q9VPQ6 USH_DROME 587 620
SEQADV 1JN7 GLY A 1 UNP Q9VPQ6 CLONING ARTIFACT
SEQADV 1JN7 SER A 2 UNP Q9VPQ6 CLONING ARTIFACT
SEQADV 1JN7 HIS A 32 UNP Q9VPQ6 CYS 616 ENGINEERED MUTATION
SEQRES 1 A 36 GLY SER ALA ALA GLU VAL MET LYS LYS TYR CYS SER THR
SEQRES 2 A 36 CYS ASP ILE SER PHE ASN TYR VAL LYS THR TYR LEU ALA
SEQRES 3 A 36 HIS LYS GLN PHE TYR HIS LYS ASN LYS PRO
HET ZN A 37 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 TYR A 20 TYR A 31 1 12
SHEET 1 A 2 TYR A 10 CYS A 11 0
SHEET 2 A 2 ILE A 16 SER A 17 -1 O ILE A 16 N CYS A 11
LINK SG CYS A 11 ZN ZN A 37 1555 1555 2.30
LINK SG CYS A 14 ZN ZN A 37 1555 1555 2.29
LINK NE2 HIS A 27 ZN ZN A 37 1555 1555 1.99
LINK NE2 HIS A 32 ZN ZN A 37 1555 1555 1.99
SITE 1 AC1 4 CYS A 11 CYS A 14 HIS A 27 HIS A 32
CRYST1 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