Header list of 2fi2.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSCRIPTION 27-DEC-05 2FI2
TITLE SOLUTION STRUCTURE OF THE SCAN HOMODIMER FROM MZF-1/ZNF42
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZINC FINGER PROTEIN 42;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SCAN DOMAIN, RESIDUES 37-128;
COMPND 5 SYNONYM: MYELOID ZINC FINGER 1, MZF-1, ZINC FINGER AND SCAN DOMAIN
COMPND 6 CONTAINING PROTEIN 6;
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: ZNF42, MZF1, ZSCAN6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SG13009[PREP4];
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE30GB1
KEYWDS SCAN DOMAIN, ZNF-42, MZF-1, HOMODIMER, TRANSCRIPTION FACTOR,
KEYWDS 2 STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, CENTER FOR
KEYWDS 3 EUKARYOTIC STRUCTURAL GENOMICS, CESG, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.F.VOLKMAN,F.C.PETERSON,T.L.SANDER,J.K.WALTNER,CENTER FOR EUKARYOTIC
AUTHOR 2 STRUCTURAL GENOMICS (CESG)
REVDAT 4 09-MAR-22 2FI2 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2FI2 1 VERSN
REVDAT 2 02-JAN-07 2FI2 1 JRNL SEQADV DBREF
REVDAT 1 17-JAN-06 2FI2 0
JRNL AUTH F.C.PETERSON,P.L.HAYES,J.K.WALTNER,A.K.HEISNER,D.R.JENSEN,
JRNL AUTH 2 T.L.SANDER,B.F.VOLKMAN
JRNL TITL STRUCTURE OF THE SCAN DOMAIN FROM THE TUMOR SUPPRESSOR
JRNL TITL 2 PROTEIN MZF1.
JRNL REF J.MOL.BIOL. V. 363 137 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16950398
JRNL DOI 10.1016/J.JMB.2006.07.063
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH 2.9.3.
REMARK 3 AUTHORS : SCHWIETERS, C.D., KUSZEWSKI, J.J., TJANDRA, N.,
REMARK 3 CLORE, G.M.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HOMODIMER STRUCTURES ARE BASED ON A TOTAL OF 4063 NOE CONSTRAINTS
REMARK 3 ( 843 INTRA, 818 SEQUENTIAL, 1029 MEDIUM, 750 INTRAMONOMER LONG
REMARK 3 RANGE AND 623 INTERMONOMER NOE CONSTRAINTS)
REMARK 3 AND 264 PHI AND PSI DIHEDRAL ANGLE CONSTRAINTS. CONSTRAINTS WERE
REMARK 3 ASSIGNED AND VALIDATED IN ONE MONOMER AND THEN DUPLICATED TO
REMARK 3 GENERATE A SYMMETRY RELATED CONSTRAINTS IN THE SECOND MONOMER.
REMARK 3 CONSTRAINT TOTALS LISTED ABOVE INCLUDE CONSTRAINTS FROM BOTH
REMARK 3 MONOMERS.
REMARK 4
REMARK 4 2FI2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000035902.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 99 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM ZNF-42 U-15N/13C, 20 MM
REMARK 210 SODIUM PHOSPHATE, 50 MM NACL, 90%
REMARK 210 H2O, 10% D2O; 1.7 MM ZNF-42 U-
REMARK 210 15N/13C, 1.7 MM UNLABELED ZNF-42,
REMARK 210 20 MM SODIUM PHOSPHATE, 50 MM
REMARK 210 NACL, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_13C-SEPARATED_NOESY (AROMATIC); 3D_13C-F1-
REMARK 210 FILTERED-13C-F3-SEPARATED_NOESY
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 : XWINNMR 3.5, NMRPIPE 2004,
REMARK 210 SPSCAN 1.1.0, XEASY 1.3, GARANT
REMARK 210 2.1, CYANA 2.1
REMARK 210 METHOD USED : AUTOMATED METHODS WERE USED FOR
REMARK 210 BACKBONE CHEMICAL SHIFT
REMARK 210 ASSIGNMENT AND ITERATIVE NOE
REMARK 210 REFINEMENT. FINAL STRUCTURES
REMARK 210 WERE OBTAINED BY MOLECULAR
REMARK 210 DYNAMICS IN EXPLICIT SOLVENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: ALL TRIPLE-RESONANCE AND NOESY SPECTRA WERE ACQUIRED USING
REMARK 210 A CRYOGENIC PROBE
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 HG SER B 79 OE1 GLU B 81 1.55
REMARK 500 HG SER A 79 OE1 GLU A 81 1.56
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 36 -174.80 -171.14
REMARK 500 1 ARG A 74 77.48 54.51
REMARK 500 1 ARG A 108 82.11 63.64
REMARK 500 1 GLU A 125 75.85 59.69
REMARK 500 1 PRO A 126 96.93 -20.88
REMARK 500 1 ARG B 74 74.06 52.39
REMARK 500 1 ARG B 108 87.58 68.86
REMARK 500 1 GLU B 125 99.75 62.69
REMARK 500 2 ARG A 74 78.73 53.25
REMARK 500 2 GLU A 125 132.32 70.72
REMARK 500 2 ARG B 74 81.06 59.30
REMARK 500 2 ARG B 108 78.41 59.53
REMARK 500 2 GLU B 125 95.51 68.66
REMARK 500 3 ARG A 74 82.51 66.50
REMARK 500 3 ARG A 108 80.54 61.97
REMARK 500 3 ARG A 124 -72.16 -161.02
REMARK 500 3 ARG B 74 76.29 60.76
REMARK 500 3 ARG B 108 80.17 63.27
REMARK 500 3 ARG B 124 -46.83 71.07
REMARK 500 4 ARG A 74 79.31 51.56
REMARK 500 4 ARG A 108 85.55 60.00
REMARK 500 4 ARG A 124 -78.14 65.97
REMARK 500 4 ARG B 74 76.64 53.23
REMARK 500 4 ARG B 108 79.60 57.71
REMARK 500 4 ARG B 124 -166.00 61.84
REMARK 500 5 ARG A 74 85.92 60.16
REMARK 500 5 GLN A 107 -60.03 -104.47
REMARK 500 5 ARG A 108 87.36 68.08
REMARK 500 5 ARG B 74 78.56 51.96
REMARK 500 5 GLN B 107 -61.98 -107.37
REMARK 500 5 ARG B 108 83.27 57.38
REMARK 500 6 SER A 36 -41.94 -161.79
REMARK 500 6 ASP A 37 96.42 65.42
REMARK 500 6 ARG A 74 87.78 48.66
REMARK 500 6 ARG A 108 86.73 65.72
REMARK 500 6 GLU A 125 79.26 66.61
REMARK 500 6 ASP B 37 113.60 63.52
REMARK 500 6 ARG B 74 77.83 55.86
REMARK 500 6 ARG B 108 78.00 54.23
REMARK 500 6 GLU B 125 93.23 65.08
REMARK 500 7 ARG A 74 77.20 60.72
REMARK 500 7 ARG A 108 87.05 64.53
REMARK 500 7 ARG A 123 18.05 -66.65
REMARK 500 7 ARG B 74 80.06 52.65
REMARK 500 7 PRO B 98 -51.51 -29.90
REMARK 500 7 ARG B 108 87.02 65.62
REMARK 500 7 ARG B 123 93.29 -66.47
REMARK 500 7 ARG B 124 -31.47 178.73
REMARK 500 8 ARG A 74 79.32 49.56
REMARK 500 8 ARG A 108 78.62 61.39
REMARK 500
REMARK 500 THIS ENTRY HAS 121 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 7 ARG B 48 0.08 SIDE CHAIN
REMARK 500 13 ARG A 44 0.07 SIDE CHAIN
REMARK 500 18 ARG B 124 0.09 SIDE CHAIN
REMARK 500 19 ARG B 123 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: GO.79132 RELATED DB: TARGETDB
DBREF 2FI2 A 37 128 UNP P28698 ZNF42_HUMAN 37 128
DBREF 2FI2 B 37 128 UNP P28698 ZNF42_HUMAN 37 128
SEQADV 2FI2 GLY A 35 UNP P28698 CLONING ARTIFACT
SEQADV 2FI2 SER A 36 UNP P28698 CLONING ARTIFACT
SEQADV 2FI2 GLY B 35 UNP P28698 CLONING ARTIFACT
SEQADV 2FI2 SER B 36 UNP P28698 CLONING ARTIFACT
SEQRES 1 A 94 GLY SER ASP PRO GLY PRO GLU ALA ALA ARG LEU ARG PHE
SEQRES 2 A 94 ARG CYS PHE HIS TYR GLU GLU ALA THR GLY PRO GLN GLU
SEQRES 3 A 94 ALA LEU ALA GLN LEU ARG GLU LEU CYS ARG GLN TRP LEU
SEQRES 4 A 94 ARG PRO GLU VAL ARG SER LYS GLU GLN MET LEU GLU LEU
SEQRES 5 A 94 LEU VAL LEU GLU GLN PHE LEU GLY ALA LEU PRO PRO GLU
SEQRES 6 A 94 ILE GLN ALA ARG VAL GLN GLY GLN ARG PRO GLY SER PRO
SEQRES 7 A 94 GLU GLU ALA ALA ALA LEU VAL ASP GLY LEU ARG ARG GLU
SEQRES 8 A 94 PRO GLY GLY
SEQRES 1 B 94 GLY SER ASP PRO GLY PRO GLU ALA ALA ARG LEU ARG PHE
SEQRES 2 B 94 ARG CYS PHE HIS TYR GLU GLU ALA THR GLY PRO GLN GLU
SEQRES 3 B 94 ALA LEU ALA GLN LEU ARG GLU LEU CYS ARG GLN TRP LEU
SEQRES 4 B 94 ARG PRO GLU VAL ARG SER LYS GLU GLN MET LEU GLU LEU
SEQRES 5 B 94 LEU VAL LEU GLU GLN PHE LEU GLY ALA LEU PRO PRO GLU
SEQRES 6 B 94 ILE GLN ALA ARG VAL GLN GLY GLN ARG PRO GLY SER PRO
SEQRES 7 B 94 GLU GLU ALA ALA ALA LEU VAL ASP GLY LEU ARG ARG GLU
SEQRES 8 B 94 PRO GLY GLY
HELIX 1 1 GLY A 39 CYS A 49 1 11
HELIX 2 2 GLY A 57 ARG A 74 1 18
HELIX 3 3 SER A 79 ALA A 95 1 17
HELIX 4 4 ILE A 100 ARG A 108 1 9
HELIX 5 5 SER A 111 ARG A 123 1 13
HELIX 6 6 GLY B 39 CYS B 49 1 11
HELIX 7 7 GLY B 57 ARG B 74 1 18
HELIX 8 8 SER B 79 ALA B 95 1 17
HELIX 9 9 ILE B 100 ARG B 108 1 9
HELIX 10 10 SER B 111 ARG B 123 1 13
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 - r 9 2 Bytes