Header list of 1tf3.pdb file
Complete list - v 3 2 Bytes
HEADER TRANSCRIPTION/DNA 01-JUL-97 1TF3
TITLE TFIIIA FINGER 1-3 BOUND TO DNA, NMR, 22 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5S RNA GENE;
COMPND 3 CHAIN: E;
COMPND 4 FRAGMENT: C-BLOCK, NT 79-93 OF 5S RNA GENE, NON-CODING AND CODING
COMPND 5 STRANDS;
COMPND 6 SYNONYM: 5S GENE;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: 5S RNA GENE;
COMPND 10 CHAIN: F;
COMPND 11 FRAGMENT: C-BLOCK, NT 79-93 OF 5S RNA GENE, NON-CODING AND CODING
COMPND 12 STRANDS;
COMPND 13 SYNONYM: 5S GENE;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: TRANSCRIPTION FACTOR IIIA;
COMPND 17 CHAIN: A;
COMPND 18 FRAGMENT: FINGERS 1-3 OF TFIIIA, RESIDUES 1, 11 - 101;
COMPND 19 SYNONYM: TFIIIA;
COMPND 20 ENGINEERED: YES;
COMPND 21 MUTATION: YES;
COMPND 22 OTHER_DETAILS: MINIMAL DNA BINDING, ZF1-3 CONTAINS THREE ZINC ATOMS,
COMPND 23 TETRAHEDRALLY COORDINATED BY TWO CYSTEINE AND TWO HISTIDINE SIDE
COMPND 24 CHAINS
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: GENE FRAGMENT ENCODING FINGERS 1-3 OF TFIIIA WAS
SOURCE 4 SUBCLONED INTO PET21A PLASMID AND EXPRESSED IN ESCHERICHIA COLI BL21
SOURCE 5 (DE3) CELLS. DNA OLIGONUCLEOTIDE WAS OBTAINED BY SOLID-PHASE
SOURCE 6 SYNTHESIS;
SOURCE 7 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES;
SOURCE 9 OTHER_DETAILS: GENE FRAGMENT ENCODING FINGERS 1-3 OF TFIIIA WAS
SOURCE 10 SUBCLONED INTO PET21A PLASMID AND EXPRESSED IN ESCHERICHIA COLI BL21
SOURCE 11 (DE3) CELLS. DNA OLIGONUCLEOTIDE WAS OBTAINED BY SOLID-PHASE
SOURCE 12 SYNTHESIS;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 15 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 16 ORGANISM_TAXID: 8355;
SOURCE 17 CELL_LINE: BL21;
SOURCE 18 CELL: OOCYTES;
SOURCE 19 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 20 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 21 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 22 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 23 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS TFIIIA, PROTEIN, DNA, TRANSCRIPTION FACTOR, 5S RNA GENE, DNA BINDING
KEYWDS 2 PROTEIN, ZINC FINGER, COMPLEX (TRANSCRIPTION REGULATION-DNA),
KEYWDS 3 TRANSCRIPTION-DNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 22
AUTHOR M.P.FOSTER,D.S.WUTTKE,I.RADHAKRISHNAN,D.A.CASE,J.M.GOTTESFELD,
AUTHOR 2 P.E.WRIGHT
REVDAT 3 03-NOV-21 1TF3 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1TF3 1 VERSN
REVDAT 1 17-SEP-97 1TF3 0
JRNL AUTH M.P.FOSTER,D.S.WUTTKE,I.RADHAKRISHNAN,D.A.CASE,
JRNL AUTH 2 J.M.GOTTESFELD,P.E.WRIGHT
JRNL TITL DOMAIN PACKING AND DYNAMICS IN THE DNA COMPLEX OF THE
JRNL TITL 2 N-TERMINAL ZINC FINGERS OF TFIIIA.
JRNL REF NAT.STRUCT.BIOL. V. 4 605 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9253405
JRNL DOI 10.1038/NSB0897-605
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.S.WUTTKE,M.P.FOSTER,D.A.CASE,J.M.GOTTESFELD,P.E.WRIGHT
REMARK 1 TITL SOLUTION STRUCTURE OF THE FIRST THREE ZINC FINGERS OF TFIIIA
REMARK 1 TITL 2 BOUND TO THE COGNATE DNA SEQUENCE: DETERMINANTS OF AFFINITY
REMARK 1 TITL 3 AND SEQUENCE SPECIFICITY
REMARK 1 REF J.MOL.BIOL. V. 273 183 1997
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,
REMARK 3 FERGUSON,SEIBEL,SINGH,WEINER,KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1TF3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176649.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NO
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AMBER
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 64
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22
REMARK 210 CONFORMERS, SELECTION CRITERIA : RESTRAINT ENERGIES < 11 KCAL, NO
REMARK 210 DISTANCE VIOLATIONS > 0.3 A
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, 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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 DT E 1 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 1 DT E 2 O4' - C1' - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 1 DG E 3 O4' - C1' - N9 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 DG E 4 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 1 DA E 5 O4' - C1' - N9 ANGL. DEV. = 4.9 DEGREES
REMARK 500 1 DG E 8 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 1 DG E 9 O4' - C1' - N9 ANGL. DEV. = 4.4 DEGREES
REMARK 500 1 DG E 11 O4' - C1' - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 DG E 15 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 1 DC F 16 O4' - C1' - N1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 DG F 17 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 1 DC F 20 O4' - C1' - N1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 DC F 22 O4' - C1' - N1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 1 DC F 23 O4' - C1' - N1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 1 DT F 26 O4' - C1' - N1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 DC F 27 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 1 DC F 28 O4' - C1' - N1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 2 DT E 1 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 2 DG E 3 O4' - C1' - N9 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 DA E 5 O4' - C1' - N9 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 DT E 6 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 2 DG E 7 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 2 DG E 8 O4' - C1' - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 DG E 9 O4' - C1' - N9 ANGL. DEV. = 3.3 DEGREES
REMARK 500 2 DG E 11 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 2 DC E 13 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 2 DG E 15 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 2 DC F 16 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 2 DC F 20 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 2 DT F 21 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 2 DC F 22 O4' - C1' - N1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 2 DC F 23 O4' - C1' - N1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 2 DT F 26 O4' - C1' - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 DC F 28 O4' - C1' - N1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 3 DT E 1 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 3 DG E 3 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 3 DA E 5 O4' - C1' - N9 ANGL. DEV. = 3.5 DEGREES
REMARK 500 3 DT E 6 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 3 DG E 9 O4' - C1' - N9 ANGL. DEV. = 4.9 DEGREES
REMARK 500 3 DG E 11 O4' - C1' - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 3 DC E 13 O4' - C1' - N1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 3 DG E 15 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 3 DC F 16 O4' - C1' - N1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 3 DG F 17 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 3 DG F 18 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 3 DC F 20 O4' - C1' - N1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 3 DC F 22 O4' - C1' - N1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 3 DC F 23 O4' - C1' - N1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 3 DT F 26 O4' - C1' - N1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 3 DC F 28 O4' - C1' - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 390 ANGLE DEVIATIONS.
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 ALA A 18 -65.29 -13.92
REMARK 500 1 PHE A 43 78.80 -112.36
REMARK 500 1 LYS A 46 -47.00 70.29
REMARK 500 1 HIS A 58 -40.41 74.48
REMARK 500 1 ASN A 72 -18.39 -145.97
REMARK 500 1 CYS A 80 44.26 -77.69
REMARK 500 1 HIS A 98 -64.48 -134.08
REMARK 500 2 ALA A 18 -65.20 -14.72
REMARK 500 2 LYS A 46 -35.36 68.18
REMARK 500 2 CYS A 50 47.67 -78.05
REMARK 500 2 CYS A 80 44.99 -77.72
REMARK 500 3 ASP A 19 -33.69 106.07
REMARK 500 3 LYS A 46 -50.17 70.54
REMARK 500 3 GLU A 47 132.10 -39.86
REMARK 500 3 CYS A 50 48.78 -78.73
REMARK 500 3 GLU A 70 45.95 -79.51
REMARK 500 3 CYS A 80 46.02 -78.07
REMARK 500 4 ALA A 18 -61.01 -19.30
REMARK 500 4 PHE A 43 76.88 -113.02
REMARK 500 4 LYS A 46 -44.95 71.53
REMARK 500 4 CYS A 50 46.19 -77.96
REMARK 500 4 CYS A 80 46.13 -77.87
REMARK 500 5 ARG A 12 80.29 74.90
REMARK 500 5 ALA A 18 -65.89 -13.35
REMARK 500 5 TYR A 24 -50.07 -143.22
REMARK 500 5 ASN A 25 -41.42 104.55
REMARK 500 5 LYS A 46 -43.18 68.30
REMARK 500 5 CYS A 50 46.43 -78.55
REMARK 500 5 CYS A 80 48.95 -78.34
REMARK 500 5 PHE A 97 -65.56 -105.25
REMARK 500 6 ALA A 18 -63.48 -15.02
REMARK 500 6 ASN A 25 0.55 -59.62
REMARK 500 6 PHE A 43 79.58 -111.67
REMARK 500 6 LYS A 46 -53.86 71.65
REMARK 500 6 CYS A 50 45.29 -78.49
REMARK 500 6 GLU A 70 49.11 -80.32
REMARK 500 6 CYS A 80 44.59 -77.85
REMARK 500 6 HIS A 98 -63.15 -134.02
REMARK 500 7 ALA A 18 -65.80 -13.88
REMARK 500 7 PHE A 43 79.61 -113.31
REMARK 500 7 GLU A 70 45.65 -79.34
REMARK 500 7 CYS A 80 48.79 -78.17
REMARK 500 7 PHE A 97 -70.47 -99.95
REMARK 500 8 ALA A 18 -64.55 -14.57
REMARK 500 8 LYS A 46 -31.96 65.57
REMARK 500 8 CYS A 50 49.81 -78.05
REMARK 500 8 CYS A 80 45.08 -77.64
REMARK 500 9 ALA A 18 -77.05 8.85
REMARK 500 9 PHE A 43 79.45 -110.12
REMARK 500 9 LYS A 46 46.01 -73.97
REMARK 500
REMARK 500 THIS ENTRY HAS 122 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 DG E 4 0.08 SIDE CHAIN
REMARK 500 1 DG E 11 0.08 SIDE CHAIN
REMARK 500 1 DA E 12 0.09 SIDE CHAIN
REMARK 500 1 DC E 13 0.08 SIDE CHAIN
REMARK 500 1 DT F 21 0.08 SIDE CHAIN
REMARK 500 1 DA F 25 0.06 SIDE CHAIN
REMARK 500 1 DT F 26 0.08 SIDE CHAIN
REMARK 500 1 DC F 28 0.08 SIDE CHAIN
REMARK 500 1 TYR A 13 0.08 SIDE CHAIN
REMARK 500 1 HIS A 37 0.10 SIDE CHAIN
REMARK 500 1 HIS A 58 0.08 SIDE CHAIN
REMARK 500 2 DT E 2 0.07 SIDE CHAIN
REMARK 500 2 DA E 10 0.06 SIDE CHAIN
REMARK 500 2 DG E 11 0.06 SIDE CHAIN
REMARK 500 2 DA E 12 0.05 SIDE CHAIN
REMARK 500 2 DC E 13 0.07 SIDE CHAIN
REMARK 500 2 DC E 14 0.11 SIDE CHAIN
REMARK 500 2 DG F 18 0.09 SIDE CHAIN
REMARK 500 2 DT F 19 0.07 SIDE CHAIN
REMARK 500 2 DC F 24 0.08 SIDE CHAIN
REMARK 500 2 DA F 25 0.08 SIDE CHAIN
REMARK 500 2 DT F 26 0.10 SIDE CHAIN
REMARK 500 2 DC F 27 0.07 SIDE CHAIN
REMARK 500 2 DC F 28 0.09 SIDE CHAIN
REMARK 500 2 TYR A 13 0.12 SIDE CHAIN
REMARK 500 2 PHE A 73 0.08 SIDE CHAIN
REMARK 500 3 DT E 2 0.06 SIDE CHAIN
REMARK 500 3 DG E 9 0.08 SIDE CHAIN
REMARK 500 3 DA E 10 0.05 SIDE CHAIN
REMARK 500 3 DC E 13 0.08 SIDE CHAIN
REMARK 500 3 DT F 21 0.07 SIDE CHAIN
REMARK 500 3 DA F 25 0.05 SIDE CHAIN
REMARK 500 3 DT F 26 0.08 SIDE CHAIN
REMARK 500 3 DC F 28 0.08 SIDE CHAIN
REMARK 500 3 TYR A 13 0.13 SIDE CHAIN
REMARK 500 3 HIS A 37 0.10 SIDE CHAIN
REMARK 500 4 DA E 12 0.06 SIDE CHAIN
REMARK 500 4 DC E 13 0.07 SIDE CHAIN
REMARK 500 4 DC E 14 0.08 SIDE CHAIN
REMARK 500 4 DC F 16 0.08 SIDE CHAIN
REMARK 500 4 DA F 25 0.06 SIDE CHAIN
REMARK 500 4 DT F 26 0.07 SIDE CHAIN
REMARK 500 4 DC F 27 0.06 SIDE CHAIN
REMARK 500 4 DC F 28 0.07 SIDE CHAIN
REMARK 500 4 TYR A 24 0.07 SIDE CHAIN
REMARK 500 4 HIS A 37 0.10 SIDE CHAIN
REMARK 500 5 DT E 2 0.06 SIDE CHAIN
REMARK 500 5 DG E 7 0.05 SIDE CHAIN
REMARK 500 5 DG E 8 0.08 SIDE CHAIN
REMARK 500 5 DA E 12 0.06 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 223 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 2 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 45 SG
REMARK 620 2 CYS A 50 SG 114.9
REMARK 620 3 HIS A 63 NE2 108.2 112.6
REMARK 620 4 HIS A 67 NE2 112.3 105.0 103.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 3 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 75 SG
REMARK 620 2 CYS A 80 SG 115.0
REMARK 620 3 HIS A 93 NE2 107.0 107.9
REMARK 620 4 HIS A 98 NE2 110.6 108.8 107.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 102 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 15 SG
REMARK 620 2 CYS A 20 SG 113.5
REMARK 620 3 HIS A 33 NE2 107.9 104.4
REMARK 620 4 HIS A 37 NE2 106.7 112.1 112.3
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 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3
DBREF 1TF3 A 1 101 UNP P03001 TF3A_XENLA 33 123
DBREF 1TF3 E 1 15 PDB 1TF3 1TF3 1 15
DBREF 1TF3 F 16 30 PDB 1TF3 1TF3 16 30
SEQADV 1TF3 MET A 1 UNP P03001 TYR 10 ENGINEERED MUTATION
SEQADV 1TF3 SER A 35 UNP P03001 CYS 35 ENGINEERED MUTATION
SEQRES 1 E 15 DT DT DG DG DA DT DG DG DG DA DG DA DC
SEQRES 2 E 15 DC DG
SEQRES 1 F 15 DC DG DG DT DC DT DC DC DC DA DT DC DC
SEQRES 2 F 15 DA DA
SEQRES 1 A 92 MET LYS ARG TYR ILE CYS SER PHE ALA ASP CYS GLY ALA
SEQRES 2 A 92 ALA TYR ASN LYS ASN TRP LYS LEU GLN ALA HIS LEU SER
SEQRES 3 A 92 LYS HIS THR GLY GLU LYS PRO PHE PRO CYS LYS GLU GLU
SEQRES 4 A 92 GLY CYS GLU LYS GLY PHE THR SER LEU HIS HIS LEU THR
SEQRES 5 A 92 ARG HIS SER LEU THR HIS THR GLY GLU LYS ASN PHE THR
SEQRES 6 A 92 CYS ASP SER ASP GLY CYS ASP LEU ARG PHE THR THR LYS
SEQRES 7 A 92 ALA ASN MET LYS LYS HIS PHE ASN ARG PHE HIS ASN ILE
SEQRES 8 A 92 LYS
HET ZN A 102 1
HET ZN A 2 1
HET ZN A 3 1
HETNAM ZN ZINC ION
FORMUL 4 ZN 3(ZN 2+)
HELIX 1 1 PHE A 17 GLY A 21 5 5
HELIX 2 2 ASN A 27 THR A 38 1 12
HELIX 3 3 LEU A 57 THR A 68 1 12
HELIX 4 4 LYS A 87 HIS A 98 1 12
SHEET 1 1 2 TYR A 13 ILE A 14 0
SHEET 2 1 2 ALA A 23 TYR A 24 -1
SHEET 1 2 2 PHE A 43 PRO A 44 0
SHEET 2 2 2 GLY A 53 PHE A 54 -1
SHEET 1 3 2 PHE A 73 THR A 74 0
SHEET 2 3 2 ARG A 83 PHE A 84 -1
LINK ZN ZN A 2 SG CYS A 45 1555 1555 2.31
LINK ZN ZN A 2 SG CYS A 50 1555 1555 2.30
LINK ZN ZN A 2 NE2 HIS A 63 1555 1555 2.09
LINK ZN ZN A 2 NE2 HIS A 67 1555 1555 2.09
LINK ZN ZN A 3 SG CYS A 75 1555 1555 2.30
LINK ZN ZN A 3 SG CYS A 80 1555 1555 2.30
LINK ZN ZN A 3 NE2 HIS A 93 1555 1555 2.09
LINK ZN ZN A 3 NE2 HIS A 98 1555 1555 2.10
LINK SG CYS A 15 ZN ZN A 102 1555 1555 2.30
LINK SG CYS A 20 ZN ZN A 102 1555 1555 2.30
LINK NE2 HIS A 33 ZN ZN A 102 1555 1555 2.09
LINK NE2 HIS A 37 ZN ZN A 102 1555 1555 2.10
SITE 1 AC1 4 CYS A 15 CYS A 20 HIS A 33 HIS A 37
SITE 1 AC2 4 CYS A 45 CYS A 50 HIS A 63 HIS A 67
SITE 1 AC3 4 CYS A 75 CYS A 80 HIS A 93 HIS A 98
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 - v 3 2 Bytes