Header list of 2lef.pdb file
Complete list - v 3 2 Bytes
HEADER GENE REGULATION/DNA 13-OCT-98 2LEF
TITLE LEF1 HMG DOMAIN (FROM MOUSE), COMPLEXED WITH DNA (15BP), NMR, 12
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(*CP*AP*CP*CP*CP*TP*TP*TP*GP*AP*AP*GP*CP*TP*C)-
COMPND 3 3');
COMPND 4 CHAIN: B;
COMPND 5 FRAGMENT: LEF-1 BINDING SITE;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (5'-D(*GP*AP*GP*CP*TP*TP*CP*AP*AP*AP*GP*GP*GP*TP*G)-
COMPND 9 3');
COMPND 10 CHAIN: C;
COMPND 11 FRAGMENT: LEF-1 BINDING SITE;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: PROTEIN (LYMPHOID ENHANCER-BINDING FACTOR);
COMPND 15 CHAIN: A;
COMPND 16 FRAGMENT: HMG;
COMPND 17 SYNONYM: LEF-1 HMG;
COMPND 18 ENGINEERED: YES;
COMPND 19 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 7 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 8 ORGANISM_TAXID: 10090;
SOURCE 9 STRAIN: BL21 (DE3);
SOURCE 10 CELL: PRE-B AND T LYMPHOCYTE;
SOURCE 11 GENE: LEF1;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 14 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 15 EXPRESSION_SYSTEM_VECTOR: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET-21A;
SOURCE 17 EXPRESSION_SYSTEM_GENE: LEF1
KEYWDS LEF1, HMG, TCR-A, TRANSCRIPTION FACTOR, DNA BINDING, DNA BENDING,
KEYWDS 2 COMPLEX (HMG DOMAIN-DNA), GENE REGULATION-DNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 12
AUTHOR X.LI,J.J.LOVE,D.A.CASE,P.E.WRIGHT
REVDAT 4 03-NOV-21 2LEF 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2LEF 1 VERSN
REVDAT 2 29-DEC-99 2LEF 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 21-OCT-98 2LEF 0
SPRSDE 21-OCT-98 2LEF 1LEF
JRNL AUTH J.J.LOVE,X.LI,D.A.CASE,K.GIESE,R.GROSSCHEDL,P.E.WRIGHT
JRNL TITL STRUCTURAL BASIS FOR DNA BENDING BY THE ARCHITECTURAL
JRNL TITL 2 TRANSCRIPTION FACTOR LEF-1.
JRNL REF NATURE V. 376 791 1995
JRNL REFN ISSN 0028-0836
JRNL PMID 7651541
JRNL DOI 10.1038/376791A0
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 2LEF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008036.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : 10 MM KCL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : CT-HNCA; CBCA(CO)NH; HNCACB;
REMARK 210 C(CO)NH-TOCSY; HCCH-COSY; HCCH-
REMARK 210 TOCSY; (15N)3D NOESY-HSQC; (13C)
REMARK 210 3D NOESY-HSQC; (13C/13C)4D HMQC-
REMARK 210 NOESY-HMQC; 2D 13C/15N DOUBLE
REMARK 210 HALF-FILTERED NOESY; 3D 13C-
REMARK 210 SELECTED(W1; W2) 12C-FILTERED
REMARK 210 (W3) NOESY; 2D 1H NOESY;
REMARK 210 AROMATIC 13C CT-HSQC; HNCA-J;
REMARK 210 HNHA; HNHB; HACAHB-COSY; HMBC;
REMARK 210 3D LRCC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500; AMX600; DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX, DIANA, AMBER
REMARK 210 METHOD USED : DG IN TORSION SPACE (DIANA) AND
REMARK 210 DYNAMICAL SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 28
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 12
REMARK 210 CONFORMERS, SELECTION CRITERIA : CONSTRAINTS VIOLATION, AMBER
REMARK 210 ENERGIES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3
REMARK 210
REMARK 210 REMARK: PRESSURE: 1 ATM SOLVENT SYSTEM: 90%H2O/10%D2O,
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: B, C, 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 DC B 1 O4' - C1' - N1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 1 DT B 6 C6 - C5 - C7 ANGL. DEV. = -4.6 DEGREES
REMARK 500 1 DA B 11 O4' - C1' - N9 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 DC B 13 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 1 DT B 14 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 1 DG C 1 O4' - C1' - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 DA C 2 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 1 DG C 3 C1' - O4' - C4' ANGL. DEV. = -6.4 DEGREES
REMARK 500 1 DG C 3 O4' - C1' - N9 ANGL. DEV. = 7.0 DEGREES
REMARK 500 1 DT C 6 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 1 DA C 10 O4' - C1' - N9 ANGL. DEV. = 3.4 DEGREES
REMARK 500 1 DG C 12 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 1 DG C 13 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 1 DT C 14 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 1 DG C 15 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 2 DC B 1 O4' - C1' - N1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 DA B 2 O4' - C1' - N9 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 DC B 5 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 2 DA B 11 O4' - C1' - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 DG B 12 O4' - C4' - C3' ANGL. DEV. = 4.1 DEGREES
REMARK 500 2 DG B 12 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 2 DC B 13 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 2 DT B 14 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 2 DG C 1 O4' - C1' - N9 ANGL. DEV. = 3.9 DEGREES
REMARK 500 2 DA C 2 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 2 DG C 3 C1' - O4' - C4' ANGL. DEV. = -6.3 DEGREES
REMARK 500 2 DG C 3 O4' - C1' - N9 ANGL. DEV. = 6.6 DEGREES
REMARK 500 2 DC C 4 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 2 DT C 6 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 2 DA C 10 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 2 DG C 12 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 2 DG C 13 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 2 DT C 14 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 2 DG C 15 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 3 DC B 1 O4' - C1' - N1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 3 DA B 2 O4' - C1' - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 3 DC B 5 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 3 DT B 6 C6 - C5 - C7 ANGL. DEV. = -3.7 DEGREES
REMARK 500 3 DA B 10 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 3 DA B 11 C1' - O4' - C4' ANGL. DEV. = -6.5 DEGREES
REMARK 500 3 DA B 11 O4' - C1' - C2' ANGL. DEV. = -5.5 DEGREES
REMARK 500 3 DA B 11 O4' - C1' - N9 ANGL. DEV. = 4.2 DEGREES
REMARK 500 3 DG B 12 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 3 DT B 14 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 3 DG C 1 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 3 DG C 3 C1' - O4' - C4' ANGL. DEV. = -6.3 DEGREES
REMARK 500 3 DG C 3 O4' - C1' - N9 ANGL. DEV. = 6.4 DEGREES
REMARK 500 3 DA C 8 C4' - C3' - C2' ANGL. DEV. = -4.7 DEGREES
REMARK 500 3 DA C 8 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 3 DA C 10 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 216 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 LYS A 4 152.66 -45.75
REMARK 500 1 PRO A 6 96.26 -66.85
REMARK 500 1 LEU A 7 143.19 -39.12
REMARK 500 1 LYS A 28 -42.39 -137.08
REMARK 500 1 GLU A 29 106.29 -39.26
REMARK 500 1 PRO A 68 103.92 -46.09
REMARK 500 1 ARG A 73 73.55 -55.67
REMARK 500 1 ASN A 75 20.93 -152.59
REMARK 500 1 LYS A 81 143.36 71.14
REMARK 500 1 LYS A 83 -59.67 60.99
REMARK 500 1 ARG A 84 -73.96 72.38
REMARK 500 2 PRO A 6 84.38 -59.67
REMARK 500 2 LEU A 7 111.40 -39.74
REMARK 500 2 LYS A 28 -45.97 -142.07
REMARK 500 2 GLU A 29 103.97 -39.65
REMARK 500 2 SER A 71 58.20 -118.94
REMARK 500 2 ARG A 84 70.04 62.09
REMARK 500 2 GLU A 85 36.69 -75.11
REMARK 500 3 LYS A 4 150.13 -44.84
REMARK 500 3 LYS A 28 -33.98 -141.22
REMARK 500 3 PRO A 68 98.88 -42.49
REMARK 500 3 ARG A 73 70.29 -65.38
REMARK 500 3 ASN A 75 16.93 -151.98
REMARK 500 3 LYS A 81 100.56 -56.59
REMARK 500 4 PRO A 6 88.10 -65.55
REMARK 500 4 LEU A 7 121.16 -39.45
REMARK 500 4 LYS A 28 -40.23 -138.71
REMARK 500 4 GLU A 29 101.07 -38.98
REMARK 500 4 ARG A 73 69.28 -33.10
REMARK 500 4 LYS A 81 68.86 -62.75
REMARK 500 4 LYS A 83 -46.94 -133.28
REMARK 500 4 ARG A 84 -144.26 -157.31
REMARK 500 5 PRO A 6 96.34 -65.93
REMARK 500 5 LEU A 7 108.42 -39.66
REMARK 500 5 LYS A 28 -44.44 -132.80
REMARK 500 5 GLU A 29 102.32 -38.95
REMARK 500 5 TRP A 70 101.47 -59.55
REMARK 500 5 SER A 71 57.13 -119.22
REMARK 500 5 LYS A 81 82.72 -68.10
REMARK 500 5 ARG A 84 -64.54 65.61
REMARK 500 6 PRO A 6 92.35 -68.26
REMARK 500 6 LEU A 7 118.75 -39.72
REMARK 500 6 LYS A 28 -33.75 -144.77
REMARK 500 6 ARG A 73 91.83 -31.50
REMARK 500 6 ARG A 82 -94.02 -105.19
REMARK 500 7 PRO A 6 94.30 -66.55
REMARK 500 7 LEU A 7 127.80 -39.72
REMARK 500 7 LYS A 28 -39.47 -141.70
REMARK 500 7 GLU A 29 106.63 -39.37
REMARK 500 7 ALA A 31 -50.44 -168.92
REMARK 500
REMARK 500 THIS ENTRY HAS 85 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 DC B 4 0.12 SIDE CHAIN
REMARK 500 1 DA B 10 0.08 SIDE CHAIN
REMARK 500 1 DG B 12 0.14 SIDE CHAIN
REMARK 500 1 DT B 14 0.07 SIDE CHAIN
REMARK 500 1 DG C 3 0.09 SIDE CHAIN
REMARK 500 1 DC C 4 0.07 SIDE CHAIN
REMARK 500 1 DA C 8 0.08 SIDE CHAIN
REMARK 500 1 DA C 9 0.13 SIDE CHAIN
REMARK 500 1 DG C 12 0.08 SIDE CHAIN
REMARK 500 1 DG C 13 0.07 SIDE CHAIN
REMARK 500 1 TYR A 13 0.07 SIDE CHAIN
REMARK 500 1 TYR A 52 0.18 SIDE CHAIN
REMARK 500 1 TYR A 53 0.12 SIDE CHAIN
REMARK 500 1 ARG A 60 0.19 SIDE CHAIN
REMARK 500 1 ARG A 82 0.14 SIDE CHAIN
REMARK 500 2 DC B 4 0.13 SIDE CHAIN
REMARK 500 2 DC B 5 0.07 SIDE CHAIN
REMARK 500 2 DT B 6 0.07 SIDE CHAIN
REMARK 500 2 DG B 9 0.09 SIDE CHAIN
REMARK 500 2 DA B 10 0.07 SIDE CHAIN
REMARK 500 2 DG C 3 0.07 SIDE CHAIN
REMARK 500 2 DA C 8 0.07 SIDE CHAIN
REMARK 500 2 DA C 9 0.12 SIDE CHAIN
REMARK 500 2 TYR A 52 0.15 SIDE CHAIN
REMARK 500 2 TYR A 53 0.19 SIDE CHAIN
REMARK 500 2 TYR A 67 0.15 SIDE CHAIN
REMARK 500 2 ARG A 82 0.11 SIDE CHAIN
REMARK 500 3 DC B 4 0.13 SIDE CHAIN
REMARK 500 3 DG B 9 0.07 SIDE CHAIN
REMARK 500 3 DA B 10 0.06 SIDE CHAIN
REMARK 500 3 DG B 12 0.13 SIDE CHAIN
REMARK 500 3 DG C 3 0.09 SIDE CHAIN
REMARK 500 3 DT C 5 0.07 SIDE CHAIN
REMARK 500 3 DC C 7 0.11 SIDE CHAIN
REMARK 500 3 DA C 8 0.08 SIDE CHAIN
REMARK 500 3 DA C 9 0.13 SIDE CHAIN
REMARK 500 3 DG C 12 0.08 SIDE CHAIN
REMARK 500 3 TYR A 13 0.07 SIDE CHAIN
REMARK 500 3 TYR A 52 0.15 SIDE CHAIN
REMARK 500 3 TYR A 53 0.11 SIDE CHAIN
REMARK 500 3 TYR A 76 0.07 SIDE CHAIN
REMARK 500 4 DC B 4 0.10 SIDE CHAIN
REMARK 500 4 DT B 6 0.07 SIDE CHAIN
REMARK 500 4 DT B 7 0.07 SIDE CHAIN
REMARK 500 4 DG B 9 0.06 SIDE CHAIN
REMARK 500 4 DA B 10 0.05 SIDE CHAIN
REMARK 500 4 DA B 11 0.06 SIDE CHAIN
REMARK 500 4 DG B 12 0.13 SIDE CHAIN
REMARK 500 4 DG C 3 0.06 SIDE CHAIN
REMARK 500 4 DA C 9 0.12 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 157 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: S1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: DNA MINOR GROOVE PACKING AND HYDROGEN BONDING.
REMARK 800
REMARK 800 SITE_IDENTIFIER: S2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: DNA MINOR GROOVE INSERTION.
DBREF 2LEF A 1 86 UNP P27782 LEF1_MOUSE 295 380
DBREF 2LEF B 1 15 PDB 2LEF 2LEF 1 15
DBREF 2LEF C 1 15 PDB 2LEF 2LEF 1 15
SEQADV 2LEF MET A 1 UNP P27782 PRO 295 CONFLICT
SEQADV 2LEF SER A 25 UNP P27782 CYS 319 ENGINEERED MUTATION
SEQRES 1 B 15 DC DA DC DC DC DT DT DT DG DA DA DG DC
SEQRES 2 B 15 DT DC
SEQRES 1 C 15 DG DA DG DC DT DT DC DA DA DA DG DG DG
SEQRES 2 C 15 DT DG
SEQRES 1 A 86 MET HIS ILE LYS LYS PRO LEU ASN ALA PHE MET LEU TYR
SEQRES 2 A 86 MET LYS GLU MET ARG ALA ASN VAL VAL ALA GLU SER THR
SEQRES 3 A 86 LEU LYS GLU SER ALA ALA ILE ASN GLN ILE LEU GLY ARG
SEQRES 4 A 86 ARG TRP HIS ALA LEU SER ARG GLU GLU GLN ALA LYS TYR
SEQRES 5 A 86 TYR GLU LEU ALA ARG LYS GLU ARG GLN LEU HIS MET GLN
SEQRES 6 A 86 LEU TYR PRO GLY TRP SER ALA ARG ASP ASN TYR GLY LYS
SEQRES 7 A 86 LYS LYS LYS ARG LYS ARG GLU LYS
HELIX 1 1 ALA A 9 GLU A 24 1 16
HELIX 2 2 SER A 30 ALA A 43 1 14
HELIX 3 3 ARG A 46 LEU A 66 1 21
SITE 1 S1 1 TYR A 76
SITE 1 S2 2 MET A 11 MET A 14
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