Header list of 1f4s.pdb file
Complete list - b 16 2 Bytes
HEADER TRANSCRIPTION/DNA 09-JUN-00 1F4S
TITLE STRUCTURE OF TRANSCRIPTIONAL FACTOR ALCR IN COMPLEX WITH A TARGET DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(P*CP*GP*TP*GP*CP*GP*GP*AP*TP*C)-3');
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: ALCR CONSENSUS HALF-TARGET;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA (5'-D(P*GP*AP*TP*CP*CP*GP*CP*AP*CP*G)-3');
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES;
COMPND 10 OTHER_DETAILS: ALCR CONSENSUS HALF-TARGET;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: ETHANOL REGULON TRANSCRIPTIONAL FACTOR;
COMPND 13 CHAIN: P;
COMPND 14 SYNONYM: REGULATORY PROTEIN ALCR;
COMPND 15 ENGINEERED: YES;
COMPND 16 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: EMERICELLA NIDULANS;
SOURCE 7 ORGANISM_TAXID: 162425;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN-DNA COMPLEX, ZINC BINUCLEAR CLUSTER PROTEIN, TRANSCRIPTION-
KEYWDS 2 DNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR B.CAHUZAC,R.CERDAN,B.FELENBOK,E.GUITTET
REVDAT 4 16-FEB-22 1F4S 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1F4S 1 VERSN
REVDAT 2 01-APR-03 1F4S 1 JRNL
REVDAT 1 28-SEP-01 1F4S 0
JRNL AUTH B.CAHUZAC,R.CERDAN,B.FELENBOK,E.GUITTET
JRNL TITL THE SOLUTION STRUCTURE OF AN ALCR-DNA COMPLEX SHEDS LIGHT
JRNL TITL 2 ONTO THE UNIQUE TIGHT AND MONOMERIC DNA BINDING OF A
JRNL TITL 3 ZN(2)CYS(6) PROTEIN.
JRNL REF STRUCTURE V. 9 827 2001
JRNL REFN ISSN 0969-2126
JRNL PMID 11566132
JRNL DOI 10.1016/S0969-2126(01)00640-2
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 1142 NOE-DERIVED CONSTRAINTS, 76 H-BOND CONSTRAINTS, 33 PHI ANGLE
REMARK 3 RESTRAINTS,
REMARK 3 118 LOOSE ANGLE RESTRAINTS ON THE DNA BACKBONE
REMARK 4
REMARK 4 1F4S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUN-00.
REMARK 100 THE DEPOSITION ID IS D_1000011242.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 5.9
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1 MM ALCR U-15N, 1.1 MM DOUBLE
REMARK 210 STRANDED DNA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : GIFA 4, DIANA
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS
REMARK 210 ARE THE 10 STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY.
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: A, B, P
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
REMARK 500 REMARK: NULL
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 2 DT A 9 C3' - C2' - C1' ANGL. DEV. = -4.9 DEGREES
REMARK 500 2 DC A 10 O4' - C4' - C3' ANGL. DEV. = -3.0 DEGREES
REMARK 500 2 DC A 10 C5' - C4' - C3' ANGL. DEV. = 8.6 DEGREES
REMARK 500 2 DC A 10 C5' - C4' - O4' ANGL. DEV. = -12.8 DEGREES
REMARK 500 2 DC A 10 C3' - C2' - C1' ANGL. DEV. = -5.8 DEGREES
REMARK 500 2 DC A 10 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 4 DC A 10 O4' - C4' - C3' ANGL. DEV. = -3.0 DEGREES
REMARK 500 4 DC A 10 C5' - C4' - C3' ANGL. DEV. = 8.5 DEGREES
REMARK 500 4 DC A 10 C5' - C4' - O4' ANGL. DEV. = -12.7 DEGREES
REMARK 500 4 DC A 10 C3' - C2' - C1' ANGL. DEV. = -5.8 DEGREES
REMARK 500 4 DC A 10 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 6 DC A 10 O4' - C4' - C3' ANGL. DEV. = -2.9 DEGREES
REMARK 500 6 DC A 10 C5' - C4' - C3' ANGL. DEV. = 8.5 DEGREES
REMARK 500 6 DC A 10 C5' - C4' - O4' ANGL. DEV. = -12.8 DEGREES
REMARK 500 6 DC A 10 C3' - C2' - C1' ANGL. DEV. = -5.8 DEGREES
REMARK 500 6 DC A 10 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 8 DC A 10 O4' - C4' - C3' ANGL. DEV. = -2.9 DEGREES
REMARK 500 8 DC A 10 C5' - C4' - C3' ANGL. DEV. = 8.4 DEGREES
REMARK 500 8 DC A 10 C5' - C4' - O4' ANGL. DEV. = -12.4 DEGREES
REMARK 500 8 DC A 10 C3' - C2' - C1' ANGL. DEV. = -5.8 DEGREES
REMARK 500 8 DC A 10 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 9 DG B 1 O4' - C4' - C3' ANGL. DEV. = -4.4 DEGREES
REMARK 500 9 DG B 1 C3' - C2' - C1' ANGL. DEV. = -9.2 DEGREES
REMARK 500 9 DA B 2 P - O5' - C5' ANGL. DEV. = -9.8 DEGREES
REMARK 500 10 DG A 2 C3' - C2' - C1' ANGL. DEV. = -5.5 DEGREES
REMARK 500 10 DC A 5 C3' - C2' - C1' ANGL. DEV. = -8.6 DEGREES
REMARK 500 10 DC B 5 C4' - C3' - C2' ANGL. DEV. = -5.5 DEGREES
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 P 0 -50.27 -149.98
REMARK 500 1 ARG P 5 -169.57 172.35
REMARK 500 1 ARG P 6 148.78 64.02
REMARK 500 1 ARG P 7 23.98 81.46
REMARK 500 1 ASN P 9 17.61 -169.90
REMARK 500 1 HIS P 10 119.33 39.93
REMARK 500 1 CYS P 22 -172.50 -171.54
REMARK 500 1 ALA P 24 97.03 -34.99
REMARK 500 1 PRO P 25 -159.69 -97.84
REMARK 500 1 TRP P 36 -123.14 -99.10
REMARK 500 1 VAL P 37 -82.06 156.89
REMARK 500 1 CYS P 39 -173.63 -53.30
REMARK 500 1 ASN P 41 -77.57 -76.25
REMARK 500 1 ASN P 46 47.15 28.06
REMARK 500 1 LYS P 47 -124.09 -72.81
REMARK 500 1 CYS P 49 91.21 -37.59
REMARK 500 1 ASN P 52 -74.37 -97.68
REMARK 500 1 ASN P 61 165.80 56.35
REMARK 500 1 SER P 62 -82.18 -82.57
REMARK 500 2 SER P 0 44.97 -150.05
REMARK 500 2 MET P 1 -45.23 -140.44
REMARK 500 2 ALA P 2 -76.83 -93.02
REMARK 500 2 ARG P 5 -164.48 -110.99
REMARK 500 2 ARG P 6 118.60 79.58
REMARK 500 2 ARG P 7 99.53 66.56
REMARK 500 2 GLN P 8 -43.24 -136.22
REMARK 500 2 ASN P 9 -8.06 -149.83
REMARK 500 2 HIS P 10 149.13 79.49
REMARK 500 2 LYS P 19 67.93 63.61
REMARK 500 2 CYS P 22 -166.63 -169.86
REMARK 500 2 ALA P 24 92.92 -38.93
REMARK 500 2 PRO P 25 -155.72 -99.18
REMARK 500 2 TRP P 36 -121.90 -119.33
REMARK 500 2 VAL P 37 -95.92 151.22
REMARK 500 2 CYS P 39 -169.40 -78.21
REMARK 500 2 ASN P 41 -85.08 -73.50
REMARK 500 2 ASN P 46 37.04 27.96
REMARK 500 2 LYS P 47 -122.53 -71.87
REMARK 500 2 ASP P 48 72.01 -150.61
REMARK 500 2 CYS P 49 85.06 -39.98
REMARK 500 2 ASN P 52 -81.19 -99.40
REMARK 500 2 SER P 55 -29.81 -39.71
REMARK 500 2 ARG P 58 -85.83 -82.89
REMARK 500 3 ARG P 6 128.13 63.99
REMARK 500 3 ARG P 7 -10.10 177.62
REMARK 500 3 GLN P 8 -155.27 -126.16
REMARK 500 3 ASN P 9 -12.81 -45.78
REMARK 500 3 HIS P 10 155.09 80.07
REMARK 500 3 LYS P 19 60.30 66.36
REMARK 500 3 VAL P 37 -83.96 -146.36
REMARK 500
REMARK 500 THIS ENTRY HAS 207 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 2 DC A 10 0.09 SIDE CHAIN
REMARK 500 4 DC A 10 0.08 SIDE CHAIN
REMARK 500 6 DC A 10 0.08 SIDE CHAIN
REMARK 500 6 DG B 6 0.07 SIDE CHAIN
REMARK 500 6 DC B 7 0.07 SIDE CHAIN
REMARK 500 8 DC A 10 0.08 SIDE CHAIN
REMARK 500 9 DG B 1 0.07 SIDE CHAIN
REMARK 500 10 DT A 3 0.10 SIDE CHAIN
REMARK 500 10 DG A 6 0.07 SIDE CHAIN
REMARK 500 10 DC B 5 0.12 SIDE CHAIN
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 P 64 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS P 12 SG
REMARK 620 2 CYS P 15 SG 115.6
REMARK 620 3 CYS P 22 SG 110.9 111.4
REMARK 620 4 CYS P 39 SG 95.5 107.9 114.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN P 65 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS P 12 SG
REMARK 620 2 CYS P 39 SG 95.4
REMARK 620 3 CYS P 42 SG 115.5 106.8
REMARK 620 4 CYS P 49 SG 107.2 119.7 111.7
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 P 64
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN P 65
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ALC RELATED DB: PDB
REMARK 900 ALCR(1-60), FREE PROTEIN, NMR MINIMIZED AVERAGED STRUCTURE
REMARK 900 RELATED ID: 3ALC RELATED DB: PDB
REMARK 900 ALCR(1-60), FREE PROTEIN, NMR, 17 STRUCTURES
DBREF 1F4S P 3 62 UNP P21228 ALCR_EMENI 1 60
DBREF 1F4S A 1 10 PDB 1F4S 1F4S 1 10
DBREF 1F4S B 1 10 PDB 1F4S 1F4S 1 10
SEQADV 1F4S GLY P -1 UNP P21228 INSERTION
SEQADV 1F4S SER P 0 UNP P21228 INSERTION
SEQADV 1F4S ASN P 61 UNP P21228 INSERTION
SEQADV 1F4S SER P 62 UNP P21228 INSERTION
SEQADV 1F4S SER P 63 UNP P21228 INSERTION
SEQRES 1 A 10 DC DG DT DG DC DG DG DA DT DC
SEQRES 1 B 10 DG DA DT DC DC DG DC DA DC DG
SEQRES 1 P 65 GLY SER MET ALA ASP THR ARG ARG ARG GLN ASN HIS SER
SEQRES 2 P 65 CYS ASP PRO CYS ARG LYS GLY LYS ARG ARG CYS ASP ALA
SEQRES 3 P 65 PRO GLU ASN ARG ASN GLU ALA ASN GLU ASN GLY TRP VAL
SEQRES 4 P 65 SER CYS SER ASN CYS LYS ARG TRP ASN LYS ASP CYS THR
SEQRES 5 P 65 PHE ASN TRP LEU SER SER GLN ARG SER LYS ASN SER SER
HET ZN P 64 1
HET ZN P 65 1
HETNAM ZN ZINC ION
FORMUL 4 ZN 2(ZN 2+)
FORMUL 6 HOH *(H2 O)
HELIX 1 1 CYS P 12 LYS P 19 1 8
HELIX 2 2 ASN P 27 ASN P 34 1 8
HELIX 3 3 CYS P 39 TRP P 45 1 7
HELIX 4 4 PHE P 51 ARG P 58 1 8
LINK SG CYS P 12 ZN ZN P 64 1555 1555 2.35
LINK SG CYS P 12 ZN ZN P 65 1555 1555 2.36
LINK SG CYS P 15 ZN ZN P 64 1555 1555 2.35
LINK SG CYS P 22 ZN ZN P 64 1555 1555 2.33
LINK SG CYS P 39 ZN ZN P 64 1555 1555 2.37
LINK SG CYS P 39 ZN ZN P 65 1555 1555 2.37
LINK SG CYS P 42 ZN ZN P 65 1555 1555 2.35
LINK SG CYS P 49 ZN ZN P 65 1555 1555 2.34
SITE 1 AC1 5 CYS P 12 CYS P 15 CYS P 22 CYS P 39
SITE 2 AC1 5 ZN P 65
SITE 1 AC2 5 CYS P 12 CYS P 39 CYS P 42 CYS P 49
SITE 2 AC2 5 ZN P 64
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 - b 16 2 Bytes