Header list of 2alc.pdb file
Complete list - 3 202 Bytes
HEADER DNA BINDING PROTEIN 20-JAN-99 2ALC
TITLE ETHANOL REGULON TRANSCRIPTIONAL ACTIVATOR DNA-BINDING DOMAIN FROM
TITLE 2 ASPERGILLUS NIDULANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (ETHANOL REGULON TRANSCRIPTIONAL ACTIVATOR);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA-BINDING DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EMERICELLA NIDULANS;
SOURCE 3 ORGANISM_TAXID: 162425;
SOURCE 4 GENE: ALCR;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM
KEYWDS ZINC BINUCLEAR CLUSTER, DNA-BINDING, TRANSCRIPTIONAL ACTIVATOR, DNA
KEYWDS 2 BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR R.CERDAN,B.CAHUZAC,B.FELENBOK,E.GUITTET
REVDAT 5 03-NOV-21 2ALC 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 2ALC 1 VERSN
REVDAT 3 01-APR-03 2ALC 1 JRNL
REVDAT 2 14-FEB-00 2ALC 1 JRNL SEQADV
REVDAT 1 21-JAN-00 2ALC 0
JRNL AUTH R.CERDAN,B.CAHUZAC,B.FELENBOK,E.GUITTET
JRNL TITL NMR SOLUTION STRUCTURE OF ALCR (1-60) PROVIDES INSIGHT IN
JRNL TITL 2 THE UNUSUAL DNA BINDING PROPERTIES OF THIS ZINC BINUCLEAR
JRNL TITL 3 CLUSTER PROTEIN.
JRNL REF J.MOL.BIOL. V. 295 729 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10656785
JRNL DOI 10.1006/JMBI.1999.3417
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ALC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-99.
REMARK 100 THE DEPOSITION ID IS D_1000007239.
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 : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA, XPLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 17
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: MINIMIZED AVERAGE STRUCTURE. 15N-LABELED PROTEIN
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 SER A 0 -71.17 -159.83
REMARK 500 THR A 4 -65.07 -123.81
REMARK 500 GLN A 8 -63.23 -135.32
REMARK 500 ALA A 24 104.47 -37.46
REMARK 500 PRO A 25 -164.06 -78.65
REMARK 500 ASN A 27 50.55 -106.65
REMARK 500 TRP A 36 -179.75 -60.67
REMARK 500 VAL A 37 -44.65 -166.17
REMARK 500 ASN A 46 67.71 60.79
REMARK 500 LYS A 47 -119.89 -104.66
REMARK 500 PHE A 51 49.59 -109.39
REMARK 500 GLN A 57 -127.03 -82.22
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 64 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 12 SG
REMARK 620 2 CYS A 15 SG 107.8
REMARK 620 3 CYS A 22 SG 120.1 110.3
REMARK 620 4 CYS A 39 SG 97.6 110.4 109.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 65 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 12 SG
REMARK 620 2 CYS A 39 SG 97.8
REMARK 620 3 CYS A 42 SG 111.4 108.3
REMARK 620 4 CYS A 49 SG 111.6 115.5 111.6
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 64
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 65
DBREF 2ALC A 1 63 UNP P21228 ALCR_EMENI 1 63
SEQADV 2ALC GLY A -1 UNP P21228 INSERTION
SEQADV 2ALC SER A 0 UNP P21228 INSERTION
SEQADV 2ALC ASN A 61 UNP P21228 ALA 61 ENGINEERED MUTATION
SEQADV 2ALC SER A 62 UNP P21228 LYS 62 ENGINEERED MUTATION
SEQADV 2ALC SER A 63 UNP P21228 GLY 63 ENGINEERED MUTATION
SEQRES 1 A 65 GLY SER MET ALA ASP THR ARG ARG ARG GLN ASN HIS SER
SEQRES 2 A 65 CYS ASP PRO CYS ARG LYS GLY LYS ARG ARG CYS ASP ALA
SEQRES 3 A 65 PRO GLU ASN ARG ASN GLU ALA ASN GLU ASN GLY TRP VAL
SEQRES 4 A 65 SER CYS SER ASN CYS LYS ARG TRP ASN LYS ASP CYS THR
SEQRES 5 A 65 PHE ASN TRP LEU SER SER GLN ARG SER LYS ASN SER SER
HET ZN A 64 1
HET ZN A 65 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 ASP A 13 GLY A 18 1 6
HELIX 2 2 ARG A 28 ASN A 34 1 7
HELIX 3 3 SER A 40 TRP A 45 1 6
HELIX 4 4 ASN A 52 SER A 55 1 4
LINK SG CYS A 12 ZN ZN A 64 1555 1555 2.37
LINK SG CYS A 12 ZN ZN A 65 1555 1555 2.36
LINK SG CYS A 15 ZN ZN A 64 1555 1555 2.34
LINK SG CYS A 22 ZN ZN A 64 1555 1555 2.35
LINK SG CYS A 39 ZN ZN A 64 1555 1555 2.36
LINK SG CYS A 39 ZN ZN A 65 1555 1555 2.37
LINK SG CYS A 42 ZN ZN A 65 1555 1555 2.34
LINK SG CYS A 49 ZN ZN A 65 1555 1555 2.35
SITE 1 AC1 5 CYS A 12 CYS A 15 CYS A 22 CYS A 39
SITE 2 AC1 5 ZN A 65
SITE 1 AC2 5 CYS A 12 CYS A 39 CYS A 42 CYS A 49
SITE 2 AC2 5 ZN A 64
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
Complete list - 3 202 Bytes