HEADER TRANSCRIPTION/DNA 20-APR-05 1ZG5
TITLE NARL COMPLEXED TO NARG-89 PROMOTER PALINDROMIC TAIL-TO-TAIL
TITLE 2 DNA SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-
COMPND 3 D(*CP*GP*TP*AP*CP*CP*CP*CP*TP*AP*TP*AP*GP*GP*GP*GP*TP*AP*CP
COMPND 4 *G)-3';
COMPND 5 CHAIN: C, D, G, H;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL;
COMPND 9 CHAIN: A, B, E, F;
COMPND 10 FRAGMENT: DNA BINDING DOMAIN (RESIDUES 147-216);
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SOLID PHASE SYNTHESIS;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 6 ORGANISM_TAXID: 562;
SOURCE 7 GENE: NARL;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PMJ05
KEYWDS PROTEIN-DNA COMPLEX, HELIX-TURN-HELIX, TWO-COMPONENT
KEYWDS 2 RESPONSE REGULATOR, DNA BENDING, TRANSCRIPTION/DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.E.MARIS,M.KACZOR-GRZESKOWIAK,Z.MA,M.L.KOPKA,R.P.GUNSALUS,
AUTHOR 2 R.E.DICKERSON
REVDAT 2 24-FEB-09 1ZG5 1 VERSN
REVDAT 1 22-NOV-05 1ZG5 0
JRNL AUTH A.E.MARIS,M.KACZOR-GRZESKOWIAK,Z.MA,M.L.KOPKA,
JRNL AUTH 2 R.P.GUNSALUS,R.E.DICKERSON
JRNL TITL PRIMARY AND SECONDARY MODES OF DNA RECOGNITION BY
JRNL TITL 2 THE NARL TWO-COMPONENT RESPONSE REGULATOR.
JRNL REF BIOCHEMISTRY V. 44 14538 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 16262254
JRNL DOI 10.1021/BI050734U
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.E.MARIS,M.R.SAWAYA,M.KACZOR-GRZESKOWIAK,
REMARK 1 AUTH 2 M.R.JARVIS,S.M.D.BEARSON,M.L.KOPKA,I.SCHROEDER,
REMARK 1 AUTH 3 R.P.GUNSALUS,R.E.DICKERSON
REMARK 1 TITL DIMERIZATION ALLOWS DNA TARGET SITE RECOGNITION BY
REMARK 1 TITL 2 THE NARL RESPONSE REGULATOR
REMARK 1 REF NAT.STRUCT.BIOL. V. 9 771 2002
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH I.BAIKALOV,I.SCHROEDER,M.KACZOR-GRZESKOWIAK,
REMARK 1 AUTH 2 K.GRZESKOWIAK,R.P.GUNSALUS,R.E.DICKERSON
REMARK 1 TITL STRUCTURE OF THE ESCHERICHIA COLI RESPONSE
REMARK 1 TITL 2 REGULATOR NARL
REMARK 1 REF BIOCHEMISTRY V. 35 11053 1996
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 30200
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1495
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3330
REMARK 3 BIN FREE R VALUE : 0.3840
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 230
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.025
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2201
REMARK 3 NUCLEIC ACID ATOMS : 1628
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.83900
REMARK 3 B22 (A**2) : 7.06500
REMARK 3 B33 (A**2) : -8.90500
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.35
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.40
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.187 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.036 ; 0.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.844 ; 0.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.910 ; 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 38.79
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER.PARAM
REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZG5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-APR-05.
REMARK 100 THE RCSB ID CODE IS RCSB032680.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34483
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : 0.13100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.68700
REMARK 200 R SYM FOR SHELL (I) : 0.95400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1JE8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 26.28500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: THE BIOLOGICAL UNIT IS A DIMER BOUND TO DNA. THERE ARE
REMARK 300 TWO BIOLOGICAL UNITS IN THE ASYMMETRIC UNIT (CHAINS A, B, C & D
REMARK 300 AND CHAINS E, F, G & H)
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, E, F
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MSE A 135
REMARK 465 ARG A 136
REMARK 465 GLY A 137
REMARK 465 SER A 138
REMARK 465 HIS A 139
REMARK 465 HIS A 140
REMARK 465 HIS A 141
REMARK 465 HIS A 142
REMARK 465 HIS A 143
REMARK 465 HIS A 144
REMARK 465 GLY A 145
REMARK 465 SER A 146
REMARK 465 ALA A 147
REMARK 465 THR A 148
REMARK 465 THR A 149
REMARK 465 GLU A 150
REMARK 465 MSE B 135
REMARK 465 ARG B 136
REMARK 465 GLY B 137
REMARK 465 SER B 138
REMARK 465 HIS B 139
REMARK 465 HIS B 140
REMARK 465 HIS B 141
REMARK 465 HIS B 142
REMARK 465 HIS B 143
REMARK 465 HIS B 144
REMARK 465 GLY B 145
REMARK 465 SER B 146
REMARK 465 ALA B 147
REMARK 465 THR B 148
REMARK 465 THR B 149
REMARK 465 GLU B 150
REMARK 465 MSE E 135
REMARK 465 ARG E 136
REMARK 465 GLY E 137
REMARK 465 SER E 138
REMARK 465 HIS E 139
REMARK 465 HIS E 140
REMARK 465 HIS E 141
REMARK 465 HIS E 142
REMARK 465 HIS E 143
REMARK 465 HIS E 144
REMARK 465 GLY E 145
REMARK 465 SER E 146
REMARK 465 ALA E 147
REMARK 465 THR E 148
REMARK 465 THR E 149
REMARK 465 MSE F 135
REMARK 465 ARG F 136
REMARK 465 GLY F 137
REMARK 465 SER F 138
REMARK 465 HIS F 139
REMARK 465 HIS F 140
REMARK 465 HIS F 141
REMARK 465 HIS F 142
REMARK 465 HIS F 143
REMARK 465 HIS F 144
REMARK 465 GLY F 145
REMARK 465 SER F 146
REMARK 465 ALA F 147
REMARK 465 THR F 148
REMARK 465 THR F 149
REMARK 465 GLU F 150
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 ARG A 214 63.89 39.11
REMARK 500 ASP E 152 109.39 63.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH H 48 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH A 321 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH D 62 DISTANCE = 5.63 ANGSTROMS
REMARK 525 HOH A 336 DISTANCE = 6.40 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 301
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 303
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 304
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 305
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 306
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 307
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 308
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 309
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 310
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 311
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 312
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZG1 RELATED DB: PDB
REMARK 900 NARL COMPLEX WITH NIRB PROMOTER NONPALINDROMIC DNA
REMARK 900 RELATED ID: 1JE8 RELATED DB: PDB
REMARK 900 NARL COMPLEX WITH NIRB PROMOTER PALINDROMIC DNA
REMARK 900 RELATED ID: 1RNL RELATED DB: PDB
REMARK 900 FULL-LENGTH UNACTIVATED NARL
REMARK 900 RELATED ID: 1A04 RELATED DB: PDB
REMARK 900 FULL-LENGTH UNACTIVATED NARL
DBREF 1ZG5 A 147 216 UNP P0AF28 NARL_ECOLI 147 216
DBREF 1ZG5 B 147 216 UNP P0AF28 NARL_ECOLI 147 216
DBREF 1ZG5 E 147 216 UNP P0AF28 NARL_ECOLI 147 216
DBREF 1ZG5 F 147 216 UNP P0AF28 NARL_ECOLI 147 216
DBREF 1ZG5 C 1 20 PDB 1ZG5 1ZG5 1 20
DBREF 1ZG5 D 21 40 PDB 1ZG5 1ZG5 21 40
DBREF 1ZG5 G 1 20 PDB 1ZG5 1ZG5 1 20
DBREF 1ZG5 H 21 40 PDB 1ZG5 1ZG5 21 40
SEQADV 1ZG5 MSE A 135 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 ARG A 136 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 GLY A 137 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 SER A 138 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS A 139 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS A 140 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS A 141 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS A 142 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS A 143 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS A 144 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 GLY A 145 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 SER A 146 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 MSE A 175 UNP P0AF28 MET 175 MODIFIED RESIDUE
SEQADV 1ZG5 MSE A 194 UNP P0AF28 MET 194 MODIFIED RESIDUE
SEQADV 1ZG5 MSE A 198 UNP P0AF28 MET 198 MODIFIED RESIDUE
SEQADV 1ZG5 MSE B 135 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 ARG B 136 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 GLY B 137 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 SER B 138 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS B 139 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS B 140 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS B 141 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS B 142 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS B 143 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS B 144 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 GLY B 145 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 SER B 146 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 MSE B 175 UNP P0AF28 MET 175 MODIFIED RESIDUE
SEQADV 1ZG5 MSE B 194 UNP P0AF28 MET 194 MODIFIED RESIDUE
SEQADV 1ZG5 MSE B 198 UNP P0AF28 MET 198 MODIFIED RESIDUE
SEQADV 1ZG5 MSE E 135 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 ARG E 136 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 GLY E 137 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 SER E 138 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS E 139 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS E 140 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS E 141 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS E 142 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS E 143 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS E 144 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 GLY E 145 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 SER E 146 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 MSE E 175 UNP P0AF28 MET 175 MODIFIED RESIDUE
SEQADV 1ZG5 MSE E 194 UNP P0AF28 MET 194 MODIFIED RESIDUE
SEQADV 1ZG5 MSE E 198 UNP P0AF28 MET 198 MODIFIED RESIDUE
SEQADV 1ZG5 MSE F 135 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 ARG F 136 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 GLY F 137 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 SER F 138 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS F 139 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS F 140 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS F 141 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS F 142 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS F 143 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 HIS F 144 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 GLY F 145 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 SER F 146 UNP P0AF28 EXPRESSION TAG
SEQADV 1ZG5 MSE F 175 UNP P0AF28 MET 175 MODIFIED RESIDUE
SEQADV 1ZG5 MSE F 194 UNP P0AF28 MET 194 MODIFIED RESIDUE
SEQADV 1ZG5 MSE F 198 UNP P0AF28 MET 198 MODIFIED RESIDUE
SEQRES 1 C 20 DC DG DT DA DC DC DC DC DT DA DT DA DG
SEQRES 2 C 20 DG DG DG DT DA DC DG
SEQRES 1 D 20 DC DG DT DA DC DC DC DC DT DA DT DA DG
SEQRES 2 D 20 DG DG DG DT DA DC DG
SEQRES 1 G 20 DC DG DT DA DC DC DC DC DT DA DT DA DG
SEQRES 2 G 20 DG DG DG DT DA DC DG
SEQRES 1 H 20 DC DG DT DA DC DC DC DC DT DA DT DA DG
SEQRES 2 H 20 DG DG DG DT DA DC DG
SEQRES 1 A 82 MSE ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA
SEQRES 2 A 82 THR THR GLU ARG ASP VAL ASN GLN LEU THR PRO ARG GLU
SEQRES 3 A 82 ARG ASP ILE LEU LYS LEU ILE ALA GLN GLY LEU PRO ASN
SEQRES 4 A 82 LYS MSE ILE ALA ARG ARG LEU ASP ILE THR GLU SER THR
SEQRES 5 A 82 VAL LYS VAL HIS VAL LYS HIS MSE LEU LYS LYS MSE LYS
SEQRES 6 A 82 LEU LYS SER ARG VAL GLU ALA ALA VAL TRP VAL HIS GLN
SEQRES 7 A 82 GLU ARG ILE PHE
SEQRES 1 B 82 MSE ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA
SEQRES 2 B 82 THR THR GLU ARG ASP VAL ASN GLN LEU THR PRO ARG GLU
SEQRES 3 B 82 ARG ASP ILE LEU LYS LEU ILE ALA GLN GLY LEU PRO ASN
SEQRES 4 B 82 LYS MSE ILE ALA ARG ARG LEU ASP ILE THR GLU SER THR
SEQRES 5 B 82 VAL LYS VAL HIS VAL LYS HIS MSE LEU LYS LYS MSE LYS
SEQRES 6 B 82 LEU LYS SER ARG VAL GLU ALA ALA VAL TRP VAL HIS GLN
SEQRES 7 B 82 GLU ARG ILE PHE
SEQRES 1 E 82 MSE ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA
SEQRES 2 E 82 THR THR GLU ARG ASP VAL ASN GLN LEU THR PRO ARG GLU
SEQRES 3 E 82 ARG ASP ILE LEU LYS LEU ILE ALA GLN GLY LEU PRO ASN
SEQRES 4 E 82 LYS MSE ILE ALA ARG ARG LEU ASP ILE THR GLU SER THR
SEQRES 5 E 82 VAL LYS VAL HIS VAL LYS HIS MSE LEU LYS LYS MSE LYS
SEQRES 6 E 82 LEU LYS SER ARG VAL GLU ALA ALA VAL TRP VAL HIS GLN
SEQRES 7 E 82 GLU ARG ILE PHE
SEQRES 1 F 82 MSE ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA
SEQRES 2 F 82 THR THR GLU ARG ASP VAL ASN GLN LEU THR PRO ARG GLU
SEQRES 3 F 82 ARG ASP ILE LEU LYS LEU ILE ALA GLN GLY LEU PRO ASN
SEQRES 4 F 82 LYS MSE ILE ALA ARG ARG LEU ASP ILE THR GLU SER THR
SEQRES 5 F 82 VAL LYS VAL HIS VAL LYS HIS MSE LEU LYS LYS MSE LYS
SEQRES 6 F 82 LEU LYS SER ARG VAL GLU ALA ALA VAL TRP VAL HIS GLN
SEQRES 7 F 82 GLU ARG ILE PHE
MODRES 1ZG5 MSE A 175 MET SELENOMETHIONINE
MODRES 1ZG5 MSE A 194 MET SELENOMETHIONINE
MODRES 1ZG5 MSE A 198 MET SELENOMETHIONINE
MODRES 1ZG5 MSE B 175 MET SELENOMETHIONINE
MODRES 1ZG5 MSE B 194 MET SELENOMETHIONINE
MODRES 1ZG5 MSE B 198 MET SELENOMETHIONINE
MODRES 1ZG5 MSE E 175 MET SELENOMETHIONINE
MODRES 1ZG5 MSE E 194 MET SELENOMETHIONINE
MODRES 1ZG5 MSE E 198 MET SELENOMETHIONINE
MODRES 1ZG5 MSE F 175 MET SELENOMETHIONINE
MODRES 1ZG5 MSE F 194 MET SELENOMETHIONINE
MODRES 1ZG5 MSE F 198 MET SELENOMETHIONINE
HET MSE A 175 8
HET MSE A 194 8
HET MSE A 198 8
HET MSE B 175 8
HET MSE B 194 8
HET MSE B 198 8
HET MSE E 175 8
HET MSE E 194 8
HET MSE E 198 8
HET MSE F 175 8
HET MSE F 194 8
HET MSE F 198 8
HET SO4 F 301 5
HET SO4 A 302 5
HET SO4 B 303 5
HET SO4 F 304 5
HET SO4 A 305 5
HET SO4 B 306 5
HET SO4 E 307 5
HET SO4 E 308 5
HET SO4 A 309 5
HET SO4 B 310 5
HET SO4 E 311 5
HET SO4 F 312 5
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
FORMUL 5 MSE 12(C5 H11 N O2 SE)
FORMUL 9 SO4 12(O4 S 2-)
FORMUL 21 HOH *260(H2 O)
HELIX 1 1 ASP A 152 LEU A 156 5 5
HELIX 2 2 THR A 157 GLN A 169 1 13
HELIX 3 3 PRO A 172 LEU A 180 1 9
HELIX 4 4 THR A 183 LYS A 199 1 17
HELIX 5 5 SER A 202 GLU A 213 1 12
HELIX 6 6 ASP B 152 LEU B 156 5 5
HELIX 7 7 THR B 157 GLN B 169 1 13
HELIX 8 8 PRO B 172 ASP B 181 1 10
HELIX 9 9 THR B 183 MSE B 198 1 16
HELIX 10 10 SER B 202 GLU B 213 1 12
HELIX 11 11 ASP E 152 LEU E 156 5 5
HELIX 12 12 THR E 157 GLN E 169 1 13
HELIX 13 13 PRO E 172 ASP E 181 1 10
HELIX 14 14 THR E 183 LYS E 199 1 17
HELIX 15 15 SER E 202 GLU E 213 1 12
HELIX 16 16 ASP F 152 LEU F 156 5 5
HELIX 17 17 THR F 157 ALA F 168 1 12
HELIX 18 18 PRO F 172 ASP F 181 1 10
HELIX 19 19 THR F 183 LYS F 199 1 17
HELIX 20 20 SER F 202 GLU F 213 1 12
LINK C LYS A 174 N MSE A 175 1555 1555 1.33
LINK C MSE A 175 N ILE A 176 1555 1555 1.33
LINK C HIS A 193 N MSE A 194 1555 1555 1.33
LINK C MSE A 194 N LEU A 195 1555 1555 1.33
LINK C LYS A 197 N MSE A 198 1555 1555 1.33
LINK C MSE A 198 N LYS A 199 1555 1555 1.32
LINK C LYS B 174 N MSE B 175 1555 1555 1.33
LINK C MSE B 175 N ILE B 176 1555 1555 1.33
LINK C HIS B 193 N MSE B 194 1555 1555 1.33
LINK C MSE B 194 N LEU B 195 1555 1555 1.34
LINK C LYS B 197 N MSE B 198 1555 1555 1.33
LINK C MSE B 198 N LYS B 199 1555 1555 1.32
LINK C LYS E 174 N MSE E 175 1555 1555 1.33
LINK C MSE E 175 N ILE E 176 1555 1555 1.33
LINK C HIS E 193 N MSE E 194 1555 1555 1.33
LINK C MSE E 194 N LEU E 195 1555 1555 1.33
LINK C LYS E 197 N MSE E 198 1555 1555 1.33
LINK C MSE E 198 N LYS E 199 1555 1555 1.33
LINK C LYS F 174 N MSE F 175 1555 1555 1.33
LINK C MSE F 175 N ILE F 176 1555 1555 1.33
LINK C HIS F 193 N MSE F 194 1555 1555 1.33
LINK C MSE F 194 N LEU F 195 1555 1555 1.33
LINK C LYS F 197 N MSE F 198 1555 1555 1.33
LINK C MSE F 198 N LYS F 199 1555 1555 1.32
SITE 1 AC1 2 ARG F 161 HOH F 342
SITE 1 AC2 1 ARG A 161
SITE 1 AC3 3 PRO B 158 ARG B 161 HOH B 329
SITE 1 AC4 8 SER F 185 LYS F 188 HOH F 325 HOH F 326
SITE 2 AC4 8 DC G 5 DC G 6 HOH H 50 HOH H 52
SITE 1 AC5 7 SER A 185 LYS A 188 HOH A 312 HOH C 27
SITE 2 AC5 7 HOH C 52 DC D 25 DC D 26
SITE 1 AC6 8 SER B 185 LYS B 188 HOH B 325 HOH B 334
SITE 2 AC6 8 HOH B 341 DC C 6 HOH D 53 HOH D 63
SITE 1 AC7 8 SER E 185 LYS E 188 HOH E 323 HOH E 324
SITE 2 AC7 8 HOH G 30 HOH G 51 DC H 25 DC H 26
SITE 1 AC8 2 PRO E 158 ARG E 161
SITE 1 AC9 1 ARG A 178
SITE 1 BC1 1 ARG B 178
SITE 1 BC2 1 ARG E 178
SITE 1 BC3 1 ARG F 178
CRYST1 76.890 52.570 84.610 90.00 90.00 90.00 P 1 21 1 8
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 0.013006 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019022 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011819 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
