HEADER TRANSCRIPTION 12-FEB-06 2G0E
TITLE STRUCTURE OF QACR MULTIDRUG TRANSCRIPTIONAL REGULATOR BOUND TO
TITLE 2 TRIVALENT AND BIVALENT DIAMIDINE DRUGS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HTH-TYPE TRANSCRIPTIONAL REGULATOR QACR;
COMPND 3 CHAIN: A, B, D, E;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS HAEMOLYTICUS;
SOURCE 3 ORGANISM_TAXID: 1283;
SOURCE 4 GENE: QACR;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5A
KEYWDS HELIX-TURN-HELIX, TRANSCIPTIONAL REPRESSOR, TRIVALENT, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.T.SCHUMAN
REVDAT 4 14-FEB-24 2G0E 1 REMARK SEQADV HETSYN
REVDAT 3 13-JUL-11 2G0E 1 VERSN
REVDAT 2 24-FEB-09 2G0E 1 VERSN
REVDAT 1 08-APR-08 2G0E 0
JRNL AUTH J.T.SCHUMAN,K.M.HARDIE,M.H.BROWN,R.A.SKURRAY,R.G.BRENNAN
JRNL TITL STRUCTURE OF QACR MULTIDRUG TRANSCRIPTIONAL REGULATOR BOUND
JRNL TITL 2 TO TRIVALENT AND BIVALENT DIAMIDINE DRUGS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.88 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 16.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2376509.010
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 33410
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) : 0.237
REMARK 3 FREE R VALUE : 0.299
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3336
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.88
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4801
REMARK 3 BIN R VALUE (WORKING SET) : 0.3590
REMARK 3 BIN FREE R VALUE : 0.4160
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 549
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6188
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 131
REMARK 3 SOLVENT ATOMS : 38
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 63.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 84.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.05000
REMARK 3 B22 (A**2) : 6.05000
REMARK 3 B33 (A**2) : -12.11000
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) : 0.41
REMARK 3 ESD FROM SIGMAA (A) : 0.49
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) : 0.51
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.61
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.720
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.830 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.160 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.380 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.840 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.28
REMARK 3 BSOL : 36.53
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : PRO_CGP_PAR.TXT
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : PRO_CGP_TOP.TXT
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2G0E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000036530.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 4.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.078
REMARK 200 MONOCHROMATOR : SILICON
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NOIR-1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33410
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.880
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.900
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 17.3
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : 0.04700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.65
REMARK 200 R MERGE FOR SHELL (I) : 0.30800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.8M AMMONIUM SULFATE, 0.1M SODIUM
REMARK 280 ACETATE, PH 4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 85.23500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 85.23500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 47.02500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 85.23500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 85.23500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 47.02500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 85.23500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 85.23500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 47.02500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 85.23500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 85.23500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 47.02500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -113.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -182.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 63940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 120620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1396.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 94.05000
REMARK 350 BIOMT1 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 94.05000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
REMARK 350 BIOMT1 5 0.000000 -1.000000 0.000000 -85.23500
REMARK 350 BIOMT2 5 1.000000 0.000000 0.000000 85.23500
REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 47.02500
REMARK 350 BIOMT1 6 0.000000 1.000000 0.000000 85.23500
REMARK 350 BIOMT2 6 -1.000000 0.000000 0.000000 -85.23500
REMARK 350 BIOMT3 6 0.000000 0.000000 1.000000 47.02500
REMARK 350 BIOMT1 7 -1.000000 0.000000 0.000000 -85.23500
REMARK 350 BIOMT2 7 0.000000 1.000000 0.000000 85.23500
REMARK 350 BIOMT3 7 0.000000 0.000000 -1.000000 47.02500
REMARK 350 BIOMT1 8 1.000000 0.000000 0.000000 85.23500
REMARK 350 BIOMT2 8 0.000000 -1.000000 0.000000 -85.23500
REMARK 350 BIOMT3 8 0.000000 0.000000 -1.000000 47.02500
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 MET A 1
REMARK 465 LYS A 188
REMARK 465 MET B 1
REMARK 465 LYS B 188
REMARK 465 MET D 1
REMARK 465 LYS D 188
REMARK 465 MET E 1
REMARK 465 LYS E 188
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 LEU A 3 -61.47 -124.40
REMARK 500 ALA A 22 -79.78 -54.69
REMARK 500 THR A 25 -9.92 -55.09
REMARK 500 VAL A 29 -77.32 -54.07
REMARK 500 SER A 34 -168.42 -101.60
REMARK 500 TYR A 40 -91.72 -156.72
REMARK 500 LYS A 71 -8.75 -56.75
REMARK 500 THR A 89 -168.42 -48.65
REMARK 500 TYR A 92 -59.24 54.87
REMARK 500 THR A 104 -70.34 -87.45
REMARK 500 SER A 111 43.92 -89.49
REMARK 500 ILE A 112 -50.22 -138.13
REMARK 500 GLU A 114 -75.23 -144.42
REMARK 500 LYS A 118 0.13 -69.84
REMARK 500 TRP A 140 -165.65 -164.56
REMARK 500 PHE A 162 41.03 -98.05
REMARK 500 THR A 163 2.96 -152.51
REMARK 500 HIS A 164 74.66 -68.74
REMARK 500 GLU A 165 42.91 172.13
REMARK 500 ASN A 167 98.64 -24.59
REMARK 500 LEU B 3 -31.29 -165.88
REMARK 500 TYR B 20 -75.30 -54.40
REMARK 500 LYS B 44 -54.46 81.06
REMARK 500 LYS B 71 21.97 -64.73
REMARK 500 TYR B 92 -81.55 56.24
REMARK 500 TYR B 93 -28.84 -39.66
REMARK 500 TYR B 106 6.43 -151.64
REMARK 500 ASN B 110 -34.76 -33.91
REMARK 500 SER B 111 -75.44 -51.74
REMARK 500 LEU B 136 34.09 -86.27
REMARK 500 ASN B 137 13.34 -159.67
REMARK 500 ALA B 152 -71.56 -54.25
REMARK 500 THR B 163 34.27 -147.70
REMARK 500 GLU B 165 -92.03 -87.82
REMARK 500 GLN B 166 -169.68 -54.31
REMARK 500 ASN B 184 33.03 -81.72
REMARK 500 LEU B 186 6.02 -67.87
REMARK 500 SER D 34 -131.27 -122.30
REMARK 500 LYS D 44 -40.99 67.63
REMARK 500 THR D 104 35.66 -87.05
REMARK 500 TYR D 106 12.44 -151.54
REMARK 500 ILE D 112 38.11 -78.57
REMARK 500 GLU D 114 -82.87 -74.97
REMARK 500 LEU D 136 23.22 -66.93
REMARK 500 TRP D 140 164.84 179.08
REMARK 500 HIS D 164 78.98 -33.00
REMARK 500 GLU D 165 105.36 168.91
REMARK 500 GLN D 166 177.60 125.51
REMARK 500 LYS E 30 -72.98 -52.33
REMARK 500 GLU E 33 70.15 52.80
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CGQ D 3025
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 699
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 799
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 299
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 249
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 239
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 599
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 899
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 399
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 289
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 199
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 779
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 780
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 220
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JT6 RELATED DB: PDB
REMARK 900 RELATED ID: 1JTX RELATED DB: PDB
DBREF 2G0E A 1 188 UNP P0A0N5 QACR_STAHA 1 188
DBREF 2G0E B 1 188 UNP P0A0N5 QACR_STAHA 1 188
DBREF 2G0E D 1 188 UNP P0A0N5 QACR_STAHA 1 188
DBREF 2G0E E 1 188 UNP P0A0N5 QACR_STAHA 1 188
SEQADV 2G0E ALA A 72 UNP P0A0N5 CYS 72 CONFLICT
SEQADV 2G0E SER A 141 UNP P0A0N5 CYS 141 CONFLICT
SEQADV 2G0E ALA B 72 UNP P0A0N5 CYS 72 CONFLICT
SEQADV 2G0E SER B 141 UNP P0A0N5 CYS 141 CONFLICT
SEQADV 2G0E ALA D 72 UNP P0A0N5 CYS 72 CONFLICT
SEQADV 2G0E SER D 141 UNP P0A0N5 CYS 141 CONFLICT
SEQADV 2G0E ALA E 72 UNP P0A0N5 CYS 72 CONFLICT
SEQADV 2G0E SER E 141 UNP P0A0N5 CYS 141 CONFLICT
SEQRES 1 A 188 MET ASN LEU LYS ASP LYS ILE LEU GLY VAL ALA LYS GLU
SEQRES 2 A 188 LEU PHE ILE LYS ASN GLY TYR ASN ALA THR THR THR GLY
SEQRES 3 A 188 GLU ILE VAL LYS LEU SER GLU SER SER LYS GLY ASN LEU
SEQRES 4 A 188 TYR TYR HIS PHE LYS THR LYS GLU ASN LEU PHE LEU GLU
SEQRES 5 A 188 ILE LEU ASN ILE GLU GLU SER LYS TRP GLN GLU GLN TRP
SEQRES 6 A 188 LYS LYS GLU GLN ILE LYS ALA LYS THR ASN ARG GLU LYS
SEQRES 7 A 188 PHE TYR LEU TYR ASN GLU LEU SER LEU THR THR GLU TYR
SEQRES 8 A 188 TYR TYR PRO LEU GLN ASN ALA ILE ILE GLU PHE TYR THR
SEQRES 9 A 188 GLU TYR TYR LYS THR ASN SER ILE ASN GLU LYS MET ASN
SEQRES 10 A 188 LYS LEU GLU ASN LYS TYR ILE ASP ALA TYR HIS VAL ILE
SEQRES 11 A 188 PHE LYS GLU GLY ASN LEU ASN GLY GLU TRP SER ILE ASN
SEQRES 12 A 188 ASP VAL ASN ALA VAL SER LYS ILE ALA ALA ASN ALA VAL
SEQRES 13 A 188 ASN GLY ILE VAL THR PHE THR HIS GLU GLN ASN ILE ASN
SEQRES 14 A 188 GLU ARG ILE LYS LEU MET ASN LYS PHE SER GLN ILE PHE
SEQRES 15 A 188 LEU ASN GLY LEU SER LYS
SEQRES 1 B 188 MET ASN LEU LYS ASP LYS ILE LEU GLY VAL ALA LYS GLU
SEQRES 2 B 188 LEU PHE ILE LYS ASN GLY TYR ASN ALA THR THR THR GLY
SEQRES 3 B 188 GLU ILE VAL LYS LEU SER GLU SER SER LYS GLY ASN LEU
SEQRES 4 B 188 TYR TYR HIS PHE LYS THR LYS GLU ASN LEU PHE LEU GLU
SEQRES 5 B 188 ILE LEU ASN ILE GLU GLU SER LYS TRP GLN GLU GLN TRP
SEQRES 6 B 188 LYS LYS GLU GLN ILE LYS ALA LYS THR ASN ARG GLU LYS
SEQRES 7 B 188 PHE TYR LEU TYR ASN GLU LEU SER LEU THR THR GLU TYR
SEQRES 8 B 188 TYR TYR PRO LEU GLN ASN ALA ILE ILE GLU PHE TYR THR
SEQRES 9 B 188 GLU TYR TYR LYS THR ASN SER ILE ASN GLU LYS MET ASN
SEQRES 10 B 188 LYS LEU GLU ASN LYS TYR ILE ASP ALA TYR HIS VAL ILE
SEQRES 11 B 188 PHE LYS GLU GLY ASN LEU ASN GLY GLU TRP SER ILE ASN
SEQRES 12 B 188 ASP VAL ASN ALA VAL SER LYS ILE ALA ALA ASN ALA VAL
SEQRES 13 B 188 ASN GLY ILE VAL THR PHE THR HIS GLU GLN ASN ILE ASN
SEQRES 14 B 188 GLU ARG ILE LYS LEU MET ASN LYS PHE SER GLN ILE PHE
SEQRES 15 B 188 LEU ASN GLY LEU SER LYS
SEQRES 1 D 188 MET ASN LEU LYS ASP LYS ILE LEU GLY VAL ALA LYS GLU
SEQRES 2 D 188 LEU PHE ILE LYS ASN GLY TYR ASN ALA THR THR THR GLY
SEQRES 3 D 188 GLU ILE VAL LYS LEU SER GLU SER SER LYS GLY ASN LEU
SEQRES 4 D 188 TYR TYR HIS PHE LYS THR LYS GLU ASN LEU PHE LEU GLU
SEQRES 5 D 188 ILE LEU ASN ILE GLU GLU SER LYS TRP GLN GLU GLN TRP
SEQRES 6 D 188 LYS LYS GLU GLN ILE LYS ALA LYS THR ASN ARG GLU LYS
SEQRES 7 D 188 PHE TYR LEU TYR ASN GLU LEU SER LEU THR THR GLU TYR
SEQRES 8 D 188 TYR TYR PRO LEU GLN ASN ALA ILE ILE GLU PHE TYR THR
SEQRES 9 D 188 GLU TYR TYR LYS THR ASN SER ILE ASN GLU LYS MET ASN
SEQRES 10 D 188 LYS LEU GLU ASN LYS TYR ILE ASP ALA TYR HIS VAL ILE
SEQRES 11 D 188 PHE LYS GLU GLY ASN LEU ASN GLY GLU TRP SER ILE ASN
SEQRES 12 D 188 ASP VAL ASN ALA VAL SER LYS ILE ALA ALA ASN ALA VAL
SEQRES 13 D 188 ASN GLY ILE VAL THR PHE THR HIS GLU GLN ASN ILE ASN
SEQRES 14 D 188 GLU ARG ILE LYS LEU MET ASN LYS PHE SER GLN ILE PHE
SEQRES 15 D 188 LEU ASN GLY LEU SER LYS
SEQRES 1 E 188 MET ASN LEU LYS ASP LYS ILE LEU GLY VAL ALA LYS GLU
SEQRES 2 E 188 LEU PHE ILE LYS ASN GLY TYR ASN ALA THR THR THR GLY
SEQRES 3 E 188 GLU ILE VAL LYS LEU SER GLU SER SER LYS GLY ASN LEU
SEQRES 4 E 188 TYR TYR HIS PHE LYS THR LYS GLU ASN LEU PHE LEU GLU
SEQRES 5 E 188 ILE LEU ASN ILE GLU GLU SER LYS TRP GLN GLU GLN TRP
SEQRES 6 E 188 LYS LYS GLU GLN ILE LYS ALA LYS THR ASN ARG GLU LYS
SEQRES 7 E 188 PHE TYR LEU TYR ASN GLU LEU SER LEU THR THR GLU TYR
SEQRES 8 E 188 TYR TYR PRO LEU GLN ASN ALA ILE ILE GLU PHE TYR THR
SEQRES 9 E 188 GLU TYR TYR LYS THR ASN SER ILE ASN GLU LYS MET ASN
SEQRES 10 E 188 LYS LEU GLU ASN LYS TYR ILE ASP ALA TYR HIS VAL ILE
SEQRES 11 E 188 PHE LYS GLU GLY ASN LEU ASN GLY GLU TRP SER ILE ASN
SEQRES 12 E 188 ASP VAL ASN ALA VAL SER LYS ILE ALA ALA ASN ALA VAL
SEQRES 13 E 188 ASN GLY ILE VAL THR PHE THR HIS GLU GLN ASN ILE ASN
SEQRES 14 E 188 GLU ARG ILE LYS LEU MET ASN LYS PHE SER GLN ILE PHE
SEQRES 15 E 188 LEU ASN GLY LEU SER LYS
HET SO4 A 199 5
HET SO4 B 270 5
HET SO4 B 999 5
HET SO4 B 899 5
HET SO4 B 601 5
HET SO4 B 779 5
HET SO4 B 780 5
HET CGQ D3025 26
HET SO4 D 699 5
HET SO4 D 299 5
HET SO4 D 801 5
HET SO4 D 279 5
HET SO4 D 599 5
HET SO4 D 800 5
HET SO4 D 501 5
HET SO4 D 220 5
HET SO4 E 799 5
HET SO4 E 900 5
HET SO4 E 249 5
HET SO4 E 239 5
HET SO4 E 399 5
HET SO4 E 289 5
HETNAM SO4 SULFATE ION
HETNAM CGQ 3-[C-[N'-(3-CARBAMIMIDOYL-BENZYLIDENIUM)-HYDRAZINO]-
HETNAM 2 CGQ [[AMINOMETHYLIDENE]AMINIUM]-IMINOMETHYL]-BENZAMIDINIUM
HETSYN CGQ CGP40215A; BIS[[3-(AMINOIMINOMETHYL)PHENYL]METHYLENE]
HETSYN 2 CGQ CARBONIMIDIC DIHYDRAZIDE
FORMUL 5 SO4 21(O4 S 2-)
FORMUL 12 CGQ C17 H22 N9 3+
FORMUL 27 HOH *38(H2 O)
HELIX 1 1 LEU A 3 ASN A 18 1 16
HELIX 2 2 THR A 24 LEU A 31 1 8
HELIX 3 3 SER A 35 LEU A 39 5 5
HELIX 4 4 THR A 45 LYS A 67 1 23
HELIX 5 5 GLU A 68 ALA A 72 5 5
HELIX 6 6 THR A 74 THR A 89 1 16
HELIX 7 7 TYR A 92 PRO A 94 5 3
HELIX 8 8 LEU A 95 TYR A 106 1 12
HELIX 9 9 ASN A 117 ASN A 137 1 21
HELIX 10 10 ASP A 144 PHE A 162 1 19
HELIX 11 11 ASN A 167 SER A 187 1 21
HELIX 12 12 LEU B 3 GLY B 19 1 17
HELIX 13 13 THR B 24 GLU B 33 1 10
HELIX 14 14 SER B 35 PHE B 43 1 9
HELIX 15 15 THR B 45 GLN B 69 1 25
HELIX 16 16 THR B 74 THR B 89 1 16
HELIX 17 17 TYR B 92 PRO B 94 5 3
HELIX 18 18 LEU B 95 THR B 104 1 10
HELIX 19 19 THR B 109 LEU B 136 1 28
HELIX 20 20 ASP B 144 PHE B 162 1 19
HELIX 21 21 ASN B 167 ASN B 184 1 18
HELIX 22 22 ASN D 2 GLY D 19 1 18
HELIX 23 23 THR D 24 SER D 32 1 9
HELIX 24 24 SER D 35 LYS D 44 1 10
HELIX 25 25 THR D 45 GLN D 69 1 25
HELIX 26 26 ILE D 70 ALA D 72 5 3
HELIX 27 27 THR D 74 TYR D 92 1 19
HELIX 28 28 LEU D 95 THR D 104 1 10
HELIX 29 29 THR D 109 ASN D 113 5 5
HELIX 30 30 GLU D 114 LEU D 136 1 23
HELIX 31 31 ASP D 144 THR D 163 1 20
HELIX 32 32 ASN D 167 GLY D 185 1 19
HELIX 33 33 ASN E 2 GLY E 19 1 18
HELIX 34 34 THR E 24 SER E 32 1 9
HELIX 35 35 SER E 35 PHE E 43 1 9
HELIX 36 36 THR E 45 ILE E 70 1 26
HELIX 37 37 THR E 74 THR E 89 1 16
HELIX 38 38 TYR E 92 PRO E 94 5 3
HELIX 39 39 LEU E 95 TYR E 107 1 13
HELIX 40 40 THR E 109 LEU E 136 1 28
HELIX 41 41 ASP E 144 THR E 161 1 18
HELIX 42 42 ASN E 167 GLY E 185 1 19
SITE 1 AC1 9 LEU D 54 GLU D 57 GLN D 64 THR D 89
SITE 2 AC1 9 TYR D 92 TYR D 93 LEU D 119 TYR D 123
SITE 3 AC1 9 HOH D3034
SITE 1 AC2 3 SER D 35 LYS D 36 LYS E 60
SITE 1 AC3 4 LYS D 36 TYR D 40 ASP E 5 LYS E 6
SITE 1 AC4 3 LYS D 4 TYR D 41 HIS D 42
SITE 1 AC5 4 THR E 24 THR E 25 GLY E 26 LYS E 36
SITE 1 AC6 3 THR B 24 THR B 25 GLY B 26
SITE 1 AC7 5 LYS E 36 TYR E 40 THR E 45 LYS E 46
SITE 2 AC7 5 GLU E 47
SITE 1 AC8 4 TYR B 20 LYS B 46 GLU B 105 TYR B 106
SITE 1 AC9 3 HIS D 128 LYS D 132 ASN D 146
SITE 1 BC1 5 ASN D 2 LEU D 3 LYS D 4 ASN D 38
SITE 2 BC1 5 HIS D 42
SITE 1 BC2 2 HIS E 128 LYS E 132
SITE 1 BC3 3 ASN D 2 ASP D 5 LYS D 6
SITE 1 BC4 2 THR B 25 LYS B 46
SITE 1 BC5 4 THR D 23 THR D 24 THR D 25 LYS D 46
SITE 1 BC6 5 LEU E 8 LYS E 12 ILE E 53 ILE E 56
SITE 2 BC6 5 GLU E 57
SITE 1 BC7 2 LYS E 4 HIS E 42
SITE 1 BC8 5 GLN A 64 TYR A 91 GLN B 64 GLU B 90
SITE 2 BC8 5 TYR B 91
SITE 1 BC9 2 TYR B 107 ASN D 2
SITE 1 CC1 4 GLU B 58 SER B 59 GLN B 62 LYS B 122
SITE 1 CC2 6 LEU D 8 LYS D 12 ILE D 53 ILE D 56
SITE 2 CC2 6 GLU D 57 LYS D 60
SITE 1 CC3 4 GLU B 13 LYS B 17 LYS B 30 GLU B 33
SITE 1 CC4 3 GLY D 26 ASN D 167 ILE D 168
CRYST1 170.470 170.470 94.050 90.00 90.00 90.00 P 42 21 2 32
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 0.005866 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005866 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010633 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
