| content |
HEADER HYDROLASE 23-FEB-17 5UXZ
TITLE X-RAY CRYSTAL STRUCTURE OF HALOTAG BOUND TO THE P9 BENZOTHIADIAZOLE
TITLE 2 FLUOROGENIC LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS RHODOCHROUS;
SOURCE 3 ORGANISM_TAXID: 1829;
SOURCE 4 GENE: DHAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET29B
KEYWDS HALOALKANE DEHALOGENASE, FLUOROGENIC, HALO, TAG, SOLVATOCHROMATIC,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.P.DUNHAM,A.K.BOAL
REVDAT 2 05-APR-17 5UXZ 1 JRNL
REVDAT 1 08-MAR-17 5UXZ 0
JRNL AUTH Y.LIU,K.MIAO,N.P.DUNHAM,H.LIU,M.FARES,A.K.BOAL,X.LI,X.ZHANG
JRNL TITL THE CATION-PI INTERACTION ENABLES A HALO-TAG FLUOROGENIC
JRNL TITL 2 PROBE FOR FAST NO-WASH LIVE CELL IMAGING AND GEL-FREE
JRNL TITL 3 PROTEIN QUANTIFICATION.
JRNL REF BIOCHEMISTRY V. 56 1585 2017
JRNL REFN ISSN 1520-4995
JRNL PMID 28221782
JRNL DOI 10.1021/ACS.BIOCHEM.7B00056
REMARK 2
REMARK 2 RESOLUTION. 1.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 81.9
REMARK 3 NUMBER OF REFLECTIONS : 33903
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 + TEST SET) : 0.270
REMARK 3 R VALUE (WORKING SET) : 0.269
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1806
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.92
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1270
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 41.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.3010
REMARK 3 BIN FREE R VALUE SET COUNT : 57
REMARK 3 BIN FREE R VALUE : 0.3670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4691
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 72
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.08000
REMARK 3 B22 (A**2) : -0.93000
REMARK 3 B33 (A**2) : -0.19000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.29000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.323
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.226
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.187
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.417
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.888
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.871
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4917 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4611 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6721 ; 0.960 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10633 ; 0.716 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 583 ; 4.618 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 229 ;30.044 ;23.362
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 743 ;12.848 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;12.408 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 710 ; 0.055 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5483 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1129 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5UXZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1000226613.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-AUG-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000, HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42358
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.920
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.92
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.51100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, AMMONIUM ACETATE, PH 4.6,
REMARK 280 EVAPORATION, TEMPERATURE 293K
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 34.56200
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 GLU A 295
REMARK 465 ILE A 296
REMARK 465 SER A 297
REMARK 465 GLY A 298
REMARK 465 LEU A 299
REMARK 465 GLU A 300
REMARK 465 ILE A 301
REMARK 465 SER A 302
REMARK 465 GLY A 303
REMARK 465 LEU A 304
REMARK 465 GLU A 305
REMARK 465 HIS A 306
REMARK 465 HIS A 307
REMARK 465 HIS A 308
REMARK 465 HIS A 309
REMARK 465 HIS A 310
REMARK 465 HIS A 311
REMARK 465 GLU B 299
REMARK 465 ILE B 300
REMARK 465 SER B 301
REMARK 465 GLY B 302
REMARK 465 LEU B 303
REMARK 465 GLU B 304
REMARK 465 HIS B 305
REMARK 465 HIS B 306
REMARK 465 HIS B 307
REMARK 465 HIS B 308
REMARK 465 HIS B 309
REMARK 465 HIS B 310
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP A 106 CG ASP A 106 OD1 0.200
REMARK 500 ASP B 106 CG ASP B 106 OD1 0.206
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 PRO A 42 49.19 -108.99
REMARK 500 THR A 43 -165.34 -102.67
REMARK 500 GLU A 98 -81.84 -95.90
REMARK 500 ASP A 106 -128.86 54.41
REMARK 500 ARG A 153 43.04 -81.93
REMARK 500 ASP A 156 -61.37 -91.32
REMARK 500 VAL A 245 -70.77 -139.84
REMARK 500 LEU A 271 -96.27 -115.27
REMARK 500 ARG B 30 46.75 -102.19
REMARK 500 PRO B 42 50.38 -105.44
REMARK 500 ASP B 76 99.17 -68.89
REMARK 500 GLU B 98 -63.20 -121.15
REMARK 500 ASP B 106 -121.27 59.39
REMARK 500 GLU B 130 61.47 38.48
REMARK 500 ASN B 166 51.90 27.65
REMARK 500 PHE B 193 69.41 -101.75
REMARK 500 ASP B 198 34.81 -95.66
REMARK 500 VAL B 245 -74.49 -138.22
REMARK 500 LEU B 271 -92.59 -117.44
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 8PM A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 8PM B 401 and ASP B
REMARK 800 106
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5UY1 RELATED DB: PDB
DBREF 5UXZ A 4 290 UNP P0A3G2 DHAA_RHORH 4 290
DBREF 5UXZ B 4 290 UNP P0A3G2 DHAA_RHORH 4 290
SEQADV 5UXZ VAL A 47 UNP P0A3G2 LEU 47 CONFLICT
SEQADV 5UXZ THR A 58 UNP P0A3G2 SER 58 CONFLICT
SEQADV 5UXZ GLY A 78 UNP P0A3G2 ASP 78 CONFLICT
SEQADV 5UXZ PHE A 87 UNP P0A3G2 TYR 87 CONFLICT
SEQADV 5UXZ MET A 88 UNP P0A3G2 LEU 88 CONFLICT
SEQADV 5UXZ PHE A 128 UNP P0A3G2 CYS 128 CONFLICT
SEQADV 5UXZ THR A 155 UNP P0A3G2 ALA 155 CONFLICT
SEQADV 5UXZ LYS A 160 UNP P0A3G2 GLU 160 CONFLICT
SEQADV 5UXZ VAL A 167 UNP P0A3G2 ALA 167 CONFLICT
SEQADV 5UXZ THR A 172 UNP P0A3G2 ALA 172 CONFLICT
SEQADV 5UXZ MET A 175 UNP P0A3G2 LYS 175 CONFLICT
SEQADV 5UXZ GLY A 176 UNP P0A3G2 CYS 176 CONFLICT
SEQADV 5UXZ ASN A 195 UNP P0A3G2 LYS 195 CONFLICT
SEQADV 5UXZ GLU A 224 UNP P0A3G2 ALA 224 CONFLICT
SEQADV 5UXZ ASP A 227 UNP P0A3G2 ASN 227 CONFLICT
SEQADV 5UXZ LYS A 257 UNP P0A3G2 GLU 257 CONFLICT
SEQADV 5UXZ ALA A 264 UNP P0A3G2 THR 264 CONFLICT
SEQADV 5UXZ ASN A 272 UNP P0A3G2 HIS 272 CONFLICT
SEQADV 5UXZ LEU A 273 UNP P0A3G2 TYR 273 CONFLICT
SEQADV 5UXZ SER A 291 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ THR A 293 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ LEU A 294 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ GLU A 295 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ ILE A 296 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ SER A 297 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ GLY A 298 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ LEU A 299 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ GLU A 300 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ ILE A 301 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ SER A 302 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ GLY A 303 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ LEU A 304 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ GLU A 305 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ HIS A 306 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ HIS A 307 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ HIS A 308 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ HIS A 309 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ HIS A 310 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ HIS A 311 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ VAL B 47 UNP P0A3G2 LEU 47 CONFLICT
SEQADV 5UXZ THR B 58 UNP P0A3G2 SER 58 CONFLICT
SEQADV 5UXZ GLY B 78 UNP P0A3G2 ASP 78 CONFLICT
SEQADV 5UXZ PHE B 87 UNP P0A3G2 TYR 87 CONFLICT
SEQADV 5UXZ MET B 88 UNP P0A3G2 LEU 88 CONFLICT
SEQADV 5UXZ PHE B 128 UNP P0A3G2 CYS 128 CONFLICT
SEQADV 5UXZ THR B 155 UNP P0A3G2 ALA 155 CONFLICT
SEQADV 5UXZ LYS B 160 UNP P0A3G2 GLU 160 CONFLICT
SEQADV 5UXZ VAL B 167 UNP P0A3G2 ALA 167 CONFLICT
SEQADV 5UXZ THR B 172 UNP P0A3G2 ALA 172 CONFLICT
SEQADV 5UXZ MET B 175 UNP P0A3G2 LYS 175 CONFLICT
SEQADV 5UXZ GLY B 176 UNP P0A3G2 CYS 176 CONFLICT
SEQADV 5UXZ ASN B 195 UNP P0A3G2 LYS 195 CONFLICT
SEQADV 5UXZ GLU B 224 UNP P0A3G2 ALA 224 CONFLICT
SEQADV 5UXZ ASP B 227 UNP P0A3G2 ASN 227 CONFLICT
SEQADV 5UXZ LYS B 257 UNP P0A3G2 GLU 257 CONFLICT
SEQADV 5UXZ ALA B 264 UNP P0A3G2 THR 264 CONFLICT
SEQADV 5UXZ ASN B 272 UNP P0A3G2 HIS 272 CONFLICT
SEQADV 5UXZ LEU B 273 UNP P0A3G2 TYR 273 CONFLICT
SEQADV 5UXZ SER B 291 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ THR B 292 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ LEU B 293 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ GLU B 294 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ ILE B 295 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ SER B 296 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ GLY B 297 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ LEU B 298 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ GLU B 299 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ ILE B 300 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ SER B 301 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ GLY B 302 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ LEU B 303 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ GLU B 304 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ HIS B 305 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ HIS B 306 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ HIS B 307 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ HIS B 308 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ HIS B 309 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UXZ HIS B 310 UNP P0A3G2 EXPRESSION TAG
SEQRES 1 A 307 ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL GLU
SEQRES 2 A 307 VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY PRO
SEQRES 3 A 307 ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 A 307 THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS VAL
SEQRES 5 A 307 ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 A 307 MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE PHE
SEQRES 7 A 307 ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU ALA
SEQRES 8 A 307 LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP TRP
SEQRES 9 A 307 GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN PRO
SEQRES 10 A 307 GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE ARG
SEQRES 11 A 307 PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA ARG
SEQRES 12 A 307 GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY ARG
SEQRES 13 A 307 LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY THR
SEQRES 14 A 307 LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL GLU
SEQRES 15 A 307 MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL ASP
SEQRES 16 A 307 ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO ILE
SEQRES 17 A 307 ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU GLU
SEQRES 18 A 307 TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS LEU
SEQRES 19 A 307 LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO ALA
SEQRES 20 A 307 GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS LYS
SEQRES 21 A 307 ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN GLU
SEQRES 22 A 307 ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG TRP
SEQRES 23 A 307 LEU SER THR LEU GLU ILE SER GLY LEU GLU ILE SER GLY
SEQRES 24 A 307 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 307 ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL GLU
SEQRES 2 B 307 VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY PRO
SEQRES 3 B 307 ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 B 307 THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS VAL
SEQRES 5 B 307 ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 B 307 MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE PHE
SEQRES 7 B 307 ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU ALA
SEQRES 8 B 307 LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP TRP
SEQRES 9 B 307 GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN PRO
SEQRES 10 B 307 GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE ARG
SEQRES 11 B 307 PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA ARG
SEQRES 12 B 307 GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY ARG
SEQRES 13 B 307 LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY THR
SEQRES 14 B 307 LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL GLU
SEQRES 15 B 307 MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL ASP
SEQRES 16 B 307 ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO ILE
SEQRES 17 B 307 ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU GLU
SEQRES 18 B 307 TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS LEU
SEQRES 19 B 307 LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO ALA
SEQRES 20 B 307 GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS LYS
SEQRES 21 B 307 ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN GLU
SEQRES 22 B 307 ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG TRP
SEQRES 23 B 307 LEU SER THR LEU GLU ILE SER GLY LEU GLU ILE SER GLY
SEQRES 24 B 307 LEU GLU HIS HIS HIS HIS HIS HIS
HET 8PM A 401 27
HET CL A 402 1
HET EDO A 403 4
HET EDO A 404 4
HET 8PM B 401 27
HET CL B 402 1
HETNAM 8PM N~2~-{[7-(DIMETHYLAMINO)-2,1,3-BENZOTHIADIAZOL-4-
HETNAM 2 8PM YL]SULFONYL}-N-HEXYL-N~2~-METHYLGLYCINAMIDE
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 8PM 2(C17 H27 N5 O3 S2)
FORMUL 4 CL 2(CL 1-)
FORMUL 5 EDO 2(C2 H6 O2)
FORMUL 9 HOH *72(H2 O)
HELIX 1 AA1 SER A 44 ARG A 49 5 6
HELIX 2 AA2 ILE A 51 ALA A 56 1 6
HELIX 3 AA3 PHE A 80 LEU A 95 1 16
HELIX 4 AA4 ASP A 106 ASN A 119 1 14
HELIX 5 AA5 PRO A 142 ARG A 153 1 12
HELIX 6 AA6 ASP A 156 ILE A 163 1 8
HELIX 7 AA7 ASN A 166 GLY A 171 1 6
HELIX 8 AA8 GLY A 171 GLY A 176 1 6
HELIX 9 AA9 THR A 182 GLU A 191 1 10
HELIX 10 AB1 PRO A 192 LEU A 194 5 3
HELIX 11 AB2 ASN A 195 ASP A 198 5 4
HELIX 12 AB3 ARG A 199 LEU A 209 1 11
HELIX 13 AB4 PRO A 215 SER A 232 1 18
HELIX 14 AB5 PRO A 248 LEU A 259 1 12
HELIX 15 AB6 LEU A 273 ASN A 278 1 6
HELIX 16 AB7 ASN A 278 LEU A 294 1 16
HELIX 17 AB8 SER B 44 ARG B 49 5 6
HELIX 18 AB9 ILE B 51 ALA B 56 1 6
HELIX 19 AC1 PHE B 80 GLY B 96 1 17
HELIX 20 AC2 TRP B 107 ASN B 119 1 13
HELIX 21 AC3 THR B 137 TRP B 141 5 5
HELIX 22 AC4 PRO B 142 ARG B 153 1 12
HELIX 23 AC5 THR B 155 ILE B 163 1 9
HELIX 24 AC6 ASN B 166 GLY B 171 1 6
HELIX 25 AC7 GLY B 171 GLY B 176 1 6
HELIX 26 AC8 THR B 182 GLU B 191 1 10
HELIX 27 AC9 ASN B 195 ASP B 198 5 4
HELIX 28 AD1 ARG B 199 LEU B 209 1 11
HELIX 29 AD2 PRO B 215 SER B 232 1 18
HELIX 30 AD3 PRO B 248 LEU B 259 1 12
HELIX 31 AD4 LEU B 273 ASN B 278 1 6
HELIX 32 AD5 ASN B 278 GLY B 297 1 20
SHEET 1 AA1 8 HIS A 13 VAL A 17 0
SHEET 2 AA1 8 GLU A 20 VAL A 27 -1 O GLU A 20 N VAL A 17
SHEET 3 AA1 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 AA1 8 VAL A 35 LEU A 38 1 N PHE A 37 O ILE A 62
SHEET 5 AA1 8 VAL A 100 HIS A 105 1 O VAL A 101 N LEU A 36
SHEET 6 AA1 8 VAL A 123 MET A 129 1 O ALA A 127 N LEU A 102
SHEET 7 AA1 8 LYS A 236 PRO A 243 1 O LEU A 237 N PHE A 128
SHEET 8 AA1 8 CYS A 262 GLY A 270 1 O ILE A 267 N TRP A 240
SHEET 1 AA2 8 HIS B 13 GLU B 16 0
SHEET 2 AA2 8 ARG B 21 VAL B 27 -1 O TYR B 24 N HIS B 13
SHEET 3 AA2 8 CYS B 61 PRO B 64 -1 O CYS B 61 N VAL B 27
SHEET 4 AA2 8 VAL B 35 LEU B 38 1 N PHE B 37 O ILE B 62
SHEET 5 AA2 8 VAL B 100 ASP B 106 1 O VAL B 101 N LEU B 36
SHEET 6 AA2 8 VAL B 123 PHE B 131 1 O ALA B 127 N LEU B 102
SHEET 7 AA2 8 LYS B 236 PRO B 243 1 O LEU B 237 N PHE B 128
SHEET 8 AA2 8 CYS B 262 GLY B 270 1 O LYS B 263 N LEU B 238
LINK OD1 ASP A 106 C27 8PM A 401 1555 1555 1.42
LINK OD1 ASP B 106 C27 8PM B 401 1555 1555 1.43
CISPEP 1 ASN A 41 PRO A 42 0 0.04
CISPEP 2 GLU A 214 PRO A 215 0 -8.83
CISPEP 3 THR A 242 PRO A 243 0 2.61
CISPEP 4 ASN B 41 PRO B 42 0 -3.50
CISPEP 5 GLU B 214 PRO B 215 0 -7.40
CISPEP 6 THR B 242 PRO B 243 0 0.72
SITE 1 AC1 13 ASN A 41 ASP A 106 TRP A 141 PRO A 142
SITE 2 AC1 13 ALA A 145 PHE A 149 THR A 172 MET A 175
SITE 3 AC1 13 GLY A 176 VAL A 245 LEU A 246 ASN A 272
SITE 4 AC1 13 CL A 402
SITE 1 AC2 4 ASN A 41 TRP A 107 PRO A 206 8PM A 401
SITE 1 AC3 3 ARG A 30 ARG A 60 LEU A 95
SITE 1 AC4 6 GLY A 5 THR A 6 GLY A 7 PRO A 9
SITE 2 AC4 6 ARG A 49 ASN A 50
SITE 1 AC5 4 ASN B 41 TRP B 107 PRO B 206 8PM B 401
SITE 1 AC6 17 GLY B 40 ASN B 41 HIS B 105 TRP B 107
SITE 2 AC6 17 GLY B 108 SER B 109 ALA B 110 GLU B 130
SITE 3 AC6 17 ILE B 132 TRP B 141 ALA B 145 PHE B 149
SITE 4 AC6 17 THR B 172 MET B 175 VAL B 245 ASN B 272
SITE 5 AC6 17 CL B 402
CRYST1 49.939 69.124 83.904 90.00 94.67 90.00 P 1 21 1 4
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 0.020024 0.000000 0.001635 0.00000
SCALE2 0.000000 0.014467 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011958 0.00000
TER 2329 LEU A 294
TER 4693 LEU B 298
MASTER 357 0 6 32 16 0 14 6 4827 2 64 48
END |