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HEADER HYDROLASE 23-FEB-17 5UY1
TITLE X-RAY CRYSTAL STRUCTURE OF APO HALOTAG
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, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.P.DUNHAM,A.K.BOAL
REVDAT 2 05-APR-17 5UY1 1 JRNL
REVDAT 1 08-MAR-17 5UY1 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. 1.35 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 133179
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7029
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) : 1.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.38
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7030
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 70.18
REMARK 3 BIN R VALUE (WORKING SET) : 0.2380
REMARK 3 BIN FREE R VALUE SET COUNT : 390
REMARK 3 BIN FREE R VALUE : 0.2540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4656
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 437
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.11000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : 0.09000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.056
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.053
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.035
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.853
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4841 ; 0.004 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4558 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6613 ; 0.997 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10499 ; 0.740 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 582 ; 4.684 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 228 ;28.752 ;23.333
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 737 ;11.406 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;15.107 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 703 ; 0.057 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5418 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1120 ; 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 : NULL
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 5UY1 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_1000226588.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-APR-16
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 : APS
REMARK 200 BEAMLINE : 21-ID-F
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 225 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 : 144106
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.79300
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 (%): 48.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NACL, AMMONIUM SULFATE, PH 7.5,
REMARK 280 EVAPORATION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 34.53850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.99650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.31400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.99650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.53850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.31400
REMARK 290 SMTRY3 4 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 294
REMARK 465 ILE A 295
REMARK 465 SER A 296
REMARK 465 GLY A 297
REMARK 465 LEU A 298
REMARK 465 GLU A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 HIS A 304
REMARK 465 HIS A 305
REMARK 465 GLU B 294
REMARK 465 ILE B 295
REMARK 465 SER B 296
REMARK 465 GLY B 297
REMARK 465 LEU B 298
REMARK 465 GLU B 299
REMARK 465 HIS B 300
REMARK 465 HIS B 301
REMARK 465 HIS B 302
REMARK 465 HIS B 303
REMARK 465 HIS B 304
REMARK 465 HIS B 305
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 GLU A 214 CG GLU A 214 CD -0.121
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 44.58 -107.59
REMARK 500 GLU A 98 -95.01 -103.10
REMARK 500 ASP A 106 -133.68 58.34
REMARK 500 GLU A 130 63.39 37.89
REMARK 500 ARG A 153 49.29 -86.48
REMARK 500 VAL A 245 -73.30 -138.04
REMARK 500 LEU A 271 -101.12 -118.57
REMARK 500 PRO B 42 44.45 -108.04
REMARK 500 GLU B 98 -93.19 -102.84
REMARK 500 ASP B 106 -134.51 57.23
REMARK 500 GLU B 130 62.60 39.84
REMARK 500 ASP B 156 -53.10 71.32
REMARK 500 VAL B 245 -69.31 -133.39
REMARK 500 LEU B 271 -97.48 -117.52
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 EDO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO 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 CL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5UXZ RELATED DB: PDB
DBREF 5UY1 A 4 290 UNP P0A3G2 DHAA_RHORH 4 290
DBREF 5UY1 B 4 290 UNP P0A3G2 DHAA_RHORH 4 290
SEQADV 5UY1 VAL A 47 UNP P0A3G2 LEU 47 CONFLICT
SEQADV 5UY1 THR A 58 UNP P0A3G2 SER 58 CONFLICT
SEQADV 5UY1 GLY A 78 UNP P0A3G2 ASP 78 CONFLICT
SEQADV 5UY1 PHE A 87 UNP P0A3G2 TYR 87 CONFLICT
SEQADV 5UY1 MET A 88 UNP P0A3G2 LEU 88 CONFLICT
SEQADV 5UY1 PHE A 128 UNP P0A3G2 CYS 128 CONFLICT
SEQADV 5UY1 THR A 155 UNP P0A3G2 ALA 155 CONFLICT
SEQADV 5UY1 LYS A 160 UNP P0A3G2 GLU 160 CONFLICT
SEQADV 5UY1 VAL A 167 UNP P0A3G2 ALA 167 CONFLICT
SEQADV 5UY1 THR A 172 UNP P0A3G2 ALA 172 CONFLICT
SEQADV 5UY1 MET A 175 UNP P0A3G2 LYS 175 CONFLICT
SEQADV 5UY1 GLY A 176 UNP P0A3G2 CYS 176 CONFLICT
SEQADV 5UY1 ASN A 195 UNP P0A3G2 LYS 195 CONFLICT
SEQADV 5UY1 GLU A 224 UNP P0A3G2 ALA 224 CONFLICT
SEQADV 5UY1 ASP A 227 UNP P0A3G2 ASN 227 CONFLICT
SEQADV 5UY1 LYS A 257 UNP P0A3G2 GLU 257 CONFLICT
SEQADV 5UY1 ALA A 264 UNP P0A3G2 THR 264 CONFLICT
SEQADV 5UY1 ASN A 272 UNP P0A3G2 HIS 272 CONFLICT
SEQADV 5UY1 LEU A 273 UNP P0A3G2 TYR 273 CONFLICT
SEQADV 5UY1 SER A 291 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 THR A 292 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 LEU A 293 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 GLU A 294 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 ILE A 295 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 SER A 296 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 GLY A 297 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 LEU A 298 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 GLU A 299 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 HIS A 300 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 HIS A 301 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 HIS A 302 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 HIS A 303 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 HIS A 304 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 HIS A 305 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 VAL B 47 UNP P0A3G2 LEU 47 CONFLICT
SEQADV 5UY1 THR B 58 UNP P0A3G2 SER 58 CONFLICT
SEQADV 5UY1 GLY B 78 UNP P0A3G2 ASP 78 CONFLICT
SEQADV 5UY1 PHE B 87 UNP P0A3G2 TYR 87 CONFLICT
SEQADV 5UY1 MET B 88 UNP P0A3G2 LEU 88 CONFLICT
SEQADV 5UY1 PHE B 128 UNP P0A3G2 CYS 128 CONFLICT
SEQADV 5UY1 THR B 155 UNP P0A3G2 ALA 155 CONFLICT
SEQADV 5UY1 LYS B 160 UNP P0A3G2 GLU 160 CONFLICT
SEQADV 5UY1 VAL B 167 UNP P0A3G2 ALA 167 CONFLICT
SEQADV 5UY1 THR B 172 UNP P0A3G2 ALA 172 CONFLICT
SEQADV 5UY1 MET B 175 UNP P0A3G2 LYS 175 CONFLICT
SEQADV 5UY1 GLY B 176 UNP P0A3G2 CYS 176 CONFLICT
SEQADV 5UY1 ASN B 195 UNP P0A3G2 LYS 195 CONFLICT
SEQADV 5UY1 GLU B 224 UNP P0A3G2 ALA 224 CONFLICT
SEQADV 5UY1 ASP B 227 UNP P0A3G2 ASN 227 CONFLICT
SEQADV 5UY1 LYS B 257 UNP P0A3G2 GLU 257 CONFLICT
SEQADV 5UY1 ALA B 264 UNP P0A3G2 THR 264 CONFLICT
SEQADV 5UY1 ASN B 272 UNP P0A3G2 HIS 272 CONFLICT
SEQADV 5UY1 LEU B 273 UNP P0A3G2 TYR 273 CONFLICT
SEQADV 5UY1 SER B 291 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 THR B 292 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 LEU B 293 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 GLU B 294 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 ILE B 295 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 SER B 296 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 GLY B 297 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 LEU B 298 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 GLU B 299 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 HIS B 300 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 HIS B 301 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 HIS B 302 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 HIS B 303 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 HIS B 304 UNP P0A3G2 EXPRESSION TAG
SEQADV 5UY1 HIS B 305 UNP P0A3G2 EXPRESSION TAG
SEQRES 1 A 302 ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL GLU
SEQRES 2 A 302 VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY PRO
SEQRES 3 A 302 ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 A 302 THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS VAL
SEQRES 5 A 302 ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 A 302 MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE PHE
SEQRES 7 A 302 ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU ALA
SEQRES 8 A 302 LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP TRP
SEQRES 9 A 302 GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN PRO
SEQRES 10 A 302 GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE ARG
SEQRES 11 A 302 PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA ARG
SEQRES 12 A 302 GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY ARG
SEQRES 13 A 302 LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY THR
SEQRES 14 A 302 LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL GLU
SEQRES 15 A 302 MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL ASP
SEQRES 16 A 302 ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO ILE
SEQRES 17 A 302 ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU GLU
SEQRES 18 A 302 TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS LEU
SEQRES 19 A 302 LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO ALA
SEQRES 20 A 302 GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS LYS
SEQRES 21 A 302 ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN GLU
SEQRES 22 A 302 ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG TRP
SEQRES 23 A 302 LEU SER THR LEU GLU ILE SER GLY LEU GLU HIS HIS HIS
SEQRES 24 A 302 HIS HIS HIS
SEQRES 1 B 302 ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL GLU
SEQRES 2 B 302 VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY PRO
SEQRES 3 B 302 ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 B 302 THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS VAL
SEQRES 5 B 302 ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 B 302 MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE PHE
SEQRES 7 B 302 ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU ALA
SEQRES 8 B 302 LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP TRP
SEQRES 9 B 302 GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN PRO
SEQRES 10 B 302 GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE ARG
SEQRES 11 B 302 PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA ARG
SEQRES 12 B 302 GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY ARG
SEQRES 13 B 302 LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY THR
SEQRES 14 B 302 LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL GLU
SEQRES 15 B 302 MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL ASP
SEQRES 16 B 302 ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO ILE
SEQRES 17 B 302 ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU GLU
SEQRES 18 B 302 TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS LEU
SEQRES 19 B 302 LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO ALA
SEQRES 20 B 302 GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS LYS
SEQRES 21 B 302 ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN GLU
SEQRES 22 B 302 ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG TRP
SEQRES 23 B 302 LEU SER THR LEU GLU ILE SER GLY LEU GLU HIS HIS HIS
SEQRES 24 B 302 HIS HIS HIS
HET EDO A 401 4
HET EDO A 402 4
HET EDO A 403 4
HET CL A 404 1
HET EDO B 401 4
HET EDO B 402 4
HET CL B 403 1
HET CL B 404 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 5(C2 H6 O2)
FORMUL 6 CL 3(CL 1-)
FORMUL 11 HOH *437(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 THR A 137 TRP A 141 5 5
HELIX 6 AA6 PRO A 142 PHE A 144 5 3
HELIX 7 AA7 ALA A 145 ARG A 153 1 9
HELIX 8 AA8 THR A 155 ILE A 163 1 9
HELIX 9 AA9 ASN A 166 GLY A 171 1 6
HELIX 10 AB1 GLY A 171 GLY A 176 1 6
HELIX 11 AB2 THR A 182 GLU A 191 1 10
HELIX 12 AB3 PRO A 192 LEU A 194 5 3
HELIX 13 AB4 ASN A 195 ASP A 198 5 4
HELIX 14 AB5 ARG A 199 LEU A 209 1 11
HELIX 15 AB6 PRO A 215 SER A 232 1 18
HELIX 16 AB7 PRO A 248 LEU A 259 1 12
HELIX 17 AB8 LEU A 273 ASN A 278 1 6
HELIX 18 AB9 ASN A 278 LEU A 293 1 16
HELIX 19 AC1 SER B 44 ARG B 49 5 6
HELIX 20 AC2 ILE B 51 ALA B 56 1 6
HELIX 21 AC3 PHE B 80 LEU B 95 1 16
HELIX 22 AC4 ASP B 106 ASN B 119 1 14
HELIX 23 AC5 THR B 137 TRP B 141 5 5
HELIX 24 AC6 PRO B 142 PHE B 144 5 3
HELIX 25 AC7 ALA B 145 ARG B 153 1 9
HELIX 26 AC8 ASP B 156 ILE B 163 1 8
HELIX 27 AC9 ASN B 166 GLY B 171 1 6
HELIX 28 AD1 GLY B 171 GLY B 176 1 6
HELIX 29 AD2 THR B 182 GLU B 191 1 10
HELIX 30 AD3 PRO B 192 LEU B 194 5 3
HELIX 31 AD4 ASN B 195 ASP B 198 5 4
HELIX 32 AD5 ARG B 199 LEU B 209 1 11
HELIX 33 AD6 PRO B 215 SER B 232 1 18
HELIX 34 AD7 PRO B 248 LEU B 259 1 12
HELIX 35 AD8 LEU B 273 ASN B 278 1 6
HELIX 36 AD9 ASN B 278 LEU B 293 1 16
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 VAL A 265 N LEU A 238
SHEET 1 AA2 8 HIS B 13 VAL B 17 0
SHEET 2 AA2 8 GLU B 20 VAL B 27 -1 O GLU B 20 N VAL B 17
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 HIS B 105 1 O VAL B 101 N LEU B 36
SHEET 6 AA2 8 VAL B 123 MET B 129 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 VAL B 265 N LEU B 238
CISPEP 1 ASN A 41 PRO A 42 0 1.15
CISPEP 2 GLU A 214 PRO A 215 0 -3.60
CISPEP 3 GLU A 214 PRO A 215 0 -3.86
CISPEP 4 THR A 242 PRO A 243 0 0.52
CISPEP 5 ASN B 41 PRO B 42 0 2.50
CISPEP 6 GLU B 214 PRO B 215 0 -5.51
CISPEP 7 THR B 242 PRO B 243 0 2.44
SITE 1 AC1 5 ASP A 26 GLY A 28 ARG A 30 PRO A 174
SITE 2 AC1 5 MET A 175
SITE 1 AC2 3 GLY A 5 THR A 6 GLY A 7
SITE 1 AC3 3 ARG A 153 ASN A 207 HOH A 525
SITE 1 AC4 3 ASN A 41 TRP A 107 PRO A 206
SITE 1 AC5 5 PHE B 149 THR B 172 GLY B 176 HOH B 520
SITE 2 AC5 5 HOH B 575
SITE 1 AC6 6 PHE B 8 SER B 45 ASP B 65 LYS B 71
SITE 2 AC6 6 HOH B 504 HOH B 513
SITE 1 AC7 3 ASN B 41 TRP B 107 PRO B 206
SITE 1 AC8 2 TRP B 228 GLN B 231
CRYST1 69.077 94.628 99.993 90.00 90.00 90.00 P 21 21 21 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 0.014477 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010568 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010001 0.00000
TER 2337 LEU A 293
TER 4666 LEU B 293
MASTER 361 0 8 36 16 0 11 6 5116 2 20 48
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