longtext: 5uy1-pdb

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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
END