longtext: 6zvw-pdb

content
HEADER    HYDROLASE                               27-JUL-20   6ZVW
TITLE     X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE HALOTAG7-Q165H LABELED
TITLE    2 WITH A CHLOROALKANE-TETRAMETHYLRHODAMINE FLUOROPHORE SUBSTRATE
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 SP.;
SOURCE   3 ORGANISM_TAXID: 1831;
SOURCE   4 GENE: DHAA;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    HALOALKANE DEHALOGENASE, HALO, TAG, HALOTAG7, SELF-LABELING PROTEIN,
KEYWDS   2 FLUOROPHORE, TETRAMETHYLRHODAMINE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.TARNAWSKI,M.FREI,J.HIBLOT,K.JOHNSSON
REVDAT   1   04-AUG-21 6ZVW    0
JRNL        AUTH   M.TARNAWSKI,M.FREI,J.HIBLOT,K.JOHNSSON
JRNL        TITL   X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE
JRNL        TITL 2 HALOTAG7-Q165H LABELED WITH A
JRNL        TITL 3 CHLOROALKANE-TETRAMETHYLRHODAMINE FLUOROPHORE SUBSTRATE
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX 1.15.2_3472
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.21
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.3
REMARK   3   NUMBER OF REFLECTIONS             : 67807
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224
REMARK   3   R VALUE            (WORKING SET) : 0.222
REMARK   3   FREE R VALUE                     : 0.266
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 3391
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 40.2100 -  4.6100    0.94     2836   150  0.1700 0.1837
REMARK   3     2  4.6100 -  3.6600    0.89     2660   140  0.1623 0.2056
REMARK   3     3  3.6600 -  3.2000    0.88     2636   139  0.1983 0.2398
REMARK   3     4  3.2000 -  2.9100    0.86     2563   134  0.2057 0.2401
REMARK   3     5  2.9100 -  2.7000    0.88     2672   141  0.2244 0.2637
REMARK   3     6  2.7000 -  2.5400    0.87     2613   138  0.2148 0.2587
REMARK   3     7  2.5400 -  2.4100    0.88     2626   138  0.2244 0.2722
REMARK   3     8  2.4100 -  2.3100    0.88     2617   138  0.2242 0.2634
REMARK   3     9  2.3100 -  2.2200    0.86     2628   138  0.2190 0.2699
REMARK   3    10  2.2200 -  2.1400    0.86     2563   135  0.2294 0.2798
REMARK   3    11  2.1400 -  2.0800    0.88     2610   137  0.2315 0.2905
REMARK   3    12  2.0800 -  2.0200    0.88     2664   140  0.2354 0.2849
REMARK   3    13  2.0200 -  1.9600    0.89     2730   144  0.2328 0.3190
REMARK   3    14  1.9600 -  1.9100    0.90     2657   140  0.2340 0.2747
REMARK   3    15  1.9100 -  1.8700    0.90     2727   143  0.2510 0.3790
REMARK   3    16  1.8700 -  1.8300    0.89     2625   139  0.2666 0.3483
REMARK   3    17  1.8300 -  1.7900    0.90     2756   145  0.2827 0.3621
REMARK   3    18  1.7900 -  1.7600    0.92     2727   143  0.2853 0.3364
REMARK   3    19  1.7600 -  1.7300    0.92     2774   146  0.3027 0.3497
REMARK   3    20  1.7300 -  1.7000    0.91     2688   142  0.3120 0.3700
REMARK   3    21  1.7000 -  1.6700    0.92     2813   148  0.3408 0.3560
REMARK   3    22  1.6700 -  1.6500    0.92     2736   144  0.3398 0.3752
REMARK   3    23  1.6500 -  1.6200    0.92     2761   145  0.3684 0.3910
REMARK   3    24  1.6200 -  1.6000    0.91     2734   144  0.3891 0.4397
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : NULL
REMARK   3   B_SOL              : NULL
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.239
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.443
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 16.92
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.49
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.008           4967
REMARK   3   ANGLE     :  0.941           6788
REMARK   3   CHIRALITY :  0.060            706
REMARK   3   PLANARITY :  0.008            952
REMARK   3   DIHEDRAL  : 16.559           2940
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 6ZVW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUL-20.
REMARK 100 THE DEPOSITION ID IS D_1292110337.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 29-JUN-19
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X10SA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000060
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67810
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
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     (%) : 89.3
REMARK 200  DATA REDUNDANCY                : 1.790
REMARK 200  R MERGE                    (I) : 0.08200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 5.0400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.70
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.78
REMARK 200  R MERGE FOR SHELL          (I) : 0.44400
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.650
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6Y7A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.0, 1.0 M LITHIUM
REMARK 280  CHLORIDE, 20% (M/V) PEG 6000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,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
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 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 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 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       48.59   -109.17
REMARK 500    THR A  43     -158.18   -101.64
REMARK 500    SER A  44     -165.25   -160.33
REMARK 500    GLU A  98      -87.35   -109.95
REMARK 500    ASP A 106     -131.67     53.63
REMARK 500    ARG A 153       42.61    -88.89
REMARK 500    ASP A 156      -69.72   -102.29
REMARK 500    VAL A 245      -68.63   -135.54
REMARK 500    LEU A 271      -96.92   -113.73
REMARK 500    THR B  43     -160.25   -102.59
REMARK 500    GLU B  98      -94.17   -100.46
REMARK 500    ASP B 106     -130.18     53.40
REMARK 500    ARG B 153       41.71    -88.84
REMARK 500    ASP B 156      -72.62    -94.94
REMARK 500    VAL B 245      -70.49   -134.73
REMARK 500    LEU B 271      -96.36   -114.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 619        DISTANCE =  6.01 ANGSTROMS
REMARK 525    HOH A 620        DISTANCE =  7.54 ANGSTROMS
REMARK 525    HOH B 623        DISTANCE =  6.36 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6ZVU   RELATED DB: PDB
REMARK 900 RELATED ID: 6ZVV   RELATED DB: PDB
REMARK 900 RELATED ID: 6ZVX   RELATED DB: PDB
REMARK 900 RELATED ID: 6ZVY   RELATED DB: PDB
DBREF  6ZVW A    4   293  UNP    P0A3G3   DHAA_RHOSO       4    293
DBREF  6ZVW B    4   293  UNP    P0A3G3   DHAA_RHOSO       4    293
SEQADV 6ZVW GLY A    3  UNP  P0A3G3              EXPRESSION TAG
SEQADV 6ZVW VAL A   47  UNP  P0A3G3    LEU    47 ENGINEERED MUTATION
SEQADV 6ZVW THR A   58  UNP  P0A3G3    SER    58 ENGINEERED MUTATION
SEQADV 6ZVW GLY A   78  UNP  P0A3G3    ASP    78 ENGINEERED MUTATION
SEQADV 6ZVW PHE A   87  UNP  P0A3G3    TYR    87 ENGINEERED MUTATION
SEQADV 6ZVW MET A   88  UNP  P0A3G3    LEU    88 ENGINEERED MUTATION
SEQADV 6ZVW PHE A  128  UNP  P0A3G3    CYS   128 ENGINEERED MUTATION
SEQADV 6ZVW THR A  155  UNP  P0A3G3    ALA   155 ENGINEERED MUTATION
SEQADV 6ZVW LYS A  160  UNP  P0A3G3    GLU   160 ENGINEERED MUTATION
SEQADV 6ZVW HIS A  165  UNP  P0A3G3    GLN   165 ENGINEERED MUTATION
SEQADV 6ZVW VAL A  167  UNP  P0A3G3    ALA   167 ENGINEERED MUTATION
SEQADV 6ZVW THR A  172  UNP  P0A3G3    ALA   172 ENGINEERED MUTATION
SEQADV 6ZVW MET A  175  UNP  P0A3G3    LYS   175 ENGINEERED MUTATION
SEQADV 6ZVW GLY A  176  UNP  P0A3G3    CYS   176 ENGINEERED MUTATION
SEQADV 6ZVW ASN A  195  UNP  P0A3G3    LYS   195 ENGINEERED MUTATION
SEQADV 6ZVW GLU A  224  UNP  P0A3G3    ALA   224 ENGINEERED MUTATION
SEQADV 6ZVW ASP A  227  UNP  P0A3G3    ASN   227 ENGINEERED MUTATION
SEQADV 6ZVW LYS A  257  UNP  P0A3G3    GLU   257 ENGINEERED MUTATION
SEQADV 6ZVW ALA A  264  UNP  P0A3G3    THR   264 ENGINEERED MUTATION
SEQADV 6ZVW ASN A  272  UNP  P0A3G3    HIS   272 ENGINEERED MUTATION
SEQADV 6ZVW LEU A  273  UNP  P0A3G3    TYR   273 ENGINEERED MUTATION
SEQADV 6ZVW SER A  291  UNP  P0A3G3    PRO   291 ENGINEERED MUTATION
SEQADV 6ZVW THR A  292  UNP  P0A3G3    ALA   292 ENGINEERED MUTATION
SEQADV 6ZVW GLU A  294  UNP  P0A3G3              EXPRESSION TAG
SEQADV 6ZVW ILE A  295  UNP  P0A3G3              EXPRESSION TAG
SEQADV 6ZVW GLY B    3  UNP  P0A3G3              EXPRESSION TAG
SEQADV 6ZVW VAL B   47  UNP  P0A3G3    LEU    47 ENGINEERED MUTATION
SEQADV 6ZVW THR B   58  UNP  P0A3G3    SER    58 ENGINEERED MUTATION
SEQADV 6ZVW GLY B   78  UNP  P0A3G3    ASP    78 ENGINEERED MUTATION
SEQADV 6ZVW PHE B   87  UNP  P0A3G3    TYR    87 ENGINEERED MUTATION
SEQADV 6ZVW MET B   88  UNP  P0A3G3    LEU    88 ENGINEERED MUTATION
SEQADV 6ZVW PHE B  128  UNP  P0A3G3    CYS   128 ENGINEERED MUTATION
SEQADV 6ZVW THR B  155  UNP  P0A3G3    ALA   155 ENGINEERED MUTATION
SEQADV 6ZVW LYS B  160  UNP  P0A3G3    GLU   160 ENGINEERED MUTATION
SEQADV 6ZVW HIS B  165  UNP  P0A3G3    GLN   165 ENGINEERED MUTATION
SEQADV 6ZVW VAL B  167  UNP  P0A3G3    ALA   167 ENGINEERED MUTATION
SEQADV 6ZVW THR B  172  UNP  P0A3G3    ALA   172 ENGINEERED MUTATION
SEQADV 6ZVW MET B  175  UNP  P0A3G3    LYS   175 ENGINEERED MUTATION
SEQADV 6ZVW GLY B  176  UNP  P0A3G3    CYS   176 ENGINEERED MUTATION
SEQADV 6ZVW ASN B  195  UNP  P0A3G3    LYS   195 ENGINEERED MUTATION
SEQADV 6ZVW GLU B  224  UNP  P0A3G3    ALA   224 ENGINEERED MUTATION
SEQADV 6ZVW ASP B  227  UNP  P0A3G3    ASN   227 ENGINEERED MUTATION
SEQADV 6ZVW LYS B  257  UNP  P0A3G3    GLU   257 ENGINEERED MUTATION
SEQADV 6ZVW ALA B  264  UNP  P0A3G3    THR   264 ENGINEERED MUTATION
SEQADV 6ZVW ASN B  272  UNP  P0A3G3    HIS   272 ENGINEERED MUTATION
SEQADV 6ZVW LEU B  273  UNP  P0A3G3    TYR   273 ENGINEERED MUTATION
SEQADV 6ZVW SER B  291  UNP  P0A3G3    PRO   291 ENGINEERED MUTATION
SEQADV 6ZVW THR B  292  UNP  P0A3G3    ALA   292 ENGINEERED MUTATION
SEQADV 6ZVW GLU B  294  UNP  P0A3G3              EXPRESSION TAG
SEQADV 6ZVW ILE B  295  UNP  P0A3G3              EXPRESSION TAG
SEQRES   1 A  293  GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES   2 A  293  GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES   3 A  293  PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES   4 A  293  PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES   5 A  293  VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES   6 A  293  GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES   7 A  293  PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES   8 A  293  ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES   9 A  293  TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES  10 A  293  PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES  11 A  293  ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES  12 A  293  ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES  13 A  293  ARG LYS LEU ILE ILE ASP HIS ASN VAL PHE ILE GLU GLY
SEQRES  14 A  293  THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES  15 A  293  GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES  16 A  293  ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES  17 A  293  ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES  18 A  293  GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES  19 A  293  LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES  20 A  293  ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES  21 A  293  LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES  22 A  293  GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES  23 A  293  TRP LEU SER THR LEU GLU ILE
SEQRES   1 B  293  GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES   2 B  293  GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES   3 B  293  PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES   4 B  293  PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES   5 B  293  VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES   6 B  293  GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES   7 B  293  PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES   8 B  293  ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES   9 B  293  TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES  10 B  293  PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES  11 B  293  ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES  12 B  293  ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES  13 B  293  ARG LYS LEU ILE ILE ASP HIS ASN VAL PHE ILE GLU GLY
SEQRES  14 B  293  THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES  15 B  293  GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES  16 B  293  ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES  17 B  293  ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES  18 B  293  GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES  19 B  293  LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES  20 B  293  ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES  21 B  293  LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES  22 B  293  GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES  23 B  293  TRP LEU SER THR LEU GLU ILE
HET    OEH  A 301      44
HET     CL  A 302       1
HET    GOL  B 301       6
HET    PEG  B 302       7
HET    OEH  B 303      44
HET     CL  B 304       1
HETNAM     OEH [9-[2-CARBOXY-5-[2-[2-(6-CHLORANYLHEXOXY)
HETNAM   2 OEH  ETHOXY]ETHYLCARBAMOYL]PHENYL]-6-(DIMETHYLAMINO)
HETNAM   3 OEH  XANTHEN-3-YLIDENE]-DIMETHYL-AZANIUM
HETNAM      CL CHLORIDE ION
HETNAM     GOL GLYCEROL
HETNAM     PEG DI(HYDROXYETHYL)ETHER
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   3  OEH    2(C35 H43 CL N3 O6 1+)
FORMUL   4   CL    2(CL 1-)
FORMUL   5  GOL    C3 H8 O3
FORMUL   6  PEG    C4 H10 O3
FORMUL   9  HOH   *443(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  ARG A  153  1                                  12
HELIX    7 AA7 ASP A  156  ILE A  163  1                                   8
HELIX    8 AA8 ASN A  166  GLY A  171  1                                   6
HELIX    9 AA9 GLY A  171  GLY A  176  1                                   6
HELIX   10 AB1 THR A  182  GLU A  191  1                                  10
HELIX   11 AB2 PRO A  192  LEU A  194  5                                   3
HELIX   12 AB3 ASN A  195  ASP A  198  5                                   4
HELIX   13 AB4 ARG A  199  LEU A  209  1                                  11
HELIX   14 AB5 PRO A  215  SER A  232  1                                  18
HELIX   15 AB6 PRO A  248  LEU A  259  1                                  12
HELIX   16 AB7 LEU A  273  ASN A  278  1                                   6
HELIX   17 AB8 ASN A  278  THR A  292  1                                  15
HELIX   18 AB9 SER B   44  ARG B   49  5                                   6
HELIX   19 AC1 ILE B   51  ALA B   56  1                                   6
HELIX   20 AC2 PHE B   80  LEU B   95  1                                  16
HELIX   21 AC3 ASP B  106  ASN B  119  1                                  14
HELIX   22 AC4 THR B  137  TRP B  141  5                                   5
HELIX   23 AC5 PRO B  142  ARG B  153  1                                  12
HELIX   24 AC6 ASP B  156  ILE B  163  1                                   8
HELIX   25 AC7 ASN B  166  GLY B  171  1                                   6
HELIX   26 AC8 LEU B  173  VAL B  177  5                                   5
HELIX   27 AC9 THR B  182  GLU B  191  1                                  10
HELIX   28 AD1 PRO B  192  LEU B  194  5                                   3
HELIX   29 AD2 ASN B  195  ASP B  198  5                                   4
HELIX   30 AD3 ARG B  199  LEU B  209  1                                  11
HELIX   31 AD4 PRO B  215  SER B  232  1                                  18
HELIX   32 AD5 PRO B  248  LEU B  259  1                                  12
HELIX   33 AD6 LEU B  273  ASN B  278  1                                   6
HELIX   34 AD7 ASN B  278  SER B  291  1                                  14
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  LYS B 263   N  LEU B 238
LINK         OD2 ASP A 106                 C20 OEH A 301     1555   1555  1.38
LINK         OD2 ASP B 106                 C20 OEH B 303     1555   1555  1.38
CISPEP   1 ASN A   41    PRO A   42          0         1.27
CISPEP   2 GLU A  214    PRO A  215          0        -9.54
CISPEP   3 THR A  242    PRO A  243          0         5.28
CISPEP   4 ASN B   41    PRO B   42          0         1.61
CISPEP   5 GLU B  214    PRO B  215          0        -8.10
CISPEP   6 THR B  242    PRO B  243          0         4.94
CRYST1   44.180   47.560   78.250  97.37  89.97 114.26 P 1           2
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      0.022635  0.010199  0.001436        0.00000
SCALE2      0.000000  0.023062  0.003273        0.00000
SCALE3      0.000000  0.000000  0.012908        0.00000
TER    2352      ILE A 295
TER    4704      ILE B 295
MASTER      260    0    6   34   16    0    0    6 5248    2  103   46
END