longtext: 6qz3-pdb

content
HEADER    STRUCTURAL GENOMICS                     11-MAR-19   6QZ3
TITLE     STRUCTURE OF MHETASE FROM IDEONELLA SAKAIENSIS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MONO(2-HYDROXYETHYL) TEREPHTHALATE HYDROLASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: MHETASE;
COMPND   5 EC: 3.1.1.102;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS (STRAIN 201-F6);
SOURCE   3 ORGANISM_TAXID: 1547922;
SOURCE   4 STRAIN: 201-F6;
SOURCE   5 GENE: ISF6_0224;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: C41;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PCJ136
KEYWDS    MHETASE, PET DEGRADATION, STRUCTURAL GENOMICS
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.D.ALLEN,C.W.JOHNSON,B.C.KNOTT,G.T.BECKHAM,J.E.MCGEEHAN
REVDAT   1   30-SEP-20 6QZ3    0
JRNL        AUTH   M.D.ALLEN,C.W.JOHNSON,B.C.KNOTT,G.T.BECKHAM,J.E.MCGEEHAN
JRNL        TITL   STRUCTURE OF FROM MHETASE FROM IDEONELLA SAKAIENSIS
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (1.13_2998: ???)
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 : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.82
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.130
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8
REMARK   3   NUMBER OF REFLECTIONS             : 161084
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.163
REMARK   3   R VALUE            (WORKING SET) : 0.162
REMARK   3   FREE R VALUE                     : 0.178
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.160
REMARK   3   FREE R VALUE TEST SET COUNT      : 8305
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 45.8403 -  4.9695    1.00     5138   227  0.1609 0.1471
REMARK   3     2  4.9695 -  3.9452    1.00     5174   226  0.1329 0.1302
REMARK   3     3  3.9452 -  3.4467    1.00     5079   290  0.1425 0.1471
REMARK   3     4  3.4467 -  3.1316    1.00     5110   269  0.1506 0.1641
REMARK   3     5  3.1316 -  2.9072    1.00     5125   246  0.1535 0.1848
REMARK   3     6  2.9072 -  2.7358    1.00     5116   289  0.1611 0.1776
REMARK   3     7  2.7358 -  2.5988    1.00     5050   322  0.1605 0.1608
REMARK   3     8  2.5988 -  2.4857    1.00     5121   247  0.1613 0.1642
REMARK   3     9  2.4857 -  2.3900    1.00     5089   283  0.1567 0.1895
REMARK   3    10  2.3900 -  2.3075    1.00     5083   291  0.1599 0.2006
REMARK   3    11  2.3075 -  2.2354    1.00     5110   260  0.1547 0.1478
REMARK   3    12  2.2354 -  2.1715    1.00     5104   282  0.1598 0.1901
REMARK   3    13  2.1715 -  2.1143    1.00     5123   274  0.1689 0.1745
REMARK   3    14  2.1143 -  2.0627    1.00     5098   262  0.1737 0.2118
REMARK   3    15  2.0627 -  2.0158    1.00     5090   313  0.1715 0.2025
REMARK   3    16  2.0158 -  1.9729    1.00     5095   300  0.1732 0.2107
REMARK   3    17  1.9729 -  1.9335    1.00     4982   324  0.1829 0.2051
REMARK   3    18  1.9335 -  1.8970    1.00     5153   273  0.1862 0.2476
REMARK   3    19  1.8970 -  1.8631    1.00     5068   310  0.1825 0.2125
REMARK   3    20  1.8631 -  1.8315    1.00     5118   265  0.1936 0.2548
REMARK   3    21  1.8315 -  1.8020    1.00     5041   287  0.1966 0.2097
REMARK   3    22  1.8020 -  1.7743    1.00     5118   301  0.1962 0.2217
REMARK   3    23  1.7743 -  1.7482    1.00     5101   296  0.1964 0.2174
REMARK   3    24  1.7482 -  1.7235    1.00     5038   324  0.1991 0.2458
REMARK   3    25  1.7235 -  1.7003    1.00     5089   254  0.2059 0.2558
REMARK   3    26  1.7003 -  1.6782    1.00     5117   251  0.2129 0.2482
REMARK   3    27  1.6782 -  1.6572    1.00     5116   308  0.2272 0.2561
REMARK   3    28  1.6572 -  1.6372    1.00     5096   255  0.2377 0.2606
REMARK   3    29  1.6372 -  1.6182    1.00     5116   227  0.2445 0.2829
REMARK   3    30  1.6182 -  1.6000    0.95     4921   249  0.2712 0.2821
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : NULL
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)     : 0.170
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.290
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
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      :  0.003           4253
REMARK   3   ANGLE     :  0.613           5799
REMARK   3   CHIRALITY :  0.043            609
REMARK   3   PLANARITY :  0.004            775
REMARK   3   DIHEDRAL  :  3.813           3359
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 6QZ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAR-19.
REMARK 100 THE DEPOSITION ID IS D_1292101169.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-18
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : DIAMOND
REMARK 200  BEAMLINE                       : I03
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 83917
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.250
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8
REMARK 200  DATA REDUNDANCY                : 12.60
REMARK 200  R MERGE                    (I) : 0.06300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 20.2000
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) : 1.69
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.56200
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: SAD
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   (%): 49.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CACODYLATE (PH 6.5), 9%
REMARK 280  PEG 8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   X,-Y,-Z
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   -X,-Y+1/2,Z+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.50800
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.82150
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.50800
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       45.82150
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 TOTAL BURIED SURFACE AREA: 360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 KCAL/MOL
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH A 843  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A1491  LIES ON A SPECIAL POSITION.
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     MSE A     1
REMARK 465     GLN A     2
REMARK 465     THR A     3
REMARK 465     THR A     4
REMARK 465     VAL A     5
REMARK 465     THR A     6
REMARK 465     THR A     7
REMARK 465     MSE A     8
REMARK 465     LEU A     9
REMARK 465     LEU A    10
REMARK 465     ALA A    11
REMARK 465     SER A    12
REMARK 465     VAL A    13
REMARK 465     ALA A    14
REMARK 465     LEU A    15
REMARK 465     ALA A    16
REMARK 465     ALA A    17
REMARK 465     CYS A    18
REMARK 465     ALA A    19
REMARK 465     GLY A    20
REMARK 465     GLY A    21
REMARK 465     GLY A    22
REMARK 465     SER A    23
REMARK 465     THR A    24
REMARK 465     PRO A    25
REMARK 465     LEU A    26
REMARK 465     PRO A    27
REMARK 465     LEU A    28
REMARK 465     PRO A    29
REMARK 465     GLN A    30
REMARK 465     GLN A    31
REMARK 465     GLN A    32
REMARK 465     PRO A    33
REMARK 465     PRO A    34
REMARK 465     GLN A    35
REMARK 465     GLN A    36
REMARK 465     GLU A    37
REMARK 465     PRO A    38
REMARK 465     PRO A    39
REMARK 465     ASP A    56
REMARK 465     GLY A    57
REMARK 465     ASN A    58
REMARK 465     GLY A    59
REMARK 465     ASP A    60
REMARK 465     MSE A    61
REMARK 465     LEU A   604
REMARK 465     GLU A   605
REMARK 465     HIS A   606
REMARK 465     HIS A   607
REMARK 465     HIS A   608
REMARK 465     HIS A   609
REMARK 465     HIS A   610
REMARK 465     HIS A   611
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    HOH A  1313     O    HOH A  1393              1.82
REMARK 500   O    HOH A  1430     O    HOH A  1480              1.83
REMARK 500   O    HOH A   860     O    HOH A   939              1.83
REMARK 500   O    HOH A  1300     O    HOH A  1383              1.83
REMARK 500   O    HOH A   808     O    HOH A  1352              1.84
REMARK 500   O    HOH A  1419     O    HOH A  1532              1.84
REMARK 500   O    HOH A  1222     O    HOH A  1487              1.86
REMARK 500   O    HOH A  1011     O    HOH A  1235              1.89
REMARK 500   O    HOH A  1217     O    HOH A  1466              1.89
REMARK 500   O    HOH A  1266     O    HOH A  1322              1.91
REMARK 500   O    HOH A  1405     O    HOH A  1535              1.92
REMARK 500   O    HOH A  1307     O    HOH A  1318              1.96
REMARK 500   O    HOH A  1324     O    HOH A  1343              1.96
REMARK 500   O    HOH A   889     O    HOH A  1372              2.00
REMARK 500   O    HOH A  1224     O    HOH A  1464              2.01
REMARK 500   O    ALA A   343     O    HOH A   801              2.01
REMARK 500   O    HOH A  1299     O    HOH A  1341              2.06
REMARK 500   O    HOH A  1378     O    HOH A  1481              2.09
REMARK 500   O    HOH A  1197     O    HOH A  1278              2.09
REMARK 500   O    HOH A  1226     O    HOH A  1268              2.13
REMARK 500   O    HOH A   909     O    HOH A  1335              2.15
REMARK 500   O    HOH A  1470     O    HOH A  1501              2.16
REMARK 500   O    HOH A   816     O    HOH A  1250              2.16
REMARK 500   O    HOH A   943     O    HOH A  1145              2.16
REMARK 500   O    HOH A  1348     O    HOH A  1404              2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH A  1334     O    HOH A  1398     4654     2.09
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    ALA A  67       33.57    -95.03
REMARK 500    ASN A 134     -144.94     57.93
REMARK 500    TYR A 194      -30.62   -154.08
REMARK 500    SER A 225     -122.36     70.06
REMARK 500    ALA A 249       59.13     31.94
REMARK 500    ASP A 311       14.53   -146.96
REMARK 500    TYR A 373      -96.44   -143.61
REMARK 500    SER A 383     -144.35   -137.15
REMARK 500    VAL A 412      -61.48    -97.08
REMARK 500    SER A 491       32.89    -99.47
REMARK 500    ASN A 527     -153.15    -87.34
REMARK 500    CYS A 529      -21.58     68.53
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 A1543        DISTANCE =  5.98 ANGSTROMS
REMARK 525    HOH A1544        DISTANCE =  6.01 ANGSTROMS
REMARK 525    HOH A1545        DISTANCE =  6.28 ANGSTROMS
REMARK 525    HOH A1546        DISTANCE =  6.33 ANGSTROMS
REMARK 525    HOH A1547        DISTANCE =  6.62 ANGSTROMS
REMARK 525    HOH A1548        DISTANCE =  6.87 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 702  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 304   O
REMARK 620 2 ASP A 304   OD1  70.7
REMARK 620 3 ASP A 307   OD1  72.0 136.5
REMARK 620 4 ASP A 307   OD2  75.7 135.6  50.2
REMARK 620 5 LEU A 309   O    83.0  82.9  71.0 121.0
REMARK 620 6 ASP A 311   OD1 145.4  75.4 134.0 136.8  86.0
REMARK 620 7 ILE A 313   O    98.7  78.7 128.9  78.6 159.7  81.2
REMARK 620 8 HOH A 823   O   142.5 146.6  72.0  73.2  95.4  71.1  95.3
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BEZ A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 702
DBREF1 6QZ3 A    1   603  UNP                  MHETH_IDESA
DBREF2 6QZ3 A     A0A0K8P8E7                          1         603
SEQADV 6QZ3 LEU A  604  UNP  A0A0K8P8E           EXPRESSION TAG
SEQADV 6QZ3 GLU A  605  UNP  A0A0K8P8E           EXPRESSION TAG
SEQADV 6QZ3 HIS A  606  UNP  A0A0K8P8E           EXPRESSION TAG
SEQADV 6QZ3 HIS A  607  UNP  A0A0K8P8E           EXPRESSION TAG
SEQADV 6QZ3 HIS A  608  UNP  A0A0K8P8E           EXPRESSION TAG
SEQADV 6QZ3 HIS A  609  UNP  A0A0K8P8E           EXPRESSION TAG
SEQADV 6QZ3 HIS A  610  UNP  A0A0K8P8E           EXPRESSION TAG
SEQADV 6QZ3 HIS A  611  UNP  A0A0K8P8E           EXPRESSION TAG
SEQRES   1 A  611  MSE GLN THR THR VAL THR THR MSE LEU LEU ALA SER VAL
SEQRES   2 A  611  ALA LEU ALA ALA CYS ALA GLY GLY GLY SER THR PRO LEU
SEQRES   3 A  611  PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO
SEQRES   4 A  611  PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA CYS GLU
SEQRES   5 A  611  ALA LEU LYS ASP GLY ASN GLY ASP MSE VAL TRP PRO ASN
SEQRES   6 A  611  ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA
SEQRES   7 A  611  ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO GLU HIS
SEQRES   8 A  611  CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR GLY ILE
SEQRES   9 A  611  ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU ARG MSE
SEQRES  10 A  611  PRO ALA GLU TRP ASN GLY ARG PHE PHE MSE GLU GLY GLY
SEQRES  11 A  611  SER GLY THR ASN GLY SER LEU SER ALA ALA THR GLY SER
SEQRES  12 A  611  ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER ARG ASN
SEQRES  13 A  611  PHE ALA THR ILE ALA THR ASP GLY GLY HIS ASP ASN ALA
SEQRES  14 A  611  VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL ALA PHE
SEQRES  15 A  611  GLY LEU ASP PRO GLN ALA ARG LEU ASP MSE GLY TYR ASN
SEQRES  16 A  611  SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA ALA VAL
SEQRES  17 A  611  ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER TYR PHE
SEQRES  18 A  611  ILE GLY CYS SER GLU GLY GLY ARG GLU GLY MSE MSE LEU
SEQRES  19 A  611  SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE VAL ALA
SEQRES  20 A  611  GLY ALA PRO GLY TYR GLN LEU PRO LYS ALA GLY ILE SER
SEQRES  21 A  611  GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA ALA VAL
SEQRES  22 A  611  GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN LYS SER
SEQRES  23 A  611  PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN ALA ILE
SEQRES  24 A  611  LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY
SEQRES  25 A  611  ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP
SEQRES  26 A  611  PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU
SEQRES  27 A  611  GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU SER PRO
SEQRES  28 A  611  VAL GLN VAL THR ALA ILE LYS ARG ALA MSE ALA GLY PRO
SEQRES  29 A  611  VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG TRP ALA
SEQRES  30 A  611  TRP ASP ALA GLY MSE SER GLY LEU SER GLY THR THR TYR
SEQRES  31 A  611  ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER PHE ASN
SEQRES  32 A  611  SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY PHE SER
SEQRES  33 A  611  ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO PRO GLU
SEQRES  34 A  611  PRO MSE PRO MSE THR GLN VAL ALA ALA ARG MSE MSE LYS
SEQRES  35 A  611  PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP ALA THR
SEQRES  36 A  611  SER GLY GLN PHE THR GLN SER SER MSE ASP TRP HIS GLY
SEQRES  37 A  611  ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP ARG GLY
SEQRES  38 A  611  GLY LYS MSE ILE LEU TYR HIS GLY MSE SER ASP ALA ALA
SEQRES  39 A  611  PHE SER ALA LEU ASP THR ALA ASP TYR TYR GLU ARG LEU
SEQRES  40 A  611  GLY ALA ALA MSE PRO GLY ALA ALA GLY PHE ALA ARG LEU
SEQRES  41 A  611  PHE LEU VAL PRO GLY MSE ASN HIS CYS SER GLY GLY PRO
SEQRES  42 A  611  GLY THR ASP ARG PHE ASP MSE LEU THR PRO LEU VAL ALA
SEQRES  43 A  611  TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE SER ALA
SEQRES  44 A  611  TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA ALA ARG
SEQRES  45 A  611  THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR
SEQRES  46 A  611  LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN PHE ALA
SEQRES  47 A  611  CYS ALA ALA PRO PRO LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 6QZ3 MSE A  117  MET  MODIFIED RESIDUE
MODRES 6QZ3 MSE A  127  MET  MODIFIED RESIDUE
MODRES 6QZ3 MSE A  192  MET  MODIFIED RESIDUE
MODRES 6QZ3 MSE A  232  MET  MODIFIED RESIDUE
MODRES 6QZ3 MSE A  233  MET  MODIFIED RESIDUE
MODRES 6QZ3 MSE A  361  MET  MODIFIED RESIDUE
MODRES 6QZ3 MSE A  382  MET  MODIFIED RESIDUE
MODRES 6QZ3 MSE A  431  MET  MODIFIED RESIDUE
MODRES 6QZ3 MSE A  433  MET  MODIFIED RESIDUE
MODRES 6QZ3 MSE A  440  MET  MODIFIED RESIDUE
MODRES 6QZ3 MSE A  441  MET  MODIFIED RESIDUE
MODRES 6QZ3 MSE A  464  MET  MODIFIED RESIDUE
MODRES 6QZ3 MSE A  484  MET  MODIFIED RESIDUE
MODRES 6QZ3 MSE A  490  MET  MODIFIED RESIDUE
MODRES 6QZ3 MSE A  511  MET  MODIFIED RESIDUE
MODRES 6QZ3 MSE A  526  MET  MODIFIED RESIDUE
MODRES 6QZ3 MSE A  540  MET  MODIFIED RESIDUE
HET    MSE  A 117       8
HET    MSE  A 127       8
HET    MSE  A 192       8
HET    MSE  A 232       8
HET    MSE  A 233       8
HET    MSE  A 361       8
HET    MSE  A 382       8
HET    MSE  A 431       8
HET    MSE  A 433       8
HET    MSE  A 440       8
HET    MSE  A 441       8
HET    MSE  A 464       8
HET    MSE  A 484       8
HET    MSE  A 490       8
HET    MSE  A 511       8
HET    MSE  A 526       8
HET    MSE  A 540       8
HET    BEZ  A 701       9
HET     CA  A 702       1
HETNAM     MSE SELENOMETHIONINE
HETNAM     BEZ BENZOIC ACID
HETNAM      CA CALCIUM ION
FORMUL   1  MSE    17(C5 H11 N O2 SE)
FORMUL   2  BEZ    C7 H6 O2
FORMUL   3   CA    CA 2+
FORMUL   4  HOH   *748(H2 O)
HELIX    1 AA1 SER A   47  ALA A   53  1                                   7
HELIX    2 AA2 ALA A  152  ASN A  156  5                                   5
HELIX    3 AA3 LEU A  177  LEU A  184  5                                   8
HELIX    4 AA4 ASP A  185  TYR A  194  1                                  10
HELIX    5 AA5 TYR A  194  GLY A  213  1                                  20
HELIX    6 AA6 SER A  225  PHE A  238  1                                  14
HELIX    7 AA7 GLN A  253  PRO A  255  5                                   3
HELIX    8 AA8 LYS A  256  ALA A  269  1                                  14
HELIX    9 AA9 PRO A  270  ALA A  272  5                                   3
HELIX   10 AB1 LEU A  282  SER A  286  5                                   5
HELIX   11 AB2 SER A  288  ASP A  304  1                                  17
HELIX   12 AB3 ALA A  305  GLY A  308  5                                   4
HELIX   13 AB4 ASN A  316  PHE A  324  1                                   9
HELIX   14 AB5 SER A  350  GLY A  363  1                                  14
HELIX   15 AB6 ASP A  379  SER A  383  5                                   5
HELIX   16 AB7 TRP A  394  LEU A  399  1                                   6
HELIX   17 AB8 GLY A  414  PHE A  424  1                                  11
HELIX   18 AB9 PRO A  432  THR A  434  5                                   3
HELIX   19 AC1 GLN A  435  LYS A  442  1                                   8
HELIX   20 AC2 ILE A  447  TRP A  453  5                                   7
HELIX   21 AC3 SER A  462  GLY A  468  1                                   7
HELIX   22 AC4 LEU A  474  ARG A  480  1                                   7
HELIX   23 AC5 SER A  496  MSE A  511  1                                  16
HELIX   24 AC6 GLY A  513  GLY A  516  5                                   4
HELIX   25 AC7 MSE A  540  GLY A  551  1                                  12
HELIX   26 AC8 THR A  563  GLY A  568  5                                   6
HELIX   27 AC9 THR A  593  ALA A  595  5                                   3
SHEET    1 AA1 9 THR A  68  ARG A  76  0
SHEET    2 AA1 9 HIS A  91  THR A 102 -1  O  HIS A  91   N  ARG A  76
SHEET    3 AA1 9 PRO A 108  PRO A 118 -1  O  LEU A 115   N  VAL A  94
SHEET    4 AA1 9 ALA A 158  THR A 162 -1  O  THR A 159   N  ARG A 116
SHEET    5 AA1 9 ARG A 124  GLU A 128  1  N  PHE A 126   O  ALA A 158
SHEET    6 AA1 9 LYS A 218  CYS A 224  1  O  TYR A 220   N  PHE A 125
SHEET    7 AA1 9 GLY A 244  GLY A 248  1  O  GLY A 248   N  GLY A 223
SHEET    8 AA1 9 LYS A 483  GLY A 489  1  O  ILE A 485   N  ILE A 245
SHEET    9 AA1 9 ALA A 518  VAL A 523  1  O  ARG A 519   N  LEU A 486
SHEET    1 AA2 2 LEU A 385  SER A 386  0
SHEET    2 AA2 2 THR A 389  TYR A 390 -1  O  THR A 389   N  SER A 386
SHEET    1 AA3 2 ILE A 557  TRP A 560  0
SHEET    2 AA3 2 THR A 573  LEU A 576 -1  O  LEU A 576   N  ILE A 557
SHEET    1 AA4 2 ILE A 582  TYR A 585  0
SHEET    2 AA4 2 PHE A 597  ALA A 600 -1  O  ALA A 600   N  ILE A 582
SSBOND   1 CYS A   51    CYS A   92                          1555   1555  2.04
SSBOND   2 CYS A  224    CYS A  529                          1555   1555  2.06
SSBOND   3 CYS A  303    CYS A  320                          1555   1555  2.05
SSBOND   4 CYS A  340    CYS A  348                          1555   1555  2.04
SSBOND   5 CYS A  577    CYS A  599                          1555   1555  2.05
LINK         C   ARG A 116                 N   MSE A 117     1555   1555  1.33
LINK         C   MSE A 117                 N   PRO A 118     1555   1555  1.33
LINK         C   PHE A 126                 N   MSE A 127     1555   1555  1.33
LINK         C   MSE A 127                 N   GLU A 128     1555   1555  1.33
LINK         C   ASP A 191                 N   MSE A 192     1555   1555  1.33
LINK         C   MSE A 192                 N   GLY A 193     1555   1555  1.33
LINK         C   GLY A 231                 N   MSE A 232     1555   1555  1.33
LINK         C   MSE A 232                 N   MSE A 233     1555   1555  1.33
LINK         C   MSE A 233                 N   LEU A 234     1555   1555  1.34
LINK         C   ALA A 360                 N   MSE A 361     1555   1555  1.33
LINK         C   MSE A 361                 N   ALA A 362     1555   1555  1.34
LINK         C   GLY A 381                 N   MSE A 382     1555   1555  1.33
LINK         C   MSE A 382                 N   SER A 383     1555   1555  1.33
LINK         C   PRO A 430                 N   MSE A 431     1555   1555  1.33
LINK         C   MSE A 431                 N   PRO A 432     1555   1555  1.34
LINK         C   PRO A 432                 N   MSE A 433     1555   1555  1.33
LINK         C   MSE A 433                 N   THR A 434     1555   1555  1.34
LINK         C   ARG A 439                 N   MSE A 440     1555   1555  1.33
LINK         C   MSE A 440                 N   MSE A 441     1555   1555  1.33
LINK         C   MSE A 441                 N   LYS A 442     1555   1555  1.33
LINK         C   SER A 463                 N   MSE A 464     1555   1555  1.33
LINK         C   MSE A 464                 N   ASP A 465     1555   1555  1.34
LINK         C   LYS A 483                 N   MSE A 484     1555   1555  1.33
LINK         C   MSE A 484                 N   ILE A 485     1555   1555  1.33
LINK         C   GLY A 489                 N   MSE A 490     1555   1555  1.33
LINK         C   MSE A 490                 N   SER A 491     1555   1555  1.34
LINK         C   ALA A 510                 N   MSE A 511     1555   1555  1.33
LINK         C   MSE A 511                 N   PRO A 512     1555   1555  1.33
LINK         C   GLY A 525                 N   MSE A 526     1555   1555  1.33
LINK         C   MSE A 526                 N   ASN A 527     1555   1555  1.33
LINK         C   ASP A 539                 N   MSE A 540     1555   1555  1.33
LINK         C   MSE A 540                 N   LEU A 541     1555   1555  1.34
LINK         O   ASP A 304                CA    CA A 702     1555   1555  2.49
LINK         OD1 ASP A 304                CA    CA A 702     1555   1555  2.45
LINK         OD1 ASP A 307                CA    CA A 702     1555   1555  2.66
LINK         OD2 ASP A 307                CA    CA A 702     1555   1555  2.49
LINK         O   LEU A 309                CA    CA A 702     1555   1555  2.33
LINK         OD1 ASP A 311                CA    CA A 702     1555   1555  2.53
LINK         O   ILE A 313                CA    CA A 702     1555   1555  2.38
LINK        CA    CA A 702                 O   HOH A 823     1555   1555  2.53
CISPEP   1 THR A  426    PRO A  427          0        -2.35
CISPEP   2 TYR A  579    PRO A  580          0         4.20
SITE     1 AC1 11 GLY A 132  SER A 225  LEU A 254  ALA A 257
SITE     2 AC1 11 TRP A 397  ARG A 411  PHE A 415  SER A 416
SITE     3 AC1 11 PHE A 495  HOH A 855  HOH A1068
SITE     1 AC2  6 ASP A 304  ASP A 307  LEU A 309  ASP A 311
SITE     2 AC2  6 ILE A 313  HOH A 823
CRYST1   77.368   89.016   91.643  90.00  90.00  90.00 P 2 21 21     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      0.012925  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011234  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010912        0.00000
TER    4128      PRO A 603
MASTER      416    0   19   27   15    0    5    6 4879    1  195   47
END