longtext: 8qwi-pdb

content
HEADER    HYDROLASE                               19-OCT-23   8QWI
TITLE     COMPARISON OF ROOM-TEMPERATURE AND CRYOGENIC STRUCTURES OF SOLUBLE
TITLE    2 EPOXIDE HYDROLASE WITH LIGANDS BOUND.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;
COMPND   3 CHAIN: A;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: EPHX2;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS    INHIBITOR, SERIAL CRYSTALLOGRAPHY, DRUG DISCOVERY, FIXED TARGET, ROOM
KEYWDS   2 TEMPERATURE, MICROCRYSTALS, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.DUNGE,O.UWANGUE,C.PHAN,M.BJELCIC,J.GUNNARSSON,G.WEHLANDER,H.KACK,
AUTHOR   2 G.BRANDEN
REVDAT   1   14-AUG-24 8QWI    0
JRNL        AUTH   A.DUNGE,C.PHAN,O.UWANGUE,M.BJELCIC,J.GUNNARSSON,G.WEHLANDER,
JRNL        AUTH 2 H.KACK,G.BRANDEN
JRNL        TITL   EXPLORING SERIAL CRYSTALLOGRAPHY FOR DRUG DISCOVERY.
JRNL        REF    IUCRJ                                      2024
JRNL        REFN                   ESSN 2052-2525
JRNL        PMID   39072424
JRNL        DOI    10.1107/S2052252524006134
REMARK   2
REMARK   2 RESOLUTION.    2.12 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : BUSTER 2.11.8
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.15
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 37504
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)  : 0.178
REMARK   3   R VALUE            (WORKING SET)  : 0.177
REMARK   3   FREE R VALUE                      : 0.204
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : NULL
REMARK   3   FREE R VALUE TEST SET COUNT       : 1913
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED               : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.12
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.13
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 100.0
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : NULL
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : NULL
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2566
REMARK   3   BIN FREE R VALUE                        : 0.3110
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 38
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4313
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 18
REMARK   3   SOLVENT ATOMS            : 209
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.42
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -3.37160
REMARK   3    B22 (A**2) : -3.37160
REMARK   3    B33 (A**2) : 6.74310
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 COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.230
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.193
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.154
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.182
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.150
REMARK   3
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK   3
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.
REMARK   3    BOND LENGTHS              : 4477   ; 2.000  ; HARMONIC
REMARK   3    BOND ANGLES               : 6075   ; 2.000  ; HARMONIC
REMARK   3    TORSION ANGLES            : 1563   ; 2.000  ; SINUSOIDAL
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL
REMARK   3    GENERAL PLANES            : 754    ; 5.000  ; HARMONIC
REMARK   3    ISOTROPIC THERMAL FACTORS : 4477   ; 10.000 ; HARMONIC
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL
REMARK   3    CHIRAL IMPROPER TORSION   : 567    ; 5.000  ; SEMIHARMONIC
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL
REMARK   3    IDEAL-DIST CONTACT TERM   : 3608   ; 4.000  ; SEMIHARMONIC
REMARK   3
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3    BOND LENGTHS                       (A) : 0.008
REMARK   3    BOND ANGLES                  (DEGREES) : 0.92
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.43
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.26
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 8QWI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-OCT-23.
REMARK 100 THE DEPOSITION ID IS D_1292134192.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-21
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : MAX IV
REMARK 200  BEAMLINE                       : BIOMAX
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL
REMARK 200  DATA SCALING SOFTWARE          : CRYSTFEL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69231
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.120
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.150
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 1116.
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 9.4200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.13
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
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: MOLECULAR REPLACEMENT
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   (%): 51.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 32-42% PEG 3350, 0.1M LI2SO4 AND 0.1M
REMARK 280  TRIS-HCL (PH 8.2), BATCH MODE, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+1/6
REMARK 290       6555   X-Y,X,Z+5/6
REMARK 290       7555   Y,X,-Z+2/3
REMARK 290       8555   X-Y,-Y,-Z
REMARK 290       9555   -X,-X+Y,-Z+1/3
REMARK 290      10555   -Y,-X,-Z+1/6
REMARK 290      11555   -X+Y,Y,-Z+1/2
REMARK 290      12555   X,X-Y,-Z+5/6
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      164.46000
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       82.23000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      123.34500
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       41.11500
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      205.57500
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      164.46000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       82.23000
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       41.11500
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      123.34500
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      205.57500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 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 350   BIOMT1   2  0.500000  0.866025  0.000000       46.97500
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      -81.36309
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -41.11500
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     GLY A     0
REMARK 465     MET A     1
REMARK 465     ASN A   548
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PHE A  20    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS A  94    CG   CD   CE   NZ
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   837     O    HOH A   896    12544     2.15
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    VAL A  13      -65.92   -123.57
REMARK 500    GLN A 204      -67.52   -104.40
REMARK 500    GLU A 269     -145.54   -115.31
REMARK 500    ASP A 335     -129.03     60.23
REMARK 500    ASN A 359      -44.93     74.74
REMARK 500    LYS A 456      -71.41    -67.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    CYS A 232        -10.42
REMARK 500
REMARK 500 REMARK: NULL
DBREF  8QWI A    1   548  UNP    P34913   HYES_HUMAN       1    548
SEQADV 8QWI GLY A    0  UNP  P34913              EXPRESSION TAG
SEQRES   1 A  549  GLY MET THR LEU ARG ALA ALA VAL PHE ASP LEU ASP GLY
SEQRES   2 A  549  VAL LEU ALA LEU PRO ALA VAL PHE GLY VAL LEU GLY ARG
SEQRES   3 A  549  THR GLU GLU ALA LEU ALA LEU PRO ARG GLY LEU LEU ASN
SEQRES   4 A  549  ASP ALA PHE GLN LYS GLY GLY PRO GLU GLY ALA THR THR
SEQRES   5 A  549  ARG LEU MET LYS GLY GLU ILE THR LEU SER GLN TRP ILE
SEQRES   6 A  549  PRO LEU MET GLU GLU ASN CYS ARG LYS CYS SER GLU THR
SEQRES   7 A  549  ALA LYS VAL CYS LEU PRO LYS ASN PHE SER ILE LYS GLU
SEQRES   8 A  549  ILE PHE ASP LYS ALA ILE SER ALA ARG LYS ILE ASN ARG
SEQRES   9 A  549  PRO MET LEU GLN ALA ALA LEU MET LEU ARG LYS LYS GLY
SEQRES  10 A  549  PHE THR THR ALA ILE LEU THR ASN THR TRP LEU ASP ASP
SEQRES  11 A  549  ARG ALA GLU ARG ASP GLY LEU ALA GLN LEU MET CYS GLU
SEQRES  12 A  549  LEU LYS MET HIS PHE ASP PHE LEU ILE GLU SER CYS GLN
SEQRES  13 A  549  VAL GLY MET VAL LYS PRO GLU PRO GLN ILE TYR LYS PHE
SEQRES  14 A  549  LEU LEU ASP THR LEU LYS ALA SER PRO SER GLU VAL VAL
SEQRES  15 A  549  PHE LEU ASP ASP ILE GLY ALA ASN LEU LYS PRO ALA ARG
SEQRES  16 A  549  ASP LEU GLY MET VAL THR ILE LEU VAL GLN ASP THR ASP
SEQRES  17 A  549  THR ALA LEU LYS GLU LEU GLU LYS VAL THR GLY ILE GLN
SEQRES  18 A  549  LEU LEU ASN THR PRO ALA PRO LEU PRO THR SER CYS ASN
SEQRES  19 A  549  PRO SER ASP MET SER HIS GLY TYR VAL THR VAL LYS PRO
SEQRES  20 A  549  ARG VAL ARG LEU HIS PHE VAL GLU LEU GLY SER GLY PRO
SEQRES  21 A  549  ALA VAL CYS LEU CYS HIS GLY PHE PRO GLU SER TRP TYR
SEQRES  22 A  549  SER TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY
SEQRES  23 A  549  TYR ARG VAL LEU ALA MET ASP MET LYS GLY TYR GLY GLU
SEQRES  24 A  549  SER SER ALA PRO PRO GLU ILE GLU GLU TYR CYS MET GLU
SEQRES  25 A  549  VAL LEU CYS LYS GLU MET VAL THR PHE LEU ASP LYS LEU
SEQRES  26 A  549  GLY LEU SER GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY
SEQRES  27 A  549  GLY MET LEU VAL TRP TYR MET ALA LEU PHE TYR PRO GLU
SEQRES  28 A  549  ARG VAL ARG ALA VAL ALA SER LEU ASN THR PRO PHE ILE
SEQRES  29 A  549  PRO ALA ASN PRO ASN MET SER PRO LEU GLU SER ILE LYS
SEQRES  30 A  549  ALA ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU
SEQRES  31 A  549  PRO GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN LEU SER
SEQRES  32 A  549  ARG THR PHE LYS SER LEU PHE ARG ALA SER ASP GLU SER
SEQRES  33 A  549  VAL LEU SER MET HIS LYS VAL CYS GLU ALA GLY GLY LEU
SEQRES  34 A  549  PHE VAL ASN SER PRO GLU GLU PRO SER LEU SER ARG MET
SEQRES  35 A  549  VAL THR GLU GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE
SEQRES  36 A  549  LYS LYS SER GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG
SEQRES  37 A  549  ASN MET GLU ARG ASN TRP LYS TRP ALA CYS LYS SER LEU
SEQRES  38 A  549  GLY ARG LYS ILE LEU ILE PRO ALA LEU MET VAL THR ALA
SEQRES  39 A  549  GLU LYS ASP PHE VAL LEU VAL PRO GLN MET SER GLN HIS
SEQRES  40 A  549  MET GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE
SEQRES  41 A  549  GLU ASP CYS GLY HIS TRP THR GLN MET ASP LYS PRO THR
SEQRES  42 A  549  GLU VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP SER ASP
SEQRES  43 A  549  ALA ARG ASN
HET    SO4  A 601       5
HET    6N4  A 602      13
HETNAM     SO4 SULFATE ION
HETNAM     6N4 2-(1H-BENZIMIDAZOL-2-YLSULFANYL)ETHANOL
FORMUL   2  SO4    O4 S 2-
FORMUL   3  6N4    C9 H10 N2 O S
FORMUL   4  HOH   *209(H2 O)
HELIX    1 AA1 ALA A   18  LEU A   30  1                                  13
HELIX    2 AA2 GLY A   35  LYS A   43  1                                   9
HELIX    3 AA3 GLY A   44  GLU A   47  5                                   4
HELIX    4 AA4 GLY A   48  LYS A   55  1                                   8
HELIX    5 AA5 THR A   59  ALA A   78  1                                  20
HELIX    6 AA6 SER A   87  ARG A   99  1                                  13
HELIX    7 AA7 ASN A  102  LYS A  115  1                                  14
HELIX    8 AA8 ARG A  133  MET A  145  1                                  13
HELIX    9 AA9 SER A  153  GLY A  157  1                                   5
HELIX   10 AB1 GLU A  162  LYS A  174  1                                  13
HELIX   11 AB2 SER A  176  SER A  178  5                                   3
HELIX   12 AB3 ILE A  186  GLY A  197  1                                  12
HELIX   13 AB4 ASP A  205  GLY A  218  1                                  14
HELIX   14 AB5 ASN A  233  MET A  237  5                                   5
HELIX   15 AB6 SER A  270  ARG A  275  5                                   6
HELIX   16 AB7 GLN A  277  ALA A  284  1                                   8
HELIX   17 AB8 GLU A  304  TYR A  308  5                                   5
HELIX   18 AB9 CYS A  309  GLY A  325  1                                  17
HELIX   19 AC1 ASP A  335  TYR A  348  1                                  14
HELIX   20 AC2 SER A  370  ASN A  378  1                                   9
HELIX   21 AC3 PRO A  379  PHE A  381  5                                   3
HELIX   22 AC4 ASP A  382  PHE A  387  1                                   6
HELIX   23 AC5 GLY A  391  ASN A  400  1                                  10
HELIX   24 AC6 ASN A  400  PHE A  409  1                                  10
HELIX   25 AC7 ALA A  411  SER A  415  5                                   5
HELIX   26 AC8 LYS A  421  GLY A  426  1                                   6
HELIX   27 AC9 THR A  443  GLY A  458  1                                  16
HELIX   28 AD1 PHE A  459  TRP A  465  1                                   7
HELIX   29 AD2 ASN A  468  CYS A  477  1                                  10
HELIX   30 AD3 LYS A  478  LEU A  480  5                                   3
HELIX   31 AD4 VAL A  500  GLN A  505  5                                   6
HELIX   32 AD5 HIS A  506  TRP A  510  5                                   5
HELIX   33 AD6 TRP A  525  LYS A  530  1                                   6
HELIX   34 AD7 LYS A  530  ALA A  546  1                                  17
SHEET    1 AA1 5 PHE A 149  GLU A 152  0
SHEET    2 AA1 5 THR A 118  THR A 123  1  N  ILE A 121   O  ILE A 151
SHEET    3 AA1 5 ALA A   5  PHE A   8  1  N  PHE A   8   O  ALA A 120
SHEET    4 AA1 5 VAL A 180  ASP A 184  1  O  LEU A 183   N  VAL A   7
SHEET    5 AA1 5 VAL A 199  LEU A 202  1  O  VAL A 199   N  PHE A 182
SHEET    1 AA2 2 ALA A  15  LEU A  16  0
SHEET    2 AA2 2 LYS A 100  ILE A 101 -1  O  LYS A 100   N  LEU A  16
SHEET    1 AA3 8 SER A 238  LYS A 245  0
SHEET    2 AA3 8 VAL A 248  LEU A 255 -1  O  PHE A 252   N  GLY A 240
SHEET    3 AA3 8 ARG A 287  MET A 291 -1  O  VAL A 288   N  LEU A 255
SHEET    4 AA3 8 ALA A 260  CYS A 264  1  N  VAL A 261   O  LEU A 289
SHEET    5 AA3 8 ALA A 329  HIS A 334  1  O  VAL A 330   N  CYS A 262
SHEET    6 AA3 8 VAL A 352  LEU A 358  1  O  ALA A 354   N  PHE A 331
SHEET    7 AA3 8 ALA A 488  ALA A 493  1  O  VAL A 491   N  SER A 357
SHEET    8 AA3 8 LYS A 515  ILE A 519  1  O  LYS A 515   N  ALA A 488
CISPEP   1 LEU A   16    PRO A   17          0        -2.11
CISPEP   2 LYS A  160    PRO A  161          0        11.76
CISPEP   3 PHE A  267    PRO A  268          0       -10.19
CRYST1   93.950   93.950  246.690  90.00  90.00 120.00 P 65 2 2     12
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      0.010644  0.006145  0.000000        0.00000
SCALE2      0.000000  0.012291  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004054        0.00000
TER    4351      ARG A 547
MASTER      325    0    2   34   15    0    0    6 4540    1   18   43
END