longtext: 7wam-pdb

content
HEADER    HYDROLASE                               14-DEC-21   7WAM
TITLE     CRYSTAL STRUCTURE OF HALOTAG COMPLEXED WITH VL1
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.8.1.5;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: 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 BL21(DE3);
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS    HALOTAG, HALOALKANE DEHALOGENASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.PRATYUSH,M.KANG,H.LEE,C.LEE,H.RHEE
REVDAT   1   02-FEB-22 7WAM    0
JRNL        AUTH   P.K.MISHRA,M.G.KANG,H.LEE,S.KIM,S.CHOI,N.SHARMA,C.M.PARK,
JRNL        AUTH 2 J.KO,C.LEE,J.K.SEO,H.W.RHEE
JRNL        TITL   A CHEMICAL TOOL FOR BLUE LIGHT-INDUCIBLE PROXIMITY
JRNL        TITL 2 PHOTO-CROSSLINKING IN LIVE CELLS
JRNL        REF    CHEM SCI                                   2022
JRNL        REFN                   ESSN 2041-6539
JRNL        DOI    10.1039/D1SC04871F
REMARK   2
REMARK   2 RESOLUTION.    1.49 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX 1.9_1692
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 : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.80
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8
REMARK   3   NUMBER OF REFLECTIONS             : 54433
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.150
REMARK   3   R VALUE            (WORKING SET) : 0.149
REMARK   3   FREE R VALUE                     : 0.188
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.670
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000
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 27.8020 -  3.5886    0.98     4023   154  0.1453 0.1724
REMARK   3     2  3.5886 -  2.8493    1.00     3876   148  0.1529 0.1714
REMARK   3     3  2.8493 -  2.4894    0.99     3820   145  0.1573 0.1930
REMARK   3     4  2.4894 -  2.2619    1.00     3789   144  0.1465 0.2000
REMARK   3     5  2.2619 -  2.0998    0.99     3767   144  0.1417 0.2078
REMARK   3     6  2.0998 -  1.9761    0.99     3735   142  0.1372 0.1719
REMARK   3     7  1.9761 -  1.8771    0.99     3744   144  0.1379 0.1849
REMARK   3     8  1.8771 -  1.7954    0.99     3693   140  0.1403 0.1681
REMARK   3     9  1.7954 -  1.7263    0.99     3720   142  0.1414 0.1984
REMARK   3    10  1.7263 -  1.6668    0.99     3680   141  0.1417 0.1953
REMARK   3    11  1.6668 -  1.6147    0.98     3653   139  0.1498 0.2007
REMARK   3    12  1.6147 -  1.5685    0.98     3644   139  0.1553 0.2093
REMARK   3    13  1.5685 -  1.5272    0.98     3687   140  0.1798 0.2576
REMARK   3    14  1.5272 -  1.4900    0.97     3602   138  0.2037 0.2818
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)     : 0.140
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.250
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.60
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      :  0.013           2470
REMARK   3   ANGLE     :  1.493           3374
REMARK   3   CHIRALITY :  0.062            354
REMARK   3   PLANARITY :  0.008            439
REMARK   3   DIHEDRAL  : 13.192            901
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 7WAM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JAN-22.
REMARK 100 THE DEPOSITION ID IS D_1300025913.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 02-APR-16
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               : PAL/PLS
REMARK 200  BEAMLINE                       : 7A (6B, 6C1)
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97960
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54493
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.490
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     (%) : 98.7
REMARK 200  DATA REDUNDANCY                : 4.700
REMARK 200  R MERGE                    (I) : 0.07000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 29.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.52
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.79900
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: PHENIX
REMARK 200 STARTING MODEL: 5Y2X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 49.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M AMMONIUM SULFATE, 0.1 M CITRIC
REMARK 280  ACID PH 5.3, AND 1% MPD, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-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       82.05600
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       31.53900
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       31.53900
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      123.08400
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       31.53900
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       31.53900
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       41.02800
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       31.53900
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       31.53900
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      123.08400
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       31.53900
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       31.53900
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       41.02800
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       82.05600
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: 130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 703  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     SER A    -1
REMARK 465     GLY A     0
REMARK 465     SER A     1
REMARK 465     ALA A     2
REMARK 465     GLU A     3
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   OD1  ASP A   106     C32  8MH A   301              1.40
REMARK 500   O    HOH A   422     O    HOH A   540              1.77
REMARK 500   O    HOH A   656     O    HOH A   714              2.07
REMARK 500   OE2  GLU A   191     O    HOH A   401              2.12
REMARK 500   O    HOH A   524     O    HOH A   711              2.13
REMARK 500   NE   ARG A    86     O    HOH A   402              2.16
REMARK 500   O    HOH A   750     O    HOH A   754              2.18
REMARK 500   O    HOH A   532     O    HOH A   653              2.18
REMARK 500   NH2  ARG A    86     O    HOH A   403              2.19
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   426     O    HOH A   690     3544     1.91
REMARK 500   O    HOH A   601     O    HOH A   653     7645     2.11
REMARK 500   O    HOH A   401     O    HOH A   548     7645     2.13
REMARK 500   O    HOH A   401     O    HOH A   605     7645     2.14
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   9       52.89    -91.90
REMARK 500    PRO A  42       45.90   -109.22
REMARK 500    THR A  43     -162.81   -100.09
REMARK 500    GLU A  98      -93.06   -108.16
REMARK 500    ASP A 106     -128.63     52.85
REMARK 500    ARG A 153       43.25    -89.33
REMARK 500    VAL A 245      -67.46   -132.55
REMARK 500    LEU A 271      -99.79   -118.38
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 753        DISTANCE =  5.93 ANGSTROMS
REMARK 525    HOH A 754        DISTANCE =  5.98 ANGSTROMS
REMARK 525    HOH A 755        DISTANCE =  6.39 ANGSTROMS
DBREF  7WAM A    2   293  UNP    P0A3G3   DHAA_RHOSO       2    293
SEQADV 7WAM SER A   -1  UNP  P0A3G3              EXPRESSION TAG
SEQADV 7WAM GLY A    0  UNP  P0A3G3              EXPRESSION TAG
SEQADV 7WAM SER A    1  UNP  P0A3G3              EXPRESSION TAG
SEQADV 7WAM ALA A    2  UNP  P0A3G3    SER     2 ENGINEERED MUTATION
SEQADV 7WAM VAL A   47  UNP  P0A3G3    LEU    47 ENGINEERED MUTATION
SEQADV 7WAM THR A   58  UNP  P0A3G3    SER    58 ENGINEERED MUTATION
SEQADV 7WAM GLY A   78  UNP  P0A3G3    ASP    78 ENGINEERED MUTATION
SEQADV 7WAM PHE A   87  UNP  P0A3G3    TYR    87 ENGINEERED MUTATION
SEQADV 7WAM MET A   88  UNP  P0A3G3    LEU    88 ENGINEERED MUTATION
SEQADV 7WAM PHE A  128  UNP  P0A3G3    CYS   128 ENGINEERED MUTATION
SEQADV 7WAM THR A  155  UNP  P0A3G3    ALA   155 ENGINEERED MUTATION
SEQADV 7WAM LYS A  160  UNP  P0A3G3    GLU   160 ENGINEERED MUTATION
SEQADV 7WAM VAL A  167  UNP  P0A3G3    ALA   167 ENGINEERED MUTATION
SEQADV 7WAM THR A  172  UNP  P0A3G3    ALA   172 ENGINEERED MUTATION
SEQADV 7WAM CYS A  175  UNP  P0A3G3    LYS   175 ENGINEERED MUTATION
SEQADV 7WAM GLY A  176  UNP  P0A3G3    CYS   176 ENGINEERED MUTATION
SEQADV 7WAM ASN A  195  UNP  P0A3G3    LYS   195 ENGINEERED MUTATION
SEQADV 7WAM GLU A  224  UNP  P0A3G3    ALA   224 ENGINEERED MUTATION
SEQADV 7WAM ASP A  227  UNP  P0A3G3    ASN   227 ENGINEERED MUTATION
SEQADV 7WAM LYS A  257  UNP  P0A3G3    GLU   257 ENGINEERED MUTATION
SEQADV 7WAM ALA A  264  UNP  P0A3G3    THR   264 ENGINEERED MUTATION
SEQADV 7WAM ASN A  272  UNP  P0A3G3    HIS   272 ENGINEERED MUTATION
SEQADV 7WAM LEU A  273  UNP  P0A3G3    TYR   273 ENGINEERED MUTATION
SEQADV 7WAM SER A  291  UNP  P0A3G3    PRO   291 ENGINEERED MUTATION
SEQADV 7WAM THR A  292  UNP  P0A3G3    ALA   292 ENGINEERED MUTATION
SEQADV 7WAM GLU A  294  UNP  P0A3G3              EXPRESSION TAG
SEQADV 7WAM ILE A  295  UNP  P0A3G3              EXPRESSION TAG
SEQADV 7WAM SER A  296  UNP  P0A3G3              EXPRESSION TAG
SEQADV 7WAM GLY A  297  UNP  P0A3G3              EXPRESSION TAG
SEQRES   1 A  299  SER GLY SER ALA GLU ILE GLY THR GLY PHE PRO PHE ASP
SEQRES   2 A  299  PRO HIS TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR
SEQRES   3 A  299  VAL ASP VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE
SEQRES   4 A  299  LEU HIS GLY ASN PRO THR SER SER TYR VAL TRP ARG ASN
SEQRES   5 A  299  ILE ILE PRO HIS VAL ALA PRO THR HIS ARG CYS ILE ALA
SEQRES   6 A  299  PRO ASP LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP
SEQRES   7 A  299  LEU GLY TYR PHE PHE ASP ASP HIS VAL ARG PHE MET ASP
SEQRES   8 A  299  ALA PHE ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU
SEQRES   9 A  299  VAL ILE HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP
SEQRES  10 A  299  ALA LYS ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE
SEQRES  11 A  299  MET GLU PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP
SEQRES  12 A  299  PRO GLU PHE ALA ARG GLU THR PHE GLN ALA PHE ARG THR
SEQRES  13 A  299  THR ASP VAL GLY ARG LYS LEU ILE ILE ASP GLN ASN VAL
SEQRES  14 A  299  PHE ILE GLU GLY THR LEU PRO CYS GLY VAL VAL ARG PRO
SEQRES  15 A  299  LEU THR GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE
SEQRES  16 A  299  LEU ASN PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO
SEQRES  17 A  299  ASN GLU LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL
SEQRES  18 A  299  ALA LEU VAL GLU GLU TYR MET ASP TRP LEU HIS GLN SER
SEQRES  19 A  299  PRO VAL PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL
SEQRES  20 A  299  LEU ILE PRO PRO ALA GLU ALA ALA ARG LEU ALA LYS SER
SEQRES  21 A  299  LEU PRO ASN CYS LYS ALA VAL ASP ILE GLY PRO GLY LEU
SEQRES  22 A  299  ASN LEU LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER
SEQRES  23 A  299  GLU ILE ALA ARG TRP LEU SER THR LEU GLU ILE SER GLY
HET    8MH  A 301      35
HET     CL  A 302       1
HETNAM     8MH 3-[6-(2-AZANYLHYDRAZINYL)-1,3-BIS(OXIDANYLIDENE)
HETNAM   2 8MH  BENZO[DE]ISOQUINOLIN-2-YL]-N-[2-(2-HEXOXYETHOXY)
HETNAM   3 8MH  ETHYL]PROPANAMIDE
HETNAM      CL CHLORIDE ION
FORMUL   2  8MH    C25 H35 N5 O5
FORMUL   3   CL    CL 1-
FORMUL   4  HOH   *355(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 THR A  155  ILE A  163  1                                   9
HELIX    8 AA8 ASN A  166  GLY A  171  1                                   6
HELIX    9 AA9 LEU A  173  VAL A  177  5                                   5
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  LEU A  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  ILE A 267   N  TRP A 240
CISPEP   1 ASN A   41    PRO A   42          0         3.49
CISPEP   2 GLU A  214    PRO A  215          0       -10.01
CISPEP   3 THR A  242    PRO A  243          0         5.58
CRYST1   63.078   63.078  164.112  90.00  90.00  90.00 P 43 21 2     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      0.015853  0.000000  0.000000        0.00000
SCALE2      0.000000  0.015853  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006093        0.00000
TER    2354      GLY A 297
MASTER      322    0    2   17    8    0    0    6 2744    1   35   23
END