longtext: 4NZZ-pdb

content
HEADER    HYDROLASE                               13-DEC-13   4NZZ
TITLE     CRYSTAL STRUCTURE OF EPOXIDE HYDROLASE FROM BACILLUS MEGATERIUM
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SOLUBLE EPOXIDE HYDROLASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 3.2.2.10;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS MEGATERIUM;
SOURCE   3 ORGANISM_TAXID: 1404;
SOURCE   4 STRAIN: ECU1001;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS    A/B HYDROLASE FOLD, EPOXIDE HYDROLASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    X.D.KONG,J.H.ZHOU,J.H.XU
REVDAT   1   29-OCT-14 4NZZ    0
JRNL        AUTH   X.D.KONG,S.YUAN,L.LI,J.H.XU,J.H.XU,J.H.ZHOU
JRNL        TITL   ENGINEERING OF AN EPOXIDE HYDROLASE FOR EFFICIENT
JRNL        TITL 2 BIORESOLUTION OF BULKY PHARMACO SUBSTRATES
JRNL        REF    PROC.NATL.ACAD.SCI.USA                     2014
JRNL        REFN                   ESSN 1091-6490
REMARK   2
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_637)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.58
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8
REMARK   3   NUMBER OF REFLECTIONS             : 57830
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.188
REMARK   3   R VALUE            (WORKING SET) : 0.186
REMARK   3   FREE R VALUE                     : 0.233
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050
REMARK   3   FREE R VALUE TEST SET COUNT      : 2918
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 35.5909 -  4.8244    0.98     2914   129  0.1515 0.1896
REMARK   3     2  4.8244 -  3.8307    1.00     2804   138  0.1344 0.1597
REMARK   3     3  3.8307 -  3.3469    1.00     2775   141  0.1653 0.2180
REMARK   3     4  3.3469 -  3.0411    1.00     2738   147  0.1989 0.2257
REMARK   3     5  3.0411 -  2.8232    1.00     2747   156  0.2016 0.2471
REMARK   3     6  2.8232 -  2.6568    1.00     2715   167  0.1989 0.2529
REMARK   3     7  2.6568 -  2.5238    1.00     2682   163  0.1972 0.2285
REMARK   3     8  2.5238 -  2.4140    0.99     2727   147  0.1986 0.2654
REMARK   3     9  2.4140 -  2.3210    0.99     2692   136  0.2029 0.2512
REMARK   3    10  2.3210 -  2.2410    0.99     2705   127  0.2031 0.2710
REMARK   3    11  2.2410 -  2.1709    0.99     2661   148  0.2073 0.2539
REMARK   3    12  2.1709 -  2.1089    0.98     2666   143  0.2050 0.2873
REMARK   3    13  2.1089 -  2.0534    0.97     2655   133  0.2134 0.2603
REMARK   3    14  2.0534 -  2.0033    0.97     2618   130  0.2244 0.2777
REMARK   3    15  2.0033 -  1.9577    0.96     2567   140  0.2254 0.2642
REMARK   3    16  1.9577 -  1.9161    0.95     2587   148  0.2234 0.2407
REMARK   3    17  1.9161 -  1.8777    0.93     2488   140  0.2207 0.2753
REMARK   3    18  1.8777 -  1.8423    0.91     2470   116  0.2417 0.3132
REMARK   3    19  1.8423 -  1.8094    0.88     2388   126  0.2674 0.3855
REMARK   3    20  1.8094 -  1.7787    0.84     2201   132  0.3051 0.3716
REMARK   3    21  1.7787 -  1.7500    0.77     2112   111  0.3274 0.3874
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.30
REMARK   3   SHRINKAGE RADIUS   : 1.06
REMARK   3   K_SOL              : 0.32
REMARK   3   B_SOL              : 38.57
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.780
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) : -3.25990
REMARK   3    B22 (A**2) : 9.25800
REMARK   3    B33 (A**2) : -5.99800
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  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      :  0.007           5006
REMARK   3   ANGLE     :  0.995           6804
REMARK   3   CHIRALITY :  0.075            693
REMARK   3   PLANARITY :  0.004            901
REMARK   3   DIHEDRAL  : 14.355           1862
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 4NZZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-14.
REMARK 100 THE RCSB ID CODE IS RCSB083868.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 26-NOV-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRF
REMARK 200  BEAMLINE                       : BL17U
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59760
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.749
REMARK 200  RESOLUTION RANGE LOW       (A) : 64.333
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.5
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: SAD
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 38.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5M LICL, 0.1M TRIS-HCL, 28% PEG
REMARK 280  6000, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K,
REMARK 280  EVAPORATION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       32.11550
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.40400
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.00300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.40400
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.11550
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.00300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A   -32
REMARK 465     GLY A   -31
REMARK 465     SER A   -30
REMARK 465     SER A   -29
REMARK 465     HIS A   -28
REMARK 465     HIS A   -27
REMARK 465     HIS A   -26
REMARK 465     HIS A   -25
REMARK 465     HIS A   -24
REMARK 465     HIS A   -23
REMARK 465     SER A   -22
REMARK 465     SER A   -21
REMARK 465     GLY A   -20
REMARK 465     LEU A   -19
REMARK 465     VAL A   -18
REMARK 465     PRO A   -17
REMARK 465     ARG A   -16
REMARK 465     GLY A   -15
REMARK 465     SER A   -14
REMARK 465     HIS A   -13
REMARK 465     MET A   -12
REMARK 465     ALA A   -11
REMARK 465     SER A   -10
REMARK 465     MET A    -9
REMARK 465     THR A    -8
REMARK 465     GLY A    -7
REMARK 465     GLY A    -6
REMARK 465     GLN A    -5
REMARK 465     GLN A    -4
REMARK 465     MET A    -3
REMARK 465     GLY A    -2
REMARK 465     ARG A    -1
REMARK 465     GLY A     0
REMARK 465     MET B   -32
REMARK 465     GLY B   -31
REMARK 465     SER B   -30
REMARK 465     SER B   -29
REMARK 465     HIS B   -28
REMARK 465     HIS B   -27
REMARK 465     HIS B   -26
REMARK 465     HIS B   -25
REMARK 465     HIS B   -24
REMARK 465     HIS B   -23
REMARK 465     SER B   -22
REMARK 465     SER B   -21
REMARK 465     GLY B   -20
REMARK 465     LEU B   -19
REMARK 465     VAL B   -18
REMARK 465     PRO B   -17
REMARK 465     ARG B   -16
REMARK 465     GLY B   -15
REMARK 465     SER B   -14
REMARK 465     HIS B   -13
REMARK 465     MET B   -12
REMARK 465     ALA B   -11
REMARK 465     SER B   -10
REMARK 465     MET B    -9
REMARK 465     THR B    -8
REMARK 465     GLY B    -7
REMARK 465     GLY B    -6
REMARK 465     GLN B    -5
REMARK 465     GLN B    -4
REMARK 465     MET B    -3
REMARK 465     GLY B    -2
REMARK 465     ARG B    -1
REMARK 465     GLY B     0
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  31       43.87   -108.32
REMARK 500    ASP A  32     -158.94    -87.75
REMARK 500    ASN A  59     -117.55     45.94
REMARK 500    LYS A  63       78.16   -118.74
REMARK 500    ASP A  97     -133.50     58.65
REMARK 500    LYS A 207       68.89   -110.87
REMARK 500    SER A 266     -131.77   -107.21
REMARK 500    PRO B  31       43.91   -106.56
REMARK 500    ASP B  32     -155.70    -92.57
REMARK 500    PHE B  33     -169.22   -169.61
REMARK 500    ASN B  59     -119.41     50.06
REMARK 500    ASP B  97     -129.97     58.27
REMARK 500    LYS B 207       73.07   -111.00
REMARK 500    SER B 266     -136.41   -107.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4O08   RELATED DB: PDB
DBREF  4NZZ A    1   287  UNP    G9BEX6   G9BEX6_BACME     1    287
DBREF  4NZZ B    1   287  UNP    G9BEX6   G9BEX6_BACME     1    287
SEQADV 4NZZ MET A  -32  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ GLY A  -31  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ SER A  -30  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ SER A  -29  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ HIS A  -28  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ HIS A  -27  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ HIS A  -26  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ HIS A  -25  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ HIS A  -24  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ HIS A  -23  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ SER A  -22  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ SER A  -21  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ GLY A  -20  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ LEU A  -19  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ VAL A  -18  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ PRO A  -17  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ ARG A  -16  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ GLY A  -15  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ SER A  -14  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ HIS A  -13  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ MET A  -12  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ ALA A  -11  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ SER A  -10  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ MET A   -9  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ THR A   -8  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ GLY A   -7  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ GLY A   -6  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ GLN A   -5  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ GLN A   -4  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ MET A   -3  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ GLY A   -2  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ ARG A   -1  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ GLY A    0  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ MET B  -32  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ GLY B  -31  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ SER B  -30  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ SER B  -29  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ HIS B  -28  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ HIS B  -27  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ HIS B  -26  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ HIS B  -25  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ HIS B  -24  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ HIS B  -23  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ SER B  -22  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ SER B  -21  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ GLY B  -20  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ LEU B  -19  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ VAL B  -18  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ PRO B  -17  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ ARG B  -16  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ GLY B  -15  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ SER B  -14  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ HIS B  -13  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ MET B  -12  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ ALA B  -11  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ SER B  -10  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ MET B   -9  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ THR B   -8  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ GLY B   -7  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ GLY B   -6  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ GLN B   -5  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ GLN B   -4  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ MET B   -3  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ GLY B   -2  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ ARG B   -1  UNP  G9BEX6              EXPRESSION TAG
SEQADV 4NZZ GLY B    0  UNP  G9BEX6              EXPRESSION TAG
SEQRES   1 A  320  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 A  320  LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES   3 A  320  GLY GLN GLN MET GLY ARG GLY MET SER LYS GLN TYR ILE
SEQRES   4 A  320  ASN VAL ASN GLY VAL ASN LEU HIS TYR ILE SER LYS GLY
SEQRES   5 A  320  GLN GLY GLU LEU MET LEU PHE LEU HIS GLY PHE PRO ASP
SEQRES   6 A  320  PHE SER HIS ILE TRP ARG HIS GLN ILE ASP GLU PHE SER
SEQRES   7 A  320  ASN ASP PHE HIS THR VAL ALA LEU ASP LEU ARG GLY TYR
SEQRES   8 A  320  ASN LEU SER GLU LYS PRO SER GLY LEU GLU SER TYR GLU
SEQRES   9 A  320  ILE ASP VAL LEU VAL GLU ASP ILE ARG GLN VAL ILE GLU
SEQRES  10 A  320  GLY LEU GLY TYR SER SER CYS THR LEU VAL VAL HIS ASP
SEQRES  11 A  320  TRP GLY ALA GLY ILE GLY TRP THR PHE ALA TYR ARG TYR
SEQRES  12 A  320  PRO GLU TYR VAL GLN LYS LEU ILE ALA PHE ASN GLY PRO
SEQRES  13 A  320  HIS PRO TYR THR PHE MET ARG GLU LEU ARG THR ASN LYS
SEQRES  14 A  320  ASN GLN GLN LYS ALA SER GLU TYR MET LYS TRP PHE GLN
SEQRES  15 A  320  LYS GLN GLU VAL GLN ASP TYR MET GLU ARG ASP ASN PHE
SEQRES  16 A  320  SER GLY LEU ARG LYS LEU VAL ILE ASP PRO GLY VAL LYS
SEQRES  17 A  320  LYS GLY TYR LEU THR ALA ASP ASP VAL GLN ALA TYR MET
SEQRES  18 A  320  ASN SER TRP GLU ASN GLY SER VAL LEU SER MET LEU SER
SEQRES  19 A  320  TYR TYR ARG ASN LEU LYS ILE PHE THR GLU GLU ASP LEU
SEQRES  20 A  320  ARG ARG LYS SER LEU PHE PRO LEU GLU GLU GLU VAL LEU
SEQRES  21 A  320  ASN ILE PRO VAL GLN ILE ILE TRP GLY ASN GLN ASP PRO
SEQRES  22 A  320  THR PHE MET PRO GLU ASN LEU ASP GLY ILE GLU GLU TYR
SEQRES  23 A  320  VAL PRO ASN ILE SER VAL HIS ARG LEU ALA GLU ALA SER
SEQRES  24 A  320  HIS ALA PRO GLN HIS GLU LYS PRO GLN GLU VAL ASN ASN
SEQRES  25 A  320  VAL MET TRP ASN PHE LEU ASN LYS
SEQRES   1 B  320  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 B  320  LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES   3 B  320  GLY GLN GLN MET GLY ARG GLY MET SER LYS GLN TYR ILE
SEQRES   4 B  320  ASN VAL ASN GLY VAL ASN LEU HIS TYR ILE SER LYS GLY
SEQRES   5 B  320  GLN GLY GLU LEU MET LEU PHE LEU HIS GLY PHE PRO ASP
SEQRES   6 B  320  PHE SER HIS ILE TRP ARG HIS GLN ILE ASP GLU PHE SER
SEQRES   7 B  320  ASN ASP PHE HIS THR VAL ALA LEU ASP LEU ARG GLY TYR
SEQRES   8 B  320  ASN LEU SER GLU LYS PRO SER GLY LEU GLU SER TYR GLU
SEQRES   9 B  320  ILE ASP VAL LEU VAL GLU ASP ILE ARG GLN VAL ILE GLU
SEQRES  10 B  320  GLY LEU GLY TYR SER SER CYS THR LEU VAL VAL HIS ASP
SEQRES  11 B  320  TRP GLY ALA GLY ILE GLY TRP THR PHE ALA TYR ARG TYR
SEQRES  12 B  320  PRO GLU TYR VAL GLN LYS LEU ILE ALA PHE ASN GLY PRO
SEQRES  13 B  320  HIS PRO TYR THR PHE MET ARG GLU LEU ARG THR ASN LYS
SEQRES  14 B  320  ASN GLN GLN LYS ALA SER GLU TYR MET LYS TRP PHE GLN
SEQRES  15 B  320  LYS GLN GLU VAL GLN ASP TYR MET GLU ARG ASP ASN PHE
SEQRES  16 B  320  SER GLY LEU ARG LYS LEU VAL ILE ASP PRO GLY VAL LYS
SEQRES  17 B  320  LYS GLY TYR LEU THR ALA ASP ASP VAL GLN ALA TYR MET
SEQRES  18 B  320  ASN SER TRP GLU ASN GLY SER VAL LEU SER MET LEU SER
SEQRES  19 B  320  TYR TYR ARG ASN LEU LYS ILE PHE THR GLU GLU ASP LEU
SEQRES  20 B  320  ARG ARG LYS SER LEU PHE PRO LEU GLU GLU GLU VAL LEU
SEQRES  21 B  320  ASN ILE PRO VAL GLN ILE ILE TRP GLY ASN GLN ASP PRO
SEQRES  22 B  320  THR PHE MET PRO GLU ASN LEU ASP GLY ILE GLU GLU TYR
SEQRES  23 B  320  VAL PRO ASN ILE SER VAL HIS ARG LEU ALA GLU ALA SER
SEQRES  24 B  320  HIS ALA PRO GLN HIS GLU LYS PRO GLN GLU VAL ASN ASN
SEQRES  25 B  320  VAL MET TRP ASN PHE LEU ASN LYS
FORMUL   3  HOH   *414(H2 O)
HELIX    1   1 PHE A   33  ILE A   36  5                                   4
HELIX    2   2 TRP A   37  SER A   45  1                                   9
HELIX    3   3 GLY A   66  TYR A   70  5                                   5
HELIX    4   4 GLU A   71  LEU A   86  1                                  16
HELIX    5   5 ASP A   97  TYR A  110  1                                  14
HELIX    6   6 HIS A  124  ASN A  135  1                                  12
HELIX    7   7 ASN A  135  SER A  142  1                                   8
HELIX    8   8 SER A  142  PHE A  148  1                                   7
HELIX    9   9 GLU A  152  LYS A  176  1                                  25
HELIX   10  10 THR A  180  GLY A  194  1                                  15
HELIX   11  11 SER A  195  TYR A  202  1                                   8
HELIX   12  12 TYR A  203  LEU A  206  5                                   4
HELIX   13  13 MET A  243  ASP A  248  5                                   6
HELIX   14  14 GLY A  249  TYR A  253  5                                   5
HELIX   15  15 ALA A  268  LYS A  273  1                                   6
HELIX   16  16 LYS A  273  LYS A  287  1                                  15
HELIX   17  17 PHE B   33  ILE B   36  5                                   4
HELIX   18  18 TRP B   37  SER B   45  1                                   9
HELIX   19  19 GLY B   66  TYR B   70  5                                   5
HELIX   20  20 GLU B   71  LEU B   86  1                                  16
HELIX   21  21 ASP B   97  TYR B  110  1                                  14
HELIX   22  22 HIS B  124  ASN B  135  1                                  12
HELIX   23  23 ASN B  135  SER B  142  1                                   8
HELIX   24  24 SER B  142  PHE B  148  1                                   7
HELIX   25  25 GLN B  149  GLN B  151  5                                   3
HELIX   26  26 GLU B  152  LYS B  176  1                                  25
HELIX   27  27 THR B  180  GLY B  194  1                                  15
HELIX   28  28 SER B  195  ARG B  204  1                                  10
HELIX   29  29 THR B  210  ARG B  215  1                                   6
HELIX   30  30 MET B  243  ASP B  248  5                                   6
HELIX   31  31 GLY B  249  TYR B  253  5                                   5
HELIX   32  32 ALA B  268  LYS B  273  1                                   6
HELIX   33  33 LYS B  273  ASN B  286  1                                  14
SHEET    1   A 8 SER A   2  VAL A   8  0
SHEET    2   A 8 VAL A  11  LYS A  18 -1  O  LEU A  13   N  ILE A   6
SHEET    3   A 8 HIS A  49  LEU A  53 -1  O  ALA A  52   N  ILE A  16
SHEET    4   A 8 LEU A  23  LEU A  27  1  N  PHE A  26   O  VAL A  51
SHEET    5   A 8 CYS A  91  VAL A  95  1  O  THR A  92   N  LEU A  23
SHEET    6   A 8 VAL A 114  ALA A 119  1  O  ILE A 118   N  LEU A  93
SHEET    7   A 8 VAL A 231  GLY A 236  1  O  GLN A 232   N  LEU A 117
SHEET    8   A 8 ILE A 257  LEU A 262  1  O  LEU A 262   N  TRP A 235
SHEET    1   B 8 SER B   2  VAL B   8  0
SHEET    2   B 8 VAL B  11  LYS B  18 -1  O  LEU B  13   N  ILE B   6
SHEET    3   B 8 HIS B  49  LEU B  53 -1  O  ALA B  52   N  ILE B  16
SHEET    4   B 8 LEU B  23  LEU B  27  1  N  MET B  24   O  VAL B  51
SHEET    5   B 8 CYS B  91  VAL B  95  1  O  THR B  92   N  LEU B  23
SHEET    6   B 8 VAL B 114  ALA B 119  1  O  ILE B 118   N  LEU B  93
SHEET    7   B 8 VAL B 231  GLY B 236  1  O  ILE B 234   N  ALA B 119
SHEET    8   B 8 ILE B 257  LEU B 262  1  O  LEU B 262   N  TRP B 235
CISPEP   1 PHE A   30    PRO A   31          0        -3.42
CISPEP   2 PHE B   30    PRO B   31          0        -2.88
CRYST1   64.231   76.006  120.808  90.00  90.00  90.00 P 21 21 21    8
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.015569  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013157  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008278        0.00000
TER    2433      LYS A 287
TER    4852      LYS B 287
MASTER      327    0    0   33   16    0    0    6 5162    2    0   50
END