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PDBsum entry 3e28

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
3e28
Jmol
Contents
Protein chains
215 a.a.
204 a.a.
Ligands
SO4 ×16
Metals
_ZN ×6
Waters ×172
HEADER    LYASE                                   05-AUG-08   3E28
TITLE     H. INFLUENZAE BETA-CARBONIC ANHYDRASE, VARIANT Y181F
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A, B, C, D, E, F;
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE 2;
COMPND   5 EC: 4.2.1.1;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;
SOURCE   3 ORGANISM_TAXID: 727;
SOURCE   4 GENE: CAN, HI1301;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTRC99
KEYWDS    BETA CARBONIC ANHYDRASE, ALLOSTERIC SITE MUTANT, LYASE, METAL-BINDING
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.S.ROWLETT,J.LEE
REVDAT   3   13-JUL-11 3E28    1       VERSN
REVDAT   2   28-JUL-09 3E28    1       JRNL
REVDAT   1   02-JUN-09 3E28    0
JRNL        AUTH   R.S.ROWLETT,C.TU,J.LEE,A.G.HERMAN,D.A.CHAPNICK,S.H.SHAH,
JRNL        AUTH 2 P.C.GAREISS
JRNL        TITL   ALLOSTERIC SITE VARIANTS OF HAEMOPHILUS INFLUENZAE
JRNL        TITL 2 BETA-CARBONIC ANHYDRASE.
JRNL        REF    BIOCHEMISTRY                  V.  48  6146 2009
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   19459702
JRNL        DOI    10.1021/BI900663H
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.84
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5
REMARK   3   NUMBER OF REFLECTIONS             : 59233
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) : 0.208
REMARK   3   R VALUE            (WORKING SET) : 0.206
REMARK   3   FREE R VALUE                     : 0.256
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2984
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4091
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.43
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2540
REMARK   3   BIN FREE R VALUE SET COUNT          : 248
REMARK   3   BIN FREE R VALUE                    : 0.3370
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 9874
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 86
REMARK   3   SOLVENT ATOMS            : 172
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.54
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.06000
REMARK   3    B22 (A**2) : -0.11000
REMARK   3    B33 (A**2) : 0.15000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.10000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.426
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.278
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.210
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.523
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10254 ; 0.012 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  6768 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13884 ; 1.311 ; 1.932
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 16457 ; 0.882 ; 3.001
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1232 ; 6.672 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   494 ;39.190 ;24.130
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1770 ;17.799 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;20.628 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1531 ; 0.072 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11275 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  2090 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2458 ; 0.223 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  6985 ; 0.195 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4980 ; 0.181 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  5277 ; 0.089 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   340 ; 0.165 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):     2 ; 0.167 ; 0.200
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    40 ; 0.182 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):   130 ; 0.218 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.261 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  7973 ; 0.647 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2528 ; 0.093 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9878 ; 0.773 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4805 ; 1.331 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4006 ; 1.941 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 6
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     1        A   221
REMARK   3    ORIGIN FOR THE GROUP (A):   7.7550  51.1520  28.1140
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1239 T22:  -0.0827
REMARK   3      T33:   0.0290 T12:   0.0722
REMARK   3      T13:  -0.0110 T23:  -0.0380
REMARK   3    L TENSOR
REMARK   3      L11:   2.1388 L22:   0.8771
REMARK   3      L33:   1.4603 L12:  -0.0747
REMARK   3      L13:   1.1413 L23:  -0.0747
REMARK   3    S TENSOR
REMARK   3      S11:   0.2323 S12:   0.1688 S13:  -0.5644
REMARK   3      S21:   0.0721 S22:  -0.0138 S23:  -0.1186
REMARK   3      S31:   0.2306 S32:   0.1632 S33:  -0.2185
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     1        B   221
REMARK   3    ORIGIN FOR THE GROUP (A):   7.2370  85.3630  23.0240
REMARK   3    T TENSOR
REMARK   3      T11:   0.0786 T22:  -0.0886
REMARK   3      T33:  -0.0982 T12:  -0.1377
REMARK   3      T13:  -0.0094 T23:   0.0676
REMARK   3    L TENSOR
REMARK   3      L11:   2.8830 L22:   1.7033
REMARK   3      L33:   3.1166 L12:  -0.1341
REMARK   3      L13:   0.6008 L23:  -0.4438
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2341 S12:   0.2402 S13:   0.5387
REMARK   3      S21:   0.0202 S22:  -0.0017 S23:  -0.1964
REMARK   3      S31:  -0.8682 S32:   0.3770 S33:   0.2358
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C     1        C   219
REMARK   3    ORIGIN FOR THE GROUP (A):  46.1570 121.5840   4.3420
REMARK   3    T TENSOR
REMARK   3      T11:   0.0021 T22:   0.0456
REMARK   3      T33:  -0.1778 T12:   0.1063
REMARK   3      T13:   0.0819 T23:   0.0442
REMARK   3    L TENSOR
REMARK   3      L11:   2.2183 L22:   2.6710
REMARK   3      L33:   2.3331 L12:  -0.4059
REMARK   3      L13:   0.5505 L23:  -0.7775
REMARK   3    S TENSOR
REMARK   3      S11:   0.0262 S12:  -0.0824 S13:   0.2503
REMARK   3      S21:  -0.0173 S22:   0.0405 S23:   0.3640
REMARK   3      S31:  -0.4889 S32:  -0.5866 S33:  -0.0667
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D     1        D   214
REMARK   3    ORIGIN FOR THE GROUP (A):  77.1680 106.4300   8.1710
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1419 T22:  -0.1033
REMARK   3      T33:  -0.1091 T12:  -0.0557
REMARK   3      T13:   0.0601 T23:   0.0160
REMARK   3    L TENSOR
REMARK   3      L11:   2.1810 L22:   1.9924
REMARK   3      L33:   1.5830 L12:  -0.0179
REMARK   3      L13:   0.3551 L23:   0.1913
REMARK   3    S TENSOR
REMARK   3      S11:   0.0013 S12:   0.0492 S13:  -0.0762
REMARK   3      S21:  -0.0426 S22:   0.0249 S23:  -0.4973
REMARK   3      S31:   0.1019 S32:   0.2340 S33:  -0.0262
REMARK   3
REMARK   3   TLS GROUP : 5
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   E     1        E   220
REMARK   3    ORIGIN FOR THE GROUP (A):  38.8650 105.6030  10.7330
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1316 T22:   0.2314
REMARK   3      T33:  -0.1147 T12:  -0.0314
REMARK   3      T13:   0.0801 T23:   0.0940
REMARK   3    L TENSOR
REMARK   3      L11:   2.3541 L22:   2.2644
REMARK   3      L33:   2.5963 L12:   0.0762
REMARK   3      L13:  -0.1762 L23:  -0.6534
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0005 S12:  -0.0662 S13:   0.0268
REMARK   3      S21:   0.0332 S22:   0.2269 S23:   0.4864
REMARK   3      S31:  -0.0958 S32:  -0.8608 S33:  -0.2264
REMARK   3
REMARK   3   TLS GROUP : 6
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   F     1        F   217
REMARK   3    ORIGIN FOR THE GROUP (A):  69.4060  90.8140   3.6670
REMARK   3    T TENSOR
REMARK   3      T11:   0.0404 T22:  -0.1211
REMARK   3      T33:  -0.1258 T12:  -0.0351
REMARK   3      T13:   0.0419 T23:   0.0002
REMARK   3    L TENSOR
REMARK   3      L11:   1.4024 L22:   2.2240
REMARK   3      L33:   1.0982 L12:   0.0429
REMARK   3      L13:   0.2419 L23:   0.6129
REMARK   3    S TENSOR
REMARK   3      S11:   0.0751 S12:   0.1012 S13:  -0.2755
REMARK   3      S21:  -0.0941 S22:   0.0030 S23:  -0.3745
REMARK   3      S31:   0.3214 S32:   0.0849 S33:  -0.0781
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3E28 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-AUG-08.
REMARK 100 THE RCSB ID CODE IS RCSB048782.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 03-FEB-03
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NI FILTER
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59536
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.841
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 4.000
REMARK 200  R MERGE                    (I) : 0.09000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 19.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.52000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: PDB ENTRY 2A8D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 55.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 1.5 M AMMONIUM SULFATE,
REMARK 280  4% PEG-400, 20 MG/ML PROTEIN, PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280  DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
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        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      115.09650
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.47150
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      115.09650
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       72.47150
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, 3, 4, 5
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 17730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -256.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350   BIOMT1   2 -1.000000  0.000000  0.000000       -3.47520
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       52.59932
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 18010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -255.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, F
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 O4   SO4 A 233  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     PHE A    26
REMARK 465     LYS A    27
REMARK 465     GLU A    28
REMARK 465     LEU A    29
REMARK 465     ALA A    30
REMARK 465     ASP A    31
REMARK 465     LYS A   222
REMARK 465     LYS A   223
REMARK 465     ASP A   224
REMARK 465     HIS A   225
REMARK 465     LEU A   226
REMARK 465     GLU A   227
REMARK 465     ASN A   228
REMARK 465     THR A   229
REMARK 465     LYS B    19
REMARK 465     GLU B    20
REMARK 465     GLU B    21
REMARK 465     ASN B    22
REMARK 465     SER B    23
REMARK 465     THR B    24
REMARK 465     TYR B    25
REMARK 465     PHE B    26
REMARK 465     LYS B    27
REMARK 465     GLU B    28
REMARK 465     LEU B    29
REMARK 465     ALA B    30
REMARK 465     ASP B    31
REMARK 465     HIS B    32
REMARK 465     GLN B    33
REMARK 465     LYS B   222
REMARK 465     LYS B   223
REMARK 465     ASP B   224
REMARK 465     HIS B   225
REMARK 465     LEU B   226
REMARK 465     GLU B   227
REMARK 465     ASN B   228
REMARK 465     THR B   229
REMARK 465     LYS C    19
REMARK 465     GLU C    20
REMARK 465     GLU C    21
REMARK 465     ASN C    22
REMARK 465     SER C    23
REMARK 465     THR C    24
REMARK 465     TYR C    25
REMARK 465     PHE C    26
REMARK 465     LYS C    27
REMARK 465     GLU C    28
REMARK 465     LEU C    29
REMARK 465     ALA C    30
REMARK 465     ASP C    31
REMARK 465     HIS C    32
REMARK 465     GLN C    33
REMARK 465     ILE C   220
REMARK 465     LEU C   221
REMARK 465     LYS C   222
REMARK 465     LYS C   223
REMARK 465     ASP C   224
REMARK 465     HIS C   225
REMARK 465     LEU C   226
REMARK 465     GLU C   227
REMARK 465     ASN C   228
REMARK 465     THR C   229
REMARK 465     LYS D    19
REMARK 465     GLU D    20
REMARK 465     GLU D    21
REMARK 465     ASN D    22
REMARK 465     SER D    23
REMARK 465     THR D    24
REMARK 465     TYR D    25
REMARK 465     PHE D    26
REMARK 465     LYS D    27
REMARK 465     GLU D    28
REMARK 465     LEU D    29
REMARK 465     ALA D    30
REMARK 465     ASP D    31
REMARK 465     LEU D   215
REMARK 465     ASP D   216
REMARK 465     GLU D   217
REMARK 465     GLU D   218
REMARK 465     ASN D   219
REMARK 465     ILE D   220
REMARK 465     LEU D   221
REMARK 465     LYS D   222
REMARK 465     LYS D   223
REMARK 465     ASP D   224
REMARK 465     HIS D   225
REMARK 465     LEU D   226
REMARK 465     GLU D   227
REMARK 465     ASN D   228
REMARK 465     THR D   229
REMARK 465     GLN E    16
REMARK 465     ARG E    17
REMARK 465     MET E    18
REMARK 465     LYS E    19
REMARK 465     GLU E    20
REMARK 465     GLU E    21
REMARK 465     ASN E    22
REMARK 465     SER E    23
REMARK 465     THR E    24
REMARK 465     TYR E    25
REMARK 465     PHE E    26
REMARK 465     LYS E    27
REMARK 465     GLU E    28
REMARK 465     LEU E    29
REMARK 465     ALA E    30
REMARK 465     ASP E    31
REMARK 465     HIS E    32
REMARK 465     GLN E    33
REMARK 465     LEU E   221
REMARK 465     LYS E   222
REMARK 465     LYS E   223
REMARK 465     ASP E   224
REMARK 465     HIS E   225
REMARK 465     LEU E   226
REMARK 465     GLU E   227
REMARK 465     ASN E   228
REMARK 465     THR E   229
REMARK 465     LYS F    19
REMARK 465     GLU F    20
REMARK 465     GLU F    21
REMARK 465     ASN F    22
REMARK 465     SER F    23
REMARK 465     THR F    24
REMARK 465     TYR F    25
REMARK 465     PHE F    26
REMARK 465     LYS F    27
REMARK 465     GLU F    28
REMARK 465     LEU F    29
REMARK 465     ALA F    30
REMARK 465     ASP F    31
REMARK 465     GLU F   218
REMARK 465     ASN F   219
REMARK 465     ILE F   220
REMARK 465     LEU F   221
REMARK 465     LYS F   222
REMARK 465     LYS F   223
REMARK 465     ASP F   224
REMARK 465     HIS F   225
REMARK 465     LEU F   226
REMARK 465     GLU F   227
REMARK 465     ASN F   228
REMARK 465     THR F   229
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   ND1  HIS F    98     O3   SO4 F   232              2.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    CYS D  42   CB    CYS D  42   SG     -0.098
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASP B  44   CB  -  CA  -  C   ANGL. DEV. = -12.4 DEGREES
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    ASP A   2      129.98    -33.05
REMARK 500    ASN A  22     -133.68   -154.27
REMARK 500    ASN A  54       56.01     39.95
REMARK 500    VAL A  87      -61.88   -104.35
REMARK 500    ARG B  17       64.78    -61.87
REMARK 500    LEU C 174      115.72   -161.00
REMARK 500    ASP C 185        5.34   -155.20
REMARK 500    GLN D  33      127.25   -177.49
REMARK 500    SER E  13      -71.39    -63.34
REMARK 500    ASN E  54       25.91     43.28
REMARK 500    ASN E 100       56.18     38.56
REMARK 500    LYS E 111      116.08    165.12
REMARK 500    LYS E 136      -33.13    153.82
REMARK 500    GLU E 140      -36.07    -34.13
REMARK 500    ARG F  46       39.22   -149.79
REMARK 500    ASN F  68       66.20     37.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 MET A    1     ASP A    2                  -99.29
REMARK 500 ILE A  220     LEU A  221                  144.84
REMARK 500 MET F    1     ASP F    2                  148.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    ASP A   2        22.9      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
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                              ZN A 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A  42   SG
REMARK 620 2 ASP A  44   OD1  86.1
REMARK 620 3 HIS A  98   NE2 102.9  92.4
REMARK 620 4 CYS A 101   SG  118.0 133.7 116.6
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B  42   SG
REMARK 620 2 ASP B  44   OD2 107.6
REMARK 620 3 HIS B  98   NE2 111.2 128.1
REMARK 620 4 CYS B 101   SG  111.3  87.2 108.6
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN C 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C  42   SG
REMARK 620 2 ASP C  44   OD2  92.0
REMARK 620 3 HIS C  98   NE2 101.3 142.1
REMARK 620 4 CYS C 101   SG  108.4  90.3 117.9
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN D 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D  42   SG
REMARK 620 2 ASP D  44   OD2 109.9
REMARK 620 3 HIS D  98   NE2 113.7 100.3
REMARK 620 4 CYS D 101   SG  112.3 116.5 103.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN E 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E  42   SG
REMARK 620 2 ASP E  44   OD2  97.1
REMARK 620 3 HIS E  98   NE2 100.7  94.7
REMARK 620 4 CYS E 101   SG  113.7 129.1 116.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN F 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F  42   SG
REMARK 620 2 ASP F  44   OD2  96.7
REMARK 620 3 HIS F  98   NE2 109.7  88.9
REMARK 620 4 CYS F 101   SG  115.8 124.9 116.6
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 233
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 234
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 233
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 233
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 232
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2A8C   RELATED DB: PDB
REMARK 900 RELATED ID: 2A8D   RELATED DB: PDB
REMARK 900 RELATED ID: 3E24   RELATED DB: PDB
REMARK 900 RELATED ID: 3E2A   RELATED DB: PDB
REMARK 900 RELATED ID: 3E2W   RELATED DB: PDB
REMARK 900 RELATED ID: 3E2X   RELATED DB: PDB
REMARK 900 RELATED ID: 3E31   RELATED DB: PDB
DBREF  3E28 A    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E28 B    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E28 C    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E28 D    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E28 E    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E28 F    1   229  UNP    P45148   CAN_HAEIN        1    229
SEQADV 3E28 PHE A  181  UNP  P45148    TYR   181 ENGINEERED
SEQADV 3E28 PHE B  181  UNP  P45148    TYR   181 ENGINEERED
SEQADV 3E28 PHE C  181  UNP  P45148    TYR   181 ENGINEERED
SEQADV 3E28 PHE D  181  UNP  P45148    TYR   181 ENGINEERED
SEQADV 3E28 PHE E  181  UNP  P45148    TYR   181 ENGINEERED
SEQADV 3E28 PHE F  181  UNP  P45148    TYR   181 ENGINEERED
SEQRES   1 A  229  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 A  229  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 A  229  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 A  229  ILE GLY CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 A  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 A  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 A  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 A  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 A  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 A  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 A  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 A  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 A  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 A  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL PHE ASP
SEQRES  15 A  229  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 A  229  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 A  229  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES  18 A  229  LYS LYS ASP HIS LEU GLU ASN THR
SEQRES   1 B  229  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 B  229  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 B  229  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 B  229  ILE GLY CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 B  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 B  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 B  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 B  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 B  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 B  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 B  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 B  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 B  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 B  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL PHE ASP
SEQRES  15 B  229  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 B  229  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 B  229  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES  18 B  229  LYS LYS ASP HIS LEU GLU ASN THR
SEQRES   1 C  229  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 C  229  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 C  229  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 C  229  ILE GLY CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 C  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 C  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 C  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 C  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 C  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 C  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 C  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 C  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 C  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 C  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL PHE ASP
SEQRES  15 C  229  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 C  229  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 C  229  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES  18 C  229  LYS LYS ASP HIS LEU GLU ASN THR
SEQRES   1 D  229  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 D  229  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 D  229  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 D  229  ILE GLY CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 D  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 D  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 D  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 D  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 D  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 D  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 D  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 D  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 D  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 D  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL PHE ASP
SEQRES  15 D  229  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 D  229  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 D  229  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES  18 D  229  LYS LYS ASP HIS LEU GLU ASN THR
SEQRES   1 E  229  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 E  229  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 E  229  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 E  229  ILE GLY CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 E  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 E  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 E  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 E  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 E  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 E  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 E  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 E  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 E  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 E  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL PHE ASP
SEQRES  15 E  229  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 E  229  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 E  229  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES  18 E  229  LYS LYS ASP HIS LEU GLU ASN THR
SEQRES   1 F  229  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 F  229  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 F  229  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 F  229  ILE GLY CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 F  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 F  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 F  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 F  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 F  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 F  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 F  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 F  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 F  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 F  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL PHE ASP
SEQRES  15 F  229  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 F  229  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 F  229  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES  18 F  229  LYS LYS ASP HIS LEU GLU ASN THR
HET     ZN  A 230       1
HET    SO4  A 231       5
HET    SO4  A 232       5
HET    SO4  A 233       5
HET    SO4  A 234       5
HET     ZN  B 230       1
HET    SO4  B 231       5
HET    SO4  B 232       5
HET     ZN  C 230       1
HET    SO4  C 231       5
HET    SO4  C 232       5
HET    SO4  C 233       5
HET     ZN  D 230       1
HET    SO4  D 231       5
HET    SO4  D 232       5
HET     ZN  E 230       1
HET    SO4  E 231       5
HET    SO4  E 232       5
HET    SO4  E 233       5
HET     ZN  F 230       1
HET    SO4  F 231       5
HET    SO4  F 232       5
HETNAM      ZN ZINC ION
HETNAM     SO4 SULFATE ION
FORMUL   7   ZN    6(ZN 2+)
FORMUL   8  SO4    16(O4 S 2-)
FORMUL  29  HOH   *172(H2 O)
HELIX    1   1 ASP A    2  ASN A   22  1                                  21
HELIX    2   2 PRO A   48  THR A   53  1                                   6
HELIX    3   3 ASP A   74  VAL A   87  1                                  14
HELIX    4   4 CYS A  101  ALA A  109  1                                   9
HELIX    5   5 GLY A  114  HIS A  130  1                                  17
HELIX    6   6 HIS A  130  LYS A  136  1                                   7
HELIX    7   7 LEU A  137  GLU A  140  5                                   4
HELIX    8   8 LYS A  141  THR A  161  1                                  21
HELIX    9   9 THR A  161  ARG A  170  1                                  10
HELIX   10  10 SER A  197  SER A  213  1                                  17
HELIX   11  11 ASP A  216  ILE A  220  5                                   5
HELIX   12  12 MET B    1  ARG B   17  1                                  17
HELIX   13  13 PRO B   48  THR B   53  1                                   6
HELIX   14  14 ASP B   74  VAL B   87  1                                  14
HELIX   15  15 CYS B  101  ALA B  109  1                                   9
HELIX   16  16 GLY B  114  HIS B  130  1                                  17
HELIX   17  17 HIS B  130  LYS B  136  1                                   7
HELIX   18  18 LEU B  137  GLU B  140  5                                   4
HELIX   19  19 LYS B  141  ARG B  160  1                                  20
HELIX   20  20 THR B  161  ARG B  170  1                                  10
HELIX   21  21 SER B  197  ILE B  214  1                                  18
HELIX   22  22 MET C    1  MET C   18  1                                  18
HELIX   23  23 PRO C   48  ASN C   54  1                                   7
HELIX   24  24 ASP C   74  VAL C   87  1                                  14
HELIX   25  25 CYS C  101  ALA C  109  1                                   9
HELIX   26  26 GLY C  114  HIS C  130  1                                  17
HELIX   27  27 HIS C  130  LEU C  137  1                                   8
HELIX   28  28 SER C  138  ARG C  160  1                                  23
HELIX   29  29 THR C  161  ARG C  170  1                                  10
HELIX   30  30 SER C  197  SER C  213  1                                  17
HELIX   31  31 MET D    1  ARG D   17  1                                  17
HELIX   32  32 PRO D   48  ASN D   54  1                                   7
HELIX   33  33 ASP D   74  VAL D   87  1                                  14
HELIX   34  34 CYS D  101  ALA D  109  1                                   9
HELIX   35  35 GLY D  114  HIS D  130  1                                  17
HELIX   36  36 HIS D  130  LYS D  136  1                                   7
HELIX   37  37 SER D  138  ARG D  160  1                                  23
HELIX   38  38 THR D  161  ARG D  170  1                                  10
HELIX   39  39 SER D  197  SER D  213  1                                  17
HELIX   40  40 ASP E    2  ALA E   15  1                                  14
HELIX   41  41 PRO E   48  ASN E   54  1                                   7
HELIX   42  42 ASP E   74  VAL E   87  1                                  14
HELIX   43  43 CYS E  101  ALA E  109  1                                   9
HELIX   44  44 GLY E  114  HIS E  130  1                                  17
HELIX   45  45 HIS E  130  GLY E  135  1                                   6
HELIX   46  46 SER E  138  GLU E  140  5                                   3
HELIX   47  47 LYS E  141  THR E  161  1                                  21
HELIX   48  48 THR E  161  ARG E  170  1                                  10
HELIX   49  49 SER E  197  ILE E  214  1                                  18
HELIX   50  50 MET F    1  MET F   18  1                                  18
HELIX   51  51 PRO F   48  ASN F   54  1                                   7
HELIX   52  52 ASP F   74  VAL F   87  1                                  14
HELIX   53  53 CYS F  101  ALA F  109  1                                   9
HELIX   54  54 GLY F  114  HIS F  130  1                                  17
HELIX   55  55 HIS F  130  LEU F  137  1                                   8
HELIX   56  56 SER F  138  GLU F  140  5                                   3
HELIX   57  57 LYS F  141  ARG F  160  1                                  20
HELIX   58  58 THR F  161  ARG F  170  1                                  10
HELIX   59  59 SER F  197  SER F  213  1                                  17
SHEET    1   A 5 LEU A  60  ASN A  65  0
SHEET    2   A 5 TYR A  37  CYS A  42  1  N  TRP A  39   O  PHE A  61
SHEET    3   A 5 HIS A  92  HIS A  98  1  O  ILE A  94   N  ILE A  40
SHEET    4   A 5 SER A 175  PHE A 181  1  O  PHE A 181   N  GLY A  97
SHEET    5   A 5 LEU A 188  ASP A 190 -1  O  VAL A 189   N  VAL A 180
SHEET    1   B 5 LEU B  60  ASN B  65  0
SHEET    2   B 5 TYR B  37  CYS B  42  1  N  TRP B  39   O  HIS B  63
SHEET    3   B 5 HIS B  92  HIS B  98  1  O  ILE B  94   N  LEU B  38
SHEET    4   B 5 SER B 175  PHE B 181  1  O  TRP B 179   N  ILE B  95
SHEET    5   B 5 LEU B 188  ASP B 190 -1  O  VAL B 189   N  VAL B 180
SHEET    1   C 5 LEU C  60  ASN C  65  0
SHEET    2   C 5 TYR C  37  CYS C  42  1  N  TRP C  39   O  PHE C  61
SHEET    3   C 5 HIS C  92  HIS C  98  1  O  CYS C  96   N  ILE C  40
SHEET    4   C 5 SER C 175  PHE C 181  1  O  HIS C 177   N  ILE C  95
SHEET    5   C 5 LEU C 188  ASP C 190 -1  O  VAL C 189   N  VAL C 180
SHEET    1   D 5 LEU D  60  ASN D  65  0
SHEET    2   D 5 TYR D  37  CYS D  42  1  N  TRP D  39   O  PHE D  61
SHEET    3   D 5 HIS D  92  HIS D  98  1  O  ILE D  94   N  LEU D  38
SHEET    4   D 5 SER D 175  ASP D 182  1  O  HIS D 177   N  ILE D  95
SHEET    5   D 5 PHE D 187  ALA D 195 -1  O  VAL D 189   N  VAL D 180
SHEET    1   E 5 LEU E  60  ASN E  65  0
SHEET    2   E 5 TYR E  37  CYS E  42  1  N  TRP E  39   O  PHE E  61
SHEET    3   E 5 HIS E  92  HIS E  98  1  O  ILE E  94   N  LEU E  38
SHEET    4   E 5 SER E 175  PHE E 181  1  O  HIS E 177   N  ILE E  95
SHEET    5   E 5 LEU E 188  ASP E 190 -1  O  VAL E 189   N  VAL E 180
SHEET    1   F 5 LEU F  60  ASN F  65  0
SHEET    2   F 5 TYR F  37  CYS F  42  1  N  TRP F  39   O  PHE F  61
SHEET    3   F 5 HIS F  92  HIS F  98  1  O  ILE F  94   N  LEU F  38
SHEET    4   F 5 SER F 175  PHE F 181  1  O  HIS F 177   N  ILE F  95
SHEET    5   F 5 LEU F 188  ALA F 195 -1  O  VAL F 189   N  VAL F 180
LINK         SG  CYS A  42                ZN    ZN A 230     1555   1555  2.32
LINK         OD1 ASP A  44                ZN    ZN A 230     1555   1555  1.97
LINK         NE2 HIS A  98                ZN    ZN A 230     1555   1555  2.09
LINK         SG  CYS A 101                ZN    ZN A 230     1555   1555  2.31
LINK         SG  CYS B  42                ZN    ZN B 230     1555   1555  2.30
LINK         OD2 ASP B  44                ZN    ZN B 230     1555   1555  2.01
LINK         NE2 HIS B  98                ZN    ZN B 230     1555   1555  2.07
LINK         SG  CYS B 101                ZN    ZN B 230     1555   1555  2.32
LINK         SG  CYS C  42                ZN    ZN C 230     1555   1555  2.33
LINK         OD2 ASP C  44                ZN    ZN C 230     1555   1555  2.00
LINK         NE2 HIS C  98                ZN    ZN C 230     1555   1555  2.09
LINK         SG  CYS C 101                ZN    ZN C 230     1555   1555  2.31
LINK         SG  CYS D  42                ZN    ZN D 230     1555   1555  2.29
LINK         OD2 ASP D  44                ZN    ZN D 230     1555   1555  2.00
LINK         NE2 HIS D  98                ZN    ZN D 230     1555   1555  2.07
LINK         SG  CYS D 101                ZN    ZN D 230     1555   1555  2.32
LINK         SG  CYS E  42                ZN    ZN E 230     1555   1555  2.31
LINK         OD2 ASP E  44                ZN    ZN E 230     1555   1555  1.98
LINK         NE2 HIS E  98                ZN    ZN E 230     1555   1555  2.07
LINK         SG  CYS E 101                ZN    ZN E 230     1555   1555  2.33
LINK         SG  CYS F  42                ZN    ZN F 230     1555   1555  2.31
LINK         OD2 ASP F  44                ZN    ZN F 230     1555   1555  1.98
LINK         NE2 HIS F  98                ZN    ZN F 230     1555   1555  2.07
LINK         SG  CYS F 101                ZN    ZN F 230     1555   1555  2.30
SITE     1 AC1  4 CYS A  42  ASP A  44  HIS A  98  CYS A 101
SITE     1 AC2  5 LEU A 121  ARG A 124  PHE A 128  ARG B 160
SITE     2 AC2  5 ARG B 198
SITE     1 AC3  6 ARG A 160  LYS A 165  ARG A 198  LEU B 121
SITE     2 AC3  6 ARG B 124  PHE B 128
SITE     1 AC4  4 PRO A  48  ALA A  49  GLU A  50  ARG A  64
SITE     1 AC5  6 SER A  45  ARG A  46  HIS A  98  THR A  99
SITE     2 AC5  6 PHE A 181  VAL A 183
SITE     1 AC6  4 CYS B  42  ASP B  44  HIS B  98  CYS B 101
SITE     1 AC7  3 PRO B  48  GLU B  50  ARG B  64
SITE     1 AC8  7 SER B  45  ARG B  46  VAL B  47  HIS B  98
SITE     2 AC8  7 THR B  99  PHE B 181  VAL B 183
SITE     1 AC9  4 CYS C  42  ASP C  44  HIS C  98  CYS C 101
SITE     1 BC1  5 LEU C 121  ARG C 124  PHE C 128  ARG D 160
SITE     2 BC1  5 ARG D 198
SITE     1 BC2  7 PRO C  48  GLU C  50  ARG C  64  HOH C 257
SITE     2 BC2  7 PRO E  48  ALA E  49  ARG E  64
SITE     1 BC3  8 ASP C  44  SER C  45  ARG C  46  VAL C  47
SITE     2 BC3  8 HIS C  98  THR C  99  PHE C 181  VAL C 183
SITE     1 BC4  4 CYS D  42  ASP D  44  HIS D  98  CYS D 101
SITE     1 BC5  4 ARG C 160  ARG C 198  LEU D 121  ARG D 124
SITE     1 BC6  7 SER D  45  ARG D  46  VAL D  47  HIS D  98
SITE     2 BC6  7 PHE D 181  VAL D 183  HOH D 240
SITE     1 BC7  4 CYS E  42  ASP E  44  HIS E  98  CYS E 101
SITE     1 BC8  4 LEU E 121  ARG E 124  ARG F 160  ARG F 198
SITE     1 BC9  5 ARG E 160  LYS E 165  ARG E 198  LEU F 121
SITE     2 BC9  5 ARG F 124
SITE     1 CC1  6 SER E  45  ARG E  46  VAL E  47  HIS E  98
SITE     2 CC1  6 PHE E 181  VAL E 183
SITE     1 CC2  4 CYS F  42  ASP F  44  HIS F  98  CYS F 101
SITE     1 CC3  7 PRO D  48  GLU D  50  ARG D  64  PRO F  48
SITE     2 CC3  7 ALA F  49  GLU F  50  ARG F  64
SITE     1 CC4  6 SER F  45  ARG F  46  VAL F  47  HIS F  98
SITE     2 CC4  6 PHE F 181  VAL F 183
CRYST1  230.193  144.943   52.714  90.00  93.78  90.00 C 1 2 1      24
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      0.004344  0.000000  0.000287        0.00000
SCALE2      0.000000  0.006899  0.000000        0.00000
SCALE3      0.000000  0.000000  0.019012        0.00000
      
PROCHECK
Go to PROCHECK summary
 References