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PDBsum entry 3e2a

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Lyase PDB id
3e2a
Jmol
Contents
Protein chains
(+ 0 more) 209 a.a.
Ligands
SO4 ×12
BCT
Metals
_ZN ×6
Waters ×158
HEADER    LYASE                                   05-AUG-08   3E2A
TITLE     H. INFLUENZAE BETA-CARBONIC ANHYDRASE, VARIANT Y181F WITH 100 MM
TITLE    2 BICARBONATE
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 3E2A    1       VERSN
REVDAT   2   28-JUL-09 3E2A    1       JRNL
REVDAT   1   02-JUN-09 3E2A    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.    2.30 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) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.78
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 77404
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) : 0.205
REMARK   3   R VALUE            (WORKING SET) : 0.201
REMARK   3   FREE R VALUE                     : 0.244
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 7808
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) : 2.30
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4982
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2150
REMARK   3   BIN FREE R VALUE SET COUNT          : 582
REMARK   3   BIN FREE R VALUE                    : 0.2700
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 9906
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 70
REMARK   3   SOLVENT ATOMS            : 158
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) : 44.23
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.12000
REMARK   3    B22 (A**2) : 0.02000
REMARK   3    B33 (A**2) : -0.14000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.03000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.282
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.222
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.148
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.150
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10192 ; 0.011 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  6746 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13784 ; 1.233 ; 1.932
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 16408 ; 0.886 ; 3.001
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1224 ; 5.921 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   490 ;37.527 ;24.204
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1777 ;16.031 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    60 ;19.481 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1529 ; 0.073 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11180 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  2050 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2230 ; 0.220 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  6722 ; 0.189 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4879 ; 0.174 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  4998 ; 0.088 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   325 ; 0.165 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):     2 ; 0.063 ; 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):    31 ; 0.177 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    89 ; 0.164 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.341 ; 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):  7980 ; 0.751 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2525 ; 0.110 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9840 ; 0.921 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4745 ; 1.481 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3944 ; 2.047 ; 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):   9.3050  52.7140  27.6510
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1853 T22:  -0.0865
REMARK   3      T33:   0.0827 T12:   0.0755
REMARK   3      T13:  -0.0468 T23:  -0.0653
REMARK   3    L TENSOR
REMARK   3      L11:   2.1854 L22:   0.7589
REMARK   3      L33:   0.9406 L12:  -0.0686
REMARK   3      L13:   0.9688 L23:  -0.2018
REMARK   3    S TENSOR
REMARK   3      S11:   0.2206 S12:   0.2303 S13:  -0.4950
REMARK   3      S21:   0.0574 S22:  -0.0119 S23:  -0.1096
REMARK   3      S31:   0.2011 S32:   0.1866 S33:  -0.2087
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):   8.8470  84.1490  23.6280
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0585 T22:  -0.0997
REMARK   3      T33:  -0.0358 T12:  -0.1418
REMARK   3      T13:  -0.0320 T23:   0.0500
REMARK   3    L TENSOR
REMARK   3      L11:   2.2628 L22:   1.8893
REMARK   3      L33:   3.0816 L12:  -0.0254
REMARK   3      L13:   0.3246 L23:  -0.4713
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1957 S12:   0.2140 S13:   0.3082
REMARK   3      S21:   0.0193 S22:   0.0059 S23:  -0.2260
REMARK   3      S31:  -0.8518 S32:   0.4807 S33:   0.1898
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):  48.3030 122.9450   4.6790
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0662 T22:  -0.1339
REMARK   3      T33:  -0.0968 T12:   0.0607
REMARK   3      T13:   0.0262 T23:  -0.0024
REMARK   3    L TENSOR
REMARK   3      L11:   1.4747 L22:   2.5835
REMARK   3      L33:   2.6425 L12:  -0.4197
REMARK   3      L13:   0.3978 L23:  -0.6997
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0356 S12:  -0.0175 S13:   0.1483
REMARK   3      S21:  -0.0103 S22:   0.0288 S23:   0.2043
REMARK   3      S31:  -0.5454 S32:  -0.3760 S33:   0.0067
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   215
REMARK   3    ORIGIN FOR THE GROUP (A):  76.6760 109.1290   7.7670
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1733 T22:  -0.1002
REMARK   3      T33:   0.0267 T12:  -0.0629
REMARK   3      T13:   0.0424 T23:   0.0206
REMARK   3    L TENSOR
REMARK   3      L11:   1.9150 L22:   1.6178
REMARK   3      L33:   1.3860 L12:  -0.0440
REMARK   3      L13:   0.4987 L23:   0.1088
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0501 S12:   0.1101 S13:   0.0778
REMARK   3      S21:  -0.0195 S22:  -0.0279 S23:  -0.4899
REMARK   3      S31:  -0.0178 S32:   0.2319 S33:   0.0781
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):  39.5390 103.8490  10.3290
REMARK   3    T TENSOR
REMARK   3      T11:  -0.2113 T22:   0.0315
REMARK   3      T33:  -0.0172 T12:  -0.0438
REMARK   3      T13:   0.0283 T23:   0.0074
REMARK   3    L TENSOR
REMARK   3      L11:   1.5629 L22:   2.2361
REMARK   3      L33:   2.2311 L12:   0.0694
REMARK   3      L13:  -0.3741 L23:  -0.5655
REMARK   3    S TENSOR
REMARK   3      S11:   0.0139 S12:  -0.0203 S13:  -0.0868
REMARK   3      S21:   0.0254 S22:   0.0763 S23:   0.5103
REMARK   3      S31:   0.0268 S32:  -0.6919 S33:  -0.0902
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   219
REMARK   3    ORIGIN FOR THE GROUP (A):  67.7480  90.2110   4.6640
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0666 T22:  -0.1719
REMARK   3      T33:  -0.0556 T12:   0.0003
REMARK   3      T13:   0.0378 T23:  -0.0008
REMARK   3    L TENSOR
REMARK   3      L11:   1.3675 L22:   2.0575
REMARK   3      L33:   0.9668 L12:   0.3030
REMARK   3      L13:   0.0736 L23:   0.2953
REMARK   3    S TENSOR
REMARK   3      S11:   0.0514 S12:   0.0170 S13:  -0.2076
REMARK   3      S21:  -0.0413 S22:  -0.0336 S23:  -0.2485
REMARK   3      S31:   0.2933 S32:   0.0624 S33:  -0.0178
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 3E2A 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 RCSB048784.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 13-APR-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          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 77406
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.301
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 3.530
REMARK 200  R MERGE                    (I) : 0.06500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 18.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.34300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.600
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   (%): 56.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 1.5 M AMMONIUM SULFATE,
REMARK 280  4% PEG 4000, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  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      115.30300
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.75600
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      115.30300
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       72.75600
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
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: -257.0 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   BIOMT1   2 -1.000000  0.000000  0.000000       -3.50948
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       53.11819
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
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: -256.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, E, D, 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 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     GLU A    20
REMARK 465     GLU A    21
REMARK 465     ASN A    22
REMARK 465     SER A    23
REMARK 465     THR A    24
REMARK 465     TYR A    25
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     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     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     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     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     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     HIS F    32
REMARK 465     GLN F    33
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     MET A  18    O
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   OG   SER D    45     O    HOH D   249              2.10
REMARK 500   O    HOH D   252     O    HOH F   250              2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   OE1  GLU A    50     O    HOH A   246     2556     1.92
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 F  44   CB  -  CA  -  C   ANGL. DEV. = -13.8 DEGREES
REMARK 500    ARG F  64   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 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    SER A  45      131.87    -31.40
REMARK 500    ASN A  54       61.56     32.90
REMARK 500    SER C 197      173.13    179.85
REMARK 500    GLU C 218       72.10    -61.45
REMARK 500    SER D  45       74.70      5.53
REMARK 500    ARG E  46      -41.75   -131.35
REMARK 500    LYS E 111      131.04   -171.77
REMARK 500    GLU E 218      -17.12    -48.50
REMARK 500    ASP F   2      -92.44     26.24
REMARK 500    SER F  45      155.68    -46.92
REMARK 500    GLU F 218      -27.10    -33.48
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 ASP D   31     HIS D   32                 -135.00
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    HIS D  32        18.0      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   OD2  82.3
REMARK 620 3 HIS A  98   NE2 106.4 138.2
REMARK 620 4 CYS A 101   SG  113.6  94.4 117.2
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  87.6
REMARK 620 3 HIS B  98   NE2 112.7 134.6
REMARK 620 4 CYS B 101   SG  113.9  96.1 110.1
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 100.5
REMARK 620 3 HIS C  98   NE2 108.4  89.2
REMARK 620 4 CYS C 101   SG  116.4 124.6 114.0
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   OD1  95.3
REMARK 620 3 HIS D  98   NE2 118.5 113.3
REMARK 620 4 CYS D 101   SG  113.7 105.9 108.9
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 106.8
REMARK 620 3 HIS E  98   NE2 108.5  93.6
REMARK 620 4 CYS E 101   SG  114.7 121.9 108.9
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   OD1  95.7
REMARK 620 3 HIS F  98   NE2 113.0 129.9
REMARK 620 4 CYS F 101   SG  114.4  89.7 112.0
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 ZN B 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 233
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT 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: 3E28   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  3E2A A    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E2A B    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E2A C    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E2A D    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E2A E    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E2A F    1   229  UNP    P45148   CAN_HAEIN        1    229
SEQADV 3E2A PHE A  181  UNP  P45148    TYR   181 ENGINEERED
SEQADV 3E2A PHE B  181  UNP  P45148    TYR   181 ENGINEERED
SEQADV 3E2A PHE C  181  UNP  P45148    TYR   181 ENGINEERED
SEQADV 3E2A PHE D  181  UNP  P45148    TYR   181 ENGINEERED
SEQADV 3E2A PHE E  181  UNP  P45148    TYR   181 ENGINEERED
SEQADV 3E2A 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     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     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    BCT  F 232       4
HETNAM      ZN ZINC ION
HETNAM     SO4 SULFATE ION
HETNAM     BCT BICARBONATE ION
FORMUL   7   ZN    6(ZN 2+)
FORMUL   8  SO4    12(O4 S 2-)
FORMUL  25  BCT    C H O3 1-
FORMUL  26  HOH   *158(H2 O)
HELIX    1   1 MET A    1  MET A   18  1                                  18
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 SER A  138  GLU A  140  5                                   3
HELIX    8   8 LYS A  141  ARG A  160  1                                  20
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  MET B   18  1                                  18
HELIX   13  13 PRO B   48  ASN B   54  1                                   7
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 LYS B  141  ARG B  160  1                                  20
HELIX   19  19 THR B  161  ARG B  170  1                                  10
HELIX   20  20 SER B  197  SER B  213  1                                  17
HELIX   21  21 MET C    1  MET C   18  1                                  18
HELIX   22  22 PRO C   48  ASN C   54  1                                   7
HELIX   23  23 ASP C   74  VAL C   87  1                                  14
HELIX   24  24 CYS C  101  ALA C  109  1                                   9
HELIX   25  25 GLY C  114  HIS C  130  1                                  17
HELIX   26  26 HIS C  130  LYS C  136  1                                   7
HELIX   27  27 SER C  138  THR C  161  1                                  24
HELIX   28  28 THR C  161  ARG C  170  1                                  10
HELIX   29  29 SER C  197  SER C  213  1                                  17
HELIX   30  30 MET D    1  MET D   18  1                                  18
HELIX   31  31 PRO D   48  THR D   53  1                                   6
HELIX   32  32 ASP D   74  VAL D   87  1                                  14
HELIX   33  33 CYS D  101  ALA D  109  1                                   9
HELIX   34  34 GLY D  114  HIS D  130  1                                  17
HELIX   35  35 HIS D  130  GLY D  135  1                                   6
HELIX   36  36 SER D  138  ARG D  160  1                                  23
HELIX   37  37 THR D  161  ARG D  170  1                                  10
HELIX   38  38 SER D  197  SER D  213  1                                  17
HELIX   39  39 MET E    1  MET E   18  1                                  18
HELIX   40  40 PRO E   48  ASN E   54  1                                   7
HELIX   41  41 ASP E   74  VAL E   87  1                                  14
HELIX   42  42 CYS E  101  ALA E  109  1                                   9
HELIX   43  43 GLY E  114  HIS E  130  1                                  17
HELIX   44  44 HIS E  130  LEU E  137  1                                   8
HELIX   45  45 SER E  138  ARG E  160  1                                  23
HELIX   46  46 THR E  161  ARG E  170  1                                  10
HELIX   47  47 SER E  197  SER E  213  1                                  17
HELIX   48  48 MET F    1  MET F   18  1                                  18
HELIX   49  49 PRO F   48  ASN F   54  1                                   7
HELIX   50  50 ASP F   74  VAL F   87  1                                  14
HELIX   51  51 CYS F  101  ALA F  109  1                                   9
HELIX   52  52 GLY F  114  HIS F  130  1                                  17
HELIX   53  53 HIS F  130  LYS F  136  1                                   7
HELIX   54  54 SER F  138  GLU F  140  5                                   3
HELIX   55  55 LYS F  141  THR F  161  1                                  21
HELIX   56  56 THR F  161  ARG F  170  1                                  10
HELIX   57  57 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  HIS A 177   N  ILE A  93
SHEET    5   A 5 LEU A 188  ALA A 195 -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  PHE B  61
SHEET    3   B 5 HIS B  92  HIS B  98  1  O  ILE B  94   N  ILE B  40
SHEET    4   B 5 SER B 175  PHE B 181  1  O  HIS B 177   N  ILE B  93
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  TYR C  37   O  PHE C  61
SHEET    3   C 5 HIS C  92  HIS C  98  1  O  ILE C  94   N  LEU C  38
SHEET    4   C 5 SER C 175  PHE C 181  1  O  TRP C 179   N  GLY C  97
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  ILE D  40
SHEET    4   D 5 SER D 175  PHE D 181  1  O  HIS D 177   N  ILE D  95
SHEET    5   D 5 LEU D 188  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  HIS E  63
SHEET    3   E 5 HIS E  92  HIS E  98  1  O  ILE E  94   N  ILE E  40
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  ALA E 195 -1  O  ALA E 195   N  LEU E 176
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  HIS F  63
SHEET    3   F 5 HIS F  92  HIS F  98  1  O  ILE F  94   N  ILE F  40
SHEET    4   F 5 SER F 175  PHE F 181  1  O  HIS F 177   N  ILE F  93
SHEET    5   F 5 LEU F 188  ALA F 195 -1  O  GLN F 191   N  GLY F 178
LINK         SG  CYS A  42                ZN    ZN A 230     1555   1555  2.34
LINK         OD2 ASP A  44                ZN    ZN A 230     1555   1555  2.03
LINK         NE2 HIS A  98                ZN    ZN A 230     1555   1555  2.07
LINK         SG  CYS A 101                ZN    ZN A 230     1555   1555  2.29
LINK         SG  CYS B  42                ZN    ZN B 230     1555   1555  2.30
LINK         OD2 ASP B  44                ZN    ZN B 230     1555   1555  2.00
LINK         NE2 HIS B  98                ZN    ZN B 230     1555   1555  2.09
LINK         SG  CYS B 101                ZN    ZN B 230     1555   1555  2.31
LINK         SG  CYS C  42                ZN    ZN C 230     1555   1555  2.31
LINK         OD2 ASP C  44                ZN    ZN C 230     1555   1555  1.99
LINK         NE2 HIS C  98                ZN    ZN C 230     1555   1555  2.08
LINK         SG  CYS C 101                ZN    ZN C 230     1555   1555  2.32
LINK         SG  CYS D  42                ZN    ZN D 230     1555   1555  2.30
LINK         OD1 ASP D  44                ZN    ZN D 230     1555   1555  2.01
LINK         NE2 HIS D  98                ZN    ZN D 230     1555   1555  2.08
LINK         SG  CYS D 101                ZN    ZN D 230     1555   1555  2.29
LINK         SG  CYS E  42                ZN    ZN E 230     1555   1555  2.29
LINK         OD2 ASP E  44                ZN    ZN E 230     1555   1555  1.99
LINK         NE2 HIS E  98                ZN    ZN E 230     1555   1555  2.07
LINK         SG  CYS E 101                ZN    ZN E 230     1555   1555  2.30
LINK         SG  CYS F  42                ZN    ZN F 230     1555   1555  2.30
LINK         OD1 ASP F  44                ZN    ZN F 230     1555   1555  2.00
LINK         NE2 HIS F  98                ZN    ZN F 230     1555   1555  2.07
LINK         SG  CYS F 101                ZN    ZN F 230     1555   1555  2.27
SITE     1 AC1  4 CYS A  42  ASP A  44  HIS A  98  CYS A 101
SITE     1 AC2  4 ARG A 124  PHE A 128  ARG B 160  ARG B 198
SITE     1 AC3  6 ARG A  46  VAL A  47  HIS A  98  THR A  99
SITE     2 AC3  6 PHE A 181  VAL A 183
SITE     1 AC4  4 CYS B  42  ASP B  44  HIS B  98  CYS B 101
SITE     1 AC5  4 ARG A 160  ARG A 198  LEU B 121  ARG B 124
SITE     1 AC6  6 ASP B  44  SER B  45  ARG B  46  VAL B  47
SITE     2 AC6  6 HIS B  98  VAL B 183
SITE     1 AC7  4 CYS C  42  ASP C  44  HIS C  98  CYS C 101
SITE     1 AC8  4 ARG C 160  ARG C 198  LEU D 121  ARG D 124
SITE     1 AC9  7 ASP C  44  SER C  45  ARG C  46  VAL C  47
SITE     2 AC9  7 HIS C  98  PHE C 181  VAL C 183
SITE     1 BC1  4 CYS D  42  ASP D  44  HIS D  98  CYS D 101
SITE     1 BC2  4 LEU C 121  ARG C 124  ARG D 160  ARG D 198
SITE     1 BC3  6 SER D  45  ARG D  46  VAL D  47  HIS D  98
SITE     2 BC3  6 PHE D 181  VAL D 183
SITE     1 BC4  4 CYS E  42  ASP E  44  HIS E  98  CYS E 101
SITE     1 BC5  6 ARG E 160  LYS E 165  ARG E 198  LEU F 121
SITE     2 BC5  6 ARG F 124  PHE F 128
SITE     1 BC6  5 LEU E 121  ARG E 124  PHE E 128  ARG F 160
SITE     2 BC6  5 ARG F 198
SITE     1 BC7  6 SER E  45  ARG E  46  VAL E  47  HIS E  98
SITE     2 BC7  6 PHE E 181  VAL E 183
SITE     1 BC8  4 CYS F  42  ASP F  44  HIS F  98  CYS F 101
SITE     1 BC9  6 SER F  45  ARG F  46  HIS F  98  THR F  99
SITE     2 BC9  6 PHE F 181  VAL F 183
SITE     1 CC1  7 ARG D  64  HOH D 240  PRO F  48  ALA F  49
SITE     2 CC1  7 GLU F  50  ARG F  64  HOH F 259
CRYST1  230.606  145.512   53.234  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      0.004336  0.000000  0.000287        0.00000
SCALE2      0.000000  0.006872  0.000000        0.00000
SCALE3      0.000000  0.000000  0.018826        0.00000
      
PROCHECK
Go to PROCHECK summary
 References