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PDBsum entry 3e2w

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Lyase PDB id
3e2w
Jmol
Contents
Protein chains
(+ 0 more) 208 a.a.
Ligands
SO4 ×12
BCT
Metals
_ZN ×6
Waters ×257
HEADER    LYASE                                   06-AUG-08   3E2W
TITLE     H. INFLUENZAE BETA-CARBONIC ANHYDRASE, VARIANT Y181F WITH 1M
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 3E2W    1       VERSN
REVDAT   2   18-AUG-10 3E2W    1       JRNL
REVDAT   1   18-AUG-09 3E2W    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) : 26.20
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.5
REMARK   3   NUMBER OF REFLECTIONS             : 77675
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) : 0.207
REMARK   3   R VALUE            (WORKING SET) : 0.205
REMARK   3   FREE R VALUE                     : 0.242
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 3911
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) : 2.35
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2066
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 34.64
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2210
REMARK   3   BIN FREE R VALUE SET COUNT          : 89
REMARK   3   BIN FREE R VALUE                    : 0.2820
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 9750
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 70
REMARK   3   SOLVENT ATOMS            : 257
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) : 67.43
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.35000
REMARK   3    B22 (A**2) : 0.06000
REMARK   3    B33 (A**2) : 0.32000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.17000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.271
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.215
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.154
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.464
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10034 ; 0.013 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  6655 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13569 ; 1.316 ; 1.932
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 16182 ; 0.962 ; 3.001
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1205 ; 5.548 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   479 ;38.364 ;24.113
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1749 ;16.192 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    60 ;18.302 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1503 ; 0.073 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11003 ; 0.003 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  2027 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1812 ; 0.199 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  5886 ; 0.176 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4491 ; 0.164 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  4637 ; 0.084 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   256 ; 0.151 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.034 ; 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):    17 ; 0.132 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    64 ; 0.195 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    16 ; 0.224 ; 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):  7871 ; 0.627 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2485 ; 0.090 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9688 ; 0.765 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4707 ; 1.227 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3881 ; 1.760 ; 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   218
REMARK   3    ORIGIN FOR THE GROUP (A):   8.5820  51.3880  28.3500
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1037 T22:  -0.1894
REMARK   3      T33:  -0.2262 T12:   0.0686
REMARK   3      T13:  -0.0736 T23:  -0.0247
REMARK   3    L TENSOR
REMARK   3      L11:   2.4336 L22:   1.3000
REMARK   3      L33:   1.0959 L12:  -0.0994
REMARK   3      L13:   0.9122 L23:  -0.3218
REMARK   3    S TENSOR
REMARK   3      S11:   0.1458 S12:   0.1474 S13:  -0.5098
REMARK   3      S21:   0.0123 S22:  -0.0440 S23:  -0.0696
REMARK   3      S31:   0.2024 S32:   0.1513 S33:  -0.1018
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   217
REMARK   3    ORIGIN FOR THE GROUP (A):   7.9990  85.5250  23.4120
REMARK   3    T TENSOR
REMARK   3      T11:   0.0954 T22:  -0.2026
REMARK   3      T33:  -0.2658 T12:  -0.1228
REMARK   3      T13:  -0.1229 T23:   0.0540
REMARK   3    L TENSOR
REMARK   3      L11:   2.7234 L22:   1.9387
REMARK   3      L33:   2.9670 L12:   0.3406
REMARK   3      L13:  -0.0580 L23:  -0.3245
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1169 S12:   0.1050 S13:   0.4794
REMARK   3      S21:   0.0034 S22:  -0.0097 S23:  -0.0825
REMARK   3      S31:  -0.8620 S32:   0.3128 S33:   0.1266
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   216
REMARK   3    ORIGIN FOR THE GROUP (A):  50.3670 121.8450   4.5430
REMARK   3    T TENSOR
REMARK   3      T11:   0.0301 T22:  -0.1820
REMARK   3      T33:  -0.3621 T12:   0.0742
REMARK   3      T13:  -0.0595 T23:   0.0016
REMARK   3    L TENSOR
REMARK   3      L11:   1.6377 L22:   3.2574
REMARK   3      L33:   3.1446 L12:  -0.1919
REMARK   3      L13:   0.4737 L23:  -0.6440
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0198 S12:  -0.0424 S13:   0.1630
REMARK   3      S21:  -0.0131 S22:   0.0554 S23:   0.4237
REMARK   3      S31:  -0.5240 S32:  -0.5791 S33:  -0.0356
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):  83.9420 106.8780   8.3700
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0921 T22:  -0.1994
REMARK   3      T33:  -0.2275 T12:  -0.0607
REMARK   3      T13:  -0.0292 T23:   0.0166
REMARK   3    L TENSOR
REMARK   3      L11:   2.7681 L22:   2.3358
REMARK   3      L33:   1.6670 L12:   0.0119
REMARK   3      L13:   0.6000 L23:   0.1037
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0442 S12:   0.1454 S13:  -0.0685
REMARK   3      S21:  -0.0691 S22:   0.0047 S23:  -0.6808
REMARK   3      S31:   0.0792 S32:   0.3031 S33:   0.0396
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   216
REMARK   3    ORIGIN FOR THE GROUP (A):  42.4290 105.7840  10.7990
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0851 T22:  -0.0320
REMARK   3      T33:  -0.2858 T12:  -0.0328
REMARK   3      T13:  -0.0428 T23:   0.0289
REMARK   3    L TENSOR
REMARK   3      L11:   2.3020 L22:   2.6120
REMARK   3      L33:   2.9695 L12:   0.3383
REMARK   3      L13:  -0.3030 L23:  -0.2538
REMARK   3    S TENSOR
REMARK   3      S11:   0.0210 S12:   0.0138 S13:   0.0918
REMARK   3      S21:   0.0042 S22:   0.0693 S23:   0.6388
REMARK   3      S31:  -0.0661 S32:  -0.8263 S33:  -0.0903
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   214
REMARK   3    ORIGIN FOR THE GROUP (A):  75.4870  90.8820   4.1450
REMARK   3    T TENSOR
REMARK   3      T11:   0.0582 T22:  -0.2638
REMARK   3      T33:  -0.3275 T12:   0.0020
REMARK   3      T13:  -0.0346 T23:  -0.0108
REMARK   3    L TENSOR
REMARK   3      L11:   1.5038 L22:   2.7711
REMARK   3      L33:   1.1978 L12:   0.1169
REMARK   3      L13:   0.1718 L23:   0.3494
REMARK   3    S TENSOR
REMARK   3      S11:   0.0523 S12:   0.0988 S13:  -0.2671
REMARK   3      S21:  -0.0770 S22:   0.0269 S23:  -0.4411
REMARK   3      S31:   0.3228 S32:   0.1657 S33:  -0.0792
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 3E2W 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 RCSB048806.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-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          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 77677
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.296
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.200
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4
REMARK 200  DATA REDUNDANCY                : 2.800
REMARK 200  R MERGE                    (I) : 0.06100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 13.7800
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     (%) : 99.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.37000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.730
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   (%): 60.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 1.5 M AMMONIUM SULFATE,
REMARK 280  4% PEG 4000, CRYSTALS SOAKED IN THIS SOLUTION PLUS 30% GLYCEROL
REMARK 280  AND 1 M SODIUM BICARBONATE, 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      125.07050
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.61250
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      125.07050
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       72.61250
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: 17800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -253.0 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       -3.52695
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       53.38262
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: 18050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -246.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH B 261  LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     SER A    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     HIS A    32
REMARK 465     ASN A   219
REMARK 465     ILE A   220
REMARK 465     LEU A   221
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     MET B    18
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     GLU B   218
REMARK 465     ASN B   219
REMARK 465     ILE B   220
REMARK 465     LEU B   221
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     GLU C   217
REMARK 465     GLU C   218
REMARK 465     ASN C   219
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     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     HIS D    32
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     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     GLU E   217
REMARK 465     GLU E   218
REMARK 465     ASN E   219
REMARK 465     ILE E   220
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     LEU F   215
REMARK 465     ASP F   216
REMARK 465     GLU F   217
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   OE1  GLU A    50     O    HOH A   268              2.07
REMARK 500   OE1  GLU F    50     O3   BCT F   231              2.18
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  77   CB    CYS D  77   SG      0.106
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. = -14.2 DEGREES
REMARK 500    LEU F  52   CA  -  CB  -  CG  ANGL. DEV. =  16.5 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    ASN A  68       56.23     39.76
REMARK 500    ASP B   2      -58.85     -6.09
REMARK 500    ASN B  54       61.40     61.17
REMARK 500    ARG D  17     -175.39    -66.55
REMARK 500    MET D  18      -12.32     71.17
REMARK 500    ASP E 185       -9.38   -155.00
REMARK 500    ASN F  68       61.24     36.57
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  92.0
REMARK 620 3 HIS A  98   NE2 109.5  94.6
REMARK 620 4 CYS A 101   SG  122.8 130.3 103.8
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  97.7
REMARK 620 3 HIS B  98   NE2 108.7 120.3
REMARK 620 4 CYS B 101   SG  118.9 105.6 106.3
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  94.4
REMARK 620 3 HIS C  98   NE2 105.4 129.7
REMARK 620 4 CYS C 101   SG  114.4  96.8 115.0
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   OD2 105.3
REMARK 620 3 HIS D  98   NE2 112.6  99.4
REMARK 620 4 CYS D 101   SG  115.2 117.2 106.3
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 103.5
REMARK 620 3 HIS E  98   NE2 111.1  87.7
REMARK 620 4 CYS E 101   SG  121.0 123.5 104.8
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 101.9
REMARK 620 3 HIS F  98   NE2 110.2  79.0
REMARK 620 4 CYS F 101   SG  115.8 130.5 113.4
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 ZN B 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 231
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 ZN D 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 233
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 ZN F 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT F 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 233
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: 3E2A   RELATED DB: PDB
REMARK 900 RELATED ID: 3E2X   RELATED DB: PDB
REMARK 900 RELATED ID: 3E31   RELATED DB: PDB
DBREF  3E2W A    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E2W B    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E2W C    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E2W D    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E2W E    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E2W F    1   229  UNP    P45148   CAN_HAEIN        1    229
SEQADV 3E2W PHE A  181  UNP  P45148    TYR   181 ENGINEERED
SEQADV 3E2W PHE B  181  UNP  P45148    TYR   181 ENGINEERED
SEQADV 3E2W PHE C  181  UNP  P45148    TYR   181 ENGINEERED
SEQADV 3E2W PHE D  181  UNP  P45148    TYR   181 ENGINEERED
SEQADV 3E2W PHE E  181  UNP  P45148    TYR   181 ENGINEERED
SEQADV 3E2W 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     ZN  B 230       1
HET    SO4  B 231       5
HET     ZN  C 230       1
HET    SO4  C 231       5
HET     ZN  D 230       1
HET    SO4  D 231       5
HET    SO4  D 232       5
HET    SO4  D 233       5
HET     ZN  E 230       1
HET    SO4  E 231       5
HET    SO4  E 232       5
HET     ZN  F 230       1
HET    BCT  F 231       4
HET    SO4  F 232       5
HET    SO4  F 233       5
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  23  BCT    C H O3 1-
FORMUL  26  HOH   *257(H2 O)
HELIX    1   1 MET A    1  ASN A   22  1                                  22
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  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 MET B    1  ARG B   17  1                                  17
HELIX   12  12 PRO B   48  ASN B   54  1                                   7
HELIX   13  13 ASP B   74  VAL B   87  1                                  14
HELIX   14  14 CYS B  101  ALA B  109  1                                   9
HELIX   15  15 GLY B  114  HIS B  130  1                                  17
HELIX   16  16 HIS B  130  LYS B  136  1                                   7
HELIX   17  17 LEU B  137  GLU B  140  5                                   4
HELIX   18  18 LYS B  141  GLY B  159  1                                  19
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  LYS C   19  1                                  19
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 LEU C  137  GLU C  140  5                                   4
HELIX   28  28 LYS C  141  THR C  161  1                                  21
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 MET D   18  ASN D   22  5                                   5
HELIX   33  33 PRO D   48  ASN D   54  1                                   7
HELIX   34  34 ASP D   74  VAL D   87  1                                  14
HELIX   35  35 CYS D  101  ALA D  109  1                                   9
HELIX   36  36 GLY D  114  HIS D  130  1                                  17
HELIX   37  37 HIS D  130  GLY D  135  1                                   6
HELIX   38  38 SER D  138  GLY D  159  1                                  22
HELIX   39  39 THR D  161  GLY D  171  1                                  11
HELIX   40  40 SER D  197  SER D  213  1                                  17
HELIX   41  41 MET E    1  MET E   18  1                                  18
HELIX   42  42 PRO E   48  ASN E   54  1                                   7
HELIX   43  43 ASP E   74  VAL E   87  1                                  14
HELIX   44  44 CYS E  101  ALA E  109  1                                   9
HELIX   45  45 GLY E  114  HIS E  130  1                                  17
HELIX   46  46 HIS E  130  LYS E  136  1                                   7
HELIX   47  47 LEU E  137  GLU E  140  5                                   4
HELIX   48  48 LYS E  141  ARG E  160  1                                  20
HELIX   49  49 THR E  161  ARG E  170  1                                  10
HELIX   50  50 SER E  197  SER E  213  1                                  17
HELIX   51  51 MET F    1  MET F   18  1                                  18
HELIX   52  52 PRO F   48  THR F   53  1                                   6
HELIX   53  53 ASP F   74  VAL F   87  1                                  14
HELIX   54  54 CYS F  101  ALA F  109  1                                   9
HELIX   55  55 LEU F  115  HIS F  130  1                                  16
HELIX   56  56 HIS F  130  LYS F  136  1                                   7
HELIX   57  57 LEU F  137  GLU F  140  5                                   4
HELIX   58  58 LYS F  141  THR F  161  1                                  21
HELIX   59  59 THR F  161  ARG F  170  1                                  10
HELIX   60  60 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  TYR A  37   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  95
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  TYR B  37   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  TRP B 179   N  GLY B  97
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  HIS C  63
SHEET    3   C 5 HIS C  92  HIS C  98  1  O  ILE C  94   N  ILE C  40
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  LEU D  38
SHEET    4   D 5 SER D 175  PHE D 181  1  O  SER D 175   N  ILE D  93
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  TYR E  37   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  SER E 175   N  ILE E  93
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  ASP F 190 -1  O  VAL F 189   N  VAL F 180
LINK         SG  CYS A  42                ZN    ZN A 230     1555   1555  2.35
LINK         OD1 ASP A  44                ZN    ZN A 230     1555   1555  2.01
LINK         NE2 HIS A  98                ZN    ZN A 230     1555   1555  2.09
LINK         SG  CYS A 101                ZN    ZN A 230     1555   1555  2.33
LINK         SG  CYS B  42                ZN    ZN B 230     1555   1555  2.35
LINK         OD2 ASP B  44                ZN    ZN B 230     1555   1555  2.00
LINK         NE2 HIS B  98                ZN    ZN B 230     1555   1555  2.08
LINK         SG  CYS B 101                ZN    ZN B 230     1555   1555  2.49
LINK         SG  CYS C  42                ZN    ZN C 230     1555   1555  2.31
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  2.34
LINK         SG  CYS D  42                ZN    ZN D 230     1555   1555  2.34
LINK         OD2 ASP D  44                ZN    ZN D 230     1555   1555  2.00
LINK         NE2 HIS D  98                ZN    ZN D 230     1555   1555  2.11
LINK         SG  CYS D 101                ZN    ZN D 230     1555   1555  2.30
LINK         SG  CYS E  42                ZN    ZN E 230     1555   1555  2.34
LINK         OD2 ASP E  44                ZN    ZN E 230     1555   1555  1.98
LINK         NE2 HIS E  98                ZN    ZN E 230     1555   1555  2.10
LINK         SG  CYS E 101                ZN    ZN E 230     1555   1555  2.32
LINK         SG  CYS F  42                ZN    ZN F 230     1555   1555  2.31
LINK         OD2 ASP F  44                ZN    ZN F 230     1555   1555  2.02
LINK         NE2 HIS F  98                ZN    ZN F 230     1555   1555  2.10
LINK         SG  CYS F 101                ZN    ZN F 230     1555   1555  2.33
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  HOH A 277  ARG B 160
SITE     2 AC2  5 ARG B 198
SITE     1 AC3  4 ARG A 160  ARG A 198  LEU B 121  ARG B 124
SITE     1 AC4  6 ARG A  46  VAL A  47  HIS A  98  PHE A 181
SITE     2 AC4  6 VAL A 183  HOH A 267
SITE     1 AC5  4 CYS B  42  ASP B  44  HIS B  98  CYS B 101
SITE     1 AC6  6 SER B  45  ARG B  46  VAL B  47  HIS B  98
SITE     2 AC6  6 PHE B 181  VAL B 183
SITE     1 AC7  4 CYS C  42  ASP C  44  HIS C  98  CYS C 101
SITE     1 AC8  4 SER C  45  ARG C  46  HIS C  98  VAL C 183
SITE     1 AC9  4 CYS D  42  ASP D  44  HIS D  98  CYS D 101
SITE     1 BC1  4 LEU C 121  ARG C 124  ARG D 160  ARG D 198
SITE     1 BC2  4 ARG C 160  ARG C 198  LEU D 121  ARG D 124
SITE     1 BC3  6 ARG D  46  VAL D  47  HIS D  98  PHE D 181
SITE     2 BC3  6 VAL D 183  HOH D 250
SITE     1 BC4  4 CYS E  42  ASP E  44  HIS E  98  CYS E 101
SITE     1 BC5  4 LEU E 121  ARG E 124  ARG F 160  ARG F 198
SITE     1 BC6  5 ARG E  46  VAL E  47  HIS E  98  PHE E 181
SITE     2 BC6  5 VAL E 183
SITE     1 BC7  4 CYS F  42  ASP F  44  HIS F  98  CYS F 101
SITE     1 BC8  7 ARG D  64  PRO F  48  ALA F  49  GLU F  50
SITE     2 BC8  7 ARG F  64  HOH F 269  HOH F 274
SITE     1 BC9  3 ARG E 160  ARG E 198  ARG F 124
SITE     1 CC1  6 ASP F  44  SER F  45  ARG F  46  HIS F  98
SITE     2 CC1  6 PHE F 181  VAL F 183
CRYST1  250.141  145.225   53.499  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      0.003998  0.000000  0.000264        0.00000
SCALE2      0.000000  0.006886  0.000000        0.00000
SCALE3      0.000000  0.000000  0.018733        0.00000
      
PROCHECK
Go to PROCHECK summary
 References