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PDBsum entry 3mf3

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
3mf3
Jmol
Contents
Protein chains
(+ 0 more) 220 a.a.
Ligands
ACT ×4
Metals
_CO ×6
Waters ×204
HEADER    LYASE                                   01-APR-10   3MF3
TITLE     COBALT(II)-SUBSTITUTED HAEMOPHILUS INFLUENZAE B-CARBONIC ANHYDRASE
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
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: PTRC99A
KEYWDS    BETA-CARBONIC ANHYDRASE, HAEMOPHILUS INFLUENZAE, BICARBONATE, ZINC
KEYWDS   2 METALLOENZYME, COBALT SUBSTITUTION, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.M.HOFFMANN,R.S.ROWLETT
REVDAT   1   20-APR-11 3MF3    0
JRNL        AUTH   K.M.HOFFMANN,D.SAMARDZIC,K.VAN DEN HEEVER,R.S.ROWLETT
JRNL        TITL   THE STRUCTURE AND PROPERTIES OF COBALT(II)-SUBSTITUTED
JRNL        TITL 2 HAEMOPHILUS INFLUENZAE B-CARBONIC ANHYDRASE.
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.87
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9
REMARK   3   NUMBER OF REFLECTIONS             : 55195
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) : 0.176
REMARK   3   R VALUE            (WORKING SET) : 0.173
REMARK   3   FREE R VALUE                     : 0.228
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 2941
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4002
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.65
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2230
REMARK   3   BIN FREE R VALUE SET COUNT          : 224
REMARK   3   BIN FREE R VALUE                    : 0.2860
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 10483
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 22
REMARK   3   SOLVENT ATOMS            : 204
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 69.15
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.02000
REMARK   3    B22 (A**2) : 0.12000
REMARK   3    B33 (A**2) : -0.08000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.11000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.411
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.256
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.189
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.373
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10729 ; 0.019 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14532 ; 1.691 ; 1.927
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1298 ; 6.293 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   525 ;38.201 ;24.286
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1877 ;19.207 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    60 ;22.531 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1608 ; 0.108 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8088 ; 0.007 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
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):  6472 ; 0.949 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10408 ; 1.818 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4257 ; 2.721 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4124 ; 4.363 ; 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  : 7
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     2        A   221
REMARK   3    ORIGIN FOR THE GROUP (A):   7.7450 -92.3840  27.8570
REMARK   3    T TENSOR
REMARK   3      T11:   0.0201 T22:   0.1920
REMARK   3      T33:   0.1979 T12:   0.0319
REMARK   3      T13:  -0.0049 T23:   0.0412
REMARK   3    L TENSOR
REMARK   3      L11:   1.6489 L22:   0.7168
REMARK   3      L33:   0.5037 L12:  -0.0837
REMARK   3      L13:   0.5191 L23:  -0.3813
REMARK   3    S TENSOR
REMARK   3      S11:   0.0241 S12:  -0.0105 S13:  -0.3131
REMARK   3      S21:   0.0098 S22:  -0.0623 S23:  -0.1229
REMARK   3      S31:   0.0509 S32:   0.0953 S33:   0.0382
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     1        B   221
REMARK   3    ORIGIN FOR THE GROUP (A):   7.2020 -58.5590  22.8780
REMARK   3    T TENSOR
REMARK   3      T11:   0.1488 T22:   0.1766
REMARK   3      T33:   0.1425 T12:  -0.0788
REMARK   3      T13:  -0.0888 T23:   0.0674
REMARK   3    L TENSOR
REMARK   3      L11:   1.3812 L22:   0.6639
REMARK   3      L33:   0.5680 L12:  -0.1415
REMARK   3      L13:  -0.2703 L23:  -0.0843
REMARK   3    S TENSOR
REMARK   3      S11:   0.0019 S12:   0.0614 S13:   0.2247
REMARK   3      S21:   0.0395 S22:  -0.1165 S23:  -0.1423
REMARK   3      S31:  -0.2755 S32:   0.1254 S33:   0.1146
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   217
REMARK   3    ORIGIN FOR THE GROUP (A):  46.4400 -22.2830   4.1490
REMARK   3    T TENSOR
REMARK   3      T11:   0.1790 T22:   0.0701
REMARK   3      T33:   0.0938 T12:   0.0131
REMARK   3      T13:  -0.0031 T23:   0.0474
REMARK   3    L TENSOR
REMARK   3      L11:   0.9435 L22:   1.9063
REMARK   3      L33:   1.1120 L12:   0.0954
REMARK   3      L13:   0.1863 L23:  -0.6714
REMARK   3    S TENSOR
REMARK   3      S11:   0.0176 S12:  -0.0192 S13:   0.1820
REMARK   3      S21:  -0.0801 S22:   0.1040 S23:   0.2123
REMARK   3      S31:  -0.2068 S32:  -0.2311 S33:  -0.1217
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     2        D   215
REMARK   3    ORIGIN FOR THE GROUP (A):  77.0410 -36.8840   7.9410
REMARK   3    T TENSOR
REMARK   3      T11:   0.1008 T22:   0.1423
REMARK   3      T33:   0.2030 T12:  -0.0409
REMARK   3      T13:   0.0186 T23:  -0.0018
REMARK   3    L TENSOR
REMARK   3      L11:   1.3730 L22:   1.7254
REMARK   3      L33:   0.4965 L12:   0.0698
REMARK   3      L13:   0.2455 L23:   0.0630
REMARK   3    S TENSOR
REMARK   3      S11:   0.0428 S12:  -0.0499 S13:  -0.0569
REMARK   3      S21:  -0.1049 S22:   0.0086 S23:  -0.5058
REMARK   3      S31:   0.0436 S32:   0.2069 S33:  -0.0515
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     2        E   216
REMARK   3    ORIGIN FOR THE GROUP (A):  39.1020 -38.1600  10.5660
REMARK   3    T TENSOR
REMARK   3      T11:   0.1062 T22:   0.1895
REMARK   3      T33:   0.1390 T12:  -0.0777
REMARK   3      T13:  -0.0053 T23:   0.1031
REMARK   3    L TENSOR
REMARK   3      L11:   1.0093 L22:   2.0520
REMARK   3      L33:   0.9436 L12:   0.2412
REMARK   3      L13:  -0.0537 L23:  -0.3683
REMARK   3    S TENSOR
REMARK   3      S11:   0.0346 S12:  -0.0864 S13:  -0.0891
REMARK   3      S21:  -0.0020 S22:   0.1788 S23:   0.4437
REMARK   3      S31:  -0.0346 S32:  -0.3151 S33:  -0.2134
REMARK   3
REMARK   3   TLS GROUP : 6
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   F     1        F   217
REMARK   3    ORIGIN FOR THE GROUP (A):  69.2180 -52.8680   3.8430
REMARK   3    T TENSOR
REMARK   3      T11:   0.3126 T22:   0.0302
REMARK   3      T33:   0.1511 T12:   0.0279
REMARK   3      T13:  -0.0034 T23:  -0.0342
REMARK   3    L TENSOR
REMARK   3      L11:   1.0071 L22:   1.6652
REMARK   3      L33:   0.6728 L12:   0.4665
REMARK   3      L13:   0.0088 L23:   0.3967
REMARK   3    S TENSOR
REMARK   3      S11:   0.0461 S12:  -0.0413 S13:  -0.2348
REMARK   3      S21:  -0.1981 S22:   0.0935 S23:  -0.2458
REMARK   3      S31:   0.3078 S32:   0.1235 S33:  -0.1396
REMARK   3
REMARK   3   TLS GROUP : 7
REMARK   3    NUMBER OF COMPONENTS GROUP : 6
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   231        A   235
REMARK   3    RESIDUE RANGE :   C   231        C   245
REMARK   3    RESIDUE RANGE :   B   231        B   242
REMARK   3    RESIDUE RANGE :   E   231        E   236
REMARK   3    RESIDUE RANGE :   D   231        D   237
REMARK   3    RESIDUE RANGE :   F   231        F   237
REMARK   3    ORIGIN FOR THE GROUP (A):  38.2480 -53.4270  14.8390
REMARK   3    T TENSOR
REMARK   3      T11:   0.1371 T22:   0.0855
REMARK   3      T33:   0.0947 T12:  -0.0174
REMARK   3      T13:  -0.0533 T23:   0.0679
REMARK   3    L TENSOR
REMARK   3      L11:   0.8089 L22:   0.5626
REMARK   3      L33:   0.1561 L12:   0.6343
REMARK   3      L13:  -0.2931 L23:  -0.1993
REMARK   3    S TENSOR
REMARK   3      S11:   0.0647 S12:  -0.0710 S13:  -0.0658
REMARK   3      S21:  -0.0007 S22:  -0.0648 S23:  -0.0609
REMARK   3      S31:  -0.0500 S32:  -0.0272 S33:   0.0001
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   : 1.40
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 3MF3 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-10.
REMARK 100 THE RCSB ID CODE IS RCSB058465.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-APR-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CHESS
REMARK 200  BEAMLINE                       : F1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95
REMARK 200  MONOCHROMATOR                  : COLLIMATING MIRROR
REMARK 200  OPTICS                         : COLLIMATING MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58139
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 122.463
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0
REMARK 200  DATA REDUNDANCY                : 4.100
REMARK 200  R MERGE                    (I) : 0.10300
REMARK 200  R SYM                      (I) : 0.10300
REMARK 200   FOR THE DATA SET  : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.42100
REMARK 200  R SYM FOR SHELL            (I) : 0.42100
REMARK 200   FOR SHELL         : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2A8C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 56.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE,    0.1 M TRIS-
REMARK 280  CL, 0.1 M AMMONIUM SULFATE, 27% PEG 4,000, PH 8.5, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K
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      114.74600
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.46450
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      114.74600
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       72.46450
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: 16510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.0 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       -3.43321
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       52.10201
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: 18000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -165.0 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     MET A     1
REMARK 465     GLU C   218
REMARK 465     ASN C   219
REMARK 465     ILE C   220
REMARK 465     LEU C   221
REMARK 465     MET D     1
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     MET E     1
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     GLU F   218
REMARK 465     ASN F   219
REMARK 465     ILE F   220
REMARK 465     LEU F   221
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     GLU B  20    CG   CD   OE1  OE2
REMARK 470     GLU B  21    CG   CD   OE1  OE2
REMARK 470     ASN D  22    CG   OD1
REMARK 470     GLU E  21    CG   CD   OE1  OE2
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   CG   GLU F    91     O    HOH F   249              2.19
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 A 101   CB    CYS A 101   SG      0.104
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    ARG A 160   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ARG B 160   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ARG B 198   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.8 DEGREES
REMARK 500    ARG D 160   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES
REMARK 500    ARG D 160   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 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    ARG A  17      -35.07    -35.46
REMARK 500    ASN A  54       49.82     34.36
REMARK 500    GLU B  20       64.47    -63.96
REMARK 500    GLU B  21       10.34    168.25
REMARK 500    ASN B  22       69.47     21.20
REMARK 500    ASP B 185      -23.37   -142.67
REMARK 500    ARG C  17       23.01    -58.03
REMARK 500    MET C  18      -31.84   -147.82
REMARK 500    THR C  24       27.48    -64.15
REMARK 500    THR D  24       49.08   -102.53
REMARK 500    GLU D  28       32.32    -70.35
REMARK 500    LEU D  29      -32.08   -146.30
REMARK 500    VAL D  87      -53.98   -122.92
REMARK 500    ASP D 185        2.91   -159.44
REMARK 500    GLU E  21       -9.58   -158.45
REMARK 500    ARG E  46      -70.23    -70.72
REMARK 500    ASP E 185      -11.83   -145.74
REMARK 500    MET E 194       46.05   -152.21
REMARK 500    HIS F  32       59.91   -115.60
REMARK 500    SER F 138      130.89    -36.81
REMARK 500    ASP F 185        1.35   -171.65
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                              CO A 230  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  98   NE2
REMARK 620 2 ASP A  44   OD1 124.1
REMARK 620 3 HIS A  98   CE1  30.1  96.7
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CO B 230  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B  44   OD2
REMARK 620 2 HIS B  98   NE2 110.3
REMARK 620 3 HIS B  98   CE1  90.0  25.6
REMARK 620 4 ASP B  44   CG   18.9  98.0  83.0
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CO E 230  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E  44   OD2
REMARK 620 2 HIS E  98   CE1 100.2
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CO C 230  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C  44   OD2
REMARK 620 2 HIS C  98   NE2 112.2
REMARK 620 3 HIS C  98   CE1  87.4  29.0
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CO F 230  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F  44   OD2
REMARK 620 2 HIS F  98   NE2 108.9
REMARK 620 3 ASP F  44   CG   23.0  99.5
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CO D 230  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D  98   NE2
REMARK 620 2 ASP D  44   OD2 109.5
REMARK 620 N                    1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO B 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO C 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO D 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO E 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO F 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 222
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 222
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 222
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 222
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2A8C   RELATED DB: PDB
REMARK 900 ZN(II) BOUND HAEMOPHILUS INFLUENZAE B-CARBONIC ANHYDRASE
DBREF  3MF3 A    1   221  UNP    P45148   CAN_HAEIN        1    221
DBREF  3MF3 B    1   221  UNP    P45148   CAN_HAEIN        1    221
DBREF  3MF3 C    1   221  UNP    P45148   CAN_HAEIN        1    221
DBREF  3MF3 D    1   221  UNP    P45148   CAN_HAEIN        1    221
DBREF  3MF3 E    1   221  UNP    P45148   CAN_HAEIN        1    221
DBREF  3MF3 F    1   221  UNP    P45148   CAN_HAEIN        1    221
SEQRES   1 A  221  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 A  221  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 A  221  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 A  221  ILE GLY CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 A  221  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 A  221  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 A  221  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 A  221  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 A  221  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 A  221  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 A  221  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 A  221  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 A  221  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 A  221  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES  15 A  221  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 A  221  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 A  221  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES   1 B  221  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 B  221  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 B  221  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 B  221  ILE GLY CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 B  221  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 B  221  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 B  221  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 B  221  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 B  221  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 B  221  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 B  221  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 B  221  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 B  221  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 B  221  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES  15 B  221  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 B  221  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 B  221  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES   1 C  221  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 C  221  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 C  221  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 C  221  ILE GLY CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 C  221  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 C  221  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 C  221  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 C  221  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 C  221  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 C  221  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 C  221  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 C  221  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 C  221  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 C  221  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES  15 C  221  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 C  221  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 C  221  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES   1 D  221  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 D  221  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 D  221  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 D  221  ILE GLY CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 D  221  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 D  221  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 D  221  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 D  221  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 D  221  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 D  221  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 D  221  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 D  221  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 D  221  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 D  221  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES  15 D  221  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 D  221  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 D  221  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES   1 E  221  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 E  221  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 E  221  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 E  221  ILE GLY CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 E  221  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 E  221  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 E  221  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 E  221  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 E  221  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 E  221  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 E  221  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 E  221  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 E  221  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 E  221  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES  15 E  221  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 E  221  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 E  221  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES   1 F  221  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 F  221  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 F  221  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 F  221  ILE GLY CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 F  221  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 F  221  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 F  221  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 F  221  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 F  221  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 F  221  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 F  221  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 F  221  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 F  221  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 F  221  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES  15 F  221  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 F  221  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 F  221  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
HET     CO  A 230       1
HET    ACT  A 222       4
HET     CO  B 230       1
HET    ACT  B 222       4
HET     CO  C 230       1
HET    ACT  D 222       4
HET     CO  D 230       1
HET    ACT  E 222       4
HET     CO  E 230       1
HET     CO  F 230       1
HETNAM      CO COBALT (II) ION
HETNAM     ACT ACETATE ION
FORMUL   7   CO    6(CO 2+)
FORMUL   8  ACT    4(C2 H3 O2 1-)
FORMUL  17  HOH   *204(H2 O)
HELIX    1   1 ASP A    2  GLU A   20  1                                  19
HELIX    2   2 SER A   23  ASP A   31  1                                   9
HELIX    3   3 PRO A   48  ASN A   54  1                                   7
HELIX    4   4 ASP A   74  VAL A   87  1                                  14
HELIX    5   5 CYS A  101  ALA A  109  1                                   9
HELIX    6   6 GLY A  114  HIS A  130  1                                  17
HELIX    7   7 HIS A  130  LYS A  136  1                                   7
HELIX    8   8 SER A  138  GLU A  140  5                                   3
HELIX    9   9 LYS A  141  ARG A  160  1                                  20
HELIX   10  10 THR A  161  ARG A  170  1                                  10
HELIX   11  11 SER A  197  SER A  213  1                                  17
HELIX   12  12 MET B    1  GLU B   20  1                                  20
HELIX   13  13 THR B   24  HIS B   32  1                                   9
HELIX   14  14 PRO B   48  ASN B   54  1                                   7
HELIX   15  15 ASP B   74  VAL B   87  1                                  14
HELIX   16  16 CYS B  101  ALA B  109  1                                   9
HELIX   17  17 GLY B  114  HIS B  130  1                                  17
HELIX   18  18 HIS B  130  LYS B  136  1                                   7
HELIX   19  19 LEU B  137  GLU B  140  5                                   4
HELIX   20  20 LYS B  141  GLY B  159  1                                  19
HELIX   21  21 THR B  161  ARG B  170  1                                  10
HELIX   22  22 SER B  197  ILE B  214  1                                  18
HELIX   23  23 ASP C    2  GLU C   20  1                                  19
HELIX   24  24 THR C   24  HIS C   32  1                                   9
HELIX   25  25 PRO C   48  ASN C   54  1                                   7
HELIX   26  26 ASP C   74  VAL C   87  1                                  14
HELIX   27  27 CYS C  101  ALA C  109  1                                   9
HELIX   28  28 GLY C  114  HIS C  130  1                                  17
HELIX   29  29 HIS C  130  LYS C  136  1                                   7
HELIX   30  30 SER C  138  GLU C  140  5                                   3
HELIX   31  31 LYS C  141  ARG C  160  1                                  20
HELIX   32  32 THR C  161  ARG C  170  1                                  10
HELIX   33  33 SER C  197  ILE C  214  1                                  18
HELIX   34  34 ASP D    2  GLU D   21  1                                  20
HELIX   35  35 PHE D   26  ASP D   31  1                                   6
HELIX   36  36 PRO D   48  ASN D   54  1                                   7
HELIX   37  37 ASP D   74  VAL D   87  1                                  14
HELIX   38  38 CYS D  101  ALA D  109  1                                   9
HELIX   39  39 GLY D  114  HIS D  130  1                                  17
HELIX   40  40 HIS D  130  LYS D  136  1                                   7
HELIX   41  41 SER D  138  THR D  161  1                                  24
HELIX   42  42 THR D  161  ARG D  170  1                                  10
HELIX   43  43 SER D  197  SER D  213  1                                  17
HELIX   44  44 ASP E    2  GLU E   20  1                                  19
HELIX   45  45 THR E   24  HIS E   32  1                                   9
HELIX   46  46 PRO E   48  ASN E   54  1                                   7
HELIX   47  47 ASP E   74  VAL E   87  1                                  14
HELIX   48  48 CYS E  101  ALA E  109  1                                   9
HELIX   49  49 GLY E  114  HIS E  130  1                                  17
HELIX   50  50 HIS E  130  LEU E  137  1                                   8
HELIX   51  51 LYS E  141  THR E  161  1                                  21
HELIX   52  52 THR E  161  ARG E  170  1                                  10
HELIX   53  53 SER E  197  SER E  213  1                                  17
HELIX   54  54 MET F    1  GLU F   21  1                                  21
HELIX   55  55 THR F   24  ASP F   31  1                                   8
HELIX   56  56 PRO F   48  ASN F   54  1                                   7
HELIX   57  57 ASP F   74  VAL F   87  1                                  14
HELIX   58  58 CYS F  101  ALA F  109  1                                   9
HELIX   59  59 LEU F  115  HIS F  130  1                                  16
HELIX   60  60 HIS F  130  LYS F  136  1                                   7
HELIX   61  61 LEU F  137  GLU F  140  5                                   4
HELIX   62  62 LYS F  141  GLY F  159  1                                  19
HELIX   63  63 THR F  161  ARG F  170  1                                  10
HELIX   64  64 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  LEU A  38
SHEET    4   A 5 SER A 175  TYR A 181  1  O  TRP A 179   N  GLY A  97
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  TYR B  37   O  PHE B  61
SHEET    3   B 5 HIS B  92  HIS B  98  1  O  CYS B  96   N  ILE B  40
SHEET    4   B 5 SER B 175  TYR B 181  1  O  TRP B 179   N  GLY B  97
SHEET    5   B 5 LEU B 188  ALA B 195 -1  O  VAL B 189   N  VAL B 180
SHEET    1   C 5 LEU C  60  ASN C  65  0
SHEET    2   C 5 TYR C  37  CYS C  42  1  N  TRP C  39   O  PHE C  61
SHEET    3   C 5 HIS C  92  HIS C  98  1  O  ILE C  94   N  LEU C  38
SHEET    4   C 5 SER C 175  TYR 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  TYR D 181  1  O  HIS D 177   N  ILE D  95
SHEET    5   D 5 LEU D 188  ALA D 195 -1  O  GLN D 191   N  GLY D 178
SHEET    1   E 5 LEU E  60  ASN E  65  0
SHEET    2   E 5 TYR E  37  CYS E  42  1  N  TRP E  39   O  PHE E  61
SHEET    3   E 5 HIS E  92  HIS E  98  1  O  ILE E  94   N  LEU E  38
SHEET    4   E 5 SER E 175  TYR E 181  1  O  HIS E 177   N  ILE E  95
SHEET    5   E 5 LEU E 188  ASP E 190 -1  O  VAL E 189   N  VAL E 180
SHEET    1   F 5 LEU F  60  ASN F  65  0
SHEET    2   F 5 TYR F  37  CYS F  42  1  N  TYR F  37   O  PHE F  61
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  TYR F 181  1  O  HIS F 177   N  ILE F  95
SHEET    5   F 5 LEU F 188  ALA F 195 -1  O  VAL F 189   N  VAL F 180
LINK         NE2 HIS A  98                CO    CO A 230     1555   1555  1.70
LINK         OD2 ASP B  44                CO    CO B 230     1555   1555  1.75
LINK         OD2 ASP E  44                CO    CO E 230     1555   1555  1.78
LINK         OD2 ASP C  44                CO    CO C 230     1555   1555  1.87
LINK         NE2 HIS B  98                CO    CO B 230     1555   1555  1.90
LINK         OD2 ASP F  44                CO    CO F 230     1555   1555  1.93
LINK         NE2 HIS C  98                CO    CO C 230     1555   1555  1.97
LINK         NE2 HIS D  98                CO    CO D 230     1555   1555  1.98
LINK         CE1 HIS E  98                CO    CO E 230     1555   1555  2.01
LINK         OD1 ASP A  44                CO    CO A 230     1555   1555  2.09
LINK         NE2 HIS F  98                CO    CO F 230     1555   1555  2.11
LINK         OD2 ASP D  44                CO    CO D 230     1555   1555  2.12
LINK         CE1 HIS A  98                CO    CO A 230     1555   1555  2.49
LINK         CE1 HIS C  98                CO    CO C 230     1555   1555  2.64
LINK         CE1 HIS B  98                CO    CO B 230     1555   1555  2.75
LINK         CG  ASP F  44                CO    CO F 230     1555   1555  2.77
LINK         CG  ASP B  44                CO    CO B 230     1555   1555  2.79
SITE     1 AC1  4 CYS A  42  ASP A  44  HIS A  98  CYS A 101
SITE     1 AC2  4 CYS B  42  ASP B  44  HIS B  98  CYS B 101
SITE     1 AC3  4 CYS C  42  ASP C  44  HIS C  98  CYS C 101
SITE     1 AC4  4 CYS D  42  ASP D  44  HIS D  98  CYS D 101
SITE     1 AC5  4 CYS E  42  ASP E  44  HIS E  98  CYS E 101
SITE     1 AC6  4 CYS F  42  ASP F  44  HIS F  98  CYS F 101
SITE     1 AC7 10 THR C  73  ASP C  74  PHE C  75  ACT D 222
SITE     2 AC7 10 HOH D 238  THR E  73  ASP E  74  PHE E  75
SITE     3 AC7 10 ASN E  76  HOH E 246
SITE     1 AC8  8 THR D  73  ASP D  74  PHE D  75  ACT E 222
SITE     2 AC8  8 HOH E 246  THR F  73  ASP F  74  PHE F  75
SITE     1 AC9  6 ACT A 222  HOH A 250  THR B  73  ASP B  74
SITE     2 AC9  6 PHE B  75  ASN B  76
SITE     1 BC1  6 THR A  73  ASP A  74  PHE A  75  HOH A 250
SITE     2 BC1  6 ACT B 222  HOH B 229
CRYST1  229.492  144.929   52.215  90.00  93.77  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      0.004357  0.000000  0.000287        0.00000
SCALE2      0.000000  0.006900  0.000000        0.00000
SCALE3      0.000000  0.000000  0.019193        0.00000
      
PROCHECK
Go to PROCHECK summary
 References