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PDBsum entry 3e31

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Top Page protein metals Protein-protein interface(s) links
Lyase PDB id
3e31
Jmol
Contents
Protein chains
183 a.a.
Metals
_ZN ×2
Waters ×16
HEADER    LYASE                                   05-AUG-08   3E31
TITLE     H. INFLUENZAE BETA-CARBONIC ANHYDRASE, VARIANT V47A
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A, B;
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 3E31    1       VERSN
REVDAT   2   26-MAY-10 3E31    1       JRNL
REVDAT   1   18-AUG-09 3E31    0
JRNL        AUTH   R.S.ROWLETT,K.M.HOFFMANN,H.FAILING,M.M.MYSLIWIEC,D.SAMARDZIC
JRNL        TITL   EVIDENCE FOR A BICARBONATE "ESCORT" SITE IN HAEMOPHILUS
JRNL        TITL 2 INFLUENZAE BETA-CARBONIC ANHYDRASE .
JRNL        REF    BIOCHEMISTRY                  V.  49  3640 2010
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   20359198
JRNL        DOI    10.1021/BI100328J
REMARK   2
REMARK   2 RESOLUTION.    2.95 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) : 2.95
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.72
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9
REMARK   3   NUMBER OF REFLECTIONS             : 14323
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) : 0.199
REMARK   3   R VALUE            (WORKING SET) : 0.197
REMARK   3   FREE R VALUE                     : 0.247
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 718
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) : 2.95
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.03
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 975
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2690
REMARK   3   BIN FREE R VALUE SET COUNT          : 57
REMARK   3   BIN FREE R VALUE                    : 0.3090
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2887
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 16
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.86
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.17000
REMARK   3    B22 (A**2) : -0.17000
REMARK   3    B33 (A**2) : 0.34000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.716
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.342
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.254
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.379
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950
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):  2959 ; 0.016 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  1953 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4009 ; 1.588 ; 1.930
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4754 ; 0.959 ; 3.002
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   362 ; 8.179 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   137 ;40.726 ;23.869
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   506 ;19.848 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;18.289 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   453 ; 0.086 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3272 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   598 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   838 ; 0.275 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2122 ; 0.207 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1467 ; 0.200 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1636 ; 0.095 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   106 ; 0.200 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.024 ; 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):    22 ; 0.207 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    29 ; 0.339 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.274 ; 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):  2268 ; 1.069 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   744 ; 0.113 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2900 ; 1.256 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1344 ; 1.736 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1109 ; 2.404 ; 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  : 2
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    33        A   215
REMARK   3    ORIGIN FOR THE GROUP (A): -25.3520 -13.2860 -16.8730
REMARK   3    T TENSOR
REMARK   3      T11:   0.2971 T22:   0.1194
REMARK   3      T33:   0.3651 T12:   0.0245
REMARK   3      T13:  -0.0718 T23:  -0.0644
REMARK   3    L TENSOR
REMARK   3      L11:   3.1950 L22:   2.7876
REMARK   3      L33:   4.0689 L12:   0.9211
REMARK   3      L13:   1.1636 L23:   1.0124
REMARK   3    S TENSOR
REMARK   3      S11:   0.1557 S12:  -0.0133 S13:   0.0258
REMARK   3      S21:  -0.5142 S22:  -0.3375 S23:   0.1654
REMARK   3      S31:  -0.3817 S32:  -0.2991 S33:   0.1819
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    34        B   214
REMARK   3    ORIGIN FOR THE GROUP (A): -27.5000  -2.4660   7.0700
REMARK   3    T TENSOR
REMARK   3      T11:   0.1903 T22:   0.1376
REMARK   3      T33:   0.4278 T12:  -0.0374
REMARK   3      T13:  -0.0297 T23:  -0.0764
REMARK   3    L TENSOR
REMARK   3      L11:   3.7839 L22:   4.4288
REMARK   3      L33:   3.5860 L12:   1.6683
REMARK   3      L13:  -0.3961 L23:   1.4514
REMARK   3    S TENSOR
REMARK   3      S11:   0.0468 S12:  -0.3800 S13:   0.3096
REMARK   3      S21:  -0.2769 S22:  -0.0702 S23:   0.5177
REMARK   3      S31:  -0.4967 S32:  -0.0829 S33:   0.0234
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 3E31 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 RCSB048811.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-07
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CHESS
REMARK 200  BEAMLINE                       : F2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.974
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14391
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.950
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.770
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 16.800
REMARK 200  R MERGE                    (I) : 0.08200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 34.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.49300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 5.800
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 2A8D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 59.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 0.7 SODIUM POTASSIUM
REMARK 280  TARTRATE, 12 MG/ML PROTEIN, PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280  DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z+1/2
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       94.39150
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       41.13850
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       41.13850
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       47.19575
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       41.13850
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       41.13850
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      141.58725
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       41.13850
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       41.13850
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       47.19575
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       41.13850
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       41.13850
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      141.58725
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       94.39150
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: 9530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 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  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  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     ASP A     2
REMARK 465     LYS A     3
REMARK 465     ILE A     4
REMARK 465     LYS A     5
REMARK 465     GLN A     6
REMARK 465     LEU A     7
REMARK 465     PHE A     8
REMARK 465     ALA A     9
REMARK 465     ASN A    10
REMARK 465     ASN A    11
REMARK 465     TYR A    12
REMARK 465     SER A    13
REMARK 465     TRP A    14
REMARK 465     ALA A    15
REMARK 465     GLN A    16
REMARK 465     ARG A    17
REMARK 465     MET A    18
REMARK 465     LYS A    19
REMARK 465     GLU A    20
REMARK 465     GLU A    21
REMARK 465     ASN A    22
REMARK 465     SER A    23
REMARK 465     THR A    24
REMARK 465     TYR A    25
REMARK 465     PHE A    26
REMARK 465     LYS A    27
REMARK 465     GLU A    28
REMARK 465     LEU A    29
REMARK 465     ALA A    30
REMARK 465     ASP A    31
REMARK 465     HIS A    32
REMARK 465     ASP A   216
REMARK 465     GLU A   217
REMARK 465     GLU A   218
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     1
REMARK 465     ASP B     2
REMARK 465     LYS B     3
REMARK 465     ILE B     4
REMARK 465     LYS B     5
REMARK 465     GLN B     6
REMARK 465     LEU B     7
REMARK 465     PHE B     8
REMARK 465     ALA B     9
REMARK 465     ASN B    10
REMARK 465     ASN B    11
REMARK 465     TYR B    12
REMARK 465     SER B    13
REMARK 465     TRP B    14
REMARK 465     ALA B    15
REMARK 465     GLN B    16
REMARK 465     ARG B    17
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     LEU B   215
REMARK 465     ASP B   216
REMARK 465     GLU B   217
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 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   O    SER B   213     O    HOH B   235              1.85
REMARK 500   O    PRO A    48     O    GLU A    50              2.11
REMARK 500   OE2  GLU A    50     O    HOH A   235              2.17
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 B  42   CB    CYS B  42   SG     -0.097
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    THR A  34      138.77     92.91
REMARK 500    ASP A  44       51.81    -60.90
REMARK 500    SER A  45       28.15     34.65
REMARK 500    PRO A  48       91.15    -57.02
REMARK 500    ALA A  49      -80.86    -44.65
REMARK 500    GLU A  50      123.49    -21.51
REMARK 500    LYS A  51      -48.11     88.31
REMARK 500    THR A  53      -68.94    -90.49
REMARK 500    ASN A  54       77.21     62.58
REMARK 500    GLU A  56       91.13     10.21
REMARK 500    GLU A  59       69.54   -109.70
REMARK 500    LEU A  60       99.96   -164.38
REMARK 500    VAL A  85      -72.27    -74.70
REMARK 500    VAL A  87      -79.97    -75.13
REMARK 500    LEU A  88       -9.93    -58.46
REMARK 500    LEU A 113       34.61    -95.92
REMARK 500    LYS A 136       79.93   -169.06
REMARK 500    SER A 138      113.85    -39.13
REMARK 500    VAL A 189       77.32    -64.53
REMARK 500    GLN A 191       95.77    -41.73
REMARK 500    ASP B  44        3.41    -61.79
REMARK 500    SER B  45      -20.37     79.45
REMARK 500    GLU B  50      -53.56    -18.36
REMARK 500    LEU B  52      -59.68    -17.38
REMARK 500    ASN B  54       44.54     92.38
REMARK 500    LEU B  55      -87.82   -123.39
REMARK 500    GLU B  56      167.22    174.70
REMARK 500    ASN B 100       89.52     13.15
REMARK 500    HIS B 130       42.97    -98.69
REMARK 500    LYS B 136       68.22    -45.52
REMARK 500    LEU B 137      162.08    178.61
REMARK 500    ALA B 143      -66.55     -5.50
REMARK 500    LEU B 188     -178.84    -63.23
REMARK 500    VAL B 189      111.65   -162.29
REMARK 500    MET B 194      118.24   -178.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 ALA A   49     GLU A   50                  142.38
REMARK 500 ASP A  190     GLN A  191                  147.52
REMARK 500 GLY B  192     VAL B  193                  143.86
REMARK 500 SER B  213     ILE B  214                  148.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A  42   SG
REMARK 620 2 ASP A  44   OD2  96.7
REMARK 620 3 HIS A  98   NE2 106.9 120.5
REMARK 620 4 CYS A 101   SG  131.7  89.8 110.5
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 101.3
REMARK 620 3 HIS B  98   NE2  95.3 103.8
REMARK 620 4 CYS B 101   SG  134.2 102.2 116.2
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 ZN B 230
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: 3E2W   RELATED DB: PDB
REMARK 900 RELATED ID: 3E2X   RELATED DB: PDB
DBREF  3E31 A    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E31 B    1   229  UNP    P45148   CAN_HAEIN        1    229
SEQADV 3E31 ALA A   47  UNP  P45148    VAL    47 ENGINEERED
SEQADV 3E31 ALA B   47  UNP  P45148    VAL    47 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 ALA 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 TYR 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 ALA 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 TYR 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
HET     ZN  A 230       1
HET     ZN  B 230       1
HETNAM      ZN ZINC ION
FORMUL   3   ZN    2(ZN 2+)
FORMUL   5  HOH   *16(H2 O)
HELIX    1   1 PRO A   48  THR A   53  1                                   6
HELIX    2   2 VAL A   66  GLN A   69  5                                   4
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  GLY A  135  1                                   6
HELIX    7   7 SER A  138  ARG A  160  1                                  23
HELIX    8   8 THR A  161  ARG A  170  1                                  10
HELIX    9   9 SER A  197  SER A  213  1                                  17
HELIX   10  10 PRO B   48  THR B   53  1                                   6
HELIX   11  11 ASP B   74  VAL B   87  1                                  14
HELIX   12  12 CYS B  101  ALA B  109  1                                   9
HELIX   13  13 GLY B  114  HIS B  130  1                                  17
HELIX   14  14 HIS B  130  LYS B  136  1                                   7
HELIX   15  15 SER B  138  GLY B  159  1                                  22
HELIX   16  16 THR B  161  ARG B  170  1                                  10
HELIX   17  17 SER B  197  LEU B  212  1                                  16
SHEET    1   A 5 PHE A  61  ASN A  65  0
SHEET    2   A 5 LEU A  38  CYS A  42  1  N  TRP A  39   O  PHE A  61
SHEET    3   A 5 HIS A  92  HIS A  98  1  O  HIS A  92   N  LEU A  38
SHEET    4   A 5 SER A 175  ASP A 182  1  O  HIS A 177   N  ILE A  95
SHEET    5   A 5 GLY A 186  PHE A 187 -1  O  GLY A 186   N  ASP A 182
SHEET    1   B 5 PHE A  61  ASN A  65  0
SHEET    2   B 5 LEU A  38  CYS A  42  1  N  TRP A  39   O  PHE A  61
SHEET    3   B 5 HIS A  92  HIS A  98  1  O  HIS A  92   N  LEU A  38
SHEET    4   B 5 SER A 175  ASP A 182  1  O  HIS A 177   N  ILE A  95
SHEET    5   B 5 VAL A 193  ALA A 195 -1  O  ALA A 195   N  LEU A 176
SHEET    1   C 5 LEU B  60  ARG B  64  0
SHEET    2   C 5 TYR B  37  GLY B  41  1  N  TRP B  39   O  PHE B  61
SHEET    3   C 5 HIS B  92  HIS B  98  1  O  ILE B  94   N  LEU B  38
SHEET    4   C 5 SER B 175  TYR B 181  1  O  TRP B 179   N  GLY B  97
SHEET    5   C 5 ASP B 190  ALA B 195 -1  O  ALA B 195   N  LEU B 176
LINK         SG  CYS A  42                ZN    ZN A 230     1555   1555  2.33
LINK         OD2 ASP A  44                ZN    ZN A 230     1555   1555  2.00
LINK         NE2 HIS A  98                ZN    ZN A 230     1555   1555  2.09
LINK         SG  CYS A 101                ZN    ZN A 230     1555   1555  2.30
LINK         SG  CYS B  42                ZN    ZN B 230     1555   1555  2.33
LINK         OD2 ASP B  44                ZN    ZN B 230     1555   1555  1.98
LINK         NE2 HIS B  98                ZN    ZN B 230     1555   1555  2.10
LINK         SG  CYS B 101                ZN    ZN B 230     1555   1555  2.27
SITE     1 AC1  4 CYS A  42  ASP A  44  HIS A  98  CYS A 101
SITE     1 AC2  4 CYS B  42  ASP B  44  HIS B  98  CYS B 101
CRYST1   82.277   82.277  188.783  90.00  90.00  90.00 P 41 21 2    16
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      0.012154  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012154  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005297        0.00000
      
PROCHECK
Go to PROCHECK summary
 References