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PDBsum entry 3e1v

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Top Page protein metals Protein-protein interface(s) links
Lyase PDB id
3e1v
Jmol
Contents
Protein chains
182 a.a.
Metals
_ZN ×2
Waters ×21
HEADER    LYASE                                   04-AUG-08   3E1V
TITLE     H. INFLUENZAE BETA-CARBONIC ANHYDRASE, VARIANT D44N
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, ACTIVE SITE MUTANT, LYASE, METAL-BINDING
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.S.ROWLETT,D.A.CHAPNICK,S.SHAH
REVDAT   3   13-JUL-11 3E1V    1       VERSN
REVDAT   2   14-JUL-09 3E1V    1       JRNL
REVDAT   1   02-JUN-09 3E1V    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.    2.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
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) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.84
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1
REMARK   3   NUMBER OF REFLECTIONS             : 16044
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) : 0.196
REMARK   3   R VALUE            (WORKING SET) : 0.194
REMARK   3   FREE R VALUE                     : 0.233
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 812
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) : 2.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1043
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.45
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2440
REMARK   3   BIN FREE R VALUE SET COUNT          : 70
REMARK   3   BIN FREE R VALUE                    : 0.2570
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2890
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 21
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) : 39.56
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.19000
REMARK   3    B22 (A**2) : 0.19000
REMARK   3    B33 (A**2) : -0.38000
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): 0.502
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.292
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.209
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.129
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.930
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.899
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2960 ; 0.012 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  1954 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4014 ; 1.349 ; 1.930
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4758 ; 0.875 ; 3.002
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   362 ; 7.186 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   136 ;40.516 ;23.824
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   508 ;19.228 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;21.982 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   456 ; 0.067 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3268 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   598 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   775 ; 0.232 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2115 ; 0.204 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1436 ; 0.186 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1583 ; 0.091 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    79 ; 0.183 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):     3 ; 0.076 ; 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):    24 ; 0.179 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    36 ; 0.328 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.279 ; 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):  2326 ; 0.714 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   744 ; 0.082 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2904 ; 0.843 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1340 ; 1.062 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1110 ; 1.677 ; 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    34        A   215
REMARK   3    ORIGIN FOR THE GROUP (A):  65.6950  53.9650 171.0400
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1555 T22:  -0.1974
REMARK   3      T33:  -0.0179 T12:  -0.0134
REMARK   3      T13:   0.0326 T23:   0.0357
REMARK   3    L TENSOR
REMARK   3      L11:   3.0411 L22:   3.2294
REMARK   3      L33:   3.4504 L12:   0.1905
REMARK   3      L13:  -0.7111 L23:  -1.0981
REMARK   3    S TENSOR
REMARK   3      S11:   0.0749 S12:   0.3821 S13:   0.0167
REMARK   3      S21:  -0.3922 S22:  -0.1149 S23:  -0.1057
REMARK   3      S31:   0.3283 S32:   0.0512 S33:   0.0400
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   215
REMARK   3    ORIGIN FOR THE GROUP (A):  68.0460  43.2020 194.6210
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0596 T22:  -0.2840
REMARK   3      T33:   0.0721 T12:   0.0091
REMARK   3      T13:  -0.0060 T23:   0.0451
REMARK   3    L TENSOR
REMARK   3      L11:   2.7702 L22:   3.7708
REMARK   3      L33:   3.6716 L12:   0.2561
REMARK   3      L13:   0.2648 L23:  -0.7848
REMARK   3    S TENSOR
REMARK   3      S11:   0.0749 S12:  -0.0962 S13:  -0.2153
REMARK   3      S21:   0.0955 S22:  -0.0139 S23:  -0.3827
REMARK   3      S31:   0.5730 S32:   0.3579 S33:  -0.0610
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 3E1V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-08.
REMARK 100 THE RCSB ID CODE IS RCSB048769.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 13-JAN-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : SEALED TUBE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : OXFORD DIFFRACTION ENHANCE ULTRA
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : OXFORD ONYX CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16060
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 74.824
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5
REMARK 200  DATA REDUNDANCY                : 10.100
REMARK 200  R MERGE                    (I) : 0.09000
REMARK 200  R SYM                      (I) : 0.09000
REMARK 200   FOR THE DATA SET  : 19.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.4
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.34100
REMARK 200  R SYM FOR SHELL            (I) : 0.34100
REMARK 200   FOR SHELL         : 2.300
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   (%): 58.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES, 0.8 M SODIUM ACETATE, PH
REMARK 280  6.5, VAPOR DIFFUSION, HANGING 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       93.92300
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       40.78700
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       40.78700
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       46.96150
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       40.78700
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       40.78700
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      140.88450
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       40.78700
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       40.78700
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       46.96150
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       40.78700
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       40.78700
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      140.88450
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       93.92300
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: 9810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 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      375.69200
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 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     GLN A    33
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     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   162     OG   SER B   166              2.11
REMARK 500   O    GLY B   178     O    ASP B   190              2.16
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    GLN A 191   CB  -  CA  -  C   ANGL. DEV. = -13.2 DEGREES
REMARK 500    GLY A 192   N   -  CA  -  C   ANGL. DEV. =  18.3 DEGREES
REMARK 500    ASP B 185   CB  -  CA  -  C   ANGL. DEV. = -14.7 DEGREES
REMARK 500    ASP B 185   N   -  CA  -  C   ANGL. DEV. =  17.4 DEGREES
REMARK 500    VAL B 189   N   -  CA  -  C   ANGL. DEV. = -27.9 DEGREES
REMARK 500    ASP B 190   CB  -  CA  -  C   ANGL. DEV. = -25.6 DEGREES
REMARK 500    ASP B 190   N   -  CA  -  C   ANGL. DEV. = -32.1 DEGREES
REMARK 500    GLN B 191   CB  -  CA  -  C   ANGL. DEV. =  23.2 DEGREES
REMARK 500    GLY B 192   C   -  N   -  CA  ANGL. DEV. =  25.6 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    HIS A  36      -13.60   -143.06
REMARK 500    ASN A  44      129.55    -34.53
REMARK 500    ASP A 185      -23.69   -168.48
REMARK 500    GLN A 191       14.18     85.56
REMARK 500    MET A 194      107.23   -176.53
REMARK 500    PRO B 139       52.57    -64.97
REMARK 500    GLU B 140      -43.37   -164.18
REMARK 500    ASP B 185      -31.39   -155.57
REMARK 500    GLN B 191      155.90     68.79
REMARK 500    ILE B 214       88.52   -152.44
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 GLN A  191     GLY A  192                 -146.46
REMARK 500 GLN B  191     GLY B  192                  136.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    ASN B  68        23.5      L          L   OUTSIDE RANGE
REMARK 500    ASP B 185        24.7      L          L   OUTSIDE RANGE
REMARK 500    VAL B 189        46.6      L          L   OUTSIDE RANGE
REMARK 500    GLN B 191        12.1      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A  42   SG
REMARK 620 2 HIS A  98   NE2  97.9
REMARK 620 3 CYS A 101   SG  118.6 102.1
REMARK 620 N                    1     2
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 HIS B  98   NE2 103.2
REMARK 620 3 CYS B 101   SG  116.4 100.1
REMARK 620 N                    1     2
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: 3E1W   RELATED DB: PDB
DBREF  3E1V A    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E1V B    1   229  UNP    P45148   CAN_HAEIN        1    229
SEQADV 3E1V ASN A   44  UNP  P45148    ASP    44 ENGINEERED
SEQADV 3E1V ASN B   44  UNP  P45148    ASP    44 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 ASN 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 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 ASN 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 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   *21(H2 O)
HELIX    1   1 PRO A   48  THR A   53  1                                   6
HELIX    2   2 ASP A   74  ASP A   86  1                                  13
HELIX    3   3 CYS A  101  ALA A  109  1                                   9
HELIX    4   4 GLY A  114  HIS A  130  1                                  17
HELIX    5   5 HIS A  130  LEU A  137  1                                   8
HELIX    6   6 SER A  138  GLU A  140  5                                   3
HELIX    7   7 LYS A  141  THR A  161  1                                  21
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 VAL B   66  GLN B   69  5                                   4
HELIX   12  12 ASP B   74  ASP B   86  1                                  13
HELIX   13  13 CYS B  101  ALA B  109  1                                   9
HELIX   14  14 LEU B  115  HIS B  130  1                                  16
HELIX   15  15 HIS B  130  LEU B  137  1                                   8
HELIX   16  16 GLU B  140  THR B  161  1                                  22
HELIX   17  17 THR B  161  ARG B  170  1                                  10
HELIX   18  18 SER B  197  SER B  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  HIS A  63
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  ASP A 182  1  O  HIS A 177   N  ILE A  93
SHEET    5   A 5 GLY A 186  PHE A 187 -1  O  GLY A 186   N  ASP A 182
SHEET    1   B 5 LEU A  60  ASN A  65  0
SHEET    2   B 5 TYR A  37  CYS A  42  1  N  TRP A  39   O  HIS A  63
SHEET    3   B 5 HIS A  92  HIS A  98  1  O  ILE A  94   N  ILE A  40
SHEET    4   B 5 SER A 175  ASP A 182  1  O  HIS A 177   N  ILE A  93
SHEET    5   B 5 MET A 194  ALA A 195 -1  O  ALA A 195   N  LEU A 176
SHEET    1   C 5 LEU B  60  ASN B  65  0
SHEET    2   C 5 TYR B  37  CYS B  42  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  HIS B 177   N  ILE B  95
SHEET    5   C 5 LEU B 188  VAL B 189 -1  O  LEU B 188   N  VAL B 180
LINK         SG  CYS A  42                ZN    ZN A 230     1555   1555  2.34
LINK         NE2 HIS A  98                ZN    ZN A 230     1555   1555  2.08
LINK         SG  CYS A 101                ZN    ZN A 230     1555   1555  2.34
LINK         SG  CYS B  42                ZN    ZN B 230     1555   1555  2.34
LINK         NE2 HIS B  98                ZN    ZN B 230     1555   1555  2.09
LINK         SG  CYS B 101                ZN    ZN B 230     1555   1555  2.27
SITE     1 AC1  5 CYS A  42  ASN A  44  HIS A  98  CYS A 101
SITE     2 AC1  5 HOH A 231
SITE     1 AC2  5 CYS B  42  ASN B  44  HIS B  98  CYS B 101
SITE     2 AC2  5 HOH B 231
CRYST1   81.574   81.574  187.846  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      0.012259  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012259  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005324        0.00000
      
PROCHECK
Go to PROCHECK summary
 References