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PDBsum entry 3e24

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
3e24
Jmol
Contents
Protein chains
186 a.a.
Ligands
PO4 ×4
Metals
_ZN ×2
Waters ×138
HEADER    LYASE                                   05-AUG-08   3E24
TITLE     H. INFLUENZAE BETA-CARBONIC ANHYDRASE, VARIANT W39F
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 3E24    1       VERSN
REVDAT   2   28-JUL-09 3E24    1       JRNL
REVDAT   1   02-JUN-09 3E24    0
JRNL        AUTH   R.S.ROWLETT,C.TU,J.LEE,A.G.HERMAN,D.A.CHAPNICK,S.H.SHAH,
JRNL        AUTH 2 P.C.GAREISS
JRNL        TITL   ALLOSTERIC SITE VARIANTS OF HAEMOPHILUS INFLUENZAE
JRNL        TITL 2 BETA-CARBONIC ANHYDRASE.
JRNL        REF    BIOCHEMISTRY                  V.  48  6146 2009
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   19459702
JRNL        DOI    10.1021/BI900663H
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.37
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 20242
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) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.191
REMARK   3   FREE R VALUE                     : 0.236
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800
REMARK   3   FREE R VALUE TEST SET COUNT      : 1990
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1305
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1860
REMARK   3   BIN FREE R VALUE SET COUNT          : 139
REMARK   3   BIN FREE R VALUE                    : 0.2550
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2920
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 22
REMARK   3   SOLVENT ATOMS            : 138
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.07
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.01000
REMARK   3    B22 (A**2) : 0.04000
REMARK   3    B33 (A**2) : -0.03000
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): 0.328
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.231
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.140
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.197
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3006 ; 0.010 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  1981 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4070 ; 1.158 ; 1.939
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4821 ; 0.907 ; 3.002
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   366 ; 6.317 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   141 ;37.348 ;24.043
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   515 ;15.170 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;17.837 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   459 ; 0.069 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3308 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   604 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   703 ; 0.211 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2065 ; 0.190 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1450 ; 0.171 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1481 ; 0.087 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   146 ; 0.185 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.051 ; 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 ; 0.160 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    76 ; 0.194 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.155 ; 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):  2365 ; 0.940 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   758 ; 0.106 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2933 ; 1.067 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1364 ; 1.369 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1137 ; 1.863 ; 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    35        A   220
REMARK   3    ORIGIN FOR THE GROUP (A):  32.9900  60.8630  17.1830
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0167 T22:  -0.0311
REMARK   3      T33:  -0.0389 T12:  -0.0014
REMARK   3      T13:   0.0203 T23:  -0.0254
REMARK   3    L TENSOR
REMARK   3      L11:   1.4544 L22:   0.5969
REMARK   3      L33:   1.1751 L12:  -0.0586
REMARK   3      L13:  -0.2726 L23:  -0.3993
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0316 S12:   0.1736 S13:  -0.1220
REMARK   3      S21:  -0.1132 S22:   0.0044 S23:  -0.0217
REMARK   3      S31:   0.1130 S32:  -0.0083 S33:   0.0272
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    35        B   216
REMARK   3    ORIGIN FOR THE GROUP (A):  26.6380  83.4810  33.1830
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0083 T22:  -0.0870
REMARK   3      T33:  -0.0231 T12:   0.0240
REMARK   3      T13:  -0.0100 T23:  -0.0006
REMARK   3    L TENSOR
REMARK   3      L11:   1.6454 L22:   1.2978
REMARK   3      L33:   1.0777 L12:  -0.4138
REMARK   3      L13:  -0.1835 L23:  -0.2595
REMARK   3    S TENSOR
REMARK   3      S11:   0.0144 S12:  -0.0098 S13:   0.1285
REMARK   3      S21:  -0.0019 S22:   0.0203 S23:  -0.0193
REMARK   3      S31:  -0.1643 S32:  -0.0518 S33:  -0.0346
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 3E24 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 RCSB048778.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-03
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 4.3
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NI FILTER
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.301
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.370
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7
REMARK 200  DATA REDUNDANCY                : 4.600
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.05900
REMARK 200   FOR THE DATA SET  : 22.2400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.31600
REMARK 200   FOR SHELL         : 4.520
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: PDB ENTRY 2A8D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.04 M AMMONIUM DIHYDROGEN PHOSPHATE,
REMARK 280  PH 4.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X,-Y+1/2,Z
REMARK 290       7555   -X+1/2,Y,-Z
REMARK 290       8555   X,-Y,-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       24.08650
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.04050
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       64.81350
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       72.04050
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.08650
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       64.81350
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       24.08650
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       64.81350
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       72.04050
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       64.81350
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       24.08650
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       72.04050
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: 11960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -121.0 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        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      129.62700
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       72.04050
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     THR A    34
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     THR B    34
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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     ARG B   64   N    CA   C    O    CB   CG   CD
REMARK 480     ARG B   64   NE   CZ   NH1  NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   OE1  GLN A   191     O    HOH A   265              2.04
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    GLN A 191      -55.68     70.76
REMARK 500    ASP A 216      -94.13    -81.74
REMARK 500    LYS B 136       45.56    -83.12
REMARK 500    ASP B 185      -50.98   -151.41
REMARK 500    ASP B 190       99.58    -58.05
REMARK 500    GLN B 191       57.79    -65.52
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  95.4
REMARK 620 3 HIS A  98   NE2 115.5 128.1
REMARK 620 4 CYS A 101   SG  114.3  96.1 106.3
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   OD1 104.4
REMARK 620 3 HIS B  98   NE2 116.3  85.8
REMARK 620 4 CYS B 101   SG  113.4 123.8 110.7
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 PO4 A 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 233
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 231
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: 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
REMARK 900 RELATED ID: 3E31   RELATED DB: PDB
DBREF  3E24 A    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E24 B    1   229  UNP    P45148   CAN_HAEIN        1    229
SEQADV 3E24 PHE A   39  UNP  P45148    TRP    39 ENGINEERED
SEQADV 3E24 PHE B   39  UNP  P45148    TRP    39 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 PHE
SEQRES   4 A  229  ILE GLY CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 A  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 A  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 A  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 A  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 A  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 A  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 A  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 A  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 A  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 A  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL 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 PHE
SEQRES   4 B  229  ILE GLY CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 B  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 B  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 B  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 B  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 B  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 B  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 B  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 B  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 B  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 B  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL 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    PO4  A 231       5
HET    PO4  A 232       5
HET    PO4  A 233       5
HET     ZN  B 230       1
HET    PO4  B 231       5
HETNAM      ZN ZINC ION
HETNAM     PO4 PHOSPHATE ION
FORMUL   3   ZN    2(ZN 2+)
FORMUL   4  PO4    4(O4 P 3-)
FORMUL   9  HOH   *138(H2 O)
HELIX    1   1 PRO A   48  ASN A   54  1                                   7
HELIX    2   2 ASP A   74  VAL A   87  1                                  14
HELIX    3   3 CYS A  101  ASP A  110  1                                  10
HELIX    4   4 LEU A  115  HIS A  130  1                                  16
HELIX    5   5 HIS A  130  LYS A  136  1                                   7
HELIX    6   6 LEU A  137  GLU A  140  5                                   4
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  ASN B   54  1                                   7
HELIX   11  11 ASP B   74  VAL B   87  1                                  14
HELIX   12  12 CYS B  101  ASP B  110  1                                  10
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  ARG B  160  1                                  23
HELIX   16  16 THR B  161  ARG B  170  1                                  10
HELIX   17  17 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  PHE A  39   O  PHE A  61
SHEET    3   A 5 HIS A  92  HIS A  98  1  O  ILE A  94   N  ILE A  40
SHEET    4   A 5 SER A 175  ASP A 182  1  O  HIS A 177   N  ILE A  95
SHEET    5   A 5 PHE A 187  ALA A 195 -1  O  PHE A 187   N  ASP A 182
SHEET    1   B 5 LEU B  60  ASN B  65  0
SHEET    2   B 5 TYR B  37  CYS B  42  1  N  TYR B  37   O  PHE B  61
SHEET    3   B 5 HIS B  92  HIS B  98  1  O  ILE B  94   N  ILE B  40
SHEET    4   B 5 SER B 175  TYR B 181  1  O  TRP B 179   N  ILE B  95
SHEET    5   B 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  2.07
LINK         SG  CYS A 101                ZN    ZN A 230     1555   1555  2.31
LINK         SG  CYS B  42                ZN    ZN B 230     1555   1555  2.32
LINK         OD1 ASP B  44                ZN    ZN B 230     1555   1555  2.00
LINK         NE2 HIS B  98                ZN    ZN B 230     1555   1555  2.08
LINK         SG  CYS B 101                ZN    ZN B 230     1555   1555  2.28
SITE     1 AC1  4 CYS A  42  ASP A  44  HIS A  98  CYS A 101
SITE     1 AC2  9 PRO A  48  ARG A  64  HOH A 285  PRO B  48
SITE     2 AC2  9 ALA B  49  GLU B  50  VAL B  62  ARG B  64
SITE     3 AC2  9 PO4 B 231
SITE     1 AC3  6 ASP A 110  LEU A 121  ARG A 124  ARG B 160
SITE     2 AC3  6 LYS B 165  ARG B 198
SITE     1 AC4  8 ARG A 160  LYS A 165  ARG A 198  HOH A 246
SITE     2 AC4  8 ASP B 110  LEU B 121  ARG B 124  HOH B 241
SITE     1 AC5  4 CYS B  42  ASP B  44  HIS B  98  CYS B 101
SITE     1 AC6  9 PRO A  48  ARG A  64  PO4 A 231  HOH A 285
SITE     2 AC6  9 PRO B  48  ALA B  49  GLU B  50  ARG B  64
SITE     3 AC6  9 HOH B 290
CRYST1   48.173  129.627  144.081  90.00  90.00  90.00 I 21 21 21   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      0.020759  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007714  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006941        0.00000
      
PROCHECK
Go to PROCHECK summary
 References