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PDBsum entry 1i6o

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Top Page protein metals Protein-protein interface(s) links
Lyase PDB id
1i6o
Jmol
Contents
Protein chains
213 a.a. *
Metals
_ZN ×2
Waters ×87
* Residue conservation analysis
HEADER    LYASE                                   02-MAR-01   1I6O
TITLE     CRYSTAL STRUCTURE OF E. COLI BETA CARBONIC ANHYDRASE (ECCA)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 4.2.1.1;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 562;
SOURCE   4 GENE: YADF;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS    CARBONIC ANHYDRASE, METALLOENZYME, ZINC COORDINATION, PH-DEPENDENT
KEYWDS   2 ACTIVITY, MAD PHASING, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.D.CRONK,J.A.ENDRIZZI,M.R.CRONK,J.W.O'NEILL,K.Y.J.ZHANG
REVDAT   4   13-JUL-11 1I6O    1       VERSN
REVDAT   3   24-FEB-09 1I6O    1       VERSN
REVDAT   2   01-APR-03 1I6O    1       JRNL
REVDAT   1   09-MAY-01 1I6O    0
JRNL        AUTH   J.D.CRONK,J.A.ENDRIZZI,M.R.CRONK,J.W.O'NEILL,K.Y.ZHANG
JRNL        TITL   CRYSTAL STRUCTURE OF E. COLI BETA-CARBONIC ANHYDRASE, AN
JRNL        TITL 2 ENZYME WITH AN UNUSUAL PH-DEPENDENT ACTIVITY.
JRNL        REF    PROTEIN SCI.                  V.  10   911 2001
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   11316870
JRNL        DOI    10.1110/PS.46301
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   J.D.CRONK,J.W.O'NEILL,M.R.CRONK,J.A.ENDRIZZI,K.Y.J.ZHANG
REMARK   1  TITL   CLONING, CRYSTALLIZATION AND PRELIMINARY CHARACTERIZATION OF
REMARK   1  TITL 2 A BETA CARBONIC ANHYDRASE FROM ESCHERICHIA COLI
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  52  1176 2000
REMARK   1  REFN                   ISSN 0907-4449
REMARK   1  DOI    10.1107/S0907444900008519
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.36
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2423088.660
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.3
REMARK   3   NUMBER OF REFLECTIONS             : 28191
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 SET) : 0.212
REMARK   3   FREE R VALUE                     : 0.243
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 2848
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.70
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4083
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2360
REMARK   3   BIN FREE R VALUE                    : 0.2650
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.40
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 476
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3421
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 87
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 23.80
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.40
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 4.85000
REMARK   3    B22 (A**2) : 4.85000
REMARK   3    B33 (A**2) : -9.70000
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 COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.26
REMARK   3   ESD FROM SIGMAA              (A) : 0.16
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.31
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.18
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.005
REMARK   3   BOND ANGLES            (DEGREES) : 1.10
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.30
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.67
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.35
REMARK   3   BSOL        : 46.96
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : ION.PARAM
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1I6O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK  99
REMARK  99 DENSITY FOR THE FOLLOWING ATOMS WITHIN THE MAIN CHAIN
REMARK  99 IS RELATIVELY WEAK AND LIKELY REFLECTS INCREASED LOCAL
REMARK  99 CONFORMATIONAL FLEXIBILITY OF THE MAIN CHAIN IN THIS
REMARK  99 REGION.
REMARK  99 ALA A 32 CA
REMARK  99 GLN B 31 C
REMARK  99 GLN B 31 O
REMARK  99 ALA B 32 CA
REMARK  99 ALA B 32 O
REMARK  99
REMARK  99 DENSITY FOR THE SIDE CHAINS OF THE LISTED RESIDUES IS
REMARK  99 RELATIVELY POORLY DEFINED.  THE MODEL REPRESENTS
REMARK  99 THE MOST PROBABLE CONFORMATIONS FOR THESE RESIDUES
REMARK  99 BASED ON THE OBSERVED DENSITY.
REMARK  99 LYS A    16
REMARK  99 GLU A    27
REMARK  99 LYS A    28
REMARK  99 GLN A    31
REMARK  99 ARG A    36
REMARK  99 GLN A   139
REMARK  99 GLU A   140
REMARK  99 ARG A   198
REMARK  99 GLU A   199
REMARK  99 LYS A   213
REMARK  99 LEU A   214
REMARK  99 LYS A   215
REMARK  99 LYS B     2
REMARK  99 LEU B    13
REMARK  99 LYS B    16
REMARK  99 GLU B    20
REMARK  99 GLU B    21
REMARK  99 LYS B    28
REMARK  99 ARG B    36
REMARK  99 GLU B   140
REMARK  99 ARG B   141
REMARK  99 LYS B   173
REMARK  99 ARG B   206
REMARK  99 ASN B   211
REMARK  99 LEU B   212
REMARK  99 LYS B   213
REMARK  99 LEU B   214
REMARK  99 LYS B   215
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAR-01.
REMARK 100 THE RCSB ID CODE IS RCSB012971.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 08-NOV-99
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ALS
REMARK 200  BEAMLINE                       : 5.0.2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96112,0.97950,0.97970,1.07812,
REMARK 200                                   1.28109
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 237761
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.130
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0
REMARK 200  DATA REDUNDANCY                : 7.700
REMARK 200  R MERGE                    (I) : 0.05400
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 25.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.13
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.25
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.25500
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 51.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PEG 400, MES PH 6.5,
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 2 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,X,Z+3/4
REMARK 290       4555   Y,-X,Z+1/4
REMARK 290       5555   -X,Y,-Z
REMARK 290       6555   X,-Y,-Z+1/2
REMARK 290       7555   Y,X,-Z+1/4
REMARK 290       8555   -Y,-X,-Z+3/4
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       81.06850
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      121.60275
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       40.53425
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       81.06850
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       40.53425
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      121.60275
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 15040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -97.0 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        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       81.06850
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     MSE A     1
REMARK 465     LYS A     2
REMARK 465     HIS A   216
REMARK 465     ALA A   217
REMARK 465     ASN A   218
REMARK 465     HIS A   219
REMARK 465     LYS A   220
REMARK 465     MSE B     1
REMARK 465     HIS B   216
REMARK 465     ALA B   217
REMARK 465     ASN B   218
REMARK 465     HIS B   219
REMARK 465     LYS B   220
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  31       80.94    -64.03
REMARK 500    ALA A  32      101.67    -32.22
REMARK 500    SER A  45       58.04     35.78
REMARK 500    ASN A  68       62.36     39.17
REMARK 500    MSE A 137      144.79   -171.48
REMARK 500    GLN A 139      -17.34    -49.98
REMARK 500    ASP A 185       -7.59   -152.27
REMARK 500    ASN B  68       58.12     39.60
REMARK 500    GLU B 136       35.77    -87.20
REMARK 500    ASP B 185       -9.11   -150.49
REMARK 500    ASP B 192       74.03     29.45
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 301  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 101   SG
REMARK 620 2 ASP A  44   OD2 111.4
REMARK 620 3 CYS A  42   SG  117.8 100.2
REMARK 620 4 HIS A  98   NE2 106.0 104.8 116.0
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 302  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B  42   SG
REMARK 620 2 HIS B  98   NE2 112.5
REMARK 620 3 CYS B 101   SG  115.7 107.0
REMARK 620 4 ASP B  44   OD2  98.9 107.7 114.8
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1I6P   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E. COLI BETA CARBONIC ANHYDRASE (ECCA)
REMARK 900 IN A DIFFERENT SPACE GROUP, P42212, SOLVED TO 2.0A
REMARK 900 RESOLUTION
DBREF  1I6O A    1   220  UNP    P61517   CAN_ECOLI        1    220
DBREF  1I6O B    1   220  UNP    P61517   CAN_ECOLI        1    220
SEQADV 1I6O MSE A    1  UNP  P61517    MET     1 MODIFIED RESIDUE
SEQADV 1I6O MSE A   17  UNP  P61517    MET    17 MODIFIED RESIDUE
SEQADV 1I6O MSE A  137  UNP  P61517    MET   137 MODIFIED RESIDUE
SEQADV 1I6O MSE A  152  UNP  P61517    MET   152 MODIFIED RESIDUE
SEQADV 1I6O MSE A  164  UNP  P61517    MET   164 MODIFIED RESIDUE
SEQADV 1I6O MSE B    1  UNP  P61517    MET     1 MODIFIED RESIDUE
SEQADV 1I6O MSE B   17  UNP  P61517    MET    17 MODIFIED RESIDUE
SEQADV 1I6O MSE B  137  UNP  P61517    MET   137 MODIFIED RESIDUE
SEQADV 1I6O MSE B  152  UNP  P61517    MET   152 MODIFIED RESIDUE
SEQADV 1I6O MSE B  164  UNP  P61517    MET   164 MODIFIED RESIDUE
SEQRES   1 A  220  MSE LYS ASP ILE ASP THR LEU ILE SER ASN ASN ALA LEU
SEQRES   2 A  220  TRP SER LYS MSE LEU VAL GLU GLU ASP PRO GLY PHE PHE
SEQRES   3 A  220  GLU LYS LEU ALA GLN ALA GLN LYS PRO ARG PHE LEU TRP
SEQRES   4 A  220  ILE GLY CYS SER ASP SER ARG VAL PRO ALA GLU ARG LEU
SEQRES   5 A  220  THR GLY LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 A  220  VAL ALA ASN LEU VAL ILE HIS THR ASP LEU ASN CYS LEU
SEQRES   7 A  220  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU GLU VAL GLU
SEQRES   8 A  220  HIS ILE ILE ILE CYS GLY HIS TYR GLY CYS GLY GLY VAL
SEQRES   9 A  220  GLN ALA ALA VAL GLU ASN PRO GLU LEU GLY LEU ILE ASN
SEQRES  10 A  220  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 A  220  SER SER LEU LEU GLY GLU MSE PRO GLN GLU ARG ARG LEU
SEQRES  12 A  220  ASP THR LEU CYS GLU LEU ASN VAL MSE GLU GLN VAL TYR
SEQRES  13 A  220  ASN LEU GLY HIS SER THR ILE MSE GLN SER ALA TRP LYS
SEQRES  14 A  220  ARG GLY GLN LYS VAL THR ILE HIS GLY TRP ALA TYR GLY
SEQRES  15 A  220  ILE HIS ASP GLY LEU LEU ARG ASP LEU ASP VAL THR ALA
SEQRES  16 A  220  THR ASN ARG GLU THR LEU GLU GLN ARG TYR ARG HIS GLY
SEQRES  17 A  220  ILE SER ASN LEU LYS LEU LYS HIS ALA ASN HIS LYS
SEQRES   1 B  220  MSE LYS ASP ILE ASP THR LEU ILE SER ASN ASN ALA LEU
SEQRES   2 B  220  TRP SER LYS MSE LEU VAL GLU GLU ASP PRO GLY PHE PHE
SEQRES   3 B  220  GLU LYS LEU ALA GLN ALA GLN LYS PRO ARG PHE LEU TRP
SEQRES   4 B  220  ILE GLY CYS SER ASP SER ARG VAL PRO ALA GLU ARG LEU
SEQRES   5 B  220  THR GLY LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 B  220  VAL ALA ASN LEU VAL ILE HIS THR ASP LEU ASN CYS LEU
SEQRES   7 B  220  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU GLU VAL GLU
SEQRES   8 B  220  HIS ILE ILE ILE CYS GLY HIS TYR GLY CYS GLY GLY VAL
SEQRES   9 B  220  GLN ALA ALA VAL GLU ASN PRO GLU LEU GLY LEU ILE ASN
SEQRES  10 B  220  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 B  220  SER SER LEU LEU GLY GLU MSE PRO GLN GLU ARG ARG LEU
SEQRES  12 B  220  ASP THR LEU CYS GLU LEU ASN VAL MSE GLU GLN VAL TYR
SEQRES  13 B  220  ASN LEU GLY HIS SER THR ILE MSE GLN SER ALA TRP LYS
SEQRES  14 B  220  ARG GLY GLN LYS VAL THR ILE HIS GLY TRP ALA TYR GLY
SEQRES  15 B  220  ILE HIS ASP GLY LEU LEU ARG ASP LEU ASP VAL THR ALA
SEQRES  16 B  220  THR ASN ARG GLU THR LEU GLU GLN ARG TYR ARG HIS GLY
SEQRES  17 B  220  ILE SER ASN LEU LYS LEU LYS HIS ALA ASN HIS LYS
MODRES 1I6O MSE A   17  MET  SELENOMETHIONINE
MODRES 1I6O MSE A  137  MET  SELENOMETHIONINE
MODRES 1I6O MSE A  152  MET  SELENOMETHIONINE
MODRES 1I6O MSE A  164  MET  SELENOMETHIONINE
MODRES 1I6O MSE B   17  MET  SELENOMETHIONINE
MODRES 1I6O MSE B  137  MET  SELENOMETHIONINE
MODRES 1I6O MSE B  152  MET  SELENOMETHIONINE
MODRES 1I6O MSE B  164  MET  SELENOMETHIONINE
HET    MSE  A  17       8
HET    MSE  A 137       8
HET    MSE  A 152       8
HET    MSE  A 164       8
HET    MSE  B  17       8
HET    MSE  B 137       8
HET    MSE  B 152       8
HET    MSE  B 164       8
HET     ZN  A 301       1
HET     ZN  B 302       1
HETNAM     MSE SELENOMETHIONINE
HETNAM      ZN ZINC ION
FORMUL   1  MSE    8(C5 H11 N O2 SE)
FORMUL   3   ZN    2(ZN 2+)
FORMUL   5  HOH   *87(H2 O)
HELIX    1   1 ASP A    3  ASP A   22  1                                  20
HELIX    2   2 GLY A   24  GLN A   31  1                                   8
HELIX    3   3 PRO A   48  GLY A   54  1                                   7
HELIX    4   4 ASP A   74  VAL A   87  1                                  14
HELIX    5   5 CYS A  101  ASN A  110  1                                  10
HELIX    6   6 LEU A  115  HIS A  130  1                                  16
HELIX    7   7 HIS A  130  GLU A  136  1                                   7
HELIX    8   8 ARG A  141  SER A  161  1                                  21
HELIX    9   9 SER A  161  ARG A  170  1                                  10
HELIX   10  10 ASN A  197  LYS A  213  1                                  17
HELIX   11  11 ASP B    3  VAL B   19  1                                  17
HELIX   12  12 PRO B   23  ALA B   30  1                                   8
HELIX   13  13 PRO B   48  GLY B   54  1                                   7
HELIX   14  14 ASP B   74  VAL B   87  1                                  14
HELIX   15  15 CYS B  101  ASN B  110  1                                  10
HELIX   16  16 LEU B  115  HIS B  130  1                                  16
HELIX   17  17 HIS B  130  GLU B  136  1                                   7
HELIX   18  18 PRO B  138  GLU B  140  5                                   3
HELIX   19  19 ARG B  141  SER B  161  1                                  21
HELIX   20  20 SER B  161  ARG B  170  1                                  10
HELIX   21  21 ASN B  197  LYS B  215  1                                  19
SHEET    1   A 5 LEU A  60  ASN A  65  0
SHEET    2   A 5 PHE A  37  CYS A  42  1  O  PHE A  37   N  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 THR A 175  TYR A 181  1  O  THR A 175   N  ILE A  93
SHEET    5   A 5 LEU A 188  ASP A 190 -1  N  ARG A 189   O  ALA A 180
SHEET    1   B 5 LEU B  60  ASN B  65  0
SHEET    2   B 5 PHE B  37  CYS B  42  1  O  PHE B  37   N  PHE B  61
SHEET    3   B 5 HIS B  92  HIS B  98  1  O  HIS B  92   N  LEU B  38
SHEET    4   B 5 THR B 175  TYR B 181  1  O  THR B 175   N  ILE B  93
SHEET    5   B 5 ARG B 189  ASP B 190 -1  N  ARG B 189   O  ALA B 180
LINK         C   LYS A  16                 N   MSE A  17     1555   1555  1.33
LINK         C   MSE A  17                 N   LEU A  18     1555   1555  1.33
LINK         C   GLU A 136                 N   MSE A 137     1555   1555  1.33
LINK         C   MSE A 137                 N   PRO A 138     1555   1555  1.34
LINK         C   VAL A 151                 N   MSE A 152     1555   1555  1.33
LINK         C   MSE A 152                 N   GLU A 153     1555   1555  1.33
LINK         C   ILE A 163                 N   MSE A 164     1555   1555  1.33
LINK         C   MSE A 164                 N   GLN A 165     1555   1555  1.33
LINK        ZN    ZN A 301                 SG  CYS A 101     1555   1555  2.39
LINK        ZN    ZN A 301                 OD2 ASP A  44     1555   1555  2.18
LINK        ZN    ZN A 301                 SG  CYS A  42     1555   1555  2.34
LINK        ZN    ZN A 301                 NE2 HIS A  98     1555   1555  2.18
LINK         C   LYS B  16                 N   MSE B  17     1555   1555  1.33
LINK         C   MSE B  17                 N   LEU B  18     1555   1555  1.33
LINK         C   GLU B 136                 N   MSE B 137     1555   1555  1.33
LINK         C   MSE B 137                 N   PRO B 138     1555   1555  1.34
LINK         C   VAL B 151                 N   MSE B 152     1555   1555  1.33
LINK         C   MSE B 152                 N   GLU B 153     1555   1555  1.33
LINK         C   ILE B 163                 N   MSE B 164     1555   1555  1.33
LINK         C   MSE B 164                 N   GLN B 165     1555   1555  1.33
LINK        ZN    ZN B 302                 SG  CYS B  42     1555   1555  2.45
LINK        ZN    ZN B 302                 NE2 HIS B  98     1555   1555  2.22
LINK        ZN    ZN B 302                 SG  CYS B 101     1555   1555  2.39
LINK        ZN    ZN B 302                 OD2 ASP B  44     1555   1555  2.12
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   81.244   81.244  162.137  90.00  90.00  90.00 P 43 2 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      0.012309  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012309  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006168        0.00000
      
PROCHECK
Go to PROCHECK summary
 References