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PDBsum entry 2esf

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
2esf
Jmol
Contents
Protein chains
213 a.a.
Ligands
BCT ×2
Metals
_ZN ×2
Waters ×178
HEADER    LYASE                                   26-OCT-05   2ESF
TITLE     IDENTIFICATION OF A NOVEL NON-CATALYTIC BICARBONATE BINDING SITE IN
TITLE    2 EUBACTERIAL BETA-CARBONIC ANHYDRASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
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: CAN, CYNT2;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL-21 (DE3);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTRC99A
KEYWDS    CARBONIC ANHYDRASE,METALLOENZYME, BICARBONATE, ZINC COORDINATION,
KEYWDS   2 LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.D.CRONK,R.S.ROWLETT,K.Y.J.ZHANG,C.TU,J.A.ENDRIZZI,P.C.GAREISS
REVDAT   3   13-JUL-11 2ESF    1       VERSN
REVDAT   2   24-FEB-09 2ESF    1       VERSN
REVDAT   1   18-APR-06 2ESF    0
JRNL        AUTH   J.D.CRONK,R.S.ROWLETT,K.Y.J.ZHANG,C.TU,J.A.ENDRIZZI,J.LEE,
JRNL        AUTH 2 P.C.GAREISS,J.R.PREISS
JRNL        TITL   IDENTIFICATION OF A NOVEL NONCATALYTIC BICARBONATE BINDING
JRNL        TITL 2 SITE IN EUBACTERIAL BETA-CARBONIC ANHYDRASE.
JRNL        REF    BIOCHEMISTRY                  V.  45  4351 2006
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   16584170
JRNL        DOI    10.1021/BI052272Q
REMARK   2
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
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) : 2.25
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.50
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.9
REMARK   3   NUMBER OF REFLECTIONS             : 27603
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) : 0.198
REMARK   3   FREE R VALUE                     : 0.228
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1351
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
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          : 10
REMARK   3   SOLVENT ATOMS            : 178
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
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 : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
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  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2ESF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-NOV-05.
REMARK 100 THE RCSB ID CODE IS RCSB035035.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 22-JUL-01
REMARK 200  TEMPERATURE           (KELVIN) : 115
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                       : 5.0.1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000
REMARK 200  MONOCHROMATOR                  : NULL
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   : 27655
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250
REMARK 200  RESOLUTION RANGE LOW       (A) : 54.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 16.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.39
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1I6O
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 55.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.65 M AMMONIUM SULFATE, 4% PEG 400,
REMARK 280  0.1 M MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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       81.10650
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      121.65975
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       40.55325
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       81.10650
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       40.55325
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      121.65975
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: 16360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 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       81.10650
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     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     MET 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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH A  1541     O    HOH A  1541     6555     1.66
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    GLU A  20      -73.56    -82.27
REMARK 500    ALA A  32      100.86    -40.48
REMARK 500    ASN A  68       64.19     37.18
REMARK 500    ASN A 110       62.31      3.05
REMARK 500    GLU A 112       85.68    -61.65
REMARK 500    ASP A 185       -7.52   -159.07
REMARK 500    GLU B  20      -70.67    -83.78
REMARK 500    ALA B  32       97.77    -53.52
REMARK 500    SER B  45       48.48     38.05
REMARK 500    ASN B  68       69.19     35.62
REMARK 500    ASN B 110       75.08      0.19
REMARK 500    GLN B 139      -73.06     36.10
REMARK 500    GLU B 140        5.10    -59.69
REMARK 500    ILE B 183       32.94    -85.90
REMARK 500    ASP B 185      -17.62   -144.13
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 300  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A  42   SG
REMARK 620 2 ASP A  44   OD2 102.1
REMARK 620 3 HIS A  98   NE2 113.3 100.9
REMARK 620 4 CYS A 101   SG  118.8 112.7 107.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 300  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B  42   SG
REMARK 620 2 ASP B  44   OD2  99.7
REMARK 620 3 HIS B  98   NE2 113.3 110.7
REMARK 620 4 CYS B 101   SG  113.2 109.5 109.9
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 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT A 1498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT B 2498
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1I6O   RELATED DB: PDB
REMARK 900 E. COLI CARBONIC ANHYDRASE
REMARK 900 RELATED ID: 1I6P   RELATED DB: PDB
REMARK 900 E. COLI CARBONIC ANHYDRASE
DBREF  2ESF A    1   220  UNP    P61517   CAN_ECOLI        1    220
DBREF  2ESF B    1   220  UNP    P61517   CAN_ECOLI        1    220
SEQRES   1 A  220  MET LYS ASP ILE ASP THR LEU ILE SER ASN ASN ALA LEU
SEQRES   2 A  220  TRP SER LYS MET 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 MET PRO GLN GLU ARG ARG LEU
SEQRES  12 A  220  ASP THR LEU CYS GLU LEU ASN VAL MET GLU GLN VAL TYR
SEQRES  13 A  220  ASN LEU GLY HIS SER THR ILE MET 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  MET LYS ASP ILE ASP THR LEU ILE SER ASN ASN ALA LEU
SEQRES   2 B  220  TRP SER LYS MET 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 MET PRO GLN GLU ARG ARG LEU
SEQRES  12 B  220  ASP THR LEU CYS GLU LEU ASN VAL MET GLU GLN VAL TYR
SEQRES  13 B  220  ASN LEU GLY HIS SER THR ILE MET 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
HET     ZN  A 300       1
HET    BCT  A1498       4
HET     ZN  B 300       1
HET    BCT  B2498       4
HETNAM      ZN ZINC ION
HETNAM     BCT BICARBONATE ION
FORMUL   3   ZN    2(ZN 2+)
FORMUL   4  BCT    2(C H O3 1-)
FORMUL   7  HOH   *178(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  GLU A  109  1                                   9
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 PRO A  138  GLU A  140  5                                   3
HELIX    9   9 ARG A  141  SER A  161  1                                  21
HELIX   10  10 SER A  161  ARG A  170  1                                  10
HELIX   11  11 ASN A  197  LYS A  215  1                                  19
HELIX   12  12 ASP B    3  GLU B   21  1                                  19
HELIX   13  13 PRO B   23  GLN B   31  1                                   9
HELIX   14  14 PRO B   48  GLY B   54  1                                   7
HELIX   15  15 ASP B   74  VAL B   87  1                                  14
HELIX   16  16 CYS B  101  GLU B  109  1                                   9
HELIX   17  17 LEU B  115  HIS B  130  1                                  16
HELIX   18  18 HIS B  130  GLU B  136  1                                   7
HELIX   19  19 ARG B  141  HIS B  160  1                                  20
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  N  PHE A  37   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 THR A 175  TYR A 181  1  O  TRP A 179   N  ILE A  95
SHEET    5   A 5 ARG A 189  ASP A 190 -1  O  ARG A 189   N  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  N  TRP B  39   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 THR B 175  TYR B 181  1  O  HIS B 177   N  ILE B  93
SHEET    5   B 5 ARG B 189  ASP B 190 -1  O  ARG B 189   N  ALA B 180
LINK        ZN    ZN A 300                 SG  CYS A  42     1555   1555  2.30
LINK        ZN    ZN A 300                 OD2 ASP A  44     1555   1555  2.27
LINK        ZN    ZN A 300                 NE2 HIS A  98     1555   1555  2.18
LINK        ZN    ZN A 300                 SG  CYS A 101     1555   1555  2.33
LINK        ZN    ZN B 300                 SG  CYS B  42     1555   1555  2.40
LINK        ZN    ZN B 300                 OD2 ASP B  44     1555   1555  2.21
LINK        ZN    ZN B 300                 NE2 HIS B  98     1555   1555  2.26
LINK        ZN    ZN B 300                 SG  CYS B 101     1555   1555  2.45
SITE     1 AC1  4 CYS A  42  ASP A  44  HIS A  98  CYS A 101
SITE     1 AC2  9 TRP A  39  VAL A  47  PRO A  48  ALA A  49
SITE     2 AC2  9 LEU A  52  ARG A  64  TYR A 181  HOH A1499
SITE     3 AC2  9 HOH A1500
SITE     1 AC3  4 CYS B  42  ASP B  44  HIS B  98  CYS B 101
SITE     1 AC4  8 TRP B  39  GLY B  41  VAL B  47  ALA B  49
SITE     2 AC4  8 ARG B  64  TYR B 181  HOH B2499  HOH B2500
CRYST1   82.866   82.866  162.213  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      0.012068  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012068  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006165        0.00000
      
PROCHECK
Go to PROCHECK summary
 References