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PDBsum entry 3ucm

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase/lyase inhibitor PDB id
3ucm
Jmol
Contents
Protein chains
222 a.a.
Ligands
SCN ×3
Metals
_ZN ×2
Waters ×276
HEADER    LYASE/LYASE INHIBITOR                   27-OCT-11   3UCM
TITLE     COCCOMYXA BETA-CARBONIC ANHYDRASE IN COMPLEX WITH THIOCYANATE
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: COCCOMYXA SP. PA;
SOURCE   3 ORGANISM_TAXID: 41892;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PMAL-C2
KEYWDS    ALPHA/BETA, STRAND EXCHANGE, LYASE-LYASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.HUANG,T.HAINZL,A.E.SAUER-ERIKSSON
REVDAT   2   28-MAR-12 3UCM    1       JRNL
REVDAT   1   23-NOV-11 3UCM    0
JRNL        AUTH   S.HUANG,T.HAINZL,C.GRUNDSTROM,C.FORSMAN,G.SAMUELSSON,
JRNL        AUTH 2 A.E.SAUER-ERIKSSON
JRNL        TITL   STRUCTURAL STUDIES OF [BETA]-CARBONIC ANHYDRASE FROM THE
JRNL        TITL 2 GREEN ALGA COCCOMYXA: INHIBITOR COMPLEXES WITH ANIONS AND
JRNL        TITL 3 ACETAZOLAMIDE.
JRNL        REF    PLOS ONE                      V.   6 28458 2011
JRNL        REFN                   ESSN 1932-6203
JRNL        PMID   22162771
JRNL        DOI    10.1371/JOURNAL.PONE.0028458
REMARK   2
REMARK   2 RESOLUTION.    2.51 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0110
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) : 2.51
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.05
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.8
REMARK   3   NUMBER OF REFLECTIONS             : 19246
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) : 0.189
REMARK   3   FREE R VALUE                     : 0.250
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.200
REMARK   3   FREE R VALUE TEST SET COUNT      : 1958
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) : 2.51
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.58
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1075
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.67
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2760
REMARK   3   BIN FREE R VALUE SET COUNT          : 122
REMARK   3   BIN FREE R VALUE                    : 0.3800
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3390
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 11
REMARK   3   SOLVENT ATOMS            : 276
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 62.60
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 3.94000
REMARK   3    B22 (A**2) : 3.94000
REMARK   3    B33 (A**2) : -7.87000
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): 0.459
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.294
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.184
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.321
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952
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):  3470 ; 0.022 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4711 ; 1.874 ; 1.948
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   442 ; 6.646 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   146 ;40.556 ;24.795
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   568 ;17.417 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;18.509 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   530 ; 0.117 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2618 ; 0.008 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
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):  2214 ; 0.835 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3537 ; 1.541 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1256 ; 2.536 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1174 ; 4.065 ; 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  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS:
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK   3  U VALUES      : REFINED INDIVIDUALLY
REMARK   4
REMARK   4 3UCM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-NOV-11.
REMARK 100 THE RCSB ID CODE IS RCSB068585.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 06-NOV-00
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.2
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9311
REMARK 200  MONOCHROMATOR                  : DIAMOND(001)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21341
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.046
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.3
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.09800
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.44900
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 3UCJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 62.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6-2.3 M SODIUM/POTASSIUM PHOSPHATE,
REMARK 280  15 MM THIOCYANATE, PH 7.2, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4
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      111.06950
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       38.41750
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       38.41750
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      166.60425
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       38.41750
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       38.41750
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       55.53475
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       38.41750
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       38.41750
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      166.60425
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       38.41750
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       38.41750
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       55.53475
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      111.06950
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: 21660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -300.0 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      222.13900
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     SER A     2
REMARK 465     ALA A     3
REMARK 465     LYS A     4
REMARK 465     ASP A     5
REMARK 465     MET B     1
REMARK 465     SER B     2
REMARK 465     ALA B     3
REMARK 465     LYS B     4
REMARK 465     ASP B     5
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 228  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SCN A 229   N
REMARK 620 2 HIS A 103   NE2 115.1
REMARK 620 3 CYS A  47   SG  101.5 111.8
REMARK 620 4 CYS A 106   SG  104.5 103.6 120.6
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 228  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SCN B 229   N
REMARK 620 2 HIS B 103   NE2 110.5
REMARK 620 3 CYS B 106   SG  102.0 117.1
REMARK 620 4 CYS B  47   SG   97.6 107.1 120.4
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 228
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 228
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN B 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN B 230
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UCJ   RELATED DB: PDB
REMARK 900 COCCOMYXA BETA-CARBONIC ANHYDRASE IN COMPLEX WITH
REMARK 900 ACETAZOLAMIDE
REMARK 900 RELATED ID: 3UCK   RELATED DB: PDB
REMARK 900 COCCOMYXA BETA-CARBONIC ANHYDRASE IN COMPLEX WITH PHOSPHATE
REMARK 900 RELATED ID: 3UCN   RELATED DB: PDB
REMARK 900 COCCOMYXA BETA-CARBONIC ANHYDRASE IN COMPLEX WITH AZIDE
REMARK 900 RELATED ID: 3UCO   RELATED DB: PDB
REMARK 900 COCCOMYXA BETA-CARBONIC ANHYDRASE IN COMPLEX WITH IODIDE
DBREF  3UCM A    1   227  UNP    Q96554   Q96554_9CHLO     1    227
DBREF  3UCM B    1   227  UNP    Q96554   Q96554_9CHLO     1    227
SEQRES   1 A  227  MET SER ALA LYS ASP THR ALA ASP LEU SER PRO LEU LEU
SEQRES   2 A  227  GLU ALA ASN ARG LYS TRP ALA ASP GLU CYS ALA ALA LYS
SEQRES   3 A  227  ASP SER THR TYR PHE SER LYS VAL ALA GLY SER GLN ALA
SEQRES   4 A  227  PRO GLU TYR LEU TYR ILE GLY CYS ALA ASP SER ARG VAL
SEQRES   5 A  227  SER PRO ALA GLN LEU PHE ASN MET ALA PRO GLY GLU VAL
SEQRES   6 A  227  PHE VAL GLN ARG ASN VAL GLY ASN LEU VAL SER ASN LYS
SEQRES   7 A  227  ASP LEU ASN CYS MET SER CYS LEU GLU TYR THR VAL ASP
SEQRES   8 A  227  HIS LEU LYS ILE LYS HIS ILE LEU VAL CYS GLY HIS TYR
SEQRES   9 A  227  ASN CYS GLY ALA CYS LYS ALA GLY LEU VAL TRP HIS PRO
SEQRES  10 A  227  LYS THR ALA GLY VAL THR ASN LEU TRP ILE SER ASP VAL
SEQRES  11 A  227  ARG GLU VAL ARG ASP LYS ASN ALA ALA LYS LEU HIS GLY
SEQRES  12 A  227  LEU SER ALA ASP ASP ALA TRP ASP LYS MET VAL GLU LEU
SEQRES  13 A  227  ASN VAL GLU ALA GLN VAL PHE ASN VAL CYS ALA SER PRO
SEQRES  14 A  227  ILE VAL GLN ALA ALA TRP ALA ARG GLY GLN PRO LEU SER
SEQRES  15 A  227  VAL HIS GLY ILE VAL TYR THR PRO GLY THR GLY LEU VAL
SEQRES  16 A  227  LYS GLU LEU ILE LYS PRO ILE THR GLY MET GLU ASP ALA
SEQRES  17 A  227  GLY ALA LEU LEU ARG ALA ASP LEU LYS GLN HIS CYS PHE
SEQRES  18 A  227  PHE SER GLU SER LEU ALA
SEQRES   1 B  227  MET SER ALA LYS ASP THR ALA ASP LEU SER PRO LEU LEU
SEQRES   2 B  227  GLU ALA ASN ARG LYS TRP ALA ASP GLU CYS ALA ALA LYS
SEQRES   3 B  227  ASP SER THR TYR PHE SER LYS VAL ALA GLY SER GLN ALA
SEQRES   4 B  227  PRO GLU TYR LEU TYR ILE GLY CYS ALA ASP SER ARG VAL
SEQRES   5 B  227  SER PRO ALA GLN LEU PHE ASN MET ALA PRO GLY GLU VAL
SEQRES   6 B  227  PHE VAL GLN ARG ASN VAL GLY ASN LEU VAL SER ASN LYS
SEQRES   7 B  227  ASP LEU ASN CYS MET SER CYS LEU GLU TYR THR VAL ASP
SEQRES   8 B  227  HIS LEU LYS ILE LYS HIS ILE LEU VAL CYS GLY HIS TYR
SEQRES   9 B  227  ASN CYS GLY ALA CYS LYS ALA GLY LEU VAL TRP HIS PRO
SEQRES  10 B  227  LYS THR ALA GLY VAL THR ASN LEU TRP ILE SER ASP VAL
SEQRES  11 B  227  ARG GLU VAL ARG ASP LYS ASN ALA ALA LYS LEU HIS GLY
SEQRES  12 B  227  LEU SER ALA ASP ASP ALA TRP ASP LYS MET VAL GLU LEU
SEQRES  13 B  227  ASN VAL GLU ALA GLN VAL PHE ASN VAL CYS ALA SER PRO
SEQRES  14 B  227  ILE VAL GLN ALA ALA TRP ALA ARG GLY GLN PRO LEU SER
SEQRES  15 B  227  VAL HIS GLY ILE VAL TYR THR PRO GLY THR GLY LEU VAL
SEQRES  16 B  227  LYS GLU LEU ILE LYS PRO ILE THR GLY MET GLU ASP ALA
SEQRES  17 B  227  GLY ALA LEU LEU ARG ALA ASP LEU LYS GLN HIS CYS PHE
SEQRES  18 B  227  PHE SER GLU SER LEU ALA
HET     ZN  A 228       1
HET    SCN  A 229       3
HET     ZN  B 228       1
HET    SCN  B 229       3
HET    SCN  B 230       3
HETNAM      ZN ZINC ION
HETNAM     SCN THIOCYANATE ION
FORMUL   3   ZN    2(ZN 2+)
FORMUL   4  SCN    3(C N S 1-)
FORMUL   8  HOH   *276(H2 O)
HELIX    1   1 LEU A    9  ASP A   27  1                                  19
HELIX    2   2 PHE A   31  ALA A   35  5                                   5
HELIX    3   3 SER A   53  ASN A   59  1                                   7
HELIX    4   4 ASP A   79  HIS A   92  1                                  14
HELIX    5   5 CYS A  106  TRP A  115  1                                  10
HELIX    6   6 GLY A  121  ILE A  127  1                                   7
HELIX    7   7 ILE A  127  LYS A  136  1                                  10
HELIX    8   8 ASN A  137  HIS A  142  1                                   6
HELIX    9   9 SER A  145  ALA A  167  1                                  23
HELIX   10  10 SER A  168  ARG A  177  1                                  10
HELIX   11  11 GLY A  204  LEU A  212  1                                   9
HELIX   12  12 ASP A  215  PHE A  221  1                                   7
HELIX   13  13 PHE A  222  LEU A  226  5                                   5
HELIX   14  14 LEU B    9  ASP B   27  1                                  19
HELIX   15  15 PHE B   31  ALA B   35  5                                   5
HELIX   16  16 SER B   53  PHE B   58  1                                   6
HELIX   17  17 ASP B   79  HIS B   92  1                                  14
HELIX   18  18 CYS B  106  TRP B  115  1                                  10
HELIX   19  19 GLY B  121  ILE B  127  1                                   7
HELIX   20  20 ILE B  127  ASN B  137  1                                  11
HELIX   21  21 ALA B  138  HIS B  142  5                                   5
HELIX   22  22 SER B  145  ALA B  167  1                                  23
HELIX   23  23 SER B  168  ARG B  177  1                                  10
HELIX   24  24 GLY B  204  LEU B  212  1                                   9
HELIX   25  25 ASP B  215  PHE B  222  1                                   8
HELIX   26  26 SER B  223  LEU B  226  5                                   4
SHEET    1   A 5 VAL A  65  ASN A  70  0
SHEET    2   A 5 TYR A  42  CYS A  47  1  N  TYR A  44   O  GLN A  68
SHEET    3   A 5 HIS A  97  HIS A 103  1  O  LEU A  99   N  LEU A  43
SHEET    4   A 5 SER A 182  TYR A 188  1  O  SER A 182   N  ILE A  98
SHEET    5   A 5 VAL A 195  ILE A 202 -1  O  ILE A 202   N  VAL A 183
SHEET    1   B 5 VAL B  65  ASN B  70  0
SHEET    2   B 5 TYR B  42  CYS B  47  1  N  GLY B  46   O  GLN B  68
SHEET    3   B 5 HIS B  97  HIS B 103  1  O  LEU B  99   N  LEU B  43
SHEET    4   B 5 SER B 182  TYR B 188  1  O  SER B 182   N  ILE B  98
SHEET    5   B 5 VAL B 195  ILE B 202 -1  O  LYS B 196   N  VAL B 187
LINK        ZN    ZN A 228                 N   SCN A 229     1555   1555  1.97
LINK        ZN    ZN B 228                 N   SCN B 229     1555   1555  1.97
LINK         NE2 HIS A 103                ZN    ZN A 228     1555   1555  2.07
LINK         NE2 HIS B 103                ZN    ZN B 228     1555   1555  2.10
LINK         SG  CYS A  47                ZN    ZN A 228     1555   1555  2.31
LINK         SG  CYS A 106                ZN    ZN A 228     1555   1555  2.35
LINK         SG  CYS B 106                ZN    ZN B 228     1555   1555  2.35
LINK         SG  CYS B  47                ZN    ZN B 228     1555   1555  2.36
SITE     1 AC1  4 CYS A  47  HIS A 103  CYS A 106  SCN A 229
SITE     1 AC2  4 CYS B  47  HIS B 103  CYS B 106  SCN B 229
SITE     1 AC3  7 CYS A  47  ASP A  49  HIS A 103  CYS A 106
SITE     2 AC3  7 GLY A 107   ZN A 228  TYR B  88
SITE     1 AC4  7 TYR A  88  CYS B  47  ASP B  49  HIS B 103
SITE     2 AC4  7 CYS B 106  GLY B 107   ZN B 228
SITE     1 AC5  4 PRO A  54  ARG A  69  PRO B  54  ARG B  69
CRYST1   76.835   76.835  222.139  90.00  90.00  90.00 P 43 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      0.013015  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013018  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004502        0.00000
      
PROCHECK
Go to PROCHECK summary
 References

 

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