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PDBsum entry 1dmx

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Top Page protein metals Protein-protein interface(s) links
Lyase (oxo-acid) PDB id
1dmx
Jmol
Contents
Protein chains
237 a.a. *
Metals
_ZN ×2
Waters ×123
* Residue conservation analysis
HEADER    LYASE (OXO-ACID)                        04-OCT-95   1DMX
TITLE     MURINE MITOCHONDRIAL CARBONIC ANYHDRASE V AT 2.45 ANGSTROMS
TITLE    2 RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MURINE CARBONIC ANHYDRASE V;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: CARBONATE DEHYDROGENASE, MCAVC;
COMPND   5 EC: 4.2.1.1;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE   4 ORGANISM_TAXID: 10090;
SOURCE   5 STRAIN: BALB/CJ;
SOURCE   6 CELL_LINE: BL21;
SOURCE   7 ORGAN: LIVER;
SOURCE   8 ORGANELLE: MITOCHONDRIA;
SOURCE   9 GENE: MCA5C;
SOURCE  10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  12 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PET31 T7;
SOURCE  14 EXPRESSION_SYSTEM_GENE: MCA5C;
SOURCE  15 OTHER_DETAILS: TRUNCATED VERSION OF PROTEIN WITH 21 N
SOURCE  16 TERMINAL RESIDUES REMOVED (SEE HECK ET AL., JBC, VOL 269
SOURCE  17 (1994) PP 24742-24746)
KEYWDS    PROTON TRANSFER, LYASE (OXO-ACID)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.A.BORIACK-SJODIN,D.W.CHRISTIANSON
REVDAT   3   24-FEB-09 1DMX    1       VERSN
REVDAT   2   01-APR-03 1DMX    1       JRNL
REVDAT   1   03-APR-96 1DMX    0
JRNL        AUTH   P.A.BORIACK-SJODIN,R.W.HECK,P.J.LAIPIS,
JRNL        AUTH 2 D.N.SILVERMAN,D.W.CHRISTIANSON
JRNL        TITL   STRUCTURE DETERMINATION OF MURINE MITOCHONDRIAL
JRNL        TITL 2 CARBONIC ANHYDRASE V AT 2.45-A RESOLUTION:
JRNL        TITL 3 IMPLICATIONS FOR CATALYTIC PROTON TRANSFER AND
JRNL        TITL 4 INHIBITOR DESIGN.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  92 10949 1995
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   7479916
JRNL        DOI    10.1073/PNAS.92.24.10949
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   R.W.HECK,S.M.TANHAUSER,R.MANDA,C.TU,P.J.LAIPIS,
REMARK   1  AUTH 2 D.N.SILVERMAN
REMARK   1  TITL   CATALYTIC PROPERTIES OF MOUSE CARBONIC ANHYDRASE V
REMARK   1  REF    J.BIOL.CHEM.                  V. 269 24742 1994
REMARK   1  REFN                   ISSN 0021-9258
REMARK   2
REMARK   2 RESOLUTION.    2.45 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
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)   (%) : 83.4
REMARK   3   NUMBER OF REFLECTIONS             : 17726
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.168
REMARK   3   FREE R VALUE                     : 0.286
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
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            : 3810
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 123
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) : 0.90
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) : 0.010
REMARK   3   BOND ANGLES            (DEGREES) : 1.80
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.12
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.40
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  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: CRYST1   TEXT TO EXPLAIN UNUSUAL
REMARK   3  UNIT-CELL DATA: TWO MOLECULES IN UNIT CELL RELATED BY
REMARK   3  NONCRYSTALLOGRAPHIC SYMMETRY SYMMETRY OPERATIONS FOR NON-
REMARK   3  STANDARD SETTING:
REMARK   4
REMARK   4 1DMX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 14-DEC-94
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : 7.2
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21760
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0
REMARK 200  DATA REDUNDANCY                : 2.000
REMARK 200  R MERGE                    (I) : 0.08200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 55.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
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
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 300 REMARK: MTRIX
REMARK 300  THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW
REMARK 300  DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE
REMARK 300  VARIOUS DOMAINS IN THIS ENTRY.  APPLYING THE APPROPRIATE
REMARK 300  MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL
REMARK 300  YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED
REMARK 300  SECOND.
REMARK 300
REMARK 300            APPLIED TO           TRANSFORMED TO
REMARK 300  MTRIX      RESIDUES               RESIDUES         RMSD
REMARK 300    M1   A   25  ..  A  261     B   25  ..  B  261   0.365
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     CYS A    22
REMARK 465     ALA A    23
REMARK 465     THR A    24
REMARK 465     LEU A   262
REMARK 465     ASP A   263
REMARK 465     ARG A   264
REMARK 465     THR A   265
REMARK 465     LYS A   266
REMARK 465     MET A   267
REMARK 465     ARG A   268
REMARK 465     SER A   269
REMARK 465     CYS B    22
REMARK 465     ALA B    23
REMARK 465     THR B    24
REMARK 465     LEU B   262
REMARK 465     ASP B   263
REMARK 465     ARG B   264
REMARK 465     THR B   265
REMARK 465     LYS B   266
REMARK 465     MET B   267
REMARK 465     ARG B   268
REMARK 465     SER B   269
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     ARG A 261    O
REMARK 470     ARG B 261    O
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    LEU B  59   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ARG A  27       60.65   -108.79
REMARK 500    GLU A  75       20.89    -67.90
REMARK 500    ASN A  86     -163.93   -167.72
REMARK 500    GLU A 138      -95.64    -10.39
REMARK 500    ASN A 244       48.45    -91.40
REMARK 500    ARG A 252     -129.47     63.95
REMARK 500    ARG B  57      -72.50   -126.52
REMARK 500    CYS B  74       90.15    -68.76
REMARK 500    ASN B 244       38.67    -92.23
REMARK 500    ARG B 252     -118.88     64.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH B 824        DISTANCE =  6.33 ANGSTROMS
REMARK 525    HOH B 825        DISTANCE =  5.44 ANGSTROMS
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 280  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 281   O
REMARK 620 2 HIS A  94   NE2  92.2
REMARK 620 3 HIS A 119   ND1 123.2 108.0
REMARK 620 4 HIS A  96   NE2 116.5 117.3 100.4
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 280  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B  96   NE2
REMARK 620 2 HIS B 119   ND1 102.6
REMARK 620 3 HOH B 781   O   131.5 103.5
REMARK 620 4 HIS B  94   NE2 119.1 111.2  87.7
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZIN
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTICALLY ACTIVE METAL ION
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 280
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 280
DBREF  1DMX A   25   269  UNP    P23589   CAH5A_MOUSE     55    299
DBREF  1DMX B   25   269  UNP    P23589   CAH5A_MOUSE     55    299
SEQADV 1DMX MET A  185  UNP  P23589    LEU   215 VARIANT
SEQADV 1DMX MET A  225  UNP  P23589    THR   255 VARIANT
SEQADV 1DMX MET B  185  UNP  P23589    LEU   215 VARIANT
SEQADV 1DMX MET B  225  UNP  P23589    THR   255 VARIANT
SEQRES   1 A  248  CYS ALA THR GLY THR ARG GLN SER PRO ILE ASN ILE GLN
SEQRES   2 A  248  TRP LYS ASP SER VAL TYR ASP PRO GLN LEU ALA PRO LEU
SEQRES   3 A  248  ARG VAL SER TYR ASP ALA ALA SER CYS ARG TYR LEU TRP
SEQRES   4 A  248  ASN THR GLY TYR PHE PHE GLN VAL GLU PHE ASP ASP SER
SEQRES   5 A  248  CYS GLU ASP SER GLY ILE SER GLY GLY PRO LEU GLY ASN
SEQRES   6 A  248  HIS TYR ARG LEU LYS GLN PHE HIS PHE HIS TRP GLY ALA
SEQRES   7 A  248  THR ASP GLU TRP GLY SER GLU HIS ALA VAL ASP GLY HIS
SEQRES   8 A  248  THR TYR PRO ALA GLU LEU HIS LEU VAL HIS TRP ASN SER
SEQRES   9 A  248  THR LYS TYR GLU ASN TYR LYS LYS ALA SER VAL GLY GLU
SEQRES  10 A  248  ASN GLY LEU ALA VAL ILE GLY VAL PHE LEU LYS LEU GLY
SEQRES  11 A  248  ALA HIS HIS GLN ALA LEU GLN LYS LEU VAL ASP VAL LEU
SEQRES  12 A  248  PRO GLU VAL ARG HIS LYS ASP THR GLN VAL ALA MET GLY
SEQRES  13 A  248  PRO PHE ASP PRO SER CYS LEU MET PRO ALA CYS ARG ASP
SEQRES  14 A  248  TYR TRP THR TYR PRO GLY SER LEU THR THR PRO PRO LEU
SEQRES  15 A  248  ALA GLU SER VAL THR TRP ILE VAL GLN LYS THR PRO VAL
SEQRES  16 A  248  GLU VAL SER PRO SER GLN LEU SER MET PHE ARG THR LEU
SEQRES  17 A  248  LEU PHE SER GLY ARG GLY GLU GLU GLU ASP VAL MET VAL
SEQRES  18 A  248  ASN ASN TYR ARG PRO LEU GLN PRO LEU ARG ASP ARG LYS
SEQRES  19 A  248  LEU ARG SER SER PHE ARG LEU ASP ARG THR LYS MET ARG
SEQRES  20 A  248  SER
SEQRES   1 B  248  CYS ALA THR GLY THR ARG GLN SER PRO ILE ASN ILE GLN
SEQRES   2 B  248  TRP LYS ASP SER VAL TYR ASP PRO GLN LEU ALA PRO LEU
SEQRES   3 B  248  ARG VAL SER TYR ASP ALA ALA SER CYS ARG TYR LEU TRP
SEQRES   4 B  248  ASN THR GLY TYR PHE PHE GLN VAL GLU PHE ASP ASP SER
SEQRES   5 B  248  CYS GLU ASP SER GLY ILE SER GLY GLY PRO LEU GLY ASN
SEQRES   6 B  248  HIS TYR ARG LEU LYS GLN PHE HIS PHE HIS TRP GLY ALA
SEQRES   7 B  248  THR ASP GLU TRP GLY SER GLU HIS ALA VAL ASP GLY HIS
SEQRES   8 B  248  THR TYR PRO ALA GLU LEU HIS LEU VAL HIS TRP ASN SER
SEQRES   9 B  248  THR LYS TYR GLU ASN TYR LYS LYS ALA SER VAL GLY GLU
SEQRES  10 B  248  ASN GLY LEU ALA VAL ILE GLY VAL PHE LEU LYS LEU GLY
SEQRES  11 B  248  ALA HIS HIS GLN ALA LEU GLN LYS LEU VAL ASP VAL LEU
SEQRES  12 B  248  PRO GLU VAL ARG HIS LYS ASP THR GLN VAL ALA MET GLY
SEQRES  13 B  248  PRO PHE ASP PRO SER CYS LEU MET PRO ALA CYS ARG ASP
SEQRES  14 B  248  TYR TRP THR TYR PRO GLY SER LEU THR THR PRO PRO LEU
SEQRES  15 B  248  ALA GLU SER VAL THR TRP ILE VAL GLN LYS THR PRO VAL
SEQRES  16 B  248  GLU VAL SER PRO SER GLN LEU SER MET PHE ARG THR LEU
SEQRES  17 B  248  LEU PHE SER GLY ARG GLY GLU GLU GLU ASP VAL MET VAL
SEQRES  18 B  248  ASN ASN TYR ARG PRO LEU GLN PRO LEU ARG ASP ARG LYS
SEQRES  19 B  248  LEU ARG SER SER PHE ARG LEU ASP ARG THR LYS MET ARG
SEQRES  20 B  248  SER
HET     ZN  A 280       1
HET     ZN  B 280       1
HETNAM      ZN ZINC ION
FORMUL   3   ZN    2(ZN 2+)
FORMUL   5  HOH   *123(H2 O)
HELIX    1   1 ALA A   53  SER A   55  5                                   3
HELIX    2   2 TYR A  131  VAL A  136  1                                   6
HELIX    3   3 GLN A  155  GLU A  166  1                                  12
HELIX    4   4 PRO A  181  LEU A  184  5                                   4
HELIX    5   5 PRO A  220  THR A  228  1                                   9
HELIX    6   6 TRP B   35  ASP B   37  5                                   3
HELIX    7   7 ALA B   53  SER B   55  5                                   3
HELIX    8   8 TYR B  131  VAL B  136  1                                   6
HELIX    9   9 GLN B  155  GLU B  166  1                                  12
HELIX   10  10 PRO B  181  LEU B  184  5                                   4
HELIX   11  11 PRO B  220  THR B  228  1                                   9
SHEET    1   A 2 SER A  38  TYR A  40  0
SHEET    2   A 2 LEU A 256  SER A 258  1  N  LEU A 256   O  VAL A  39
SHEET    1   B 2 ARG A  48  SER A  50  0
SHEET    2   B 2 GLY A  78  SER A  80 -1  N  SER A  80   O  ARG A  48
SHEET    1   C 8 GLN A 173  ALA A 175  0
SHEET    2   C 8 CYS A  56  ASN A  61 -1  N  LEU A  59   O  VAL A 174
SHEET    3   C 8 PHE A  66  PHE A  70 -1  N  GLU A  69   O  ARG A  57
SHEET    4   C 8 TYR A  88  TRP A  97 -1  N  PHE A  93   O  VAL A  68
SHEET    5   C 8 ALA A 116  ASN A 124 -1  N  TRP A 123   O  ARG A  89
SHEET    6   C 8 LEU A 141  LEU A 148 -1  N  LEU A 148   O  ALA A 116
SHEET    7   C 8 VAL A 207  GLN A 212  1  N  THR A 208   O  LEU A 141
SHEET    8   C 8 TYR A 191  GLY A 196 -1  N  GLY A 196   O  VAL A 207
SHEET    1   D 2 LEU A 148  LEU A 150  0
SHEET    2   D 2 VAL A 216  VAL A 218  1  N  VAL A 216   O  LYS A 149
SHEET    1   E 2 SER B  38  TYR B  40  0
SHEET    2   E 2 LEU B 256  SER B 258  1  N  LEU B 256   O  VAL B  39
SHEET    1   F 8 GLN B 173  ALA B 175  0
SHEET    2   F 8 CYS B  56  ASN B  61 -1  N  LEU B  59   O  VAL B 174
SHEET    3   F 8 PHE B  66  PHE B  70 -1  N  GLU B  69   O  ARG B  57
SHEET    4   F 8 TYR B  88  TRP B  97 -1  N  PHE B  93   O  VAL B  68
SHEET    5   F 8 ALA B 116  ASN B 124 -1  N  TRP B 123   O  ARG B  89
SHEET    6   F 8 LEU B 141  LEU B 148 -1  N  LEU B 148   O  ALA B 116
SHEET    7   F 8 VAL B 207  GLN B 212  1  N  THR B 208   O  LEU B 141
SHEET    8   F 8 TYR B 191  GLY B 196 -1  N  GLY B 196   O  VAL B 207
SHEET    1   G 2 LEU B 148  LEU B 150  0
SHEET    2   G 2 VAL B 216  VAL B 218  1  N  VAL B 216   O  LYS B 149
SHEET    1   H 2 ALA B  45  SER B  50  0
SHEET    2   H 2 GLY B  78  GLY B  82 -1  N  GLY B  82   O  ALA B  45
LINK        ZN    ZN A 280                 O   HOH A 281     1555   1555  2.04
LINK        ZN    ZN A 280                 NE2 HIS A  94     1555   1555  2.38
LINK        ZN    ZN A 280                 ND1 HIS A 119     1555   1555  2.03
LINK        ZN    ZN A 280                 NE2 HIS A  96     1555   1555  2.14
LINK        ZN    ZN B 280                 NE2 HIS B  96     1555   1555  2.05
LINK        ZN    ZN B 280                 ND1 HIS B 119     1555   1555  2.30
LINK        ZN    ZN B 280                 O   HOH B 781     1555   1555  1.94
LINK        ZN    ZN B 280                 NE2 HIS B  94     1555   1555  2.09
CISPEP   1 SER A   29    PRO A   30          0        -0.02
CISPEP   2 PRO A  201    PRO A  202          0         0.46
CISPEP   3 SER B   29    PRO B   30          0        -0.25
CISPEP   4 PRO B  201    PRO B  202          0         0.15
SITE     1 ZIN  2  ZN A 280   ZN B 280
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  HOH A 281
SITE     1 AC2  4 HIS B  94  HIS B  96  HIS B 119  HOH B 781
CRYST1   48.690   60.370   60.440  67.65  75.26  75.21 P 1           2
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      0.020538 -0.005423 -0.003797        0.00000
SCALE2      0.000000  0.017132 -0.006137        0.00000
SCALE3      0.000000  0.000000  0.018173        0.00000
MTRIX1   1 -0.999729  0.015547 -0.017320      115.91269    1
MTRIX2   1  0.011121 -0.334626 -0.942285      108.89589    1
MTRIX3   1 -0.020446 -0.942223  0.334362       37.20825    1
      
PROCHECK
Go to PROCHECK summary
 References