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PDBsum entry 3kne

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Lyase PDB id
3kne
Jmol
Contents
Protein chain
257 a.a.
Ligands
BE7
DAW
Metals
_ZN
Waters ×219
HEADER    LYASE                                   12-NOV-09   3KNE
TITLE     CARBONIC ANHYDRASE II H64C MUTANT IN COMPLEX WITH AN IN SITU FORMED
TITLE    2 TRIAZOLE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONIC ANHYDRASE II, CA-II, CARBONATE DEHYDRATASE II,
COMPND   5 CARBONIC ANHYDRASE C, CAC;
COMPND   6 EC: 4.2.1.1;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_TAXID: 9606;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21 CODON+;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PGEX-4T1
KEYWDS    10 STRANDED; TWISTED BETA-SHEETS; LYASE; ACETYLATION, METAL-BINDING,
KEYWDS   2 CLICK-CHEMISTRY, AZIDE, ALKYNE, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.SCHULZE-WISCHELER,A.HEINE,G.KLEBE
REVDAT   1   18-MAY-11 3KNE    0
JRNL        AUTH   J.SCHULZE WISCHELER,D.SUN,N.U.SANDNER,U.LINNE,A.HEINE,
JRNL        AUTH 2 U.KOERT,G.KLEBE
JRNL        TITL   STEREO- AND REGIOSELECTIVE AZIDE/ALKYNE CYCLOADDITIONS IN
JRNL        TITL 2 CARBONIC ANHYDRASE II VIA TETHERING, MONITORED BY
JRNL        TITL 3 CRYSTALLOGRAPHY AND MASS SPECTROMETRY.
JRNL        REF    CHEMISTRY                     V.  17  5842 2011
JRNL        REFN                   ISSN 0947-6539
JRNL        PMID   21506176
JRNL        DOI    10.1002/CHEM.201002437
REMARK   2
REMARK   2 RESOLUTION.    1.35 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : SHELXL-97
REMARK   3   AUTHORS     : G.M.SHELDRICK
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 4.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.7
REMARK   3   CROSS-VALIDATION METHOD           : FREE R
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.129
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.128
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.183
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2538
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 50551
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.121
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.120
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.173
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 2128
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 42802
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 2030
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 44
REMARK   3   SOLVENT ATOMS      : 219
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 2289.56
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 1983.00
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 8
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 20979
REMARK   3   NUMBER OF RESTRAINTS                     : 26509
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.012
REMARK   3   ANGLE DISTANCES                      (A) : 0.028
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.030
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.064
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.068
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.042
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.004
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.051
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.083
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: NULL
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY THE
REMARK   3  METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28(1995)53-56
REMARK   4
REMARK   4 3KNE COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-NOV-09.
REMARK 100 THE RCSB ID CODE IS RCSB056208.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 04-NOV-09
REMARK 200  TEMPERATURE           (KELVIN) : 110
REMARK 200  PH                             : 7.8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : BESSY
REMARK 200  BEAMLINE                       : 14.2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91841
REMARK 200  MONOCHROMATOR                  : SI-111 CRYSTALL
REMARK 200  OPTICS                         : SILICON
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52457
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.350
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2
REMARK 200  DATA REDUNDANCY                : 3.000
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.07400
REMARK 200   FOR THE DATA SET  : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.37
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.33500
REMARK 200   FOR SHELL         : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5M AMMONIUM SULFATE, 50MM TRIS,
REMARK 280  0.1MM P-CHLOROMERCURICBENZOIC ACID,500 M ALKYNE, 500 M AZIDE, 500
REMARK 280  M DTT, PH 7.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y+1/2,-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   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       20.75000
REMARK 290   SMTRY3   2  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 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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     GLY A    -4
REMARK 465     SER A    -3
REMARK 465     PRO A    -2
REMARK 465     GLU A    -1
REMARK 465     PHE A     0
REMARK 465     MET A     1
REMARK 465     SER A     2
REMARK 465     HIS A     3
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     LYS A 224    CG   CD   CE   NZ
REMARK 470     GLU A 238    CG   CD   OE1  OE2
REMARK 470     ASN A 252    CG   OD1
REMARK 470     LYS A 260    CG   CD   CE   NZ
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    ARG A  58   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    CYS A  64   CA  -  CB  -  SG  ANGL. DEV. =   7.1 DEGREES
REMARK 500    ASP A 129   CB  -  CG  -  OD1 ANGL. DEV. =   8.3 DEGREES
REMARK 500    LEU A 188   O   -  C   -  N   ANGL. DEV. = -12.7 DEGREES
REMARK 500    ARG A 226   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 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       51.89   -143.32
REMARK 500    LYS A  76      -50.68   -126.12
REMARK 500    GLU A 106      -62.82    -92.50
REMARK 500    LYS A 111       -2.74     73.87
REMARK 500    ASN A 243       49.08    -90.18
REMARK 500    LYS A 251     -137.08     53.45
REMARK 500    ASN A 252       45.15    -89.80
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 A1201        DISTANCE =  5.41 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     BE7 A  501
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 500  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  94   NE2
REMARK 620 2 HIS A  96   NE2 103.8
REMARK 620 3 HIS A 119   ND1 113.3  98.9
REMARK 620 4 DAW A 502   N1  112.6 113.3 113.8
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             BE7 A 501  HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 136   O
REMARK 620 2 BE7 A 501   C5   96.8
REMARK 620 3 GLU A 204   O    91.8  85.2
REMARK 620 N                    1     2
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 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BE7 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAW A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KIG   RELATED DB: PDB
REMARK 900 MUTANT CARBONIC ANHYDRASE II IN COMPLEX WITH AN AZIDE AND
REMARK 900 AN ALKYNE
DBREF  3KNE A    1   260  UNP    P00918   CAH2_HUMAN       1    260
SEQADV 3KNE GLY A   -4  UNP  P00918              EXPRESSION TAG
SEQADV 3KNE SER A   -3  UNP  P00918              EXPRESSION TAG
SEQADV 3KNE PRO A   -2  UNP  P00918              EXPRESSION TAG
SEQADV 3KNE GLU A   -1  UNP  P00918              EXPRESSION TAG
SEQADV 3KNE PHE A    0  UNP  P00918              EXPRESSION TAG
SEQADV 3KNE CYS A   64  UNP  P00918    HIS    64 ENGINEERED
SEQRES   1 A  265  GLY SER PRO GLU PHE MET SER HIS HIS TRP GLY TYR GLY
SEQRES   2 A  265  LYS HIS ASN GLY PRO GLU HIS TRP HIS LYS ASP PHE PRO
SEQRES   3 A  265  ILE ALA LYS GLY GLU ARG GLN SER PRO VAL ASP ILE ASP
SEQRES   4 A  265  THR HIS THR ALA LYS TYR ASP PRO SER LEU LYS PRO LEU
SEQRES   5 A  265  SER VAL SER TYR ASP GLN ALA THR SER LEU ARG ILE LEU
SEQRES   6 A  265  ASN ASN GLY CYS ALA PHE ASN VAL GLU PHE ASP ASP SER
SEQRES   7 A  265  GLN ASP LYS ALA VAL LEU LYS GLY GLY PRO LEU ASP GLY
SEQRES   8 A  265  THR TYR ARG LEU ILE GLN PHE HIS PHE HIS TRP GLY SER
SEQRES   9 A  265  LEU ASP GLY GLN GLY SER GLU HIS THR VAL ASP LYS LYS
SEQRES  10 A  265  LYS TYR ALA ALA GLU LEU HIS LEU VAL HIS TRP ASN THR
SEQRES  11 A  265  LYS TYR GLY ASP PHE GLY LYS ALA VAL GLN GLN PRO ASP
SEQRES  12 A  265  GLY LEU ALA VAL LEU GLY ILE PHE LEU LYS VAL GLY SER
SEQRES  13 A  265  ALA LYS PRO GLY LEU GLN LYS VAL VAL ASP VAL LEU ASP
SEQRES  14 A  265  SER ILE LYS THR LYS GLY LYS SER ALA ASP PHE THR ASN
SEQRES  15 A  265  PHE ASP PRO ARG GLY LEU LEU PRO GLU SER LEU ASP TYR
SEQRES  16 A  265  TRP THR TYR PRO GLY SER LEU THR THR PRO PRO LEU LEU
SEQRES  17 A  265  GLU CYS VAL THR TRP ILE VAL LEU LYS GLU PRO ILE SER
SEQRES  18 A  265  VAL SER SER GLU GLN VAL LEU LYS PHE ARG LYS LEU ASN
SEQRES  19 A  265  PHE ASN GLY GLU GLY GLU PRO GLU GLU LEU MET VAL ASP
SEQRES  20 A  265  ASN TRP ARG PRO ALA GLN PRO LEU LYS ASN ARG GLN ILE
SEQRES  21 A  265  LYS ALA SER PHE LYS
HET     ZN  A 500       1
HET    BE7  A 501      10
HET    DAW  A 502      41
HETNAM      ZN ZINC ION
HETNAM     BE7 (4-CARBOXYPHENYL)(CHLORO)MERCURY
HETNAM     DAW N-[(S)-(1-{2-OXO-2-[(3-SULFANYLPROPYL)AMINO]ETHYL}-1H-
HETNAM   2 DAW  1,2,3-TRIAZOL-5-YL)(PHENYL)METHYL]-4-
HETNAM   3 DAW  SULFAMOYLBENZAMIDE
HETSYN     BE7 P-CHLOROMERCURIBENZOIC ACID
FORMUL   2   ZN    ZN 2+
FORMUL   3  BE7    C7 H5 CL HG O2
FORMUL   4  DAW    C21 H24 N6 O4 S2
FORMUL   5  HOH   *219(H2 O)
HELIX    1   1 HIS A   15  ASP A   19  5                                   5
HELIX    2   2 PHE A   20  GLY A   25  5                                   6
HELIX    3   3 LYS A  126  GLY A  128  5                                   3
HELIX    4   4 ASP A  129  VAL A  134  1                                   6
HELIX    5   5 LYS A  153  GLY A  155  5                                   3
HELIX    6   6 LEU A  156  LEU A  163  1                                   8
HELIX    7   7 ASP A  164  ILE A  166  5                                   3
HELIX    8   8 ASP A  179  LEU A  184  5                                   6
HELIX    9   9 SER A  218  ARG A  226  1                                   9
SHEET    1   A 2 ASP A  32  ILE A  33  0
SHEET    2   A 2 THR A 108  VAL A 109  1  O  THR A 108   N  ILE A  33
SHEET    1   B10 LYS A  39  TYR A  40  0
SHEET    2   B10 LYS A 256  ALA A 257  1  O  ALA A 257   N  LYS A  39
SHEET    3   B10 TYR A 190  GLY A 195 -1  N  THR A 192   O  LYS A 256
SHEET    4   B10 VAL A 206  LEU A 211 -1  O  VAL A 206   N  GLY A 195
SHEET    5   B10 LEU A 140  VAL A 149  1  N  GLY A 144   O  LEU A 211
SHEET    6   B10 ALA A 116  ASN A 124 -1  N  LEU A 118   O  ILE A 145
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  GLN A  92   O  VAL A 121
SHEET    8   B10 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET    9   B10 SER A  56  ASN A  61 -1  N  LEU A  57   O  GLU A  69
SHEET   10   B10 SER A 172  ASP A 174 -1  O  ALA A 173   N  ILE A  59
SHEET    1   C 6 LYS A  45  SER A  50  0
SHEET    2   C 6 VAL A  78  GLY A  82 -1  O  LYS A  80   N  SER A  48
SHEET    3   C 6 TYR A  88  TRP A  97 -1  O  TYR A  88   N  LEU A  79
SHEET    4   C 6 ALA A 116  ASN A 124 -1  O  VAL A 121   N  GLN A  92
SHEET    5   C 6 LEU A 140  VAL A 149 -1  O  ILE A 145   N  LEU A 118
SHEET    6   C 6 ILE A 215  VAL A 217  1  O  ILE A 215   N  PHE A 146
LINK         NE2 HIS A  94                ZN    ZN A 500     1555   1555  2.00
LINK         NE2 HIS A  96                ZN    ZN A 500     1555   1555  2.02
LINK         ND1 HIS A 119                ZN    ZN A 500     1555   1555  2.11
LINK        ZN    ZN A 500                 N1  DAW A 502     1555   1555  1.93
LINK         SG ACYS A  64                 S2 ADAW A 502     1555   1555  1.89
LINK         O   GLN A 136                HG   BE7 A 501     1555   1555  2.95
LINK         O   GLU A 204                HG   BE7 A 501     1555   1555  3.14
CISPEP   1 SER A   29    PRO A   30          0        -0.22
CISPEP   2 PRO A  200    PRO A  201          0        13.47
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  DAW A 502
SITE     1 AC2  5 GLN A 135  GLN A 136  PRO A 137  GLU A 204
SITE     2 AC2  5 CYS A 205
SITE     1 AC3 17 TYR A   7  ASN A  62  CYS A  64  ALA A  65
SITE     2 AC3 17 ASN A  67  GLN A  92  HIS A  94  HIS A  96
SITE     3 AC3 17 HIS A 119  PHE A 130  LEU A 197  THR A 198
SITE     4 AC3 17 THR A 199  TRP A 208   ZN A 500  HOH A1043
SITE     5 AC3 17 HOH A1046
CRYST1   42.400   41.500   72.000  90.00 104.30  90.00 P 1 21 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      0.023585  0.000000  0.006012        0.00000
SCALE2      0.000000  0.024096  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014333        0.00000
      
PROCHECK
Go to PROCHECK summary
 References