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PDBsum entry 2nnv

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Lyase PDB id
2nnv
Jmol
Contents
Protein chain
259 a.a.
Ligands
M29 ×2
GOL
Metals
_ZN
Waters ×256
HEADER    LYASE                                   24-OCT-06   2NNV
TITLE     STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE II
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONIC ANHYDRASE II, CARBONATE DEHYDRATASE II, CA-II,
COMPND   5 CARBONIC ANHYDRASE C;
COMPND   6 EC: 4.2.1.1;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: CA2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS    ZINC METALLOENZYME, SULFONAMIDE, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.W.CHRISTIANSON,K.M.JUDE
REVDAT   3   13-JUL-11 2NNV    1       VERSN
REVDAT   2   24-FEB-09 2NNV    1       VERSN
REVDAT   1   08-MAY-07 2NNV    0
JRNL        AUTH   D.K.SRIVASTAVA,K.M.JUDE,A.L.BANERJEE,M.HALDAR,S.MANOKARAN,
JRNL        AUTH 2 J.KOOREN,S.MALLIK,D.W.CHRISTIANSON
JRNL        TITL   STRUCTURAL ANALYSIS OF CHARGE DISCRIMINATION IN THE BINDING
JRNL        TITL 2 OF INHIBITORS TO HUMAN CARBONIC ANHYDRASES I AND II.
JRNL        REF    J.AM.CHEM.SOC.                V. 129  5528 2007
JRNL        REFN                   ISSN 0002-7863
JRNL        PMID   17407288
JRNL        DOI    10.1021/JA068359W
REMARK   2
REMARK   2 RESOLUTION.    1.10 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) : 1.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 80.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.5
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) : 0.133
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.132
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.164
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 2.000
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 1802
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.122
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.121
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.152
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 2.000
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 1469
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 72147
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 2066
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 41
REMARK   3   SOLVENT ATOMS      : 256
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 21825
REMARK   3   NUMBER OF RESTRAINTS                     : 27367
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.015
REMARK   3   ANGLE DISTANCES                      (A) : 0.031
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.031
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.093
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.086
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.077
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.005
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.050
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.092
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-228
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REDUCED FREE R
REMARK   3  (NO CUTOFF) BY 0.0385. ADDITION OF RIDING HYDROGENS REDUCED FREE
REMARK   3  R BY 0.0157.
REMARK   4
REMARK   4 2NNV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-OCT-06.
REMARK 100 THE RCSB ID CODE IS RCSB040090.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-NOV-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.7
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) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 90979
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 80.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.7
REMARK 200  DATA REDUNDANCY                : 2.400
REMARK 200  R MERGE                    (I) : 0.07200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.14
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.34800
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2CBA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: (NH4)2SO4, TRIS, PH 7.7, VAPOR
REMARK 280  DIFFUSION, TEMPERATURE 277K
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       20.60650
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 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     MET A     1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    HIS A  15   ND1   HIS A  15   CE1    -0.100
REMARK 500
REMARK 500 REMARK: NULL
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    HIS A  15   CG  -  ND1 -  CE1 ANGL. DEV. =  13.3 DEGREES
REMARK 500    HIS A  15   ND1 -  CE1 -  NE2 ANGL. DEV. =  -7.4 DEGREES
REMARK 500    TYR A  40   CB  -  CG  -  CD2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    TYR A  40   CB  -  CG  -  CD1 ANGL. DEV. =   4.4 DEGREES
REMARK 500    ASP A 130   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES
REMARK 500    ARG A 182   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    GLU A 221   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.8 DEGREES
REMARK 500    GLU A 239   CA  -  CB  -  CG  ANGL. DEV. =  14.3 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    ASN A  11       15.23   -143.21
REMARK 500    ARG A  27       55.90   -144.39
REMARK 500    GLU A 106      -60.57    -91.02
REMARK 500    LYS A 111       -1.10     75.20
REMARK 500    PHE A 176       61.94   -151.61
REMARK 500    ASN A 244       48.01    -92.90
REMARK 500    LYS A 252     -139.03     53.68
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 A 626        DISTANCE =  5.60 ANGSTROMS
REMARK 525    HOH A 651        DISTANCE =  5.18 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                             CMH A 206  HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 137   O
REMARK 620 2 CMH A 206   SG   89.9
REMARK 620 3 CMH A 206   CM   90.5 179.4
REMARK 620 4 HOH A 556   O   142.7  95.4  84.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 119   ND1
REMARK 620 2 HIS A  94   NE2 111.7
REMARK 620 3 M29 A 301   N   116.2 112.4
REMARK 620 4 HIS A  96   NE2  98.7 102.6 113.7
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 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE M29 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE M29 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 311
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2NMX   RELATED DB: PDB
REMARK 900 STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE I
REMARK 900 RELATED ID: 2NN1   RELATED DB: PDB
REMARK 900 STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE I
REMARK 900 RELATED ID: 2NNG   RELATED DB: PDB
REMARK 900 STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 2NN7   RELATED DB: PDB
REMARK 900 STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE I
REMARK 900 RELATED ID: 2NNS   RELATED DB: PDB
REMARK 900 STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 2NNO   RELATED DB: PDB
REMARK 900 STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE II
DBREF  2NNV A    2   261  UNP    P00918   CAH2_HUMAN       1    259
SEQADV 2NNV MET A    1  UNP  P00918              CLONING ARTIFACT
SEQRES   1 A  260  MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO
SEQRES   2 A  260  GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES   3 A  260  ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES   4 A  260  TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES   5 A  260  GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA
SEQRES   6 A  260  PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES   7 A  260  LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES   8 A  260  GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY
SEQRES   9 A  260  SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES  10 A  260  LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES  11 A  260  GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES  12 A  260  GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES  13 A  260  GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES  14 A  260  GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES  15 A  260  LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES  16 A  260  SER LEU THR THR PRO PRO LEU LEU GLU CMH VAL THR TRP
SEQRES  17 A  260  ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES  18 A  260  VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES  19 A  260  GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA
SEQRES  20 A  260  GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
MODRES 2NNV CMH A  206  CYS  S-(METHYLMERCURY)-L-CYSTEINE
HET    CMH  A 206      10
HET     ZN  A 262       1
HET    M29  A 301      17
HET    M29  A 302      17
HET    GOL  A 311       6
HETNAM     CMH S-(METHYLMERCURY)-L-CYSTEINE
HETNAM      ZN ZINC ION
HETNAM     M29 ETHYL 3-[4-(AMINOSULFONYL)PHENYL]PROPANOATE
HETNAM     GOL GLYCEROL
HETSYN     M29 4-PROPYL BENZENESULFONAMIDE ETHYL ESTER
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   1  CMH    C4 H9 HG N O2 S
FORMUL   2   ZN    ZN 2+
FORMUL   3  M29    2(C11 H15 N O4 S)
FORMUL   5  GOL    C3 H8 O3
FORMUL   6  HOH   *256(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  127  GLY A  129  5                                   3
HELIX    4   4 ASP A  130  VAL A  135  1                                   6
HELIX    5   5 LYS A  154  GLY A  156  5                                   3
HELIX    6   6 LEU A  157  LEU A  164  1                                   8
HELIX    7   7 ASP A  165  ILE A  167  5                                   3
HELIX    8   8 ASP A  180  LEU A  185  5                                   6
HELIX    9   9 SER A  219  ARG A  227  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 257  ALA A 258  1  O  ALA A 258   N  LYS A  39
SHEET    3   B10 TYR A 191  GLY A 196 -1  N  THR A 193   O  LYS A 257
SHEET    4   B10 VAL A 207  LEU A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5   B10 LEU A 141  VAL A 150  1  N  GLY A 145   O  LEU A 212
SHEET    6   B10 ALA A 116  ASN A 124 -1  N  LEU A 118   O  ILE A 146
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  HIS A  94   O  HIS A 119
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 173  ASP A 175 -1  O  ALA A 174   N  ILE A  59
SHEET    1   C 6 LEU A  47  SER A  50  0
SHEET    2   C 6 VAL A  78  GLY A  81 -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  HIS A 119   N  HIS A  94
SHEET    5   C 6 LEU A 141  VAL A 150 -1  O  ILE A 146   N  LEU A 118
SHEET    6   C 6 ILE A 216  VAL A 218  1  O  ILE A 216   N  PHE A 147
LINK         C   GLU A 205                 N   CMH A 206     1555   1555  1.33
LINK         C   CMH A 206                 N   VAL A 207     1555   1555  1.32
LINK        HG  ACMH A 206                 O   GLN A 137     1555   1555  3.00
LINK        HG  ACMH A 206                 O   HOH A 556     1555   1555  3.06
LINK        ZN    ZN A 262                 ND1 HIS A 119     1555   1555  2.03
LINK        ZN    ZN A 262                 NE2 HIS A  94     1555   1555  1.99
LINK        ZN    ZN A 262                 N   M29 A 301     1555   1555  1.92
LINK        ZN    ZN A 262                 NE2 HIS A  96     1555   1555  2.00
CISPEP   1 SER A   29    PRO A   30          0        -3.43
CISPEP   2 PRO A  201    PRO A  202          0         8.69
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  M29 A 301
SITE     1 AC2  8 HIS A  94  HIS A  96  HIS A 119  LEU A 198
SITE     2 AC2  8 THR A 199  THR A 200  TRP A 209   ZN A 262
SITE     1 AC3 10 TRP A   5  HIS A  10  ASN A  11  HIS A  15
SITE     2 AC3 10 TRP A  16  ASP A  19  PHE A  20  GLY A 156
SITE     3 AC3 10 HOH A 453  HOH A 513
SITE     1 AC4 10 ASN A  62  HIS A  64  ALA A  65  ASN A  67
SITE     2 AC4 10 GLN A  92  HIS A  94  THR A 200  HOH A 409
SITE     3 AC4 10 HOH A 414  HOH A 632
CRYST1   42.365   41.213   72.145  90.00 104.83  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      0.023604  0.000000  0.006250        0.00000
SCALE2      0.000000  0.024264  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014339        0.00000
      
PROCHECK
Go to PROCHECK summary
 References