spacer
spacer

PDBsum entry 1zfk

Go to PDB code: 
Top Page protein ligands metals links
Lyase PDB id
1zfk
Jmol
Contents
Protein chain
256 a.a.
Ligands
SO4
NR2 ×2
BE7
GOL
Metals
_ZN
Waters ×266
HEADER    LYASE                                   20-APR-05   1ZFK
TITLE     CARBONIC ANHYDRASE II IN COMPLEX WITH N-4-SULFONAMIDPHENYL-N'-4-
TITLE    2 METHYLBENZOSULFONYLUREASE AS SULFONAMIDE INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE II;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE II, CA-II, CARBONIC ANHYDRASE C;
COMPND   5 EC: 4.2.1.1;
COMPND   6 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;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    10 STRANDED, TWISTED BETA-SHEETS, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    V.S.HONNDORF,A.HEINE,G.KLEBE,C.T.SUPURAN
REVDAT   3   13-JUL-11 1ZFK    1       VERSN
REVDAT   2   24-FEB-09 1ZFK    1       VERSN
REVDAT   1   23-MAY-06 1ZFK    0
JRNL        AUTH   V.S.HONNDORF,A.HEINE,G.KLEBE,C.T.SUPURAN
JRNL        TITL   CARBONIC ANHYDRASE II IN COMPLEX WITH
JRNL        TITL 2 N-4-SULFONAMIDPHENYL-N'-4-METHYLBENZOSULFONYLUREASE AS
JRNL        TITL 3 SULFONAMIDE INHIBITOR
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.56 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) : 1.56
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
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) : 0.164
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.164
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.224
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 1599
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 32371
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 2031
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 70
REMARK   3   SOLVENT ATOMS      : 266
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       : NULL
REMARK   3   NUMBER OF RESTRAINTS                     : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.009
REMARK   3   ANGLE DISTANCES                      (A) : 0.027
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.030
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.059
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.055
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : NULL
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: NULL
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & 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 1ZFK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-05.
REMARK 100 THE RCSB ID CODE IS RCSB032661.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 09-FEB-05
REMARK 200  TEMPERATURE           (KELVIN) : 103
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32665
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.560
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.1
REMARK 200  DATA REDUNDANCY                : 3.500
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.07000
REMARK 200   FOR THE DATA SET  : 14.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.59
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.4
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.19600
REMARK 200   FOR SHELL         : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, SODIUM CHLORIDE, P-
REMARK 280  CHLOROMERCURIBENZOIC ACID, TRIS HCL , PH 8.0, COCRYSTALLIZATION,
REMARK 280  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       20.75500
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     SER A  1002
REMARK 465     HIS A  1003
REMARK 465     LYS A  1261
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 A1009    CG   CD   CE   NZ
REMARK 470     GLN A1053    CG   CD   OE1  NE2
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 A1027   CA  -  CB  -  CG  ANGL. DEV. =  13.7 DEGREES
REMARK 500    TYR A1051   CB  -  CG  -  CD1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    PHE A1226   CB  -  CG  -  CD2 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    ARG A1227   CD  -  NE  -  CZ  ANGL. DEV. =   8.8 DEGREES
REMARK 500    ASN A1253   C   -  N   -  CA  ANGL. DEV. =  17.8 DEGREES
REMARK 500    ARG A1254   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG A1254   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 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 A1011       18.49   -140.95
REMARK 500    ARG A1027       50.87   -146.17
REMARK 500    ALA A1065     -166.72   -161.03
REMARK 500    LYS A1076      -81.94    -70.07
REMARK 500    PHE A1176       61.64   -150.28
REMARK 500    ASN A1244       49.30    -95.17
REMARK 500    LYS A1252     -138.23     53.91
REMARK 500    ASN A1253       46.61    -84.52
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 A3223        DISTANCE =  5.50 ANGSTROMS
REMARK 525    HOH A3258        DISTANCE =  5.22 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 1700
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                             BE7 A1700  HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1206   SG
REMARK 620 2 BE7 A1700   C5  172.7
REMARK 620 3 GLU A1205   O    97.2  77.5
REMARK 620 4 GLN A1137   O    85.7  99.4  92.4
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A1300  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A1119   ND1
REMARK 620 2 HIS A1094   NE2 113.1
REMARK 620 3 NR2 A1400   N24 115.9 108.3
REMARK 620 4 HIS A1096   NE2  97.7 105.7 115.5
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 1300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NR2 A 1400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NR2 A 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BE7 A 1700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1900
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A42   RELATED DB: PDB
REMARK 900 CA II IN COMPLEX WITH BRINZOLAMIDE
REMARK 900 RELATED ID: 1OQ5   RELATED DB: PDB
REMARK 900 CA II IN COMPLEX WITH CELECOXIB
REMARK 900 RELATED ID: 1Z9Y   RELATED DB: PDB
REMARK 900 CA II IN COMPLEX WITH FUROSEMIDE
DBREF  1ZFK A 1002  1260  UNP    P00918   CAH2_HUMAN       1    259
SEQRES   1 A  259  SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU
SEQRES   2 A  259  HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG
SEQRES   3 A  259  GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR
SEQRES   4 A  259  ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN
SEQRES   5 A  259  ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE
SEQRES   6 A  259  ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU
SEQRES   7 A  259  LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN
SEQRES   8 A  259  PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER
SEQRES   9 A  259  GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU
SEQRES  10 A  259  HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY
SEQRES  11 A  259  LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY
SEQRES  12 A  259  ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN
SEQRES  13 A  259  LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY
SEQRES  14 A  259  LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU
SEQRES  15 A  259  LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER
SEQRES  16 A  259  LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE
SEQRES  17 A  259  VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL
SEQRES  18 A  259  LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU
SEQRES  19 A  259  PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN
SEQRES  20 A  259  PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     ZN  A1300       1
HET    SO4  A1600       5
HET    NR2  A1400      24
HET    NR2  A1500      24
HET    BE7  A1700      10
HET    GOL  A1900       6
HETNAM      ZN ZINC ION
HETNAM     SO4 SULFATE ION
HETNAM     NR2 N-({[4-(AMINOSULFONYL)PHENYL]AMINO}CARBONYL)-4-
HETNAM   2 NR2  METHYLBENZENESULFONAMIDE
HETNAM     BE7 (4-CARBOXYPHENYL)(CHLORO)MERCURY
HETNAM     GOL GLYCEROL
HETSYN     BE7 P-CHLOROMERCURIBENZOIC ACID
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2   ZN    ZN 2+
FORMUL   3  SO4    O4 S 2-
FORMUL   4  NR2    2(C14 H15 N3 O5 S2)
FORMUL   6  BE7    C7 H5 CL HG O2
FORMUL   7  GOL    C3 H8 O3
FORMUL   8  HOH   *266(H2 O)
HELIX    1   1 HIS A 1015  ASP A 1019  5                                   5
HELIX    2   2 PHE A 1020  GLY A 1025  5                                   6
HELIX    3   3 LYS A 1127  GLY A 1129  5                                   3
HELIX    4   4 ASP A 1130  VAL A 1135  1                                   6
HELIX    5   5 LYS A 1154  GLY A 1156  5                                   3
HELIX    6   6 LEU A 1157  LEU A 1164  1                                   8
HELIX    7   7 ASP A 1165  LYS A 1168  5                                   4
HELIX    8   8 ASP A 1180  LEU A 1185  5                                   6
HELIX    9   9 SER A 1220  ARG A 1227  1                                   8
SHEET    1   A 2 ASP A1032  ILE A1033  0
SHEET    2   A 2 THR A1108  VAL A1109  1  O  THR A1108   N  ILE A1033
SHEET    1   B10 LYS A1039  TYR A1040  0
SHEET    2   B10 LYS A1257  ALA A1258  1  O  ALA A1258   N  LYS A1039
SHEET    3   B10 TYR A1191  GLY A1196 -1  N  THR A1193   O  LYS A1257
SHEET    4   B10 VAL A1207  LEU A1212 -1  O  VAL A1207   N  GLY A1196
SHEET    5   B10 LEU A1141  GLY A1151  1  N  GLY A1145   O  LEU A1212
SHEET    6   B10 ALA A1116  ASN A1124 -1  N  LEU A1118   O  ILE A1146
SHEET    7   B10 THR A1087  TRP A1097 -1  N  HIS A1094   O  HIS A1119
SHEET    8   B10 PHE A1066  PHE A1070 -1  N  VAL A1068   O  PHE A1093
SHEET    9   B10 SER A1056  ASN A1061 -1  N  LEU A1057   O  GLU A1069
SHEET   10   B10 SER A1173  ASP A1175 -1  O  ALA A1174   N  ILE A1059
SHEET    1   C 6 LEU A1047  SER A1050  0
SHEET    2   C 6 VAL A1078  GLY A1081 -1  O  LYS A1080   N  SER A1048
SHEET    3   C 6 THR A1087  TRP A1097 -1  O  TYR A1088   N  LEU A1079
SHEET    4   C 6 ALA A1116  ASN A1124 -1  O  HIS A1119   N  HIS A1094
SHEET    5   C 6 LEU A1141  GLY A1151 -1  O  ILE A1146   N  LEU A1118
SHEET    6   C 6 ILE A1216  SER A1219  1  O  ILE A1216   N  PHE A1147
LINK         SG  CYS A1206                HG   BE7 A1700     1555   1555  1.89
LINK        ZN    ZN A1300                 ND1 HIS A1119     1555   1555  2.02
LINK        ZN    ZN A1300                 NE2 HIS A1094     1555   1555  1.99
LINK        ZN    ZN A1300                 N24 NR2 A1400     1555   1555  1.98
LINK        ZN    ZN A1300                 NE2 HIS A1096     1555   1555  2.02
LINK        HG   BE7 A1700                 O   GLU A1205     1555   1555  3.08
LINK        HG   BE7 A1700                 O   GLN A1137     1555   1555  2.95
CISPEP   1 SER A 1029    PRO A 1030          0        -1.33
CISPEP   2 PRO A 1201    PRO A 1202          0         5.60
SITE     1 AC1  4 HIS A1094  HIS A1096  HIS A1119  NR2 A1400
SITE     1 AC2  6 TRP A1005  ASN A1011  HIS A1015  TRP A1016
SITE     2 AC2  6 ASP A1019  HOH A3171
SITE     1 AC3 13 GLN A1092  HIS A1094  HIS A1096  HIS A1119
SITE     2 AC3 13 PHE A1131  LEU A1198  THR A1199  THR A1200
SITE     3 AC3 13 PRO A1202  TRP A1209   ZN A1300  GOL A1900
SITE     4 AC3 13 HOH A3160
SITE     1 AC4  9 LEU A1057  PHE A1070  ASP A1071  ASP A1072
SITE     2 AC4  9 SER A1073  ILE A1091  HOH A3030  HOH A3170
SITE     3 AC4  9 HOH A3207
SITE     1 AC5  5 GLN A1136  GLN A1137  PRO A1138  GLU A1205
SITE     2 AC5  5 CYS A1206
SITE     1 AC6 10 ASN A1062  HIS A1064  ASN A1067  GLN A1092
SITE     2 AC6 10 HIS A1094  THR A1200  NR2 A1400  HOH A3024
SITE     3 AC6 10 HOH A3064  HOH A3107
CRYST1   42.490   41.510   72.410  90.00 104.45  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      0.023535  0.000000  0.006065        0.00000
SCALE2      0.000000  0.024091  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014261        0.00000
      
PROCHECK
Go to PROCHECK summary
 References