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PDBsum entry 3hs4

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Lyase PDB id
3hs4
Jmol
Contents
Protein chain
257 a.a.
Ligands
GOL
AZM ×3
Metals
_ZN
Waters ×404
HEADER    LYASE                                   10-JUN-09   3HS4
TITLE     HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH ACETAZOLAMIDE
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
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;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS    CARBONIC ANHYDRASE 2, CARBONIC ANHYDRASE II, LYASE, CA II, CA 2,
KEYWDS   2 ACETAZOLAMIDE, 5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE, DISEASE
KEYWDS   3 MUTATION, METAL-BINDING
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.H.ROBBINS,C.GENIS,J.DOMSIC,K.H.SIPPEL,M.AGBANDJE-MCKENNA,R.MCKENNA
REVDAT   2   13-JUL-11 3HS4    1       VERSN
REVDAT   1   08-DEC-09 3HS4    0
JRNL        AUTH   K.H.SIPPEL,A.H.ROBBINS,J.DOMSIC,C.GENIS,M.AGBANDJE-MCKENNA,
JRNL        AUTH 2 R.MCKENNA
JRNL        TITL   HIGH-RESOLUTION STRUCTURE OF HUMAN CARBONIC ANHYDRASE II
JRNL        TITL 2 COMPLEXED WITH ACETAZOLAMIDE REVEALS INSIGHTS INTO INHIBITOR
JRNL        TITL 3 DRUG DESIGN.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  65   992 2009
JRNL        REFN                   ESSN 1744-3091
JRNL        PMID   19851004
JRNL        DOI    10.1107/S1744309109036665
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   J.VIDGREN,A.LILJAS,N.P.WALKER
REMARK   1  TITL   REFINED STRUCTURE OF THE ACETAZOLAMIDE COMPLEX OF HUMAN
REMARK   1  TITL 2 CARBONIC ANHYDRASE II AT 1.9 A.
REMARK   1  REF    INT.J.BIOL.MACROMOL.          V.  12   342 1990
REMARK   1  REFN                   ISSN 0141-8130
REMARK   1  PMID   2128470
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) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.6
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT
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) : 0.113
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.113
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.140
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 4628
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)) : 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      : 2049
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 46
REMARK   3   SOLVENT ATOMS      : 404
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) : 0.015
REMARK   3   ANGLE DISTANCES                      (A) : 0.031
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.031
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.094
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.100
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.082
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.105
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: USED CONJUGATE GRADIENT LEAST SQUARES
REMARK   3  PROCEDURE.
REMARK   4
REMARK   4 3HS4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-09.
REMARK 100 THE RCSB ID CODE IS RCSB053516.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-NOV-06
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 9.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CHESS
REMARK 200  BEAMLINE                       : A1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.997
REMARK 200  MONOCHROMATOR                  : ASYMMETRIC CUT SI(111)
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 92557
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.6
REMARK 200  DATA REDUNDANCY                : 2.900
REMARK 200  R MERGE                    (I) : 0.07300
REMARK 200  R SYM                      (I) : NULL
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) : 1.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.14
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20
REMARK 200  R MERGE FOR SHELL          (I) : 0.30300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.300
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 2ILI
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: 1.3 M SODIUM CITRATE, 100 MM TRIS-HCL
REMARK 280  PH 9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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       20.54850
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     MET A     1
REMARK 465     SER A     2
REMARK 465     HIS A     3
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       55.96   -142.52
REMARK 500    LYS A 111       -3.01     72.07
REMARK 500    PHE A 176       61.17   -150.32
REMARK 500    ASN A 244       49.88    -95.34
REMARK 500    LYS A 252     -138.34     51.95
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 A1242        DISTANCE =  5.34 ANGSTROMS
REMARK 525    HOH A1251        DISTANCE =  5.51 ANGSTROMS
REMARK 525    HOH A1351        DISTANCE =  6.18 ANGSTROMS
REMARK 525    HOH A1387        DISTANCE =  5.11 ANGSTROMS
REMARK 525    HOH A1389        DISTANCE =  6.22 ANGSTROMS
REMARK 525    HOH A1400        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                              ZN A 301  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  94   NE2
REMARK 620 2 HIS A  96   NE2 105.2
REMARK 620 3 HIS A 119   ND1 111.9 100.3
REMARK 620 4 AZM A 701   N1  112.0 112.8 113.7
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZM A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZM A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZM A 703
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YDA   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II MUTANT L198E COMPLEXED WITH
REMARK 900 ACETAZOLAMIDE
REMARK 900 RELATED ID: 1YDB   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II MUTANT L198F COMPLEXED WITH
REMARK 900 ACETAZOLAMIDE
REMARK 900 RELATED ID: 1YDD   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II MUTANT L198R COMPLEXED WITH
REMARK 900 ACETAZOLAMIDE
REMARK 900 RELATED ID: 1ZSB   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II MUTANT E117Q COMPLEXED WITH
REMARK 900 ACETAZOLAMIDE
REMARK 900 RELATED ID: 2H4N   RELATED DB: PDB
REMARK 900 CARBONIC ANHYDRASE II MUTANT H94N COMPLEXED WITH
REMARK 900 ACETAZOLAMIDE
DBREF  3HS4 A    1   261  UNP    P00918   CAH2_HUMAN       1    260
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 CYS 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
HET     ZN  A 301       1
HET    GOL  A 400       6
HET    AZM  A 701      13
HET    AZM  A 702      13
HET    AZM  A 703      13
HETNAM      ZN ZINC ION
HETNAM     GOL GLYCEROL
HETNAM     AZM 5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2   ZN    ZN 2+
FORMUL   3  GOL    C3 H8 O3
FORMUL   4  AZM    3(C4 H6 N4 O3 S2)
FORMUL   7  HOH   *404(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  LYS A  168  5                                   4
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  VAL A  78   N  SER A  50
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         NE2 HIS A  94                ZN    ZN A 301     1555   1555  1.99
LINK         NE2 HIS A  96                ZN    ZN A 301     1555   1555  1.99
LINK         ND1 HIS A 119                ZN    ZN A 301     1555   1555  2.01
LINK        ZN    ZN A 301                 N1  AZM A 701     1555   1555  1.94
CISPEP   1 SER A   29    PRO A   30          0        -4.39
CISPEP   2 PRO A  201    PRO A  202          0        13.36
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  AZM A 701
SITE     1 AC2  9 ASN A  62  HIS A  64  ASN A  67  GLN A  92
SITE     2 AC2  9 THR A 200  AZM A 701  HOH A1013  HOH A1216
SITE     3 AC2  9 HOH A1342
SITE     1 AC3 14 GLN A  92  HIS A  94  HIS A  96  HIS A 119
SITE     2 AC3 14 VAL A 121  PHE A 131  LEU A 198  THR A 199
SITE     3 AC3 14 THR A 200  TRP A 209   ZN A 301  GOL A 400
SITE     4 AC3 14 HOH A1011  HOH A1191
SITE     1 AC4 10 LYS A 112  TYR A 114  TRP A 192  LYS A 213
SITE     2 AC4 10 PRO A 215  HOH A1085  HOH A1233  HOH A1257
SITE     3 AC4 10 HOH A1334  HOH A1346
SITE     1 AC5 13 HIS A   4  TRP A   5  ASN A  11  HIS A  15
SITE     2 AC5 13 TRP A  16  ASP A  19  PHE A  20  ASP A 180
SITE     3 AC5 13 ARG A 182  GLY A 183  HOH A1288  HOH A1332
SITE     4 AC5 13 HOH A1335
CRYST1   42.252   41.097   71.820  90.00 104.31  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      0.023668  0.000000  0.006037        0.00000
SCALE2      0.000000  0.024333  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014370        0.00000
      
PROCHECK
Go to PROCHECK summary
 References