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PDBsum entry 3p5a

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Lyase/inhibitor PDB id
3p5a
Jmol
Contents
Protein chain
257 a.a.
Ligands
IT2
DMS
Metals
_ZN
Waters ×300
HEADER    LYASE/INHIBITOR                         08-OCT-10   3P5A
TITLE     HUMAN CARBONIC ANHYDRASE COMPLEXED WITH SODIUM
TITLE    2 MORPHOLINOCARBODITHIOATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE II, CARBONIC ANHYDRASE C, CAC,
COMPND   5 CARBONIC ANHYDRASE II, CA-II;
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: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS    CARBOTHIOATES, HCAII INHIBITORS, LYASE-INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.AGGARWAL,R.MCKENNA
REVDAT   3   10-OCT-12 3P5A    1
REVDAT   2   25-JAN-12 3P5A    1       JRNL
REVDAT   1   19-OCT-11 3P5A    0
JRNL        AUTH   F.CARTA,M.AGGARWAL,A.MARESCA,A.SCOZZAFAVA,R.MCKENNA,
JRNL        AUTH 2 E.MASINI,C.T.SUPURAN
JRNL        TITL   DITHIOCARBAMATES STRONGLY INHIBIT CARBONIC ANHYDRASES AND
JRNL        TITL 2 SHOW ANTIGLAUCOMA ACTION IN VIVO
JRNL        REF    J.MED.CHEM.                   V.  55  1721 2012
JRNL        REFN                   ISSN 0022-2623
JRNL        PMID   22276570
JRNL        DOI    10.1021/JM300031J
REMARK   2
REMARK   2 RESOLUTION.    1.49 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.3_467)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.32
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9
REMARK   3   NUMBER OF REFLECTIONS             : 39047
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.149
REMARK   3   R VALUE            (WORKING SET) : 0.148
REMARK   3   FREE R VALUE                     : 0.169
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.960
REMARK   3   FREE R VALUE TEST SET COUNT      : 1938
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 25.3188 -  3.2112    0.99     3839   202  0.1486 0.1643
REMARK   3     2  3.2112 -  2.5496    1.00     3773   196  0.1344 0.1466
REMARK   3     3  2.5496 -  2.2275    1.00     3747   198  0.1325 0.1588
REMARK   3     4  2.2275 -  2.0239    1.00     3732   190  0.1370 0.1648
REMARK   3     5  2.0239 -  1.8789    0.99     3738   191  0.1307 0.1557
REMARK   3     6  1.8789 -  1.7682    0.99     3694   191  0.1286 0.1659
REMARK   3     7  1.7682 -  1.6796    0.99     3712   194  0.1417 0.1666
REMARK   3     8  1.6796 -  1.6065    0.99     3680   207  0.1720 0.1934
REMARK   3     9  1.6065 -  1.5447    0.98     3641   183  0.2258 0.2178
REMARK   3    10  1.5447 -  1.4900    0.95     3553   186  0.3498 0.4152
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.65
REMARK   3   K_SOL              : 0.48
REMARK   3   B_SOL              : 51.32
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.62
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.14140
REMARK   3    B22 (A**2) : -1.45260
REMARK   3    B33 (A**2) : 2.59400
REMARK   3    B12 (A**2) : -0.00000
REMARK   3    B13 (A**2) : -0.53480
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.012           2158
REMARK   3   ANGLE     :  1.488           2936
REMARK   3   CHIRALITY :  0.091            308
REMARK   3   PLANARITY :  0.008            379
REMARK   3   DIHEDRAL  : 13.194            799
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 1
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: Chain A
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.6341  -1.7798  15.9657
REMARK   3    T TENSOR
REMARK   3      T11:   0.0855 T22:   0.0812
REMARK   3      T33:   0.0875 T12:  -0.0021
REMARK   3      T13:   0.0015 T23:   0.0011
REMARK   3    L TENSOR
REMARK   3      L11:   0.5035 L22:   0.3112
REMARK   3      L33:   0.3726 L12:  -0.0860
REMARK   3      L13:   0.0395 L23:  -0.0203
REMARK   3    S TENSOR
REMARK   3      S11:   0.0023 S12:  -0.0285 S13:   0.0167
REMARK   3      S21:  -0.0191 S22:   0.0030 S23:   0.0077
REMARK   3      S31:   0.0048 S32:   0.0067 S33:   0.0000
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3P5A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-10.
REMARK 100 THE RCSB ID CODE IS RCSB061973.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 14-JUL-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
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 RUH3R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : VARIMAX OPTICS
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39395
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.490
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4
REMARK 200  DATA REDUNDANCY                : 3.700
REMARK 200  R MERGE                    (I) : 0.06400
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 32.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.54
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.18100
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M SODIUM CITRATE, 50 MM TRIS-CL, PH
REMARK 280  8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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       20.60500
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    ASN A  11       15.11   -140.21
REMARK 500    ARG A  27       55.74   -144.63
REMARK 500    LYS A 111       -1.37     72.58
REMARK 500    PHE A 176       62.12   -151.72
REMARK 500    ASN A 244       50.81    -96.31
REMARK 500    LYS A 252     -138.22     55.10
REMARK 500
REMARK 500 REMARK: NULL
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 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  96   NE2
REMARK 620 2 HIS A  94   NE2 103.9
REMARK 620 3 HIS A 119   ND1  94.6 107.8
REMARK 620 4 IT2 A 263   SAB 112.2 107.3 128.3
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 IT2 A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 3092
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3P58   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE COMPLEXED WITH SODIUM
REMARK 900 BENZYLMETHYLCARBAMODITHIOATE
REMARK 900 RELATED ID: 3P5L   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE COMPLEXED WITH SODIUM 4-CYANO-4-
REMARK 900 PHENYLPIPERIDINE-1-CARBODITHIOATE
DBREF  3P5A 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 262       1
HET    IT2  A 263       9
HET    DMS  A3092       4
HETNAM      ZN ZINC ION
HETNAM     IT2 MORPHOLINE-4-CARBODITHIOIC ACID
HETNAM     DMS DIMETHYL SULFOXIDE
FORMUL   2   ZN    ZN 2+
FORMUL   3  IT2    C5 H9 N O S2
FORMUL   4  DMS    C2 H6 O S
FORMUL   5  HOH   *300(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  ILE A 210
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  96                ZN    ZN A 262     1555   1555  2.05
LINK         NE2 HIS A  94                ZN    ZN A 262     1555   1555  2.06
LINK         ND1 HIS A 119                ZN    ZN A 262     1555   1555  2.08
LINK        ZN    ZN A 262                 SAB IT2 A 263     1555   1555  2.29
CISPEP   1 SER A   29    PRO A   30          0         0.04
CISPEP   2 PRO A  201    PRO A  202          0         9.67
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  IT2 A 263
SITE     1 AC2  7 GLN A  92  HIS A  94  HIS A  96  THR A 199
SITE     2 AC2  7 THR A 200   ZN A 262  HOH A 531
SITE     1 AC3  3 TYR A   7  ASP A 243  TRP A 245
CRYST1   42.262   41.210   72.151  90.00 104.21  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      0.023662  0.000000  0.005993        0.00000
SCALE2      0.000000  0.024266  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014297        0.00000
      
PROCHECK
Go to PROCHECK summary
 References