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PDBsum entry 3v3g

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Lyase PDB id
3v3g
Jmol
Contents
Protein chain
258 a.a.
Metals
_CL
_ZN
Waters ×277
HEADER    LYASE                                   13-DEC-11   3V3G
TITLE     KINETIC AND STRUCTURAL STUDIES OF THERMOSTABILIZED MUTANTS OF HCA II.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: B;
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;
COMPND   8 MUTATION: 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    THERMOSTABILE, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.D.BOONE,S.Z.FISHER,R.MCKENNA
REVDAT   2   01-AUG-12 3V3G    1       JRNL
REVDAT   1   20-JUN-12 3V3G    0
JRNL        AUTH   Z.FISHER,C.D.BOONE,S.M.BISWAS,B.VENKATAKRISHNAN,M.AGGARWAL,
JRNL        AUTH 2 C.TU,M.AGBANDJE-MCKENNA,D.SILVERMAN,R.MCKENNA
JRNL        TITL   KINETIC AND STRUCTURAL CHARACTERIZATION OF THERMOSTABILIZED
JRNL        TITL 2 MUTANTS OF HUMAN CARBONIC ANHYDRASE II.
JRNL        REF    PROTEIN ENG.DES.SEL.          V.  25   347 2012
JRNL        REFN                   ISSN 1741-0126
JRNL        PMID   22691706
JRNL        DOI    10.1093/PROTEIN/GZS027
REMARK   2
REMARK   2 RESOLUTION.    1.56 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.2_869)
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) : 1.56
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.48
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4
REMARK   3   NUMBER OF REFLECTIONS             : 32275
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172
REMARK   3   R VALUE            (WORKING SET) : 0.170
REMARK   3   FREE R VALUE                     : 0.200
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.060
REMARK   3   FREE R VALUE TEST SET COUNT      : 1956
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 19.4862 -  3.7471    1.00     2372   156  0.1597 0.1612
REMARK   3     2  3.7471 -  2.9776    1.00     2276   147  0.1659 0.1952
REMARK   3     3  2.9776 -  2.6022    1.00     2234   141  0.1638 0.2149
REMARK   3     4  2.6022 -  2.3647    1.00     2238   141  0.1650 0.2354
REMARK   3     5  2.3647 -  2.1955    0.99     2193   148  0.1528 0.1862
REMARK   3     6  2.1955 -  2.0662    1.00     2228   139  0.1602 0.1808
REMARK   3     7  2.0662 -  1.9628    0.99     2178   145  0.1585 0.1736
REMARK   3     8  1.9628 -  1.8774    0.97     2144   144  0.1491 0.2033
REMARK   3     9  1.8774 -  1.8052    0.97     2147   131  0.1597 0.1830
REMARK   3    10  1.8052 -  1.7430    0.97     2110   144  0.1751 0.2092
REMARK   3    11  1.7430 -  1.6885    0.96     2109   129  0.2105 0.2601
REMARK   3    12  1.6885 -  1.6403    0.95     2078   143  0.2349 0.2956
REMARK   3    13  1.6403 -  1.5971    0.94     2049   127  0.2960 0.3294
REMARK   3    14  1.5971 -  1.5581    0.90     1963   121  0.3521 0.3946
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.00
REMARK   3   SHRINKAGE RADIUS   : 0.73
REMARK   3   K_SOL              : 0.35
REMARK   3   B_SOL              : 31.50
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.440
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.490
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.59
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.06400
REMARK   3    B22 (A**2) : 1.94150
REMARK   3    B33 (A**2) : -0.87750
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.00000
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      :  0.009           2199
REMARK   3   ANGLE     :  1.245           2999
REMARK   3   CHIRALITY :  0.080            310
REMARK   3   PLANARITY :  0.007            392
REMARK   3   DIHEDRAL  : 12.312            831
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
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 3V3G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JAN-12.
REMARK 100 THE RCSB ID CODE IS RCSB069546.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 16-SEP-11
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.5
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   : 32937
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.558
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4
REMARK 200  DATA REDUNDANCY                : 6.900
REMARK 200  R MERGE                    (I) : 0.07800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 16.8000
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) : 1.62
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.48800
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   (%): 36.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% W/V PEG 4000, 0.2M MAGNESIUM
REMARK 280  CHLORIDE HEXAHYDRATE, 0.1M TRIS HYDROCHLORIDE, PH 8.5, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-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       21.02500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.35050
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.02850
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.35050
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.02500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.02850
REMARK 290   SMTRY3   4  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: B
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 B     1
REMARK 465     SER B     2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   HE2  HIS B     3     O    HOH B   664              1.31
REMARK 500   NE2  HIS B     3     O    HOH B   664              1.86
REMARK 500   O    HOH B   597     O    HOH B   622              2.16
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    LYS B 111       -5.85     76.38
REMARK 500    PHE B 176       59.01   -154.94
REMARK 500    ASN B 244       44.86    -96.42
REMARK 500    LYS B 252     -130.99     53.65
REMARK 500    ASN B 253       33.36    -95.44
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 B 301  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 417   O
REMARK 620 2 HIS B  94   NE2 108.9
REMARK 620 3 HIS B  96   NE2 113.3 106.0
REMARK 620 4 HIS B 119   ND1 115.4 113.5  99.1
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 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3V3F   RELATED DB: PDB
REMARK 900 RELATED ID: 3V3J   RELATED DB: PDB
REMARK 900 RELATED ID: 3V3H   RELATED DB: PDB
REMARK 900 RELATED ID: 3V3I   RELATED DB: PDB
DBREF  3V3G B    1   261  UNP    P00918   CAH2_HUMAN       1    260
SEQADV 3V3G PHE B    7  UNP  P00918    TYR     7 ENGINEERED MUTATION
SEQADV 3V3G HIS B  100  UNP  P00918    LEU   100 ENGINEERED MUTATION
SEQADV 3V3G SER B  224  UNP  P00918    LEU   223 ENGINEERED MUTATION
SEQADV 3V3G PRO B  240  UNP  P00918    LEU   239 ENGINEERED MUTATION
SEQRES   1 B  260  MET SER HIS HIS TRP GLY PHE GLY LYS HIS ASN GLY PRO
SEQRES   2 B  260  GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES   3 B  260  ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES   4 B  260  TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES   5 B  260  GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA
SEQRES   6 B  260  PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES   7 B  260  LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES   8 B  260  GLN PHE HIS PHE HIS TRP GLY SER HIS ASP GLY GLN GLY
SEQRES   9 B  260  SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES  10 B  260  LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES  11 B  260  GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES  12 B  260  GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES  13 B  260  GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES  14 B  260  GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES  15 B  260  LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES  16 B  260  SER LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP
SEQRES  17 B  260  ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES  18 B  260  VAL SER LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES  19 B  260  GLU PRO GLU GLU PRO MET VAL ASP ASN TRP ARG PRO ALA
SEQRES  20 B  260  GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     ZN  B 301       1
HET     CL  B 302       1
HETNAM      ZN ZINC ION
HETNAM      CL CHLORIDE ION
FORMUL   2   ZN    ZN 2+
FORMUL   3   CL    CL 1-
FORMUL   4  HOH   *274(H2 O)
HELIX    1   1 GLY B   12  ASP B   19  5                                   8
HELIX    2   2 PHE B   20  GLY B   25  5                                   6
HELIX    3   3 LYS B  127  GLY B  129  5                                   3
HELIX    4   4 ASP B  130  VAL B  135  1                                   6
HELIX    5   5 LYS B  154  GLY B  156  5                                   3
HELIX    6   6 LEU B  157  LEU B  164  1                                   8
HELIX    7   7 ASP B  165  LYS B  168  5                                   4
HELIX    8   8 ASP B  180  LEU B  185  5                                   6
HELIX    9   9 SER B  219  ARG B  227  1                                   9
SHEET    1   A 2 ASP B  32  ILE B  33  0
SHEET    2   A 2 THR B 108  VAL B 109  1  O  THR B 108   N  ILE B  33
SHEET    1   B10 LYS B  39  TYR B  40  0
SHEET    2   B10 LYS B 257  ALA B 258  1  O  ALA B 258   N  LYS B  39
SHEET    3   B10 TYR B 191  GLY B 196 -1  N  THR B 193   O  LYS B 257
SHEET    4   B10 VAL B 207  LEU B 212 -1  O  VAL B 207   N  GLY B 196
SHEET    5   B10 LEU B 141  VAL B 150  1  N  GLY B 145   O  LEU B 212
SHEET    6   B10 ALA B 116  ASN B 124 -1  N  LEU B 118   O  ILE B 146
SHEET    7   B10 TYR B  88  TRP B  97 -1  N  HIS B  94   O  HIS B 119
SHEET    8   B10 PHE B  66  PHE B  70 -1  N  VAL B  68   O  PHE B  93
SHEET    9   B10 SER B  56  ASN B  61 -1  N  LEU B  57   O  GLU B  69
SHEET   10   B10 SER B 173  ASP B 175 -1  O  ALA B 174   N  ILE B  59
SHEET    1   C 6 LEU B  47  SER B  50  0
SHEET    2   C 6 VAL B  78  GLY B  81 -1  O  VAL B  78   N  SER B  50
SHEET    3   C 6 TYR B  88  TRP B  97 -1  O  TYR B  88   N  LEU B  79
SHEET    4   C 6 ALA B 116  ASN B 124 -1  O  HIS B 119   N  HIS B  94
SHEET    5   C 6 LEU B 141  VAL B 150 -1  O  ILE B 146   N  LEU B 118
SHEET    6   C 6 ILE B 216  VAL B 218  1  O  ILE B 216   N  PHE B 147
LINK        ZN    ZN B 301                 O   HOH B 417     1555   1555  1.98
LINK         NE2 HIS B  94                ZN    ZN B 301     1555   1555  2.01
LINK         NE2 HIS B  96                ZN    ZN B 301     1555   1555  2.02
LINK         ND1 HIS B 119                ZN    ZN B 301     1555   1555  2.03
CISPEP   1 SER B   29    PRO B   30          0        -1.84
CISPEP   2 PRO B  201    PRO B  202          0        10.33
SITE     1 AC1  4 HIS B  94  HIS B  96  HIS B 119  HOH B 417
SITE     1 AC2  4 GLN B 158  GLU B 221  LYS B 225  HOH B 625
CRYST1   42.050   72.057   74.701  90.00  90.00  90.00 P 21 21 21    4
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      0.023781  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013878  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013387        0.00000
      
PROCHECK
Go to PROCHECK summary
 References