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PDBsum entry 3mwo

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Top Page protein metals Protein-protein interface(s) links
Lyase PDB id
3mwo
Jmol
Contents
Protein chain
257 a.a.
Metals
_ZN ×2
Waters ×745
HEADER    LYASE                                   06-MAY-10   3MWO
TITLE     HUMAN CARBONIC ANHYDRASE II IN A DOUBLED MONOCLINIC CELL: A RE-
TITLE    2 DETERMINATION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A, B;
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, HCA2;
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;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS    DOUBLED UNIT CELL, LYASE, PSEUDOSYMMETRY, TRANSLATIONAL NCS
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.H.ROBBINS,R.MCKENNA
REVDAT   3   21-MAR-12 3MWO    1       JRNL   VERSN
REVDAT   2   28-JUL-10 3MWO    1       JRNL
REVDAT   1   09-JUN-10 3MWO    0
SPRSDE     09-JUN-10 3MWO      3KS1
JRNL        AUTH   A.H.ROBBINS,J.F.DOMSIC,M.AGBANDJE-MCKENNA,R.MCKENNA
JRNL        TITL   EMERGING FROM PSEUDO-SYMMETRY: THE REDETERMINATION OF HUMAN
JRNL        TITL 2 CARBONIC ANHYDRASE II IN MONOCLINIC P2(1) WITH A DOUBLED A
JRNL        TITL 3 AXIS.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  66   950 2010
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   20693695
JRNL        DOI    10.1107/S0907444910023723
REMARK   2
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.1_348)
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) : 1.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 18.28
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.600
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2
REMARK   3   NUMBER OF REFLECTIONS             : 90110
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.167
REMARK   3   R VALUE            (WORKING SET) : 0.166
REMARK   3   FREE R VALUE                     : 0.184
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080
REMARK   3   FREE R VALUE TEST SET COUNT      : 4581
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 18.2810 -  4.3310    0.85     2631   141  0.2190 0.1740
REMARK   3     2  4.3310 -  3.4450    0.95     2845   161  0.1550 0.1730
REMARK   3     3  3.4450 -  3.0120    0.98     2959   133  0.1600 0.1760
REMARK   3     4  3.0120 -  2.7380    0.98     2883   172  0.1640 0.1780
REMARK   3     5  2.7380 -  2.5420    0.98     2911   170  0.1640 0.1850
REMARK   3     6  2.5420 -  2.3920    0.98     2910   156  0.1590 0.1720
REMARK   3     7  2.3920 -  2.2730    0.98     2910   152  0.1460 0.1720
REMARK   3     8  2.2730 -  2.1740    0.97     2899   147  0.1500 0.1890
REMARK   3     9  2.1740 -  2.0910    0.97     2924   144  0.1470 0.1750
REMARK   3    10  2.0910 -  2.0190    0.98     2886   164  0.1490 0.1560
REMARK   3    11  2.0190 -  1.9560    0.98     2862   152  0.1540 0.1780
REMARK   3    12  1.9560 -  1.9000    0.97     2905   148  0.1510 0.1650
REMARK   3    13  1.9000 -  1.8500    0.97     2897   161  0.1560 0.1530
REMARK   3    14  1.8500 -  1.8050    0.97     2839   171  0.1550 0.1720
REMARK   3    15  1.8050 -  1.7640    0.97     2858   153  0.1570 0.2150
REMARK   3    16  1.7640 -  1.7260    0.97     2846   147  0.1560 0.1730
REMARK   3    17  1.7260 -  1.6920    0.97     2899   155  0.1580 0.1780
REMARK   3    18  1.6920 -  1.6600    0.97     2836   164  0.1630 0.2220
REMARK   3    19  1.6600 -  1.6300    0.97     2859   121  0.1620 0.2020
REMARK   3    20  1.6300 -  1.6020    0.97     2877   152  0.1620 0.1870
REMARK   3    21  1.6020 -  1.5770    0.97     2830   145  0.1590 0.1840
REMARK   3    22  1.5770 -  1.5520    0.96     2850   145  0.1640 0.2050
REMARK   3    23  1.5520 -  1.5300    0.96     2811   150  0.1700 0.2100
REMARK   3    24  1.5300 -  1.5080    0.96     2835   164  0.1840 0.2040
REMARK   3    25  1.5080 -  1.4880    0.96     2837   149  0.1750 0.1980
REMARK   3    26  1.4880 -  1.4680    0.96     2773   177  0.1750 0.1960
REMARK   3    27  1.4680 -  1.4500    0.96     2821   146  0.1830 0.2120
REMARK   3    28  1.4500 -  1.4330    0.95     2826   140  0.1840 0.1890
REMARK   3    29  1.4330 -  1.4160    0.96     2800   150  0.1910 0.2160
REMARK   3    30  1.4160 -  1.4000    0.92     2710   151  0.1980 0.2430
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : 0.47
REMARK   3   B_SOL              : 45.70
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.140
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 18.60
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.01
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.50700
REMARK   3    B22 (A**2) : -0.47700
REMARK   3    B33 (A**2) : -1.03000
REMARK   3    B12 (A**2) : -0.00000
REMARK   3    B13 (A**2) : -0.00200
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           4343
REMARK   3   ANGLE     :  1.257           5925
REMARK   3   CHIRALITY :  0.076            622
REMARK   3   PLANARITY :  0.007            771
REMARK   3   DIHEDRAL  : 11.980           1623
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 2
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: chain A and not chain S
REMARK   3    ORIGIN FOR THE GROUP (A):   9.4947   1.3853  15.8306
REMARK   3    T TENSOR
REMARK   3      T11:   0.0390 T22:   0.0319
REMARK   3      T33:   0.0325 T12:  -0.0045
REMARK   3      T13:   0.0005 T23:   0.0004
REMARK   3    L TENSOR
REMARK   3      L11:   0.5207 L22:   0.4946
REMARK   3      L33:   0.6131 L12:  -0.0162
REMARK   3      L13:   0.0012 L23:  -0.1280
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0120 S12:  -0.0325 S13:  -0.0102
REMARK   3      S21:  -0.0779 S22:   0.0104 S23:   0.0182
REMARK   3      S31:   0.0395 S32:  -0.0124 S33:   0.0027
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: chain B
REMARK   3    ORIGIN FOR THE GROUP (A):  51.6287   1.3954  15.7135
REMARK   3    T TENSOR
REMARK   3      T11:   0.0356 T22:   0.0355
REMARK   3      T33:   0.0427 T12:  -0.0007
REMARK   3      T13:  -0.0033 T23:  -0.0041
REMARK   3    L TENSOR
REMARK   3      L11:   0.6026 L22:   0.4635
REMARK   3      L33:   0.4402 L12:  -0.0830
REMARK   3      L13:  -0.0696 L23:   0.0093
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0117 S12:  -0.0481 S13:   0.0032
REMARK   3      S21:  -0.0010 S22:   0.0199 S23:  -0.0227
REMARK   3      S31:   0.0132 S32:  -0.0053 S33:  -0.0086
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: 3KS1, CHAIN B (ALTLOC B REMOVED), MODEL
REMARK   3  TRANSLATED X'=X-1/4 AND RE-REFINED
REMARK   4
REMARK   4 3MWO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-10.
REMARK 100 THE RCSB ID CODE IS RCSB059087.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 22-APR-09
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.8
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) : 0.978
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
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 90618
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400
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     (%) : 96.8
REMARK 200  DATA REDUNDANCY                : 3.100
REMARK 200  R MERGE                    (I) : 0.06400
REMARK 200  R SYM                      (I) : 0.06400
REMARK 200   FOR THE DATA SET  : 15.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.45
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.19400
REMARK 200  R SYM FOR SHELL            (I) : 0.19400
REMARK 200   FOR SHELL         : 6.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NA
REMARK 200 STARTING MODEL: 3KS1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 39.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM TRIS, 1.2 M SODIUM CITRATE, 5 UL
REMARK 280  + 5 UL DROPLET, PH 7.8, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  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       20.52850
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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 A     1
REMARK 465     SER A     2
REMARK 465     HIS A     3
REMARK 465     MET B     1
REMARK 465     SER B     2
REMARK 465     HIS B     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    LYS A 111       -2.10     72.09
REMARK 500    PHE A 176       83.18   -155.43
REMARK 500    ASN A 244       46.28    -93.57
REMARK 500    LYS A 252     -132.26     52.53
REMARK 500    ARG B  27       56.07   -141.42
REMARK 500    LYS B 111       -1.89     72.92
REMARK 500    PHE B 176       79.22   -154.02
REMARK 500    ASN B 244       45.11    -92.45
REMARK 500    LYS B 252     -136.24     52.57
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 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 269   O
REMARK 620 2 HIS B  96   NE2 115.0
REMARK 620 3 HIS B  94   NE2 108.8 106.6
REMARK 620 4 HIS B 119   ND1 114.5  99.8 111.8
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 HOH A 263   O
REMARK 620 2 HIS A  96   NE2 115.9
REMARK 620 3 HIS A  94   NE2 107.7 105.6
REMARK 620 4 HIS A 119   ND1 114.3 100.8 112.2
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 ZN B 262
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE NUMBERING FOLLOWS THAT REPORTED FOR THE HUMAN CARBONIC
REMARK 999 ANHYDRASE ISOFORM II, PDB CODE 1CA2.
DBREF  3MWO A    1   261  UNP    P00918   CAH2_HUMAN       1    260
DBREF  3MWO B    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
SEQRES   1 B  260  MET SER HIS HIS TRP GLY TYR 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 LEU 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 LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES  19 B  260  GLU PRO GLU GLU LEU 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  A 262       1
HET     ZN  B 262       1
HETNAM      ZN ZINC ION
FORMUL   3   ZN    2(ZN 2+)
FORMUL   5  HOH   *745(H2 O)
HELIX    1   1 GLY A   12  ASP A   19  5                                   8
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
HELIX   10  10 GLY B   12  ASP B   19  5                                   8
HELIX   11  11 PHE B   20  GLY B   25  5                                   6
HELIX   12  12 LYS B  127  GLY B  129  5                                   3
HELIX   13  13 ASP B  130  VAL B  135  1                                   6
HELIX   14  14 LYS B  154  GLY B  156  5                                   3
HELIX   15  15 LEU B  157  LEU B  164  1                                   8
HELIX   16  16 ASP B  165  LYS B  168  5                                   4
HELIX   17  17 ASP B  180  LEU B  185  5                                   6
HELIX   18  18 SER B  219  ARG B  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 THR A  87  TRP A  97 -1  N  HIS A  94   O  HIS A 119
SHEET    8   B10 PHE A  66  PHE A  70 -1  N  PHE A  70   O  ILE A  91
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 THR A  87  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
SHEET    1   D 2 ASP B  32  ILE B  33  0
SHEET    2   D 2 THR B 108  VAL B 109  1  O  THR B 108   N  ILE B  33
SHEET    1   E10 LYS B  39  TYR B  40  0
SHEET    2   E10 LYS B 257  ALA B 258  1  O  ALA B 258   N  LYS B  39
SHEET    3   E10 TYR B 191  GLY B 196 -1  N  THR B 193   O  LYS B 257
SHEET    4   E10 VAL B 207  LEU B 212 -1  O  VAL B 207   N  GLY B 196
SHEET    5   E10 LEU B 141  VAL B 150  1  N  GLY B 145   O  ILE B 210
SHEET    6   E10 ALA B 116  ASN B 124 -1  N  LEU B 118   O  ILE B 146
SHEET    7   E10 THR B  87  TRP B  97 -1  N  HIS B  94   O  HIS B 119
SHEET    8   E10 PHE B  66  PHE B  70 -1  N  VAL B  68   O  PHE B  93
SHEET    9   E10 SER B  56  ASN B  61 -1  N  LEU B  57   O  GLU B  69
SHEET   10   E10 SER B 173  ASP B 175 -1  O  ALA B 174   N  ILE B  59
SHEET    1   F 6 LEU B  47  SER B  50  0
SHEET    2   F 6 VAL B  78  GLY B  81 -1  O  LYS B  80   N  SER B  48
SHEET    3   F 6 THR B  87  TRP B  97 -1  O  TYR B  88   N  LEU B  79
SHEET    4   F 6 ALA B 116  ASN B 124 -1  O  HIS B 119   N  HIS B  94
SHEET    5   F 6 LEU B 141  VAL B 150 -1  O  ILE B 146   N  LEU B 118
SHEET    6   F 6 ILE B 216  VAL B 218  1  O  ILE B 216   N  PHE B 147
LINK        ZN    ZN B 262                 O   HOH B 269     1555   1555  1.93
LINK        ZN    ZN A 262                 O   HOH A 263     1555   1555  1.95
LINK         NE2 HIS A  96                ZN    ZN A 262     1555   1555  2.01
LINK         NE2 HIS B  96                ZN    ZN B 262     1555   1555  2.01
LINK         NE2 HIS A  94                ZN    ZN A 262     1555   1555  2.03
LINK         NE2 HIS B  94                ZN    ZN B 262     1555   1555  2.04
LINK         ND1 HIS B 119                ZN    ZN B 262     1555   1555  2.04
LINK         ND1 HIS A 119                ZN    ZN A 262     1555   1555  2.05
CISPEP   1 SER A   29    PRO A   30          0        -1.23
CISPEP   2 PRO A  201    PRO A  202          0        12.82
CISPEP   3 SER B   29    PRO B   30          0        -0.29
CISPEP   4 PRO B  201    PRO B  202          0        12.62
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  HOH A 263
SITE     1 AC2  4 HIS B  94  HIS B  96  HIS B 119  HOH B 269
CRYST1   83.981   41.057   73.586  90.00 109.33  90.00 P 1 21 1      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      0.011907  0.000000  0.004177        0.00000
SCALE2      0.000000  0.024356  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014401        0.00000
      
PROCHECK
Go to PROCHECK summary
 References