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PDBsum entry 3tvn

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Lyase PDB id
3tvn
Jmol
Contents
Protein chain
258 a.a.
Metals
_ZN
Waters ×373
HEADER    LYASE                                   20-SEP-11   3TVN
TITLE     HUMAN CARBONIC ANHYDRASE II PROTON TRANSFER MUTANT
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: X;
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: 511693;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS    GLOBULAR PROTEIN, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.L.MIKULSKI,D.M.WEST,K.H.SIPPEL,B.S.AVVARU,T.CHINGKUANG,R.MCKENNA
REVDAT   3   23-JAN-13 3TVN    1       JRNL
REVDAT   2   26-DEC-12 3TVN    1       JRNL
REVDAT   1   08-AUG-12 3TVN    0
JRNL        AUTH   R.MIKULSKI,D.WEST,K.H.SIPPEL,B.S.AVVARU,M.AGGARWAL,C.TU,
JRNL        AUTH 2 R.MCKENNA,D.N.SILVERMAN
JRNL        TITL   WATER NETWORKS IN FAST PROTON TRANSFER DURING CATALYSIS BY
JRNL        TITL 2 HUMAN CARBONIC ANHYDRASE II.
JRNL        REF    BIOCHEMISTRY                  V.  52   125 2013
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   23215152
JRNL        DOI    10.1021/BI301099K
REMARK   2
REMARK   2 RESOLUTION.    1.50 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) : 1.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.64
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.0
REMARK   3   NUMBER OF REFLECTIONS             : 35285
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177
REMARK   3   R VALUE            (WORKING SET) : 0.175
REMARK   3   FREE R VALUE                     : 0.211
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.580
REMARK   3   FREE R VALUE TEST SET COUNT      : 1968
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 26.6410 -  3.2234    0.93     3515   203  0.1492 0.1959
REMARK   3     2  3.2234 -  2.5592    0.95     3490   206  0.1643 0.1828
REMARK   3     3  2.5592 -  2.2359    0.95     3506   214  0.1632 0.2028
REMARK   3     4  2.2359 -  2.0315    0.94     3425   196  0.1705 0.1989
REMARK   3     5  2.0315 -  1.8860    0.93     3397   192  0.1645 0.1872
REMARK   3     6  1.8860 -  1.7748    0.91     3306   203  0.1635 0.2224
REMARK   3     7  1.7748 -  1.6859    0.90     3266   196  0.1980 0.2390
REMARK   3     8  1.6859 -  1.6125    0.89     3250   188  0.2683 0.2927
REMARK   3     9  1.6125 -  1.5505    0.87     3171   188  0.3457 0.3557
REMARK   3    10  1.5505 -  1.4970    0.82     2991   182  0.4886 0.5168
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 0.90
REMARK   3   SHRINKAGE RADIUS   : 0.61
REMARK   3   K_SOL              : 0.37
REMARK   3   B_SOL              : 40.57
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.310
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.17
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.52400
REMARK   3    B22 (A**2) : -3.83180
REMARK   3    B33 (A**2) : 4.35580
REMARK   3    B12 (A**2) : -0.00000
REMARK   3    B13 (A**2) : -0.12040
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      :  0.006           2255
REMARK   3   ANGLE     :  1.086           3081
REMARK   3   CHIRALITY :  0.075            327
REMARK   3   PLANARITY :  0.004            401
REMARK   3   DIHEDRAL  : 12.227            853
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 5
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: chain X and resid 3:9
REMARK   3    ORIGIN FOR THE GROUP (A):   7.8712  -5.4376  10.6752
REMARK   3    T TENSOR
REMARK   3      T11:   0.1594 T22:   0.2107
REMARK   3      T33:   0.3919 T12:  -0.0050
REMARK   3      T13:   0.0752 T23:  -0.0074
REMARK   3    L TENSOR
REMARK   3      L11:   0.0897 L22:   0.1696
REMARK   3      L33:   0.2684 L12:   0.0992
REMARK   3      L13:  -0.1010 L23:  -0.1070
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0273 S12:   0.1468 S13:  -0.4650
REMARK   3      S21:  -0.1104 S22:  -0.1113 S23:  -0.6529
REMARK   3      S31:  -0.1134 S32:   0.2166 S33:   0.1254
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: chain X and resid 10:45
REMARK   3    ORIGIN FOR THE GROUP (A):   -2.205   -4.309   26.419
REMARK   3    T TENSOR
REMARK   3      T11:   0.1152 T22:   0.1677
REMARK   3      T33:   0.1335 T12:   0.0050
REMARK   3      T13:  -0.0021 T23:  -0.0093
REMARK   3    L TENSOR
REMARK   3      L11:   0.2131 L22:   0.8363
REMARK   3      L33:   0.6233 L12:  -0.1225
REMARK   3      L13:   0.3441 L23:  -0.1706
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1257 S12:  -0.1801 S13:  -0.0127
REMARK   3      S21:   0.0868 S22:   0.0744 S23:  -0.1927
REMARK   3      S31:   0.0934 S32:   0.0514 S33:   0.0205
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: chain X and resid 46:87
REMARK   3    ORIGIN FOR THE GROUP (A): -16.6372   5.6575  12.9839
REMARK   3    T TENSOR
REMARK   3      T11:   0.2237 T22:   0.1286
REMARK   3      T33:   0.1741 T12:   0.0043
REMARK   3      T13:  -0.0197 T23:   0.0236
REMARK   3    L TENSOR
REMARK   3      L11:   0.7818 L22:   0.6204
REMARK   3      L33:   0.5907 L12:  -0.2605
REMARK   3      L13:   0.0469 L23:   0.4644
REMARK   3    S TENSOR
REMARK   3      S11:   0.0966 S12:  -0.0673 S13:   0.1922
REMARK   3      S21:  -0.3012 S22:  -0.0048 S23:   0.0661
REMARK   3      S31:  -0.3341 S32:  -0.0425 S33:  -0.0521
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: chain X and resid 88:251
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1249  -4.7586  13.1923
REMARK   3    T TENSOR
REMARK   3      T11:   0.1386 T22:   0.1151
REMARK   3      T33:   0.1002 T12:  -0.0090
REMARK   3      T13:  -0.0006 T23:   0.0077
REMARK   3    L TENSOR
REMARK   3      L11:   0.5175 L22:   0.7551
REMARK   3      L33:   0.2669 L12:   0.1089
REMARK   3      L13:   0.0552 L23:   0.3883
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0316 S12:  -0.0104 S13:  -0.0015
REMARK   3      S21:  -0.1437 S22:   0.0520 S23:   0.0004
REMARK   3      S31:  -0.0727 S32:   0.0108 S33:  -0.0136
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: chain X and resid 252:261
REMARK   3    ORIGIN FOR THE GROUP (A): -10.9174  -4.4089  34.2706
REMARK   3    T TENSOR
REMARK   3      T11:   0.1914 T22:   0.2552
REMARK   3      T33:   0.1400 T12:   0.0004
REMARK   3      T13:   0.0120 T23:  -0.0196
REMARK   3    L TENSOR
REMARK   3      L11:   0.9629 L22:   0.5746
REMARK   3      L33:   0.1044 L12:  -0.2157
REMARK   3      L13:   0.0717 L23:   0.0671
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1621 S12:  -0.4283 S13:   0.0546
REMARK   3      S21:   0.3090 S22:   0.1834 S23:  -0.0163
REMARK   3      S31:   0.1886 S32:  -0.0270 S33:  -0.0317
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 3TVN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-11.
REMARK 100 THE RCSB ID CODE IS RCSB067976.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-MAR-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 RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE
REMARK 200  OPTICS                         : OSMIC MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35808
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.497
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.641
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.5
REMARK 200  DATA REDUNDANCY                : 5.700
REMARK 200  R MERGE                    (I) : 0.07300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 22.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.38900
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   (%): 40.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.25 M SODIUM CITRATE, 100 MM TRIS-
REMARK 280  HCL, PH 8.0, 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       20.61150
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: X
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 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 X  27       55.55   -140.87
REMARK 500    LYS X  76      -88.10   -126.07
REMARK 500    LYS X 111       -3.04     74.08
REMARK 500    ASN X 244       48.07    -93.59
REMARK 500    LYS X 252     -135.04     52.27
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 X 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH X 394   O
REMARK 620 2 HIS X  96   NE2 112.1
REMARK 620 3 HIS X  94   NE2 107.9 107.3
REMARK 620 4 HIS X 119   ND1 119.5  97.7 111.5
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 X 262
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2NXT   RELATED DB: PDB
REMARK 900 HCAII Y7F SINGLE MUTANT
REMARK 900 RELATED ID: 3TVO   RELATED DB: PDB
REMARK 900 HCAII Y7F/N67Q DOUBLE MUTANT
DBREF  3TVN X    3   261  UNP    P00918   CAH2_HUMAN       3    260
SEQADV 3TVN GLN X   67  UNP  P00918    ASN    67 ENGINEERED MUTATION
SEQRES   1 X  258  HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU HIS
SEQRES   2 X  258  TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG GLN
SEQRES   3 X  258  SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR ASP
SEQRES   4 X  258  PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN ALA
SEQRES   5 X  258  THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE GLN
SEQRES   6 X  258  VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU LYS
SEQRES   7 X  258  GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN PHE
SEQRES   8 X  258  HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER GLU
SEQRES   9 X  258  HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU HIS
SEQRES  10 X  258  LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY LYS
SEQRES  11 X  258  ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY ILE
SEQRES  12 X  258  PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN LYS
SEQRES  13 X  258  VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY LYS
SEQRES  14 X  258  SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU LEU
SEQRES  15 X  258  PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER LEU
SEQRES  16 X  258  THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE VAL
SEQRES  17 X  258  LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL LEU
SEQRES  18 X  258  LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU PRO
SEQRES  19 X  258  GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN PRO
SEQRES  20 X  258  LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     ZN  X 262       1
HETNAM      ZN ZINC ION
FORMUL   2   ZN    ZN 2+
FORMUL   3  HOH   *373(H2 O)
HELIX    1   1 HIS X   15  ASP X   19  5                                   5
HELIX    2   2 PHE X   20  GLY X   25  5                                   6
HELIX    3   3 LYS X  127  GLY X  129  5                                   3
HELIX    4   4 ASP X  130  VAL X  135  1                                   6
HELIX    5   5 LYS X  154  GLY X  156  5                                   3
HELIX    6   6 LEU X  157  LEU X  164  1                                   8
HELIX    7   7 ASP X  165  LYS X  168  5                                   4
HELIX    8   8 ASP X  180  LEU X  185  5                                   6
HELIX    9   9 SER X  219  ARG X  227  1                                   9
SHEET    1   A 2 ASP X  32  ILE X  33  0
SHEET    2   A 2 THR X 108  VAL X 109  1  O  THR X 108   N  ILE X  33
SHEET    1   B10 LYS X  39  TYR X  40  0
SHEET    2   B10 LYS X 257  ALA X 258  1  O  ALA X 258   N  LYS X  39
SHEET    3   B10 TYR X 191  GLY X 196 -1  N  THR X 193   O  LYS X 257
SHEET    4   B10 VAL X 207  LEU X 212 -1  O  VAL X 207   N  GLY X 196
SHEET    5   B10 LEU X 141  VAL X 150  1  N  GLY X 145   O  ILE X 210
SHEET    6   B10 ALA X 116  ASN X 124 -1  N  LEU X 118   O  ILE X 146
SHEET    7   B10 THR X  87  TRP X  97 -1  N  GLN X  92   O  VAL X 121
SHEET    8   B10 PHE X  66  PHE X  70 -1  N  VAL X  68   O  PHE X  93
SHEET    9   B10 SER X  56  ASN X  61 -1  N  LEU X  57   O  GLU X  69
SHEET   10   B10 SER X 173  ASP X 175 -1  O  ALA X 174   N  ILE X  59
SHEET    1   C 6 LEU X  47  SER X  50  0
SHEET    2   C 6 VAL X  78  GLY X  81 -1  O  LYS X  80   N  SER X  48
SHEET    3   C 6 THR X  87  TRP X  97 -1  O  TYR X  88   N  LEU X  79
SHEET    4   C 6 ALA X 116  ASN X 124 -1  O  VAL X 121   N  GLN X  92
SHEET    5   C 6 LEU X 141  VAL X 150 -1  O  ILE X 146   N  LEU X 118
SHEET    6   C 6 ILE X 216  VAL X 218  1  O  ILE X 216   N  PHE X 147
LINK        ZN    ZN X 262                 O   HOH X 394     1555   1555  1.98
LINK         NE2 HIS X  96                ZN    ZN X 262     1555   1555  2.02
LINK         NE2 HIS X  94                ZN    ZN X 262     1555   1555  2.05
LINK         ND1 HIS X 119                ZN    ZN X 262     1555   1555  2.11
CISPEP   1 SER X   29    PRO X   30          0         1.10
CISPEP   2 PRO X  201    PRO X  202          0         9.73
SITE     1 AC1  4 HIS X  94  HIS X  96  HIS X 119  HOH X 394
CRYST1   42.005   41.223   72.059  90.00 104.32  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      0.023807  0.000000  0.006076        0.00000
SCALE2      0.000000  0.024258  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014322        0.00000
      
PROCHECK
Go to PROCHECK summary
 References