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PDBsum entry 3uyq

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Lyase PDB id
3uyq
Jmol
Contents
Protein chain
259 a.a.
Metals
_ZN
Waters ×304
HEADER    LYASE                                   06-DEC-11   3UYQ
TITLE     HCA 3
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 3;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE III, CARBONIC ANHYDRASE III, CA-III;
COMPND   5 EC: 4.2.1.1;
COMPND   6 ENGINEERED: YES;
COMPND   7 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: CA3, HCA3;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET
KEYWDS    PROTON SHUTTLE, HCA III, PROTON TRANSFER, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Z.FISHER,R.MCKENNA
REVDAT   1   21-DEC-11 3UYQ    0
SPRSDE     21-DEC-11 3UYQ      2HFX
JRNL        AUTH   I.ELDER,Z.FISHER,P.J.LAIPIS,C.TU,R.MCKENNA,D.N.SILVERMAN
JRNL        TITL   STRUCTURAL AND KINETIC ANALYSIS OF PROTON SHUTTLE RESIDUES
JRNL        TITL 2 IN THE ACTIVE SITE OF HUMAN CARBONIC ANHYDRASE III.
JRNL        REF    PROTEINS                      V.  68   337 2007
JRNL        REFN                   ISSN 0887-3585
JRNL        PMID   17427958
JRNL        DOI    10.1002/PROT.21403
REMARK   2
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 27406
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : RANDOM
REMARK   3   FREE R VALUE TEST SET SELECTION  : THROUGHOUT
REMARK   3   R VALUE            (WORKING SET) : 0.205
REMARK   3   FREE R VALUE                     : 0.219
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 2666
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2082
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 1
REMARK   3   SOLVENT ATOMS            : 304
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3UYQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-DEC-11.
REMARK 100 THE RCSB ID CODE IS RCSB069376.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 04-JUN-07
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : 5.8
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 RU300
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27406
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700
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     (%) : 96.4
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 41.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M  SODIUM
REMARK 280  ACETATE, 30% PEG 4K, PH 5.8, VAPOR DIFFUSION, TEMPERATURE 277K
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       20.88500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.95000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.39000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.95000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.88500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       25.39000
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: 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 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   3       59.64    -54.02
REMARK 500    THR A  65     -178.97    178.87
REMARK 500    ARG A  76      -67.21   -106.09
REMARK 500    ASN A 128      -54.13     78.80
REMARK 500    ARG A 226       32.92    -95.95
REMARK 500    ASN A 234       83.64     38.87
REMARK 500    PRO A 236      102.00    -35.63
REMARK 500    ASN A 243       42.68   -151.08
REMARK 500    ASN A 251     -130.71     52.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 ASN A  234     GLU A  235                  124.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    GLU A   4        23.6      L          L   OUTSIDE RANGE
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 261  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  96   NE2
REMARK 620 2 HIS A 119   ND1  96.8
REMARK 620 3 HIS A  94   NE2 110.0 117.4
REMARK 620 4 HOH A 271   O   126.6 101.3 105.1
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 A 261
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UYN   RELATED DB: PDB
DBREF  3UYQ A    1   260  UNP    P07451   CAH3_HUMAN       1    260
SEQADV 3UYQ ILE A   31  UNP  P07451    VAL    31 ENGINEERED MUTATION
SEQADV 3UYQ HIS A   64  UNP  P07451    LYS    64 ENGINEERED MUTATION
SEQADV 3UYQ SER A  182  UNP  P07451    CYS   182 ENGINEERED MUTATION
SEQADV 3UYQ SER A  187  UNP  P07451    CYS   187 ENGINEERED MUTATION
SEQRES   1 A  260  MET ALA LYS GLU TRP GLY TYR ALA SER HIS ASN GLY PRO
SEQRES   2 A  260  ASP HIS TRP HIS GLU LEU PHE PRO ASN ALA LYS GLY GLU
SEQRES   3 A  260  ASN GLN SER PRO ILE GLU LEU HIS THR LYS ASP ILE ARG
SEQRES   4 A  260  HIS ASP PRO SER LEU GLN PRO TRP SER VAL SER TYR ASP
SEQRES   5 A  260  GLY GLY SER ALA LYS THR ILE LEU ASN ASN GLY HIS THR
SEQRES   6 A  260  CYS ARG VAL VAL PHE ASP ASP THR TYR ASP ARG SER MET
SEQRES   7 A  260  LEU ARG GLY GLY PRO LEU PRO GLY PRO TYR ARG LEU ARG
SEQRES   8 A  260  GLN PHE HIS LEU HIS TRP GLY SER SER ASP ASP HIS GLY
SEQRES   9 A  260  SER GLU HIS THR VAL ASP GLY VAL LYS TYR ALA ALA GLU
SEQRES  10 A  260  LEU HIS LEU VAL HIS TRP ASN PRO LYS TYR ASN THR PHE
SEQRES  11 A  260  LYS GLU ALA LEU LYS GLN ARG ASP GLY ILE ALA VAL ILE
SEQRES  12 A  260  GLY ILE PHE LEU LYS ILE GLY HIS GLU ASN GLY GLU PHE
SEQRES  13 A  260  GLN ILE PHE LEU ASP ALA LEU ASP LYS ILE LYS THR LYS
SEQRES  14 A  260  GLY LYS GLU ALA PRO PHE THR LYS PHE ASP PRO SER SER
SEQRES  15 A  260  LEU PHE PRO ALA SER ARG ASP TYR TRP THR TYR GLN GLY
SEQRES  16 A  260  SER PHE THR THR PRO PRO CYS GLU GLU CYS ILE VAL TRP
SEQRES  17 A  260  LEU LEU LEU LYS GLU PRO MET THR VAL SER SER ASP GLN
SEQRES  18 A  260  MET ALA LYS LEU ARG SER LEU LEU SER SER ALA GLU ASN
SEQRES  19 A  260  GLU PRO PRO VAL PRO LEU VAL SER ASN TRP ARG PRO PRO
SEQRES  20 A  260  GLN PRO ILE ASN ASN ARG VAL VAL ARG ALA SER PHE LYS
HET     ZN  A 261       1
HETNAM      ZN ZINC ION
FORMUL   2   ZN    ZN 2+
FORMUL   3  HOH   *304(H2 O)
HELIX    1   1 HIS A   15  LEU A   19  5                                   5
HELIX    2   2 PHE A   20  GLY A   25  5                                   6
HELIX    3   3 HIS A   34  ILE A   38  5                                   5
HELIX    4   4 ASP A   52  GLY A   54  5                                   3
HELIX    5   5 PRO A  125  ASN A  128  5                                   4
HELIX    6   6 THR A  129  LEU A  134  1                                   6
HELIX    7   7 ASN A  153  ASP A  161  1                                   9
HELIX    8   8 ALA A  162  ILE A  166  5                                   5
HELIX    9   9 ASP A  179  PHE A  184  5                                   6
HELIX   10  10 SER A  218  ARG A  226  1                                   9
SHEET    1   A 2 GLU A  32  LEU A  33  0
SHEET    2   A 2 THR A 108  VAL A 109  1  O  THR A 108   N  LEU A  33
SHEET    1   B10 ARG A  39  HIS A  40  0
SHEET    2   B10 ARG A 256  ALA A 257  1  O  ALA A 257   N  ARG A  39
SHEET    3   B10 TYR A 190  GLY A 195 -1  N  THR A 192   O  ARG A 256
SHEET    4   B10 ILE A 206  LEU A 211 -1  O  TRP A 208   N  TYR A 193
SHEET    5   B10 ILE A 140  ILE A 149  1  N  VAL A 142   O  LEU A 209
SHEET    6   B10 ALA A 116  TRP A 123 -1  N  LEU A 118   O  ILE A 145
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  GLN A  92   O  VAL A 121
SHEET    8   B10 CYS A  66  PHE A  70 -1  N  PHE A  70   O  ARG A  91
SHEET    9   B10 ALA A  56  ASN A  61 -1  N  LEU A  60   O  ARG A  67
SHEET   10   B10 GLU A 172  PRO A 174 -1  O  ALA A 173   N  ILE A  59
SHEET    1   C 6 TRP A  47  SER A  50  0
SHEET    2   C 6 MET A  78  GLY A  81 -1  O  ARG A  80   N  SER A  48
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  TRP A 123 -1  O  VAL A 121   N  GLN A  92
SHEET    5   C 6 ILE A 140  ILE A 149 -1  O  ILE A 145   N  LEU A 118
SHEET    6   C 6 MET A 215  VAL A 217  1  O  MET A 215   N  LYS A 148
LINK         NE2 HIS A  96                ZN    ZN A 261     1555   1555  2.13
LINK         ND1 HIS A 119                ZN    ZN A 261     1555   1555  2.17
LINK         NE2 HIS A  94                ZN    ZN A 261     1555   1555  2.20
LINK        ZN    ZN A 261                 O   HOH A 271     1555   1555  2.69
CISPEP   1 SER A   29    PRO A   30          0         0.00
CISPEP   2 PRO A  200    PRO A  201          0        11.09
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  HOH A 271
CRYST1   41.770   50.780  117.900  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      0.023941  0.000000  0.000000        0.00000
SCALE2      0.000000  0.019693  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008482        0.00000
      
PROCHECK
Go to PROCHECK summary
 References