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PDBsum entry 1g6v

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Top Page protein metals Protein-protein interface(s) links
Lyase/immune system PDB id
1g6v
Jmol
Contents
Protein chains
256 a.a. *
126 a.a. *
Metals
_ZN
* Residue conservation analysis
HEADER    LYASE/IMMUNE SYSTEM                     08-NOV-00   1G6V
TITLE     COMPLEX OF THE CAMELID HEAVY-CHAIN ANTIBODY FRAGMENT CAB-
TITLE    2 CA05 WITH BOVINE CARBONIC ANHYDRASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 4.2.1.1;
COMPND   5 MOL_ID: 2;
COMPND   6 MOLECULE: ANTIBODY HEAVY CHAIN;
COMPND   7 CHAIN: K;
COMPND   8 FRAGMENT: CAB-CA05, VARIABLE DOMAIN;
COMPND   9 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE   3 ORGANISM_COMMON: CATTLE;
SOURCE   4 ORGANISM_TAXID: 9913;
SOURCE   5 MOL_ID: 2;
SOURCE   6 ORGANISM_SCIENTIFIC: CAMELUS DROMEDARIUS;
SOURCE   7 ORGANISM_COMMON: ARABIAN CAMEL;
SOURCE   8 ORGANISM_TAXID: 9838;
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    ANTIBODY, ANTIGEN, COMPLEX, IMMUNOGLOBULIN, LYASE/IMMUNE
KEYWDS   2 SYSTEM COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.DESMYTER,K.DECANNIERE,S.MUYLDERMANS,L.WYNS
REVDAT   3   24-FEB-09 1G6V    1       VERSN
REVDAT   2   05-APR-05 1G6V    1       JRNL
REVDAT   1   22-NOV-00 1G6V    0
JRNL        AUTH   A.DESMYTER,K.DECANNIERE,S.MUYLDERMANS,L.WYNS
JRNL        TITL   ANTIGEN SPECIFICITY AND HIGH AFFINITY BINDING
JRNL        TITL 2 PROVIDED BY ONE SINGLE LOOP OF A CAMEL
JRNL        TITL 3 SINGLE-DOMAIN ANTIBODY.
JRNL        REF    J.BIOL.CHEM.                  V. 276 26285 2001
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   11342547
JRNL        DOI    10.1074/JBC.M102107200
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
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 BASED CNS LIBRARIES
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.50
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
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             : 10533
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.210
REMARK   3   FREE R VALUE                     : 0.276
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 502
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            : 2988
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 1
REMARK   3   SOLVENT ATOMS            : 0
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) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.36
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : GROUPED ISOTROPIC
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 1G6V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-NOV-00.
REMARK 100 THE RCSB ID CODE IS RCSB012307.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-98
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : 5.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG
REMARK 200  BEAMLINE                       : BW7A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10533
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0
REMARK 200  DATA REDUNDANCY                : 5.600
REMARK 200  R MERGE                    (I) : 0.15900
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 4.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.96
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.34500
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.100
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: 1F2X, 1CA2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 73.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM CITRATE, PH 5.6,
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z+1/2
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        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      112.02500
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       41.93000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       41.93000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       56.01250
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       41.93000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       41.93000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      168.03750
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       41.93000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       41.93000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       56.01250
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       41.93000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       41.93000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      168.03750
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      112.02500
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, K
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     LYS A   261
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    HIS A  17       -4.95    -54.69
REMARK 500    ALA A  23        1.33    -68.48
REMARK 500    PRO A  30     -168.68    -75.96
REMARK 500    PRO A  42        3.14    -65.16
REMARK 500    TYR A  51       30.97    -87.40
REMARK 500    HIS A  64        3.51   -150.17
REMARK 500    ALA A  65     -172.88    174.79
REMARK 500    LYS A  80     -155.53   -137.50
REMARK 500    LYS A 111       16.77     56.81
REMARK 500    VAL A 135       23.75    -78.66
REMARK 500    PRO A 138       -3.82    -57.97
REMARK 500    ASP A 139       -2.55   -141.50
REMARK 500    VAL A 150      150.85    -44.73
REMARK 500    VAL A 160      -70.14   -101.64
REMARK 500    ILE A 167       41.47   -142.96
REMARK 500    ASN A 178       91.88     57.19
REMARK 500    THR A 199       36.49    -88.97
REMARK 500    THR A 200      147.77   -173.18
REMARK 500    PRO A 201      138.47    -39.64
REMARK 500    CYS A 206      -10.47   -145.44
REMARK 500    THR A 208       65.09   -106.62
REMARK 500    TRP A 209      139.66    -33.81
REMARK 500    VAL A 223      -15.20    -48.94
REMARK 500    ARG A 227       33.22    -76.03
REMARK 500    ASN A 244       34.34   -150.51
REMARK 500    LYS A 252     -109.89     38.37
REMARK 500    ASN A 253      -83.74    -90.44
REMARK 500    ARG A 254     -151.54     22.99
REMARK 500    GLN A 255      139.07    163.96
REMARK 500    SER K 817      140.33   -177.40
REMARK 500    VAL K 829       -7.65    -49.46
REMARK 500    VAL K 848      -65.69    -95.67
REMARK 500    ASP K 860      -30.71    -37.63
REMARK 500    ASN K 872      -22.58    -35.86
REMARK 500    ASN K 875       67.16     39.93
REMARK 500    ALA K 890     -175.24   -179.98
REMARK 500    LEU K 908       64.91     68.47
REMARK 500    ARG K 909       54.50   -140.60
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 A1001  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  96   NE2
REMARK 620 2 HIS A  94   NE2 105.4
REMARK 620 3 HIS A 119   ND1  84.1 122.7
REMARK 620 N                    1     2
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 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F2X   RELATED DB: PDB
REMARK 900 STRUCTURE OF THE UNCOMPLEXED ANTIBODY
DBREF  1G6V A    1   261  UNP    P00921   CAH2_BOVIN       0    260
DBREF  1G6V K  801   926  PDB    1G6V     1G6V           801    926
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 K  126  GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER VAL GLN
SEQRES   2 K  126  ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES   3 K  126  TYR THR VAL SER THR TYR CYS MET GLY TRP PHE ARG GLN
SEQRES   4 K  126  ALA PRO GLY LYS GLU ARG GLU GLY VAL ALA THR ILE LEU
SEQRES   5 K  126  GLY GLY SER THR TYR TYR GLY ASP SER VAL LYS GLY ARG
SEQRES   6 K  126  PHE THR ILE SER GLN ASP ASN ALA LYS ASN THR VAL TYR
SEQRES   7 K  126  LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA ILE
SEQRES   8 K  126  TYR TYR CYS ALA GLY SER THR VAL ALA SER THR GLY TRP
SEQRES   9 K  126  CYS SER ARG LEU ARG PRO TYR ASP TYR HIS TYR ARG GLY
SEQRES  10 K  126  GLN GLY THR GLN VAL THR VAL SER SER
HET     ZN  A1001       1
HETNAM      ZN ZINC ION
FORMUL   3   ZN    ZN 2+
HELIX    1   1 HIS A   15  PHE A   20  1                                   6
HELIX    2   2 PRO A   21  GLY A   25  5                                   5
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  ASP A  162  1                                   9
HELIX    6   6 VAL A  163  LYS A  168  5                                   6
HELIX    7   7 ASP A  180  LEU A  185  5                                   6
HELIX    8   8 GLN A  222  ARG A  227  1                                   6
HELIX    9   9 LYS K  885  THR K  889  5                                   5
HELIX   10  10 SER K  901  SER K  906  1                                   6
HELIX   11  11 ARG K  909  TYR K  913  5                                   5
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   B16 LYS A  39  TYR A  40  0
SHEET    2   B16 LYS A 257  ALA A 258  1  N  ALA A 258   O  LYS A  39
SHEET    3   B16 TYR A 191  THR A 193 -1  O  THR A 193   N  LYS A 257
SHEET    4   B16 ILE A 210  LEU A 212 -1  O  VAL A 211   N  TRP A 192
SHEET    5   B16 LEU A 141  GLY A 151  1  O  VAL A 143   N  ILE A 210
SHEET    6   B16 ILE A 216  SER A 219  1  N  ILE A 216   O  PHE A 147
SHEET    7   B16 LEU A 141  GLY A 151  1  O  PHE A 147   N  ILE A 216
SHEET    8   B16 ALA A 116  ASN A 124 -1  O  ALA A 116   N  LEU A 148
SHEET    9   B16 TYR A  88  TRP A  97 -1  N  ARG A  89   O  TRP A 123
SHEET   10   B16 VAL A  78  GLY A  81 -1  N  LEU A  79   O  TYR A  88
SHEET   11   B16 LEU A  47  SER A  50 -1  O  SER A  48   N  LYS A  80
SHEET   12   B16 VAL A  78  GLY A  81 -1  N  VAL A  78   O  SER A  50
SHEET   13   B16 TYR A  88  TRP A  97 -1  O  TYR A  88   N  LEU A  79
SHEET   14   B16 PHE A  66  PHE A  70 -1  O  PHE A  66   N  PHE A  95
SHEET   15   B16 SER A  56  ASN A  61 -1  N  LEU A  57   O  GLU A  69
SHEET   16   B16 SER A 173  ALA A 174 -1  O  ALA A 174   N  ILE A  59
SHEET    1   C 4 GLN K 803  SER K 807  0
SHEET    2   C 4 SER K 817  SER K 825 -1  N  SER K 821   O  SER K 807
SHEET    3   C 4 VAL K 877  ASN K 882 -1  N  VAL K 877   O  CYS K 822
SHEET    4   C 4 PHE K 866  GLN K 870 -1  O  THR K 867   N  GLN K 880
SHEET    1   D 8 GLY K 810  GLN K 813  0
SHEET    2   D 8 THR K 920  SER K 925  1  O  GLN K 921   N  GLY K 810
SHEET    3   D 8 ALA K 890  GLY K 896 -1  O  ALA K 890   N  VAL K 922
SHEET    4   D 8 TYR K 915  ARG K 916 -1  O  TYR K 915   N  GLY K 896
SHEET    5   D 8 ALA K 890  GLY K 896 -1  N  GLY K 896   O  TYR K 915
SHEET    6   D 8 MET K 834  GLN K 839 -1  O  GLY K 835   N  ALA K 895
SHEET    7   D 8 GLU K 846  LEU K 852 -1  O  GLU K 846   N  ARG K 838
SHEET    8   D 8 SER K 855  TYR K 858 -1  O  SER K 855   N  LEU K 852
SSBOND   1 CYS K  822    CYS K  894                          1555   1555  2.03
SSBOND   2 CYS K  833    CYS K  905                          1555   1555  2.03
LINK        ZN    ZN A1001                 NE2 HIS A  96     1555   1555  2.23
LINK        ZN    ZN A1001                 NE2 HIS A  94     1555   1555  2.67
LINK        ZN    ZN A1001                 ND1 HIS A 119     1555   1555  2.39
CISPEP   1 SER A   29    PRO A   30          0        -0.19
CISPEP   2 PRO A  201    PRO A  202          0         0.26
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  THR A 199
CRYST1   83.860   83.860  224.050  90.00  90.00  90.00 P 41 21 2     8
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      0.011925  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011925  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004463        0.00000
      
PROCHECK
Go to PROCHECK summary
 References