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PDBsum entry 1znc

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
1znc
Jmol
Contents
Protein chains
262 a.a. *
247 a.a. *
Ligands
SO4 ×2
Metals
_ZN ×2
Waters ×32
* Residue conservation analysis
HEADER    LYASE                                   17-SEP-96   1ZNC
TITLE     HUMAN CARBONIC ANHYDRASE IV
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE IV;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 4.2.1.1;
COMPND   5 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: HUMAN CAIV;
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: CHO-CELLS;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCAGGS
KEYWDS    GPI-ANCHOR, MEMBRANE, LYASE, ZINC, SIGNAL
EXPDTA    X-RAY DIFFRACTION
AUTHOR    T.STAMS,D.W.CHRISTIANSON
REVDAT   2   24-FEB-09 1ZNC    1       VERSN
REVDAT   1   17-SEP-97 1ZNC    0
JRNL        AUTH   T.STAMS,S.K.NAIR,T.OKUYAMA,A.WAHEED,W.S.SLY,
JRNL        AUTH 2 D.W.CHRISTIANSON
JRNL        TITL   CRYSTAL STRUCTURE OF THE SECRETORY FORM OF
JRNL        TITL 2 MEMBRANE-ASSOCIATED HUMAN CARBONIC ANHYDRASE IV AT
JRNL        TITL 3 2.8-A RESOLUTION.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  93 13589 1996
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   8942978
JRNL        DOI    10.1073/PNAS.93.24.13589
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   A.WAHEED,T.OKUYAMA,T.HEYDUK,W.S.SLY
REMARK   1  TITL   CARBONIC ANHYDRASE IV: PURIFICATION OF A SECRETORY
REMARK   1  TITL 2 FORM OF THE RECOMBINANT HUMAN ENZYME AND
REMARK   1  TITL 3 IDENTIFICATION OF THE POSITIONS AND IMPORTANCE OF
REMARK   1  TITL 4 ITS DISULFIDE BONDS
REMARK   1  REF    ARCH.BIOCHEM.BIOPHYS.         V. 333   432 1996
REMARK   1  REFN                   ISSN 0003-9861
REMARK   2
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.0
REMARK   3   NUMBER OF REFLECTIONS             : 12067
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : FREE-R
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.197
REMARK   3   FREE R VALUE                     : 0.252
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.500
REMARK   3   FREE R VALUE TEST SET COUNT      : 650
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) : 2.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.93
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 72.40
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1261
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2800
REMARK   3   BIN FREE R VALUE                    : 0.3460
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.50
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 78
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            : 4089
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 34
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.30
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) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.40
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.80
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.20
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  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : 0.20  ; 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 1ZNC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 298
REMARK 200  PH                             : 5.1
REMARK 200  NUMBER OF CRYSTALS USED        : 2
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 RUH2R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (AGROVATA, ROTAVATA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13626
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
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     (%) : 95.0
REMARK 200  DATA REDUNDANCY                : 3.400
REMARK 200  R MERGE                    (I) : 0.08000
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) : 2.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.87
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30
REMARK 200  R MERGE FOR SHELL          (I) : 0.25300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: POLYALANINE MODEL OF CAII MISSING N-TERMINAL 30
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3,350; 100MM NA ACETATE PH
REMARK 280  5.1
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       44.75000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.85000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       44.75000
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.85000
REMARK 290   SMTRY3   4  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 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 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     ALA A     1
REMARK 465     GLU A     2
REMARK 465     SER A     3
REMARK 465     HIS A     4
REMARK 465     ALA B     1
REMARK 465     GLU B     2
REMARK 465     SER B     3
REMARK 465     HIS B     4
REMARK 465     LYS B   123A
REMARK 465     GLU B   123B
REMARK 465     LYS B   123C
REMARK 465     GLY B   123D
REMARK 465     THR B   123E
REMARK 465     SER B   123F
REMARK 465     ARG B   123G
REMARK 465     ASN B   123H
REMARK 465     VAL B   123I
REMARK 465     LYS B   123J
REMARK 465     GLU B   123K
REMARK 465     ALA B   123L
REMARK 465     GLN B   123M
REMARK 465     ASP B   123N
REMARK 465     PRO B   123O
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    CYS A  11G     142.33   -173.64
REMARK 500    ASN A  72       15.09     59.98
REMARK 500    LYS A 103       35.77   -147.07
REMARK 500    ILE A 167       50.77   -140.69
REMARK 500    GLU A 171       -6.81     74.55
REMARK 500    LYS A 206       39.83   -144.23
REMARK 500    LEU A 248      154.60    -49.20
REMARK 500    CYS B  11G     142.87   -174.52
REMARK 500    LYS B 103       35.95   -147.37
REMARK 500    ILE B 167       50.43   -140.66
REMARK 500    GLU B 171       -7.65     74.14
REMARK 500    THR B 199       30.82    -99.78
REMARK 500    LYS B 206       39.92   -143.70
REMARK 500    LEU B 248      154.66    -47.15
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 301  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  94   NE2
REMARK 620 2 HIS A  96   NE2  93.1
REMARK 620 3 HIS A 119   ND1 104.1  94.3
REMARK 620 4 SO4 A 601   O3  111.7 132.7 116.0
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 302  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B  94   NE2
REMARK 620 2 HIS B  96   NE2  93.5
REMARK 620 3 HIS B 119   ND1 100.4  92.2
REMARK 620 4 SO4 B 701   O3  112.2 139.0 112.6
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CTA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ZINC COORDINATED BY HIS A 94, HIS A 96, AND
REMARK 800  HIS A 119. ALSO COORDINATED BY AN OXYGEN ON THE SULFATE GROUP.
REMARK 800 SITE_IDENTIFIER: CTB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ZINC COORDINATED BY HIS B 94, HIS B 96, AND
REMARK 800  HIS B 119. ALSO COORDINATED BY AN OXYGEN ON THE SULFATE GROUP.
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 601
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 302
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 701
REMARK 999
REMARK 999 SEQUENCE
REMARK 999
REMARK 999 THE RESIDUE NUMBERING IS BASED ON THE RESIDUE NUMBERING OF
REMARK 999 CARBONIC ANHYDRASE II.  INSERTIONS ARE MARKED WITH THE
REMARK 999 ADDITION OF AN ALPHABETIC CHARACTER (A, B, ...) AFTER THE
REMARK 999 RESIDUE NUMBER.  DELETIONS ARE DENOTED BY MISSING RESIDUE
REMARK 999 NUMBERS.
DBREF  1ZNC A    1   259  UNP    P22748   CAH4_HUMAN      19    284
DBREF  1ZNC B    1   259  UNP    P22748   CAH4_HUMAN      19    284
SEQRES   1 A  266  ALA GLU SER HIS TRP CYS TYR GLU VAL GLN ALA GLU SER
SEQRES   2 A  266  SER ASN TYR PRO CYS LEU VAL PRO VAL LYS TRP GLY GLY
SEQRES   3 A  266  ASN CYS GLN LYS ASP ARG GLN SER PRO ILE ASN ILE VAL
SEQRES   4 A  266  THR THR LYS ALA LYS VAL ASP LYS LYS LEU GLY ARG PHE
SEQRES   5 A  266  PHE PHE SER GLY TYR ASP LYS LYS GLN THR TRP THR VAL
SEQRES   6 A  266  GLN ASN ASN GLY HIS SER VAL MET MET LEU LEU GLU ASN
SEQRES   7 A  266  LYS ALA SER ILE SER GLY GLY GLY LEU PRO ALA PRO TYR
SEQRES   8 A  266  GLN ALA LYS GLN LEU HIS LEU HIS TRP SER ASP LEU PRO
SEQRES   9 A  266  TYR LYS GLY SER GLU HIS SER LEU ASP GLY GLU HIS PHE
SEQRES  10 A  266  ALA MET GLU MET HIS ILE VAL HIS GLU LYS GLU LYS GLY
SEQRES  11 A  266  THR SER ARG ASN VAL LYS GLU ALA GLN ASP PRO GLU ASP
SEQRES  12 A  266  GLU ILE ALA VAL LEU ALA PHE LEU VAL GLU ALA GLY THR
SEQRES  13 A  266  GLN VAL ASN GLU GLY PHE GLN PRO LEU VAL GLU ALA LEU
SEQRES  14 A  266  SER ASN ILE PRO LYS PRO GLU MET SER THR THR MET ALA
SEQRES  15 A  266  GLU SER SER LEU LEU ASP LEU LEU PRO LYS GLU GLU LYS
SEQRES  16 A  266  LEU ARG HIS TYR PHE ARG TYR LEU GLY SER LEU THR THR
SEQRES  17 A  266  PRO THR CYS ASP GLU LYS VAL VAL TRP THR VAL PHE ARG
SEQRES  18 A  266  GLU PRO ILE GLN LEU HIS ARG GLU GLN ILE LEU ALA PHE
SEQRES  19 A  266  SER GLN LYS LEU TYR TYR ASP LYS GLU GLN THR VAL SER
SEQRES  20 A  266  MET LYS ASP ASN VAL ARG PRO LEU GLN GLN LEU GLY GLN
SEQRES  21 A  266  ARG THR VAL ILE LYS SER
SEQRES   1 B  266  ALA GLU SER HIS TRP CYS TYR GLU VAL GLN ALA GLU SER
SEQRES   2 B  266  SER ASN TYR PRO CYS LEU VAL PRO VAL LYS TRP GLY GLY
SEQRES   3 B  266  ASN CYS GLN LYS ASP ARG GLN SER PRO ILE ASN ILE VAL
SEQRES   4 B  266  THR THR LYS ALA LYS VAL ASP LYS LYS LEU GLY ARG PHE
SEQRES   5 B  266  PHE PHE SER GLY TYR ASP LYS LYS GLN THR TRP THR VAL
SEQRES   6 B  266  GLN ASN ASN GLY HIS SER VAL MET MET LEU LEU GLU ASN
SEQRES   7 B  266  LYS ALA SER ILE SER GLY GLY GLY LEU PRO ALA PRO TYR
SEQRES   8 B  266  GLN ALA LYS GLN LEU HIS LEU HIS TRP SER ASP LEU PRO
SEQRES   9 B  266  TYR LYS GLY SER GLU HIS SER LEU ASP GLY GLU HIS PHE
SEQRES  10 B  266  ALA MET GLU MET HIS ILE VAL HIS GLU LYS GLU LYS GLY
SEQRES  11 B  266  THR SER ARG ASN VAL LYS GLU ALA GLN ASP PRO GLU ASP
SEQRES  12 B  266  GLU ILE ALA VAL LEU ALA PHE LEU VAL GLU ALA GLY THR
SEQRES  13 B  266  GLN VAL ASN GLU GLY PHE GLN PRO LEU VAL GLU ALA LEU
SEQRES  14 B  266  SER ASN ILE PRO LYS PRO GLU MET SER THR THR MET ALA
SEQRES  15 B  266  GLU SER SER LEU LEU ASP LEU LEU PRO LYS GLU GLU LYS
SEQRES  16 B  266  LEU ARG HIS TYR PHE ARG TYR LEU GLY SER LEU THR THR
SEQRES  17 B  266  PRO THR CYS ASP GLU LYS VAL VAL TRP THR VAL PHE ARG
SEQRES  18 B  266  GLU PRO ILE GLN LEU HIS ARG GLU GLN ILE LEU ALA PHE
SEQRES  19 B  266  SER GLN LYS LEU TYR TYR ASP LYS GLU GLN THR VAL SER
SEQRES  20 B  266  MET LYS ASP ASN VAL ARG PRO LEU GLN GLN LEU GLY GLN
SEQRES  21 B  266  ARG THR VAL ILE LYS SER
HET    SO4  A 601       5
HET     ZN  A 301       1
HET     ZN  B 302       1
HET    SO4  B 701       5
HETNAM     SO4 SULFATE ION
HETNAM      ZN ZINC ION
FORMUL   3  SO4    2(O4 S 2-)
FORMUL   4   ZN    2(ZN 2+)
FORMUL   7  HOH   *32(H2 O)
HELIX    1   1 GLU A    8  SER A   11B 1                                   6
HELIX    2   2 PRO A   13  LYS A   15  5                                   3
HELIX    3   3 GLY A   21  GLN A   24  5                                   4
HELIX    4   4 THR A   35  LYS A   37  5                                   3
HELIX    5   5 GLU A  155  ILE A  167  1                                  13
HELIX    6   6 LEU A  181  ASP A  183  5                                   3
HELIX    7   7 GLU A  187A ARG A  189A 5                                   5
HELIX    8   8 ARG A  220  LYS A  228  1                                  10
HELIX    9   9 GLU B    8  SER B   11B 1                                   6
HELIX   10  10 PRO B   13  LYS B   15  5                                   3
HELIX   11  11 GLY B   21  GLN B   24  5                                   4
HELIX   12  12 THR B   35  LYS B   37  5                                   3
HELIX   13  13 GLU B  155  ILE B  167  1                                  13
HELIX   14  14 LEU B  181  ASP B  183  5                                   3
HELIX   15  15 LYS B  188  ARG B  189A 5                                   3
HELIX   16  16 ARG B  220  LYS B  228  1                                  10
SHEET    1   A 2 PHE A  47  SER A  50  0
SHEET    2   A 2 SER A  78  GLY A  81 -1  N  SER A  80   O  PHE A  48
SHEET    1   B 8 SER A 173  MET A 176  0
SHEET    2   B 8 TRP A  57  ASN A  61 -1  N  VAL A  59   O  THR A 174
SHEET    3   B 8 VAL A  66  LEU A  69 -1  N  LEU A  69   O  THR A  58
SHEET    4   B 8 TYR A  88  TRP A  97 -1  N  LEU A  93   O  MET A  68
SHEET    5   B 8 MET A 116  LYS A 124 -1  N  GLU A 123   O  GLN A  89
SHEET    6   B 8 ILE A 141  VAL A 148 -1  N  VAL A 148   O  MET A 116
SHEET    7   B 8 VAL A 207  PHE A 212  1  N  VAL A 208   O  ILE A 141
SHEET    8   B 8 TYR A 191  GLY A 196 -1  N  GLY A 196   O  VAL A 207
SHEET    1   C 2 VAL A 148  GLY A 151  0
SHEET    2   C 2 ILE A 216  HIS A 219  1  N  ILE A 216   O  GLU A 149
SHEET    1   D 2 PHE B  47  SER B  50  0
SHEET    2   D 2 SER B  78  GLY B  81 -1  N  SER B  80   O  PHE B  48
SHEET    1   E 8 SER B 173  MET B 176  0
SHEET    2   E 8 TRP B  57  ASN B  61 -1  N  VAL B  59   O  THR B 174
SHEET    3   E 8 VAL B  66  LEU B  69 -1  N  LEU B  69   O  THR B  58
SHEET    4   E 8 GLN B  89  TRP B  97 -1  N  LEU B  93   O  MET B  68
SHEET    5   E 8 MET B 116  GLU B 123 -1  N  GLU B 123   O  GLN B  89
SHEET    6   E 8 ILE B 141  VAL B 148 -1  N  VAL B 148   O  MET B 116
SHEET    7   E 8 VAL B 207  PHE B 212  1  N  VAL B 208   O  ILE B 141
SHEET    8   E 8 TYR B 191  GLY B 196 -1  N  GLY B 196   O  VAL B 207
SHEET    1   F 2 VAL B 148  GLY B 151  0
SHEET    2   F 2 ILE B 216  HIS B 219  1  N  ILE B 216   O  GLU B 149
SSBOND   1 CYS A    6    CYS A   11G                         1555   1555  2.45
SSBOND   2 CYS A   23    CYS A  203                          1555   1555  2.34
SSBOND   3 CYS B    6    CYS B   11G                         1555   1555  2.51
SSBOND   4 CYS B   23    CYS B  203                          1555   1555  2.49
LINK        ZN    ZN A 301                 NE2 HIS A  94     1555   1555  2.20
LINK        ZN    ZN A 301                 NE2 HIS A  96     1555   1555  2.34
LINK        ZN    ZN A 301                 ND1 HIS A 119     1555   1555  2.07
LINK        ZN    ZN B 302                 NE2 HIS B  94     1555   1555  2.25
LINK        ZN    ZN B 302                 NE2 HIS B  96     1555   1555  2.36
LINK        ZN    ZN B 302                 ND1 HIS B 119     1555   1555  2.14
LINK        ZN    ZN B 302                 O3  SO4 B 701     1555   1555  2.31
LINK        ZN    ZN A 301                 O3  SO4 A 601     1555   1555  2.42
CISPEP   1 SER A   29    PRO A   30          0         0.42
CISPEP   2 PRO A  201    THR A  202          0         0.11
CISPEP   3 SER B   29    PRO B   30          0         0.32
CISPEP   4 PRO B  201    THR B  202          0         0.25
SITE     1 CTA  5 HIS A  94  HIS A  96  HIS A 119   ZN A 301
SITE     2 CTA  5 SO4 A 601
SITE     1 CTB  5 HIS B  94  HIS B  96  HIS B 119   ZN B 302
SITE     2 CTB  5 SO4 B 701
SITE     1 AC1  4 LEU A 198  THR A 199  TRP A 209   ZN A 301
SITE     1 AC2  5 HIS A  94  HIS A  96  HIS A 119  THR A 199
SITE     2 AC2  5 SO4 A 601
SITE     1 AC3  5 HIS B  94  HIS B  96  HIS B 119  THR B 199
SITE     2 AC3  5 SO4 B 701
SITE     1 AC4  5 HIS B 119  LEU B 198  THR B 199  TRP B 209
SITE     2 AC4  5  ZN B 302
CRYST1   89.500   47.700  141.000  90.00 106.30  90.00 C 1 2 1       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      0.011173  0.000000  0.003267        0.00000
SCALE2      0.000000  0.020964  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007389        0.00000
      
PROCHECK
Go to PROCHECK summary
 References

 

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