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PDBsum entry 1rj6

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
1rj6
Jmol
Contents
Protein chains
259 a.a. *
Ligands
NAG-NAG
AZM ×2
NAG-NAG-BMA-MAN
Metals
_ZN ×2
Waters ×32
* Residue conservation analysis
HEADER    LYASE                                   18-NOV-03   1RJ6
TITLE     CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF MURINE CARBONIC
TITLE    2 ANHYDRASE XIV IN COMPLEX WITH ACETAZOLAMIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE XIV;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND   5 SYNONYM: CARBONATE DEHYDRATASE XIV, CA-XIV;
COMPND   6 EC: 4.2.1.1;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE   4 ORGANISM_TAXID: 10090;
SOURCE   5 GENE: CA14, CAR14, CATM;
SOURCE   6 EXPRESSION_SYSTEM: CHLOROCEBUS AETHIOPS;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: AFRICAN GREEN MONKEY;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9534;
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: COS-7;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PCXN
KEYWDS    BETA-SHEET, ALPHA-HELIX, ZINC ENZYME, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.A.WHITTINGTON,J.H.GRUBB,A.WAHEED,G.N.SHAH,W.S.SLY,D.W.CHRISTIANSON
REVDAT   3   13-JUL-11 1RJ6    1       VERSN
REVDAT   2   24-FEB-09 1RJ6    1       VERSN
REVDAT   1   09-MAR-04 1RJ6    0
JRNL        AUTH   D.A.WHITTINGTON,J.H.GRUBB,A.WAHEED,G.N.SHAH,W.S.SLY,
JRNL        AUTH 2 D.W.CHRISTIANSON
JRNL        TITL   EXPRESSION, ASSAY, AND STRUCTURE OF THE EXTRACELLULAR DOMAIN
JRNL        TITL 2 OF MURINE CARBONIC ANHYDRASE XIV: IMPLICATIONS FOR SELECTIVE
JRNL        TITL 3 INHIBITION OF MEMBRANE-ASSOCIATED ISOZYMES.
JRNL        REF    J.BIOL.CHEM.                  V. 279  7223 2004
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   14660577
JRNL        DOI    10.1074/JBC.M310809200
REMARK   2
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
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) : 2.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 953197.740
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.0
REMARK   3   NUMBER OF REFLECTIONS             : 13535
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) : 0.207
REMARK   3   FREE R VALUE                     : 0.253
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1087
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 72.60
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1609
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3470
REMARK   3   BIN FREE R VALUE                    : 0.3870
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 6.50
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 111
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.037
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4114
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 106
REMARK   3   SOLVENT ATOMS            : 32
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 55.90
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.70
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 15.36000
REMARK   3    B22 (A**2) : -23.03000
REMARK   3    B33 (A**2) : 7.68000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -11.46000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.36
REMARK   3   ESD FROM SIGMAA              (A) : 0.54
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.46
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.61
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) : 24.50
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.00
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : GROUPED
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 : FLAT MODEL
REMARK   3   KSOL        : 0.35
REMARK   3   BSOL        : 49.35
REMARK   3
REMARK   3  NCS MODEL : CONSTR
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  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : ION.PARAM
REMARK   3  PARAMETER FILE  4  : CARBOHYDRATE.PARAM
REMARK   3  PARAMETER FILE  5  : AZM.PARAM
REMARK   3  PARAMETER FILE  6  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP
REMARK   3  TOPOLOGY FILE  3   : ION.TOP
REMARK   3  TOPOLOGY FILE  4   : CARBOHYDRATE.TOP
REMARK   3  TOPOLOGY FILE  5   : AZM.TOP
REMARK   3  TOPOLOGY FILE  6   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: RESOLUTION-DEPENDENT WEIGHTING SCHEME;
REMARK   3  BULK SOLVENT MODEL USED
REMARK   4
REMARK   4 1RJ6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-03.
REMARK 100 THE RCSB ID CODE IS RCSB020792.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 29-MAY-03
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X12C
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.10004
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : BRANDEIS - B4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13548
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0
REMARK 200  DATA REDUNDANCY                : 3.200
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.08500
REMARK 200   FOR THE DATA SET  : 8.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 68.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.27400
REMARK 200   FOR SHELL         : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 55.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM ACETATE, SODIUM
REMARK 280  CHLORIDE, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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       37.90000
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 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     GLY A     1
REMARK 465     GLY A     2
REMARK 465     GLY B     1
REMARK 465     GLY B     2
REMARK 465     HIS B     3
REMARK 465     HIS B     4
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (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,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    GLY A  63   N   -  CA  -  C   ANGL. DEV. = -15.3 DEGREES
REMARK 500    LEU A  93   CA  -  CB  -  CG  ANGL. DEV. =  14.4 DEGREES
REMARK 500    ARG A 163   CD  -  NE  -  CZ  ANGL. DEV. =  12.2 DEGREES
REMARK 500    ARG A 163   NE  -  CZ  -  NH1 ANGL. DEV. =   7.9 DEGREES
REMARK 500    ARG A 163   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.4 DEGREES
REMARK 500    GLY B  63   N   -  CA  -  C   ANGL. DEV. = -16.2 DEGREES
REMARK 500    LEU B  93   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES
REMARK 500    ARG B 163   CD  -  NE  -  CZ  ANGL. DEV. =  11.4 DEGREES
REMARK 500    ARG B 163   NE  -  CZ  -  NH1 ANGL. DEV. =  -8.0 DEGREES
REMARK 500    ARG B 163   NE  -  CZ  -  NH2 ANGL. DEV. =   7.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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    GLN A  13       -8.61    -53.08
REMARK 500    ALA A  27       55.85   -144.46
REMARK 500    GLN A  53       75.64   -112.63
REMARK 500    THR A  65     -177.45   -173.96
REMARK 500    GLN A 139       19.52     56.39
REMARK 500    ASP A 171       -6.55     61.06
REMARK 500    GLU A 228       67.96   -108.94
REMARK 500    THR A 228A     -37.91   -154.81
REMARK 500    PRO A 240      114.72    -39.79
REMARK 500    ASN A 244       44.47   -100.10
REMARK 500    ALA B  27       56.53   -143.36
REMARK 500    GLN B  53       76.00   -112.46
REMARK 500    THR B  65     -177.49   -173.84
REMARK 500    ASP B 124       83.05    -67.15
REMARK 500    ASP B 171       -7.08     61.91
REMARK 500    GLU B 228       67.59   -108.67
REMARK 500    THR B 228A     -38.98   -153.87
REMARK 500    PRO B 240      114.98    -39.88
REMARK 500    ASN B 244       44.52    -99.14
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 601  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  94   NE2
REMARK 620 2 HIS A  96   NE2 119.9
REMARK 620 3 HIS A 119   ND1 117.6 110.5
REMARK 620 4 AZM A 400   N1   80.6 116.6 107.9
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 601  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B  94   NE2
REMARK 620 2 HIS B  96   NE2 125.3
REMARK 620 3 HIS B 119   ND1 112.8 114.1
REMARK 620 4 AZM B 401   N1   90.5 108.8  98.2
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 NAG A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZM A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZM B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RJ5   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT ACETAZOLAMIDE.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHORS MAINTAIN THAT FOR THIS RESIDUE
REMARK 999 THE SEQUENCING RESULTS CONDUCTED BY THEM DO
REMARK 999 NOT AGREE WITH THAT DEPOSITED IN THE SEQUENCE
REMARK 999 DATABASE.
DBREF  1RJ6 A    1   260  UNP    Q9WVT6   CAHE_MOUSE      18    278
DBREF  1RJ6 B    1   260  UNP    Q9WVT6   CAHE_MOUSE      18    278
SEQADV 1RJ6 HIS A  108  UNP  Q9WVT6    GLN   124 SEE REMARK 999
SEQADV 1RJ6 HIS B  108  UNP  Q9WVT6    GLN   124 SEE REMARK 999
SEQRES   1 A  261  GLY GLY HIS HIS TRP THR TYR GLU GLY PRO HIS GLY GLN
SEQRES   2 A  261  ASP HIS TRP PRO THR SER TYR PRO GLU CYS GLY GLY ASP
SEQRES   3 A  261  ALA GLN SER PRO ILE ASN ILE GLN THR ASP SER VAL ILE
SEQRES   4 A  261  PHE ASP PRO ASP LEU PRO ALA VAL GLN PRO HIS GLY TYR
SEQRES   5 A  261  ASP GLN LEU GLY THR GLU PRO LEU ASP LEU HIS ASN ASN
SEQRES   6 A  261  GLY HIS THR VAL GLN LEU SER LEU PRO PRO THR LEU HIS
SEQRES   7 A  261  LEU GLY GLY LEU PRO ARG LYS TYR THR ALA ALA GLN LEU
SEQRES   8 A  261  HIS LEU HIS TRP GLY GLN ARG GLY SER LEU GLU GLY SER
SEQRES   9 A  261  GLU HIS HIS ILE ASN SER GLU ALA THR ALA ALA GLU LEU
SEQRES  10 A  261  HIS VAL VAL HIS TYR ASP SER GLN SER TYR SER SER LEU
SEQRES  11 A  261  SER GLU ALA ALA GLN LYS PRO GLN GLY LEU ALA VAL LEU
SEQRES  12 A  261  GLY ILE LEU ILE GLU VAL GLY GLU THR GLU ASN PRO ALA
SEQRES  13 A  261  TYR ASP HIS ILE LEU SER ARG LEU HIS GLU ILE ARG TYR
SEQRES  14 A  261  LYS ASP GLN LYS THR SER VAL PRO PRO PHE SER VAL ARG
SEQRES  15 A  261  GLU LEU PHE PRO GLN GLN LEU GLU GLN PHE PHE ARG TYR
SEQRES  16 A  261  ASN GLY SER LEU THR THR PRO PRO CYS TYR GLN SER VAL
SEQRES  17 A  261  LEU TRP THR VAL PHE ASN ARG ARG ALA GLN ILE SER MET
SEQRES  18 A  261  GLY GLN LEU GLU LYS LEU GLN GLU THR LEU SER SER THR
SEQRES  19 A  261  GLU GLU ASP PRO SER GLU PRO LEU VAL GLN ASN TYR ARG
SEQRES  20 A  261  VAL PRO GLN PRO LEU ASN GLN ARG THR ILE PHE ALA SER
SEQRES  21 A  261  PHE
SEQRES   1 B  261  GLY GLY HIS HIS TRP THR TYR GLU GLY PRO HIS GLY GLN
SEQRES   2 B  261  ASP HIS TRP PRO THR SER TYR PRO GLU CYS GLY GLY ASP
SEQRES   3 B  261  ALA GLN SER PRO ILE ASN ILE GLN THR ASP SER VAL ILE
SEQRES   4 B  261  PHE ASP PRO ASP LEU PRO ALA VAL GLN PRO HIS GLY TYR
SEQRES   5 B  261  ASP GLN LEU GLY THR GLU PRO LEU ASP LEU HIS ASN ASN
SEQRES   6 B  261  GLY HIS THR VAL GLN LEU SER LEU PRO PRO THR LEU HIS
SEQRES   7 B  261  LEU GLY GLY LEU PRO ARG LYS TYR THR ALA ALA GLN LEU
SEQRES   8 B  261  HIS LEU HIS TRP GLY GLN ARG GLY SER LEU GLU GLY SER
SEQRES   9 B  261  GLU HIS HIS ILE ASN SER GLU ALA THR ALA ALA GLU LEU
SEQRES  10 B  261  HIS VAL VAL HIS TYR ASP SER GLN SER TYR SER SER LEU
SEQRES  11 B  261  SER GLU ALA ALA GLN LYS PRO GLN GLY LEU ALA VAL LEU
SEQRES  12 B  261  GLY ILE LEU ILE GLU VAL GLY GLU THR GLU ASN PRO ALA
SEQRES  13 B  261  TYR ASP HIS ILE LEU SER ARG LEU HIS GLU ILE ARG TYR
SEQRES  14 B  261  LYS ASP GLN LYS THR SER VAL PRO PRO PHE SER VAL ARG
SEQRES  15 B  261  GLU LEU PHE PRO GLN GLN LEU GLU GLN PHE PHE ARG TYR
SEQRES  16 B  261  ASN GLY SER LEU THR THR PRO PRO CYS TYR GLN SER VAL
SEQRES  17 B  261  LEU TRP THR VAL PHE ASN ARG ARG ALA GLN ILE SER MET
SEQRES  18 B  261  GLY GLN LEU GLU LYS LEU GLN GLU THR LEU SER SER THR
SEQRES  19 B  261  GLU GLU ASP PRO SER GLU PRO LEU VAL GLN ASN TYR ARG
SEQRES  20 B  261  VAL PRO GLN PRO LEU ASN GLN ARG THR ILE PHE ALA SER
SEQRES  21 B  261  PHE
MODRES 1RJ6 ASN A  195  ASN  GLYCOSYLATION SITE
MODRES 1RJ6 ASN B  195  ASN  GLYCOSYLATION SITE
HET    NAG  A 801      14
HET    NAG  A 802      14
HET    NAG  B 901      14
HET    NAG  B 902      14
HET    BMA  B 903      11
HET    MAN  B 904      11
HET     ZN  A 601       1
HET     ZN  B 601       1
HET    AZM  A 400      13
HET    AZM  B 401      13
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM      ZN ZINC ION
HETNAM     AZM 5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE
FORMUL   3  NAG    4(C8 H15 N O6)
FORMUL   4  BMA    C6 H12 O6
FORMUL   4  MAN    C6 H12 O6
FORMUL   5   ZN    2(ZN 2+)
FORMUL   7  AZM    2(C4 H6 N4 O3 S2)
FORMUL   9  HOH   *32(H2 O)
HELIX    1   1 HIS A   15  TYR A   20  1                                   6
HELIX    2   2 PRO A   21  GLY A   25  5                                   5
HELIX    3   3 SER A  130  GLN A  136  1                                   7
HELIX    4   4 ASN A  154  SER A  162  1                                   9
HELIX    5   5 ARG A  163  ARG A  168  5                                   6
HELIX    6   6 SER A  180  PHE A  185  5                                   6
HELIX    7   7 MET A  220  GLU A  228  1                                   9
HELIX    8   8 HIS B   15  TYR B   20  1                                   6
HELIX    9   9 PRO B   21  GLY B   25  5                                   5
HELIX   10  10 GLN B  126  TYR B  128  5                                   3
HELIX   11  11 SER B  130  ALA B  135  1                                   6
HELIX   12  12 ASN B  154  SER B  162  1                                   9
HELIX   13  13 ARG B  163  ARG B  168  5                                   6
HELIX   14  14 SER B  180  PHE B  185  5                                   6
HELIX   15  15 MET B  220  GLU B  228  1                                   9
SHEET    1   A 2 ASN A  32  ILE A  33  0
SHEET    2   A 2 HIS A 108  ILE A 109  1  O  HIS A 108   N  ILE A  33
SHEET    1   B10 ILE A  39  PHE A  40  0
SHEET    2   B10 PHE A 257  ALA A 258  1  O  ALA A 258   N  ILE A  39
SHEET    3   B10 PHE A 191  GLY A 196 -1  N  ARG A 193   O  PHE A 257
SHEET    4   B10 VAL A 207  PHE A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5   B10 LEU A 141  GLY A 151  1  N  GLY A 145   O  THR A 210
SHEET    6   B10 ALA A 116  ASP A 124 -1  N  ALA A 116   O  ILE A 148
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  GLN A  92   O  VAL A 121
SHEET    8   B10 VAL A  66  SER A  69 -1  N  LEU A  68   O  LEU A  93
SHEET    9   B10 LEU A  57  ASN A  61 -1  N  HIS A  60   O  GLN A  67
SHEET   10   B10 LYS A 173  VAL A 176 -1  O  THR A 174   N  LEU A  59
SHEET    1   C 6 GLN A  48  HIS A  50  0
SHEET    2   C 6 HIS A  78  GLY A  80 -1  O  GLY A  80   N  GLN 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  ASP A 124 -1  O  VAL A 121   N  GLN A  92
SHEET    5   C 6 LEU A 141  GLY A 151 -1  O  ILE A 148   N  ALA A 116
SHEET    6   C 6 ALA A 216  SER A 219  1  O  ALA A 216   N  GLU A 149
SHEET    1   D 2 ASN B  32  ILE B  33  0
SHEET    2   D 2 HIS B 108  ILE B 109  1  O  HIS B 108   N  ILE B  33
SHEET    1   E10 ILE B  39  PHE B  40  0
SHEET    2   E10 PHE B 257  ALA B 258  1  O  ALA B 258   N  ILE B  39
SHEET    3   E10 PHE B 191  GLY B 196 -1  N  ARG B 193   O  PHE B 257
SHEET    4   E10 VAL B 207  PHE B 212 -1  O  VAL B 207   N  GLY B 196
SHEET    5   E10 LEU B 141  GLY B 151  1  N  GLY B 145   O  THR B 210
SHEET    6   E10 ALA B 116  ASP B 124 -1  N  ALA B 116   O  ILE B 148
SHEET    7   E10 TYR B  88  TRP B  97 -1  N  GLN B  92   O  VAL B 121
SHEET    8   E10 VAL B  66  SER B  69 -1  N  LEU B  68   O  LEU B  93
SHEET    9   E10 LEU B  57  ASN B  61 -1  N  HIS B  60   O  GLN B  67
SHEET   10   E10 LYS B 173  VAL B 176 -1  O  THR B 174   N  LEU B  59
SHEET    1   F 6 GLN B  48  HIS B  50  0
SHEET    2   F 6 HIS B  78  GLY B  80 -1  O  HIS B  78   N  HIS B  50
SHEET    3   F 6 TYR B  88  TRP B  97 -1  O  TYR B  88   N  LEU B  79
SHEET    4   F 6 ALA B 116  ASP B 124 -1  O  VAL B 121   N  GLN B  92
SHEET    5   F 6 LEU B 141  GLY B 151 -1  O  ILE B 148   N  ALA B 116
SHEET    6   F 6 ALA B 216  SER B 219  1  O  ALA B 216   N  GLU B 149
SSBOND   1 CYS A   23    CYS A  203                          1555   1555  2.03
SSBOND   2 CYS B   23    CYS B  203                          1555   1555  2.03
LINK         ND2 ASN A 195                 C1  NAG A 801     1555   1555  1.45
LINK         ND2 ASN B 195                 C1  NAG B 901     1555   1555  1.46
LINK         O4  NAG A 801                 C1  NAG A 802     1555   1555  1.40
LINK         O4  NAG B 901                 C1  NAG B 902     1555   1555  1.39
LINK         O4  NAG B 902                 C1  BMA B 903     1555   1555  1.39
LINK         O6  BMA B 903                 C1  MAN B 904     1555   1555  1.41
LINK        ZN    ZN A 601                 NE2 HIS A  94     1555   1555  2.26
LINK        ZN    ZN A 601                 NE2 HIS A  96     1555   1555  2.19
LINK        ZN    ZN A 601                 ND1 HIS A 119     1555   1555  2.29
LINK        ZN    ZN B 601                 NE2 HIS B  94     1555   1555  2.32
LINK        ZN    ZN B 601                 NE2 HIS B  96     1555   1555  2.03
LINK        ZN    ZN B 601                 ND1 HIS B 119     1555   1555  2.36
LINK        ZN    ZN A 601                 N1  AZM A 400     1555   1555  2.18
LINK        ZN    ZN B 601                 N1  AZM B 401     1555   1555  2.35
CISPEP   1 SER A   29    PRO A   30          0        -0.13
CISPEP   2 PRO A  201    PRO A  202          0         0.19
CISPEP   3 ASP A  236    PRO A  237          0        -0.07
CISPEP   4 SER B   29    PRO B   30          0         0.13
CISPEP   5 PRO B  201    PRO B  202          0         0.29
CISPEP   6 ASP B  236    PRO B  237          0         0.04
SITE     1 AC1  4 TYR A 194  ASN A 195  PHE A 257  NAG A 802
SITE     1 AC2  1 NAG A 801
SITE     1 AC3  4 GLN B 139  ASN B 195  PHE B 257  NAG B 902
SITE     1 AC4  3 NAG B 901  BMA B 903  HOH B 917
SITE     1 AC5  3 NAG B 902  MAN B 904  HOH B 917
SITE     1 AC6  1 BMA B 903
SITE     1 AC7  4 HIS A  94  HIS A  96  HIS A 119  AZM A 400
SITE     1 AC8  4 HIS B  94  HIS B  96  HIS B 119  AZM B 401
SITE     1 AC9  8 GLN A  92  HIS A  94  HIS A 119  VAL A 121
SITE     2 AC9  8 LEU A 198  THR A 199  THR A 200   ZN A 601
SITE     1 BC1 10 GLN B  92  HIS B  94  HIS B  96  HIS B 119
SITE     2 BC1 10 LEU B 131  LEU B 198  THR B 199  THR B 200
SITE     3 BC1 10 TRP B 209   ZN B 601
CRYST1   59.200   75.800   73.800  90.00  99.20  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      0.016905  0.000000  0.002737        0.00000
SCALE2      0.000000  0.013201  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013725        0.00000
      
PROCHECK
Go to PROCHECK summary
 References