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 4 29-JUL-20 1RJ6 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
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) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.000
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. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020792.
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 <I/SIGMA(I)> 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 <I/SIGMA(I)> 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, C
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, D
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 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 C 1 14
HET NAG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET BMA D 3 11
HET MAN D 4 11
HET ZN A 601 1
HET AZM A 400 13
HET ZN B 601 1
HET AZM B 401 13
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
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 6 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 C 1 1555 1555 1.45
LINK ND2 ASN B 195 C1 NAG D 1 1555 1555 1.46
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.40
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.39
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.39
LINK O6 BMA D 3 C1 MAN D 4 1555 1555 1.41
LINK NE2 HIS A 94 ZN ZN A 601 1555 1555 2.26
LINK NE2 HIS A 96 ZN ZN A 601 1555 1555 2.19
LINK ND1 HIS A 119 ZN ZN A 601 1555 1555 2.29
LINK N1 AZM A 400 ZN ZN A 601 1555 1555 2.18
LINK NE2 HIS B 94 ZN ZN B 601 1555 1555 2.32
LINK NE2 HIS B 96 ZN ZN B 601 1555 1555 2.03
LINK ND1 HIS B 119 ZN ZN B 601 1555 1555 2.36
LINK N1 AZM B 401 ZN ZN B 601 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
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
(ATOM LINES ARE NOT SHOWN.)
END
