HEADER TRANSFERASE 07-MAR-06 2G9Z
TITLE THIAMIN PYROPHOSPHOKINASE FROM CANDIDA ALBICANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIAMINE PYROPHOSPHOKINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.7.6.2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA ALBICANS;
SOURCE 3 ORGANISM_TAXID: 5476;
SOURCE 4 STRAIN: NIH3147;
SOURCE 5 GENE: CA1462;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K12;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: K12;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PSF04, PQE80
KEYWDS THIAMIN-PNP, TPK, THIAMIN PYROPHOSPHOKINASE, STRUCTURAL GENOMICS,
KEYWDS 2 PROFUN, BACTERIAL TARGETS AT IGS-CNRS, FRANCE, BIGS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.ABERGEL,S.SANTINI,V.MONCHOIS,T.ROUSSELLE,J.M.CLAVERIE,BACTERIAL
AUTHOR 2 TARGETS AT IGS-CNRS,FRANCE (BIGS)
REVDAT 8 25-OCT-23 2G9Z 1 COMPND REMARK SEQADV HETNAM
REVDAT 8 2 1 LINK
REVDAT 7 13-JUL-11 2G9Z 1 VERSN
REVDAT 6 09-JUN-09 2G9Z 1 REVDAT
REVDAT 5 24-FEB-09 2G9Z 1 VERSN
REVDAT 4 20-JAN-09 2G9Z 1 JRNL
REVDAT 3 26-FEB-08 2G9Z 1 HETATM
REVDAT 2 08-AUG-06 2G9Z 3 HETATM HET
REVDAT 1 04-APR-06 2G9Z 0
JRNL AUTH S.SANTINI,V.MONCHOIS,N.MOUZ,C.SIGOILLOT,T.ROUSSELLE,
JRNL AUTH 2 J.M.CLAVERIE,C.ABERGEL
JRNL TITL STRUCTURAL CHARACTERIZATION OF CA1462, THE CANDIDA ALBICANS
JRNL TITL 2 THIAMINE PYROPHOSPHOKINASE.
JRNL REF BMC STRUCT.BIOL. V. 8 33 2008
JRNL REFN ESSN 1472-6807
JRNL PMID 18652651
JRNL DOI 10.1186/1472-6807-8-33
REMARK 2
REMARK 2 RESOLUTION. 1.96 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 3 NUMBER OF REFLECTIONS : 40488
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 + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4073
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) : 1.96
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.03
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.1870
REMARK 3 BIN FREE R VALUE SET COUNT : 4073
REMARK 3 BIN FREE R VALUE : 0.2360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4775
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 520
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.28000
REMARK 3 B22 (A**2) : 0.07000
REMARK 3 B33 (A**2) : 2.23000
REMARK 3 B12 (A**2) : -3.48000
REMARK 3 B13 (A**2) : 1.20000
REMARK 3 B23 (A**2) : -0.20000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: MAXIMUM LIKELIHOOD TARGET USING
REMARK 3 AMPLITUDES
REMARK 4
REMARK 4 2G9Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000036874.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95372
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40488
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
REMARK 200 RESOLUTION RANGE LOW (A) : 29.440
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.03500
REMARK 200 R SYM (I) : 0.03500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 60.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.00
REMARK 200 R MERGE FOR SHELL (I) : 0.19500
REMARK 200 R SYM FOR SHELL (I) : 0.19500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
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: 1IG0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17.5% PEG4000, 0.2M MAGNESIUM
REMARK 280 CHLORIDE, 0.1M TRIS, 10% GLYCEROL, PROTEIN INCUBATED WITH
REMARK 280 THIAMIN AND AMP-PNP, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -114.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 MET A -12
REMARK 465 ALA A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 GLY A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 GLN A 0
REMARK 465 LEU A 1
REMARK 465 SER A 2
REMARK 465 GLU A 3
REMARK 465 ASP A 4
REMARK 465 SER A 24
REMARK 465 ASP A 25
REMARK 465 SER A 26
REMARK 465 SER A 27
REMARK 465 SER A 28
REMARK 465 SER A 29
REMARK 465 GLU A 41
REMARK 465 SER A 42
REMARK 465 THR A 43
REMARK 465 ALA A 44
REMARK 465 THR A 45
REMARK 465 THR A 46
REMARK 465 GLN A 47
REMARK 465 THR A 48
REMARK 465 ASN A 49
REMARK 465 ASP A 90
REMARK 465 ASN A 91
REMARK 465 ASN A 92
REMARK 465 HIS A 93
REMARK 465 HIS A 94
REMARK 465 HIS A 95
REMARK 465 HIS A 96
REMARK 465 HIS A 97
REMARK 465 GLU A 98
REMARK 465 ASN A 99
REMARK 465 GLN A 327
REMARK 465 LEU A 328
REMARK 465 ASP A 329
REMARK 465 GLY A 330
REMARK 465 ASP A 331
REMARK 465 LEU A 332
REMARK 465 GLU A 333
REMARK 465 ALA A 334
REMARK 465 ALA A 335
REMARK 465 MET B -12
REMARK 465 ALA B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 GLY B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 GLN B 0
REMARK 465 LEU B 1
REMARK 465 SER B 2
REMARK 465 GLU B 3
REMARK 465 ASP B 4
REMARK 465 SER B 5
REMARK 465 SER B 24
REMARK 465 ASP B 25
REMARK 465 SER B 26
REMARK 465 SER B 27
REMARK 465 SER B 28
REMARK 465 SER B 29
REMARK 465 GLU B 41
REMARK 465 SER B 42
REMARK 465 THR B 43
REMARK 465 ALA B 44
REMARK 465 THR B 45
REMARK 465 THR B 46
REMARK 465 GLN B 47
REMARK 465 THR B 48
REMARK 465 ASN B 49
REMARK 465 ASP B 90
REMARK 465 ASN B 91
REMARK 465 ASN B 92
REMARK 465 HIS B 93
REMARK 465 HIS B 94
REMARK 465 HIS B 95
REMARK 465 HIS B 96
REMARK 465 HIS B 97
REMARK 465 GLU B 98
REMARK 465 ASN B 99
REMARK 465 VAL B 326
REMARK 465 GLN B 327
REMARK 465 LEU B 328
REMARK 465 ASP B 329
REMARK 465 GLY B 330
REMARK 465 ASP B 331
REMARK 465 LEU B 332
REMARK 465 GLU B 333
REMARK 465 ALA B 334
REMARK 465 ALA B 335
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASN A 257 CB CG OD1 ND2
REMARK 470 ASN B 257 CB CG OD1 ND2
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 ASP A 78 -111.19 42.65
REMARK 500 ASP A 171 40.83 -142.24
REMARK 500 LYS A 255 124.87 -39.18
REMARK 500 ASP A 256 124.24 -30.81
REMARK 500 ASN A 257 -132.24 -78.59
REMARK 500 ASP A 325 76.51 -154.95
REMARK 500 ASP B 78 -108.33 40.99
REMARK 500 ASP B 171 39.62 -140.80
REMARK 500 ASP B 189 71.25 -112.76
REMARK 500 ASP B 256 125.61 -32.73
REMARK 500 ASN B 257 -128.34 -92.36
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 MG A 702 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 78 OD2
REMARK 620 2 ASP A 113 OD1 93.7
REMARK 620 3 ASP A 115 OD1 81.4 83.8
REMARK 620 4 ASP A 142 OD2 100.4 105.8 170.0
REMARK 620 5 VNP A 602 O1B 171.4 92.8 93.7 83.2
REMARK 620 6 HOH A 906 O 95.7 165.2 86.3 83.7 76.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 704 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 113 OD2
REMARK 620 2 ASP A 115 OD2 94.4
REMARK 620 3 VNP A 602 O2G 155.3 106.6
REMARK 620 4 VNP A 602 O1B 97.5 116.7 84.7
REMARK 620 5 PO4 A 707 O1 77.4 97.4 86.9 145.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 701 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 78 OD2
REMARK 620 2 ASP B 113 OD1 90.6
REMARK 620 3 ASP B 115 OD1 78.0 84.0
REMARK 620 4 ASP B 142 OD2 99.5 103.2 172.5
REMARK 620 5 VNP B 601 O1B 170.8 93.7 94.4 87.4
REMARK 620 6 HOH B 874 O 98.3 163.7 84.5 88.9 75.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 703 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 113 OD2
REMARK 620 2 ASP B 115 OD2 97.6
REMARK 620 3 VNP B 601 O1B 94.3 103.6
REMARK 620 4 VNP B 601 O2G 165.3 97.1 82.1
REMARK 620 5 PO4 B 708 O3 82.9 106.7 149.6 93.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VNP A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VNP B 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IG0 RELATED DB: PDB
REMARK 900 SACCHAROMYCES CEREVISIAE ORTHOLOGUE TPK
REMARK 900 RELATED ID: PF-CAL:CA1462 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 IDENTICAL TO THE SEQUENCE FROM CANDIDA ALBICANS SC5314
DBREF 2G9Z A 2 326 UNP Q59N99 Q59N99_CANAL 5 329
DBREF 2G9Z B 2 326 UNP Q59N99 Q59N99_CANAL 5 329
SEQADV 2G9Z MET A -12 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z ALA A -11 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z HIS A -10 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z HIS A -9 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z HIS A -8 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z HIS A -7 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z HIS A -6 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z HIS A -5 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z GLY A -4 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z HIS A -3 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z HIS A -2 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z HIS A -1 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z GLN A 0 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z LEU A 1 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z GLN A 327 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z LEU A 328 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z ASP A 329 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z GLY A 330 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z ASP A 331 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z LEU A 332 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z GLU A 333 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z ALA A 334 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z ALA A 335 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z MET B -12 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z ALA B -11 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z HIS B -10 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z HIS B -9 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z HIS B -8 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z HIS B -7 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z HIS B -6 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z HIS B -5 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z GLY B -4 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z HIS B -3 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z HIS B -2 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z HIS B -1 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z GLN B 0 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z LEU B 1 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z GLN B 327 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z LEU B 328 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z ASP B 329 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z GLY B 330 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z ASP B 331 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z LEU B 332 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z GLU B 333 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z ALA B 334 UNP Q59N99 EXPRESSION TAG
SEQADV 2G9Z ALA B 335 UNP Q59N99 EXPRESSION TAG
SEQRES 1 A 348 MET ALA HIS HIS HIS HIS HIS HIS GLY HIS HIS HIS GLN
SEQRES 2 A 348 LEU SER GLU ASP SER GLU LEU ILE GLU GLN VAL ILE GLU
SEQRES 3 A 348 GLN PRO ASP SER LEU ILE ILE SER PRO PRO SER ASP SER
SEQRES 4 A 348 SER SER SER SER TYR ASN HIS ILE GLN PRO PHE VAL TYR
SEQRES 5 A 348 LEU GLU SER THR ALA THR THR GLN THR ASN HIS ASN VAL
SEQRES 6 A 348 LEU LEU ILE LEU ASN GLN LYS ILE THR ILE ASP LEU ILE
SEQRES 7 A 348 SER LEU TRP LYS LYS CYS GLU ILE ILE VAL CYS ALA ASP
SEQRES 8 A 348 GLY GLY ALA ASN SER LEU TYR GLU TYR PHE ASN ASP ASN
SEQRES 9 A 348 ASN HIS HIS HIS HIS HIS GLU ASN LEU GLN ARG SER ASP
SEQRES 10 A 348 TYR ILE PRO ASP TYR ILE VAL GLY ASP PHE ASP SER ILE
SEQRES 11 A 348 SER PRO ASP VAL LYS THR TYR TYR GLU SER HIS GLY SER
SEQRES 12 A 348 LYS ILE ILE ARG GLN SER SER GLN TYR TYR ASN ASP PHE
SEQRES 13 A 348 THR LYS SER ILE HIS CYS ILE GLN LEU HIS TYR GLN LEU
SEQRES 14 A 348 ASN HIS THR LYS GLU ASN TRP PHE GLU SER ILE ASP GLU
SEQRES 15 A 348 VAL ASP GLY LEU ALA LYS LEU TRP ASN GLY LEU ASN ASN
SEQRES 16 A 348 SER SER ASP VAL VAL VAL ASP ILE ASP ILE THR ILE TYR
SEQRES 17 A 348 VAL LEU ASN ALA ILE GLY GLY ARG PHE ASP GLN THR VAL
SEQRES 18 A 348 GLN SER ILE ASN GLN LEU TYR ILE MET ASN GLU ASP TYR
SEQRES 19 A 348 PRO LYS VAL THR VAL PHE PHE ILE THR THR ASN ASP ILE
SEQRES 20 A 348 ILE PHE LEU LEU LYS LYS GLY VAL ASN TYR ILE SER TYR
SEQRES 21 A 348 LYS ASN ARG LEU MET PHE HIS LYS ASP ASN GLY SER SER
SEQRES 22 A 348 PRO THR PRO THR CYS GLY LEU LEU PRO LEU SER ASN LYS
SEQRES 23 A 348 THR PRO ILE ILE LEU ASN SER TYR GLY LEU LYS TYR ASP
SEQRES 24 A 348 MET ARG ASN TRP LYS THR GLU MET LEU GLY GLN VAL SER
SEQRES 25 A 348 SER SER ASN ARG ILE SER GLY GLU THR GLY PHE ILE VAL
SEQRES 26 A 348 GLU CYS SER ASP ASP ILE VAL MET ASN ILE GLU ILE ASP
SEQRES 27 A 348 VAL GLN LEU ASP GLY ASP LEU GLU ALA ALA
SEQRES 1 B 348 MET ALA HIS HIS HIS HIS HIS HIS GLY HIS HIS HIS GLN
SEQRES 2 B 348 LEU SER GLU ASP SER GLU LEU ILE GLU GLN VAL ILE GLU
SEQRES 3 B 348 GLN PRO ASP SER LEU ILE ILE SER PRO PRO SER ASP SER
SEQRES 4 B 348 SER SER SER SER TYR ASN HIS ILE GLN PRO PHE VAL TYR
SEQRES 5 B 348 LEU GLU SER THR ALA THR THR GLN THR ASN HIS ASN VAL
SEQRES 6 B 348 LEU LEU ILE LEU ASN GLN LYS ILE THR ILE ASP LEU ILE
SEQRES 7 B 348 SER LEU TRP LYS LYS CYS GLU ILE ILE VAL CYS ALA ASP
SEQRES 8 B 348 GLY GLY ALA ASN SER LEU TYR GLU TYR PHE ASN ASP ASN
SEQRES 9 B 348 ASN HIS HIS HIS HIS HIS GLU ASN LEU GLN ARG SER ASP
SEQRES 10 B 348 TYR ILE PRO ASP TYR ILE VAL GLY ASP PHE ASP SER ILE
SEQRES 11 B 348 SER PRO ASP VAL LYS THR TYR TYR GLU SER HIS GLY SER
SEQRES 12 B 348 LYS ILE ILE ARG GLN SER SER GLN TYR TYR ASN ASP PHE
SEQRES 13 B 348 THR LYS SER ILE HIS CYS ILE GLN LEU HIS TYR GLN LEU
SEQRES 14 B 348 ASN HIS THR LYS GLU ASN TRP PHE GLU SER ILE ASP GLU
SEQRES 15 B 348 VAL ASP GLY LEU ALA LYS LEU TRP ASN GLY LEU ASN ASN
SEQRES 16 B 348 SER SER ASP VAL VAL VAL ASP ILE ASP ILE THR ILE TYR
SEQRES 17 B 348 VAL LEU ASN ALA ILE GLY GLY ARG PHE ASP GLN THR VAL
SEQRES 18 B 348 GLN SER ILE ASN GLN LEU TYR ILE MET ASN GLU ASP TYR
SEQRES 19 B 348 PRO LYS VAL THR VAL PHE PHE ILE THR THR ASN ASP ILE
SEQRES 20 B 348 ILE PHE LEU LEU LYS LYS GLY VAL ASN TYR ILE SER TYR
SEQRES 21 B 348 LYS ASN ARG LEU MET PHE HIS LYS ASP ASN GLY SER SER
SEQRES 22 B 348 PRO THR PRO THR CYS GLY LEU LEU PRO LEU SER ASN LYS
SEQRES 23 B 348 THR PRO ILE ILE LEU ASN SER TYR GLY LEU LYS TYR ASP
SEQRES 24 B 348 MET ARG ASN TRP LYS THR GLU MET LEU GLY GLN VAL SER
SEQRES 25 B 348 SER SER ASN ARG ILE SER GLY GLU THR GLY PHE ILE VAL
SEQRES 26 B 348 GLU CYS SER ASP ASP ILE VAL MET ASN ILE GLU ILE ASP
SEQRES 27 B 348 VAL GLN LEU ASP GLY ASP LEU GLU ALA ALA
HET MG A 702 1
HET MG A 704 1
HET MG A 801 1
HET CL A 705 1
HET PO4 A 707 5
HET VNP A 602 26
HET MG B 701 1
HET MG B 703 1
HET MG B 802 1
HET CL B 706 1
HET PO4 B 708 5
HET VNP B 601 26
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM PO4 PHOSPHATE ION
HETNAM VNP 3-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-5-(2-
HETNAM 2 VNP {[HYDROXY(PHOSPHONOAMINO)PHOSPHORYL]OXY}ETHYL)-4-
HETNAM 3 VNP METHYL-1,3-THIAZOL-3-I UM
HETSYN VNP THIAMIN-PNP; [2-[3-[(4-AMINO-2-METHYL-PYRIMIDIN-5-YL)
HETSYN 2 VNP METHYL]-4-METHYL-1-THIA-3-AZON IACYCLOPENTA-2,4-DIEN-
HETSYN 3 VNP 5-YL]ETHOXY-HYDROXY-PHOSPHORYL]AMINOPHOSPHONIC ACID
FORMUL 3 MG 6(MG 2+)
FORMUL 6 CL 2(CL 1-)
FORMUL 7 PO4 2(O4 P 3-)
FORMUL 8 VNP 2(C12 H20 N5 O6 P2 S 1+)
FORMUL 15 HOH *520(H2 O)
HELIX 1 1 ASP A 63 LYS A 69 1 7
HELIX 2 2 GLY A 79 PHE A 88 1 10
HELIX 3 3 GLN A 101 TYR A 105 5 5
HELIX 4 4 SER A 118 SER A 127 1 10
HELIX 5 5 ASN A 141 ASN A 157 1 17
HELIX 6 6 ASP A 171 SER A 183 1 13
HELIX 7 7 ARG A 203 TYR A 221 1 19
HELIX 8 8 ASN A 249 PHE A 253 5 5
HELIX 9 9 ASP B 63 LYS B 69 1 7
HELIX 10 10 GLY B 79 PHE B 88 1 10
HELIX 11 11 GLN B 101 TYR B 105 5 5
HELIX 12 12 SER B 118 SER B 127 1 10
HELIX 13 13 ASN B 141 ASN B 157 1 17
HELIX 14 14 ASP B 171 SER B 183 1 13
HELIX 15 15 ARG B 203 TYR B 221 1 19
HELIX 16 16 ASN B 249 PHE B 253 5 5
SHEET 1 A 2 GLN A 10 GLU A 13 0
SHEET 2 A 2 TYR A 285 ARG A 288 -1 O ASP A 286 N ILE A 12
SHEET 1 B 5 ASN A 32 ILE A 34 0
SHEET 2 B 5 GLY A 241 SER A 246 1 O VAL A 242 N ASN A 32
SHEET 3 B 5 GLY A 309 CYS A 314 -1 O CYS A 314 N GLY A 241
SHEET 4 B 5 ILE A 276 TYR A 281 -1 N ASN A 279 O GLU A 313
SHEET 5 B 5 TRP A 290 THR A 292 -1 O THR A 292 N ILE A 276
SHEET 1 C10 LYS A 131 ARG A 134 0
SHEET 2 C10 TYR A 109 GLY A 112 1 N ILE A 110 O ILE A 133
SHEET 3 C10 ILE A 73 ALA A 77 1 N CYS A 76 O TYR A 109
SHEET 4 C10 ASN A 51 ILE A 55 1 N LEU A 53 O VAL A 75
SHEET 5 C10 ILE A 192 LEU A 197 1 O TYR A 195 N VAL A 52
SHEET 6 C10 VAL A 224 ILE A 229 1 O THR A 225 N ILE A 192
SHEET 7 C10 ASP A 233 LEU A 238 -1 O ILE A 235 N PHE A 228
SHEET 8 C10 ILE A 318 GLU A 323 -1 O ILE A 318 N LEU A 238
SHEET 9 C10 THR A 264 LEU A 268 -1 N LEU A 268 O VAL A 319
SHEET 10 C10 SER A 299 ARG A 303 -1 O ASN A 302 N CYS A 265
SHEET 1 D 2 GLN B 10 GLU B 13 0
SHEET 2 D 2 TYR B 285 ARG B 288 -1 O ASP B 286 N ILE B 12
SHEET 1 E 5 ASN B 32 ILE B 34 0
SHEET 2 E 5 GLY B 241 SER B 246 1 O TYR B 244 N ASN B 32
SHEET 3 E 5 GLY B 309 CYS B 314 -1 O CYS B 314 N GLY B 241
SHEET 4 E 5 ILE B 276 TYR B 281 -1 N ASN B 279 O GLU B 313
SHEET 5 E 5 TRP B 290 THR B 292 -1 O THR B 292 N ILE B 276
SHEET 1 F10 LYS B 131 ARG B 134 0
SHEET 2 F10 TYR B 109 GLY B 112 1 N ILE B 110 O ILE B 133
SHEET 3 F10 ILE B 73 ALA B 77 1 N CYS B 76 O TYR B 109
SHEET 4 F10 ASN B 51 ILE B 55 1 N LEU B 53 O VAL B 75
SHEET 5 F10 ILE B 192 LEU B 197 1 O TYR B 195 N VAL B 52
SHEET 6 F10 VAL B 224 ILE B 229 1 O THR B 225 N ILE B 192
SHEET 7 F10 ASP B 233 LEU B 238 -1 O ILE B 235 N PHE B 228
SHEET 8 F10 ILE B 318 GLU B 323 -1 O ILE B 318 N LEU B 238
SHEET 9 F10 THR B 264 LEU B 268 -1 N LEU B 268 O VAL B 319
SHEET 10 F10 SER B 299 ARG B 303 -1 O ASN B 302 N CYS B 265
LINK OD2 ASP A 78 MG MG A 702 1555 1555 2.34
LINK OD1 ASP A 113 MG MG A 702 1555 1555 2.25
LINK OD2 ASP A 113 MG MG A 704 1555 1555 2.23
LINK OD1 ASP A 115 MG MG A 702 1555 1555 2.33
LINK OD2 ASP A 115 MG MG A 704 1555 1555 2.15
LINK OD2 ASP A 142 MG MG A 702 1555 1555 2.18
LINK O1B VNP A 602 MG MG A 702 1555 1555 2.24
LINK O2G VNP A 602 MG MG A 704 1555 1555 2.08
LINK O1B VNP A 602 MG MG A 704 1555 1555 2.20
LINK MG MG A 702 O HOH A 906 1555 1555 2.37
LINK MG MG A 704 O1 PO4 A 707 1555 1555 2.25
LINK OD2 ASP B 78 MG MG B 701 1555 1555 2.27
LINK OD1 ASP B 113 MG MG B 701 1555 1555 2.25
LINK OD2 ASP B 113 MG MG B 703 1555 1555 2.17
LINK OD1 ASP B 115 MG MG B 701 1555 1555 2.31
LINK OD2 ASP B 115 MG MG B 703 1555 1555 2.15
LINK OD2 ASP B 142 MG MG B 701 1555 1555 2.18
LINK O1B VNP B 601 MG MG B 701 1555 1555 2.17
LINK O1B VNP B 601 MG MG B 703 1555 1555 2.32
LINK O2G VNP B 601 MG MG B 703 1555 1555 2.06
LINK MG MG B 701 O HOH B 874 1555 1555 2.34
LINK MG MG B 703 O3 PO4 B 708 1555 1555 2.28
CISPEP 1 THR A 274 PRO A 275 0 -0.27
CISPEP 2 THR B 274 PRO B 275 0 -0.34
SITE 1 AC1 7 ASP A 78 ASP A 113 ASP A 115 ASP A 142
SITE 2 AC1 7 VNP A 602 MG A 704 HOH A 906
SITE 1 AC2 5 ASP A 113 ASP A 115 VNP A 602 MG A 702
SITE 2 AC2 5 PO4 A 707
SITE 1 AC3 6 ASP A 113 TYR A 140 ASN A 141 ASP A 142
SITE 2 AC3 6 LYS A 145 VNP A 602
SITE 1 AC4 2 ARG A 250 GLN B 10
SITE 1 AC5 9 ASP A 113 ASP A 115 SER A 137 GLN A 138
SITE 2 AC5 9 VNP A 602 MG A 704 HOH A1055 ARG B 303
SITE 3 AC5 9 HOH B 829
SITE 1 AC6 7 ASP B 78 ASP B 113 ASP B 115 ASP B 142
SITE 2 AC6 7 VNP B 601 MG B 703 HOH B 874
SITE 1 AC7 5 ASP B 113 ASP B 115 VNP B 601 MG B 701
SITE 2 AC7 5 PO4 B 708
SITE 1 AC8 6 ASP B 113 TYR B 140 ASN B 141 ASP B 142
SITE 2 AC8 6 LYS B 145 VNP B 601
SITE 1 AC9 2 GLN A 10 ARG B 250
SITE 1 BC1 7 ARG A 303 ASP B 113 ASP B 115 SER B 137
SITE 2 BC1 7 GLN B 138 VNP B 601 MG B 703
SITE 1 BC2 24 ASP A 113 ASP A 115 GLN A 138 TYR A 139
SITE 2 BC2 24 TYR A 140 ASN A 141 ASP A 142 ARG A 203
SITE 3 BC2 24 MG A 702 MG A 704 PO4 A 707 MG A 801
SITE 4 BC2 24 HOH A 825 HOH A 906 HOH A 960 HOH A1063
SITE 5 BC2 24 TYR B 285 TRP B 290 SER B 299 SER B 300
SITE 6 BC2 24 SER B 301 ASN B 302 ARG B 303 HOH B 828
SITE 1 BC3 22 TYR A 285 TRP A 290 SER A 299 SER A 300
SITE 2 BC3 22 SER A 301 ASN A 302 ARG A 303 ASP B 113
SITE 3 BC3 22 ASP B 115 GLN B 138 TYR B 139 TYR B 140
SITE 4 BC3 22 ASN B 141 ASP B 142 ARG B 203 MG B 701
SITE 5 BC3 22 MG B 703 PO4 B 708 MG B 802 HOH B 848
SITE 6 BC3 22 HOH B 874 HOH B 962
CRYST1 50.825 60.331 63.722 66.14 89.94 65.07 P 1 2
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 0.019675 -0.009146 0.004529 0.00000
SCALE2 0.000000 0.018278 -0.009097 0.00000
SCALE3 0.000000 0.000000 0.017530 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
