HEADER HYDROLASE 18-AUG-10 3OI7
TITLE STRUCTURE OF THE STRUCTURE OF THE H13A MUTANT OF YKR043C IN COMPLEX
TITLE 2 WITH SEDOHEPTULOSE-1,7-BISPHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN YKR043C;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.3.11;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 STRAIN: S288C;
SOURCE 6 GENE: YKR043C;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIPL;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: P15TVLIC
KEYWDS BETA-FURANOSE, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, ALPHA-
KEYWDS 3 BETA, SEDOHEPTULOSE-1, 7-BISPHOSPHATASE, PHOSPHATASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.U.SINGER,X.XU,A.DONG,H.CUI,M.F.CLASQUIN,A.A.CAUDY,A.M.EDWARDS,
AUTHOR 2 A.SAVCHENKO,A.JOACHIMIAK,A.F.YAKUNIN,MIDWEST CENTER FOR STRUCTURAL
AUTHOR 3 GENOMICS (MCSG)
REVDAT 5 06-DEC-23 3OI7 1 REMARK
REVDAT 4 06-SEP-23 3OI7 1 HETSYN
REVDAT 3 29-JUL-20 3OI7 1 REMARK SEQADV LINK SITE
REVDAT 2 24-AUG-11 3OI7 1 JRNL VERSN
REVDAT 1 17-NOV-10 3OI7 0
JRNL AUTH M.F.CLASQUIN,E.MELAMUD,A.SINGER,J.R.GOODING,X.XU,A.DONG,
JRNL AUTH 2 H.CUI,S.R.CAMPAGNA,A.SAVCHENKO,A.F.YAKUNIN,J.D.RABINOWITZ,
JRNL AUTH 3 A.A.CAUDY
JRNL TITL RIBONEOGENESIS IN YEAST.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 145 969 2011
JRNL REFN ISSN 0092-8674
JRNL PMID 21663798
JRNL DOI 10.1016/J.CELL.2011.05.022
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 3 NUMBER OF REFLECTIONS : 46894
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) : 0.230
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 2567
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2861
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 76.16
REMARK 3 BIN R VALUE (WORKING SET) : 0.2690
REMARK 3 BIN FREE R VALUE SET COUNT : 142
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8392
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 135
REMARK 3 SOLVENT ATOMS : 246
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.01000
REMARK 3 B12 (A**2) : 0.02000
REMARK 3 B13 (A**2) : 0.01000
REMARK 3 B23 (A**2) : -0.01000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.503
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.284
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.179
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.448
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.915
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.891
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8763 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11884 ; 1.355 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1048 ; 6.149 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 450 ;36.255 ;23.200
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1488 ;15.964 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 93 ;16.248 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1274 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6721 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3891 ; 0.211 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5917 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 475 ; 0.156 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 7 ; 0.254 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 92 ; 0.227 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.123 ; 0.200
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): 5201 ; 0.740 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8413 ; 1.566 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3700 ; 2.760 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3470 ; 4.735 ; 4.500
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 301 1
REMARK 3 1 B 1 B 301 1
REMARK 3 1 C 1 C 301 1
REMARK 3 1 D 1 D 301 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 2082 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 2082 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 2082 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 2082 ; 0.02 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 2082 ; 0.06 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 2082 ; 0.06 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 2082 ; 0.06 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 2082 ; 0.06 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3OI7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1000061147.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
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 FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : VARIMAX HF
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN A200
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57671
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 82.6
REMARK 200 DATA REDUNDANCY : 1.600
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 36.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.30
REMARK 200 R MERGE FOR SHELL (I) : 0.11200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.020
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB 3F3K MOLECULE A PROTEIN ATOMS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES 7.5, 10%ISO-PROPNAL,
REMARK 280 22%PEG4K, 4%GLYCEROL, 0.03 MG/ML TRYPSIN, SOAKING 10MIN IN WELL
REMARK 280 SOLUTION W/10MM SEDOHEPTULOSE. CRYOPROTECTED IN PARATONE-N OIL,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K, PH 7.5
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, 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
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 MSE A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 ARG A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 GLY A 0
REMARK 465 MSE A 1
REMARK 465 PRO A 2
REMARK 465 SER A 3
REMARK 465 GLU A 264
REMARK 465 GLU A 265
REMARK 465 SER A 266
REMARK 465 GLN A 267
REMARK 465 HIS A 268
REMARK 465 GLY A 269
REMARK 465 ASP A 270
REMARK 465 VAL A 271
REMARK 465 MSE B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 ARG B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
REMARK 465 GLY B 0
REMARK 465 MSE B 1
REMARK 465 PRO B 2
REMARK 465 SER B 3
REMARK 465 GLU B 264
REMARK 465 GLU B 265
REMARK 465 SER B 266
REMARK 465 GLN B 267
REMARK 465 HIS B 268
REMARK 465 GLY B 269
REMARK 465 ASP B 270
REMARK 465 VAL B 271
REMARK 465 MSE C -20
REMARK 465 GLY C -19
REMARK 465 SER C -18
REMARK 465 SER C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 SER C -10
REMARK 465 SER C -9
REMARK 465 GLY C -8
REMARK 465 ARG C -7
REMARK 465 GLU C -6
REMARK 465 ASN C -5
REMARK 465 LEU C -4
REMARK 465 TYR C -3
REMARK 465 PHE C -2
REMARK 465 GLN C -1
REMARK 465 GLY C 0
REMARK 465 MSE C 1
REMARK 465 PRO C 2
REMARK 465 SER C 3
REMARK 465 GLU C 264
REMARK 465 GLU C 265
REMARK 465 SER C 266
REMARK 465 GLN C 267
REMARK 465 HIS C 268
REMARK 465 GLY C 269
REMARK 465 ASP C 270
REMARK 465 VAL C 271
REMARK 465 MSE D -20
REMARK 465 GLY D -19
REMARK 465 SER D -18
REMARK 465 SER D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 SER D -10
REMARK 465 SER D -9
REMARK 465 GLY D -8
REMARK 465 ARG D -7
REMARK 465 GLU D -6
REMARK 465 ASN D -5
REMARK 465 LEU D -4
REMARK 465 TYR D -3
REMARK 465 PHE D -2
REMARK 465 GLN D -1
REMARK 465 GLY D 0
REMARK 465 MSE D 1
REMARK 465 PRO D 2
REMARK 465 SER D 3
REMARK 465 GLU D 264
REMARK 465 GLU D 265
REMARK 465 SER D 266
REMARK 465 GLN D 267
REMARK 465 HIS D 268
REMARK 465 GLY D 269
REMARK 465 ASP D 270
REMARK 465 VAL D 271
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD2 ASP D 123 O HOH D 305 2.17
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 ARG A 49 -81.58 -102.12
REMARK 500 ALA A 175 -130.06 -150.49
REMARK 500 CYS A 229 53.53 70.70
REMARK 500 SER A 241 -142.22 -147.69
REMARK 500 ARG B 49 -82.98 -104.47
REMARK 500 ASN B 137 13.49 58.12
REMARK 500 ALA B 175 -131.55 -152.58
REMARK 500 LYS B 206 62.90 60.06
REMARK 500 ALA B 234 125.80 -39.71
REMARK 500 SER B 241 -145.52 -146.16
REMARK 500 ARG C 49 -82.41 -102.87
REMARK 500 ASN C 137 12.45 59.28
REMARK 500 ALA C 175 -129.65 -151.07
REMARK 500 LYS C 206 62.20 60.27
REMARK 500 CYS C 229 54.06 70.63
REMARK 500 ALA C 234 125.44 -38.57
REMARK 500 SER C 241 -144.68 -144.18
REMARK 500 ARG D 49 -83.13 -103.27
REMARK 500 ALA D 175 -131.71 -152.68
REMARK 500 CYS D 229 52.27 72.12
REMARK 500 SER D 241 -143.49 -147.23
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 311 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 16 OG1
REMARK 620 2 OI7 A 301 O1P 118.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 272 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 154 O
REMARK 620 2 PRO A 214 O 125.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 272 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 14 O
REMARK 620 2 OI7 B 301 O1P 137.9
REMARK 620 3 OI7 B 301 O2P 137.5 50.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 272 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 14 O
REMARK 620 2 OI7 C 301 O1P 137.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 311 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 16 OG1
REMARK 620 2 OI7 C 301 O1P 116.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 272 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY D 14 O
REMARK 620 2 OI7 D 301 O1P 138.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 311 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 16 OG1
REMARK 620 2 OI7 D 301 O1P 118.1
REMARK 620 N 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3F3K RELATED DB: PDB
REMARK 900 THE STRUCTURE OF UNCHARACTERIZED PROTEIN YKR043C FROM SACCHAROMYCES
REMARK 900 CEREVISIAE
REMARK 900 RELATED ID: 3LG2 RELATED DB: PDB
REMARK 900 A YKR043C/ FRUCTOSE-1,6-BISPHOSPHATE PRODUCT COMPLEX FOLLOWING
REMARK 900 LIGAND SOAKING
REMARK 900 RELATED ID: 3LL4 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE H13A MUTANT OF YKR043C IN COMPLEX WITH FRUCTOSE-1,
REMARK 900 6-BISPHOSPHATE
REMARK 900 RELATED ID: APC7730 RELATED DB: TARGETDB
DBREF 3OI7 A 1 271 UNP P36136 YK23_YEAST 1 271
DBREF 3OI7 B 1 271 UNP P36136 YK23_YEAST 1 271
DBREF 3OI7 C 1 271 UNP P36136 YK23_YEAST 1 271
DBREF 3OI7 D 1 271 UNP P36136 YK23_YEAST 1 271
SEQADV 3OI7 MSE A -20 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLY A -19 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 SER A -18 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 SER A -17 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS A -16 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS A -15 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS A -14 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS A -13 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS A -12 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS A -11 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 SER A -10 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 SER A -9 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLY A -8 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 ARG A -7 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLU A -6 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 ASN A -5 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 LEU A -4 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 TYR A -3 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 PHE A -2 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLN A -1 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLY A 0 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 ALA A 13 UNP P36136 HIS 13 ENGINEERED MUTATION
SEQADV 3OI7 MSE B -20 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLY B -19 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 SER B -18 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 SER B -17 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS B -16 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS B -15 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS B -14 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS B -13 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS B -12 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS B -11 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 SER B -10 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 SER B -9 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLY B -8 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 ARG B -7 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLU B -6 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 ASN B -5 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 LEU B -4 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 TYR B -3 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 PHE B -2 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLN B -1 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLY B 0 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 ALA B 13 UNP P36136 HIS 13 ENGINEERED MUTATION
SEQADV 3OI7 MSE C -20 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLY C -19 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 SER C -18 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 SER C -17 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS C -16 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS C -15 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS C -14 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS C -13 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS C -12 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS C -11 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 SER C -10 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 SER C -9 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLY C -8 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 ARG C -7 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLU C -6 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 ASN C -5 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 LEU C -4 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 TYR C -3 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 PHE C -2 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLN C -1 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLY C 0 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 ALA C 13 UNP P36136 HIS 13 ENGINEERED MUTATION
SEQADV 3OI7 MSE D -20 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLY D -19 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 SER D -18 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 SER D -17 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS D -16 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS D -15 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS D -14 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS D -13 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS D -12 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 HIS D -11 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 SER D -10 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 SER D -9 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLY D -8 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 ARG D -7 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLU D -6 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 ASN D -5 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 LEU D -4 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 TYR D -3 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 PHE D -2 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLN D -1 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 GLY D 0 UNP P36136 EXPRESSION TAG
SEQADV 3OI7 ALA D 13 UNP P36136 HIS 13 ENGINEERED MUTATION
SEQRES 1 A 292 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 292 ARG GLU ASN LEU TYR PHE GLN GLY MSE PRO SER LEU THR
SEQRES 3 A 292 PRO ARG CYS ILE ILE VAL ARG ALA GLY GLN THR GLU TRP
SEQRES 4 A 292 SER LYS SER GLY GLN TYR THR GLY LEU THR ASP LEU PRO
SEQRES 5 A 292 LEU THR PRO TYR GLY GLU GLY GLN MSE LEU ARG THR GLY
SEQRES 6 A 292 GLU SER VAL PHE ARG ASN ASN GLN PHE LEU ASN PRO ASP
SEQRES 7 A 292 ASN ILE THR TYR ILE PHE THR SER PRO ARG LEU ARG ALA
SEQRES 8 A 292 ARG GLN THR VAL ASP LEU VAL LEU LYS PRO LEU SER ASP
SEQRES 9 A 292 GLU GLN ARG ALA LYS ILE ARG VAL VAL VAL ASP ASP ASP
SEQRES 10 A 292 LEU ARG GLU TRP GLU TYR GLY ASP TYR GLU GLY MSE LEU
SEQRES 11 A 292 THR ARG GLU ILE ILE GLU LEU ARG LYS SER ARG GLY LEU
SEQRES 12 A 292 ASP LYS GLU ARG PRO TRP ASN ILE TRP ARG ASP GLY CYS
SEQRES 13 A 292 GLU ASN GLY GLU THR THR GLN GLN ILE GLY LEU ARG LEU
SEQRES 14 A 292 SER ARG ALA ILE ALA ARG ILE GLN ASN LEU HIS ARG LYS
SEQRES 15 A 292 HIS GLN SER GLU GLY ARG ALA SER ASP ILE MSE VAL PHE
SEQRES 16 A 292 ALA HIS GLY HIS ALA LEU ARG TYR PHE ALA ALA ILE TRP
SEQRES 17 A 292 PHE GLY LEU GLY VAL GLN LYS LYS CYS GLU THR ILE GLU
SEQRES 18 A 292 GLU ILE GLN ASN VAL LYS SER TYR ASP ASP ASP THR VAL
SEQRES 19 A 292 PRO TYR VAL LYS LEU GLU SER TYR ARG HIS LEU VAL ASP
SEQRES 20 A 292 ASN PRO CYS PHE LEU LEU ASP ALA GLY GLY ILE GLY VAL
SEQRES 21 A 292 LEU SER TYR ALA HIS HIS ASN ILE ASP GLU PRO ALA LEU
SEQRES 22 A 292 GLU LEU ALA GLY PRO PHE VAL SER PRO PRO GLU GLU GLU
SEQRES 23 A 292 SER GLN HIS GLY ASP VAL
SEQRES 1 B 292 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 292 ARG GLU ASN LEU TYR PHE GLN GLY MSE PRO SER LEU THR
SEQRES 3 B 292 PRO ARG CYS ILE ILE VAL ARG ALA GLY GLN THR GLU TRP
SEQRES 4 B 292 SER LYS SER GLY GLN TYR THR GLY LEU THR ASP LEU PRO
SEQRES 5 B 292 LEU THR PRO TYR GLY GLU GLY GLN MSE LEU ARG THR GLY
SEQRES 6 B 292 GLU SER VAL PHE ARG ASN ASN GLN PHE LEU ASN PRO ASP
SEQRES 7 B 292 ASN ILE THR TYR ILE PHE THR SER PRO ARG LEU ARG ALA
SEQRES 8 B 292 ARG GLN THR VAL ASP LEU VAL LEU LYS PRO LEU SER ASP
SEQRES 9 B 292 GLU GLN ARG ALA LYS ILE ARG VAL VAL VAL ASP ASP ASP
SEQRES 10 B 292 LEU ARG GLU TRP GLU TYR GLY ASP TYR GLU GLY MSE LEU
SEQRES 11 B 292 THR ARG GLU ILE ILE GLU LEU ARG LYS SER ARG GLY LEU
SEQRES 12 B 292 ASP LYS GLU ARG PRO TRP ASN ILE TRP ARG ASP GLY CYS
SEQRES 13 B 292 GLU ASN GLY GLU THR THR GLN GLN ILE GLY LEU ARG LEU
SEQRES 14 B 292 SER ARG ALA ILE ALA ARG ILE GLN ASN LEU HIS ARG LYS
SEQRES 15 B 292 HIS GLN SER GLU GLY ARG ALA SER ASP ILE MSE VAL PHE
SEQRES 16 B 292 ALA HIS GLY HIS ALA LEU ARG TYR PHE ALA ALA ILE TRP
SEQRES 17 B 292 PHE GLY LEU GLY VAL GLN LYS LYS CYS GLU THR ILE GLU
SEQRES 18 B 292 GLU ILE GLN ASN VAL LYS SER TYR ASP ASP ASP THR VAL
SEQRES 19 B 292 PRO TYR VAL LYS LEU GLU SER TYR ARG HIS LEU VAL ASP
SEQRES 20 B 292 ASN PRO CYS PHE LEU LEU ASP ALA GLY GLY ILE GLY VAL
SEQRES 21 B 292 LEU SER TYR ALA HIS HIS ASN ILE ASP GLU PRO ALA LEU
SEQRES 22 B 292 GLU LEU ALA GLY PRO PHE VAL SER PRO PRO GLU GLU GLU
SEQRES 23 B 292 SER GLN HIS GLY ASP VAL
SEQRES 1 C 292 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 292 ARG GLU ASN LEU TYR PHE GLN GLY MSE PRO SER LEU THR
SEQRES 3 C 292 PRO ARG CYS ILE ILE VAL ARG ALA GLY GLN THR GLU TRP
SEQRES 4 C 292 SER LYS SER GLY GLN TYR THR GLY LEU THR ASP LEU PRO
SEQRES 5 C 292 LEU THR PRO TYR GLY GLU GLY GLN MSE LEU ARG THR GLY
SEQRES 6 C 292 GLU SER VAL PHE ARG ASN ASN GLN PHE LEU ASN PRO ASP
SEQRES 7 C 292 ASN ILE THR TYR ILE PHE THR SER PRO ARG LEU ARG ALA
SEQRES 8 C 292 ARG GLN THR VAL ASP LEU VAL LEU LYS PRO LEU SER ASP
SEQRES 9 C 292 GLU GLN ARG ALA LYS ILE ARG VAL VAL VAL ASP ASP ASP
SEQRES 10 C 292 LEU ARG GLU TRP GLU TYR GLY ASP TYR GLU GLY MSE LEU
SEQRES 11 C 292 THR ARG GLU ILE ILE GLU LEU ARG LYS SER ARG GLY LEU
SEQRES 12 C 292 ASP LYS GLU ARG PRO TRP ASN ILE TRP ARG ASP GLY CYS
SEQRES 13 C 292 GLU ASN GLY GLU THR THR GLN GLN ILE GLY LEU ARG LEU
SEQRES 14 C 292 SER ARG ALA ILE ALA ARG ILE GLN ASN LEU HIS ARG LYS
SEQRES 15 C 292 HIS GLN SER GLU GLY ARG ALA SER ASP ILE MSE VAL PHE
SEQRES 16 C 292 ALA HIS GLY HIS ALA LEU ARG TYR PHE ALA ALA ILE TRP
SEQRES 17 C 292 PHE GLY LEU GLY VAL GLN LYS LYS CYS GLU THR ILE GLU
SEQRES 18 C 292 GLU ILE GLN ASN VAL LYS SER TYR ASP ASP ASP THR VAL
SEQRES 19 C 292 PRO TYR VAL LYS LEU GLU SER TYR ARG HIS LEU VAL ASP
SEQRES 20 C 292 ASN PRO CYS PHE LEU LEU ASP ALA GLY GLY ILE GLY VAL
SEQRES 21 C 292 LEU SER TYR ALA HIS HIS ASN ILE ASP GLU PRO ALA LEU
SEQRES 22 C 292 GLU LEU ALA GLY PRO PHE VAL SER PRO PRO GLU GLU GLU
SEQRES 23 C 292 SER GLN HIS GLY ASP VAL
SEQRES 1 D 292 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 292 ARG GLU ASN LEU TYR PHE GLN GLY MSE PRO SER LEU THR
SEQRES 3 D 292 PRO ARG CYS ILE ILE VAL ARG ALA GLY GLN THR GLU TRP
SEQRES 4 D 292 SER LYS SER GLY GLN TYR THR GLY LEU THR ASP LEU PRO
SEQRES 5 D 292 LEU THR PRO TYR GLY GLU GLY GLN MSE LEU ARG THR GLY
SEQRES 6 D 292 GLU SER VAL PHE ARG ASN ASN GLN PHE LEU ASN PRO ASP
SEQRES 7 D 292 ASN ILE THR TYR ILE PHE THR SER PRO ARG LEU ARG ALA
SEQRES 8 D 292 ARG GLN THR VAL ASP LEU VAL LEU LYS PRO LEU SER ASP
SEQRES 9 D 292 GLU GLN ARG ALA LYS ILE ARG VAL VAL VAL ASP ASP ASP
SEQRES 10 D 292 LEU ARG GLU TRP GLU TYR GLY ASP TYR GLU GLY MSE LEU
SEQRES 11 D 292 THR ARG GLU ILE ILE GLU LEU ARG LYS SER ARG GLY LEU
SEQRES 12 D 292 ASP LYS GLU ARG PRO TRP ASN ILE TRP ARG ASP GLY CYS
SEQRES 13 D 292 GLU ASN GLY GLU THR THR GLN GLN ILE GLY LEU ARG LEU
SEQRES 14 D 292 SER ARG ALA ILE ALA ARG ILE GLN ASN LEU HIS ARG LYS
SEQRES 15 D 292 HIS GLN SER GLU GLY ARG ALA SER ASP ILE MSE VAL PHE
SEQRES 16 D 292 ALA HIS GLY HIS ALA LEU ARG TYR PHE ALA ALA ILE TRP
SEQRES 17 D 292 PHE GLY LEU GLY VAL GLN LYS LYS CYS GLU THR ILE GLU
SEQRES 18 D 292 GLU ILE GLN ASN VAL LYS SER TYR ASP ASP ASP THR VAL
SEQRES 19 D 292 PRO TYR VAL LYS LEU GLU SER TYR ARG HIS LEU VAL ASP
SEQRES 20 D 292 ASN PRO CYS PHE LEU LEU ASP ALA GLY GLY ILE GLY VAL
SEQRES 21 D 292 LEU SER TYR ALA HIS HIS ASN ILE ASP GLU PRO ALA LEU
SEQRES 22 D 292 GLU LEU ALA GLY PRO PHE VAL SER PRO PRO GLU GLU GLU
SEQRES 23 D 292 SER GLN HIS GLY ASP VAL
MODRES 3OI7 MSE A 40 MET SELENOMETHIONINE
MODRES 3OI7 MSE A 108 MET SELENOMETHIONINE
MODRES 3OI7 MSE A 172 MET SELENOMETHIONINE
MODRES 3OI7 MSE B 40 MET SELENOMETHIONINE
MODRES 3OI7 MSE B 108 MET SELENOMETHIONINE
MODRES 3OI7 MSE B 172 MET SELENOMETHIONINE
MODRES 3OI7 MSE C 40 MET SELENOMETHIONINE
MODRES 3OI7 MSE C 108 MET SELENOMETHIONINE
MODRES 3OI7 MSE C 172 MET SELENOMETHIONINE
MODRES 3OI7 MSE D 40 MET SELENOMETHIONINE
MODRES 3OI7 MSE D 108 MET SELENOMETHIONINE
MODRES 3OI7 MSE D 172 MET SELENOMETHIONINE
HET MSE A 40 8
HET MSE A 108 8
HET MSE A 172 8
HET MSE B 40 8
HET MSE B 108 8
HET MSE B 172 8
HET MSE C 40 8
HET MSE C 108 8
HET MSE C 172 8
HET MSE D 40 8
HET MSE D 108 8
HET MSE D 172 8
HET OI7 A 301 22
HET MG A 311 1
HET NA A 272 1
HET EDO A 273 4
HET EDO A 274 4
HET GOL A 275 6
HET OI7 B 301 22
HET MG B 311 1
HET NA B 272 1
HET EDO B 273 4
HET OI7 C 301 22
HET MG C 311 1
HET NA C 272 1
HET NA C 273 1
HET EDO C 274 4
HET EDO C 275 4
HET OI7 D 301 22
HET MG D 311 1
HET NA D 272 1
HET EDO D 273 4
HET EDO D 274 4
HET EDO D 275 4
HETNAM MSE SELENOMETHIONINE
HETNAM OI7 1,7-DI-O-PHOSPHONO-BETA-D-ALTRO-HEPT-2-ULOFURANOSE
HETNAM MG MAGNESIUM ION
HETNAM NA SODIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETSYN OI7 1,7-DI-O-PHOSPHONO-BETA-D-ALTRO-HEPT-2-ULOSE; 1,7-DI-O-
HETSYN 2 OI7 PHOSPHONO-D-ALTRO-HEPT-2-ULOSE; 1,7-DI-O-PHOSPHONO-
HETSYN 3 OI7 ALTRO-HEPT-2-ULOSE
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 5 OI7 4(C7 H16 O13 P2)
FORMUL 6 MG 4(MG 2+)
FORMUL 7 NA 5(NA 1+)
FORMUL 8 EDO 8(C2 H6 O2)
FORMUL 10 GOL C3 H8 O3
FORMUL 27 HOH *246(H2 O)
HELIX 1 1 THR A 16 GLY A 22 1 7
HELIX 2 2 THR A 33 ARG A 49 1 17
HELIX 3 3 ASN A 55 ASP A 57 5 3
HELIX 4 4 ARG A 67 LEU A 78 1 12
HELIX 5 5 SER A 82 LYS A 88 1 7
HELIX 6 6 ASP A 95 ARG A 98 5 4
HELIX 7 7 TYR A 102 GLU A 106 5 5
HELIX 8 8 LEU A 109 ARG A 120 1 12
HELIX 9 9 ASN A 129 GLY A 134 1 6
HELIX 10 10 THR A 140 GLU A 165 1 26
HELIX 11 11 HIS A 176 PHE A 188 1 13
HELIX 12 12 THR A 198 GLN A 203 1 6
HELIX 13 13 THR B 16 GLY B 22 1 7
HELIX 14 14 THR B 33 ARG B 49 1 17
HELIX 15 15 ASN B 55 ASP B 57 5 3
HELIX 16 16 ARG B 67 LEU B 78 1 12
HELIX 17 17 SER B 82 LYS B 88 1 7
HELIX 18 18 ASP B 95 ARG B 98 5 4
HELIX 19 19 TYR B 102 GLU B 106 5 5
HELIX 20 20 LEU B 109 ARG B 120 1 12
HELIX 21 21 ASN B 129 GLY B 134 1 6
HELIX 22 22 THR B 140 GLU B 165 1 26
HELIX 23 23 HIS B 176 PHE B 188 1 13
HELIX 24 24 THR B 198 GLN B 203 1 6
HELIX 25 25 THR C 16 GLY C 22 1 7
HELIX 26 26 THR C 33 ARG C 49 1 17
HELIX 27 27 ASN C 55 ASP C 57 5 3
HELIX 28 28 ARG C 67 LEU C 78 1 12
HELIX 29 29 SER C 82 LYS C 88 1 7
HELIX 30 30 ASP C 95 ARG C 98 5 4
HELIX 31 31 TYR C 102 GLU C 106 5 5
HELIX 32 32 LEU C 109 ARG C 120 1 12
HELIX 33 33 ASN C 129 GLY C 134 1 6
HELIX 34 34 THR C 140 GLU C 165 1 26
HELIX 35 35 HIS C 176 PHE C 188 1 13
HELIX 36 36 THR C 198 GLN C 203 1 6
HELIX 37 37 THR D 16 GLY D 22 1 7
HELIX 38 38 THR D 33 ARG D 49 1 17
HELIX 39 39 ASN D 55 ASP D 57 5 3
HELIX 40 40 ARG D 67 LEU D 78 1 12
HELIX 41 41 SER D 82 LYS D 88 1 7
HELIX 42 42 ASP D 95 ARG D 98 5 4
HELIX 43 43 TYR D 102 GLU D 106 5 5
HELIX 44 44 LEU D 109 ARG D 120 1 12
HELIX 45 45 ASN D 129 GLY D 134 1 6
HELIX 46 46 THR D 140 GLU D 165 1 26
HELIX 47 47 HIS D 176 PHE D 188 1 13
HELIX 48 48 THR D 198 GLN D 203 1 6
SHEET 1 A 7 ARG A 90 VAL A 93 0
SHEET 2 A 7 ILE A 59 THR A 64 1 N ILE A 62 O ARG A 90
SHEET 3 A 7 ASP A 170 ALA A 175 1 O MSE A 172 N PHE A 63
SHEET 4 A 7 ARG A 7 ARG A 12 1 N VAL A 11 O VAL A 173
SHEET 5 A 7 ILE A 237 TYR A 242 -1 O LEU A 240 N CYS A 8
SHEET 6 A 7 PRO A 250 GLU A 253 -1 O ALA A 251 N SER A 241
SHEET 7 A 7 PHE C 230 LEU C 231 1 O LEU C 231 N LEU A 252
SHEET 1 B 2 VAL A 192 LYS A 195 0
SHEET 2 B 2 SER A 220 HIS A 223 -1 O TYR A 221 N LYS A 194
SHEET 1 C 7 PHE A 230 LEU A 231 0
SHEET 2 C 7 PRO C 250 GLU C 253 1 O LEU C 252 N LEU A 231
SHEET 3 C 7 ILE C 237 TYR C 242 -1 N SER C 241 O ALA C 251
SHEET 4 C 7 ARG C 7 ARG C 12 -1 N CYS C 8 O LEU C 240
SHEET 5 C 7 ASP C 170 ALA C 175 1 O VAL C 173 N VAL C 11
SHEET 6 C 7 ILE C 59 THR C 64 1 N PHE C 63 O MSE C 172
SHEET 7 C 7 ARG C 90 VAL C 93 1 O ARG C 90 N ILE C 62
SHEET 1 D 6 ARG B 90 VAL B 93 0
SHEET 2 D 6 ILE B 59 THR B 64 1 N ILE B 62 O ARG B 90
SHEET 3 D 6 ASP B 170 ALA B 175 1 O MSE B 172 N PHE B 63
SHEET 4 D 6 ARG B 7 ARG B 12 1 N VAL B 11 O VAL B 173
SHEET 5 D 6 ILE B 237 TYR B 242 -1 O LEU B 240 N CYS B 8
SHEET 6 D 6 PRO B 250 LEU B 252 -1 O ALA B 251 N SER B 241
SHEET 1 E 2 VAL B 192 LYS B 195 0
SHEET 2 E 2 SER B 220 HIS B 223 -1 O TYR B 221 N LYS B 194
SHEET 1 F 2 VAL C 192 LYS C 195 0
SHEET 2 F 2 SER C 220 HIS C 223 -1 O HIS C 223 N VAL C 192
SHEET 1 G 6 ARG D 90 VAL D 93 0
SHEET 2 G 6 ILE D 59 THR D 64 1 N ILE D 62 O ARG D 90
SHEET 3 G 6 ASP D 170 ALA D 175 1 O MSE D 172 N PHE D 63
SHEET 4 G 6 ARG D 7 ARG D 12 1 N VAL D 11 O VAL D 173
SHEET 5 G 6 ILE D 237 TYR D 242 -1 O LEU D 240 N CYS D 8
SHEET 6 G 6 PRO D 250 LEU D 252 -1 O ALA D 251 N SER D 241
SHEET 1 H 2 VAL D 192 LYS D 195 0
SHEET 2 H 2 SER D 220 HIS D 223 -1 O TYR D 221 N LYS D 194
LINK C GLN A 39 N MSE A 40 1555 1555 1.33
LINK C MSE A 40 N LEU A 41 1555 1555 1.33
LINK C GLY A 107 N MSE A 108 1555 1555 1.34
LINK C MSE A 108 N LEU A 109 1555 1555 1.34
LINK C ILE A 171 N MSE A 172 1555 1555 1.33
LINK C MSE A 172 N VAL A 173 1555 1555 1.32
LINK C GLN B 39 N MSE B 40 1555 1555 1.33
LINK C MSE B 40 N LEU B 41 1555 1555 1.33
LINK C GLY B 107 N MSE B 108 1555 1555 1.34
LINK C MSE B 108 N LEU B 109 1555 1555 1.33
LINK C ILE B 171 N MSE B 172 1555 1555 1.33
LINK C MSE B 172 N VAL B 173 1555 1555 1.32
LINK C GLN C 39 N MSE C 40 1555 1555 1.33
LINK C MSE C 40 N LEU C 41 1555 1555 1.33
LINK C GLY C 107 N MSE C 108 1555 1555 1.33
LINK C MSE C 108 N LEU C 109 1555 1555 1.33
LINK C ILE C 171 N MSE C 172 1555 1555 1.33
LINK C MSE C 172 N VAL C 173 1555 1555 1.32
LINK C GLN D 39 N MSE D 40 1555 1555 1.33
LINK C MSE D 40 N LEU D 41 1555 1555 1.33
LINK C GLY D 107 N MSE D 108 1555 1555 1.34
LINK C MSE D 108 N LEU D 109 1555 1555 1.33
LINK C ILE D 171 N MSE D 172 1555 1555 1.33
LINK C MSE D 172 N VAL D 173 1555 1555 1.32
LINK OG1 THR A 16 MG MG A 311 1555 1555 2.17
LINK O ARG A 154 NA NA A 272 1555 1555 2.82
LINK O PRO A 214 NA NA A 272 1555 1555 2.89
LINK O1P OI7 A 301 MG MG A 311 1555 1555 2.86
LINK O GLY B 14 NA NA B 272 1555 1555 3.05
LINK OG1 THR B 16 MG MG B 311 1555 1555 2.17
LINK NA NA B 272 O1P OI7 B 301 1555 1555 2.24
LINK NA NA B 272 O2P OI7 B 301 1555 1555 3.19
LINK O GLY C 14 NA NA C 272 1555 1555 3.00
LINK OG1 THR C 16 MG MG C 311 1555 1555 2.17
LINK O PRO C 31 NA NA C 273 1555 1555 2.73
LINK NA NA C 272 O1P OI7 C 301 1555 1555 2.25
LINK O1P OI7 C 301 MG MG C 311 1555 1555 2.91
LINK O GLY D 14 NA NA D 272 1555 1555 2.99
LINK OG1 THR D 16 MG MG D 311 1555 1555 2.16
LINK NA NA D 272 O1P OI7 D 301 1555 1555 2.24
LINK O1P OI7 D 301 MG MG D 311 1555 1555 2.92
CRYST1 58.559 74.945 83.615 90.04 89.92 77.22 P 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 0.017077 -0.003873 -0.000026 0.00000
SCALE2 0.000000 0.013682 0.000013 0.00000
SCALE3 0.000000 0.000000 0.011960 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
