HEADER TRANSFERASE 22-JUN-09 3HYO
TITLE CRYSTAL STRUCTURE OF PYRIDOXAL KINASE FROM LACTOBACILLUS PLANTARUM IN
TITLE 2 COMPLEX WITH ADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRIDOXAL KINASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.7.1.35;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS PLANTARUM;
SOURCE 3 ORGANISM_TAXID: 1590;
SOURCE 4 STRAIN: WCFS1;
SOURCE 5 GENE: PDX, LP_0863;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSGX3(BC)
KEYWDS PYRIDOXAL KINASE, ADP, PSI-II, 11208C, STRUCTURAL GENOMICS, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, NYSGXRC, KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.BAGARIA,D.KUMARAN,S.K.BURLEY,S.SWAMINATHAN,NEW YORK SGX RESEARCH
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 5 22-NOV-23 3HYO 1 REMARK
REVDAT 4 06-SEP-23 3HYO 1 REMARK
REVDAT 3 10-FEB-21 3HYO 1 AUTHOR JRNL REMARK SEQADV
REVDAT 3 2 1 LINK
REVDAT 2 01-NOV-17 3HYO 1 REMARK
REVDAT 1 30-JUN-09 3HYO 0
JRNL AUTH A.BAGARIA,D.KUMARAN,S.K.BURLEY,S.SWAMINATHAN
JRNL TITL CRYSTAL STRUCTURE OF PYRIDOXAL KINASE FROM LACTOBACILLUS
JRNL TITL 2 PLANTARUM IN COMPLEX WITH ADP
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.85 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 24694
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1324
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1765
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2180
REMARK 3 BIN FREE R VALUE SET COUNT : 95
REMARK 3 BIN FREE R VALUE : 0.3050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2045
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 246
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.132
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.129
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.083
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.679
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2112 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2902 ; 1.478 ; 1.981
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 272 ; 5.531 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 86 ;35.989 ;25.233
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 315 ;12.313 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;18.587 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 352 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1585 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 995 ; 0.197 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1460 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 215 ; 0.208 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.103 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 55 ; 0.186 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.131 ; 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): 1395 ; 1.110 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2169 ; 1.600 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 830 ; 2.525 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 733 ; 3.754 ; 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 : 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 : 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 3HYO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUN-09.
REMARK 100 THE DEPOSITION ID IS D_1000053744.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 0.979
REMARK 200 MONOCHROMATOR : SI(111)CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24694
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 24.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 9.000
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.90
REMARK 200 R MERGE FOR SHELL (I) : 0.31300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MR
REMARK 200 STARTING MODEL: PDB ENTRY 3H74
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MGCL2, 0.1M HEPES PH 6.5, 25%
REMARK 280 PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.46200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.46200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 32.29700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.88050
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.29700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.88050
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 66.46200
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.29700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 34.88050
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 66.46200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.29700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 34.88050
REMARK 290 SMTRY3 8 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 -1
REMARK 465 SER A 0
REMARK 465 GLY A 274
REMARK 465 HIS A 275
REMARK 465 HIS A 276
REMARK 465 HIS A 277
REMARK 465 HIS A 278
REMARK 465 HIS A 279
REMARK 465 HIS A 280
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 SER A 17 -134.50 55.90
REMARK 500 GLN A 29 32.07 75.08
REMARK 500 VAL A 81 -65.19 -103.78
REMARK 500 LEU A 108 -29.15 -144.17
REMARK 500 ALA A 182 -118.18 55.27
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 282 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A 281 O2B
REMARK 620 2 HOH A 307 O 88.5
REMARK 620 3 HOH A 318 O 162.8 108.5
REMARK 620 4 HOH A 346 O 89.0 96.7 90.8
REMARK 620 5 HOH A 382 O 94.7 84.2 85.4 176.2
REMARK 620 6 HOH A 522 O 84.0 172.2 78.8 85.7 93.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 282
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-11208C RELATED DB: TARGETDB
DBREF 3HYO A 2 272 UNP Q88YB5 Q88YB5_LACPL 2 272
SEQADV 3HYO MSE A -1 UNP Q88YB5 EXPRESSION TAG
SEQADV 3HYO SER A 0 UNP Q88YB5 EXPRESSION TAG
SEQADV 3HYO LEU A 1 UNP Q88YB5 EXPRESSION TAG
SEQADV 3HYO GLU A 273 UNP Q88YB5 EXPRESSION TAG
SEQADV 3HYO GLY A 274 UNP Q88YB5 EXPRESSION TAG
SEQADV 3HYO HIS A 275 UNP Q88YB5 EXPRESSION TAG
SEQADV 3HYO HIS A 276 UNP Q88YB5 EXPRESSION TAG
SEQADV 3HYO HIS A 277 UNP Q88YB5 EXPRESSION TAG
SEQADV 3HYO HIS A 278 UNP Q88YB5 EXPRESSION TAG
SEQADV 3HYO HIS A 279 UNP Q88YB5 EXPRESSION TAG
SEQADV 3HYO HIS A 280 UNP Q88YB5 EXPRESSION TAG
SEQRES 1 A 282 MSE SER LEU SER THR MSE LEU VAL ALA GLU ASP LEU SER
SEQRES 2 A 282 ALA VAL GLY GLY ILE SER LEU SER SER ALA LEU PRO VAL
SEQRES 3 A 282 LEU THR ALA MSE GLN TYR ASP VAL ALA ALA LEU PRO THR
SEQRES 4 A 282 SER LEU LEU SER THR HIS THR SER GLY TYR GLY THR PRO
SEQRES 5 A 282 ALA VAL VAL ASP LEU SER THR TRP LEU PRO GLN VAL PHE
SEQRES 6 A 282 ALA HIS TRP THR ARG ALA GLN LEU HIS PHE ASP GLN ALA
SEQRES 7 A 282 LEU ILE GLY TYR VAL GLY SER VAL ALA LEU CYS GLN GLN
SEQRES 8 A 282 ILE THR THR TYR LEU GLU GLN GLN THR LEU SER LEU LEU
SEQRES 9 A 282 VAL VAL ASP PRO VAL LEU GLY ASP LEU GLY GLN LEU TYR
SEQRES 10 A 282 GLN GLY PHE ASP GLN ASP TYR VAL ALA ALA MSE ARG GLN
SEQRES 11 A 282 LEU ILE GLN GLN ALA ASP VAL ILE LEU PRO ASN THR THR
SEQRES 12 A 282 GLU ALA ALA LEU LEU THR GLY ALA PRO TYR GLN VAL THR
SEQRES 13 A 282 PRO ASP LEU GLU VAL ILE LEU PRO ALA LEU GLN ALA GLN
SEQRES 14 A 282 LEU LYS THR GLY ALA HIS ALA VAL ILE THR ASP VAL GLN
SEQRES 15 A 282 ARG ALA ASP GLN ILE GLY CYS ALA TRP LEU ASP GLU ALA
SEQRES 16 A 282 GLY HIS VAL GLN TYR CYS GLY ALA ARG ARG LEU PRO GLY
SEQRES 17 A 282 HIS TYR ASN GLY THR GLY ASP THR LEU ALA ALA VAL ILE
SEQRES 18 A 282 ALA GLY LEU LEU GLY ARG GLY TYR PRO LEU ALA PRO THR
SEQRES 19 A 282 LEU ALA ARG ALA ASN GLN TRP LEU ASN MSE ALA VAL ALA
SEQRES 20 A 282 GLU THR ILE ALA GLN ASN ARG THR ASP ASP ARG GLN GLY
SEQRES 21 A 282 VAL ALA LEU GLY ASP LEU LEU GLN ALA ILE LEU ALA LEU
SEQRES 22 A 282 ASN GLU GLY HIS HIS HIS HIS HIS HIS
MODRES 3HYO MSE A 4 MET SELENOMETHIONINE
MODRES 3HYO MSE A 28 MET SELENOMETHIONINE
MODRES 3HYO MSE A 126 MET SELENOMETHIONINE
MODRES 3HYO MSE A 242 MET SELENOMETHIONINE
HET MSE A 4 8
HET MSE A 28 8
HET MSE A 126 8
HET MSE A 242 8
HET ADP A 281 27
HET MG A 282 1
HETNAM MSE SELENOMETHIONINE
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 2 ADP C10 H15 N5 O10 P2
FORMUL 3 MG MG 2+
FORMUL 4 HOH *246(H2 O)
HELIX 1 1 SER A 17 MSE A 28 1 12
HELIX 2 2 TRP A 58 GLN A 70 1 13
HELIX 3 3 SER A 83 GLN A 97 1 15
HELIX 4 4 ASP A 119 GLN A 131 1 13
HELIX 5 5 ASN A 139 GLY A 148 1 10
HELIX 6 6 ASP A 156 ALA A 166 1 11
HELIX 7 7 GLY A 210 GLY A 224 1 15
HELIX 8 8 PRO A 228 GLN A 250 1 23
HELIX 9 9 LEU A 261 GLU A 273 1 13
SHEET 1 A 7 VAL A 52 VAL A 53 0
SHEET 2 A 7 ASP A 31 THR A 42 -1 N LEU A 39 O VAL A 53
SHEET 3 A 7 THR A 3 VAL A 13 1 N VAL A 6 O ALA A 33
SHEET 4 A 7 GLN A 75 ILE A 78 1 O LEU A 77 N LEU A 5
SHEET 5 A 7 LEU A 101 VAL A 104 1 O VAL A 103 N ILE A 78
SHEET 6 A 7 VAL A 135 ILE A 136 1 O VAL A 135 N VAL A 104
SHEET 7 A 7 HIS A 173 ALA A 174 1 O HIS A 173 N ILE A 136
SHEET 1 B 2 GLY A 109 ASP A 110 0
SHEET 2 B 2 GLN A 113 LEU A 114 -1 O GLN A 113 N ASP A 110
SHEET 1 C 3 ILE A 176 ARG A 181 0
SHEET 2 C 3 GLN A 184 LEU A 190 -1 O ALA A 188 N ILE A 176
SHEET 3 C 3 VAL A 196 ARG A 202 -1 O GLN A 197 N TRP A 189
LINK C THR A 3 N MSE A 4 1555 1555 1.33
LINK C MSE A 4 N LEU A 5 1555 1555 1.33
LINK C ALA A 27 N MSE A 28 1555 1555 1.34
LINK C MSE A 28 N GLN A 29 1555 1555 1.33
LINK C ALA A 125 N MSE A 126 1555 1555 1.33
LINK C MSE A 126 N ARG A 127 1555 1555 1.34
LINK C ASN A 241 N MSE A 242 1555 1555 1.33
LINK C MSE A 242 N ALA A 243 1555 1555 1.34
LINK O2B ADP A 281 MG MG A 282 1555 1555 2.07
LINK MG MG A 282 O HOH A 307 1555 1555 2.20
LINK MG MG A 282 O HOH A 318 1555 1555 2.16
LINK MG MG A 282 O HOH A 346 1555 1555 2.16
LINK MG MG A 282 O HOH A 382 1555 1555 2.14
LINK MG MG A 282 O HOH A 522 1555 1555 2.11
SITE 1 AC1 18 THR A 177 ASP A 178 ILE A 185 LEU A 204
SITE 2 AC1 18 GLY A 206 THR A 211 GLY A 212 ASN A 237
SITE 3 AC1 18 LEU A 240 ASN A 241 MG A 282 HOH A 307
SITE 4 AC1 18 HOH A 328 HOH A 339 HOH A 346 HOH A 388
SITE 5 AC1 18 HOH A 491 HOH A 522
SITE 1 AC2 7 ADP A 281 HOH A 307 HOH A 318 HOH A 346
SITE 2 AC2 7 HOH A 382 HOH A 446 HOH A 522
CRYST1 64.594 69.761 132.924 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015481 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014335 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007523 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
