HEADER TRANSFERASE 19-JUN-07 2QCV
TITLE CRYSTAL STRUCTURE OF A PUTATIVE 5-DEHYDRO-2-DEOXYGLUCONOKINASE (IOLC)
TITLE 2 FROM BACILLUS HALODURANS C-125 AT 1.90 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE 5-DEHYDRO-2-DEOXYGLUCONOKINASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS HALODURANS C-125;
SOURCE 3 ORGANISM_TAXID: 272558;
SOURCE 4 STRAIN: C-125, DSM 18197, FERM 7344, JCM 9153;
SOURCE 5 ATCC: BAA-125;
SOURCE 6 GENE: NP_243185.1, IOLC, BH2319;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS PUTATIVE 5-DEHYDRO-2- DEOXYGLUCONOKINASE, STRUCTURAL GENOMICS, JOINT
KEYWDS 2 CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 3 PSI-2, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 8 25-JAN-23 2QCV 1 REMARK SEQADV
REVDAT 7 24-JUL-19 2QCV 1 REMARK LINK
REVDAT 6 25-OCT-17 2QCV 1 REMARK
REVDAT 5 18-OCT-17 2QCV 1 REMARK
REVDAT 4 13-JUL-11 2QCV 1 VERSN
REVDAT 3 28-JUL-10 2QCV 1 TITLE KEYWDS
REVDAT 2 24-FEB-09 2QCV 1 VERSN
REVDAT 1 07-AUG-07 2QCV 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE
JRNL TITL 2 5-DEHYDRO-2-DEOXYGLUCONOKINASE (NP_243185.1) FROM BACILLUS
JRNL TITL 3 HALODURANS AT 1.90 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 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 WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 42439
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2143
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2881
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.67
REMARK 3 BIN R VALUE (WORKING SET) : 0.2110
REMARK 3 BIN FREE R VALUE SET COUNT : 183
REMARK 3 BIN FREE R VALUE : 0.2650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2509
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 221
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.50000
REMARK 3 B22 (A**2) : -0.50000
REMARK 3 B33 (A**2) : 0.75000
REMARK 3 B12 (A**2) : -0.25000
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): 0.107
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.101
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.063
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.168
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2707 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1856 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3664 ; 1.543 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4546 ; 1.037 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 353 ; 5.975 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 114 ;34.727 ;24.035
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 475 ;13.232 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;17.047 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 417 ; 0.184 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3006 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 545 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 500 ; 0.221 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1940 ; 0.197 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1310 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1410 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 187 ; 0.141 ; 0.200
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): 18 ; 0.212 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 52 ; 0.239 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.214 ; 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): 1815 ; 2.210 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 690 ; 0.544 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2719 ; 2.946 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1119 ; 5.640 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 934 ; 7.413 ;11.000
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 331
REMARK 3 ORIGIN FOR THE GROUP (A): 77.1020 22.0710 0.8500
REMARK 3 T TENSOR
REMARK 3 T11: -0.0465 T22: -0.1124
REMARK 3 T33: -0.0515 T12: 0.0241
REMARK 3 T13: -0.0198 T23: 0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 0.4431 L22: 0.6944
REMARK 3 L33: 0.3109 L12: -0.2363
REMARK 3 L13: -0.2112 L23: 0.1637
REMARK 3 S TENSOR
REMARK 3 S11: -0.0435 S12: -0.0184 S13: -0.0330
REMARK 3 S21: -0.0238 S22: 0.0216 S23: 0.1123
REMARK 3 S31: 0.0034 S32: -0.0247 S33: 0.0219
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:
REMARK 3 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
REMARK 3 2. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY.
REMARK 3 3. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE
REMARK 3 INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY
REMARK 3 OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75
REMARK 3 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL
REMARK 3 S-MET INCORPORATION.
REMARK 3 4. PGE WERE MODELED AS FRAGMENTS OF PEG-200 FROM THE
REMARK 3 CRYSTALLIZATION CONDITIONS.
REMARK 3 5. RESIDUES 1 AND 306-310 HAVE POOR DENSITY AND WERE NOT
REMARK 3 MODELED.
REMARK 3 6. THERE ARE NUMEROUS SMALL BLOBS OF DIFFERENCE DENSITY
REMARK 3 THAT WERE NOT MODELED.
REMARK 4
REMARK 4 2QCV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000043438.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUN-07
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 : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97901
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) BENT
REMARK 200 (HORIZONTAL FOCUSING)
REMARK 200 OPTICS : FLAT MIRROR (VERTICAL FOCUSING)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42457
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 29.161
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.40
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : 0.09300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.67100
REMARK 200 R SYM FOR SHELL (I) : 0.67100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NANODROP, 0.2M MGCL2, 50.0% PEG 200,
REMARK 280 0.1M CACODYLATE PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+1/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 16.02767
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 32.05533
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 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 16.02767
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 32.05533
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 16.02767
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 32.05533
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 16.02767
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 32.05533
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300 SIZE EXCLUSION CHROMATOGRAPHY SUPPORTS THE ASSIGNMENT
REMARK 300 OF A TETRAMER AS A SIGNIFICANT OLIGOMERIZATION STATE
REMARK 300 IN SOLUTION.
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 194.00100
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 194.00100
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 358 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 498 LIES ON A SPECIAL POSITION.
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 0
REMARK 465 MSE A 1
REMARK 465 HIS A 306
REMARK 465 SER A 307
REMARK 465 SER A 308
REMARK 465 SER A 309
REMARK 465 ASP A 310
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 LYS A 59 CD CE NZ
REMARK 470 GLU A 110 CG CD OE1 OE2
REMARK 470 GLU A 128 CD OE1 OE2
REMARK 470 ARG A 178 CZ NH1 NH2
REMARK 470 GLU A 207 CD OE1 OE2
REMARK 470 ARG A 226 NE CZ NH1 NH2
REMARK 470 LYS A 263 CG CD CE NZ
REMARK 470 GLU A 323 CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD2 ASP A 8 OH TYR A 255 12554 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 137 NE - CZ - NH1 ANGL. DEV. = 3.2 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 HIS A 231 -151.55 -120.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 332
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 333
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 375195 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE
REMARK 999 LEAVING ONLY A GLYCINE FOLLOWED BY THE TARGET SEQUENCE.
DBREF 2QCV A 1 331 UNP Q9KAG8 Q9KAG8_BACHD 1 331
SEQADV 2QCV GLY A 0 UNP Q9KAG8 EXPRESSION TAG
SEQADV 2QCV MSE A 1 UNP Q9KAG8 MET 1 MODIFIED RESIDUE
SEQADV 2QCV MSE A 32 UNP Q9KAG8 MET 32 MODIFIED RESIDUE
SEQADV 2QCV MSE A 36 UNP Q9KAG8 MET 36 MODIFIED RESIDUE
SEQADV 2QCV MSE A 79 UNP Q9KAG8 MET 79 MODIFIED RESIDUE
SEQADV 2QCV MSE A 115 UNP Q9KAG8 MET 115 MODIFIED RESIDUE
SEQADV 2QCV MSE A 312 UNP Q9KAG8 MET 312 MODIFIED RESIDUE
SEQRES 1 A 332 GLY MSE THR TYR GLU LEU SER THR ASP ARG GLU PHE ASP
SEQRES 2 A 332 LEU ILE ALA ILE GLY ARG ALA CYS ILE ASP LEU ASN ALA
SEQRES 3 A 332 VAL GLU TYR ASN ARG PRO MSE GLU GLU THR MSE THR PHE
SEQRES 4 A 332 SER LYS TYR VAL GLY GLY SER PRO ALA ASN ILE VAL ILE
SEQRES 5 A 332 GLY SER SER LYS LEU GLY LEU LYS ALA GLY PHE ILE GLY
SEQRES 6 A 332 LYS ILE ALA ASP ASP GLN HIS GLY ARG PHE ILE GLU SER
SEQRES 7 A 332 TYR MSE ARG GLY VAL GLY VAL ASP THR SER ASN LEU VAL
SEQRES 8 A 332 VAL ASP GLN GLU GLY HIS LYS THR GLY LEU ALA PHE THR
SEQRES 9 A 332 GLU ILE LYS SER PRO GLU GLU CYS SER ILE LEU MSE TYR
SEQRES 10 A 332 ARG GLN ASP VAL ALA ASP LEU TYR LEU SER PRO GLU GLU
SEQRES 11 A 332 VAL ASN GLU ALA TYR ILE ARG ARG SER LYS LEU LEU LEU
SEQRES 12 A 332 VAL SER GLY THR ALA LEU SER LYS SER PRO SER ARG GLU
SEQRES 13 A 332 ALA VAL LEU LYS ALA ILE ARG LEU ALA LYS ARG ASN ASP
SEQRES 14 A 332 VAL LYS VAL VAL PHE GLU LEU ASP TYR ARG PRO TYR SER
SEQRES 15 A 332 TRP GLU THR PRO GLU GLU THR ALA VAL TYR TYR SER LEU
SEQRES 16 A 332 VAL ALA GLU GLN SER ASP ILE VAL ILE GLY THR ARG GLU
SEQRES 17 A 332 GLU PHE ASP VAL LEU GLU ASN ARG THR GLU LYS GLY ASP
SEQRES 18 A 332 ASN ASP GLU THR ILE ARG TYR LEU PHE LYS HIS SER PRO
SEQRES 19 A 332 GLU LEU ILE VAL ILE LYS HIS GLY VAL GLU GLY SER PHE
SEQRES 20 A 332 ALA TYR THR LYS ALA GLY GLU ALA TYR ARG GLY TYR ALA
SEQRES 21 A 332 TYR LYS THR LYS VAL LEU LYS THR PHE GLY ALA GLY ASP
SEQRES 22 A 332 SER TYR ALA SER ALA PHE LEU TYR ALA LEU ILE SER GLY
SEQRES 23 A 332 LYS GLY ILE GLU THR ALA LEU LYS TYR GLY SER ALA SER
SEQRES 24 A 332 ALA SER ILE VAL VAL SER LYS HIS SER SER SER ASP ALA
SEQRES 25 A 332 MSE PRO SER VAL GLU GLU ILE GLU ALA LEU ILE GLU LYS
SEQRES 26 A 332 ASP GLU THR ILE THR ILE ALA
MODRES 2QCV MSE A 32 MET SELENOMETHIONINE
MODRES 2QCV MSE A 36 MET SELENOMETHIONINE
MODRES 2QCV MSE A 79 MET SELENOMETHIONINE
MODRES 2QCV MSE A 115 MET SELENOMETHIONINE
MODRES 2QCV MSE A 312 MET SELENOMETHIONINE
HET MSE A 32 8
HET MSE A 36 8
HET MSE A 79 8
HET MSE A 115 8
HET MSE A 312 8
HET PGE A 332 20
HET PGE A 333 10
HETNAM MSE SELENOMETHIONINE
HETNAM PGE TRIETHYLENE GLYCOL
FORMUL 1 MSE 5(C5 H11 N O2 SE)
FORMUL 2 PGE 2(C6 H14 O4)
FORMUL 4 HOH *221(H2 O)
HELIX 1 1 PRO A 31 THR A 35 5 5
HELIX 2 2 GLY A 44 LEU A 56 1 13
HELIX 3 3 ASP A 69 VAL A 82 1 14
HELIX 4 4 VAL A 120 LEU A 125 5 6
HELIX 5 5 SER A 126 VAL A 130 5 5
HELIX 6 6 ASN A 131 ARG A 136 1 6
HELIX 7 7 THR A 146 SER A 149 5 4
HELIX 8 8 PRO A 152 ASN A 167 1 16
HELIX 9 9 ARG A 178 TRP A 182 5 5
HELIX 10 10 THR A 184 SER A 199 1 16
HELIX 11 11 ARG A 206 GLU A 213 1 8
HELIX 12 12 ASP A 220 PHE A 229 1 10
HELIX 13 13 GLY A 241 GLU A 243 5 3
HELIX 14 14 GLY A 269 SER A 284 1 16
HELIX 15 15 GLY A 287 LYS A 305 1 19
HELIX 16 16 SER A 314 ASP A 325 1 12
SHEET 1 A 9 LEU A 89 VAL A 91 0
SHEET 2 A 9 ALA A 60 ILE A 66 1 N GLY A 64 O VAL A 90
SHEET 3 A 9 PHE A 11 ILE A 16 1 N ALA A 15 O ILE A 63
SHEET 4 A 9 SER A 138 SER A 144 1 O LEU A 142 N ILE A 14
SHEET 5 A 9 LYS A 170 GLU A 174 1 O VAL A 172 N LEU A 141
SHEET 6 A 9 ILE A 201 THR A 205 1 O ILE A 201 N PHE A 173
SHEET 7 A 9 LEU A 235 LYS A 239 1 O VAL A 237 N VAL A 202
SHEET 8 A 9 SER A 245 THR A 249 -1 O PHE A 246 N ILE A 238
SHEET 9 A 9 ALA A 254 GLY A 257 -1 O GLY A 257 N SER A 245
SHEET 1 B 4 PHE A 38 GLY A 43 0
SHEET 2 B 4 CYS A 20 ALA A 25 -1 N ASP A 22 O TYR A 41
SHEET 3 B 4 LEU A 100 SER A 107 1 O ALA A 101 N LEU A 23
SHEET 4 B 4 GLU A 110 TYR A 116 -1 O SER A 112 N GLU A 104
LINK C PRO A 31 N MSE A 32 1555 1555 1.33
LINK C MSE A 32 N GLU A 33 1555 1555 1.33
LINK C THR A 35 N MSE A 36 1555 1555 1.33
LINK C MSE A 36 N THR A 37 1555 1555 1.34
LINK C TYR A 78 N MSE A 79 1555 1555 1.34
LINK C MSE A 79 N ARG A 80 1555 1555 1.33
LINK C LEU A 114 N MSE A 115 1555 1555 1.33
LINK C MSE A 115 N TYR A 116 1555 1555 1.33
LINK C ALA A 311 N MSE A 312 1555 1555 1.33
LINK C MSE A 312 N PRO A 313 1555 1555 1.35
CISPEP 1 SER A 151 PRO A 152 0 0.59
SITE 1 AC1 11 GLU A 174 ASP A 176 THR A 205 GLU A 208
SITE 2 AC1 11 LYS A 239 ALA A 270 GLY A 271 ASP A 272
SITE 3 AC1 11 TYR A 274 ALA A 299 HOH A 442
SITE 1 AC2 9 LYS A 159 ARG A 162 GLU A 186 SER A 193
SITE 2 AC2 9 LEU A 212 ASN A 214 TYR A 227 HOH A 382
SITE 3 AC2 9 HOH A 440
CRYST1 194.001 194.001 48.083 90.00 90.00 120.00 P 64 2 2 12
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 0.005155 0.002976 0.000000 0.00000
SCALE2 0.000000 0.005952 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020797 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
