| 6qla-pdb | HEADER HYDROLASE 31-JAN-19 6QLA
TITLE CRYSTAL STRUCTURE OF THE PMGL2 ESTERASE (POINT MUTANT 1) FROM
TITLE 2 PERMAFROST METAGENOMIC LIBRARY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PMGL2;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASE, PERMAFROST, METAGENOME, HSL FAMILY, GCSAG MOTIF, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.M.BOYKO,D.GARSIA,A.Y.NIKOLAEVA,D.A.KORZHENEVSKIY,M.V.KRYUKOVA,
AUTHOR 2 L.E.PETROVSKAYA,K.A.NOVOTOTSKAYA-VLASOVA,E.M.RIVKINA,D.A.DOLGIKH,
AUTHOR 3 M.P.KIRPICHNIKOV,V.O.POPOV
REVDAT 1 25-DEC-19 6QLA 0
JRNL AUTH K.M.BOYKO,M.V.KRYUKOVA,A.Y.NIKOLAEVA,D.A.KORZHENEVSKIY,
JRNL AUTH 2 L.E.PETROVSKAYA,K.A.NOVOTOTSKAYA-VLASOVA,E.M.RIVKINA,
JRNL AUTH 3 D.A.DOLGIKH,M.P.KIRPICHNIKOV,V.O.POPOV
JRNL TITL CRYSTAL STRUCTURE OF THE PMGL2 ESTERASE WITH GCSAG MOTIF
JRNL TITL 2 AROUND THE CATALYTIC SERINE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.43 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
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) : 1.43
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 104774
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) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 5606
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) : 1.43
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.47
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7502
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.71
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE SET COUNT : 393
REMARK 3 BIN FREE R VALUE : 0.3140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4805
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 577
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.27000
REMARK 3 B22 (A**2) : 0.26000
REMARK 3 B33 (A**2) : -0.70000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.49000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.059
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.062
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.045
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.201
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.974
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5060 ; 0.015 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4726 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6880 ; 1.921 ; 1.649
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10877 ; 1.691 ; 1.567
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 641 ; 6.234 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 285 ;24.759 ;19.123
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 727 ;13.397 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 61 ;20.935 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 634 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5775 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1176 ; 0.002 ; 0.020
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 14 332 B 14 332 10244 0.090 0.050
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6QLA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1292100391.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JAN-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.31
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 110412
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.430
REMARK 200 RESOLUTION RANGE LOW (A) : 56.460
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.95900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 6QIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 250MM MAGNESIUM CHLORIDE, 12-18%
REMARK 280 PEG3350, 100MM HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 288K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 46.09000
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 1
REMARK 465 ALA A 2
REMARK 465 SER A 3
REMARK 465 GLY A 4
REMARK 465 SER A 5
REMARK 465 ALA A 6
REMARK 465 SER A 7
REMARK 465 SER A 8
REMARK 465 ALA A 9
REMARK 465 GLN A 10
REMARK 465 THR A 11
REMARK 465 PRO A 12
REMARK 465 GLY A 13
REMARK 465 SER A 333
REMARK 465 SER A 334
REMARK 465 SER A 335
REMARK 465 ILE A 336
REMARK 465 PRO A 337
REMARK 465 THR A 338
REMARK 465 PRO A 339
REMARK 465 ARG A 340
REMARK 465 SER A 341
REMARK 465 PRO A 342
REMARK 465 SER A 343
REMARK 465 LEU A 344
REMARK 465 GLU A 345
REMARK 465 HIS A 346
REMARK 465 HIS A 347
REMARK 465 HIS A 348
REMARK 465 HIS A 349
REMARK 465 HIS A 350
REMARK 465 HIS A 351
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 SER B 3
REMARK 465 GLY B 4
REMARK 465 SER B 5
REMARK 465 ALA B 6
REMARK 465 SER B 7
REMARK 465 SER B 8
REMARK 465 ALA B 9
REMARK 465 GLN B 10
REMARK 465 THR B 11
REMARK 465 PRO B 12
REMARK 465 GLY B 13
REMARK 465 SER B 333
REMARK 465 SER B 334
REMARK 465 SER B 335
REMARK 465 ILE B 336
REMARK 465 PRO B 337
REMARK 465 THR B 338
REMARK 465 PRO B 339
REMARK 465 ARG B 340
REMARK 465 SER B 341
REMARK 465 PRO B 342
REMARK 465 SER B 343
REMARK 465 LEU B 344
REMARK 465 GLU B 345
REMARK 465 HIS B 346
REMARK 465 HIS B 347
REMARK 465 HIS B 348
REMARK 465 HIS B 349
REMARK 465 HIS B 350
REMARK 465 HIS B 351
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 LEU A 14 CG CD1 CD2
REMARK 470 SER A 16 OG
REMARK 470 LYS A 39 CG CD CE NZ
REMARK 470 ASN A 44 CG OD1 ND2
REMARK 470 LYS A 226 CD CE NZ
REMARK 470 LYS B 39 CG CD CE NZ
REMARK 470 ARG B 97 CZ NH1 NH2
REMARK 470 VAL B 225 CG1 CG2
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 NH2 ARG B 66 OE1 GLU B 73 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 34 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 283 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 284 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 ARG B 66 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG B 66 NE - CZ - NH2 ANGL. DEV. = -6.0 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 PRO A 146 32.63 -97.40
REMARK 500 SER A 174 -122.69 63.44
REMARK 500 PRO A 235 48.30 -92.92
REMARK 500 PRO B 146 30.21 -98.51
REMARK 500 SER B 174 -121.15 63.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 801 DISTANCE = 5.92 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PG6 A 402
REMARK 610 PG6 A 403
REMARK 610 PG6 B 401
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 404 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 613 O
REMARK 620 2 HOH A 532 O 169.4
REMARK 620 3 HOH B 743 O 90.5 99.8
REMARK 620 4 HOH A 529 O 80.1 89.5 170.2
REMARK 620 5 HOH A 705 O 88.8 88.5 90.3 86.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 580 O
REMARK 620 2 HOH B 531 O 94.3
REMARK 620 3 HOH A 558 O 173.8 86.1
REMARK 620 4 HOH B 718 O 94.3 163.3 83.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 539 O
REMARK 620 2 HOH B 664 O 75.7
REMARK 620 3 HOH B 689 O 85.6 91.5
REMARK 620 4 HOH B 547 O 80.1 155.3 91.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG6 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG6 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG6 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6QIN RELATED DB: PDB
REMARK 900 WILD TYPE PROTEIN
DBREF1 6QLA A 1 343 UNP A0A142J6I6_9BACT
DBREF2 6QLA A A0A142J6I6 1 343
DBREF1 6QLA B 1 343 UNP A0A142J6I6_9BACT
DBREF2 6QLA B A0A142J6I6 1 343
SEQADV 6QLA THR A 173 UNP A0A142J6I CYS 173 CONFLICT
SEQADV 6QLA SER A 202 UNP A0A142J6I CYS 202 CONFLICT
SEQADV 6QLA LEU A 344 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QLA GLU A 345 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QLA HIS A 346 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QLA HIS A 347 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QLA HIS A 348 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QLA HIS A 349 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QLA HIS A 350 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QLA HIS A 351 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QLA THR B 173 UNP A0A142J6I CYS 173 CONFLICT
SEQADV 6QLA SER B 202 UNP A0A142J6I CYS 202 CONFLICT
SEQADV 6QLA LEU B 344 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QLA GLU B 345 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QLA HIS B 346 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QLA HIS B 347 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QLA HIS B 348 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QLA HIS B 349 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QLA HIS B 350 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QLA HIS B 351 UNP A0A142J6I EXPRESSION TAG
SEQRES 1 A 351 MET ALA SER GLY SER ALA SER SER ALA GLN THR PRO GLY
SEQRES 2 A 351 LEU MET SER TRP LEU PRO PRO SER ASN GLN LEU SER PRO
SEQRES 3 A 351 GLU ALA ARG SER VAL LEU ASP ARG MET ASP ALA ALA LYS
SEQRES 4 A 351 ALA PRO GLU PHE ASN GLY ASP LEU VAL ARG GLN ARG ALA
SEQRES 5 A 351 PHE TYR GLN GLN PHE ASN ASP ASP ARG LEU VAL GLU MET
SEQRES 6 A 351 ARG ARG VAL PHE ARG THR ARG GLU ARG HIS GLU THR LEU
SEQRES 7 A 351 ASN ALA VAL HIS VAL GLN VAL VAL GLU PRO ALA ASP GLY
SEQRES 8 A 351 VAL SER ALA ARG ASN ARG ASP ARG VAL LEU ILE ASN VAL
SEQRES 9 A 351 HIS GLY GLY ALA PHE MET TRP GLY ALA GLY SER GLY ALA
SEQRES 10 A 351 LEU VAL GLU ALA ILE PRO ILE ALA ALA THR MET GLY VAL
SEQRES 11 A 351 SER VAL VAL THR VAL ASP TYR ARG LEU ALA PRO GLU ASN
SEQRES 12 A 351 ARG TYR PRO ALA ALA SER GLU ASP VAL THR ALA VAL TYR
SEQRES 13 A 351 ARG ALA LEU LEU GLU ARG TYR PRO ALA ALA ASN ILE GLY
SEQRES 14 A 351 ILE PHE GLY THR SER ALA GLY GLY VAL ILE THR ALA GLN
SEQRES 15 A 351 ALA VAL THR TRP ILE ARG ARG GLU GLY LEU PRO ARG PRO
SEQRES 16 A 351 GLY ALA ILE GLY THR LEU SER GLY THR GLY ALA PRO TYR
SEQRES 17 A 351 SER GLY ASP SER PRO TYR LEU ALA GLY VAL VAL PRO VAL
SEQRES 18 A 351 GLY PRO GLY VAL LYS ALA PRO PRO LEU PRO GLY LEU LEU
SEQRES 19 A 351 PRO THR ALA TYR MET GLU GLY VAL GLY ALA ASP ASP ALA
SEQRES 20 A 351 ARG ALA TYR PRO LEU THR SER ASP ALA GLU THR VAL PHE
SEQRES 21 A 351 MET PRO PRO THR LEU LEU LEU ALA GLY GLY ARG ASP PHE
SEQRES 22 A 351 ALA VAL SER ALA LEU SER LEU ALA HIS ARG ARG LEU ALA
SEQRES 23 A 351 ARG ALA GLY VAL ASP SER GLU LEU HIS LEU PHE ASP GLY
SEQRES 24 A 351 LEU PRO HIS ALA PHE PHE VAL TRP PRO ASP MET PRO GLU
SEQRES 25 A 351 SER LEU GLU ALA TYR ALA LEU ILE ALA GLY PHE PHE ASP
SEQRES 26 A 351 SER ARG LEU GLY LEU THR PRO SER SER SER ILE PRO THR
SEQRES 27 A 351 PRO ARG SER PRO SER LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 351 MET ALA SER GLY SER ALA SER SER ALA GLN THR PRO GLY
SEQRES 2 B 351 LEU MET SER TRP LEU PRO PRO SER ASN GLN LEU SER PRO
SEQRES 3 B 351 GLU ALA ARG SER VAL LEU ASP ARG MET ASP ALA ALA LYS
SEQRES 4 B 351 ALA PRO GLU PHE ASN GLY ASP LEU VAL ARG GLN ARG ALA
SEQRES 5 B 351 PHE TYR GLN GLN PHE ASN ASP ASP ARG LEU VAL GLU MET
SEQRES 6 B 351 ARG ARG VAL PHE ARG THR ARG GLU ARG HIS GLU THR LEU
SEQRES 7 B 351 ASN ALA VAL HIS VAL GLN VAL VAL GLU PRO ALA ASP GLY
SEQRES 8 B 351 VAL SER ALA ARG ASN ARG ASP ARG VAL LEU ILE ASN VAL
SEQRES 9 B 351 HIS GLY GLY ALA PHE MET TRP GLY ALA GLY SER GLY ALA
SEQRES 10 B 351 LEU VAL GLU ALA ILE PRO ILE ALA ALA THR MET GLY VAL
SEQRES 11 B 351 SER VAL VAL THR VAL ASP TYR ARG LEU ALA PRO GLU ASN
SEQRES 12 B 351 ARG TYR PRO ALA ALA SER GLU ASP VAL THR ALA VAL TYR
SEQRES 13 B 351 ARG ALA LEU LEU GLU ARG TYR PRO ALA ALA ASN ILE GLY
SEQRES 14 B 351 ILE PHE GLY THR SER ALA GLY GLY VAL ILE THR ALA GLN
SEQRES 15 B 351 ALA VAL THR TRP ILE ARG ARG GLU GLY LEU PRO ARG PRO
SEQRES 16 B 351 GLY ALA ILE GLY THR LEU SER GLY THR GLY ALA PRO TYR
SEQRES 17 B 351 SER GLY ASP SER PRO TYR LEU ALA GLY VAL VAL PRO VAL
SEQRES 18 B 351 GLY PRO GLY VAL LYS ALA PRO PRO LEU PRO GLY LEU LEU
SEQRES 19 B 351 PRO THR ALA TYR MET GLU GLY VAL GLY ALA ASP ASP ALA
SEQRES 20 B 351 ARG ALA TYR PRO LEU THR SER ASP ALA GLU THR VAL PHE
SEQRES 21 B 351 MET PRO PRO THR LEU LEU LEU ALA GLY GLY ARG ASP PHE
SEQRES 22 B 351 ALA VAL SER ALA LEU SER LEU ALA HIS ARG ARG LEU ALA
SEQRES 23 B 351 ARG ALA GLY VAL ASP SER GLU LEU HIS LEU PHE ASP GLY
SEQRES 24 B 351 LEU PRO HIS ALA PHE PHE VAL TRP PRO ASP MET PRO GLU
SEQRES 25 B 351 SER LEU GLU ALA TYR ALA LEU ILE ALA GLY PHE PHE ASP
SEQRES 26 B 351 SER ARG LEU GLY LEU THR PRO SER SER SER ILE PRO THR
SEQRES 27 B 351 PRO ARG SER PRO SER LEU GLU HIS HIS HIS HIS HIS HIS
HET CL A 401 1
HET PG6 A 402 17
HET PG6 A 403 14
HET MG A 404 1
HET PG6 B 401 14
HET MG B 402 1
HET MG B 403 1
HETNAM CL CHLORIDE ION
HETNAM PG6 1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-
HETNAM 2 PG6 ETHOXY}-ETHANE
HETNAM MG MAGNESIUM ION
FORMUL 3 CL CL 1-
FORMUL 4 PG6 3(C12 H26 O6)
FORMUL 6 MG 3(MG 2+)
FORMUL 10 HOH *577(H2 O)
HELIX 1 AA1 LEU A 14 LEU A 18 5 5
HELIX 2 AA2 SER A 25 ALA A 38 1 14
HELIX 3 AA3 ASP A 46 PHE A 69 1 24
HELIX 4 AA4 SER A 93 ARG A 97 5 5
HELIX 5 AA5 GLY A 114 GLY A 129 1 16
HELIX 6 AA6 PRO A 146 LEU A 160 1 15
HELIX 7 AA7 PRO A 164 ALA A 166 5 3
HELIX 8 AA8 SER A 174 GLU A 190 1 17
HELIX 9 AA9 ASP A 211 ALA A 216 1 6
HELIX 10 AB1 THR A 236 GLU A 240 5 5
HELIX 11 AB2 TYR A 250 THR A 253 5 4
HELIX 12 AB3 SER A 254 PHE A 260 1 7
HELIX 13 AB4 ALA A 274 ALA A 288 1 15
HELIX 14 AB5 ALA A 303 TRP A 307 5 5
HELIX 15 AB6 MET A 310 LEU A 328 1 19
HELIX 16 AB7 LEU B 14 LEU B 18 5 5
HELIX 17 AB8 SER B 25 ALA B 38 1 14
HELIX 18 AB9 ASP B 46 PHE B 69 1 24
HELIX 19 AC1 SER B 93 ARG B 97 5 5
HELIX 20 AC2 GLY B 114 GLY B 129 1 16
HELIX 21 AC3 PRO B 146 LEU B 160 1 15
HELIX 22 AC4 PRO B 164 ALA B 166 5 3
HELIX 23 AC5 SER B 174 GLU B 190 1 17
HELIX 24 AC6 ASP B 211 ALA B 216 1 6
HELIX 25 AC7 THR B 236 GLU B 240 5 5
HELIX 26 AC8 TYR B 250 THR B 253 5 4
HELIX 27 AC9 SER B 254 PHE B 260 1 7
HELIX 28 AD1 ALA B 274 ALA B 288 1 15
HELIX 29 AD2 ALA B 303 TRP B 307 5 5
HELIX 30 AD3 MET B 310 LEU B 328 1 19
SHEET 1 AA1 8 THR A 71 LEU A 78 0
SHEET 2 AA1 8 VAL A 81 PRO A 88 -1 O VAL A 85 N ARG A 74
SHEET 3 AA1 8 VAL A 132 VAL A 135 -1 O VAL A 132 N VAL A 86
SHEET 4 AA1 8 VAL A 100 VAL A 104 1 N LEU A 101 O VAL A 133
SHEET 5 AA1 8 ILE A 168 THR A 173 1 O GLY A 169 N ILE A 102
SHEET 6 AA1 8 ALA A 197 LEU A 201 1 O LEU A 201 N GLY A 172
SHEET 7 AA1 8 THR A 264 GLY A 269 1 O LEU A 265 N THR A 200
SHEET 8 AA1 8 SER A 292 PHE A 297 1 O GLU A 293 N LEU A 266
SHEET 1 AA2 8 THR B 71 LEU B 78 0
SHEET 2 AA2 8 VAL B 81 PRO B 88 -1 O VAL B 85 N ARG B 74
SHEET 3 AA2 8 VAL B 132 VAL B 135 -1 O VAL B 132 N VAL B 86
SHEET 4 AA2 8 VAL B 100 VAL B 104 1 N LEU B 101 O VAL B 133
SHEET 5 AA2 8 ILE B 168 THR B 173 1 O GLY B 169 N ILE B 102
SHEET 6 AA2 8 ALA B 197 LEU B 201 1 O LEU B 201 N GLY B 172
SHEET 7 AA2 8 THR B 264 GLY B 269 1 O LEU B 265 N THR B 200
SHEET 8 AA2 8 SER B 292 PHE B 297 1 O GLU B 293 N LEU B 266
LINK MG MG A 404 O HOH B 613 1555 1555 2.08
LINK MG MG A 404 O HOH A 532 1555 1555 2.04
LINK MG MG A 404 O HOH B 743 1555 1555 2.08
LINK MG MG A 404 O HOH A 529 1555 1555 2.12
LINK MG MG A 404 O HOH A 705 1555 1555 2.13
LINK MG MG B 402 O HOH B 580 1555 1555 2.03
LINK MG MG B 402 O HOH B 531 1555 1555 2.13
LINK MG MG B 402 O HOH A 558 1555 1555 2.06
LINK MG MG B 403 O HOH B 539 1555 1555 2.11
LINK MG MG B 403 O HOH B 664 1555 1555 2.06
LINK MG MG B 403 O HOH B 689 1555 1555 2.09
LINK MG MG B 403 O HOH B 547 1555 1555 2.80
LINK MG MG B 402 O HOH B 718 1555 2645 2.09
CISPEP 1 ALA A 140 PRO A 141 0 -2.58
CISPEP 2 TYR A 145 PRO A 146 0 1.18
CISPEP 3 ALA B 140 PRO B 141 0 -4.44
CISPEP 4 TYR B 145 PRO B 146 0 2.08
SITE 1 AC1 7 HIS A 282 GLU A 293 LEU A 294 HIS B 282
SITE 2 AC1 7 GLU B 293 LEU B 294 HOH B 727
SITE 1 AC2 12 PHE A 109 SER A 174 ALA A 175 GLY A 203
SITE 2 AC2 12 THR A 204 ALA A 206 TYR A 208 PRO A 235
SITE 3 AC2 12 PHE A 273 ALA A 274 PG6 A 403 HOH A 658
SITE 1 AC3 12 SER A 174 ALA A 175 GLY A 203 THR A 204
SITE 2 AC3 12 ALA A 206 PRO A 207 TYR A 208 PHE A 273
SITE 3 AC3 12 ALA A 277 HIS A 302 PG6 A 402 HOH A 658
SITE 1 AC4 6 GLU A 293 HOH A 529 HOH A 532 HOH A 705
SITE 2 AC4 6 HOH B 613 HOH B 743
SITE 1 AC5 9 SER B 174 ALA B 175 GLY B 203 THR B 204
SITE 2 AC5 9 ALA B 206 PHE B 273 ALA B 274 ALA B 277
SITE 3 AC5 9 HOH B 702
SITE 1 AC6 4 HOH A 558 GLU B 293 HOH B 531 HOH B 580
SITE 1 AC7 6 ASN B 79 GLU B 161 HOH B 539 HOH B 547
SITE 2 AC7 6 HOH B 664 HOH B 689
CRYST1 47.140 92.180 74.460 90.00 106.41 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.021213 0.000000 0.006247 0.00000
SCALE2 0.000000 0.010848 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014000 0.00000
TER 2456 PRO A 332
TER 4884 PRO B 332
MASTER 461 0 7 30 16 0 16 6 5431 2 61 54
END
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