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HEADER HYDROLASE 21-JAN-19 6QIN
TITLE CRYSTAL STRUCTURE OF THE PMGL2 ESTERASE FROM PERMAFROST METAGENOMIC
TITLE 2 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,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 6QIN 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. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 73837
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) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3883
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4731
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 590
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.42000
REMARK 3 B22 (A**2) : -0.13000
REMARK 3 B33 (A**2) : -0.67000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.82000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.083
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.083
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.057
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.659
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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 6QIN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1292100231.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-16
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) : 1.0
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 : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.23
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77747
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 56.310
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.65300
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: 3L1H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.47
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 46.17500
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 LEU A 14
REMARK 465 VAL A 221
REMARK 465 GLY A 222
REMARK 465 PRO A 223
REMARK 465 GLY A 224
REMARK 465 VAL A 225
REMARK 465 LYS A 226
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 HIS A 344
REMARK 465 HIS A 345
REMARK 465 HIS A 346
REMARK 465 HIS A 347
REMARK 465 HIS A 348
REMARK 465 HIS A 349
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 LEU B 14
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 HIS B 344
REMARK 465 HIS B 345
REMARK 465 HIS B 346
REMARK 465 HIS B 347
REMARK 465 HIS B 348
REMARK 465 HIS B 349
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 SER A 16 OG
REMARK 470 TRP A 17 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 17 CZ3 CH2
REMARK 470 LYS A 39 CG CD CE NZ
REMARK 470 GLU A 42 CG CD OE1 OE2
REMARK 470 SER B 16 OG
REMARK 470 TRP B 17 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 17 CZ3 CH2
REMARK 470 LYS B 39 CG CD CE NZ
REMARK 470 ARG B 97 CZ NH1 NH2
REMARK 470 VAL B 221 CG1 CG2
REMARK 470 LYS B 226 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 142 CD GLU A 142 OE1 0.077
REMARK 500 TYR A 208 C TYR A 208 O 0.132
REMARK 500 GLU B 120 CD GLU B 120 OE1 0.075
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 29 CG - CD - NE ANGL. DEV. = -15.0 DEGREES
REMARK 500 ARG A 29 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 67 CA - CB - CG ANGL. DEV. = 16.8 DEGREES
REMARK 500 HIS A 82 CA - CB - CG ANGL. DEV. = -10.5 DEGREES
REMARK 500 ARG A 144 CB - CG - CD ANGL. DEV. = -24.4 DEGREES
REMARK 500 TYR A 208 CB - CA - C ANGL. DEV. = 20.6 DEGREES
REMARK 500 TYR A 208 CB - CG - CD2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 TYR A 208 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 TYR A 208 CB - CG - CD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 TYR A 208 CB - CG - CD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 287 CG - CD - NE ANGL. DEV. = 14.0 DEGREES
REMARK 500 SER B 30 CA - CB - OG ANGL. DEV. = -20.0 DEGREES
REMARK 500 ASP B 59 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG B 66 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 74 CB - CA - C ANGL. DEV. = 13.2 DEGREES
REMARK 500 ARG B 144 CB - CG - CD ANGL. DEV. = -16.5 DEGREES
REMARK 500 ARG B 194 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 TYR B 208 CB - CA - C ANGL. DEV. = 24.4 DEGREES
REMARK 500 TYR B 208 CA - CB - CG ANGL. DEV. = 13.8 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 34.55 -98.33
REMARK 500 SER A 174 -116.98 70.40
REMARK 500 PRO A 235 3.50 -69.36
REMARK 500 ASP A 309 47.74 -90.67
REMARK 500 PRO B 146 34.61 -99.04
REMARK 500 SER B 174 -123.76 69.93
REMARK 500 ASP B 309 55.63 -93.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 TYR A 208 10.37
REMARK 500 PRO A 235 -10.63
REMARK 500 PRO A 235 10.14
REMARK 500 TYR B 208 11.71
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 A 804 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH B 784 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B 785 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH B 786 DISTANCE = 6.63 ANGSTROMS
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 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 593 O
REMARK 620 2 HOH A 741 O 89.7
REMARK 620 3 HOH A 600 O 165.5 93.0
REMARK 620 4 HOH B 733 O 93.5 84.7 101.0
REMARK 620 5 HOH A 510 O 82.3 93.3 83.3 175.4
REMARK 620 6 HOH A 622 O 87.7 175.8 90.4 92.2 89.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 526 O
REMARK 620 2 HOH B 633 O 102.5
REMARK 620 3 HOH B 729 O 93.9 88.0
REMARK 620 4 HOH A 570 O 77.9 176.3 88.3
REMARK 620 5 HOH A 753 O 173.4 84.1 86.8 95.6
REMARK 620 6 HOH B 603 O 90.8 100.0 169.6 83.7 87.5
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 CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 401
DBREF1 6QIN A 1 343 UNP A0A142J6I6_9BACT
DBREF2 6QIN A A0A142J6I6 1 343
DBREF1 6QIN B 1 343 UNP A0A142J6I6_9BACT
DBREF2 6QIN B A0A142J6I6 1 343
SEQADV 6QIN HIS A 344 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QIN HIS A 345 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QIN HIS A 346 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QIN HIS A 347 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QIN HIS A 348 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QIN HIS A 349 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QIN HIS B 344 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QIN HIS B 345 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QIN HIS B 346 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QIN HIS B 347 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QIN HIS B 348 UNP A0A142J6I EXPRESSION TAG
SEQADV 6QIN HIS B 349 UNP A0A142J6I EXPRESSION TAG
SEQRES 1 A 349 MET ALA SER GLY SER ALA SER SER ALA GLN THR PRO GLY
SEQRES 2 A 349 LEU MET SER TRP LEU PRO PRO SER ASN GLN LEU SER PRO
SEQRES 3 A 349 GLU ALA ARG SER VAL LEU ASP ARG MET ASP ALA ALA LYS
SEQRES 4 A 349 ALA PRO GLU PHE ASN GLY ASP LEU VAL ARG GLN ARG ALA
SEQRES 5 A 349 PHE TYR GLN GLN PHE ASN ASP ASP ARG LEU VAL GLU MET
SEQRES 6 A 349 ARG ARG VAL PHE ARG THR ARG GLU ARG HIS GLU THR LEU
SEQRES 7 A 349 ASN ALA VAL HIS VAL GLN VAL VAL GLU PRO ALA ASP GLY
SEQRES 8 A 349 VAL SER ALA ARG ASN ARG ASP ARG VAL LEU ILE ASN VAL
SEQRES 9 A 349 HIS GLY GLY ALA PHE MET TRP GLY ALA GLY SER GLY ALA
SEQRES 10 A 349 LEU VAL GLU ALA ILE PRO ILE ALA ALA THR MET GLY VAL
SEQRES 11 A 349 SER VAL VAL THR VAL ASP TYR ARG LEU ALA PRO GLU ASN
SEQRES 12 A 349 ARG TYR PRO ALA ALA SER GLU ASP VAL THR ALA VAL TYR
SEQRES 13 A 349 ARG ALA LEU LEU GLU ARG TYR PRO ALA ALA ASN ILE GLY
SEQRES 14 A 349 ILE PHE GLY CYS SER ALA GLY GLY VAL ILE THR ALA GLN
SEQRES 15 A 349 ALA VAL THR TRP ILE ARG ARG GLU GLY LEU PRO ARG PRO
SEQRES 16 A 349 GLY ALA ILE GLY THR LEU CYS GLY THR GLY ALA PRO TYR
SEQRES 17 A 349 SER GLY ASP SER PRO TYR LEU ALA GLY VAL VAL PRO VAL
SEQRES 18 A 349 GLY PRO GLY VAL LYS ALA PRO PRO LEU PRO GLY LEU LEU
SEQRES 19 A 349 PRO THR ALA TYR MET GLU GLY VAL GLY ALA ASP ASP ALA
SEQRES 20 A 349 ARG ALA TYR PRO LEU THR SER ASP ALA GLU THR VAL PHE
SEQRES 21 A 349 MET PRO PRO THR LEU LEU LEU ALA GLY GLY ARG ASP PHE
SEQRES 22 A 349 ALA VAL SER ALA LEU SER LEU ALA HIS ARG ARG LEU ALA
SEQRES 23 A 349 ARG ALA GLY VAL ASP SER GLU LEU HIS LEU PHE ASP GLY
SEQRES 24 A 349 LEU PRO HIS ALA PHE PHE VAL TRP PRO ASP MET PRO GLU
SEQRES 25 A 349 SER LEU GLU ALA TYR ALA LEU ILE ALA GLY PHE PHE ASP
SEQRES 26 A 349 SER ARG LEU GLY LEU THR PRO SER SER SER ILE PRO THR
SEQRES 27 A 349 PRO ARG SER PRO SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 349 MET ALA SER GLY SER ALA SER SER ALA GLN THR PRO GLY
SEQRES 2 B 349 LEU MET SER TRP LEU PRO PRO SER ASN GLN LEU SER PRO
SEQRES 3 B 349 GLU ALA ARG SER VAL LEU ASP ARG MET ASP ALA ALA LYS
SEQRES 4 B 349 ALA PRO GLU PHE ASN GLY ASP LEU VAL ARG GLN ARG ALA
SEQRES 5 B 349 PHE TYR GLN GLN PHE ASN ASP ASP ARG LEU VAL GLU MET
SEQRES 6 B 349 ARG ARG VAL PHE ARG THR ARG GLU ARG HIS GLU THR LEU
SEQRES 7 B 349 ASN ALA VAL HIS VAL GLN VAL VAL GLU PRO ALA ASP GLY
SEQRES 8 B 349 VAL SER ALA ARG ASN ARG ASP ARG VAL LEU ILE ASN VAL
SEQRES 9 B 349 HIS GLY GLY ALA PHE MET TRP GLY ALA GLY SER GLY ALA
SEQRES 10 B 349 LEU VAL GLU ALA ILE PRO ILE ALA ALA THR MET GLY VAL
SEQRES 11 B 349 SER VAL VAL THR VAL ASP TYR ARG LEU ALA PRO GLU ASN
SEQRES 12 B 349 ARG TYR PRO ALA ALA SER GLU ASP VAL THR ALA VAL TYR
SEQRES 13 B 349 ARG ALA LEU LEU GLU ARG TYR PRO ALA ALA ASN ILE GLY
SEQRES 14 B 349 ILE PHE GLY CYS SER ALA GLY GLY VAL ILE THR ALA GLN
SEQRES 15 B 349 ALA VAL THR TRP ILE ARG ARG GLU GLY LEU PRO ARG PRO
SEQRES 16 B 349 GLY ALA ILE GLY THR LEU CYS GLY THR GLY ALA PRO TYR
SEQRES 17 B 349 SER GLY ASP SER PRO TYR LEU ALA GLY VAL VAL PRO VAL
SEQRES 18 B 349 GLY PRO GLY VAL LYS ALA PRO PRO LEU PRO GLY LEU LEU
SEQRES 19 B 349 PRO THR ALA TYR MET GLU GLY VAL GLY ALA ASP ASP ALA
SEQRES 20 B 349 ARG ALA TYR PRO LEU THR SER ASP ALA GLU THR VAL PHE
SEQRES 21 B 349 MET PRO PRO THR LEU LEU LEU ALA GLY GLY ARG ASP PHE
SEQRES 22 B 349 ALA VAL SER ALA LEU SER LEU ALA HIS ARG ARG LEU ALA
SEQRES 23 B 349 ARG ALA GLY VAL ASP SER GLU LEU HIS LEU PHE ASP GLY
SEQRES 24 B 349 LEU PRO HIS ALA PHE PHE VAL TRP PRO ASP MET PRO GLU
SEQRES 25 B 349 SER LEU GLU ALA TYR ALA LEU ILE ALA GLY PHE PHE ASP
SEQRES 26 B 349 SER ARG LEU GLY LEU THR PRO SER SER SER ILE PRO THR
SEQRES 27 B 349 PRO ARG SER PRO SER HIS HIS HIS HIS HIS HIS
HET CL A 401 1
HET MG A 402 1
HET MG B 401 1
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
FORMUL 3 CL CL 1-
FORMUL 4 MG 2(MG 2+)
FORMUL 6 HOH *590(H2 O)
HELIX 1 AA1 SER A 25 ALA A 38 1 14
HELIX 2 AA2 ASP A 46 PHE A 69 1 24
HELIX 3 AA3 GLY A 114 GLY A 129 1 16
HELIX 4 AA4 PRO A 146 LEU A 160 1 15
HELIX 5 AA5 PRO A 164 ALA A 166 5 3
HELIX 6 AA6 SER A 174 GLU A 190 1 17
HELIX 7 AA7 ASP A 211 ALA A 216 1 6
HELIX 8 AA8 THR A 236 GLU A 240 5 5
HELIX 9 AA9 TYR A 250 THR A 253 5 4
HELIX 10 AB1 SER A 254 PHE A 260 1 7
HELIX 11 AB2 ALA A 274 ALA A 288 1 15
HELIX 12 AB3 ALA A 303 TRP A 307 5 5
HELIX 13 AB4 MET A 310 LEU A 328 1 19
HELIX 14 AB5 SER B 25 ALA B 38 1 14
HELIX 15 AB6 ASP B 46 PHE B 69 1 24
HELIX 16 AB7 SER B 93 ARG B 97 5 5
HELIX 17 AB8 GLY B 114 GLY B 129 1 16
HELIX 18 AB9 PRO B 146 LEU B 160 1 15
HELIX 19 AC1 PRO B 164 ALA B 166 5 3
HELIX 20 AC2 SER B 174 GLY B 191 1 18
HELIX 21 AC3 ASP B 211 ALA B 216 1 6
HELIX 22 AC4 THR B 236 GLU B 240 5 5
HELIX 23 AC5 TYR B 250 THR B 253 5 4
HELIX 24 AC6 SER B 254 PHE B 260 1 7
HELIX 25 AC7 ALA B 274 ALA B 288 1 15
HELIX 26 AC8 ALA B 303 TRP B 307 5 5
HELIX 27 AC9 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 81 N LEU A 78
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 CYS A 173 1 O PHE A 171 N ILE A 102
SHEET 6 AA1 8 ALA A 197 LEU A 201 1 O GLY A 199 N ILE A 170
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 81 N LEU B 78
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 CYS B 173 1 O GLY B 169 N ILE B 102
SHEET 6 AA2 8 ALA B 197 LEU B 201 1 O GLY B 199 N ILE B 170
SHEET 7 AA2 8 THR B 264 GLY B 269 1 O LEU B 265 N ILE B 198
SHEET 8 AA2 8 SER B 292 PHE B 297 1 O GLU B 293 N LEU B 266
LINK MG MG A 402 O HOH B 593 1555 1555 2.14
LINK MG MG A 402 O HOH A 741 1555 1555 2.06
LINK MG MG A 402 O HOH A 600 1555 1555 1.83
LINK MG MG A 402 O HOH B 733 1555 1555 2.08
LINK MG MG A 402 O HOH A 510 1555 1555 2.08
LINK MG MG A 402 O HOH A 622 1555 1555 2.10
LINK MG MG B 401 O HOH B 526 1555 1555 2.07
LINK MG MG B 401 O HOH B 633 1555 1555 2.04
LINK MG MG B 401 O HOH B 729 1555 1555 2.12
LINK MG MG B 401 O HOH A 570 1555 1555 2.13
LINK MG MG B 401 O HOH A 753 1555 1555 2.04
LINK MG MG B 401 O HOH B 603 1555 1555 2.11
CISPEP 1 ALA A 140 PRO A 141 0 -3.98
CISPEP 2 TYR A 145 PRO A 146 0 1.51
CISPEP 3 ALA B 140 PRO B 141 0 -4.02
CISPEP 4 TYR B 145 PRO B 146 0 2.34
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 710
SITE 1 AC2 7 GLU A 293 HOH A 510 HOH A 600 HOH A 622
SITE 2 AC2 7 HOH A 741 HOH B 593 HOH B 733
SITE 1 AC3 7 HOH A 570 HOH A 753 GLU B 293 HOH B 526
SITE 2 AC3 7 HOH B 603 HOH B 633 HOH B 729
CRYST1 47.010 92.350 74.230 90.00 106.83 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 0.021272 0.000000 0.006435 0.00000
SCALE2 0.000000 0.010828 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014074 0.00000
TER 2396 PRO A 332
TER 4797 PRO B 332
MASTER 434 0 3 27 16 0 6 6 5324 2 16 54
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