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HEADER HYDROLASE 19-JAN-24 8XY5
TITLE OPEN CONFORMATION OF BURKHOLDERIA STAGNALIS LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TRIACYLGLYCEROL LIPASE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA STAGNALIS;
SOURCE 3 ORGANISM_TAXID: 1503054;
SOURCE 4 STRAIN: PL266-QLM
KEYWDS HYDROLASE, TRIACYLGLYCEROL LIPASE, BURKHOLDERIA
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KATAOKA,T.KUBOTA,K.ISHIKAWA
REVDAT 1 22-JAN-25 8XY5 0
JRNL AUTH S.KATAOKA,T.KUBOTA,K.ISHIKAWA
JRNL TITL STRUCTURAL AND FUNCTIONAL STUDIES OF LIPASE FROM
JRNL TITL 2 BURKHOLDERIA STAGNALIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0419
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.24
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 109215
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.095
REMARK 3 FREE R VALUE TEST SET COUNT : 5565
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7614
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.30
REMARK 3 BIN R VALUE (WORKING SET) : 0.2880
REMARK 3 BIN FREE R VALUE SET COUNT : 440
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4682
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 601
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00100
REMARK 3 B22 (A**2) : 0.00100
REMARK 3 B33 (A**2) : -0.00200
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): 0.059
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.060
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.039
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.020
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4840 ; 0.003 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 4526 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6634 ; 1.190 ; 1.784
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10350 ; 0.441 ; 1.715
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 646 ; 6.122 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 22 ; 4.802 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 690 ; 9.793 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 789 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5856 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1112 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1020 ; 0.213 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 112 ; 0.228 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2529 ; 0.173 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 432 ; 0.108 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 11 ; 0.076 ; 0.200
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): 2562 ; 0.642 ; 1.475
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2562 ; 0.642 ; 1.475
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3202 ; 1.015 ; 2.654
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3203 ; 1.015 ; 2.654
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2278 ; 1.120 ; 1.632
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2279 ; 1.119 ; 1.633
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3426 ; 1.795 ; 2.951
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3427 ; 1.795 ; 2.951
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 BULK SOLVENT
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 THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 8XY5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JAN-24.
REMARK 100 THE DEPOSITION ID IS D_1300044348.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-FEB-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 109236
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.399
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 24.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.83500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.0, 45% MPD, 1 M
REMARK 280 AMMONIUM FLUORIDE, 3% METHANOL, VAPOR DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 80.32150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.60500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 80.32150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.60500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 90 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 90 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ARG A 3
REMARK 465 ALA A 4
REMARK 465 MET A 5
REMARK 465 ARG A 6
REMARK 465 SER A 7
REMARK 465 ARG A 8
REMARK 465 VAL A 9
REMARK 465 VAL A 10
REMARK 465 ALA A 11
REMARK 465 GLY A 12
REMARK 465 VAL A 13
REMARK 465 VAL A 14
REMARK 465 ALA A 15
REMARK 465 CYS A 16
REMARK 465 ALA A 17
REMARK 465 MET A 18
REMARK 465 SER A 19
REMARK 465 ALA A 20
REMARK 465 ALA A 21
REMARK 465 PRO A 22
REMARK 465 PHE A 23
REMARK 465 ALA A 24
REMARK 465 GLY A 25
REMARK 465 MET A 26
REMARK 465 THR A 27
REMARK 465 ALA A 28
REMARK 465 LEU A 29
REMARK 465 ALA A 30
REMARK 465 THR A 31
REMARK 465 ALA A 32
REMARK 465 ALA A 33
REMARK 465 THR A 34
REMARK 465 THR A 35
REMARK 465 ARG A 36
REMARK 465 ALA A 37
REMARK 465 ALA A 38
REMARK 465 VAL A 39
REMARK 465 ALA A 40
REMARK 465 ALA A 41
REMARK 465 THR A 42
REMARK 465 ALA A 43
REMARK 465 PRO A 44
REMARK 465 ALA A 45
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ARG B 3
REMARK 465 ALA B 4
REMARK 465 MET B 5
REMARK 465 ARG B 6
REMARK 465 SER B 7
REMARK 465 ARG B 8
REMARK 465 VAL B 9
REMARK 465 VAL B 10
REMARK 465 ALA B 11
REMARK 465 GLY B 12
REMARK 465 VAL B 13
REMARK 465 VAL B 14
REMARK 465 ALA B 15
REMARK 465 CYS B 16
REMARK 465 ALA B 17
REMARK 465 MET B 18
REMARK 465 SER B 19
REMARK 465 ALA B 20
REMARK 465 ALA B 21
REMARK 465 PRO B 22
REMARK 465 PHE B 23
REMARK 465 ALA B 24
REMARK 465 GLY B 25
REMARK 465 MET B 26
REMARK 465 THR B 27
REMARK 465 ALA B 28
REMARK 465 LEU B 29
REMARK 465 ALA B 30
REMARK 465 THR B 31
REMARK 465 ALA B 32
REMARK 465 ALA B 33
REMARK 465 THR B 34
REMARK 465 THR B 35
REMARK 465 ARG B 36
REMARK 465 ALA B 37
REMARK 465 ALA B 38
REMARK 465 VAL B 39
REMARK 465 ALA B 40
REMARK 465 ALA B 41
REMARK 465 THR B 42
REMARK 465 ALA B 43
REMARK 465 PRO B 44
REMARK 465 ALA B 45
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 THR A 62 -12.10 79.71
REMARK 500 SER A 131 -124.10 57.77
REMARK 500 THR A 261 -103.77 -120.33
REMARK 500 VAL A 278 -62.00 76.62
REMARK 500 VAL A 310 -14.10 -140.58
REMARK 500 THR B 62 -11.83 80.34
REMARK 500 SER B 131 -124.07 57.27
REMARK 500 THR B 261 -107.86 -120.71
REMARK 500 VAL B 278 -62.88 77.30
REMARK 500 VAL B 310 -37.41 -135.38
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 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 286 OD2
REMARK 620 2 ASP A 332 OD1 169.9
REMARK 620 3 GLN A 336 O 90.3 95.0
REMARK 620 4 VAL A 340 O 89.0 99.8 86.4
REMARK 620 5 HOH A 528 O 85.6 85.8 90.7 173.9
REMARK 620 6 HOH A 584 O 89.0 85.2 176.4 97.1 85.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 286 OD2
REMARK 620 2 ASP B 332 OD1 169.5
REMARK 620 3 GLN B 336 O 90.2 95.0
REMARK 620 4 VAL B 340 O 87.9 101.5 86.6
REMARK 620 5 HOH B 533 O 84.8 86.3 88.6 171.2
REMARK 620 6 HOH B 600 O 89.1 84.9 175.0 98.4 86.3
REMARK 620 N 1 2 3 4 5
DBREF1 8XY5 A 1 364 UNP A0A108C1V7_9BURK
DBREF2 8XY5 A A0A108C1V7 1 364
DBREF1 8XY5 B 1 364 UNP A0A108C1V7_9BURK
DBREF2 8XY5 B A0A108C1V7 1 364
SEQADV 8XY5 THR A 136 UNP A0A108C1V SER 136 VARIANT
SEQADV 8XY5 SER A 264 UNP A0A108C1V ALA 264 VARIANT
SEQADV 8XY5 THR B 136 UNP A0A108C1V SER 136 VARIANT
SEQADV 8XY5 SER B 264 UNP A0A108C1V ALA 264 VARIANT
SEQRES 1 A 364 MET ALA ARG ALA MET ARG SER ARG VAL VAL ALA GLY VAL
SEQRES 2 A 364 VAL ALA CYS ALA MET SER ALA ALA PRO PHE ALA GLY MET
SEQRES 3 A 364 THR ALA LEU ALA THR ALA ALA THR THR ARG ALA ALA VAL
SEQRES 4 A 364 ALA ALA THR ALA PRO ALA ASP ASP TYR ALA ALA THR ARG
SEQRES 5 A 364 TYR PRO ILE ILE LEU VAL HIS GLY LEU THR GLY THR ASP
SEQRES 6 A 364 LYS TYR ALA GLY VAL LEU ASP TYR PHE TYR GLY ILE GLN
SEQRES 7 A 364 GLN ASP LEU GLN GLN ARG GLY ALA ASN VAL TYR VAL ALA
SEQRES 8 A 364 ASN LEU SER GLY PHE GLN SER ASP ASP GLY PRO ASN GLY
SEQRES 9 A 364 ARG GLY GLU GLN LEU LEU ALA TYR VAL LYS GLN VAL LEU
SEQRES 10 A 364 ALA GLN THR GLY ALA THR LYS VAL ASN LEU ILE GLY HIS
SEQRES 11 A 364 SER GLN GLY GLY LEU THR SER ARG TYR VAL ALA ALA VAL
SEQRES 12 A 364 ALA PRO GLU LEU VAL ALA SER VAL THR THR ILE GLY THR
SEQRES 13 A 364 PRO HIS ARG GLY SER GLU PHE ALA ASP PHE VAL GLN GLY
SEQRES 14 A 364 VAL LEU ALA TYR ASP PRO THR GLY LEU SER SER THR VAL
SEQRES 15 A 364 ILE ALA ALA PHE VAL ASN VAL PHE GLY ALA LEU THR ASN
SEQRES 16 A 364 SER THR HIS ASN THR ASN GLN ASP ALA LEU ALA ALA LEU
SEQRES 17 A 364 GLN THR LEU THR THR ALA ARG ALA ALA THR TYR ASN GLN
SEQRES 18 A 364 ASN TYR PRO SER ALA GLY LEU GLY ALA PRO GLY SER CYS
SEQRES 19 A 364 GLN THR GLY ALA PRO THR GLU THR VAL GLY GLY ASN THR
SEQRES 20 A 364 HIS LEU LEU TYR SER TRP ALA GLY THR ALA ILE GLN PRO
SEQRES 21 A 364 THR PHE SER SER LEU GLY VAL THR GLY ALA THR ASP THR
SEQRES 22 A 364 SER THR ILE PRO VAL VAL ASP PRO ALA ASN ALA LEU ASP
SEQRES 23 A 364 ALA SER THR LEU ALA LEU LEU GLY SER GLY THR VAL MET
SEQRES 24 A 364 VAL ASN ARG GLY SER GLY GLU ASN ASP GLY VAL VAL SER
SEQRES 25 A 364 LYS CYS SER ALA LEU PHE GLY GLN VAL LEU SER THR ARG
SEQRES 26 A 364 TYR LYS TRP ASN HIS VAL ASP GLU ILE ASN GLN LEU LEU
SEQRES 27 A 364 GLY VAL ARG GLY ALA TYR ALA GLU ASP PRO VAL ALA VAL
SEQRES 28 A 364 ILE ARG THR HIS ALA ASN ARG LEU LYS LEU ALA GLY VAL
SEQRES 1 B 364 MET ALA ARG ALA MET ARG SER ARG VAL VAL ALA GLY VAL
SEQRES 2 B 364 VAL ALA CYS ALA MET SER ALA ALA PRO PHE ALA GLY MET
SEQRES 3 B 364 THR ALA LEU ALA THR ALA ALA THR THR ARG ALA ALA VAL
SEQRES 4 B 364 ALA ALA THR ALA PRO ALA ASP ASP TYR ALA ALA THR ARG
SEQRES 5 B 364 TYR PRO ILE ILE LEU VAL HIS GLY LEU THR GLY THR ASP
SEQRES 6 B 364 LYS TYR ALA GLY VAL LEU ASP TYR PHE TYR GLY ILE GLN
SEQRES 7 B 364 GLN ASP LEU GLN GLN ARG GLY ALA ASN VAL TYR VAL ALA
SEQRES 8 B 364 ASN LEU SER GLY PHE GLN SER ASP ASP GLY PRO ASN GLY
SEQRES 9 B 364 ARG GLY GLU GLN LEU LEU ALA TYR VAL LYS GLN VAL LEU
SEQRES 10 B 364 ALA GLN THR GLY ALA THR LYS VAL ASN LEU ILE GLY HIS
SEQRES 11 B 364 SER GLN GLY GLY LEU THR SER ARG TYR VAL ALA ALA VAL
SEQRES 12 B 364 ALA PRO GLU LEU VAL ALA SER VAL THR THR ILE GLY THR
SEQRES 13 B 364 PRO HIS ARG GLY SER GLU PHE ALA ASP PHE VAL GLN GLY
SEQRES 14 B 364 VAL LEU ALA TYR ASP PRO THR GLY LEU SER SER THR VAL
SEQRES 15 B 364 ILE ALA ALA PHE VAL ASN VAL PHE GLY ALA LEU THR ASN
SEQRES 16 B 364 SER THR HIS ASN THR ASN GLN ASP ALA LEU ALA ALA LEU
SEQRES 17 B 364 GLN THR LEU THR THR ALA ARG ALA ALA THR TYR ASN GLN
SEQRES 18 B 364 ASN TYR PRO SER ALA GLY LEU GLY ALA PRO GLY SER CYS
SEQRES 19 B 364 GLN THR GLY ALA PRO THR GLU THR VAL GLY GLY ASN THR
SEQRES 20 B 364 HIS LEU LEU TYR SER TRP ALA GLY THR ALA ILE GLN PRO
SEQRES 21 B 364 THR PHE SER SER LEU GLY VAL THR GLY ALA THR ASP THR
SEQRES 22 B 364 SER THR ILE PRO VAL VAL ASP PRO ALA ASN ALA LEU ASP
SEQRES 23 B 364 ALA SER THR LEU ALA LEU LEU GLY SER GLY THR VAL MET
SEQRES 24 B 364 VAL ASN ARG GLY SER GLY GLU ASN ASP GLY VAL VAL SER
SEQRES 25 B 364 LYS CYS SER ALA LEU PHE GLY GLN VAL LEU SER THR ARG
SEQRES 26 B 364 TYR LYS TRP ASN HIS VAL ASP GLU ILE ASN GLN LEU LEU
SEQRES 27 B 364 GLY VAL ARG GLY ALA TYR ALA GLU ASP PRO VAL ALA VAL
SEQRES 28 B 364 ILE ARG THR HIS ALA ASN ARG LEU LYS LEU ALA GLY VAL
HET CA A 401 1
HET SO4 A 402 5
HET MPD A 403 8
HET MPD A 404 8
HET MPD A 405 8
HET MPD B 401 8
HET CA B 402 1
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 3 CA 2(CA 2+)
FORMUL 4 SO4 O4 S 2-
FORMUL 5 MPD 4(C6 H14 O2)
FORMUL 10 HOH *601(H2 O)
HELIX 1 AA1 ALA A 68 VAL A 70 5 3
HELIX 2 AA2 GLY A 76 ARG A 84 1 9
HELIX 3 AA3 GLY A 104 GLY A 121 1 18
HELIX 4 AA4 SER A 131 ALA A 144 1 14
HELIX 5 AA5 SER A 161 ALA A 172 1 12
HELIX 6 AA6 GLY A 177 ASN A 195 1 19
HELIX 7 AA7 ASP A 203 LEU A 211 1 9
HELIX 8 AA8 THR A 212 TYR A 223 1 12
HELIX 9 AA9 ASP A 280 ASP A 286 1 7
HELIX 10 AB1 ALA A 287 ASN A 301 1 15
HELIX 11 AB2 SER A 312 LEU A 317 1 6
HELIX 12 AB3 VAL A 331 ASN A 335 5 5
HELIX 13 AB4 ASP A 347 ALA A 362 1 16
HELIX 14 AB5 ALA B 68 VAL B 70 5 3
HELIX 15 AB6 GLY B 76 ARG B 84 1 9
HELIX 16 AB7 GLY B 104 GLY B 121 1 18
HELIX 17 AB8 SER B 131 ALA B 144 1 14
HELIX 18 AB9 SER B 161 ALA B 172 1 12
HELIX 19 AC1 GLY B 177 ASN B 195 1 19
HELIX 20 AC2 ASP B 203 LEU B 211 1 9
HELIX 21 AC3 THR B 212 TYR B 223 1 12
HELIX 22 AC4 ASP B 280 ASP B 286 1 7
HELIX 23 AC5 ALA B 287 ASN B 301 1 15
HELIX 24 AC6 SER B 312 LEU B 317 1 6
HELIX 25 AC7 VAL B 331 ASN B 335 5 5
HELIX 26 AC8 ASP B 347 ALA B 362 1 16
SHEET 1 AA1 6 VAL A 88 VAL A 90 0
SHEET 2 AA1 6 ILE A 55 VAL A 58 1 N ILE A 55 O TYR A 89
SHEET 3 AA1 6 VAL A 125 HIS A 130 1 O ILE A 128 N VAL A 58
SHEET 4 AA1 6 VAL A 148 ILE A 154 1 O ALA A 149 N VAL A 125
SHEET 5 AA1 6 ASN A 246 GLY A 255 1 O LEU A 249 N VAL A 151
SHEET 6 AA1 6 THR A 240 VAL A 243 -1 N GLU A 241 O HIS A 248
SHEET 1 AA2 6 VAL A 88 VAL A 90 0
SHEET 2 AA2 6 ILE A 55 VAL A 58 1 N ILE A 55 O TYR A 89
SHEET 3 AA2 6 VAL A 125 HIS A 130 1 O ILE A 128 N VAL A 58
SHEET 4 AA2 6 VAL A 148 ILE A 154 1 O ALA A 149 N VAL A 125
SHEET 5 AA2 6 ASN A 246 GLY A 255 1 O LEU A 249 N VAL A 151
SHEET 6 AA2 6 GLN A 320 TYR A 326 1 O GLN A 320 N LEU A 250
SHEET 1 AA3 2 LYS A 66 TYR A 67 0
SHEET 2 AA3 2 LEU A 71 ASP A 72 -1 O LEU A 71 N TYR A 67
SHEET 1 AA4 2 ILE A 258 SER A 264 0
SHEET 2 AA4 2 VAL A 267 ASP A 272 -1 O THR A 271 N GLN A 259
SHEET 1 AA5 6 VAL B 88 VAL B 90 0
SHEET 2 AA5 6 ILE B 55 VAL B 58 1 N ILE B 55 O TYR B 89
SHEET 3 AA5 6 VAL B 125 HIS B 130 1 O ASN B 126 N ILE B 56
SHEET 4 AA5 6 VAL B 148 ILE B 154 1 O ALA B 149 N VAL B 125
SHEET 5 AA5 6 ASN B 246 GLY B 255 1 O LEU B 249 N VAL B 151
SHEET 6 AA5 6 THR B 240 VAL B 243 -1 N GLU B 241 O HIS B 248
SHEET 1 AA6 6 VAL B 88 VAL B 90 0
SHEET 2 AA6 6 ILE B 55 VAL B 58 1 N ILE B 55 O TYR B 89
SHEET 3 AA6 6 VAL B 125 HIS B 130 1 O ASN B 126 N ILE B 56
SHEET 4 AA6 6 VAL B 148 ILE B 154 1 O ALA B 149 N VAL B 125
SHEET 5 AA6 6 ASN B 246 GLY B 255 1 O LEU B 249 N VAL B 151
SHEET 6 AA6 6 GLN B 320 TYR B 326 1 O GLN B 320 N LEU B 250
SHEET 1 AA7 2 LYS B 66 TYR B 67 0
SHEET 2 AA7 2 LEU B 71 ASP B 72 -1 O LEU B 71 N TYR B 67
SHEET 1 AA8 2 ILE B 258 SER B 264 0
SHEET 2 AA8 2 VAL B 267 ASP B 272 -1 O GLY B 269 N PHE B 262
SSBOND 1 CYS A 234 CYS A 314 1555 1555 2.04
SSBOND 2 CYS B 234 CYS B 314 1555 1555 2.04
LINK OD2 ASP A 286 CA CA A 401 1555 1555 2.36
LINK OD1 ASP A 332 CA CA A 401 1555 1555 2.32
LINK O GLN A 336 CA CA A 401 1555 1555 2.40
LINK O VAL A 340 CA CA A 401 1555 1555 2.31
LINK CA CA A 401 O HOH A 528 1555 1555 2.38
LINK CA CA A 401 O HOH A 584 1555 1555 2.38
LINK OD2 ASP B 286 CA CA B 402 1555 1555 2.35
LINK OD1 ASP B 332 CA CA B 402 1555 1555 2.34
LINK O GLN B 336 CA CA B 402 1555 1555 2.43
LINK O VAL B 340 CA CA B 402 1555 1555 2.33
LINK CA CA B 402 O HOH B 533 1555 1555 2.35
LINK CA CA B 402 O HOH B 600 1555 1555 2.32
CISPEP 1 GLN A 336 LEU A 337 0 -5.09
CISPEP 2 GLN B 336 LEU B 337 0 -4.39
CRYST1 160.643 69.210 51.322 90.00 98.53 90.00 C 1 2 1 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 0.006225 0.000000 0.000934 0.00000
SCALE2 0.000000 0.014449 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019703 0.00000
TER 2357 VAL A 364
TER 4714 VAL B 364
MASTER 401 0 7 26 32 0 0 6 5322 2 57 56
END |