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HEADER HYDROLASE 28-APR-20 6WPX
TITLE CRYSTAL STRUCTURE OF BACILLUS LICHENIFORMIS LIPASE BLEST2 IN PROPETIDE
TITLE 2 FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BLEST2;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS LICHENIFORMIS;
SOURCE 3 ORGANISM_TAXID: 1402;
SOURCE 4 GENE: DW032_06865;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASE, LIPASE, PROPETIDE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.NAKAMURA,A.S.GODOY,M.A.S.KADOWAKI,I.POLIKARPOV
REVDAT 1 09-JUN-21 6WPX 0
JRNL AUTH A.M.NAKAMURA,A.S.GODOY,M.A.S.KADOWAKI,I.POLIKARPOV
JRNL TITL THE FIRST STRUCTURE OF BACILLUS LICHENIFORMIS LIPASE BLEST2
JRNL TITL 2 IN ITS PROPEPTIDE AND MATURE FORM REVEALING MOLECULAR
JRNL TITL 3 DETAILS OF INHIBITION BY ITS C-TERMINAL DOMAINS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 59727
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.320
REMARK 3 FREE R VALUE TEST SET COUNT : 1983
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.05
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.52
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4344
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2230
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4200
REMARK 3 BIN R VALUE (WORKING SET) : 0.2220
REMARK 3 BIN FREE R VALUE : 0.2530
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.31
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 144
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7010
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 442
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.19760
REMARK 3 B22 (A**2) : 2.36010
REMARK 3 B33 (A**2) : -3.55780
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.250
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.202
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.162
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.196
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.161
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 7205 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 9760 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2428 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 185 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1058 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 7205 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 920 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 8995 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.06
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.60
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.72
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -4.4737 10.2828 -22.1752
REMARK 3 T TENSOR
REMARK 3 T11: -0.0815 T22: -0.0682
REMARK 3 T33: -0.0308 T12: 0.0407
REMARK 3 T13: -0.0300 T23: -0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 1.2898 L22: 1.8532
REMARK 3 L33: 1.0601 L12: -1.3081
REMARK 3 L13: -0.4904 L23: 0.9682
REMARK 3 S TENSOR
REMARK 3 S11: -0.1636 S12: -0.1198 S13: -0.1215
REMARK 3 S21: 0.1283 S22: 0.1105 S23: 0.1336
REMARK 3 S31: 0.0306 S32: 0.1022 S33: 0.0531
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -29.1220 10.4069 -62.0619
REMARK 3 T TENSOR
REMARK 3 T11: -0.0366 T22: -0.0221
REMARK 3 T33: -0.0894 T12: -0.0636
REMARK 3 T13: -0.0051 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 0.8474 L22: 1.6228
REMARK 3 L33: 0.3230 L12: 0.2188
REMARK 3 L13: -0.0592 L23: -0.2678
REMARK 3 S TENSOR
REMARK 3 S11: 0.0444 S12: -0.0760 S13: 0.0259
REMARK 3 S21: -0.0668 S22: 0.0162 S23: -0.0655
REMARK 3 S31: -0.0105 S32: -0.0201 S33: -0.0606
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6WPX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-APR-20.
REMARK 100 THE DEPOSITION ID IS D_1000248804.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAY-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LNLS
REMARK 200 BEAMLINE : W01B-MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.459
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59739
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.160
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.8800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: SAD
REMARK 200 SOFTWARE USED: CRANK2
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM CHLORIDE, 0.1 M TRIS PH
REMARK 280 8.0 AND 28% (W/V) POLYETHYLENE GLYCOL (PEG), VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 33.44500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.24300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.15750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.24300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.44500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.15750
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 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 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 LYS A 2
REMARK 465 LYS A 3
REMARK 465 LEU A 4
REMARK 465 VAL A 5
REMARK 465 LEU A 6
REMARK 465 LEU A 7
REMARK 465 MET A 8
REMARK 465 LEU A 9
REMARK 465 VAL A 10
REMARK 465 LEU A 11
REMARK 465 LEU A 12
REMARK 465 LEU A 13
REMARK 465 VAL A 14
REMARK 465 TYR A 15
REMARK 465 PRO A 16
REMARK 465 HIS A 17
REMARK 465 VAL A 18
REMARK 465 SER A 19
REMARK 465 LYS A 20
REMARK 465 ALA A 21
REMARK 465 GLY A 22
REMARK 465 GLY A 23
REMARK 465 PHE A 24
REMARK 465 LYS A 25
REMARK 465 GLY A 26
REMARK 465 GLY A 27
REMARK 465 GLY A 28
REMARK 465 THR A 283
REMARK 465 LYS A 284
REMARK 465 GLU A 285
REMARK 465 ASN A 286
REMARK 465 SER A 483
REMARK 465 PRO A 484
REMARK 465 LEU A 485
REMARK 465 SER A 486
REMARK 465 ASP A 487
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 LYS B 3
REMARK 465 LEU B 4
REMARK 465 VAL B 5
REMARK 465 LEU B 6
REMARK 465 LEU B 7
REMARK 465 MET B 8
REMARK 465 LEU B 9
REMARK 465 VAL B 10
REMARK 465 LEU B 11
REMARK 465 LEU B 12
REMARK 465 LEU B 13
REMARK 465 VAL B 14
REMARK 465 TYR B 15
REMARK 465 PRO B 16
REMARK 465 HIS B 17
REMARK 465 VAL B 18
REMARK 465 SER B 19
REMARK 465 LYS B 20
REMARK 465 ALA B 21
REMARK 465 GLY B 22
REMARK 465 GLY B 23
REMARK 465 PHE B 24
REMARK 465 LYS B 25
REMARK 465 GLY B 26
REMARK 465 GLY B 27
REMARK 465 THR B 283
REMARK 465 LYS B 284
REMARK 465 GLU B 285
REMARK 465 ASN B 286
REMARK 465 SER B 483
REMARK 465 PRO B 484
REMARK 465 LEU B 485
REMARK 465 SER B 486
REMARK 465 ASP B 487
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 328 CG CD CE NZ
REMARK 470 LYS A 374 CG CD CE NZ
REMARK 470 ARG A 399 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 400 CG CD OE1 OE2
REMARK 470 LYS A 442 CG CD CE NZ
REMARK 470 ARG B 399 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 400 CG CD OE1 OE2
REMARK 470 LYS B 476 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 119 -132.29 53.22
REMARK 500 ASP A 347 -123.85 47.57
REMARK 500 ASN A 361 61.02 39.35
REMARK 500 GLU A 400 156.09 -48.68
REMARK 500 SER B 119 -131.98 51.86
REMARK 500 ASP B 347 -114.35 43.08
REMARK 500 ASN B 361 62.27 38.34
REMARK 500 THR B 398 -90.61 -113.43
REMARK 500 ARG B 399 -151.00 -71.28
REMARK 500 GLU B 400 -84.07 -107.15
REMARK 500 SER B 401 54.57 16.46
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 IOD A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 511
DBREF1 6WPX A 1 487 UNP A0A415J7C9_BACLI
DBREF2 6WPX A A0A415J7C9 1 487
DBREF1 6WPX B 1 487 UNP A0A415J7C9_BACLI
DBREF2 6WPX B A0A415J7C9 1 487
SEQRES 1 A 487 MET LYS LYS LEU VAL LEU LEU MET LEU VAL LEU LEU LEU
SEQRES 2 A 487 VAL TYR PRO HIS VAL SER LYS ALA GLY GLY PHE LYS GLY
SEQRES 3 A 487 GLY GLY GLY ASN PRO GLY TYR TRP PHE ALA GLY ASP PRO
SEQRES 4 A 487 VAL GLU HIS PRO ASP PRO ALA LYS PRO PRO ILE VAL PHE
SEQRES 5 A 487 VAL HIS GLY LEU ASN GLY SER SER SER ALA TRP PHE ASP
SEQRES 6 A 487 GLU ASN ASP MET ALA GLU GLN ALA TRP LYS ASN GLY TYR
SEQRES 7 A 487 ASP ALA ALA PHE ILE ASP LEU HIS PRO ASP LYS ASP MET
SEQRES 8 A 487 GLN ASP ASN GLY ALA MET LEU ALA ALA LYS LEU ARG GLU
SEQRES 9 A 487 ILE TYR GLN TYR PHE GLY ARG LYS VAL ILE LEU VAL SER
SEQRES 10 A 487 TYR SER LYS GLY GLY ILE ASP SER GLN SER ALA LEU ILE
SEQRES 11 A 487 HIS HIS ASN ALA TYR HIS TYR VAL GLU ARG VAL ILE THR
SEQRES 12 A 487 LEU GLY THR PRO HIS HIS GLY SER GLN LEU ALA ASP LEU
SEQRES 13 A 487 ALA TYR SER ASN TRP ALA GLY TRP LEU ALA ASP ILE LEU
SEQRES 14 A 487 GLY GLN LYS ASN ASP ALA VAL TYR SER LEU GLN THR GLY
SEQRES 15 A 487 PHE MET LYS SER PHE ARG ASP GLN THR ASP ASN HIS PRO
SEQRES 16 A 487 ASN ARG LEU LYS THR LYS TYR PHE THR LEU ALA GLY ASN
SEQRES 17 A 487 LYS ILE GLY GLY PHE GLY SER ALA LEU PHE PHE GLY GLY
SEQRES 18 A 487 VAL TYR LEU ASN MET PHE GLY GLU ASN ASP GLY ALA VAL
SEQRES 19 A 487 THR GLU LYS ASN ALA ARG LEU PRO TYR ALA THR ASN LEU
SEQRES 20 A 487 ASP THR GLY LYS TRP ASP HIS PHE SER ILE ILE LYS GLY
SEQRES 21 A 487 ASN LEU THR PHE PRO VAL PHE MET PRO LEU LEU THR ILE
SEQRES 22 A 487 GLN ALA ASN ALA ASN GLU THR ALA ALA THR LYS GLU ASN
SEQRES 23 A 487 LEU SER TYR PRO PHE ILE ARG GLY GLY GLU ASN HIS GLY
SEQRES 24 A 487 LEU ARG GLU GLU GLU PHE ALA VAL GLU LYS GLY VAL LYS
SEQRES 25 A 487 GLU ILE THR VAL HIS TRP LEU SER ASN HIS SER SER GLY
SEQRES 26 A 487 ASN ILE LYS LEU THR ASP PRO ARG GLY LYS PRO PHE LYS
SEQRES 27 A 487 ASP PHE SER ILE ALA LYS THR ALA ASP VAL PHE GLU GLY
SEQRES 28 A 487 GLY PHE VAL HIS SER ALA ALA ILE LYS ASN PRO ALA ALA
SEQRES 29 A 487 GLY THR TRP LYS ILE ALA SER SER VAL LYS GLN LYS GLU
SEQRES 30 A 487 ALA PHE LEU PHE ILE VAL THR PHE ASP SER PRO LEU ASN
SEQRES 31 A 487 GLN GLN ILE LYS ASN ALA VAL THR ARG GLU SER SER ASN
SEQRES 32 A 487 LEU ALA ASN VAL LYS ALA SER VAL ARG SER ILE ARG TYR
SEQRES 33 A 487 GLU ASN GLY LYS GLN ALA GLU LYS LYS SER LEU LYS PRO
SEQRES 34 A 487 ALA SER ILE ASN ALA LEU GLN ASN SER LEU SER PHE LYS
SEQRES 35 A 487 LYS ALA GLY MET TYR SER VAL THR ILE ASP LEU SER GLY
SEQRES 36 A 487 LYS THR ALA ASP ASN SER PRO PHE ASN ARG THR ILE ILE
SEQRES 37 A 487 ARG SER ILE TYR VAL ASN ASP LYS GLY GLU LYS PHE GLU
SEQRES 38 A 487 ASN SER PRO LEU SER ASP
SEQRES 1 B 487 MET LYS LYS LEU VAL LEU LEU MET LEU VAL LEU LEU LEU
SEQRES 2 B 487 VAL TYR PRO HIS VAL SER LYS ALA GLY GLY PHE LYS GLY
SEQRES 3 B 487 GLY GLY GLY ASN PRO GLY TYR TRP PHE ALA GLY ASP PRO
SEQRES 4 B 487 VAL GLU HIS PRO ASP PRO ALA LYS PRO PRO ILE VAL PHE
SEQRES 5 B 487 VAL HIS GLY LEU ASN GLY SER SER SER ALA TRP PHE ASP
SEQRES 6 B 487 GLU ASN ASP MET ALA GLU GLN ALA TRP LYS ASN GLY TYR
SEQRES 7 B 487 ASP ALA ALA PHE ILE ASP LEU HIS PRO ASP LYS ASP MET
SEQRES 8 B 487 GLN ASP ASN GLY ALA MET LEU ALA ALA LYS LEU ARG GLU
SEQRES 9 B 487 ILE TYR GLN TYR PHE GLY ARG LYS VAL ILE LEU VAL SER
SEQRES 10 B 487 TYR SER LYS GLY GLY ILE ASP SER GLN SER ALA LEU ILE
SEQRES 11 B 487 HIS HIS ASN ALA TYR HIS TYR VAL GLU ARG VAL ILE THR
SEQRES 12 B 487 LEU GLY THR PRO HIS HIS GLY SER GLN LEU ALA ASP LEU
SEQRES 13 B 487 ALA TYR SER ASN TRP ALA GLY TRP LEU ALA ASP ILE LEU
SEQRES 14 B 487 GLY GLN LYS ASN ASP ALA VAL TYR SER LEU GLN THR GLY
SEQRES 15 B 487 PHE MET LYS SER PHE ARG ASP GLN THR ASP ASN HIS PRO
SEQRES 16 B 487 ASN ARG LEU LYS THR LYS TYR PHE THR LEU ALA GLY ASN
SEQRES 17 B 487 LYS ILE GLY GLY PHE GLY SER ALA LEU PHE PHE GLY GLY
SEQRES 18 B 487 VAL TYR LEU ASN MET PHE GLY GLU ASN ASP GLY ALA VAL
SEQRES 19 B 487 THR GLU LYS ASN ALA ARG LEU PRO TYR ALA THR ASN LEU
SEQRES 20 B 487 ASP THR GLY LYS TRP ASP HIS PHE SER ILE ILE LYS GLY
SEQRES 21 B 487 ASN LEU THR PHE PRO VAL PHE MET PRO LEU LEU THR ILE
SEQRES 22 B 487 GLN ALA ASN ALA ASN GLU THR ALA ALA THR LYS GLU ASN
SEQRES 23 B 487 LEU SER TYR PRO PHE ILE ARG GLY GLY GLU ASN HIS GLY
SEQRES 24 B 487 LEU ARG GLU GLU GLU PHE ALA VAL GLU LYS GLY VAL LYS
SEQRES 25 B 487 GLU ILE THR VAL HIS TRP LEU SER ASN HIS SER SER GLY
SEQRES 26 B 487 ASN ILE LYS LEU THR ASP PRO ARG GLY LYS PRO PHE LYS
SEQRES 27 B 487 ASP PHE SER ILE ALA LYS THR ALA ASP VAL PHE GLU GLY
SEQRES 28 B 487 GLY PHE VAL HIS SER ALA ALA ILE LYS ASN PRO ALA ALA
SEQRES 29 B 487 GLY THR TRP LYS ILE ALA SER SER VAL LYS GLN LYS GLU
SEQRES 30 B 487 ALA PHE LEU PHE ILE VAL THR PHE ASP SER PRO LEU ASN
SEQRES 31 B 487 GLN GLN ILE LYS ASN ALA VAL THR ARG GLU SER SER ASN
SEQRES 32 B 487 LEU ALA ASN VAL LYS ALA SER VAL ARG SER ILE ARG TYR
SEQRES 33 B 487 GLU ASN GLY LYS GLN ALA GLU LYS LYS SER LEU LYS PRO
SEQRES 34 B 487 ALA SER ILE ASN ALA LEU GLN ASN SER LEU SER PHE LYS
SEQRES 35 B 487 LYS ALA GLY MET TYR SER VAL THR ILE ASP LEU SER GLY
SEQRES 36 B 487 LYS THR ALA ASP ASN SER PRO PHE ASN ARG THR ILE ILE
SEQRES 37 B 487 ARG SER ILE TYR VAL ASN ASP LYS GLY GLU LYS PHE GLU
SEQRES 38 B 487 ASN SER PRO LEU SER ASP
HET IOD A 501 1
HET IOD A 502 1
HET IOD A 503 1
HET IOD A 504 1
HET IOD A 505 1
HET IOD A 506 1
HET IOD A 507 1
HET IOD A 508 1
HET IOD A 509 1
HET IOD A 510 1
HET IOD A 511 1
HET IOD A 512 1
HET IOD A 513 1
HET IOD B 501 1
HET IOD B 502 1
HET IOD B 503 1
HET IOD B 504 1
HET IOD B 505 1
HET IOD B 506 1
HET IOD B 507 1
HET IOD B 508 1
HET IOD B 509 1
HET IOD B 510 1
HET IOD B 511 1
HETNAM IOD IODIDE ION
FORMUL 3 IOD 24(I 1-)
FORMUL 27 HOH *442(H2 O)
HELIX 1 AA1 SER A 59 PHE A 64 5 6
HELIX 2 AA2 ASP A 68 ASN A 76 1 9
HELIX 3 AA3 ASP A 90 GLY A 110 1 21
HELIX 4 AA4 LYS A 120 HIS A 132 1 13
HELIX 5 AA5 ASN A 133 HIS A 136 5 4
HELIX 6 AA6 SER A 151 TYR A 158 1 8
HELIX 7 AA7 ALA A 162 GLY A 170 1 9
HELIX 8 AA8 ASN A 173 LEU A 179 1 7
HELIX 9 AA9 GLN A 180 ASP A 192 1 13
HELIX 10 AB1 HIS A 194 THR A 200 5 7
HELIX 11 AB2 LEU A 217 ASN A 225 1 9
HELIX 12 AB3 GLU A 236 ARG A 240 5 5
HELIX 13 AB4 PHE A 255 ILE A 258 5 4
HELIX 14 AB5 LYS A 259 MET A 268 1 10
HELIX 15 AB6 PRO A 269 THR A 272 5 4
HELIX 16 AB7 ALA A 346 GLU A 350 5 5
HELIX 17 AB8 PRO A 388 THR A 398 1 11
HELIX 18 AB9 ILE A 432 LEU A 439 1 8
HELIX 19 AC1 SER B 59 PHE B 64 5 6
HELIX 20 AC2 ASP B 68 ASN B 76 1 9
HELIX 21 AC3 ASP B 90 GLY B 110 1 21
HELIX 22 AC4 LYS B 120 HIS B 132 1 13
HELIX 23 AC5 ASN B 133 HIS B 136 5 4
HELIX 24 AC6 SER B 151 TYR B 158 1 8
HELIX 25 AC7 ALA B 162 LEU B 169 1 8
HELIX 26 AC8 ASN B 173 LEU B 179 1 7
HELIX 27 AC9 GLN B 180 ASP B 192 1 13
HELIX 28 AD1 HIS B 194 THR B 200 5 7
HELIX 29 AD2 LEU B 217 ASN B 225 1 9
HELIX 30 AD3 GLU B 236 ARG B 240 5 5
HELIX 31 AD4 PHE B 255 ILE B 258 5 4
HELIX 32 AD5 LYS B 259 MET B 268 1 10
HELIX 33 AD6 PRO B 269 THR B 272 5 4
HELIX 34 AD7 ALA B 346 GLU B 350 5 5
HELIX 35 AD8 LEU B 389 THR B 398 1 10
HELIX 36 AD9 ALA B 434 LEU B 439 1 6
SHEET 1 AA1 7 TRP A 34 ALA A 36 0
SHEET 2 AA1 7 ALA A 80 ILE A 83 -1 O PHE A 82 N PHE A 35
SHEET 3 AA1 7 ILE A 50 VAL A 53 1 N PHE A 52 O ALA A 81
SHEET 4 AA1 7 VAL A 113 TYR A 118 1 O ILE A 114 N VAL A 51
SHEET 5 AA1 7 VAL A 138 LEU A 144 1 O ILE A 142 N LEU A 115
SHEET 6 AA1 7 LYS A 201 LEU A 205 1 O PHE A 203 N THR A 143
SHEET 7 AA1 7 THR A 245 ASN A 246 1 O THR A 245 N TYR A 202
SHEET 1 AA2 5 PRO A 290 ASN A 297 0
SHEET 2 AA2 5 GLU A 377 ASP A 386 -1 O PHE A 381 N ARG A 293
SHEET 3 AA2 5 GLU A 313 SER A 320 -1 N LEU A 319 O LEU A 380
SHEET 4 AA2 5 PHE A 353 LYS A 360 -1 O PHE A 353 N SER A 320
SHEET 5 AA2 5 SER A 341 LYS A 344 -1 N SER A 341 O SER A 356
SHEET 1 AA3 4 LEU A 300 VAL A 307 0
SHEET 2 AA3 4 GLY A 365 SER A 372 -1 O TRP A 367 N PHE A 305
SHEET 3 AA3 4 ASN A 326 THR A 330 -1 N THR A 330 O LYS A 368
SHEET 4 AA3 4 PRO A 336 PHE A 337 -1 O PHE A 337 N LEU A 329
SHEET 1 AA4 5 LYS A 420 SER A 431 0
SHEET 2 AA4 5 ALA A 405 GLU A 417 -1 N ARG A 415 O GLU A 423
SHEET 3 AA4 5 GLY A 445 LYS A 456 -1 O THR A 450 N ARG A 412
SHEET 4 AA4 5 PRO A 462 VAL A 473 -1 O ILE A 471 N TYR A 447
SHEET 5 AA4 5 LYS A 479 PHE A 480 -1 O PHE A 480 N TYR A 472
SHEET 1 AA5 7 TRP B 34 ALA B 36 0
SHEET 2 AA5 7 ALA B 80 ILE B 83 -1 O PHE B 82 N PHE B 35
SHEET 3 AA5 7 ILE B 50 VAL B 53 1 N PHE B 52 O ALA B 81
SHEET 4 AA5 7 VAL B 113 TYR B 118 1 O ILE B 114 N VAL B 51
SHEET 5 AA5 7 VAL B 138 LEU B 144 1 O ILE B 142 N LEU B 115
SHEET 6 AA5 7 LYS B 201 LEU B 205 1 O PHE B 203 N THR B 143
SHEET 7 AA5 7 THR B 245 ASN B 246 1 O THR B 245 N TYR B 202
SHEET 1 AA6 5 PRO B 290 ASN B 297 0
SHEET 2 AA6 5 GLU B 377 ASP B 386 -1 O PHE B 381 N ARG B 293
SHEET 3 AA6 5 GLU B 313 SER B 320 -1 N LEU B 319 O LEU B 380
SHEET 4 AA6 5 PHE B 353 LYS B 360 -1 O PHE B 353 N SER B 320
SHEET 5 AA6 5 SER B 341 LYS B 344 -1 N SER B 341 O SER B 356
SHEET 1 AA7 4 LEU B 300 VAL B 307 0
SHEET 2 AA7 4 GLY B 365 SER B 372 -1 O TRP B 367 N PHE B 305
SHEET 3 AA7 4 ASN B 326 THR B 330 -1 N ASN B 326 O SER B 372
SHEET 4 AA7 4 PRO B 336 PHE B 337 -1 O PHE B 337 N LEU B 329
SHEET 1 AA8 5 LYS B 420 SER B 431 0
SHEET 2 AA8 5 ALA B 405 GLU B 417 -1 N VAL B 411 O LEU B 427
SHEET 3 AA8 5 GLY B 445 LYS B 456 -1 O THR B 450 N ARG B 412
SHEET 4 AA8 5 PRO B 462 VAL B 473 -1 O ILE B 467 N ILE B 451
SHEET 5 AA8 5 LYS B 479 PHE B 480 -1 O PHE B 480 N TYR B 472
SITE 1 AC1 2 SER A 426 GLN B 421
SITE 1 AC2 1 ARG A 111
SITE 1 AC3 3 HIS A 149 LEU A 241 PRO A 242
SITE 1 AC4 3 GLY A 55 ALA A 62 TYR A 118
SITE 1 AC5 3 TYR A 289 ASN A 390 ARG A 465
SITE 1 AC6 3 LYS A 344 LYS A 456 ASN A 460
SITE 1 AC7 2 ASN A 160 ARG A 412
SITE 1 AC8 2 GLN A 92 SER A 127
SITE 1 AC9 2 TYR A 177 ASN A 418
SITE 1 AD1 3 SER A 413 ARG A 415 GLU A 423
SITE 1 AD2 3 ALA A 216 GLY A 220 ALA A 346
SITE 1 AD3 3 TYR B 289 ASN B 390 ARG B 465
SITE 1 AD4 4 HIS B 149 LEU B 241 PRO B 242 HOH B 628
SITE 1 AD5 3 GLN A 421 SER B 426 LYS B 428
SITE 1 AD6 2 ASN B 160 ARG B 412
SITE 1 AD7 4 GLY B 55 GLY B 58 ALA B 62 TYR B 118
SITE 1 AD8 2 GLN B 92 SER B 127
SITE 1 AD9 2 ALA B 216 GLY B 220
SITE 1 AE1 2 TYR B 177 ASN B 418
SITE 1 AE2 2 SER B 413 GLU B 423
CRYST1 66.890 78.315 166.486 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014950 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012769 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006007 0.00000
TER 3505 ASN A 482
TER 7025 ASN B 482
MASTER 454 0 24 36 42 0 20 6 7476 2 0 76
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