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HEADER HYDROLASE 19-JUN-18 6GUL
TITLE SIDEROPHORE HYDROLASE ESTB MUTANT E211Q FROM ASPERGILLUS FUMIGATUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIDEROPHORE ESTERASE IROE-LIKE, PUTATIVE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS FUMIGATUS AF293;
SOURCE 3 ORGANISM_TAXID: 330879;
SOURCE 4 GENE: AFUA_3G03660;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA-HYDROLASE, SIDEROPHORE, HYDROLYSIS, FUNGI, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.ECKER,H.HAAS,M.GROLL,E.M.HUBER
REVDAT 1 15-AUG-18 6GUL 0
JRNL AUTH F.ECKER,H.HAAS,M.GROLL,E.HUBER
JRNL TITL IRON SCAVENGING IN ASPERGILLUS SPECIES: STRUCTURAL AND
JRNL TITL 2 BIOCHEMICAL INSIGHTS INTO FUNGAL SIDEROPHORE ESTERASES.
JRNL REF ANGEW. CHEM. INT. ED. ENGL. 2018
JRNL REFN ESSN 1521-3773
JRNL PMID 30070018
JRNL DOI 10.1002/ANIE.201807093
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0230
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 27731
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1460
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1977
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.30
REMARK 3 BIN R VALUE (WORKING SET) : 0.2340
REMARK 3 BIN FREE R VALUE SET COUNT : 104
REMARK 3 BIN FREE R VALUE : 0.3410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4457
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
REMARK 3 SOLVENT ATOMS : 184
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.99000
REMARK 3 B22 (A**2) : 0.64000
REMARK 3 B33 (A**2) : -1.63000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.243
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.168
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.330
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.891
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4643 ; 0.003 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 3997 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6325 ; 0.731 ; 1.654
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9367 ; 0.670 ; 1.631
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 565 ; 5.203 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 249 ;33.261 ;21.004
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 694 ;11.520 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;11.419 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 582 ; 0.030 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5251 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 929 ; 0.001 ; 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): 2257 ; 0.597 ; 3.469
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2256 ; 0.596 ; 3.468
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2817 ; 0.867 ; 5.195
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2818 ; 0.867 ; 5.196
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2386 ; 0.511 ; 3.595
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2374 ; 0.507 ; 3.582
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3489 ; 0.749 ; 5.329
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5203 ; 1.812 ;40.106
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5175 ; 1.737 ;40.033
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 8640 ; 0.157 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 97 ;25.643 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 8592 ;16.941 ; 5.000
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 : NULL
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
REMARK 4
REMARK 4 6GUL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUN-18.
REMARK 100 THE DEPOSITION ID IS D_1200010578.
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 : ESRF
REMARK 200 BEAMLINE : ID30B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97264
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29327
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 45.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.41700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.000
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: 6GUD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M AMMONIUM SULFATE, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
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 27.33500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.27500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.91500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.27500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.33500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.91500
REMARK 290 SMTRY3 4 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: 5910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 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 GLY A 1
REMARK 465 SER A 2
REMARK 465 ASP A 3
REMARK 465 ARG A 4
REMARK 465 LYS A 194
REMARK 465 VAL A 195
REMARK 465 SER A 196
REMARK 465 HIS A 197
REMARK 465 ASP A 198
REMARK 465 GLY A 292
REMARK 465 GLY B 1
REMARK 465 SER B 2
REMARK 465 ASP B 3
REMARK 465 ARG B 4
REMARK 465 PRO B 5
REMARK 465 LYS B 194
REMARK 465 VAL B 195
REMARK 465 SER B 196
REMARK 465 HIS B 197
REMARK 465 ASP B 198
REMARK 465 GLY B 292
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 148 -109.14 61.66
REMARK 500 GLU A 191 33.82 -95.25
REMARK 500 SER B 148 -108.12 64.48
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 GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 305
DBREF 6GUL A 3 292 UNP Q4WF29 Q4WF29_ASPFU 3 292
DBREF 6GUL B 3 292 UNP Q4WF29 Q4WF29_ASPFU 3 292
SEQADV 6GUL GLY A 1 UNP Q4WF29 EXPRESSION TAG
SEQADV 6GUL SER A 2 UNP Q4WF29 EXPRESSION TAG
SEQADV 6GUL GLN A 211 UNP Q4WF29 GLU 211 ENGINEERED MUTATION
SEQADV 6GUL GLY B 1 UNP Q4WF29 EXPRESSION TAG
SEQADV 6GUL SER B 2 UNP Q4WF29 EXPRESSION TAG
SEQADV 6GUL GLN B 211 UNP Q4WF29 GLU 211 ENGINEERED MUTATION
SEQRES 1 A 292 GLY SER ASP ARG PRO THR PRO VAL PRO LEU PRO ASN SER
SEQRES 2 A 292 GLU GLN PHE TYR LEU GLU ASN ASP ARG GLY GLU PRO TYR
SEQRES 3 A 292 LEU ILE GLN VAL SER TRP PRO LEU HIS TRP GLU ASP LYS
SEQRES 4 A 292 GLN THR GLY ARG GLY PRO LEU PRO ILE ILE TYR ILE VAL
SEQRES 5 A 292 ASP GLY ASN ALA LEU PHE LEU THR ALA THR GLU ALA ALA
SEQRES 6 A 292 TRP ARG ARG ALA ALA ALA SER HIS PHE ALA GLY GLY GLY
SEQRES 7 A 292 ILE ILE VAL ALA ILE GLY TYR PRO LEU LYS GLY LYS LEU
SEQRES 8 A 292 TYR ASP ALA ARG ARG ARG SER PHE ASP LEU THR PRO PRO
SEQRES 9 A 292 THR ALA CYS ALA PRO VAL GLY TYR GLY GLY ALA ASP VAL
SEQRES 10 A 292 PHE LEU ASP PHE ILE GLU ASN SER VAL ARG PRO ALA VAL
SEQRES 11 A 292 GLN ALA ARG PHE PRO GLN VAL SER LEU ALA ARG GLU ALA
SEQRES 12 A 292 LEU TYR GLY HIS SER TYR GLY GLY LEU LEU ALA LEU HIS
SEQRES 13 A 292 ALA LEU PHE THR ARG PRO GLN SER PHE ASP CYS TYR ILE
SEQRES 14 A 292 ALA SER SER PRO SER ILE TRP TRP ASN SER LEU CYS ILE
SEQRES 15 A 292 LEU HIS GLU ALA LYS ALA PHE VAL GLU THR LYS LYS VAL
SEQRES 16 A 292 SER HIS ASP GLN SER PRO SER LEU MET VAL SER TRP GLY
SEQRES 17 A 292 SER TRP GLN GLN HIS PRO PRO ARG TRP ALA ASP GLU LEU
SEQRES 18 A 292 LEU ASP HIS TYR GLU ALA ARG LYS ARG THR ALA ALA GLU
SEQRES 19 A 292 LEU ARG MET ALA ASP ASN ALA LEU ASP LEU CYS ALA MET
SEQRES 20 A 292 LEU HIS GLY CYS SER ARG LEU HIS ALA LEU ILE LYS THR
SEQRES 21 A 292 GLU TYR GLU GLY GLU ASP HIS THR SER VAL MET SER CYS
SEQRES 22 A 292 SER VAL SER ARG GLY LEU THR MET PHE PHE GLU ASP TRP
SEQRES 23 A 292 PRO PHE HIS GLN SER GLY
SEQRES 1 B 292 GLY SER ASP ARG PRO THR PRO VAL PRO LEU PRO ASN SER
SEQRES 2 B 292 GLU GLN PHE TYR LEU GLU ASN ASP ARG GLY GLU PRO TYR
SEQRES 3 B 292 LEU ILE GLN VAL SER TRP PRO LEU HIS TRP GLU ASP LYS
SEQRES 4 B 292 GLN THR GLY ARG GLY PRO LEU PRO ILE ILE TYR ILE VAL
SEQRES 5 B 292 ASP GLY ASN ALA LEU PHE LEU THR ALA THR GLU ALA ALA
SEQRES 6 B 292 TRP ARG ARG ALA ALA ALA SER HIS PHE ALA GLY GLY GLY
SEQRES 7 B 292 ILE ILE VAL ALA ILE GLY TYR PRO LEU LYS GLY LYS LEU
SEQRES 8 B 292 TYR ASP ALA ARG ARG ARG SER PHE ASP LEU THR PRO PRO
SEQRES 9 B 292 THR ALA CYS ALA PRO VAL GLY TYR GLY GLY ALA ASP VAL
SEQRES 10 B 292 PHE LEU ASP PHE ILE GLU ASN SER VAL ARG PRO ALA VAL
SEQRES 11 B 292 GLN ALA ARG PHE PRO GLN VAL SER LEU ALA ARG GLU ALA
SEQRES 12 B 292 LEU TYR GLY HIS SER TYR GLY GLY LEU LEU ALA LEU HIS
SEQRES 13 B 292 ALA LEU PHE THR ARG PRO GLN SER PHE ASP CYS TYR ILE
SEQRES 14 B 292 ALA SER SER PRO SER ILE TRP TRP ASN SER LEU CYS ILE
SEQRES 15 B 292 LEU HIS GLU ALA LYS ALA PHE VAL GLU THR LYS LYS VAL
SEQRES 16 B 292 SER HIS ASP GLN SER PRO SER LEU MET VAL SER TRP GLY
SEQRES 17 B 292 SER TRP GLN GLN HIS PRO PRO ARG TRP ALA ASP GLU LEU
SEQRES 18 B 292 LEU ASP HIS TYR GLU ALA ARG LYS ARG THR ALA ALA GLU
SEQRES 19 B 292 LEU ARG MET ALA ASP ASN ALA LEU ASP LEU CYS ALA MET
SEQRES 20 B 292 LEU HIS GLY CYS SER ARG LEU HIS ALA LEU ILE LYS THR
SEQRES 21 B 292 GLU TYR GLU GLY GLU ASP HIS THR SER VAL MET SER CYS
SEQRES 22 B 292 SER VAL SER ARG GLY LEU THR MET PHE PHE GLU ASP TRP
SEQRES 23 B 292 PRO PHE HIS GLN SER GLY
HET GOL A 301 6
HET SO4 A 302 5
HET CL A 303 1
HET GOL B 301 6
HET GOL B 302 6
HET SO4 B 303 5
HET SO4 B 304 5
HET CL B 305 1
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 3(C3 H8 O3)
FORMUL 4 SO4 3(O4 S 2-)
FORMUL 5 CL 2(CL 1-)
FORMUL 11 HOH *184(H2 O)
HELIX 1 AA1 ASP A 38 GLY A 42 5 5
HELIX 2 AA2 GLY A 54 ALA A 56 5 3
HELIX 3 AA3 LEU A 57 ARG A 68 1 12
HELIX 4 AA4 ALA A 69 ALA A 71 5 3
HELIX 5 AA5 ASP A 93 LEU A 101 1 9
HELIX 6 AA6 GLY A 114 SER A 125 1 12
HELIX 7 AA7 SER A 125 PHE A 134 1 10
HELIX 8 AA8 SER A 148 ARG A 161 1 14
HELIX 9 AA9 TRP A 176 CYS A 181 1 6
HELIX 10 AB1 CYS A 181 GLU A 191 1 11
HELIX 11 AB2 LEU A 221 ARG A 236 1 16
HELIX 12 AB3 ARG A 236 HIS A 249 1 14
HELIX 13 AB4 SER A 269 ASP A 285 1 17
HELIX 14 AB5 ASP B 53 ARG B 68 1 16
HELIX 15 AB6 ALA B 69 ALA B 71 5 3
HELIX 16 AB7 ASP B 93 LEU B 101 1 9
HELIX 17 AB8 GLY B 114 SER B 125 1 12
HELIX 18 AB9 SER B 125 PHE B 134 1 10
HELIX 19 AC1 SER B 148 ARG B 161 1 14
HELIX 20 AC2 TRP B 176 CYS B 181 1 6
HELIX 21 AC3 CYS B 181 THR B 192 1 12
HELIX 22 AC4 SER B 209 HIS B 213 1 5
HELIX 23 AC5 LEU B 221 ARG B 236 1 16
HELIX 24 AC6 ARG B 236 LEU B 248 1 13
HELIX 25 AC7 SER B 269 ASP B 285 1 17
SHEET 1 AA1 8 SER A 13 GLU A 19 0
SHEET 2 AA1 8 PRO A 25 SER A 31 -1 O VAL A 30 N GLU A 14
SHEET 3 AA1 8 ILE A 79 GLY A 84 -1 O ALA A 82 N GLN A 29
SHEET 4 AA1 8 GLY A 44 VAL A 52 1 N ILE A 51 O VAL A 81
SHEET 5 AA1 8 VAL A 137 HIS A 147 1 O TYR A 145 N TYR A 50
SHEET 6 AA1 8 CYS A 167 SER A 171 1 O SER A 171 N GLY A 146
SHEET 7 AA1 8 SER A 202 GLY A 208 1 O MET A 204 N TYR A 168
SHEET 8 AA1 8 ALA A 256 TYR A 262 1 O ILE A 258 N VAL A 205
SHEET 1 AA2 8 SER B 13 GLU B 19 0
SHEET 2 AA2 8 PRO B 25 SER B 31 -1 O VAL B 30 N GLU B 14
SHEET 3 AA2 8 ILE B 79 GLY B 84 -1 O ALA B 82 N GLN B 29
SHEET 4 AA2 8 GLY B 44 VAL B 52 1 N ILE B 51 O VAL B 81
SHEET 5 AA2 8 VAL B 137 HIS B 147 1 O TYR B 145 N TYR B 50
SHEET 6 AA2 8 CYS B 167 SER B 171 1 O ILE B 169 N LEU B 144
SHEET 7 AA2 8 SER B 202 GLY B 208 1 O MET B 204 N TYR B 168
SHEET 8 AA2 8 ALA B 256 TYR B 262 1 O ALA B 256 N LEU B 203
CISPEP 1 TRP A 286 PRO A 287 0 -1.54
CISPEP 2 TRP B 286 PRO B 287 0 -1.79
SITE 1 AC1 6 ASN A 55 LEU A 87 LYS A 90 HOH A 419
SITE 2 AC1 6 HOH A 424 HOH B 401
SITE 1 AC2 5 ALA A 71 SER A 72 HOH A 432 HIS B 267
SITE 2 AC2 5 HOH B 469
SITE 1 AC3 1 CYS A 107
SITE 1 AC4 2 GLN B 199 HIS B 255
SITE 1 AC5 6 HOH A 402 ASN B 55 LEU B 87 LYS B 90
SITE 2 AC5 6 HOH B 409 HOH B 412
SITE 1 AC6 4 ALA A 70 LYS B 90 LEU B 91 TYR B 92
SITE 1 AC7 5 HIS A 267 THR A 268 HOH A 441 ALA B 71
SITE 2 AC7 5 SER B 72
SITE 1 AC8 2 CYS B 107 ASN B 178
CRYST1 54.670 91.830 130.550 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 0.018292 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010890 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007660 0.00000
TER 2239 SER A 291
TER 4474 SER B 291
MASTER 320 0 8 25 16 0 12 6 4676 2 33 46
END |