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HEADER HYDROLASE 19-JUN-18 6GUP
TITLE SIDEROPHORE HYDROLASE ESTB FROM ASPERGILLUS FUMIGATUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIDEROPHORE BIOSYNTHESIS LIPASE/ESTERASE, PUTATIVE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS FUMIGATUS;
SOURCE 3 ORGANISM_TAXID: 746128;
SOURCE 4 GENE: AFUA_3G03390;
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 6GUP 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. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 50664
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2666
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3701
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.3330
REMARK 3 BIN FREE R VALUE SET COUNT : 195
REMARK 3 BIN FREE R VALUE : 0.3900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5105
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 266
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.69000
REMARK 3 B22 (A**2) : -2.52000
REMARK 3 B33 (A**2) : 1.97000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.87000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.617
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.151
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.138
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.889
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5226 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4786 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7103 ; 1.115 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11116 ; 0.888 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 654 ; 5.458 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 221 ;34.730 ;23.846
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 853 ;12.971 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;19.546 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 807 ; 0.058 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5788 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1039 ; 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): 2637 ; 1.377 ; 4.796
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2636 ; 1.373 ; 4.793
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3284 ; 1.466 ; 7.171
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3285 ; 1.466 ; 7.174
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2589 ; 1.320 ; 5.206
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2589 ; 1.319 ; 5.206
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3820 ; 1.238 ; 7.673
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5839 ; 2.193 ;58.064
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5839 ; 2.193 ;58.062
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 10012 ; 1.479 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 137 ;23.212 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 10026 ; 4.330 ; 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 6GUP 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_1200010582.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUN-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 : SLS
REMARK 200 BEAMLINE : X06SA
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 EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53434
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
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 (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.50100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 5.5 17% PEG 400, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 51.42500
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: 3110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 0
REMARK 465 SER A 1
REMARK 465 TYR A 2
REMARK 465 SER A 3
REMARK 465 LYS A 4
REMARK 465 PHE A 5
REMARK 465 PRO A 142
REMARK 465 ALA A 143
REMARK 465 PHE A 144
REMARK 465 ASP A 145
REMARK 465 PRO A 146
REMARK 465 TYR A 147
REMARK 465 LEU A 148
REMARK 465 GLU A 149
REMARK 465 HIS A 150
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 TYR B 2
REMARK 465 SER B 3
REMARK 465 LYS B 4
REMARK 465 PHE B 5
REMARK 465 TRP B 80
REMARK 465 GLY B 81
REMARK 465 LEU B 82
REMARK 465 ASN B 136
REMARK 465 PRO B 137
REMARK 465 HIS B 138
REMARK 465 THR B 139
REMARK 465 HIS B 140
REMARK 465 THR B 141
REMARK 465 PRO B 142
REMARK 465 ALA B 143
REMARK 465 PHE B 144
REMARK 465 ASP B 145
REMARK 465 PRO B 146
REMARK 465 TYR B 147
REMARK 465 LEU B 148
REMARK 465 GLU B 149
REMARK 465 ARG B 203
REMARK 465 ASP B 204
REMARK 465 ALA B 205
REMARK 465 ASP B 206
REMARK 465 ALA B 207
REMARK 465 GLY B 208
REMARK 465 PRO B 242
REMARK 465 GLU B 243
REMARK 465 SER B 244
REMARK 465 LYS B 353
REMARK 465 ALA B 354
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 51 -94.82 -108.38
REMARK 500 SER A 52 -115.16 52.39
REMARK 500 GLN A 78 72.95 -109.53
REMARK 500 SER A 122 -123.26 55.47
REMARK 500 HIS A 138 60.35 -115.84
REMARK 500 THR A 263 -76.85 -116.72
REMARK 500 THR B 51 -86.65 -103.75
REMARK 500 SER B 52 -119.86 56.64
REMARK 500 SER B 122 -107.76 55.07
REMARK 500 THR B 263 -74.58 -114.21
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 513 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH A 514 DISTANCE = 6.71 ANGSTROMS
REMARK 525 HOH A 515 DISTANCE = 6.85 ANGSTROMS
REMARK 525 HOH A 516 DISTANCE = 8.83 ANGSTROMS
REMARK 525 HOH A 517 DISTANCE = 9.48 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 401
DBREF 6GUP A 2 354 UNP Q4WF56 Q4WF56_ASPFU 2 354
DBREF 6GUP B 2 354 UNP Q4WF56 Q4WF56_ASPFU 2 354
SEQADV 6GUP GLY A 0 UNP Q4WF56 EXPRESSION TAG
SEQADV 6GUP SER A 1 UNP Q4WF56 EXPRESSION TAG
SEQADV 6GUP GLY B 0 UNP Q4WF56 EXPRESSION TAG
SEQADV 6GUP SER B 1 UNP Q4WF56 EXPRESSION TAG
SEQRES 1 A 355 GLY SER TYR SER LYS PHE TRP PRO LYS GLY GLY LEU PRO
SEQRES 2 A 355 GLY ILE LEU HIS HIS TYR THR GLU THR LEU VAL THR PHE
SEQRES 3 A 355 GLU TYR THR THR THR THR THR ARG LYS PRO HIS SER LEU
SEQRES 4 A 355 LEU PHE VAL GLY GLY LEU GLY ASP GLY LEU ALA THR THR
SEQRES 5 A 355 SER TYR LEU ALA ASP LEU ALA HIS ALA LEU GLN PRO THR
SEQRES 6 A 355 GLU TRP SER LEU PHE THR LEU THR LEU THR SER SER TYR
SEQRES 7 A 355 GLN SER TRP GLY LEU GLY HIS LEU ASP ARG ASP THR ASN
SEQRES 8 A 355 GLU ILE ALA GLN CYS LEU LYS TYR ILE LYS GLU TYR LYS
SEQRES 9 A 355 THR GLU LYS PHE GLY GLY SER ALA SER SER GLY LYS ILE
SEQRES 10 A 355 VAL LEU MET GLY HIS SER THR GLY SER GLN CYS VAL LEU
SEQRES 11 A 355 HIS TYR LEU SER ARG PRO ASN PRO HIS THR HIS THR PRO
SEQRES 12 A 355 ALA PHE ASP PRO TYR LEU GLU HIS VAL GLU ARG MET PRO
SEQRES 13 A 355 LEU ASP GLY ALA ILE MET GLN ALA PRO VAL SER ASP ARG
SEQRES 14 A 355 GLU ALA ILE GLN TRP VAL LEU ALA GLU GLY LEU GLY ASP
SEQRES 15 A 355 ARG THR PRO ALA GLU ILE ARG PRO VAL PHE GLU LYS LEU
SEQRES 16 A 355 THR SER MET ALA ARG GLU ALA ALA ARG ASP ALA ASP ALA
SEQRES 17 A 355 GLY THR ASP VAL LEU LEU PRO LEU ALA MET THR SER LEU
SEQRES 18 A 355 VAL TYR PRO ALA HIS THR PRO LEU SER ALA ARG ARG PHE
SEQRES 19 A 355 LEU SER LEU THR SER PRO GLU SER PRO GLU SER PRO SER
SEQRES 20 A 355 GLU ASP ASP LEU PHE SER SER ASP LEU SER ASP GLU GLN
SEQRES 21 A 355 LEU GLY LYS THR PHE GLY MET ILE ARG GLU GLN GLY LEU
SEQRES 22 A 355 LEU ARG GLY LYS LEU MET VAL LEU PHE SER GLY ALA ASP
SEQRES 23 A 355 GLN SER VAL PRO ALA TRP VAL ASP LYS ASP THR LEU LEU
SEQRES 24 A 355 SER ARG TRP ARG ASN ALA THR ASP HIS ASN GLY GLU ALA
SEQRES 25 A 355 ALA ILE TRP ASP GLU ASN SER GLY ILE ILE PRO ASN ALA
SEQRES 26 A 355 SER HIS ALA LEU SER ASN ASP ASP GLN ALA GLU PRO ARG
SEQRES 27 A 355 ASN PHE LEU VAL ASN LYS VAL LEU GLY TYR LEU SER ALA
SEQRES 28 A 355 LEU VAL LYS ALA
SEQRES 1 B 355 GLY SER TYR SER LYS PHE TRP PRO LYS GLY GLY LEU PRO
SEQRES 2 B 355 GLY ILE LEU HIS HIS TYR THR GLU THR LEU VAL THR PHE
SEQRES 3 B 355 GLU TYR THR THR THR THR THR ARG LYS PRO HIS SER LEU
SEQRES 4 B 355 LEU PHE VAL GLY GLY LEU GLY ASP GLY LEU ALA THR THR
SEQRES 5 B 355 SER TYR LEU ALA ASP LEU ALA HIS ALA LEU GLN PRO THR
SEQRES 6 B 355 GLU TRP SER LEU PHE THR LEU THR LEU THR SER SER TYR
SEQRES 7 B 355 GLN SER TRP GLY LEU GLY HIS LEU ASP ARG ASP THR ASN
SEQRES 8 B 355 GLU ILE ALA GLN CYS LEU LYS TYR ILE LYS GLU TYR LYS
SEQRES 9 B 355 THR GLU LYS PHE GLY GLY SER ALA SER SER GLY LYS ILE
SEQRES 10 B 355 VAL LEU MET GLY HIS SER THR GLY SER GLN CYS VAL LEU
SEQRES 11 B 355 HIS TYR LEU SER ARG PRO ASN PRO HIS THR HIS THR PRO
SEQRES 12 B 355 ALA PHE ASP PRO TYR LEU GLU HIS VAL GLU ARG MET PRO
SEQRES 13 B 355 LEU ASP GLY ALA ILE MET GLN ALA PRO VAL SER ASP ARG
SEQRES 14 B 355 GLU ALA ILE GLN TRP VAL LEU ALA GLU GLY LEU GLY ASP
SEQRES 15 B 355 ARG THR PRO ALA GLU ILE ARG PRO VAL PHE GLU LYS LEU
SEQRES 16 B 355 THR SER MET ALA ARG GLU ALA ALA ARG ASP ALA ASP ALA
SEQRES 17 B 355 GLY THR ASP VAL LEU LEU PRO LEU ALA MET THR SER LEU
SEQRES 18 B 355 VAL TYR PRO ALA HIS THR PRO LEU SER ALA ARG ARG PHE
SEQRES 19 B 355 LEU SER LEU THR SER PRO GLU SER PRO GLU SER PRO SER
SEQRES 20 B 355 GLU ASP ASP LEU PHE SER SER ASP LEU SER ASP GLU GLN
SEQRES 21 B 355 LEU GLY LYS THR PHE GLY MET ILE ARG GLU GLN GLY LEU
SEQRES 22 B 355 LEU ARG GLY LYS LEU MET VAL LEU PHE SER GLY ALA ASP
SEQRES 23 B 355 GLN SER VAL PRO ALA TRP VAL ASP LYS ASP THR LEU LEU
SEQRES 24 B 355 SER ARG TRP ARG ASN ALA THR ASP HIS ASN GLY GLU ALA
SEQRES 25 B 355 ALA ILE TRP ASP GLU ASN SER GLY ILE ILE PRO ASN ALA
SEQRES 26 B 355 SER HIS ALA LEU SER ASN ASP ASP GLN ALA GLU PRO ARG
SEQRES 27 B 355 ASN PHE LEU VAL ASN LYS VAL LEU GLY TYR LEU SER ALA
SEQRES 28 B 355 LEU VAL LYS ALA
HET GOL B 401 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *266(H2 O)
HELIX 1 AA1 TYR A 53 LEU A 61 1 9
HELIX 2 AA2 LEU A 73 GLN A 78 1 6
HELIX 3 AA3 HIS A 84 GLY A 108 1 25
HELIX 4 AA4 THR A 123 ARG A 134 1 12
HELIX 5 AA5 SER A 166 GLY A 178 1 13
HELIX 6 AA6 THR A 183 ALA A 205 1 23
HELIX 7 AA7 PRO A 214 TYR A 222 1 9
HELIX 8 AA8 SER A 229 SER A 238 1 10
HELIX 9 AA9 SER A 256 LYS A 262 1 7
HELIX 10 AB1 THR A 263 GLY A 265 5 3
HELIX 11 AB2 MET A 266 GLY A 271 1 6
HELIX 12 AB3 ASP A 293 HIS A 307 1 15
HELIX 13 AB4 GLN A 333 LYS A 353 1 21
HELIX 14 AB5 TYR B 53 GLN B 62 1 10
HELIX 15 AB6 LEU B 73 SER B 79 1 7
HELIX 16 AB7 HIS B 84 GLY B 108 1 25
HELIX 17 AB8 GLY B 109 SER B 113 5 5
HELIX 18 AB9 THR B 123 ARG B 134 1 12
HELIX 19 AC1 SER B 166 GLY B 178 1 13
HELIX 20 AC2 THR B 183 ALA B 202 1 20
HELIX 21 AC3 PRO B 214 TYR B 222 1 9
HELIX 22 AC4 SER B 229 SER B 238 1 10
HELIX 23 AC5 SER B 256 LYS B 262 1 7
HELIX 24 AC6 GLY B 265 GLY B 271 1 7
HELIX 25 AC7 ASP B 293 ASP B 306 1 14
HELIX 26 AC8 ASN B 330 ASP B 332 5 3
HELIX 27 AC9 GLN B 333 VAL B 352 1 20
SHEET 1 AA116 GLY A 319 ILE A 321 0
SHEET 2 AA116 LEU A 277 SER A 282 1 N PHE A 281 O ILE A 321
SHEET 3 AA116 GLY A 158 GLN A 162 1 N MET A 161 O LEU A 280
SHEET 4 AA116 ILE A 116 HIS A 121 1 N GLY A 120 O GLN A 162
SHEET 5 AA116 HIS A 36 VAL A 41 1 N VAL A 41 O MET A 119
SHEET 6 AA116 TRP A 66 LEU A 71 1 O PHE A 69 N PHE A 40
SHEET 7 AA116 VAL A 23 TYR A 27 -1 N TYR A 27 O LEU A 68
SHEET 8 AA116 LEU A 11 HIS A 17 -1 N ILE A 14 O GLU A 26
SHEET 9 AA116 LEU B 11 HIS B 17 -1 O GLY B 13 N GLY A 13
SHEET 10 AA116 VAL B 23 TYR B 27 -1 O GLU B 26 N ILE B 14
SHEET 11 AA116 TRP B 66 LEU B 71 -1 O LEU B 68 N TYR B 27
SHEET 12 AA116 HIS B 36 VAL B 41 1 N PHE B 40 O PHE B 69
SHEET 13 AA116 ILE B 116 HIS B 121 1 O MET B 119 N LEU B 39
SHEET 14 AA116 GLY B 158 GLN B 162 1 O ILE B 160 N GLY B 120
SHEET 15 AA116 LEU B 277 SER B 282 1 O LEU B 280 N MET B 161
SHEET 16 AA116 GLY B 319 ILE B 321 1 O ILE B 321 N PHE B 281
SHEET 1 AA2 2 ASP A 210 LEU A 212 0
SHEET 2 AA2 2 ASP B 210 LEU B 212 -1 O ASP B 210 N LEU A 212
SITE 1 AC1 2 TYR B 98 HOH B 533
CRYST1 48.930 102.850 65.060 90.00 92.14 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 0.020437 0.000000 0.000762 0.00000
SCALE2 0.000000 0.009723 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015381 0.00000
TER 2625 ALA A 354
TER 5107 VAL B 352
MASTER 336 0 1 27 18 0 1 6 5377 2 6 56
END |