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HEADER HYDROLASE 19-JUN-18 6GUN
TITLE SIDEROPHORE HYDROLASE ESTB FROM ASPERGILLUS NIDULANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTB FROM ASPERGILLUS NIDULANS;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIDULANS FGSC A4;
SOURCE 3 ORGANISM_TAXID: 227321;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 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 6GUN 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. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 77699
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) : 0.195
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4089
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5667
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.43
REMARK 3 BIN R VALUE (WORKING SET) : 0.3260
REMARK 3 BIN FREE R VALUE SET COUNT : 298
REMARK 3 BIN FREE R VALUE : 0.3420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9312
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 479
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.66000
REMARK 3 B22 (A**2) : 0.97000
REMARK 3 B33 (A**2) : 1.04000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.85000
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): 0.171
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.155
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.384
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9584 ; 0.003 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 8312 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12996 ; 0.761 ; 1.654
REMARK 3 BOND ANGLES OTHERS (DEGREES): 19495 ; 0.685 ; 1.632
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1164 ; 5.612 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 553 ;30.225 ;20.344
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1513 ;13.583 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 92 ;15.544 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1167 ; 0.033 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10926 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1894 ; 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): 4680 ; 0.859 ; 5.116
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4679 ; 0.859 ; 5.115
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5836 ; 1.279 ; 7.665
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5837 ; 1.279 ; 7.666
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4904 ; 0.707 ; 5.280
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4904 ; 0.707 ; 5.280
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 7161 ; 1.019 ; 7.866
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 10889 ; 2.323 ;58.641
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 10799 ; 2.189 ;58.526
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 17896 ; 0.172 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 216 ;27.347 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 17902 ;25.229 ; 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 6GUN 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_1200010580.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-FEB-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 : 82011
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 97.1
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.0000
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) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.58100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.700
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 (%): 46.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.0 20 % PEG3350, 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 36.02500
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 4540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 40.44249
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -36.02500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -100.24976
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 THR A 2
REMARK 465 GLN A 3
REMARK 465 ILE A 4
REMARK 465 ILE A 200
REMARK 465 LYS A 201
REMARK 465 GLU A 202
REMARK 465 ASN A 203
REMARK 465 GLU A 304
REMARK 465 GLU A 305
REMARK 465 SER A 306
REMARK 465 VAL A 307
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 THR B 2
REMARK 465 GLN B 3
REMARK 465 ILE B 4
REMARK 465 ASP B 5
REMARK 465 LYS B 6
REMARK 465 GLU B 202
REMARK 465 ASN B 203
REMARK 465 GLY B 204
REMARK 465 ALA B 205
REMARK 465 TYR B 206
REMARK 465 THR B 207
REMARK 465 ASN B 208
REMARK 465 GLY B 209
REMARK 465 GLU B 304
REMARK 465 GLU B 305
REMARK 465 SER B 306
REMARK 465 VAL B 307
REMARK 465 GLY C 0
REMARK 465 SER C 1
REMARK 465 THR C 2
REMARK 465 GLN C 3
REMARK 465 ILE C 4
REMARK 465 ASP C 5
REMARK 465 LYS C 6
REMARK 465 ILE C 200
REMARK 465 LYS C 201
REMARK 465 GLU C 202
REMARK 465 ASN C 203
REMARK 465 GLY C 204
REMARK 465 ALA C 205
REMARK 465 TYR C 206
REMARK 465 THR C 207
REMARK 465 ASN C 208
REMARK 465 GLY C 209
REMARK 465 VAL C 307
REMARK 465 GLY D 0
REMARK 465 SER D 1
REMARK 465 THR D 2
REMARK 465 GLN D 3
REMARK 465 LYS D 201
REMARK 465 GLU D 202
REMARK 465 ASN D 203
REMARK 465 GLU D 305
REMARK 465 SER D 306
REMARK 465 VAL D 307
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 ASP A 40 -124.42 62.26
REMARK 500 PHE A 141 77.00 -118.10
REMARK 500 SER A 155 -113.56 68.71
REMARK 500 SER A 179 60.15 37.20
REMARK 500 ASP B 40 -102.74 57.43
REMARK 500 SER B 155 -113.75 68.49
REMARK 500 SER B 179 59.22 39.93
REMARK 500 ASN B 231 109.51 -56.68
REMARK 500 ASP C 40 -123.47 60.03
REMARK 500 ASN C 48 51.78 -154.29
REMARK 500 HIS C 77 30.86 -97.51
REMARK 500 THR C 111 78.77 -115.36
REMARK 500 PHE C 141 76.40 -117.75
REMARK 500 SER C 155 -113.38 66.79
REMARK 500 SER C 179 59.37 38.52
REMARK 500 ASN C 231 109.67 -55.26
REMARK 500 ASP C 298 52.03 -116.42
REMARK 500 ASP D 5 32.40 -92.86
REMARK 500 ASP D 40 -129.68 63.10
REMARK 500 SER D 155 -109.16 64.73
REMARK 500 ASP D 226 77.63 -119.04
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 D 568 DISTANCE = 6.43 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 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 401
DBREF 6GUN A 0 307 PDB 6GUN 6GUN 0 307
DBREF 6GUN B 0 307 PDB 6GUN 6GUN 0 307
DBREF 6GUN C 0 307 PDB 6GUN 6GUN 0 307
DBREF 6GUN D 0 307 PDB 6GUN 6GUN 0 307
SEQRES 1 A 308 GLY SER THR GLN ILE ASP LYS PRO ALA VAL VAL SER LEU
SEQRES 2 A 308 PRO SER SER GLU GLN PHE TYR LEU ASN ASN SER ARG GLY
SEQRES 3 A 308 GLU ARG TYR LEU ILE GLN VAL SER TRP PRO LEU HIS TRP
SEQRES 4 A 308 LYS ASP HIS LYS PRO ASP THR ASP ARG ASN ASP VAL PRO
SEQRES 5 A 308 LEU ILE TYR ILE VAL ASP GLY ASN ALA LEU PHE LEU THR
SEQRES 6 A 308 ALA THR GLU ALA LEU TRP ARG ARG SER ALA ASP SER HIS
SEQRES 7 A 308 TYR CYS GLY GLY GLY ILE VAL VAL ALA ILE GLY TYR PRO
SEQRES 8 A 308 LEU GLU GLY THR GLY LYS VAL TYR HIS ARG VAL ARG ARG
SEQRES 9 A 308 GLY PHE ASP LEU THR VAL PRO THR PRO ASP SER PRO VAL
SEQRES 10 A 308 GLU GLY HIS GLY GLY ALA ASP ILE LEU LEU ASP PHE ILE
SEQRES 11 A 308 ALA GLU THR VAL ARG PRO ALA VAL ARG GLU ARG PHE PRO
SEQRES 12 A 308 ASP VAL SER VAL SER ARG GLU ALA LEU TYR GLY HIS SER
SEQRES 13 A 308 TYR GLY GLY LEU PHE ALA LEU HIS ALA LEU PHE THR ARG
SEQRES 14 A 308 PRO SER MET PHE ASP ALA TYR ILE ALA SER SER PRO SER
SEQRES 15 A 308 ILE TRP TRP ASN GLY ARG CYS ILE LEU ASN GLU ALA LYS
SEQRES 16 A 308 ALA PHE THR ARG LYS ILE LYS GLU ASN GLY ALA TYR THR
SEQRES 17 A 308 ASN GLY GLU LYS LYS LEU PRO SER LEU MET MET TYR LEU
SEQRES 18 A 308 GLY GLY LEU GLU GLN ASP PRO ARG ARG TRP ASN ASP GLU
SEQRES 19 A 308 PRO ASP GLU SER TRP GLU GLY ARG LYS ARG ASP ALA GLU
SEQRES 20 A 308 ALA PHE ASN MET LYS VAL ASN LEU LEU GLU LEU MET GLY
SEQRES 21 A 308 LEU ILE ARG GLY CYS THR ARG LEU HIS ALA VAL SER PHE
SEQRES 22 A 308 SER GLU TYR ALA GLY GLU ASP HIS GLY THR VAL MET ALA
SEQRES 23 A 308 CYS SER LEU GLY ARG GLY PHE SER THR PHE MET GLU ASP
SEQRES 24 A 308 TRP PRO VAL PRO ARG GLU GLU SER VAL
SEQRES 1 B 308 GLY SER THR GLN ILE ASP LYS PRO ALA VAL VAL SER LEU
SEQRES 2 B 308 PRO SER SER GLU GLN PHE TYR LEU ASN ASN SER ARG GLY
SEQRES 3 B 308 GLU ARG TYR LEU ILE GLN VAL SER TRP PRO LEU HIS TRP
SEQRES 4 B 308 LYS ASP HIS LYS PRO ASP THR ASP ARG ASN ASP VAL PRO
SEQRES 5 B 308 LEU ILE TYR ILE VAL ASP GLY ASN ALA LEU PHE LEU THR
SEQRES 6 B 308 ALA THR GLU ALA LEU TRP ARG ARG SER ALA ASP SER HIS
SEQRES 7 B 308 TYR CYS GLY GLY GLY ILE VAL VAL ALA ILE GLY TYR PRO
SEQRES 8 B 308 LEU GLU GLY THR GLY LYS VAL TYR HIS ARG VAL ARG ARG
SEQRES 9 B 308 GLY PHE ASP LEU THR VAL PRO THR PRO ASP SER PRO VAL
SEQRES 10 B 308 GLU GLY HIS GLY GLY ALA ASP ILE LEU LEU ASP PHE ILE
SEQRES 11 B 308 ALA GLU THR VAL ARG PRO ALA VAL ARG GLU ARG PHE PRO
SEQRES 12 B 308 ASP VAL SER VAL SER ARG GLU ALA LEU TYR GLY HIS SER
SEQRES 13 B 308 TYR GLY GLY LEU PHE ALA LEU HIS ALA LEU PHE THR ARG
SEQRES 14 B 308 PRO SER MET PHE ASP ALA TYR ILE ALA SER SER PRO SER
SEQRES 15 B 308 ILE TRP TRP ASN GLY ARG CYS ILE LEU ASN GLU ALA LYS
SEQRES 16 B 308 ALA PHE THR ARG LYS ILE LYS GLU ASN GLY ALA TYR THR
SEQRES 17 B 308 ASN GLY GLU LYS LYS LEU PRO SER LEU MET MET TYR LEU
SEQRES 18 B 308 GLY GLY LEU GLU GLN ASP PRO ARG ARG TRP ASN ASP GLU
SEQRES 19 B 308 PRO ASP GLU SER TRP GLU GLY ARG LYS ARG ASP ALA GLU
SEQRES 20 B 308 ALA PHE ASN MET LYS VAL ASN LEU LEU GLU LEU MET GLY
SEQRES 21 B 308 LEU ILE ARG GLY CYS THR ARG LEU HIS ALA VAL SER PHE
SEQRES 22 B 308 SER GLU TYR ALA GLY GLU ASP HIS GLY THR VAL MET ALA
SEQRES 23 B 308 CYS SER LEU GLY ARG GLY PHE SER THR PHE MET GLU ASP
SEQRES 24 B 308 TRP PRO VAL PRO ARG GLU GLU SER VAL
SEQRES 1 C 308 GLY SER THR GLN ILE ASP LYS PRO ALA VAL VAL SER LEU
SEQRES 2 C 308 PRO SER SER GLU GLN PHE TYR LEU ASN ASN SER ARG GLY
SEQRES 3 C 308 GLU ARG TYR LEU ILE GLN VAL SER TRP PRO LEU HIS TRP
SEQRES 4 C 308 LYS ASP HIS LYS PRO ASP THR ASP ARG ASN ASP VAL PRO
SEQRES 5 C 308 LEU ILE TYR ILE VAL ASP GLY ASN ALA LEU PHE LEU THR
SEQRES 6 C 308 ALA THR GLU ALA LEU TRP ARG ARG SER ALA ASP SER HIS
SEQRES 7 C 308 TYR CYS GLY GLY GLY ILE VAL VAL ALA ILE GLY TYR PRO
SEQRES 8 C 308 LEU GLU GLY THR GLY LYS VAL TYR HIS ARG VAL ARG ARG
SEQRES 9 C 308 GLY PHE ASP LEU THR VAL PRO THR PRO ASP SER PRO VAL
SEQRES 10 C 308 GLU GLY HIS GLY GLY ALA ASP ILE LEU LEU ASP PHE ILE
SEQRES 11 C 308 ALA GLU THR VAL ARG PRO ALA VAL ARG GLU ARG PHE PRO
SEQRES 12 C 308 ASP VAL SER VAL SER ARG GLU ALA LEU TYR GLY HIS SER
SEQRES 13 C 308 TYR GLY GLY LEU PHE ALA LEU HIS ALA LEU PHE THR ARG
SEQRES 14 C 308 PRO SER MET PHE ASP ALA TYR ILE ALA SER SER PRO SER
SEQRES 15 C 308 ILE TRP TRP ASN GLY ARG CYS ILE LEU ASN GLU ALA LYS
SEQRES 16 C 308 ALA PHE THR ARG LYS ILE LYS GLU ASN GLY ALA TYR THR
SEQRES 17 C 308 ASN GLY GLU LYS LYS LEU PRO SER LEU MET MET TYR LEU
SEQRES 18 C 308 GLY GLY LEU GLU GLN ASP PRO ARG ARG TRP ASN ASP GLU
SEQRES 19 C 308 PRO ASP GLU SER TRP GLU GLY ARG LYS ARG ASP ALA GLU
SEQRES 20 C 308 ALA PHE ASN MET LYS VAL ASN LEU LEU GLU LEU MET GLY
SEQRES 21 C 308 LEU ILE ARG GLY CYS THR ARG LEU HIS ALA VAL SER PHE
SEQRES 22 C 308 SER GLU TYR ALA GLY GLU ASP HIS GLY THR VAL MET ALA
SEQRES 23 C 308 CYS SER LEU GLY ARG GLY PHE SER THR PHE MET GLU ASP
SEQRES 24 C 308 TRP PRO VAL PRO ARG GLU GLU SER VAL
SEQRES 1 D 308 GLY SER THR GLN ILE ASP LYS PRO ALA VAL VAL SER LEU
SEQRES 2 D 308 PRO SER SER GLU GLN PHE TYR LEU ASN ASN SER ARG GLY
SEQRES 3 D 308 GLU ARG TYR LEU ILE GLN VAL SER TRP PRO LEU HIS TRP
SEQRES 4 D 308 LYS ASP HIS LYS PRO ASP THR ASP ARG ASN ASP VAL PRO
SEQRES 5 D 308 LEU ILE TYR ILE VAL ASP GLY ASN ALA LEU PHE LEU THR
SEQRES 6 D 308 ALA THR GLU ALA LEU TRP ARG ARG SER ALA ASP SER HIS
SEQRES 7 D 308 TYR CYS GLY GLY GLY ILE VAL VAL ALA ILE GLY TYR PRO
SEQRES 8 D 308 LEU GLU GLY THR GLY LYS VAL TYR HIS ARG VAL ARG ARG
SEQRES 9 D 308 GLY PHE ASP LEU THR VAL PRO THR PRO ASP SER PRO VAL
SEQRES 10 D 308 GLU GLY HIS GLY GLY ALA ASP ILE LEU LEU ASP PHE ILE
SEQRES 11 D 308 ALA GLU THR VAL ARG PRO ALA VAL ARG GLU ARG PHE PRO
SEQRES 12 D 308 ASP VAL SER VAL SER ARG GLU ALA LEU TYR GLY HIS SER
SEQRES 13 D 308 TYR GLY GLY LEU PHE ALA LEU HIS ALA LEU PHE THR ARG
SEQRES 14 D 308 PRO SER MET PHE ASP ALA TYR ILE ALA SER SER PRO SER
SEQRES 15 D 308 ILE TRP TRP ASN GLY ARG CYS ILE LEU ASN GLU ALA LYS
SEQRES 16 D 308 ALA PHE THR ARG LYS ILE LYS GLU ASN GLY ALA TYR THR
SEQRES 17 D 308 ASN GLY GLU LYS LYS LEU PRO SER LEU MET MET TYR LEU
SEQRES 18 D 308 GLY GLY LEU GLU GLN ASP PRO ARG ARG TRP ASN ASP GLU
SEQRES 19 D 308 PRO ASP GLU SER TRP GLU GLY ARG LYS ARG ASP ALA GLU
SEQRES 20 D 308 ALA PHE ASN MET LYS VAL ASN LEU LEU GLU LEU MET GLY
SEQRES 21 D 308 LEU ILE ARG GLY CYS THR ARG LEU HIS ALA VAL SER PHE
SEQRES 22 D 308 SER GLU TYR ALA GLY GLU ASP HIS GLY THR VAL MET ALA
SEQRES 23 D 308 CYS SER LEU GLY ARG GLY PHE SER THR PHE MET GLU ASP
SEQRES 24 D 308 TRP PRO VAL PRO ARG GLU GLU SER VAL
HET GOL A 401 6
HET GOL D 401 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 7 HOH *479(H2 O)
HELIX 1 AA1 ASP A 57 SER A 73 1 17
HELIX 2 AA2 HIS A 99 LEU A 107 1 9
HELIX 3 AA3 GLY A 121 THR A 132 1 12
HELIX 4 AA4 THR A 132 PHE A 141 1 10
HELIX 5 AA5 SER A 155 ARG A 168 1 14
HELIX 6 AA6 TRP A 183 CYS A 188 1 6
HELIX 7 AA7 CYS A 188 LYS A 199 1 12
HELIX 8 AA8 PRO A 234 ASN A 249 1 16
HELIX 9 AA9 ASN A 249 ARG A 262 1 14
HELIX 10 AB1 THR A 282 ASP A 298 1 17
HELIX 11 AB2 ASP B 57 SER B 73 1 17
HELIX 12 AB3 HIS B 99 LEU B 107 1 9
HELIX 13 AB4 GLY B 121 THR B 132 1 12
HELIX 14 AB5 THR B 132 PHE B 141 1 10
HELIX 15 AB6 SER B 155 ARG B 168 1 14
HELIX 16 AB7 TRP B 183 CYS B 188 1 6
HELIX 17 AB8 CYS B 188 LYS B 199 1 12
HELIX 18 AB9 GLY B 222 ASP B 226 1 5
HELIX 19 AC1 PRO B 234 ASN B 249 1 16
HELIX 20 AC2 ASN B 249 ARG B 262 1 14
HELIX 21 AC3 THR B 282 ASP B 298 1 17
HELIX 22 AC4 ASP C 57 ARG C 72 1 16
HELIX 23 AC5 SER C 73 ASP C 75 5 3
HELIX 24 AC6 HIS C 99 THR C 108 1 10
HELIX 25 AC7 GLY C 121 THR C 132 1 12
HELIX 26 AC8 THR C 132 PHE C 141 1 10
HELIX 27 AC9 SER C 155 ARG C 168 1 14
HELIX 28 AD1 TRP C 183 CYS C 188 1 6
HELIX 29 AD2 CYS C 188 ARG C 198 1 11
HELIX 30 AD3 GLY C 222 ASP C 226 1 5
HELIX 31 AD4 PRO C 234 ASN C 249 1 16
HELIX 32 AD5 ASN C 249 ARG C 262 1 14
HELIX 33 AD6 THR C 282 ASP C 298 1 17
HELIX 34 AD7 ASP D 57 SER D 73 1 17
HELIX 35 AD8 HIS D 99 LEU D 107 1 9
HELIX 36 AD9 GLY D 121 THR D 132 1 12
HELIX 37 AE1 THR D 132 PHE D 141 1 10
HELIX 38 AE2 SER D 155 ARG D 168 1 14
HELIX 39 AE3 TRP D 183 CYS D 188 1 6
HELIX 40 AE4 CYS D 188 LYS D 199 1 12
HELIX 41 AE5 PRO D 234 ASN D 249 1 16
HELIX 42 AE6 ASN D 249 ARG D 262 1 14
HELIX 43 AE7 THR D 282 ASP D 298 1 17
SHEET 1 AA1 8 SER A 15 ASN A 21 0
SHEET 2 AA1 8 ARG A 27 SER A 33 -1 O VAL A 32 N GLU A 16
SHEET 3 AA1 8 ILE A 83 GLY A 88 -1 O ALA A 86 N GLN A 31
SHEET 4 AA1 8 ASP A 49 VAL A 56 1 N ILE A 55 O ILE A 87
SHEET 5 AA1 8 SER A 145 HIS A 154 1 O ALA A 150 N TYR A 54
SHEET 6 AA1 8 ALA A 174 SER A 178 1 O ILE A 176 N LEU A 151
SHEET 7 AA1 8 SER A 215 GLY A 221 1 O MET A 217 N TYR A 175
SHEET 8 AA1 8 ALA A 269 TYR A 275 1 O TYR A 275 N LEU A 220
SHEET 1 AA2 8 SER B 15 ASN B 21 0
SHEET 2 AA2 8 ARG B 27 SER B 33 -1 O ILE B 30 N PHE B 18
SHEET 3 AA2 8 ILE B 83 GLY B 88 -1 O ALA B 86 N GLN B 31
SHEET 4 AA2 8 ASP B 49 VAL B 56 1 N ILE B 55 O ILE B 87
SHEET 5 AA2 8 SER B 145 HIS B 154 1 O TYR B 152 N TYR B 54
SHEET 6 AA2 8 ALA B 174 SER B 178 1 O ILE B 176 N LEU B 151
SHEET 7 AA2 8 SER B 215 GLY B 221 1 O MET B 217 N TYR B 175
SHEET 8 AA2 8 ALA B 269 TYR B 275 1 O TYR B 275 N LEU B 220
SHEET 1 AA3 8 SER C 15 ASN C 21 0
SHEET 2 AA3 8 ARG C 27 SER C 33 -1 O ILE C 30 N PHE C 18
SHEET 3 AA3 8 ILE C 83 GLY C 88 -1 O GLY C 88 N LEU C 29
SHEET 4 AA3 8 ASP C 49 VAL C 56 1 N ILE C 55 O ILE C 87
SHEET 5 AA3 8 SER C 145 HIS C 154 1 O TYR C 152 N TYR C 54
SHEET 6 AA3 8 ALA C 174 SER C 178 1 O ILE C 176 N LEU C 151
SHEET 7 AA3 8 SER C 215 GLY C 221 1 O MET C 217 N TYR C 175
SHEET 8 AA3 8 ALA C 269 TYR C 275 1 O TYR C 275 N LEU C 220
SHEET 1 AA4 8 SER D 15 ASN D 21 0
SHEET 2 AA4 8 ARG D 27 SER D 33 -1 O VAL D 32 N GLU D 16
SHEET 3 AA4 8 ILE D 83 GLY D 88 -1 O GLY D 88 N LEU D 29
SHEET 4 AA4 8 ASP D 49 VAL D 56 1 N ILE D 55 O ILE D 87
SHEET 5 AA4 8 SER D 145 HIS D 154 1 O TYR D 152 N TYR D 54
SHEET 6 AA4 8 ALA D 174 SER D 178 1 O ILE D 176 N LEU D 151
SHEET 7 AA4 8 SER D 215 GLY D 221 1 O MET D 217 N TYR D 175
SHEET 8 AA4 8 ALA D 269 TYR D 275 1 O SER D 271 N MET D 218
CISPEP 1 TRP A 299 PRO A 300 0 0.07
CISPEP 2 TRP B 299 PRO B 300 0 0.10
CISPEP 3 TRP C 299 PRO C 300 0 -3.08
CISPEP 4 TRP D 299 PRO D 300 0 0.13
SITE 1 AC1 6 HIS A 37 ASP A 44 ARG A 47 SER A 73
SITE 2 AC1 6 TYR A 78 TYR D 206
SITE 1 AC2 6 ARG B 100 HIS B 119 TYR B 156 HOH B 425
SITE 2 AC2 6 GLY D 209 LYS D 211
CRYST1 87.460 72.050 108.100 90.00 111.97 90.00 P 1 21 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 0.011434 0.000000 0.004613 0.00000
SCALE2 0.000000 0.013879 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009975 0.00000
TER 2341 ARG A 303
TER 4642 ARG B 303
TER 6950 SER C 306
TER 9316 GLU D 304
MASTER 374 0 2 43 32 0 4 6 9803 4 12 96
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