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HEADER HYDROLASE 13-AUG-15 5D7B
TITLE TRIGONAL CRYSTAL STRUCTURE OF AN ACETYLESTER HYDROLASE FROM
TITLE 2 CORYNEBACTERIUM GLUTAMICUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOMOSERINE O-ACETYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACETYL ESTER HYDROLASE;
COMPND 5 EC: 2.3.1.-,2.3.1.31;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CORYNEBACTERIUM GLUTAMICUM;
SOURCE 3 ORGANISM_TAXID: 1718;
SOURCE 4 GENE: CG0961, CGL0839;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHWG771
KEYWDS ACETYLESTER HYDROLASE, ALPHA/BETA-HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.NIEFIND,C.TOELZER,S.PAL,J.ALTENBUCHNER,H.WATZLAWICK
REVDAT 1 16-DEC-15 5D7B 0
JRNL AUTH C.TOELZER,S.PAL,H.WATZLAWICK,J.ALTENBUCHNER,K.NIEFIND
JRNL TITL A NOVEL ESTERASE SUBFAMILY WITH ALPHA/BETA-HYDROLASE FOLD
JRNL TITL 2 SUGGESTED BY STRUCTURES OF TWO BACTERIAL ENZYMES HOMOLOGOUS
JRNL TITL 3 TO L-HOMOSERINE O-ACETYL TRANSFERASES
JRNL REF FEBS LETT. 2015
JRNL REFN ISSN 0014-5793
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 39329
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.850
REMARK 3 FREE R VALUE TEST SET COUNT : 1120
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 48.5349 - 6.3958 1.00 5009 132 0.1867 0.2037
REMARK 3 2 6.3958 - 5.0783 1.00 4806 145 0.1796 0.1964
REMARK 3 3 5.0783 - 4.4369 1.00 4791 139 0.1515 0.1573
REMARK 3 4 4.4369 - 4.0314 1.00 4752 130 0.1585 0.1839
REMARK 3 5 4.0314 - 3.7426 1.00 4738 141 0.1889 0.1872
REMARK 3 6 3.7426 - 3.5220 1.00 4725 142 0.2178 0.2200
REMARK 3 7 3.5220 - 3.3457 1.00 4681 141 0.2355 0.2719
REMARK 3 8 3.3457 - 3.2001 1.00 4707 150 0.2676 0.2650
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.730
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 5726
REMARK 3 ANGLE : 0.603 7758
REMARK 3 CHIRALITY : 0.021 822
REMARK 3 PLANARITY : 0.003 1016
REMARK 3 DIHEDRAL : 11.582 2050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A'
REMARK 3 ORIGIN FOR THE GROUP (A): 76.3272 -12.9307 49.4163
REMARK 3 T TENSOR
REMARK 3 T11: 0.8890 T22: 0.3014
REMARK 3 T33: 0.5933 T12: 0.0888
REMARK 3 T13: -0.0156 T23: -0.1183
REMARK 3 L TENSOR
REMARK 3 L11: 1.7574 L22: 2.1951
REMARK 3 L33: 1.7186 L12: -0.8488
REMARK 3 L13: 0.5486 L23: -0.7424
REMARK 3 S TENSOR
REMARK 3 S11: 0.2634 S12: 0.1492 S13: -0.3007
REMARK 3 S21: -0.0257 S22: -0.0874 S23: 0.2627
REMARK 3 S31: 0.2943 S32: 0.2266 S33: -0.1428
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B'
REMARK 3 ORIGIN FOR THE GROUP (A): 52.1928 5.2849 23.5326
REMARK 3 T TENSOR
REMARK 3 T11: 0.9622 T22: 0.5310
REMARK 3 T33: 0.8152 T12: 0.2328
REMARK 3 T13: -0.1990 T23: -0.1798
REMARK 3 L TENSOR
REMARK 3 L11: 1.8229 L22: 2.3467
REMARK 3 L33: 2.0062 L12: -0.8488
REMARK 3 L13: 0.5730 L23: -1.0783
REMARK 3 S TENSOR
REMARK 3 S11: 0.3170 S12: 0.3500 S13: -0.4316
REMARK 3 S21: -0.4947 S22: -0.1609 S23: 0.5815
REMARK 3 S31: 0.1506 S32: -0.2330 S33: -0.1235
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1:349 )
REMARK 3 SELECTION : CHAIN 'B' AND (RESSEQ 1:349 )
REMARK 3 ATOM PAIRS NUMBER : 2753
REMARK 3 RMSD : 0.034
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5D7B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000212784.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39336
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 48.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.24500
REMARK 200 FOR THE DATA SET : 24.6600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.70
REMARK 200 R MERGE FOR SHELL (I) : 1.01000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.660
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 2B61
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 83.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 7.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR: 25.5 %(W/V)
REMARK 280 POLYETHYLENGLYCOL 4000, 15 %(V/V) GLYCEROL, 0.17 M LITHIUM
REMARK 280 SULFATE, 85 MM TRIS/HCL, PH 8.5 DROP: 0.4 MICROLITER RESERVOIR
REMARK 280 SOLUTION PLUT 0.8 MICROLITER PROTEIN SOLUTION WITH 5 MG/ML
REMARK 280 PROTEIN CONCENTRATION, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.92767
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 131.85533
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 131.85533
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 65.92767
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: 5580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24240 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 510 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 161 CD - NE - CZ ANGL. DEV. = 8.9 DEGREES
REMARK 500 ARG A 161 NE - CZ - NH1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG A 161 NE - CZ - NH2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG B 22 NE - CZ - NH1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG B 22 NE - CZ - NH2 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG B 161 NE - CZ - NH1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG B 161 NE - CZ - NH2 ANGL. DEV. = 5.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 61 -140.42 -127.60
REMARK 500 GLN A 68 -41.54 -135.78
REMARK 500 ASN A 99 -1.92 -151.32
REMARK 500 MET A 107 -117.66 57.09
REMARK 500 SER A 142 -111.02 55.08
REMARK 500 PHE A 155 76.54 -115.17
REMARK 500 GLU A 196 57.69 -112.08
REMARK 500 PHE A 219 -133.77 -113.58
REMARK 500 PHE A 244 -68.63 -136.26
REMARK 500 THR B 61 -140.25 -127.37
REMARK 500 GLN B 68 -41.70 -135.89
REMARK 500 ASN B 99 -2.15 -151.08
REMARK 500 MET B 107 -117.63 57.02
REMARK 500 SER B 142 -111.16 54.99
REMARK 500 PHE B 155 76.37 -115.07
REMARK 500 GLU B 196 57.76 -111.89
REMARK 500 PHE B 219 -133.61 -113.58
REMARK 500 PHE B 244 -68.58 -136.41
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 409
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5D60 RELATED DB: PDB
REMARK 900 5D60 CONTAINS THE SAME PROTEIN IN A DIFFERENT CRYSTAL PACKING
DBREF 5D7B A 1 349 UNP Q8NS43 Q8NS43_CORGL 1 349
DBREF 5D7B B 1 349 UNP Q8NS43 Q8NS43_CORGL 1 349
SEQRES 1 A 349 MET LEU ASP ASN SER PHE TYR THR ALA GLU VAL GLN GLY
SEQRES 2 A 349 PRO TYR GLU THR ALA SER ILE GLY ARG LEU GLU LEU GLU
SEQRES 3 A 349 GLU GLY GLY VAL ILE GLU ASP CYS TRP LEU ALA TYR ALA
SEQRES 4 A 349 THR ALA GLY THR LEU ASN GLU ASP LYS SER ASN ALA ILE
SEQRES 5 A 349 LEU ILE PRO THR TRP TYR SER GLY THR HIS GLN THR TRP
SEQRES 6 A 349 PHE GLN GLN TYR ILE GLY THR ASP HIS ALA LEU ASP PRO
SEQRES 7 A 349 SER LYS TYR PHE ILE ILE SER ILE ASN GLN ILE GLY ASN
SEQRES 8 A 349 GLY LEU SER VAL SER PRO ALA ASN THR ALA ASP ASP SER
SEQRES 9 A 349 ILE SER MET SER LYS PHE PRO ASN VAL ARG ILE GLY ASP
SEQRES 10 A 349 ASP VAL VAL ALA GLN ASP ARG LEU LEU ARG GLN GLU PHE
SEQRES 11 A 349 GLY ILE THR GLU LEU PHE ALA VAL VAL GLY GLY SER MET
SEQRES 12 A 349 GLY ALA GLN GLN THR TYR GLU TRP ILE VAL ARG PHE PRO
SEQRES 13 A 349 ASP GLN VAL HIS ARG ALA ALA PRO ILE ALA GLY THR ALA
SEQRES 14 A 349 LYS ASN THR PRO HIS ASP PHE ILE PHE THR GLN THR LEU
SEQRES 15 A 349 ASN GLU THR VAL GLU ALA ASP PRO GLY PHE ASN GLY GLY
SEQRES 16 A 349 GLU TYR SER SER HIS GLU GLU VAL ALA ASP GLY LEU ARG
SEQRES 17 A 349 ARG GLN SER HIS LEU TRP ALA ALA MET GLY PHE SER THR
SEQRES 18 A 349 GLU PHE TRP LYS GLN GLU ALA TRP ARG ARG LEU GLY LEU
SEQRES 19 A 349 GLU SER LYS GLU SER VAL LEU ALA ASP PHE LEU ASP PRO
SEQRES 20 A 349 LEU PHE MET SER MET ASP PRO ASN THR LEU LEU ASN ASN
SEQRES 21 A 349 ALA TRP LYS TRP GLN HIS GLY ASP VAL SER ARG HIS THR
SEQRES 22 A 349 GLY GLY ASP LEU ALA ALA ALA LEU GLY ARG VAL LYS ALA
SEQRES 23 A 349 LYS THR PHE VAL MET PRO ILE SER GLU ASP MET PHE PHE
SEQRES 24 A 349 PRO VAL ARG ASP CYS ALA ALA GLU GLN ALA LEU ILE PRO
SEQRES 25 A 349 GLY SER GLU LEU ARG VAL ILE GLU ASP ILE ALA GLY HIS
SEQRES 26 A 349 LEU GLY LEU PHE ASN VAL SER GLU ASN TYR ILE PRO GLN
SEQRES 27 A 349 ILE ASP LYS ASN LEU LYS GLU LEU PHE GLU SER
SEQRES 1 B 349 MET LEU ASP ASN SER PHE TYR THR ALA GLU VAL GLN GLY
SEQRES 2 B 349 PRO TYR GLU THR ALA SER ILE GLY ARG LEU GLU LEU GLU
SEQRES 3 B 349 GLU GLY GLY VAL ILE GLU ASP CYS TRP LEU ALA TYR ALA
SEQRES 4 B 349 THR ALA GLY THR LEU ASN GLU ASP LYS SER ASN ALA ILE
SEQRES 5 B 349 LEU ILE PRO THR TRP TYR SER GLY THR HIS GLN THR TRP
SEQRES 6 B 349 PHE GLN GLN TYR ILE GLY THR ASP HIS ALA LEU ASP PRO
SEQRES 7 B 349 SER LYS TYR PHE ILE ILE SER ILE ASN GLN ILE GLY ASN
SEQRES 8 B 349 GLY LEU SER VAL SER PRO ALA ASN THR ALA ASP ASP SER
SEQRES 9 B 349 ILE SER MET SER LYS PHE PRO ASN VAL ARG ILE GLY ASP
SEQRES 10 B 349 ASP VAL VAL ALA GLN ASP ARG LEU LEU ARG GLN GLU PHE
SEQRES 11 B 349 GLY ILE THR GLU LEU PHE ALA VAL VAL GLY GLY SER MET
SEQRES 12 B 349 GLY ALA GLN GLN THR TYR GLU TRP ILE VAL ARG PHE PRO
SEQRES 13 B 349 ASP GLN VAL HIS ARG ALA ALA PRO ILE ALA GLY THR ALA
SEQRES 14 B 349 LYS ASN THR PRO HIS ASP PHE ILE PHE THR GLN THR LEU
SEQRES 15 B 349 ASN GLU THR VAL GLU ALA ASP PRO GLY PHE ASN GLY GLY
SEQRES 16 B 349 GLU TYR SER SER HIS GLU GLU VAL ALA ASP GLY LEU ARG
SEQRES 17 B 349 ARG GLN SER HIS LEU TRP ALA ALA MET GLY PHE SER THR
SEQRES 18 B 349 GLU PHE TRP LYS GLN GLU ALA TRP ARG ARG LEU GLY LEU
SEQRES 19 B 349 GLU SER LYS GLU SER VAL LEU ALA ASP PHE LEU ASP PRO
SEQRES 20 B 349 LEU PHE MET SER MET ASP PRO ASN THR LEU LEU ASN ASN
SEQRES 21 B 349 ALA TRP LYS TRP GLN HIS GLY ASP VAL SER ARG HIS THR
SEQRES 22 B 349 GLY GLY ASP LEU ALA ALA ALA LEU GLY ARG VAL LYS ALA
SEQRES 23 B 349 LYS THR PHE VAL MET PRO ILE SER GLU ASP MET PHE PHE
SEQRES 24 B 349 PRO VAL ARG ASP CYS ALA ALA GLU GLN ALA LEU ILE PRO
SEQRES 25 B 349 GLY SER GLU LEU ARG VAL ILE GLU ASP ILE ALA GLY HIS
SEQRES 26 B 349 LEU GLY LEU PHE ASN VAL SER GLU ASN TYR ILE PRO GLN
SEQRES 27 B 349 ILE ASP LYS ASN LEU LYS GLU LEU PHE GLU SER
HET GOL A 401 6
HET GOL A 402 6
HET GOL A 403 6
HET GOL A 404 6
HET GOL A 405 6
HET GOL A 406 6
HET GOL B 401 6
HET GOL B 402 6
HET GOL B 403 6
HET GOL B 404 6
HET GOL B 405 6
HET GOL B 406 6
HET GOL B 407 6
HET GOL B 408 6
HET GOL B 409 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 15(C3 H8 O3)
FORMUL 18 HOH *17(H2 O)
HELIX 1 AA1 THR A 8 GLY A 13 1 6
HELIX 2 AA2 HIS A 62 TYR A 69 1 8
HELIX 3 AA3 SER A 106 PHE A 110 5 5
HELIX 4 AA4 ARG A 114 GLY A 131 1 18
HELIX 5 AA5 SER A 142 PHE A 155 1 14
HELIX 6 AA6 PRO A 156 VAL A 159 5 4
HELIX 7 AA7 THR A 172 ALA A 188 1 17
HELIX 8 AA8 ASP A 189 GLU A 196 5 8
HELIX 9 AA9 SER A 199 GLU A 202 5 4
HELIX 10 AB1 VAL A 203 GLY A 218 1 16
HELIX 11 AB2 SER A 220 GLN A 226 1 7
HELIX 12 AB3 GLU A 227 GLY A 233 5 7
HELIX 13 AB4 SER A 236 ASP A 243 1 8
HELIX 14 AB5 PHE A 244 MET A 250 1 7
HELIX 15 AB6 ASP A 253 HIS A 266 1 14
HELIX 16 AB7 GLY A 267 GLY A 274 5 8
HELIX 17 AB8 ASP A 276 ARG A 283 1 8
HELIX 18 AB9 PRO A 300 ALA A 309 1 10
HELIX 19 AC1 ALA A 323 ASN A 330 5 8
HELIX 20 AC2 ASN A 334 SER A 349 1 16
HELIX 21 AC3 THR B 8 GLY B 13 1 6
HELIX 22 AC4 HIS B 62 TYR B 69 1 8
HELIX 23 AC5 SER B 106 PHE B 110 5 5
HELIX 24 AC6 ARG B 114 GLY B 131 1 18
HELIX 25 AC7 SER B 142 PHE B 155 1 14
HELIX 26 AC8 PRO B 156 VAL B 159 5 4
HELIX 27 AC9 THR B 172 ALA B 188 1 17
HELIX 28 AD1 ASP B 189 GLU B 196 5 8
HELIX 29 AD2 SER B 199 GLU B 202 5 4
HELIX 30 AD3 VAL B 203 GLY B 218 1 16
HELIX 31 AD4 SER B 220 GLN B 226 1 7
HELIX 32 AD5 GLU B 227 GLY B 233 5 7
HELIX 33 AD6 SER B 236 ASP B 243 1 8
HELIX 34 AD7 PHE B 244 MET B 250 1 7
HELIX 35 AD8 ASP B 253 HIS B 266 1 14
HELIX 36 AD9 GLY B 267 GLY B 274 5 8
HELIX 37 AE1 ASP B 276 ARG B 283 1 8
HELIX 38 AE2 PRO B 300 ALA B 309 1 10
HELIX 39 AE3 ALA B 323 ASN B 330 5 8
HELIX 40 AE4 ASN B 334 SER B 349 1 16
SHEET 1 AA1 8 GLU A 16 GLU A 24 0
SHEET 2 AA1 8 VAL A 30 ALA A 41 -1 O TYR A 38 N GLU A 16
SHEET 3 AA1 8 PHE A 82 ILE A 86 -1 O SER A 85 N ALA A 39
SHEET 4 AA1 8 ALA A 51 LEU A 53 1 N ILE A 52 O PHE A 82
SHEET 5 AA1 8 ALA A 137 GLY A 141 1 O VAL A 139 N LEU A 53
SHEET 6 AA1 8 ARG A 161 ILE A 165 1 O ILE A 165 N GLY A 140
SHEET 7 AA1 8 LYS A 287 VAL A 290 1 O LYS A 287 N ALA A 162
SHEET 8 AA1 8 GLU A 315 LEU A 316 1 O GLU A 315 N THR A 288
SHEET 1 AA2 8 GLU B 16 GLU B 24 0
SHEET 2 AA2 8 VAL B 30 ALA B 41 -1 O TYR B 38 N GLU B 16
SHEET 3 AA2 8 PHE B 82 ILE B 86 -1 O SER B 85 N ALA B 39
SHEET 4 AA2 8 ALA B 51 LEU B 53 1 N ILE B 52 O PHE B 82
SHEET 5 AA2 8 ALA B 137 GLY B 141 1 O VAL B 139 N LEU B 53
SHEET 6 AA2 8 ARG B 161 ILE B 165 1 O ILE B 165 N GLY B 140
SHEET 7 AA2 8 LYS B 287 VAL B 290 1 O LYS B 287 N ALA B 162
SHEET 8 AA2 8 GLU B 315 LEU B 316 1 O GLU B 315 N THR B 288
SITE 1 AC1 2 THR A 17 GOL A 406
SITE 1 AC2 2 TYR A 15 THR A 17
SITE 1 AC3 1 LEU A 44
SITE 1 AC4 4 PHE A 244 PHE A 329 ASN A 330 HOH A 502
SITE 1 AC5 1 GOL A 401
SITE 1 AC6 1 GOL B 407
SITE 1 AC7 1 GOL B 403
SITE 1 AC8 2 GLN B 63 GOL B 402
SITE 1 AC9 8 TRP B 57 TYR B 58 SER B 59 SER B 142
SITE 2 AC9 8 TRP B 214 HIS B 325 LEU B 326 PHE B 329
SITE 1 AD1 2 ARG B 231 GOL B 409
SITE 1 AD2 1 GOL B 401
SITE 1 AD3 3 PHE B 244 ASN B 330 GOL B 405
CRYST1 143.393 143.393 197.783 90.00 90.00 120.00 P 31 2 1 12
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 0.006974 0.004026 0.000000 0.00000
SCALE2 0.000000 0.008053 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005056 0.00000
TER 2754 SER A 349
TER 5508 SER B 349
MASTER 370 0 15 40 16 0 13 6 5591 2 90 54
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