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HEADER HYDROLASE 27-SEP-19 6SYA
TITLE STRUCTURE OF S192A-ESTER-HYDROLASE EH3 FROM THE METAGENOME OF MARINE
TITLE 2 SEDIMENTS AT MILAZZO HARBOR (SICILY, ITALY) COMPLEXED WITH METHYL
TITLE 3 (2R)-2-PHENYLPROPANOATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI MC1061;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 1211845;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PBXNH3
KEYWDS ESTER HYDROLASE, COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.CEA-RAMA,J.SANZ-APARICIO
REVDAT 1 07-APR-21 6SYA 0
JRNL AUTH I.CEA-RAMA,J.SANZ-APARICIO
JRNL TITL STRUCTURE OF S192A-ESTER-HYDROLASE EH3 FROM THE METAGENOME
JRNL TITL 2 OF MARINE SEDIMENTS AT MILAZZO HARBOR (SICILY, ITALY)
JRNL TITL 3 COMPLEXED WITH METHYL (2R)-2-PHENYLPROPANOATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.27 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
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) : 2.27
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 28826
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1531
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) : 2.27
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.33
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2123
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.51
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE SET COUNT : 122
REMARK 3 BIN FREE R VALUE : 0.2900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5146
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 72
REMARK 3 SOLVENT ATOMS : 247
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.91000
REMARK 3 B22 (A**2) : -2.10000
REMARK 3 B33 (A**2) : -0.81000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.09000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.433
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.243
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.180
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.242
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5326 ; 0.004 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4889 ; 0.003 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7201 ; 1.413 ; 1.645
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11385 ; 1.261 ; 1.581
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 681 ; 6.556 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 266 ;34.774 ;23.459
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 880 ;13.692 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;18.893 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 694 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6033 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1041 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 9 346 B 9 346 11158 0.060 0.050
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6SYA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-SEP-19.
REMARK 100 THE DEPOSITION ID IS D_1292104541.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-SEP-18
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 : ALBA
REMARK 200 BEAMLINE : XALOC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97924
REMARK 200 MONOCHROMATOR : SI(111) CHANNEL-CUT, CRYOCOOLED
REMARK 200 OPTICS : KB FOCUSING MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 1.11.12
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30378
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.270
REMARK 200 RESOLUTION RANGE LOW (A) : 45.960
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.17200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.65600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 6SXP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG3000, 0.2M MGCL2X6H2O, 0.1M BIS
REMARK 280 -TRIS PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 92.04900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.58550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 92.04900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.58550
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: 3910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 MET A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 LEU A -7
REMARK 465 GLU A -6
REMARK 465 VAL A -5
REMARK 465 LEU A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 GLY A -1
REMARK 465 PRO A 0
REMARK 465 SER A 1
REMARK 465 PRO A 2
REMARK 465 ASP A 3
REMARK 465 THR A 4
REMARK 465 THR A 5
REMARK 465 SER A 6
REMARK 465 LEU A 7
REMARK 465 ASN A 8
REMARK 465 GLY A 348
REMARK 465 ALA A 349
REMARK 465 MET B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 LEU B -7
REMARK 465 GLU B -6
REMARK 465 VAL B -5
REMARK 465 LEU B -4
REMARK 465 PHE B -3
REMARK 465 GLN B -2
REMARK 465 GLY B -1
REMARK 465 PRO B 0
REMARK 465 SER B 1
REMARK 465 PRO B 2
REMARK 465 ASP B 3
REMARK 465 THR B 4
REMARK 465 THR B 5
REMARK 465 SER B 6
REMARK 465 LEU B 7
REMARK 465 ASN B 8
REMARK 465 ALA B 349
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 MET A 28 73.09 66.31
REMARK 500 MET A 117 168.94 75.86
REMARK 500 ASP A 142 76.07 -106.29
REMARK 500 LEU A 147 -55.78 -125.63
REMARK 500 SER A 150 -154.55 -87.97
REMARK 500 PRO A 159 31.35 -98.14
REMARK 500 ALA A 192 -120.14 62.62
REMARK 500 CYS A 221 57.58 34.39
REMARK 500 ILE A 224 -9.00 -141.18
REMARK 500 MET A 243 -55.21 72.62
REMARK 500 HIS A 321 122.77 -39.52
REMARK 500 GLN B 31 -2.19 88.43
REMARK 500 MET B 117 167.96 75.99
REMARK 500 ASP B 142 75.47 -106.05
REMARK 500 LEU B 147 -56.00 -125.45
REMARK 500 SER B 150 -154.50 -87.49
REMARK 500 PRO B 159 32.22 -98.40
REMARK 500 ALA B 192 -119.53 61.53
REMARK 500 CYS B 221 57.91 33.11
REMARK 500 ILE B 224 -9.41 -142.28
REMARK 500 MET B 243 -55.69 72.82
REMARK 500 HIS B 321 122.66 -39.82
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 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LY8 A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LY8 B 404
DBREF1 6SYA A 2 348 UNP A0A2K8JN75_9BACT
DBREF2 6SYA A A0A2K8JN75 2 348
DBREF1 6SYA B 2 348 UNP A0A2K8JN75_9BACT
DBREF2 6SYA B A0A2K8JN75 2 348
SEQADV 6SYA MET A -18 UNP A0A2K8JN7 INITIATING METHIONINE
SEQADV 6SYA HIS A -17 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA HIS A -16 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA HIS A -15 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA HIS A -14 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA HIS A -13 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA HIS A -12 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA HIS A -11 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA HIS A -10 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA HIS A -9 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA HIS A -8 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA LEU A -7 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA GLU A -6 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA VAL A -5 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA LEU A -4 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA PHE A -3 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA GLN A -2 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA GLY A -1 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA PRO A 0 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA SER A 1 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA ALA A 192 UNP A0A2K8JN7 SER 192 CONFLICT
SEQADV 6SYA ALA A 349 UNP A0A2K8JN7 INSERTION
SEQADV 6SYA MET B -18 UNP A0A2K8JN7 INITIATING METHIONINE
SEQADV 6SYA HIS B -17 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA HIS B -16 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA HIS B -15 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA HIS B -14 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA HIS B -13 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA HIS B -12 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA HIS B -11 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA HIS B -10 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA HIS B -9 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA HIS B -8 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA LEU B -7 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA GLU B -6 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA VAL B -5 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA LEU B -4 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA PHE B -3 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA GLN B -2 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA GLY B -1 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA PRO B 0 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA SER B 1 UNP A0A2K8JN7 EXPRESSION TAG
SEQADV 6SYA ALA B 192 UNP A0A2K8JN7 SER 192 CONFLICT
SEQADV 6SYA ALA B 349 UNP A0A2K8JN7 INSERTION
SEQRES 1 A 368 MET HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS LEU GLU
SEQRES 2 A 368 VAL LEU PHE GLN GLY PRO SER PRO ASP THR THR SER LEU
SEQRES 3 A 368 ASN ILE ALA ASP ASP VAL ARG MET ASP PRO ARG LEU LYS
SEQRES 4 A 368 ALA MET LEU ALA ALA PHE PRO MET MET GLU GLN GLN THR
SEQRES 5 A 368 PHE GLN THR ARG GLU GLU GLN VAL ALA ASN ALA ASN THR
SEQRES 6 A 368 PRO GLU ALA THR ALA ALA ARG GLU GLN LEU LYS MET MET
SEQRES 7 A 368 MET ASP MET MET ASP SER GLU GLU PHE ALA PRO SER ASP
SEQRES 8 A 368 ASN LEU ASP ILE SER THR ARG GLU PHE THR SER SER PRO
SEQRES 9 A 368 ASP GLY ASN ALA ILE LYS ILE GLN PHE ILE ARG PRO LYS
SEQRES 10 A 368 GLY LYS GLN LYS VAL PRO CYS VAL TYR TYR ILE HIS GLY
SEQRES 11 A 368 GLY GLY MET MET ILE MET SER ALA PHE TYR GLY ASN TYR
SEQRES 12 A 368 ARG ALA TRP GLY LYS MET ILE ALA ASN ASN GLY VAL ALA
SEQRES 13 A 368 VAL ALA MET VAL ASP PHE ARG ASN CYS LEU SER PRO SER
SEQRES 14 A 368 SER ALA PRO GLU VAL ALA PRO PHE PRO ALA GLY LEU ASN
SEQRES 15 A 368 ASP CYS VAL SER GLY LEU LYS TRP VAL SER GLU ASN ALA
SEQRES 16 A 368 ASP GLU LEU SER ILE ASP LYS ASN LYS ILE ILE ILE ALA
SEQRES 17 A 368 GLY GLU ALA GLY GLY GLY ASN LEU THR LEU ALA THR GLY
SEQRES 18 A 368 LEU LYS LEU LYS GLN ASP GLY ASN ILE ASP LEU VAL LYS
SEQRES 19 A 368 GLY LEU TYR ALA LEU CYS PRO TYR ILE ALA GLY LYS TRP
SEQRES 20 A 368 PRO GLN ASP ARG PHE PRO SER SER SER GLU ASN ASN GLY
SEQRES 21 A 368 ILE MET ILE GLU LEU HIS ASN ASN GLN GLY ALA LEU ALA
SEQRES 22 A 368 TYR GLY ILE GLU GLN LEU GLU ALA GLU ASN PRO LEU ALA
SEQRES 23 A 368 TRP PRO SER PHE ALA SER ALA GLU ASP MET GLN GLY LEU
SEQRES 24 A 368 PRO PRO THR VAL ILE ASN VAL ASN GLU CYS ASP PRO LEU
SEQRES 25 A 368 ARG ASP GLU GLY ILE ASP PHE TYR ARG ARG LEU MET ALA
SEQRES 26 A 368 ALA GLY VAL PRO ALA ARG CYS ARG GLN VAL MET GLY THR
SEQRES 27 A 368 CYS HIS ALA GLY ASP MET PHE VAL ALA VAL ILE PRO ASP
SEQRES 28 A 368 VAL SER ALA ASP THR ALA ALA ASP ILE ALA ARG THR ALA
SEQRES 29 A 368 LYS GLY GLY ALA
SEQRES 1 B 368 MET HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS LEU GLU
SEQRES 2 B 368 VAL LEU PHE GLN GLY PRO SER PRO ASP THR THR SER LEU
SEQRES 3 B 368 ASN ILE ALA ASP ASP VAL ARG MET ASP PRO ARG LEU LYS
SEQRES 4 B 368 ALA MET LEU ALA ALA PHE PRO MET MET GLU GLN GLN THR
SEQRES 5 B 368 PHE GLN THR ARG GLU GLU GLN VAL ALA ASN ALA ASN THR
SEQRES 6 B 368 PRO GLU ALA THR ALA ALA ARG GLU GLN LEU LYS MET MET
SEQRES 7 B 368 MET ASP MET MET ASP SER GLU GLU PHE ALA PRO SER ASP
SEQRES 8 B 368 ASN LEU ASP ILE SER THR ARG GLU PHE THR SER SER PRO
SEQRES 9 B 368 ASP GLY ASN ALA ILE LYS ILE GLN PHE ILE ARG PRO LYS
SEQRES 10 B 368 GLY LYS GLN LYS VAL PRO CYS VAL TYR TYR ILE HIS GLY
SEQRES 11 B 368 GLY GLY MET MET ILE MET SER ALA PHE TYR GLY ASN TYR
SEQRES 12 B 368 ARG ALA TRP GLY LYS MET ILE ALA ASN ASN GLY VAL ALA
SEQRES 13 B 368 VAL ALA MET VAL ASP PHE ARG ASN CYS LEU SER PRO SER
SEQRES 14 B 368 SER ALA PRO GLU VAL ALA PRO PHE PRO ALA GLY LEU ASN
SEQRES 15 B 368 ASP CYS VAL SER GLY LEU LYS TRP VAL SER GLU ASN ALA
SEQRES 16 B 368 ASP GLU LEU SER ILE ASP LYS ASN LYS ILE ILE ILE ALA
SEQRES 17 B 368 GLY GLU ALA GLY GLY GLY ASN LEU THR LEU ALA THR GLY
SEQRES 18 B 368 LEU LYS LEU LYS GLN ASP GLY ASN ILE ASP LEU VAL LYS
SEQRES 19 B 368 GLY LEU TYR ALA LEU CYS PRO TYR ILE ALA GLY LYS TRP
SEQRES 20 B 368 PRO GLN ASP ARG PHE PRO SER SER SER GLU ASN ASN GLY
SEQRES 21 B 368 ILE MET ILE GLU LEU HIS ASN ASN GLN GLY ALA LEU ALA
SEQRES 22 B 368 TYR GLY ILE GLU GLN LEU GLU ALA GLU ASN PRO LEU ALA
SEQRES 23 B 368 TRP PRO SER PHE ALA SER ALA GLU ASP MET GLN GLY LEU
SEQRES 24 B 368 PRO PRO THR VAL ILE ASN VAL ASN GLU CYS ASP PRO LEU
SEQRES 25 B 368 ARG ASP GLU GLY ILE ASP PHE TYR ARG ARG LEU MET ALA
SEQRES 26 B 368 ALA GLY VAL PRO ALA ARG CYS ARG GLN VAL MET GLY THR
SEQRES 27 B 368 CYS HIS ALA GLY ASP MET PHE VAL ALA VAL ILE PRO ASP
SEQRES 28 B 368 VAL SER ALA ASP THR ALA ALA ASP ILE ALA ARG THR ALA
SEQRES 29 B 368 LYS GLY GLY ALA
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 LY8 A 406 12
HET GOL B 401 6
HET GOL B 402 6
HET GOL B 403 6
HET LY8 B 404 12
HETNAM GOL GLYCEROL
HETNAM LY8 METHYL (2~{R})-2-PHENYLPROPANOATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 8(C3 H8 O3)
FORMUL 8 LY8 2(C10 H12 O2)
FORMUL 13 HOH *247(H2 O)
HELIX 1 AA1 ASP A 16 ALA A 25 1 10
HELIX 2 AA2 THR A 36 ASN A 45 1 10
HELIX 3 AA3 THR A 46 MET A 62 1 17
HELIX 4 AA4 TYR A 121 ASN A 133 1 13
HELIX 5 AA5 PRO A 159 ASN A 175 1 17
HELIX 6 AA6 ASN A 175 SER A 180 1 6
HELIX 7 AA7 ALA A 192 ASP A 208 1 17
HELIX 8 AA8 ASN A 210 VAL A 214 5 5
HELIX 9 AA9 PRO A 234 ASN A 239 1 6
HELIX 10 AB1 ASN A 249 ALA A 262 1 14
HELIX 11 AB2 TRP A 268 ALA A 272 5 5
HELIX 12 AB3 SER A 273 GLN A 278 1 6
HELIX 13 AB4 LEU A 293 ALA A 307 1 15
HELIX 14 AB5 ALA A 322 PHE A 326 5 5
HELIX 15 AB6 ILE A 330 GLY A 347 1 18
HELIX 16 AB7 ASP B 16 PHE B 26 1 11
HELIX 17 AB8 THR B 36 ALA B 44 1 9
HELIX 18 AB9 THR B 46 MET B 62 1 17
HELIX 19 AC1 TYR B 121 ASN B 133 1 13
HELIX 20 AC2 PRO B 159 ASN B 175 1 17
HELIX 21 AC3 ASN B 175 SER B 180 1 6
HELIX 22 AC4 ALA B 192 ASP B 208 1 17
HELIX 23 AC5 ASN B 210 VAL B 214 5 5
HELIX 24 AC6 PRO B 234 ASN B 239 1 6
HELIX 25 AC7 ASN B 249 ALA B 262 1 14
HELIX 26 AC8 TRP B 268 ALA B 272 5 5
HELIX 27 AC9 SER B 273 GLN B 278 1 6
HELIX 28 AD1 LEU B 293 ALA B 307 1 15
HELIX 29 AD2 ALA B 322 PHE B 326 5 5
HELIX 30 AD3 ILE B 330 GLY B 347 1 18
SHEET 1 AA116 LEU A 74 THR A 82 0
SHEET 2 AA116 ALA A 89 PRO A 97 -1 O PHE A 94 N SER A 77
SHEET 3 AA116 ALA A 137 ASP A 142 -1 O VAL A 138 N ILE A 95
SHEET 4 AA116 VAL A 103 ILE A 109 1 N VAL A 106 O ALA A 137
SHEET 5 AA116 ILE A 181 GLU A 191 1 O ILE A 187 N TYR A 107
SHEET 6 AA116 GLY A 216 LEU A 220 1 O LEU A 220 N GLY A 190
SHEET 7 AA116 THR A 283 ASN A 288 1 O VAL A 284 N ALA A 219
SHEET 8 AA116 ALA A 311 VAL A 316 1 O VAL A 316 N VAL A 287
SHEET 9 AA116 ALA B 311 VAL B 316 -1 O GLN B 315 N GLN A 315
SHEET 10 AA116 THR B 283 ASN B 288 1 N VAL B 287 O VAL B 316
SHEET 11 AA116 GLY B 216 LEU B 220 1 N ALA B 219 O VAL B 284
SHEET 12 AA116 ILE B 181 GLU B 191 1 N GLY B 190 O LEU B 220
SHEET 13 AA116 VAL B 103 ILE B 109 1 N TYR B 107 O ILE B 187
SHEET 14 AA116 ALA B 137 ASP B 142 1 O ALA B 137 N VAL B 106
SHEET 15 AA116 ALA B 89 PRO B 97 -1 N ILE B 95 O VAL B 138
SHEET 16 AA116 LEU B 74 THR B 82 -1 N SER B 77 O PHE B 94
CISPEP 1 SER A 84 PRO A 85 0 6.24
CISPEP 2 SER A 84 PRO A 85 0 6.56
CISPEP 3 PHE A 158 PRO A 159 0 -0.44
CISPEP 4 TRP A 228 PRO A 229 0 -2.13
CISPEP 5 SER B 84 PRO B 85 0 3.74
CISPEP 6 SER B 84 PRO B 85 0 5.12
CISPEP 7 PHE B 158 PRO B 159 0 -1.02
CISPEP 8 TRP B 228 PRO B 229 0 -2.00
SITE 1 AC1 8 TYR A 223 TRP A 228 GLU A 245 LEU A 246
SITE 2 AC1 8 ASN A 248 GLN A 250 GLY A 251 LY8 A 406
SITE 1 AC2 2 MET A 63 MET B 63
SITE 1 AC3 4 ILE A 211 ASP A 212 HOH A 566 HOH A 575
SITE 1 AC4 1 GLN A 259
SITE 1 AC5 8 GLN A 55 MET A 305 GLY A 308 VAL A 309
SITE 2 AC5 8 ALA A 311 ASP B 16 ARG B 18 HOH B 501
SITE 1 AC6 8 GLY A 112 GLY A 113 ALA A 192 GLY A 193
SITE 2 AC6 8 TYR A 223 HIS A 321 GOL A 401 HOH A 513
SITE 1 AC7 10 GLY B 111 GLY B 112 MET B 117 ASN B 123
SITE 2 AC7 10 TYR B 124 GLU B 191 ALA B 192 MET B 243
SITE 3 AC7 10 PHE B 326 LY8 B 404
SITE 1 AC8 7 TYR B 223 TRP B 228 GLU B 245 ASN B 248
SITE 2 AC8 7 GLN B 250 GLY B 251 LY8 B 404
SITE 1 AC9 6 ARG A 294 GLN A 315 ARG B 294 ILE B 298
SITE 2 AC9 6 GLN B 315 HOH B 587
SITE 1 AD1 9 MET B 29 GLY B 112 GLY B 113 ALA B 192
SITE 2 AD1 9 GLY B 193 TYR B 223 HIS B 321 GOL B 401
SITE 3 AD1 9 GOL B 402
CRYST1 184.098 51.171 70.437 90.00 93.96 90.00 C 1 2 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 0.005432 0.000000 0.000376 0.00000
SCALE2 0.000000 0.019542 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014231 0.00000
TER 2578 GLY A 347
TER 5160 GLY B 348
MASTER 386 0 10 30 16 0 19 6 5465 2 72 58
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