| content |
HEADER HYDROLASE 17-DEC-15 5FRD
TITLE STRUCTURE OF A THERMOPHILIC ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE (EST-2);
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ESTERASE;
COMPND 5 EC: 3.1.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 3 ORGANISM_TAXID: 2234;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: CODONPLUS-RIPL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET28
KEYWDS HYDROLASE, ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.SAYER,W.FINNIGAN,M.N.ISUPOV,M.LEVISSON,S.W.M.KENGEN,J.VAN DER OOST,
AUTHOR 2 N.HARMER,J.A.LITTLECHILD
REVDAT 1 25-MAY-16 5FRD 0
JRNL AUTH C.SAYER,W.FINNIGAN,M.N.ISUPOV,M.LEVISSON,S.W.KENGEN,
JRNL AUTH 2 J.VAN DER OOST,N.J.HARMER,J.A.LITTLECHILD
JRNL TITL STRUCTURAL AND BIOCHEMICAL CHARACTERISATION OF
JRNL TITL 2 ARCHAEOGLOBUS FULGIDUS ESTERASE REVEALS A BOUND COA
JRNL TITL 3 MOLECULE IN THE VICINITY OF THE ACTIVE SITE.
JRNL REF SCI.REP. V. 6 25542 2016
JRNL REFN ISSN 2045-2322
JRNL PMID 27160974
JRNL DOI 10.1038/SREP25542
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.29
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.77
REMARK 3 NUMBER OF REFLECTIONS : 100085
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) : 0.15686
REMARK 3 R VALUE (WORKING SET) : 0.15649
REMARK 3 FREE R VALUE : 0.17347
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2013
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) : 1.400
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.437
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6538
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.308
REMARK 3 BIN FREE R VALUE SET COUNT : 125
REMARK 3 BIN FREE R VALUE : 0.354
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4704
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 128
REMARK 3 SOLVENT ATOMS : 514
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.568
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.59
REMARK 3 B22 (A**2) : 0.41
REMARK 3 B33 (A**2) : -0.99
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.058
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.057
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.043
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.107
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.970
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5024 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5109 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6935 ; 1.631 ; 2.019
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11981 ; 1.394 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 716 ; 5.236 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 237 ;37.053 ;24.473
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1048 ;14.495 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;13.126 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 776 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5701 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1091 ; 0.006 ; 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): 2287 ; 3.612 ; 7.640
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2286 ; 3.589 ; 7.635
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2915 ; 4.658 ;11.434
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2737 ; 7.484 ;10.332
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 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 : MASK
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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 5FRD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-DEC-15.
REMARK 100 THE PDBE ID CODE IS EBI-65800.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 102188
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.40
REMARK 200 RESOLUTION RANGE LOW (A) : 70.30
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 5.6
REMARK 200 R MERGE (I) : 0.04
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.5
REMARK 200 R MERGE FOR SHELL (I) : 0.46
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.00
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: PDB ENTRY 1A8Q
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.4
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 27.53500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.28500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.60000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.28500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.53500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.60000
REMARK 290 SMTRY3 4 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 HIS A 257
REMARK 465 HIS A 258
REMARK 465 HIS A 259
REMARK 465 HIS A 260
REMARK 465 GLU B 253
REMARK 465 VAL B 254
REMARK 465 HIS B 255
REMARK 465 HIS B 256
REMARK 465 HIS B 257
REMARK 465 HIS B 258
REMARK 465 HIS B 259
REMARK 465 HIS B 260
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD2B ASP A 8 O HOH A 2025 1.95
REMARK 500 CD B ARG A 20 O HOH A 2042 1.80
REMARK 500 NE B ARG A 20 O HOH A 2042 1.25
REMARK 500 CZ B ARG A 20 O HOH A 2042 0.94
REMARK 500 NH1B ARG A 20 O HOH A 2042 1.15
REMARK 500 OE2A GLU A 21 O HOH A 2046 2.13
REMARK 500 CD C GLU A 21 O HOH A 2037 1.96
REMARK 500 OE2C GLU A 21 O HOH A 2037 1.33
REMARK 500 CD A ARG A 101 O HOH A 2110 1.88
REMARK 500 NE A ARG A 101 O HOH A 2110 1.25
REMARK 500 CZ A ARG A 101 O HOH A 2110 1.67
REMARK 500 CD A GLU A 149 O HOH A 2172 2.08
REMARK 500 OE1A GLU A 149 O HOH A 2172 1.76
REMARK 500 OE2A GLU A 149 O HOH A 2172 1.94
REMARK 500 CD B GLU A 150 O HOH A 2170 2.05
REMARK 500 OE1B GLU A 150 O HOH A 2170 1.12
REMARK 500 NZ B LYS A 154 O HOH A 2064 1.07
REMARK 500 CD B GLU A 219 O HOH A 2238 1.63
REMARK 500 OE2B GLU A 219 O HOH A 2238 0.78
REMARK 500 OE2A GLU A 243 O HOH A 2050 1.74
REMARK 500 CD B GLU A 243 O HOH A 2082 1.99
REMARK 500 CD B GLU A 243 O HOH A 2250 1.85
REMARK 500 OE1B GLU A 243 O HOH A 2250 0.81
REMARK 500 OE2B GLU A 243 O HOH A 2082 1.36
REMARK 500 CZ A ARG B 20 O HOH B 2022 1.92
REMARK 500 NH1A ARG B 20 O HOH B 2022 0.93
REMARK 500 NZ B LYS B 23 O HOH B 2031 0.95
REMARK 500 CD B GLU B 61 O HOH B 2064 2.16
REMARK 500 OE1B GLU B 61 O HOH B 2064 1.17
REMARK 500 ND2B ASN B 63 O HOH B 2069 1.98
REMARK 500 OE2B GLU B 67 O HOH B 2065 1.62
REMARK 500 CD A ARG B 101 O HOH B 2074 1.85
REMARK 500 NE A ARG B 101 O HOH B 2074 1.25
REMARK 500 CZ A ARG B 101 O HOH B 2074 1.95
REMARK 500 CD B GLU B 104 O HOH B 2095 1.66
REMARK 500 OE2B GLU B 104 O HOH B 2095 0.47
REMARK 500 OE2A GLU B 126 O HOH B 2116 1.79
REMARK 500 OE1A GLU B 131 O HOH B 2123 2.04
REMARK 500 OE2B GLU B 131 O HOH B 2108 2.14
REMARK 500 OE1B GLU B 152 O HOH B 2149 1.63
REMARK 500 CD A ARG B 156 O HOH B 2160 1.50
REMARK 500 CE B LYS B 201 O HOH B 2201 2.04
REMARK 500 NZ B LYS B 201 O HOH B 2201 1.00
REMARK 500 OE2A GLU B 219 O HOH B 2190 1.25
REMARK 500 OE2A GLU B 240 O HOH B 2228 1.80
REMARK 500 CD B GLU B 243 O HOH B 2225 1.78
REMARK 500 OE1B GLU B 243 O HOH B 2225 1.63
REMARK 500 OE2B GLU B 243 O HOH B 2225 1.96
REMARK 500 O HOH A 2017 O HOH A 2032 2.18
REMARK 500 O HOH A 2032 O HOH A 2033 1.70
REMARK 500
REMARK 500 THIS ENTRY HAS 56 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2B ARG A 182 OE2B GLU B 61 3545 2.18
REMARK 500 OE1A GLU B 126 OE2B GLU B 237 3455 1.66
REMARK 500 OE1B GLU B 126 OE1B GLU B 237 3455 1.71
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 SER A 32 -164.69 -116.98
REMARK 500 SER A 89 -117.16 56.10
REMARK 500 SER A 227 -141.22 -112.69
REMARK 500 MET A 229 44.53 -89.02
REMARK 500 SER B 32 -165.24 -114.64
REMARK 500 ASN B 53 -0.84 80.52
REMARK 500 SER B 89 -117.20 57.29
REMARK 500 ASN B 217 28.65 -68.69
REMARK 500 SER B 227 -140.59 -107.99
REMARK 500 MET B 229 48.73 -89.47
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 PGE B1253
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC B1254
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA B1255
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A1257
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1258
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1257
DBREF 5FRD A 1 256 UNP O28735 O28735_ARCFU 1 256
DBREF 5FRD B 1 252 UNP O28735 O28735_ARCFU 1 252
SEQADV 5FRD HIS A 257 UNP O28735 EXPRESSION TAG
SEQADV 5FRD HIS A 258 UNP O28735 EXPRESSION TAG
SEQADV 5FRD HIS A 259 UNP O28735 EXPRESSION TAG
SEQADV 5FRD HIS A 260 UNP O28735 EXPRESSION TAG
SEQADV 5FRD GLU B 253 UNP O28735 EXPRESSION TAG
SEQADV 5FRD VAL B 254 UNP O28735 EXPRESSION TAG
SEQADV 5FRD HIS B 255 UNP O28735 EXPRESSION TAG
SEQADV 5FRD HIS B 256 UNP O28735 EXPRESSION TAG
SEQADV 5FRD HIS B 257 UNP O28735 EXPRESSION TAG
SEQADV 5FRD HIS B 258 UNP O28735 EXPRESSION TAG
SEQADV 5FRD HIS B 259 UNP O28735 EXPRESSION TAG
SEQADV 5FRD HIS B 260 UNP O28735 EXPRESSION TAG
SEQRES 1 A 260 MET LEU GLU ARG VAL PHE ILE ASP VAL ASP GLY VAL LYS
SEQRES 2 A 260 VAL SER LEU LEU LYS GLY ARG GLU ARG LYS VAL PHE TYR
SEQRES 3 A 260 ILE HIS SER SER GLY SER ASP ALA THR GLN TRP VAL ASN
SEQRES 4 A 260 GLN LEU THR ALA ILE GLY GLY TYR ALA ILE ASP LEU PRO
SEQRES 5 A 260 ASN HIS GLY GLN SER ASP THR VAL GLU VAL ASN SER VAL
SEQRES 6 A 260 ASP GLU TYR ALA TYR TYR ALA SER GLU SER LEU LYS LYS
SEQRES 7 A 260 THR VAL GLY LYS ALA VAL VAL VAL GLY HIS SER LEU GLY
SEQRES 8 A 260 GLY ALA VAL ALA GLN LYS LEU TYR LEU ARG ASN PRO GLU
SEQRES 9 A 260 ILE CYS LEU ALA LEU VAL LEU VAL GLY THR GLY ALA ARG
SEQRES 10 A 260 LEU ARG VAL LEU PRO GLU ILE LEU GLU GLY LEU LYS LYS
SEQRES 11 A 260 GLU PRO GLU LYS ALA VAL ASP LEU MET LEU SER MET ALA
SEQRES 12 A 260 PHE ALA SER LYS GLY GLU GLU TYR GLU LYS LYS ARG ARG
SEQRES 13 A 260 GLU PHE LEU ASP ARG VAL ASP VAL LEU HIS LEU ASP LEU
SEQRES 14 A 260 SER LEU CYS ASP ARG PHE ASP LEU LEU GLU ASP TYR ARG
SEQRES 15 A 260 ASN GLY LYS LEU LYS ILE GLY VAL PRO THR LEU VAL ILE
SEQRES 16 A 260 VAL GLY GLU GLU ASP LYS LEU THR PRO LEU LYS TYR HIS
SEQRES 17 A 260 GLU PHE PHE HIS LYS HIS ILE PRO ASN SER GLU LEU VAL
SEQRES 18 A 260 VAL ILE PRO GLY ALA SER HIS MET VAL MET LEU GLU LYS
SEQRES 19 A 260 HIS VAL GLU PHE ASN GLU ALA LEU GLU LYS PHE LEU LYS
SEQRES 20 A 260 LYS VAL GLY VAL ALA GLU VAL HIS HIS HIS HIS HIS HIS
SEQRES 1 B 260 MET LEU GLU ARG VAL PHE ILE ASP VAL ASP GLY VAL LYS
SEQRES 2 B 260 VAL SER LEU LEU LYS GLY ARG GLU ARG LYS VAL PHE TYR
SEQRES 3 B 260 ILE HIS SER SER GLY SER ASP ALA THR GLN TRP VAL ASN
SEQRES 4 B 260 GLN LEU THR ALA ILE GLY GLY TYR ALA ILE ASP LEU PRO
SEQRES 5 B 260 ASN HIS GLY GLN SER ASP THR VAL GLU VAL ASN SER VAL
SEQRES 6 B 260 ASP GLU TYR ALA TYR TYR ALA SER GLU SER LEU LYS LYS
SEQRES 7 B 260 THR VAL GLY LYS ALA VAL VAL VAL GLY HIS SER LEU GLY
SEQRES 8 B 260 GLY ALA VAL ALA GLN LYS LEU TYR LEU ARG ASN PRO GLU
SEQRES 9 B 260 ILE CYS LEU ALA LEU VAL LEU VAL GLY THR GLY ALA ARG
SEQRES 10 B 260 LEU ARG VAL LEU PRO GLU ILE LEU GLU GLY LEU LYS LYS
SEQRES 11 B 260 GLU PRO GLU LYS ALA VAL ASP LEU MET LEU SER MET ALA
SEQRES 12 B 260 PHE ALA SER LYS GLY GLU GLU TYR GLU LYS LYS ARG ARG
SEQRES 13 B 260 GLU PHE LEU ASP ARG VAL ASP VAL LEU HIS LEU ASP LEU
SEQRES 14 B 260 SER LEU CYS ASP ARG PHE ASP LEU LEU GLU ASP TYR ARG
SEQRES 15 B 260 ASN GLY LYS LEU LYS ILE GLY VAL PRO THR LEU VAL ILE
SEQRES 16 B 260 VAL GLY GLU GLU ASP LYS LEU THR PRO LEU LYS TYR HIS
SEQRES 17 B 260 GLU PHE PHE HIS LYS HIS ILE PRO ASN SER GLU LEU VAL
SEQRES 18 B 260 VAL ILE PRO GLY ALA SER HIS MET VAL MET LEU GLU LYS
SEQRES 19 B 260 HIS VAL GLU PHE ASN GLU ALA LEU GLU LYS PHE LEU LYS
SEQRES 20 B 260 LYS VAL GLY VAL ALA GLU VAL HIS HIS HIS HIS HIS HIS
HET PGE B1253 10
HET FLC B1254 13
HET COA B1255 48
HET COA A1257 48
HET CL B1256 1
HET CL A1258 1
HET PEG B1257 7
HETNAM COA COENZYME A
HETNAM FLC CITRATE ANION
HETNAM CL CHLORIDE ION
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 3 COA 2(C21 H36 N7 O16 P3 S)
FORMUL 4 FLC C6 H5 O7 3-
FORMUL 5 CL 2(CL 1-)
FORMUL 6 PGE C6 H14 O4
FORMUL 7 PEG C4 H10 O3
FORMUL 8 HOH *514(H2 O)
HELIX 1 1 ASP A 33 GLN A 36 5 4
HELIX 2 2 TRP A 37 ILE A 44 1 8
HELIX 3 3 SER A 64 VAL A 80 1 17
HELIX 4 4 SER A 89 ASN A 102 1 14
HELIX 5 5 LEU A 121 GLU A 126 1 6
HELIX 6 6 GLU A 126 GLU A 131 1 6
HELIX 7 7 GLU A 131 MET A 142 1 12
HELIX 8 8 GLY A 148 ARG A 161 1 14
HELIX 9 9 ARG A 161 ARG A 174 1 14
HELIX 10 10 LEU A 177 ASN A 183 1 7
HELIX 11 11 PRO A 204 ILE A 215 1 12
HELIX 12 12 MET A 229 LYS A 234 1 6
HELIX 13 13 LYS A 234 GLY A 250 1 17
HELIX 14 14 ASP B 33 GLN B 36 5 4
HELIX 15 15 TRP B 37 ILE B 44 1 8
HELIX 16 16 SER B 64 VAL B 80 1 17
HELIX 17 17 SER B 89 ASN B 102 1 14
HELIX 18 18 LEU B 121 GLU B 126 1 6
HELIX 19 19 GLU B 131 MET B 142 1 12
HELIX 20 20 GLY B 148 ARG B 161 1 14
HELIX 21 21 ARG B 161 ARG B 174 1 14
HELIX 22 22 LEU B 177 ASN B 183 1 7
HELIX 23 23 PRO B 204 ILE B 215 1 12
HELIX 24 24 MET B 229 LYS B 234 1 6
HELIX 25 25 LYS B 234 GLY B 250 1 17
SHEET 1 AA 8 GLU A 3 VAL A 9 0
SHEET 2 AA 8 VAL A 12 LYS A 18 -1 O VAL A 12 N VAL A 9
SHEET 3 AA 8 TYR A 47 ILE A 49 -1 O ALA A 48 N LEU A 17
SHEET 4 AA 8 VAL A 24 ILE A 27 1 O VAL A 24 N TYR A 47
SHEET 5 AA 8 ALA A 83 HIS A 88 1 O VAL A 84 N PHE A 25
SHEET 6 AA 8 CYS A 106 VAL A 112 1 N LEU A 107 O ALA A 83
SHEET 7 AA 8 THR A 192 GLY A 197 1 O LEU A 193 N LEU A 111
SHEET 8 AA 8 SER A 218 ILE A 223 1 O GLU A 219 N VAL A 194
SHEET 1 BA 8 GLU B 3 VAL B 9 0
SHEET 2 BA 8 VAL B 12 LYS B 18 -1 O VAL B 12 N VAL B 9
SHEET 3 BA 8 TYR B 47 ILE B 49 -1 O ALA B 48 N LEU B 17
SHEET 4 BA 8 VAL B 24 ILE B 27 1 O VAL B 24 N TYR B 47
SHEET 5 BA 8 ALA B 83 HIS B 88 1 O VAL B 84 N PHE B 25
SHEET 6 BA 8 CYS B 106 VAL B 112 1 N LEU B 107 O ALA B 83
SHEET 7 BA 8 THR B 192 GLY B 197 1 O LEU B 193 N LEU B 111
SHEET 8 BA 8 SER B 218 ILE B 223 1 O GLU B 219 N VAL B 194
SITE 1 AC1 4 THR B 42 GLU B 123 HOH B2241 HOH B2243
SITE 1 AC2 12 LYS A 153 ARG A 156 GLU A 157 ASP A 160
SITE 2 AC2 12 ARG A 161 HOH A2175 HOH A2183 GLU B 152
SITE 3 AC2 12 ARG B 155 HOH B2156 HOH B2159 HOH B2244
SITE 1 AC3 21 ALA B 116 ARG B 117 ARG B 119 VAL B 120
SITE 2 AC3 21 LEU B 121 GLU B 149 LEU B 202 LYS B 206
SITE 3 AC3 21 TYR B 207 HOH B2097 HOH B2098 HOH B2105
SITE 4 AC3 21 HOH B2152 HOH B2153 HOH B2184 HOH B2206
SITE 5 AC3 21 HOH B2245 HOH B2246 HOH B2247 HOH B2248
SITE 6 AC3 21 HOH B2249
SITE 1 AC4 14 ALA A 116 ARG A 117 ARG A 119 VAL A 120
SITE 2 AC4 14 LEU A 121 LEU A 202 TYR A 207 HOH A2139
SITE 3 AC4 14 HOH A2140 HOH A2143 HOH A2202 HOH A2227
SITE 4 AC4 14 HOH A2262 HOH A2263
SITE 1 AC5 4 SER B 30 SER B 89 LEU B 90 HOH B2090
SITE 1 AC6 3 SER A 30 SER A 89 LEU A 90
SITE 1 AC7 6 LEU A 2 HOH A2016 ARG B 182 GLY B 184
SITE 2 AC7 6 HOH B2182 HOH B2211
CRYST1 55.070 67.200 140.570 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018159 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014881 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007114 0.00000
MTRIX1 1 0.858880 0.493590 0.136720 -24.40808 1
MTRIX2 1 0.470640 -0.865900 0.169470 -0.45999 1
MTRIX3 1 0.202030 -0.081210 -0.976010 33.27924 1
TER 2407 HIS A 256
TER 4706 ALA B 252
MASTER 396 0 7 25 16 0 18 9 5346 2 126 40
END |