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HEADER HYDROLASE 03-NOV-20 7AUY
TITLE STRUCTURE OF ESTD11 IN COMPLEX WITH FLUORESCEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTD11;
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 BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET22
KEYWDS ESTERASE HORMONE-SENSITIVE LIPASE METAGENOME LIBRARY CRYSTAL
KEYWDS 2 STRUCTURE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.MIGUEL-RUANO,I.RIVERA,J.A.HERMOSO
REVDAT 1 03-MAR-21 7AUY 0
JRNL AUTH V.MIGUEL-RUANO,I.RIVERA,J.RAJKOVIC,K.KNAPIK,A.TORRADO,
JRNL AUTH 2 J.M.OTERO,E.BENEVENTI,M.BECERRA,M.SANCHEZ-COSTA,A.HIDALGO,
JRNL AUTH 3 J.BERENGUER,M.I.GONZALEZ-SISO,J.CRUCES,M.L.RUA,J.A.HERMOSO
JRNL TITL BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF A NOVEL
JRNL TITL 2 THERMOPHILIC ESTERASE ESTD11 PROVIDE CATALYTIC INSIGHTS FOR
JRNL TITL 3 THE HSL FAMILY
JRNL REF COMPUT STRUCT BIOTECHNOL J 2021
JRNL REFN ESSN 2001-0370
JRNL DOI 10.1016/J.CSBJ.2021.01.047
REMARK 2
REMARK 2 RESOLUTION. 2.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : 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) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 24960
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) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1304
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) : 2.28
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1831
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.3300
REMARK 3 BIN FREE R VALUE SET COUNT : 92
REMARK 3 BIN FREE R VALUE : 0.3790
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3985
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 103
REMARK 3 SOLVENT ATOMS : 43
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.82000
REMARK 3 B22 (A**2) : -0.44000
REMARK 3 B33 (A**2) : 3.26000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.343
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.228
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.192
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.595
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4193 ; 0.004 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 3992 ; 0.003 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5733 ; 1.380 ; 1.681
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9136 ; 1.180 ; 1.584
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 519 ; 5.852 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 219 ;29.007 ;20.046
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 644 ;17.330 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 45 ;22.767 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 528 ; 0.060 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4745 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 945 ; 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 3 295 B 3 295 7248 0.130 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 : 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 RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7AUY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-NOV-20.
REMARK 100 THE DEPOSITION ID IS D_1292112093.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-20
REMARK 200 TEMPERATURE (KELVIN) : 291
REMARK 200 PH : 5
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) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26303
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.280
REMARK 200 RESOLUTION RANGE LOW (A) : 48.180
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.28
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 1.20500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.100
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: 7AT0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.2M SODIUM FORMATE + 0.1M CITRIC ACID
REMARK 280 PH 5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
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 24.08800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.61350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.60050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 73.61350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.08800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.60050
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 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 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 MET A 1
REMARK 465 ILE A 180
REMARK 465 GLY A 181
REMARK 465 GLU A 182
REMARK 465 SER A 183
REMARK 465 MET A 184
REMARK 465 THR A 185
REMARK 465 THR A 186
REMARK 465 LYS A 187
REMARK 465 ALA A 188
REMARK 465 ALA A 189
REMARK 465 VAL A 190
REMARK 465 ASP A 191
REMARK 465 PRO A 192
REMARK 465 MET A 193
REMARK 465 VAL A 194
REMARK 465 GLN A 195
REMARK 465 ARG A 196
REMARK 465 GLU A 197
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ARG B 17
REMARK 465 PRO B 18
REMARK 465 LEU B 177
REMARK 465 GLU B 178
REMARK 465 GLY B 179
REMARK 465 ILE B 180
REMARK 465 GLY B 181
REMARK 465 GLU B 182
REMARK 465 SER B 183
REMARK 465 MET B 184
REMARK 465 THR B 185
REMARK 465 THR B 186
REMARK 465 LYS B 187
REMARK 465 ALA B 188
REMARK 465 ALA B 189
REMARK 465 VAL B 190
REMARK 465 ASP B 191
REMARK 465 PRO B 192
REMARK 465 MET B 193
REMARK 465 VAL B 194
REMARK 465 GLN B 195
REMARK 465 ARG B 196
REMARK 465 GLU B 197
REMARK 465 PRO B 198
REMARK 465 LEU B 199
REMARK 465 LEU B 200
REMARK 465 ARG B 201
REMARK 465 MET B 202
REMARK 465 ALA B 203
REMARK 465 SER B 204
REMARK 465 MET B 205
REMARK 465 TYR B 206
REMARK 465 LEU B 207
REMARK 465 ALA B 208
REMARK 465 GLY B 209
REMARK 465 GLN B 210
REMARK 465 ASP B 211
REMARK 465 PRO B 212
REMARK 465 ARG B 213
REMARK 465 THR B 214
REMARK 465 PRO B 215
REMARK 465 LEU B 216
REMARK 465 ALA B 217
REMARK 465 ALA B 218
REMARK 465 PRO B 219
REMARK 465 LEU B 220
REMARK 465 TYR B 221
REMARK 465 ALA B 222
REMARK 465 GLN B 296
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 LEU A 19 -61.92 -95.52
REMARK 500 PRO A 115 30.94 -99.48
REMARK 500 SER A 144 -120.00 50.05
REMARK 500 PRO A 219 2.98 -68.23
REMARK 500 GLN A 257 92.17 -64.33
REMARK 500 GLN A 257 94.20 -68.91
REMARK 500 VAL A 269 52.15 39.77
REMARK 500 GLU B 4 -80.13 -77.27
REMARK 500 PRO B 115 41.09 -101.21
REMARK 500 SER B 144 -121.85 51.76
REMARK 500 ALA B 237 46.41 -100.90
REMARK 500 GLN B 257 96.10 -69.92
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 FMT A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FDS A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FDS A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FDS B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FDS B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7AT0 RELATED DB: PDB
REMARK 900 RELATED ID: 7AT2 RELATED DB: PDB
REMARK 900 RELATED ID: 7AT4 RELATED DB: PDB
REMARK 900 RELATED ID: 7AT3 RELATED DB: PDB
REMARK 900 RELATED ID: 7ATD RELATED DB: PDB
REMARK 900 RELATED ID: 7ATF RELATED DB: PDB
REMARK 900 RELATED ID: 7ATQ RELATED DB: PDB
DBREF 7AUY A 1 296 PDB 7AUY 7AUY 1 296
DBREF 7AUY B 1 296 PDB 7AUY 7AUY 1 296
SEQRES 1 A 296 MET ALA SER GLU ALA LEU THR MET ILE VAL ASN LEU LEU
SEQRES 2 A 296 ARG SER GLN ARG PRO LEU GLN GLU PRO THR VAL GLU GLN
SEQRES 3 A 296 MET ARG ALA GLY LEU GLU ALA MET ALA GLN MET SER PRO
SEQRES 4 A 296 LEU PRO ALA ASP VAL GLU LEU THR THR VAL ASP ALA GLY
SEQRES 5 A 296 GLY VAL PRO GLY ALA TRP VAL ARG VAL PRO GLU SER ASP
SEQRES 6 A 296 PRO ASP ARG VAL VAL LEU TYR LEU HIS GLY GLY GLY TYR
SEQRES 7 A 296 VAL ILE GLY SER ILE ARG THR HIS ARG ASP LEU ALA GLN
SEQRES 8 A 296 ARG ILE ALA ARG ALA ALA ARG CYS ARG VAL LEU LEU ILE
SEQRES 9 A 296 ASP TYR ARG LEU ALA PRO GLU HIS PRO HIS PRO ALA ALA
SEQRES 10 A 296 VAL GLU ASP SER THR ARG ALA TYR ARG TRP LEU LEU GLU
SEQRES 11 A 296 THR GLY SER ASP PRO LYS ARG MET ALA ILE ALA GLY ASP
SEQRES 12 A 296 SER ALA GLY GLY GLY LEU THR VAL ALA THR LEU VAL ALA
SEQRES 13 A 296 LEU ARG ASP ALA GLY VAL PRO LEU PRO ALA ALA ALA VAL
SEQRES 14 A 296 CYS LEU SER PRO TRP VAL ASP LEU GLU GLY ILE GLY GLU
SEQRES 15 A 296 SER MET THR THR LYS ALA ALA VAL ASP PRO MET VAL GLN
SEQRES 16 A 296 ARG GLU PRO LEU LEU ARG MET ALA SER MET TYR LEU ALA
SEQRES 17 A 296 GLY GLN ASP PRO ARG THR PRO LEU ALA ALA PRO LEU TYR
SEQRES 18 A 296 ALA ASP LEU ARG GLY LEU PRO PRO LEU LEU ILE GLN VAL
SEQRES 19 A 296 GLY THR ALA GLU THR LEU LEU ASP ASP SER VAL ARG LEU
SEQRES 20 A 296 ALA GLU ARG ALA ARG ALA ALA GLY VAL GLN VAL THR LEU
SEQRES 21 A 296 GLU PRO TRP GLU ASP MET ILE HIS VAL TRP GLN ALA PHE
SEQRES 22 A 296 ALA ALA MET LEU PRO GLU GLY GLN GLN ALA ILE GLU ARG
SEQRES 23 A 296 ILE GLY GLU PHE LEU ARG GLN HIS TRP GLN
SEQRES 1 B 296 MET ALA SER GLU ALA LEU THR MET ILE VAL ASN LEU LEU
SEQRES 2 B 296 ARG SER GLN ARG PRO LEU GLN GLU PRO THR VAL GLU GLN
SEQRES 3 B 296 MET ARG ALA GLY LEU GLU ALA MET ALA GLN MET SER PRO
SEQRES 4 B 296 LEU PRO ALA ASP VAL GLU LEU THR THR VAL ASP ALA GLY
SEQRES 5 B 296 GLY VAL PRO GLY ALA TRP VAL ARG VAL PRO GLU SER ASP
SEQRES 6 B 296 PRO ASP ARG VAL VAL LEU TYR LEU HIS GLY GLY GLY TYR
SEQRES 7 B 296 VAL ILE GLY SER ILE ARG THR HIS ARG ASP LEU ALA GLN
SEQRES 8 B 296 ARG ILE ALA ARG ALA ALA ARG CYS ARG VAL LEU LEU ILE
SEQRES 9 B 296 ASP TYR ARG LEU ALA PRO GLU HIS PRO HIS PRO ALA ALA
SEQRES 10 B 296 VAL GLU ASP SER THR ARG ALA TYR ARG TRP LEU LEU GLU
SEQRES 11 B 296 THR GLY SER ASP PRO LYS ARG MET ALA ILE ALA GLY ASP
SEQRES 12 B 296 SER ALA GLY GLY GLY LEU THR VAL ALA THR LEU VAL ALA
SEQRES 13 B 296 LEU ARG ASP ALA GLY VAL PRO LEU PRO ALA ALA ALA VAL
SEQRES 14 B 296 CYS LEU SER PRO TRP VAL ASP LEU GLU GLY ILE GLY GLU
SEQRES 15 B 296 SER MET THR THR LYS ALA ALA VAL ASP PRO MET VAL GLN
SEQRES 16 B 296 ARG GLU PRO LEU LEU ARG MET ALA SER MET TYR LEU ALA
SEQRES 17 B 296 GLY GLN ASP PRO ARG THR PRO LEU ALA ALA PRO LEU TYR
SEQRES 18 B 296 ALA ASP LEU ARG GLY LEU PRO PRO LEU LEU ILE GLN VAL
SEQRES 19 B 296 GLY THR ALA GLU THR LEU LEU ASP ASP SER VAL ARG LEU
SEQRES 20 B 296 ALA GLU ARG ALA ARG ALA ALA GLY VAL GLN VAL THR LEU
SEQRES 21 B 296 GLU PRO TRP GLU ASP MET ILE HIS VAL TRP GLN ALA PHE
SEQRES 22 B 296 ALA ALA MET LEU PRO GLU GLY GLN GLN ALA ILE GLU ARG
SEQRES 23 B 296 ILE GLY GLU PHE LEU ARG GLN HIS TRP GLN
HET FMT A 501 3
HET FDS A 502 25
HET FDS A 503 25
HET FDS B 301 25
HET FDS B 302 25
HETNAM FMT FORMIC ACID
HETNAM FDS FLUORESCIN
FORMUL 3 FMT C H2 O2
FORMUL 4 FDS 4(C20 H14 O5)
FORMUL 8 HOH *43(H2 O)
HELIX 1 AA1 SER A 3 GLN A 16 1 14
HELIX 2 AA2 THR A 23 MET A 37 1 15
HELIX 3 AA3 HIS A 86 ARG A 98 1 13
HELIX 4 AA4 PRO A 115 THR A 131 1 17
HELIX 5 AA5 ASP A 134 LYS A 136 5 3
HELIX 6 AA6 ALA A 145 ALA A 160 1 16
HELIX 7 AA7 LEU A 199 ALA A 208 1 10
HELIX 8 AA8 ALA A 218 ALA A 222 5 5
HELIX 9 AA9 LEU A 240 ALA A 254 1 15
HELIX 10 AB1 VAL A 269 ALA A 274 5 6
HELIX 11 AB2 LEU A 277 GLN A 296 1 20
HELIX 12 AB3 ALA B 5 GLN B 16 1 12
HELIX 13 AB4 THR B 23 MET B 37 1 15
HELIX 14 AB5 HIS B 86 ARG B 98 1 13
HELIX 15 AB6 PRO B 115 THR B 131 1 17
HELIX 16 AB7 ASP B 134 LYS B 136 5 3
HELIX 17 AB8 ALA B 145 ALA B 160 1 16
HELIX 18 AB9 LEU B 240 ALA B 254 1 15
HELIX 19 AC1 VAL B 269 ALA B 274 5 6
HELIX 20 AC2 LEU B 277 TRP B 295 1 19
SHEET 1 AA1 8 GLU A 45 ALA A 51 0
SHEET 2 AA1 8 VAL A 54 ARG A 60 -1 O VAL A 54 N ALA A 51
SHEET 3 AA1 8 CYS A 99 ILE A 104 -1 O VAL A 101 N VAL A 59
SHEET 4 AA1 8 ASP A 65 LEU A 73 1 N ARG A 68 O ARG A 100
SHEET 5 AA1 8 MET A 138 ASP A 143 1 O ALA A 141 N LEU A 73
SHEET 6 AA1 8 ALA A 167 LEU A 171 1 O LEU A 171 N GLY A 142
SHEET 7 AA1 8 LEU A 230 GLY A 235 1 O LEU A 231 N CYS A 170
SHEET 8 AA1 8 VAL A 258 TRP A 263 1 O GLU A 261 N ILE A 232
SHEET 1 AA2 8 GLU B 45 ALA B 51 0
SHEET 2 AA2 8 VAL B 54 ARG B 60 -1 O ARG B 60 N GLU B 45
SHEET 3 AA2 8 CYS B 99 ILE B 104 -1 O VAL B 101 N VAL B 59
SHEET 4 AA2 8 ASP B 65 LEU B 73 1 N ARG B 68 O ARG B 100
SHEET 5 AA2 8 MET B 138 ASP B 143 1 O ALA B 141 N LEU B 73
SHEET 6 AA2 8 ALA B 167 LEU B 171 1 O LEU B 171 N GLY B 142
SHEET 7 AA2 8 LEU B 230 GLY B 235 1 O LEU B 231 N CYS B 170
SHEET 8 AA2 8 VAL B 258 TRP B 263 1 O GLU B 261 N ILE B 232
CISPEP 1 ALA A 109 PRO A 110 0 1.59
CISPEP 2 HIS A 114 PRO A 115 0 6.67
CISPEP 3 ALA B 109 PRO B 110 0 4.37
CISPEP 4 HIS B 114 PRO B 115 0 -0.48
SITE 1 AC1 5 GLY A 76 GLY A 77 SER A 144 ALA A 145
SITE 2 AC1 5 HIS A 268
SITE 1 AC2 7 GLY A 75 GLY A 76 HIS A 86 ASP A 143
SITE 2 AC2 7 MET A 202 ILE A 267 HIS A 268
SITE 1 AC3 10 VAL A 162 PRO A 163 LEU A 164 GLY A 226
SITE 2 AC3 10 THR A 236 LEU A 241 LEU A 260 PRO A 262
SITE 3 AC3 10 GLU A 264 HOH A 607
SITE 1 AC4 9 LEU B 31 GLY B 75 GLY B 76 HIS B 86
SITE 2 AC4 9 ASP B 143 ILE B 267 HIS B 268 PHE B 273
SITE 3 AC4 9 FDS B 302
SITE 1 AC5 9 GLN B 16 LEU B 31 MET B 34 ALA B 35
SITE 2 AC5 9 THR B 85 ALA B 272 PHE B 273 MET B 276
SITE 3 AC5 9 FDS B 301
CRYST1 48.176 81.201 147.227 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 0.020757 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012315 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006792 0.00000
TER 2124 GLN A 296
TER 3996 TRP B 295
MASTER 380 0 5 20 16 0 13 6 4131 2 103 46
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