| content |
HEADER HYDROLASE 25-JAN-21 7NB5
TITLE STRUCTURE OF ESTD11 S144A IN COMPLEX WITH NAPROXEN P-NITROPHENOL ESTER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTD11 S144A;
COMPND 3 CHAIN: A;
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
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 7NB5 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. 2.13 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0258
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) : 2.13
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.36
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 14812
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 768
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) : 2.13
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.19
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1081
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.1670
REMARK 3 BIN FREE R VALUE SET COUNT : 65
REMARK 3 BIN FREE R VALUE : 0.2580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2247
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 99
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.33000
REMARK 3 B22 (A**2) : 4.43000
REMARK 3 B33 (A**2) : -2.09000
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): 0.244
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.198
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.153
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.629
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2335 ; 0.008 ; 0.018
REMARK 3 BOND LENGTHS OTHERS (A): 2226 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3190 ; 1.237 ; 1.906
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5125 ; 1.049 ; 2.938
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 296 ; 5.200 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 97 ;30.465 ;22.577
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 369 ;13.875 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;19.041 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 361 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2619 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 469 ; 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): 1184 ; 6.263 ; 1.338
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1183 ; 6.265 ; 1.333
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1480 ; 7.492 ; 1.972
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1481 ; 7.515 ; 1.976
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1150 ;10.773 ; 1.994
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1151 ;10.769 ; 1.996
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1710 ;13.177 ; 2.717
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2661 ;13.991 ;17.977
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2649 ;14.026 ;17.832
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 296
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5760 19.5920 16.2720
REMARK 3 T TENSOR
REMARK 3 T11: 0.1173 T22: 0.2069
REMARK 3 T33: 0.0684 T12: 0.0426
REMARK 3 T13: -0.0042 T23: -0.0800
REMARK 3 L TENSOR
REMARK 3 L11: 3.9291 L22: 0.8602
REMARK 3 L33: 2.1733 L12: -0.3068
REMARK 3 L13: 0.0194 L23: 0.2854
REMARK 3 S TENSOR
REMARK 3 S11: 0.1293 S12: 0.6490 S13: -0.0618
REMARK 3 S21: -0.0644 S22: -0.1084 S23: 0.0678
REMARK 3 S31: 0.0142 S32: -0.1875 S33: -0.0209
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.10
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 7NB5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-JAN-21.
REMARK 100 THE DEPOSITION ID IS D_1292113672.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-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 : 15581
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.130
REMARK 200 RESOLUTION RANGE LOW (A) : 44.840
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.13
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.23100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 8.200
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 (%): 41.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM FORMATE 3.2M AND CITRATE PH 5
REMARK 280 0.1M, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 23.99950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 44.85250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 62.88100
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 23.99950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 44.85250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 62.88100
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 23.99950
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 44.85250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 62.88100
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 23.99950
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 44.85250
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 62.88100
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: 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 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 403 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 420 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 488 LIES ON A SPECIAL POSITION.
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 ALA A 144 -117.39 50.95
REMARK 500 ALA A 189 -40.85 124.27
REMARK 500 VAL A 194 94.39 47.09
REMARK 500 ASP A 265 -0.60 69.05
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 U68 A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7AT0 RELATED DB: PDB
REMARK 900 ESTD11
REMARK 900 RELATED ID: 7AT2 RELATED DB: PDB
REMARK 900 ESTD11 S144A
REMARK 900 RELATED ID: 7AT4 RELATED DB: PDB
REMARK 900 RELATED ID: 7ATD RELATED DB: PDB
REMARK 900 RELATED ID: 7ATF RELATED DB: PDB
REMARK 900 RELATED ID: 7AUY RELATED DB: PDB
REMARK 900 RELATED ID: 7AV5 RELATED DB: PDB
REMARK 900 RELATED ID: 7ATQ RELATED DB: NDB
REMARK 900 RELATED ID: 7AT3 RELATED DB: PDB
DBREF 7NB5 A 2 296 PDB 7NB5 7NB5 2 296
SEQRES 1 A 295 ALA SER GLU ALA LEU THR MET ILE VAL ASN LEU LEU ARG
SEQRES 2 A 295 SER GLN ARG PRO LEU GLN GLU PRO THR VAL GLU GLN MET
SEQRES 3 A 295 ARG ALA GLY LEU GLU ALA MET ALA GLN MET SER PRO LEU
SEQRES 4 A 295 PRO ALA ASP VAL GLU LEU THR THR VAL ASP ALA GLY GLY
SEQRES 5 A 295 VAL PRO GLY ALA TRP VAL ARG VAL PRO GLU SER ASP PRO
SEQRES 6 A 295 ASP ARG VAL VAL LEU TYR LEU HIS GLY GLY GLY TYR VAL
SEQRES 7 A 295 ILE GLY SER ILE ARG THR HIS ARG ASP LEU ALA GLN ARG
SEQRES 8 A 295 ILE ALA ARG ALA ALA ARG CYS ARG VAL LEU LEU ILE ASP
SEQRES 9 A 295 TYR ARG LEU ALA PRO GLU HIS PRO HIS PRO ALA ALA VAL
SEQRES 10 A 295 GLU ASP SER THR ARG ALA TYR ARG TRP LEU LEU GLU THR
SEQRES 11 A 295 GLY SER ASP PRO LYS ARG MET ALA ILE ALA GLY ASP ALA
SEQRES 12 A 295 ALA GLY GLY GLY LEU THR VAL ALA THR LEU VAL ALA LEU
SEQRES 13 A 295 ARG ASP ALA GLY VAL PRO LEU PRO ALA ALA ALA VAL CYS
SEQRES 14 A 295 LEU SER PRO TRP VAL ASP LEU GLU GLY ILE GLY GLU SER
SEQRES 15 A 295 MET THR THR LYS ALA ALA VAL ASP PRO MET VAL GLN ARG
SEQRES 16 A 295 GLU PRO LEU LEU ARG MET ALA SER MET TYR LEU ALA GLY
SEQRES 17 A 295 GLN ASP PRO ARG THR PRO LEU ALA ALA PRO LEU TYR ALA
SEQRES 18 A 295 ASP LEU ARG GLY LEU PRO PRO LEU LEU ILE GLN VAL GLY
SEQRES 19 A 295 THR ALA GLU THR LEU LEU ASP ASP SER VAL ARG LEU ALA
SEQRES 20 A 295 GLU ARG ALA ARG ALA ALA GLY VAL GLN VAL THR LEU GLU
SEQRES 21 A 295 PRO TRP GLU ASP MET ILE HIS VAL TRP GLN ALA PHE ALA
SEQRES 22 A 295 ALA MET LEU PRO GLU GLY GLN GLN ALA ILE GLU ARG ILE
SEQRES 23 A 295 GLY GLU PHE LEU ARG GLN HIS TRP GLN
HET U68 A 301 26
HETNAM U68 (4-NITROPHENYL) (2~{S})-2-(6-METHOXYNAPHTHALEN-2-YL)
HETNAM 2 U68 PROPANOATE
FORMUL 2 U68 C20 H19 N O5
FORMUL 3 HOH *99(H2 O)
HELIX 1 AA1 SER A 3 ARG A 17 1 15
HELIX 2 AA2 THR A 23 GLN A 36 1 14
HELIX 3 AA3 SER A 82 ALA A 97 1 16
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 144 ALA A 160 1 17
HELIX 7 AA7 GLY A 181 THR A 185 5 5
HELIX 8 AA8 GLN A 195 ALA A 208 1 14
HELIX 9 AA9 ALA A 218 ALA A 222 5 5
HELIX 10 AB1 LEU A 240 ALA A 254 1 15
HELIX 11 AB2 VAL A 269 ALA A 274 5 6
HELIX 12 AB3 LEU A 277 GLN A 296 1 20
SHEET 1 AA1 8 GLU A 45 ASP A 50 0
SHEET 2 AA1 8 PRO A 55 ARG A 60 -1 O ARG A 60 N GLU A 45
SHEET 3 AA1 8 CYS A 99 ILE A 104 -1 O LEU A 103 N ALA A 57
SHEET 4 AA1 8 ASP A 65 LEU A 73 1 N VAL A 70 O LEU A 102
SHEET 5 AA1 8 MET A 138 ASP A 143 1 O ALA A 139 N LEU A 71
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
CISPEP 1 ALA A 109 PRO A 110 0 -4.12
CISPEP 2 HIS A 114 PRO A 115 0 10.56
SITE 1 AC1 15 LEU A 31 GLY A 75 GLY A 76 GLY A 77
SITE 2 AC1 15 THR A 85 HIS A 86 ASP A 143 ALA A 144
SITE 3 AC1 15 ALA A 145 TRP A 174 LEU A 199 MET A 202
SITE 4 AC1 15 HIS A 268 VAL A 269 ALA A 272
CRYST1 47.999 89.705 125.762 90.00 90.00 90.00 I 2 2 2 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 0.020834 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011148 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007952 0.00000
TER 2259 GLN A 296
MASTER 318 0 1 12 8 0 4 6 2372 1 26 23
END |