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HEADER HYDROLASE 24-OCT-16 5H3H
TITLE ESTERASE (EAEST) FROM EXIGUOBACTERIUM ANTARCTICUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ABHYDROLASE DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EXIGUOBACTERIUM ANTARCTICUM (STRAIN B7);
SOURCE 3 ORGANISM_TAXID: 1087448;
SOURCE 4 STRAIN: B7;
SOURCE 5 GENE: EAB7_1456;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PERHYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.H.LEE,C.W.LEE
REVDAT 1 11-JAN-17 5H3H 0
JRNL AUTH J.H.LEE,C.W.LEE
JRNL TITL ESTERASE (EAEST) FROM EXIGUOBACTERIUM ANTARCTICUM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0151
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 33467
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1768
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2463
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.1930
REMARK 3 BIN FREE R VALUE SET COUNT : 120
REMARK 3 BIN FREE R VALUE : 0.2620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4214
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.01000
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): 0.186
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.166
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.121
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.073
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4314 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4020 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5822 ; 1.971 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9276 ; 1.159 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 535 ; 6.706 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 208 ;38.479 ;24.904
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 737 ;18.649 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;13.402 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 625 ; 0.143 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4921 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 985 ; 0.002 ; 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): 2148 ; 2.354 ; 2.497
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2145 ; 2.336 ; 2.496
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2679 ; 3.185 ; 3.731
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2680 ; 3.185 ; 3.732
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2166 ; 3.334 ; 2.886
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2166 ; 3.334 ; 2.886
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3144 ; 5.088 ; 4.181
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4916 ; 6.488 ;30.315
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4878 ; 6.448 ;30.151
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5H3H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1300001946.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-APR-16
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 : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35239
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 43.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 0.1M HEPES:NAOH
REMARK 280 PH 7.5, 27%(W/V) PEG3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,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 -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 0.00000
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 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 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 SER A 269
REMARK 465 GLN A 270
REMARK 465 THR A 271
REMARK 465 VAL A 272
REMARK 465 GLN B 270
REMARK 465 THR B 271
REMARK 465 VAL B 272
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 O MET A 1 OH TYR A 14 1.99
REMARK 500
REMARK 500 REMARK: NULL
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 153 NE - CZ - NH1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 153 NE - CZ - NH2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG A 197 NE - CZ - NH1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG A 197 NE - CZ - NH2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 LEU B 45 CB - CG - CD1 ANGL. DEV. = 10.9 DEGREES
REMARK 500 MET B 250 CG - SD - CE ANGL. DEV. = -9.7 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 ALA A 32 -141.48 -93.11
REMARK 500 SER A 96 -119.45 54.00
REMARK 500 TYR A 133 69.44 -154.94
REMARK 500 PRO A 134 41.08 -86.50
REMARK 500 LYS A 267 -88.09 -66.98
REMARK 500 THR B 3 -113.36 -152.88
REMARK 500 PRO B 31 56.99 -116.73
REMARK 500 ALA B 32 -141.15 -99.03
REMARK 500 SER B 96 -119.02 57.78
REMARK 500 ASP B 131 -77.95 -6.91
REMARK 500 ASP B 152 82.84 -166.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR B 3 PHE B 4 -147.63
REMARK 500 GLY B 21 GLN B 22 -148.28
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 F50 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue F50 B 301
DBREF 5H3H A 1 272 UNP K0ACL0 K0ACL0_EXIAB 1 272
DBREF 5H3H B 1 272 UNP K0ACL0 K0ACL0_EXIAB 1 272
SEQRES 1 A 272 MET GLY THR PHE ILE GLN ALA VAL ASP GLY THR LYS ILE
SEQRES 2 A 272 TYR VAL GLU ASP ILE GLY SER GLY GLN PRO VAL VAL MET
SEQRES 3 A 272 LEU HIS GLY TRP PRO ALA ASN ASN ASN MET PHE GLU TYR
SEQRES 4 A 272 GLN LYS ASN ARG LEU LEU GLU GLU GLY TYR ARG TYR ILE
SEQRES 5 A 272 GLY VAL ASP TYR ARG GLY TYR GLY LYS SER ASP ALA PRO
SEQRES 6 A 272 ALA THR GLY TYR ASP TYR THR THR MET ALA SER ASP ILE
SEQRES 7 A 272 ASN GLU VAL ILE GLN GLN LEU LYS LEU THR ASN VAL THR
SEQRES 8 A 272 LEU LEU GLY PHE SER MET GLY GLY GLY ILE ALA LEU LYS
SEQRES 9 A 272 TYR LEU LEU ASN HIS GLY GLU SER ASN VAL SER LYS LEU
SEQRES 10 A 272 ILE LEU ALA GLY ALA ALA ALA PRO VAL PHE THR GLN ARG
SEQRES 11 A 272 ASP GLY TYR PRO TYR GLY MET THR LYS ASP GLU VAL ASP
SEQRES 12 A 272 ALA LEU ILE GLU ASP THR LYS GLN ASP ARG PRO SER MET
SEQRES 13 A 272 LEU LYS GLY PHE GLY GLU ILE PHE PHE ALA LYS GLU HIS
SEQRES 14 A 272 PRO GLU PRO LEU GLN GLN TRP PHE HIS ASN LEU SER VAL
SEQRES 15 A 272 ASP ALA SER SER HIS GLY THR ILE GLN SER ALA ILE ALA
SEQRES 16 A 272 LEU ARG ASP GLU ASP LEU ARG ASP GLY LEU PRO LYS ILE
SEQRES 17 A 272 THR VAL ASP THR LEU ILE MET HIS GLY LYS LYS ASP GLN
SEQRES 18 A 272 VAL CYS PRO PHE GLU PHE ALA GLU VAL MET HIS GLU ASN
SEQRES 19 A 272 ILE ALA GLY SER ARG LEU GLU VAL PHE GLU GLU SER GLY
SEQRES 20 A 272 HIS GLY MET PHE LEU ASP GLU ARG GLU LYS PHE THR GLU
SEQRES 21 A 272 THR LEU VAL SER TYR VAL LYS SER SER GLN THR VAL
SEQRES 1 B 272 MET GLY THR PHE ILE GLN ALA VAL ASP GLY THR LYS ILE
SEQRES 2 B 272 TYR VAL GLU ASP ILE GLY SER GLY GLN PRO VAL VAL MET
SEQRES 3 B 272 LEU HIS GLY TRP PRO ALA ASN ASN ASN MET PHE GLU TYR
SEQRES 4 B 272 GLN LYS ASN ARG LEU LEU GLU GLU GLY TYR ARG TYR ILE
SEQRES 5 B 272 GLY VAL ASP TYR ARG GLY TYR GLY LYS SER ASP ALA PRO
SEQRES 6 B 272 ALA THR GLY TYR ASP TYR THR THR MET ALA SER ASP ILE
SEQRES 7 B 272 ASN GLU VAL ILE GLN GLN LEU LYS LEU THR ASN VAL THR
SEQRES 8 B 272 LEU LEU GLY PHE SER MET GLY GLY GLY ILE ALA LEU LYS
SEQRES 9 B 272 TYR LEU LEU ASN HIS GLY GLU SER ASN VAL SER LYS LEU
SEQRES 10 B 272 ILE LEU ALA GLY ALA ALA ALA PRO VAL PHE THR GLN ARG
SEQRES 11 B 272 ASP GLY TYR PRO TYR GLY MET THR LYS ASP GLU VAL ASP
SEQRES 12 B 272 ALA LEU ILE GLU ASP THR LYS GLN ASP ARG PRO SER MET
SEQRES 13 B 272 LEU LYS GLY PHE GLY GLU ILE PHE PHE ALA LYS GLU HIS
SEQRES 14 B 272 PRO GLU PRO LEU GLN GLN TRP PHE HIS ASN LEU SER VAL
SEQRES 15 B 272 ASP ALA SER SER HIS GLY THR ILE GLN SER ALA ILE ALA
SEQRES 16 B 272 LEU ARG ASP GLU ASP LEU ARG ASP GLY LEU PRO LYS ILE
SEQRES 17 B 272 THR VAL ASP THR LEU ILE MET HIS GLY LYS LYS ASP GLN
SEQRES 18 B 272 VAL CYS PRO PHE GLU PHE ALA GLU VAL MET HIS GLU ASN
SEQRES 19 B 272 ILE ALA GLY SER ARG LEU GLU VAL PHE GLU GLU SER GLY
SEQRES 20 B 272 HIS GLY MET PHE LEU ASP GLU ARG GLU LYS PHE THR GLU
SEQRES 21 B 272 THR LEU VAL SER TYR VAL LYS SER SER GLN THR VAL
HET F50 A 301 5
HET F50 B 301 5
HETNAM F50 ETHANEPEROXOIC ACID
FORMUL 3 F50 2(C2 H4 O3)
FORMUL 5 HOH *190(H2 O)
HELIX 1 AA1 ASN A 33 MET A 36 5 4
HELIX 2 AA2 PHE A 37 GLY A 48 1 12
HELIX 3 AA3 ASP A 70 LYS A 86 1 17
HELIX 4 AA4 MET A 97 GLY A 110 1 14
HELIX 5 AA5 THR A 138 LYS A 150 1 13
HELIX 6 AA6 ASP A 152 PHE A 165 1 14
HELIX 7 AA7 PRO A 170 ASP A 183 1 14
HELIX 8 AA8 SER A 185 GLU A 199 1 15
HELIX 9 AA9 GLY A 204 ILE A 208 5 5
HELIX 10 AB1 PRO A 224 ILE A 235 1 12
HELIX 11 AB2 GLY A 249 GLU A 254 1 6
HELIX 12 AB3 GLU A 254 SER A 268 1 15
HELIX 13 AB4 ASN B 33 MET B 36 5 4
HELIX 14 AB5 PHE B 37 GLU B 47 1 11
HELIX 15 AB6 ASP B 70 LYS B 86 1 17
HELIX 16 AB7 SER B 96 GLY B 110 1 15
HELIX 17 AB8 THR B 138 LYS B 150 1 13
HELIX 18 AB9 ASP B 152 PHE B 165 1 14
HELIX 19 AC1 PRO B 170 ASP B 183 1 14
HELIX 20 AC2 SER B 185 GLU B 199 1 15
HELIX 21 AC3 LEU B 201 ILE B 208 5 8
HELIX 22 AC4 PRO B 224 ILE B 235 1 12
HELIX 23 AC5 GLY B 249 GLU B 254 1 6
HELIX 24 AC6 GLU B 254 SER B 268 1 15
SHEET 1 AA1 8 PHE A 4 GLN A 6 0
SHEET 2 AA1 8 LYS A 12 ILE A 18 -1 O ILE A 13 N ILE A 5
SHEET 3 AA1 8 ARG A 50 VAL A 54 -1 O GLY A 53 N GLU A 16
SHEET 4 AA1 8 PRO A 23 LEU A 27 1 N VAL A 24 O ILE A 52
SHEET 5 AA1 8 VAL A 90 PHE A 95 1 O LEU A 93 N VAL A 25
SHEET 6 AA1 8 VAL A 114 ALA A 120 1 O ILE A 118 N LEU A 92
SHEET 7 AA1 8 ASP A 211 GLY A 217 1 O MET A 215 N LEU A 119
SHEET 8 AA1 8 ARG A 239 PHE A 243 1 O ARG A 239 N ILE A 214
SHEET 1 AA2 8 PHE B 4 GLN B 6 0
SHEET 2 AA2 8 LYS B 12 ILE B 18 -1 O ILE B 13 N ILE B 5
SHEET 3 AA2 8 ARG B 50 VAL B 54 -1 O GLY B 53 N GLU B 16
SHEET 4 AA2 8 PRO B 23 LEU B 27 1 N VAL B 24 O ILE B 52
SHEET 5 AA2 8 VAL B 90 PHE B 95 1 O LEU B 93 N LEU B 27
SHEET 6 AA2 8 VAL B 114 ALA B 120 1 O LYS B 116 N LEU B 92
SHEET 7 AA2 8 ASP B 211 GLY B 217 1 O LEU B 213 N LEU B 119
SHEET 8 AA2 8 ARG B 239 PHE B 243 1 O GLU B 241 N ILE B 214
CISPEP 1 TRP A 30 PRO A 31 0 -4.35
CISPEP 2 ALA A 124 PRO A 125 0 0.04
CISPEP 3 MET B 1 GLY B 2 0 -7.05
CISPEP 4 TRP B 30 PRO B 31 0 -6.46
CISPEP 5 ALA B 124 PRO B 125 0 0.49
SITE 1 AC1 7 GLY A 29 TRP A 30 PHE A 95 SER A 96
SITE 2 AC1 7 MET A 97 PHE A 164 HIS A 248
SITE 1 AC2 5 GLY B 29 TRP B 30 SER B 96 MET B 97
SITE 2 AC2 5 HIS B 248
CRYST1 76.765 76.765 68.161 90.00 90.00 120.00 P 3 6
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 0.013027 0.007521 0.000000 0.00000
SCALE2 0.000000 0.015042 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014671 0.00000
TER 2105 SER A 268
TER 4216 SER B 269
MASTER 328 0 2 24 16 0 4 6 4414 2 10 42
END |