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HEADER HYDROLASE 20-JUN-12 4FOL
TITLE S-FORMYLGLUTATHIONE HYDROLASE VARIANT H160I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S-FORMYLGLUTATHIONE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: FGH;
COMPND 5 EC: 3.1.2.12;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: YJL068C, HRE299, J1102;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS D-TYPE ESTERASE, OXIDATION SENSOR MOTIF, ESTERASE ACTIVITY
KEYWDS 2 ACTIVATION, ESTERASE ACTIVITY INHIBITION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.M.LEGLER,C.B.MILLARD
REVDAT 1 05-SEP-12 4FOL 0
JRNL AUTH P.M.LEGLER,D.H.LEARY,W.J.HERVEY,C.B.MILLARD
JRNL TITL A ROLE FOR HIS-160 IN PEROXIDE INHIBITION OF S. CEREVISIAE
JRNL TITL 2 S-FORMYLGLUTATHIONE HYDROLASE: EVIDENCE FOR AN OXIDATION
JRNL TITL 3 SENSITIVE MOTIF.
JRNL REF ARCH.BIOCHEM.BIOPHYS. 2012
JRNL REFN ESSN 1096-0384
JRNL PMID 22906720
JRNL DOI 10.1016/J.ABB.2012.08.001
REMARK 2
REMARK 2 RESOLUTION. 2.07 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.07
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.9
REMARK 3 NUMBER OF REFLECTIONS : 71543
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) : 0.283
REMARK 3 R VALUE (WORKING SET) : 0.281
REMARK 3 FREE R VALUE : 0.327
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3777
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) : 2.07
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.12
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2907
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 51.12
REMARK 3 BIN R VALUE (WORKING SET) : 0.4150
REMARK 3 BIN FREE R VALUE SET COUNT : 164
REMARK 3 BIN FREE R VALUE : 0.4400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9060
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 183
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.11000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.12000
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): 0.316
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.255
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.825
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.770
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9340 ; 0.011 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12666 ; 1.319 ; 1.937
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1116 ; 6.499 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 455 ;33.313 ;24.154
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1458 ;16.882 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;16.089 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1299 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7287 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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:
REMARK 3 HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
REMARK 3 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4FOL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-12.
REMARK 100 THE RCSB ID CODE IS RCSB073159.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER PLATINUM 135
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75437
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.070
REMARK 200 RESOLUTION RANGE LOW (A) : 69.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.9
REMARK 200 DATA REDUNDANCY : 4.110
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.21080
REMARK 200 FOR THE DATA SET : 5.4900
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1PV1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17 M AMMONIUM ACETATE, 0.085 M
REMARK 280 SODIUM ACETATE TRIHYDRATE, PH 4.6, 25.5% PEG4000, 15% GLYCEROL,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
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 33.15000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.60000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.87000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.60000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.15000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.87000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 1760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 ASP A 42
REMARK 465 PHE A 43
REMARK 465 PRO A 44
REMARK 465 ARG A 45
REMARK 465 ASN A 46
REMARK 465 LYS A 47
REMARK 465 LYS A 143
REMARK 465 ASN A 144
REMARK 465 GLY A 145
REMARK 465 ASP A 146
REMARK 465 VAL A 147
REMARK 465 GLU A 208
REMARK 465 GLU A 209
REMARK 465 LYS A 210
REMARK 465 ALA A 211
REMARK 465 GLN A 212
REMARK 465 GLN B 41
REMARK 465 ASP B 42
REMARK 465 PHE B 43
REMARK 465 PRO B 44
REMARK 465 ARG B 45
REMARK 465 ASN B 46
REMARK 465 LYS B 47
REMARK 465 LYS B 143
REMARK 465 ASN B 144
REMARK 465 GLY B 145
REMARK 465 ASP B 146
REMARK 465 VAL B 147
REMARK 465 GLU B 209
REMARK 465 LYS B 210
REMARK 465 ALA B 211
REMARK 465 GLN B 212
REMARK 465 ASP C 42
REMARK 465 PHE C 43
REMARK 465 PRO C 44
REMARK 465 ARG C 45
REMARK 465 ASN C 46
REMARK 465 LYS C 47
REMARK 465 LYS C 143
REMARK 465 ASN C 144
REMARK 465 GLY C 145
REMARK 465 ASP C 146
REMARK 465 VAL C 147
REMARK 465 LYS C 148
REMARK 465 GLU C 208
REMARK 465 GLU C 209
REMARK 465 LYS C 210
REMARK 465 ALA C 211
REMARK 465 GLN C 212
REMARK 465 GLN D 41
REMARK 465 ASP D 42
REMARK 465 PHE D 43
REMARK 465 PRO D 44
REMARK 465 ARG D 45
REMARK 465 ASN D 46
REMARK 465 LYS D 47
REMARK 465 ARG D 48
REMARK 465 LYS D 143
REMARK 465 ASN D 144
REMARK 465 GLY D 145
REMARK 465 ASP D 146
REMARK 465 VAL D 147
REMARK 465 GLU D 209
REMARK 465 LYS D 210
REMARK 465 ALA D 211
REMARK 465 GLN D 212
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS B 227 NE2 HIS B 227 CD2 -0.089
REMARK 500 TRP D 262 NE1 TRP D 262 CE2 -0.086
REMARK 500 ASP D 275 CB ASP D 275 CG -0.127
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 CYS A 10 -131.90 47.39
REMARK 500 THR A 59 -10.56 67.60
REMARK 500 ALA A 108 46.32 -159.16
REMARK 500 GLN A 124 50.79 -103.96
REMARK 500 LYS A 131 -64.72 -108.51
REMARK 500 ASP A 153 -78.19 -99.93
REMARK 500 SER A 161 -111.26 57.52
REMARK 500 ASP A 231 132.99 -39.67
REMARK 500 LEU A 248 -67.44 -104.69
REMARK 500 LYS B 5 139.00 -177.06
REMARK 500 CYS B 10 -129.45 44.62
REMARK 500 THR B 59 -19.88 70.83
REMARK 500 SER B 88 166.14 179.48
REMARK 500 ALA B 108 50.12 -152.44
REMARK 500 PHE B 110 17.58 46.53
REMARK 500 GLN B 124 57.43 -101.44
REMARK 500 LEU B 152 -40.97 -132.71
REMARK 500 ASP B 153 -63.35 -94.53
REMARK 500 SER B 161 -112.64 54.23
REMARK 500 ALA B 187 56.85 34.75
REMARK 500 LEU B 248 -68.50 -108.81
REMARK 500 ASP B 264 6.33 83.43
REMARK 500 CYS C 10 -133.67 51.01
REMARK 500 THR C 59 -16.68 78.09
REMARK 500 ALA C 108 53.01 -157.84
REMARK 500 HIS C 122 -31.25 -142.44
REMARK 500 GLN C 124 55.38 -101.26
REMARK 500 LYS C 131 -48.44 -134.28
REMARK 500 ASP C 153 -80.60 -101.52
REMARK 500 SER C 161 -105.43 56.61
REMARK 500 ALA C 187 55.74 36.16
REMARK 500 ASN C 191 79.66 -119.48
REMARK 500 GLU C 245 -39.74 91.47
REMARK 500 LYS D 5 148.11 -174.36
REMARK 500 CYS D 10 -125.34 44.15
REMARK 500 THR D 59 -12.91 72.76
REMARK 500 ALA D 108 55.68 -153.28
REMARK 500 GLN D 124 58.27 -104.54
REMARK 500 LYS D 131 -64.93 -106.99
REMARK 500 ASP D 153 -87.03 -104.00
REMARK 500 SER D 161 -103.79 55.86
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 GLN D 116 GLU D 117 -143.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU A 117 22.7 L L OUTSIDE RANGE
REMARK 500 SER A 182 24.9 L L OUTSIDE RANGE
REMARK 500 GLU B 117 20.2 L L OUTSIDE RANGE
REMARK 500 ASN D 154 23.9 L L OUTSIDE RANGE
REMARK 500 LYS D 173 24.3 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 340 DISTANCE = 5.96 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PV1 RELATED DB: PDB
REMARK 900 S-FORMYLGLUTATHIONE HYDROLASE
REMARK 900 RELATED ID: 3C6B RELATED DB: PDB
REMARK 900 S-FORMYLGLUTATHIONE HYDROLASE W197I VARIANT INHIBITED WITH
REMARK 900 PARAOXON
REMARK 900 RELATED ID: 4FLM RELATED DB: PDB
REMARK 900 S-FORMYLGLUTATHIONE HYDROLASE W197I VARIANT INHIBITED WITH
REMARK 900 PARAOXON AND COPPER
DBREF 4FOL A 1 299 UNP P40363 SFGH_YEAST 1 299
DBREF 4FOL B 1 299 UNP P40363 SFGH_YEAST 1 299
DBREF 4FOL C 1 299 UNP P40363 SFGH_YEAST 1 299
DBREF 4FOL D 1 299 UNP P40363 SFGH_YEAST 1 299
SEQADV 4FOL ILE A 160 UNP P40363 HIS 160 ENGINEERED MUTATION
SEQADV 4FOL ILE B 160 UNP P40363 HIS 160 ENGINEERED MUTATION
SEQADV 4FOL ILE C 160 UNP P40363 HIS 160 ENGINEERED MUTATION
SEQADV 4FOL ILE D 160 UNP P40363 HIS 160 ENGINEERED MUTATION
SEQRES 1 A 299 MET LYS VAL VAL LYS GLU PHE SER VAL CYS GLY GLY ARG
SEQRES 2 A 299 LEU ILE LYS LEU SER HIS ASN SER ASN SER THR LYS THR
SEQRES 3 A 299 SER MET ASN VAL ASN ILE TYR LEU PRO LYS HIS TYR TYR
SEQRES 4 A 299 ALA GLN ASP PHE PRO ARG ASN LYS ARG ILE PRO THR VAL
SEQRES 5 A 299 PHE TYR LEU SER GLY LEU THR CYS THR PRO ASP ASN ALA
SEQRES 6 A 299 SER GLU LYS ALA PHE TRP GLN PHE GLN ALA ASP LYS TYR
SEQRES 7 A 299 GLY PHE ALA ILE VAL PHE PRO ASP THR SER PRO ARG GLY
SEQRES 8 A 299 ASP GLU VAL ALA ASN ASP PRO GLU GLY SER TRP ASP PHE
SEQRES 9 A 299 GLY GLN GLY ALA GLY PHE TYR LEU ASN ALA THR GLN GLU
SEQRES 10 A 299 PRO TYR ALA GLN HIS TYR GLN MET TYR ASP TYR ILE HIS
SEQRES 11 A 299 LYS GLU LEU PRO GLN THR LEU ASP SER HIS PHE ASN LYS
SEQRES 12 A 299 ASN GLY ASP VAL LYS LEU ASP PHE LEU ASP ASN VAL ALA
SEQRES 13 A 299 ILE THR GLY ILE SER MET GLY GLY TYR GLY ALA ILE CYS
SEQRES 14 A 299 GLY TYR LEU LYS GLY TYR SER GLY LYS ARG TYR LYS SER
SEQRES 15 A 299 CYS SER ALA PHE ALA PRO ILE VAL ASN PRO SER ASN VAL
SEQRES 16 A 299 PRO TRP GLY GLN LYS ALA PHE LYS GLY TYR LEU GLY GLU
SEQRES 17 A 299 GLU LYS ALA GLN TRP GLU ALA TYR ASP PRO CYS LEU LEU
SEQRES 18 A 299 ILE LYS ASN ILE ARG HIS VAL GLY ASP ASP ARG ILE LEU
SEQRES 19 A 299 ILE HIS VAL GLY ASP SER ASP PRO PHE LEU GLU GLU HIS
SEQRES 20 A 299 LEU LYS PRO GLU LEU LEU LEU GLU ALA VAL LYS ALA THR
SEQRES 21 A 299 SER TRP GLN ASP TYR VAL GLU ILE LYS LYS VAL HIS GLY
SEQRES 22 A 299 PHE ASP HIS SER TYR TYR PHE VAL SER THR PHE VAL PRO
SEQRES 23 A 299 GLU HIS ALA GLU PHE HIS ALA ARG ASN LEU GLY LEU ILE
SEQRES 1 B 299 MET LYS VAL VAL LYS GLU PHE SER VAL CYS GLY GLY ARG
SEQRES 2 B 299 LEU ILE LYS LEU SER HIS ASN SER ASN SER THR LYS THR
SEQRES 3 B 299 SER MET ASN VAL ASN ILE TYR LEU PRO LYS HIS TYR TYR
SEQRES 4 B 299 ALA GLN ASP PHE PRO ARG ASN LYS ARG ILE PRO THR VAL
SEQRES 5 B 299 PHE TYR LEU SER GLY LEU THR CYS THR PRO ASP ASN ALA
SEQRES 6 B 299 SER GLU LYS ALA PHE TRP GLN PHE GLN ALA ASP LYS TYR
SEQRES 7 B 299 GLY PHE ALA ILE VAL PHE PRO ASP THR SER PRO ARG GLY
SEQRES 8 B 299 ASP GLU VAL ALA ASN ASP PRO GLU GLY SER TRP ASP PHE
SEQRES 9 B 299 GLY GLN GLY ALA GLY PHE TYR LEU ASN ALA THR GLN GLU
SEQRES 10 B 299 PRO TYR ALA GLN HIS TYR GLN MET TYR ASP TYR ILE HIS
SEQRES 11 B 299 LYS GLU LEU PRO GLN THR LEU ASP SER HIS PHE ASN LYS
SEQRES 12 B 299 ASN GLY ASP VAL LYS LEU ASP PHE LEU ASP ASN VAL ALA
SEQRES 13 B 299 ILE THR GLY ILE SER MET GLY GLY TYR GLY ALA ILE CYS
SEQRES 14 B 299 GLY TYR LEU LYS GLY TYR SER GLY LYS ARG TYR LYS SER
SEQRES 15 B 299 CYS SER ALA PHE ALA PRO ILE VAL ASN PRO SER ASN VAL
SEQRES 16 B 299 PRO TRP GLY GLN LYS ALA PHE LYS GLY TYR LEU GLY GLU
SEQRES 17 B 299 GLU LYS ALA GLN TRP GLU ALA TYR ASP PRO CYS LEU LEU
SEQRES 18 B 299 ILE LYS ASN ILE ARG HIS VAL GLY ASP ASP ARG ILE LEU
SEQRES 19 B 299 ILE HIS VAL GLY ASP SER ASP PRO PHE LEU GLU GLU HIS
SEQRES 20 B 299 LEU LYS PRO GLU LEU LEU LEU GLU ALA VAL LYS ALA THR
SEQRES 21 B 299 SER TRP GLN ASP TYR VAL GLU ILE LYS LYS VAL HIS GLY
SEQRES 22 B 299 PHE ASP HIS SER TYR TYR PHE VAL SER THR PHE VAL PRO
SEQRES 23 B 299 GLU HIS ALA GLU PHE HIS ALA ARG ASN LEU GLY LEU ILE
SEQRES 1 C 299 MET LYS VAL VAL LYS GLU PHE SER VAL CYS GLY GLY ARG
SEQRES 2 C 299 LEU ILE LYS LEU SER HIS ASN SER ASN SER THR LYS THR
SEQRES 3 C 299 SER MET ASN VAL ASN ILE TYR LEU PRO LYS HIS TYR TYR
SEQRES 4 C 299 ALA GLN ASP PHE PRO ARG ASN LYS ARG ILE PRO THR VAL
SEQRES 5 C 299 PHE TYR LEU SER GLY LEU THR CYS THR PRO ASP ASN ALA
SEQRES 6 C 299 SER GLU LYS ALA PHE TRP GLN PHE GLN ALA ASP LYS TYR
SEQRES 7 C 299 GLY PHE ALA ILE VAL PHE PRO ASP THR SER PRO ARG GLY
SEQRES 8 C 299 ASP GLU VAL ALA ASN ASP PRO GLU GLY SER TRP ASP PHE
SEQRES 9 C 299 GLY GLN GLY ALA GLY PHE TYR LEU ASN ALA THR GLN GLU
SEQRES 10 C 299 PRO TYR ALA GLN HIS TYR GLN MET TYR ASP TYR ILE HIS
SEQRES 11 C 299 LYS GLU LEU PRO GLN THR LEU ASP SER HIS PHE ASN LYS
SEQRES 12 C 299 ASN GLY ASP VAL LYS LEU ASP PHE LEU ASP ASN VAL ALA
SEQRES 13 C 299 ILE THR GLY ILE SER MET GLY GLY TYR GLY ALA ILE CYS
SEQRES 14 C 299 GLY TYR LEU LYS GLY TYR SER GLY LYS ARG TYR LYS SER
SEQRES 15 C 299 CYS SER ALA PHE ALA PRO ILE VAL ASN PRO SER ASN VAL
SEQRES 16 C 299 PRO TRP GLY GLN LYS ALA PHE LYS GLY TYR LEU GLY GLU
SEQRES 17 C 299 GLU LYS ALA GLN TRP GLU ALA TYR ASP PRO CYS LEU LEU
SEQRES 18 C 299 ILE LYS ASN ILE ARG HIS VAL GLY ASP ASP ARG ILE LEU
SEQRES 19 C 299 ILE HIS VAL GLY ASP SER ASP PRO PHE LEU GLU GLU HIS
SEQRES 20 C 299 LEU LYS PRO GLU LEU LEU LEU GLU ALA VAL LYS ALA THR
SEQRES 21 C 299 SER TRP GLN ASP TYR VAL GLU ILE LYS LYS VAL HIS GLY
SEQRES 22 C 299 PHE ASP HIS SER TYR TYR PHE VAL SER THR PHE VAL PRO
SEQRES 23 C 299 GLU HIS ALA GLU PHE HIS ALA ARG ASN LEU GLY LEU ILE
SEQRES 1 D 299 MET LYS VAL VAL LYS GLU PHE SER VAL CYS GLY GLY ARG
SEQRES 2 D 299 LEU ILE LYS LEU SER HIS ASN SER ASN SER THR LYS THR
SEQRES 3 D 299 SER MET ASN VAL ASN ILE TYR LEU PRO LYS HIS TYR TYR
SEQRES 4 D 299 ALA GLN ASP PHE PRO ARG ASN LYS ARG ILE PRO THR VAL
SEQRES 5 D 299 PHE TYR LEU SER GLY LEU THR CYS THR PRO ASP ASN ALA
SEQRES 6 D 299 SER GLU LYS ALA PHE TRP GLN PHE GLN ALA ASP LYS TYR
SEQRES 7 D 299 GLY PHE ALA ILE VAL PHE PRO ASP THR SER PRO ARG GLY
SEQRES 8 D 299 ASP GLU VAL ALA ASN ASP PRO GLU GLY SER TRP ASP PHE
SEQRES 9 D 299 GLY GLN GLY ALA GLY PHE TYR LEU ASN ALA THR GLN GLU
SEQRES 10 D 299 PRO TYR ALA GLN HIS TYR GLN MET TYR ASP TYR ILE HIS
SEQRES 11 D 299 LYS GLU LEU PRO GLN THR LEU ASP SER HIS PHE ASN LYS
SEQRES 12 D 299 ASN GLY ASP VAL LYS LEU ASP PHE LEU ASP ASN VAL ALA
SEQRES 13 D 299 ILE THR GLY ILE SER MET GLY GLY TYR GLY ALA ILE CYS
SEQRES 14 D 299 GLY TYR LEU LYS GLY TYR SER GLY LYS ARG TYR LYS SER
SEQRES 15 D 299 CYS SER ALA PHE ALA PRO ILE VAL ASN PRO SER ASN VAL
SEQRES 16 D 299 PRO TRP GLY GLN LYS ALA PHE LYS GLY TYR LEU GLY GLU
SEQRES 17 D 299 GLU LYS ALA GLN TRP GLU ALA TYR ASP PRO CYS LEU LEU
SEQRES 18 D 299 ILE LYS ASN ILE ARG HIS VAL GLY ASP ASP ARG ILE LEU
SEQRES 19 D 299 ILE HIS VAL GLY ASP SER ASP PRO PHE LEU GLU GLU HIS
SEQRES 20 D 299 LEU LYS PRO GLU LEU LEU LEU GLU ALA VAL LYS ALA THR
SEQRES 21 D 299 SER TRP GLN ASP TYR VAL GLU ILE LYS LYS VAL HIS GLY
SEQRES 22 D 299 PHE ASP HIS SER TYR TYR PHE VAL SER THR PHE VAL PRO
SEQRES 23 D 299 GLU HIS ALA GLU PHE HIS ALA ARG ASN LEU GLY LEU ILE
FORMUL 5 HOH *183(H2 O)
HELIX 1 1 PRO A 35 ALA A 40 5 6
HELIX 2 2 THR A 61 ALA A 69 1 9
HELIX 3 3 PHE A 70 GLY A 79 1 10
HELIX 4 4 GLN A 116 GLN A 121 1 6
HELIX 5 5 GLN A 124 LYS A 131 1 8
HELIX 6 6 LYS A 131 ASN A 142 1 12
HELIX 7 7 SER A 161 GLY A 174 1 14
HELIX 8 8 TYR A 175 LYS A 178 5 4
HELIX 9 9 ASN A 191 ASN A 194 5 4
HELIX 10 10 VAL A 195 LEU A 206 1 12
HELIX 11 11 TRP A 213 TYR A 216 5 4
HELIX 12 12 ASP A 217 ILE A 222 1 6
HELIX 13 13 LYS A 223 ILE A 225 5 3
HELIX 14 14 PHE A 243 LEU A 248 1 6
HELIX 15 15 PRO A 250 LYS A 258 1 9
HELIX 16 16 SER A 277 LEU A 296 1 20
HELIX 17 17 PRO B 35 ALA B 40 5 6
HELIX 18 18 PRO B 62 ALA B 69 1 8
HELIX 19 19 PHE B 70 GLY B 79 1 10
HELIX 20 20 GLN B 116 GLN B 121 1 6
HELIX 21 21 GLN B 124 LYS B 131 1 8
HELIX 22 22 GLU B 132 ASN B 142 1 11
HELIX 23 23 SER B 161 GLY B 174 1 14
HELIX 24 24 ASN B 191 ASN B 194 5 4
HELIX 25 25 VAL B 195 GLY B 207 1 13
HELIX 26 26 TRP B 213 TYR B 216 5 4
HELIX 27 27 ASP B 217 ILE B 222 1 6
HELIX 28 28 LYS B 223 ILE B 225 5 3
HELIX 29 29 PHE B 243 LEU B 248 1 6
HELIX 30 30 PRO B 250 VAL B 257 1 8
HELIX 31 31 LYS B 258 THR B 260 5 3
HELIX 32 32 SER B 277 LEU B 296 1 20
HELIX 33 33 PRO C 35 ALA C 40 5 6
HELIX 34 34 PRO C 62 ALA C 69 1 8
HELIX 35 35 PHE C 70 GLY C 79 1 10
HELIX 36 36 PRO C 118 HIS C 122 5 5
HELIX 37 37 GLN C 124 LYS C 131 1 8
HELIX 38 38 GLU C 132 ASN C 142 1 11
HELIX 39 39 SER C 161 GLY C 174 1 14
HELIX 40 40 TYR C 175 LYS C 178 5 4
HELIX 41 41 ASN C 191 ASN C 194 5 4
HELIX 42 42 VAL C 195 LEU C 206 1 12
HELIX 43 43 TRP C 213 TYR C 216 5 4
HELIX 44 44 ASP C 217 ILE C 222 1 6
HELIX 45 45 LYS C 223 ILE C 225 5 3
HELIX 46 46 PRO C 250 LYS C 258 1 9
HELIX 47 47 SER C 277 LEU C 296 1 20
HELIX 48 48 PRO D 35 ALA D 40 5 6
HELIX 49 49 PRO D 62 ALA D 69 1 8
HELIX 50 50 PHE D 70 GLY D 79 1 10
HELIX 51 51 GLN D 116 GLN D 121 1 6
HELIX 52 52 GLN D 124 LYS D 131 1 8
HELIX 53 53 LYS D 131 ASN D 142 1 12
HELIX 54 54 SER D 161 GLY D 174 1 14
HELIX 55 55 TYR D 175 LYS D 178 5 4
HELIX 56 56 ASN D 191 ASN D 194 5 4
HELIX 57 57 VAL D 195 LEU D 206 1 12
HELIX 58 58 TRP D 213 TYR D 216 5 4
HELIX 59 59 ASP D 217 ILE D 222 1 6
HELIX 60 60 PRO D 250 VAL D 257 1 8
HELIX 61 61 SER D 277 LEU D 296 1 20
SHEET 1 A 9 LYS A 2 VAL A 9 0
SHEET 2 A 9 GLY A 12 ASN A 20 -1 O LEU A 14 N PHE A 7
SHEET 3 A 9 SER A 27 LEU A 34 -1 O VAL A 30 N LEU A 17
SHEET 4 A 9 ALA A 81 PRO A 85 -1 O PHE A 84 N ASN A 31
SHEET 5 A 9 THR A 51 LEU A 55 1 N TYR A 54 O VAL A 83
SHEET 6 A 9 VAL A 155 GLY A 159 1 O ALA A 156 N THR A 51
SHEET 7 A 9 SER A 182 PHE A 186 1 O PHE A 186 N GLY A 159
SHEET 8 A 9 ILE A 233 GLY A 238 1 O HIS A 236 N ALA A 185
SHEET 9 A 9 VAL A 266 VAL A 271 1 O VAL A 271 N VAL A 237
SHEET 1 B 6 LYS B 2 VAL B 9 0
SHEET 2 B 6 GLY B 12 SER B 21 -1 O LYS B 16 N LYS B 5
SHEET 3 B 6 THR B 26 LEU B 34 -1 O VAL B 30 N LEU B 17
SHEET 4 B 6 ALA B 81 PRO B 85 -1 O PHE B 84 N ASN B 31
SHEET 5 B 6 ILE B 49 LEU B 55 1 N VAL B 52 O VAL B 83
SHEET 6 B 6 LEU B 149 GLY B 159 1 O ASP B 150 N ILE B 49
SHEET 1 C 3 CYS B 183 PHE B 186 0
SHEET 2 C 3 ILE B 233 GLY B 238 1 O HIS B 236 N ALA B 185
SHEET 3 C 3 VAL B 266 VAL B 271 1 O LYS B 269 N ILE B 235
SHEET 1 D 9 LYS C 2 VAL C 9 0
SHEET 2 D 9 GLY C 12 ASN C 20 -1 O LYS C 16 N VAL C 4
SHEET 3 D 9 SER C 27 LEU C 34 -1 O LEU C 34 N ARG C 13
SHEET 4 D 9 ALA C 81 PRO C 85 -1 O PHE C 84 N ASN C 31
SHEET 5 D 9 THR C 51 LEU C 55 1 N VAL C 52 O ALA C 81
SHEET 6 D 9 VAL C 155 GLY C 159 1 O ALA C 156 N PHE C 53
SHEET 7 D 9 SER C 182 PHE C 186 1 O PHE C 186 N GLY C 159
SHEET 8 D 9 ILE C 233 GLY C 238 1 O HIS C 236 N ALA C 185
SHEET 9 D 9 VAL C 266 VAL C 271 1 O LYS C 269 N ILE C 235
SHEET 1 E 9 LYS D 2 VAL D 9 0
SHEET 2 E 9 GLY D 12 ASN D 20 -1 O SER D 18 N LYS D 2
SHEET 3 E 9 SER D 27 LEU D 34 -1 O VAL D 30 N LEU D 17
SHEET 4 E 9 ALA D 81 PHE D 84 -1 O PHE D 84 N ASN D 31
SHEET 5 E 9 PRO D 50 LEU D 55 1 N TYR D 54 O VAL D 83
SHEET 6 E 9 ASP D 150 GLY D 159 1 O ALA D 156 N PHE D 53
SHEET 7 E 9 SER D 182 PHE D 186 1 O SER D 182 N ILE D 157
SHEET 8 E 9 ILE D 233 GLY D 238 1 O LEU D 234 N ALA D 185
SHEET 9 E 9 VAL D 266 VAL D 271 1 O LYS D 269 N ILE D 235
CISPEP 1 GLU C 117 PRO C 118 0 16.76
CISPEP 2 LYS D 173 GLY D 174 0 15.96
CRYST1 66.300 119.740 169.200 90.00 90.00 90.00 P 21 21 21 16
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 0.015083 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008351 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005910 0.00000
TER 2271 ILE A 299
TER 4542 ILE B 299
TER 6804 ILE C 299
TER 9067 ILE D 299
MASTER 456 0 0 61 36 0 0 6 9243 4 0 92
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