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HEADER HYDROLASE 17-OCT-98 1EHY
TITLE X-RAY STRUCTURE OF THE EPOXIDE HYDROLASE FROM AGROBACTERIUM
TITLE 2 RADIOBACTER AD1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SOLUBLE EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.3.2.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 BIOLOGICAL_UNIT: MONOMER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AGROBACTERIUM RADIOBACTER;
SOURCE 3 STRAIN: AD1;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PGELAF+
KEYWDS HYDROLASE, ALPHA/BETA HYDROLASE FOLD, EPOXIDE DEGRADATION,
KEYWDS 2 EPICHLOROHYDRIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.NARDINI,I.S.RIDDER,H.J.ROZEBOOM,K.H.KALK,R.RINK,
AUTHOR 2 D.B.JANSSEN,B.W.DIJKSTRA
REVDAT 1 16-OCT-99 3STD 0
JRNL AUTH M.NARDINI,I.S.RIDDER,H.J.ROZEBOOM,K.H.KALK,R.RINK,
JRNL AUTH 2 D.B.JANSSEN,B.W.DIJKSTRA
JRNL TITL THE X-RAY STRUCTURE OF EPOXIDE HYDROLASE FROM
JRNL TITL 2 AGROBACTERIUM RADIOBACTER AD1. AN ENZYME TO
JRNL TITL 3 DETOXIFY HARMFUL EPOXIDES
JRNL REF J.BIOL.CHEM. V. 274 14579 1999
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 0071
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.H.LUTJE SPELBERG,R.RINK,R.M.KELLOGG,D.B.JANSSEN
REMARK 1 TITL ENANTIOSELECTIVITY OF A RECOMBINANT EPOXIDE
REMARK 1 TITL 2 HYDROLASE FROM AGROBACTERIUM RADIOBACTER
REMARK 1 REF TETRAHEDRON V. 9 459 1998
REMARK 1 REFN ASTM TETRAB UK ISSN 0040-4020 0016
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.RINK,M.FENNEMA,M.SMIDS,U.DEHMEL,D.B.JANSSEN
REMARK 1 TITL PRIMARY STRUCTURE AND CATALYTIC MECHANISM OF THE
REMARK 1 TITL 2 EPOXIDE HYDROLASE FROM AGROBACTERIUM RADIOBACTER
REMARK 1 TITL 3 AD1
REMARK 1 REF J.BIOL.CHEM. V. 272 14650 1997
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.H.J.JACOBS,A.J.VAN DEN WIJNGAARD,M.PENTENGA,
REMARK 1 AUTH 2 D.B.JANSSEN
REMARK 1 TITL KINETIC MECHANISM OF THE ENANTIOSELECTIVE
REMARK 1 TITL 2 CONVERSION OF STYRENE OXIDE BY EPOXIDE HYDROLASE
REMARK 1 TITL 3 FROM AGROBACTERIUM RADIODACTER AD1
REMARK 1 REF BIOCHEMISTRY V. 37 18119 1998
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033
REMARK 1 REFERENCE 4
REMARK 1 AUTH R.RINK,J.H.LUTJE SPELBERG,R.J.PIETERS,J.KINGMA,
REMARK 1 AUTH 2 M.NARDINI,R.M.KELLOGG,B.W.DIJKSTRA,D.B.JANSSEN
REMARK 1 TITL MUTATION OF TYROSINE RESIDUES INVOLVED IN THE
REMARK 1 TITL 2 ALKYLATION HALF REACTION OF EPOXIDE HYDROLASE FROM
REMARK 1 TITL 3 AGROBACTERIUM RADIODACTER AD1 RESULTS IN IMPROVED
REMARK 1 TITL 4 ENANTIOSELECTIVITY
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN 0353
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.843
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.5
REMARK 3 NUMBER OF REFLECTIONS : 68692
REMARK 3
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : SHELLS
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 3544
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 12
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 71.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4538
REMARK 3 BIN R VALUE (WORKING SET) : 0.2860
REMARK 3 BIN FREE R VALUE : 0.3180
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 214
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9262
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 610
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : 0.290
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.30
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.33
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.17
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3
REMARK 3 NCS MODEL : RESTRAINTS
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.WAT
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.WAT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT CORRECTION USED
REMARK 3 DURING THE REFINEMENT
REMARK 4
REMARK 4 1EHY COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 7
REMARK 7 IN ALL 4 MOLECULES IN THE ASYMMETRIC UNIT THE LOOP 246-251
REMARK 7 SHOWS POOR ELECTRON DENSITY. HOWEVER CLEAR ELECTRON DENSITY
REMARK 7 IS PRESENT FOR THE SS BOND BETWEEN RESIDUES C248 AND D248.
REMARK 7 DUE TO A SLIGHTLY DIFFERENT CONFORMATION OF THAT LOOP IN
REMARK 7 MONOMER A, NO SS BOND IS OBSERVED BETWEEN RESIDUES A248
REMARK 7 AND B248
REMARK 8
REMARK 8 DUE TO A CRYSTAL CONTACT BETWEEN LOOP RESIDUES 246-251 OF
REMARK 8 MONOMERS C AND D AND MONOMERS A AND B, IN ALL 4 MONOMERS
REMARK 8 THE CATALYTIC ASP 246 IS PULLED OUT FROM THE ACTIVE SITE,
REMARK 8 SO ALLOWING RESIDUE GLN 134 TO MOVE INTO THE ACTIVE SITE.
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-1999.
REMARK 100 THE RCSB ID CODE IS RCSB007036.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-AUG-1997
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73445
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.5
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.570
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M KH2PO4/K2HPO4
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+Y,-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 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 73.31200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.10050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 73.31200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 50.10050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 SSS
REMARK 295 M 1 B 2 .. 294 A 2 .. 294 0.528
REMARK 295 M 2 C 2 .. 294 A 2 .. 294 0.570
REMARK 295 M 3 D 2 .. 294 A 2 .. 294 0.547
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 295
REMARK 295 REMARK:
REMARK 295 TRANSFORMATION RELATES C-ALPHA CHAIN B TO C-ALPHA CHAIN
REMARK 295 A
REMARK 295 TRANSFORMATION RELATES C-ALPHA CHAIN C TO C-ALPHA CHAIN
REMARK 295 A
REMARK 295 TRANSFORMATION RELATES C-ALPHA CHAIN D TO C-ALPHA CHAIN
REMARK 295 A
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 GLY A 138
REMARK 465 PRO A 139
REMARK 465 VAL A 140
REMARK 465 TYR A 141
REMARK 465 PHE A 142
REMARK 465 GLY A 143
REMARK 465 LEU A 144
REMARK 465 GLY A 145
REMARK 465 HIS A 146
REMARK 465 VAL A 147
REMARK 465 HIS A 148
REMARK 465 MET B 1
REMARK 465 GLY B 138
REMARK 465 PRO B 139
REMARK 465 VAL B 140
REMARK 465 TYR B 141
REMARK 465 PHE B 142
REMARK 465 GLY B 143
REMARK 465 LEU B 144
REMARK 465 GLY B 145
REMARK 465 HIS B 146
REMARK 465 VAL B 147
REMARK 465 HIS B 148
REMARK 465 MET C 1
REMARK 465 GLY C 138
REMARK 465 PRO C 139
REMARK 465 VAL C 140
REMARK 465 TYR C 141
REMARK 465 PHE C 142
REMARK 465 GLY C 143
REMARK 465 LEU C 144
REMARK 465 GLY C 145
REMARK 465 HIS C 146
REMARK 465 VAL C 147
REMARK 465 HIS C 148
REMARK 465 MET D 1
REMARK 465 GLY D 138
REMARK 465 PRO D 139
REMARK 465 VAL D 140
REMARK 465 TYR D 141
REMARK 465 PHE D 142
REMARK 465 GLY D 143
REMARK 465 LEU D 144
REMARK 465 GLY D 145
REMARK 465 HIS D 146
REMARK 465 VAL D 147
REMARK 465 HIS D 148
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG C 294 CG CD NE CZ NH1 NH2
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 4*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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 4 N - CA - C ANGL. DEV. = -7.6 DEGREES
REMARK 500 HIS A 11 N - CA - C ANGL. DEV. = 5.7 DEGREES
REMARK 500 GLN A 15 N - CA - C ANGL. DEV. = -7.1 DEGREES
REMARK 500 LEU A 16 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 VAL A 24 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 TRP A 43 N - CA - C ANGL. DEV. = 6.1 DEGREES
REMARK 500 SER A 46 N - CA - C ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASP A 57 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 ASP A 62 N - CA - C ANGL. DEV. = -8.9 DEGREES
REMARK 500 ARG A 64 N - CA - C ANGL. DEV. = -5.7 DEGREES
REMARK 500 LYS A 71 N - CA - C ANGL. DEV. = -7.0 DEGREES
REMARK 500 LEU A 74 N - CA - C ANGL. DEV. = 5.7 DEGREES
REMARK 500 LEU A 82 CA - CB - CG ANGL. DEV. = -5.5 DEGREES
REMARK 500 LEU A 92 CA - CB - CG ANGL. DEV. = 6.6 DEGREES
REMARK 500 TYR A 102 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 ALA A 110 N - CA - C ANGL. DEV. = -6.4 DEGREES
REMARK 500 LYS A 126 N - CA - C ANGL. DEV. = -6.3 DEGREES
REMARK 500 PRO A 135 N - CA - C ANGL. DEV. = 9.6 DEGREES
REMARK 500 PHE A 137 N - CA - C ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP A 187 N - CA - C ANGL. DEV. = 6.2 DEGREES
REMARK 500 THR A 191 N - CA - C ANGL. DEV. = -8.0 DEGREES
REMARK 500 ASP A 206 N - CA - C ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASN A 218 N - CA - C ANGL. DEV. = 6.7 DEGREES
REMARK 500 LEU A 236 CA - CB - CG ANGL. DEV. = 7.2 DEGREES
REMARK 500 VAL A 249 CA - C - N ANGL. DEV. = 11.4 DEGREES
REMARK 500 VAL A 249 O - C - N ANGL. DEV. =-12.2 DEGREES
REMARK 500 PRO A 250 CA - C - N ANGL. DEV. = 8.3 DEGREES
REMARK 500 PRO A 250 O - C - N ANGL. DEV. = -7.0 DEGREES
REMARK 500 PHE A 257 N - CA - C ANGL. DEV. = 5.8 DEGREES
REMARK 500 GLN B 15 N - CA - C ANGL. DEV. = -5.7 DEGREES
REMARK 500 LEU B 16 N - CA - C ANGL. DEV. = -6.7 DEGREES
REMARK 500 VAL B 24 N - CA - C ANGL. DEV. = -7.0 DEGREES
REMARK 500 LEU B 33 CA - CB - CG ANGL. DEV. = 6.6 DEGREES
REMARK 500 TRP B 43 N - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 SER B 46 N - CA - C ANGL. DEV. = 7.0 DEGREES
REMARK 500 ASP B 57 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 ASP B 62 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 LYS B 71 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 LEU B 92 CA - CB - CG ANGL. DEV. = 6.4 DEGREES
REMARK 500 TYR B 102 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 ILE B 125 N - CA - C ANGL. DEV. = -6.8 DEGREES
REMARK 500 PRO B 135 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 PRO B 135 C - N - CA ANGL. DEV. = 5.6 DEGREES
REMARK 500 SER B 150 N - CA - C ANGL. DEV. = -5.9 DEGREES
REMARK 500 THR B 191 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 ASP B 206 N - CA - C ANGL. DEV. = 7.6 DEGREES
REMARK 500 ASN B 218 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 VAL B 249 CA - C - N ANGL. DEV. = 6.0 DEGREES
REMARK 500 VAL B 249 O - C - N ANGL. DEV. = -6.6 DEGREES
REMARK 500 PHE B 257 N - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 HIS B 275 N - CA - C ANGL. DEV. = 5.6 DEGREES
REMARK 500 PHE B 293 N - CA - C ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG C 4 N - CA - C ANGL. DEV. = -6.1 DEGREES
REMARK 500 LEU C 16 N - CA - C ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP C 18 N - CA - C ANGL. DEV. = 6.0 DEGREES
REMARK 500 LYS C 20 N - CA - C ANGL. DEV. = -6.1 DEGREES
REMARK 500 VAL C 24 N - CA - C ANGL. DEV. = -7.3 DEGREES
REMARK 500 LEU C 33 CA - CB - CG ANGL. DEV. = 6.8 DEGREES
REMARK 500 TRP C 43 N - CA - C ANGL. DEV. = 6.6 DEGREES
REMARK 500 SER C 46 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 ASP C 57 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 VAL C 58 C - N - CA ANGL. DEV. = -6.8 DEGREES
REMARK 500 ASP C 62 N - CA - C ANGL. DEV. =-10.6 DEGREES
REMARK 500 LEU C 63 N - CA - C ANGL. DEV. = -6.5 DEGREES
REMARK 500 SER C 69 N - CA - C ANGL. DEV. = -6.7 DEGREES
REMARK 500 LYS C 71 N - CA - C ANGL. DEV. = -6.5 DEGREES
REMARK 500 LEU C 92 CA - CB - CG ANGL. DEV. = 6.9 DEGREES
REMARK 500 TYR C 102 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 ALA C 110 N - CA - C ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP C 131 N - CA - C ANGL. DEV. = 5.8 DEGREES
REMARK 500 PRO C 135 C - CA - CB ANGL. DEV. = 5.7 DEGREES
REMARK 500 PRO C 135 N - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 THR C 191 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 ASP C 206 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 ALA C 217 N - CA - C ANGL. DEV. = 6.2 DEGREES
REMARK 500 VAL C 249 N - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500 TYR C 251 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 PHE C 257 N - CA - C ANGL. DEV. = 6.1 DEGREES
REMARK 500 THR C 269 N - CA - C ANGL. DEV. = -6.6 DEGREES
REMARK 500 HIS C 275 N - CA - C ANGL. DEV. = 6.4 DEGREES
REMARK 500 PHE C 293 N - CA - C ANGL. DEV. = 6.9 DEGREES
REMARK 500 GLU D 13 N - CA - C ANGL. DEV. = -7.1 DEGREES
REMARK 500 LEU D 16 N - CA - C ANGL. DEV. = -6.3 DEGREES
REMARK 500 VAL D 24 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 LEU D 33 CA - CB - CG ANGL. DEV. = 6.8 DEGREES
REMARK 500 TRP D 43 N - CA - C ANGL. DEV. = 6.8 DEGREES
REMARK 500 SER D 46 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 VAL D 48 N - CA - CB ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP D 57 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 ASP D 62 N - CA - C ANGL. DEV. =-10.8 DEGREES
REMARK 500 LYS D 71 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 LEU D 92 CA - CB - CG ANGL. DEV. = 7.0 DEGREES
REMARK 500 TYR D 102 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 PRO D 135 N - CA - C ANGL. DEV. = 9.9 DEGREES
REMARK 500 PRO D 135 C - N - CA ANGL. DEV. = 6.9 DEGREES
REMARK 500 SER D 150 N - CA - C ANGL. DEV. = -6.1 DEGREES
REMARK 500 LEU D 158 N - CA - C ANGL. DEV. = 5.8 DEGREES
REMARK 500 THR D 191 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 ASP D 206 N - CA - C ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASN D 218 N - CA - C ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG D 220 N - CA - C ANGL. DEV. = -6.7 DEGREES
REMARK 500 ALA D 223 N - CA - C ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP D 226 N - CA - C ANGL. DEV. = 5.9 DEGREES
REMARK 500 TYR D 251 N - CA - C ANGL. DEV. = 6.4 DEGREES
REMARK 500 PHE D 257 N - CA - C ANGL. DEV. = 7.6 DEGREES
REMARK 500 PHE D 293 N - CA - C ANGL. DEV. = 5.9 DEGREES
DBREF 1EHY A 1 294 GB CAA73331 Y12804 1 294
DBREF 1EHY B 1 294 GB CAA73331 Y12804 1 294
DBREF 1EHY C 1 294 GB CAA73331 Y12804 1 294
DBREF 1EHY D 1 294 GB CAA73331 Y12804 1 294
SEQADV 1EHY ALA A 2 GB CAA73331 THR 2 CLONING ARTIFACT
SEQADV 1EHY ALA B 2 GB CAA73331 THR 2 CLONING ARTIFACT
SEQADV 1EHY ALA C 2 GB CAA73331 THR 2 CLONING ARTIFACT
SEQADV 1EHY ALA D 2 GB CAA73331 THR 2 CLONING ARTIFACT
SEQRES 1 A 294 MET ALA ILE ARG ARG PRO GLU ASP PHE LYS HIS TYR GLU
SEQRES 2 A 294 VAL GLN LEU PRO ASP VAL LYS ILE HIS TYR VAL ARG GLU
SEQRES 3 A 294 GLY ALA GLY PRO THR LEU LEU LEU LEU HIS GLY TRP PRO
SEQRES 4 A 294 GLY PHE TRP TRP GLU TRP SER LYS VAL ILE GLY PRO LEU
SEQRES 5 A 294 ALA GLU HIS TYR ASP VAL ILE VAL PRO ASP LEU ARG GLY
SEQRES 6 A 294 PHE GLY ASP SER GLU LYS PRO ASP LEU ASN ASP LEU SER
SEQRES 7 A 294 LYS TYR SER LEU ASP LYS ALA ALA ASP ASP GLN ALA ALA
SEQRES 8 A 294 LEU LEU ASP ALA LEU GLY ILE GLU LYS ALA TYR VAL VAL
SEQRES 9 A 294 GLY HIS ASP PHE ALA ALA ILE VAL LEU HIS LYS PHE ILE
SEQRES 10 A 294 ARG LYS TYR SER ASP ARG VAL ILE LYS ALA ALA ILE PHE
SEQRES 11 A 294 ASP PRO ILE GLN PRO ASP PHE GLY PRO VAL TYR PHE GLY
SEQRES 12 A 294 LEU GLY HIS VAL HIS GLU SER TRP TYR SER GLN PHE HIS
SEQRES 13 A 294 GLN LEU ASP MET ALA VAL GLU VAL VAL GLY SER SER ARG
SEQRES 14 A 294 GLU VAL CYS LYS LYS TYR PHE LYS HIS PHE PHE ASP HIS
SEQRES 15 A 294 TRP SER TYR ARG ASP GLU LEU LEU THR GLU GLU GLU LEU
SEQRES 16 A 294 GLU VAL HIS VAL ASP ASN CYS MET LYS PRO ASP ASN ILE
SEQRES 17 A 294 HIS GLY GLY PHE ASN TYR TYR ARG ALA ASN ILE ARG PRO
SEQRES 18 A 294 ASP ALA ALA LEU TRP THR ASP LEU ASP HIS THR MET SER
SEQRES 19 A 294 ASP LEU PRO VAL THR MET ILE TRP GLY LEU GLY ASP THR
SEQRES 20 A 294 CYS VAL PRO TYR ALA PRO LEU ILE GLU PHE VAL PRO LYS
SEQRES 21 A 294 TYR TYR SER ASN TYR THR MET GLU THR ILE GLU ASP CYS
SEQRES 22 A 294 GLY HIS PHE LEU MET VAL GLU LYS PRO GLU ILE ALA ILE
SEQRES 23 A 294 ASP ARG ILE LYS THR ALA PHE ARG
SEQRES 1 B 294 MET ALA ILE ARG ARG PRO GLU ASP PHE LYS HIS TYR GLU
SEQRES 2 B 294 VAL GLN LEU PRO ASP VAL LYS ILE HIS TYR VAL ARG GLU
SEQRES 3 B 294 GLY ALA GLY PRO THR LEU LEU LEU LEU HIS GLY TRP PRO
SEQRES 4 B 294 GLY PHE TRP TRP GLU TRP SER LYS VAL ILE GLY PRO LEU
SEQRES 5 B 294 ALA GLU HIS TYR ASP VAL ILE VAL PRO ASP LEU ARG GLY
SEQRES 6 B 294 PHE GLY ASP SER GLU LYS PRO ASP LEU ASN ASP LEU SER
SEQRES 7 B 294 LYS TYR SER LEU ASP LYS ALA ALA ASP ASP GLN ALA ALA
SEQRES 8 B 294 LEU LEU ASP ALA LEU GLY ILE GLU LYS ALA TYR VAL VAL
SEQRES 9 B 294 GLY HIS ASP PHE ALA ALA ILE VAL LEU HIS LYS PHE ILE
SEQRES 10 B 294 ARG LYS TYR SER ASP ARG VAL ILE LYS ALA ALA ILE PHE
SEQRES 11 B 294 ASP PRO ILE GLN PRO ASP PHE GLY PRO VAL TYR PHE GLY
SEQRES 12 B 294 LEU GLY HIS VAL HIS GLU SER TRP TYR SER GLN PHE HIS
SEQRES 13 B 294 GLN LEU ASP MET ALA VAL GLU VAL VAL GLY SER SER ARG
SEQRES 14 B 294 GLU VAL CYS LYS LYS TYR PHE LYS HIS PHE PHE ASP HIS
SEQRES 15 B 294 TRP SER TYR ARG ASP GLU LEU LEU THR GLU GLU GLU LEU
SEQRES 16 B 294 GLU VAL HIS VAL ASP ASN CYS MET LYS PRO ASP ASN ILE
SEQRES 17 B 294 HIS GLY GLY PHE ASN TYR TYR ARG ALA ASN ILE ARG PRO
SEQRES 18 B 294 ASP ALA ALA LEU TRP THR ASP LEU ASP HIS THR MET SER
SEQRES 19 B 294 ASP LEU PRO VAL THR MET ILE TRP GLY LEU GLY ASP THR
SEQRES 20 B 294 CYS VAL PRO TYR ALA PRO LEU ILE GLU PHE VAL PRO LYS
SEQRES 21 B 294 TYR TYR SER ASN TYR THR MET GLU THR ILE GLU ASP CYS
SEQRES 22 B 294 GLY HIS PHE LEU MET VAL GLU LYS PRO GLU ILE ALA ILE
SEQRES 23 B 294 ASP ARG ILE LYS THR ALA PHE ARG
SEQRES 1 C 294 MET ALA ILE ARG ARG PRO GLU ASP PHE LYS HIS TYR GLU
SEQRES 2 C 294 VAL GLN LEU PRO ASP VAL LYS ILE HIS TYR VAL ARG GLU
SEQRES 3 C 294 GLY ALA GLY PRO THR LEU LEU LEU LEU HIS GLY TRP PRO
SEQRES 4 C 294 GLY PHE TRP TRP GLU TRP SER LYS VAL ILE GLY PRO LEU
SEQRES 5 C 294 ALA GLU HIS TYR ASP VAL ILE VAL PRO ASP LEU ARG GLY
SEQRES 6 C 294 PHE GLY ASP SER GLU LYS PRO ASP LEU ASN ASP LEU SER
SEQRES 7 C 294 LYS TYR SER LEU ASP LYS ALA ALA ASP ASP GLN ALA ALA
SEQRES 8 C 294 LEU LEU ASP ALA LEU GLY ILE GLU LYS ALA TYR VAL VAL
SEQRES 9 C 294 GLY HIS ASP PHE ALA ALA ILE VAL LEU HIS LYS PHE ILE
SEQRES 10 C 294 ARG LYS TYR SER ASP ARG VAL ILE LYS ALA ALA ILE PHE
SEQRES 11 C 294 ASP PRO ILE GLN PRO ASP PHE GLY PRO VAL TYR PHE GLY
SEQRES 12 C 294 LEU GLY HIS VAL HIS GLU SER TRP TYR SER GLN PHE HIS
SEQRES 13 C 294 GLN LEU ASP MET ALA VAL GLU VAL VAL GLY SER SER ARG
SEQRES 14 C 294 GLU VAL CYS LYS LYS TYR PHE LYS HIS PHE PHE ASP HIS
SEQRES 15 C 294 TRP SER TYR ARG ASP GLU LEU LEU THR GLU GLU GLU LEU
SEQRES 16 C 294 GLU VAL HIS VAL ASP ASN CYS MET LYS PRO ASP ASN ILE
SEQRES 17 C 294 HIS GLY GLY PHE ASN TYR TYR ARG ALA ASN ILE ARG PRO
SEQRES 18 C 294 ASP ALA ALA LEU TRP THR ASP LEU ASP HIS THR MET SER
SEQRES 19 C 294 ASP LEU PRO VAL THR MET ILE TRP GLY LEU GLY ASP THR
SEQRES 20 C 294 CYS VAL PRO TYR ALA PRO LEU ILE GLU PHE VAL PRO LYS
SEQRES 21 C 294 TYR TYR SER ASN TYR THR MET GLU THR ILE GLU ASP CYS
SEQRES 22 C 294 GLY HIS PHE LEU MET VAL GLU LYS PRO GLU ILE ALA ILE
SEQRES 23 C 294 ASP ARG ILE LYS THR ALA PHE ARG
SEQRES 1 D 294 MET ALA ILE ARG ARG PRO GLU ASP PHE LYS HIS TYR GLU
SEQRES 2 D 294 VAL GLN LEU PRO ASP VAL LYS ILE HIS TYR VAL ARG GLU
SEQRES 3 D 294 GLY ALA GLY PRO THR LEU LEU LEU LEU HIS GLY TRP PRO
SEQRES 4 D 294 GLY PHE TRP TRP GLU TRP SER LYS VAL ILE GLY PRO LEU
SEQRES 5 D 294 ALA GLU HIS TYR ASP VAL ILE VAL PRO ASP LEU ARG GLY
SEQRES 6 D 294 PHE GLY ASP SER GLU LYS PRO ASP LEU ASN ASP LEU SER
SEQRES 7 D 294 LYS TYR SER LEU ASP LYS ALA ALA ASP ASP GLN ALA ALA
SEQRES 8 D 294 LEU LEU ASP ALA LEU GLY ILE GLU LYS ALA TYR VAL VAL
SEQRES 9 D 294 GLY HIS ASP PHE ALA ALA ILE VAL LEU HIS LYS PHE ILE
SEQRES 10 D 294 ARG LYS TYR SER ASP ARG VAL ILE LYS ALA ALA ILE PHE
SEQRES 11 D 294 ASP PRO ILE GLN PRO ASP PHE GLY PRO VAL TYR PHE GLY
SEQRES 12 D 294 LEU GLY HIS VAL HIS GLU SER TRP TYR SER GLN PHE HIS
SEQRES 13 D 294 GLN LEU ASP MET ALA VAL GLU VAL VAL GLY SER SER ARG
SEQRES 14 D 294 GLU VAL CYS LYS LYS TYR PHE LYS HIS PHE PHE ASP HIS
SEQRES 15 D 294 TRP SER TYR ARG ASP GLU LEU LEU THR GLU GLU GLU LEU
SEQRES 16 D 294 GLU VAL HIS VAL ASP ASN CYS MET LYS PRO ASP ASN ILE
SEQRES 17 D 294 HIS GLY GLY PHE ASN TYR TYR ARG ALA ASN ILE ARG PRO
SEQRES 18 D 294 ASP ALA ALA LEU TRP THR ASP LEU ASP HIS THR MET SER
SEQRES 19 D 294 ASP LEU PRO VAL THR MET ILE TRP GLY LEU GLY ASP THR
SEQRES 20 D 294 CYS VAL PRO TYR ALA PRO LEU ILE GLU PHE VAL PRO LYS
SEQRES 21 D 294 TYR TYR SER ASN TYR THR MET GLU THR ILE GLU ASP CYS
SEQRES 22 D 294 GLY HIS PHE LEU MET VAL GLU LYS PRO GLU ILE ALA ILE
SEQRES 23 D 294 ASP ARG ILE LYS THR ALA PHE ARG
HET K 295 1
HET K 296 1
HET K 297 1
HET K 298 1
HETNAM K POTASSIUM ION
FORMUL 5 K 4(K1 1+)
FORMUL 9 HOH *577(H2 O1)
HELIX 1 1 PRO A 6 ASP A 8 5 3
HELIX 2 2 TRP A 42 GLU A 54 5 13
HELIX 3 3 LEU A 77 TYR A 80 5 4
HELIX 4 4 LEU A 82 ALA A 95 1 14
HELIX 5 5 ASP A 107 LYS A 119 5 13
HELIX 6 6 SER A 121 ARG A 123 5 3
HELIX 7 7 TRP A 151 GLN A 157 1 7
HELIX 8 8 ASP A 159 VAL A 165 1 7
HELIX 9 9 ARG A 169 HIS A 182 1 14
HELIX 10 10 GLU A 192 CYS A 202 1 11
HELIX 11 11 ASN A 207 ASN A 218 1 12
HELIX 12 12 LEU A 229 HIS A 231 5 3
HELIX 13 13 ALA A 252 TYR A 261 1 10
HELIX 14 14 LEU A 277 GLU A 280 1 4
HELIX 15 15 PRO A 282 ALA A 292 1 11
HELIX 16 16 PRO B 6 ASP B 8 5 3
HELIX 17 17 TRP B 42 GLU B 54 5 13
HELIX 18 18 LEU B 77 TYR B 80 5 4
HELIX 19 19 LEU B 82 ALA B 95 1 14
HELIX 20 20 ASP B 107 LYS B 119 5 13
HELIX 21 21 SER B 121 ARG B 123 5 3
HELIX 22 22 TRP B 151 GLN B 157 1 7
HELIX 23 23 ASP B 159 VAL B 165 1 7
HELIX 24 24 ARG B 169 HIS B 182 1 14
HELIX 25 25 GLU B 192 CYS B 202 1 11
HELIX 26 26 ASN B 207 ASN B 218 1 12
HELIX 27 27 LEU B 229 HIS B 231 5 3
HELIX 28 28 ALA B 252 LYS B 260 1 9
HELIX 29 29 LEU B 277 GLU B 280 1 4
HELIX 30 30 PRO B 282 ALA B 292 1 11
HELIX 31 31 PRO C 6 ASP C 8 5 3
HELIX 32 32 TRP C 42 GLU C 54 5 13
HELIX 33 33 LEU C 77 TYR C 80 5 4
HELIX 34 34 LEU C 82 ALA C 95 1 14
HELIX 35 35 ASP C 107 LYS C 119 5 13
HELIX 36 36 SER C 121 ARG C 123 5 3
HELIX 37 37 TRP C 151 GLN C 157 1 7
HELIX 38 38 ASP C 159 VAL C 165 1 7
HELIX 39 39 ARG C 169 HIS C 182 1 14
HELIX 40 40 GLU C 192 CYS C 202 1 11
HELIX 41 41 ASN C 207 ASN C 218 1 12
HELIX 42 42 LEU C 229 HIS C 231 5 3
HELIX 43 43 VAL C 249 LYS C 260 1 12
HELIX 44 44 LEU C 277 GLU C 280 1 4
HELIX 45 45 PRO C 282 ALA C 292 1 11
HELIX 46 46 PRO D 6 ASP D 8 5 3
HELIX 47 47 TRP D 42 GLU D 54 5 13
HELIX 48 48 LEU D 77 TYR D 80 5 4
HELIX 49 49 LEU D 82 ALA D 95 1 14
HELIX 50 50 ASP D 107 LYS D 119 5 13
HELIX 51 51 SER D 121 ARG D 123 5 3
HELIX 52 52 TRP D 151 GLN D 157 1 7
HELIX 53 53 ASP D 159 VAL D 165 1 7
HELIX 54 54 ARG D 169 HIS D 182 1 14
HELIX 55 55 GLU D 192 CYS D 202 1 11
HELIX 56 56 ASN D 207 ASN D 218 1 12
HELIX 57 57 LEU D 229 HIS D 231 5 3
HELIX 58 58 VAL D 249 TYR D 261 1 13
HELIX 59 59 LEU D 277 GLU D 280 1 4
HELIX 60 60 PRO D 282 ALA D 292 1 11
SHEET 1 A 8 HIS A 11 GLN A 15 0
SHEET 2 A 8 LYS A 20 GLY A 27 -1 N TYR A 23 O TYR A 12
SHEET 3 A 8 TYR A 56 PRO A 61 -1 N VAL A 60 O VAL A 24
SHEET 4 A 8 PRO A 30 LEU A 35 1 N PRO A 30 O ASP A 57
SHEET 5 A 8 TYR A 102 HIS A 106 1 N TYR A 102 O LEU A 33
SHEET 6 A 8 ALA A 127 PHE A 130 1 N ALA A 128 O VAL A 103
SHEET 7 A 8 VAL A 238 GLY A 243 1 N THR A 239 O ALA A 127
SHEET 8 A 8 TYR A 265 ILE A 270 1 N THR A 266 O VAL A 238
SHEET 1 B 8 HIS B 11 GLN B 15 0
SHEET 2 B 8 LYS B 20 GLY B 27 -1 N TYR B 23 O TYR B 12
SHEET 3 B 8 TYR B 56 PRO B 61 -1 N VAL B 60 O VAL B 24
SHEET 4 B 8 PRO B 30 LEU B 35 1 N PRO B 30 O ASP B 57
SHEET 5 B 8 TYR B 102 HIS B 106 1 N TYR B 102 O LEU B 33
SHEET 6 B 8 ALA B 127 PHE B 130 1 N ALA B 128 O VAL B 103
SHEET 7 B 8 VAL B 238 GLY B 243 1 N THR B 239 O ALA B 127
SHEET 8 B 8 TYR B 265 ILE B 270 1 N THR B 266 O VAL B 238
SHEET 1 C 8 HIS C 11 GLN C 15 0
SHEET 2 C 8 LYS C 20 GLY C 27 -1 N TYR C 23 O TYR C 12
SHEET 3 C 8 TYR C 56 PRO C 61 -1 N VAL C 60 O VAL C 24
SHEET 4 C 8 PRO C 30 LEU C 35 1 N PRO C 30 O ASP C 57
SHEET 5 C 8 TYR C 102 HIS C 106 1 N TYR C 102 O LEU C 33
SHEET 6 C 8 ALA C 127 PHE C 130 1 N ALA C 128 O VAL C 103
SHEET 7 C 8 VAL C 238 GLY C 243 1 N THR C 239 O ALA C 127
SHEET 8 C 8 TYR C 265 ILE C 270 1 N THR C 266 O VAL C 238
SHEET 1 D 8 HIS D 11 GLN D 15 0
SHEET 2 D 8 LYS D 20 GLY D 27 -1 N TYR D 23 O TYR D 12
SHEET 3 D 8 TYR D 56 PRO D 61 -1 N VAL D 60 O VAL D 24
SHEET 4 D 8 PRO D 30 LEU D 35 1 N PRO D 30 O ASP D 57
SHEET 5 D 8 TYR D 102 HIS D 106 1 N TYR D 102 O LEU D 33
SHEET 6 D 8 ALA D 127 PHE D 130 1 N ALA D 128 O VAL D 103
SHEET 7 D 8 VAL D 238 GLY D 243 1 N THR D 239 O ALA D 127
SHEET 8 D 8 TYR D 265 ILE D 270 1 N THR D 266 O VAL D 238
SSBOND 1 CYS C 248 CYS D 248
CISPEP 1 TRP A 38 PRO A 39 0 -0.24
CISPEP 2 TRP B 38 PRO B 39 0 0.04
CISPEP 3 TRP C 38 PRO C 39 0 0.36
CISPEP 4 TRP D 38 PRO D 39 0 -0.02
CRYST1 146.624 100.201 96.879 90.00 100.68 90.00 C 1 2 1 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 0.006820 0.000000 0.001286 0.00000
SCALE2 0.000000 0.009980 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010504 0.00000
MTRIX1 1 -0.610100 0.647800 -0.456200 47.78990 1
MTRIX2 1 0.661100 0.098900 -0.743700 71.06300 1
MTRIX3 1 -0.436700 -0.755300 -0.488600 144.75270 1
MTRIX1 2 -0.042900 0.103200 0.993700 -48.09120 1
MTRIX2 2 0.127500 -0.986000 0.107800 62.66960 1
MTRIX3 2 0.990900 0.131300 0.029200 38.98360 1
MTRIX1 3 -0.361500 -0.759300 -0.541100 104.02440 1
MTRIX2 3 -0.726700 -0.134100 0.673700 16.71750 1
MTRIX3 3 -0.584100 0.636800 -0.503300 94.62400 1
END |