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HEADER DEHALOGENASE 08-AUG-96 1HDE
TITLE HALOALKANE DEHALOGENASE MUTANT WITH PHE 172 REPLACED WITH
TITLE 2 TRP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: F172W
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XANTHOBACTER AUTOTROPHICUS;
SOURCE 3 STRAIN: GJ10;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PGELAF+
KEYWDS DEHALOGENASE, HYDROLASE, DETOXIFICATION
EXPDTA X-RAY DIFFRACTION
AUTHOR I.S.RIDDER,K.H.KALK,B.W.DIJKSTRA
REVDAT 1 12-FEB-97 1HDE 0
JRNL AUTH J.P.SCHANSTRA,I.S.RIDDER,G.J.HEIMERIKS,R.RINK,
JRNL AUTH 2 G.J.POELARENDS,K.H.KALK,B.W.DIJKSTRA,D.B.JANSSEN
JRNL TITL KINETIC CHARACTERIZATION AND X-RAY STRUCTURE OF A
JRNL TITL 2 MUTANT OF HALOALKANE DEHALOGENASE WITH HIGHER
JRNL TITL 3 CATALYTIC ACTIVITY AND MODIFIED SUBSTRATE RANGE
JRNL REF BIOCHEMISTRY V. 35 13186 1996
JRNL REFN ASTM BICHAW US ISSN 0006-2960 0033
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.H.VERSCHUEREN,S.M.FRANKEN,H.J.ROZEBOOM,K.H.KALK,
REMARK 1 AUTH 2 B.W.DIJKSTRA
REMARK 1 TITL REFINED X-RAY STRUCTURES OF HALOALKANE DEHALOGENASE
REMARK 1 TITL 2 AT PH 6.2 AND PH 8.2 AND IMPLICATIONS FOR THE
REMARK 1 TITL 3 REACTION MECHANISM
REMARK 1 REF J.MOL.BIOL. V. 232 856 1993
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.H.VERSCHUEREN,F.SELJEE,H.J.ROZEBOOM,K.H.KALK,
REMARK 1 AUTH 2 B.W.DIJKSTRA
REMARK 1 TITL CRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC
REMARK 1 TITL 2 MECHANISM OF HALOALKANE DEHALOGENASE
REMARK 1 REF NATURE V. 363 693 1993
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006
REMARK 1 REFERENCE 3
REMARK 1 AUTH S.M.FRANKEN,H.J.ROZEBOOM,K.H.KALK,B.W.DIJKSTRA
REMARK 1 TITL CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE: AN
REMARK 1 TITL 2 ENZYME TO DETOXIFY HALOGENATED ALKANES
REMARK 1 REF EMBO J. V. 10 1297 1991
REMARK 1 REFN ASTM EMJODG UK ISSN 0261-4189 0897
REMARK 1 REFERENCE 4
REMARK 1 AUTH H.J.ROZEBOOM,J.KINGMA,D.B.JANSSEN,B.W.DIJKSTRA
REMARK 1 TITL CRYSTALLIZATION OF HALOALKANE DEHALOGENASE FROM
REMARK 1 TITL 2 XANTHOBACTER AUTOTROPHICUS GJ10
REMARK 1 REF J.MOL.BIOL. V. 200 611 1988
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070
REMARK 2
REMARK 2 RESOLUTION. 2.7 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 14413
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4964
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.15
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) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
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) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 NCS MODEL : NULL
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 : NULL
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 ESTIMATED COORD. ERROR 0.25 ANGSTROMS
REMARK 3
REMARK 3 REFINEMENT WAS DONE WITH THE FOLLOWING RESTRAINTS
REMARK 3 ON THE ATOMS OF THE NCS-RELATED MOLECULES A & B W=300
REMARK 3 KCAL/MOL, WEIGHTING W*SQ((X-<X>)) FOR EQUIVALENT ATOMS
REMARK 3 SIGB=1.5(A**2), WEIGHTING SQ((B-<B>))/SQ(SIGB) FOR
REMARK 3 EQUIVALENT ATOMS.
REMARK 4
REMARK 4 1HDE COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAY-1994
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
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) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : FAST AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : ENRAF-NONIUS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MADNES
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15796
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 200 DATA REDUNDANCY : 2.7
REMARK 200 R MERGE (I) : 0.101
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 40.
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 36.76471
REMARK 290 SMTRY3 2 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 1 .. 310 A 1 .. 310 0.080
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 295
REMARK 295 REMARK: NULL
DBREF 1HDE A 1 310 SWS P22643 HALO_XANAU 1 310
DBREF 1HDE B 1 310 SWS P22643 HALO_XANAU 1 310
SEQADV 1HDE TRP A 172 SWS P22643 PHE 172 ENGINEERED
SEQADV 1HDE TRP B 172 SWS P22643 PHE 172 ENGINEERED
SEQRES 1 A 310 MET ILE ASN ALA ILE ARG THR PRO ASP GLN ARG PHE SER
SEQRES 2 A 310 ASN LEU ASP GLN TYR PRO PHE SER PRO ASN TYR LEU ASP
SEQRES 3 A 310 ASP LEU PRO GLY TYR PRO GLY LEU ARG ALA HIS TYR LEU
SEQRES 4 A 310 ASP GLU GLY ASN SER ASP ALA GLU ASP VAL PHE LEU CYS
SEQRES 5 A 310 LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG LYS
SEQRES 6 A 310 MET ILE PRO VAL PHE ALA GLU SER GLY ALA ARG VAL ILE
SEQRES 7 A 310 ALA PRO ASP PHE PHE GLY PHE GLY LYS SER ASP LYS PRO
SEQRES 8 A 310 VAL ASP GLU GLU ASP TYR THR PHE GLU PHE HIS ARG ASN
SEQRES 9 A 310 PHE LEU LEU ALA LEU ILE GLU ARG LEU ASP LEU ARG ASN
SEQRES 10 A 310 ILE THR LEU VAL VAL GLN ASP TRP GLY GLY PHE LEU GLY
SEQRES 11 A 310 LEU THR LEU PRO MET ALA ASP PRO SER ARG PHE LYS ARG
SEQRES 12 A 310 LEU ILE ILE MET ASN ALA CYS LEU MET THR ASP PRO VAL
SEQRES 13 A 310 THR GLN PRO ALA PHE SER ALA PHE VAL THR GLN PRO ALA
SEQRES 14 A 310 ASP GLY TRP THR ALA TRP LYS TYR ASP LEU VAL THR PRO
SEQRES 15 A 310 SER ASP LEU ARG LEU ASP GLN PHE MET LYS ARG TRP ALA
SEQRES 16 A 310 PRO THR LEU THR GLU ALA GLU ALA SER ALA TYR ALA ALA
SEQRES 17 A 310 PRO PHE PRO ASP THR SER TYR GLN ALA GLY VAL ARG LYS
SEQRES 18 A 310 PHE PRO LYS MET VAL ALA GLN ARG ASP GLN ALA CYS ILE
SEQRES 19 A 310 ASP ILE SER THR GLU ALA ILE SER PHE TRP GLN ASN ASP
SEQRES 20 A 310 TRP ASN GLY GLN THR PHE MET ALA ILE GLY MET LYS ASP
SEQRES 21 A 310 LYS LEU LEU GLY PRO ASP VAL MET TYR PRO MET LYS ALA
SEQRES 22 A 310 LEU ILE ASN GLY CYS PRO GLU PRO LEU GLU ILE ALA ASP
SEQRES 23 A 310 ALA GLY HIS PHE VAL GLN GLU PHE GLY GLU GLN VAL ALA
SEQRES 24 A 310 ARG GLU ALA LEU LYS HIS PHE ALA GLU THR GLU
SEQRES 1 B 310 MET ILE ASN ALA ILE ARG THR PRO ASP GLN ARG PHE SER
SEQRES 2 B 310 ASN LEU ASP GLN TYR PRO PHE SER PRO ASN TYR LEU ASP
SEQRES 3 B 310 ASP LEU PRO GLY TYR PRO GLY LEU ARG ALA HIS TYR LEU
SEQRES 4 B 310 ASP GLU GLY ASN SER ASP ALA GLU ASP VAL PHE LEU CYS
SEQRES 5 B 310 LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG LYS
SEQRES 6 B 310 MET ILE PRO VAL PHE ALA GLU SER GLY ALA ARG VAL ILE
SEQRES 7 B 310 ALA PRO ASP PHE PHE GLY PHE GLY LYS SER ASP LYS PRO
SEQRES 8 B 310 VAL ASP GLU GLU ASP TYR THR PHE GLU PHE HIS ARG ASN
SEQRES 9 B 310 PHE LEU LEU ALA LEU ILE GLU ARG LEU ASP LEU ARG ASN
SEQRES 10 B 310 ILE THR LEU VAL VAL GLN ASP TRP GLY GLY PHE LEU GLY
SEQRES 11 B 310 LEU THR LEU PRO MET ALA ASP PRO SER ARG PHE LYS ARG
SEQRES 12 B 310 LEU ILE ILE MET ASN ALA CYS LEU MET THR ASP PRO VAL
SEQRES 13 B 310 THR GLN PRO ALA PHE SER ALA PHE VAL THR GLN PRO ALA
SEQRES 14 B 310 ASP GLY TRP THR ALA TRP LYS TYR ASP LEU VAL THR PRO
SEQRES 15 B 310 SER ASP LEU ARG LEU ASP GLN PHE MET LYS ARG TRP ALA
SEQRES 16 B 310 PRO THR LEU THR GLU ALA GLU ALA SER ALA TYR ALA ALA
SEQRES 17 B 310 PRO PHE PRO ASP THR SER TYR GLN ALA GLY VAL ARG LYS
SEQRES 18 B 310 PHE PRO LYS MET VAL ALA GLN ARG ASP GLN ALA CYS ILE
SEQRES 19 B 310 ASP ILE SER THR GLU ALA ILE SER PHE TRP GLN ASN ASP
SEQRES 20 B 310 TRP ASN GLY GLN THR PHE MET ALA ILE GLY MET LYS ASP
SEQRES 21 B 310 LYS LEU LEU GLY PRO ASP VAL MET TYR PRO MET LYS ALA
SEQRES 22 B 310 LEU ILE ASN GLY CYS PRO GLU PRO LEU GLU ILE ALA ASP
SEQRES 23 B 310 ALA GLY HIS PHE VAL GLN GLU PHE GLY GLU GLN VAL ALA
SEQRES 24 B 310 ARG GLU ALA LEU LYS HIS PHE ALA GLU THR GLU
HELIX 1 1 ASP A 9 PHE A 12 5 4
HELIX 2 2 SER A 60 SER A 73 5 14
HELIX 3 3 GLU A 94 ASP A 96 5 3
HELIX 4 4 PHE A 99 ARG A 112 1 14
HELIX 5 5 ASP A 124 THR A 132 1 9
HELIX 6 6 PRO A 134 ALA A 136 5 3
HELIX 7 7 PRO A 138 ARG A 140 5 3
HELIX 8 8 PRO A 159 THR A 166 5 8
HELIX 9 9 TRP A 172 VAL A 180 1 9
HELIX 10 10 LEU A 187 TRP A 194 1 8
HELIX 11 11 GLU A 200 ALA A 207 1 8
HELIX 12 12 THR A 213 TYR A 215 5 3
HELIX 13 13 ALA A 217 ALA A 227 1 11
HELIX 14 14 GLN A 231 ASN A 246 1 16
HELIX 15 15 PRO A 265 LEU A 274 1 10
HELIX 16 16 VAL A 291 ALA A 307 5 17
HELIX 17 17 ASP B 9 PHE B 12 5 4
HELIX 18 18 SER B 60 SER B 73 5 14
HELIX 19 19 GLU B 94 ASP B 96 5 3
HELIX 20 20 PHE B 99 LEU B 113 1 15
HELIX 21 21 ASP B 124 THR B 132 1 9
HELIX 22 22 PRO B 134 ALA B 136 5 3
HELIX 23 23 PRO B 138 ARG B 140 5 3
HELIX 24 24 PRO B 159 THR B 166 5 8
HELIX 25 25 TRP B 172 VAL B 180 1 9
HELIX 26 26 LEU B 187 TRP B 194 1 8
HELIX 27 27 GLU B 200 ALA B 207 1 8
HELIX 28 28 THR B 213 TYR B 215 5 3
HELIX 29 29 ALA B 217 ALA B 227 1 11
HELIX 30 30 GLN B 231 ASN B 246 1 16
HELIX 31 31 PRO B 265 LEU B 274 1 10
HELIX 32 32 VAL B 291 ALA B 307 5 17
SHEET 1 A 8 ASN A 23 LEU A 25 0
SHEET 2 A 8 ALA A 36 GLY A 42 -1 N TYR A 38 O ASN A 23
SHEET 3 A 8 ARG A 76 PRO A 80 -1 N ALA A 79 O LEU A 39
SHEET 4 A 8 VAL A 49 CYS A 52 1 N PHE A 50 O ARG A 76
SHEET 5 A 8 ILE A 118 VAL A 122 1 N THR A 119 O VAL A 49
SHEET 6 A 8 PHE A 141 MET A 147 1 N LYS A 142 O ILE A 118
SHEET 7 A 8 GLN A 251 GLY A 257 1 N GLN A 251 O LEU A 144
SHEET 8 A 8 LEU A 282 ILE A 284 1 N LEU A 282 O ILE A 256
SHEET 1 B 8 ASN B 23 LEU B 25 0
SHEET 2 B 8 ALA B 36 GLY B 42 -1 N TYR B 38 O ASN B 23
SHEET 3 B 8 ARG B 76 PRO B 80 -1 N ALA B 79 O LEU B 39
SHEET 4 B 8 VAL B 49 CYS B 52 1 N PHE B 50 O ARG B 76
SHEET 5 B 8 ILE B 118 VAL B 122 1 N THR B 119 O VAL B 49
SHEET 6 B 8 PHE B 141 MET B 147 1 N LYS B 142 O ILE B 118
SHEET 7 B 8 GLN B 251 GLY B 257 1 N GLN B 251 O LEU B 144
SHEET 8 B 8 LEU B 282 ILE B 284 1 N LEU B 282 O ILE B 256
CISPEP 1 GLU A 56 PRO A 57 0 -5.00
CISPEP 2 GLN A 167 PRO A 168 0 1.29
CISPEP 3 GLU B 56 PRO B 57 0 -4.34
CISPEP 4 GLN B 167 PRO B 168 0 -1.35
CRYST1 95.680 73.530 41.600 90.00 91.32 90.00 P 1 21 1 4
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 0.010452 0.000000 0.000241 0.00000
SCALE2 0.000000 0.013600 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024045 0.00000
MTRIX1 1 0.997561 -0.056672 0.040741 -48.53100 1
MTRIX2 1 -0.056932 -0.998364 0.005252 12.07800 1
MTRIX3 1 0.040376 -0.007558 -0.999156 39.56100 1 |