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AUTHOR I.S.RIDDER,H.J.ROZEBOOM,K.H.KALK,B.W.DIJKSTRA
REVDAT 1 29-SEP-99 1CIJ 0
JRNL AUTH M.G.PIKKEMAAT,I.S.RIDDER,H.J.ROZEBOOM,K.H.KALK,
JRNL AUTH 2 B.W.DIJKSTRA,D.B.JANSSEN
JRNL TITL CRYSTALLOGRAPHIC AND KINETIC EVIDENCE OF A
JRNL TITL 2 COLLISION COMPLEX FORMED DURING HALIDE IMPORT IN
JRNL TITL 3 HALOALKANE DEHALOGENASE
JRNL REF BIOCHEMISTRY V. 38 12052 1999
JRNL REFN ASTM BICHAW US ISSN 0006-2960 0033
REMARK 1
REMARK 1 REFERENCE 1
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 2
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
REMARK 1 TITL 2 DEHALOGENASE AT PH 6.2 AND PH 8.2 AND IMPLICATIONS
REMARK 1 TITL 3 FOR THE 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 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. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0001
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 11923
REMARK 3
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT, EXCEPT
REMARK 3 LAST STEP IN WHICH
REMARK 3 ALL DATA (WORK+TEST
REMARK 3 SET) WERE USED
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM EXTENSION OF
REMARK 3 SET USED FOR 1BE0
REMARK 3 MODEL
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1000
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.40
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1299
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE : 0.3630
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 125
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 : 2478
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.20
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) : 0.300
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) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.60
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.20
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.83 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.18 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.10 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.55 ; 2.500
REMARK 3
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.WAT
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.SOL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE VALUES LISTED AS WORKING IN
REMARK 3 REMARK 3 APPLY TO THE LAST CYCLE OF THE REFINEMENT IN
REMARK 3 WHICH ALL DATA (WORK + FREE) WERE USED.
REMARK 4
REMARK 4 1CIJ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-1999.
REMARK 100 THE RCSB ID CODE IS RCSB000776.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-DEC-1997
REMARK 200 TEMPERATURE (KELVIN) : 120.0
REMARK 200 PH : 5.80
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : FR 591
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : DOUBLE MIRRORS (MAC-XOS)
REMARK 200
REMARK 200 DETECTOR TYPE : DIP-2030H
REMARK 200 DETECTOR MANUFACTURER : MACSCIENCE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12688
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10800
REMARK 200 FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.36300
REMARK 200 FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1BE0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 % AMMONIUM SULFATE 100 MM
REMARK 280 MES BUFFER, PH 5.9
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 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 46.70350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.98200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.70350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.98200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 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 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 VAL A 2 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 SER A 13 N - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASN A 14 N - CA - C ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASN A 23 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 LEU A 28 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 LEU A 28 C - N - CA ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASP A 40 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 PRO A 57 N - CA - C ANGL. DEV. = -7.4 DEGREES
REMARK 500 PRO A 57 C - N - CA ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG A 64 N - CA - C ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG A 76 N - CA - C ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP A 81 N - CA - C ANGL. DEV. = -6.5 DEGREES
REMARK 500 LYS A 90 N - CA - C ANGL. DEV. = 5.7 DEGREES
REMARK 500 THR A 119 N - CA - C ANGL. DEV. = -7.4 DEGREES
REMARK 500 VAL A 122 N - CA - C ANGL. DEV. = 7.0 DEGREES
REMARK 500 GLY A 126 N - CA - C ANGL. DEV. = -5.8 DEGREES
REMARK 500 LEU A 133 N - CA - C ANGL. DEV. = 6.0 DEGREES
REMARK 500 PRO A 134 N - CA - C ANGL. DEV. = 5.7 DEGREES
REMARK 500 PRO A 138 N - CA - C ANGL. DEV. = 6.8 DEGREES
REMARK 500 ILE A 145 N - CA - C ANGL. DEV. = -6.6 DEGREES
REMARK 500 MET A 147 N - CA - C ANGL. DEV. = -7.1 DEGREES
REMARK 500 ASN A 148 N - CA - C ANGL. DEV. = 6.4 DEGREES
REMARK 500 LEU A 151 CA - CB - CG ANGL. DEV. = -6.4 DEGREES
REMARK 500 VAL A 180 N - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 THR A 181 N - CA - C ANGL. DEV. = 7.1 DEGREES
REMARK 500 LEU A 187 CA - CB - CG ANGL. DEV. = -6.9 DEGREES
REMARK 500 ALA A 195 N - CA - C ANGL. DEV. = -6.2 DEGREES
REMARK 500 THR A 199 N - CA - C ANGL. DEV. = -7.1 DEGREES
REMARK 500 ALA A 208 N - CA - C ANGL. DEV. = 6.6 DEGREES
REMARK 500 THR A 213 N - CA - C ANGL. DEV. = 6.4 DEGREES
REMARK 500 GLN A 216 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 ASN A 246 N - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASP A 247 N - CA - C ANGL. DEV. = 6.0 DEGREES
REMARK 500 GLY A 257 N - CA - C ANGL. DEV. = -7.3 DEGREES
REMARK 500 MET A 258 CG - SD - CE ANGL. DEV. = 8.9 DEGREES
REMARK 500 LEU A 262 CA - CB - CG ANGL. DEV. = 6.6 DEGREES
REMARK 500 MET A 268 N - CA - C ANGL. DEV. = 6.8 DEGREES
REMARK 500 LEU A 282 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 ALA A 285 N - CA - C ANGL. DEV. = 6.0 DEGREES
REMARK 500 PHE A 294 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 GLY A 295 N - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: BR1
REMARK 800 SITE_DESCRIPTION:
REMARK 800 PRIMARY BROMIDE BINDING SITE IN ACTIVE SITE CAVITY
REMARK 800
REMARK 800 SITE_IDENTIFIER: BR2
REMARK 800 SITE_DESCRIPTION:
REMARK 800 LOCATION OF COLLISION COMPLEX IN HALIDE IMPORT
REMARK 800
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 DISCREPANCY AT 2 IS DUE TO EXPRESSION SYSTEM
DBREF 1CIJ A 1 310 SWS P22643 HALO_XANAU 1 310
SEQADV 1CIJ VAL A 2 SWS P22643 ILE 2 CLONING ARTIFACT
SEQRES 1 A 310 MET VAL 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 PHE 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
HET BR A 401 1
HET BR A 402 1
HET BR A 403 1
HETNAM BR BROMIDE ION
FORMUL 2 BR 3(BR1 1-)
FORMUL 5 HOH *160(H2 O1)
HELIX 1 1 ASP A 9 PHE A 12 5 4
HELIX 2 2 SER A 60 TYR A 63 5 4
HELIX 3 3 ILE A 67 GLU A 72 1 6
HELIX 4 4 GLU A 94 ASP A 96 5 3
HELIX 5 5 PHE A 99 ARG A 112 1 14
HELIX 6 6 ASP A 124 THR A 132 5 9
HELIX 7 7 PRO A 134 ALA A 136 5 3
HELIX 8 8 PRO A 138 ARG A 140 5 3
HELIX 9 9 PRO A 159 PHE A 161 5 3
HELIX 10 10 ALA A 163 THR A 166 1 4
HELIX 11 11 PHE A 172 VAL A 180 1 9
HELIX 12 12 LEU A 187 TRP A 194 1 8
HELIX 13 13 GLU A 200 ALA A 207 1 8
HELIX 14 14 THR A 213 TYR A 215 5 3
HELIX 15 15 ALA A 217 ALA A 227 1 11
HELIX 16 16 GLN A 231 ASN A 246 1 16
HELIX 17 17 PRO A 265 LEU A 274 1 10
HELIX 18 18 VAL A 291 ALA A 307 5 17
SHEET 1 A 8 ASN A 23 ASP A 26 0
SHEET 2 A 8 ARG A 35 GLU A 41 -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
CISPEP 1 GLU A 56 PRO A 57 0 -0.76
CISPEP 2 GLN A 167 PRO A 168 0 -0.16
SITE 1 BR1 2 TRP A 125 TRP A 175
SITE 1 BR2 2 THR A 197 PHE A 294
CRYST1 93.407 71.964 40.968 90.00 90.00 90.00 P 21 21 2 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 0.010706 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013896 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024409 0.00000 |