| content |
HEADER HYDROLASE 30-JUN-12 4FWB
TITLE STRUCTURE OF RHODOCOCCUS RHODOCHROUS HALOALKANE DEHALOGENASE MUTANT
TITLE 2 DHAA31 IN COMPLEX WITH 1, 2, 3 - TRICHLOROPROPANE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS RHODOCHROUS;
SOURCE 3 ORGANISM_TAXID: 1829;
SOURCE 4 STRAIN: NCIB 13064;
SOURCE 5 GENE: DHAA, DHAA31;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PAQN
KEYWDS CATALYTIC PENTAD, STRUCTURAL GENOMICS, ENZYME FUNCTION INITIATIVE,
KEYWDS 2 ALPHA/BETA HYDROLASE FOLD, HYDROLASE, HALIDE BINDING, HYDROLYTIC
KEYWDS 3 DEHALOGENATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.LAHODA,A.STSIAPANAVA,J.MESTERS,I.KUTA SMATANOVA
REVDAT 1 05-SEP-12 4FWB 0
SPRSDE 05-SEP-12 4FWB 3RLT
JRNL AUTH M.LAHODA,A.STSIAPANAVA,J.MESTERS,R.CHALOUPKOVA,J.DAMBORSKY,
JRNL AUTH 2 I.KUTA SMATANOVA
JRNL TITL CRYSTALLOGRAPHIC ANALYSIS OF 1,2,3 TRICHLOROPROPANE
JRNL TITL 2 BIODEGRADATION BY HALOALKANE DEHALOGENASE DHAA31
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.136
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.136
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.166
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3454
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 69189
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2361
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 353
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 26
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 ANGLE DISTANCES (A) : 0.029
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.027
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.102
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: conjugate gradient least squares
REMARK 3 refinement in SHELXL 97 with anisotropic adps for all atoms
REMARK 3 except for water molecules above a certain adp cut off
REMARK 4
REMARK 4 4FWB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-12.
REMARK 100 THE RCSB ID CODE IS RCSB073436.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X12
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.260
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.03300
REMARK 200 R SYM (I) : 0.03300
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.26
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.06100
REMARK 200 R SYM FOR SHELL (I) : 0.06100
REMARK 200 FOR SHELL : 17.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3FBW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES SODIUM SALT, 29% (W/V) PEG
REMARK 280 4000; 1,2,3-TRICHLOROPROPANE WAS ADDED AT ROOM TEMPERATURE, PH
REMARK 280 6.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,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
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 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 21 NE - CZ - NH2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 30 NE - CZ - NH1 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ARG A 86 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ASP A 106 CA - CB - CG ANGL. DEV. = 17.1 DEGREES
REMARK 500 ASP A 106 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG A 133 CA - CB - CG ANGL. DEV. = 14.1 DEGREES
REMARK 500 ARG A 133 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 GLU A 140 CA - CB - CG ANGL. DEV. = 16.1 DEGREES
REMARK 500 GLU A 140 CB - CG - CD ANGL. DEV. = 29.1 DEGREES
REMARK 500 ARG A 153 O - C - N ANGL. DEV. = -14.0 DEGREES
REMARK 500 ARG A 179 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 190 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 GLU A 214 OE1 - CD - OE2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 LEU A 221 CA - CB - CG ANGL. DEV. = 18.4 DEGREES
REMARK 500 TYR A 225 CA - CB - CG ANGL. DEV. = 12.2 DEGREES
REMARK 500 TYR A 225 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 THR A 264 CA - CB - CG2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 ARG A 288 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 288 NE - CZ - NH2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 TRP A 289 CA - CB - CG ANGL. DEV. = 11.6 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 ASP A 31 52.01 -106.74
REMARK 500 PRO A 42 46.97 -102.80
REMARK 500 THR A 43 -162.23 -103.67
REMARK 500 GLU A 98 -91.57 -112.43
REMARK 500 ASP A 106 -131.75 53.29
REMARK 500 ASP A 156 -61.01 79.02
REMARK 500 PHE A 245 -82.45 -146.46
REMARK 500 LEU A 271 -97.24 -116.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ARG A 153 12.78
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 3KP A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2005
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3RK4 RELATED DB: PDB
REMARK 900 HALOALKANE DEHALOGENASE MUTANT DHAA31
REMARK 900 RELATED ID: 3FBW RELATED DB: PDB
REMARK 900 HALOALKANE DEHALOGENASE DHAA MUTANT C176Y
REMARK 900 RELATED ID: 3G9X RELATED DB: PDB
REMARK 900 HALOALKANE DEHALOGENASE DHAA MUTANT I135F
REMARK 900 RELATED ID: 3FWH RELATED DB: PDB
REMARK 900 HALOALKANE DEHALOGENASE DHAA MUTANT C176Y, I135F
REMARK 900 RELATED ID: 1BN6 RELATED DB: PDB
REMARK 900 HALOALKANE DEHALOGENASE DHAA
REMARK 900 RELATED ID: 1CQW RELATED DB: PDB
REMARK 900 HALOALKANE DEHALOGENASE DHAA WITH IODIDE ION
DBREF 4FWB A 4 293 UNP P0A3G2 DHAA_RHORH 4 293
SEQADV 4FWB PHE A 135 UNP P0A3G2 ILE 135 ENGINEERED MUTATION
SEQADV 4FWB TYR A 176 UNP P0A3G2 CYS 176 ENGINEERED MUTATION
SEQADV 4FWB PHE A 245 UNP P0A3G2 VAL 245 ENGINEERED MUTATION
SEQADV 4FWB ILE A 246 UNP P0A3G2 LEU 246 ENGINEERED MUTATION
SEQADV 4FWB PHE A 273 UNP P0A3G2 TYR 273 ENGINEERED MUTATION
SEQADV 4FWB HIS A 294 UNP P0A3G2 EXPRESSION TAG
SEQADV 4FWB HIS A 295 UNP P0A3G2 EXPRESSION TAG
SEQRES 1 A 292 ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL GLU
SEQRES 2 A 292 VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY PRO
SEQRES 3 A 292 ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 A 292 THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO HIS VAL
SEQRES 5 A 292 ALA PRO SER HIS ARG CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 A 292 MET GLY LYS SER ASP LYS PRO ASP LEU ASP TYR PHE PHE
SEQRES 7 A 292 ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU ALA
SEQRES 8 A 292 LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP TRP
SEQRES 9 A 292 GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN PRO
SEQRES 10 A 292 GLU ARG VAL LYS GLY ILE ALA CYS MET GLU PHE ILE ARG
SEQRES 11 A 292 PRO PHE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA ARG
SEQRES 12 A 292 GLU THR PHE GLN ALA PHE ARG THR ALA ASP VAL GLY ARG
SEQRES 13 A 292 GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE GLU GLY ALA
SEQRES 14 A 292 LEU PRO LYS TYR VAL VAL ARG PRO LEU THR GLU VAL GLU
SEQRES 15 A 292 MET ASP HIS TYR ARG GLU PRO PHE LEU LYS PRO VAL ASP
SEQRES 16 A 292 ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO ILE
SEQRES 17 A 292 ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU ALA
SEQRES 18 A 292 TYR MET ASN TRP LEU HIS GLN SER PRO VAL PRO LYS LEU
SEQRES 19 A 292 LEU PHE TRP GLY THR PRO GLY PHE ILE ILE PRO PRO ALA
SEQRES 20 A 292 GLU ALA ALA ARG LEU ALA GLU SER LEU PRO ASN CYS LYS
SEQRES 21 A 292 THR VAL ASP ILE GLY PRO GLY LEU HIS PHE LEU GLN GLU
SEQRES 22 A 292 ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG TRP
SEQRES 23 A 292 LEU PRO ALA LEU HIS HIS
HET 3KP A2001 6
HET CL A2002 1
HET CL A2003 1
HET CL A2004 1
HET CL A2005 1
HETNAM 3KP 1,2,3-TRICHLOROPROPANE
HETNAM CL CHLORIDE ION
FORMUL 2 3KP C3 H5 CL3
FORMUL 3 CL 4(CL 1-)
FORMUL 7 HOH *353(H2 O)
HELIX 1 1 SER A 44 ARG A 49 5 6
HELIX 2 2 ILE A 51 ALA A 56 1 6
HELIX 3 3 PHE A 80 LEU A 95 1 16
HELIX 4 4 ASP A 106 ASN A 119 1 14
HELIX 5 5 THR A 137 TRP A 141 5 5
HELIX 6 6 PRO A 142 PHE A 144 5 3
HELIX 7 7 ALA A 145 ARG A 153 1 9
HELIX 8 8 ASP A 156 ILE A 163 1 8
HELIX 9 9 ASN A 166 GLY A 171 1 6
HELIX 10 10 GLY A 171 TYR A 176 1 6
HELIX 11 11 THR A 182 GLU A 191 1 10
HELIX 12 12 PRO A 192 LEU A 194 5 3
HELIX 13 13 LYS A 195 ASP A 198 5 4
HELIX 14 14 ARG A 199 LEU A 209 1 11
HELIX 15 15 PRO A 215 SER A 232 1 18
HELIX 16 16 PRO A 248 LEU A 259 1 12
HELIX 17 17 PHE A 273 ASN A 278 1 6
HELIX 18 18 ASN A 278 LEU A 290 1 13
HELIX 19 19 PRO A 291 HIS A 294 5 4
SHEET 1 A 8 TYR A 14 VAL A 17 0
SHEET 2 A 8 GLU A 20 VAL A 27 -1 O GLU A 20 N VAL A 17
SHEET 3 A 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 A 8 VAL A 35 LEU A 38 1 N PHE A 37 O ILE A 62
SHEET 5 A 8 VAL A 100 HIS A 105 1 O VAL A 101 N LEU A 36
SHEET 6 A 8 VAL A 123 MET A 129 1 O ALA A 127 N LEU A 102
SHEET 7 A 8 LYS A 236 PRO A 243 1 O LEU A 237 N CYS A 128
SHEET 8 A 8 CYS A 262 GLY A 270 1 O ILE A 267 N TRP A 240
CISPEP 1 ASN A 41 PRO A 42 0 -6.57
CISPEP 2 GLU A 214 PRO A 215 0 -6.23
CISPEP 3 THR A 242 PRO A 243 0 2.35
SITE 1 AC1 10 ASP A 106 ILE A 132 TRP A 141 PHE A 168
SITE 2 AC1 10 ILE A 246 HIS A 272 CL A2002 CL A2003
SITE 3 AC1 10 CL A2004 CL A2005
SITE 1 AC2 5 ASN A 41 TRP A 107 PHE A 205 PRO A 206
SITE 2 AC2 5 3KP A2001
SITE 1 AC3 6 ASP A 106 PHE A 245 ILE A 246 HIS A 272
SITE 2 AC3 6 3KP A2001 CL A2004
SITE 1 AC4 5 PHE A 149 PHE A 245 3KP A2001 CL A2003
SITE 2 AC4 5 CL A2005
SITE 1 AC5 4 PHE A 168 TYR A 176 3KP A2001 CL A2004
CRYST1 42.498 44.395 46.538 115.32 97.70 109.58 P 1 1
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 0.023531 0.008370 0.008601 0.00000
SCALE2 0.000000 0.023908 0.014031 0.00000
SCALE3 0.000000 0.000000 0.025142 0.00000
TER 2462 HIS A 295
MASTER 280 0 5 19 8 0 10 6 2724 1 6 23
END |