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HEADER HYDROLASE 22-JUN-11 3SK0
TITLE STRUCTURE OF RHODOCOCCUS RHODOCHROUS HALOALKANE DEHALOGENASE DHAA
TITLE 2 MUTANT DHAA12
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 GENE: DHAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PAQN
KEYWDS CATALYTIC PENTAD, ALPHA/BETA-HYDROLASE FOLD, HYDROLASE, HALIDE
KEYWDS 2 BINDING, HYDROLYTIC DEHALOGENATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.LAHODA,A.STSIAPANAVA,J.MESTERS,T.KOUDELAKOVA,J.DAMBORSKY,I.KUTA-
AUTHOR 2 SMATANOVA
REVDAT 1 27-JUN-12 3SK0 0
JRNL AUTH J.SYKORA,J.BREZOVSKY,T.KOUDELAKOVA,M.LAHODA,R.CHALOUPKOVA,
JRNL AUTH 2 T.CHERNAVETS,A.FORTOVA,Z.PROKOP,I.KUTA-SMATANOVA,M.HOF,
JRNL AUTH 3 J.DAMBORSKY
JRNL TITL DYNAMICS AND HYDRATION: TWO PARAMETERS TO BE CHALLENGED BY
JRNL TITL 2 RATIONAL DESIGN OF ENZYME CATALYSTS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M LAHODA,T.KOUDELAKOVA,A.STSIAPANAVA,J.MESTERS,J.DAMBORSKY,
REMARK 1 AUTH 2 I.KUTA-SMATANOVA
REMARK 1 TITL CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE MUTANT DHAA12
REMARK 1 TITL 2 FROM GRAM-POSITIVE BACTERIUM RHODOCOCCUS RHODOCHROUS
REMARK 1 TITL 3 NCIMB13064
REMARK 2
REMARK 2 RESOLUTION. 1.78 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) : 1.78
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) : 0.176
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.176
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1734
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.161
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)) : 27459
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2480
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 270
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2751.00
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 2288.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 15
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 11235
REMARK 3 NUMBER OF RESTRAINTS : 10651
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 ANGLE DISTANCES (A) : 0.024
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.023
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.037
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.043
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.010
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.061
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
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
REMARK 4
REMARK 4 3SK0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-11.
REMARK 100 THE RCSB ID CODE IS RCSB066296.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34658
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : 0.08400
REMARK 200 FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.37000
REMARK 200 R SYM FOR SHELL (I) : 0.37000
REMARK 200 FOR SHELL : 4.200
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 (%): 41.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES SODIUM SALT, 20% PEG 4000,
REMARK 280 PH 6.1, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 25.79150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.18500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.34450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.18500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.79150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.34450
REMARK 290 SMTRY3 4 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 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 SER A 2
REMARK 465 GLU A 3
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 30 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 86 CD - NE - CZ ANGL. DEV. = 13.6 DEGREES
REMARK 500 TYR A 236 CA - CB - CG ANGL. DEV. = 13.0 DEGREES
REMARK 500 TYR A 236 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 265 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 265 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 TYR A 284 CB - CG - CD1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 TRP A 300 CA - CB - CG ANGL. DEV. = 11.7 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 PRO A 42 50.06 -108.29
REMARK 500 GLU A 98 -90.21 -101.25
REMARK 500 ASP A 106 -129.32 54.40
REMARK 500 GLU A 130 59.74 39.81
REMARK 500 ASP A 167 -52.18 66.24
REMARK 500 ARG A 182 -56.22 -124.19
REMARK 500 ALA A 256 -79.83 -142.93
REMARK 500 LEU A 282 -115.37 -118.65
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 CL A 2002
REMARK 900
REMARK 900 RELATED ENTRIES
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 3SK0 A 1 304 UNP P0A3G2 DHAA_RHORH 1 293
SEQADV 3SK0 PHE A 141 UNP P0A3G2 TRP 141 ENGINEERED MUTATION
SEQADV 3SK0 HIS A 142 UNP P0A3G2 INSERTION
SEQADV 3SK0 HIS A 143 UNP P0A3G2 INSERTION
SEQADV 3SK0 THR A 144 UNP P0A3G2 INSERTION
SEQADV 3SK0 GLU A 145 UNP P0A3G2 INSERTION
SEQADV 3SK0 VAL A 146 UNP P0A3G2 INSERTION
SEQADV 3SK0 ALA A 147 UNP P0A3G2 INSERTION
SEQADV 3SK0 GLU A 148 UNP P0A3G2 INSERTION
SEQADV 3SK0 GLU A 149 UNP P0A3G2 INSERTION
SEQADV 3SK0 GLN A 150 UNP P0A3G2 INSERTION
SEQADV 3SK0 ASP A 151 UNP P0A3G2 INSERTION
SEQADV 3SK0 HIS A 152 UNP P0A3G2 INSERTION
SEQADV 3SK0 ALA A 153 UNP P0A3G2 PRO 142 ENGINEERED MUTATION
SEQADV 3SK0 ALA A 155 UNP P0A3G2 PHE 144 ENGINEERED MUTATION
SEQADV 3SK0 ARG A 182 UNP P0A3G2 GLY 171 ENGINEERED MUTATION
SEQADV 3SK0 VAL A 183 UNP P0A3G2 ALA 172 ENGINEERED MUTATION
SEQADV 3SK0 GLY A 186 UNP P0A3G2 LYS 175 ENGINEERED MUTATION
SEQADV 3SK0 GLY A 187 UNP P0A3G2 CYS 176 ENGINEERED MUTATION
SEQADV 3SK0 ALA A 256 UNP P0A3G2 VAL 245 ENGINEERED MUTATION
SEQADV 3SK0 GLU A 305 UNP P0A3G2 EXPRESSION TAG
SEQADV 3SK0 HIS A 306 UNP P0A3G2 EXPRESSION TAG
SEQADV 3SK0 HIS A 307 UNP P0A3G2 EXPRESSION TAG
SEQADV 3SK0 HIS A 308 UNP P0A3G2 EXPRESSION TAG
SEQADV 3SK0 HIS A 309 UNP P0A3G2 EXPRESSION TAG
SEQADV 3SK0 HIS A 310 UNP P0A3G2 EXPRESSION TAG
SEQADV 3SK0 HIS A 311 UNP P0A3G2 EXPRESSION TAG
SEQRES 1 A 311 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 A 311 TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP
SEQRES 3 A 311 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 A 311 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 A 311 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 A 311 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 A 311 TYR PHE PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 A 311 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 A 311 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 A 311 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA CYS MET GLU
SEQRES 11 A 311 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU PHE HIS HIS
SEQRES 12 A 311 THR GLU VAL ALA GLU GLU GLN ASP HIS ALA GLU ALA ALA
SEQRES 13 A 311 ARG GLU THR PHE GLN ALA PHE ARG THR ALA ASP VAL GLY
SEQRES 14 A 311 ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE GLU ARG
SEQRES 15 A 311 VAL LEU PRO GLY GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 16 A 311 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS PRO VAL
SEQRES 17 A 311 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 18 A 311 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 19 A 311 ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 20 A 311 LEU LEU PHE TRP GLY THR PRO GLY ALA LEU ILE PRO PRO
SEQRES 21 A 311 ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO ASN CYS
SEQRES 22 A 311 LYS THR VAL ASP ILE GLY PRO GLY LEU HIS TYR LEU GLN
SEQRES 23 A 311 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 24 A 311 TRP LEU PRO ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET CL A2002 1
HETNAM CL CHLORIDE ION
FORMUL 2 CL CL 1-
FORMUL 3 HOH *270(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 PHE A 141 5 5
HELIX 6 6 VAL A 146 GLU A 148 5 3
HELIX 7 7 GLU A 149 ARG A 164 1 16
HELIX 8 8 ASP A 167 ILE A 174 1 8
HELIX 9 9 ASN A 177 ARG A 182 1 6
HELIX 10 10 ARG A 182 GLY A 187 1 6
HELIX 11 11 THR A 193 GLU A 202 1 10
HELIX 12 12 PRO A 203 LEU A 205 5 3
HELIX 13 13 LYS A 206 ASP A 209 5 4
HELIX 14 14 ARG A 210 LEU A 220 1 11
HELIX 15 15 PRO A 226 SER A 243 1 18
HELIX 16 16 PRO A 259 LEU A 270 1 12
HELIX 17 17 TYR A 284 ASP A 288 5 5
HELIX 18 18 ASN A 289 LEU A 301 1 13
HELIX 19 19 PRO A 302 HIS A 306 5 5
SHEET 1 A 8 HIS A 13 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 ARG A 60 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 A 8 PRO A 34 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 LYS A 124 N VAL A 100
SHEET 7 A 8 LYS A 247 PRO A 254 1 O LEU A 248 N CYS A 128
SHEET 8 A 8 CYS A 273 GLY A 281 1 O ILE A 278 N TRP A 251
CISPEP 1 ASN A 41 PRO A 42 0 -7.18
CISPEP 2 GLU A 225 PRO A 226 0 -3.61
CISPEP 3 THR A 253 PRO A 254 0 4.98
SITE 1 AC1 5 ASN A 41 TRP A 107 PHE A 179 PRO A 217
SITE 2 AC1 5 HOH A3107
CRYST1 51.583 68.689 84.370 90.00 90.00 90.00 P 21 21 21 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 0.019386 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014558 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011853 0.00000
TER 2538 HIS A 311
MASTER 257 0 1 19 8 0 2 6 2751 1 0 24
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