| content |
HEADER HYDROLASE 14-MAY-12 4F5Z
TITLE CRYSTAL STRUCTURE OF RHODOCOCCUS RHODOCHROUS HALOALKANE DEHALOGENASE
TITLE 2 MUTANT (L95V, A172V).
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: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS MUTATION IN ACCESS TUNNEL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.KULIK,I.KUTA-SMATANOVA,P.REZACOVA
REVDAT 1 23-JAN-13 4F5Z 0
JRNL AUTH T.KOUDELAKOVA,R.CHALOUPKOVA,J.BREZOVSKY,Z.PROKOP,
JRNL AUTH 2 E.SEBESTOVA,M.HESSELER,M.KHABIRI,M.PLEVAKA,D.KULIK,
JRNL AUTH 3 I.KUTA SMATANOVA,P.REZACOVA,R.ETTRICH,U.T.BORNSCHEUER,
JRNL AUTH 4 J.DAMBORSKY
JRNL TITL ENGINEERING ENZYME STABILITY AND RESISTANCE TO AN ORGANIC
JRNL TITL 2 COSOLVENT BY MODIFICATION OF RESIDUES IN THE ACCESS TUNNEL.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. 2013
JRNL REFN ESSN 1521-3773
JRNL PMID 23303607
JRNL DOI 10.1002/ANIE.201206708
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0037
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 17.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.6
REMARK 3 NUMBER OF REFLECTIONS : 74518
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.122
REMARK 3 R VALUE (WORKING SET) : 0.120
REMARK 3 FREE R VALUE : 0.155
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3937
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4150
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 69.16
REMARK 3 BIN R VALUE (WORKING SET) : 0.1550
REMARK 3 BIN FREE R VALUE SET COUNT : 209
REMARK 3 BIN FREE R VALUE : 0.1760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2350
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 745
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 7.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.19000
REMARK 3 B22 (A**2) : 0.23000
REMARK 3 B33 (A**2) : -0.14000
REMARK 3 B12 (A**2) : 0.09000
REMARK 3 B13 (A**2) : 0.17000
REMARK 3 B23 (A**2) : 0.19000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.040
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.040
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.022
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.065
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.980
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.970
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2586 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3578 ; 1.531 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 330 ; 5.773 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 126 ;32.803 ;23.651
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 394 ;12.094 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;18.440 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 382 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2081 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1388 ; 0.211 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1767 ; 0.323 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 567 ; 0.160 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 40 ; 0.171 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 102 ; 0.163 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1574 ; 1.296 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2555 ; 1.819 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1145 ; 2.570 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1004 ; 3.365 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2719 ; 1.777 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 746 ; 5.659 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2478 ; 4.208 ; 3.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4F5Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-12.
REMARK 100 THE RCSB ID CODE IS RCSB072497.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JAN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978
REMARK 200 MONOCHROMATOR : SI 111 DOUBLE CRYSTAL
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-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78455
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.03500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.8500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.19100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
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 (%): 40.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35 % (W/V) PEG4000, PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 279K
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 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 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASP A 82 O HOH A 955 1.94
REMARK 500 ND1 HIS A 294 O HOH A 1144 1.95
REMARK 500 O HOH A 800 O HOH A 1142 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 666 O HOH A 1142 1455 2.04
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 49.07 -106.34
REMARK 500 THR A 43 -160.54 -103.39
REMARK 500 GLU A 98 -89.69 -113.26
REMARK 500 ASP A 106 -130.16 54.29
REMARK 500 ARG A 153 48.51 -88.98
REMARK 500 ASP A 156 -73.93 -102.51
REMARK 500 VAL A 245 -77.33 -132.88
REMARK 500 LEU A 271 -98.78 -117.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 721 DISTANCE = 5.16 ANGSTROMS
REMARK 525 HOH A 896 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH A1030 DISTANCE = 7.46 ANGSTROMS
REMARK 525 HOH A1035 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH A1043 DISTANCE = 5.32 ANGSTROMS
REMARK 525 HOH A1067 DISTANCE = 8.15 ANGSTROMS
REMARK 525 HOH A1072 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A1127 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH A1129 DISTANCE = 6.24 ANGSTROMS
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ A 302
DBREF 4F5Z A 1 293 UNP P0A3G2 DHAA_RHORH 1 293
SEQADV 4F5Z VAL A 95 UNP P0A3G2 LEU 95 ENGINEERED MUTATION
SEQADV 4F5Z VAL A 172 UNP P0A3G2 ALA 172 ENGINEERED MUTATION
SEQADV 4F5Z HIS A 294 UNP P0A3G2 EXPRESSION TAG
SEQADV 4F5Z HIS A 295 UNP P0A3G2 EXPRESSION TAG
SEQADV 4F5Z HIS A 296 UNP P0A3G2 EXPRESSION TAG
SEQADV 4F5Z HIS A 297 UNP P0A3G2 EXPRESSION TAG
SEQADV 4F5Z HIS A 298 UNP P0A3G2 EXPRESSION TAG
SEQADV 4F5Z HIS A 299 UNP P0A3G2 EXPRESSION TAG
SEQRES 1 A 299 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 A 299 TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP
SEQRES 3 A 299 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 A 299 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 A 299 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 A 299 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 A 299 TYR PHE PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 A 299 ILE GLU ALA VAL GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 A 299 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 A 299 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA CYS MET GLU
SEQRES 11 A 299 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 A 299 PHE ALA ARG GLU THR PHE GLN ALA PHE ARG THR ALA ASP
SEQRES 13 A 299 VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE
SEQRES 14 A 299 GLU GLY VAL LEU PRO LYS CYS VAL VAL ARG PRO LEU THR
SEQRES 15 A 299 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 A 299 PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 A 299 LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU
SEQRES 18 A 299 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 A 299 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 A 299 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 A 299 ASN CYS LYS THR VAL ASP ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 A 299 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 A 299 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS
HET CL A 301 1
HET BEZ A 302 9
HETNAM CL CHLORIDE ION
HETNAM BEZ BENZOIC ACID
FORMUL 2 CL CL 1-
FORMUL 3 BEZ C7 H6 O2
FORMUL 4 HOH *745(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 VAL 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 CYS 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 TYR 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 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 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 -2.97
CISPEP 2 GLU A 214 PRO A 215 0 -4.93
CISPEP 3 THR A 242 PRO A 243 0 2.84
SITE 1 AC1 6 ASN A 41 TRP A 107 PRO A 206 BEZ A 302
SITE 2 AC1 6 HOH A1140 HOH A1145
SITE 1 AC2 10 ASN A 41 ASP A 106 TRP A 107 PHE A 168
SITE 2 AC2 10 LEU A 209 HIS A 272 TYR A 273 CL A 301
SITE 3 AC2 10 HOH A1140 HOH A1145
CRYST1 42.663 44.489 46.389 115.28 98.61 109.55 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 0.023440 0.008324 0.009097 0.00000
SCALE2 0.000000 0.023853 0.014221 0.00000
SCALE3 0.000000 0.000000 0.025384 0.00000
TER 2470 HIS A 295
MASTER 318 0 2 19 8 0 5 6 3105 1 9 23
END |