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HEADER HYDROLASE 15-APR-21 7O8B
TITLE STRUCTURE OF HALOALKANE DEHALOGENASE VARIANT DHAA80 FROM RHODOCOCCUS
TITLE 2 RHODOCHROUS
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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ALPHA/BETA HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SHAPOSHNIKOVA,T.PRUDNIKOVA,I.KUTA SMATANOVA
REVDAT 1 08-SEP-21 7O8B 0
JRNL AUTH A.SHAPOSHNIKOVA,M.KUTY,R.CHALOUPKOVA,J.DAMBORSKY,B.MINOFAR,
JRNL AUTH 2 T.PRUDNIKOVA
JRNL TITL STABILIZATION OF HALOALKANE DEHALOGENASE STRUCTURE BY
JRNL TITL 2 INTERFACIAL INTERACTION WITH IONIC LIQUIDS
JRNL REF CRYSTALS V. 11 2021
JRNL REFN ESSN 2073-4352
JRNL DOI 10.3390/CRYST11091052
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 29090
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) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1532
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2013
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.3690
REMARK 3 BIN FREE R VALUE SET COUNT : 106
REMARK 3 BIN FREE R VALUE : 0.3760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2343
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 133
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.37000
REMARK 3 B22 (A**2) : 2.36000
REMARK 3 B33 (A**2) : 1.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.134
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.117
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.107
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.281
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2450 ; 0.004 ; 0.017
REMARK 3 BOND LENGTHS OTHERS (A): 2264 ; 0.001 ; 0.019
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3356 ; 1.071 ; 1.852
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5230 ; 0.974 ; 2.628
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 293 ; 5.087 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 135 ;30.294 ;21.704
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 371 ;11.940 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;17.305 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 352 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2758 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 564 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1169 ; 0.698 ; 0.944
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1168 ; 0.693 ; 0.942
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1463 ; 1.168 ; 1.412
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1464 ; 1.168 ; 1.414
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1281 ; 0.937 ; 1.026
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1276 ; 0.813 ; 1.017
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1886 ; 1.303 ; 1.495
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2766 ; 4.977 ;11.718
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2755 ; 4.945 ;11.531
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 293
REMARK 3 ORIGIN FOR THE GROUP (A): -10.1560 13.0570 -17.4730
REMARK 3 T TENSOR
REMARK 3 T11: 0.3106 T22: 0.0115
REMARK 3 T33: 0.0635 T12: 0.0066
REMARK 3 T13: -0.0374 T23: -0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 1.8292 L22: 2.3554
REMARK 3 L33: 1.3163 L12: 0.2824
REMARK 3 L13: -0.0915 L23: 0.1094
REMARK 3 S TENSOR
REMARK 3 S11: 0.0154 S12: 0.0993 S13: -0.0288
REMARK 3 S21: -0.1625 S22: -0.0282 S23: 0.1799
REMARK 3 S31: 0.0014 S32: -0.0882 S33: 0.0129
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 7O8B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-APR-21.
REMARK 100 THE DEPOSITION ID IS D_1292115283.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JAN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
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 : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29090
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 32.150
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 1.8600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
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 FOR SHELL : NULL
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: 4F60
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BISTRIS PROPANE, 0.2M SODIUM
REMARK 280 FLUORIDE,20% PEG3350, 50% W/V 1-BUTYL-3-METHYLIMIDAZOLIUM METHYL
REMARK 280 SULFATE, PH 6.5, 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 25.44450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.95800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.77550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.95800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.44450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.77550
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 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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: 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 -47.25 -166.66
REMARK 500 PRO A 42 52.17 -104.05
REMARK 500 THR A 43 -161.49 -104.39
REMARK 500 GLU A 98 -85.58 -101.17
REMARK 500 ASP A 106 -123.52 54.45
REMARK 500 GLU A 130 58.56 39.08
REMARK 500 ASP A 156 -59.15 73.72
REMARK 500 VAL A 245 -72.85 -133.02
REMARK 500 LEU A 271 -98.24 -116.10
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 V5B A 301
DBREF 7O8B A 4 293 UNP P0A3G2 DHAA_RHORH 4 293
SEQADV 7O8B LEU A 148 UNP P0A3G2 THR 148 ENGINEERED MUTATION
SEQADV 7O8B GLN A 171 UNP P0A3G2 GLY 171 ENGINEERED MUTATION
SEQADV 7O8B VAL A 172 UNP P0A3G2 ALA 172 ENGINEERED MUTATION
SEQADV 7O8B PHE A 176 UNP P0A3G2 CYS 176 ENGINEERED MUTATION
SEQRES 1 A 290 ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL GLU
SEQRES 2 A 290 VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY PRO
SEQRES 3 A 290 ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 A 290 THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO HIS VAL
SEQRES 5 A 290 ALA PRO SER HIS ARG CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 A 290 MET GLY LYS SER ASP LYS PRO ASP LEU ASP TYR PHE PHE
SEQRES 7 A 290 ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU ALA
SEQRES 8 A 290 LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP TRP
SEQRES 9 A 290 GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN PRO
SEQRES 10 A 290 GLU ARG VAL LYS GLY ILE ALA CYS MET GLU PHE ILE ARG
SEQRES 11 A 290 PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA ARG
SEQRES 12 A 290 GLU LEU PHE GLN ALA PHE ARG THR ALA ASP VAL GLY ARG
SEQRES 13 A 290 GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE GLU GLN VAL
SEQRES 14 A 290 LEU PRO LYS PHE VAL VAL ARG PRO LEU THR GLU VAL GLU
SEQRES 15 A 290 MET ASP HIS TYR ARG GLU PRO PHE LEU LYS PRO VAL ASP
SEQRES 16 A 290 ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO ILE
SEQRES 17 A 290 ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU ALA
SEQRES 18 A 290 TYR MET ASN TRP LEU HIS GLN SER PRO VAL PRO LYS LEU
SEQRES 19 A 290 LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO ALA
SEQRES 20 A 290 GLU ALA ALA ARG LEU ALA GLU SER LEU PRO ASN CYS LYS
SEQRES 21 A 290 THR VAL ASP ILE GLY PRO GLY LEU HIS TYR LEU GLN GLU
SEQRES 22 A 290 ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG TRP
SEQRES 23 A 290 LEU PRO ALA LEU
HET V5B A 301 6
HETNAM V5B METHYL SULFATE
FORMUL 2 V5B C H4 O4 S
FORMUL 3 HOH *133(H2 O)
HELIX 1 AA1 SER A 44 ARG A 49 5 6
HELIX 2 AA2 ILE A 51 ALA A 56 1 6
HELIX 3 AA3 PHE A 80 LEU A 95 1 16
HELIX 4 AA4 ASP A 106 ASN A 119 1 14
HELIX 5 AA5 THR A 137 TRP A 141 5 5
HELIX 6 AA6 PRO A 142 PHE A 144 5 3
HELIX 7 AA7 ALA A 145 ARG A 153 1 9
HELIX 8 AA8 ASP A 156 ILE A 163 1 8
HELIX 9 AA9 ASN A 166 GLN A 171 1 6
HELIX 10 AB1 GLN A 171 PHE A 176 1 6
HELIX 11 AB2 THR A 182 GLU A 191 1 10
HELIX 12 AB3 PRO A 192 LEU A 194 5 3
HELIX 13 AB4 LYS A 195 ASP A 198 5 4
HELIX 14 AB5 ARG A 199 PHE A 205 1 7
HELIX 15 AB6 PRO A 215 GLN A 231 1 17
HELIX 16 AB7 PRO A 248 LEU A 259 1 12
HELIX 17 AB8 TYR A 273 ASN A 278 1 6
HELIX 18 AB9 ASN A 278 LEU A 290 1 13
HELIX 19 AC1 PRO A 291 LEU A 293 5 3
SHEET 1 AA1 8 HIS A 13 VAL A 17 0
SHEET 2 AA1 8 GLU A 20 VAL A 27 -1 O GLU A 20 N VAL A 17
SHEET 3 AA1 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 AA1 8 VAL A 35 LEU A 38 1 N PHE A 37 O ILE A 62
SHEET 5 AA1 8 VAL A 100 HIS A 105 1 O VAL A 101 N LEU A 36
SHEET 6 AA1 8 VAL A 123 MET A 129 1 O LYS A 124 N VAL A 100
SHEET 7 AA1 8 LYS A 236 PRO A 243 1 O LEU A 237 N CYS A 128
SHEET 8 AA1 8 CYS A 262 GLY A 270 1 O VAL A 265 N LEU A 238
CISPEP 1 ASN A 41 PRO A 42 0 -7.00
CISPEP 2 GLU A 214 PRO A 215 0 -4.49
CISPEP 3 THR A 242 PRO A 243 0 3.37
SITE 1 AC1 10 ASN A 41 ASP A 106 TRP A 107 PHE A 149
SITE 2 AC1 10 PHE A 168 PHE A 205 PRO A 206 LEU A 209
SITE 3 AC1 10 HIS A 272 TYR A 273
CRYST1 50.889 69.551 83.916 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 0.019651 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014378 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011917 0.00000
TER 2362 LEU A 293
MASTER 290 0 1 19 8 0 3 6 2482 1 6 23
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