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HEADER HYDROLASE 10-JUL-15 5CH8
TITLE CRYSTAL STRUCTURE OF MDLA N225Q MUTANT FORM PENICILLIUM CYCLOPIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONO- AND DIACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MDGL;
COMPND 5 EC: 3.1.1.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PENICILLIUM CYCLOPIUM;
SOURCE 3 ORGANISM_TAXID: 60167;
SOURCE 4 GENE: MDLA;
SOURCE 5 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: X33
KEYWDS LIPASE, MONO- AND DIACYLGLYCEROL LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.XU,H.XU,S.HOU,J.LIU
REVDAT 1 20-APR-16 5CH8 0
JRNL AUTH Q.TANG,G.M.POPOWICZ,X.WANG,J.LIU,I.V.PAVLIDIS,Y.WANG
JRNL TITL LIPASE-DRIVEN EPOXIDATION IS A TWO-STAGE SYNERGISTIC PROCESS
JRNL REF CHEMISTRYSELECT V. 4 836 2016
JRNL DOI 10.1002/SLCT.201600254
REMARK 2
REMARK 2 RESOLUTION. 1.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
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) : 1.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 24482
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) : 0.137
REMARK 3 R VALUE (WORKING SET) : 0.135
REMARK 3 FREE R VALUE : 0.166
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1299
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) : 1.62
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.66
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1844
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.1360
REMARK 3 BIN FREE R VALUE SET COUNT : 114
REMARK 3 BIN FREE R VALUE : 0.1580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2067
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 245
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 7.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07000
REMARK 3 B22 (A**2) : 0.78000
REMARK 3 B33 (A**2) : -0.28000
REMARK 3 B12 (A**2) : -0.40000
REMARK 3 B13 (A**2) : 0.04000
REMARK 3 B23 (A**2) : 0.61000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.089
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.086
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.049
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.353
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2158 ; 0.012 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1955 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2958 ; 1.510 ; 1.931
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4507 ; 0.984 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 279 ; 6.437 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 95 ;32.770 ;24.737
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 314 ;10.901 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;13.725 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 335 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2486 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 500 ; 0.002 ; 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): 1089 ; 0.614 ; 0.630
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1088 ; 0.596 ; 0.628
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1362 ; 1.009 ; 0.942
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
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 : 0.80
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 5CH8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211626.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9785
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.2.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25794
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.620
REMARK 200 RESOLUTION RANGE LOW (A) : 37.320
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.15100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 11.50
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 31.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.02M ZINC CHLORIDE, 20% W/V
REMARK 280 POLYETHYLENE GLYCOL 3350, VAPOR DIFFUSION, TEMPERATURE 293K
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 TOTAL BURIED SURFACE AREA: 1120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -98.0 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 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 GLY A 271
REMARK 465 PRO A 272
REMARK 465 GLY A 273
REMARK 465 LEU A 274
REMARK 465 PRO A 275
REMARK 465 PHE A 276
REMARK 465 LYS A 277
REMARK 465 ARG A 278
REMARK 465 VAL A 279
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 MET A 209 CG - SD - CE ANGL. DEV. = 11.8 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 SER A 58 -162.22 -163.48
REMARK 500 SER A 145 -136.75 62.35
REMARK 500 THR A 197 -113.71 36.28
REMARK 500 PHE A 263 -54.72 70.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 8 OD1
REMARK 620 2 GLU A 43 OE2 177.8
REMARK 620 3 HOH A 408 O 82.3 97.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 237 OD2
REMARK 620 2 ASP A 239 OD2 99.5
REMARK 620 3 HOH A 606 O 104.9 102.7
REMARK 620 4 GLU A 129 OE1 29.4 71.2 118.5
REMARK 620 5 GLU A 129 OE2 26.8 73.9 118.0 2.7
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 308
DBREF 5CH8 A 1 279 UNP P61869 MDLA_PENCY 27 305
SEQADV 5CH8 GLN A 225 UNP P61869 ASN 251 ENGINEERED MUTATION
SEQRES 1 A 279 ASP VAL SER THR SER GLU LEU ASP GLN PHE GLU PHE TRP
SEQRES 2 A 279 VAL GLN TYR ALA ALA ALA SER TYR TYR GLU ALA ASP TYR
SEQRES 3 A 279 THR ALA GLN VAL GLY ASP LYS LEU SER CYS SER LYS GLY
SEQRES 4 A 279 ASN CYS PRO GLU VAL GLU ALA THR GLY ALA THR VAL SER
SEQRES 5 A 279 TYR ASP PHE SER ASP SER THR ILE THR ASP THR ALA GLY
SEQRES 6 A 279 TYR ILE ALA VAL ASP HIS THR ASN SER ALA VAL VAL LEU
SEQRES 7 A 279 ALA PHE ARG GLY SER TYR SER VAL ARG ASN TRP VAL ALA
SEQRES 8 A 279 ASP ALA THR PHE VAL HIS THR ASN PRO GLY LEU CYS ASP
SEQRES 9 A 279 GLY CYS LEU ALA GLU LEU GLY PHE TRP SER SER TRP LYS
SEQRES 10 A 279 LEU VAL ARG ASP ASP ILE ILE LYS GLU LEU LYS GLU VAL
SEQRES 11 A 279 VAL ALA GLN ASN PRO ASN TYR GLU LEU VAL VAL VAL GLY
SEQRES 12 A 279 HIS SER LEU GLY ALA ALA VAL ALA THR LEU ALA ALA THR
SEQRES 13 A 279 ASP LEU ARG GLY LYS GLY TYR PRO SER ALA LYS LEU TYR
SEQRES 14 A 279 ALA TYR ALA SER PRO ARG VAL GLY ASN ALA ALA LEU ALA
SEQRES 15 A 279 LYS TYR ILE THR ALA GLN GLY ASN ASN PHE ARG PHE THR
SEQRES 16 A 279 HIS THR ASN ASP PRO VAL PRO LYS LEU PRO LEU LEU SER
SEQRES 17 A 279 MET GLY TYR VAL HIS VAL SER PRO GLU TYR TRP ILE THR
SEQRES 18 A 279 SER PRO ASN GLN ALA THR VAL SER THR SER ASP ILE LYS
SEQRES 19 A 279 VAL ILE ASP GLY ASP VAL SER PHE ASP GLY ASN THR GLY
SEQRES 20 A 279 THR GLY LEU PRO LEU LEU THR ASP PHE GLU ALA HIS ILE
SEQRES 21 A 279 TRP TYR PHE VAL GLN VAL ASP ALA GLY LYS GLY PRO GLY
SEQRES 22 A 279 LEU PRO PHE LYS ARG VAL
HET ZN A 301 1
HET ZN A 302 1
HET CL A 303 1
HET CL A 304 1
HET CL A 305 1
HET CL A 306 1
HET CL A 307 1
HET GOL A 308 6
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ZN 2(ZN 2+)
FORMUL 4 CL 5(CL 1-)
FORMUL 9 GOL C3 H8 O3
FORMUL 10 HOH *245(H2 O)
HELIX 1 AA1 SER A 3 SER A 20 1 18
HELIX 2 AA2 TYR A 22 THR A 27 1 6
HELIX 3 AA3 CYS A 41 THR A 47 1 7
HELIX 4 AA4 SER A 85 ALA A 93 1 9
HELIX 5 AA5 LEU A 110 ASN A 134 1 25
HELIX 6 AA6 SER A 145 GLY A 160 1 16
HELIX 7 AA7 ALA A 179 GLY A 189 1 11
HELIX 8 AA8 PRO A 200 LEU A 204 5 5
HELIX 9 AA9 LEU A 206 MET A 209 5 4
HELIX 10 AB1 SER A 229 SER A 231 5 3
HELIX 11 AB2 ASP A 243 GLY A 249 5 7
HELIX 12 AB3 LEU A 252 ILE A 260 5 9
SHEET 1 AA1 8 THR A 50 PHE A 55 0
SHEET 2 AA1 8 ALA A 64 ASP A 70 -1 O ILE A 67 N SER A 52
SHEET 3 AA1 8 ALA A 75 ARG A 81 -1 O VAL A 77 N ALA A 68
SHEET 4 AA1 8 GLU A 138 HIS A 144 1 O GLU A 138 N VAL A 76
SHEET 5 AA1 8 LYS A 167 TYR A 171 1 O LYS A 167 N VAL A 141
SHEET 6 AA1 8 ASN A 191 HIS A 196 1 O PHE A 192 N LEU A 168
SHEET 7 AA1 8 GLU A 217 ILE A 220 1 O TYR A 218 N ARG A 193
SHEET 8 AA1 8 ILE A 233 ILE A 236 -1 O LYS A 234 N TRP A 219
SHEET 1 AA2 2 HIS A 97 THR A 98 0
SHEET 2 AA2 2 ALA A 108 GLU A 109 -1 O ALA A 108 N THR A 98
SHEET 1 AA3 2 GLY A 177 ASN A 178 0
SHEET 2 AA3 2 TYR A 211 VAL A 212 -1 O VAL A 212 N GLY A 177
SSBOND 1 CYS A 36 CYS A 41 1555 1555 2.05
SSBOND 2 CYS A 103 CYS A 106 1555 1555 2.07
LINK OD1AASP A 8 ZN ZN A 302 1555 1555 2.00
LINK OE2 GLU A 43 ZN ZN A 302 1555 1555 1.96
LINK OD2 ASP A 237 ZN ZN A 301 1555 1555 1.98
LINK OD2 ASP A 239 ZN ZN A 301 1555 1555 1.94
LINK ZN ZN A 301 O HOH A 606 1555 1555 2.08
LINK ZN ZN A 302 O HOH A 408 1555 1555 2.11
LINK OE1 GLU A 129 ZN ZN A 301 1555 1546 2.04
LINK OE2 GLU A 129 ZN ZN A 301 1555 1546 2.53
CISPEP 1 LEU A 204 PRO A 205 0 -12.97
CISPEP 2 SER A 215 PRO A 216 0 0.04
SITE 1 AC1 4 GLU A 129 ASP A 237 ASP A 239 HOH A 606
SITE 1 AC2 3 ASP A 8 GLU A 43 HOH A 408
SITE 1 AC3 3 PHE A 12 ASN A 73 HOH A 528
SITE 1 AC4 2 TYR A 21 SER A 145
SITE 1 AC5 4 THR A 197 ASN A 224 HOH A 421 HOH A 552
SITE 1 AC6 4 SER A 58 ILE A 60 THR A 61 HOH A 409
SITE 1 AC7 3 LYS A 33 ASP A 104 HOH A 585
SITE 1 AC8 11 ASP A 62 THR A 63 GLY A 82 SER A 83
SITE 2 AC8 11 GLY A 111 PHE A 112 SER A 115 LEU A 146
SITE 3 AC8 11 VAL A 150 HOH A 461 HOH A 468
CRYST1 33.330 44.520 44.760 61.27 68.65 78.17 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 0.030003 -0.006284 -0.009972 0.00000
SCALE2 0.000000 0.022949 -0.011420 0.00000
SCALE3 0.000000 0.000000 0.026793 0.00000
TER 2093 LYS A 270
MASTER 337 0 8 12 12 0 10 6 2325 1 18 22
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