| content |
HEADER HYDROLASE 15-OCT-24 9K0H
TITLE THE CRYSTAL STRUCTURE OF DSPETASE05 FROM BIORTUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONADOTA BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 1977087;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS POLYESTERASE-LIPASE-CUTINASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.WAN,F.WANG,Z.LV,D.LIN,W.PAN,H.SHANG,J.SUN
REVDAT 1 22-OCT-25 9K0H 0
JRNL AUTH T.WAN,F.WANG,Z.LV,D.LIN,W.PAN,H.SHANG,J.SUN
JRNL TITL THE CRYSTAL STRUCTURE OF DSPETASE05 FROM BIORTUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0430
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 33835
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.048
REMARK 3 FREE R VALUE TEST SET COUNT : 1708
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2275
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.09
REMARK 3 BIN R VALUE (WORKING SET) : 0.2040
REMARK 3 BIN FREE R VALUE SET COUNT : 123
REMARK 3 BIN FREE R VALUE : 0.2340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3794
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 523
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.66900
REMARK 3 B22 (A**2) : -1.35400
REMARK 3 B33 (A**2) : 0.45200
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.96600
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.161
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.143
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.105
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.727
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3961 ; 0.008 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 3466 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5411 ; 1.539 ; 1.757
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7988 ; 0.539 ; 1.726
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 528 ; 6.918 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 20 ; 8.057 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 544 ; 9.845 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 583 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4916 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 976 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 816 ; 0.213 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 69 ; 0.150 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2033 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 444 ; 0.194 ; 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): 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): 2072 ; 1.323 ; 1.301
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2072 ; 1.296 ; 1.301
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2591 ; 2.085 ; 2.329
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2592 ; 2.086 ; 2.331
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1889 ; 1.770 ; 1.446
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1890 ; 1.769 ; 1.447
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2811 ; 2.750 ; 2.577
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2812 ; 2.750 ; 2.578
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 BULK SOLVENT
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 THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 9K0H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 18-OCT-24.
REMARK 100 THE DEPOSITION ID IS D_1300052591.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-24
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 : BL02U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979191
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33866
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.948
REMARK 200 RESOLUTION RANGE LOW (A) : 35.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
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: MORDA
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH7.5, 25% PEG3,350, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 33.63650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 1
REMARK 465 GLY A 2
REMARK 465 THR A 3
REMARK 465 ASN A 4
REMARK 465 PRO A 5
REMARK 465 GLY A 6
REMARK 465 GLY A 7
REMARK 465 GLY A 8
REMARK 465 GLY A 9
REMARK 465 GLY A 10
REMARK 465 GLY A 11
REMARK 465 GLY B 1
REMARK 465 GLY B 2
REMARK 465 THR B 3
REMARK 465 ASN B 4
REMARK 465 PRO B 5
REMARK 465 GLY B 6
REMARK 465 GLY B 7
REMARK 465 GLY B 8
REMARK 465 GLY B 9
REMARK 465 GLY B 10
REMARK 465 GLY B 11
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 OG SER B 221 O HOH B 401 2.10
REMARK 500 O HOH A 462 O HOH A 487 2.10
REMARK 500 O HOH B 565 O HOH B 587 2.10
REMARK 500 OG SER A 221 O HOH A 401 2.11
REMARK 500 O HOH B 436 O HOH B 469 2.17
REMARK 500 O HOH A 615 O HOH A 645 2.18
REMARK 500 O HOH A 609 O HOH A 691 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 263 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG A 263 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG B 128 NE - CZ - NH1 ANGL. DEV. = 3.4 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 THR A 68 -6.80 77.30
REMARK 500 SER A 135 -122.59 60.44
REMARK 500 ALA A 188 74.29 -110.59
REMARK 500 SER B 135 -123.87 65.15
REMARK 500 ALA B 188 68.92 -113.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 128 0.10 SIDE CHAIN
REMARK 500 ARG A 234 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9K0H A 1 268 PDB 9K0H 9K0H 1 268
DBREF 9K0H B 1 268 PDB 9K0H 9K0H 1 268
SEQRES 1 A 268 GLY GLY THR ASN PRO GLY GLY GLY GLY GLY GLY SER ASN
SEQRES 2 A 268 PRO ASP THR GLY THR GLY PHE PRO GLY VAL SER SER PHE
SEQRES 3 A 268 SER ALA ASP GLY SER PHE ALA THR THR SER GLY SER ALA
SEQRES 4 A 268 GLY LEU SER CYS THR VAL PHE ARG PRO SER THR LEU GLY
SEQRES 5 A 268 ALA ASN GLY LEU LYS HIS PRO ILE ILE VAL TRP GLY ASN
SEQRES 6 A 268 GLY THR THR ALA SER PRO SER THR TYR SER GLY ILE LEU
SEQRES 7 A 268 GLU HIS TRP ALA SER HIS GLY PHE VAL VAL ILE ALA ALA
SEQRES 8 A 268 ASN THR SER ASN ALA GLY THR GLY GLN ASP MET LEU ASN
SEQRES 9 A 268 CYS VAL ASP TYR LEU THR THR GLN ASN ASN ARG SER THR
SEQRES 10 A 268 GLY THR TYR ALA ASN LYS LEU ASP LEU ASN ARG ILE GLY
SEQRES 11 A 268 ALA ALA GLY HIS SER GLN GLY GLY GLY GLY THR ILE MET
SEQRES 12 A 268 ALA GLY GLN ASP TYR ARG ILE LYS VAL THR ALA PRO PHE
SEQRES 13 A 268 GLN PRO TYR THR ILE GLY LEU GLY HIS ASN SER SER SER
SEQRES 14 A 268 GLN SER ASN GLN ASN GLY PRO MET PHE LEU MET THR GLY
SEQRES 15 A 268 SER ALA ASP THR ILE ALA SER PRO THR LEU ASN ALA LEU
SEQRES 16 A 268 PRO VAL TYR ASN ARG ALA ASN VAL PRO VAL PHE TRP GLY
SEQRES 17 A 268 GLU LEU SER GLY ALA SER HIS PHE GLU PRO VAL GLY SER
SEQRES 18 A 268 ALA GLY ASP PHE ARG GLY PRO SER THR ALA TRP PHE ARG
SEQRES 19 A 268 TYR HIS LEU MET ASP ASP ALA SER ALA GLU ASP THR PHE
SEQRES 20 A 268 TYR GLY SER ASN CYS ASP LEU CYS THR ASP ASN ASP TRP
SEQRES 21 A 268 ASP VAL ARG ARG LYS GLY ILE ASN
SEQRES 1 B 268 GLY GLY THR ASN PRO GLY GLY GLY GLY GLY GLY SER ASN
SEQRES 2 B 268 PRO ASP THR GLY THR GLY PHE PRO GLY VAL SER SER PHE
SEQRES 3 B 268 SER ALA ASP GLY SER PHE ALA THR THR SER GLY SER ALA
SEQRES 4 B 268 GLY LEU SER CYS THR VAL PHE ARG PRO SER THR LEU GLY
SEQRES 5 B 268 ALA ASN GLY LEU LYS HIS PRO ILE ILE VAL TRP GLY ASN
SEQRES 6 B 268 GLY THR THR ALA SER PRO SER THR TYR SER GLY ILE LEU
SEQRES 7 B 268 GLU HIS TRP ALA SER HIS GLY PHE VAL VAL ILE ALA ALA
SEQRES 8 B 268 ASN THR SER ASN ALA GLY THR GLY GLN ASP MET LEU ASN
SEQRES 9 B 268 CYS VAL ASP TYR LEU THR THR GLN ASN ASN ARG SER THR
SEQRES 10 B 268 GLY THR TYR ALA ASN LYS LEU ASP LEU ASN ARG ILE GLY
SEQRES 11 B 268 ALA ALA GLY HIS SER GLN GLY GLY GLY GLY THR ILE MET
SEQRES 12 B 268 ALA GLY GLN ASP TYR ARG ILE LYS VAL THR ALA PRO PHE
SEQRES 13 B 268 GLN PRO TYR THR ILE GLY LEU GLY HIS ASN SER SER SER
SEQRES 14 B 268 GLN SER ASN GLN ASN GLY PRO MET PHE LEU MET THR GLY
SEQRES 15 B 268 SER ALA ASP THR ILE ALA SER PRO THR LEU ASN ALA LEU
SEQRES 16 B 268 PRO VAL TYR ASN ARG ALA ASN VAL PRO VAL PHE TRP GLY
SEQRES 17 B 268 GLU LEU SER GLY ALA SER HIS PHE GLU PRO VAL GLY SER
SEQRES 18 B 268 ALA GLY ASP PHE ARG GLY PRO SER THR ALA TRP PHE ARG
SEQRES 19 B 268 TYR HIS LEU MET ASP ASP ALA SER ALA GLU ASP THR PHE
SEQRES 20 B 268 TYR GLY SER ASN CYS ASP LEU CYS THR ASP ASN ASP TRP
SEQRES 21 B 268 ASP VAL ARG ARG LYS GLY ILE ASN
HET GOL A 301 6
HET GOL B 301 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 HOH *523(H2 O)
HELIX 1 AA1 GLY A 52 LEU A 56 5 5
HELIX 2 AA2 SER A 70 THR A 73 5 4
HELIX 3 AA3 TYR A 74 HIS A 84 1 11
HELIX 4 AA4 GLY A 99 ASN A 114 1 16
HELIX 5 AA5 GLN A 136 GLY A 145 1 10
HELIX 6 AA6 ASN A 166 ASN A 172 5 7
HELIX 7 AA7 SER A 189 ALA A 194 1 6
HELIX 8 AA8 ALA A 194 ALA A 201 1 8
HELIX 9 AA9 ALA A 222 ASP A 224 5 3
HELIX 10 AB1 PHE A 225 ASP A 239 1 15
HELIX 11 AB2 ASP A 240 PHE A 247 5 8
HELIX 12 AB3 CYS A 252 ASP A 257 1 6
HELIX 13 AB4 GLY B 52 LEU B 56 5 5
HELIX 14 AB5 SER B 70 THR B 73 5 4
HELIX 15 AB6 TYR B 74 HIS B 84 1 11
HELIX 16 AB7 GLY B 99 ARG B 115 1 17
HELIX 17 AB8 GLN B 136 GLY B 145 1 10
HELIX 18 AB9 ASN B 166 ASN B 172 5 7
HELIX 19 AC1 SER B 189 ALA B 194 1 6
HELIX 20 AC2 ALA B 194 ALA B 201 1 8
HELIX 21 AC3 ALA B 222 ASP B 224 5 3
HELIX 22 AC4 PHE B 225 ASP B 239 1 15
HELIX 23 AC5 ASP B 240 PHE B 247 5 8
HELIX 24 AC6 CYS B 252 ASP B 257 1 6
SHEET 1 AA1 6 THR A 34 SER A 38 0
SHEET 2 AA1 6 CYS A 43 PRO A 48 -1 O VAL A 45 N GLY A 37
SHEET 3 AA1 6 VAL A 87 ALA A 91 -1 O ALA A 90 N THR A 44
SHEET 4 AA1 6 HIS A 58 GLY A 64 1 N TRP A 63 O ILE A 89
SHEET 5 AA1 6 LEU A 124 SER A 135 1 O ASP A 125 N HIS A 58
SHEET 6 AA1 6 VAL A 152 PRO A 158 1 O PHE A 156 N GLY A 133
SHEET 1 AA2 3 MET A 177 GLY A 182 0
SHEET 2 AA2 3 VAL A 205 LEU A 210 1 O LEU A 210 N THR A 181
SHEET 3 AA2 3 TRP A 260 LYS A 265 -1 O ARG A 263 N TRP A 207
SHEET 1 AA3 6 THR B 34 SER B 38 0
SHEET 2 AA3 6 CYS B 43 PRO B 48 -1 O VAL B 45 N GLY B 37
SHEET 3 AA3 6 VAL B 87 ALA B 91 -1 O ALA B 90 N THR B 44
SHEET 4 AA3 6 HIS B 58 GLY B 64 1 N TRP B 63 O ILE B 89
SHEET 5 AA3 6 LEU B 124 SER B 135 1 O ASP B 125 N HIS B 58
SHEET 6 AA3 6 VAL B 152 PRO B 158 1 O PHE B 156 N GLY B 133
SHEET 1 AA4 3 MET B 177 GLY B 182 0
SHEET 2 AA4 3 VAL B 205 LEU B 210 1 O PHE B 206 N MET B 177
SHEET 3 AA4 3 TRP B 260 LYS B 265 -1 O ASP B 261 N GLU B 209
SSBOND 1 CYS A 252 CYS A 255 1555 1555 2.33
SSBOND 2 CYS B 252 CYS B 255 1555 1555 2.76
CRYST1 41.066 67.273 85.446 90.00 96.53 90.00 P 1 21 1 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 0.024351 0.000000 0.002787 0.00000
SCALE2 0.000000 0.014865 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011780 0.00000
TER 1923 ASN A 268
TER 3845 ASN B 268
MASTER 348 0 2 24 18 0 0 6 4329 2 16 42
END |