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HEADER HYDROLASE 10-FEB-09 3G7N
TITLE CRYSTAL STRUCTURE OF A TRIACYLGLYCEROL LIPASE FROM
TITLE 2 PENICILLIUM EXPANSUM AT 1.3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TRIACYLGLYCEROL LIPASE;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PENICILLIUM EXPANSUM;
SOURCE 3 ORGANISM_TAXID: 27334;
SOURCE 4 GENE: PEL;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PPIC9K
KEYWDS HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.B.BIAN,C.YUAN,L.Q.CHEN,J.M.EDWARD,L.LIN,L.G.JIANG,
AUTHOR 2 Z.X.HUANG,M.D.HUANG
REVDAT 1 23-FEB-10 3G7N 0
JRNL AUTH C.B.BIAN,C.YUAN,L.Q.CHEN,E.J.MEEHAN,L.G.JIANG,
JRNL AUTH 2 Z.X.HUANG,L.LIN,M.D.HUANG
JRNL TITL CRYSTAL STRUCTURE OF A TRIACYLGLYCEROL LIPASE FROM
JRNL TITL 2 PENICILLIUM EXPANSUM AT 1.3 A DETERMINED BY SULFUR
JRNL TITL 3 SAD
JRNL REF PROTEINS 2009
JRNL REFN ESSN 1097-0134
JRNL PMID 20146362
JRNL DOI 10.1002/PROT.22676
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 116585
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6161
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) : 1.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.33
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8495
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.3010
REMARK 3 BIN FREE R VALUE SET COUNT : 454
REMARK 3 BIN FREE R VALUE : 0.3390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3826
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 358
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.01000
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): 0.051
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.053
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.031
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.707
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3981 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5409 ; 1.138 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 516 ; 7.030 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 149 ;34.949 ;24.027
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 592 ;11.895 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;20.030 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 619 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2957 ; 0.020 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1898 ; 0.194 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2795 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 261 ; 0.080 ; 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): 64 ; 0.180 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.132 ; 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): 2548 ; 1.650 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4096 ; 2.647 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1433 ; 3.937 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1313 ; 5.630 ; 4.500
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 : 1.40
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3G7N COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051525.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAR-06; 10-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; APS
REMARK 200 BEAMLINE : 22-ID; 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.9; 1.0
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE; MAR
REMARK 200 SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 123399
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 13.400
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 40.1300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.70
REMARK 200 R MERGE FOR SHELL (I) : 0.51600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE,PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AS, PEG400, PH 8.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.30800
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 44.13500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 44.13500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 94.96200
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 44.13500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 44.13500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 31.65400
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 44.13500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 44.13500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 94.96200
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 44.13500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 44.13500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 31.65400
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 63.30800
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 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 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 ASP A 70
REMARK 465 PHE A 71
REMARK 465 VAL A 72
REMARK 465 ASN A 73
REMARK 465 SER B 258
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 O HOH B 314 O HOH B 344 2.13
REMARK 500 C2 PEG A 266 O HOH A 326 2.15
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 OH TYR B 235 C2 PEG A 264 6455 1.87
REMARK 500 OH TYR B 235 C1 PEG A 264 6455 2.03
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 PHE A 30 -123.33 51.88
REMARK 500 SER A 132 -124.15 64.25
REMARK 500 CYS A 228 -145.27 -117.15
REMARK 500 ALA A 236 -150.41 59.47
REMARK 500 LEU A 250 -5.22 81.39
REMARK 500 PHE B 30 -124.69 52.55
REMARK 500 SER B 132 -124.28 63.85
REMARK 500 ASN B 200 35.08 73.97
REMARK 500 CYS B 228 -146.16 -106.72
REMARK 500 ALA B 236 -151.91 59.68
REMARK 500 LEU B 250 -8.15 84.59
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 PHE A 245 0.08 SIDE CHAIN
REMARK 500 PHE B 245 0.08 SIDE CHAIN
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 SO4 A 259
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 261
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 259
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE B 261
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 WILD TYPE PROTEIN WAS USED IN THE STUDY. THE SEQUENCE OBTAINED
REMARK 999 IN THE STRUCTURE IS RELIABLE.
DBREF 3G7N A 1 258 UNP Q9HFW6 Q9HFW6_PENEN 1 258
DBREF 3G7N B 1 258 UNP Q9HFW6 Q9HFW6_PENEN 1 258
SEQADV 3G7N VAL A 35 UNP Q9HFW6 ALA 35 SEE REMARK 999
SEQADV 3G7N VAL B 35 UNP Q9HFW6 ALA 35 SEE REMARK 999
SEQRES 1 A 258 ALA THR ALA ASP ALA ALA ALA PHE PRO ASP LEU HIS ARG
SEQRES 2 A 258 ALA ALA LYS LEU SER SER ALA ALA TYR THR GLY CYS ILE
SEQRES 3 A 258 GLY LYS ALA PHE ASP VAL THR ILE VAL LYS ARG ILE TYR
SEQRES 4 A 258 ASP LEU VAL THR ASP THR ASN GLY PHE VAL GLY TYR SER
SEQRES 5 A 258 THR GLU LYS LYS THR ILE ALA VAL ILE MET ARG GLY SER
SEQRES 6 A 258 THR THR ILE THR ASP PHE VAL ASN ASP ILE ASP ILE ALA
SEQRES 7 A 258 LEU ILE THR PRO GLU LEU SER GLY VAL THR PHE PRO SER
SEQRES 8 A 258 ASP VAL LYS ILE MET ARG GLY VAL HIS ARG PRO TRP SER
SEQRES 9 A 258 ALA VAL HIS ASP THR ILE ILE THR GLU VAL LYS ALA LEU
SEQRES 10 A 258 ILE ALA LYS TYR PRO ASP TYR THR LEU GLU ALA VAL GLY
SEQRES 11 A 258 HIS SER LEU GLY GLY ALA LEU THR SER ILE ALA HIS VAL
SEQRES 12 A 258 ALA LEU ALA GLN ASN PHE PRO ASP LYS SER LEU VAL SER
SEQRES 13 A 258 ASN ALA LEU ASN ALA PHE PRO ILE GLY ASN GLN ALA TRP
SEQRES 14 A 258 ALA ASP PHE GLY THR ALA GLN ALA GLY THR PHE ASN ARG
SEQRES 15 A 258 GLY ASN ASN VAL LEU ASP GLY VAL PRO ASN MET TYR SER
SEQRES 16 A 258 SER PRO LEU VAL ASN PHE LYS HIS TYR GLY THR GLU TYR
SEQRES 17 A 258 TYR SER SER GLY THR GLU ALA SER THR VAL LYS CYS GLU
SEQRES 18 A 258 GLY GLN ARG ASP LYS SER CYS SER ALA GLY ASN GLY MET
SEQRES 19 A 258 TYR ALA VAL THR PRO GLY HIS ILE ALA SER PHE GLY VAL
SEQRES 20 A 258 VAL MET LEU THR ALA GLY CYS GLY TYR LEU SER
SEQRES 1 B 258 ALA THR ALA ASP ALA ALA ALA PHE PRO ASP LEU HIS ARG
SEQRES 2 B 258 ALA ALA LYS LEU SER SER ALA ALA TYR THR GLY CYS ILE
SEQRES 3 B 258 GLY LYS ALA PHE ASP VAL THR ILE VAL LYS ARG ILE TYR
SEQRES 4 B 258 ASP LEU VAL THR ASP THR ASN GLY PHE VAL GLY TYR SER
SEQRES 5 B 258 THR GLU LYS LYS THR ILE ALA VAL ILE MET ARG GLY SER
SEQRES 6 B 258 THR THR ILE THR ASP PHE VAL ASN ASP ILE ASP ILE ALA
SEQRES 7 B 258 LEU ILE THR PRO GLU LEU SER GLY VAL THR PHE PRO SER
SEQRES 8 B 258 ASP VAL LYS ILE MET ARG GLY VAL HIS ARG PRO TRP SER
SEQRES 9 B 258 ALA VAL HIS ASP THR ILE ILE THR GLU VAL LYS ALA LEU
SEQRES 10 B 258 ILE ALA LYS TYR PRO ASP TYR THR LEU GLU ALA VAL GLY
SEQRES 11 B 258 HIS SER LEU GLY GLY ALA LEU THR SER ILE ALA HIS VAL
SEQRES 12 B 258 ALA LEU ALA GLN ASN PHE PRO ASP LYS SER LEU VAL SER
SEQRES 13 B 258 ASN ALA LEU ASN ALA PHE PRO ILE GLY ASN GLN ALA TRP
SEQRES 14 B 258 ALA ASP PHE GLY THR ALA GLN ALA GLY THR PHE ASN ARG
SEQRES 15 B 258 GLY ASN ASN VAL LEU ASP GLY VAL PRO ASN MET TYR SER
SEQRES 16 B 258 SER PRO LEU VAL ASN PHE LYS HIS TYR GLY THR GLU TYR
SEQRES 17 B 258 TYR SER SER GLY THR GLU ALA SER THR VAL LYS CYS GLU
SEQRES 18 B 258 GLY GLN ARG ASP LYS SER CYS SER ALA GLY ASN GLY MET
SEQRES 19 B 258 TYR ALA VAL THR PRO GLY HIS ILE ALA SER PHE GLY VAL
SEQRES 20 B 258 VAL MET LEU THR ALA GLY CYS GLY TYR LEU SER
HET SO4 A 259 5
HET SO4 A 260 5
HET SO4 A 261 5
HET PEG A 262 7
HET PEG A 263 7
HET PEG A 264 7
HET PEG A 265 7
HET PEG A 266 7
HET SO4 B 259 5
HET SO4 B 260 5
HET 1PE B 261 16
HETNAM SO4 SULFATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 3 SO4 5(O4 S 2-)
FORMUL 6 PEG 5(C4 H10 O3)
FORMUL 13 1PE C10 H22 O6
FORMUL 14 HOH *358(H2 O)
HELIX 1 1 ALA A 7 GLY A 24 1 18
HELIX 2 2 ARG A 97 TYR A 121 1 25
HELIX 3 3 SER A 132 PHE A 149 1 18
HELIX 4 4 ASN A 166 GLN A 176 1 11
HELIX 5 5 GLY A 189 MET A 193 5 5
HELIX 6 6 CYS A 228 ASN A 232 5 5
HELIX 7 7 THR A 238 HIS A 241 5 4
HELIX 8 8 ALA B 7 GLY B 24 1 18
HELIX 9 9 ASP B 70 ASP B 74 5 5
HELIX 10 10 ARG B 97 TYR B 121 1 25
HELIX 11 11 SER B 132 PHE B 149 1 18
HELIX 12 12 ASN B 166 GLN B 176 1 11
HELIX 13 13 GLY B 189 MET B 193 5 5
HELIX 14 14 THR B 213 SER B 216 5 4
HELIX 15 15 CYS B 228 ASN B 232 5 5
HELIX 16 16 THR B 238 HIS B 241 5 4
SHEET 1 A10 THR A 2 ALA A 3 0
SHEET 2 A10 VAL A 218 LYS A 219 -1 O LYS A 219 N THR A 2
SHEET 3 A10 THR A 206 SER A 210 -1 N TYR A 209 O VAL A 218
SHEET 4 A10 THR A 179 ASN A 185 1 N ASN A 184 O TYR A 208
SHEET 5 A10 LEU A 154 LEU A 159 1 N SER A 156 O ASN A 181
SHEET 6 A10 THR A 125 HIS A 131 1 N GLY A 130 O LEU A 159
SHEET 7 A10 THR A 57 MET A 62 1 N MET A 62 O VAL A 129
SHEET 8 A10 THR A 45 SER A 52 -1 N PHE A 48 O ILE A 61
SHEET 9 A10 VAL A 32 ASP A 40 -1 N THR A 33 O TYR A 51
SHEET 10 A10 LYS A 28 ALA A 29 -1 N ALA A 29 O VAL A 32
SHEET 1 B 2 LEU A 79 ILE A 80 0
SHEET 2 B 2 ILE A 95 MET A 96 -1 O ILE A 95 N ILE A 80
SHEET 1 C 2 ALA A 243 SER A 244 0
SHEET 2 C 2 VAL A 247 VAL A 248 -1 O VAL A 247 N SER A 244
SHEET 1 D10 THR B 2 ALA B 3 0
SHEET 2 D10 VAL B 218 LYS B 219 -1 O LYS B 219 N THR B 2
SHEET 3 D10 THR B 206 SER B 210 -1 N TYR B 209 O VAL B 218
SHEET 4 D10 THR B 179 ASN B 185 1 N ARG B 182 O THR B 206
SHEET 5 D10 LEU B 154 LEU B 159 1 N SER B 156 O ASN B 181
SHEET 6 D10 THR B 125 HIS B 131 1 N GLY B 130 O LEU B 159
SHEET 7 D10 THR B 57 MET B 62 1 N MET B 62 O VAL B 129
SHEET 8 D10 THR B 45 SER B 52 -1 N SER B 52 O THR B 57
SHEET 9 D10 VAL B 32 ASP B 40 -1 N THR B 33 O TYR B 51
SHEET 10 D10 LYS B 28 ALA B 29 -1 N ALA B 29 O VAL B 32
SHEET 1 E 2 LEU B 79 ILE B 80 0
SHEET 2 E 2 ILE B 95 MET B 96 -1 O ILE B 95 N ILE B 80
SHEET 1 F 2 ALA B 243 SER B 244 0
SHEET 2 F 2 VAL B 247 VAL B 248 -1 O VAL B 247 N SER B 244
SSBOND 1 CYS A 25 CYS A 254 1555 1555 2.01
SSBOND 2 CYS A 220 CYS A 228 1555 1555 2.06
SSBOND 3 CYS B 25 CYS B 254 1555 1555 2.04
SSBOND 4 CYS B 220 CYS B 228 1555 1555 2.06
SITE 1 AC1 5 SER A 65 ILE A 68 SER A 132 VAL A 237
SITE 2 AC1 5 PEG A 265
SITE 1 AC2 2 ARG A 101 SER A 227
SITE 1 AC3 7 LYS A 16 PHE A 30 SER A 258 HOH A 376
SITE 2 AC3 7 PRO B 90 SER B 91 HOH B 403
SITE 1 AC4 5 ILE A 77 TYR A 194 SER A 196 TYR A 235
SITE 2 AC4 5 THR B 238
SITE 1 AC5 5 GLU A 221 GLY A 222 GLN A 223 ARG A 224
SITE 2 AC5 5 ASP A 225
SITE 1 AC6 7 THR A 238 HOH A 299 TYR B 194 SER B 195
SITE 2 AC6 7 SER B 196 VAL B 199 TYR B 235
SITE 1 AC7 4 ASP A 74 SO4 A 259 HOH A 324 HOH A 335
SITE 1 AC8 7 VAL A 35 TYR A 51 GLU A 113 HOH A 326
SITE 2 AC8 7 HOH A 431 ASP B 171 HOH B 294
SITE 1 AC9 3 ARG B 224 HOH B 402 HOH B 432
SITE 1 BC1 6 ARG B 101 VAL B 186 LEU B 187 TYR B 209
SITE 2 BC1 6 ASN B 232 HOH B 383
SITE 1 BC2 5 SER A 196 GLY A 233 TYR A 235 HOH A 377
SITE 2 BC2 5 PRO B 239
CRYST1 88.270 88.270 126.616 90.00 90.00 90.00 P 43 21 2 16
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 0.011329 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011329 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007898 0.00000
TER 1901 SER A 258
TER 3828 LEU B 257
MASTER 393 0 11 16 28 0 19 6 4260 2 84 40
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