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HEADER HYDROLASE 25-OCT-07 2VEO
TITLE X-RAY STRUCTURE OF CANDIDA ANTARCTICA LIPASE A IN ITS
TITLE 2 CLOSED STATE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE A;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 3 EXPRESSION_SYSTEM_STRAIN: X33;
SOURCE 4 EXPRESSION_SYSTEM_PLASMID: PPICZALPHA-C;
SOURCE 5 ORGANISM_SCIENTIFIC: CANDIDA ANTARCTICA;
SOURCE 6 ATCC: DSM70725;
SOURCE 7 OTHER_DETAILS: CANDIDA ANTARCTICA RECLASSIFIED AS
SOURCE 8 PSEUDOZYMA APHIDIS IN 2006.
KEYWDS LIPASE, INTERFACIAL ACTIVATION, HYDROLASE, X-RAY STRUCTURE,
KEYWDS 2 SUBSTRATE SPECIFICITY
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.ERICSSON,A.KASRAYAN,P.JOHANSSON,T.BERGFORS,
AUTHOR 2 A.G.SANDSTROM,J.E.BACKVALL,S.L.MOWBRAY
REVDAT 1 06-NOV-07 2VEO 0
JRNL AUTH D.J.ERICSSON,A.KASRAYAN,P.JOHANSSON,T.BERGFORS,
JRNL AUTH 2 A.G.SANDSTROM,J.E.BACKVALL,S.L.MOWBRAY
JRNL TITL X-RAY STRUCTURE OF CANDIDA ANTARCTICA LIPASE A
JRNL TITL 2 SHOWS A NOVEL LID STRUCTURE AND A LIKELY MODE OF
JRNL TITL 3 INTERFACIAL ACTIVATION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.2 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 59774
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) : 0.19204
REMARK 3 R VALUE (WORKING SET) : 0.19049
REMARK 3 FREE R VALUE : 0.22108
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 3194
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) : 2.200
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.257
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3679
REMARK 3 BIN R VALUE (WORKING SET) : 0.256
REMARK 3 BIN FREE R VALUE SET COUNT : 194
REMARK 3 BIN FREE R VALUE : 0.315
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6504
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 466
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.7
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.726
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07
REMARK 3 B22 (A**2) : 0.07
REMARK 3 B33 (A**2) : -0.14
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.200
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.169
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.095
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.698
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 6705 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED (DEGREES): 9176 ; 0.937 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 858 ; 4.622 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 274 ;33.447 ;25.109
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 970 ;13.176 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;15.224 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1030 ; 0.061 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 5184 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED (A): 3198 ; 0.171 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED (A): 4675 ; 0.300 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED (A): 430 ; 0.096 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 45 ; 0.176 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED (A): 10 ; 0.151 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 4395 ; 0.255 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 6948 ; 0.457 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 2630 ; 0.564 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 2228 ; 0.953 ; 4.500
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF 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 2VEO COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 25-OCT-2007.
REMARK 100 THE EBI ID CODE IS EBI-34197.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-2006
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF BEAMLINE ID29
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63098
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.20
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 4.0
REMARK 200 R MERGE (I) : 0.14
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.5
REMARK 200 R MERGE FOR SHELL (I) : 0.62
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SHELXD, MLPHARE, SHARP, O
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 MICROLITER 10
REMARK 280 MILLIGRAM/MILLILITER PROTEIN IN 0.002M TRIS-HCL, PH 8.0
REMARK 280 MIXED WITH 1 MICROLITER 0.2M AMMONIUM SULFATE, 0.1M
REMARK 280 BIS-TRIS, PH 5.5, AND 25% (W/V) PEG 3350.
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,1/2+Z
REMARK 290 3555 1/2-Y,1/2+X,3/4+Z
REMARK 290 4555 1/2+Y,1/2-X,1/4+Z
REMARK 290 5555 1/2-X,1/2+Y,3/4-Z
REMARK 290 6555 1/2+X,1/2-Y,1/4-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 149.92100
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 45.76950
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 45.76950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 224.88150
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 45.76950
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 45.76950
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 74.96050
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 45.76950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 45.76950
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 224.88150
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 45.76950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 45.76950
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 74.96050
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 149.92100
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 M 1 B 11 .. 440 A 11 .. 440 0.298
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK ALSO PROVIDES 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: PQS
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: PQS
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 ALA A 1
REMARK 465 PRO A 2
REMARK 465 ALA A 3
REMARK 465 THR A 4
REMARK 465 GLU A 5
REMARK 465 THR A 6
REMARK 465 LEU A 7
REMARK 465 ASP A 8
REMARK 465 ARG A 9
REMARK 465 ARG A 10
REMARK 465 PRO A 441
REMARK 465 ALA B 1
REMARK 465 PRO B 2
REMARK 465 ALA B 3
REMARK 465 THR B 4
REMARK 465 GLU B 5
REMARK 465 THR B 6
REMARK 465 LEU B 7
REMARK 465 ASP B 8
REMARK 465 ARG B 9
REMARK 465 ARG B 10
REMARK 465 PRO B 441
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 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 TYR A 22 42.70 -97.00
REMARK 500 LEU A 121 -91.78 -100.88
REMARK 500 SER A 184 -125.06 61.96
REMARK 500 CYS A 273 -162.31 -120.40
REMARK 500 GLU A 308 52.31 -92.65
REMARK 500 ILE A 336 -50.15 -121.03
REMARK 500 TYR B 22 40.65 -96.43
REMARK 500 ASN B 27 30.05 -93.57
REMARK 500 LEU B 121 -88.82 -96.00
REMARK 500 SER B 184 -122.98 60.82
REMARK 500 CYS B 273 -165.59 -117.65
REMARK 500 GLU B 308 53.09 -91.30
REMARK 500 PRO B 333 32.73 -84.85
REMARK 500 ILE B 404 -67.27 -106.39
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 600
REMARK 600 HETEROGEN
REMARK 600 URANYL (VI) ION (IUM): URANYL OXYGENS IMPOSSIBLE TO PLACE
REMARK 600 DUE TO LOW OCCUPANCY.
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: IUM BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: IUM BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: IUM BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: IUM BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: PG4 BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN B
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 PRIMARY AMINO ACID SEQUENCE UNAVAILABLE FROM ANY DATABASE
REMARK 999 AT TIME OF DEPOSITION.
DBREF 2VEO A 1 441 PDB 2VEO 2VEO 1 441
DBREF 2VEO B 1 441 PDB 2VEO 2VEO 1 441
SEQRES 1 A 441 ALA PRO ALA THR GLU THR LEU ASP ARG ARG ALA ALA LEU
SEQRES 2 A 441 PRO ASN PRO TYR ASP ASP PRO PHE TYR THR THR PRO SER
SEQRES 3 A 441 ASN ILE GLY THR PHE ALA LYS GLY GLN VAL ILE GLN SER
SEQRES 4 A 441 ARG LYS VAL PRO THR ASP ILE GLY ASN ALA ASN ASN ALA
SEQRES 5 A 441 ALA SER PHE GLN LEU GLN TYR ARG THR THR ASN THR GLN
SEQRES 6 A 441 ASN GLU ALA VAL ALA ASP VAL ALA THR VAL TRP ILE PRO
SEQRES 7 A 441 ALA LYS PRO ALA SER PRO PRO LYS ILE PHE SER TYR GLN
SEQRES 8 A 441 VAL TYR GLU ASP ALA THR ALA LEU ASP CYS ALA PRO SER
SEQRES 9 A 441 TYR SER TYR LEU THR GLY LEU ASP GLN PRO ASN LYS VAL
SEQRES 10 A 441 THR ALA VAL LEU ASP THR PRO ILE ILE ILE GLY TRP ALA
SEQRES 11 A 441 LEU GLN GLN GLY TYR TYR VAL VAL SER SER ASP HIS GLU
SEQRES 12 A 441 GLY PHE LYS ALA ALA PHE ILE ALA GLY TYR GLU GLU GLY
SEQRES 13 A 441 MET ALA ILE LEU ASP GLY ILE ARG ALA LEU LYS ASN TYR
SEQRES 14 A 441 GLN ASN LEU PRO SER ASP SER LYS VAL ALA LEU GLU GLY
SEQRES 15 A 441 TYR SER GLY GLY ALA HIS ALA THR VAL TRP ALA THR SER
SEQRES 16 A 441 LEU ALA ASP SER TYR ALA PRO GLU LEU ASN ILE VAL GLY
SEQRES 17 A 441 ALA SER HIS GLY GLY THR PRO VAL SER ALA LYS ASP THR
SEQRES 18 A 441 PHE THR PHE LEU ASN GLY GLY PRO PHE ALA GLY PHE ALA
SEQRES 19 A 441 LEU ALA GLY VAL SER GLY LEU SER LEU ALA HIS PRO ASP
SEQRES 20 A 441 MET GLU SER PHE ILE GLU ALA ARG LEU ASN ALA LYS GLY
SEQRES 21 A 441 GLN GLN THR LEU LYS GLN ILE ARG GLY ARG GLY PHE CYS
SEQRES 22 A 441 LEU PRO GLN VAL VAL LEU THR TYR PRO PHE LEU ASN VAL
SEQRES 23 A 441 PHE SER LEU VAL ASN ASP THR ASN LEU LEU ASN GLU ALA
SEQRES 24 A 441 PRO ILE ALA GLY ILE LEU LYS GLN GLU THR VAL VAL GLN
SEQRES 25 A 441 ALA GLU ALA SER TYR THR VAL SER VAL PRO LYS PHE PRO
SEQRES 26 A 441 ARG PHE ILE TRP HIS ALA ILE PRO ASP GLU ILE VAL PRO
SEQRES 27 A 441 TYR GLN PRO ALA ALA THR TYR VAL LYS GLU GLN CYS ALA
SEQRES 28 A 441 LYS GLY ALA ASN ILE ASN PHE SER PRO TYR PRO ILE ALA
SEQRES 29 A 441 GLU HIS LEU THR ALA GLU ILE PHE GLY LEU VAL PRO SER
SEQRES 30 A 441 LEU TRP PHE ILE LYS GLN ALA PHE ASP GLY THR THR PRO
SEQRES 31 A 441 LYS VAL ILE CYS GLY THR PRO ILE PRO ALA ILE ALA GLY
SEQRES 32 A 441 ILE THR THR PRO SER ALA ASP GLN VAL LEU GLY SER ASP
SEQRES 33 A 441 LEU ALA ASN GLN LEU ARG SER LEU ASN GLY LYS GLN SER
SEQRES 34 A 441 ALA PHE GLY LYS PRO PHE GLY PRO ILE THR PRO PRO
SEQRES 1 B 441 ALA PRO ALA THR GLU THR LEU ASP ARG ARG ALA ALA LEU
SEQRES 2 B 441 PRO ASN PRO TYR ASP ASP PRO PHE TYR THR THR PRO SER
SEQRES 3 B 441 ASN ILE GLY THR PHE ALA LYS GLY GLN VAL ILE GLN SER
SEQRES 4 B 441 ARG LYS VAL PRO THR ASP ILE GLY ASN ALA ASN ASN ALA
SEQRES 5 B 441 ALA SER PHE GLN LEU GLN TYR ARG THR THR ASN THR GLN
SEQRES 6 B 441 ASN GLU ALA VAL ALA ASP VAL ALA THR VAL TRP ILE PRO
SEQRES 7 B 441 ALA LYS PRO ALA SER PRO PRO LYS ILE PHE SER TYR GLN
SEQRES 8 B 441 VAL TYR GLU ASP ALA THR ALA LEU ASP CYS ALA PRO SER
SEQRES 9 B 441 TYR SER TYR LEU THR GLY LEU ASP GLN PRO ASN LYS VAL
SEQRES 10 B 441 THR ALA VAL LEU ASP THR PRO ILE ILE ILE GLY TRP ALA
SEQRES 11 B 441 LEU GLN GLN GLY TYR TYR VAL VAL SER SER ASP HIS GLU
SEQRES 12 B 441 GLY PHE LYS ALA ALA PHE ILE ALA GLY TYR GLU GLU GLY
SEQRES 13 B 441 MET ALA ILE LEU ASP GLY ILE ARG ALA LEU LYS ASN TYR
SEQRES 14 B 441 GLN ASN LEU PRO SER ASP SER LYS VAL ALA LEU GLU GLY
SEQRES 15 B 441 TYR SER GLY GLY ALA HIS ALA THR VAL TRP ALA THR SER
SEQRES 16 B 441 LEU ALA ASP SER TYR ALA PRO GLU LEU ASN ILE VAL GLY
SEQRES 17 B 441 ALA SER HIS GLY GLY THR PRO VAL SER ALA LYS ASP THR
SEQRES 18 B 441 PHE THR PHE LEU ASN GLY GLY PRO PHE ALA GLY PHE ALA
SEQRES 19 B 441 LEU ALA GLY VAL SER GLY LEU SER LEU ALA HIS PRO ASP
SEQRES 20 B 441 MET GLU SER PHE ILE GLU ALA ARG LEU ASN ALA LYS GLY
SEQRES 21 B 441 GLN GLN THR LEU LYS GLN ILE ARG GLY ARG GLY PHE CYS
SEQRES 22 B 441 LEU PRO GLN VAL VAL LEU THR TYR PRO PHE LEU ASN VAL
SEQRES 23 B 441 PHE SER LEU VAL ASN ASP THR ASN LEU LEU ASN GLU ALA
SEQRES 24 B 441 PRO ILE ALA GLY ILE LEU LYS GLN GLU THR VAL VAL GLN
SEQRES 25 B 441 ALA GLU ALA SER TYR THR VAL SER VAL PRO LYS PHE PRO
SEQRES 26 B 441 ARG PHE ILE TRP HIS ALA ILE PRO ASP GLU ILE VAL PRO
SEQRES 27 B 441 TYR GLN PRO ALA ALA THR TYR VAL LYS GLU GLN CYS ALA
SEQRES 28 B 441 LYS GLY ALA ASN ILE ASN PHE SER PRO TYR PRO ILE ALA
SEQRES 29 B 441 GLU HIS LEU THR ALA GLU ILE PHE GLY LEU VAL PRO SER
SEQRES 30 B 441 LEU TRP PHE ILE LYS GLN ALA PHE ASP GLY THR THR PRO
SEQRES 31 B 441 LYS VAL ILE CYS GLY THR PRO ILE PRO ALA ILE ALA GLY
SEQRES 32 B 441 ILE THR THR PRO SER ALA ASP GLN VAL LEU GLY SER ASP
SEQRES 33 B 441 LEU ALA ASN GLN LEU ARG SER LEU ASN GLY LYS GLN SER
SEQRES 34 B 441 ALA PHE GLY LYS PRO PHE GLY PRO ILE THR PRO PRO
HET IUM A1441 1
HET IUM A1442 1
HET IUM B1441 1
HET IUM B1442 1
HET PG4 A1443 13
HET GOL B1443 6
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM GOL GLYCEROL
HETNAM IUM URANYL (VI) ION
FORMUL 3 PG4 C8 H18 O5
FORMUL 4 GOL C3 H8 O3
FORMUL 5 IUM 4(O2 U 2+)
FORMUL 6 HOH *466(H2 O1)
HELIX 1 1 ASP A 45 ASN A 50 1 6
HELIX 2 2 ASP A 122 GLN A 133 1 12
HELIX 3 3 ALA A 151 GLN A 170 1 20
HELIX 4 4 GLY A 185 ALA A 197 1 13
HELIX 5 5 SER A 217 ASN A 226 1 10
HELIX 6 6 ALA A 231 HIS A 245 1 15
HELIX 7 7 PRO A 246 ARG A 255 1 10
HELIX 8 8 ASN A 257 ARG A 268 1 12
HELIX 9 9 CYS A 273 THR A 280 1 8
HELIX 10 10 PRO A 300 GLU A 308 1 9
HELIX 11 11 TYR A 339 LYS A 352 1 14
HELIX 12 12 GLU A 365 ASP A 386 1 22
HELIX 13 13 SER A 408 LEU A 413 1 6
HELIX 14 14 GLY A 414 SER A 423 1 10
HELIX 15 15 ASP B 45 ASN B 50 1 6
HELIX 16 16 ASP B 122 GLN B 133 1 12
HELIX 17 17 ALA B 151 GLN B 170 1 20
HELIX 18 18 GLY B 185 ALA B 197 1 13
HELIX 19 19 SER B 217 ASN B 226 1 10
HELIX 20 20 ALA B 231 HIS B 245 1 15
HELIX 21 21 PRO B 246 ARG B 255 1 10
HELIX 22 22 ASN B 257 ARG B 268 1 12
HELIX 23 23 CYS B 273 THR B 280 1 8
HELIX 24 24 PRO B 300 GLU B 308 1 9
HELIX 25 25 TYR B 339 LYS B 352 1 14
HELIX 26 26 GLU B 365 ASP B 386 1 22
HELIX 27 27 SER B 408 LEU B 413 1 6
HELIX 28 28 GLY B 414 SER B 423 1 10
SHEET 1 AA 9 VAL A 36 VAL A 42 0
SHEET 2 AA 9 ALA A 53 ASN A 63 -1 O SER A 54 N VAL A 42
SHEET 3 AA 9 ASN A 66 ILE A 77 -1 N ASN A 66 O ASN A 63
SHEET 4 AA 9 PRO A 85 GLN A 91 1 O LYS A 86 N TYR A 136
SHEET 5 AA 9 TYR A 136 ASP A 141 -1 N VAL A 137 O TRP A 76
SHEET 6 AA 9 LYS A 177 TYR A 183 1 O LYS A 177 N ILE A 87
SHEET 7 AA 9 VAL A 207 GLY A 213 1 N VAL A 207 O VAL A 178
SHEET 8 AA 9 PRO A 325 ILE A 332 1 N PHE A 327 O ALA A 209
SHEET 9 AA 9 ASN A 355 TYR A 361 1 O ASN A 355 N ARG A 326
SHEET 1 AB 2 GLY A 426 SER A 429 0
SHEET 2 AB 2 GLY A 432 PHE A 435 -1 O LYS A 433 N SER A 429
SHEET 1 BA 9 GLN A 35 VAL A 42 0
SHEET 2 BA 9 ALA A 53 ASN A 63 -1 O SER A 54 N VAL A 42
SHEET 3 BA 9 ASN A 66 ILE A 77 -1 N ASN A 66 O ASN A 63
SHEET 4 BA 9 PRO A 85 GLN A 91 1 O LYS A 86 N TYR A 136
SHEET 5 BA 9 TYR A 136 ASP A 141 -1 N VAL A 137 O TRP A 76
SHEET 6 BA 9 LYS A 177 TYR A 183 1 O LYS A 177 N ILE A 87
SHEET 7 BA 9 VAL A 207 GLY A 213 1 N VAL A 207 O VAL A 178
SHEET 8 BA 9 PRO A 325 ILE A 332 1 N PHE A 327 O ALA A 209
SHEET 9 BA 9 ASN A 355 TYR A 361 1 O ASN A 355 N ARG A 326
SHEET 1 BB 2 GLY A 426 SER A 429 0
SHEET 2 BB 2 GLY A 432 PHE A 435 -1 O LYS A 433 N SER A 429
SSBOND 1 CYS A 101 CYS A 273 1555 1555 2.03
SSBOND 2 CYS A 350 CYS A 394 1555 1555 2.03
SSBOND 3 CYS B 101 CYS B 273 1555 1555 2.03
SSBOND 4 CYS B 350 CYS B 394 1555 1555 2.04
CISPEP 1 SER A 83 PRO A 84 0 -0.60
CISPEP 2 ALA A 299 PRO A 300 0 2.40
CISPEP 3 SER B 83 PRO B 84 0 -1.70
CISPEP 4 ALA B 299 PRO B 300 0 1.49
SITE 1 AC1 2 ASP A 292 GLU A 298
SITE 1 AC2 2 ASP A 220 GLU A 314
SITE 1 AC3 2 ASP B 292 GLU B 298
SITE 1 AC4 2 ASP B 220 GLU B 314
SITE 1 AC5 8 ASP A 95 PHE A 149 SER A 184 ALA A 218
SITE 2 AC5 8 THR A 221 PHE A 222 PHE A 233 GLY A 237
SITE 1 AC6 6 ASP B 95 PHE B 149 SER B 184 GLY B 185
SITE 2 AC6 6 THR B 221 PHE B 431
CRYST1 91.539 91.539 299.842 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 0.010924 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010924 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003335 0.00000
MTRIX1 1 -0.702500 -0.706800 0.083700 80.88880 1
MTRIX2 1 0.702700 -0.707400 -0.076100 -27.22560 1
MTRIX3 1 0.113000 0.005300 0.993600 32.11400 1
TER 3253 PRO A 440
TER 6506 PRO B 440
MASTER 356 0 6 28 22 0 8 9 6993 2 27 68
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