HEADER METAL TRANSPORT 01-DEC-10 3PSA
TITLE CLASSIFICATION OF A HAEMOPHILUS INFLUENZAE ABC TRANSPORTER HI1470/71
TITLE 2 THROUGH ITS COGNATE MOLYBDATE PERIPLASMIC BINDING PROTEIN MOLA (MOLA
TITLE 3 BOUND TO TUNGSTATE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN HI_1472;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 22-347;
COMPND 5 SYNONYM: PERIPLASMIC BINDING PROTEIN MOLA;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;
SOURCE 3 ORGANISM_TAXID: 727;
SOURCE 4 GENE: HI_1472;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PERIPLASMIC BINDING PROTEIN, SUBSTRATE BINDING PROTEIN, OXYANION
KEYWDS 2 BINDING PROTEIN, METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR L.TIRADO-LEE,A.LEE,D.C.REES,H.W.PINKETT
REVDAT 3 21-FEB-24 3PSA 1 REMARK
REVDAT 2 08-NOV-17 3PSA 1 REMARK
REVDAT 1 30-NOV-11 3PSA 0
JRNL AUTH L.TIRADO-LEE,A.LEE,D.C.REES,H.W.PINKETT
JRNL TITL CLASSIFICATION OF A HAEMOPHILUS INFLUENZAE ABC TRANSPORTER
JRNL TITL 2 HI1470/71 THROUGH ITS COGNATE MOLYBDATE PERIPLASMIC BINDING
JRNL TITL 3 PROTEIN, MOLA.
JRNL REF STRUCTURE V. 19 1701 2011
JRNL REFN ISSN 0969-2126
JRNL PMID 22078568
JRNL DOI 10.1016/J.STR.2011.10.004
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 99137
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) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4868
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) : 1.69
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6547
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.40
REMARK 3 BIN R VALUE (WORKING SET) : 0.2300
REMARK 3 BIN FREE R VALUE SET COUNT : 332
REMARK 3 BIN FREE R VALUE : 0.2490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2578
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 139
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.13000
REMARK 3 B22 (A**2) : 0.13000
REMARK 3 B33 (A**2) : -0.25000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.015
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.063
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.024
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.898
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.888
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2638 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3582 ; 1.555 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 327 ; 5.349 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 122 ;35.110 ;25.574
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 471 ;13.041 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;10.867 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 403 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1985 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1629 ; 0.819 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2632 ; 1.296 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1009 ; 2.320 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 949 ; 3.388 ; 4.500
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 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.511
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -H,-K,L
REMARK 3 TWIN FRACTION : 0.489
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 RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3PSA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000062755.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-OCT-10; NULL
REMARK 200 TEMPERATURE (KELVIN) : 100; NULL
REMARK 200 PH : 4.5
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 : 21-ID-F; 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856; 1.2143
REMARK 200 MONOCHROMATOR : KOHZU; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; NULL
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 99140
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.000
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.34800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 79.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG2000 MME, 0.1 M SODIUM ACETATE,
REMARK 280 0.2 M AMMONIUM SULFATE, 12% GLYCEROL, PH 4.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 34.40500
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 68.81000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 68.81000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 34.40500
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 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: 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 SD MET A 89 O HOH A 415 1.72
REMARK 500 O ALA A 58 O HOH A 463 2.06
REMARK 500 O1 WO4 A 770 O HOH A 461 2.11
REMARK 500 O HOH A 5 O HOH A 365 2.12
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 LEU A 45 40.73 -98.96
REMARK 500 ASN A 68 30.36 -97.61
REMARK 500 ASP A 92 -152.80 -143.73
REMARK 500 THR A 137 -110.05 -91.08
REMARK 500 TYR A 265 57.32 -116.73
REMARK 500 LYS A 288 57.35 -116.74
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 WO4 A 770
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PSH RELATED DB: PDB
REMARK 900 HI1470/71 WITHOUT TUNGSTATE
DBREF 3PSA A 22 347 UNP P44206 Y1472_HAEIN 22 347
SEQRES 1 A 326 ASP ARG ILE ILE THR ASP GLN LEU ASP ARG LYS VAL THR
SEQRES 2 A 326 ILE PRO ASP HIS ILE ASN ARG ALA VAL VAL LEU GLN HIS
SEQRES 3 A 326 GLN THR LEU ASN ILE ALA VAL GLN LEU ASP ALA THR LYS
SEQRES 4 A 326 GLN ILE VAL GLY VAL LEU SER ASN TRP LYS LYS GLN LEU
SEQRES 5 A 326 GLY LYS ASN TYR VAL ARG LEU ALA PRO GLU LEU GLU ASN
SEQRES 6 A 326 MET ALA MET PRO GLY ASP LEU ASN SER VAL ASN ILE GLU
SEQRES 7 A 326 SER LEU LEU ALA LEU LYS PRO ASP VAL VAL PHE VAL THR
SEQRES 8 A 326 ASN TYR ALA PRO SER GLU MET ILE LYS GLN ILE SER ASP
SEQRES 9 A 326 VAL ASN ILE PRO VAL VAL ALA ILE SER LEU ARG THR GLY
SEQRES 10 A 326 GLU VAL GLY GLU LYS GLY LYS LEU ASN PRO THR LEU THR
SEQRES 11 A 326 ASP GLU ASP LYS ALA TYR ASN ASP GLY LEU LYS GLN GLY
SEQRES 12 A 326 ILE GLU LEU ILE ALA GLU VAL PHE GLU LYS LYS GLN GLN
SEQRES 13 A 326 GLY ASP GLU LEU VAL LYS ALA ALA PHE ALA ASN ARG LYS
SEQRES 14 A 326 LEU LEU ALA ASP ARG LEU GLY ASP VAL SER ALA ASP LYS
SEQRES 15 A 326 ARG VAL ARG THR TYR MET ALA ASN PRO ASP LEU GLY THR
SEQRES 16 A 326 TYR GLY SER GLY LYS TYR THR GLY LEU MET MET GLU HIS
SEQRES 17 A 326 ALA GLY ALA TYR ASN VAL ALA ALA ALA THR ILE LYS GLY
SEQRES 18 A 326 PHE LYS GLN VAL SER LEU GLU ASN VAL LEU GLU TRP ASN
SEQRES 19 A 326 PRO ALA VAL ILE LEU VAL GLN ASP ARG TYR PRO ASP VAL
SEQRES 20 A 326 VAL PRO GLN ILE LEU ASN ASP GLN GLY TRP ALA ASN ILE
SEQRES 21 A 326 GLN ALA LEU LYS ASP LYS LYS VAL PHE LEU MET PRO GLU
SEQRES 22 A 326 TYR ALA LYS ALA TRP GLY TYR PRO MET PRO GLU ALA LEU
SEQRES 23 A 326 ALA LEU GLY GLU VAL TRP LEU ALA LYS ALA LEU TYR PRO
SEQRES 24 A 326 GLN ARG PHE GLN ASP VAL ASP LEU ASP LYS MET VAL ASN
SEQRES 25 A 326 ASP TYR TYR GLN LYS PHE TYR ARG THR SER TYR LYS PRO
SEQRES 26 A 326 ASP
HET WO4 A 770 5
HETNAM WO4 TUNGSTATE(VI)ION
FORMUL 2 WO4 O4 W 2-
FORMUL 3 HOH *139(H2 O)
HELIX 1 1 GLN A 46 LEU A 56 1 11
HELIX 2 2 ASP A 57 LYS A 60 5 4
HELIX 3 3 ASN A 68 GLY A 74 1 7
HELIX 4 4 ASN A 76 ALA A 81 1 6
HELIX 5 5 PRO A 82 MET A 87 5 6
HELIX 6 6 ASN A 97 ALA A 103 1 7
HELIX 7 7 PRO A 116 VAL A 126 1 11
HELIX 8 8 GLU A 139 LYS A 143 5 5
HELIX 9 9 ASP A 152 GLU A 173 1 22
HELIX 10 10 LYS A 174 ALA A 187 1 14
HELIX 11 11 ASN A 188 LEU A 196 1 9
HELIX 12 12 LYS A 221 ALA A 230 1 10
HELIX 13 13 ALA A 236 THR A 239 5 4
HELIX 14 14 SER A 247 ASN A 255 1 9
HELIX 15 15 ASP A 267 ASN A 274 1 8
HELIX 16 16 ASP A 275 ALA A 279 5 5
HELIX 17 17 ILE A 281 ASP A 286 1 6
HELIX 18 18 MET A 303 LEU A 309 1 7
HELIX 19 19 LEU A 309 TYR A 319 1 11
HELIX 20 20 PRO A 320 PHE A 323 5 4
HELIX 21 21 ASP A 327 TYR A 340 1 14
SHEET 1 A 2 ARG A 23 THR A 26 0
SHEET 2 A 2 LYS A 32 ILE A 35 -1 O ILE A 35 N ARG A 23
SHEET 1 B 4 ILE A 62 VAL A 65 0
SHEET 2 B 4 ALA A 42 LEU A 45 1 N ALA A 42 O VAL A 63
SHEET 3 B 4 VAL A 108 THR A 112 1 O PHE A 110 N LEU A 45
SHEET 4 B 4 VAL A 130 ILE A 133 1 O VAL A 131 N VAL A 109
SHEET 1 C 4 ALA A 232 ASN A 234 0
SHEET 2 C 4 VAL A 205 MET A 209 1 N THR A 207 O TYR A 233
SHEET 3 C 4 VAL A 258 VAL A 261 1 O LEU A 260 N TYR A 208
SHEET 4 C 4 VAL A 289 LEU A 291 1 O PHE A 290 N ILE A 259
SHEET 1 D 2 GLY A 215 TYR A 217 0
SHEET 2 D 2 PHE A 243 GLN A 245 -1 O LYS A 244 N THR A 216
SITE 1 AC1 9 HIS A 47 GLN A 48 TYR A 217 ARG A 264
SITE 2 AC1 9 TRP A 299 GLY A 300 TYR A 301 HOH A 460
SITE 3 AC1 9 HOH A 461
CRYST1 122.711 122.711 103.215 90.00 90.00 120.00 P 31 2 1 6
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 0.008149 0.004705 0.000000 0.00000
SCALE2 0.000000 0.009410 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009689 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
