HEADER SIGNALING PROTEIN 31-OCT-07 3B7N
TITLE CRYSTAL STRUCTURE OF YEAST SEC14 HOMOLOG SFH1 IN COMPLEX WITH
TITLE 2 PHOSPHATIDYLINOSITOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN YKL091C;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 STRAIN: BY4741;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS (DE3)-RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28-SFH1
KEYWDS SEC14, GOLGI, PHOSPHOLIPID, PHOSPHATIDYLINOSITOL, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.A.ORTLUND,G.SCHAAF,M.R.REDINBO,V.BANKAITIS
REVDAT 5 21-FEB-24 3B7N 1 REMARK SEQADV
REVDAT 4 14-FEB-18 3B7N 1 REMARK
REVDAT 3 25-OCT-17 3B7N 1 REMARK
REVDAT 2 24-FEB-09 3B7N 1 VERSN
REVDAT 1 19-FEB-08 3B7N 0
JRNL AUTH G.SCHAAF,E.A.ORTLUND,K.R.TYERYAR,C.J.MOUSLEY,K.E.ILE,
JRNL AUTH 2 T.A.GARRETT,J.REN,M.J.WOOLLS,C.R.RAETZ,M.R.REDINBO,
JRNL AUTH 3 V.A.BANKAITIS
JRNL TITL FUNCTIONAL ANATOMY OF PHOSPHOLIPID BINDING AND REGULATION OF
JRNL TITL 2 PHOSPHOINOSITIDE HOMEOSTASIS BY PROTEINS OF THE SEC14
JRNL TITL 3 SUPERFAMILY
JRNL REF MOL.CELL V. 29 191 2008
JRNL REFN ISSN 1097-2765
JRNL PMID 18243114
JRNL DOI 10.1016/J.MOLCEL.2007.11.026
REMARK 2
REMARK 2 RESOLUTION. 1.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 166573.609
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 27304
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 SET) : 0.191
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1888
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.86
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3918
REMARK 3 BIN R VALUE (WORKING SET) : 0.2410
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 280
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2522
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 73
REMARK 3 SOLVENT ATOMS : 265
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.85000
REMARK 3 B22 (A**2) : -3.77000
REMARK 3 B33 (A**2) : 1.92000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.15
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.800
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 37.90
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ACT.PAR
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : PI_18_1.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : PI_18_1.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3B7N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000045180.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28130
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.36700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-25% PEG 3350, 5% GLYCEROL, AND
REMARK 280 EITHER 100 MM AMMONIUM SULFATE OR 100MM POTASSIUM PHOSPHATE, 100
REMARK 280 MM AMMONIUM ACETATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 25.07900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.58850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.70350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.58850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.07900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.70350
REMARK 290 SMTRY3 4 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 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 MET A -9
REMARK 465 GLY A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 THR A 3
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 LYS A 46 -43.75 -133.57
REMARK 500 ASN A 94 36.02 -149.01
REMARK 500 HIS A 115 -147.56 63.87
REMARK 500 ASP A 283 64.00 -154.84
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 PO4 A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B7N A 314
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3B74 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF YEAST SEC14 HOMOLOG SFH1 IN COMPLEX WITH
REMARK 900 PHOSPHATIDYLETHANOLAMINE
REMARK 900 RELATED ID: 3B7Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF YEAST SEC14 HOMOLOG SFH1 IN COMPLEX WITH
REMARK 900 PHOSPHATIDYLCHOLINE
REMARK 900 RELATED ID: 3B7Z RELATED DB: PDB
DBREF 3B7N A 1 310 UNP P33324 YKJ1_YEAST 1 310
SEQADV 3B7N MET A -9 UNP P33324 EXPRESSION TAG
SEQADV 3B7N GLY A -8 UNP P33324 EXPRESSION TAG
SEQADV 3B7N HIS A -7 UNP P33324 EXPRESSION TAG
SEQADV 3B7N HIS A -6 UNP P33324 EXPRESSION TAG
SEQADV 3B7N HIS A -5 UNP P33324 EXPRESSION TAG
SEQADV 3B7N HIS A -4 UNP P33324 EXPRESSION TAG
SEQADV 3B7N HIS A -3 UNP P33324 EXPRESSION TAG
SEQADV 3B7N HIS A -2 UNP P33324 EXPRESSION TAG
SEQADV 3B7N HIS A -1 UNP P33324 EXPRESSION TAG
SEQADV 3B7N HIS A 0 UNP P33324 EXPRESSION TAG
SEQRES 1 A 320 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS MET THR THR
SEQRES 2 A 320 SER ILE LEU ASP THR TYR PRO GLN ILE CYS SER PRO ASN
SEQRES 3 A 320 ALA LEU PRO GLY THR PRO GLY ASN LEU THR LYS GLU GLN
SEQRES 4 A 320 GLU GLU ALA LEU LEU GLN PHE ARG SER ILE LEU LEU GLU
SEQRES 5 A 320 LYS ASN TYR LYS GLU ARG LEU ASP ASP SER THR LEU LEU
SEQRES 6 A 320 ARG PHE LEU ARG ALA ARG LYS PHE ASP ILE ASN ALA SER
SEQRES 7 A 320 VAL GLU MET PHE VAL GLU THR GLU ARG TRP ARG GLU GLU
SEQRES 8 A 320 TYR GLY ALA ASN THR ILE ILE GLU ASP TYR GLU ASN ASN
SEQRES 9 A 320 LYS GLU ALA GLU ASP LYS GLU ARG ILE LYS LEU ALA LYS
SEQRES 10 A 320 MET TYR PRO GLN TYR TYR HIS HIS VAL ASP LYS ASP GLY
SEQRES 11 A 320 ARG PRO LEU TYR PHE GLU GLU LEU GLY GLY ILE ASN LEU
SEQRES 12 A 320 LYS LYS MET TYR LYS ILE THR THR GLU LYS GLN MET LEU
SEQRES 13 A 320 ARG ASN LEU VAL LYS GLU TYR GLU LEU PHE ALA THR TYR
SEQRES 14 A 320 ARG VAL PRO ALA CYS SER ARG ARG ALA GLY TYR LEU ILE
SEQRES 15 A 320 GLU THR SER CYS THR VAL LEU ASP LEU LYS GLY ILE SER
SEQRES 16 A 320 LEU SER ASN ALA TYR HIS VAL LEU SER TYR ILE LYS ASP
SEQRES 17 A 320 VAL ALA ASP ILE SER GLN ASN TYR TYR PRO GLU ARG MET
SEQRES 18 A 320 GLY LYS PHE TYR ILE ILE HIS SER PRO PHE GLY PHE SER
SEQRES 19 A 320 THR MET PHE LYS MET VAL LYS PRO PHE LEU ASP PRO VAL
SEQRES 20 A 320 THR VAL SER LYS ILE PHE ILE LEU GLY SER SER TYR LYS
SEQRES 21 A 320 LYS GLU LEU LEU LYS GLN ILE PRO ILE GLU ASN LEU PRO
SEQRES 22 A 320 VAL LYS TYR GLY GLY THR SER VAL LEU HIS ASN PRO ASN
SEQRES 23 A 320 ASP LYS PHE TYR TYR SER ASP ILE GLY PRO TRP ARG ASP
SEQRES 24 A 320 PRO ARG TYR ILE GLY PRO GLU GLY GLU ILE PRO ASN ILE
SEQRES 25 A 320 PHE GLY LYS PHE THR VAL THR SER
HET PO4 A 311 5
HET PO4 A 312 5
HET ACT A 313 4
HET B7N A 314 59
HETNAM PO4 PHOSPHATE ION
HETNAM ACT ACETATE ION
HETNAM B7N (1R)-2-{[(S)-HYDROXY{[(1S,2R,3R,4S,5S,6R)-2,3,4,5,6-
HETNAM 2 B7N PENTAHYDROXYCYCLOHEXYL]OXY}PHOSPHORYL]OXY}-1-
HETNAM 3 B7N [(OCTADECANOYLOXY)METHYL]ETHYL (9Z)-OCTADEC-9-ENOATE
FORMUL 2 PO4 2(O4 P 3-)
FORMUL 4 ACT C2 H3 O2 1-
FORMUL 5 B7N C45 H85 O13 P
FORMUL 6 HOH *265(H2 O)
HELIX 1 1 SER A 4 TYR A 9 5 6
HELIX 2 2 THR A 26 LYS A 43 1 18
HELIX 3 3 ASP A 50 ARG A 61 1 12
HELIX 4 4 ASP A 64 TYR A 82 1 19
HELIX 5 5 THR A 86 ASN A 93 1 8
HELIX 6 6 ASN A 94 LYS A 107 1 14
HELIX 7 7 ASN A 132 TYR A 137 1 6
HELIX 8 8 THR A 141 TYR A 159 1 19
HELIX 9 9 TYR A 159 GLY A 169 1 11
HELIX 10 10 SER A 185 VAL A 192 1 8
HELIX 11 11 VAL A 192 TYR A 207 1 16
HELIX 12 12 GLY A 222 LYS A 228 1 7
HELIX 13 13 MET A 229 LEU A 234 5 6
HELIX 14 14 ASP A 235 SER A 240 1 6
HELIX 15 15 SER A 248 LEU A 254 1 7
HELIX 16 16 PRO A 263 GLY A 267 5 5
HELIX 17 17 LYS A 278 SER A 282 5 5
HELIX 18 18 GLY A 285 ASP A 289 5 5
HELIX 19 19 PHE A 303 THR A 307 5 5
SHEET 1 A 5 GLN A 111 VAL A 116 0
SHEET 2 A 5 PRO A 122 GLU A 127 -1 O PHE A 125 N TYR A 112
SHEET 3 A 5 SER A 175 ASP A 180 1 O ASP A 180 N GLU A 126
SHEET 4 A 5 MET A 211 ILE A 217 1 O TYR A 215 N LEU A 179
SHEET 5 A 5 ILE A 242 ILE A 244 1 O PHE A 243 N PHE A 214
SITE 1 AC1 9 LEU A 245 GLY A 246 SER A 248 VAL A 271
SITE 2 AC1 9 HIS A 273 HOH A 349 HOH A 398 HOH A 434
SITE 3 AC1 9 HOH A 491
SITE 1 AC2 8 HIS A 115 LYS A 250 GLY A 285 PRO A 286
SITE 2 AC2 8 HOH A 427 HOH A 492 HOH A 533 HOH A 579
SITE 1 AC3 5 HIS A 218 TYR A 249 LYS A 250 HOH A 427
SITE 2 AC3 5 HOH A 462
SITE 1 AC4 33 ALA A 60 ARG A 61 MET A 71 TYR A 109
SITE 2 AC4 33 GLU A 126 LEU A 128 ILE A 131 MET A 136
SITE 3 AC4 33 MET A 145 TYR A 153 ALA A 189 VAL A 192
SITE 4 AC4 33 TYR A 195 ILE A 196 SER A 203 GLN A 204
SITE 5 AC4 33 TYR A 207 PRO A 208 GLU A 209 ARG A 210
SITE 6 AC4 33 MET A 211 PHE A 223 LEU A 234 ASP A 235
SITE 7 AC4 33 VAL A 237 THR A 238 LYS A 241 HOH A 358
SITE 8 AC4 33 HOH A 368 HOH A 373 HOH A 379 HOH A 440
SITE 9 AC4 33 HOH A 578
CRYST1 50.158 71.407 91.177 90.00 90.00 90.00 P 21 21 21 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 0.019937 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014004 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010968 0.00000
(ATOM LINES ARE NOT SHOWN.)
END