HEADER TRANSPORT PROTEIN 19-JUL-12 4B2Z
TITLE STRUCTURE OF OSH6 IN COMPLEX WITH PHOSPHATIDYLSERINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OXYSTEROL-BINDING PROTEIN HOMOLOG 6;
COMPND 3 CHAIN: A, B;
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 GENE: OSH6, YKR003W, YK102;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: STAR
KEYWDS TRANSPORT PROTEIN, LIPID TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR K.MAEDA,K.ANAND,A.CHIAPPARINO,A.KUMAR,M.POLETTO,M.KAKSONEN,A.C.GAVIN
REVDAT 6 20-DEC-23 4B2Z 1 REMARK
REVDAT 5 12-DEC-18 4B2Z 1 COMPND SOURCE REMARK DBREF
REVDAT 4 18-SEP-13 4B2Z 1 JRNL
REVDAT 3 21-AUG-13 4B2Z 1 JRNL
REVDAT 2 07-AUG-13 4B2Z 1 JRNL
REVDAT 1 26-JUN-13 4B2Z 0
JRNL AUTH K.MAEDA,K.ANAND,A.CHIAPPARINO,A.KUMAR,M.POLETTO,M.KAKSONEN,
JRNL AUTH 2 A.C.GAVIN
JRNL TITL INTERACTOME MAP UNCOVERS PHOSPHATIDYLSERINE TRANSPORT BY
JRNL TITL 2 OXYSTEROL-BINDING PROTEINS
JRNL REF NATURE V. 501 257 2013
JRNL REFN ISSN 0028-0836
JRNL PMID 23934110
JRNL DOI 10.1038/NATURE12430
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.57
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 3 NUMBER OF REFLECTIONS : 65887
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1318
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 46.5794 - 4.0554 1.00 7963 163 0.1821 0.2176
REMARK 3 2 4.0554 - 3.2191 1.00 7842 160 0.1740 0.2021
REMARK 3 3 3.2191 - 2.8123 1.00 7790 159 0.1904 0.2044
REMARK 3 4 2.8123 - 2.5552 1.00 7837 160 0.2010 0.2588
REMARK 3 5 2.5552 - 2.3720 1.00 7781 159 0.2031 0.2528
REMARK 3 6 2.3720 - 2.2322 1.00 7741 158 0.2011 0.2441
REMARK 3 7 2.2322 - 2.1204 0.93 7220 147 0.2085 0.2630
REMARK 3 8 2.1204 - 2.0281 0.74 5743 117 0.2201 0.3137
REMARK 3 9 2.0281 - 1.9500 0.60 4652 95 0.2534 0.3029
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 31.39
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.760
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.18600
REMARK 3 B22 (A**2) : -2.96460
REMARK 3 B33 (A**2) : 7.15060
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -4.30050
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 6832
REMARK 3 ANGLE : 1.219 9216
REMARK 3 CHIRALITY : 0.095 963
REMARK 3 PLANARITY : 0.006 1183
REMARK 3 DIHEDRAL : 19.982 2662
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9179 -17.9992 30.9626
REMARK 3 T TENSOR
REMARK 3 T11: 0.0798 T22: 0.1168
REMARK 3 T33: 0.0765 T12: -0.0099
REMARK 3 T13: -0.0147 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.5846 L22: 0.3148
REMARK 3 L33: 0.5060 L12: 0.0597
REMARK 3 L13: -0.0103 L23: -0.0990
REMARK 3 S TENSOR
REMARK 3 S11: 0.0117 S12: 0.1578 S13: 0.0427
REMARK 3 S21: -0.0134 S22: 0.0409 S23: 0.0140
REMARK 3 S31: 0.0467 S32: 0.0334 S33: -0.0442
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 36:191 OR RESSEQ
REMARK 3 193:218 OR RESSEQ 223:259 OR RESSEQ 261:
REMARK 3 270 OR RESSEQ 272:320 OR RESSEQ 326:381
REMARK 3 OR RESSEQ 385:396 )
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 35:191 OR RESSEQ
REMARK 3 193:218 OR RESSEQ 223:259 OR RESSEQ 261:
REMARK 3 270 OR RESSEQ 272:320 OR RESSEQ 326:381
REMARK 3 OR RESSEQ 385:396 )
REMARK 3 ATOM PAIRS NUMBER : 2839
REMARK 3 RMSD : 0.057
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4B2Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1290053401.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 5
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93340
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65896
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.630
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.0000
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 (%) : 59.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.65000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
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: PDB ENTRY 1ZHT
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH6.5, 13% PEG6000, 5% MPD
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 60.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.30000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 60.00000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.30000
REMARK 290 SMTRY3 4 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 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 MET A 1
REMARK 465 GLY A 2
REMARK 465 SER A 3
REMARK 465 LYS A 4
REMARK 465 LYS A 5
REMARK 465 LEU A 6
REMARK 465 THR A 7
REMARK 465 VAL A 8
REMARK 465 GLY A 9
REMARK 465 SER A 10
REMARK 465 ASP A 11
REMARK 465 SER A 12
REMARK 465 HIS A 13
REMARK 465 ARG A 14
REMARK 465 LEU A 15
REMARK 465 SER A 16
REMARK 465 LYS A 17
REMARK 465 SER A 18
REMARK 465 SER A 19
REMARK 465 PHE A 20
REMARK 465 SER A 21
REMARK 465 SER A 22
REMARK 465 ASN A 23
REMARK 465 LYS A 24
REMARK 465 SER A 25
REMARK 465 SER A 26
REMARK 465 HIS A 27
REMARK 465 SER A 28
REMARK 465 ALA A 29
REMARK 465 THR A 30
REMARK 465 LYS A 31
REMARK 465 ASP A 32
REMARK 465 GLN A 33
REMARK 465 PRO A 34
REMARK 465 ILE A 35
REMARK 465 LYS A 435
REMARK 465 LYS A 436
REMARK 465 MET A 437
REMARK 465 ILE A 438
REMARK 465 GLU A 439
REMARK 465 ASN A 440
REMARK 465 GLU A 441
REMARK 465 LYS A 442
REMARK 465 GLN A 443
REMARK 465 ASN A 444
REMARK 465 PRO A 445
REMARK 465 ALA A 446
REMARK 465 LYS A 447
REMARK 465 GLN A 448
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 SER B 3
REMARK 465 LYS B 4
REMARK 465 LYS B 5
REMARK 465 LEU B 6
REMARK 465 THR B 7
REMARK 465 VAL B 8
REMARK 465 GLY B 9
REMARK 465 SER B 10
REMARK 465 ASP B 11
REMARK 465 SER B 12
REMARK 465 HIS B 13
REMARK 465 ARG B 14
REMARK 465 LEU B 15
REMARK 465 SER B 16
REMARK 465 LYS B 17
REMARK 465 SER B 18
REMARK 465 SER B 19
REMARK 465 PHE B 20
REMARK 465 SER B 21
REMARK 465 SER B 22
REMARK 465 ASN B 23
REMARK 465 LYS B 24
REMARK 465 SER B 25
REMARK 465 SER B 26
REMARK 465 HIS B 27
REMARK 465 SER B 28
REMARK 465 ALA B 29
REMARK 465 THR B 30
REMARK 465 LYS B 31
REMARK 465 ASP B 32
REMARK 465 GLN B 33
REMARK 465 PRO B 34
REMARK 465 LYS B 435
REMARK 465 LYS B 436
REMARK 465 MET B 437
REMARK 465 ILE B 438
REMARK 465 GLU B 439
REMARK 465 ASN B 440
REMARK 465 GLU B 441
REMARK 465 LYS B 442
REMARK 465 GLN B 443
REMARK 465 ASN B 444
REMARK 465 PRO B 445
REMARK 465 ALA B 446
REMARK 465 LYS B 447
REMARK 465 GLN B 448
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ILE B 35 CG1 CG2 CD1
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LEU A 52 CB CG CD1 CD2
REMARK 480 GLN A 57 CG CD OE1 NE2
REMARK 480 ARG A 59 CB CG CD NE CZ NH1 NH2
REMARK 480 PHE B 229 CB CG CD1 CD2 CE1 CE2 CZ
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 GLY B 237 O HOH B 2113 2.08
REMARK 500 O HOH A 2010 O HOH A 2022 2.16
REMARK 500 O GLY B 237 O PHE B 253 2.19
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 O HOH B 2011 O HOH B 2195 4556 2.16
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 TYR A 258 N - CA - C ANGL. DEV. = 16.4 DEGREES
REMARK 500 VAL A 259 CB - CA - C ANGL. DEV. = -12.6 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 LYS A 76 47.52 -89.00
REMARK 500 LEU A 228 -63.47 -101.18
REMARK 500 ASP A 238 -114.44 -113.18
REMARK 500 PHE A 260 64.88 -100.58
REMARK 500 ASP A 287 -106.27 -140.36
REMARK 500 ARG A 318 150.38 -45.63
REMARK 500 LYS B 76 47.21 -88.91
REMARK 500 LEU B 228 -64.91 -100.22
REMARK 500 ASP B 238 -115.91 -112.90
REMARK 500 PHE B 260 -0.84 75.15
REMARK 500 ASP B 287 -109.15 -142.06
REMARK 500 ARG B 318 150.48 -46.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 257 TYR A 258 80.73
REMARK 500 GLY B 257 TYR B 258 130.70
REMARK 500 PHE B 260 GLY B 261 132.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 P5S A 1436
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 1435
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1435
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P5S A 1436
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P5S B 1436
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTU A 1437
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT B 1437
DBREF 4B2Z A 1 448 UNP Q02201 OSH6_YEAST 1 448
DBREF 4B2Z B 1 448 UNP Q02201 OSH6_YEAST 1 448
SEQRES 1 A 448 MET GLY SER LYS LYS LEU THR VAL GLY SER ASP SER HIS
SEQRES 2 A 448 ARG LEU SER LYS SER SER PHE SER SER ASN LYS SER SER
SEQRES 3 A 448 HIS SER ALA THR LYS ASP GLN PRO ILE ASP THR ASP ASP
SEQRES 4 A 448 ILE ASP GLU ASP ASP GLU SER GLY HIS ASN ILE ILE LEU
SEQRES 5 A 448 ASN ILE ILE SER GLN LEU ARG PRO GLY CYS ASP LEU THR
SEQRES 6 A 448 ARG ILE THR LEU PRO THR PHE ILE LEU GLU LYS LYS SER
SEQRES 7 A 448 MET LEU GLU ARG VAL THR ASN GLN LEU GLN PHE PRO GLU
SEQRES 8 A 448 PHE LEU LEU GLN ALA HIS SER GLU LYS ASP PRO LEU LYS
SEQRES 9 A 448 ARG PHE LEU TYR VAL MET LYS TRP TYR LEU ALA GLY TRP
SEQRES 10 A 448 HIS ILE ALA PRO LYS ALA VAL LYS LYS PRO LEU ASN PRO
SEQRES 11 A 448 VAL LEU GLY GLU TYR PHE THR ALA TYR TRP ASP LEU PRO
SEQRES 12 A 448 ASN LYS GLN GLN ALA TYR TYR ILE SER GLU GLN THR SER
SEQRES 13 A 448 HIS HIS PRO PRO GLU CYS ALA TYR PHE TYR MET ILE PRO
SEQRES 14 A 448 GLU SER SER ILE ARG VAL ASP GLY VAL VAL ILE PRO LYS
SEQRES 15 A 448 SER ARG PHE LEU GLY ASN SER SER ALA ALA MET MET ASP
SEQRES 16 A 448 GLY SER THR VAL LEU GLN PHE LEU ASP ILE LYS ASP GLY
SEQRES 17 A 448 ASN GLY LYS PRO GLU LYS TYR VAL LEU THR GLN PRO ASN
SEQRES 18 A 448 VAL TYR VAL ARG GLY ILE LEU PHE GLY LYS MET ARG ILE
SEQRES 19 A 448 GLU LEU GLY ASP HIS MET ILE ILE LYS SER PRO ASN PHE
SEQRES 20 A 448 GLN ALA ASP ILE GLU PHE LYS THR LYS GLY TYR VAL PHE
SEQRES 21 A 448 GLY THR TYR ASP ALA ILE GLU GLY THR VAL LYS ASP TYR
SEQRES 22 A 448 ASP GLY ASN ALA TYR TYR GLU ILE SER GLY LYS TRP ASN
SEQRES 23 A 448 ASP VAL MET TYR LEU LYS ASP LEU LYS GLN PRO ARG SER
SEQRES 24 A 448 SER PRO LYS VAL PHE LEU ASP THR HIS LYS GLU SER PRO
SEQRES 25 A 448 LEU ARG PRO LYS VAL ARG PRO LEU SER GLU GLN GLY GLU
SEQRES 26 A 448 TYR GLU SER ARG LYS LEU TRP LYS LYS VAL THR ASP ALA
SEQRES 27 A 448 LEU ALA VAL ARG ASN HIS PRO VAL ALA THR GLU GLU LYS
SEQRES 28 A 448 PHE GLN ILE GLU ASP HIS GLN ARG GLN LEU ALA LYS LYS
SEQRES 29 A 448 ARG ILE GLU ASP GLY VAL GLU PHE HIS PRO LYS LEU PHE
SEQRES 30 A 448 ARG ARG SER LYS PRO GLY GLU ASP LEU ASP TYR CYS ILE
SEQRES 31 A 448 TYR LYS ASN ILE PRO VAL ASP GLU ASP PRO GLU LYS GLN
SEQRES 32 A 448 ILE ARG SER ILE LEU GLN ILE ALA PRO ILE LEU PRO GLY
SEQRES 33 A 448 GLN GLN PHE THR ASP LYS PHE PHE ILE PRO ALA PHE GLU
SEQRES 34 A 448 LYS ILE LYS SER GLN LYS LYS MET ILE GLU ASN GLU LYS
SEQRES 35 A 448 GLN ASN PRO ALA LYS GLN
SEQRES 1 B 448 MET GLY SER LYS LYS LEU THR VAL GLY SER ASP SER HIS
SEQRES 2 B 448 ARG LEU SER LYS SER SER PHE SER SER ASN LYS SER SER
SEQRES 3 B 448 HIS SER ALA THR LYS ASP GLN PRO ILE ASP THR ASP ASP
SEQRES 4 B 448 ILE ASP GLU ASP ASP GLU SER GLY HIS ASN ILE ILE LEU
SEQRES 5 B 448 ASN ILE ILE SER GLN LEU ARG PRO GLY CYS ASP LEU THR
SEQRES 6 B 448 ARG ILE THR LEU PRO THR PHE ILE LEU GLU LYS LYS SER
SEQRES 7 B 448 MET LEU GLU ARG VAL THR ASN GLN LEU GLN PHE PRO GLU
SEQRES 8 B 448 PHE LEU LEU GLN ALA HIS SER GLU LYS ASP PRO LEU LYS
SEQRES 9 B 448 ARG PHE LEU TYR VAL MET LYS TRP TYR LEU ALA GLY TRP
SEQRES 10 B 448 HIS ILE ALA PRO LYS ALA VAL LYS LYS PRO LEU ASN PRO
SEQRES 11 B 448 VAL LEU GLY GLU TYR PHE THR ALA TYR TRP ASP LEU PRO
SEQRES 12 B 448 ASN LYS GLN GLN ALA TYR TYR ILE SER GLU GLN THR SER
SEQRES 13 B 448 HIS HIS PRO PRO GLU CYS ALA TYR PHE TYR MET ILE PRO
SEQRES 14 B 448 GLU SER SER ILE ARG VAL ASP GLY VAL VAL ILE PRO LYS
SEQRES 15 B 448 SER ARG PHE LEU GLY ASN SER SER ALA ALA MET MET ASP
SEQRES 16 B 448 GLY SER THR VAL LEU GLN PHE LEU ASP ILE LYS ASP GLY
SEQRES 17 B 448 ASN GLY LYS PRO GLU LYS TYR VAL LEU THR GLN PRO ASN
SEQRES 18 B 448 VAL TYR VAL ARG GLY ILE LEU PHE GLY LYS MET ARG ILE
SEQRES 19 B 448 GLU LEU GLY ASP HIS MET ILE ILE LYS SER PRO ASN PHE
SEQRES 20 B 448 GLN ALA ASP ILE GLU PHE LYS THR LYS GLY TYR VAL PHE
SEQRES 21 B 448 GLY THR TYR ASP ALA ILE GLU GLY THR VAL LYS ASP TYR
SEQRES 22 B 448 ASP GLY ASN ALA TYR TYR GLU ILE SER GLY LYS TRP ASN
SEQRES 23 B 448 ASP VAL MET TYR LEU LYS ASP LEU LYS GLN PRO ARG SER
SEQRES 24 B 448 SER PRO LYS VAL PHE LEU ASP THR HIS LYS GLU SER PRO
SEQRES 25 B 448 LEU ARG PRO LYS VAL ARG PRO LEU SER GLU GLN GLY GLU
SEQRES 26 B 448 TYR GLU SER ARG LYS LEU TRP LYS LYS VAL THR ASP ALA
SEQRES 27 B 448 LEU ALA VAL ARG ASN HIS PRO VAL ALA THR GLU GLU LYS
SEQRES 28 B 448 PHE GLN ILE GLU ASP HIS GLN ARG GLN LEU ALA LYS LYS
SEQRES 29 B 448 ARG ILE GLU ASP GLY VAL GLU PHE HIS PRO LYS LEU PHE
SEQRES 30 B 448 ARG ARG SER LYS PRO GLY GLU ASP LEU ASP TYR CYS ILE
SEQRES 31 B 448 TYR LYS ASN ILE PRO VAL ASP GLU ASP PRO GLU LYS GLN
SEQRES 32 B 448 ILE ARG SER ILE LEU GLN ILE ALA PRO ILE LEU PRO GLY
SEQRES 33 B 448 GLN GLN PHE THR ASP LYS PHE PHE ILE PRO ALA PHE GLU
SEQRES 34 B 448 LYS ILE LYS SER GLN LYS LYS MET ILE GLU ASN GLU LYS
SEQRES 35 B 448 GLN ASN PRO ALA LYS GLN
HET SO4 A1435 5
HET P5S A1436 53
HET DTU A1437 8
HET SO4 B1435 5
HET P5S B1436 54
HET DTT B1437 8
HETNAM SO4 SULFATE ION
HETNAM P5S O-[(R)-{[(2R)-2,3-BIS(OCTADECANOYLOXY)
HETNAM 2 P5S PROPYL]OXY}(HYDROXY)PHOSPHORYL]-L-SERINE
HETNAM DTU (2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL
HETNAM DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE
HETSYN P5S PHOSPHATIDYL SERINE
HETSYN DTT 1,4-DITHIOTHREITOL
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 P5S 2(C42 H82 N O10 P)
FORMUL 5 DTU C4 H10 O2 S2
FORMUL 8 DTT C4 H10 O2 S2
FORMUL 9 HOH *363(H2 O)
HELIX 1 1 ASP A 36 ILE A 40 5 5
HELIX 2 2 ASP A 44 SER A 56 1 13
HELIX 3 3 PRO A 70 PHE A 72 5 3
HELIX 4 4 MET A 79 GLN A 86 1 8
HELIX 5 5 PHE A 89 GLU A 99 1 11
HELIX 6 6 ASP A 101 GLY A 116 1 16
HELIX 7 7 PRO A 169 SER A 171 5 3
HELIX 8 8 PRO A 319 GLN A 323 5 5
HELIX 9 9 GLU A 327 TRP A 332 1 6
HELIX 10 10 TRP A 332 VAL A 341 1 10
HELIX 11 11 ASN A 343 ASP A 368 1 26
HELIX 12 12 ASP A 399 ALA A 411 1 13
HELIX 13 13 THR A 420 ILE A 425 1 6
HELIX 14 14 PRO A 426 GLN A 434 1 9
HELIX 15 15 ASP B 36 ILE B 40 5 5
HELIX 16 16 ASP B 44 SER B 56 1 13
HELIX 17 17 PRO B 70 PHE B 72 5 3
HELIX 18 18 MET B 79 GLN B 86 1 8
HELIX 19 19 PHE B 89 GLU B 99 1 11
HELIX 20 20 ASP B 101 GLY B 116 1 16
HELIX 21 21 PRO B 169 SER B 171 5 3
HELIX 22 22 PRO B 319 GLN B 323 5 5
HELIX 23 23 GLU B 327 TRP B 332 1 6
HELIX 24 24 TRP B 332 VAL B 341 1 10
HELIX 25 25 ASN B 343 ASP B 368 1 26
HELIX 26 26 ASP B 399 GLN B 409 1 11
HELIX 27 27 PRO B 426 GLN B 434 1 9
SHEET 1 AA 2 LEU A 74 SER A 78 0
SHEET 2 AA 2 LYS A 126 LEU A 128 1 O LYS A 126 N GLU A 75
SHEET 1 AB12 TYR A 135 ASP A 141 0
SHEET 2 AB12 GLN A 147 SER A 156 -1 O ALA A 148 N TRP A 140
SHEET 3 AB12 GLU A 161 ILE A 168 -1 O GLU A 161 N SER A 156
SHEET 4 AB12 ILE A 173 VAL A 179 -1 O ILE A 173 N ILE A 168
SHEET 5 AB12 SER A 197 LYS A 206 -1 O SER A 197 N VAL A 178
SHEET 6 AB12 PRO A 212 THR A 218 -1 O GLU A 213 N PHE A 202
SHEET 7 AB12 HIS A 239 LYS A 243 -1 O ILE A 241 N THR A 218
SHEET 8 AB12 GLN A 248 PHE A 253 -1 O ALA A 249 N ILE A 242
SHEET 9 AB12 ILE A 266 LYS A 271 -1 O GLU A 267 N GLU A 252
SHEET 10 AB12 ALA A 277 GLY A 283 -1 N TYR A 278 O VAL A 270
SHEET 11 AB12 VAL A 288 ASP A 293 -1 O TYR A 290 N SER A 282
SHEET 12 AB12 LYS A 302 ASP A 306 -1 O LYS A 302 N LEU A 291
SHEET 1 AC 4 PRO A 181 PHE A 185 0
SHEET 2 AC 4 SER A 189 MET A 194 -1 O ALA A 191 N ARG A 184
SHEET 3 AC 4 VAL A 222 ARG A 225 -1 O VAL A 222 N ALA A 192
SHEET 4 AC 4 ARG A 233 LEU A 236 -1 O ARG A 233 N ARG A 225
SHEET 1 AD 2 PHE A 377 ARG A 379 0
SHEET 2 AD 2 TYR A 388 ILE A 390 -1 O CYS A 389 N ARG A 378
SHEET 1 BA 2 LEU B 74 SER B 78 0
SHEET 2 BA 2 LYS B 126 LEU B 128 1 O LYS B 126 N GLU B 75
SHEET 1 BB12 TYR B 135 ASP B 141 0
SHEET 2 BB12 GLN B 147 SER B 156 -1 O ALA B 148 N TRP B 140
SHEET 3 BB12 GLU B 161 ILE B 168 -1 O GLU B 161 N SER B 156
SHEET 4 BB12 ILE B 173 VAL B 179 -1 O ILE B 173 N ILE B 168
SHEET 5 BB12 SER B 197 LYS B 206 -1 O SER B 197 N VAL B 178
SHEET 6 BB12 PRO B 212 THR B 218 -1 O GLU B 213 N PHE B 202
SHEET 7 BB12 HIS B 239 LYS B 243 -1 O ILE B 241 N THR B 218
SHEET 8 BB12 GLN B 248 PHE B 253 -1 O ALA B 249 N ILE B 242
SHEET 9 BB12 ILE B 266 LYS B 271 -1 O GLU B 267 N GLU B 252
SHEET 10 BB12 ALA B 277 GLY B 283 -1 N TYR B 278 O VAL B 270
SHEET 11 BB12 VAL B 288 ASP B 293 -1 O TYR B 290 N SER B 282
SHEET 12 BB12 LYS B 302 ASP B 306 -1 O LYS B 302 N LEU B 291
SHEET 1 BC 4 PRO B 181 PHE B 185 0
SHEET 2 BC 4 SER B 189 MET B 194 -1 O ALA B 191 N ARG B 184
SHEET 3 BC 4 VAL B 222 ARG B 225 -1 O VAL B 222 N ALA B 192
SHEET 4 BC 4 ARG B 233 LEU B 236 -1 O ARG B 233 N ARG B 225
SHEET 1 BD 2 PHE B 377 ARG B 379 0
SHEET 2 BD 2 TYR B 388 ILE B 390 -1 O CYS B 389 N ARG B 378
CISPEP 1 HIS A 158 PRO A 159 0 -0.87
CISPEP 2 HIS B 158 PRO B 159 0 -1.55
SITE 1 AC1 7 LEU A 132 GLY A 133 PHE A 372 LYS A 375
SITE 2 AC1 7 HOH A2059 HOH A2145 HOH A2167
SITE 1 AC2 9 MET B 79 PRO B 130 GLN B 154 PRO B 160
SITE 2 AC2 9 GLU B 161 CYS B 162 VAL B 179 PRO B 181
SITE 3 AC2 9 HOH B2061
SITE 1 AC3 26 LEU A 64 ILE A 67 LEU A 69 ILE A 73
SITE 2 AC3 26 MET A 79 ARG A 82 GLN A 86 TRP A 112
SITE 3 AC3 26 LYS A 125 LYS A 126 PRO A 127 ASN A 129
SITE 4 AC3 26 PRO A 160 SER A 183 SER A 190 ALA A 191
SITE 5 AC3 26 ALA A 192 MET A 194 THR A 198 VAL A 222
SITE 6 AC3 26 MET A 232 ILE A 234 HOH A2049 HOH A2054
SITE 7 AC3 26 HOH A2055 HOH A2087
SITE 1 AC4 26 LEU B 64 ILE B 67 THR B 68 LEU B 69
SITE 2 AC4 26 MET B 79 GLN B 86 TRP B 112 TYR B 113
SITE 3 AC4 26 VAL B 124 LYS B 126 PRO B 127 ASN B 129
SITE 4 AC4 26 PRO B 160 TYR B 164 SER B 183 SER B 190
SITE 5 AC4 26 ALA B 191 ALA B 192 THR B 198 VAL B 222
SITE 6 AC4 26 MET B 232 HOH B2055 HOH B2061 HOH B2062
SITE 7 AC4 26 HOH B2063 HOH B2096
SITE 1 AC5 10 LEU A 408 GLN A 409 PRO A 412 GLN A 417
SITE 2 AC5 10 GLN A 418 PHE A 419 THR A 420 LYS A 422
SITE 3 AC5 10 PHE A 423 HOH A2158
SITE 1 AC6 8 LYS A 243 SER A 244 PRO A 245 TYR A 273
SITE 2 AC6 8 GLY B 61 ARG B 184 LEU B 186 MET B 193
CRYST1 120.000 72.600 122.900 90.00 111.40 90.00 C 1 2 1 8
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 0.008333 0.000000 0.003266 0.00000
SCALE2 0.000000 0.013774 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008739 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
