HEADER MEMBRANE PROTEIN 22-JUN-12 4AYW
TITLE STRUCTURE OF THE HUMAN MITOCHONDRIAL ABC TRANSPORTER, ABCB10 (PLATE
TITLE 2 FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP-BINDING CASSETTE SUB-FAMILY B MEMBER 10;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ABC TRANSPORTER, RESIDUES 1-5,126-738;
COMPND 5 SYNONYM: ATP-BINDING CASSETTE TRANSPORTER 10, ABC TRANSPORTER 10
COMPND 6 PROTEIN, MITOCHONDRIAL ATP-BINDING CASSETTE 2, M-ABC2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFB-LIC-BSE
KEYWDS MEMBRANE PROTEIN, MITOCHONDRIAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.W.PIKE,C.A.SHINTRE,Q.LI,J.KIM,F.VON DELFT,A.J.BARR,S.DAS,
AUTHOR 2 A.CHAIKUAD,X.XIA,A.QUIGLEY,Y.DONG,L.DONG,T.KROJER,M.VOLLMAR,
AUTHOR 3 J.R.C.MUNIZ,J.E.BRAY,G.BERRIDGE,R.CHALK,O.GILEADI,N.BURGESS-BROWN,
AUTHOR 4 L.SHRESTHA,S.GOUBIN,J.YANG,P.MAHAJAN,S.MUKHOPADHYAY,A.N.BULLOCK,
AUTHOR 5 C.H.ARROWSMITH,J.WEIGELT,C.BOUNTRA,A.M.EDWARDS,E.P.CARPENTER
REVDAT 7 24-JAN-18 4AYW 1 AUTHOR JRNL
REVDAT 6 25-MAR-15 4AYW 1 JRNL
REVDAT 5 07-AUG-13 4AYW 1 JRNL
REVDAT 4 12-JUN-13 4AYW 1 JRNL
REVDAT 3 05-JUN-13 4AYW 1 AUTHOR JRNL
REVDAT 2 27-FEB-13 4AYW 1 SEQADV
REVDAT 1 11-JUL-12 4AYW 0
SPRSDE 11-JUL-12 4AYW 4AA3
JRNL AUTH C.A.SHINTRE,A.C.W.PIKE,Q.LI,J.KIM,A.J.BARR,F.VON DELFT,
JRNL AUTH 2 S.GOUB,L.SHRESTHA,J.YANG,G.BERRIDGE,J.ROSS,P.J.STANSFELD,
JRNL AUTH 3 M.S.P.SANSOA,M.EDWARDS,C.BOUNTRA,B.D.MARSDEN,F.VON DELFT,
JRNL AUTH 4 A.N.BULLOCK,O.GILEADI,N.BURGESS-BROWN,E.P.CARPENTER
JRNL TITL STRUCTURES OF ABCB10, A HUMAN ATP-BINDING CASSETTE
JRNL TITL 2 TRANSPORTER IN APO- AND NUCLEOTIDE-BOUND STATES
JRNL REF PROC.NATL.ACAD.SCI.USA V. 110 9710 2013
JRNL REFN ISSN 0027-8424
JRNL PMID 23716676
JRNL DOI 10.1073/PNAS.1217042110
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 14134
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) : 0.252
REMARK 3 R VALUE (WORKING SET) : 0.251
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.140
REMARK 3 FREE R VALUE TEST SET COUNT : 585
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 7
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.56
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.31
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2646
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2632
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2538
REMARK 3 BIN R VALUE (WORKING SET) : 0.2623
REMARK 3 BIN FREE R VALUE : 0.2844
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.08
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 108
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4061
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 91
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 86.82
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 109.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -14.67700
REMARK 3 B22 (A**2) : -14.67700
REMARK 3 B33 (A**2) : 29.35400
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) : 0.985
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.516
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.886
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.812
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4233 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5777 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1936 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 74 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 649 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4233 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 595 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 4906 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 0.94
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.96
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.68
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESID 154-276
REMARK 3 ORIGIN FOR THE GROUP (A): -25.5657 26.6117 -34.6055
REMARK 3 T TENSOR
REMARK 3 T11: 0.0449 T22: -0.0754
REMARK 3 T33: -0.1706 T12: -0.1243
REMARK 3 T13: 0.0917 T23: 0.0643
REMARK 3 L TENSOR
REMARK 3 L11: 1.0889 L22: 1.5297
REMARK 3 L33: 7.4760 L12: 0.3694
REMARK 3 L13: 0.1760 L23: -1.4449
REMARK 3 S TENSOR
REMARK 3 S11: -0.0009 S12: -0.3701 S13: -0.2619
REMARK 3 S21: -0.2004 S22: -0.0884 S23: -0.1547
REMARK 3 S31: 0.4623 S32: 0.6273 S33: 0.0893
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESID 277 - 448
REMARK 3 ORIGIN FOR THE GROUP (A): -14.8463 48.6026 -33.7008
REMARK 3 T TENSOR
REMARK 3 T11: 0.1713 T22: 0.1046
REMARK 3 T33: -0.2202 T12: -0.2434
REMARK 3 T13: 0.0671 T23: 0.0498
REMARK 3 L TENSOR
REMARK 3 L11: 0.4207 L22: 0.5252
REMARK 3 L33: 1.3932 L12: 0.1294
REMARK 3 L13: 1.0409 L23: -0.0809
REMARK 3 S TENSOR
REMARK 3 S11: -0.0711 S12: -0.1830 S13: -0.0531
REMARK 3 S21: 0.0300 S22: -0.2150 S23: 0.0053
REMARK 3 S31: 0.0145 S32: 0.1620 S33: 0.2861
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND RESID 449-513
REMARK 3 ORIGIN FOR THE GROUP (A): -15.5267 26.2898 3.4420
REMARK 3 T TENSOR
REMARK 3 T11: -0.1673 T22: 0.5822
REMARK 3 T33: -0.4024 T12: -0.0858
REMARK 3 T13: -0.0875 T23: 0.3024
REMARK 3 L TENSOR
REMARK 3 L11: 1.4635 L22: 2.1844
REMARK 3 L33: 2.5695 L12: 1.5757
REMARK 3 L13: -3.3392 L23: -1.2367
REMARK 3 S TENSOR
REMARK 3 S11: -0.1155 S12: -0.2336 S13: -0.1970
REMARK 3 S21: 0.1965 S22: 0.1069 S23: -0.1738
REMARK 3 S31: -0.1505 S32: 0.3189 S33: 0.0087
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND RESID 514-643
REMARK 3 ORIGIN FOR THE GROUP (A): -34.3732 23.0221 15.2006
REMARK 3 T TENSOR
REMARK 3 T11: 0.2693 T22: -0.0363
REMARK 3 T33: -0.6161 T12: -0.1530
REMARK 3 T13: -0.0660 T23: 0.1585
REMARK 3 L TENSOR
REMARK 3 L11: 8.7094 L22: 0.9485
REMARK 3 L33: 6.5293 L12: -0.4912
REMARK 3 L13: -0.3403 L23: -1.8341
REMARK 3 S TENSOR
REMARK 3 S11: -0.2424 S12: -0.1699 S13: -0.3448
REMARK 3 S21: 0.4150 S22: -0.3989 S23: 0.1917
REMARK 3 S31: -0.7218 S32: 0.8180 S33: 0.6413
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND RESID 644-717
REMARK 3 ORIGIN FOR THE GROUP (A): -34.1062 26.0949 28.1226
REMARK 3 T TENSOR
REMARK 3 T11: 0.2416 T22: 0.3089
REMARK 3 T33: -0.4686 T12: -0.0682
REMARK 3 T13: -0.0430 T23: 0.2594
REMARK 3 L TENSOR
REMARK 3 L11: 1.8410 L22: -0.2400
REMARK 3 L33: 8.5386 L12: 0.3236
REMARK 3 L13: -1.0656 L23: 2.7881
REMARK 3 S TENSOR
REMARK 3 S11: 0.0262 S12: -0.3139 S13: 0.2246
REMARK 3 S21: 0.1411 S22: -0.1498 S23: 0.0995
REMARK 3 S31: -0.2551 S32: 0.4062 S33: 0.1236
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 4AYT USED AS LSSR TARGET RESTRAINTS
REMARK 3 WITH A TARGET WEIGHT OF 0.1. THIS ENTRY HAS BEEN REREFINED WITH
REMARK 3 A MORE RECENT VERSION OF BUSTER V.2.11.2 AND REPLACES A PREVIOUS
REMARK 3 ENTRY 4AA3.
REMARK 4
REMARK 4 4AYW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1290053010.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.265
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14186
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 38.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 9.100
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SHELXD SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: DATA WERE HIGHLY ANISOTROPIC AND INTEGRATED WITH A SIGCUT
REMARK 200 1.0 IN MOSFLM
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CHLORIDE,
REMARK 280 5%(V/V)JEFFAMINE M-600, 0.1 M GLYCINE PH 9.5, 34%(V/V) PEG 400
REMARK 280 CRYSTAL SOAKED BRIEFLY IN 10MM LUTETIUM CHLORIDE PRIOR TO DATA
REMARK 280 COLLECTION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+2/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 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 196.48667
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 98.24333
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 196.48667
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 98.24333
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 196.48667
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 98.24333
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 196.48667
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 98.24333
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -101.8 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 -50.85000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 88.07478
REMARK 350 BIOMT3 2 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 SER A 120
REMARK 465 MET A 121
REMARK 465 ARG A 122
REMARK 465 GLY A 123
REMARK 465 PRO A 124
REMARK 465 PRO A 125
REMARK 465 ALA A 126
REMARK 465 TRP A 127
REMARK 465 ALA A 128
REMARK 465 GLY A 129
REMARK 465 ASP A 130
REMARK 465 GLU A 131
REMARK 465 ALA A 132
REMARK 465 TRP A 133
REMARK 465 ARG A 134
REMARK 465 ARG A 135
REMARK 465 GLY A 136
REMARK 465 PRO A 137
REMARK 465 ALA A 138
REMARK 465 ALA A 139
REMARK 465 PRO A 140
REMARK 465 PRO A 141
REMARK 465 GLY A 142
REMARK 465 ASP A 143
REMARK 465 LYS A 144
REMARK 465 GLY A 145
REMARK 465 ARG A 146
REMARK 465 LEU A 147
REMARK 465 ARG A 148
REMARK 465 PRO A 149
REMARK 465 ALA A 150
REMARK 465 ALA A 151
REMARK 465 ALA A 152
REMARK 465 GLY A 153
REMARK 465 ALA A 660
REMARK 465 THR A 661
REMARK 465 SER A 662
REMARK 465 ALA A 663
REMARK 465 LEU A 718
REMARK 465 LEU A 719
REMARK 465 SER A 720
REMARK 465 LYS A 721
REMARK 465 PRO A 722
REMARK 465 ASN A 723
REMARK 465 GLY A 724
REMARK 465 ILE A 725
REMARK 465 TYR A 726
REMARK 465 ARG A 727
REMARK 465 LYS A 728
REMARK 465 LEU A 729
REMARK 465 MET A 730
REMARK 465 ASN A 731
REMARK 465 LYS A 732
REMARK 465 GLN A 733
REMARK 465 SER A 734
REMARK 465 PHE A 735
REMARK 465 ILE A 736
REMARK 465 SER A 737
REMARK 465 ALA A 738
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 GLU A 156 CG CD OE1 OE2
REMARK 470 ARG A 158 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 159 CG CD CE NZ
REMARK 470 LEU A 160 CG CD1 CD2
REMARK 470 ARG A 257 NE CZ NH1 NH2
REMARK 470 LYS A 265 CG CD CE NZ
REMARK 470 ARG A 267 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 274 CZ NH1 NH2
REMARK 470 LYS A 338 CG CD CE NZ
REMARK 470 ARG A 362 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 380 CG CD CE NZ
REMARK 470 GLN A 386 CG CD OE1 NE2
REMARK 470 LYS A 390 CG CD CE NZ
REMARK 470 GLU A 467 CG CD OE1 OE2
REMARK 470 GLU A 470 CG CD OE1 OE2
REMARK 470 LYS A 474 CG CD CE NZ
REMARK 470 LEU A 475 CG CD1 CD2
REMARK 470 GLU A 479 CG CD OE1 OE2
REMARK 470 LEU A 483 CG CD1 CD2
REMARK 470 ASN A 484 CG OD1 ND2
REMARK 470 GLU A 485 CG CD OE1 OE2
REMARK 470 LYS A 486 CG CD CE NZ
REMARK 470 SER A 487 OG
REMARK 470 PHE A 488 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 493 CG CD OE1 OE2
REMARK 470 PHE A 494 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 495 CG CD CE NZ
REMARK 470 ARG A 504 NE CZ NH1 NH2
REMARK 470 PHE A 510 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 513 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL A 526 CG1 CG2
REMARK 470 SER A 529 OG
REMARK 470 LYS A 533 CG CD CE NZ
REMARK 470 LEU A 540 CG CD1 CD2
REMARK 470 LEU A 566 CG CD1 CD2
REMARK 470 LYS A 569 CE NZ
REMARK 470 GLN A 575 CG CD OE1 NE2
REMARK 470 GLU A 576 CG CD OE1 OE2
REMARK 470 ARG A 605 CD NE CZ NH1 NH2
REMARK 470 ARG A 617 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 629 CG CD OE1 OE2
REMARK 470 LYS A 630 CG CD CE NZ
REMARK 470 LEU A 633 CG CD1 CD2
REMARK 470 LYS A 639 CE NZ
REMARK 470 GLN A 640 CG CD OE1 NE2
REMARK 470 LYS A 653 CG CD CE NZ
REMARK 470 LEU A 664 CG CD1 CD2
REMARK 470 GLU A 667 CG CD OE1 OE2
REMARK 470 HIS A 690 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 691 CG ND1 CD2 CE1 NE2
REMARK 470 LEU A 692 CG CD1 CD2
REMARK 470 LYS A 696 CG CD CE NZ
REMARK 470 GLN A 706 CG CD OE1 NE2
REMARK 470 LYS A 708 CG CD CE NZ
REMARK 470 GLU A 711 CG CD OE1 OE2
REMARK 470 GLU A 716 CG CD OE1 OE2
REMARK 470 GLU A 717 CG CD OE1 OE2
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 THR A 201 -84.49 -83.47
REMARK 500 THR A 287 -91.89 -129.89
REMARK 500 ASP A 512 62.51 65.42
REMARK 500 VAL A 627 -156.55 -105.71
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 LMT A 1724
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 1719
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT A 1724
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Y01 A 1730
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4AYT RELATED DB: PDB
REMARK 900 STRUCTURE OF THE HUMAN MITOCHONDRIAL ABC TRANSPORTER, ABCB10
REMARK 900 RELATED ID: 4AYX RELATED DB: PDB
REMARK 900 STRUCTURE OF THE HUMAN MITOCHONDRIAL ABC TRANSPORTER, ABCB10 (ROD
REMARK 900 FORM B)
DBREF 4AYW A 121 125 UNP Q9NRK6 ABCBA_HUMAN 1 5
DBREF 4AYW A 126 738 UNP Q9NRK6 ABCBA_HUMAN 126 738
SEQADV 4AYW SER A 120 UNP Q9NRK6 EXPRESSION TAG
SEQADV 4AYW HIS A 691 UNP Q9NRK6 ARG 691 CLONING ARTIFACT
SEQRES 1 A 619 SER MET ARG GLY PRO PRO ALA TRP ALA GLY ASP GLU ALA
SEQRES 2 A 619 TRP ARG ARG GLY PRO ALA ALA PRO PRO GLY ASP LYS GLY
SEQRES 3 A 619 ARG LEU ARG PRO ALA ALA ALA GLY LEU PRO GLU ALA ARG
SEQRES 4 A 619 LYS LEU LEU GLY LEU ALA TYR PRO GLU ARG ARG ARG LEU
SEQRES 5 A 619 ALA ALA ALA VAL GLY PHE LEU THR MET SER SER VAL ILE
SEQRES 6 A 619 SER MET SER ALA PRO PHE PHE LEU GLY LYS ILE ILE ASP
SEQRES 7 A 619 VAL ILE TYR THR ASN PRO THR VAL ASP TYR SER ASP ASN
SEQRES 8 A 619 LEU THR ARG LEU CYS LEU GLY LEU SER ALA VAL PHE LEU
SEQRES 9 A 619 CYS GLY ALA ALA ALA ASN ALA ILE ARG VAL TYR LEU MET
SEQRES 10 A 619 GLN THR SER GLY GLN ARG ILE VAL ASN ARG LEU ARG THR
SEQRES 11 A 619 SER LEU PHE SER SER ILE LEU ARG GLN GLU VAL ALA PHE
SEQRES 12 A 619 PHE ASP LYS THR ARG THR GLY GLU LEU ILE ASN ARG LEU
SEQRES 13 A 619 SER SER ASP THR ALA LEU LEU GLY ARG SER VAL THR GLU
SEQRES 14 A 619 ASN LEU SER ASP GLY LEU ARG ALA GLY ALA GLN ALA SER
SEQRES 15 A 619 VAL GLY ILE SER MET MET PHE PHE VAL SER PRO ASN LEU
SEQRES 16 A 619 ALA THR PHE VAL LEU SER VAL VAL PRO PRO VAL SER ILE
SEQRES 17 A 619 ILE ALA VAL ILE TYR GLY ARG TYR LEU ARG LYS LEU THR
SEQRES 18 A 619 LYS VAL THR GLN ASP SER LEU ALA GLN ALA THR GLN LEU
SEQRES 19 A 619 ALA GLU GLU ARG ILE GLY ASN VAL ARG THR VAL ARG ALA
SEQRES 20 A 619 PHE GLY LYS GLU MET THR GLU ILE GLU LYS TYR ALA SER
SEQRES 21 A 619 LYS VAL ASP HIS VAL MET GLN LEU ALA ARG LYS GLU ALA
SEQRES 22 A 619 PHE ALA ARG ALA GLY PHE PHE GLY ALA THR GLY LEU SER
SEQRES 23 A 619 GLY ASN LEU ILE VAL LEU SER VAL LEU TYR LYS GLY GLY
SEQRES 24 A 619 LEU LEU MET GLY SER ALA HIS MET THR VAL GLY GLU LEU
SEQRES 25 A 619 SER SER PHE LEU MET TYR ALA PHE TRP VAL GLY ILE SER
SEQRES 26 A 619 ILE GLY GLY LEU SER SER PHE TYR SER GLU LEU MET LYS
SEQRES 27 A 619 GLY LEU GLY ALA GLY GLY ARG LEU TRP GLU LEU LEU GLU
SEQRES 28 A 619 ARG GLU PRO LYS LEU PRO PHE ASN GLU GLY VAL ILE LEU
SEQRES 29 A 619 ASN GLU LYS SER PHE GLN GLY ALA LEU GLU PHE LYS ASN
SEQRES 30 A 619 VAL HIS PHE ALA TYR PRO ALA ARG PRO GLU VAL PRO ILE
SEQRES 31 A 619 PHE GLN ASP PHE SER LEU SER ILE PRO SER GLY SER VAL
SEQRES 32 A 619 THR ALA LEU VAL GLY PRO SER GLY SER GLY LYS SER THR
SEQRES 33 A 619 VAL LEU SER LEU LEU LEU ARG LEU TYR ASP PRO ALA SER
SEQRES 34 A 619 GLY THR ILE SER LEU ASP GLY HIS ASP ILE ARG GLN LEU
SEQRES 35 A 619 ASN PRO VAL TRP LEU ARG SER LYS ILE GLY THR VAL SER
SEQRES 36 A 619 GLN GLU PRO ILE LEU PHE SER CYS SER ILE ALA GLU ASN
SEQRES 37 A 619 ILE ALA TYR GLY ALA ASP ASP PRO SER SER VAL THR ALA
SEQRES 38 A 619 GLU GLU ILE GLN ARG VAL ALA GLU VAL ALA ASN ALA VAL
SEQRES 39 A 619 ALA PHE ILE ARG ASN PHE PRO GLN GLY PHE ASN THR VAL
SEQRES 40 A 619 VAL GLY GLU LYS GLY VAL LEU LEU SER GLY GLY GLN LYS
SEQRES 41 A 619 GLN ARG ILE ALA ILE ALA ARG ALA LEU LEU LYS ASN PRO
SEQRES 42 A 619 LYS ILE LEU LEU LEU ASP GLU ALA THR SER ALA LEU ASP
SEQRES 43 A 619 ALA GLU ASN GLU TYR LEU VAL GLN GLU ALA LEU ASP ARG
SEQRES 44 A 619 LEU MET ASP GLY ARG THR VAL LEU VAL ILE ALA HIS HIS
SEQRES 45 A 619 LEU SER THR ILE LYS ASN ALA ASN MET VAL ALA VAL LEU
SEQRES 46 A 619 ASP GLN GLY LYS ILE THR GLU TYR GLY LYS HIS GLU GLU
SEQRES 47 A 619 LEU LEU SER LYS PRO ASN GLY ILE TYR ARG LYS LEU MET
SEQRES 48 A 619 ASN LYS GLN SER PHE ILE SER ALA
HET ANP A1719 31
HET LMT A1724 25
HET Y01 A1730 35
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM LMT DODECYL-BETA-D-MALTOSIDE
HETNAM Y01 CHOLESTEROL HEMISUCCINATE
FORMUL 2 ANP C10 H17 N6 O12 P3
FORMUL 3 LMT C24 H46 O11
FORMUL 4 Y01 C31 H50 O4
HELIX 1 1 LEU A 154 TYR A 165 1 12
HELIX 2 2 GLU A 167 THR A 201 1 35
HELIX 3 3 ASP A 206 GLN A 258 1 53
HELIX 4 4 GLU A 259 THR A 266 1 8
HELIX 5 5 ARG A 267 VAL A 286 1 20
HELIX 6 6 THR A 287 SER A 311 1 25
HELIX 7 7 SER A 311 PHE A 367 1 57
HELIX 8 8 LYS A 369 LEU A 419 1 51
HELIX 9 9 THR A 427 GLU A 470 1 44
HELIX 10 10 SER A 534 LEU A 541 1 8
HELIX 11 11 ASN A 562 LYS A 569 1 8
HELIX 12 12 SER A 583 TYR A 590 1 8
HELIX 13 13 THR A 599 ALA A 610 1 12
HELIX 14 14 ALA A 612 ASN A 618 1 7
HELIX 15 15 GLN A 621 THR A 625 5 5
HELIX 16 16 SER A 635 ASN A 651 1 17
HELIX 17 17 ASP A 665 ASP A 681 1 17
HELIX 18 18 HIS A 691 ASN A 697 1 7
SHEET 1 AA 4 PHE A 510 ILE A 517 0
SHEET 2 AA 4 LEU A 492 PHE A 499 -1 O LEU A 492 N ILE A 517
SHEET 3 AA 4 SER A 548 LEU A 553 -1 O SER A 548 N HIS A 498
SHEET 4 AA 4 HIS A 556 ASP A 557 -1 O HIS A 556 N LEU A 553
SHEET 1 AB 6 ILE A 570 VAL A 573 0
SHEET 2 AB 6 ILE A 654 ASP A 658 1 O ILE A 654 N GLY A 571
SHEET 3 AB 6 THR A 684 ILE A 688 1 O THR A 684 N LEU A 655
SHEET 4 AB 6 VAL A 522 VAL A 526 1 O THR A 523 N VAL A 687
SHEET 5 AB 6 MET A 700 ASP A 705 1 O MET A 700 N ALA A 524
SHEET 6 AB 6 LYS A 708 GLY A 713 -1 O LYS A 708 N ASP A 705
CISPEP 1 MET A 421 GLY A 422 0 -5.38
SITE 1 AC1 8 ASP A 264 TYR A 501 SER A 529 GLY A 530
SITE 2 AC1 8 GLY A 532 LYS A 533 SER A 534 THR A 535
SITE 1 AC2 5 LYS A 416 LEU A 419 ASP A 677 ARG A 678
SITE 2 AC2 5 ASP A 681
SITE 1 AC3 10 ARG A 170 ARG A 213 ALA A 227 ALA A 230
SITE 2 AC3 10 TYR A 234 LEU A 235 ARG A 389 PHE A 393
SITE 3 AC3 10 GLY A 397 LEU A 404
CRYST1 101.700 101.700 294.730 90.00 90.00 120.00 P 62 2 2 12
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 0.009833 0.005677 0.000000 0.00000
SCALE2 0.000000 0.011354 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003393 0.00000
(ATOM LINES ARE NOT SHOWN.)
END