HEADER MEMBRANE PROTEIN 05-FEB-09 3G61
TITLE STRUCTURE OF P-GLYCOPROTEIN REVEALS A MOLECULAR BASIS FOR POLY-
TITLE 2 SPECIFIC DRUG BINDING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MULTIDRUG RESISTANCE PROTEIN 1A;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MCG1178;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ABCB1A, MCG_1178
KEYWDS P-GLYCOPROTEIN, PGP, MULTIDRUG RESISTANCE, MEMBRANE PROTEIN, CYCLE
KEYWDS 2 PEPTIDES, ATP-BINDING, NUCLEOTIDE-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.G.ALLER,J.YU,A.WARD,Y.WENG,S.CHITTABOINA,R.ZHUO,P.M.HARRELL,
AUTHOR 2 Y.T.TRINH,Q.ZHANG,I.L.URBATSCH,G.CHANG
REVDAT 5 21-FEB-24 3G61 1 REMARK
REVDAT 4 21-OCT-20 3G61 1 REMARK SEQADV HETSYN
REVDAT 3 13-NOV-13 3G61 1 HETATM HETNAM HETSYN HET
REVDAT 3 2 1 FORMUL VERSN REMARK
REVDAT 2 21-APR-09 3G61 1 JRNL
REVDAT 1 24-MAR-09 3G61 0
JRNL AUTH S.G.ALLER,J.YU,A.WARD,Y.WENG,S.CHITTABOINA,R.ZHUO,
JRNL AUTH 2 P.M.HARRELL,Y.T.TRINH,Q.ZHANG,I.L.URBATSCH,G.CHANG
JRNL TITL STRUCTURE OF P-GLYCOPROTEIN REVEALS A MOLECULAR BASIS FOR
JRNL TITL 2 POLY-SPECIFIC DRUG BINDING.
JRNL REF SCIENCE V. 323 1718 2009
JRNL REFN ISSN 0036-8075
JRNL PMID 19325113
JRNL DOI 10.1126/SCIENCE.1168750
REMARK 2
REMARK 2 RESOLUTION. 4.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 4.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 120841.900
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.3
REMARK 3 NUMBER OF REFLECTIONS : 26489
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) : 0.308
REMARK 3 FREE R VALUE : 0.356
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2642
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 4.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 4.62
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3624
REMARK 3 BIN R VALUE (WORKING SET) : 0.4600
REMARK 3 BIN FREE R VALUE : 0.4980
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 376
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.026
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 18342
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 106
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 103.5
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 182.6
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -16.49000
REMARK 3 B22 (A**2) : 50.71000
REMARK 3 B33 (A**2) : -34.21000
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) : 0.91
REMARK 3 ESD FROM SIGMAA (A) : 1.05
REMARK 3 LOW RESOLUTION CUTOFF (A) : 20.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 1.15
REMARK 3 ESD FROM C-V SIGMAA (A) : 1.33
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.910
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) : 13.950; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 21.610; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 15.020; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 21.740; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.15
REMARK 3 BSOL : 27.22
REMARK 3
REMARK 3 NCS MODEL : CONSTR
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 : QZ59SSS.PAR
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3G61 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-09.
REMARK 100 THE DEPOSITION ID IS D_1000051467.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-08
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97854
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26489
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.350
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-23% PEG400, 0.05M TRIS, 0.04%
REMARK 280 SODIUM CHOLATE, PH 7.8, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 278K
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 48.87100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 187.90500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.48900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 187.90500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.87100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.48900
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 GLU A 2
REMARK 465 LEU A 3
REMARK 465 GLU A 4
REMARK 465 GLU A 5
REMARK 465 ASP A 6
REMARK 465 LEU A 7
REMARK 465 LYS A 8
REMARK 465 GLY A 9
REMARK 465 ARG A 10
REMARK 465 ALA A 11
REMARK 465 ASP A 12
REMARK 465 LYS A 13
REMARK 465 ASN A 14
REMARK 465 PHE A 15
REMARK 465 SER A 16
REMARK 465 LYS A 17
REMARK 465 MET A 18
REMARK 465 GLY A 19
REMARK 465 LYS A 20
REMARK 465 LYS A 21
REMARK 465 SER A 22
REMARK 465 LYS A 23
REMARK 465 LYS A 24
REMARK 465 GLU A 25
REMARK 465 LYS A 26
REMARK 465 LYS A 27
REMARK 465 GLU A 28
REMARK 465 LYS A 29
REMARK 465 LYS A 30
REMARK 465 PRO A 31
REMARK 465 ALA A 32
REMARK 465 ALA A 627
REMARK 465 GLY A 628
REMARK 465 ASN A 629
REMARK 465 GLU A 630
REMARK 465 ILE A 631
REMARK 465 GLU A 632
REMARK 465 LEU A 633
REMARK 465 GLY A 634
REMARK 465 ASN A 635
REMARK 465 GLU A 636
REMARK 465 ALA A 637
REMARK 465 CYS A 638
REMARK 465 LYS A 639
REMARK 465 SER A 640
REMARK 465 LYS A 641
REMARK 465 ASP A 642
REMARK 465 GLU A 643
REMARK 465 ILE A 644
REMARK 465 ASP A 645
REMARK 465 ASN A 646
REMARK 465 LEU A 647
REMARK 465 ASP A 648
REMARK 465 MET A 649
REMARK 465 SER A 650
REMARK 465 SER A 651
REMARK 465 LYS A 652
REMARK 465 ASP A 653
REMARK 465 SER A 654
REMARK 465 GLY A 655
REMARK 465 SER A 656
REMARK 465 SER A 657
REMARK 465 LEU A 658
REMARK 465 ILE A 659
REMARK 465 ARG A 660
REMARK 465 ARG A 661
REMARK 465 ARG A 662
REMARK 465 SER A 663
REMARK 465 THR A 664
REMARK 465 ARG A 665
REMARK 465 LYS A 666
REMARK 465 SER A 667
REMARK 465 ILE A 668
REMARK 465 CYS A 669
REMARK 465 GLY A 670
REMARK 465 PRO A 671
REMARK 465 HIS A 672
REMARK 465 ASP A 673
REMARK 465 GLN A 674
REMARK 465 ASP A 675
REMARK 465 ARG A 676
REMARK 465 LYS A 677
REMARK 465 LEU A 678
REMARK 465 SER A 679
REMARK 465 THR A 680
REMARK 465 LYS A 681
REMARK 465 GLU A 682
REMARK 465 ALA A 683
REMARK 465 GLY A 1272
REMARK 465 ALA A 1273
REMARK 465 LYS A 1274
REMARK 465 ARG A 1275
REMARK 465 SER A 1276
REMARK 465 TYR A 1277
REMARK 465 VAL A 1278
REMARK 465 HIS A 1279
REMARK 465 HIS A 1280
REMARK 465 HIS A 1281
REMARK 465 HIS A 1282
REMARK 465 HIS A 1283
REMARK 465 HIS A 1284
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 LEU B 3
REMARK 465 GLU B 4
REMARK 465 GLU B 5
REMARK 465 ASP B 6
REMARK 465 LEU B 7
REMARK 465 LYS B 8
REMARK 465 GLY B 9
REMARK 465 ARG B 10
REMARK 465 ALA B 11
REMARK 465 ASP B 12
REMARK 465 LYS B 13
REMARK 465 ASN B 14
REMARK 465 PHE B 15
REMARK 465 SER B 16
REMARK 465 LYS B 17
REMARK 465 MET B 18
REMARK 465 GLY B 19
REMARK 465 LYS B 20
REMARK 465 LYS B 21
REMARK 465 SER B 22
REMARK 465 LYS B 23
REMARK 465 LYS B 24
REMARK 465 GLU B 25
REMARK 465 LYS B 26
REMARK 465 LYS B 27
REMARK 465 GLU B 28
REMARK 465 LYS B 29
REMARK 465 LYS B 30
REMARK 465 PRO B 31
REMARK 465 ALA B 32
REMARK 465 ALA B 627
REMARK 465 GLY B 628
REMARK 465 ASN B 629
REMARK 465 GLU B 630
REMARK 465 ILE B 631
REMARK 465 GLU B 632
REMARK 465 LEU B 633
REMARK 465 GLY B 634
REMARK 465 ASN B 635
REMARK 465 GLU B 636
REMARK 465 ALA B 637
REMARK 465 CYS B 638
REMARK 465 LYS B 639
REMARK 465 SER B 640
REMARK 465 LYS B 641
REMARK 465 ASP B 642
REMARK 465 GLU B 643
REMARK 465 ILE B 644
REMARK 465 ASP B 645
REMARK 465 ASN B 646
REMARK 465 LEU B 647
REMARK 465 ASP B 648
REMARK 465 MET B 649
REMARK 465 SER B 650
REMARK 465 SER B 651
REMARK 465 LYS B 652
REMARK 465 ASP B 653
REMARK 465 SER B 654
REMARK 465 GLY B 655
REMARK 465 SER B 656
REMARK 465 SER B 657
REMARK 465 LEU B 658
REMARK 465 ILE B 659
REMARK 465 ARG B 660
REMARK 465 ARG B 661
REMARK 465 ARG B 662
REMARK 465 SER B 663
REMARK 465 THR B 664
REMARK 465 ARG B 665
REMARK 465 LYS B 666
REMARK 465 SER B 667
REMARK 465 ILE B 668
REMARK 465 CYS B 669
REMARK 465 GLY B 670
REMARK 465 PRO B 671
REMARK 465 HIS B 672
REMARK 465 ASP B 673
REMARK 465 GLN B 674
REMARK 465 ASP B 675
REMARK 465 ARG B 676
REMARK 465 LYS B 677
REMARK 465 LEU B 678
REMARK 465 SER B 679
REMARK 465 THR B 680
REMARK 465 LYS B 681
REMARK 465 GLU B 682
REMARK 465 ALA B 683
REMARK 465 GLY B 1272
REMARK 465 ALA B 1273
REMARK 465 LYS B 1274
REMARK 465 ARG B 1275
REMARK 465 SER B 1276
REMARK 465 TYR B 1277
REMARK 465 VAL B 1278
REMARK 465 HIS B 1279
REMARK 465 HIS B 1280
REMARK 465 HIS B 1281
REMARK 465 HIS B 1282
REMARK 465 HIS B 1283
REMARK 465 HIS B 1284
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 GLU B 155 N GLY B 157 2.03
REMARK 500 O GLU A 155 N GLY A 157 2.05
REMARK 500 O GLU B 552 N THR B 554 2.11
REMARK 500 O ARG A 589 N ALA A 591 2.17
REMARK 500 O GLU B 321 N SER B 323 2.17
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 PRO A 65 C - N - CA ANGL. DEV. = -13.1 DEGREES
REMARK 500 GLY A 165 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 LYS A 267 N - CA - C ANGL. DEV. = 18.1 DEGREES
REMARK 500 PRO A 346 C - N - CA ANGL. DEV. = -11.0 DEGREES
REMARK 500 PHE A 374 N - CA - C ANGL. DEV. = 22.5 DEGREES
REMARK 500 ASP A 450 N - CA - C ANGL. DEV. = -21.7 DEGREES
REMARK 500 GLY A 575 N - CA - C ANGL. DEV. = -15.1 DEGREES
REMARK 500 PRO A 923 C - N - CA ANGL. DEV. = -9.1 DEGREES
REMARK 500 TYR A1017 N - CA - C ANGL. DEV. = 16.6 DEGREES
REMARK 500 LYS A1098 N - CA - C ANGL. DEV. = -21.0 DEGREES
REMARK 500 ASP A1159 N - CA - C ANGL. DEV. = -20.0 DEGREES
REMARK 500 PRO B 65 C - N - CA ANGL. DEV. = -13.0 DEGREES
REMARK 500 PRO B 65 C - N - CD ANGL. DEV. = 12.6 DEGREES
REMARK 500 GLY B 165 N - CA - C ANGL. DEV. = -17.3 DEGREES
REMARK 500 PRO B 346 C - N - CA ANGL. DEV. = -10.5 DEGREES
REMARK 500 SER B 370 N - CA - C ANGL. DEV. = 27.3 DEGREES
REMARK 500 LYS B1098 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 ASP B1159 N - CA - C ANGL. DEV. = -22.7 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 SER A 34 -64.16 -16.22
REMARK 500 VAL A 35 -80.33 -41.82
REMARK 500 THR A 37 -70.60 -61.64
REMARK 500 PHE A 39 -71.18 -49.45
REMARK 500 ALA A 42 117.30 79.99
REMARK 500 TRP A 44 -92.36 -66.09
REMARK 500 VAL A 52 -77.94 -28.89
REMARK 500 ASP A 73 -54.08 -20.65
REMARK 500 SER A 88 -22.03 51.23
REMARK 500 ASN A 90 -135.57 -173.23
REMARK 500 LEU A 103 -74.27 -61.49
REMARK 500 PHE A 131 -85.80 -49.63
REMARK 500 TRP A 132 -70.72 -15.12
REMARK 500 CYS A 133 -102.12 -62.83
REMARK 500 LEU A 134 -68.97 -8.57
REMARK 500 ALA A 135 -89.26 -45.29
REMARK 500 ILE A 140 -75.52 -42.63
REMARK 500 HIS A 141 -48.06 -28.54
REMARK 500 ARG A 144 -81.80 -55.02
REMARK 500 PHE A 148 -71.21 -43.61
REMARK 500 MET A 152 -16.97 -46.19
REMARK 500 GLU A 155 174.97 45.09
REMARK 500 ILE A 156 -47.97 1.68
REMARK 500 ASP A 160 -79.90 -32.54
REMARK 500 VAL A 161 -146.20 -105.70
REMARK 500 HIS A 162 173.17 72.00
REMARK 500 VAL A 164 -12.91 45.34
REMARK 500 PHE A 190 -78.06 -30.20
REMARK 500 PHE A 196 -71.86 -61.71
REMARK 500 PHE A 200 -76.61 -76.67
REMARK 500 ILE A 201 -82.57 -26.87
REMARK 500 PHE A 204 -75.48 -158.88
REMARK 500 TRP A 208 -6.62 50.30
REMARK 500 LYS A 209 -14.46 173.76
REMARK 500 ILE A 214 -74.10 -60.66
REMARK 500 LEU A 215 -53.50 -29.06
REMARK 500 ALA A 216 -82.90 -57.38
REMARK 500 SER A 218 -79.37 -61.44
REMARK 500 PRO A 219 -35.90 -39.64
REMARK 500 ILE A 227 -72.16 -55.01
REMARK 500 GLU A 251 -62.55 -105.68
REMARK 500 GLU A 252 175.61 61.52
REMARK 500 ALA A 255 -157.69 -81.49
REMARK 500 ALA A 256 18.49 51.29
REMARK 500 ARG A 258 -73.47 -49.26
REMARK 500 PHE A 263 -32.11 -132.82
REMARK 500 GLN A 266 -70.81 -54.01
REMARK 500 LYS A 267 -12.09 50.31
REMARK 500 LYS A 268 -60.73 -98.73
REMARK 500 GLU A 269 -73.65 -37.02
REMARK 500
REMARK 500 THIS ENTRY HAS 553 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 916 0.07 SIDE CHAIN
REMARK 500 TYR B 916 0.06 SIDE CHAIN
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 2J8 A 6002
REMARK 610 2J8 B 6004
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2J8 A 6001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2J8 A 6002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2J8 B 6003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2J8 B 6004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3G5U RELATED DB: PDB
REMARK 900 RELATED ID: 3G60 RELATED DB: PDB
DBREF 3G61 A 1 1276 UNP Q5I1Y5 Q5I1Y5_MOUSE 1 1276
DBREF 3G61 B 1 1276 UNP Q5I1Y5 Q5I1Y5_MOUSE 1 1276
SEQADV 3G61 TYR A 1277 UNP Q5I1Y5 EXPRESSION TAG
SEQADV 3G61 VAL A 1278 UNP Q5I1Y5 EXPRESSION TAG
SEQADV 3G61 HIS A 1279 UNP Q5I1Y5 EXPRESSION TAG
SEQADV 3G61 HIS A 1280 UNP Q5I1Y5 EXPRESSION TAG
SEQADV 3G61 HIS A 1281 UNP Q5I1Y5 EXPRESSION TAG
SEQADV 3G61 HIS A 1282 UNP Q5I1Y5 EXPRESSION TAG
SEQADV 3G61 HIS A 1283 UNP Q5I1Y5 EXPRESSION TAG
SEQADV 3G61 HIS A 1284 UNP Q5I1Y5 EXPRESSION TAG
SEQADV 3G61 TYR B 1277 UNP Q5I1Y5 EXPRESSION TAG
SEQADV 3G61 VAL B 1278 UNP Q5I1Y5 EXPRESSION TAG
SEQADV 3G61 HIS B 1279 UNP Q5I1Y5 EXPRESSION TAG
SEQADV 3G61 HIS B 1280 UNP Q5I1Y5 EXPRESSION TAG
SEQADV 3G61 HIS B 1281 UNP Q5I1Y5 EXPRESSION TAG
SEQADV 3G61 HIS B 1282 UNP Q5I1Y5 EXPRESSION TAG
SEQADV 3G61 HIS B 1283 UNP Q5I1Y5 EXPRESSION TAG
SEQADV 3G61 HIS B 1284 UNP Q5I1Y5 EXPRESSION TAG
SEQRES 1 A 1284 MET GLU LEU GLU GLU ASP LEU LYS GLY ARG ALA ASP LYS
SEQRES 2 A 1284 ASN PHE SER LYS MET GLY LYS LYS SER LYS LYS GLU LYS
SEQRES 3 A 1284 LYS GLU LYS LYS PRO ALA VAL SER VAL LEU THR MET PHE
SEQRES 4 A 1284 ARG TYR ALA GLY TRP LEU ASP ARG LEU TYR MET LEU VAL
SEQRES 5 A 1284 GLY THR LEU ALA ALA ILE ILE HIS GLY VAL ALA LEU PRO
SEQRES 6 A 1284 LEU MET MET LEU ILE PHE GLY ASP MET THR ASP SER PHE
SEQRES 7 A 1284 ALA SER VAL GLY ASN VAL SER LYS ASN SER THR ASN MET
SEQRES 8 A 1284 SER GLU ALA ASP LYS ARG ALA MET PHE ALA LYS LEU GLU
SEQRES 9 A 1284 GLU GLU MET THR THR TYR ALA TYR TYR TYR THR GLY ILE
SEQRES 10 A 1284 GLY ALA GLY VAL LEU ILE VAL ALA TYR ILE GLN VAL SER
SEQRES 11 A 1284 PHE TRP CYS LEU ALA ALA GLY ARG GLN ILE HIS LYS ILE
SEQRES 12 A 1284 ARG GLN LYS PHE PHE HIS ALA ILE MET ASN GLN GLU ILE
SEQRES 13 A 1284 GLY TRP PHE ASP VAL HIS ASP VAL GLY GLU LEU ASN THR
SEQRES 14 A 1284 ARG LEU THR ASP ASP VAL SER LYS ILE ASN GLU GLY ILE
SEQRES 15 A 1284 GLY ASP LYS ILE GLY MET PHE PHE GLN ALA MET ALA THR
SEQRES 16 A 1284 PHE PHE GLY GLY PHE ILE ILE GLY PHE THR ARG GLY TRP
SEQRES 17 A 1284 LYS LEU THR LEU VAL ILE LEU ALA ILE SER PRO VAL LEU
SEQRES 18 A 1284 GLY LEU SER ALA GLY ILE TRP ALA LYS ILE LEU SER SER
SEQRES 19 A 1284 PHE THR ASP LYS GLU LEU HIS ALA TYR ALA LYS ALA GLY
SEQRES 20 A 1284 ALA VAL ALA GLU GLU VAL LEU ALA ALA ILE ARG THR VAL
SEQRES 21 A 1284 ILE ALA PHE GLY GLY GLN LYS LYS GLU LEU GLU ARG TYR
SEQRES 22 A 1284 ASN ASN ASN LEU GLU GLU ALA LYS ARG LEU GLY ILE LYS
SEQRES 23 A 1284 LYS ALA ILE THR ALA ASN ILE SER MET GLY ALA ALA PHE
SEQRES 24 A 1284 LEU LEU ILE TYR ALA SER TYR ALA LEU ALA PHE TRP TYR
SEQRES 25 A 1284 GLY THR SER LEU VAL ILE SER LYS GLU TYR SER ILE GLY
SEQRES 26 A 1284 GLN VAL LEU THR VAL PHE PHE SER VAL LEU ILE GLY ALA
SEQRES 27 A 1284 PHE SER VAL GLY GLN ALA SER PRO ASN ILE GLU ALA PHE
SEQRES 28 A 1284 ALA ASN ALA ARG GLY ALA ALA TYR GLU VAL PHE LYS ILE
SEQRES 29 A 1284 ILE ASP ASN LYS PRO SER ILE ASP SER PHE SER LYS SER
SEQRES 30 A 1284 GLY HIS LYS PRO ASP ASN ILE GLN GLY ASN LEU GLU PHE
SEQRES 31 A 1284 LYS ASN ILE HIS PHE SER TYR PRO SER ARG LYS GLU VAL
SEQRES 32 A 1284 GLN ILE LEU LYS GLY LEU ASN LEU LYS VAL LYS SER GLY
SEQRES 33 A 1284 GLN THR VAL ALA LEU VAL GLY ASN SER GLY CYS GLY LYS
SEQRES 34 A 1284 SER THR THR VAL GLN LEU MET GLN ARG LEU TYR ASP PRO
SEQRES 35 A 1284 LEU ASP GLY MET VAL SER ILE ASP GLY GLN ASP ILE ARG
SEQRES 36 A 1284 THR ILE ASN VAL ARG TYR LEU ARG GLU ILE ILE GLY VAL
SEQRES 37 A 1284 VAL SER GLN GLU PRO VAL LEU PHE ALA THR THR ILE ALA
SEQRES 38 A 1284 GLU ASN ILE ARG TYR GLY ARG GLU ASP VAL THR MET ASP
SEQRES 39 A 1284 GLU ILE GLU LYS ALA VAL LYS GLU ALA ASN ALA TYR ASP
SEQRES 40 A 1284 PHE ILE MET LYS LEU PRO HIS GLN PHE ASP THR LEU VAL
SEQRES 41 A 1284 GLY GLU ARG GLY ALA GLN LEU SER GLY GLY GLN LYS GLN
SEQRES 42 A 1284 ARG ILE ALA ILE ALA ARG ALA LEU VAL ARG ASN PRO LYS
SEQRES 43 A 1284 ILE LEU LEU LEU ASP GLU ALA THR SER ALA LEU ASP THR
SEQRES 44 A 1284 GLU SER GLU ALA VAL VAL GLN ALA ALA LEU ASP LYS ALA
SEQRES 45 A 1284 ARG GLU GLY ARG THR THR ILE VAL ILE ALA HIS ARG LEU
SEQRES 46 A 1284 SER THR VAL ARG ASN ALA ASP VAL ILE ALA GLY PHE ASP
SEQRES 47 A 1284 GLY GLY VAL ILE VAL GLU GLN GLY ASN HIS ASP GLU LEU
SEQRES 48 A 1284 MET ARG GLU LYS GLY ILE TYR PHE LYS LEU VAL MET THR
SEQRES 49 A 1284 GLN THR ALA GLY ASN GLU ILE GLU LEU GLY ASN GLU ALA
SEQRES 50 A 1284 CYS LYS SER LYS ASP GLU ILE ASP ASN LEU ASP MET SER
SEQRES 51 A 1284 SER LYS ASP SER GLY SER SER LEU ILE ARG ARG ARG SER
SEQRES 52 A 1284 THR ARG LYS SER ILE CYS GLY PRO HIS ASP GLN ASP ARG
SEQRES 53 A 1284 LYS LEU SER THR LYS GLU ALA LEU ASP GLU ASP VAL PRO
SEQRES 54 A 1284 PRO ALA SER PHE TRP ARG ILE LEU LYS LEU ASN SER THR
SEQRES 55 A 1284 GLU TRP PRO TYR PHE VAL VAL GLY ILE PHE CYS ALA ILE
SEQRES 56 A 1284 ILE ASN GLY GLY LEU GLN PRO ALA PHE SER VAL ILE PHE
SEQRES 57 A 1284 SER LYS VAL VAL GLY VAL PHE THR ASN GLY GLY PRO PRO
SEQRES 58 A 1284 GLU THR GLN ARG GLN ASN SER ASN LEU PHE SER LEU LEU
SEQRES 59 A 1284 PHE LEU ILE LEU GLY ILE ILE SER PHE ILE THR PHE PHE
SEQRES 60 A 1284 LEU GLN GLY PHE THR PHE GLY LYS ALA GLY GLU ILE LEU
SEQRES 61 A 1284 THR LYS ARG LEU ARG TYR MET VAL PHE LYS SER MET LEU
SEQRES 62 A 1284 ARG GLN ASP VAL SER TRP PHE ASP ASP PRO LYS ASN THR
SEQRES 63 A 1284 THR GLY ALA LEU THR THR ARG LEU ALA ASN ASP ALA ALA
SEQRES 64 A 1284 GLN VAL LYS GLY ALA THR GLY SER ARG LEU ALA VAL ILE
SEQRES 65 A 1284 PHE GLN ASN ILE ALA ASN LEU GLY THR GLY ILE ILE ILE
SEQRES 66 A 1284 SER LEU ILE TYR GLY TRP GLN LEU THR LEU LEU LEU LEU
SEQRES 67 A 1284 ALA ILE VAL PRO ILE ILE ALA ILE ALA GLY VAL VAL GLU
SEQRES 68 A 1284 MET LYS MET LEU SER GLY GLN ALA LEU LYS ASP LYS LYS
SEQRES 69 A 1284 GLU LEU GLU GLY SER GLY LYS ILE ALA THR GLU ALA ILE
SEQRES 70 A 1284 GLU ASN PHE ARG THR VAL VAL SER LEU THR ARG GLU GLN
SEQRES 71 A 1284 LYS PHE GLU THR MET TYR ALA GLN SER LEU GLN ILE PRO
SEQRES 72 A 1284 TYR ARG ASN ALA MET LYS LYS ALA HIS VAL PHE GLY ILE
SEQRES 73 A 1284 THR PHE SER PHE THR GLN ALA MET MET TYR PHE SER TYR
SEQRES 74 A 1284 ALA ALA CYS PHE ARG PHE GLY ALA TYR LEU VAL THR GLN
SEQRES 75 A 1284 GLN LEU MET THR PHE GLU ASN VAL LEU LEU VAL PHE SER
SEQRES 76 A 1284 ALA ILE VAL PHE GLY ALA MET ALA VAL GLY GLN VAL SER
SEQRES 77 A 1284 SER PHE ALA PRO ASP TYR ALA LYS ALA THR VAL SER ALA
SEQRES 78 A 1284 SER HIS ILE ILE ARG ILE ILE GLU LYS THR PRO GLU ILE
SEQRES 79 A 1284 ASP SER TYR SER THR GLN GLY LEU LYS PRO ASN MET LEU
SEQRES 80 A 1284 GLU GLY ASN VAL GLN PHE SER GLY VAL VAL PHE ASN TYR
SEQRES 81 A 1284 PRO THR ARG PRO SER ILE PRO VAL LEU GLN GLY LEU SER
SEQRES 82 A 1284 LEU GLU VAL LYS LYS GLY GLN THR LEU ALA LEU VAL GLY
SEQRES 83 A 1284 SER SER GLY CYS GLY LYS SER THR VAL VAL GLN LEU LEU
SEQRES 84 A 1284 GLU ARG PHE TYR ASP PRO MET ALA GLY SER VAL PHE LEU
SEQRES 85 A 1284 ASP GLY LYS GLU ILE LYS GLN LEU ASN VAL GLN TRP LEU
SEQRES 86 A 1284 ARG ALA GLN LEU GLY ILE VAL SER GLN GLU PRO ILE LEU
SEQRES 87 A 1284 PHE ASP CYS SER ILE ALA GLU ASN ILE ALA TYR GLY ASP
SEQRES 88 A 1284 ASN SER ARG VAL VAL SER TYR GLU GLU ILE VAL ARG ALA
SEQRES 89 A 1284 ALA LYS GLU ALA ASN ILE HIS GLN PHE ILE ASP SER LEU
SEQRES 90 A 1284 PRO ASP LYS TYR ASN THR ARG VAL GLY ASP LYS GLY THR
SEQRES 91 A 1284 GLN LEU SER GLY GLY GLN LYS GLN ARG ILE ALA ILE ALA
SEQRES 92 A 1284 ARG ALA LEU VAL ARG GLN PRO HIS ILE LEU LEU LEU ASP
SEQRES 93 A 1284 GLU ALA THR SER ALA LEU ASP THR GLU SER GLU LYS VAL
SEQRES 94 A 1284 VAL GLN GLU ALA LEU ASP LYS ALA ARG GLU GLY ARG THR
SEQRES 95 A 1284 CYS ILE VAL ILE ALA HIS ARG LEU SER THR ILE GLN ASN
SEQRES 96 A 1284 ALA ASP LEU ILE VAL VAL ILE GLN ASN GLY LYS VAL LYS
SEQRES 97 A 1284 GLU HIS GLY THR HIS GLN GLN LEU LEU ALA GLN LYS GLY
SEQRES 98 A 1284 ILE TYR PHE SER MET VAL SER VAL GLN ALA GLY ALA LYS
SEQRES 99 A 1284 ARG SER TYR VAL HIS HIS HIS HIS HIS HIS
SEQRES 1 B 1284 MET GLU LEU GLU GLU ASP LEU LYS GLY ARG ALA ASP LYS
SEQRES 2 B 1284 ASN PHE SER LYS MET GLY LYS LYS SER LYS LYS GLU LYS
SEQRES 3 B 1284 LYS GLU LYS LYS PRO ALA VAL SER VAL LEU THR MET PHE
SEQRES 4 B 1284 ARG TYR ALA GLY TRP LEU ASP ARG LEU TYR MET LEU VAL
SEQRES 5 B 1284 GLY THR LEU ALA ALA ILE ILE HIS GLY VAL ALA LEU PRO
SEQRES 6 B 1284 LEU MET MET LEU ILE PHE GLY ASP MET THR ASP SER PHE
SEQRES 7 B 1284 ALA SER VAL GLY ASN VAL SER LYS ASN SER THR ASN MET
SEQRES 8 B 1284 SER GLU ALA ASP LYS ARG ALA MET PHE ALA LYS LEU GLU
SEQRES 9 B 1284 GLU GLU MET THR THR TYR ALA TYR TYR TYR THR GLY ILE
SEQRES 10 B 1284 GLY ALA GLY VAL LEU ILE VAL ALA TYR ILE GLN VAL SER
SEQRES 11 B 1284 PHE TRP CYS LEU ALA ALA GLY ARG GLN ILE HIS LYS ILE
SEQRES 12 B 1284 ARG GLN LYS PHE PHE HIS ALA ILE MET ASN GLN GLU ILE
SEQRES 13 B 1284 GLY TRP PHE ASP VAL HIS ASP VAL GLY GLU LEU ASN THR
SEQRES 14 B 1284 ARG LEU THR ASP ASP VAL SER LYS ILE ASN GLU GLY ILE
SEQRES 15 B 1284 GLY ASP LYS ILE GLY MET PHE PHE GLN ALA MET ALA THR
SEQRES 16 B 1284 PHE PHE GLY GLY PHE ILE ILE GLY PHE THR ARG GLY TRP
SEQRES 17 B 1284 LYS LEU THR LEU VAL ILE LEU ALA ILE SER PRO VAL LEU
SEQRES 18 B 1284 GLY LEU SER ALA GLY ILE TRP ALA LYS ILE LEU SER SER
SEQRES 19 B 1284 PHE THR ASP LYS GLU LEU HIS ALA TYR ALA LYS ALA GLY
SEQRES 20 B 1284 ALA VAL ALA GLU GLU VAL LEU ALA ALA ILE ARG THR VAL
SEQRES 21 B 1284 ILE ALA PHE GLY GLY GLN LYS LYS GLU LEU GLU ARG TYR
SEQRES 22 B 1284 ASN ASN ASN LEU GLU GLU ALA LYS ARG LEU GLY ILE LYS
SEQRES 23 B 1284 LYS ALA ILE THR ALA ASN ILE SER MET GLY ALA ALA PHE
SEQRES 24 B 1284 LEU LEU ILE TYR ALA SER TYR ALA LEU ALA PHE TRP TYR
SEQRES 25 B 1284 GLY THR SER LEU VAL ILE SER LYS GLU TYR SER ILE GLY
SEQRES 26 B 1284 GLN VAL LEU THR VAL PHE PHE SER VAL LEU ILE GLY ALA
SEQRES 27 B 1284 PHE SER VAL GLY GLN ALA SER PRO ASN ILE GLU ALA PHE
SEQRES 28 B 1284 ALA ASN ALA ARG GLY ALA ALA TYR GLU VAL PHE LYS ILE
SEQRES 29 B 1284 ILE ASP ASN LYS PRO SER ILE ASP SER PHE SER LYS SER
SEQRES 30 B 1284 GLY HIS LYS PRO ASP ASN ILE GLN GLY ASN LEU GLU PHE
SEQRES 31 B 1284 LYS ASN ILE HIS PHE SER TYR PRO SER ARG LYS GLU VAL
SEQRES 32 B 1284 GLN ILE LEU LYS GLY LEU ASN LEU LYS VAL LYS SER GLY
SEQRES 33 B 1284 GLN THR VAL ALA LEU VAL GLY ASN SER GLY CYS GLY LYS
SEQRES 34 B 1284 SER THR THR VAL GLN LEU MET GLN ARG LEU TYR ASP PRO
SEQRES 35 B 1284 LEU ASP GLY MET VAL SER ILE ASP GLY GLN ASP ILE ARG
SEQRES 36 B 1284 THR ILE ASN VAL ARG TYR LEU ARG GLU ILE ILE GLY VAL
SEQRES 37 B 1284 VAL SER GLN GLU PRO VAL LEU PHE ALA THR THR ILE ALA
SEQRES 38 B 1284 GLU ASN ILE ARG TYR GLY ARG GLU ASP VAL THR MET ASP
SEQRES 39 B 1284 GLU ILE GLU LYS ALA VAL LYS GLU ALA ASN ALA TYR ASP
SEQRES 40 B 1284 PHE ILE MET LYS LEU PRO HIS GLN PHE ASP THR LEU VAL
SEQRES 41 B 1284 GLY GLU ARG GLY ALA GLN LEU SER GLY GLY GLN LYS GLN
SEQRES 42 B 1284 ARG ILE ALA ILE ALA ARG ALA LEU VAL ARG ASN PRO LYS
SEQRES 43 B 1284 ILE LEU LEU LEU ASP GLU ALA THR SER ALA LEU ASP THR
SEQRES 44 B 1284 GLU SER GLU ALA VAL VAL GLN ALA ALA LEU ASP LYS ALA
SEQRES 45 B 1284 ARG GLU GLY ARG THR THR ILE VAL ILE ALA HIS ARG LEU
SEQRES 46 B 1284 SER THR VAL ARG ASN ALA ASP VAL ILE ALA GLY PHE ASP
SEQRES 47 B 1284 GLY GLY VAL ILE VAL GLU GLN GLY ASN HIS ASP GLU LEU
SEQRES 48 B 1284 MET ARG GLU LYS GLY ILE TYR PHE LYS LEU VAL MET THR
SEQRES 49 B 1284 GLN THR ALA GLY ASN GLU ILE GLU LEU GLY ASN GLU ALA
SEQRES 50 B 1284 CYS LYS SER LYS ASP GLU ILE ASP ASN LEU ASP MET SER
SEQRES 51 B 1284 SER LYS ASP SER GLY SER SER LEU ILE ARG ARG ARG SER
SEQRES 52 B 1284 THR ARG LYS SER ILE CYS GLY PRO HIS ASP GLN ASP ARG
SEQRES 53 B 1284 LYS LEU SER THR LYS GLU ALA LEU ASP GLU ASP VAL PRO
SEQRES 54 B 1284 PRO ALA SER PHE TRP ARG ILE LEU LYS LEU ASN SER THR
SEQRES 55 B 1284 GLU TRP PRO TYR PHE VAL VAL GLY ILE PHE CYS ALA ILE
SEQRES 56 B 1284 ILE ASN GLY GLY LEU GLN PRO ALA PHE SER VAL ILE PHE
SEQRES 57 B 1284 SER LYS VAL VAL GLY VAL PHE THR ASN GLY GLY PRO PRO
SEQRES 58 B 1284 GLU THR GLN ARG GLN ASN SER ASN LEU PHE SER LEU LEU
SEQRES 59 B 1284 PHE LEU ILE LEU GLY ILE ILE SER PHE ILE THR PHE PHE
SEQRES 60 B 1284 LEU GLN GLY PHE THR PHE GLY LYS ALA GLY GLU ILE LEU
SEQRES 61 B 1284 THR LYS ARG LEU ARG TYR MET VAL PHE LYS SER MET LEU
SEQRES 62 B 1284 ARG GLN ASP VAL SER TRP PHE ASP ASP PRO LYS ASN THR
SEQRES 63 B 1284 THR GLY ALA LEU THR THR ARG LEU ALA ASN ASP ALA ALA
SEQRES 64 B 1284 GLN VAL LYS GLY ALA THR GLY SER ARG LEU ALA VAL ILE
SEQRES 65 B 1284 PHE GLN ASN ILE ALA ASN LEU GLY THR GLY ILE ILE ILE
SEQRES 66 B 1284 SER LEU ILE TYR GLY TRP GLN LEU THR LEU LEU LEU LEU
SEQRES 67 B 1284 ALA ILE VAL PRO ILE ILE ALA ILE ALA GLY VAL VAL GLU
SEQRES 68 B 1284 MET LYS MET LEU SER GLY GLN ALA LEU LYS ASP LYS LYS
SEQRES 69 B 1284 GLU LEU GLU GLY SER GLY LYS ILE ALA THR GLU ALA ILE
SEQRES 70 B 1284 GLU ASN PHE ARG THR VAL VAL SER LEU THR ARG GLU GLN
SEQRES 71 B 1284 LYS PHE GLU THR MET TYR ALA GLN SER LEU GLN ILE PRO
SEQRES 72 B 1284 TYR ARG ASN ALA MET LYS LYS ALA HIS VAL PHE GLY ILE
SEQRES 73 B 1284 THR PHE SER PHE THR GLN ALA MET MET TYR PHE SER TYR
SEQRES 74 B 1284 ALA ALA CYS PHE ARG PHE GLY ALA TYR LEU VAL THR GLN
SEQRES 75 B 1284 GLN LEU MET THR PHE GLU ASN VAL LEU LEU VAL PHE SER
SEQRES 76 B 1284 ALA ILE VAL PHE GLY ALA MET ALA VAL GLY GLN VAL SER
SEQRES 77 B 1284 SER PHE ALA PRO ASP TYR ALA LYS ALA THR VAL SER ALA
SEQRES 78 B 1284 SER HIS ILE ILE ARG ILE ILE GLU LYS THR PRO GLU ILE
SEQRES 79 B 1284 ASP SER TYR SER THR GLN GLY LEU LYS PRO ASN MET LEU
SEQRES 80 B 1284 GLU GLY ASN VAL GLN PHE SER GLY VAL VAL PHE ASN TYR
SEQRES 81 B 1284 PRO THR ARG PRO SER ILE PRO VAL LEU GLN GLY LEU SER
SEQRES 82 B 1284 LEU GLU VAL LYS LYS GLY GLN THR LEU ALA LEU VAL GLY
SEQRES 83 B 1284 SER SER GLY CYS GLY LYS SER THR VAL VAL GLN LEU LEU
SEQRES 84 B 1284 GLU ARG PHE TYR ASP PRO MET ALA GLY SER VAL PHE LEU
SEQRES 85 B 1284 ASP GLY LYS GLU ILE LYS GLN LEU ASN VAL GLN TRP LEU
SEQRES 86 B 1284 ARG ALA GLN LEU GLY ILE VAL SER GLN GLU PRO ILE LEU
SEQRES 87 B 1284 PHE ASP CYS SER ILE ALA GLU ASN ILE ALA TYR GLY ASP
SEQRES 88 B 1284 ASN SER ARG VAL VAL SER TYR GLU GLU ILE VAL ARG ALA
SEQRES 89 B 1284 ALA LYS GLU ALA ASN ILE HIS GLN PHE ILE ASP SER LEU
SEQRES 90 B 1284 PRO ASP LYS TYR ASN THR ARG VAL GLY ASP LYS GLY THR
SEQRES 91 B 1284 GLN LEU SER GLY GLY GLN LYS GLN ARG ILE ALA ILE ALA
SEQRES 92 B 1284 ARG ALA LEU VAL ARG GLN PRO HIS ILE LEU LEU LEU ASP
SEQRES 93 B 1284 GLU ALA THR SER ALA LEU ASP THR GLU SER GLU LYS VAL
SEQRES 94 B 1284 VAL GLN GLU ALA LEU ASP LYS ALA ARG GLU GLY ARG THR
SEQRES 95 B 1284 CYS ILE VAL ILE ALA HIS ARG LEU SER THR ILE GLN ASN
SEQRES 96 B 1284 ALA ASP LEU ILE VAL VAL ILE GLN ASN GLY LYS VAL LYS
SEQRES 97 B 1284 GLU HIS GLY THR HIS GLN GLN LEU LEU ALA GLN LYS GLY
SEQRES 98 B 1284 ILE TYR PHE SER MET VAL SER VAL GLN ALA GLY ALA LYS
SEQRES 99 B 1284 ARG SER TYR VAL HIS HIS HIS HIS HIS HIS
HET 2J8 A6001 36
HET 2J8 A6002 17
HET 2J8 B6003 36
HET 2J8 B6004 17
HETNAM 2J8 (4S,11S,18S)-4,11,18-TRI(PROPAN-2-YL)-6,13,20-
HETNAM 2 2J8 TRISELENA-3,10,17,22,23,24-
HETNAM 3 2J8 HEXAAZATETRACYCLO[17.2.1.1~5,8~.1~12,15~]TETRACOSA-
HETNAM 4 2J8 1(21),5(24),7,12(23),14,19(22)-HEXAENE-2,9,16-TRIONE
HETSYN 2J8 CYCLIC-TRIS-(S)-VALINESELENAZOLE; QZ59-SSS
FORMUL 3 2J8 4(C24 H30 N6 O3 SE3)
HELIX 1 1 VAL A 35 ARG A 40 1 6
HELIX 2 2 GLY A 43 SER A 88 1 46
HELIX 3 3 SER A 92 MET A 152 1 61
HELIX 4 4 ASN A 153 GLU A 155 5 3
HELIX 5 5 ILE A 156 VAL A 161 1 6
HELIX 6 6 GLY A 165 ARG A 206 1 42
HELIX 7 7 LYS A 209 VAL A 249 1 41
HELIX 8 8 ALA A 256 ALA A 262 1 7
HELIX 9 9 LYS A 268 ILE A 318 1 51
HELIX 10 10 VAL A 327 ASN A 367 1 41
HELIX 11 11 GLY A 428 MET A 436 1 9
HELIX 12 12 ASN A 458 ILE A 465 1 8
HELIX 13 13 THR A 479 ARG A 488 1 10
HELIX 14 14 THR A 492 ALA A 503 1 12
HELIX 15 15 ALA A 505 LEU A 512 1 8
HELIX 16 16 HIS A 514 THR A 518 5 5
HELIX 17 17 SER A 528 ASN A 544 1 17
HELIX 18 18 ASP A 558 ARG A 573 1 16
HELIX 19 19 ARG A 584 ASN A 590 1 7
HELIX 20 20 ASN A 607 ARG A 613 1 7
HELIX 21 21 GLY A 616 THR A 626 1 11
HELIX 22 22 TRP A 694 TRP A 704 1 11
HELIX 23 23 PHE A 707 ASN A 737 1 31
HELIX 24 24 GLU A 742 ARG A 794 1 53
HELIX 25 25 VAL A 797 ASP A 802 1 6
HELIX 26 26 THR A 806 TYR A 849 1 44
HELIX 27 27 GLN A 852 ASN A 899 1 48
HELIX 28 28 ARG A 908 TYR A 958 1 51
HELIX 29 29 ASN A 969 SER A 989 1 21
HELIX 30 30 TYR A 994 LYS A 1010 1 17
HELIX 31 31 THR A 1042 ILE A 1046 5 5
HELIX 32 32 GLY A 1071 ARG A 1081 1 11
HELIX 33 33 ASN A 1101 ARG A 1106 1 6
HELIX 34 34 SER A 1122 ALA A 1128 1 7
HELIX 35 35 SER A 1137 ALA A 1148 1 12
HELIX 36 36 ILE A 1150 SER A 1156 1 7
HELIX 37 37 SER A 1173 GLN A 1189 1 17
HELIX 38 38 ASP A 1203 ALA A 1217 1 15
HELIX 39 39 THR A 1252 GLN A 1259 1 8
HELIX 40 40 GLY A 1261 ALA A 1271 1 11
HELIX 41 41 VAL B 35 ARG B 40 1 6
HELIX 42 42 GLY B 43 SER B 88 1 46
HELIX 43 43 SER B 92 MET B 152 1 61
HELIX 44 44 ASN B 153 GLU B 155 5 3
HELIX 45 45 ILE B 156 VAL B 161 1 6
HELIX 46 46 GLY B 165 ARG B 206 1 42
HELIX 47 47 LYS B 209 VAL B 249 1 41
HELIX 48 48 ALA B 256 ALA B 262 1 7
HELIX 49 49 LYS B 268 ILE B 318 1 51
HELIX 50 50 VAL B 327 ASN B 367 1 41
HELIX 51 51 GLY B 428 GLN B 437 1 10
HELIX 52 52 ASN B 458 ILE B 465 1 8
HELIX 53 53 THR B 479 ARG B 488 1 10
HELIX 54 54 THR B 492 ALA B 503 1 12
HELIX 55 55 ALA B 505 LEU B 512 1 8
HELIX 56 56 HIS B 514 THR B 518 5 5
HELIX 57 57 SER B 528 ASN B 544 1 17
HELIX 58 58 ASP B 558 ARG B 573 1 16
HELIX 59 59 ARG B 584 ASN B 590 1 7
HELIX 60 60 ASN B 607 ARG B 613 1 7
HELIX 61 61 GLY B 616 THR B 626 1 11
HELIX 62 62 TRP B 694 TRP B 704 1 11
HELIX 63 63 PHE B 707 ASN B 737 1 31
HELIX 64 64 GLU B 742 ARG B 794 1 53
HELIX 65 65 VAL B 797 ASP B 802 1 6
HELIX 66 66 THR B 806 TYR B 849 1 44
HELIX 67 67 GLN B 852 ASN B 899 1 48
HELIX 68 68 ARG B 908 TYR B 958 1 51
HELIX 69 69 ASN B 969 SER B 989 1 21
HELIX 70 70 TYR B 994 GLU B 1009 1 16
HELIX 71 71 THR B 1042 ILE B 1046 5 5
HELIX 72 72 GLY B 1071 ARG B 1081 1 11
HELIX 73 73 ASN B 1101 ARG B 1106 1 6
HELIX 74 74 SER B 1122 ALA B 1128 1 7
HELIX 75 75 SER B 1137 ALA B 1148 1 12
HELIX 76 76 ILE B 1150 SER B 1156 1 7
HELIX 77 77 SER B 1173 GLN B 1189 1 17
HELIX 78 78 ASP B 1203 ALA B 1217 1 15
HELIX 79 79 THR B 1252 GLN B 1259 1 8
HELIX 80 80 GLY B 1261 ALA B 1271 1 11
SHEET 1 A 4 LEU A 409 VAL A 413 0
SHEET 2 A 4 LEU A 388 HIS A 394 -1 N PHE A 390 O LEU A 411
SHEET 3 A 4 ASP A 444 ILE A 449 -1 O SER A 448 N GLU A 389
SHEET 4 A 4 GLN A 452 ASP A 453 -1 O GLN A 452 N ILE A 449
SHEET 1 B 6 ILE A 466 VAL A 469 0
SHEET 2 B 6 ILE A 547 ASP A 551 1 O ILE A 547 N GLY A 467
SHEET 3 B 6 THR A 577 ILE A 581 1 O ILE A 581 N LEU A 550
SHEET 4 B 6 THR A 418 VAL A 422 1 N VAL A 419 O THR A 578
SHEET 5 B 6 VAL A 593 GLY A 596 1 O ALA A 595 N VAL A 422
SHEET 6 B 6 GLN A 605 GLY A 606 -1 O GLY A 606 N ILE A 594
SHEET 1 C 3 LEU A1054 VAL A1056 0
SHEET 2 C 3 VAL A1031 VAL A1037 -1 N PHE A1033 O LEU A1054
SHEET 3 C 3 ALA A1087 PHE A1091 -1 O SER A1089 N SER A1034
SHEET 1 D 6 ILE A1111 VAL A1112 0
SHEET 2 D 6 ILE A1192 ASP A1196 1 O LEU A1194 N VAL A1112
SHEET 3 D 6 THR A1222 ILE A1226 1 O ILE A1224 N LEU A1195
SHEET 4 D 6 THR A1061 VAL A1065 1 N LEU A1062 O CYS A1223
SHEET 5 D 6 LEU A1238 GLN A1243 1 O ILE A1242 N VAL A1065
SHEET 6 D 6 LYS A1246 GLY A1251 -1 O LYS A1246 N GLN A1243
SHEET 1 E 4 LEU B 409 VAL B 413 0
SHEET 2 E 4 LEU B 388 HIS B 394 -1 N PHE B 390 O LEU B 411
SHEET 3 E 4 ASP B 444 ILE B 449 -1 O SER B 448 N GLU B 389
SHEET 4 E 4 GLN B 452 ASP B 453 -1 O GLN B 452 N ILE B 449
SHEET 1 F 6 ILE B 466 VAL B 469 0
SHEET 2 F 6 ILE B 547 ASP B 551 1 O ILE B 547 N GLY B 467
SHEET 3 F 6 THR B 577 ILE B 581 1 O ILE B 581 N LEU B 550
SHEET 4 F 6 THR B 418 VAL B 422 1 N VAL B 419 O THR B 578
SHEET 5 F 6 VAL B 593 GLY B 596 1 O ALA B 595 N VAL B 422
SHEET 6 F 6 GLN B 605 GLY B 606 -1 O GLY B 606 N ILE B 594
SHEET 1 G 3 GLU B1055 VAL B1056 0
SHEET 2 G 3 VAL B1031 VAL B1037 -1 N VAL B1031 O VAL B1056
SHEET 3 G 3 ALA B1087 PHE B1091 -1 O SER B1089 N SER B1034
SHEET 1 H 6 ILE B1111 VAL B1112 0
SHEET 2 H 6 ILE B1192 ASP B1196 1 O LEU B1194 N VAL B1112
SHEET 3 H 6 THR B1222 ILE B1226 1 O ILE B1224 N LEU B1195
SHEET 4 H 6 THR B1061 VAL B1065 1 N LEU B1062 O CYS B1223
SHEET 5 H 6 LEU B1238 GLN B1243 1 O ILE B1242 N VAL B1065
SHEET 6 H 6 LYS B1246 GLY B1251 -1 O LYS B1246 N GLN B1243
SITE 1 AC1 5 LEU A 300 TYR A 303 PHE A 339 VAL A 978
SITE 2 AC1 5 GLY A 985
SITE 1 AC2 7 PHE A 332 PHE A 728 TYR A 949 LEU A 971
SITE 2 AC2 7 PHE A 974 ILE A 977 VAL A 978
SITE 1 AC3 9 TYR B 303 PHE B 339 GLN B 721 PHE B 724
SITE 2 AC3 9 VAL B 978 MET B 982 GLY B 985 GLN B 986
SITE 3 AC3 9 SER B 989
SITE 1 AC4 5 PHE B 332 ILE B 336 TYR B 949 PHE B 974
SITE 2 AC4 5 VAL B 978
CRYST1 97.742 114.978 375.810 90.00 90.00 90.00 P 21 21 21 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 0.010231 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008697 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002661 0.00000
(ATOM LINES ARE NOT SHOWN.)
END