HEADER APOPTOSIS REGULATOR/INHIBITOR 26-JUL-13 4LVT
TITLE BCL_2-NAVITOCLAX (ABT-263) COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPTOSIS REGULATOR BCL-2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 1-34, 92-207;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BCL2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS 8 HELICES, APOPTOSIS REGULATOR-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.H.PARK
REVDAT 2 02-AUG-17 4LVT 1 SOURCE REMARK
REVDAT 1 14-AUG-13 4LVT 0
JRNL AUTH A.J.SOUERS,J.D.LEVERSON,E.R.BOGHAERT,S.L.ACKLER,N.D.CATRON,
JRNL AUTH 2 J.CHEN,B.D.DAYTON,H.DING,S.H.ENSCHEDE,W.J.FAIRBROTHER,
JRNL AUTH 3 D.C.HUANG,S.G.HYMOWITZ,S.JIN,S.L.KHAW,P.J.KOVAR,L.T.LAM,
JRNL AUTH 4 J.LEE,H.L.MAECKER,K.C.MARSH,K.D.MASON,M.J.MITTEN,P.M.NIMMER,
JRNL AUTH 5 A.OLEKSIJEW,C.H.PARK,C.M.PARK,D.C.PHILLIPS,A.W.ROBERTS,
JRNL AUTH 6 D.SAMPATH,J.F.SEYMOUR,M.L.SMITH,G.M.SULLIVAN,S.K.TAHIR,
JRNL AUTH 7 C.TSE,M.D.WENDT,Y.XIAO,J.C.XUE,H.ZHANG,R.A.HUMERICKHOUSE,
JRNL AUTH 8 S.H.ROSENBERG,S.W.ELMORE
JRNL TITL ABT-199, A POTENT AND SELECTIVE BCL-2 INHIBITOR, ACHIEVES
JRNL TITL 2 ANTITUMOR ACTIVITY WHILE SPARING PLATELETS.
JRNL REF NAT.MED. (N.Y.) V. 19 202 2013
JRNL REFN ISSN 1078-8956
JRNL PMID 23291630
JRNL DOI 10.1038/NM.3048
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT 2.5.1
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 19115
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.150
REMARK 3 FREE R VALUE TEST SET COUNT : 984
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 : 9
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.17
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.55
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3019
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1761
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2864
REMARK 3 BIN R VALUE (WORKING SET) : 0.1733
REMARK 3 BIN FREE R VALUE : 0.2309
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.13
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 155
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 : 2324
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 130
REMARK 3 SOLVENT ATOMS : 175
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.07
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.80522
REMARK 3 B22 (A**2) : 5.96173
REMARK 3 B33 (A**2) : 3.84349
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.95546
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
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 : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : NULL ; NULL ; NULL
REMARK 3 BOND ANGLES : NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : NULL ; NULL ; NULL
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 : NULL ; NULL ; NULL
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 : NULL ; NULL ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL
REMARK 3 OTHER TORSION ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4LVT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1000081148.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19115
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 65.120
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
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) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5 M (NH4)2SO4, 0.1 M NA ACETATE, 0.2
REMARK 280 M NACL, PH 4.2, VAPOR DIFFUSION, TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 34.04000
REMARK 290 SMTRY3 2 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 ALA A 0
REMARK 465 HIS A 1
REMARK 465 PRO A 2
REMARK 465 GLY A 3
REMARK 465 ARG A 4
REMARK 465 THR A 5
REMARK 465 GLY A 6
REMARK 465 GLY A 31
REMARK 465 ASP A 32
REMARK 465 ASP A 73
REMARK 465 VAL A 74
REMARK 465 GLU A 75
REMARK 465 GLU A 76
REMARK 465 ASN A 77
REMARK 465 ARG A 78
REMARK 465 THR A 79
REMARK 465 GLU A 80
REMARK 465 ALA A 81
REMARK 465 PRO A 82
REMARK 465 GLU A 83
REMARK 465 GLY A 84
REMARK 465 THR A 85
REMARK 465 GLU A 86
REMARK 465 SER A 202
REMARK 465 MET A 203
REMARK 465 ARG A 204
REMARK 465 MET B -1
REMARK 465 ALA B 0
REMARK 465 HIS B 1
REMARK 465 PRO B 2
REMARK 465 GLY B 3
REMARK 465 ARG B 4
REMARK 465 THR B 5
REMARK 465 GLY B 6
REMARK 465 GLY B 31
REMARK 465 ASP B 32
REMARK 465 ASP B 73
REMARK 465 VAL B 74
REMARK 465 GLU B 75
REMARK 465 GLU B 76
REMARK 465 ASN B 77
REMARK 465 ARG B 78
REMARK 465 THR B 79
REMARK 465 GLU B 80
REMARK 465 ALA B 81
REMARK 465 PRO B 82
REMARK 465 GLU B 83
REMARK 465 GLY B 84
REMARK 465 THR B 85
REMARK 465 GLU B 86
REMARK 465 SER B 202
REMARK 465 MET B 203
REMARK 465 ARG B 204
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 201 C - N - CD ANGL. DEV. = -22.4 DEGREES
REMARK 500 PRO B 201 C - N - CD ANGL. DEV. = -22.0 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 TYR A 105 53.28 -119.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1XJ A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1XJ B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LXD RELATED DB: PDB
REMARK 900 RELATED ID: 4LXE RELATED DB: PDB
DBREF 4LVT A -1 32 UNP P10415 BCL2_HUMAN 1 34
DBREF 4LVT A 89 204 UNP P10415 BCL2_HUMAN 92 207
DBREF 4LVT B -1 32 UNP P10415 BCL2_HUMAN 1 34
DBREF 4LVT B 89 204 UNP P10415 BCL2_HUMAN 92 207
SEQADV 4LVT PRO A 2 UNP P10415 ALA 4 ENGINEERED MUTATION
SEQADV 4LVT ASP A 73 UNP P10415 LINKER
SEQADV 4LVT VAL A 74 UNP P10415 LINKER
SEQADV 4LVT GLU A 75 UNP P10415 LINKER
SEQADV 4LVT GLU A 76 UNP P10415 LINKER
SEQADV 4LVT ASN A 77 UNP P10415 LINKER
SEQADV 4LVT ARG A 78 UNP P10415 LINKER
SEQADV 4LVT THR A 79 UNP P10415 LINKER
SEQADV 4LVT GLU A 80 UNP P10415 LINKER
SEQADV 4LVT ALA A 81 UNP P10415 LINKER
SEQADV 4LVT PRO A 82 UNP P10415 LINKER
SEQADV 4LVT GLU A 83 UNP P10415 LINKER
SEQADV 4LVT GLY A 84 UNP P10415 LINKER
SEQADV 4LVT THR A 85 UNP P10415 LINKER
SEQADV 4LVT GLU A 86 UNP P10415 LINKER
SEQADV 4LVT SER A 87 UNP P10415 LINKER
SEQADV 4LVT GLU A 88 UNP P10415 LINKER
SEQADV 4LVT PRO B 2 UNP P10415 ALA 4 ENGINEERED MUTATION
SEQADV 4LVT ASP B 73 UNP P10415 LINKER
SEQADV 4LVT VAL B 74 UNP P10415 LINKER
SEQADV 4LVT GLU B 75 UNP P10415 LINKER
SEQADV 4LVT GLU B 76 UNP P10415 LINKER
SEQADV 4LVT ASN B 77 UNP P10415 LINKER
SEQADV 4LVT ARG B 78 UNP P10415 LINKER
SEQADV 4LVT THR B 79 UNP P10415 LINKER
SEQADV 4LVT GLU B 80 UNP P10415 LINKER
SEQADV 4LVT ALA B 81 UNP P10415 LINKER
SEQADV 4LVT PRO B 82 UNP P10415 LINKER
SEQADV 4LVT GLU B 83 UNP P10415 LINKER
SEQADV 4LVT GLY B 84 UNP P10415 LINKER
SEQADV 4LVT THR B 85 UNP P10415 LINKER
SEQADV 4LVT GLU B 86 UNP P10415 LINKER
SEQADV 4LVT SER B 87 UNP P10415 LINKER
SEQADV 4LVT GLU B 88 UNP P10415 LINKER
SEQRES 1 A 166 MET ALA HIS PRO GLY ARG THR GLY TYR ASP ASN ARG GLU
SEQRES 2 A 166 ILE VAL MET LYS TYR ILE HIS TYR LYS LEU SER GLN ARG
SEQRES 3 A 166 GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL GLU GLU ASN
SEQRES 4 A 166 ARG THR GLU ALA PRO GLU GLY THR GLU SER GLU VAL VAL
SEQRES 5 A 166 HIS LEU THR LEU ARG GLN ALA GLY ASP ASP PHE SER ARG
SEQRES 6 A 166 ARG TYR ARG ARG ASP PHE ALA GLU MET SER SER GLN LEU
SEQRES 7 A 166 HIS LEU THR PRO PHE THR ALA ARG GLY ARG PHE ALA THR
SEQRES 8 A 166 VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL ASN TRP GLY
SEQRES 9 A 166 ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY VAL MET CYS
SEQRES 10 A 166 VAL GLU SER VAL ASN ARG GLU MET SER PRO LEU VAL ASP
SEQRES 11 A 166 ASN ILE ALA LEU TRP MET THR GLU TYR LEU ASN ARG HIS
SEQRES 12 A 166 LEU HIS THR TRP ILE GLN ASP ASN GLY GLY TRP ASP ALA
SEQRES 13 A 166 PHE VAL GLU LEU TYR GLY PRO SER MET ARG
SEQRES 1 B 166 MET ALA HIS PRO GLY ARG THR GLY TYR ASP ASN ARG GLU
SEQRES 2 B 166 ILE VAL MET LYS TYR ILE HIS TYR LYS LEU SER GLN ARG
SEQRES 3 B 166 GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL GLU GLU ASN
SEQRES 4 B 166 ARG THR GLU ALA PRO GLU GLY THR GLU SER GLU VAL VAL
SEQRES 5 B 166 HIS LEU THR LEU ARG GLN ALA GLY ASP ASP PHE SER ARG
SEQRES 6 B 166 ARG TYR ARG ARG ASP PHE ALA GLU MET SER SER GLN LEU
SEQRES 7 B 166 HIS LEU THR PRO PHE THR ALA ARG GLY ARG PHE ALA THR
SEQRES 8 B 166 VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL ASN TRP GLY
SEQRES 9 B 166 ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY VAL MET CYS
SEQRES 10 B 166 VAL GLU SER VAL ASN ARG GLU MET SER PRO LEU VAL ASP
SEQRES 11 B 166 ASN ILE ALA LEU TRP MET THR GLU TYR LEU ASN ARG HIS
SEQRES 12 B 166 LEU HIS THR TRP ILE GLN ASP ASN GLY GLY TRP ASP ALA
SEQRES 13 B 166 PHE VAL GLU LEU TYR GLY PRO SER MET ARG
HET 1XJ A 301 65
HET 1XJ B 301 65
HETNAM 1XJ 4-(4-{[2-(4-CHLOROPHENYL)-5,5-DIMETHYLCYCLOHEX-1-EN-1-
HETNAM 2 1XJ YL]METHYL}PIPERAZIN-1-YL)-N-[(4-{[(2R)-4-(MORPHOLIN-4-
HETNAM 3 1XJ YL)-1-(PHENYLSULFANYL)BUTAN-2-YL]AMINO}-3-
HETNAM 4 1XJ [(TRIFLUOROMETHYL)SULFONYL]PHENYL)SULFONYL]BENZAMIDE
FORMUL 3 1XJ 2(C47 H55 CL F3 N5 O6 S3)
FORMUL 5 HOH *175(H2 O)
HELIX 1 1 ASP A 8 GLN A 23 1 16
HELIX 2 2 GLU A 88 TYR A 105 1 18
HELIX 3 3 TYR A 105 GLN A 115 1 11
HELIX 4 4 THR A 122 PHE A 135 1 14
HELIX 5 5 ASN A 140 ARG A 161 1 22
HELIX 6 6 PRO A 165 LEU A 182 1 18
HELIX 7 7 LEU A 182 ASN A 189 1 8
HELIX 8 8 GLY A 191 GLY A 200 1 10
HELIX 9 9 ASP B 8 GLN B 23 1 16
HELIX 10 10 GLU B 88 TYR B 105 1 18
HELIX 11 11 TYR B 105 GLN B 115 1 11
HELIX 12 12 THR B 122 PHE B 135 1 14
HELIX 13 13 ASN B 140 ARG B 161 1 22
HELIX 14 14 PRO B 165 LEU B 182 1 18
HELIX 15 15 LEU B 182 ASN B 189 1 8
HELIX 16 16 GLY B 191 GLY B 200 1 10
CISPEP 1 GLY A 200 PRO A 201 0 6.16
CISPEP 2 GLY B 200 PRO B 201 0 6.68
SITE 1 AC1 19 ALA A 97 ASP A 100 PHE A 101 ARG A 104
SITE 2 AC1 19 TYR A 105 ASP A 108 PHE A 109 ASN A 140
SITE 3 AC1 19 TRP A 141 GLY A 142 ARG A 143 VAL A 145
SITE 4 AC1 19 ALA A 146 PHE A 195 LEU A 198 TYR A 199
SITE 5 AC1 19 HOH A 431 HOH A 434 HOH A 491
SITE 1 AC2 16 ALA B 97 ASP B 100 PHE B 101 TYR B 105
SITE 2 AC2 16 PHE B 109 VAL B 130 ASN B 140 TRP B 141
SITE 3 AC2 16 GLY B 142 VAL B 145 ALA B 146 VAL B 153
SITE 4 AC2 16 PHE B 195 LEU B 198 TYR B 199 HOH B 456
CRYST1 34.770 68.080 65.470 90.00 95.96 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.028760 0.000000 0.003003 0.00000
SCALE2 0.000000 0.014689 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015357 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
