HEADER APOPTOSIS REGULATOR/INHIBITOR 16-AUG-13 4MAN
TITLE BCL_2-NAVITOCLAX ANALOG (WITH INDOLE) 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
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 3 15-NOV-17 4MAN 1 REMARK
REVDAT 2 02-AUG-17 4MAN 1 SOURCE REMARK
REVDAT 1 29-JAN-14 4MAN 0
SPRSDE 29-JAN-14 4MAN 4LXE
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. 2.07 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.4
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) : 2.07
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 30912
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) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1561
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 : 16
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.07
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.14
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.88
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2829
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2362
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2672
REMARK 3 BIN R VALUE (WORKING SET) : 0.2362
REMARK 3 BIN FREE R VALUE : 0.2351
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.55
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 157
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 : 2266
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 130
REMARK 3 SOLVENT ATOMS : 260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.00600
REMARK 3 B22 (A**2) : -4.00600
REMARK 3 B33 (A**2) : 8.01210
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) : 0.267
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) : 0.160
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 : 0.926
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2509 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3425 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 840 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 58 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 416 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2509 ; 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 : 272 ; 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 : 3055 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.04
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.63
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.67
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 4MAN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000081676.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
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 : MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30912
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.070
REMARK 200 RESOLUTION RANGE LOW (A) : 18.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
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) : 2.07
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
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 (%): 63.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M LI2SO4, 0.1 M TRIS HCL, PH 8.5,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 50.74600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 76.11900
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 25.37300
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 ALA A 2
REMARK 465 GLY A 3
REMARK 465 ARG A 4
REMARK 465 THR A 5
REMARK 465 TRP A 28
REMARK 465 ASP A 29
REMARK 465 ALA A 30
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 87
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 ALA B 2
REMARK 465 GLY B 3
REMARK 465 ARG B 4
REMARK 465 THR B 5
REMARK 465 TRP B 28
REMARK 465 ASP B 29
REMARK 465 ALA B 30
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 87
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: 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 7 -119.39 -68.78
REMARK 500 TYR B 7 -139.28 -175.19
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 1Y1 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1Y1 B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LVT RELATED DB: PDB
REMARK 900 RELATED ID: 4LXD RELATED DB: PDB
DBREF 4MAN A -1 32 UNP P10415 BCL2_HUMAN 1 34
DBREF 4MAN A 89 204 UNP P10415 BCL2_HUMAN 92 207
DBREF 4MAN B -1 32 UNP P10415 BCL2_HUMAN 1 34
DBREF 4MAN B 89 204 UNP P10415 BCL2_HUMAN 92 207
SEQADV 4MAN ASP A 73 UNP P10415 LINKER
SEQADV 4MAN VAL A 74 UNP P10415 LINKER
SEQADV 4MAN GLU A 75 UNP P10415 LINKER
SEQADV 4MAN GLU A 76 UNP P10415 LINKER
SEQADV 4MAN ASN A 77 UNP P10415 LINKER
SEQADV 4MAN ARG A 78 UNP P10415 LINKER
SEQADV 4MAN THR A 79 UNP P10415 LINKER
SEQADV 4MAN GLU A 80 UNP P10415 LINKER
SEQADV 4MAN ALA A 81 UNP P10415 LINKER
SEQADV 4MAN PRO A 82 UNP P10415 LINKER
SEQADV 4MAN GLU A 83 UNP P10415 LINKER
SEQADV 4MAN GLY A 84 UNP P10415 LINKER
SEQADV 4MAN THR A 85 UNP P10415 LINKER
SEQADV 4MAN GLU A 86 UNP P10415 LINKER
SEQADV 4MAN SER A 87 UNP P10415 LINKER
SEQADV 4MAN GLU A 88 UNP P10415 LINKER
SEQADV 4MAN ASP B 73 UNP P10415 LINKER
SEQADV 4MAN VAL B 74 UNP P10415 LINKER
SEQADV 4MAN GLU B 75 UNP P10415 LINKER
SEQADV 4MAN GLU B 76 UNP P10415 LINKER
SEQADV 4MAN ASN B 77 UNP P10415 LINKER
SEQADV 4MAN ARG B 78 UNP P10415 LINKER
SEQADV 4MAN THR B 79 UNP P10415 LINKER
SEQADV 4MAN GLU B 80 UNP P10415 LINKER
SEQADV 4MAN ALA B 81 UNP P10415 LINKER
SEQADV 4MAN PRO B 82 UNP P10415 LINKER
SEQADV 4MAN GLU B 83 UNP P10415 LINKER
SEQADV 4MAN GLY B 84 UNP P10415 LINKER
SEQADV 4MAN THR B 85 UNP P10415 LINKER
SEQADV 4MAN GLU B 86 UNP P10415 LINKER
SEQADV 4MAN SER B 87 UNP P10415 LINKER
SEQADV 4MAN GLU B 88 UNP P10415 LINKER
SEQRES 1 A 166 MET ALA HIS ALA 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 ALA 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 1Y1 A 301 84
HET 1Y1 B 301 85
HETNAM 1Y1 4-[4-({4'-CHLORO-3-[2-(DIMETHYLAMINO)ETHOXY]BIPHENYL-2-
HETNAM 2 1Y1 YL}METHYL)PIPERAZIN-1-YL]-2-(1H-INDOL-5-YLOXY)-N-({3-
HETNAM 3 1Y1 NITRO-4-[(TETRAHYDRO-2H-PYRAN-4-YLMETHYL)
HETNAM 4 1Y1 AMINO]PHENYL}SULFONYL)BENZAMIDE
FORMUL 3 1Y1 2(C48 H52 CL N7 O8 S)
FORMUL 5 HOH *260(H2 O)
HELIX 1 1 ASP A 8 ARG A 24 1 17
HELIX 2 2 VAL A 89 TYR A 105 1 17
HELIX 3 3 TYR A 105 SER A 114 1 10
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 190 GLY A 200 1 11
HELIX 9 9 ASP B 8 ARG B 24 1 17
HELIX 10 10 VAL B 89 TYR B 105 1 17
HELIX 11 11 TYR B 105 SER B 114 1 10
HELIX 12 12 THR B 122 ARG B 136 1 15
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 190 GLY B 200 1 11
SITE 1 AC1 21 ALA A 97 ASP A 100 PHE A 101 TYR A 105
SITE 2 AC1 21 ASP A 108 PHE A 109 MET A 112 LEU A 134
SITE 3 AC1 21 TRP A 141 GLY A 142 ARG A 143 ALA A 146
SITE 4 AC1 21 ASN A 160 GLU A 162 SER A 164 PRO A 165
SITE 5 AC1 21 TYR A 199 HOH A 406 HOH A 519 HOH A 521
SITE 6 AC1 21 HOH A 531
SITE 1 AC2 20 HOH A 501 ALA B 97 ASP B 100 PHE B 101
SITE 2 AC2 20 TYR B 105 ASP B 108 PHE B 109 MET B 112
SITE 3 AC2 20 LEU B 134 TRP B 141 GLY B 142 ARG B 143
SITE 4 AC2 20 ALA B 146 GLU B 162 SER B 164 PRO B 165
SITE 5 AC2 20 TYR B 199 HOH B 406 HOH B 518 HOH B 524
CRYST1 71.375 71.375 101.492 90.00 90.00 90.00 P 43 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 0.014011 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014011 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009853 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
