HEADER TRANSCRIPTION/INHIBITOR 07-APR-17 5VFC
TITLE WDR5 BOUND TO INHIBITOR MM-589
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: WD REPEAT-CONTAINING PROTEIN 5;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BMP2-INDUCED 3-KB GENE PROTEIN;
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: WDR5, BIG3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS INHIBITOR, COMPLEX, WD REPEAT, TRANSCRIPTION, TRANSCRIPTION-INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.STUCKEY
REVDAT 5 13-MAR-24 5VFC 1 REMARK
REVDAT 4 04-DEC-19 5VFC 1 REMARK
REVDAT 3 20-SEP-17 5VFC 1 REMARK
REVDAT 2 05-JUL-17 5VFC 1 JRNL
REVDAT 1 28-JUN-17 5VFC 0
JRNL AUTH H.KARATAS,Y.LI,L.LIU,J.JI,S.LEE,Y.CHEN,J.YANG,L.HUANG,
JRNL AUTH 2 D.BERNARD,J.XU,E.C.TOWNSEND,F.CAO,X.RAN,X.LI,B.WEN,D.SUN,
JRNL AUTH 3 J.A.STUCKEY,M.LEI,Y.DOU,S.WANG
JRNL TITL DISCOVERY OF A HIGHLY POTENT, CELL-PERMEABLE MACROCYCLIC
JRNL TITL 2 PEPTIDOMIMETIC (MM-589) TARGETING THE WD REPEAT DOMAIN 5
JRNL TITL 3 PROTEIN (WDR5)-MIXED LINEAGE LEUKEMIA (MLL) PROTEIN-PROTEIN
JRNL TITL 4 INTERACTION.
JRNL REF J. MED. CHEM. V. 60 4818 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 28603984
JRNL DOI 10.1021/ACS.JMEDCHEM.6B01796
REMARK 2
REMARK 2 RESOLUTION. 1.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
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) : 1.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 35269
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) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.174
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 1807
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 18
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.64
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.69
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.34
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2817
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1380
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2664
REMARK 3 BIN R VALUE (WORKING SET) : 0.1360
REMARK 3 BIN FREE R VALUE : 0.1740
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.43
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 153
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2327
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 74
REMARK 3 SOLVENT ATOMS : 215
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.98
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.48530
REMARK 3 B22 (A**2) : 0.07450
REMARK 3 B33 (A**2) : -0.55980
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.45610
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.150
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.081
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.078
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.079
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.078
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 : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
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 : 3440 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 837 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 54 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 378 ; 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 : 328 ; 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 : 3116 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.14
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 5.23
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 13.58
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2505 0.3083 15.4169
REMARK 3 T TENSOR
REMARK 3 T11: -0.0184 T22: -0.0231
REMARK 3 T33: -0.0435 T12: 0.0014
REMARK 3 T13: -0.0006 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 0.6087 L22: 0.5516
REMARK 3 L33: 0.4763 L12: -0.1684
REMARK 3 L13: 0.0366 L23: 0.1970
REMARK 3 S TENSOR
REMARK 3 S11: 0.0406 S12: 0.0983 S13: 0.0074
REMARK 3 S21: -0.0686 S22: -0.0039 S23: 0.0170
REMARK 3 S31: -0.0185 S32: 0.0113 S33: -0.0367
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5VFC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1000227345.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-NOV-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9787
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300-HS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35269
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640
REMARK 200 RESOLUTION RANGE LOW (A) : 15.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA BIS-TRIS PH 6.5, 26% PEG 8000
REMARK 280 AND 0.1 M AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 44.17400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.27950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 44.17400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.27950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 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 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 THR A 24
REMARK 465 GLN A 25
REMARK 465 SER A 26
REMARK 465 LYS A 27
REMARK 465 PRO A 28
REMARK 465 THR A 29
REMARK 465 PRO A 30
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 VAL A 31 CG1 CG2
REMARK 470 LYS A 78 CG CD CE NZ
REMARK 470 LYS A 87 CE NZ
REMARK 470 LYS A 120 CG CD CE NZ
REMARK 470 LYS A 159 CD CE NZ
REMARK 470 LYS A 207 CE NZ
REMARK 470 LYS A 227 CD CE NZ
REMARK 470 LYS A 245 CD CE NZ
REMARK 470 LYS A 247 CG CD CE NZ
REMARK 470 LYS A 331 CD CE NZ
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 LEU A 234 47.65 -78.84
REMARK 500 LYS A 259 -45.57 -131.26
REMARK 500 LYS A 291 -2.12 76.63
REMARK 500 ASP A 324 -62.00 -134.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 630
REMARK 630 MOLECULE TYPE: CYCLIC PEPTIDE INHIBITOR
REMARK 630 MOLECULE NAME: N-{(3R,6S,9S,12R)-6-ETHYL-12-METHYL-9-[3-(N'-
REMARK 630 METHYLCARBAMIMIDAMIDO)PROPYL]-2,5,8,11-TETRAOXO-3-PHENYL-1,4,7,10-
REMARK 630 TETRAAZACYCLOTETRADECAN-12-YL}-2-METHYLPROPANAMIDE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 9BA A 401
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: NMM ABA 9BP PG9
REMARK 630 DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9BA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 409
DBREF 5VFC A 24 334 UNP P61964 WDR5_HUMAN 24 334
SEQRES 1 A 311 THR GLN SER LYS PRO THR PRO VAL LYS PRO ASN TYR ALA
SEQRES 2 A 311 LEU LYS PHE THR LEU ALA GLY HIS THR LYS ALA VAL SER
SEQRES 3 A 311 SER VAL LYS PHE SER PRO ASN GLY GLU TRP LEU ALA SER
SEQRES 4 A 311 SER SER ALA ASP LYS LEU ILE LYS ILE TRP GLY ALA TYR
SEQRES 5 A 311 ASP GLY LYS PHE GLU LYS THR ILE SER GLY HIS LYS LEU
SEQRES 6 A 311 GLY ILE SER ASP VAL ALA TRP SER SER ASP SER ASN LEU
SEQRES 7 A 311 LEU VAL SER ALA SER ASP ASP LYS THR LEU LYS ILE TRP
SEQRES 8 A 311 ASP VAL SER SER GLY LYS CYS LEU LYS THR LEU LYS GLY
SEQRES 9 A 311 HIS SER ASN TYR VAL PHE CYS CYS ASN PHE ASN PRO GLN
SEQRES 10 A 311 SER ASN LEU ILE VAL SER GLY SER PHE ASP GLU SER VAL
SEQRES 11 A 311 ARG ILE TRP ASP VAL LYS THR GLY LYS CYS LEU LYS THR
SEQRES 12 A 311 LEU PRO ALA HIS SER ASP PRO VAL SER ALA VAL HIS PHE
SEQRES 13 A 311 ASN ARG ASP GLY SER LEU ILE VAL SER SER SER TYR ASP
SEQRES 14 A 311 GLY LEU CYS ARG ILE TRP ASP THR ALA SER GLY GLN CYS
SEQRES 15 A 311 LEU LYS THR LEU ILE ASP ASP ASP ASN PRO PRO VAL SER
SEQRES 16 A 311 PHE VAL LYS PHE SER PRO ASN GLY LYS TYR ILE LEU ALA
SEQRES 17 A 311 ALA THR LEU ASP ASN THR LEU LYS LEU TRP ASP TYR SER
SEQRES 18 A 311 LYS GLY LYS CYS LEU LYS THR TYR THR GLY HIS LYS ASN
SEQRES 19 A 311 GLU LYS TYR CYS ILE PHE ALA ASN PHE SER VAL THR GLY
SEQRES 20 A 311 GLY LYS TRP ILE VAL SER GLY SER GLU ASP ASN LEU VAL
SEQRES 21 A 311 TYR ILE TRP ASN LEU GLN THR LYS GLU ILE VAL GLN LYS
SEQRES 22 A 311 LEU GLN GLY HIS THR ASP VAL VAL ILE SER THR ALA CYS
SEQRES 23 A 311 HIS PRO THR GLU ASN ILE ILE ALA SER ALA ALA LEU GLU
SEQRES 24 A 311 ASN ASP LYS THR ILE LYS LEU TRP LYS SER ASP CYS
HET 9BA A 401 85
HET SO4 A 402 5
HET EDO A 403 4
HET EDO A 404 4
HET EDO A 405 4
HET EDO A 406 4
HET EDO A 407 4
HET EDO A 408 4
HET EDO A 409 4
HETNAM 9BA N-{(3R,6S,9S,12R)-6-ETHYL-12-METHYL-9-[3-(N'-
HETNAM 2 9BA METHYLCARBAMIMIDAMIDO)PROPYL]-2,5,8,11-TETRAOXO-3-
HETNAM 3 9BA PHENYL-1,4,7,10-TETRAAZACYCLOTETRADECAN-12-YL}-2-
HETNAM 4 9BA METHYLPROPANAMIDE
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 9BA C28 H44 N8 O5
FORMUL 3 SO4 O4 S 2-
FORMUL 4 EDO 7(C2 H6 O2)
FORMUL 11 HOH *215(H2 O)
SHEET 1 AA1 4 ALA A 36 LEU A 41 0
SHEET 2 AA1 4 ILE A 327 LYS A 331 -1 O ILE A 327 N LEU A 41
SHEET 3 AA1 4 ILE A 315 ALA A 320 -1 N SER A 318 O LYS A 328
SHEET 4 AA1 4 VAL A 304 CYS A 309 -1 N ALA A 308 O ALA A 317
SHEET 1 AA2 4 VAL A 48 PHE A 53 0
SHEET 2 AA2 4 TRP A 59 SER A 64 -1 O ALA A 61 N LYS A 52
SHEET 3 AA2 4 LEU A 68 GLY A 73 -1 O TRP A 72 N LEU A 60
SHEET 4 AA2 4 PHE A 79 SER A 84 -1 O GLU A 80 N ILE A 71
SHEET 1 AA3 4 ILE A 90 TRP A 95 0
SHEET 2 AA3 4 LEU A 101 SER A 106 -1 O VAL A 103 N ALA A 94
SHEET 3 AA3 4 LEU A 111 ASP A 115 -1 O TRP A 114 N LEU A 102
SHEET 4 AA3 4 CYS A 121 LEU A 125 -1 O LEU A 125 N LEU A 111
SHEET 1 AA4 4 VAL A 132 PHE A 137 0
SHEET 2 AA4 4 LEU A 143 SER A 148 -1 O VAL A 145 N ASN A 136
SHEET 3 AA4 4 VAL A 153 ASP A 157 -1 O TRP A 156 N ILE A 144
SHEET 4 AA4 4 CYS A 163 LEU A 167 -1 O LEU A 167 N VAL A 153
SHEET 1 AA5 4 VAL A 174 PHE A 179 0
SHEET 2 AA5 4 LEU A 185 SER A 190 -1 O VAL A 187 N HIS A 178
SHEET 3 AA5 4 CYS A 195 ASP A 199 -1 O TRP A 198 N ILE A 186
SHEET 4 AA5 4 CYS A 205 LEU A 209 -1 O LEU A 209 N CYS A 195
SHEET 1 AA6 4 VAL A 217 PHE A 222 0
SHEET 2 AA6 4 ILE A 229 THR A 233 -1 O LEU A 230 N LYS A 221
SHEET 3 AA6 4 THR A 237 ASP A 242 -1 O TRP A 241 N ILE A 229
SHEET 4 AA6 4 LYS A 247 THR A 253 -1 O LYS A 247 N ASP A 242
SHEET 1 AA7 4 ALA A 264 SER A 267 0
SHEET 2 AA7 4 TRP A 273 SER A 276 -1 O VAL A 275 N ASN A 265
SHEET 3 AA7 4 VAL A 283 ASN A 287 -1 O TYR A 284 N SER A 276
SHEET 4 AA7 4 ILE A 293 LEU A 297 -1 O VAL A 294 N ILE A 285
SITE 1 AC1 23 SER A 49 ILE A 90 SER A 91 ASP A 92
SITE 2 AC1 23 ASP A 107 PHE A 133 CYS A 134 SER A 175
SITE 3 AC1 23 THR A 253 GLY A 254 LYS A 259 TYR A 260
SITE 4 AC1 23 CYS A 261 PHE A 263 THR A 290 LYS A 291
SITE 5 AC1 23 GLU A 292 HOH A 519 HOH A 530 HOH A 542
SITE 6 AC1 23 HOH A 564 HOH A 567 HOH A 609
SITE 1 AC2 6 HIS A 178 LYS A 221 EDO A 404 HOH A 524
SITE 2 AC2 6 HOH A 619 HOH A 628
SITE 1 AC3 4 LEU A 143 LYS A 165 THR A 200 ALA A 201
SITE 1 AC4 5 TRP A 95 SER A 97 PHE A 137 ASN A 138
SITE 2 AC4 5 SO4 A 402
SITE 1 AC5 3 TYR A 228 LYS A 250 GLN A 289
SITE 1 AC6 5 LYS A 38 LYS A 162 LYS A 331 ASP A 333
SITE 2 AC6 5 HOH A 554
SITE 1 AC7 3 ILE A 113 LYS A 123 VAL A 158
SITE 1 AC8 5 PHE A 39 ALA A 74 TYR A 75 LEU A 329
SITE 2 AC8 5 HOH A 656
SITE 1 AC9 1 HOH A 535
CRYST1 88.348 58.559 56.801 90.00 96.16 90.00 C 1 2 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 0.011319 0.000000 0.001222 0.00000
SCALE2 0.000000 0.017077 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017708 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
