HEADER TRANSCRIPTION 23-OCT-17 6ESN
TITLE LIGAND COMPLEX OF RORG LBD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR RECEPTOR ROR-GAMMA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NUCLEAR RECEPTOR RZR-GAMMA,NUCLEAR RECEPTOR SUBFAMILY 1
COMPND 5 GROUP F MEMBER 3,RAR-RELATED ORPHAN RECEPTOR C,RETINOID-RELATED
COMPND 6 ORPHAN RECEPTOR-GAMMA;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: LYS-HIS-LYS-ILE-LEU-HIS-ARG-LEU-LEU-GLN-ASP-SER;
COMPND 10 CHAIN: C;
COMPND 11 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: RORC, NR1F3, RORG, RZRG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS RAR-RELATED ORPHAN RECEPTOR-G (RORG), TRANSCRIPTION, RORG LIGAND,
KEYWDS 2 STRUCTURE-BASED DESIGN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.XUE,A.AAGAARD,F.NARJES
REVDAT 3 16-OCT-19 6ESN 1 REMARK
REVDAT 2 24-OCT-18 6ESN 1 JRNL
REVDAT 1 22-AUG-18 6ESN 0
JRNL AUTH F.NARJES,Y.XUE,S.VON BERG,J.MALMBERG,A.LLINAS,R.I.OLSSON,
JRNL AUTH 2 J.JIRHOLT,H.GRINDEBACKE,A.LEFFLER,N.HOSSAIN,M.LEPISTO,
JRNL AUTH 3 L.THUNBERG,H.LEEK,A.AAGAARD,J.MCPHEAT,E.L.HANSSON,E.BACK,
JRNL AUTH 4 S.TANGEFJORD,R.CHEN,Y.XIONG,G.HONGBIN,T.G.HANSSON
JRNL TITL POTENT AND ORALLY BIOAVAILABLE INVERSE AGONISTS OF ROR GAMMA
JRNL TITL 2 T RESULTING FROM STRUCTURE-BASED DESIGN.
JRNL REF J. MED. CHEM. V. 61 7796 2018
JRNL REFN ISSN 1520-4804
JRNL PMID 30095900
JRNL DOI 10.1021/ACS.JMEDCHEM.8B00783
REMARK 2
REMARK 2 RESOLUTION. 1.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.5 PACIOREK
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) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 25959
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) : 0.212
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1312
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 : 13
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.92
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.66
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2147
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.3164
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2054
REMARK 3 BIN R VALUE (WORKING SET) : 0.3160
REMARK 3 BIN FREE R VALUE : 0.3249
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.33
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 93
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 : 2159
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 258
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.21
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.28380
REMARK 3 B22 (A**2) : -2.28380
REMARK 3 B33 (A**2) : 4.56770
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) : 0.301
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.170
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.158
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.155
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.150
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 : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2254 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3037 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 813 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 53 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 336 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2254 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 271 ; 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 : 2788 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.99
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 6ESN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1200007191.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-SEP-14
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 : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26861
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 48.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 12.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.3000
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ~1.3M NAFORMATE 0.1M HEPES PH 7-7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 78.65000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.12500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.12500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 39.32500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.12500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.12500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 117.97500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.12500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.12500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 39.32500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.12500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.12500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 117.97500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 78.65000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 243
REMARK 465 HIS A 244
REMARK 465 ASN A 245
REMARK 465 HIS A 246
REMARK 465 ASN A 247
REMARK 465 HIS A 248
REMARK 465 ASN A 249
REMARK 465 HIS A 250
REMARK 465 ASN A 251
REMARK 465 HIS A 252
REMARK 465 ASN A 253
REMARK 465 HIS A 254
REMARK 465 ASN A 255
REMARK 465 GLY A 256
REMARK 465 GLY A 257
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 GLN A 286 -66.23 71.40
REMARK 500 CYS A 393 50.29 -152.26
REMARK 500 GLU A 435 66.93 -106.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 602 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 366 O
REMARK 620 2 TYR A 369 O 90.3
REMARK 620 3 SER A 408 OG 95.3 102.8
REMARK 620 4 HOH A 750 O 169.1 78.8 87.2
REMARK 620 5 HOH A 840 O 76.4 162.4 90.0 114.2
REMARK 620 6 HOH A 755 O 93.3 86.9 166.9 86.1 82.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BWE A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 602
DBREF 6ESN A 265 507 UNP P51449 RORG_HUMAN 244 486
DBREF 6ESN C 686 697 PDB 6ESN 6ESN 686 697
SEQADV 6ESN MET A 243 UNP P51449 INITIATING METHIONINE
SEQADV 6ESN HIS A 244 UNP P51449 EXPRESSION TAG
SEQADV 6ESN ASN A 245 UNP P51449 EXPRESSION TAG
SEQADV 6ESN HIS A 246 UNP P51449 EXPRESSION TAG
SEQADV 6ESN ASN A 247 UNP P51449 EXPRESSION TAG
SEQADV 6ESN HIS A 248 UNP P51449 EXPRESSION TAG
SEQADV 6ESN ASN A 249 UNP P51449 EXPRESSION TAG
SEQADV 6ESN HIS A 250 UNP P51449 EXPRESSION TAG
SEQADV 6ESN ASN A 251 UNP P51449 EXPRESSION TAG
SEQADV 6ESN HIS A 252 UNP P51449 EXPRESSION TAG
SEQADV 6ESN ASN A 253 UNP P51449 EXPRESSION TAG
SEQADV 6ESN HIS A 254 UNP P51449 EXPRESSION TAG
SEQADV 6ESN ASN A 255 UNP P51449 EXPRESSION TAG
SEQADV 6ESN GLY A 256 UNP P51449 EXPRESSION TAG
SEQADV 6ESN GLY A 257 UNP P51449 EXPRESSION TAG
SEQADV 6ESN GLU A 258 UNP P51449 EXPRESSION TAG
SEQADV 6ESN ASN A 259 UNP P51449 EXPRESSION TAG
SEQADV 6ESN LEU A 260 UNP P51449 EXPRESSION TAG
SEQADV 6ESN TYR A 261 UNP P51449 EXPRESSION TAG
SEQADV 6ESN PHE A 262 UNP P51449 EXPRESSION TAG
SEQADV 6ESN GLN A 263 UNP P51449 EXPRESSION TAG
SEQADV 6ESN GLY A 264 UNP P51449 EXPRESSION TAG
SEQADV 6ESN GLY A 508 UNP P51449 EXPRESSION TAG
SEQADV 6ESN GLY A 509 UNP P51449 EXPRESSION TAG
SEQRES 1 A 267 MET HIS ASN HIS ASN HIS ASN HIS ASN HIS ASN HIS ASN
SEQRES 2 A 267 GLY GLY GLU ASN LEU TYR PHE GLN GLY ALA SER LEU THR
SEQRES 3 A 267 GLU ILE GLU HIS LEU VAL GLN SER VAL CYS LYS SER TYR
SEQRES 4 A 267 ARG GLU THR CYS GLN LEU ARG LEU GLU ASP LEU LEU ARG
SEQRES 5 A 267 GLN ARG SER ASN ILE PHE SER ARG GLU GLU VAL THR GLY
SEQRES 6 A 267 TYR GLN ARG LYS SER MET TRP GLU MET TRP GLU ARG CYS
SEQRES 7 A 267 ALA HIS HIS LEU THR GLU ALA ILE GLN TYR VAL VAL GLU
SEQRES 8 A 267 PHE ALA LYS ARG LEU SER GLY PHE MET GLU LEU CYS GLN
SEQRES 9 A 267 ASN ASP GLN ILE VAL LEU LEU LYS ALA GLY ALA MET GLU
SEQRES 10 A 267 VAL VAL LEU VAL ARG MET CYS ARG ALA TYR ASN ALA ASP
SEQRES 11 A 267 ASN ARG THR VAL PHE PHE GLU GLY LYS TYR GLY GLY MET
SEQRES 12 A 267 GLU LEU PHE ARG ALA LEU GLY CYS SER GLU LEU ILE SER
SEQRES 13 A 267 SER ILE PHE ASP PHE SER HIS SER LEU SER ALA LEU HIS
SEQRES 14 A 267 PHE SER GLU ASP GLU ILE ALA LEU TYR THR ALA LEU VAL
SEQRES 15 A 267 LEU ILE ASN ALA HIS ARG PRO GLY LEU GLN GLU LYS ARG
SEQRES 16 A 267 LYS VAL GLU GLN LEU GLN TYR ASN LEU GLU LEU ALA PHE
SEQRES 17 A 267 HIS HIS HIS LEU CYS LYS THR HIS ARG GLN SER ILE LEU
SEQRES 18 A 267 ALA LYS LEU PRO PRO LYS GLY LYS LEU ARG SER LEU CYS
SEQRES 19 A 267 SER GLN HIS VAL GLU ARG LEU GLN ILE PHE GLN HIS LEU
SEQRES 20 A 267 HIS PRO ILE VAL VAL GLN ALA ALA PHE PRO PRO LEU TYR
SEQRES 21 A 267 LYS GLU LEU PHE SER GLY GLY
SEQRES 1 C 12 LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER
HET BWE A 601 35
HET NA A 602 1
HETNAM BWE (2~{R})-2-ACETAMIDO-~{N}-[4-(5-CYANO-3-FLUORANYL-2-
HETNAM 2 BWE METHOXY-PHENYL)THIOPHEN-2-YL]-2-(4-
HETNAM 3 BWE ETHYLSULFONYLPHENYL)ETHANAMIDE
HETNAM NA SODIUM ION
FORMUL 3 BWE C24 H22 F N3 O5 S2
FORMUL 4 NA NA 1+
FORMUL 5 HOH *258(H2 O)
HELIX 1 AA1 ASN A 259 GLN A 263 5 5
HELIX 2 AA2 SER A 266 GLU A 283 1 18
HELIX 3 AA3 ARG A 288 GLN A 295 1 8
HELIX 4 AA4 ARG A 296 ASN A 298 5 3
HELIX 5 AA5 SER A 301 LYS A 311 1 11
HELIX 6 AA6 SER A 312 LEU A 338 1 27
HELIX 7 AA7 GLY A 340 LEU A 344 5 5
HELIX 8 AA8 CYS A 345 CYS A 366 1 22
HELIX 9 AA9 GLY A 384 GLY A 392 5 9
HELIX 10 AB1 CYS A 393 ALA A 409 1 17
HELIX 11 AB2 SER A 413 ILE A 426 1 14
HELIX 12 AB3 GLU A 435 THR A 457 1 23
HELIX 13 AB4 ARG A 459 LEU A 466 5 8
HELIX 14 AB5 PRO A 468 HIS A 490 1 23
HELIX 15 AB6 HIS A 490 PHE A 498 1 9
HELIX 16 AB7 PRO A 499 SER A 507 1 9
HELIX 17 AB8 LYS C 688 ASP C 696 1 9
SHEET 1 AA1 3 TYR A 369 ASN A 370 0
SHEET 2 AA1 3 THR A 375 PHE A 378 -1 O THR A 375 N ASN A 370
SHEET 3 AA1 3 LYS A 381 GLY A 383 -1 O LYS A 381 N PHE A 378
LINK O CYS A 366 NA NA A 602 1555 1555 2.30
LINK O TYR A 369 NA NA A 602 1555 1555 2.46
LINK OG SER A 408 NA NA A 602 1555 1555 2.43
LINK NA NA A 602 O HOH A 750 1555 1555 2.73
LINK NA NA A 602 O HOH A 840 1555 1555 2.73
LINK NA NA A 602 O HOH A 755 1555 1555 2.59
SITE 1 AC1 18 CYS A 285 GLN A 286 LEU A 287 HIS A 323
SITE 2 AC1 18 ARG A 364 ARG A 367 ALA A 368 VAL A 376
SITE 3 AC1 18 PHE A 377 PHE A 378 GLU A 379 PHE A 388
SITE 4 AC1 18 ILE A 397 ILE A 400 PHE A 401 SER A 404
SITE 5 AC1 18 HOH A 706 HOH A 825
SITE 1 AC2 6 CYS A 366 TYR A 369 SER A 408 HOH A 750
SITE 2 AC2 6 HOH A 755 HOH A 840
CRYST1 62.250 62.250 157.300 90.00 90.00 90.00 P 41 21 2 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 0.016064 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016064 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006357 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
