HEADER SIGNALING PROTEIN 20-SEP-17 6B30
TITLE STRUCTURE OF RORGT IN COMPLEX WITH A NOVEL INVERSE AGONIST 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR RECEPTOR ROR-GAMMA;
COMPND 3 CHAIN: A, B;
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
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
KEYWDS COMPLEX, INVERSE AGONIST, NUCLEAR HORMONE RECEPTOR, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.J.SKENE,I.HOFFMAN
REVDAT 3 13-MAR-24 6B30 1 REMARK
REVDAT 2 10-JAN-18 6B30 1 JRNL
REVDAT 1 03-JAN-18 6B30 0
JRNL AUTH J.SHIRAI,Y.TOMATA,M.KONO,A.OCHIDA,Y.FUKASE,A.SATO,S.MASADA,
JRNL AUTH 2 T.KAWAMOTO,K.YONEMORI,R.KOYAMA,H.NAKAGAWA,M.NAKAYAMA,K.UGA,
JRNL AUTH 3 A.SHIBATA,K.KOGA,T.OKUI,M.SHIRASAKI,R.SKENE,B.SANG,
JRNL AUTH 4 I.HOFFMAN,W.LANE,Y.FUJITANI,M.YAMASAKI,S.YAMAMOTO
JRNL TITL DISCOVERY OF ORALLY EFFICACIOUS ROR GAMMA T INVERSE
JRNL TITL 2 AGONISTS, PART 1: IDENTIFICATION OF NOVEL PHENYLGLYCINAMIDES
JRNL TITL 3 AS LEAD SCAFFOLDS.
JRNL REF BIOORG. MED. CHEM. V. 26 483 2018
JRNL REFN ESSN 1464-3391
JRNL PMID 29262987
JRNL DOI 10.1016/J.BMC.2017.12.006
REMARK 2
REMARK 2 RESOLUTION. 2.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 18452
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 991
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3475
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 47
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 76.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.74000
REMARK 3 B22 (A**2) : 0.74000
REMARK 3 B33 (A**2) : -2.39000
REMARK 3 B12 (A**2) : 0.37000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.485
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.284
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.229
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.164
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 6B30 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1000230187.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUN-12
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 : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19499
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.690
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.85900
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M SODIUM FORMATE, 3% MPD, AND 100
REMARK 280 MM HEPES (PH 7.5), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.85367
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 87.70733
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 65.78050
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 109.63417
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 21.92683
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 SER B 477
REMARK 465 GLN B 478
REMARK 465 HIS B 479
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 -58.51 74.94
REMARK 500 CYS A 393 77.06 -154.61
REMARK 500 GLU A 435 61.60 -118.96
REMARK 500 GLN B 286 -59.56 86.05
REMARK 500 CYS B 393 68.11 -155.74
REMARK 500 GLU B 435 59.50 -104.35
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 CFG A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CFG B 600
DBREF 6B30 A 265 479 UNP P51449 RORG_HUMAN 265 479
DBREF 6B30 B 265 479 UNP P51449 RORG_HUMAN 265 479
SEQRES 1 A 215 ALA SER LEU THR GLU ILE GLU HIS LEU VAL GLN SER VAL
SEQRES 2 A 215 CYS LYS SER TYR ARG GLU THR CYS GLN LEU ARG LEU GLU
SEQRES 3 A 215 ASP LEU LEU ARG GLN ARG SER ASN ILE PHE SER ARG GLU
SEQRES 4 A 215 GLU VAL THR GLY TYR GLN ARG LYS SER MET TRP GLU MET
SEQRES 5 A 215 TRP GLU ARG CYS ALA HIS HIS LEU THR GLU ALA ILE GLN
SEQRES 6 A 215 TYR VAL VAL GLU PHE ALA LYS ARG LEU SER GLY PHE MET
SEQRES 7 A 215 GLU LEU CYS GLN ASN ASP GLN ILE VAL LEU LEU LYS ALA
SEQRES 8 A 215 GLY ALA MET GLU VAL VAL LEU VAL ARG MET CYS ARG ALA
SEQRES 9 A 215 TYR ASN ALA ASP ASN ARG THR VAL PHE PHE GLU GLY LYS
SEQRES 10 A 215 TYR GLY GLY MET GLU LEU PHE ARG ALA LEU GLY CYS SER
SEQRES 11 A 215 GLU LEU ILE SER SER ILE PHE ASP PHE SER HIS SER LEU
SEQRES 12 A 215 SER ALA LEU HIS PHE SER GLU ASP GLU ILE ALA LEU TYR
SEQRES 13 A 215 THR ALA LEU VAL LEU ILE ASN ALA HIS ARG PRO GLY LEU
SEQRES 14 A 215 GLN GLU LYS ARG LYS VAL GLU GLN LEU GLN TYR ASN LEU
SEQRES 15 A 215 GLU LEU ALA PHE HIS HIS HIS LEU CYS LYS THR HIS ARG
SEQRES 16 A 215 GLN SER ILE LEU ALA LYS LEU PRO PRO LYS GLY LYS LEU
SEQRES 17 A 215 ARG SER LEU CYS SER GLN HIS
SEQRES 1 B 215 ALA SER LEU THR GLU ILE GLU HIS LEU VAL GLN SER VAL
SEQRES 2 B 215 CYS LYS SER TYR ARG GLU THR CYS GLN LEU ARG LEU GLU
SEQRES 3 B 215 ASP LEU LEU ARG GLN ARG SER ASN ILE PHE SER ARG GLU
SEQRES 4 B 215 GLU VAL THR GLY TYR GLN ARG LYS SER MET TRP GLU MET
SEQRES 5 B 215 TRP GLU ARG CYS ALA HIS HIS LEU THR GLU ALA ILE GLN
SEQRES 6 B 215 TYR VAL VAL GLU PHE ALA LYS ARG LEU SER GLY PHE MET
SEQRES 7 B 215 GLU LEU CYS GLN ASN ASP GLN ILE VAL LEU LEU LYS ALA
SEQRES 8 B 215 GLY ALA MET GLU VAL VAL LEU VAL ARG MET CYS ARG ALA
SEQRES 9 B 215 TYR ASN ALA ASP ASN ARG THR VAL PHE PHE GLU GLY LYS
SEQRES 10 B 215 TYR GLY GLY MET GLU LEU PHE ARG ALA LEU GLY CYS SER
SEQRES 11 B 215 GLU LEU ILE SER SER ILE PHE ASP PHE SER HIS SER LEU
SEQRES 12 B 215 SER ALA LEU HIS PHE SER GLU ASP GLU ILE ALA LEU TYR
SEQRES 13 B 215 THR ALA LEU VAL LEU ILE ASN ALA HIS ARG PRO GLY LEU
SEQRES 14 B 215 GLN GLU LYS ARG LYS VAL GLU GLN LEU GLN TYR ASN LEU
SEQRES 15 B 215 GLU LEU ALA PHE HIS HIS HIS LEU CYS LYS THR HIS ARG
SEQRES 16 B 215 GLN SER ILE LEU ALA LYS LEU PRO PRO LYS GLY LYS LEU
SEQRES 17 B 215 ARG SER LEU CYS SER GLN HIS
HET CFG A 600 32
HET CFG B 600 32
HETNAM CFG N-[(1R)-1-(4-METHOXYPHENYL)-2-OXO-2-{[4-
HETNAM 2 CFG (TRIMETHYLSILYL)PHENYL]AMINO}ETHYL]-N-METHYL-3-OXO-2,
HETNAM 3 CFG 3-DIHYDRO-1,2-OXAZOLE-5-CARBOXAMIDE
FORMUL 3 CFG 2(C23 H27 N3 O5 SI)
FORMUL 5 HOH *47(H2 O)
HELIX 1 AA1 SER A 266 CYS A 285 1 20
HELIX 2 AA2 ARG A 288 GLN A 295 1 8
HELIX 3 AA3 ARG A 296 ASN A 298 5 3
HELIX 4 AA4 SER A 301 LYS A 311 1 11
HELIX 5 AA5 SER A 312 ARG A 337 1 26
HELIX 6 AA6 CYS A 345 CYS A 366 1 22
HELIX 7 AA7 GLY A 384 GLY A 392 5 9
HELIX 8 AA8 CYS A 393 LEU A 410 1 18
HELIX 9 AA9 SER A 413 ILE A 426 1 14
HELIX 10 AB1 GLU A 435 THR A 457 1 23
HELIX 11 AB2 SER A 461 LEU A 466 1 6
HELIX 12 AB3 GLY A 470 LEU A 475 1 6
HELIX 13 AB4 SER B 266 CYS B 285 1 20
HELIX 14 AB5 ARG B 288 GLN B 295 1 8
HELIX 15 AB6 ARG B 296 ASN B 298 5 3
HELIX 16 AB7 SER B 301 ARG B 310 1 10
HELIX 17 AB8 SER B 312 LEU B 338 1 27
HELIX 18 AB9 CYS B 345 CYS B 366 1 22
HELIX 19 AC1 GLY B 384 GLY B 392 5 9
HELIX 20 AC2 CYS B 393 LEU B 410 1 18
HELIX 21 AC3 SER B 413 ILE B 426 1 14
HELIX 22 AC4 GLU B 435 THR B 457 1 23
HELIX 23 AC5 SER B 461 LEU B 466 1 6
HELIX 24 AC6 GLY B 470 LEU B 475 1 6
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
SHEET 1 AA2 3 TYR B 369 ASN B 370 0
SHEET 2 AA2 3 THR B 375 PHE B 378 -1 O THR B 375 N ASN B 370
SHEET 3 AA2 3 LYS B 381 GLY B 383 -1 O LYS B 381 N PHE B 378
SITE 1 AC1 9 GLN A 286 LEU A 287 CYS A 320 HIS A 323
SITE 2 AC1 9 MET A 365 PHE A 377 PHE A 378 GLU A 379
SITE 3 AC1 9 HOH A 706
SITE 1 AC2 10 GLN B 286 LEU B 287 HIS B 323 ARG B 364
SITE 2 AC2 10 MET B 365 ALA B 368 PHE B 377 PHE B 378
SITE 3 AC2 10 GLU B 379 HOH B 702
CRYST1 97.217 97.217 131.561 90.00 90.00 120.00 P 61 12
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 0.010286 0.005939 0.000000 0.00000
SCALE2 0.000000 0.011878 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007601 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
