HEADER IMMUNE SYSTEM 24-MAR-16 5IZ0
TITLE RORGAMMA IN COMPLEX WITH AGONIST BIO592 AND COACTIVATOR EBI96
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR RECEPTOR ROR-GAMMA;
COMPND 3 CHAIN: A, B, D, G;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN;
COMPND 5 SYNONYM: NUCLEAR RECEPTOR RZR-GAMMA,NUCLEAR RECEPTOR SUBFAMILY 1
COMPND 6 GROUP F MEMBER 3,RAR-RELATED ORPHAN RECEPTOR C,RETINOID-RELATED
COMPND 7 ORPHAN RECEPTOR-GAMMA;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: GLU-PHE-PRO-TYR-LEU-LEU-SER-LEU-LEU-GLY-GLU-VAL-SER-PRO-
COMPND 11 GLN;
COMPND 12 CHAIN: C, E, F, H;
COMPND 13 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: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS RORGAMMA, NUCLEAR HORMONE RECEPTOR, AGONIST, AF2 HELIX, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.MARCOTTE
REVDAT 2 27-SEP-23 5IZ0 1 REMARK
REVDAT 1 15-JUN-16 5IZ0 0
JRNL AUTH D.J.MARCOTTE,Y.LIU,K.LITTLE,J.H.JONES,N.A.POWELL,C.P.WILDES,
JRNL AUTH 2 L.F.SILVIAN,J.V.CHODAPARAMBIL
JRNL TITL STRUCTURAL DETERMINANT FOR INDUCING RORGAMMA SPECIFIC
JRNL TITL 2 INVERSE AGONISM TRIGGERED BY A SYNTHETIC BENZOXAZINONE
JRNL TITL 3 LIGAND.
JRNL REF BMC STRUCT.BIOL. V. 16 7 2016
JRNL REFN ESSN 1472-6807
JRNL PMID 27246200
JRNL DOI 10.1186/S12900-016-0059-3
REMARK 2
REMARK 2 RESOLUTION. 2.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 80.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 29379
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1557
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.64
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.70
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2157
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.61
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE SET COUNT : 117
REMARK 3 BIN FREE R VALUE : 0.3590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8239
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 143
REMARK 3 SOLVENT ATOMS : 150
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.369
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.297
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.388
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.908
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8542 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8202 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11539 ; 1.655 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18785 ; 1.099 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1009 ; 5.687 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 408 ;36.096 ;23.113
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1516 ;17.455 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 65 ;20.323 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1267 ; 0.116 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9506 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2107 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4067 ; 1.906 ; 3.269
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4058 ; 1.905 ; 3.268
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5063 ; 3.077 ; 4.899
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5IZ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000219625.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
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 : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31077
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.635
REMARK 200 RESOLUTION RANGE LOW (A) : 80.558
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 2.630
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3LOL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 8.0 0.2M NACL 25%
REMARK 280 PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 34.05550
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, 3, 4
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: 1840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 1620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E
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: 3
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: 1570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F
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: 4
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: 1650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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 GLY A 257
REMARK 465 PRO A 258
REMARK 465 THR A 259
REMARK 465 PRO A 260
REMARK 465 GLU A 261
REMARK 465 ALA A 262
REMARK 465 PRO A 263
REMARK 465 TYR A 264
REMARK 465 THR A 509
REMARK 465 GLU A 510
REMARK 465 THR A 511
REMARK 465 GLU A 512
REMARK 465 SER A 513
REMARK 465 PRO A 514
REMARK 465 VAL A 515
REMARK 465 GLY A 516
REMARK 465 LEU A 517
REMARK 465 SER A 518
REMARK 465 LYS A 519
REMARK 465 GLU C 14
REMARK 465 VAL C 15
REMARK 465 SER C 16
REMARK 465 PRO C 17
REMARK 465 GLN C 18
REMARK 465 GLY B 257
REMARK 465 PRO B 258
REMARK 465 THR B 259
REMARK 465 PRO B 260
REMARK 465 GLU B 261
REMARK 465 ALA B 262
REMARK 465 THR B 508
REMARK 465 THR B 509
REMARK 465 GLU B 510
REMARK 465 THR B 511
REMARK 465 GLU B 512
REMARK 465 SER B 513
REMARK 465 PRO B 514
REMARK 465 VAL B 515
REMARK 465 GLY B 516
REMARK 465 LEU B 517
REMARK 465 SER B 518
REMARK 465 LYS B 519
REMARK 465 GLU E 14
REMARK 465 VAL E 15
REMARK 465 SER E 16
REMARK 465 PRO E 17
REMARK 465 GLN E 18
REMARK 465 GLY D 257
REMARK 465 PRO D 258
REMARK 465 THR D 259
REMARK 465 PRO D 260
REMARK 465 GLU D 261
REMARK 465 ALA D 262
REMARK 465 PRO D 263
REMARK 465 TYR D 264
REMARK 465 THR D 508
REMARK 465 THR D 509
REMARK 465 GLU D 510
REMARK 465 THR D 511
REMARK 465 GLU D 512
REMARK 465 SER D 513
REMARK 465 PRO D 514
REMARK 465 VAL D 515
REMARK 465 GLY D 516
REMARK 465 LEU D 517
REMARK 465 SER D 518
REMARK 465 LYS D 519
REMARK 465 GLU F 14
REMARK 465 VAL F 15
REMARK 465 SER F 16
REMARK 465 PRO F 17
REMARK 465 GLN F 18
REMARK 465 GLY G 257
REMARK 465 PRO G 258
REMARK 465 THR G 259
REMARK 465 PRO G 260
REMARK 465 GLU G 261
REMARK 465 ALA G 262
REMARK 465 THR G 509
REMARK 465 GLU G 510
REMARK 465 THR G 511
REMARK 465 GLU G 512
REMARK 465 SER G 513
REMARK 465 PRO G 514
REMARK 465 VAL G 515
REMARK 465 GLY G 516
REMARK 465 LEU G 517
REMARK 465 SER G 518
REMARK 465 LYS G 519
REMARK 465 GLU H 4
REMARK 465 GLU H 14
REMARK 465 VAL H 15
REMARK 465 SER H 16
REMARK 465 PRO H 17
REMARK 465 GLN H 18
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 ARG A 294 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 354 CG CD CE NZ
REMARK 470 THR A 508 OG1 CG2
REMARK 470 GLU C 4 CG CD OE1 OE2
REMARK 470 TYR B 264 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 359 O
REMARK 470 LYS D 354 CG CD CE NZ
REMARK 470 ARG D 437 CG CD NE CZ NH1 NH2
REMARK 470 TYR D 444 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS D 469 CG CD CE NZ
REMARK 470 LYS D 471 CG CD CE NZ
REMARK 470 GLN D 495 CG CD OE1 NE2
REMARK 470 GLU F 4 CG CD OE1 OE2
REMARK 470 TYR G 264 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG G 437 CG CD NE CZ NH1 NH2
REMARK 470 THR G 508 OG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O PRO D 467 O PRO D 468 1.74
REMARK 500 O PRO G 491 OE1 GLN G 495 1.92
REMARK 500
REMARK 500 REMARK: NULL
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 GLN A 286 CB - CA - C ANGL. DEV. = -18.5 DEGREES
REMARK 500 PRO B 263 CA - N - CD ANGL. DEV. = -13.8 DEGREES
REMARK 500 GLN B 286 CB - CA - C ANGL. DEV. = -24.0 DEGREES
REMARK 500 LEU B 287 N - CA - CB ANGL. DEV. = 13.9 DEGREES
REMARK 500 ARG B 473 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 GLN D 286 CB - CA - C ANGL. DEV. = -20.3 DEGREES
REMARK 500 LYS D 471 CB - CA - C ANGL. DEV. = -12.1 DEGREES
REMARK 500 LYS D 471 N - CA - C ANGL. DEV. = 22.7 DEGREES
REMARK 500 PRO G 263 CA - N - CD ANGL. DEV. = -13.5 DEGREES
REMARK 500 GLN G 286 CB - CA - C ANGL. DEV. = -20.8 DEGREES
REMARK 500 GLN G 286 N - CA - C ANGL. DEV. = 16.5 DEGREES
REMARK 500 LEU G 287 N - CA - CB ANGL. DEV. = 13.3 DEGREES
REMARK 500 MET G 385 CB - CA - C ANGL. DEV. = -14.5 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 GLN A 286 -5.32 58.85
REMARK 500 GLU A 435 61.62 -107.97
REMARK 500 GLN B 286 8.90 56.51
REMARK 500 LEU B 287 125.75 -172.27
REMARK 500 GLN D 286 3.97 56.40
REMARK 500 PRO D 468 -139.89 -33.49
REMARK 500 LYS D 469 75.05 -154.47
REMARK 500 LYS D 471 -54.49 -23.84
REMARK 500 GLN G 286 -1.26 53.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY D 470 LYS D 471 60.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D 739 DISTANCE = 6.05 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6F1 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6F1 B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6F1 D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6F1 G 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 606
DBREF 5IZ0 A 259 519 UNP P51449 RORG_HUMAN 238 497
DBREF 5IZ0 C 4 18 PDB 5IZ0 5IZ0 4 18
DBREF 5IZ0 B 259 519 UNP P51449 RORG_HUMAN 238 497
DBREF 5IZ0 E 4 18 PDB 5IZ0 5IZ0 4 18
DBREF 5IZ0 D 259 519 UNP P51449 RORG_HUMAN 238 497
DBREF 5IZ0 F 4 18 PDB 5IZ0 5IZ0 4 18
DBREF 5IZ0 G 259 519 UNP P51449 RORG_HUMAN 238 497
DBREF 5IZ0 H 4 18 PDB 5IZ0 5IZ0 4 18
SEQADV 5IZ0 GLY A 257 UNP P51449 EXPRESSION TAG
SEQADV 5IZ0 PRO A 258 UNP P51449 EXPRESSION TAG
SEQADV 5IZ0 THR A 508 UNP P51449 INSERTION
SEQADV 5IZ0 GLY B 257 UNP P51449 EXPRESSION TAG
SEQADV 5IZ0 PRO B 258 UNP P51449 EXPRESSION TAG
SEQADV 5IZ0 THR B 508 UNP P51449 INSERTION
SEQADV 5IZ0 GLY D 257 UNP P51449 EXPRESSION TAG
SEQADV 5IZ0 PRO D 258 UNP P51449 EXPRESSION TAG
SEQADV 5IZ0 THR D 508 UNP P51449 INSERTION
SEQADV 5IZ0 GLY G 257 UNP P51449 EXPRESSION TAG
SEQADV 5IZ0 PRO G 258 UNP P51449 EXPRESSION TAG
SEQADV 5IZ0 THR G 508 UNP P51449 INSERTION
SEQRES 1 A 263 GLY PRO THR PRO GLU ALA PRO TYR ALA SER LEU THR GLU
SEQRES 2 A 263 ILE GLU HIS LEU VAL GLN SER VAL CYS LYS SER TYR ARG
SEQRES 3 A 263 GLU THR CYS GLN LEU ARG LEU GLU ASP LEU LEU ARG GLN
SEQRES 4 A 263 ARG SER ASN ILE PHE SER ARG GLU GLU VAL THR GLY TYR
SEQRES 5 A 263 GLN ARG LYS SER MET TRP GLU MET TRP GLU ARG CYS ALA
SEQRES 6 A 263 HIS HIS LEU THR GLU ALA ILE GLN TYR VAL VAL GLU PHE
SEQRES 7 A 263 ALA LYS ARG LEU SER GLY PHE MET GLU LEU CYS GLN ASN
SEQRES 8 A 263 ASP GLN ILE VAL LEU LEU LYS ALA GLY ALA MET GLU VAL
SEQRES 9 A 263 VAL LEU VAL ARG MET CYS ARG ALA TYR ASN ALA ASP ASN
SEQRES 10 A 263 ARG THR VAL PHE PHE GLU GLY LYS TYR GLY GLY MET GLU
SEQRES 11 A 263 LEU PHE ARG ALA LEU GLY CYS SER GLU LEU ILE SER SER
SEQRES 12 A 263 ILE PHE ASP PHE SER HIS SER LEU SER ALA LEU HIS PHE
SEQRES 13 A 263 SER GLU ASP GLU ILE ALA LEU TYR THR ALA LEU VAL LEU
SEQRES 14 A 263 ILE ASN ALA HIS ARG PRO GLY LEU GLN GLU LYS ARG LYS
SEQRES 15 A 263 VAL GLU GLN LEU GLN TYR ASN LEU GLU LEU ALA PHE HIS
SEQRES 16 A 263 HIS HIS LEU CYS LYS THR HIS ARG GLN SER ILE LEU ALA
SEQRES 17 A 263 LYS LEU PRO PRO LYS GLY LYS LEU ARG SER LEU CYS SER
SEQRES 18 A 263 GLN HIS VAL GLU ARG LEU GLN ILE PHE GLN HIS LEU HIS
SEQRES 19 A 263 PRO ILE VAL VAL GLN ALA ALA PHE PRO PRO LEU TYR LYS
SEQRES 20 A 263 GLU LEU PHE SER THR THR GLU THR GLU SER PRO VAL GLY
SEQRES 21 A 263 LEU SER LYS
SEQRES 1 C 15 GLU PHE PRO TYR LEU LEU SER LEU LEU GLY GLU VAL SER
SEQRES 2 C 15 PRO GLN
SEQRES 1 B 263 GLY PRO THR PRO GLU ALA PRO TYR ALA SER LEU THR GLU
SEQRES 2 B 263 ILE GLU HIS LEU VAL GLN SER VAL CYS LYS SER TYR ARG
SEQRES 3 B 263 GLU THR CYS GLN LEU ARG LEU GLU ASP LEU LEU ARG GLN
SEQRES 4 B 263 ARG SER ASN ILE PHE SER ARG GLU GLU VAL THR GLY TYR
SEQRES 5 B 263 GLN ARG LYS SER MET TRP GLU MET TRP GLU ARG CYS ALA
SEQRES 6 B 263 HIS HIS LEU THR GLU ALA ILE GLN TYR VAL VAL GLU PHE
SEQRES 7 B 263 ALA LYS ARG LEU SER GLY PHE MET GLU LEU CYS GLN ASN
SEQRES 8 B 263 ASP GLN ILE VAL LEU LEU LYS ALA GLY ALA MET GLU VAL
SEQRES 9 B 263 VAL LEU VAL ARG MET CYS ARG ALA TYR ASN ALA ASP ASN
SEQRES 10 B 263 ARG THR VAL PHE PHE GLU GLY LYS TYR GLY GLY MET GLU
SEQRES 11 B 263 LEU PHE ARG ALA LEU GLY CYS SER GLU LEU ILE SER SER
SEQRES 12 B 263 ILE PHE ASP PHE SER HIS SER LEU SER ALA LEU HIS PHE
SEQRES 13 B 263 SER GLU ASP GLU ILE ALA LEU TYR THR ALA LEU VAL LEU
SEQRES 14 B 263 ILE ASN ALA HIS ARG PRO GLY LEU GLN GLU LYS ARG LYS
SEQRES 15 B 263 VAL GLU GLN LEU GLN TYR ASN LEU GLU LEU ALA PHE HIS
SEQRES 16 B 263 HIS HIS LEU CYS LYS THR HIS ARG GLN SER ILE LEU ALA
SEQRES 17 B 263 LYS LEU PRO PRO LYS GLY LYS LEU ARG SER LEU CYS SER
SEQRES 18 B 263 GLN HIS VAL GLU ARG LEU GLN ILE PHE GLN HIS LEU HIS
SEQRES 19 B 263 PRO ILE VAL VAL GLN ALA ALA PHE PRO PRO LEU TYR LYS
SEQRES 20 B 263 GLU LEU PHE SER THR THR GLU THR GLU SER PRO VAL GLY
SEQRES 21 B 263 LEU SER LYS
SEQRES 1 E 15 GLU PHE PRO TYR LEU LEU SER LEU LEU GLY GLU VAL SER
SEQRES 2 E 15 PRO GLN
SEQRES 1 D 263 GLY PRO THR PRO GLU ALA PRO TYR ALA SER LEU THR GLU
SEQRES 2 D 263 ILE GLU HIS LEU VAL GLN SER VAL CYS LYS SER TYR ARG
SEQRES 3 D 263 GLU THR CYS GLN LEU ARG LEU GLU ASP LEU LEU ARG GLN
SEQRES 4 D 263 ARG SER ASN ILE PHE SER ARG GLU GLU VAL THR GLY TYR
SEQRES 5 D 263 GLN ARG LYS SER MET TRP GLU MET TRP GLU ARG CYS ALA
SEQRES 6 D 263 HIS HIS LEU THR GLU ALA ILE GLN TYR VAL VAL GLU PHE
SEQRES 7 D 263 ALA LYS ARG LEU SER GLY PHE MET GLU LEU CYS GLN ASN
SEQRES 8 D 263 ASP GLN ILE VAL LEU LEU LYS ALA GLY ALA MET GLU VAL
SEQRES 9 D 263 VAL LEU VAL ARG MET CYS ARG ALA TYR ASN ALA ASP ASN
SEQRES 10 D 263 ARG THR VAL PHE PHE GLU GLY LYS TYR GLY GLY MET GLU
SEQRES 11 D 263 LEU PHE ARG ALA LEU GLY CYS SER GLU LEU ILE SER SER
SEQRES 12 D 263 ILE PHE ASP PHE SER HIS SER LEU SER ALA LEU HIS PHE
SEQRES 13 D 263 SER GLU ASP GLU ILE ALA LEU TYR THR ALA LEU VAL LEU
SEQRES 14 D 263 ILE ASN ALA HIS ARG PRO GLY LEU GLN GLU LYS ARG LYS
SEQRES 15 D 263 VAL GLU GLN LEU GLN TYR ASN LEU GLU LEU ALA PHE HIS
SEQRES 16 D 263 HIS HIS LEU CYS LYS THR HIS ARG GLN SER ILE LEU ALA
SEQRES 17 D 263 LYS LEU PRO PRO LYS GLY LYS LEU ARG SER LEU CYS SER
SEQRES 18 D 263 GLN HIS VAL GLU ARG LEU GLN ILE PHE GLN HIS LEU HIS
SEQRES 19 D 263 PRO ILE VAL VAL GLN ALA ALA PHE PRO PRO LEU TYR LYS
SEQRES 20 D 263 GLU LEU PHE SER THR THR GLU THR GLU SER PRO VAL GLY
SEQRES 21 D 263 LEU SER LYS
SEQRES 1 F 15 GLU PHE PRO TYR LEU LEU SER LEU LEU GLY GLU VAL SER
SEQRES 2 F 15 PRO GLN
SEQRES 1 G 263 GLY PRO THR PRO GLU ALA PRO TYR ALA SER LEU THR GLU
SEQRES 2 G 263 ILE GLU HIS LEU VAL GLN SER VAL CYS LYS SER TYR ARG
SEQRES 3 G 263 GLU THR CYS GLN LEU ARG LEU GLU ASP LEU LEU ARG GLN
SEQRES 4 G 263 ARG SER ASN ILE PHE SER ARG GLU GLU VAL THR GLY TYR
SEQRES 5 G 263 GLN ARG LYS SER MET TRP GLU MET TRP GLU ARG CYS ALA
SEQRES 6 G 263 HIS HIS LEU THR GLU ALA ILE GLN TYR VAL VAL GLU PHE
SEQRES 7 G 263 ALA LYS ARG LEU SER GLY PHE MET GLU LEU CYS GLN ASN
SEQRES 8 G 263 ASP GLN ILE VAL LEU LEU LYS ALA GLY ALA MET GLU VAL
SEQRES 9 G 263 VAL LEU VAL ARG MET CYS ARG ALA TYR ASN ALA ASP ASN
SEQRES 10 G 263 ARG THR VAL PHE PHE GLU GLY LYS TYR GLY GLY MET GLU
SEQRES 11 G 263 LEU PHE ARG ALA LEU GLY CYS SER GLU LEU ILE SER SER
SEQRES 12 G 263 ILE PHE ASP PHE SER HIS SER LEU SER ALA LEU HIS PHE
SEQRES 13 G 263 SER GLU ASP GLU ILE ALA LEU TYR THR ALA LEU VAL LEU
SEQRES 14 G 263 ILE ASN ALA HIS ARG PRO GLY LEU GLN GLU LYS ARG LYS
SEQRES 15 G 263 VAL GLU GLN LEU GLN TYR ASN LEU GLU LEU ALA PHE HIS
SEQRES 16 G 263 HIS HIS LEU CYS LYS THR HIS ARG GLN SER ILE LEU ALA
SEQRES 17 G 263 LYS LEU PRO PRO LYS GLY LYS LEU ARG SER LEU CYS SER
SEQRES 18 G 263 GLN HIS VAL GLU ARG LEU GLN ILE PHE GLN HIS LEU HIS
SEQRES 19 G 263 PRO ILE VAL VAL GLN ALA ALA PHE PRO PRO LEU TYR LYS
SEQRES 20 G 263 GLU LEU PHE SER THR THR GLU THR GLU SER PRO VAL GLY
SEQRES 21 G 263 LEU SER LYS
SEQRES 1 H 15 GLU PHE PRO TYR LEU LEU SER LEU LEU GLY GLU VAL SER
SEQRES 2 H 15 PRO GLN
HET 6F1 A 601 30
HET CL A 602 1
HET CL A 603 1
HET CL A 604 1
HET CL A 605 1
HET CL A 606 1
HET CL A 607 1
HET CL A 608 1
HET CL A 609 1
HET 6F1 B 601 30
HET CL B 602 1
HET CL B 603 1
HET CL B 604 1
HET CL B 605 1
HET CL B 606 1
HET CL B 607 1
HET 6F1 D 601 30
HET CL D 602 1
HET CL D 603 1
HET CL D 604 1
HET CL D 605 1
HET 6F1 G 601 30
HET CL G 602 1
HET CL G 603 1
HET CL G 604 1
HET CL G 605 1
HET CL G 606 1
HETNAM 6F1 N-(4-ETHYL-3-OXO-3,4-DIHYDRO-2H-1,4-BENZOXAZIN-7-YL)-3,
HETNAM 2 6F1 4-DIMETHYL-N-(2,2,2-TRIFLUOROETHYL)BENZENE-1-
HETNAM 3 6F1 SULFONAMIDE
HETNAM CL CHLORIDE ION
FORMUL 9 6F1 4(C20 H21 F3 N2 O4 S)
FORMUL 10 CL 23(CL 1-)
FORMUL 36 HOH *150(H2 O)
HELIX 1 AA1 SER A 266 GLU A 283 1 18
HELIX 2 AA2 ARG A 288 GLN A 295 1 8
HELIX 3 AA3 SER A 301 LYS A 311 1 11
HELIX 4 AA4 SER A 312 LEU A 338 1 27
HELIX 5 AA5 CYS A 345 MET A 365 1 21
HELIX 6 AA6 GLY A 384 GLY A 392 5 9
HELIX 7 AA7 CYS A 393 ALA A 409 1 17
HELIX 8 AA8 SER A 413 ILE A 426 1 14
HELIX 9 AA9 GLU A 435 THR A 457 1 23
HELIX 10 AB1 ARG A 459 LEU A 466 5 8
HELIX 11 AB2 GLY A 470 HIS A 490 1 21
HELIX 12 AB3 HIS A 490 PHE A 498 1 9
HELIX 13 AB4 PRO A 499 SER A 507 1 9
HELIX 14 AB5 PHE C 5 GLY C 13 1 9
HELIX 15 AB6 TYR B 264 GLU B 283 1 20
HELIX 16 AB7 ARG B 288 GLN B 295 1 8
HELIX 17 AB8 SER B 301 ARG B 310 1 10
HELIX 18 AB9 SER B 312 LEU B 338 1 27
HELIX 19 AC1 CYS B 345 ALA B 357 1 13
HELIX 20 AC2 ALA B 357 MET B 365 1 9
HELIX 21 AC3 GLY B 384 GLY B 392 5 9
HELIX 22 AC4 CYS B 393 ALA B 409 1 17
HELIX 23 AC5 SER B 413 ILE B 426 1 14
HELIX 24 AC6 GLU B 435 THR B 457 1 23
HELIX 25 AC7 ARG B 459 LEU B 466 5 8
HELIX 26 AC8 GLY B 470 HIS B 490 1 21
HELIX 27 AC9 HIS B 490 PHE B 498 1 9
HELIX 28 AD1 PRO B 499 SER B 507 1 9
HELIX 29 AD2 PHE E 5 GLY E 13 1 9
HELIX 30 AD3 SER D 266 GLU D 283 1 18
HELIX 31 AD4 ARG D 288 GLN D 295 1 8
HELIX 32 AD5 ARG D 296 ASN D 298 5 3
HELIX 33 AD6 SER D 301 LYS D 311 1 11
HELIX 34 AD7 SER D 312 LEU D 338 1 27
HELIX 35 AD8 CYS D 345 MET D 365 1 21
HELIX 36 AD9 GLY D 384 GLY D 392 5 9
HELIX 37 AE1 CYS D 393 ALA D 409 1 17
HELIX 38 AE2 SER D 413 ILE D 426 1 14
HELIX 39 AE3 GLU D 435 THR D 457 1 23
HELIX 40 AE4 ARG D 459 LEU D 466 5 8
HELIX 41 AE5 LYS D 471 HIS D 490 1 20
HELIX 42 AE6 HIS D 490 PHE D 498 1 9
HELIX 43 AE7 PRO D 499 SER D 507 1 9
HELIX 44 AE8 PHE F 5 LEU F 11 1 7
HELIX 45 AE9 TYR G 264 GLU G 283 1 20
HELIX 46 AF1 ARG G 288 GLN G 295 1 8
HELIX 47 AF2 SER G 301 ARG G 310 1 10
HELIX 48 AF3 SER G 312 LEU G 338 1 27
HELIX 49 AF4 CYS G 345 MET G 365 1 21
HELIX 50 AF5 GLY G 384 GLY G 392 5 9
HELIX 51 AF6 CYS G 393 ALA G 409 1 17
HELIX 52 AF7 SER G 413 ILE G 426 1 14
HELIX 53 AF8 GLU G 435 LYS G 456 1 22
HELIX 54 AF9 THR G 457 HIS G 458 5 2
HELIX 55 AG1 ARG G 459 LEU G 466 5 8
HELIX 56 AG2 GLY G 470 HIS G 490 1 21
HELIX 57 AG3 HIS G 490 ALA G 497 1 8
HELIX 58 AG4 PRO G 499 SER G 507 1 9
HELIX 59 AG5 PRO H 6 GLY H 13 1 8
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
SHEET 1 AA3 3 TYR D 369 ASN D 370 0
SHEET 2 AA3 3 THR D 375 PHE D 378 -1 O THR D 375 N ASN D 370
SHEET 3 AA3 3 LYS D 381 GLY D 383 -1 O LYS D 381 N PHE D 378
SHEET 1 AA4 3 TYR G 369 ASN G 370 0
SHEET 2 AA4 3 THR G 375 PHE G 378 -1 O THR G 375 N ASN G 370
SHEET 3 AA4 3 LYS G 381 GLY G 383 -1 O LYS G 381 N PHE G 378
SSBOND 1 CYS D 455 CYS G 455 1555 1455 2.59
SITE 1 AC1 12 CYS A 320 HIS A 323 LEU A 324 ALA A 327
SITE 2 AC1 12 MET A 358 VAL A 361 MET A 365 PHE A 378
SITE 3 AC1 12 PHE A 388 ILE A 400 HIS A 479 HOH A 705
SITE 1 AC2 4 PHE A 334 VAL A 360 ARG A 364 THR A 421
SITE 1 AC3 3 HIS A 458 ARG A 459 GLN A 460
SITE 1 AC4 5 ARG A 296 ARG A 367 TYR A 369 TYR A 382
SITE 2 AC4 5 HOH A 722
SITE 1 AC5 4 LEU A 362 CYS A 366 PHE A 403 SER A 404
SITE 1 AC6 3 HIS A 322 HIS B 322 PRO B 499
SITE 1 AC7 4 LEU A 352 GLY A 356 LEU A 425 ARG A 430
SITE 1 AC8 6 TYR A 308 GLN A 309 LEU A 387 PHE A 388
SITE 2 AC8 6 ARG A 389 ALA A 390
SITE 1 AC9 15 CYS B 320 HIS B 323 LEU B 324 ALA B 327
SITE 2 AC9 15 MET B 358 VAL B 361 VAL B 376 PHE B 378
SITE 3 AC9 15 PHE B 388 LEU B 396 ILE B 400 PHE B 401
SITE 4 AC9 15 HIS B 479 HOH B 710 HOH B 721
SITE 1 AD1 3 LYS A 456 HIS B 458 GLN B 460
SITE 1 AD2 4 HIS B 490 PRO B 491 ILE B 492 VAL B 493
SITE 1 AD3 5 TYR B 281 PHE B 334 VAL B 360 ARG B 364
SITE 2 AD3 5 THR B 421
SITE 1 AD4 3 LEU B 352 LEU B 425 ARG B 430
SITE 1 AD5 5 ARG B 296 ASN B 370 ASN B 373 THR B 375
SITE 2 AD5 5 TYR B 382
SITE 1 AD6 4 ARG B 296 ARG B 367 TYR B 369 TYR B 382
SITE 1 AD7 12 CYS D 320 HIS D 323 LEU D 324 ALA D 327
SITE 2 AD7 12 MET D 358 VAL D 361 VAL D 376 PHE D 378
SITE 3 AD7 12 PHE D 388 ILE D 400 HIS D 479 HOH D 714
SITE 1 AD8 4 CYS D 393 SER D 394 GLU D 395 ARG D 482
SITE 1 AD9 4 TYR D 281 PHE D 334 ARG D 364 THR D 421
SITE 1 AE1 4 LEU D 344 CYS D 345 ASP D 348 GLU D 435
SITE 1 AE2 14 CYS G 320 HIS G 323 LEU G 324 ALA G 327
SITE 2 AE2 14 MET G 358 VAL G 361 MET G 365 VAL G 376
SITE 3 AE2 14 PHE G 378 PHE G 388 LEU G 396 ILE G 400
SITE 4 AE2 14 PHE G 401 HIS G 479
SITE 1 AE3 4 TYR G 281 PHE G 334 ARG G 364 THR G 421
SITE 1 AE4 4 LEU G 344 CYS G 345 ASP G 348 GLU G 435
SITE 1 AE5 3 LYS D 456 HIS G 458 GLN G 460
SITE 1 AE6 5 HIS D 322 GLU D 326 GLU G 315 GLU G 318
SITE 2 AE6 5 ARG G 319
SITE 1 AE7 4 HIS G 490 PRO G 491 ILE G 492 VAL G 493
CRYST1 85.672 68.111 96.056 90.00 109.90 90.00 P 1 21 1 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 0.011672 0.000000 0.004225 0.00000
SCALE2 0.000000 0.014682 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011071 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
