LinkDB: 6FZU
Original site: 6FZU
Chemical substance (1) PDB-CCD (1) Gene (2) KEGG GENES (2) Protein sequence (8) UniProt (2) SWISS-PROT (2) PDBSTR (4) DNA sequence (1) EMBL (1) Protein domain (6) InterPro (5) PROSITE (1) Literature (1) PubMed (1) All databases (19)
Download RDF
HEADER TRANSCRIPTION 15-MAR-18 6FZU
TITLE RORGT (264-518;C455S) IN COMPLEX WITH THE FRAGMENT ("CPD-1") AND
TITLE 2 RIP140 PEPTIDE AT 1.80A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR RECEPTOR ROR-GAMMA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN, 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 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: NUCLEAR RECEPTOR-INTERACTING PROTEIN 1;
COMPND 12 CHAIN: P, Q;
COMPND 13 SYNONYM: NUCLEAR FACTOR RIP140,RECEPTOR-INTERACTING PROTEIN 140
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 BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28-DERIVED VECTOR;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS FBS, NUCLEAR HORMONE RECEPTOR, LIGAND-BINDING DOMAIN, INVERSE
KEYWDS 2 AGONIST, SIGNALING PROTEIN, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.KALLEN
REVDAT 4 17-JAN-24 6FZU 1 REMARK
REVDAT 3 03-OCT-18 6FZU 1 REMARK
REVDAT 2 22-AUG-18 6FZU 1 JRNL
REVDAT 1 18-JUL-18 6FZU 0
JRNL AUTH D.A.CARCACHE,A.VULPETTI,J.KALLEN,H.MATTES,D.ORAIN,
JRNL AUTH 2 R.STRINGER,E.VANGREVELINGHE,R.M.WOLF,K.KAUPMANN,J.OTTL,
JRNL AUTH 3 J.DAWSON,N.G.COOKE,K.HOEGENAUER,A.BILLICH,J.WAGNER,
JRNL AUTH 4 C.GUNTERMANN,S.HINTERMANN
JRNL TITL OPTIMIZING A WEAKLY BINDING FRAGMENT INTO A POTENT ROR GAMMA
JRNL TITL 2 T INVERSE AGONIST WITH EFFICACY IN AN IN VIVO INFLAMMATION
JRNL TITL 3 MODEL.
JRNL REF J. MED. CHEM. V. 61 6724 2018
JRNL REFN ISSN 1520-4804
JRNL PMID 29990434
JRNL DOI 10.1021/ACS.JMEDCHEM.8B00529
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 44128
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) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2323
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4150
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 266
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.46000
REMARK 3 B22 (A**2) : 0.12000
REMARK 3 B33 (A**2) : -1.32000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.79000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.164
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.148
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.102
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.284
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 : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6FZU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1200009199.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAY-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46451
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 19.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.55900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5NTI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG3350, 0.2M AMMONIUM ACETATE,
REMARK 280 0.1M BIS-TRIS, PH 5.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 33.93700
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
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: 1000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P
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: 940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, Q
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 262
REMARK 465 PRO A 263
REMARK 465 GLU A 509
REMARK 465 THR A 510
REMARK 465 GLU A 511
REMARK 465 SER A 512
REMARK 465 PRO A 513
REMARK 465 VAL A 514
REMARK 465 GLY A 515
REMARK 465 LEU A 516
REMARK 465 SER A 517
REMARK 465 LYS A 518
REMARK 465 GLY B 262
REMARK 465 PRO B 263
REMARK 465 GLU B 509
REMARK 465 THR B 510
REMARK 465 GLU B 511
REMARK 465 SER B 512
REMARK 465 PRO B 513
REMARK 465 VAL B 514
REMARK 465 GLY B 515
REMARK 465 LEU B 516
REMARK 465 SER B 517
REMARK 465 LYS B 518
REMARK 465 ASN P 493
REMARK 465 SER P 494
REMARK 465 HIS P 495
REMARK 465 GLN P 496
REMARK 465 LYS P 497
REMARK 465 VAL P 498
REMARK 465 LYS P 508
REMARK 465 ASN P 509
REMARK 465 GLU P 510
REMARK 465 GLU P 511
REMARK 465 ASN P 512
REMARK 465 ASN Q 493
REMARK 465 SER Q 494
REMARK 465 HIS Q 495
REMARK 465 GLN Q 496
REMARK 465 LYS Q 497
REMARK 465 VAL Q 498
REMARK 465 LYS Q 508
REMARK 465 ASN Q 509
REMARK 465 GLU Q 510
REMARK 465 GLU Q 511
REMARK 465 ASN Q 512
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 773 O HOH B 814 1455 2.14
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 B 286 -61.63 71.15
REMARK 500 CYS B 393 57.64 -144.40
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 EE8 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EE8 B 601
DBREF 6FZU A 263 518 UNP P51449 RORG_HUMAN 263 518
DBREF 6FZU B 263 518 UNP P51449 RORG_HUMAN 263 518
DBREF 6FZU P 493 512 UNP P48552 NRIP1_HUMAN 493 512
DBREF 6FZU Q 493 512 UNP P48552 NRIP1_HUMAN 493 512
SEQADV 6FZU GLY A 262 UNP P51449 EXPRESSION TAG
SEQADV 6FZU SER A 455 UNP P51449 CYS 455 ENGINEERED MUTATION
SEQADV 6FZU GLY B 262 UNP P51449 EXPRESSION TAG
SEQADV 6FZU SER B 455 UNP P51449 CYS 455 ENGINEERED MUTATION
SEQRES 1 A 257 GLY PRO TYR ALA SER LEU THR GLU ILE GLU HIS LEU VAL
SEQRES 2 A 257 GLN SER VAL CYS LYS SER TYR ARG GLU THR CYS GLN LEU
SEQRES 3 A 257 ARG LEU GLU ASP LEU LEU ARG GLN ARG SER ASN ILE PHE
SEQRES 4 A 257 SER ARG GLU GLU VAL THR GLY TYR GLN ARG LYS SER MET
SEQRES 5 A 257 TRP GLU MET TRP GLU ARG CYS ALA HIS HIS LEU THR GLU
SEQRES 6 A 257 ALA ILE GLN TYR VAL VAL GLU PHE ALA LYS ARG LEU SER
SEQRES 7 A 257 GLY PHE MET GLU LEU CYS GLN ASN ASP GLN ILE VAL LEU
SEQRES 8 A 257 LEU LYS ALA GLY ALA MET GLU VAL VAL LEU VAL ARG MET
SEQRES 9 A 257 CYS ARG ALA TYR ASN ALA ASP ASN ARG THR VAL PHE PHE
SEQRES 10 A 257 GLU GLY LYS TYR GLY GLY MET GLU LEU PHE ARG ALA LEU
SEQRES 11 A 257 GLY CYS SER GLU LEU ILE SER SER ILE PHE ASP PHE SER
SEQRES 12 A 257 HIS SER LEU SER ALA LEU HIS PHE SER GLU ASP GLU ILE
SEQRES 13 A 257 ALA LEU TYR THR ALA LEU VAL LEU ILE ASN ALA HIS ARG
SEQRES 14 A 257 PRO GLY LEU GLN GLU LYS ARG LYS VAL GLU GLN LEU GLN
SEQRES 15 A 257 TYR ASN LEU GLU LEU ALA PHE HIS HIS HIS LEU SER LYS
SEQRES 16 A 257 THR HIS ARG GLN SER ILE LEU ALA LYS LEU PRO PRO LYS
SEQRES 17 A 257 GLY LYS LEU ARG SER LEU CYS SER GLN HIS VAL GLU ARG
SEQRES 18 A 257 LEU GLN ILE PHE GLN HIS LEU HIS PRO ILE VAL VAL GLN
SEQRES 19 A 257 ALA ALA PHE PRO PRO LEU TYR LYS GLU LEU PHE SER THR
SEQRES 20 A 257 GLU THR GLU SER PRO VAL GLY LEU SER LYS
SEQRES 1 B 257 GLY PRO TYR ALA SER LEU THR GLU ILE GLU HIS LEU VAL
SEQRES 2 B 257 GLN SER VAL CYS LYS SER TYR ARG GLU THR CYS GLN LEU
SEQRES 3 B 257 ARG LEU GLU ASP LEU LEU ARG GLN ARG SER ASN ILE PHE
SEQRES 4 B 257 SER ARG GLU GLU VAL THR GLY TYR GLN ARG LYS SER MET
SEQRES 5 B 257 TRP GLU MET TRP GLU ARG CYS ALA HIS HIS LEU THR GLU
SEQRES 6 B 257 ALA ILE GLN TYR VAL VAL GLU PHE ALA LYS ARG LEU SER
SEQRES 7 B 257 GLY PHE MET GLU LEU CYS GLN ASN ASP GLN ILE VAL LEU
SEQRES 8 B 257 LEU LYS ALA GLY ALA MET GLU VAL VAL LEU VAL ARG MET
SEQRES 9 B 257 CYS ARG ALA TYR ASN ALA ASP ASN ARG THR VAL PHE PHE
SEQRES 10 B 257 GLU GLY LYS TYR GLY GLY MET GLU LEU PHE ARG ALA LEU
SEQRES 11 B 257 GLY CYS SER GLU LEU ILE SER SER ILE PHE ASP PHE SER
SEQRES 12 B 257 HIS SER LEU SER ALA LEU HIS PHE SER GLU ASP GLU ILE
SEQRES 13 B 257 ALA LEU TYR THR ALA LEU VAL LEU ILE ASN ALA HIS ARG
SEQRES 14 B 257 PRO GLY LEU GLN GLU LYS ARG LYS VAL GLU GLN LEU GLN
SEQRES 15 B 257 TYR ASN LEU GLU LEU ALA PHE HIS HIS HIS LEU SER LYS
SEQRES 16 B 257 THR HIS ARG GLN SER ILE LEU ALA LYS LEU PRO PRO LYS
SEQRES 17 B 257 GLY LYS LEU ARG SER LEU CYS SER GLN HIS VAL GLU ARG
SEQRES 18 B 257 LEU GLN ILE PHE GLN HIS LEU HIS PRO ILE VAL VAL GLN
SEQRES 19 B 257 ALA ALA PHE PRO PRO LEU TYR LYS GLU LEU PHE SER THR
SEQRES 20 B 257 GLU THR GLU SER PRO VAL GLY LEU SER LYS
SEQRES 1 P 20 ASN SER HIS GLN LYS VAL THR LEU LEU GLN LEU LEU LEU
SEQRES 2 P 20 GLY HIS LYS ASN GLU GLU ASN
SEQRES 1 Q 20 ASN SER HIS GLN LYS VAL THR LEU LEU GLN LEU LEU LEU
SEQRES 2 Q 20 GLY HIS LYS ASN GLU GLU ASN
HET EE8 A 601 14
HET EE8 B 601 14
HETNAM EE8 ~{N}-(3-CHLORANYL-4-ETHOXY-PHENYL)ETHANAMIDE
FORMUL 5 EE8 2(C10 H12 CL N O2)
FORMUL 7 HOH *266(H2 O)
HELIX 1 AA1 SER A 266 THR A 284 1 19
HELIX 2 AA2 ARG A 288 ARG A 294 1 7
HELIX 3 AA3 SER A 301 ARG A 310 1 10
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 HIS A 458 LEU A 466 5 9
HELIX 11 AB2 PRO A 468 HIS A 490 1 23
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 SER B 266 THR B 284 1 19
HELIX 15 AB6 ARG B 288 GLN B 295 1 8
HELIX 16 AB7 SER B 301 LYS B 311 1 11
HELIX 17 AB8 SER B 312 LEU B 338 1 27
HELIX 18 AB9 CYS B 345 MET B 365 1 21
HELIX 19 AC1 GLY B 384 GLY B 392 5 9
HELIX 20 AC2 CYS B 393 ALA B 409 1 17
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 ARG B 459 LEU B 466 5 8
HELIX 24 AC6 PRO B 468 HIS B 490 1 23
HELIX 25 AC7 HIS B 490 PHE B 498 1 9
HELIX 26 AC8 PRO B 499 SER B 507 1 9
HELIX 27 AC9 LEU P 500 LEU P 505 1 6
HELIX 28 AD1 LEU Q 500 GLY Q 506 1 7
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 5 CYS A 320 HIS A 323 PHE A 377 PHE A 378
SITE 2 AC1 5 HOH A 706
SITE 1 AC2 5 CYS B 320 HIS B 323 PHE B 377 PHE B 378
SITE 2 AC2 5 HOH B 731
CRYST1 47.918 67.874 82.451 90.00 101.85 90.00 P 1 21 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 0.020869 0.000000 0.004378 0.00000
SCALE2 0.000000 0.014733 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012392 0.00000
(ATOM LINES ARE NOT SHOWN.)
END