HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 23-DEC-12 4IJW
TITLE CRYSTAL STRUCTURE OF 11B-HSD1 DOUBLE MUTANT (L262R, F278E) IN COMPLEX
TITLE 2 WITH 3-[1-(4-CHLOROPHENYL)CYCLOPROPYL]-8-CYCLOPROPYL[1,2,
TITLE 3 4]TRIAZOLO[4,3-A]PYRIDINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CORTICOSTEROID 11-BETA-DEHYDROGENASE ISOZYME 1;
COMPND 3 CHAIN: A, B, D, E;
COMPND 4 SYNONYM: 11-BETA-HYDROXYSTEROID DEHYDROGENASE 1, 11-DH, 11-BETA-HSD1;
COMPND 5 EC: 1.1.1.146;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HSD11B1, HSD11, HSD11L;
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 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS 11B-HSD1, SDR, DEHYDROGENASE, HYDROXYSTEROID, INHIBITOR,
KEYWDS 2 OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SHERIFF
REVDAT 4 03-APR-24 4IJW 1 REMARK
REVDAT 3 28-FEB-24 4IJW 1 REMARK SEQADV
REVDAT 2 06-AUG-14 4IJW 1 JRNL
REVDAT 1 11-JUN-14 4IJW 0
JRNL AUTH J.LI,L.J.KENNEDY,H.WANG,J.J.LI,S.J.WALKER,Z.HONG,
JRNL AUTH 2 S.P.O'CONNOR,A.NAYEEM,D.M.CAMAC,P.E.MORIN,S.SHERIFF,M.WANG,
JRNL AUTH 3 T.HARPER,R.GOLLA,R.SEETHALA,T.HARRITY,R.P.PONTICIELLO,
JRNL AUTH 4 N.N.MORGAN,J.R.TAYLOR,R.ZEBO,D.A.GORDON,J.A.ROBL
JRNL TITL OPTIMIZATION OF 1,2,4-TRIAZOLOPYRIDINES AS INHIBITORS OF
JRNL TITL 2 HUMAN 11 BETA-HYDROXYSTEROID DEHYDROGENASE TYPE 1 (11
JRNL TITL 3 BETA-HSD-1).
JRNL REF ACS MED CHEM LETT V. 5 803 2014
JRNL REFN ESSN 1464-3405
JRNL PMID 25050169
JRNL DOI 10.1021/ML500144H
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT BUSTER-TNT 2.5.1
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 48295
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.260
REMARK 3 FREE R VALUE TEST SET COUNT : 1093
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.41
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.79
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3009
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2242
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2941
REMARK 3 BIN R VALUE (WORKING SET) : 0.2239
REMARK 3 BIN FREE R VALUE : 0.2369
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.26
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 68
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 : 8239
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 280
REMARK 3 SOLVENT ATOMS : 202
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.27
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.90240
REMARK 3 B22 (A**2) : -1.96050
REMARK 3 B33 (A**2) : -4.94190
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) : 0.307
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.395
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.237
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.390
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.239
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 : 0.905
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.881
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 8680 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 11765 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 3143 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 165 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1338 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 8680 ; 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 : NULL ; NULL ; NULL
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 : NULL ; NULL ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.12
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL
REMARK 3 OTHER TORSION ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESTRAINT 1 : CSDX_PROTGEO.DAT (V1.40)
REMARK 3 20080428 RESTRAINT 2 : NUCLGEO.DAT (V1.10) 20070206 RESTRAINT 3 :
REMARK 3 BCORREL.DAT (V1.15) 20080423 RESTRAINT 4 : CONTACT.DAT (V1.15)
REMARK 3 20070207 RESTRAINT 5 : ASSUME.DAT (V1.8) 20070124 NCS MODEL :
REMARK 3 RESTRAINT LSSR TARGET RESTRAINT : NONE
REMARK 4
REMARK 4 4IJW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-13.
REMARK 100 THE DEPOSITION ID IS D_1000076844.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MICROMAX CONFOCAL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 92
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 (DENZO)
REMARK 200 DATA SCALING SOFTWARE : HKL-2000 (SCALEPACK)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48368
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 83.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.37900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 11BHSD/LIGAND
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM POTASSIUM FORMATE, PH 7.3, 22%
REMARK 280 (W/V) PEG3350, 1.5 MM ZWITTERGENT 3-12, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 37.25000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.70000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.15000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.70000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.25000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.15000
REMARK 290 SMTRY3 4 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: 8110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: 7750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 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 7
REMARK 465 SER A 8
REMARK 465 HIS A 9
REMARK 465 MET A 10
REMARK 465 ALA A 11
REMARK 465 SER A 12
REMARK 465 MET A 13
REMARK 465 THR A 14
REMARK 465 GLY A 15
REMARK 465 GLY A 16
REMARK 465 GLN A 17
REMARK 465 GLN A 18
REMARK 465 MET A 19
REMARK 465 GLY A 20
REMARK 465 ARG A 21
REMARK 465 GLY A 22
REMARK 465 SER A 23
REMARK 465 ASN A 24
REMARK 465 GLU A 25
REMARK 465 PHE A 289
REMARK 465 ILE A 290
REMARK 465 ASN A 291
REMARK 465 LYS A 292
REMARK 465 GLY B 7
REMARK 465 SER B 8
REMARK 465 HIS B 9
REMARK 465 PHE B 289
REMARK 465 ILE B 290
REMARK 465 ASN B 291
REMARK 465 LYS B 292
REMARK 465 GLY D 7
REMARK 465 SER D 8
REMARK 465 HIS D 9
REMARK 465 ASN D 285
REMARK 465 MET D 286
REMARK 465 ASP D 287
REMARK 465 ARG D 288
REMARK 465 PHE D 289
REMARK 465 ILE D 290
REMARK 465 ASN D 291
REMARK 465 LYS D 292
REMARK 465 GLY E 7
REMARK 465 SER E 8
REMARK 465 HIS E 9
REMARK 465 MET E 10
REMARK 465 ALA E 11
REMARK 465 SER E 12
REMARK 465 MET E 13
REMARK 465 THR E 14
REMARK 465 GLY E 15
REMARK 465 GLY E 16
REMARK 465 GLN E 17
REMARK 465 GLN E 18
REMARK 465 MET E 19
REMARK 465 GLY E 20
REMARK 465 ARG E 21
REMARK 465 GLY E 22
REMARK 465 SER E 23
REMARK 465 ASN E 24
REMARK 465 PHE E 289
REMARK 465 ILE E 290
REMARK 465 ASN E 291
REMARK 465 LYS E 292
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 GLN B 17 CG CD OE1 NE2
REMARK 470 ARG B 21 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 73 CG CD CE NZ
REMARK 470 SER D 12 OG
REMARK 470 GLU D 25 CG CD OE1 OE2
REMARK 470 HIS D 130 CG ND1 CD2 CE1 NE2
REMARK 470 ARG E 262 CG CD NE CZ NH1 NH2
REMARK 470 TRP E 263 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP E 263 CZ3 CH2
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 ALA A 65 179.26 169.25
REMARK 500 HIS A 130 -69.06 -121.14
REMARK 500 ASP A 131 15.30 -151.31
REMARK 500 PHE A 144 -62.38 -127.95
REMARK 500 SER A 169 -160.54 -122.25
REMARK 500 LYS A 174 -36.61 -135.49
REMARK 500 ASP A 219 39.91 -72.01
REMARK 500 HIS A 232 77.87 -111.01
REMARK 500 ALA B 65 -178.10 178.43
REMARK 500 HIS B 130 -69.14 -121.45
REMARK 500 ASP B 131 14.87 -150.40
REMARK 500 PHE B 144 -61.30 -121.62
REMARK 500 SER B 169 -158.76 -121.77
REMARK 500 LYS B 174 -36.05 -136.19
REMARK 500 ASP B 219 39.65 -72.64
REMARK 500 ALA D 11 -48.98 60.42
REMARK 500 ALA D 65 179.38 177.48
REMARK 500 HIS D 130 -69.07 -122.20
REMARK 500 ASP D 131 16.28 -150.22
REMARK 500 PHE D 144 -62.65 -123.36
REMARK 500 SER D 169 -160.60 -123.19
REMARK 500 LYS D 174 -36.61 -137.33
REMARK 500 ASP D 219 38.87 -72.82
REMARK 500 ALA E 65 -180.00 174.43
REMARK 500 ASN E 119 -30.04 -130.55
REMARK 500 HIS E 130 -69.80 -121.32
REMARK 500 ASP E 131 15.34 -151.12
REMARK 500 PHE E 144 -61.54 -124.66
REMARK 500 SER E 169 -159.97 -122.28
REMARK 500 LYS E 174 -35.50 -136.98
REMARK 500 ASP E 219 39.29 -72.76
REMARK 500 SER E 283 -31.58 -156.93
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 NAP A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1EQ A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1EQ B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1EQ D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1EQ E 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4IJU RELATED DB: PDB
REMARK 900 RELATED ID: 4IJV RELATED DB: PDB
DBREF 4IJW A 11 292 UNP P28845 DHI1_HUMAN 23 292
DBREF 4IJW B 11 292 UNP P28845 DHI1_HUMAN 23 292
DBREF 4IJW D 11 292 UNP P28845 DHI1_HUMAN 23 292
DBREF 4IJW E 11 292 UNP P28845 DHI1_HUMAN 23 292
SEQADV 4IJW GLY A 7 UNP P28845 EXPRESSION TAG
SEQADV 4IJW SER A 8 UNP P28845 EXPRESSION TAG
SEQADV 4IJW HIS A 9 UNP P28845 EXPRESSION TAG
SEQADV 4IJW MET A 10 UNP P28845 EXPRESSION TAG
SEQADV 4IJW SER A 12 UNP P28845 EXPRESSION TAG
SEQADV 4IJW MET A 13 UNP P28845 EXPRESSION TAG
SEQADV 4IJW THR A 14 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLY A 15 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLY A 16 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLN A 17 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLN A 18 UNP P28845 EXPRESSION TAG
SEQADV 4IJW MET A 19 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLY A 20 UNP P28845 EXPRESSION TAG
SEQADV 4IJW ARG A 21 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLY A 22 UNP P28845 EXPRESSION TAG
SEQADV 4IJW SER A 23 UNP P28845 EXPRESSION TAG
SEQADV 4IJW ARG A 262 UNP P28845 LEU 262 ENGINEERED MUTATION
SEQADV 4IJW GLU A 278 UNP P28845 PHE 278 ENGINEERED MUTATION
SEQADV 4IJW GLY B 7 UNP P28845 EXPRESSION TAG
SEQADV 4IJW SER B 8 UNP P28845 EXPRESSION TAG
SEQADV 4IJW HIS B 9 UNP P28845 EXPRESSION TAG
SEQADV 4IJW MET B 10 UNP P28845 EXPRESSION TAG
SEQADV 4IJW SER B 12 UNP P28845 EXPRESSION TAG
SEQADV 4IJW MET B 13 UNP P28845 EXPRESSION TAG
SEQADV 4IJW THR B 14 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLY B 15 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLY B 16 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLN B 17 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLN B 18 UNP P28845 EXPRESSION TAG
SEQADV 4IJW MET B 19 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLY B 20 UNP P28845 EXPRESSION TAG
SEQADV 4IJW ARG B 21 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLY B 22 UNP P28845 EXPRESSION TAG
SEQADV 4IJW SER B 23 UNP P28845 EXPRESSION TAG
SEQADV 4IJW ARG B 262 UNP P28845 LEU 262 ENGINEERED MUTATION
SEQADV 4IJW GLU B 278 UNP P28845 PHE 278 ENGINEERED MUTATION
SEQADV 4IJW GLY D 7 UNP P28845 EXPRESSION TAG
SEQADV 4IJW SER D 8 UNP P28845 EXPRESSION TAG
SEQADV 4IJW HIS D 9 UNP P28845 EXPRESSION TAG
SEQADV 4IJW MET D 10 UNP P28845 EXPRESSION TAG
SEQADV 4IJW SER D 12 UNP P28845 EXPRESSION TAG
SEQADV 4IJW MET D 13 UNP P28845 EXPRESSION TAG
SEQADV 4IJW THR D 14 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLY D 15 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLY D 16 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLN D 17 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLN D 18 UNP P28845 EXPRESSION TAG
SEQADV 4IJW MET D 19 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLY D 20 UNP P28845 EXPRESSION TAG
SEQADV 4IJW ARG D 21 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLY D 22 UNP P28845 EXPRESSION TAG
SEQADV 4IJW SER D 23 UNP P28845 EXPRESSION TAG
SEQADV 4IJW ARG D 262 UNP P28845 LEU 262 ENGINEERED MUTATION
SEQADV 4IJW GLU D 278 UNP P28845 PHE 278 ENGINEERED MUTATION
SEQADV 4IJW GLY E 7 UNP P28845 EXPRESSION TAG
SEQADV 4IJW SER E 8 UNP P28845 EXPRESSION TAG
SEQADV 4IJW HIS E 9 UNP P28845 EXPRESSION TAG
SEQADV 4IJW MET E 10 UNP P28845 EXPRESSION TAG
SEQADV 4IJW SER E 12 UNP P28845 EXPRESSION TAG
SEQADV 4IJW MET E 13 UNP P28845 EXPRESSION TAG
SEQADV 4IJW THR E 14 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLY E 15 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLY E 16 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLN E 17 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLN E 18 UNP P28845 EXPRESSION TAG
SEQADV 4IJW MET E 19 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLY E 20 UNP P28845 EXPRESSION TAG
SEQADV 4IJW ARG E 21 UNP P28845 EXPRESSION TAG
SEQADV 4IJW GLY E 22 UNP P28845 EXPRESSION TAG
SEQADV 4IJW SER E 23 UNP P28845 EXPRESSION TAG
SEQADV 4IJW ARG E 262 UNP P28845 LEU 262 ENGINEERED MUTATION
SEQADV 4IJW GLU E 278 UNP P28845 PHE 278 ENGINEERED MUTATION
SEQRES 1 A 286 GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET
SEQRES 2 A 286 GLY ARG GLY SER ASN GLU GLU PHE ARG PRO GLU MET LEU
SEQRES 3 A 286 GLN GLY LYS LYS VAL ILE VAL THR GLY ALA SER LYS GLY
SEQRES 4 A 286 ILE GLY ARG GLU MET ALA TYR HIS LEU ALA LYS MET GLY
SEQRES 5 A 286 ALA HIS VAL VAL VAL THR ALA ARG SER LYS GLU THR LEU
SEQRES 6 A 286 GLN LYS VAL VAL SER HIS CYS LEU GLU LEU GLY ALA ALA
SEQRES 7 A 286 SER ALA HIS TYR ILE ALA GLY THR MET GLU ASP MET THR
SEQRES 8 A 286 PHE ALA GLU GLN PHE VAL ALA GLN ALA GLY LYS LEU MET
SEQRES 9 A 286 GLY GLY LEU ASP MET LEU ILE LEU ASN HIS ILE THR ASN
SEQRES 10 A 286 THR SER LEU ASN LEU PHE HIS ASP ASP ILE HIS HIS VAL
SEQRES 11 A 286 ARG LYS SER MET GLU VAL ASN PHE LEU SER TYR VAL VAL
SEQRES 12 A 286 LEU THR VAL ALA ALA LEU PRO MET LEU LYS GLN SER ASN
SEQRES 13 A 286 GLY SER ILE VAL VAL VAL SER SER LEU ALA GLY LYS VAL
SEQRES 14 A 286 ALA TYR PRO MET VAL ALA ALA TYR SER ALA SER LYS PHE
SEQRES 15 A 286 ALA LEU ASP GLY PHE PHE SER SER ILE ARG LYS GLU TYR
SEQRES 16 A 286 SER VAL SER ARG VAL ASN VAL SER ILE THR LEU CYS VAL
SEQRES 17 A 286 LEU GLY LEU ILE ASP THR GLU THR ALA MET LYS ALA VAL
SEQRES 18 A 286 SER GLY ILE VAL HIS MET GLN ALA ALA PRO LYS GLU GLU
SEQRES 19 A 286 CYS ALA LEU GLU ILE ILE LYS GLY GLY ALA LEU ARG GLN
SEQRES 20 A 286 GLU GLU VAL TYR TYR ASP SER SER ARG TRP THR THR LEU
SEQRES 21 A 286 LEU ILE ARG ASN PRO CYS ARG LYS ILE LEU GLU GLU LEU
SEQRES 22 A 286 TYR SER THR SER TYR ASN MET ASP ARG PHE ILE ASN LYS
SEQRES 1 B 286 GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET
SEQRES 2 B 286 GLY ARG GLY SER ASN GLU GLU PHE ARG PRO GLU MET LEU
SEQRES 3 B 286 GLN GLY LYS LYS VAL ILE VAL THR GLY ALA SER LYS GLY
SEQRES 4 B 286 ILE GLY ARG GLU MET ALA TYR HIS LEU ALA LYS MET GLY
SEQRES 5 B 286 ALA HIS VAL VAL VAL THR ALA ARG SER LYS GLU THR LEU
SEQRES 6 B 286 GLN LYS VAL VAL SER HIS CYS LEU GLU LEU GLY ALA ALA
SEQRES 7 B 286 SER ALA HIS TYR ILE ALA GLY THR MET GLU ASP MET THR
SEQRES 8 B 286 PHE ALA GLU GLN PHE VAL ALA GLN ALA GLY LYS LEU MET
SEQRES 9 B 286 GLY GLY LEU ASP MET LEU ILE LEU ASN HIS ILE THR ASN
SEQRES 10 B 286 THR SER LEU ASN LEU PHE HIS ASP ASP ILE HIS HIS VAL
SEQRES 11 B 286 ARG LYS SER MET GLU VAL ASN PHE LEU SER TYR VAL VAL
SEQRES 12 B 286 LEU THR VAL ALA ALA LEU PRO MET LEU LYS GLN SER ASN
SEQRES 13 B 286 GLY SER ILE VAL VAL VAL SER SER LEU ALA GLY LYS VAL
SEQRES 14 B 286 ALA TYR PRO MET VAL ALA ALA TYR SER ALA SER LYS PHE
SEQRES 15 B 286 ALA LEU ASP GLY PHE PHE SER SER ILE ARG LYS GLU TYR
SEQRES 16 B 286 SER VAL SER ARG VAL ASN VAL SER ILE THR LEU CYS VAL
SEQRES 17 B 286 LEU GLY LEU ILE ASP THR GLU THR ALA MET LYS ALA VAL
SEQRES 18 B 286 SER GLY ILE VAL HIS MET GLN ALA ALA PRO LYS GLU GLU
SEQRES 19 B 286 CYS ALA LEU GLU ILE ILE LYS GLY GLY ALA LEU ARG GLN
SEQRES 20 B 286 GLU GLU VAL TYR TYR ASP SER SER ARG TRP THR THR LEU
SEQRES 21 B 286 LEU ILE ARG ASN PRO CYS ARG LYS ILE LEU GLU GLU LEU
SEQRES 22 B 286 TYR SER THR SER TYR ASN MET ASP ARG PHE ILE ASN LYS
SEQRES 1 D 286 GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET
SEQRES 2 D 286 GLY ARG GLY SER ASN GLU GLU PHE ARG PRO GLU MET LEU
SEQRES 3 D 286 GLN GLY LYS LYS VAL ILE VAL THR GLY ALA SER LYS GLY
SEQRES 4 D 286 ILE GLY ARG GLU MET ALA TYR HIS LEU ALA LYS MET GLY
SEQRES 5 D 286 ALA HIS VAL VAL VAL THR ALA ARG SER LYS GLU THR LEU
SEQRES 6 D 286 GLN LYS VAL VAL SER HIS CYS LEU GLU LEU GLY ALA ALA
SEQRES 7 D 286 SER ALA HIS TYR ILE ALA GLY THR MET GLU ASP MET THR
SEQRES 8 D 286 PHE ALA GLU GLN PHE VAL ALA GLN ALA GLY LYS LEU MET
SEQRES 9 D 286 GLY GLY LEU ASP MET LEU ILE LEU ASN HIS ILE THR ASN
SEQRES 10 D 286 THR SER LEU ASN LEU PHE HIS ASP ASP ILE HIS HIS VAL
SEQRES 11 D 286 ARG LYS SER MET GLU VAL ASN PHE LEU SER TYR VAL VAL
SEQRES 12 D 286 LEU THR VAL ALA ALA LEU PRO MET LEU LYS GLN SER ASN
SEQRES 13 D 286 GLY SER ILE VAL VAL VAL SER SER LEU ALA GLY LYS VAL
SEQRES 14 D 286 ALA TYR PRO MET VAL ALA ALA TYR SER ALA SER LYS PHE
SEQRES 15 D 286 ALA LEU ASP GLY PHE PHE SER SER ILE ARG LYS GLU TYR
SEQRES 16 D 286 SER VAL SER ARG VAL ASN VAL SER ILE THR LEU CYS VAL
SEQRES 17 D 286 LEU GLY LEU ILE ASP THR GLU THR ALA MET LYS ALA VAL
SEQRES 18 D 286 SER GLY ILE VAL HIS MET GLN ALA ALA PRO LYS GLU GLU
SEQRES 19 D 286 CYS ALA LEU GLU ILE ILE LYS GLY GLY ALA LEU ARG GLN
SEQRES 20 D 286 GLU GLU VAL TYR TYR ASP SER SER ARG TRP THR THR LEU
SEQRES 21 D 286 LEU ILE ARG ASN PRO CYS ARG LYS ILE LEU GLU GLU LEU
SEQRES 22 D 286 TYR SER THR SER TYR ASN MET ASP ARG PHE ILE ASN LYS
SEQRES 1 E 286 GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET
SEQRES 2 E 286 GLY ARG GLY SER ASN GLU GLU PHE ARG PRO GLU MET LEU
SEQRES 3 E 286 GLN GLY LYS LYS VAL ILE VAL THR GLY ALA SER LYS GLY
SEQRES 4 E 286 ILE GLY ARG GLU MET ALA TYR HIS LEU ALA LYS MET GLY
SEQRES 5 E 286 ALA HIS VAL VAL VAL THR ALA ARG SER LYS GLU THR LEU
SEQRES 6 E 286 GLN LYS VAL VAL SER HIS CYS LEU GLU LEU GLY ALA ALA
SEQRES 7 E 286 SER ALA HIS TYR ILE ALA GLY THR MET GLU ASP MET THR
SEQRES 8 E 286 PHE ALA GLU GLN PHE VAL ALA GLN ALA GLY LYS LEU MET
SEQRES 9 E 286 GLY GLY LEU ASP MET LEU ILE LEU ASN HIS ILE THR ASN
SEQRES 10 E 286 THR SER LEU ASN LEU PHE HIS ASP ASP ILE HIS HIS VAL
SEQRES 11 E 286 ARG LYS SER MET GLU VAL ASN PHE LEU SER TYR VAL VAL
SEQRES 12 E 286 LEU THR VAL ALA ALA LEU PRO MET LEU LYS GLN SER ASN
SEQRES 13 E 286 GLY SER ILE VAL VAL VAL SER SER LEU ALA GLY LYS VAL
SEQRES 14 E 286 ALA TYR PRO MET VAL ALA ALA TYR SER ALA SER LYS PHE
SEQRES 15 E 286 ALA LEU ASP GLY PHE PHE SER SER ILE ARG LYS GLU TYR
SEQRES 16 E 286 SER VAL SER ARG VAL ASN VAL SER ILE THR LEU CYS VAL
SEQRES 17 E 286 LEU GLY LEU ILE ASP THR GLU THR ALA MET LYS ALA VAL
SEQRES 18 E 286 SER GLY ILE VAL HIS MET GLN ALA ALA PRO LYS GLU GLU
SEQRES 19 E 286 CYS ALA LEU GLU ILE ILE LYS GLY GLY ALA LEU ARG GLN
SEQRES 20 E 286 GLU GLU VAL TYR TYR ASP SER SER ARG TRP THR THR LEU
SEQRES 21 E 286 LEU ILE ARG ASN PRO CYS ARG LYS ILE LEU GLU GLU LEU
SEQRES 22 E 286 TYR SER THR SER TYR ASN MET ASP ARG PHE ILE ASN LYS
HET NAP A 301 48
HET 1EQ A 302 22
HET NAP B 301 48
HET 1EQ B 302 22
HET NAP D 301 48
HET 1EQ D 302 22
HET NAP E 301 48
HET 1EQ E 302 22
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM 1EQ 3-[1-(4-CHLOROPHENYL)CYCLOPROPYL]-8-CYCLOPROPYL[1,2,
HETNAM 2 1EQ 4]TRIAZOLO[4,3-A]PYRIDINE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 5 NAP 4(C21 H28 N7 O17 P3)
FORMUL 6 1EQ 4(C18 H16 CL N3)
FORMUL 13 HOH *202(H2 O)
HELIX 1 1 ARG A 28 GLN A 33 5 6
HELIX 2 2 LYS A 44 MET A 57 1 14
HELIX 3 3 SER A 67 GLY A 82 1 16
HELIX 4 4 ASP A 95 GLY A 111 1 17
HELIX 5 5 ASP A 132 PHE A 144 1 13
HELIX 6 6 PHE A 144 ASN A 162 1 19
HELIX 7 7 SER A 170 LYS A 174 5 5
HELIX 8 8 VAL A 180 SER A 204 1 25
HELIX 9 9 THR A 220 SER A 228 1 9
HELIX 10 10 PRO A 237 LEU A 251 1 15
HELIX 11 11 SER A 261 ARG A 269 1 9
HELIX 12 12 ASN A 270 TYR A 280 1 11
HELIX 13 13 MET B 10 THR B 14 5 5
HELIX 14 14 ARG B 28 GLN B 33 5 6
HELIX 15 15 LYS B 44 MET B 57 1 14
HELIX 16 16 SER B 67 GLY B 82 1 16
HELIX 17 17 ASP B 95 GLY B 111 1 17
HELIX 18 18 ASP B 132 PHE B 144 1 13
HELIX 19 19 PHE B 144 ASN B 162 1 19
HELIX 20 20 SER B 170 LYS B 174 5 5
HELIX 21 21 VAL B 180 SER B 204 1 25
HELIX 22 22 THR B 220 SER B 228 1 9
HELIX 23 23 PRO B 237 LEU B 251 1 15
HELIX 24 24 TRP B 263 ILE B 268 1 6
HELIX 25 25 ASN B 270 THR B 282 1 13
HELIX 26 26 ARG D 28 GLN D 33 5 6
HELIX 27 27 LYS D 44 MET D 57 1 14
HELIX 28 28 SER D 67 GLY D 82 1 16
HELIX 29 29 ASP D 95 GLY D 111 1 17
HELIX 30 30 ASP D 132 PHE D 144 1 13
HELIX 31 31 PHE D 144 ASN D 162 1 19
HELIX 32 32 SER D 170 LYS D 174 5 5
HELIX 33 33 VAL D 180 SER D 204 1 25
HELIX 34 34 THR D 220 SER D 228 1 9
HELIX 35 35 PRO D 237 LEU D 251 1 15
HELIX 36 36 SER D 261 ILE D 268 1 8
HELIX 37 37 ASN D 270 SER D 281 1 12
HELIX 38 38 THR D 282 TYR D 284 5 3
HELIX 39 39 ARG E 28 GLN E 33 5 6
HELIX 40 40 LYS E 44 MET E 57 1 14
HELIX 41 41 SER E 67 GLY E 82 1 16
HELIX 42 42 ASP E 95 GLY E 111 1 17
HELIX 43 43 ASP E 132 PHE E 144 1 13
HELIX 44 44 PHE E 144 ASN E 162 1 19
HELIX 45 45 SER E 170 LYS E 174 5 5
HELIX 46 46 VAL E 180 SER E 204 1 25
HELIX 47 47 THR E 220 SER E 228 1 9
HELIX 48 48 PRO E 237 LEU E 251 1 15
HELIX 49 49 SER E 261 ILE E 268 1 8
HELIX 50 50 ASN E 270 LEU E 279 1 10
SHEET 1 A 7 SER A 85 ALA A 90 0
SHEET 2 A 7 HIS A 60 ALA A 65 1 N VAL A 63 O HIS A 87
SHEET 3 A 7 LYS A 36 VAL A 39 1 N VAL A 37 O HIS A 60
SHEET 4 A 7 MET A 115 LEU A 118 1 O ILE A 117 N ILE A 38
SHEET 5 A 7 SER A 164 VAL A 168 1 O VAL A 166 N LEU A 118
SHEET 6 A 7 SER A 209 LEU A 215 1 O THR A 211 N VAL A 167
SHEET 7 A 7 GLU A 255 TYR A 258 1 O VAL A 256 N VAL A 214
SHEET 1 B 7 SER B 85 ALA B 90 0
SHEET 2 B 7 HIS B 60 ALA B 65 1 N VAL B 63 O HIS B 87
SHEET 3 B 7 LYS B 36 VAL B 39 1 N VAL B 37 O HIS B 60
SHEET 4 B 7 MET B 115 LEU B 118 1 O ILE B 117 N ILE B 38
SHEET 5 B 7 SER B 164 VAL B 168 1 O VAL B 166 N LEU B 118
SHEET 6 B 7 SER B 209 LEU B 215 1 O THR B 211 N VAL B 167
SHEET 7 B 7 GLU B 255 TYR B 258 1 O VAL B 256 N VAL B 214
SHEET 1 C 7 SER D 85 ALA D 90 0
SHEET 2 C 7 HIS D 60 ALA D 65 1 N VAL D 63 O HIS D 87
SHEET 3 C 7 LYS D 36 VAL D 39 1 N VAL D 37 O HIS D 60
SHEET 4 C 7 MET D 115 LEU D 118 1 N MET D 115 O LYS D 36
SHEET 5 C 7 SER D 164 VAL D 168 1 O VAL D 166 N LEU D 118
SHEET 6 C 7 SER D 209 LEU D 215 1 O THR D 211 N VAL D 167
SHEET 7 C 7 GLU D 255 TYR D 258 1 O VAL D 256 N VAL D 214
SHEET 1 D 7 SER E 85 ALA E 90 0
SHEET 2 D 7 HIS E 60 ALA E 65 1 N VAL E 63 O HIS E 87
SHEET 3 D 7 LYS E 36 VAL E 39 1 N VAL E 37 O HIS E 60
SHEET 4 D 7 MET E 115 LEU E 118 1 O ILE E 117 N ILE E 38
SHEET 5 D 7 SER E 164 VAL E 168 1 O VAL E 166 N LEU E 118
SHEET 6 D 7 SER E 209 LEU E 215 1 O THR E 211 N VAL E 167
SHEET 7 D 7 GLU E 255 TYR E 258 1 O VAL E 256 N VAL E 214
SITE 1 AC1 27 GLY A 41 SER A 43 LYS A 44 GLY A 45
SITE 2 AC1 27 ILE A 46 ALA A 65 ARG A 66 SER A 67
SITE 3 AC1 27 THR A 92 MET A 93 GLU A 94 ASN A 119
SITE 4 AC1 27 ILE A 121 VAL A 168 SER A 169 SER A 170
SITE 5 AC1 27 TYR A 183 LYS A 187 LEU A 215 GLY A 216
SITE 6 AC1 27 ILE A 218 THR A 220 THR A 222 ALA A 223
SITE 7 AC1 27 1EQ A 302 HOH A 401 HOH A 436
SITE 1 AC2 11 ILE A 121 SER A 170 TYR A 177 PRO A 178
SITE 2 AC2 11 TYR A 183 GLY A 216 LEU A 217 ALA A 223
SITE 3 AC2 11 VAL A 231 NAP A 301 TYR B 284
SITE 1 AC3 32 GLY B 41 ALA B 42 SER B 43 LYS B 44
SITE 2 AC3 32 GLY B 45 ILE B 46 ALA B 65 ARG B 66
SITE 3 AC3 32 SER B 67 THR B 92 MET B 93 ASN B 119
SITE 4 AC3 32 ILE B 121 VAL B 168 SER B 169 SER B 170
SITE 5 AC3 32 TYR B 183 LYS B 187 LEU B 215 GLY B 216
SITE 6 AC3 32 LEU B 217 ILE B 218 THR B 220 THR B 222
SITE 7 AC3 32 ALA B 223 1EQ B 302 HOH B 408 HOH B 420
SITE 8 AC3 32 HOH B 422 HOH B 426 HOH B 438 HOH B 445
SITE 1 AC4 13 TYR A 284 THR B 124 SER B 170 TYR B 177
SITE 2 AC4 13 PRO B 178 VAL B 180 TYR B 183 GLY B 216
SITE 3 AC4 13 LEU B 217 VAL B 227 VAL B 231 MET B 233
SITE 4 AC4 13 NAP B 301
SITE 1 AC5 30 GLY D 41 ALA D 42 SER D 43 LYS D 44
SITE 2 AC5 30 GLY D 45 ILE D 46 ALA D 65 ARG D 66
SITE 3 AC5 30 SER D 67 THR D 92 MET D 93 ASN D 119
SITE 4 AC5 30 ILE D 121 VAL D 168 SER D 169 SER D 170
SITE 5 AC5 30 TYR D 183 LYS D 187 LEU D 215 GLY D 216
SITE 6 AC5 30 ILE D 218 THR D 220 THR D 222 ALA D 223
SITE 7 AC5 30 1EQ D 302 HOH D 402 HOH D 404 HOH D 405
SITE 8 AC5 30 HOH D 436 HOH D 437
SITE 1 AC6 11 ILE D 121 SER D 170 TYR D 177 PRO D 178
SITE 2 AC6 11 MET D 179 TYR D 183 GLY D 216 LEU D 217
SITE 3 AC6 11 ALA D 223 NAP D 301 TYR E 284
SITE 1 AC7 32 GLY E 41 SER E 43 LYS E 44 GLY E 45
SITE 2 AC7 32 ILE E 46 ALA E 65 ARG E 66 SER E 67
SITE 3 AC7 32 THR E 92 MET E 93 ASN E 119 HIS E 120
SITE 4 AC7 32 ILE E 121 VAL E 168 SER E 169 SER E 170
SITE 5 AC7 32 TYR E 183 LYS E 187 LEU E 215 GLY E 216
SITE 6 AC7 32 LEU E 217 ILE E 218 THR E 220 THR E 222
SITE 7 AC7 32 ALA E 223 1EQ E 302 HOH E 406 HOH E 410
SITE 8 AC7 32 HOH E 412 HOH E 413 HOH E 433 HOH E 439
SITE 1 AC8 10 ILE E 121 SER E 170 TYR E 177 PRO E 178
SITE 2 AC8 10 TYR E 183 GLY E 216 LEU E 217 ALA E 223
SITE 3 AC8 10 VAL E 231 NAP E 301
CRYST1 74.500 94.300 167.400 90.00 90.00 90.00 P 21 21 21 16
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 0.013423 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010604 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005974 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
