HEADER TRANSCRIPTION 19-SEP-12 4H6J
TITLE IDENTIFICATION OF CYS 255 IN HIF-1 AS A NOVEL SITE FOR DEVELOPMENT OF
TITLE 2 COVALENT INHIBITORS OF HIF-1 /ARNT PASB DOMAIN PROTEIN-PROTEIN
TITLE 3 INTERACTION.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOXIA INDUCIBLE FACTOR 1-ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PAS-B DOMAIN, UNP RESIDUES 238-348;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ARYL HYDROCARBON NUCLEAR TRANSLOCATOR;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: PAS-B DOMAIN, UNP RESIDUES 357-470;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 GENE: HIF-1 ALPHA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (AI);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: T7 PROMOTER;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCECC-N1;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: ARNT;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21 (AI);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: T7 PROMOTER;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PCECC-N1
KEYWDS PAS DOMAIN, HETERODIMER, HYPOXIA INDUCIBLE FACTOR, TRANSCRIPTION
KEYWDS 2 FACTOR, ARNT, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR R.CARDOSO,R.A.LOVE,C.NILSSON,S.BERGQVIST,D.NOWLIN,J.YAN,K.LIU,J.ZHU,
AUTHOR 2 P.CHEN,Y.-L.DENG,H.J.DYSON,M.J.GREIG,A.BROOUN
REVDAT 4 28-FEB-24 4H6J 1 SEQADV
REVDAT 3 24-JAN-18 4H6J 1 AUTHOR
REVDAT 2 28-AUG-13 4H6J 1 JRNL
REVDAT 1 05-DEC-12 4H6J 0
JRNL AUTH R.CARDOSO,R.LOVE,C.L.NILSSON,S.BERGQVIST,D.NOWLIN,J.YAN,
JRNL AUTH 2 K.K.LIU,J.ZHU,P.CHEN,Y.L.DENG,H.J.DYSON,M.J.GREIG,A.BROOUN
JRNL TITL IDENTIFICATION OF CYS255 IN HIF-1 ALPHA AS A NOVEL SITE FOR
JRNL TITL 2 DEVELOPMENT OF COVALENT INHIBITORS OF HIF-1 ALPHA /ARNT PASB
JRNL TITL 3 DOMAIN PROTEIN-PROTEIN INTERACTION.
JRNL REF PROTEIN SCI. V. 21 1885 2012
JRNL REFN ISSN 0961-8368
JRNL PMID 23033253
JRNL DOI 10.1002/PRO.2172
REMARK 2
REMARK 2 RESOLUTION. 1.52 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.52
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.79
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1013880.240
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 35782
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) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1776
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.2160
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.2150
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1776
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0060
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 35782
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 63.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3806
REMARK 3 BIN R VALUE (WORKING SET) : 0.2890
REMARK 3 BIN FREE R VALUE : 0.3350
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 213
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.023
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1783
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 154
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.86000
REMARK 3 B22 (A**2) : 0.16000
REMARK 3 B33 (A**2) : -2.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 3.77000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.15
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.17
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 0.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.580
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.330 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.130 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.070 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.110 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 50.41
REMARK 3
REMARK 3 NCS MODEL : NONE
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARA
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARA
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4H6J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-SEP-12.
REMARK 100 THE DEPOSITION ID IS D_1000075081.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JAN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : CUSTOM
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PROCESS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35783
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.520
REMARK 200 RESOLUTION RANGE LOW (A) : 38.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : 0.04700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.52
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.43000
REMARK 200 R SYM FOR SHELL (I) : 0.43000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000, 0.2M MGCL2, 0.1M TRIS PH
REMARK 280 8.5 , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 34.42050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.47000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 34.42050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.47000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 576 LIES ON A SPECIAL POSITION.
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 236
REMARK 465 SER A 237
REMARK 465 GLY A 344
REMARK 465 ILE A 345
REMARK 465 ILE A 346
REMARK 465 GLN A 347
REMARK 465 HIS A 348
REMARK 465 GLY B 355
REMARK 465 SER B 467
REMARK 465 SER B 468
REMARK 465 GLN B 469
REMARK 465 GLU B 470
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 THR A 327 OG1 CG2
REMARK 470 LYS A 328 CG CD CE NZ
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3F1P RELATED DB: PDB
REMARK 900 HIF-2ALPHA + ARNT HETERODIMER
DBREF 4H6J A 238 348 UNP Q16665 HIF1A_HUMAN 238 348
DBREF 4H6J B 357 470 UNP P27540 ARNT_HUMAN 357 470
SEQADV 4H6J GLY A 236 UNP Q16665 EXPRESSION TAG
SEQADV 4H6J SER A 237 UNP Q16665 EXPRESSION TAG
SEQADV 4H6J GLU A 245 UNP Q16665 ARG 245 ENGINEERED MUTATION
SEQADV 4H6J GLY B 355 UNP P27540 EXPRESSION TAG
SEQADV 4H6J SER B 356 UNP P27540 EXPRESSION TAG
SEQADV 4H6J ARG B 362 UNP P27540 GLU 362 ENGINEERED MUTATION
SEQRES 1 A 113 GLY SER ASP SER LYS THR PHE LEU SER GLU HIS SER LEU
SEQRES 2 A 113 ASP MET LYS PHE SER TYR CYS ASP GLU ARG ILE THR GLU
SEQRES 3 A 113 LEU MET GLY TYR GLU PRO GLU GLU LEU LEU GLY ARG SER
SEQRES 4 A 113 ILE TYR GLU TYR TYR HIS ALA LEU ASP SER ASP HIS LEU
SEQRES 5 A 113 THR LYS THR HIS HIS ASP MET PHE THR LYS GLY GLN VAL
SEQRES 6 A 113 THR THR GLY GLN TYR ARG MET LEU ALA LYS ARG GLY GLY
SEQRES 7 A 113 TYR VAL TRP VAL GLU THR GLN ALA THR VAL ILE TYR ASN
SEQRES 8 A 113 THR LYS ASN SER GLN PRO GLN CYS ILE VAL CYS VAL ASN
SEQRES 9 A 113 TYR VAL VAL SER GLY ILE ILE GLN HIS
SEQRES 1 B 116 GLY SER VAL CYS GLN PRO THR ARG PHE ILE SER ARG HIS
SEQRES 2 B 116 ASN ILE GLU GLY ILE PHE THR PHE VAL ASP HIS ARG CYS
SEQRES 3 B 116 VAL ALA THR VAL GLY TYR GLN PRO GLN GLU LEU LEU GLY
SEQRES 4 B 116 LYS ASN ILE VAL GLU PHE CYS HIS PRO GLU ASP GLN GLN
SEQRES 5 B 116 LEU LEU ARG ASP SER PHE GLN GLN VAL VAL LYS LEU LYS
SEQRES 6 B 116 GLY GLN VAL LEU SER VAL MET PHE ARG PHE ARG SER LYS
SEQRES 7 B 116 ASN GLN GLU TRP LEU TRP MET ARG THR SER SER PHE THR
SEQRES 8 B 116 PHE GLN ASN PRO TYR SER ASP GLU ILE GLU TYR ILE ILE
SEQRES 9 B 116 CYS THR ASN THR ASN VAL LYS ASN SER SER GLN GLU
FORMUL 3 HOH *154(H2 O)
HELIX 1 1 GLU A 257 GLY A 264 1 8
HELIX 2 2 GLU A 266 LEU A 271 1 6
HELIX 3 3 SER A 274 TYR A 278 5 5
HELIX 4 4 ASP A 283 GLY A 298 1 16
HELIX 5 5 ARG B 379 GLY B 385 1 7
HELIX 6 6 GLN B 387 LEU B 391 5 5
HELIX 7 7 ASN B 395 CYS B 400 5 6
HELIX 8 8 ASP B 404 LEU B 418 1 15
SHEET 1 A 5 PHE A 252 CYS A 255 0
SHEET 2 A 5 THR A 241 HIS A 246 -1 N GLU A 245 O SER A 253
SHEET 3 A 5 PRO A 332 VAL A 341 -1 O CYS A 337 N SER A 244
SHEET 4 A 5 TYR A 314 TYR A 325 -1 N ILE A 324 O GLN A 333
SHEET 5 A 5 GLN A 299 THR A 301 -1 N VAL A 300 O ALA A 321
SHEET 1 B 5 PHE A 252 CYS A 255 0
SHEET 2 B 5 THR A 241 HIS A 246 -1 N GLU A 245 O SER A 253
SHEET 3 B 5 PRO A 332 VAL A 341 -1 O CYS A 337 N SER A 244
SHEET 4 B 5 TYR A 314 TYR A 325 -1 N ILE A 324 O GLN A 333
SHEET 5 B 5 TYR A 305 LEU A 308 -1 N TYR A 305 O VAL A 317
SHEET 1 C 5 PHE B 373 VAL B 376 0
SHEET 2 C 5 ARG B 362 HIS B 367 -1 N ARG B 366 O THR B 374
SHEET 3 C 5 TYR B 456 ASN B 463 -1 O CYS B 459 N SER B 365
SHEET 4 C 5 TRP B 436 PHE B 446 -1 N PHE B 444 O ILE B 458
SHEET 5 C 5 LEU B 423 ARG B 430 -1 N PHE B 427 O MET B 439
CRYST1 68.841 44.940 78.087 90.00 96.54 90.00 C 1 2 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 0.014526 0.000000 0.001665 0.00000
SCALE2 0.000000 0.022252 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012890 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
