HEADER TRANSFERASE/TRANSFERASE INHIBITOR 05-AUG-18 5QIL
TITLE TGF-BETA RECEPTOR TYPE 1 KINASE DOMAIN (T204D) IN COMPLEX WITH N-{4-
TITLE 2 [3-(6-METHOXYPYRIDIN-3-YL)-1H-PYRROLO[3,2-B]PYRIDIN-2-YL]PYRIDIN-2-
TITLE 3 YL}ACETAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TGF-BETA RECEPTOR TYPE-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN, UNP RESIDUES 200-503;
COMPND 5 SYNONYM: TGFR-1,ACTIVIN A RECEPTOR TYPE II-LIKE PROTEIN KINASE OF
COMPND 6 53KD,ACTIVIN RECEPTOR-LIKE KINASE 5,ALK5,SERINE/THREONINE-PROTEIN
COMPND 7 KINASE RECEPTOR R4,SKR4,TGF-BETA TYPE I RECEPTOR,TRANSFORMING GROWTH
COMPND 8 FACTOR-BETA RECEPTOR TYPE I,TBETAR-I;
COMPND 9 EC: 2.7.11.30;
COMPND 10 ENGINEERED: YES;
COMPND 11 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: TGFBR1, ALK5, SKR4;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS ALK5, SB431542, KINASE DOMAIN, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS 2 COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SHERIFF
REVDAT 4 06-MAR-24 5QIL 1 REMARK
REVDAT 3 12-MAY-21 5QIL 1 REMARK
REVDAT 2 26-DEC-18 5QIL 1 JRNL
REVDAT 1 31-OCT-18 5QIL 0
JRNL AUTH Y.ZHANG,Y.ZHAO,A.J.TEBBEN,S.SHERIFF,M.RUZANOV,M.P.FERESHTEH,
JRNL AUTH 2 Y.FAN,J.LIPPY,J.SWANSON,C.P.HO,B.S.WAUTLET,A.ROSE,K.PARRISH,
JRNL AUTH 3 Z.YANG,A.F.DONNELL,L.ZHANG,B.E.FINK,G.D.VITE,
JRNL AUTH 4 K.AUGUSTINE-RAUCH,J.FARGNOLI,R.M.BORZILLERI
JRNL TITL DISCOVERY OF 4-AZAINDOLE INHIBITORS OF TGF BETA RI AS
JRNL TITL 2 IMMUNO-ONCOLOGY AGENTS.
JRNL REF ACS MED CHEM LETT V. 9 1117 2018
JRNL REFN ISSN 1948-5875
JRNL PMID 30429955
JRNL DOI 10.1021/ACSMEDCHEMLETT.8B00357
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.6
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 20531
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) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.810
REMARK 3 FREE R VALUE TEST SET COUNT : 987
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.09
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2934
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1807
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2794
REMARK 3 BIN R VALUE (WORKING SET) : 0.1773
REMARK 3 BIN FREE R VALUE : 0.2470
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.77
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 140
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 : 2408
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 156
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.27
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.86620
REMARK 3 B22 (A**2) : -13.53260
REMARK 3 B33 (A**2) : 8.66640
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) : 0.188
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.179
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.150
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.170
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.147
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 : 0.925
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2514 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3409 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 891 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 55 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 408 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2514 ; 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 : 320 ; 5.000 ; SEMIHARMONIC
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 : 3072 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.01
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.57
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.61
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5QIL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-18.
REMARK 100 THE DEPOSITION ID IS D_1001401994.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-FEB-15
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.6
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20725
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 41.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.36500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.500
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: 3TZM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23%(W/V) PEG3350, 3%(V/V) GLCYEROL, PH
REMARK 280 5.6, VAPOR DIFFUSION, HANGING 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 20.80000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.54000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.49000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.54000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.80000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.49000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 500
REMARK 465 ILE A 501
REMARK 465 LYS A 502
REMARK 465 MET A 503
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 HIS A 198 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 213 CD CE NZ
REMARK 470 HIS A 371 CG ND1 CD2 CE1 NE2
REMARK 470 ASN A 456 CG OD1 ND2
REMARK 470 GLN A 497 CG CD OE1 NE2
REMARK 470 GLN A 498 CG CD OE1 NE2
REMARK 470 GLU A 499 CG CD OE1 OE2
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 PHE A 216 -51.16 -124.67
REMARK 500 GLN A 324 71.12 -105.07
REMARK 500 ARG A 332 -4.23 75.30
REMARK 500 ASP A 333 38.32 -148.89
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 J2V A 601
DBREF 5QIL A 200 503 UNP P36897 TGFR1_HUMAN 200 503
SEQADV 5QIL GLY A 197 UNP P36897 EXPRESSION TAG
SEQADV 5QIL HIS A 198 UNP P36897 EXPRESSION TAG
SEQADV 5QIL MET A 199 UNP P36897 EXPRESSION TAG
SEQADV 5QIL ASP A 204 UNP P36897 THR 204 ENGINEERED MUTATION
SEQRES 1 A 307 GLY HIS MET THR ILE ALA ARG ASP ILE VAL LEU GLN GLU
SEQRES 2 A 307 SER ILE GLY LYS GLY ARG PHE GLY GLU VAL TRP ARG GLY
SEQRES 3 A 307 LYS TRP ARG GLY GLU GLU VAL ALA VAL LYS ILE PHE SER
SEQRES 4 A 307 SER ARG GLU GLU ARG SER TRP PHE ARG GLU ALA GLU ILE
SEQRES 5 A 307 TYR GLN THR VAL MET LEU ARG HIS GLU ASN ILE LEU GLY
SEQRES 6 A 307 PHE ILE ALA ALA ASP ASN LYS ASP ASN GLY THR TRP THR
SEQRES 7 A 307 GLN LEU TRP LEU VAL SER ASP TYR HIS GLU HIS GLY SER
SEQRES 8 A 307 LEU PHE ASP TYR LEU ASN ARG TYR THR VAL THR VAL GLU
SEQRES 9 A 307 GLY MET ILE LYS LEU ALA LEU SER THR ALA SER GLY LEU
SEQRES 10 A 307 ALA HIS LEU HIS MET GLU ILE VAL GLY THR GLN GLY LYS
SEQRES 11 A 307 PRO ALA ILE ALA HIS ARG ASP LEU LYS SER LYS ASN ILE
SEQRES 12 A 307 LEU VAL LYS LYS ASN GLY THR CYS CYS ILE ALA ASP LEU
SEQRES 13 A 307 GLY LEU ALA VAL ARG HIS ASP SER ALA THR ASP THR ILE
SEQRES 14 A 307 ASP ILE ALA PRO ASN HIS ARG VAL GLY THR LYS ARG TYR
SEQRES 15 A 307 MET ALA PRO GLU VAL LEU ASP ASP SER ILE ASN MET LYS
SEQRES 16 A 307 HIS PHE GLU SER PHE LYS ARG ALA ASP ILE TYR ALA MET
SEQRES 17 A 307 GLY LEU VAL PHE TRP GLU ILE ALA ARG ARG CYS SER ILE
SEQRES 18 A 307 GLY GLY ILE HIS GLU ASP TYR GLN LEU PRO TYR TYR ASP
SEQRES 19 A 307 LEU VAL PRO SER ASP PRO SER VAL GLU GLU MET ARG LYS
SEQRES 20 A 307 VAL VAL CYS GLU GLN LYS LEU ARG PRO ASN ILE PRO ASN
SEQRES 21 A 307 ARG TRP GLN SER CYS GLU ALA LEU ARG VAL MET ALA LYS
SEQRES 22 A 307 ILE MET ARG GLU CYS TRP TYR ALA ASN GLY ALA ALA ARG
SEQRES 23 A 307 LEU THR ALA LEU ARG ILE LYS LYS THR LEU SER GLN LEU
SEQRES 24 A 307 SER GLN GLN GLU GLY ILE LYS MET
HET J2V A 601 44
HETNAM J2V N-{4-[3-(6-METHOXYPYRIDIN-3-YL)-1H-PYRROLO[3,2-
HETNAM 2 J2V B]PYRIDIN-2-YL]PYRIDIN-2-YL}ACETAMIDE
FORMUL 2 J2V C20 H17 N5 O2
FORMUL 3 HOH *156(H2 O)
HELIX 1 AA1 ILE A 201 ARG A 203 5 3
HELIX 2 AA2 GLU A 238 GLN A 250 1 13
HELIX 3 AA3 SER A 287 TYR A 295 1 9
HELIX 4 AA4 THR A 298 MET A 318 1 21
HELIX 5 AA5 THR A 375 MET A 379 5 5
HELIX 6 AA6 ALA A 380 ASP A 385 1 6
HELIX 7 AA7 PHE A 393 ARG A 414 1 22
HELIX 8 AA8 SER A 437 CYS A 446 1 10
HELIX 9 AA9 PRO A 455 SER A 460 5 6
HELIX 10 AB1 CYS A 461 TRP A 475 1 15
HELIX 11 AB2 ASN A 478 ARG A 482 5 5
HELIX 12 AB3 THR A 484 GLU A 499 1 16
SHEET 1 AA1 5 ILE A 205 LYS A 213 0
SHEET 2 AA1 5 GLU A 218 TRP A 224 -1 O ARG A 221 N GLN A 208
SHEET 3 AA1 5 GLU A 227 SER A 235 -1 O GLU A 227 N TRP A 224
SHEET 4 AA1 5 THR A 274 ASP A 281 -1 O LEU A 278 N LYS A 232
SHEET 5 AA1 5 PHE A 262 ASP A 269 -1 N ILE A 263 O VAL A 279
SHEET 1 AA2 3 ALA A 328 ALA A 330 0
SHEET 2 AA2 3 VAL A 356 ASP A 359 -1 O HIS A 358 N ALA A 328
SHEET 3 AA2 3 THR A 364 ILE A 365 -1 O THR A 364 N ASP A 359
SHEET 1 AA3 2 ILE A 339 VAL A 341 0
SHEET 2 AA3 2 CYS A 347 ILE A 349 -1 O CYS A 348 N LEU A 340
SITE 1 AC1 16 ILE A 211 VAL A 219 ALA A 230 LYS A 232
SITE 2 AC1 16 LEU A 260 SER A 280 ASP A 281 TYR A 282
SITE 3 AC1 16 HIS A 283 GLU A 284 GLY A 286 THR A 323
SITE 4 AC1 16 LEU A 340 ASP A 351 HOH A 704 HOH A 714
CRYST1 41.600 76.980 89.080 90.00 90.00 90.00 P 21 21 21 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 0.024038 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012990 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011226 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
