HEADER TRANSFERASE/TRANSFERASE INHIBITOR 14-OCT-15 5E8Y
TITLE TGF-BETA RECEPTOR TYPE 2 KINASE DOMAIN (E431A,R433A,E485A,K488A,R493A,
TITLE 2 R495A) IN COMPLEX WITH STAUROSPORINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TGF-BETA RECEPTOR TYPE-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN, UNP RESIDUES 237-549;
COMPND 5 SYNONYM: TGFR-2,TGF-BETA TYPE II RECEPTOR,TRANSFORMING GROWTH FACTOR-
COMPND 6 BETA RECEPTOR TYPE II,TBETAR-II;
COMPND 7 EC: 2.7.11.30;
COMPND 8 ENGINEERED: YES;
COMPND 9 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: TGFBR2;
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: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS KINASE DOMAIN, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SHERIFF
REVDAT 3 27-SEP-23 5E8Y 1 REMARK
REVDAT 2 18-APR-18 5E8Y 1 JRNL REMARK
REVDAT 1 11-MAY-16 5E8Y 0
JRNL AUTH A.J.TEBBEN,M.RUZANOV,M.GAO,D.XIE,S.E.KIEFER,C.YAN,
JRNL AUTH 2 J.A.NEWITT,L.ZHANG,K.KIM,H.LU,L.M.KOPCHO,S.SHERIFF
JRNL TITL CRYSTAL STRUCTURES OF APO AND INHIBITOR-BOUND TGF BETA R2
JRNL TITL 2 KINASE DOMAIN: INSIGHTS INTO TGF BETA R ISOFORM SELECTIVITY.
JRNL REF ACTA CRYSTALLOGR D STRUCT V. 72 658 2016
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 27139629
JRNL DOI 10.1107/S2059798316003624
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT 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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 23736
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 1159
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 : 12
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.14
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.62
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2750
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2023
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2616
REMARK 3 BIN R VALUE (WORKING SET) : 0.2011
REMARK 3 BIN FREE R VALUE : 0.2262
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.87
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 134
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 : 2261
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
REMARK 3 SOLVENT ATOMS : 89
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.79520
REMARK 3 B22 (A**2) : -12.19700
REMARK 3 B33 (A**2) : 4.40180
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) : 0.267
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.168
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.148
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.166
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 : 0.930
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2381 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3273 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 781 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 47 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 394 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2381 ; 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 : 316 ; 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 : 2736 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.08
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.51
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.64
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 5E8Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214552.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAR-15
REMARK 200 TEMPERATURE (KELVIN) : 100.0
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 : 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 : 23791
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 37.990
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.43400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
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 (%): 52.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, PH 8.5, 150 MM MGCL2,
REMARK 280 24%(W/V) PEG4000, 20%(V/V) GLCYEROL, 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 32.45000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.49000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.98500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.49000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.45000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.98500
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 234
REMARK 465 HIS A 235
REMARK 465 MET A 236
REMARK 465 HIS A 237
REMARK 465 ASN A 238
REMARK 465 THR A 239
REMARK 465 ASN A 266
REMARK 465 THR A 267
REMARK 465 SER A 268
REMARK 465 GLU A 269
REMARK 465 GLU A 542
REMARK 465 HIS A 543
REMARK 465 LEU A 544
REMARK 465 ASP A 545
REMARK 465 ARG A 546
REMARK 465 LEU A 547
REMARK 465 SER A 548
REMARK 465 GLY A 549
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 GLU A 240 CG CD OE1 OE2
REMARK 470 GLU A 245 CG CD OE1 OE2
REMARK 470 ARG A 254 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 264 CG CD CE NZ
REMARK 470 GLN A 265 CG CD OE1 NE2
REMARK 470 GLN A 270 CG CD OE1 NE2
REMARK 470 GLU A 272 CG CD OE1 OE2
REMARK 470 LYS A 300 CE NZ
REMARK 470 GLU A 316 CG CD OE1 OE2
REMARK 470 LEU A 317 CG CD1 CD2
REMARK 470 ARG A 348 CZ NH1 NH2
REMARK 470 ARG A 370 CG CD NE CZ NH1 NH2
REMARK 470 SER A 409 OG
REMARK 470 VAL A 410 CG1 CG2
REMARK 470 ASP A 411 CG OD1 OD2
REMARK 470 ASP A 412 CG OD1 OD2
REMARK 470 LEU A 413 CG CD1 CD2
REMARK 470 ASN A 415 CG OD1 ND2
REMARK 470 SER A 416 OG
REMARK 470 GLU A 437 CG CD OE1 OE2
REMARK 470 ASN A 438 CG OD1 ND2
REMARK 470 VAL A 439 CG1 CG2
REMARK 470 GLU A 440 CD OE1 OE2
REMARK 470 GLU A 466 CG CD OE1 OE2
REMARK 470 LYS A 468 CG CD CE NZ
REMARK 470 GLU A 471 CG CD OE1 OE2
REMARK 470 SER A 476 OG
REMARK 470 LYS A 477 CD CE NZ
REMARK 470 GLU A 480 CG CD OE1 OE2
REMARK 470 GLN A 508 CG CD OE1 NE2
REMARK 470 MET A 512 CG SD CE
REMARK 470 GLU A 540 CG CD OE1 OE2
REMARK 470 LEU A 541 CG CD1 CD2
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 ASP A 247 -61.96 -109.63
REMARK 500 LYS A 300 117.73 -35.68
REMARK 500 LEU A 308 -62.36 -100.00
REMARK 500 THR A 315 -168.91 -110.69
REMARK 500 ARG A 378 -7.12 75.99
REMARK 500 ASP A 379 50.21 -144.71
REMARK 500 CYS A 396 -29.88 -147.57
REMARK 500 GLU A 440 -21.58 121.01
REMARK 500 LEU A 492 -67.53 -90.02
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 STU A 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5E8S RELATED DB: PDB
REMARK 900 RELATED ID: 5E8T RELATED DB: PDB
REMARK 900 RELATED ID: 5E8U RELATED DB: PDB
REMARK 900 RELATED ID: 5E8V RELATED DB: PDB
REMARK 900 RELATED ID: 5E8W RELATED DB: PDB
REMARK 900 RELATED ID: 5E8X RELATED DB: PDB
REMARK 900 RELATED ID: 5E8Z RELATED DB: PDB
REMARK 900 RELATED ID: 5E90 RELATED DB: PDB
REMARK 900 RELATED ID: 5E91 RELATED DB: PDB
REMARK 900 RELATED ID: 5E92 RELATED DB: PDB
DBREF 5E8Y A 237 549 UNP P37173 TGFR2_HUMAN 237 549
SEQADV 5E8Y GLY A 234 UNP P37173 EXPRESSION TAG
SEQADV 5E8Y HIS A 235 UNP P37173 EXPRESSION TAG
SEQADV 5E8Y MET A 236 UNP P37173 EXPRESSION TAG
SEQADV 5E8Y ALA A 431 UNP P37173 GLU 431 ENGINEERED MUTATION
SEQADV 5E8Y ALA A 433 UNP P37173 ARG 433 ENGINEERED MUTATION
SEQADV 5E8Y ALA A 485 UNP P37173 GLU 485 ENGINEERED MUTATION
SEQADV 5E8Y ALA A 488 UNP P37173 LYS 488 ENGINEERED MUTATION
SEQADV 5E8Y ALA A 493 UNP P37173 ARG 493 ENGINEERED MUTATION
SEQADV 5E8Y ALA A 495 UNP P37173 ARG 495 ENGINEERED MUTATION
SEQRES 1 A 316 GLY HIS MET HIS ASN THR GLU LEU LEU PRO ILE GLU LEU
SEQRES 2 A 316 ASP THR LEU VAL GLY LYS GLY ARG PHE ALA GLU VAL TYR
SEQRES 3 A 316 LYS ALA LYS LEU LYS GLN ASN THR SER GLU GLN PHE GLU
SEQRES 4 A 316 THR VAL ALA VAL LYS ILE PHE PRO TYR GLU GLU TYR ALA
SEQRES 5 A 316 SER TRP LYS THR GLU LYS ASP ILE PHE SER ASP ILE ASN
SEQRES 6 A 316 LEU LYS HIS GLU ASN ILE LEU GLN PHE LEU THR ALA GLU
SEQRES 7 A 316 GLU ARG LYS THR GLU LEU GLY LYS GLN TYR TRP LEU ILE
SEQRES 8 A 316 THR ALA PHE HIS ALA LYS GLY ASN LEU GLN GLU TYR LEU
SEQRES 9 A 316 THR ARG HIS VAL ILE SER TRP GLU ASP LEU ARG LYS LEU
SEQRES 10 A 316 GLY SER SER LEU ALA ARG GLY ILE ALA HIS LEU HIS SER
SEQRES 11 A 316 ASP HIS THR PRO CYS GLY ARG PRO LYS MET PRO ILE VAL
SEQRES 12 A 316 HIS ARG ASP LEU LYS SER SER ASN ILE LEU VAL LYS ASN
SEQRES 13 A 316 ASP LEU THR CYS CYS LEU CYS ASP PHE GLY LEU SER LEU
SEQRES 14 A 316 ARG LEU ASP PRO THR LEU SER VAL ASP ASP LEU ALA ASN
SEQRES 15 A 316 SER GLY GLN VAL GLY THR ALA ARG TYR MET ALA PRO GLU
SEQRES 16 A 316 VAL LEU ALA SER ALA MET ASN LEU GLU ASN VAL GLU SER
SEQRES 17 A 316 PHE LYS GLN THR ASP VAL TYR SER MET ALA LEU VAL LEU
SEQRES 18 A 316 TRP GLU MET THR SER ARG CYS ASN ALA VAL GLY GLU VAL
SEQRES 19 A 316 LYS ASP TYR GLU PRO PRO PHE GLY SER LYS VAL ARG GLU
SEQRES 20 A 316 HIS PRO CYS VAL ALA SER MET ALA ASP ASN VAL LEU ALA
SEQRES 21 A 316 ASP ALA GLY ARG PRO GLU ILE PRO SER PHE TRP LEU ASN
SEQRES 22 A 316 HIS GLN GLY ILE GLN MET VAL CYS GLU THR LEU THR GLU
SEQRES 23 A 316 CYS TRP ASP HIS ASP PRO GLU ALA ARG LEU THR ALA GLN
SEQRES 24 A 316 CYS VAL ALA GLU ARG PHE SER GLU LEU GLU HIS LEU ASP
SEQRES 25 A 316 ARG LEU SER GLY
HET STU A 601 61
HETNAM STU STAUROSPORINE
FORMUL 2 STU C28 H26 N4 O3
FORMUL 3 HOH *89(H2 O)
HELIX 1 AA1 GLU A 283 ASP A 296 1 14
HELIX 2 AA2 ILE A 297 LYS A 300 5 4
HELIX 3 AA3 ASN A 332 HIS A 340 1 9
HELIX 4 AA4 SER A 343 SER A 363 1 21
HELIX 5 AA5 LYS A 381 SER A 383 5 3
HELIX 6 AA6 SER A 409 SER A 416 1 8
HELIX 7 AA7 THR A 421 MET A 425 5 5
HELIX 8 AA8 ALA A 426 ALA A 431 1 6
HELIX 9 AA9 GLU A 440 SER A 459 1 20
HELIX 10 AB1 ARG A 460 GLY A 465 5 6
HELIX 11 AB2 CYS A 483 LEU A 492 1 10
HELIX 12 AB3 PRO A 501 ASN A 506 5 6
HELIX 13 AB4 HIS A 507 TRP A 521 1 15
HELIX 14 AB5 ASP A 524 ARG A 528 5 5
HELIX 15 AB6 THR A 530 LEU A 541 1 12
SHEET 1 AA1 5 ILE A 244 LYS A 252 0
SHEET 2 AA1 5 GLU A 257 LEU A 263 -1 O VAL A 258 N VAL A 250
SHEET 3 AA1 5 GLU A 272 PRO A 280 -1 O GLU A 272 N LEU A 263
SHEET 4 AA1 5 LYS A 319 ALA A 326 -1 O TYR A 321 N PHE A 279
SHEET 5 AA1 5 PHE A 307 LYS A 314 -1 N ARG A 313 O GLN A 320
SHEET 1 AA2 2 ILE A 375 VAL A 376 0
SHEET 2 AA2 2 LEU A 402 ARG A 403 -1 O LEU A 402 N VAL A 376
SHEET 1 AA3 2 ILE A 385 VAL A 387 0
SHEET 2 AA3 2 CYS A 393 LEU A 395 -1 O CYS A 394 N LEU A 386
SITE 1 AC1 14 VAL A 250 GLY A 251 VAL A 258 ALA A 275
SITE 2 AC1 14 LYS A 277 ALA A 326 PHE A 327 HIS A 328
SITE 3 AC1 14 GLY A 331 ASN A 332 SER A 383 LEU A 386
SITE 4 AC1 14 CYS A 396 ASP A 397
CRYST1 64.900 75.970 74.980 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 0.015408 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013163 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013337 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
