HEADER TRANSFERASE 25-MAY-99 1QPJ
TITLE CRYSTAL STRUCTURE OF THE LYMPHOCYTE-SPECIFIC KINASE LCK IN COMPLEX
TITLE 2 WITH STAUROSPORINE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LCK TYROSINE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 EC: 2.7.1.112;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL: LYMPHOCYTE;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS ALPHA BETA FOLD, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.ZHU,J.L.KIM,P.E.ROSE,D.R.STOVER,L.M.TOLEDO
REVDAT 6 15-NOV-23 1QPJ 1 REMARK SEQADV LINK ATOM
REVDAT 5 02-MAR-10 1QPJ 1 REMARK HETATM
REVDAT 4 24-FEB-09 1QPJ 1 VERSN
REVDAT 3 01-APR-03 1QPJ 1 JRNL
REVDAT 2 26-SEP-01 1QPJ 3 ATOM CONECT
REVDAT 1 31-MAY-00 1QPJ 0
JRNL AUTH X.ZHU,J.L.KIM,J.R.NEWCOMB,P.E.ROSE,D.R.STOVER,L.M.TOLEDO,
JRNL AUTH 2 H.ZHAO,K.A.MORGENSTERN
JRNL TITL STRUCTURAL ANALYSIS OF THE LYMPHOCYTE-SPECIFIC KINASE LCK IN
JRNL TITL 2 COMPLEX WITH NON-SELECTIVE AND SRC FAMILY SELECTIVE KINASE
JRNL TITL 3 INHIBITORS.
JRNL REF STRUCTURE FOLD.DES. V. 7 651 1999
JRNL REFN ISSN 0969-2126
JRNL PMID 10404594
JRNL DOI 10.1016/S0969-2126(99)80086-0
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 98.0
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 14310
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 712
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 2138
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.017
REMARK 3 BOND ANGLES (DEGREES) : 2.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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 NCS MODEL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QPJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAY-99.
REMARK 100 THE DEPOSITION ID IS D_1000009116.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-FEB-99
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) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16145
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.20200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5 0.25 M LI2SO4 20%
REMARK 280 POLYETHYLENE GLYCOL 6000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 30.77000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.86500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.52000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.86500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.77000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.52000
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 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 LYS A 231
REMARK 465 PRO A 232
REMARK 465 TRP A 233
REMARK 465 TRP A 234
REMARK 465 GLU A 235
REMARK 465 GLU A 502
REMARK 465 GLY A 503
REMARK 465 GLN A 504
REMARK 465 TYR A 505
REMARK 465 GLN A 506
REMARK 465 PRO A 507
REMARK 465 GLN A 508
REMARK 465 PRO A 509
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 A 277 CG CD OE1 NE2
REMARK 470 GLN A 309 CG CD OE1 NE2
REMARK 470 ARG A 397 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 401 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP A 483 CA ASP A 483 CB 0.147
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASN A 392 N - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500 PRO A 403 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 ASP A 422 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
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 ARG A 363 -4.26 71.81
REMARK 500 ASP A 382 82.59 60.31
REMARK 500 ASN A 392 -19.04 -22.38
REMARK 500 PRO A 403 95.29 -60.20
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 SO4 A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE STU A 902
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QPC RELATED DB: PDB
REMARK 900 RELATED ID: 1QPD RELATED DB: PDB
REMARK 900 RELATED ID: 1QPE RELATED DB: PDB
DBREF 1QPJ A 231 509 UNP P06239 LCK_HUMAN 230 508
SEQADV 1QPJ PTR A 394 UNP P06239 TYR 393 MODIFIED RESIDUE
SEQRES 1 A 279 LYS PRO TRP TRP GLU ASP GLU TRP GLU VAL PRO ARG GLU
SEQRES 2 A 279 THR LEU LYS LEU VAL GLU ARG LEU GLY ALA GLY GLN PHE
SEQRES 3 A 279 GLY GLU VAL TRP MET GLY TYR TYR ASN GLY HIS THR LYS
SEQRES 4 A 279 VAL ALA VAL LYS SER LEU LYS GLN GLY SER MET SER PRO
SEQRES 5 A 279 ASP ALA PHE LEU ALA GLU ALA ASN LEU MET LYS GLN LEU
SEQRES 6 A 279 GLN HIS GLN ARG LEU VAL ARG LEU TYR ALA VAL VAL THR
SEQRES 7 A 279 GLN GLU PRO ILE TYR ILE ILE THR GLU TYR MET GLU ASN
SEQRES 8 A 279 GLY SER LEU VAL ASP PHE LEU LYS THR PRO SER GLY ILE
SEQRES 9 A 279 LYS LEU THR ILE ASN LYS LEU LEU ASP MET ALA ALA GLN
SEQRES 10 A 279 ILE ALA GLU GLY MET ALA PHE ILE GLU GLU ARG ASN TYR
SEQRES 11 A 279 ILE HIS ARG ASP LEU ARG ALA ALA ASN ILE LEU VAL SER
SEQRES 12 A 279 ASP THR LEU SER CYS LYS ILE ALA ASP PHE GLY LEU ALA
SEQRES 13 A 279 ARG LEU ILE GLU ASP ASN GLU PTR THR ALA ARG GLU GLY
SEQRES 14 A 279 ALA LYS PHE PRO ILE LYS TRP THR ALA PRO GLU ALA ILE
SEQRES 15 A 279 ASN TYR GLY THR PHE THR ILE LYS SER ASP VAL TRP SER
SEQRES 16 A 279 PHE GLY ILE LEU LEU THR GLU ILE VAL THR HIS GLY ARG
SEQRES 17 A 279 ILE PRO TYR PRO GLY MET THR ASN PRO GLU VAL ILE GLN
SEQRES 18 A 279 ASN LEU GLU ARG GLY TYR ARG MET VAL ARG PRO ASP ASN
SEQRES 19 A 279 CYS PRO GLU GLU LEU TYR GLN LEU MET ARG LEU CYS TRP
SEQRES 20 A 279 LYS GLU ARG PRO GLU ASP ARG PRO THR PHE ASP TYR LEU
SEQRES 21 A 279 ARG SER VAL LEU GLU ASP PHE PHE THR ALA THR GLU GLY
SEQRES 22 A 279 GLN TYR GLN PRO GLN PRO
MODRES 1QPJ PTR A 394 TYR O-PHOSPHOTYROSINE
HET PTR A 394 17
HET SO4 A 901 5
HET STU A 902 37
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM SO4 SULFATE ION
HETNAM STU STAUROSPORINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 PTR C9 H12 N O6 P
FORMUL 2 SO4 O4 S 2-
FORMUL 3 STU C28 H26 N4 O3
FORMUL 4 HOH *110(H2 O)
HELIX 1 1 PRO A 241 GLU A 243 5 3
HELIX 2 2 SER A 281 LEU A 295 1 15
HELIX 3 3 SER A 323 LEU A 328 1 6
HELIX 4 4 THR A 330 LYS A 335 1 6
HELIX 5 5 THR A 337 ARG A 358 1 22
HELIX 6 6 ARG A 366 ALA A 368 5 3
HELIX 7 7 ALA A 408 GLY A 415 1 8
HELIX 8 8 THR A 418 THR A 435 1 18
HELIX 9 9 THR A 445 ARG A 455 1 11
HELIX 10 10 PRO A 466 CYS A 476 1 11
HELIX 11 11 ARG A 480 ARG A 484 5 5
HELIX 12 12 THR A 486 THR A 501 1 16
SHEET 1 A 5 LEU A 245 GLY A 254 0
SHEET 2 A 5 GLY A 257 TYR A 264 -1 O GLY A 257 N GLY A 254
SHEET 3 A 5 THR A 268 SER A 274 -1 O THR A 268 N TYR A 264
SHEET 4 A 5 TYR A 313 GLU A 317 -1 O ILE A 314 N LYS A 273
SHEET 5 A 5 LEU A 303 VAL A 307 -1 N TYR A 304 O ILE A 315
SHEET 1 B 2 TYR A 360 ILE A 361 0
SHEET 2 B 2 ARG A 387 LEU A 388 -1 O ARG A 387 N ILE A 361
SHEET 1 C 2 ILE A 370 VAL A 372 0
SHEET 2 C 2 CYS A 378 ILE A 380 -1 O LYS A 379 N LEU A 371
LINK C GLU A 393 N PTR A 394 1555 1555 1.32
LINK C PTR A 394 N THR A 395 1555 1555 1.33
CISPEP 1 GLU A 310 PRO A 311 0 -0.67
SITE 1 AC1 9 HOH A 24 HOH A 35 GLN A 298 ARG A 299
SITE 2 AC1 9 SER A 377 LYS A 379 TYR A 457 ARG A 458
SITE 3 AC1 9 ARG A 474
SITE 1 AC2 13 LEU A 251 GLY A 252 ALA A 271 LYS A 273
SITE 2 AC2 13 THR A 316 GLU A 317 TYR A 318 MET A 319
SITE 3 AC2 13 GLY A 322 SER A 323 ALA A 368 LEU A 371
SITE 4 AC2 13 ASP A 382
CRYST1 61.540 69.040 73.730 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 0.016250 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014484 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013563 0.00000
(ATOM LINES ARE NOT SHOWN.)
END