HEADER TRANSFERASE 18-APR-07 2PL0
TITLE LCK BOUND TO IMATINIB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE LCK;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PROTEIN KINASE;
COMPND 5 SYNONYM: P56-LCK, LYMPHOCYTE CELL-SPECIFIC PROTEIN-TYROSINE KINASE,
COMPND 6 LSK, T CELL- SPECIFIC PROTEIN-TYROSINE KINASE;
COMPND 7 EC: 2.7.10.2;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: LCK;
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: PBEV1
KEYWDS KINASE PHOSPHORYLATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.D.JACOBS
REVDAT 5 21-FEB-24 2PL0 1 REMARK SEQADV HETSYN
REVDAT 4 24-FEB-09 2PL0 1 VERSN
REVDAT 3 26-FEB-08 2PL0 1 JRNL
REVDAT 2 20-NOV-07 2PL0 1 JRNL
REVDAT 1 09-OCT-07 2PL0 0
JRNL AUTH M.D.JACOBS,P.R.CARON,B.J.HARE
JRNL TITL CLASSIFYING PROTEIN KINASE STRUCTURES GUIDES USE OF
JRNL TITL 2 LIGAND-SELECTIVITY PROFILES TO PREDICT INACTIVE
JRNL TITL 3 CONFORMATIONS: STRUCTURE OF LCK/IMATINIB COMPLEX.
JRNL REF PROTEINS V. 70 1451 2007
JRNL REFN ISSN 0887-3585
JRNL PMID 17910071
JRNL DOI 10.1002/PROT.21633
REMARK 2
REMARK 2 RESOLUTION. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1044136.688
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 10474
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 534
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.011
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.2520
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.2500
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 534
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 10474
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1624
REMARK 3 BIN R VALUE (WORKING SET) : 0.3060
REMARK 3 BIN FREE R VALUE : 0.3270
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 68
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2182
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 93
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -18.32000
REMARK 3 B22 (A**2) : 17.39000
REMARK 3 B33 (A**2) : 0.93000
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) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.42
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) : 0.43
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.60
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.550
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) : 1.410 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.520 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.920 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.120 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 47.07
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : INHIB.PAR
REMARK 3 PARAMETER FILE 4 : PARMXRAY.XPL
REMARK 3 PARAMETER FILE 5 : &_1_PARAMETER_INFILE_5
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : INHIB.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2PL0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-APR-07.
REMARK 100 THE DEPOSITION ID IS D_1000042493.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10512
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 29.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.870
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.99
REMARK 200 R MERGE FOR SHELL (I) : 0.40900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULFATE, 100 MM HEPES
REMARK 280 PH 7.5, 1% PEG-3350, 10 MM DTT, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 37.60500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.58500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.60500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.58500
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 GLY A 221
REMARK 465 SER A 222
REMARK 465 HIS A 223
REMARK 465 MET A 224
REMARK 465 GLN A 225
REMARK 465 THR A 226
REMARK 465 GLN A 227
REMARK 465 LYS A 228
REMARK 465 PRO A 229
REMARK 465 GLN A 230
REMARK 465 THR A 499
REMARK 465 ALA A 500
REMARK 465 THR A 501
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 LYS A 231 CG CD CE NZ
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 256 12.07 -149.48
REMARK 500 HIS A 297 145.50 -179.84
REMARK 500 ASN A 359 43.12 70.88
REMARK 500 ARG A 363 -24.94 88.99
REMARK 500 ALA A 396 31.32 -145.94
REMARK 500 ASN A 464 -23.22 72.25
REMARK 500 PRO A 485 176.84 -58.46
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 STI A 200
DBREF 2PL0 A 225 509 UNP P06239 LCK_HUMAN 225 509
SEQADV 2PL0 GLY A 221 UNP P06239 EXPRESSION TAG
SEQADV 2PL0 SER A 222 UNP P06239 EXPRESSION TAG
SEQADV 2PL0 HIS A 223 UNP P06239 EXPRESSION TAG
SEQADV 2PL0 MET A 224 UNP P06239 EXPRESSION TAG
SEQRES 1 A 289 GLY SER HIS MET GLN THR GLN LYS PRO GLN LYS PRO TRP
SEQRES 2 A 289 TRP GLU ASP GLU TRP GLU VAL PRO ARG GLU THR LEU LYS
SEQRES 3 A 289 LEU VAL GLU ARG LEU GLY ALA GLY GLN PHE GLY GLU VAL
SEQRES 4 A 289 TRP MET GLY TYR TYR ASN GLY HIS THR LYS VAL ALA VAL
SEQRES 5 A 289 LYS SER LEU LYS GLN GLY SER MET SER PRO ASP ALA PHE
SEQRES 6 A 289 LEU ALA GLU ALA ASN LEU MET LYS GLN LEU GLN HIS GLN
SEQRES 7 A 289 ARG LEU VAL ARG LEU TYR ALA VAL VAL THR GLN GLU PRO
SEQRES 8 A 289 ILE TYR ILE ILE THR GLU TYR MET GLU ASN GLY SER LEU
SEQRES 9 A 289 VAL ASP PHE LEU LYS THR PRO SER GLY ILE LYS LEU THR
SEQRES 10 A 289 ILE ASN LYS LEU LEU ASP MET ALA ALA GLN ILE ALA GLU
SEQRES 11 A 289 GLY MET ALA PHE ILE GLU GLU ARG ASN TYR ILE HIS ARG
SEQRES 12 A 289 ASP LEU ARG ALA ALA ASN ILE LEU VAL SER ASP THR LEU
SEQRES 13 A 289 SER CYS LYS ILE ALA ASP PHE GLY LEU ALA ARG LEU ILE
SEQRES 14 A 289 GLU ASP ASN GLU TYR THR ALA ARG GLU GLY ALA LYS PHE
SEQRES 15 A 289 PRO ILE LYS TRP THR ALA PRO GLU ALA ILE ASN TYR GLY
SEQRES 16 A 289 THR PHE THR ILE LYS SER ASP VAL TRP SER PHE GLY ILE
SEQRES 17 A 289 LEU LEU THR GLU ILE VAL THR HIS GLY ARG ILE PRO TYR
SEQRES 18 A 289 PRO GLY MET THR ASN PRO GLU VAL ILE GLN ASN LEU GLU
SEQRES 19 A 289 ARG GLY TYR ARG MET VAL ARG PRO ASP ASN CYS PRO GLU
SEQRES 20 A 289 GLU LEU TYR GLN LEU MET ARG LEU CYS TRP LYS GLU ARG
SEQRES 21 A 289 PRO GLU ASP ARG PRO THR PHE ASP TYR LEU ARG SER VAL
SEQRES 22 A 289 LEU GLU ASP PHE PHE THR ALA THR GLU GLY GLN TYR GLN
SEQRES 23 A 289 PRO GLN PRO
HET STI A 200 37
HETNAM STI 4-(4-METHYL-PIPERAZIN-1-YLMETHYL)-N-[4-METHYL-3-(4-
HETNAM 2 STI PYRIDIN-3-YL-PYRIMIDIN-2-YLAMINO)-PHENYL]-BENZAMIDE
HETSYN STI STI-571; IMATINIB
FORMUL 2 STI C29 H31 N7 O
FORMUL 3 HOH *93(H2 O)
HELIX 1 1 PRO A 232 ASP A 236 5 5
HELIX 2 2 PRO A 241 GLU A 243 5 3
HELIX 3 3 SER A 281 LEU A 295 1 15
HELIX 4 4 SER A 323 THR A 330 1 8
HELIX 5 5 THR A 330 LYS A 335 1 6
HELIX 6 6 THR A 337 ARG A 358 1 22
HELIX 7 7 ARG A 366 ALA A 368 5 3
HELIX 8 8 LEU A 385 ILE A 389 5 5
HELIX 9 9 PRO A 403 THR A 407 5 5
HELIX 10 10 ALA A 408 GLY A 415 1 8
HELIX 11 11 THR A 418 VAL A 434 1 17
HELIX 12 12 THR A 445 ARG A 455 1 11
HELIX 13 13 PRO A 466 TRP A 477 1 12
HELIX 14 14 ARG A 480 ARG A 484 5 5
HELIX 15 15 THR A 486 ASP A 496 1 11
SHEET 1 A 5 LEU A 245 ARG A 250 0
SHEET 2 A 5 VAL A 259 TYR A 264 -1 O MET A 261 N VAL A 248
SHEET 3 A 5 THR A 268 SER A 274 -1 O VAL A 272 N TRP A 260
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 ALA A 305 O ILE A 315
SHEET 1 B 2 ILE A 370 VAL A 372 0
SHEET 2 B 2 CYS A 378 ILE A 380 -1 O LYS A 379 N LEU A 371
CISPEP 1 GLU A 310 PRO A 311 0 -9.40
SITE 1 AC1 16 HOH A 86 ALA A 271 LYS A 273 GLU A 288
SITE 2 AC1 16 LEU A 291 MET A 292 VAL A 301 ILE A 314
SITE 3 AC1 16 THR A 316 TYR A 318 MET A 319 ILE A 361
SITE 4 AC1 16 HIS A 362 ALA A 381 ASP A 382 PHE A 383
CRYST1 75.210 103.170 52.330 90.00 90.00 90.00 P 21 21 2 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 0.013296 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009693 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019109 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
