HEADER TRANSFERASE 08-JUN-05 2BU6
TITLE CRYSTAL STRUCTURES OF HUMAN PYRUVATE DEHYDROGENASE KINASE 2 CONTAINING
TITLE 2 PHYSIOLOGICAL AND SYNTHETIC LIGANDS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRUVATE DEHYDROGENASE KINASE ISOENZYME 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PYRUVATE DEHYDROGENASE KINASE ISOFORM 2;
COMPND 5 EC: 2.7.1.99;
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 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS GHKL MOTIF REGULATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.R.KNOECHEL,A.D.TUCKER,C.M.ROBINSON,C.PHILLIPS,W.TAYLOR,P.J.BUNGAY,
AUTHOR 2 S.A.KASTEN,T.E.ROCHE,D.G.BROWN
REVDAT 4 03-APR-19 2BU6 1 REMARK
REVDAT 3 27-MAR-19 2BU6 1 SOURCE
REVDAT 2 24-FEB-09 2BU6 1 VERSN
REVDAT 1 02-FEB-06 2BU6 0
JRNL AUTH T.R.KNOECHEL,A.D.TUCKER,C.M.ROBINSON,C.PHILLIPS,W.TAYLOR,
JRNL AUTH 2 P.J.BUNGAY,S.A.KASTEN,T.E.ROCHE,D.G.BROWN
JRNL TITL REGULATORY ROLES OF THE N-TERMINAL DOMAIN BASED ON CRYSTAL
JRNL TITL 2 STRUCTURES OF HUMAN PYRUVATE DEHYDROGENASE KINASE 2
JRNL TITL 3 CONTAINING PHYSIOLOGICAL AND SYNTHETIC LIGANDS.
JRNL REF BIOCHEMISTRY V. 45 402 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16401071
JRNL DOI 10.1021/BI051402S
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
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 : 21614
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) : 0.247
REMARK 3 R VALUE (WORKING SET) : 0.247
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1054
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 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 : 2846
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 60
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.42300
REMARK 3 B22 (A**2) : -3.42300
REMARK 3 B33 (A**2) : 6.84500
REMARK 3 B12 (A**2) : -5.14800
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) : 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) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.309
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : BABINET
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 53.35
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 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2BU6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1290024424.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.80
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9326
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21614
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 3.820
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.4900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.24000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.380
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES PH5.8-6, 10% ISOPROPANOL,
REMARK 280 200MM CALCIUM ACETATE, 10MG/ML PROTEIN 4 DEGREES, PH 5.80,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 28.06733
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 56.13467
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 28.06733
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 56.13467
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: PQS
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 54.43650
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 94.28678
REMARK 350 BIOMT3 2 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 32
REMARK 465 SER A 33
REMARK 465 SER A 34
REMARK 465 ASN A 35
REMARK 465 GLY A 170
REMARK 465 SER A 171
REMARK 465 THR A 172
REMARK 465 ASN A 173
REMARK 465 PRO A 174
REMARK 465 ALA A 175
REMARK 465 HIS A 176
REMARK 465 PRO A 177
REMARK 465 THR A 305
REMARK 465 PRO A 306
REMARK 465 GLN A 307
REMARK 465 PRO A 308
REMARK 465 GLY A 309
REMARK 465 THR A 310
REMARK 465 GLY A 311
REMARK 465 GLY A 312
REMARK 465 THR A 313
REMARK 465 PRO A 314
REMARK 465 LEU A 315
REMARK 465 ALA A 316
REMARK 465 GLY A 317
REMARK 465 PHE A 318
REMARK 465 PRO A 386
REMARK 465 SER A 387
REMARK 465 THR A 388
REMARK 465 GLU A 389
REMARK 465 PRO A 390
REMARK 465 LYS A 391
REMARK 465 ASN A 392
REMARK 465 THR A 393
REMARK 465 SER A 394
REMARK 465 THR A 395
REMARK 465 TYR A 396
REMARK 465 ARG A 397
REMARK 465 VAL A 398
REMARK 465 SER A 399
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 378 CG CD OE1 NE2
REMARK 470 GLU A 379 CG CD OE1 OE2
REMARK 470 VAL A 385 CA C O CB CG1 CG2
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 HIS A 14 -71.25 -67.09
REMARK 500 CYS A 37 106.45 64.26
REMARK 500 PRO A 64 137.28 -36.73
REMARK 500 GLU A 89 -47.62 -29.97
REMARK 500 PRO A 95 -137.22 -65.51
REMARK 500 GLU A 96 -46.90 64.83
REMARK 500 HIS A 98 2.49 -53.99
REMARK 500 ALA A 210 143.06 -171.85
REMARK 500 SER A 224 -47.15 -17.83
REMARK 500 PHE A 344 -71.94 -135.81
REMARK 500 GLU A 379 97.67 -177.48
REMARK 500 ALA A 380 105.48 78.59
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 TF2 A1386
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BTZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF HUMAN PYRUVATE DEHYDROGENASE KINASE 2
REMARK 900 CONTAINING PHYSIOLOGICAL AND SYNTHETIC LIGANDS
REMARK 900 RELATED ID: 2BU2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF HUMAN PYRUVATE DEHYDROGENASE KINASE 2
REMARK 900 CONTAINING PHYSIOLOGICAL AND SYNTHETIC LIGANDS
REMARK 900 RELATED ID: 2BU5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF HUMAN PYRUVATE DEHYDROGENASE KINASE 2
REMARK 900 CONTAINING PHYSIOLOGICAL AND SYNTHETIC LIGANDS
REMARK 900 RELATED ID: 2BU7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF HUMAN PYRUVATE DEHYDROGENASE KINASE 2
REMARK 900 CONTAINING PHYSIOLOGICAL AND SYNTHETIC LIGANDS
REMARK 900 RELATED ID: 2BU8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF HUMAN PYRUVATE DEHYDROGENASE KINASE 2
REMARK 900 CONTAINING PHYSIOLOGICAL AND SYNTHETIC LIGANDS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 N -TERMINAL GS CLONING ARTEFACT
DBREF 2BU6 A 6 7 PDB 2BU6 2BU6 6 7
DBREF 2BU6 A 8 399 UNP Q15119 PDK2_HUMAN 16 407
SEQRES 1 A 394 GLY SER ALA PRO LYS TYR ILE GLU HIS PHE SER LYS PHE
SEQRES 2 A 394 SER PRO SER PRO LEU SER MET LYS GLN PHE LEU ASP PHE
SEQRES 3 A 394 GLY SER SER ASN ALA CYS GLU LYS THR SER PHE THR PHE
SEQRES 4 A 394 LEU ARG GLN GLU LEU PRO VAL ARG LEU ALA ASN ILE MET
SEQRES 5 A 394 LYS GLU ILE ASN LEU LEU PRO ASP ARG VAL LEU SER THR
SEQRES 6 A 394 PRO SER VAL GLN LEU VAL GLN SER TRP TYR VAL GLN SER
SEQRES 7 A 394 LEU LEU ASP ILE MET GLU PHE LEU ASP LYS ASP PRO GLU
SEQRES 8 A 394 ASP HIS ARG THR LEU SER GLN PHE THR ASP ALA LEU VAL
SEQRES 9 A 394 THR ILE ARG ASN ARG HIS ASN ASP VAL VAL PRO THR MET
SEQRES 10 A 394 ALA GLN GLY VAL LEU GLU TYR LYS ASP THR TYR GLY ASP
SEQRES 11 A 394 ASP PRO VAL SER ASN GLN ASN ILE GLN TYR PHE LEU ASP
SEQRES 12 A 394 ARG PHE TYR LEU SER ARG ILE SER ILE ARG MET LEU ILE
SEQRES 13 A 394 ASN GLN HIS THR LEU ILE PHE ASP GLY SER THR ASN PRO
SEQRES 14 A 394 ALA HIS PRO LYS HIS ILE GLY SER ILE ASP PRO ASN CYS
SEQRES 15 A 394 ASN VAL SER GLU VAL VAL LYS ASP ALA TYR ASP MET ALA
SEQRES 16 A 394 LYS LEU LEU CYS ASP LYS TYR TYR MET ALA SER PRO ASP
SEQRES 17 A 394 LEU GLU ILE GLN GLU ILE ASN ALA ALA ASN SER LYS GLN
SEQRES 18 A 394 PRO ILE HIS MET VAL TYR VAL PRO SER HIS LEU TYR HIS
SEQRES 19 A 394 MET LEU PHE GLU LEU PHE LYS ASN ALA MET ARG ALA THR
SEQRES 20 A 394 VAL GLU SER HIS GLU SER SER LEU ILE LEU PRO PRO ILE
SEQRES 21 A 394 LYS VAL MET VAL ALA LEU GLY GLU GLU ASP LEU SER ILE
SEQRES 22 A 394 LYS MET SER ASP ARG GLY GLY GLY VAL PRO LEU ARG LYS
SEQRES 23 A 394 ILE GLU ARG LEU PHE SER TYR MET TYR SER THR ALA PRO
SEQRES 24 A 394 THR PRO GLN PRO GLY THR GLY GLY THR PRO LEU ALA GLY
SEQRES 25 A 394 PHE GLY TYR GLY LEU PRO ILE SER ARG LEU TYR ALA LYS
SEQRES 26 A 394 TYR PHE GLN GLY ASP LEU GLN LEU PHE SER MET GLU GLY
SEQRES 27 A 394 PHE GLY THR ASP ALA VAL ILE TYR LEU LYS ALA LEU SER
SEQRES 28 A 394 THR ASP SER VAL GLU ARG LEU PRO VAL TYR ASN LYS SER
SEQRES 29 A 394 ALA TRP ARG HIS TYR GLN THR ILE GLN GLU ALA GLY ASP
SEQRES 30 A 394 TRP CYS VAL PRO SER THR GLU PRO LYS ASN THR SER THR
SEQRES 31 A 394 TYR ARG VAL SER
HET TF2 A1386 29
HETNAM TF2 (N-{4-[(ETHYLANILINO)SULFONYL]-2-METHYLPHENYL}-3,3,3-
HETNAM 2 TF2 TRIFLUORO-2-HYDROXY-2-METHYLPROPANAMIDE
FORMUL 2 TF2 C19 H21 F3 N2 O4 S
FORMUL 3 HOH *60(H2 O)
HELIX 1 1 SER A 7 SER A 16 1 10
HELIX 2 2 SER A 24 ASP A 30 1 7
HELIX 3 3 CYS A 37 ASN A 61 1 25
HELIX 4 4 PRO A 64 SER A 69 1 6
HELIX 5 5 THR A 70 GLU A 89 1 20
HELIX 6 6 PHE A 90 ASP A 92 5 3
HELIX 7 7 LEU A 101 HIS A 115 1 15
HELIX 8 8 ASP A 117 GLY A 134 1 18
HELIX 9 9 ASP A 136 PHE A 168 1 33
HELIX 10 10 VAL A 189 MET A 209 1 21
HELIX 11 11 VAL A 233 HIS A 256 1 24
HELIX 12 12 PRO A 288 PHE A 296 1 9
HELIX 13 13 TYR A 320 PHE A 332 1 13
HELIX 14 14 ASN A 367 ARG A 372 1 6
HELIX 15 15 HIS A 373 GLN A 375 5 3
SHEET 1 AA 2 ASP A 184 ASN A 188 0
SHEET 2 AA 2 HIS A 229 TYR A 232 -1 O MET A 230 N CYS A 187
SHEET 1 AB 5 LEU A 214 ASN A 220 0
SHEET 2 AB 5 ILE A 265 LEU A 271 1 O ILE A 265 N GLU A 215
SHEET 3 AB 5 ASP A 275 GLY A 285 -1 O SER A 277 N ALA A 270
SHEET 4 AB 5 PHE A 344 LYS A 353 -1 O PHE A 344 N GLY A 285
SHEET 5 AB 5 ASP A 335 MET A 341 -1 O ASP A 335 N TYR A 351
CISPEP 1 ALA A 303 PRO A 304 0 -0.72
SITE 1 AC1 10 LEU A 23 GLN A 27 PHE A 28 PHE A 31
SITE 2 AC1 10 SER A 41 PHE A 44 LEU A 45 LEU A 160
SITE 3 AC1 10 GLN A 163 HOH A2013
CRYST1 108.873 108.873 84.202 90.00 90.00 120.00 P 64 6
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 0.009185 0.005303 0.000000 0.00000
SCALE2 0.000000 0.010606 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011876 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
