HEADER TRANSFERASE/TRANSFERASE INHIBITOR 21-SEP-12 4H85
TITLE CRYSTAL STRUCTURE OF BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE
TITLE 2 KINASE/(R)-ALPHA-CHLOROISOCAPROATE COMPLEX WITH ADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: [3-METHYL-2-OXOBUTANOATE DEHYDROGENASE [LIPOAMIDE]] KINASE,
COMPND 3 MITOCHONDRIAL;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE KINASE, BCKD-
COMPND 6 KINASE, BCKDHKIN;
COMPND 7 EC: 2.7.11.4;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: BCKDK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21GROESL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTRCKHISB
KEYWDS GHKL PROTEIN KINASE, ALLOSTERIC KINASE INHIBITOR, BRANCHED-CHAIN
KEYWDS 2 ALPHA-KETOACID, BRANCHED-CHAIN AMINO ACIDS, MAPLE SYRUP URINE
KEYWDS 3 DISEASE, DIABETES AND OBESITY, BERGERAT NUCLEOTIDE-BINDING FOLD,
KEYWDS 4 PROTEIN KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.C.TSO,J.L.CHUANG,W.J.GUI,R.M.WYNN,J.LI,D.T.CHUANG
REVDAT 3 28-FEB-24 4H85 1 REMARK SEQADV LINK
REVDAT 2 18-SEP-19 4H85 1 JRNL
REVDAT 1 05-JUN-13 4H85 0
JRNL AUTH S.C.TSO,X.QI,W.J.GUI,J.L.CHUANG,L.K.MORLOCK,A.L.WALLACE,
JRNL AUTH 2 K.AHMED,S.LAXMAN,P.M.CAMPEAU,B.H.LEE,S.M.HUTSON,B.P.TU,
JRNL AUTH 3 N.S.WILLIAMS,U.K.TAMBAR,R.M.WYNN,D.T.CHUANG
JRNL TITL STRUCTURE-BASED DESIGN AND MECHANISMS OF ALLOSTERIC
JRNL TITL 2 INHIBITORS FOR MITOCHONDRIAL BRANCHED-CHAIN ALPHA-KETOACID
JRNL TITL 3 DEHYDROGENASE KINASE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 110 9728 2013
JRNL REFN ESSN 1091-6490
JRNL PMID 23716694
JRNL DOI 10.1073/PNAS.1303220110
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 36359
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.500
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 40.3641 - 5.0433 0.98 2614 153 0.2194 0.2534
REMARK 3 2 5.0433 - 4.0042 1.00 2522 146 0.1725 0.1918
REMARK 3 3 4.0042 - 3.4984 1.00 2492 146 0.1983 0.2176
REMARK 3 4 3.4984 - 3.1786 1.00 2483 144 0.2022 0.2317
REMARK 3 5 3.1786 - 2.9509 1.00 2436 142 0.2102 0.2436
REMARK 3 6 2.9509 - 2.7770 1.00 2454 143 0.2114 0.2472
REMARK 3 7 2.7770 - 2.6379 1.00 2449 142 0.1981 0.2197
REMARK 3 8 2.6379 - 2.5231 1.00 2465 144 0.1951 0.2416
REMARK 3 9 2.5231 - 2.4260 1.00 2439 142 0.1862 0.2370
REMARK 3 10 2.4260 - 2.3423 1.00 2419 140 0.1845 0.1935
REMARK 3 11 2.3423 - 2.2690 1.00 2406 140 0.1886 0.2162
REMARK 3 12 2.2690 - 2.2042 1.00 2424 142 0.2038 0.2395
REMARK 3 13 2.2042 - 2.1462 1.00 2435 141 0.2065 0.2506
REMARK 3 14 2.1462 - 2.0938 0.96 2321 135 0.2252 0.2849
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.06
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 43.79
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.520
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.030
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) : -1.52140
REMARK 3 B22 (A**2) : -1.52140
REMARK 3 B33 (A**2) : 3.04280
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 2560
REMARK 3 ANGLE : 1.098 3467
REMARK 3 CHIRALITY : 0.071 382
REMARK 3 PLANARITY : 0.005 442
REMARK 3 DIHEDRAL : 14.550 973
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 3.1297 -30.4763 9.4080
REMARK 3 T TENSOR
REMARK 3 T11: 0.2279 T22: 0.2357
REMARK 3 T33: 0.2609 T12: 0.0045
REMARK 3 T13: 0.0032 T23: 0.0533
REMARK 3 L TENSOR
REMARK 3 L11: 3.5498 L22: 1.4019
REMARK 3 L33: 0.8816 L12: 0.5663
REMARK 3 L13: -0.9945 L23: -0.3697
REMARK 3 S TENSOR
REMARK 3 S11: -0.0731 S12: -0.3743 S13: -0.2670
REMARK 3 S21: 0.0040 S22: -0.0102 S23: 0.1940
REMARK 3 S31: 0.0741 S32: -0.0002 S33: 0.0715
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4H85 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-SEP-12.
REMARK 100 THE DEPOSITION ID IS D_1000075139.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUN-12
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 : APS
REMARK 200 BEAMLINE : 19-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 : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36412
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 9.500
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : 0.05300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.70
REMARK 200 R MERGE FOR SHELL (I) : 0.71000
REMARK 200 R SYM FOR SHELL (I) : 0.64600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.7.1_743
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG8000, 0.1 M TRIS. 1.2 M NACL,
REMARK 280 125MM KCL, 150MM ARG-HCL,20MM MGCL2, 5% GLYCEROL, PH 7.5, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 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 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 63.80950
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 63.80950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.99350
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 63.80950
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 63.80950
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 36.99350
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 63.80950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.80950
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 36.99350
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 63.80950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.80950
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 36.99350
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 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: DIMERIC
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 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
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 MET A -29
REMARK 465 ILE A -28
REMARK 465 LEU A -27
REMARK 465 THR A -26
REMARK 465 SER A -25
REMARK 465 VAL A -24
REMARK 465 LEU A -23
REMARK 465 GLY A -22
REMARK 465 SER A -21
REMARK 465 GLY A -20
REMARK 465 PRO A -19
REMARK 465 ARG A -18
REMARK 465 SER A -17
REMARK 465 GLY A -16
REMARK 465 SER A -15
REMARK 465 SER A -14
REMARK 465 LEU A -13
REMARK 465 TRP A -12
REMARK 465 PRO A -11
REMARK 465 LEU A -10
REMARK 465 LEU A -9
REMARK 465 GLY A -8
REMARK 465 SER A -7
REMARK 465 SER A -6
REMARK 465 LEU A -5
REMARK 465 SER A -4
REMARK 465 LEU A -3
REMARK 465 ARG A -2
REMARK 465 VAL A -1
REMARK 465 ARG A 0
REMARK 465 SER A 1
REMARK 465 THR A 2
REMARK 465 SER A 3
REMARK 465 ALA A 4
REMARK 465 THR A 5
REMARK 465 ASP A 6
REMARK 465 THR A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 VAL A 10
REMARK 465 GLU A 11
REMARK 465 LEU A 12
REMARK 465 ALA A 13
REMARK 465 ARG A 14
REMARK 465 GLU A 15
REMARK 465 ARG A 16
REMARK 465 SER A 17
REMARK 465 LYS A 18
REMARK 465 THR A 19
REMARK 465 VAL A 20
REMARK 465 THR A 21
REMARK 465 SER A 22
REMARK 465 PHE A 23
REMARK 465 TYR A 24
REMARK 465 ASN A 25
REMARK 465 GLN A 26
REMARK 465 SER A 27
REMARK 465 ALA A 28
REMARK 465 ILE A 29
REMARK 465 ASP A 30
REMARK 465 VAL A 31
REMARK 465 VAL A 32
REMARK 465 ALA A 33
REMARK 465 GLU A 34
REMARK 465 LYS A 35
REMARK 465 PRO A 36
REMARK 465 SER A 37
REMARK 465 VAL A 38
REMARK 465 ARG A 39
REMARK 465 LEU A 40
REMARK 465 THR A 41
REMARK 465 PRO A 42
REMARK 465 THR A 43
REMARK 465 GLU A 307
REMARK 465 ALA A 308
REMARK 465 SER A 309
REMARK 465 THR A 310
REMARK 465 GLN A 311
REMARK 465 ASP A 312
REMARK 465 PRO A 313
REMARK 465 ARG A 314
REMARK 465 ILE A 315
REMARK 465 SER A 316
REMARK 465 PRO A 317
REMARK 465 LEU A 318
REMARK 465 PHE A 319
REMARK 465 GLY A 320
REMARK 465 HIS A 321
REMARK 465 LEU A 322
REMARK 465 ASP A 323
REMARK 465 MET A 324
REMARK 465 HIS A 325
REMARK 465 SER A 326
REMARK 465 GLY A 327
REMARK 465 GLY A 328
REMARK 465 GLN A 329
REMARK 465 SER A 330
REMARK 465 GLY A 331
REMARK 465 PRO A 332
REMARK 465 MET A 333
REMARK 465 HIS A 334
REMARK 465 ARG A 376
REMARK 465 GLU A 377
REMARK 465 GLU A 378
REMARK 465 SER A 379
REMARK 465 PHE A 380
REMARK 465 ARG A 381
REMARK 465 ILE A 382
REMARK 465 HIS A 383
REMARK 465 HIS A 384
REMARK 465 HIS A 385
REMARK 465 HIS A 386
REMARK 465 HIS A 387
REMARK 465 HIS A 388
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 152 99.90 -63.47
REMARK 500 HIS A 302 -20.41 84.18
REMARK 500 ILE A 362 -58.74 -122.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 249 OD1
REMARK 620 2 ADP A 401 O1A 92.6
REMARK 620 3 ADP A 401 O1B 91.4 92.1
REMARK 620 4 HOH A 501 O 176.1 90.6 86.3
REMARK 620 5 HOH A 502 O 86.1 88.3 177.5 96.2
REMARK 620 6 HOH A 558 O 86.4 177.3 85.3 90.2 94.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 403 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 298 O
REMARK 620 2 ASP A 300 O 94.5
REMARK 620 3 PHE A 303 O 119.7 101.1
REMARK 620 4 GLY A 337 O 152.5 78.6 87.8
REMARK 620 5 ADP A 401 O2A 90.6 150.0 101.9 83.3
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HRI A 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DZY RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH DIFFERENT INHIBITOR
REMARK 900 RELATED ID: 4H7Q RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH DIFFERENT INHIBITOR
REMARK 900 RELATED ID: 3TZ4 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH DIFFERENT INHIBITOR
REMARK 900 RELATED ID: 3TZ5 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH DIFFERENT INHIBITOR
REMARK 900 RELATED ID: 4E00 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH DIFFERENT INHIBITOR
REMARK 900 RELATED ID: 4H81 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH DIFFERENT INHIBITOR
DBREF 4H85 A -29 382 UNP Q00972 BCKD_RAT 1 412
SEQADV 4H85 HIS A 383 UNP Q00972 EXPRESSION TAG
SEQADV 4H85 HIS A 384 UNP Q00972 EXPRESSION TAG
SEQADV 4H85 HIS A 385 UNP Q00972 EXPRESSION TAG
SEQADV 4H85 HIS A 386 UNP Q00972 EXPRESSION TAG
SEQADV 4H85 HIS A 387 UNP Q00972 EXPRESSION TAG
SEQADV 4H85 HIS A 388 UNP Q00972 EXPRESSION TAG
SEQRES 1 A 418 MET ILE LEU THR SER VAL LEU GLY SER GLY PRO ARG SER
SEQRES 2 A 418 GLY SER SER LEU TRP PRO LEU LEU GLY SER SER LEU SER
SEQRES 3 A 418 LEU ARG VAL ARG SER THR SER ALA THR ASP THR HIS HIS
SEQRES 4 A 418 VAL GLU LEU ALA ARG GLU ARG SER LYS THR VAL THR SER
SEQRES 5 A 418 PHE TYR ASN GLN SER ALA ILE ASP VAL VAL ALA GLU LYS
SEQRES 6 A 418 PRO SER VAL ARG LEU THR PRO THR MET MET LEU TYR SER
SEQRES 7 A 418 GLY ARG SER GLN ASP GLY SER HIS LEU LEU LYS SER GLY
SEQRES 8 A 418 ARG TYR LEU GLN GLN GLU LEU PRO VAL ARG ILE ALA HIS
SEQRES 9 A 418 ARG ILE LYS GLY PHE ARG SER LEU PRO PHE ILE ILE GLY
SEQRES 10 A 418 CYS ASN PRO THR ILE LEU HIS VAL HIS GLU LEU TYR ILE
SEQRES 11 A 418 ARG ALA PHE GLN LYS LEU THR ASP PHE PRO PRO ILE LYS
SEQRES 12 A 418 ASP GLN ALA ASP GLU ALA GLN TYR CYS GLN LEU VAL ARG
SEQRES 13 A 418 GLN LEU LEU ASP ASP HIS LYS ASP VAL VAL THR LEU LEU
SEQRES 14 A 418 ALA GLU GLY LEU ARG GLU SER ARG LYS HIS ILE GLU ASP
SEQRES 15 A 418 GLU LYS LEU VAL ARG TYR PHE LEU ASP LYS THR LEU THR
SEQRES 16 A 418 SER ARG LEU GLY ILE ARG MET LEU ALA THR HIS HIS LEU
SEQRES 17 A 418 ALA LEU HIS GLU ASP LYS PRO ASP PHE VAL GLY ILE ILE
SEQRES 18 A 418 CYS THR ARG LEU SER PRO LYS LYS ILE ILE GLU LYS TRP
SEQRES 19 A 418 VAL ASP PHE ALA ARG ARG LEU CYS GLU HIS LYS TYR GLY
SEQRES 20 A 418 ASN ALA PRO ARG VAL ARG ILE ASN GLY HIS VAL ALA ALA
SEQRES 21 A 418 ARG PHE PRO PHE ILE PRO MET PRO LEU ASP TYR ILE LEU
SEQRES 22 A 418 PRO GLU LEU LEU LYS ASN ALA MET ARG ALA THR MET GLU
SEQRES 23 A 418 SER HIS LEU ASP THR PRO TYR ASN VAL PRO ASP VAL VAL
SEQRES 24 A 418 ILE THR ILE ALA ASN ASN ASP VAL ASP LEU ILE ILE ARG
SEQRES 25 A 418 ILE SER ASP ARG GLY GLY GLY ILE ALA HIS LYS ASP LEU
SEQRES 26 A 418 ASP ARG VAL MET ASP TYR HIS PHE THR THR ALA GLU ALA
SEQRES 27 A 418 SER THR GLN ASP PRO ARG ILE SER PRO LEU PHE GLY HIS
SEQRES 28 A 418 LEU ASP MET HIS SER GLY GLY GLN SER GLY PRO MET HIS
SEQRES 29 A 418 GLY PHE GLY PHE GLY LEU PRO THR SER ARG ALA TYR ALA
SEQRES 30 A 418 GLU TYR LEU GLY GLY SER LEU GLN LEU GLN SER LEU GLN
SEQRES 31 A 418 GLY ILE GLY THR ASP VAL TYR LEU ARG LEU ARG HIS ILE
SEQRES 32 A 418 ASP GLY ARG GLU GLU SER PHE ARG ILE HIS HIS HIS HIS
SEQRES 33 A 418 HIS HIS
HET ADP A 401 27
HET MG A 402 1
HET K A 403 1
HET HRI A 404 9
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM K POTASSIUM ION
HETNAM HRI ALPHA-CHLOROISOCAPROIC ACID
FORMUL 2 ADP C10 H15 N5 O10 P2
FORMUL 3 MG MG 2+
FORMUL 4 K K 1+
FORMUL 5 HRI C6 H11 CL O2
FORMUL 6 HOH *101(H2 O)
HELIX 1 1 GLY A 54 LEU A 82 1 29
HELIX 2 2 PRO A 83 CYS A 88 1 6
HELIX 3 3 ASN A 89 PHE A 109 1 21
HELIX 4 4 ASP A 114 HIS A 132 1 19
HELIX 5 5 ASP A 134 ARG A 147 1 14
HELIX 6 6 LYS A 148 ILE A 150 5 3
HELIX 7 7 GLU A 153 LEU A 180 1 28
HELIX 8 8 SER A 196 GLY A 217 1 22
HELIX 9 9 PRO A 236 SER A 257 1 22
HELIX 10 10 ALA A 291 ASP A 296 1 6
HELIX 11 11 PHE A 338 LEU A 350 1 13
SHEET 1 A 3 PHE A 187 VAL A 188 0
SHEET 2 A 3 ILE A 191 LEU A 195 -1 O ILE A 191 N VAL A 188
SHEET 3 A 3 PHE A 232 PHE A 234 -1 O PHE A 234 N CYS A 192
SHEET 1 B 5 VAL A 222 GLY A 226 0
SHEET 2 B 5 VAL A 268 ASN A 274 1 O ILE A 270 N ARG A 223
SHEET 3 B 5 ASP A 278 ASP A 285 -1 O ILE A 280 N ALA A 273
SHEET 4 B 5 GLY A 363 ARG A 371 -1 O LEU A 368 N ILE A 281
SHEET 5 B 5 SER A 353 LEU A 359 -1 N GLN A 355 O TYR A 367
LINK OD1 ASN A 249 MG MG A 402 1555 1555 2.25
LINK O VAL A 298 K K A 403 1555 1555 2.85
LINK O ASP A 300 K K A 403 1555 1555 2.82
LINK O PHE A 303 K K A 403 1555 1555 2.89
LINK O GLY A 337 K K A 403 1555 1555 2.96
LINK O1A ADP A 401 MG MG A 402 1555 1555 2.13
LINK O1B ADP A 401 MG MG A 402 1555 1555 2.20
LINK O2A ADP A 401 K K A 403 1555 1555 2.86
LINK MG MG A 402 O HOH A 501 1555 1555 2.33
LINK MG MG A 402 O HOH A 502 1555 1555 2.17
LINK MG MG A 402 O HOH A 558 1555 1555 2.52
SITE 1 AC1 25 ASN A 249 ARG A 252 ALA A 253 ASP A 285
SITE 2 AC1 25 GLY A 289 ILE A 290 VAL A 298 PHE A 303
SITE 3 AC1 25 THR A 304 THR A 305 GLY A 335 PHE A 336
SITE 4 AC1 25 GLY A 337 GLY A 339 LEU A 340 PRO A 341
SITE 5 AC1 25 THR A 364 MG A 402 K A 403 HOH A 501
SITE 6 AC1 25 HOH A 502 HOH A 505 HOH A 516 HOH A 534
SITE 7 AC1 25 HOH A 536
SITE 1 AC2 5 ASN A 249 ADP A 401 HOH A 501 HOH A 502
SITE 2 AC2 5 HOH A 558
SITE 1 AC3 6 VAL A 298 ASP A 300 PHE A 303 GLY A 337
SITE 2 AC3 6 PRO A 341 ADP A 401
SITE 1 AC4 6 ILE A 72 TYR A 99 HIS A 132 ARG A 167
SITE 2 AC4 6 ILE A 170 ARG A 171
CRYST1 127.619 127.619 73.987 90.00 90.00 90.00 P 42 21 2 8
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 0.007836 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007836 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013516 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
