HEADER HYDROLASE/HYDROLASE INHIBITOR 15-MAY-14 4PKU
TITLE ANTHRAX TOXIN LETHAL FACTOR WITH BOUND SMALL MOLECULE INHIBITOR 15
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LETHAL FACTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 298-809;
COMPND 5 SYNONYM: LF,ANTHRAX LETHAL TOXIN ENDOPEPTIDASE COMPONENT;
COMPND 6 EC: 3.4.24.83;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;
SOURCE 3 ORGANISM_TAXID: 1392;
SOURCE 4 GENE: LEF, PXO1-107, BXA0172, GBAA_PXO1_0172;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2 PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG10
KEYWDS ANTHRAX TOXIN, LETHAL FACTOR, METALLOPROTEINASE, METALLOPROTEASE,
KEYWDS 2 STRUCTURAL DYNAMICS, LIGAND-INDUCED CONFORMATIONAL CHANGE,
KEYWDS 3 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.M.MAIZE,T.DE LA MORA,B.C.FINZEL
REVDAT 5 27-DEC-23 4PKU 1 REMARK
REVDAT 4 11-DEC-19 4PKU 1 REMARK
REVDAT 3 27-SEP-17 4PKU 1 SOURCE KEYWDS REMARK
REVDAT 2 26-NOV-14 4PKU 1 JRNL
REVDAT 1 12-NOV-14 4PKU 0
JRNL AUTH K.M.MAIZE,E.K.KURBANOV,T.DE LA MORA-REY,T.W.GEDERS,
JRNL AUTH 2 D.J.HWANG,M.A.WALTERS,R.L.JOHNSON,E.A.AMIN,B.C.FINZEL
JRNL TITL ANTHRAX TOXIN LETHAL FACTOR DOMAIN 3 IS HIGHLY MOBILE AND
JRNL TITL 2 RESPONSIVE TO LIGAND BINDING.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 2813 2014
JRNL REFN ESSN 1399-0047
JRNL PMID 25372673
JRNL DOI 10.1107/S1399004714018161
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 24080
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 1223
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 45.5224 - 4.9903 1.00 2698 148 0.1734 0.2102
REMARK 3 2 4.9903 - 3.9616 1.00 2565 139 0.1628 0.2331
REMARK 3 3 3.9616 - 3.4611 1.00 2547 140 0.1839 0.2413
REMARK 3 4 3.4611 - 3.1447 1.00 2527 146 0.2256 0.2793
REMARK 3 5 3.1447 - 2.9193 1.00 2520 113 0.2364 0.2866
REMARK 3 6 2.9193 - 2.7473 1.00 2540 121 0.2292 0.2867
REMARK 3 7 2.7473 - 2.6097 1.00 2484 138 0.2319 0.2877
REMARK 3 8 2.6097 - 2.4961 1.00 2492 151 0.2286 0.2784
REMARK 3 9 2.4961 - 2.4000 1.00 2484 127 0.2318 0.2955
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.470
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.67
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.23
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 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 : 0.003 4037
REMARK 3 ANGLE : 0.752 5452
REMARK 3 CHIRALITY : 0.028 603
REMARK 3 PLANARITY : 0.003 702
REMARK 3 DIHEDRAL : 15.545 1519
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 4PKU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000201583.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
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) : 1.000
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 2.5.1
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24160
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 143.360
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11-16% PEG 8K, 50 MM BIS-TRIS, 100 MM
REMARK 280 MAGNESIUM ACETATE, PH 6.8, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 286K
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 30.66850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.67900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.94750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.67900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.66850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.94750
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 SER A 262
REMARK 465 ASN A 263
REMARK 465 ALA A 264
REMARK 465 LEU A 265
REMARK 465 ILE A 345
REMARK 465 ARG A 346
REMARK 465 ASP A 347
REMARK 465 SER A 348
REMARK 465 LEU A 349
REMARK 465 SER A 350
REMARK 465 GLU A 351
REMARK 465 GLU A 352
REMARK 465 GLU A 353
REMARK 465 LYS A 354
REMARK 465 GLU A 355
REMARK 465 LEU A 356
REMARK 465 LEU A 357
REMARK 465 ASN A 358
REMARK 465 ARG A 359
REMARK 465 ILE A 360
REMARK 465 GLN A 361
REMARK 465 VAL A 362
REMARK 465 ASP A 363
REMARK 465 SER A 364
REMARK 465 SER A 365
REMARK 465 ASN A 366
REMARK 465 LEU A 777
REMARK 465 VAL A 778
REMARK 465 PRO A 779
REMARK 465 ARG A 780
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 272 CG CD OE1 OE2
REMARK 470 LYS A 304 CG CD CE NZ
REMARK 470 HIS A 309 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 317 CG CD OE1 OE2
REMARK 470 LEU A 318 CG CD1 CD2
REMARK 470 LYS A 320 CG CD CE NZ
REMARK 470 ARG A 321 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 322 CG1 CG2 CD1
REMARK 470 GLN A 323 CG CD OE1 NE2
REMARK 470 ILE A 324 CG1 CG2 CD1
REMARK 470 ASP A 325 CG OD1 OD2
REMARK 470 SER A 326 OG
REMARK 470 GLU A 333 CG CD OE1 OE2
REMARK 470 LYS A 335 CG CD CE NZ
REMARK 470 GLU A 336 CG CD OE1 OE2
REMARK 470 LYS A 340 CG CD CE NZ
REMARK 470 ASP A 344 CG OD1 OD2
REMARK 470 GLU A 372 CG CD OE1 OE2
REMARK 470 ASP A 495 CG OD1 OD2
REMARK 470 ASN A 496 CG OD1 ND2
REMARK 470 SER A 538 OG
REMARK 470 GLU A 539 CG CD OE1 OE2
REMARK 470 LYS A 578 CG CD CE NZ
REMARK 470 ASP A 701 CG OD1 OD2
REMARK 470 ASN A 703 CG OD1 ND2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU A 269 OG SER A 312 4455 2.19
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 ASN A 586 77.48 -110.00
REMARK 500 LEU A 725 -127.19 -117.79
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 ZN A 802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 686 NE2
REMARK 620 2 HIS A 690 NE2 83.4
REMARK 620 3 GLU A 735 OE1 91.2 105.2
REMARK 620 4 30P A 801 O5 91.7 92.0 162.8
REMARK 620 5 30P A 801 O3 93.5 169.6 84.8 78.1
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 30P A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 802
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JKY RELATED DB: PDB
REMARK 900 THE FULL-LENGTH PROTEIN IN A I4132 SPACEGROUP
REMARK 900 RELATED ID: 1J7N RELATED DB: PDB
REMARK 900 THE FULL-LENGTH PROTEIN WITH BOUND ZINC IN A P21 SPACEGROUP
REMARK 900 RELATED ID: 1PWP RELATED DB: PDB
REMARK 900 THE FULL-LENGTH PROTEIN COMPLEXED WITH SMALL MOLECULE INHIBITOR NSC
REMARK 900 12155 IN A P21 SPACEGROUP
REMARK 900 RELATED ID: 1PWQ RELATED DB: PDB
REMARK 900 THE FULL-LENGTH PROTEIN COMPLEXED WITH A METAL-CHELATING PEPTIDYL
REMARK 900 SMALL MOLECULE INHIBITOR IN A P21 SPACEGROUP
REMARK 900 RELATED ID: 1PWU RELATED DB: PDB
REMARK 900 THE FULL-LENGTH PROTEIN COMPLEXED WITH GM6001 IN A P21 SPACEGROUP
REMARK 900 RELATED ID: 1PWV RELATED DB: PDB
REMARK 900 THE FULL-LENGTH PROTEIN COMPLEXED WITH AN OPTIMIZED PEPTIDE
REMARK 900 SUBSTRATE IN A P21 SPACEGROUP
REMARK 900 RELATED ID: 1PWW RELATED DB: PDB
REMARK 900 THE FULL-LENGTH INACTIVE MUTANT PROTEIN COMPLEXED WITH AN OPTIMIZED
REMARK 900 PEPTIDE SUBSTRATE AND ZINC IN A P21 SPACEGROUP.
REMARK 900 RELATED ID: 1ZXV RELATED DB: PDB
REMARK 900 THE FULL-LENGTH PROTEIN COMPLEXED WITH A SMALL MOLECULE INHIBITOR
REMARK 900 IN A P21 SPACEGROUP
REMARK 900 RELATED ID: 1YQY RELATED DB: PDB
REMARK 900 THE N-TERMINALLY TRUNCATED PROTEIN COMPLEXED WITH A SMALL MOLECULE
REMARK 900 INHIBITOR IN A P212121 SPACEGROUP
REMARK 900 RELATED ID: 4PKQ RELATED DB: PDB
REMARK 900 RELATED ID: 4PKR RELATED DB: PDB
REMARK 900 RELATED ID: 4PKS RELATED DB: PDB
REMARK 900 RELATED ID: 4PKT RELATED DB: PDB
REMARK 900 RELATED ID: 4PKV RELATED DB: PDB
REMARK 900 RELATED ID: 4PKW RELATED DB: PDB
DBREF 4PKU A 265 776 UNP P15917 LEF_BACAN 298 809
SEQADV 4PKU SER A 262 UNP P15917 EXPRESSION TAG
SEQADV 4PKU ASN A 263 UNP P15917 EXPRESSION TAG
SEQADV 4PKU ALA A 264 UNP P15917 EXPRESSION TAG
SEQADV 4PKU SER A 266 UNP P15917 ALA 299 ENGINEERED MUTATION
SEQADV 4PKU LEU A 777 UNP P15917 EXPRESSION TAG
SEQADV 4PKU VAL A 778 UNP P15917 EXPRESSION TAG
SEQADV 4PKU PRO A 779 UNP P15917 EXPRESSION TAG
SEQADV 4PKU ARG A 780 UNP P15917 EXPRESSION TAG
SEQRES 1 A 519 SER ASN ALA LEU SER ARG TYR GLU LYS TRP GLU LYS ILE
SEQRES 2 A 519 LYS GLN HIS TYR GLN HIS TRP SER ASP SER LEU SER GLU
SEQRES 3 A 519 GLU GLY ARG GLY LEU LEU LYS LYS LEU GLN ILE PRO ILE
SEQRES 4 A 519 GLU PRO LYS LYS ASP ASP ILE ILE HIS SER LEU SER GLN
SEQRES 5 A 519 GLU GLU LYS GLU LEU LEU LYS ARG ILE GLN ILE ASP SER
SEQRES 6 A 519 SER ASP PHE LEU SER THR GLU GLU LYS GLU PHE LEU LYS
SEQRES 7 A 519 LYS LEU GLN ILE ASP ILE ARG ASP SER LEU SER GLU GLU
SEQRES 8 A 519 GLU LYS GLU LEU LEU ASN ARG ILE GLN VAL ASP SER SER
SEQRES 9 A 519 ASN PRO LEU SER GLU LYS GLU LYS GLU PHE LEU LYS LYS
SEQRES 10 A 519 LEU LYS LEU ASP ILE GLN PRO TYR ASP ILE ASN GLN ARG
SEQRES 11 A 519 LEU GLN ASP THR GLY GLY LEU ILE ASP SER PRO SER ILE
SEQRES 12 A 519 ASN LEU ASP VAL ARG LYS GLN TYR LYS ARG ASP ILE GLN
SEQRES 13 A 519 ASN ILE ASP ALA LEU LEU HIS GLN SER ILE GLY SER THR
SEQRES 14 A 519 LEU TYR ASN LYS ILE TYR LEU TYR GLU ASN MET ASN ILE
SEQRES 15 A 519 ASN ASN LEU THR ALA THR LEU GLY ALA ASP LEU VAL ASP
SEQRES 16 A 519 SER THR ASP ASN THR LYS ILE ASN ARG GLY ILE PHE ASN
SEQRES 17 A 519 GLU PHE LYS LYS ASN PHE LYS TYR SER ILE SER SER ASN
SEQRES 18 A 519 TYR MET ILE VAL ASP ILE ASN GLU ARG PRO ALA LEU ASP
SEQRES 19 A 519 ASN GLU ARG LEU LYS TRP ARG ILE GLN LEU SER PRO ASP
SEQRES 20 A 519 THR ARG ALA GLY TYR LEU GLU ASN GLY LYS LEU ILE LEU
SEQRES 21 A 519 GLN ARG ASN ILE GLY LEU GLU ILE LYS ASP VAL GLN ILE
SEQRES 22 A 519 ILE LYS GLN SER GLU LYS GLU TYR ILE ARG ILE ASP ALA
SEQRES 23 A 519 LYS VAL VAL PRO LYS SER LYS ILE ASP THR LYS ILE GLN
SEQRES 24 A 519 GLU ALA GLN LEU ASN ILE ASN GLN GLU TRP ASN LYS ALA
SEQRES 25 A 519 LEU GLY LEU PRO LYS TYR THR LYS LEU ILE THR PHE ASN
SEQRES 26 A 519 VAL HIS ASN ARG TYR ALA SER ASN ILE VAL GLU SER ALA
SEQRES 27 A 519 TYR LEU ILE LEU ASN GLU TRP LYS ASN ASN ILE GLN SER
SEQRES 28 A 519 ASP LEU ILE LYS LYS VAL THR ASN TYR LEU VAL ASP GLY
SEQRES 29 A 519 ASN GLY ARG PHE VAL PHE THR ASP ILE THR LEU PRO ASN
SEQRES 30 A 519 ILE ALA GLU GLN TYR THR HIS GLN ASP GLU ILE TYR GLU
SEQRES 31 A 519 GLN VAL HIS SER LYS GLY LEU TYR VAL PRO GLU SER ARG
SEQRES 32 A 519 SER ILE LEU LEU HIS GLY PRO SER LYS GLY VAL GLU LEU
SEQRES 33 A 519 ARG ASN ASP SER GLU GLY PHE ILE HIS GLU PHE GLY HIS
SEQRES 34 A 519 ALA VAL ASP ASP TYR ALA GLY TYR LEU LEU ASP LYS ASN
SEQRES 35 A 519 GLN SER ASP LEU VAL THR ASN SER LYS LYS PHE ILE ASP
SEQRES 36 A 519 ILE PHE LYS GLU GLU GLY SER ASN LEU THR SER TYR GLY
SEQRES 37 A 519 ARG THR ASN GLU ALA GLU PHE PHE ALA GLU ALA PHE ARG
SEQRES 38 A 519 LEU MET HIS SER THR ASP HIS ALA GLU ARG LEU LYS VAL
SEQRES 39 A 519 GLN LYS ASN ALA PRO LYS THR PHE GLN PHE ILE ASN ASP
SEQRES 40 A 519 GLN ILE LYS PHE ILE ILE ASN SER LEU VAL PRO ARG
HET 30P A 801 26
HET ZN A 802 1
HETNAM 30P N~2~-(3-AMINOBENZYL)-N~2~-[(4-FLUORO-3-METHYLPHENYL)
HETNAM 2 30P SULFONYL]-N-HYDROXY-D-ALANINAMIDE
HETNAM ZN ZINC ION
FORMUL 2 30P C17 H20 F N3 O4 S
FORMUL 3 ZN ZN 2+
FORMUL 4 HOH *81(H2 O)
HELIX 1 AA1 SER A 266 TYR A 278 1 13
HELIX 2 AA2 TYR A 278 SER A 284 1 7
HELIX 3 AA3 SER A 286 ILE A 298 1 13
HELIX 4 AA4 LYS A 303 LEU A 311 1 9
HELIX 5 AA5 SER A 312 ILE A 322 1 11
HELIX 6 AA6 GLN A 323 SER A 327 5 5
HELIX 7 AA7 SER A 331 ILE A 343 1 13
HELIX 8 AA8 SER A 369 ILE A 383 1 15
HELIX 9 AA9 ASP A 387 GLY A 396 1 10
HELIX 10 AB1 ASN A 405 LEU A 423 1 19
HELIX 11 AB2 ASN A 442 LEU A 446 5 5
HELIX 12 AB3 THR A 447 ALA A 452 1 6
HELIX 13 AB4 ASN A 464 ASN A 474 1 11
HELIX 14 AB5 PRO A 551 GLY A 575 1 25
HELIX 15 AB6 TYR A 591 ILE A 610 1 20
HELIX 16 AB7 GLN A 611 GLY A 625 1 15
HELIX 17 AB8 THR A 635 ASN A 638 5 4
HELIX 18 AB9 ILE A 639 THR A 644 1 6
HELIX 19 AC1 GLU A 648 GLN A 652 5 5
HELIX 20 AC2 ASN A 679 ASP A 701 1 23
HELIX 21 AC3 LEU A 707 ASN A 710 5 4
HELIX 22 AC4 SER A 711 GLY A 722 1 12
HELIX 23 AC5 SER A 727 THR A 731 5 5
HELIX 24 AC6 ASN A 732 HIS A 745 1 14
HELIX 25 AC7 ASP A 748 ALA A 759 1 12
HELIX 26 AC8 ALA A 759 SER A 776 1 18
SHEET 1 AA1 5 TYR A 436 MET A 441 0
SHEET 2 AA1 5 LEU A 499 GLN A 504 -1 O ILE A 503 N LEU A 437
SHEET 3 AA1 5 GLU A 541 VAL A 550 1 O ILE A 543 N LYS A 500
SHEET 4 AA1 5 ILE A 525 LYS A 536 -1 N ILE A 535 O TYR A 542
SHEET 5 AA1 5 TYR A 477 SER A 480 -1 N SER A 478 O LEU A 527
SHEET 1 AA2 3 ILE A 485 ASP A 487 0
SHEET 2 AA2 3 LYS A 518 LEU A 521 -1 O LEU A 519 N VAL A 486
SHEET 3 AA2 3 ALA A 511 LEU A 514 -1 N LEU A 514 O LYS A 518
SHEET 1 AA3 4 ILE A 583 ASN A 586 0
SHEET 2 AA3 4 PHE A 629 THR A 632 1 O PHE A 629 N THR A 584
SHEET 3 AA3 4 SER A 665 HIS A 669 1 O ILE A 666 N VAL A 630
SHEET 4 AA3 4 GLY A 657 VAL A 660 -1 N LEU A 658 O LEU A 667
LINK NE2 HIS A 686 ZN ZN A 802 1555 1555 2.48
LINK NE2 HIS A 690 ZN ZN A 802 1555 1555 2.47
LINK OE1 GLU A 735 ZN ZN A 802 1555 1555 2.44
LINK O5 30P A 801 ZN ZN A 802 1555 1555 2.08
LINK O3 30P A 801 ZN ZN A 802 1555 1555 2.08
SITE 1 AC1 17 ASP A 328 HIS A 654 SER A 655 LYS A 656
SITE 2 AC1 17 GLY A 657 VAL A 675 LEU A 677 HIS A 686
SITE 3 AC1 17 GLU A 687 HIS A 690 TYR A 728 GLU A 735
SITE 4 AC1 17 GLU A 739 ARG A 742 ZN A 802 HOH A 924
SITE 5 AC1 17 HOH A 968
SITE 1 AC2 5 HIS A 686 HIS A 690 GLU A 735 30P A 801
SITE 2 AC2 5 HOH A 968
CRYST1 61.337 67.895 143.358 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 0.016303 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014729 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006976 0.00000
(ATOM LINES ARE NOT SHOWN.)
END