HEADER TOXIN,HYDROLASE 14-JAN-15 4XM6
TITLE ANTHRAX TOXIN LETHAL FACTOR WITH LIGAND-INDUCED BINDING POCKET
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, TOXIN,
KEYWDS 3 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.M.MAIZE,T.DE LA MORA-REY,B.C.FINZEL
REVDAT 6 27-SEP-23 4XM6 1 REMARK
REVDAT 5 11-DEC-19 4XM6 1 REMARK
REVDAT 4 27-SEP-17 4XM6 1 JRNL REMARK
REVDAT 3 30-DEC-15 4XM6 1 JRNL
REVDAT 2 02-DEC-15 4XM6 1 JRNL
REVDAT 1 11-NOV-15 4XM6 0
JRNL AUTH K.M.MAIZE,E.K.KURBANOV,R.L.JOHNSON,E.A.AMIN,B.C.FINZEL
JRNL TITL LIGAND-INDUCED EXPANSION OF THE S1' SITE IN THE ANTHRAX
JRNL TITL 2 TOXIN LETHAL FACTOR.
JRNL REF FEBS LETT. V. 589 3836 2015
JRNL REFN ISSN 0014-5793
JRNL PMID 26578066
JRNL DOI 10.1016/J.FEBSLET.2015.11.005
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.38
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 25917
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 1316
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 23.3814 - 4.8792 0.99 2903 168 0.1783 0.2154
REMARK 3 2 4.8792 - 3.8785 0.99 2794 161 0.1659 0.1990
REMARK 3 3 3.8785 - 3.3899 1.00 2799 147 0.1912 0.2444
REMARK 3 4 3.3899 - 3.0807 1.00 2758 159 0.2306 0.2824
REMARK 3 5 3.0807 - 2.8603 0.99 2755 134 0.2634 0.2784
REMARK 3 6 2.8603 - 2.6919 0.98 2678 141 0.2515 0.2790
REMARK 3 7 2.6919 - 2.5573 0.97 2644 151 0.2582 0.3226
REMARK 3 8 2.5573 - 2.4461 0.97 2680 135 0.2498 0.3344
REMARK 3 9 2.4461 - 2.3520 0.94 2590 120 0.2490 0.2739
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.49
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.25
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 : 0.005 4095
REMARK 3 ANGLE : 0.889 5512
REMARK 3 CHIRALITY : 0.036 604
REMARK 3 PLANARITY : 0.003 710
REMARK 3 DIHEDRAL : 14.744 1573
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 4XM6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000205815.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
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 MICROMAX-007 HF
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25999
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.24700
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: 1YQY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
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 28.96800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.28800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.46100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.28800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.96800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.46100
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 ASP A 328
REMARK 465 PHE A 329
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 PRO A 367
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 LEU A 330 CG CD1 CD2
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 NH1 ARG A 321 NE2 HIS A 749 3545 1.93
REMARK 500 CZ ARG A 321 NE2 HIS A 749 3545 2.01
REMARK 500 NH1 ARG A 321 CE1 HIS A 749 3545 2.06
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 ASP A 325 4.76 -66.49
REMARK 500 ASN A 405 133.51 -39.08
REMARK 500 ASN A 482 -169.12 -113.28
REMARK 500 LEU A 494 -167.68 -102.74
REMARK 500 GLU A 497 76.29 -115.36
REMARK 500 GLU A 676 1.49 59.21
REMARK 500 ASP A 701 86.71 -160.76
REMARK 500 GLN A 704 57.60 39.45
REMARK 500 LEU A 725 -150.41 -121.05
REMARK 500 LYS A 757 -60.85 -92.25
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 99.6
REMARK 620 3 GLU A 735 OE1 79.0 98.8
REMARK 620 4 GLU A 735 OE2 139.2 82.6 60.5
REMARK 620 5 41R A 801 O4 91.3 168.6 80.2 87.1
REMARK 620 6 41R A 801 O5 107.1 107.2 151.6 111.1 72.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 41R 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 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 804
REMARK 900
REMARK 900 RELATED ENTRIES
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: 4PKU RELATED DB: PDB
REMARK 900 RELATED ID: 4PKV RELATED DB: PDB
REMARK 900 RELATED ID: 4PKW RELATED DB: PDB
REMARK 900 RELATED ID: 4WF6 RELATED DB: PDB
REMARK 900 RELATED ID: 1YQY RELATED DB: PDB
REMARK 900 RELATED ID: 4XM7 RELATED DB: PDB
REMARK 900 RELATED ID: 4XM8 RELATED DB: PDB
DBREF 4XM6 A 265 776 UNP P15917 LEF_BACAN 298 809
SEQADV 4XM6 SER A 262 UNP P15917 EXPRESSION TAG
SEQADV 4XM6 ASN A 263 UNP P15917 EXPRESSION TAG
SEQADV 4XM6 ALA A 264 UNP P15917 EXPRESSION TAG
SEQADV 4XM6 SER A 266 UNP P15917 ALA 299 ENGINEERED MUTATION
SEQADV 4XM6 LEU A 777 UNP P15917 EXPRESSION TAG
SEQADV 4XM6 VAL A 778 UNP P15917 EXPRESSION TAG
SEQADV 4XM6 PRO A 779 UNP P15917 EXPRESSION TAG
SEQADV 4XM6 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 41R A 801 24
HET ZN A 802 1
HET EDO A 803 4
HET EDO A 804 4
HETNAM 41R N~2~-[(4-FLUORO-3-METHYLPHENYL)SULFONYL]-N-HYDROXY-
HETNAM 2 41R N~2~-(2-METHYLPROPYL)-D-VALINAMIDE
HETNAM ZN ZINC ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 41R C16 H25 F N2 O4 S
FORMUL 3 ZN ZN 2+
FORMUL 4 EDO 2(C2 H6 O2)
FORMUL 6 HOH *121(H2 O)
HELIX 1 AA1 SER A 266 SER A 284 1 19
HELIX 2 AA2 SER A 286 ILE A 298 1 13
HELIX 3 AA3 LYS A 303 LEU A 311 1 9
HELIX 4 AA4 SER A 312 ILE A 322 1 11
HELIX 5 AA5 SER A 331 ILE A 343 1 13
HELIX 6 AA6 SER A 369 LYS A 380 1 12
HELIX 7 AA7 LEU A 381 ILE A 383 5 3
HELIX 8 AA8 ASP A 387 GLY A 396 1 10
HELIX 9 AA9 ASN A 405 LEU A 423 1 19
HELIX 10 AB1 ASN A 442 LEU A 446 5 5
HELIX 11 AB2 THR A 447 ASP A 453 1 7
HELIX 12 AB3 ASN A 464 ASN A 474 1 11
HELIX 13 AB4 PRO A 551 LEU A 574 1 24
HELIX 14 AB5 TYR A 591 ILE A 610 1 20
HELIX 15 AB6 GLN A 611 GLY A 625 1 15
HELIX 16 AB7 THR A 635 ASN A 638 5 4
HELIX 17 AB8 ILE A 639 THR A 644 1 6
HELIX 18 AB9 GLU A 648 GLN A 652 5 5
HELIX 19 AC1 PRO A 661 ARG A 664 5 4
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 THR A 726 THR A 731 5 6
HELIX 24 AC6 ASN A 732 MET A 744 1 13
HELIX 25 AC7 ASP A 748 ALA A 759 1 12
HELIX 26 AC8 ALA A 759 ASN A 775 1 17
SHEET 1 AA1 5 LEU A 437 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 545 N ARG A 502
SHEET 4 AA1 5 ILE A 525 LYS A 536 -1 N GLN A 533 O ARG A 544
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 GLY A 512 O ILE A 520
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 2.29
LINK NE2 HIS A 690 ZN ZN A 802 1555 1555 2.32
LINK OE1 GLU A 735 ZN ZN A 802 1555 1555 2.09
LINK OE2 GLU A 735 ZN ZN A 802 1555 1555 2.25
LINK O4 41R A 801 ZN ZN A 802 1555 1555 2.22
LINK O5 41R A 801 ZN ZN A 802 1555 1555 2.39
SITE 1 AC1 14 SER A 655 LYS A 656 GLY A 657 LEU A 668
SITE 2 AC1 14 GLY A 674 VAL A 675 LEU A 677 GLY A 683
SITE 3 AC1 14 HIS A 686 GLU A 687 TYR A 728 GLU A 735
SITE 4 AC1 14 ZN A 802 HOH A 977
SITE 1 AC2 4 HIS A 686 HIS A 690 GLU A 735 41R A 801
SITE 1 AC3 2 GLU A 569 ALA A 573
SITE 1 AC4 6 ASP A 394 SER A 403 THR A 635 PRO A 637
SITE 2 AC4 6 ASN A 638 HOH A 929
CRYST1 57.936 76.922 138.576 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 0.017260 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013000 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007216 0.00000
(ATOM LINES ARE NOT SHOWN.)
END