HEADER HYDROLASE 02-JUL-03 1PWU
TITLE CRYSTAL STRUCTURE OF ANTHRAX LETHAL FACTOR COMPLEXED WITH (3-(N-
TITLE 2 HYDROXYCARBOXAMIDO)-2-ISOBUTYLPROPANOYL-TRP-METHYLAMIDE), A KNOWN
TITLE 3 SMALL MOLECULE INHIBITOR OF MATRIX METALLOPROTEASES.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LETHAL FACTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LF, ANTHRAX LETHAL TOXIN ENDOPEPTIDASE COMPONENT;
COMPND 5 EC: 3.4.24.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;
SOURCE 3 ORGANISM_TAXID: 1392;
SOURCE 4 GENE: LEF OR PXO1-107;
SOURCE 5 EXPRESSION_SYSTEM: BACILLUS ANTHRACIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 1392;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BH441;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PX01
KEYWDS ANTHRAX TOXIN, LETHAL FACTOR, SMALL MOLECULE PEPTIDIC INHIBITOR,
KEYWDS 2 HYDROXAMIC ACID., HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.Y.WONG,R.SCHWARZENBACHER,R.C.LIDDINGTON
REVDAT 4 16-AUG-23 1PWU 1 REMARK
REVDAT 3 27-OCT-21 1PWU 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1PWU 1 VERSN
REVDAT 1 03-FEB-04 1PWU 0
JRNL AUTH B.E.TURK,T.Y.WONG,R.SCHWARZENBACHER,E.T.JARRELL,S.H.LEPPLA,
JRNL AUTH 2 R.J.COLLIER,R.C.LIDDINGTON,L.C.CANTLEY
JRNL TITL THE STRUCTURAL BASIS FOR SUBSTRATE AND INHIBITOR SELECTIVITY
JRNL TITL 2 OF THE ANTHRAX LETHAL FACTOR.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 11 60 2004
JRNL REFN ISSN 1545-9993
JRNL PMID 14718924
JRNL DOI 10.1038/NSMB708
REMARK 2
REMARK 2 RESOLUTION. 2.70 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 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 256376.700
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 65063
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 SET) : 0.235
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3280
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8453
REMARK 3 BIN R VALUE (WORKING SET) : 0.3550
REMARK 3 BIN FREE R VALUE : 0.3920
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 457
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12180
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.77000
REMARK 3 B22 (A**2) : -0.13000
REMARK 3 B33 (A**2) : -3.64000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 5.21000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM SIGMAA (A) : 0.45
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) : 0.44
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.49
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.790
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) : 1.450 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.510 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.870 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.920 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 37.84
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 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : GM6001-INHC.PAR
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : GM6001FIN_GM.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PWU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019648.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72275
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
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 : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ID 1J7N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, TRIS-HCL, EDTA., PH
REMARK 280 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 68.70000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: THE BIOLOGICAL UNIT IS A MONOMER.
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 ALA A 1
REMARK 465 GLY A 2
REMARK 465 GLY A 3
REMARK 465 HIS A 4
REMARK 465 GLY A 5
REMARK 465 ASP A 6
REMARK 465 VAL A 7
REMARK 465 GLY A 8
REMARK 465 MET A 9
REMARK 465 HIS A 10
REMARK 465 VAL A 11
REMARK 465 LYS A 12
REMARK 465 GLU A 13
REMARK 465 LYS A 14
REMARK 465 GLU A 15
REMARK 465 LYS A 16
REMARK 465 ASN A 17
REMARK 465 LYS A 18
REMARK 465 ASP A 19
REMARK 465 GLU A 20
REMARK 465 ASN A 21
REMARK 465 LYS A 22
REMARK 465 ARG A 23
REMARK 465 LYS A 24
REMARK 465 ASP A 25
REMARK 465 GLU A 26
REMARK 465 GLU A 27
REMARK 465 ARG A 28
REMARK 465 ASN A 29
REMARK 465 ALA B 1
REMARK 465 GLY B 2
REMARK 465 GLY B 3
REMARK 465 HIS B 4
REMARK 465 GLY B 5
REMARK 465 ASP B 6
REMARK 465 VAL B 7
REMARK 465 GLY B 8
REMARK 465 MET B 9
REMARK 465 HIS B 10
REMARK 465 VAL B 11
REMARK 465 LYS B 12
REMARK 465 GLU B 13
REMARK 465 LYS B 14
REMARK 465 GLU B 15
REMARK 465 LYS B 16
REMARK 465 ASN B 17
REMARK 465 LYS B 18
REMARK 465 ASP B 19
REMARK 465 GLU B 20
REMARK 465 ASN B 21
REMARK 465 LYS B 22
REMARK 465 ARG B 23
REMARK 465 LYS B 24
REMARK 465 ASP B 25
REMARK 465 GLU B 26
REMARK 465 GLU B 27
REMARK 465 ARG B 28
REMARK 465 ASN B 29
REMARK 465 LYS B 30
REMARK 465 THR B 31
REMARK 465 GLN B 32
REMARK 465 ASN B 358
REMARK 465 ARG B 359
REMARK 465 ILE B 360
REMARK 465 GLN B 361
REMARK 465 VAL B 362
REMARK 465 ASP B 363
REMARK 465 SER B 364
REMARK 465 SER B 365
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 127 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 TYR B 118 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 TYR B 118 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
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 LEU A 36 -78.19 -59.65
REMARK 500 LYS A 49 -73.01 -107.55
REMARK 500 GLU A 52 36.88 -88.37
REMARK 500 LYS A 90 43.12 -82.32
REMARK 500 ALA A 96 13.45 -64.76
REMARK 500 LYS A 102 10.42 -53.85
REMARK 500 ASP A 111 150.62 -46.54
REMARK 500 TYR A 120 136.79 -176.88
REMARK 500 GLU A 123 -154.03 -67.64
REMARK 500 SER A 134 149.21 -173.36
REMARK 500 ASN A 140 71.02 -66.52
REMARK 500 ILE A 159 -70.62 -95.75
REMARK 500 TYR A 167 -149.50 -131.81
REMARK 500 SER A 181 -74.81 -62.24
REMARK 500 PRO A 198 -85.22 -65.02
REMARK 500 PRO A 227 -38.72 -38.90
REMARK 500 GLN A 250 -82.83 -104.61
REMARK 500 GLU A 251 -16.92 -39.19
REMARK 500 ILE A 307 -70.17 -41.37
REMARK 500 SER A 310 8.65 -65.68
REMARK 500 LEU A 311 -109.58 -72.16
REMARK 500 SER A 312 143.44 175.71
REMARK 500 ARG A 321 78.50 -159.98
REMARK 500 ARG A 346 101.03 -52.62
REMARK 500 ASP A 347 -89.75 -128.30
REMARK 500 LEU A 349 51.32 86.02
REMARK 500 SER A 350 -54.13 -26.03
REMARK 500 GLU A 351 -39.76 -39.06
REMARK 500 SER A 365 -174.78 88.67
REMARK 500 PRO A 367 -146.37 -42.61
REMARK 500 LEU A 368 -147.90 -131.72
REMARK 500 SER A 369 118.78 177.50
REMARK 500 GLU A 370 -86.54 -54.28
REMARK 500 LYS A 371 -37.68 -30.62
REMARK 500 ILE A 399 -9.41 -56.54
REMARK 500 PRO A 402 45.93 -81.89
REMARK 500 ASN A 433 -124.34 -108.86
REMARK 500 THR A 458 -72.69 -67.59
REMARK 500 LYS A 473 -85.04 -20.86
REMARK 500 ASN A 474 44.98 -108.27
REMARK 500 ASN A 516 27.61 -76.67
REMARK 500 GLU A 539 -2.32 60.11
REMARK 500 LEU A 582 -60.15 -101.82
REMARK 500 ASN A 586 79.67 -106.12
REMARK 500 GLU A 641 -13.75 -49.51
REMARK 500 SER A 655 -169.91 -171.37
REMARK 500 PRO A 671 -32.63 -39.88
REMARK 500 GLU A 676 79.09 17.65
REMARK 500 ARG A 678 -75.85 -29.06
REMARK 500 LEU A 700 -78.17 -62.68
REMARK 500
REMARK 500 THIS ENTRY HAS 99 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 GM6001 IS A COMMERCIALLY AVAILABLE KNOWN
REMARK 600 INHIBITOR OF MATRIX METALLOPROTEASES. IT
REMARK 600 HAS AN N-TERMINAL HYDROXAMIC ACID MOEITY
REMARK 600 WITH A LEU MIMETIC, FOLLOWED BY A TRP
REMARK 600 RESIDUE AND A C-TERMINAL METHYLAMIDE.
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 A9001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 686 NE2
REMARK 620 2 HIS A 690 NE2 98.3
REMARK 620 3 GLU A 735 OE1 109.5 111.4
REMARK 620 4 GM6 A1001 OAG 109.2 85.2 134.7
REMARK 620 5 GM6 A1001 OAE 105.8 145.4 83.8 63.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B9002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 686 NE2
REMARK 620 2 HIS B 690 NE2 107.2
REMARK 620 3 GLU B 735 OE1 102.7 101.6
REMARK 620 4 GM6 B2001 OAE 84.2 159.2 92.4
REMARK 620 5 GM6 B2001 OAG 95.8 90.4 153.7 70.8
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 ZN A 9001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 9002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GM6 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GM6 B 2001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PWV RELATED DB: PDB
REMARK 900 LETHAL FACTOR (WILD-TYPE) COMPLEXED WITH AN OPTIMISED PEPTIDE
REMARK 900 SUBSTRATE.
REMARK 900 RELATED ID: 1PWW RELATED DB: PDB
REMARK 900 LETHAL FACTOR (ACTIVE SITE MUTANT) COMPLEXED WITH AN OPTIMISED
REMARK 900 PEPTIDE SUBSTRATE.
REMARK 900 RELATED ID: 1PQW RELATED DB: PDB
REMARK 900 LETHAL FACTOR COMPLEXED WITH A SMALL MOLECULE INHIBITOR OF METAL-
REMARK 900 CHELATING MOEITY COUPLED TO THE N-TERMINUS OF A SHORT PEPTIDE WITH
REMARK 900 C-TERMINUS AMIDE MODIFICATION.
REMARK 900 RELATED ID: 1PWP RELATED DB: PDB
REMARK 900 LETHAL FACTOR COMPLEXED WITH A NON-PEPTIDIC SMALL MOLECULE
REMARK 900 INHIBITOR, NCS 12155
DBREF 1PWU A 1 776 UNP P15917 LEF_BACAN 34 809
DBREF 1PWU B 1 776 UNP P15917 LEF_BACAN 34 809
SEQADV 1PWU CYS A 687 UNP P15917 GLU 720 ENGINEERED MUTATION
SEQADV 1PWU CYS B 687 UNP P15917 GLU 720 ENGINEERED MUTATION
SEQRES 1 A 776 ALA GLY GLY HIS GLY ASP VAL GLY MET HIS VAL LYS GLU
SEQRES 2 A 776 LYS GLU LYS ASN LYS ASP GLU ASN LYS ARG LYS ASP GLU
SEQRES 3 A 776 GLU ARG ASN LYS THR GLN GLU GLU HIS LEU LYS GLU ILE
SEQRES 4 A 776 MET LYS HIS ILE VAL LYS ILE GLU VAL LYS GLY GLU GLU
SEQRES 5 A 776 ALA VAL LYS LYS GLU ALA ALA GLU LYS LEU LEU GLU LYS
SEQRES 6 A 776 VAL PRO SER ASP VAL LEU GLU MET TYR LYS ALA ILE GLY
SEQRES 7 A 776 GLY LYS ILE TYR ILE VAL ASP GLY ASP ILE THR LYS HIS
SEQRES 8 A 776 ILE SER LEU GLU ALA LEU SER GLU ASP LYS LYS LYS ILE
SEQRES 9 A 776 LYS ASP ILE TYR GLY LYS ASP ALA LEU LEU HIS GLU HIS
SEQRES 10 A 776 TYR VAL TYR ALA LYS GLU GLY TYR GLU PRO VAL LEU VAL
SEQRES 11 A 776 ILE GLN SER SER GLU ASP TYR VAL GLU ASN THR GLU LYS
SEQRES 12 A 776 ALA LEU ASN VAL TYR TYR GLU ILE GLY LYS ILE LEU SER
SEQRES 13 A 776 ARG ASP ILE LEU SER LYS ILE ASN GLN PRO TYR GLN LYS
SEQRES 14 A 776 PHE LEU ASP VAL LEU ASN THR ILE LYS ASN ALA SER ASP
SEQRES 15 A 776 SER ASP GLY GLN ASP LEU LEU PHE THR ASN GLN LEU LYS
SEQRES 16 A 776 GLU HIS PRO THR ASP PHE SER VAL GLU PHE LEU GLU GLN
SEQRES 17 A 776 ASN SER ASN GLU VAL GLN GLU VAL PHE ALA LYS ALA PHE
SEQRES 18 A 776 ALA TYR TYR ILE GLU PRO GLN HIS ARG ASP VAL LEU GLN
SEQRES 19 A 776 LEU TYR ALA PRO GLU ALA PHE ASN TYR MET ASP LYS PHE
SEQRES 20 A 776 ASN GLU GLN GLU ILE ASN LEU SER LEU GLU GLU LEU LYS
SEQRES 21 A 776 ASP GLN ARG MET LEU SER ARG TYR GLU LYS TRP GLU LYS
SEQRES 22 A 776 ILE LYS GLN HIS TYR GLN HIS TRP SER ASP SER LEU SER
SEQRES 23 A 776 GLU GLU GLY ARG GLY LEU LEU LYS LYS LEU GLN ILE PRO
SEQRES 24 A 776 ILE GLU PRO LYS LYS ASP ASP ILE ILE HIS SER LEU SER
SEQRES 25 A 776 GLN GLU GLU LYS GLU LEU LEU LYS ARG ILE GLN ILE ASP
SEQRES 26 A 776 SER SER ASP PHE LEU SER THR GLU GLU LYS GLU PHE LEU
SEQRES 27 A 776 LYS LYS LEU GLN ILE ASP ILE ARG ASP SER LEU SER GLU
SEQRES 28 A 776 GLU GLU LYS GLU LEU LEU ASN ARG ILE GLN VAL ASP SER
SEQRES 29 A 776 SER ASN PRO LEU SER GLU LYS GLU LYS GLU PHE LEU LYS
SEQRES 30 A 776 LYS LEU LYS LEU ASP ILE GLN PRO TYR ASP ILE ASN GLN
SEQRES 31 A 776 ARG LEU GLN ASP THR GLY GLY LEU ILE ASP SER PRO SER
SEQRES 32 A 776 ILE ASN LEU ASP VAL ARG LYS GLN TYR LYS ARG ASP ILE
SEQRES 33 A 776 GLN ASN ILE ASP ALA LEU LEU HIS GLN SER ILE GLY SER
SEQRES 34 A 776 THR LEU TYR ASN LYS ILE TYR LEU TYR GLU ASN MET ASN
SEQRES 35 A 776 ILE ASN ASN LEU THR ALA THR LEU GLY ALA ASP LEU VAL
SEQRES 36 A 776 ASP SER THR ASP ASN THR LYS ILE ASN ARG GLY ILE PHE
SEQRES 37 A 776 ASN GLU PHE LYS LYS ASN PHE LYS TYR SER ILE SER SER
SEQRES 38 A 776 ASN TYR MET ILE VAL ASP ILE ASN GLU ARG PRO ALA LEU
SEQRES 39 A 776 ASP ASN GLU ARG LEU LYS TRP ARG ILE GLN LEU SER PRO
SEQRES 40 A 776 ASP THR ARG ALA GLY TYR LEU GLU ASN GLY LYS LEU ILE
SEQRES 41 A 776 LEU GLN ARG ASN ILE GLY LEU GLU ILE LYS ASP VAL GLN
SEQRES 42 A 776 ILE ILE LYS GLN SER GLU LYS GLU TYR ILE ARG ILE ASP
SEQRES 43 A 776 ALA LYS VAL VAL PRO LYS SER LYS ILE ASP THR LYS ILE
SEQRES 44 A 776 GLN GLU ALA GLN LEU ASN ILE ASN GLN GLU TRP ASN LYS
SEQRES 45 A 776 ALA LEU GLY LEU PRO LYS TYR THR LYS LEU ILE THR PHE
SEQRES 46 A 776 ASN VAL HIS ASN ARG TYR ALA SER ASN ILE VAL GLU SER
SEQRES 47 A 776 ALA TYR LEU ILE LEU ASN GLU TRP LYS ASN ASN ILE GLN
SEQRES 48 A 776 SER ASP LEU ILE LYS LYS VAL THR ASN TYR LEU VAL ASP
SEQRES 49 A 776 GLY ASN GLY ARG PHE VAL PHE THR ASP ILE THR LEU PRO
SEQRES 50 A 776 ASN ILE ALA GLU GLN TYR THR HIS GLN ASP GLU ILE TYR
SEQRES 51 A 776 GLU GLN VAL HIS SER LYS GLY LEU TYR VAL PRO GLU SER
SEQRES 52 A 776 ARG SER ILE LEU LEU HIS GLY PRO SER LYS GLY VAL GLU
SEQRES 53 A 776 LEU ARG ASN ASP SER GLU GLY PHE ILE HIS CYS PHE GLY
SEQRES 54 A 776 HIS ALA VAL ASP ASP TYR ALA GLY TYR LEU LEU ASP LYS
SEQRES 55 A 776 ASN GLN SER ASP LEU VAL THR ASN SER LYS LYS PHE ILE
SEQRES 56 A 776 ASP ILE PHE LYS GLU GLU GLY SER ASN LEU THR SER TYR
SEQRES 57 A 776 GLY ARG THR ASN GLU ALA GLU PHE PHE ALA GLU ALA PHE
SEQRES 58 A 776 ARG LEU MET HIS SER THR ASP HIS ALA GLU ARG LEU LYS
SEQRES 59 A 776 VAL GLN LYS ASN ALA PRO LYS THR PHE GLN PHE ILE ASN
SEQRES 60 A 776 ASP GLN ILE LYS PHE ILE ILE ASN SER
SEQRES 1 B 776 ALA GLY GLY HIS GLY ASP VAL GLY MET HIS VAL LYS GLU
SEQRES 2 B 776 LYS GLU LYS ASN LYS ASP GLU ASN LYS ARG LYS ASP GLU
SEQRES 3 B 776 GLU ARG ASN LYS THR GLN GLU GLU HIS LEU LYS GLU ILE
SEQRES 4 B 776 MET LYS HIS ILE VAL LYS ILE GLU VAL LYS GLY GLU GLU
SEQRES 5 B 776 ALA VAL LYS LYS GLU ALA ALA GLU LYS LEU LEU GLU LYS
SEQRES 6 B 776 VAL PRO SER ASP VAL LEU GLU MET TYR LYS ALA ILE GLY
SEQRES 7 B 776 GLY LYS ILE TYR ILE VAL ASP GLY ASP ILE THR LYS HIS
SEQRES 8 B 776 ILE SER LEU GLU ALA LEU SER GLU ASP LYS LYS LYS ILE
SEQRES 9 B 776 LYS ASP ILE TYR GLY LYS ASP ALA LEU LEU HIS GLU HIS
SEQRES 10 B 776 TYR VAL TYR ALA LYS GLU GLY TYR GLU PRO VAL LEU VAL
SEQRES 11 B 776 ILE GLN SER SER GLU ASP TYR VAL GLU ASN THR GLU LYS
SEQRES 12 B 776 ALA LEU ASN VAL TYR TYR GLU ILE GLY LYS ILE LEU SER
SEQRES 13 B 776 ARG ASP ILE LEU SER LYS ILE ASN GLN PRO TYR GLN LYS
SEQRES 14 B 776 PHE LEU ASP VAL LEU ASN THR ILE LYS ASN ALA SER ASP
SEQRES 15 B 776 SER ASP GLY GLN ASP LEU LEU PHE THR ASN GLN LEU LYS
SEQRES 16 B 776 GLU HIS PRO THR ASP PHE SER VAL GLU PHE LEU GLU GLN
SEQRES 17 B 776 ASN SER ASN GLU VAL GLN GLU VAL PHE ALA LYS ALA PHE
SEQRES 18 B 776 ALA TYR TYR ILE GLU PRO GLN HIS ARG ASP VAL LEU GLN
SEQRES 19 B 776 LEU TYR ALA PRO GLU ALA PHE ASN TYR MET ASP LYS PHE
SEQRES 20 B 776 ASN GLU GLN GLU ILE ASN LEU SER LEU GLU GLU LEU LYS
SEQRES 21 B 776 ASP GLN ARG MET LEU SER ARG TYR GLU LYS TRP GLU LYS
SEQRES 22 B 776 ILE LYS GLN HIS TYR GLN HIS TRP SER ASP SER LEU SER
SEQRES 23 B 776 GLU GLU GLY ARG GLY LEU LEU LYS LYS LEU GLN ILE PRO
SEQRES 24 B 776 ILE GLU PRO LYS LYS ASP ASP ILE ILE HIS SER LEU SER
SEQRES 25 B 776 GLN GLU GLU LYS GLU LEU LEU LYS ARG ILE GLN ILE ASP
SEQRES 26 B 776 SER SER ASP PHE LEU SER THR GLU GLU LYS GLU PHE LEU
SEQRES 27 B 776 LYS LYS LEU GLN ILE ASP ILE ARG ASP SER LEU SER GLU
SEQRES 28 B 776 GLU GLU LYS GLU LEU LEU ASN ARG ILE GLN VAL ASP SER
SEQRES 29 B 776 SER ASN PRO LEU SER GLU LYS GLU LYS GLU PHE LEU LYS
SEQRES 30 B 776 LYS LEU LYS LEU ASP ILE GLN PRO TYR ASP ILE ASN GLN
SEQRES 31 B 776 ARG LEU GLN ASP THR GLY GLY LEU ILE ASP SER PRO SER
SEQRES 32 B 776 ILE ASN LEU ASP VAL ARG LYS GLN TYR LYS ARG ASP ILE
SEQRES 33 B 776 GLN ASN ILE ASP ALA LEU LEU HIS GLN SER ILE GLY SER
SEQRES 34 B 776 THR LEU TYR ASN LYS ILE TYR LEU TYR GLU ASN MET ASN
SEQRES 35 B 776 ILE ASN ASN LEU THR ALA THR LEU GLY ALA ASP LEU VAL
SEQRES 36 B 776 ASP SER THR ASP ASN THR LYS ILE ASN ARG GLY ILE PHE
SEQRES 37 B 776 ASN GLU PHE LYS LYS ASN PHE LYS TYR SER ILE SER SER
SEQRES 38 B 776 ASN TYR MET ILE VAL ASP ILE ASN GLU ARG PRO ALA LEU
SEQRES 39 B 776 ASP ASN GLU ARG LEU LYS TRP ARG ILE GLN LEU SER PRO
SEQRES 40 B 776 ASP THR ARG ALA GLY TYR LEU GLU ASN GLY LYS LEU ILE
SEQRES 41 B 776 LEU GLN ARG ASN ILE GLY LEU GLU ILE LYS ASP VAL GLN
SEQRES 42 B 776 ILE ILE LYS GLN SER GLU LYS GLU TYR ILE ARG ILE ASP
SEQRES 43 B 776 ALA LYS VAL VAL PRO LYS SER LYS ILE ASP THR LYS ILE
SEQRES 44 B 776 GLN GLU ALA GLN LEU ASN ILE ASN GLN GLU TRP ASN LYS
SEQRES 45 B 776 ALA LEU GLY LEU PRO LYS TYR THR LYS LEU ILE THR PHE
SEQRES 46 B 776 ASN VAL HIS ASN ARG TYR ALA SER ASN ILE VAL GLU SER
SEQRES 47 B 776 ALA TYR LEU ILE LEU ASN GLU TRP LYS ASN ASN ILE GLN
SEQRES 48 B 776 SER ASP LEU ILE LYS LYS VAL THR ASN TYR LEU VAL ASP
SEQRES 49 B 776 GLY ASN GLY ARG PHE VAL PHE THR ASP ILE THR LEU PRO
SEQRES 50 B 776 ASN ILE ALA GLU GLN TYR THR HIS GLN ASP GLU ILE TYR
SEQRES 51 B 776 GLU GLN VAL HIS SER LYS GLY LEU TYR VAL PRO GLU SER
SEQRES 52 B 776 ARG SER ILE LEU LEU HIS GLY PRO SER LYS GLY VAL GLU
SEQRES 53 B 776 LEU ARG ASN ASP SER GLU GLY PHE ILE HIS CYS PHE GLY
SEQRES 54 B 776 HIS ALA VAL ASP ASP TYR ALA GLY TYR LEU LEU ASP LYS
SEQRES 55 B 776 ASN GLN SER ASP LEU VAL THR ASN SER LYS LYS PHE ILE
SEQRES 56 B 776 ASP ILE PHE LYS GLU GLU GLY SER ASN LEU THR SER TYR
SEQRES 57 B 776 GLY ARG THR ASN GLU ALA GLU PHE PHE ALA GLU ALA PHE
SEQRES 58 B 776 ARG LEU MET HIS SER THR ASP HIS ALA GLU ARG LEU LYS
SEQRES 59 B 776 VAL GLN LYS ASN ALA PRO LYS THR PHE GLN PHE ILE ASN
SEQRES 60 B 776 ASP GLN ILE LYS PHE ILE ILE ASN SER
HET ZN A9001 1
HET GM6 A1001 28
HET ZN B9002 1
HET GM6 B2001 28
HETNAM ZN ZINC ION
HETNAM GM6 3-(N-HYDROXYCARBOXAMIDO)-2-ISOBUTYLPROPANOYL-TRP-
HETNAM 2 GM6 METHYLAMIDE
HETSYN GM6 GM6001
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 GM6 2(C20 H28 N4 O4)
HELIX 1 1 LYS A 30 ILE A 43 1 14
HELIX 2 2 ALA A 53 GLU A 64 1 12
HELIX 3 3 PRO A 67 ILE A 77 1 11
HELIX 4 4 ILE A 92 LEU A 97 5 6
HELIX 5 5 HIS A 115 HIS A 117 5 3
HELIX 6 6 GLU A 135 GLU A 139 5 5
HELIX 7 7 ASN A 140 ASP A 158 1 19
HELIX 8 8 ILE A 159 ASN A 164 5 6
HELIX 9 9 TYR A 167 ALA A 180 1 14
HELIX 10 10 SER A 183 PHE A 190 1 8
HELIX 11 11 THR A 191 GLU A 196 1 6
HELIX 12 12 SER A 202 ASN A 209 1 8
HELIX 13 13 ASN A 209 GLU A 226 1 18
HELIX 14 14 HIS A 229 ALA A 237 1 9
HELIX 15 15 ALA A 237 GLN A 250 1 14
HELIX 16 16 GLU A 251 GLN A 262 1 12
HELIX 17 17 ARG A 263 SER A 284 1 22
HELIX 18 18 SER A 286 LEU A 296 1 11
HELIX 19 19 LYS A 303 SER A 310 1 8
HELIX 20 20 GLU A 314 LYS A 320 1 7
HELIX 21 21 ARG A 321 ILE A 322 5 2
HELIX 22 22 GLN A 323 SER A 327 5 5
HELIX 23 23 SER A 331 ILE A 343 1 13
HELIX 24 24 SER A 350 GLN A 361 1 12
HELIX 25 25 SER A 369 ILE A 383 1 15
HELIX 26 26 ASP A 387 GLY A 396 1 10
HELIX 27 27 ASN A 405 LEU A 423 1 19
HELIX 28 28 ASN A 442 LEU A 446 5 5
HELIX 29 29 THR A 447 ALA A 452 1 6
HELIX 30 30 ASN A 464 LYS A 473 1 10
HELIX 31 31 PRO A 551 GLY A 575 1 25
HELIX 32 32 TYR A 591 ASN A 608 1 18
HELIX 33 33 GLN A 611 GLY A 625 1 15
HELIX 34 34 THR A 635 ASN A 638 5 4
HELIX 35 35 ILE A 639 THR A 644 1 6
HELIX 36 36 GLU A 648 GLN A 652 5 5
HELIX 37 37 ASN A 679 ASP A 701 1 23
HELIX 38 38 SER A 711 LYS A 719 1 9
HELIX 39 39 THR A 726 THR A 731 5 6
HELIX 40 40 ASN A 732 MET A 744 1 13
HELIX 41 41 ASP A 748 ALA A 759 1 12
HELIX 42 42 ALA A 759 ASN A 775 1 17
HELIX 43 43 GLU B 33 ILE B 43 1 11
HELIX 44 44 ALA B 53 GLU B 64 1 12
HELIX 45 45 PRO B 67 ILE B 77 1 11
HELIX 46 46 ASP B 87 HIS B 91 5 5
HELIX 47 47 SER B 98 LYS B 101 5 4
HELIX 48 48 ASN B 140 ASP B 158 1 19
HELIX 49 49 ILE B 159 ASN B 164 5 6
HELIX 50 50 TYR B 167 ASN B 179 1 13
HELIX 51 51 SER B 183 PHE B 190 1 8
HELIX 52 52 THR B 191 GLU B 196 1 6
HELIX 53 53 SER B 202 ASN B 209 1 8
HELIX 54 54 ASN B 209 GLU B 226 1 18
HELIX 55 55 GLU B 226 ALA B 237 1 12
HELIX 56 56 ALA B 237 GLN B 250 1 14
HELIX 57 57 GLU B 251 ASP B 261 1 11
HELIX 58 58 ARG B 263 TYR B 278 1 16
HELIX 59 59 TYR B 278 LEU B 285 1 8
HELIX 60 60 SER B 286 ILE B 298 1 13
HELIX 61 61 LYS B 303 HIS B 309 1 7
HELIX 62 62 SER B 312 ILE B 322 1 11
HELIX 63 63 GLN B 323 SER B 327 5 5
HELIX 64 64 SER B 331 ASP B 347 1 17
HELIX 65 65 LEU B 349 LEU B 357 1 9
HELIX 66 66 SER B 369 ILE B 383 1 15
HELIX 67 67 ASP B 387 GLY B 396 1 10
HELIX 68 68 ASN B 405 LEU B 423 1 19
HELIX 69 69 ILE B 443 ALA B 452 1 10
HELIX 70 70 ASN B 464 ASN B 474 1 11
HELIX 71 71 PRO B 551 LEU B 574 1 24
HELIX 72 72 TYR B 591 ASN B 609 1 19
HELIX 73 73 GLN B 611 GLY B 625 1 15
HELIX 74 74 THR B 635 ASN B 638 5 4
HELIX 75 75 ILE B 639 THR B 644 1 6
HELIX 76 76 GLU B 648 GLN B 652 5 5
HELIX 77 77 ASN B 679 LEU B 700 1 22
HELIX 78 78 LEU B 707 ASN B 710 5 4
HELIX 79 79 SER B 711 GLY B 722 1 12
HELIX 80 80 SER B 727 THR B 731 5 5
HELIX 81 81 ASN B 732 HIS B 745 1 14
HELIX 82 82 ASP B 748 ALA B 759 1 12
HELIX 83 83 ALA B 759 ASN B 775 1 17
SHEET 1 A 4 VAL A 44 GLU A 47 0
SHEET 2 A 4 LYS A 80 VAL A 84 1 O ILE A 83 N GLU A 47
SHEET 3 A 4 VAL A 128 GLN A 132 1 O LEU A 129 N TYR A 82
SHEET 4 A 4 VAL A 119 LYS A 122 -1 N TYR A 120 O VAL A 130
SHEET 1 B 2 LYS A 103 LYS A 105 0
SHEET 2 B 2 ASP A 111 LEU A 113 -1 O ALA A 112 N ILE A 104
SHEET 1 C 5 TYR A 436 MET A 441 0
SHEET 2 C 5 LEU A 499 GLN A 504 -1 O TRP A 501 N GLU A 439
SHEET 3 C 5 LYS A 540 VAL A 550 1 O ILE A 545 N ARG A 502
SHEET 4 C 5 ILE A 525 GLN A 537 -1 N ILE A 535 O TYR A 542
SHEET 5 C 5 TYR A 477 SER A 480 -1 N SER A 478 O LEU A 527
SHEET 1 D 3 ILE A 485 ASP A 487 0
SHEET 2 D 3 LYS A 518 LEU A 521 -1 O LEU A 519 N VAL A 486
SHEET 3 D 3 ALA A 511 LEU A 514 -1 N LEU A 514 O LYS A 518
SHEET 1 E 4 ILE A 583 ASN A 586 0
SHEET 2 E 4 PHE A 629 THR A 632 1 O PHE A 629 N THR A 584
SHEET 3 E 4 SER A 665 HIS A 669 1 O LEU A 668 N VAL A 630
SHEET 4 E 4 GLY A 657 VAL A 660 -1 N LEU A 658 O LEU A 667
SHEET 1 F 4 VAL B 44 LYS B 45 0
SHEET 2 F 4 ILE B 81 VAL B 84 1 O ILE B 81 N LYS B 45
SHEET 3 F 4 VAL B 128 GLN B 132 1 O ILE B 131 N TYR B 82
SHEET 4 F 4 VAL B 119 LYS B 122 -1 N TYR B 120 O VAL B 130
SHEET 1 G 2 LYS B 103 LYS B 105 0
SHEET 2 G 2 ASP B 111 LEU B 113 -1 O ALA B 112 N ILE B 104
SHEET 1 H 5 TYR B 436 ASN B 442 0
SHEET 2 H 5 GLU B 497 GLN B 504 -1 O TRP B 501 N GLU B 439
SHEET 3 H 5 LYS B 540 VAL B 550 1 O ILE B 543 N LYS B 500
SHEET 4 H 5 ILE B 525 GLN B 537 -1 N ASP B 531 O ASP B 546
SHEET 5 H 5 TYR B 477 SER B 480 -1 N SER B 478 O LEU B 527
SHEET 1 I 3 ILE B 485 ASP B 487 0
SHEET 2 I 3 LYS B 518 LEU B 521 -1 O LEU B 519 N VAL B 486
SHEET 3 I 3 ALA B 511 LEU B 514 -1 N LEU B 514 O LYS B 518
SHEET 1 J 4 ILE B 583 ASN B 586 0
SHEET 2 J 4 PHE B 629 THR B 632 1 O PHE B 631 N THR B 584
SHEET 3 J 4 SER B 665 HIS B 669 1 O LEU B 668 N VAL B 630
SHEET 4 J 4 GLY B 657 VAL B 660 -1 N VAL B 660 O SER B 665
LINK NE2 HIS A 686 ZN ZN A9001 1555 1555 2.46
LINK NE2 HIS A 690 ZN ZN A9001 1555 1555 2.28
LINK OE1 GLU A 735 ZN ZN A9001 1555 1555 2.46
LINK OAG GM6 A1001 ZN ZN A9001 1555 1555 2.74
LINK OAE GM6 A1001 ZN ZN A9001 1555 1555 2.38
LINK NE2 HIS B 686 ZN ZN B9002 1555 1555 2.32
LINK NE2 HIS B 690 ZN ZN B9002 1555 1555 2.25
LINK OE1 GLU B 735 ZN ZN B9002 1555 1555 2.23
LINK OAE GM6 B2001 ZN ZN B9002 1555 1555 2.23
LINK OAG GM6 B2001 ZN ZN B9002 1555 1555 2.46
CISPEP 1 GLN A 165 PRO A 166 0 0.01
CISPEP 2 GLN B 165 PRO B 166 0 -0.25
SITE 1 AC1 4 HIS A 686 HIS A 690 GLU A 735 GM6 A1001
SITE 1 AC2 4 HIS B 686 HIS B 690 GLU B 735 GM6 B2001
SITE 1 AC3 12 ASP A 328 HIS A 654 SER A 655 LYS A 656
SITE 2 AC3 12 GLY A 657 GLY A 674 VAL A 675 LEU A 677
SITE 3 AC3 12 HIS A 690 TYR A 728 GLU A 735 ZN A9001
SITE 1 AC4 12 HIS B 654 SER B 655 LYS B 656 GLY B 657
SITE 2 AC4 12 GLY B 674 VAL B 675 LEU B 677 HIS B 686
SITE 3 AC4 12 HIS B 690 TYR B 728 GLU B 735 ZN B9002
CRYST1 96.700 137.400 98.300 90.00 98.00 90.00 P 1 21 1 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 0.010341 0.000000 0.001453 0.00000
SCALE2 0.000000 0.007278 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010273 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
