HEADER HYDROLASE 10-AUG-12 4GK8
TITLE CRYSTAL STRUCTURE OF HISTIDINOL PHOSPHATE PHOSPHATASE (HISK) FROM
TITLE 2 LACTOCOCCUS LACTIS SUBSP. LACTIS IL1403 COMPLEXED WITH ZN AND L-
TITLE 3 HISTIDINOL ARSENATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTIDINOL-PHOSPHATASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HOLPASE;
COMPND 5 EC: 3.1.3.15;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOCOCCUS LACTIS SUBSP. LACTIS;
SOURCE 3 ORGANISM_TAXID: 272623;
SOURCE 4 STRAIN: IL1403;
SOURCE 5 GENE: HISK, LL1216, L37351;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHP FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.FEDOROV,E.V.FEDOROV,S.GHODGE,F.M.RAUSHEL,S.C.ALMO
REVDAT 2 13-SEP-23 4GK8 1 REMARK SEQADV LINK
REVDAT 1 27-FEB-13 4GK8 0
JRNL AUTH S.V.GHODGE,A.A.FEDOROV,E.V.FEDOROV,B.HILLERICH,R.SEIDEL,
JRNL AUTH 2 S.C.ALMO,F.M.RAUSHEL
JRNL TITL STRUCTURAL AND MECHANISTIC CHARACTERIZATION OF L-HISTIDINOL
JRNL TITL 2 PHOSPHATE PHOSPHATASE FROM THE POLYMERASE AND HISTIDINOL
JRNL TITL 3 PHOSPHATASE FAMILY OF PROTEINS.
JRNL REF BIOCHEMISTRY V. 52 1101 2013
JRNL REFN ISSN 0006-2960
JRNL PMID 23327428
JRNL DOI 10.1021/BI301496P
REMARK 2
REMARK 2 RESOLUTION. 1.93 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.31
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 25741
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1314
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 43.3219 - 4.0196 1.00 2911 146 0.1456 0.1655
REMARK 3 2 4.0196 - 3.1908 1.00 2767 146 0.1493 0.1756
REMARK 3 3 3.1908 - 2.7875 1.00 2733 150 0.1778 0.2051
REMARK 3 4 2.7875 - 2.5327 1.00 2709 147 0.1802 0.2190
REMARK 3 5 2.5327 - 2.3512 1.00 2700 160 0.1667 0.1916
REMARK 3 6 2.3512 - 2.2126 1.00 2700 146 0.1644 0.2389
REMARK 3 7 2.2126 - 2.1018 1.00 2696 128 0.1552 0.1907
REMARK 3 8 2.1018 - 2.0103 1.00 2698 149 0.1666 0.2201
REMARK 3 9 2.0103 - 1.9329 0.94 2513 142 0.1810 0.2174
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.350
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.007 2267
REMARK 3 ANGLE : 1.082 3047
REMARK 3 CHIRALITY : 0.078 319
REMARK 3 PLANARITY : 0.005 393
REMARK 3 DIHEDRAL : 15.714 843
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 4GK8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1000074287.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUN-12
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 : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25741
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.933
REMARK 200 RESOLUTION RANGE LOW (A) : 43.311
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: PHENIX
REMARK 200 STARTING MODEL: 4GC3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% SODIUM CHLORIDE, 0.1M IMIDAZOLE,
REMARK 280 0.5 MM ZINC CHLORIDE, 100 MM SODIUM ARSENATE, 50MM L-
REMARK 280 HISTIDINOL.HCL PH 8.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 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 -X+1/2,Y+1/2,-Z
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 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 -1.000000 0.000000 0.000000 42.93000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.31100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.93000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.31100
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 MET A 1
REMARK 465 ASN A 265
REMARK 465 LYS A 266
REMARK 465 LYS A 267
REMARK 465 SER A 268
REMARK 465 ILE A 269
REMARK 465 LYS A 270
REMARK 465 GLU A 271
REMARK 465 LYS A 272
REMARK 465 LEU A 273
REMARK 465 ALA A 274
REMARK 465 ALA A 275
REMARK 465 ALA A 276
REMARK 465 LEU A 277
REMARK 465 GLU A 278
REMARK 465 HIS A 279
REMARK 465 HIS A 280
REMARK 465 HIS A 281
REMARK 465 HIS A 282
REMARK 465 HIS A 283
REMARK 465 HIS A 284
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 HIS A 9 105.90 -160.94
REMARK 500 PHE A 52 75.75 -103.89
REMARK 500 HIS A 154 80.32 18.95
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 303 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 9 NE2
REMARK 620 2 HIS A 11 NE2 99.4
REMARK 620 3 GLU A 81 OE1 88.5 90.4
REMARK 620 4 ASP A 228 OD1 83.1 95.7 170.3
REMARK 620 5 GK8 A 305 O3 169.4 86.8 100.1 87.8
REMARK 620 6 HOH A 575 O 92.3 168.0 87.3 88.2 82.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 17 OD2
REMARK 620 2 HIS A 42 NE2 106.9
REMARK 620 3 HIS A 230 NE2 102.2 130.4
REMARK 620 4 GK8 A 305 O4 91.7 106.6 111.7
REMARK 620 5 GK8 A 305 O3 162.2 79.1 85.1 70.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 304 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 32 NE2
REMARK 620 2 HIS A 240 NE2 111.9
REMARK 620 3 IMD A 309 N3 101.6 114.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 81 OE2
REMARK 620 2 HIS A 109 NE2 94.1
REMARK 620 3 HIS A 154 NE2 101.7 102.6
REMARK 620 4 GK8 A 305 O2 132.1 84.7 125.4
REMARK 620 5 HOH A 575 O 84.8 163.1 94.2 83.6
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GK8 A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 310
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GC3 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN APO FORM
DBREF 4GK8 A 4 271 UNP Q02150 HIS9_LACLA 2 269
SEQADV 4GK8 MET A 1 UNP Q02150 EXPRESSION TAG
SEQADV 4GK8 SER A 2 UNP Q02150 EXPRESSION TAG
SEQADV 4GK8 LEU A 3 UNP Q02150 EXPRESSION TAG
SEQADV 4GK8 GLN A 65 UNP Q02150 ARG 63 ENGINEERED MUTATION
SEQADV 4GK8 THR A 127 UNP Q02150 ILE 125 ENGINEERED MUTATION
SEQADV 4GK8 ARG A 217 UNP Q02150 LYS 215 ENGINEERED MUTATION
SEQADV 4GK8 LYS A 272 UNP Q02150 EXPRESSION TAG
SEQADV 4GK8 LEU A 273 UNP Q02150 EXPRESSION TAG
SEQADV 4GK8 ALA A 274 UNP Q02150 EXPRESSION TAG
SEQADV 4GK8 ALA A 275 UNP Q02150 EXPRESSION TAG
SEQADV 4GK8 ALA A 276 UNP Q02150 EXPRESSION TAG
SEQADV 4GK8 LEU A 277 UNP Q02150 EXPRESSION TAG
SEQADV 4GK8 GLU A 278 UNP Q02150 EXPRESSION TAG
SEQADV 4GK8 HIS A 279 UNP Q02150 EXPRESSION TAG
SEQADV 4GK8 HIS A 280 UNP Q02150 EXPRESSION TAG
SEQADV 4GK8 HIS A 281 UNP Q02150 EXPRESSION TAG
SEQADV 4GK8 HIS A 282 UNP Q02150 EXPRESSION TAG
SEQADV 4GK8 HIS A 283 UNP Q02150 EXPRESSION TAG
SEQADV 4GK8 HIS A 284 UNP Q02150 EXPRESSION TAG
SEQRES 1 A 284 MET SER LEU LYS LYS LEU ASP TYR HIS PHE HIS SER HIS
SEQRES 2 A 284 PHE SER ALA ASP SER GLU GLU LEU PRO ARG LYS HIS VAL
SEQRES 3 A 284 THR GLU ALA ILE ALA HIS GLY LEU GLU GLU ILE CYS PHE
SEQRES 4 A 284 THR GLU HIS ARG ASP PHE TYR PHE PRO GLY MET ASP PHE
SEQRES 5 A 284 SER LEU ASN LEU PRO GLU TYR PHE GLN GLU ILE ASN GLN
SEQRES 6 A 284 LEU GLN ALA GLU PHE LYS ASP LYS ILE LYS ILE LYS ILE
SEQRES 7 A 284 GLY LEU GLU MET GLY ILE ASP LEU ARG PHE LYS SER GLU
SEQRES 8 A 284 ILE ASN GLN PHE ILE ASP SER ALA PRO PHE ASP PHE VAL
SEQRES 9 A 284 ILE ALA SER VAL HIS GLU ILE GLY ASP ILE GLU VAL TYR
SEQRES 10 A 284 ASP GLY THR GLU PHE TYR LEU GLN LYS THR LYS GLU GLU
SEQRES 11 A 284 ALA GLN ARG GLU TYR LEU LEU ALA CYS LEU ASP VAL VAL
SEQRES 12 A 284 GLN ASN PHE GLU ASN TYR ASN SER PHE GLY HIS LEU ASP
SEQRES 13 A 284 TYR VAL ALA ARG TYR GLY PRO TYR THR ASP LYS SER ILE
SEQRES 14 A 284 LYS PHE ALA GLU ASN ARG GLU ILE LEU PHE GLU ILE LEU
SEQRES 15 A 284 ARG ALA LEU ALA SER LYS GLU LYS ALA LEU GLU ILE ASN
SEQRES 16 A 284 THR ARG LEU PHE ASP ASP PRO LYS THR GLU GLN PHE TYR
SEQRES 17 A 284 SER ASP LEU LEU ILE ASN PHE LYS ARG LEU GLY GLY LYS
SEQRES 18 A 284 PHE ILE THR LEU GLY THR ASP SER HIS ILE ALA LYS ARG
SEQRES 19 A 284 ASP TRP LEU SER ILE HIS LYS ALA ARG THR LEU ILE LYS
SEQRES 20 A 284 LYS ALA GLY PHE HIS GLU LEU ALA THR PHE SER GLY MET
SEQRES 21 A 284 LYS ILE ASP LYS ASN LYS LYS SER ILE LYS GLU LYS LEU
SEQRES 22 A 284 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET ZN A 301 1
HET ZN A 302 1
HET ZN A 303 1
HET ZN A 304 1
HET GK8 A 305 14
HET CL A 306 1
HET CL A 307 1
HET CL A 308 1
HET IMD A 309 5
HET PEG A 310 7
HETNAM ZN ZINC ION
HETNAM GK8 {[(2S)-2-AMINO-3-(1H-IMIDAZOL-5-YL)
HETNAM 2 GK8 PROPYL]OXY}(TRIHYDROXY)-LAMBDA~5~-ARSANYL
HETNAM CL CHLORIDE ION
HETNAM IMD IMIDAZOLE
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 2 ZN 4(ZN 2+)
FORMUL 6 GK8 C6 H13 AS N3 O4
FORMUL 7 CL 3(CL 1-)
FORMUL 10 IMD C3 H5 N2 1+
FORMUL 11 PEG C4 H10 O3
FORMUL 12 HOH *181(H2 O)
HELIX 1 1 LEU A 21 GLY A 33 1 13
HELIX 2 2 ASN A 55 PHE A 70 1 16
HELIX 3 3 ASP A 85 ARG A 87 5 3
HELIX 4 4 PHE A 88 SER A 98 1 11
HELIX 5 5 THR A 120 LEU A 124 5 5
HELIX 6 6 THR A 127 PHE A 146 1 20
HELIX 7 7 ASP A 156 TYR A 161 5 6
HELIX 8 8 PHE A 171 GLU A 173 5 3
HELIX 9 9 ASN A 174 LYS A 188 1 15
HELIX 10 10 ASP A 201 LEU A 218 1 18
HELIX 11 11 ASP A 235 ALA A 249 1 15
SHEET 1 A 7 LEU A 6 ASP A 7 0
SHEET 2 A 7 GLU A 36 ARG A 43 1 O CYS A 38 N ASP A 7
SHEET 3 A 7 LYS A 75 GLY A 83 1 O LYS A 77 N ILE A 37
SHEET 4 A 7 PHE A 103 SER A 107 1 O ILE A 105 N MET A 82
SHEET 5 A 7 SER A 151 PHE A 152 1 O SER A 151 N ALA A 106
SHEET 6 A 7 ALA A 191 ASN A 195 1 O ALA A 191 N PHE A 152
SHEET 7 A 7 ILE A 223 GLY A 226 1 O THR A 224 N ILE A 194
SHEET 1 B 2 GLU A 110 ILE A 111 0
SHEET 2 B 2 ILE A 114 GLU A 115 -1 O ILE A 114 N ILE A 111
SHEET 1 C 2 PHE A 257 SER A 258 0
SHEET 2 C 2 LYS A 261 ILE A 262 -1 O LYS A 261 N SER A 258
LINK NE2 HIS A 9 ZN ZN A 303 1555 1555 2.13
LINK NE2 HIS A 11 ZN ZN A 303 1555 1555 2.16
LINK OD2 ASP A 17 ZN ZN A 302 1555 1555 2.09
LINK NE2 HIS A 32 ZN ZN A 304 1555 1555 2.01
LINK NE2 HIS A 42 ZN ZN A 302 1555 1555 2.08
LINK OE2 GLU A 81 ZN ZN A 301 1555 1555 2.00
LINK OE1 GLU A 81 ZN ZN A 303 1555 1555 2.21
LINK NE2 HIS A 109 ZN ZN A 301 1555 1555 2.08
LINK NE2 HIS A 154 ZN ZN A 301 1555 1555 2.13
LINK OD1 ASP A 228 ZN ZN A 303 1555 1555 2.25
LINK NE2 HIS A 230 ZN ZN A 302 1555 1555 2.10
LINK NE2 HIS A 240 ZN ZN A 304 1555 1555 2.04
LINK ZN ZN A 301 O2 GK8 A 305 1555 1555 1.94
LINK ZN ZN A 301 O HOH A 575 1555 1555 2.06
LINK ZN ZN A 302 O4 GK8 A 305 1555 1555 2.15
LINK ZN ZN A 302 O3 GK8 A 305 1555 1555 2.69
LINK ZN ZN A 303 O3 GK8 A 305 1555 1555 1.84
LINK ZN ZN A 303 O HOH A 575 1555 1555 2.11
LINK ZN ZN A 304 N3 IMD A 309 1555 1555 2.01
SITE 1 AC1 6 GLU A 81 HIS A 109 HIS A 154 ZN A 303
SITE 2 AC1 6 GK8 A 305 HOH A 575
SITE 1 AC2 4 ASP A 17 HIS A 42 HIS A 230 GK8 A 305
SITE 1 AC3 7 HIS A 9 HIS A 11 GLU A 81 ASP A 228
SITE 2 AC3 7 ZN A 301 GK8 A 305 HOH A 575
SITE 1 AC4 4 HIS A 32 HIS A 240 CL A 306 IMD A 309
SITE 1 AC5 18 HIS A 11 ASP A 17 HIS A 42 GLU A 81
SITE 2 AC5 18 HIS A 109 GLU A 115 HIS A 154 TYR A 157
SITE 3 AC5 18 ARG A 160 ARG A 197 ASP A 228 HIS A 230
SITE 4 AC5 18 ZN A 301 ZN A 302 ZN A 303 HOH A 446
SITE 5 AC5 18 HOH A 557 HOH A 575
SITE 1 AC6 4 HIS A 32 HIS A 240 ZN A 304 IMD A 309
SITE 1 AC7 3 ARG A 43 PHE A 45 TYR A 46
SITE 1 AC8 3 LYS A 89 ASN A 93 GLU A 147
SITE 1 AC9 9 LYS A 5 HIS A 32 TYR A 46 ARG A 87
SITE 2 AC9 9 PHE A 88 ASP A 113 HIS A 240 ZN A 304
SITE 3 AC9 9 CL A 306
SITE 1 BC1 2 PHE A 60 SER A 98
CRYST1 85.860 86.622 45.093 90.00 90.00 90.00 P 21 21 2 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 0.011647 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011544 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022176 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
