HEADER HYDROLASE 31-DEC-09 3L8E
TITLE CRYSTAL STRUCTURE OF APO FORM OF D,D-HEPTOSE 1.7-BISPHOSPHATE
TITLE 2 PHOSPHATASE FROM E. COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D,D-HEPTOSE 1,7-BISPHOSPHATE PHOSPHATASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: D-GLYCERO-D-MANNO-HEPTOSE 1,7-BISPHOSPHATE PHOSPHATASE;
COMPND 5 EC: 3.1.3.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: B0200, GMHB, JW0196, YAED;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B-834;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3
KEYWDS HAD SUPERFAMILY, GMHB, D-GLYCERO-D-MANNO-HEPTOSE-1, 7-BISPHOSPHATE
KEYWDS 2 PHOSPHATASE, CARBOHYDRATE METABOLISM, CYTOPLASM, HYDROLASE,
KEYWDS 3 LIPOPOLYSACCHARIDE BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR H.NGUYEN,E.PEISACH,K.N.ALLEN
REVDAT 4 21-FEB-24 3L8E 1 REMARK LINK
REVDAT 3 01-NOV-17 3L8E 1 REMARK
REVDAT 2 23-FEB-10 3L8E 1 JRNL
REVDAT 1 02-FEB-10 3L8E 0
JRNL AUTH H.H.NGUYEN,L.WANG,H.HUANG,E.PEISACH,D.DUNAWAY-MARIANO,
JRNL AUTH 2 K.N.ALLEN
JRNL TITL STRUCTURAL DETERMINANTS OF SUBSTRATE RECOGNITION IN THE HAD
JRNL TITL 2 SUPERFAMILY MEMBER
JRNL TITL 3 D-GLYCERO-D-MANNO-HEPTOSE-1,7-BISPHOSPHATE PHOSPHATASE
JRNL TITL 4 (GMHB) .
JRNL REF BIOCHEMISTRY V. 49 1082 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 20050614
JRNL DOI 10.1021/BI902019Q
REMARK 2
REMARK 2 RESOLUTION. 1.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.5_2
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) : 1.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.11
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 76862
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.810
REMARK 3 FREE R VALUE TEST SET COUNT : 7540
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 25.1083 - 5.0823 0.99 2392 280 0.1931 0.2262
REMARK 3 2 5.0823 - 4.0394 1.00 2482 218 0.1530 0.2044
REMARK 3 3 4.0394 - 3.5304 0.99 2376 322 0.1492 0.1668
REMARK 3 4 3.5304 - 3.2083 1.00 2403 261 0.1469 0.1738
REMARK 3 5 3.2083 - 2.9787 0.99 2497 230 0.1644 0.1979
REMARK 3 6 2.9787 - 2.8034 0.99 2430 240 0.1630 0.2013
REMARK 3 7 2.8034 - 2.6631 0.99 2439 232 0.1698 0.2353
REMARK 3 8 2.6631 - 2.5473 0.99 2433 277 0.1746 0.2423
REMARK 3 9 2.5473 - 2.4493 0.98 2359 284 0.1728 0.2225
REMARK 3 10 2.4493 - 2.3649 0.98 2380 250 0.1686 0.2018
REMARK 3 11 2.3649 - 2.2910 0.97 2352 292 0.1618 0.2090
REMARK 3 12 2.2910 - 2.2255 0.97 2384 236 0.1594 0.1982
REMARK 3 13 2.2255 - 2.1670 0.97 2313 290 0.1544 0.1873
REMARK 3 14 2.1670 - 2.1141 0.96 2387 252 0.1558 0.2050
REMARK 3 15 2.1141 - 2.0661 0.96 2258 284 0.1632 0.2066
REMARK 3 16 2.0661 - 2.0222 0.96 2355 285 0.1563 0.1850
REMARK 3 17 2.0222 - 1.9817 0.97 2383 236 0.1574 0.2316
REMARK 3 18 1.9817 - 1.9443 0.96 2312 264 0.1761 0.2329
REMARK 3 19 1.9443 - 1.9096 0.94 2250 282 0.1727 0.2157
REMARK 3 20 1.9096 - 1.8773 0.94 2298 257 0.1659 0.2563
REMARK 3 21 1.8773 - 1.8470 0.92 2192 270 0.1757 0.2180
REMARK 3 22 1.8470 - 1.8186 0.93 2303 249 0.1707 0.2240
REMARK 3 23 1.8186 - 1.7919 0.90 2206 201 0.1831 0.2073
REMARK 3 24 1.7919 - 1.7666 0.91 2308 211 0.1861 0.1978
REMARK 3 25 1.7666 - 1.7428 0.90 2171 250 0.1862 0.2434
REMARK 3 26 1.7428 - 1.7201 0.90 2161 239 0.1913 0.2329
REMARK 3 27 1.7201 - 1.6986 0.86 2127 218 0.2023 0.2542
REMARK 3 28 1.6986 - 1.6782 0.88 2158 198 0.2143 0.2514
REMARK 3 29 1.6782 - 1.6587 0.84 2081 224 0.2208 0.2481
REMARK 3 30 1.6587 - 1.6400 0.88 2132 208 0.2190 0.2555
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 : 0.42
REMARK 3 B_SOL : 44.49
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.660
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.58600
REMARK 3 B22 (A**2) : -3.08600
REMARK 3 B33 (A**2) : 3.67200
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 : 0.006 2958
REMARK 3 ANGLE : 1.065 4013
REMARK 3 CHIRALITY : 0.069 442
REMARK 3 PLANARITY : 0.005 529
REMARK 3 DIHEDRAL : 18.031 1073
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 3L8E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JAN-10.
REMARK 100 THE DEPOSITION ID IS D_1000056962.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-NOV-06
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 : NSLS
REMARK 200 BEAMLINE : X12B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9786
REMARK 200 MONOCHROMATOR : SI(111)
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 : 76862
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.49100
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 5MM MGCL2, 25% PEG 3350, PH
REMARK 280 7.5, HANGING DROP, TEMPERATURE 298K
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 25.88300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.59800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.98350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.59800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.88300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.98350
REMARK 290 SMTRY3 4 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 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 LYS B 3
REMARK 465 GLN B 187
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 ARG A 12 -77.53 -94.78
REMARK 500 THR A 15 -52.91 -123.96
REMARK 500 ARG B 12 -79.76 -96.10
REMARK 500 THR B 15 -50.40 -124.78
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 801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 92 SG
REMARK 620 2 HIS A 94 ND1 110.7
REMARK 620 3 CYS A 107 SG 107.2 101.3
REMARK 620 4 CYS A 109 SG 122.5 102.4 110.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 92 SG
REMARK 620 2 HIS B 94 ND1 110.5
REMARK 620 3 CYS B 107 SG 106.8 101.8
REMARK 620 4 CYS B 109 SG 125.2 102.1 108.0
REMARK 620 N 1 2 3
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 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B 902
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3L8F RELATED DB: PDB
REMARK 900 RELATED ID: 3L8G RELATED DB: PDB
REMARK 900 RELATED ID: 3L8H RELATED DB: PDB
DBREF 3L8E A 1 187 UNP P63228 GMHB_ECOLI 1 187
DBREF 3L8E B 1 187 UNP P63228 GMHB_ECOLI 1 187
SEQRES 1 A 187 MET ALA LYS SER VAL PRO ALA ILE PHE LEU ASP ARG ASP
SEQRES 2 A 187 GLY THR ILE ASN VAL ASP HIS GLY TYR VAL HIS GLU ILE
SEQRES 3 A 187 ASP ASN PHE GLU PHE ILE ASP GLY VAL ILE ASP ALA MET
SEQRES 4 A 187 ARG GLU LEU LYS LYS MET GLY PHE ALA LEU VAL VAL VAL
SEQRES 5 A 187 THR ASN GLN SER GLY ILE ALA ARG GLY LYS PHE THR GLU
SEQRES 6 A 187 ALA GLN PHE GLU THR LEU THR GLU TRP MET ASP TRP SER
SEQRES 7 A 187 LEU ALA ASP ARG ASP VAL ASP LEU ASP GLY ILE TYR TYR
SEQRES 8 A 187 CYS PRO HIS HIS PRO GLN GLY SER VAL GLU GLU PHE ARG
SEQRES 9 A 187 GLN VAL CYS ASP CYS ARG LYS PRO HIS PRO GLY MET LEU
SEQRES 10 A 187 LEU SER ALA ARG ASP TYR LEU HIS ILE ASP MET ALA ALA
SEQRES 11 A 187 SER TYR MET VAL GLY ASP LYS LEU GLU ASP MET GLN ALA
SEQRES 12 A 187 ALA VAL ALA ALA ASN VAL GLY THR LYS VAL LEU VAL ARG
SEQRES 13 A 187 THR GLY LYS PRO ILE THR PRO GLU ALA GLU ASN ALA ALA
SEQRES 14 A 187 ASP TRP VAL LEU ASN SER LEU ALA ASP LEU PRO GLN ALA
SEQRES 15 A 187 ILE LYS LYS GLN GLN
SEQRES 1 B 187 MET ALA LYS SER VAL PRO ALA ILE PHE LEU ASP ARG ASP
SEQRES 2 B 187 GLY THR ILE ASN VAL ASP HIS GLY TYR VAL HIS GLU ILE
SEQRES 3 B 187 ASP ASN PHE GLU PHE ILE ASP GLY VAL ILE ASP ALA MET
SEQRES 4 B 187 ARG GLU LEU LYS LYS MET GLY PHE ALA LEU VAL VAL VAL
SEQRES 5 B 187 THR ASN GLN SER GLY ILE ALA ARG GLY LYS PHE THR GLU
SEQRES 6 B 187 ALA GLN PHE GLU THR LEU THR GLU TRP MET ASP TRP SER
SEQRES 7 B 187 LEU ALA ASP ARG ASP VAL ASP LEU ASP GLY ILE TYR TYR
SEQRES 8 B 187 CYS PRO HIS HIS PRO GLN GLY SER VAL GLU GLU PHE ARG
SEQRES 9 B 187 GLN VAL CYS ASP CYS ARG LYS PRO HIS PRO GLY MET LEU
SEQRES 10 B 187 LEU SER ALA ARG ASP TYR LEU HIS ILE ASP MET ALA ALA
SEQRES 11 B 187 SER TYR MET VAL GLY ASP LYS LEU GLU ASP MET GLN ALA
SEQRES 12 B 187 ALA VAL ALA ALA ASN VAL GLY THR LYS VAL LEU VAL ARG
SEQRES 13 B 187 THR GLY LYS PRO ILE THR PRO GLU ALA GLU ASN ALA ALA
SEQRES 14 B 187 ASP TRP VAL LEU ASN SER LEU ALA ASP LEU PRO GLN ALA
SEQRES 15 B 187 ILE LYS LYS GLN GLN
HET ZN A 801 1
HET ACY A 901 4
HET ZN B 802 1
HET ACY B 902 4
HETNAM ZN ZINC ION
HETNAM ACY ACETIC ACID
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 ACY 2(C2 H4 O2)
FORMUL 7 HOH *378(H2 O)
HELIX 1 1 GLU A 25 PHE A 29 5 5
HELIX 2 2 GLY A 34 MET A 45 1 12
HELIX 3 3 THR A 64 ARG A 82 1 19
HELIX 4 4 VAL A 100 ARG A 104 5 5
HELIX 5 5 PRO A 114 HIS A 125 1 12
HELIX 6 6 ASP A 127 ALA A 130 5 4
HELIX 7 7 LYS A 137 ALA A 147 1 11
HELIX 8 8 THR A 162 ALA A 168 1 7
HELIX 9 9 SER A 175 ALA A 177 5 3
HELIX 10 10 ASP A 178 LYS A 185 1 8
HELIX 11 11 GLU B 25 PHE B 29 5 5
HELIX 12 12 GLY B 34 MET B 45 1 12
HELIX 13 13 THR B 64 ARG B 82 1 19
HELIX 14 14 VAL B 100 ARG B 104 5 5
HELIX 15 15 PRO B 114 HIS B 125 1 12
HELIX 16 16 ASP B 127 ALA B 130 5 4
HELIX 17 17 LYS B 137 ALA B 147 1 11
HELIX 18 18 THR B 162 ALA B 169 1 8
HELIX 19 19 SER B 175 ALA B 177 5 3
HELIX 20 20 ASP B 178 GLN B 186 1 9
SHEET 1 A 6 GLY A 88 CYS A 92 0
SHEET 2 A 6 ALA A 48 ASN A 54 1 N VAL A 51 O TYR A 90
SHEET 3 A 6 ALA A 7 LEU A 10 1 N LEU A 10 O VAL A 52
SHEET 4 A 6 TYR A 132 GLY A 135 1 O TYR A 132 N PHE A 9
SHEET 5 A 6 THR A 151 VAL A 155 1 O VAL A 153 N MET A 133
SHEET 6 A 6 TRP A 171 LEU A 173 1 O LEU A 173 N LEU A 154
SHEET 1 B 6 GLY B 88 CYS B 92 0
SHEET 2 B 6 ALA B 48 ASN B 54 1 N VAL B 51 O TYR B 90
SHEET 3 B 6 ALA B 7 LEU B 10 1 N LEU B 10 O VAL B 52
SHEET 4 B 6 TYR B 132 GLY B 135 1 O TYR B 132 N PHE B 9
SHEET 5 B 6 THR B 151 VAL B 155 1 O VAL B 153 N MET B 133
SHEET 6 B 6 TRP B 171 LEU B 173 1 O LEU B 173 N LEU B 154
LINK SG CYS A 92 ZN ZN A 801 1555 1555 2.29
LINK ND1 HIS A 94 ZN ZN A 801 1555 1555 2.19
LINK SG CYS A 107 ZN ZN A 801 1555 1555 2.34
LINK SG CYS A 109 ZN ZN A 801 1555 1555 2.29
LINK SG CYS B 92 ZN ZN B 802 1555 1555 2.27
LINK ND1 HIS B 94 ZN ZN B 802 1555 1555 2.18
LINK SG CYS B 107 ZN ZN B 802 1555 1555 2.38
LINK SG CYS B 109 ZN ZN B 802 1555 1555 2.32
CISPEP 1 LYS A 111 PRO A 112 0 13.43
CISPEP 2 LYS B 111 PRO B 112 0 17.89
SITE 1 AC1 5 CYS A 92 HIS A 94 CYS A 107 CYS A 109
SITE 2 AC1 5 ARG A 110
SITE 1 AC2 8 ASP A 11 ARG A 12 ASP A 13 THR A 53
SITE 2 AC2 8 ASN A 54 LYS A 111 LYS A 137 HOH A 202
SITE 1 AC3 5 CYS B 92 HIS B 94 CYS B 107 CYS B 109
SITE 2 AC3 5 ARG B 110
SITE 1 AC4 8 ASP B 11 ARG B 12 ASP B 13 THR B 53
SITE 2 AC4 8 ASN B 54 LYS B 111 LYS B 137 HOH B 193
CRYST1 51.766 63.967 103.196 90.00 90.00 90.00 P 21 21 21 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 0.019318 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015633 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009690 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
