HEADER LYASE 30-JAN-08 3C4U
TITLE STRUCTURE OF CLASS II FRUCTOSE-BIPHOSPHATE ALDOLASE FROM HELICOBACTER
TITLE 2 PYLORI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FRUCTOSE-BISPHOSPHATE ALDOLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 4.1.2.13;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;
SOURCE 3 ORGANISM_COMMON: CAMPYLOBACTER PYLORI;
SOURCE 4 GENE: FBA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PKK233-3
KEYWDS FBP ALDOLASE, CLASS II, ZINC, GLYCOLYSIS, LYASE, METAL-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR M.COINCON,J.SYGUSCH
REVDAT 4 30-AUG-23 3C4U 1 REMARK SEQADV
REVDAT 3 24-FEB-09 3C4U 1 VERSN
REVDAT 2 14-OCT-08 3C4U 1 JRNL
REVDAT 1 26-AUG-08 3C4U 0
JRNL AUTH M.FONVIELLE,M.COINCON,R.DAHER,N.DESBENOIT,K.KOSIERADZKA,
JRNL AUTH 2 N.BARILONE,B.GICQUEL,J.SYGUSCH,M.JACKSON,M.THERISOD
JRNL TITL SYNTHESIS AND BIOCHEMICAL EVALUATION OF SELECTIVE INHIBITORS
JRNL TITL 2 OF CLASS II FRUCTOSE BISPHOSPHATE ALDOLASES: TOWARDS NEW
JRNL TITL 3 SYNTHETIC ANTIBIOTICS.
JRNL REF CHEMISTRY V. 14 8521 2008
JRNL REFN ISSN 0947-6539
JRNL PMID 18688832
JRNL DOI 10.1002/CHEM.200800857
REMARK 2
REMARK 2 RESOLUTION. 1.83 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 1.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 47885
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.070
REMARK 3 FREE R VALUE TEST SET COUNT : 4824
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 33.4100 - 5.6770 0.97 1531 141 0.1900 0.2280
REMARK 3 2 5.6770 - 4.5100 0.99 1546 163 0.1640 0.1810
REMARK 3 3 4.5100 - 3.9410 0.99 1495 166 0.1470 0.1580
REMARK 3 4 3.9410 - 3.5810 0.99 1500 179 0.1560 0.1580
REMARK 3 5 3.5810 - 3.3240 0.99 1509 166 0.1570 0.1910
REMARK 3 6 3.3240 - 3.1290 0.99 1517 166 0.1640 0.1760
REMARK 3 7 3.1290 - 2.9720 0.98 1464 172 0.1820 0.1710
REMARK 3 8 2.9720 - 2.8430 0.98 1482 166 0.1780 0.1830
REMARK 3 9 2.8430 - 2.7330 0.97 1464 179 0.1880 0.2130
REMARK 3 10 2.7330 - 2.6390 0.98 1479 151 0.1890 0.2060
REMARK 3 11 2.6390 - 2.5570 0.97 1471 166 0.1890 0.2090
REMARK 3 12 2.5570 - 2.4840 0.98 1489 152 0.1890 0.2120
REMARK 3 13 2.4840 - 2.4180 0.96 1425 173 0.1970 0.2500
REMARK 3 14 2.4180 - 2.3590 0.96 1459 168 0.1930 0.2300
REMARK 3 15 2.3590 - 2.3060 0.96 1420 177 0.1810 0.2170
REMARK 3 16 2.3060 - 2.2570 0.96 1450 169 0.1840 0.2130
REMARK 3 17 2.2570 - 2.2110 0.95 1449 163 0.1860 0.2080
REMARK 3 18 2.2110 - 2.1700 0.96 1388 161 0.1960 0.2210
REMARK 3 19 2.1700 - 2.1310 0.96 1470 177 0.1810 0.2010
REMARK 3 20 2.1310 - 2.0950 0.95 1450 144 0.1920 0.2070
REMARK 3 21 2.0950 - 2.0610 0.94 1384 137 0.2050 0.2200
REMARK 3 22 2.0610 - 2.0290 0.94 1430 160 0.2060 0.2600
REMARK 3 23 2.0290 - 2.0000 0.92 1371 173 0.1970 0.2150
REMARK 3 24 2.0000 - 1.9710 0.92 1368 159 0.2070 0.2520
REMARK 3 25 1.9710 - 1.9450 0.91 1349 148 0.2230 0.2410
REMARK 3 26 1.9450 - 1.9190 0.89 1368 162 0.2130 0.2500
REMARK 3 27 1.9190 - 1.8950 0.91 1331 171 0.2300 0.2460
REMARK 3 28 1.8950 - 1.8730 0.89 1365 136 0.2220 0.2620
REMARK 3 29 1.8730 - 1.8510 0.89 1325 141 0.2270 0.2790
REMARK 3 30 1.8510 - 1.8300 0.88 1312 138 0.2300 0.2620
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 : 0.38
REMARK 3 B_SOL : 47.26
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.72500
REMARK 3 B22 (A**2) : 3.67900
REMARK 3 B33 (A**2) : -1.95400
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.26300
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 : 0.004 4600
REMARK 3 ANGLE : 0.573 6184
REMARK 3 CHIRALITY : 0.035 688
REMARK 3 PLANARITY : 0.002 806
REMARK 3 DIHEDRAL : 14.871 1708
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: THE FRIEDEL PAIRS WERE USED IN PHASING
REMARK 4
REMARK 4 3C4U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-08.
REMARK 100 THE DEPOSITION ID IS D_1000046342.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71999
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.620
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 : 8.640
REMARK 200 R MERGE (I) : 0.10100
REMARK 200 R SYM (I) : 0.24500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 1.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.69700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1RVG
REMARK 200
REMARK 200 REMARK: THE STRUCTURE FACTOR FILE CONTAINS FRIEDEL PAIRS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 297K
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 41.28000
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4100 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 LEU A 138
REMARK 465 MET A 139
REMARK 465 GLY A 140
REMARK 465 ILE A 141
REMARK 465 GLU A 142
REMARK 465 ASP A 143
REMARK 465 ASN A 144
REMARK 465 ILE A 145
REMARK 465 SER A 146
REMARK 465 VAL A 147
REMARK 465 ASP A 148
REMARK 465 GLU A 149
REMARK 465 LYS A 150
REMARK 465 ASP A 151
REMARK 465 ALA A 152
REMARK 465 LEU B 138
REMARK 465 MET B 139
REMARK 465 GLY B 140
REMARK 465 ILE B 141
REMARK 465 GLU B 142
REMARK 465 ASP B 143
REMARK 465 ASN B 144
REMARK 465 ILE B 145
REMARK 465 SER B 146
REMARK 465 VAL B 147
REMARK 465 ASP B 148
REMARK 465 GLU B 149
REMARK 465 LYS B 150
REMARK 465 ASP B 151
REMARK 465 ALA B 152
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 N MET B 1 SG CYS B 69 2.10
REMARK 500 N MET A 1 SG CYS A 69 2.12
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 ALA A 212 63.62 -110.40
REMARK 500 ASP A 255 -58.73 -141.56
REMARK 500 ALA B 212 62.98 -111.12
REMARK 500 ILE B 215 73.89 48.33
REMARK 500 ASP B 255 -58.13 -141.49
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 309 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 83 NE2
REMARK 620 2 GLU A 134 OE1 113.3
REMARK 620 3 HIS A 180 NE2 96.5 144.1
REMARK 620 4 HIS A 210 ND1 89.9 98.2 101.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 309 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 83 NE2
REMARK 620 2 GLU B 134 OE1 111.2
REMARK 620 3 HIS B 180 NE2 102.8 141.7
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 309
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3C52 RELATED DB: PDB
REMARK 900 SAME PROTEIN IN COMPLEX WITH PHOSPHOGLYCOLOHYDROXAMIC ACID (PGH).
REMARK 900 RELATED ID: 3C56 RELATED DB: PDB
REMARK 900 SAME PROTEIN IN COMPLEX WITH PH4.
DBREF 3C4U A 1 307 UNP P56109 ALF_HELPY 1 307
DBREF 3C4U B 1 307 UNP P56109 ALF_HELPY 1 307
SEQADV 3C4U ALA A 48 UNP P56109 THR 48 CONFLICT
SEQADV 3C4U ILE A 67 UNP P56109 THR 67 CONFLICT
SEQADV 3C4U ALA B 48 UNP P56109 THR 48 CONFLICT
SEQADV 3C4U ILE B 67 UNP P56109 THR 67 CONFLICT
SEQRES 1 A 307 MET LEU VAL LYS GLY ASN GLU ILE LEU LEU LYS ALA HIS
SEQRES 2 A 307 LYS GLU GLY TYR GLY VAL GLY ALA PHE ASN PHE VAL ASN
SEQRES 3 A 307 PHE GLU MET LEU ASN ALA ILE PHE GLU ALA GLY ASN GLU
SEQRES 4 A 307 GLU ASN SER PRO LEU PHE ILE GLN ALA SER GLU GLY ALA
SEQRES 5 A 307 ILE LYS TYR MET GLY ILE ASP MET ALA VAL GLY MET VAL
SEQRES 6 A 307 LYS ILE MET CYS GLU ARG TYR PRO HIS ILE PRO VAL ALA
SEQRES 7 A 307 LEU HIS LEU ASP HIS GLY THR THR PHE GLU SER CYS GLU
SEQRES 8 A 307 LYS ALA VAL LYS ALA GLY PHE THR SER VAL MET ILE ASP
SEQRES 9 A 307 ALA SER HIS HIS ALA PHE GLU GLU ASN LEU GLU LEU THR
SEQRES 10 A 307 SER LYS VAL VAL LYS MET ALA HIS ASN ALA GLY VAL SER
SEQRES 11 A 307 VAL GLU ALA GLU LEU GLY ARG LEU MET GLY ILE GLU ASP
SEQRES 12 A 307 ASN ILE SER VAL ASP GLU LYS ASP ALA VAL LEU VAL ASN
SEQRES 13 A 307 PRO LYS GLU ALA GLU GLN PHE VAL LYS GLU SER GLN VAL
SEQRES 14 A 307 ASP TYR LEU ALA PRO ALA ILE GLY THR SER HIS GLY ALA
SEQRES 15 A 307 PHE LYS PHE LYS GLY GLU PRO LYS LEU ASP PHE GLU ARG
SEQRES 16 A 307 LEU GLN GLU VAL LYS ARG LEU THR ASN ILE PRO LEU VAL
SEQRES 17 A 307 LEU HIS GLY ALA SER ALA ILE PRO ASP ASN VAL ARG LYS
SEQRES 18 A 307 SER TYR LEU ASP ALA GLY GLY ASP LEU LYS GLY SER LYS
SEQRES 19 A 307 GLY VAL PRO PHE GLU PHE LEU GLN GLU SER VAL LYS GLY
SEQRES 20 A 307 GLY ILE ASN LYS VAL ASN THR ASP THR ASP LEU ARG ILE
SEQRES 21 A 307 ALA PHE ILE ALA GLU VAL ARG LYS VAL ALA ASN GLU ASP
SEQRES 22 A 307 LYS SER GLN PHE ASP LEU ARG LYS PHE PHE SER PRO ALA
SEQRES 23 A 307 GLN LEU ALA LEU LYS ASN VAL VAL LYS GLU ARG MET LYS
SEQRES 24 A 307 LEU LEU GLY SER ALA ASN LYS ILE
SEQRES 1 B 307 MET LEU VAL LYS GLY ASN GLU ILE LEU LEU LYS ALA HIS
SEQRES 2 B 307 LYS GLU GLY TYR GLY VAL GLY ALA PHE ASN PHE VAL ASN
SEQRES 3 B 307 PHE GLU MET LEU ASN ALA ILE PHE GLU ALA GLY ASN GLU
SEQRES 4 B 307 GLU ASN SER PRO LEU PHE ILE GLN ALA SER GLU GLY ALA
SEQRES 5 B 307 ILE LYS TYR MET GLY ILE ASP MET ALA VAL GLY MET VAL
SEQRES 6 B 307 LYS ILE MET CYS GLU ARG TYR PRO HIS ILE PRO VAL ALA
SEQRES 7 B 307 LEU HIS LEU ASP HIS GLY THR THR PHE GLU SER CYS GLU
SEQRES 8 B 307 LYS ALA VAL LYS ALA GLY PHE THR SER VAL MET ILE ASP
SEQRES 9 B 307 ALA SER HIS HIS ALA PHE GLU GLU ASN LEU GLU LEU THR
SEQRES 10 B 307 SER LYS VAL VAL LYS MET ALA HIS ASN ALA GLY VAL SER
SEQRES 11 B 307 VAL GLU ALA GLU LEU GLY ARG LEU MET GLY ILE GLU ASP
SEQRES 12 B 307 ASN ILE SER VAL ASP GLU LYS ASP ALA VAL LEU VAL ASN
SEQRES 13 B 307 PRO LYS GLU ALA GLU GLN PHE VAL LYS GLU SER GLN VAL
SEQRES 14 B 307 ASP TYR LEU ALA PRO ALA ILE GLY THR SER HIS GLY ALA
SEQRES 15 B 307 PHE LYS PHE LYS GLY GLU PRO LYS LEU ASP PHE GLU ARG
SEQRES 16 B 307 LEU GLN GLU VAL LYS ARG LEU THR ASN ILE PRO LEU VAL
SEQRES 17 B 307 LEU HIS GLY ALA SER ALA ILE PRO ASP ASN VAL ARG LYS
SEQRES 18 B 307 SER TYR LEU ASP ALA GLY GLY ASP LEU LYS GLY SER LYS
SEQRES 19 B 307 GLY VAL PRO PHE GLU PHE LEU GLN GLU SER VAL LYS GLY
SEQRES 20 B 307 GLY ILE ASN LYS VAL ASN THR ASP THR ASP LEU ARG ILE
SEQRES 21 B 307 ALA PHE ILE ALA GLU VAL ARG LYS VAL ALA ASN GLU ASP
SEQRES 22 B 307 LYS SER GLN PHE ASP LEU ARG LYS PHE PHE SER PRO ALA
SEQRES 23 B 307 GLN LEU ALA LEU LYS ASN VAL VAL LYS GLU ARG MET LYS
SEQRES 24 B 307 LEU LEU GLY SER ALA ASN LYS ILE
HET NA A 308 1
HET ZN A 309 1
HET NA B 308 1
HET ZN B 309 1
HETNAM NA SODIUM ION
HETNAM ZN ZINC ION
FORMUL 3 NA 2(NA 1+)
FORMUL 4 ZN 2(ZN 2+)
FORMUL 7 HOH *933(H2 O)
HELIX 1 1 LYS A 4 GLY A 16 1 13
HELIX 2 2 ASN A 26 ASN A 41 1 16
HELIX 3 3 GLU A 50 GLY A 57 1 8
HELIX 4 4 GLY A 57 TYR A 72 1 16
HELIX 5 5 THR A 86 GLY A 97 1 12
HELIX 6 6 ALA A 109 ALA A 127 1 19
HELIX 7 7 ASN A 156 GLN A 168 1 13
HELIX 8 8 HIS A 180 LYS A 184 5 5
HELIX 9 9 ASP A 192 ASN A 204 1 13
HELIX 10 10 PRO A 216 ALA A 226 1 11
HELIX 11 11 PRO A 237 GLY A 248 1 12
HELIX 12 12 ASP A 255 ASP A 273 1 19
HELIX 13 13 ASP A 278 GLY A 302 1 25
HELIX 14 14 LYS B 4 GLY B 16 1 13
HELIX 15 15 ASN B 26 ASN B 41 1 16
HELIX 16 16 GLU B 50 GLY B 57 1 8
HELIX 17 17 GLY B 57 TYR B 72 1 16
HELIX 18 18 THR B 86 GLY B 97 1 12
HELIX 19 19 ALA B 109 ALA B 127 1 19
HELIX 20 20 ASN B 156 GLN B 168 1 13
HELIX 21 21 HIS B 180 LYS B 184 5 5
HELIX 22 22 ASP B 192 ASN B 204 1 13
HELIX 23 23 PRO B 216 ALA B 226 1 11
HELIX 24 24 PRO B 237 GLY B 248 1 12
HELIX 25 25 ASP B 255 ASP B 273 1 19
HELIX 26 26 ASP B 278 GLY B 302 1 25
SHEET 1 A 9 VAL A 19 ASN A 23 0
SHEET 2 A 9 LEU A 44 SER A 49 1 O GLN A 47 N PHE A 22
SHEET 3 A 9 VAL A 77 GLY A 84 1 O HIS A 80 N ILE A 46
SHEET 4 A 9 SER A 100 ILE A 103 1 O SER A 100 N LEU A 81
SHEET 5 A 9 SER A 130 LEU A 135 1 O GLU A 132 N ILE A 103
SHEET 6 A 9 TYR A 171 PRO A 174 1 O ALA A 173 N ALA A 133
SHEET 7 A 9 LEU A 207 LEU A 209 1 O VAL A 208 N LEU A 172
SHEET 8 A 9 ILE A 249 THR A 254 1 O LYS A 251 N LEU A 209
SHEET 9 A 9 VAL A 19 ASN A 23 1 N ALA A 21 O THR A 254
SHEET 1 B 9 VAL B 19 ASN B 23 0
SHEET 2 B 9 LEU B 44 SER B 49 1 O GLN B 47 N PHE B 22
SHEET 3 B 9 VAL B 77 GLY B 84 1 O HIS B 80 N ILE B 46
SHEET 4 B 9 SER B 100 ILE B 103 1 O SER B 100 N LEU B 81
SHEET 5 B 9 SER B 130 LEU B 135 1 O GLU B 132 N ILE B 103
SHEET 6 B 9 TYR B 171 PRO B 174 1 O ALA B 173 N ALA B 133
SHEET 7 B 9 LEU B 207 LEU B 209 1 O VAL B 208 N LEU B 172
SHEET 8 B 9 ILE B 249 THR B 254 1 O LYS B 251 N LEU B 209
SHEET 9 B 9 VAL B 19 ASN B 23 1 N ALA B 21 O THR B 254
LINK NE2 HIS A 83 ZN ZN A 309 1555 1555 2.26
LINK OE1 GLU A 134 ZN ZN A 309 1555 1555 2.21
LINK NE2 HIS A 180 ZN ZN A 309 1555 1555 2.19
LINK ND1 HIS A 210 ZN ZN A 309 1555 1555 2.38
LINK NE2 HIS B 83 ZN ZN B 309 1555 1555 2.25
LINK OE1 GLU B 134 ZN ZN B 309 1555 1555 2.21
LINK NE2 HIS B 180 ZN ZN B 309 1555 1555 2.16
SITE 1 AC1 7 GLN A 47 HIS A 80 ASP A 82 MET A 102
SITE 2 AC1 7 GLU A 132 LYS A 251 ASN A 253
SITE 1 AC2 8 GLN B 47 HIS B 80 ASP B 82 MET B 102
SITE 2 AC2 8 GLU B 132 HIS B 210 LYS B 251 ASN B 253
SITE 1 AC3 4 HIS B 83 GLU B 134 HIS B 180 HIS B 210
SITE 1 AC4 4 HIS A 83 GLU A 134 HIS A 180 HIS A 210
CRYST1 39.023 82.560 91.272 90.00 99.66 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 0.025626 0.000000 0.004362 0.00000
SCALE2 0.000000 0.012112 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011114 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
