HEADER OXIDOREDUCTASE 17-APR-04 1T1S
TITLE CRYSTAL STRUCTURE OF THE REDUCTOISOMERASE COMPLEXED WITH A
TITLE 2 BISPHOSPHONATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DXP REDUCTOISOMERASE, 1-DEOXYXYLULOSE-5-PHOSPHATE
COMPND 5 REDUCTOISOMERASE;
COMPND 6 EC: 1.1.1.267;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: ISPC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS THREE DOMAINS, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.YAJIMA,K.HARA,J.M.SANDERS,F.YIN,K.OHSAWA,J.WIESNER,H.JOMAA,
AUTHOR 2 E.OLDFIELD
REVDAT 3 13-MAR-24 1T1S 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1T1S 1 VERSN
REVDAT 1 14-SEP-04 1T1S 0
JRNL AUTH S.YAJIMA,K.HARA,J.M.SANDERS,F.YIN,K.OHSAWA,J.WIESNER,
JRNL AUTH 2 H.JOMAA,E.OLDFIELD
JRNL TITL CRYSTALLOGRAPHIC STRUCTURES OF TWO
JRNL TITL 2 BISPHOSPHONATE:1-DEOXYXYLULOSE-5-PHOSPHATE REDUCTOISOMERASE
JRNL TITL 3 COMPLEXES
JRNL REF J.AM.CHEM.SOC. V. 126 10824 2004
JRNL REFN ISSN 0002-7863
JRNL PMID 15339150
JRNL DOI 10.1021/JA040126M
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 37871
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) : 0.213
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3755
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6052
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1T1S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022203.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-NOV-03
REMARK 200 TEMPERATURE (KELVIN) : 95.0
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : MIRROR
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38020
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 16.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
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) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, POTASSIUM SODIUM
REMARK 280 TARTRATE, GLYCEROL, DTT, SODIUM CITRATE, PH 5.6, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277K
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 91.45850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.62300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 91.45850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.62300
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER.
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 KCAL/MOL
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 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 LYS A 142 33.10 70.34
REMARK 500 ASN A 166 43.47 -144.56
REMARK 500 ASN A 210 -73.91 -94.69
REMARK 500 SER A 257 169.82 152.41
REMARK 500 ASN A 287 -166.90 -103.28
REMARK 500 ASP A 367 -81.83 -93.65
REMARK 500 MET A 368 136.07 -23.55
REMARK 500 GLU A 370 100.76 25.32
REMARK 500 ALA A 396 49.50 -79.76
REMARK 500 ASN B 23 58.83 -142.32
REMARK 500 ASP B 57 142.82 161.17
REMARK 500 ASN B 123 42.81 -76.37
REMARK 500 LYS B 124 -11.87 -47.53
REMARK 500 SER B 141 -4.53 -143.19
REMARK 500 LYS B 142 19.95 59.85
REMARK 500 ASN B 166 33.01 71.61
REMARK 500 ASN B 210 -83.90 -108.39
REMARK 500 SER B 257 164.81 156.21
REMARK 500 PRO B 273 30.87 -81.79
REMARK 500 ASN B 287 -166.36 -106.27
REMARK 500 MET B 366 -91.18 -49.45
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 MG A1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 149 OD2
REMARK 620 2 GLU A 151 OE2 105.1
REMARK 620 3 GLU A 230 OE2 157.7 90.3
REMARK 620 4 CBQ A2001 O2 110.0 76.4 89.0
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 SO4 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBQ A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBQ B 3001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JVS RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT A BISPHOSPHONATE
REMARK 900 RELATED ID: 1T1R RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH ANOTHER BISPHOSHONATE
DBREF 1T1S A 1 397 UNP P45568 DXR_ECOLI 2 398
DBREF 1T1S B 1 397 UNP P45568 DXR_ECOLI 2 398
SEQADV 1T1S GLY A 0 UNP P45568 CLONING ARTIFACT
SEQADV 1T1S GLY B 0 UNP P45568 CLONING ARTIFACT
SEQRES 1 A 398 GLY LYS GLN LEU THR ILE LEU GLY SER THR GLY SER ILE
SEQRES 2 A 398 GLY CYS SER THR LEU ASP VAL VAL ARG HIS ASN PRO GLU
SEQRES 3 A 398 HIS PHE ARG VAL VAL ALA LEU VAL ALA GLY LYS ASN VAL
SEQRES 4 A 398 THR ARG MET VAL GLU GLN CYS LEU GLU PHE SER PRO ARG
SEQRES 5 A 398 TYR ALA VAL MET ASP ASP GLU ALA SER ALA LYS LEU LEU
SEQRES 6 A 398 LYS THR MET LEU GLN GLN GLN GLY SER ARG THR GLU VAL
SEQRES 7 A 398 LEU SER GLY GLN GLN ALA ALA CYS ASP MET ALA ALA LEU
SEQRES 8 A 398 GLU ASP VAL ASP GLN VAL MET ALA ALA ILE VAL GLY ALA
SEQRES 9 A 398 ALA GLY LEU LEU PRO THR LEU ALA ALA ILE ARG ALA GLY
SEQRES 10 A 398 LYS THR ILE LEU LEU ALA ASN LYS GLU SER LEU VAL THR
SEQRES 11 A 398 CYS GLY ARG LEU PHE MET ASP ALA VAL LYS GLN SER LYS
SEQRES 12 A 398 ALA GLN LEU LEU PRO VAL ASP SER GLU HIS ASN ALA ILE
SEQRES 13 A 398 PHE GLN SER LEU PRO GLN PRO ILE GLN HIS ASN LEU GLY
SEQRES 14 A 398 TYR ALA ASP LEU GLU GLN ASN GLY VAL VAL SER ILE LEU
SEQRES 15 A 398 LEU THR GLY SER GLY GLY PRO PHE ARG GLU THR PRO LEU
SEQRES 16 A 398 ARG ASP LEU ALA THR MET THR PRO ASP GLN ALA CYS ARG
SEQRES 17 A 398 HIS PRO ASN TRP SER MET GLY ARG LYS ILE SER VAL ASP
SEQRES 18 A 398 SER ALA THR MET MET ASN LYS GLY LEU GLU TYR ILE GLU
SEQRES 19 A 398 ALA ARG TRP LEU PHE ASN ALA SER ALA SER GLN MET GLU
SEQRES 20 A 398 VAL LEU ILE HIS PRO GLN SER VAL ILE HIS SER MET VAL
SEQRES 21 A 398 ARG TYR GLN ASP GLY SER VAL LEU ALA GLN LEU GLY GLU
SEQRES 22 A 398 PRO ASP MET ARG THR PRO ILE ALA HIS THR MET ALA TRP
SEQRES 23 A 398 PRO ASN ARG VAL ASN SER GLY VAL LYS PRO LEU ASP PHE
SEQRES 24 A 398 CYS LYS LEU SER ALA LEU THR PHE ALA ALA PRO ASP TYR
SEQRES 25 A 398 ASP ARG TYR PRO CYS LEU LYS LEU ALA MET GLU ALA PHE
SEQRES 26 A 398 GLU GLN GLY GLN ALA ALA THR THR ALA LEU ASN ALA ALA
SEQRES 27 A 398 ASN GLU ILE THR VAL ALA ALA PHE LEU ALA GLN GLN ILE
SEQRES 28 A 398 ARG PHE THR ASP ILE ALA ALA LEU ASN LEU SER VAL LEU
SEQRES 29 A 398 GLU LYS MET ASP MET ARG GLU PRO GLN CYS VAL ASP ASP
SEQRES 30 A 398 VAL LEU SER VAL ASP ALA ASN ALA ARG GLU VAL ALA ARG
SEQRES 31 A 398 LYS GLU VAL MET ARG LEU ALA SER
SEQRES 1 B 398 GLY LYS GLN LEU THR ILE LEU GLY SER THR GLY SER ILE
SEQRES 2 B 398 GLY CYS SER THR LEU ASP VAL VAL ARG HIS ASN PRO GLU
SEQRES 3 B 398 HIS PHE ARG VAL VAL ALA LEU VAL ALA GLY LYS ASN VAL
SEQRES 4 B 398 THR ARG MET VAL GLU GLN CYS LEU GLU PHE SER PRO ARG
SEQRES 5 B 398 TYR ALA VAL MET ASP ASP GLU ALA SER ALA LYS LEU LEU
SEQRES 6 B 398 LYS THR MET LEU GLN GLN GLN GLY SER ARG THR GLU VAL
SEQRES 7 B 398 LEU SER GLY GLN GLN ALA ALA CYS ASP MET ALA ALA LEU
SEQRES 8 B 398 GLU ASP VAL ASP GLN VAL MET ALA ALA ILE VAL GLY ALA
SEQRES 9 B 398 ALA GLY LEU LEU PRO THR LEU ALA ALA ILE ARG ALA GLY
SEQRES 10 B 398 LYS THR ILE LEU LEU ALA ASN LYS GLU SER LEU VAL THR
SEQRES 11 B 398 CYS GLY ARG LEU PHE MET ASP ALA VAL LYS GLN SER LYS
SEQRES 12 B 398 ALA GLN LEU LEU PRO VAL ASP SER GLU HIS ASN ALA ILE
SEQRES 13 B 398 PHE GLN SER LEU PRO GLN PRO ILE GLN HIS ASN LEU GLY
SEQRES 14 B 398 TYR ALA ASP LEU GLU GLN ASN GLY VAL VAL SER ILE LEU
SEQRES 15 B 398 LEU THR GLY SER GLY GLY PRO PHE ARG GLU THR PRO LEU
SEQRES 16 B 398 ARG ASP LEU ALA THR MET THR PRO ASP GLN ALA CYS ARG
SEQRES 17 B 398 HIS PRO ASN TRP SER MET GLY ARG LYS ILE SER VAL ASP
SEQRES 18 B 398 SER ALA THR MET MET ASN LYS GLY LEU GLU TYR ILE GLU
SEQRES 19 B 398 ALA ARG TRP LEU PHE ASN ALA SER ALA SER GLN MET GLU
SEQRES 20 B 398 VAL LEU ILE HIS PRO GLN SER VAL ILE HIS SER MET VAL
SEQRES 21 B 398 ARG TYR GLN ASP GLY SER VAL LEU ALA GLN LEU GLY GLU
SEQRES 22 B 398 PRO ASP MET ARG THR PRO ILE ALA HIS THR MET ALA TRP
SEQRES 23 B 398 PRO ASN ARG VAL ASN SER GLY VAL LYS PRO LEU ASP PHE
SEQRES 24 B 398 CYS LYS LEU SER ALA LEU THR PHE ALA ALA PRO ASP TYR
SEQRES 25 B 398 ASP ARG TYR PRO CYS LEU LYS LEU ALA MET GLU ALA PHE
SEQRES 26 B 398 GLU GLN GLY GLN ALA ALA THR THR ALA LEU ASN ALA ALA
SEQRES 27 B 398 ASN GLU ILE THR VAL ALA ALA PHE LEU ALA GLN GLN ILE
SEQRES 28 B 398 ARG PHE THR ASP ILE ALA ALA LEU ASN LEU SER VAL LEU
SEQRES 29 B 398 GLU LYS MET ASP MET ARG GLU PRO GLN CYS VAL ASP ASP
SEQRES 30 B 398 VAL LEU SER VAL ASP ALA ASN ALA ARG GLU VAL ALA ARG
SEQRES 31 B 398 LYS GLU VAL MET ARG LEU ALA SER
HET SO4 A1001 5
HET MG A1002 1
HET CBQ A2001 17
HET SO4 B1002 5
HET CBQ B3001 17
HETNAM SO4 SULFATE ION
HETNAM MG MAGNESIUM ION
HETNAM CBQ [(5-CHLORO-PYRIDIN-2-YLAMINO)-PHOSPHONO-METHYL]-
HETNAM 2 CBQ PHOSPHONIC ACID
HETSYN CBQ [{(5-CHLORO-2-PYRIDINYL)AMINO} METHYLENE]-1,1-
HETSYN 2 CBQ BISPHOSPHONATE
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 MG MG 2+
FORMUL 5 CBQ 2(C6 H9 CL N2 O6 P2)
FORMUL 8 HOH *160(H2 O)
HELIX 1 1 GLY A 10 ASN A 23 1 14
HELIX 2 2 ASN A 37 SER A 49 1 13
HELIX 3 3 ASP A 57 GLN A 71 1 15
HELIX 4 4 GLY A 80 ALA A 88 1 9
HELIX 5 5 GLY A 105 ALA A 115 1 11
HELIX 6 6 LYS A 124 LYS A 142 1 19
HELIX 7 7 ASP A 149 SER A 158 1 10
HELIX 8 8 PRO A 160 HIS A 165 1 6
HELIX 9 9 PRO A 193 MET A 200 5 8
HELIX 10 10 THR A 201 CYS A 206 1 6
HELIX 11 11 GLY A 214 THR A 223 1 10
HELIX 12 12 MET A 224 PHE A 238 1 15
HELIX 13 13 SER A 241 SER A 243 5 3
HELIX 14 14 MET A 275 TRP A 285 1 11
HELIX 15 15 ASP A 297 LEU A 301 5 5
HELIX 16 16 TYR A 314 GLY A 327 1 14
HELIX 17 17 GLY A 327 ALA A 347 1 21
HELIX 18 18 THR A 353 MET A 366 1 14
HELIX 19 19 CYS A 373 ALA A 396 1 24
HELIX 20 20 GLY B 10 ASN B 23 1 14
HELIX 21 21 ASN B 37 SER B 49 1 13
HELIX 22 22 ASP B 57 GLN B 71 1 15
HELIX 23 23 GLY B 80 ALA B 89 1 10
HELIX 24 24 GLY B 102 ALA B 104 5 3
HELIX 25 25 GLY B 105 ALA B 115 1 11
HELIX 26 26 GLU B 125 GLN B 140 1 16
HELIX 27 27 ASP B 149 LEU B 159 1 11
HELIX 28 28 PRO B 160 HIS B 165 1 6
HELIX 29 29 LEU B 172 ASN B 175 5 4
HELIX 30 30 PRO B 193 MET B 200 5 8
HELIX 31 31 THR B 201 CYS B 206 1 6
HELIX 32 32 GLY B 214 THR B 223 1 10
HELIX 33 33 MET B 224 PHE B 238 1 15
HELIX 34 34 SER B 241 SER B 243 5 3
HELIX 35 35 MET B 275 TRP B 285 1 11
HELIX 36 36 ASP B 297 LEU B 301 5 5
HELIX 37 37 TYR B 314 GLY B 327 1 14
HELIX 38 38 GLY B 327 ALA B 347 1 21
HELIX 39 39 THR B 353 ASP B 367 1 15
HELIX 40 40 CYS B 373 SER B 397 1 25
SHEET 1 A 7 GLU A 76 SER A 79 0
SHEET 2 A 7 TYR A 52 MET A 55 1 N ALA A 53 O LEU A 78
SHEET 3 A 7 PHE A 27 VAL A 33 1 N VAL A 30 O TYR A 52
SHEET 4 A 7 LYS A 1 LEU A 6 1 N ILE A 5 O ALA A 31
SHEET 5 A 7 GLN A 95 ALA A 98 1 O MET A 97 N LEU A 6
SHEET 6 A 7 THR A 118 LEU A 121 1 O THR A 118 N VAL A 96
SHEET 7 A 7 GLN A 144 PRO A 147 1 O LEU A 146 N ILE A 119
SHEET 1 B 8 MET A 245 ILE A 249 0
SHEET 2 B 8 VAL A 177 GLY A 184 1 N LEU A 182 O GLU A 246
SHEET 3 B 8 ILE A 255 TYR A 261 -1 O MET A 258 N LEU A 181
SHEET 4 B 8 VAL A 266 LEU A 270 -1 O GLN A 269 N HIS A 256
SHEET 5 B 8 VAL B 266 LEU B 270 -1 O VAL B 266 N LEU A 270
SHEET 6 B 8 ILE B 255 TYR B 261 -1 N HIS B 256 O GLN B 269
SHEET 7 B 8 VAL B 177 GLY B 184 -1 N SER B 179 O ARG B 260
SHEET 8 B 8 MET B 245 ILE B 249 1 O LEU B 248 N LEU B 182
SHEET 1 C 7 GLU B 76 SER B 79 0
SHEET 2 C 7 TYR B 52 MET B 55 1 N MET B 55 O LEU B 78
SHEET 3 C 7 PHE B 27 ALA B 34 1 N ALA B 34 O VAL B 54
SHEET 4 C 7 LYS B 1 LEU B 6 1 N LYS B 1 O ARG B 28
SHEET 5 C 7 GLN B 95 ALA B 98 1 O MET B 97 N LEU B 6
SHEET 6 C 7 THR B 118 LEU B 121 1 O LEU B 120 N VAL B 96
SHEET 7 C 7 GLN B 144 PRO B 147 1 O LEU B 146 N ILE B 119
LINK OD2 ASP A 149 MG MG A1002 1555 1555 2.48
LINK OE2 GLU A 151 MG MG A1002 1555 1555 2.28
LINK OE2 GLU A 230 MG MG A1002 1555 1555 2.69
LINK MG MG A1002 O2 CBQ A2001 1555 1555 2.06
CISPEP 1 TRP A 285 PRO A 286 0 0.30
CISPEP 2 TRP B 285 PRO B 286 0 0.37
SITE 1 AC1 7 GLY A 184 SER A 185 HIS A 208 SER A 221
SITE 2 AC1 7 LYS A 227 CBQ A2001 HOH A2051
SITE 1 AC2 9 GLY B 184 SER B 185 HIS B 208 TRP B 211
SITE 2 AC2 9 SER B 221 ASN B 226 LYS B 227 CBQ B3001
SITE 3 AC2 9 HOH B3046
SITE 1 AC3 5 LYS A 124 ASP A 149 GLU A 151 GLU A 230
SITE 2 AC3 5 CBQ A2001
SITE 1 AC4 13 LYS A 124 ASP A 149 SER A 150 GLU A 151
SITE 2 AC4 13 TRP A 211 MET A 213 ILE A 217 ASN A 226
SITE 3 AC4 13 GLU A 230 HIS A 256 PRO A 273 SO4 A1001
SITE 4 AC4 13 MG A1002
SITE 1 AC5 11 LYS B 124 ASP B 149 SER B 150 GLU B 151
SITE 2 AC5 11 TRP B 211 MET B 213 ASN B 226 GLU B 230
SITE 3 AC5 11 HIS B 256 PRO B 273 SO4 B1002
CRYST1 182.917 59.246 86.988 90.00 90.00 90.00 P 21 21 2 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 0.005467 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016879 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011496 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
