HEADER HYDROLASE 15-MAY-06 2H0Y
TITLE CRYSTAL STRUCTURE OF THE M69V E166A DOUBLE MUTANT OF SHV-1 B-LACTAMASE
TITLE 2 COMPLEXED TO SULBACTAM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-LACTAMASE SHV-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PIT-2;
COMPND 5 EC: 3.5.2.6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLEBSIELLA PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 573;
SOURCE 4 GENE: BLA, SHV1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ANTIBIOTIC RESISTANCE, B-LACTAMASE INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.VAN DEN AKKER,P.S.PADAYATTI
REVDAT 5 30-AUG-23 2H0Y 1 REMARK
REVDAT 4 20-OCT-21 2H0Y 1 REMARK SEQADV LINK
REVDAT 3 18-OCT-17 2H0Y 1 REMARK
REVDAT 2 24-FEB-09 2H0Y 1 VERSN
REVDAT 1 30-JAN-07 2H0Y 0
JRNL AUTH M.A.TOTIR,P.S.PADAYATTI,M.S.HELFAND,M.P.CAREY,R.A.BONOMO,
JRNL AUTH 2 P.R.CAREY,F.VAN DEN AKKER
JRNL TITL EFFECT OF THE INHIBITOR-RESISTANT M69V SUBSTITUTION ON THE
JRNL TITL 2 STRUCTURES AND POPULATIONS OF TRANS-ENAMINE BETA-LACTAMASE
JRNL TITL 3 INTERMEDIATES.
JRNL REF BIOCHEMISTRY V. 45 11895 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 17002290
JRNL DOI 10.1021/BI060990M
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 9.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1253567.720
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 25308
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) : 0.175
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2504
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3759
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE : 0.3170
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 403
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2019
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 65
REMARK 3 SOLVENT ATOMS : 226
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.55000
REMARK 3 B22 (A**2) : -3.00000
REMARK 3 B33 (A**2) : 1.46000
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.19
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) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.950
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) : 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 : FLAT MODEL
REMARK 3 KSOL : 0.46
REMARK 3 BSOL : 85.74
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : PRODR_SUL1.PAR
REMARK 3 PARAMETER FILE 4 : NEW_CYMAL.PAR
REMARK 3 PARAMETER FILE 5 : HEPES.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NEW_LIGANDS_SUL1.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2H0Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-06.
REMARK 100 THE DEPOSITION ID IS D_1000037792.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-SEP-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 4.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.46
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NOIR-1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SOFTWARE AT ALS 4.2.2.
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25354
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 9.990
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
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: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1RCJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 6000, 0.1 M HEPES, 0.56MM
REMARK 280 CYMAL-6. CRYSTAL SOAKED FOR 10 MINUTES IN 50MM SUBLACTAM PRIOR
REMARK 280 TO FREEZING AND DATA COLLECTION, PH 7.0, VAPOR DIFFUSION,
REMARK 280 SITTING 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 24.79500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.81500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.65500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.81500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.79500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.65500
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: PROTEIN 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 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 OG SER A 70 O8 TSL A 501 2.15
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 VAL A 69 -144.60 45.83
REMARK 500 TYR A 105 84.26 66.67
REMARK 500 THR A 167 -68.19 105.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 MA4 A 401
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TSL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MA4 A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MA4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ESA A 600
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2A49 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CLAVULANIC ACID BOUND TO E166A VARIANT OF SHV-
REMARK 900 1 B-LACTAMASE
REMARK 900 RELATED ID: 2A3U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SULBACTAM BOUND TO E166A VARIANT OF SHV-1 B-
REMARK 900 LACTAMASE
REMARK 900 RELATED ID: 1RCJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E166A MUTANT OF SHV-1 B-LACTAMASE WITH THE
REMARK 900 TRANS-ENAMINE INTERMEDIATE OF TAZOBACTAM
REMARK 900 RELATED ID: 2H10 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE M69V E166A DOUBLE MUTANT OF SHV-1 B-
REMARK 900 LACTAMASE COMPLEXED TO TAZOBACTAM
DBREF 2H0Y A 26 290 UNP P0AD64 BLA1_KLEPN 22 286
SEQADV 2H0Y VAL A 69 UNP P0AD64 MET 65 ENGINEERED MUTATION
SEQADV 2H0Y ALA A 166 UNP P0AD64 GLU 162 ENGINEERED MUTATION
SEQRES 1 A 265 SER PRO GLN PRO LEU GLU GLN ILE LYS LEU SER GLU SER
SEQRES 2 A 265 GLN LEU SER GLY ARG VAL GLY MET ILE GLU MET ASP LEU
SEQRES 3 A 265 ALA SER GLY ARG THR LEU THR ALA TRP ARG ALA ASP GLU
SEQRES 4 A 265 ARG PHE PRO MET VAL SER THR PHE LYS VAL VAL LEU CYS
SEQRES 5 A 265 GLY ALA VAL LEU ALA ARG VAL ASP ALA GLY ASP GLU GLN
SEQRES 6 A 265 LEU GLU ARG LYS ILE HIS TYR ARG GLN GLN ASP LEU VAL
SEQRES 7 A 265 ASP TYR SER PRO VAL SER GLU LYS HIS LEU ALA ASP GLY
SEQRES 8 A 265 MET THR VAL GLY GLU LEU CYS ALA ALA ALA ILE THR MET
SEQRES 9 A 265 SER ASP ASN SER ALA ALA ASN LEU LEU LEU ALA THR VAL
SEQRES 10 A 265 GLY GLY PRO ALA GLY LEU THR ALA PHE LEU ARG GLN ILE
SEQRES 11 A 265 GLY ASP ASN VAL THR ARG LEU ASP ARG TRP ALA THR GLU
SEQRES 12 A 265 LEU ASN GLU ALA LEU PRO GLY ASP ALA ARG ASP THR THR
SEQRES 13 A 265 THR PRO ALA SER MET ALA ALA THR LEU ARG LYS LEU LEU
SEQRES 14 A 265 THR SER GLN ARG LEU SER ALA ARG SER GLN ARG GLN LEU
SEQRES 15 A 265 LEU GLN TRP MET VAL ASP ASP ARG VAL ALA GLY PRO LEU
SEQRES 16 A 265 ILE ARG SER VAL LEU PRO ALA GLY TRP PHE ILE ALA ASP
SEQRES 17 A 265 LYS THR GLY ALA GLY GLU ARG GLY ALA ARG GLY ILE VAL
SEQRES 18 A 265 ALA LEU LEU GLY PRO ASN ASN LYS ALA GLU ARG ILE VAL
SEQRES 19 A 265 VAL ILE TYR LEU ARG ASP THR PRO ALA SER MET ALA GLU
SEQRES 20 A 265 ARG ASN GLN GLN ILE ALA GLY ILE GLY ALA ALA LEU ILE
SEQRES 21 A 265 GLU HIS TRP GLN ARG
HET TSL A 501 15
HET MA4 A 400 35
HET MA4 A 401 9
HET ESA A 600 6
HETNAM TSL TRANS-ENAMINE INTERMEDIATE OF SULBACTAM
HETNAM MA4 CYCLOHEXYL-HEXYL-BETA-D-MALTOSIDE
HETNAM ESA ETHANESULFONIC ACID
FORMUL 2 TSL C8 H13 N O5 S
FORMUL 3 MA4 2(C24 H44 O11)
FORMUL 5 ESA C2 H6 O3 S
FORMUL 6 HOH *226(H2 O)
HELIX 1 1 GLN A 28 SER A 41 1 14
HELIX 2 2 THR A 71 ALA A 86 1 16
HELIX 3 3 ARG A 98 LEU A 102 5 5
HELIX 4 4 VAL A 108 HIS A 112 5 5
HELIX 5 5 VAL A 119 SER A 130 1 12
HELIX 6 6 ASP A 131 VAL A 142 1 12
HELIX 7 7 GLY A 143 ILE A 155 1 13
HELIX 8 8 THR A 167 GLU A 171 5 5
HELIX 9 9 THR A 182 SER A 196 1 15
HELIX 10 10 SER A 200 ASP A 213 1 14
HELIX 11 11 ALA A 217 LEU A 225 1 9
HELIX 12 12 GLU A 240 GLY A 242 5 3
HELIX 13 13 SER A 271 HIS A 289 1 19
SHEET 1 A 5 THR A 56 TRP A 60 0
SHEET 2 A 5 ARG A 43 ASP A 50 -1 N GLU A 48 O LEU A 57
SHEET 3 A 5 ARG A 259 ARG A 266 -1 O ILE A 260 N MET A 49
SHEET 4 A 5 ARG A 244 GLY A 251 -1 N ALA A 248 O VAL A 261
SHEET 5 A 5 PHE A 230 ALA A 237 -1 N PHE A 230 O GLY A 251
SHEET 1 B 2 PHE A 66 PRO A 67 0
SHEET 2 B 2 THR A 180 THR A 181 -1 O THR A 181 N PHE A 66
SHEET 1 C 2 LYS A 94 ILE A 95 0
SHEET 2 C 2 MET A 117 THR A 118 -1 O MET A 117 N ILE A 95
SSBOND 1 CYS A 77 CYS A 123 1555 1555 2.04
LINK OG SER A 70 C7 TSL A 501 1555 1555 1.36
SITE 1 AC1 9 SER A 70 ASP A 104 TYR A 105 ASN A 132
SITE 2 AC1 9 THR A 167 ASN A 170 GLY A 236 ALA A 237
SITE 3 AC1 9 ESA A 600
SITE 1 AC2 15 ARG A 93 HIS A 96 ARG A 98 VAL A 224
SITE 2 AC2 15 PRO A 226 ALA A 248 VAL A 261 ILE A 263
SITE 3 AC2 15 ALA A 280 ALA A 284 GLU A 288 HOH A 604
SITE 4 AC2 15 HOH A 652 HOH A 739 HOH A 759
SITE 1 AC3 2 ARG A 244 ILE A 279
SITE 1 AC4 8 SER A 70 SER A 130 VAL A 216 LYS A 234
SITE 2 AC4 8 THR A 235 GLY A 236 ARG A 244 TSL A 501
CRYST1 49.590 55.310 83.630 90.00 90.00 90.00 P 21 21 21 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 0.020165 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018080 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011957 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
