HEADER HYDROLASE 17-AUG-12 4GNU
TITLE CRYSTAL STRUCTURE OF GES-5 CARBAPENEMASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-LACTAMASE GES-5;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: EXTENDED SPECTRUM BETA-LACTAMASE GES-5, EXTENDED-SPECTRUM
COMPND 5 BETA-LACTAMASE GES-5, GES-5, GES-5 EXTENDED-SPECTRUM BETA-LACTAMASE,
COMPND 6 METALLO-BETA-LACTAMASE BLAGES-5;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 GENE: BLAGES-5;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BETA-LACTAMASE, CARBAPENEMASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.A.SMITH,S.B.VAKULENKO
REVDAT 1 24-JUL-13 4GNU 0
JRNL AUTH C.A.SMITH,H.FRASE,M.TOTH,M.KUMARASIRI,K.WIAFE,J.MUNOZ,
JRNL AUTH 2 S.MOBASHERY,S.B.VAKULENKO
JRNL TITL STRUCTURAL BASIS FOR PROGRESSION TOWARD THE CARBAPENEMASE
JRNL TITL 2 ACTIVITY IN THE GES FAMILY OF BETA-LACTAMASES.
JRNL REF J.AM.CHEM.SOC. V. 134 19512 2012
JRNL REFN ISSN 0002-7863
JRNL PMID 23148776
JRNL DOI 10.1021/JA308197J
REMARK 2
REMARK 2 RESOLUTION. 1.09 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.02
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 190745
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.172
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9538
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 32.0338 - 3.3856 0.97 6145 324 0.1633 0.1727
REMARK 3 2 3.3856 - 2.6877 0.99 6174 324 0.1615 0.1606
REMARK 3 3 2.6877 - 2.3481 0.99 6198 327 0.1583 0.1701
REMARK 3 4 2.3481 - 2.1334 0.99 6132 322 0.1495 0.1715
REMARK 3 5 2.1334 - 1.9805 0.99 6186 327 0.1539 0.1675
REMARK 3 6 1.9805 - 1.8638 0.99 6162 325 0.1513 0.1617
REMARK 3 7 1.8638 - 1.7704 0.99 6144 321 0.1439 0.1570
REMARK 3 8 1.7704 - 1.6934 0.99 6119 320 0.1380 0.1579
REMARK 3 9 1.6934 - 1.6282 0.98 6080 321 0.1304 0.1564
REMARK 3 10 1.6282 - 1.5720 0.98 6055 319 0.1266 0.1559
REMARK 3 11 1.5720 - 1.5229 0.98 6078 323 0.1250 0.1623
REMARK 3 12 1.5229 - 1.4793 0.98 6051 320 0.1263 0.1513
REMARK 3 13 1.4793 - 1.4404 0.98 6082 320 0.1311 0.1411
REMARK 3 14 1.4404 - 1.4052 0.98 6055 315 0.1354 0.1684
REMARK 3 15 1.4052 - 1.3733 0.98 6014 319 0.1398 0.1695
REMARK 3 16 1.3733 - 1.3441 0.97 5980 316 0.1451 0.1784
REMARK 3 17 1.3441 - 1.3172 0.97 6050 319 0.1526 0.1718
REMARK 3 18 1.3172 - 1.2923 0.97 6016 318 0.1569 0.1751
REMARK 3 19 1.2923 - 1.2692 0.97 5999 314 0.1598 0.1852
REMARK 3 20 1.2692 - 1.2477 0.97 5964 314 0.1735 0.1894
REMARK 3 21 1.2477 - 1.2276 0.97 6047 318 0.1706 0.1928
REMARK 3 22 1.2276 - 1.2087 0.97 5968 314 0.1797 0.2014
REMARK 3 23 1.2087 - 1.1909 0.97 6008 317 0.1829 0.2065
REMARK 3 24 1.1909 - 1.1742 0.97 5938 314 0.1844 0.1989
REMARK 3 25 1.1742 - 1.1583 0.96 5975 312 0.1868 0.2119
REMARK 3 26 1.1583 - 1.1433 0.96 5950 314 0.1908 0.1979
REMARK 3 27 1.1433 - 1.1290 0.96 5906 312 0.2092 0.2219
REMARK 3 28 1.1290 - 1.1154 0.96 5957 314 0.2181 0.2443
REMARK 3 29 1.1154 - 1.1024 0.96 5939 312 0.2325 0.2639
REMARK 3 30 1.1024 - 1.0900 0.94 5835 303 0.2525 0.2623
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.41
REMARK 3 B_SOL : 45.17
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.330
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) : 0.93650
REMARK 3 B22 (A**2) : 0.16980
REMARK 3 B33 (A**2) : -1.10620
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -2.33860
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 4369
REMARK 3 ANGLE : 1.147 5964
REMARK 3 CHIRALITY : 0.078 684
REMARK 3 PLANARITY : 0.006 777
REMARK 3 DIHEDRAL : 14.185 1704
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 4GNU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-OCT-12.
REMARK 100 THE RCSB ID CODE IS RCSB074417.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.82654
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-325
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 191963
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.086
REMARK 200 RESOLUTION RANGE LOW (A) : 32.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.50100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.110
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 (%): 35.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: UNBUFFERED 0.2% SODIUM IODIDE AND 18-
REMARK 280 20% PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 40.23500
REMARK 290 SMTRY3 2 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 ARG A 2
REMARK 465 PHE A 3
REMARK 465 ILE A 4
REMARK 465 HIS A 5
REMARK 465 ALA A 6
REMARK 465 LEU A 7
REMARK 465 LEU A 8
REMARK 465 LEU A 9
REMARK 465 ALA A 10
REMARK 465 GLY A 11
REMARK 465 ILE A 12
REMARK 465 ALA A 13
REMARK 465 HIS A 14
REMARK 465 SER A 15
REMARK 465 ALA A 16
REMARK 465 TYR A 17
REMARK 465 ALA A 18
REMARK 465 SER A 19
REMARK 465 GLU A 20
REMARK 465 ASP A 286
REMARK 465 LYS A 287
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 PHE B 3
REMARK 465 ILE B 4
REMARK 465 HIS B 5
REMARK 465 ALA B 6
REMARK 465 LEU B 7
REMARK 465 LEU B 8
REMARK 465 LEU B 9
REMARK 465 ALA B 10
REMARK 465 GLY B 11
REMARK 465 ILE B 12
REMARK 465 ALA B 13
REMARK 465 HIS B 14
REMARK 465 SER B 15
REMARK 465 ALA B 16
REMARK 465 TYR B 17
REMARK 465 ALA B 18
REMARK 465 SER B 19
REMARK 465 THR B 285
REMARK 465 ASP B 286
REMARK 465 LYS B 287
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 CYS A 63 -142.67 45.63
REMARK 500 TRP A 99 70.18 54.69
REMARK 500 THR A 215 -130.26 -106.63
REMARK 500 GLN A 247 -112.76 56.89
REMARK 500 CYS B 63 -146.72 50.22
REMARK 500 THR B 215 -128.13 -106.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GOG RELATED DB: PDB
REMARK 900 RELATED ID: 4H8R RELATED DB: PDB
DBREF 4GNU A 1 287 UNP A0EL75 A0EL75_PSEAI 1 287
DBREF 4GNU B 1 287 UNP A0EL75 A0EL75_PSEAI 1 287
SEQRES 1 A 287 MET ARG PHE ILE HIS ALA LEU LEU LEU ALA GLY ILE ALA
SEQRES 2 A 287 HIS SER ALA TYR ALA SER GLU LYS LEU THR PHE LYS THR
SEQRES 3 A 287 ASP LEU GLU LYS LEU GLU ARG GLU LYS ALA ALA GLN ILE
SEQRES 4 A 287 GLY VAL ALA ILE VAL ASP PRO GLN GLY GLU ILE VAL ALA
SEQRES 5 A 287 GLY HIS ARG MET ALA GLN ARG PHE ALA MET CYS SER THR
SEQRES 6 A 287 PHE LYS PHE PRO LEU ALA ALA LEU VAL PHE GLU ARG ILE
SEQRES 7 A 287 ASP SER GLY THR GLU ARG GLY ASP ARG LYS LEU SER TYR
SEQRES 8 A 287 GLY PRO ASP MET ILE VAL GLU TRP SER PRO ALA THR GLU
SEQRES 9 A 287 ARG PHE LEU ALA SER GLY HIS MET THR VAL LEU GLU ALA
SEQRES 10 A 287 ALA GLN ALA ALA VAL GLN LEU SER ASP ASN GLY ALA THR
SEQRES 11 A 287 ASN LEU LEU LEU ARG GLU ILE GLY GLY PRO ALA ALA MET
SEQRES 12 A 287 THR GLN TYR PHE ARG LYS ILE GLY ASP SER VAL SER ARG
SEQRES 13 A 287 LEU ASP ARG LYS GLU PRO GLU MET SER ASP ASN THR PRO
SEQRES 14 A 287 GLY ASP LEU ARG ASP THR THR THR PRO ILE ALA MET ALA
SEQRES 15 A 287 ARG THR VAL ALA LYS VAL LEU TYR GLY GLY ALA LEU THR
SEQRES 16 A 287 SER THR SER THR HIS THR ILE GLU ARG TRP LEU ILE GLY
SEQRES 17 A 287 ASN GLN THR GLY ASP ALA THR LEU ARG ALA GLY PHE PRO
SEQRES 18 A 287 LYS ASP TRP VAL VAL GLY GLU LYS THR GLY THR CYS ALA
SEQRES 19 A 287 ASN GLY GLY ARG ASN ASP ILE GLY PHE PHE LYS ALA GLN
SEQRES 20 A 287 GLU ARG ASP TYR ALA VAL ALA VAL TYR THR THR ALA PRO
SEQRES 21 A 287 LYS LEU SER ALA VAL GLU ARG ASP GLU LEU VAL ALA SER
SEQRES 22 A 287 VAL GLY GLN VAL ILE THR GLN LEU ILE LEU SER THR ASP
SEQRES 23 A 287 LYS
SEQRES 1 B 287 MET ARG PHE ILE HIS ALA LEU LEU LEU ALA GLY ILE ALA
SEQRES 2 B 287 HIS SER ALA TYR ALA SER GLU LYS LEU THR PHE LYS THR
SEQRES 3 B 287 ASP LEU GLU LYS LEU GLU ARG GLU LYS ALA ALA GLN ILE
SEQRES 4 B 287 GLY VAL ALA ILE VAL ASP PRO GLN GLY GLU ILE VAL ALA
SEQRES 5 B 287 GLY HIS ARG MET ALA GLN ARG PHE ALA MET CYS SER THR
SEQRES 6 B 287 PHE LYS PHE PRO LEU ALA ALA LEU VAL PHE GLU ARG ILE
SEQRES 7 B 287 ASP SER GLY THR GLU ARG GLY ASP ARG LYS LEU SER TYR
SEQRES 8 B 287 GLY PRO ASP MET ILE VAL GLU TRP SER PRO ALA THR GLU
SEQRES 9 B 287 ARG PHE LEU ALA SER GLY HIS MET THR VAL LEU GLU ALA
SEQRES 10 B 287 ALA GLN ALA ALA VAL GLN LEU SER ASP ASN GLY ALA THR
SEQRES 11 B 287 ASN LEU LEU LEU ARG GLU ILE GLY GLY PRO ALA ALA MET
SEQRES 12 B 287 THR GLN TYR PHE ARG LYS ILE GLY ASP SER VAL SER ARG
SEQRES 13 B 287 LEU ASP ARG LYS GLU PRO GLU MET SER ASP ASN THR PRO
SEQRES 14 B 287 GLY ASP LEU ARG ASP THR THR THR PRO ILE ALA MET ALA
SEQRES 15 B 287 ARG THR VAL ALA LYS VAL LEU TYR GLY GLY ALA LEU THR
SEQRES 16 B 287 SER THR SER THR HIS THR ILE GLU ARG TRP LEU ILE GLY
SEQRES 17 B 287 ASN GLN THR GLY ASP ALA THR LEU ARG ALA GLY PHE PRO
SEQRES 18 B 287 LYS ASP TRP VAL VAL GLY GLU LYS THR GLY THR CYS ALA
SEQRES 19 B 287 ASN GLY GLY ARG ASN ASP ILE GLY PHE PHE LYS ALA GLN
SEQRES 20 B 287 GLU ARG ASP TYR ALA VAL ALA VAL TYR THR THR ALA PRO
SEQRES 21 B 287 LYS LEU SER ALA VAL GLU ARG ASP GLU LEU VAL ALA SER
SEQRES 22 B 287 VAL GLY GLN VAL ILE THR GLN LEU ILE LEU SER THR ASP
SEQRES 23 B 287 LYS
HET EPE A 301 15
HET EPE B 301 15
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EPE HEPES
FORMUL 3 EPE 2(C8 H18 N2 O4 S)
FORMUL 5 HOH *583(H2 O)
HELIX 1 1 LYS A 21 ALA A 36 1 16
HELIX 2 2 CYS A 63 THR A 65 5 3
HELIX 3 3 PHE A 66 SER A 80 1 15
HELIX 4 4 GLY A 92 ILE A 96 5 5
HELIX 5 5 SER A 100 LEU A 107 1 8
HELIX 6 6 VAL A 114 SER A 125 1 12
HELIX 7 7 ASP A 126 GLY A 138 1 13
HELIX 8 8 GLY A 138 ILE A 150 1 13
HELIX 9 9 PRO A 162 ASP A 166 5 5
HELIX 10 10 THR A 177 TYR A 190 1 14
HELIX 11 11 THR A 195 GLY A 208 1 14
HELIX 12 12 THR A 215 PHE A 220 5 6
HELIX 13 13 SER A 263 SER A 284 1 22
HELIX 14 14 LYS B 21 ALA B 36 1 16
HELIX 15 15 CYS B 63 THR B 65 5 3
HELIX 16 16 PHE B 66 SER B 80 1 15
HELIX 17 17 GLY B 92 ILE B 96 5 5
HELIX 18 18 SER B 100 LEU B 107 1 8
HELIX 19 19 VAL B 114 SER B 125 1 12
HELIX 20 20 ASP B 126 GLY B 138 1 13
HELIX 21 21 GLY B 138 ILE B 150 1 13
HELIX 22 22 PRO B 162 ASP B 166 5 5
HELIX 23 23 THR B 177 GLY B 191 1 15
HELIX 24 24 THR B 195 GLY B 208 1 14
HELIX 25 25 THR B 215 PHE B 220 1 6
HELIX 26 26 SER B 263 SER B 284 1 22
SHEET 1 A 5 ILE A 50 HIS A 54 0
SHEET 2 A 5 GLN A 38 VAL A 44 -1 N ILE A 43 O VAL A 51
SHEET 3 A 5 ARG A 249 THR A 258 -1 O TYR A 256 N GLY A 40
SHEET 4 A 5 GLY A 237 ALA A 246 -1 N GLY A 242 O VAL A 253
SHEET 5 A 5 VAL A 225 CYS A 233 -1 N LYS A 229 O ILE A 241
SHEET 1 B 2 PHE A 60 ALA A 61 0
SHEET 2 B 2 THR A 175 THR A 176 -1 O THR A 176 N PHE A 60
SHEET 1 C 2 LYS A 88 SER A 90 0
SHEET 2 C 2 HIS A 111 THR A 113 -1 O MET A 112 N LEU A 89
SHEET 1 D 5 ILE B 50 HIS B 54 0
SHEET 2 D 5 GLN B 38 VAL B 44 -1 N ILE B 43 O VAL B 51
SHEET 3 D 5 ARG B 249 THR B 258 -1 O TYR B 256 N GLY B 40
SHEET 4 D 5 GLY B 237 ALA B 246 -1 N GLY B 242 O VAL B 253
SHEET 5 D 5 VAL B 225 CYS B 233 -1 N LYS B 229 O ILE B 241
SHEET 1 E 2 PHE B 60 ALA B 61 0
SHEET 2 E 2 THR B 175 THR B 176 -1 O THR B 176 N PHE B 60
SHEET 1 F 2 LYS B 88 SER B 90 0
SHEET 2 F 2 HIS B 111 THR B 113 -1 O MET B 112 N LEU B 89
SSBOND 1 CYS A 63 CYS A 233 1555 1555 2.02
SSBOND 2 CYS B 63 CYS B 233 1555 1555 2.01
CISPEP 1 GLU A 161 PRO A 162 0 0.96
CISPEP 2 GLU B 161 PRO B 162 0 1.82
SITE 1 AC1 12 SER A 64 TRP A 99 SER A 125 LYS A 229
SITE 2 AC1 12 THR A 230 GLY A 231 THR A 232 ARG A 238
SITE 3 AC1 12 HOH A 401 HOH A 625 HOH A 633 HOH A 644
SITE 1 AC2 10 SER B 64 TRP B 99 SER B 125 LYS B 229
SITE 2 AC2 10 THR B 230 GLY B 231 THR B 232 ARG B 238
SITE 3 AC2 10 HOH B 401 HOH B 527
CRYST1 42.660 80.470 71.230 90.00 101.48 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 0.023441 0.000000 0.004762 0.00000
SCALE2 0.000000 0.012427 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014326 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
