HEADER HYDROLASE/HYDROLASE INHIBITOR 01-FEB-09 3G31
TITLE CTX-M-9 CLASS A BETA-LACTAMASE COMPLEXED WITH COMPOUND 4 (GF1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-LACTAMASE CTX-M-9A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 29-291;
COMPND 5 SYNONYM: BETA-LACTAMASE, CTX-M-9 BETA-LACTAMASE, BETALACTAMASE CTX-M-
COMPND 6 9;
COMPND 7 EC: 3.5.2.6;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: BLACTX-M-9, BLACTX-M-9A, CTX-M;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-9A
KEYWDS CTX-M, BETA-LACTAMASE, MOLECULAR DOCKING, FRAGMENT, INHIBITOR,
KEYWDS 2 ANTIBIOTIC RESISTANCE, HYDROLASE, PLASMID, HYDROLASE-HYDROLASE
KEYWDS 3 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.CHEN,B.K.SHOICHET
REVDAT 4 06-SEP-23 3G31 1 REMARK
REVDAT 3 01-NOV-17 3G31 1 REMARK
REVDAT 2 05-MAY-09 3G31 1 JRNL
REVDAT 1 24-MAR-09 3G31 0
JRNL AUTH Y.CHEN,B.K.SHOICHET
JRNL TITL MOLECULAR DOCKING AND LIGAND SPECIFICITY IN FRAGMENT-BASED
JRNL TITL 2 INHIBITOR DISCOVERY
JRNL REF NAT.CHEM.BIOL. V. 5 358 2009
JRNL REFN ISSN 1552-4450
JRNL PMID 19305397
JRNL DOI 10.1038/NCHEMBIO.155
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 48236
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 + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2443
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2992
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.40
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE SET COUNT : 144
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3901
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 107
REMARK 3 SOLVENT ATOMS : 356
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : -0.44000
REMARK 3 B33 (A**2) : 1.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.40000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.116
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.109
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.072
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.139
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4129 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5650 ; 1.668 ; 1.998
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 535 ; 5.910 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 168 ;39.194 ;24.643
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 667 ;12.329 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;13.557 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 676 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3127 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2122 ; 0.199 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2927 ; 0.300 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 323 ; 0.118 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 74 ; 0.177 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 38 ; 0.094 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2688 ; 0.714 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4227 ; 1.149 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1591 ; 1.968 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1419 ; 3.051 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3G31 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-09.
REMARK 100 THE DEPOSITION ID IS D_1000051359.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-APR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.11587
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM Q315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48267
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.10300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8170
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
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: REFMAC 5.2.0019
REMARK 200 STARTING MODEL: PDB ENTRY 1YLJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM PHOSPHATE, PH 8.7, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 292K
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 53.38250
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 GLN A 25
REMARK 465 GLN B 25
REMARK 465 THR B 26
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 69 -136.85 46.86
REMARK 500 VAL A 103 -134.78 -109.24
REMARK 500 TYR A 105 97.43 -165.94
REMARK 500 SER A 220 -128.83 -103.98
REMARK 500 CYS B 69 -139.81 49.83
REMARK 500 VAL B 103 -136.74 -110.44
REMARK 500 TYR B 105 97.66 -164.24
REMARK 500 SER B 220 -132.31 -105.76
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 GF1 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GF1 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GF1 A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GF1 B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GF1 B 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3G2Y RELATED DB: PDB
REMARK 900 RELATED ID: 3G2Z RELATED DB: PDB
REMARK 900 RELATED ID: 3G30 RELATED DB: PDB
REMARK 900 RELATED ID: 3G32 RELATED DB: PDB
REMARK 900 RELATED ID: 3G34 RELATED DB: PDB
REMARK 900 RELATED ID: 3G35 RELATED DB: PDB
DBREF 3G31 A 25 290 UNP Q9L5C8 Q9L5C8_ECOLX 29 291
DBREF 3G31 B 25 290 UNP Q9L5C8 Q9L5C8_ECOLX 29 291
SEQRES 1 A 263 GLN THR SER ALA VAL GLN GLN LYS LEU ALA ALA LEU GLU
SEQRES 2 A 263 LYS SER SER GLY GLY ARG LEU GLY VAL ALA LEU ILE ASP
SEQRES 3 A 263 THR ALA ASP ASN THR GLN VAL LEU TYR ARG GLY ASP GLU
SEQRES 4 A 263 ARG PHE PRO MET CYS SER THR SER LYS VAL MET ALA ALA
SEQRES 5 A 263 ALA ALA VAL LEU LYS GLN SER GLU THR GLN LYS GLN LEU
SEQRES 6 A 263 LEU ASN GLN PRO VAL GLU ILE LYS PRO ALA ASP LEU VAL
SEQRES 7 A 263 ASN TYR ASN PRO ILE ALA GLU LYS HIS VAL ASN GLY THR
SEQRES 8 A 263 MET THR LEU ALA GLU LEU SER ALA ALA ALA LEU GLN TYR
SEQRES 9 A 263 SER ASP ASN THR ALA MET ASN LYS LEU ILE ALA GLN LEU
SEQRES 10 A 263 GLY GLY PRO GLY GLY VAL THR ALA PHE ALA ARG ALA ILE
SEQRES 11 A 263 GLY ASP GLU THR PHE ARG LEU ASP ARG THR GLU PRO THR
SEQRES 12 A 263 LEU ASN THR ALA ILE PRO GLY ASP PRO ARG ASP THR THR
SEQRES 13 A 263 THR PRO ARG ALA MET ALA GLN THR LEU ARG GLN LEU THR
SEQRES 14 A 263 LEU GLY HIS ALA LEU GLY GLU THR GLN ARG ALA GLN LEU
SEQRES 15 A 263 VAL THR TRP LEU LYS GLY ASN THR THR GLY ALA ALA SER
SEQRES 16 A 263 ILE ARG ALA GLY LEU PRO THR SER TRP THR ALA GLY ASP
SEQRES 17 A 263 LYS THR GLY SER GLY ASP TYR GLY THR THR ASN ASP ILE
SEQRES 18 A 263 ALA VAL ILE TRP PRO GLN GLY ARG ALA PRO LEU VAL LEU
SEQRES 19 A 263 VAL THR TYR PHE THR GLN PRO GLN GLN ASN ALA GLU SER
SEQRES 20 A 263 ARG ARG ASP VAL LEU ALA SER ALA ALA ARG ILE ILE ALA
SEQRES 21 A 263 GLU GLY LEU
SEQRES 1 B 263 GLN THR SER ALA VAL GLN GLN LYS LEU ALA ALA LEU GLU
SEQRES 2 B 263 LYS SER SER GLY GLY ARG LEU GLY VAL ALA LEU ILE ASP
SEQRES 3 B 263 THR ALA ASP ASN THR GLN VAL LEU TYR ARG GLY ASP GLU
SEQRES 4 B 263 ARG PHE PRO MET CYS SER THR SER LYS VAL MET ALA ALA
SEQRES 5 B 263 ALA ALA VAL LEU LYS GLN SER GLU THR GLN LYS GLN LEU
SEQRES 6 B 263 LEU ASN GLN PRO VAL GLU ILE LYS PRO ALA ASP LEU VAL
SEQRES 7 B 263 ASN TYR ASN PRO ILE ALA GLU LYS HIS VAL ASN GLY THR
SEQRES 8 B 263 MET THR LEU ALA GLU LEU SER ALA ALA ALA LEU GLN TYR
SEQRES 9 B 263 SER ASP ASN THR ALA MET ASN LYS LEU ILE ALA GLN LEU
SEQRES 10 B 263 GLY GLY PRO GLY GLY VAL THR ALA PHE ALA ARG ALA ILE
SEQRES 11 B 263 GLY ASP GLU THR PHE ARG LEU ASP ARG THR GLU PRO THR
SEQRES 12 B 263 LEU ASN THR ALA ILE PRO GLY ASP PRO ARG ASP THR THR
SEQRES 13 B 263 THR PRO ARG ALA MET ALA GLN THR LEU ARG GLN LEU THR
SEQRES 14 B 263 LEU GLY HIS ALA LEU GLY GLU THR GLN ARG ALA GLN LEU
SEQRES 15 B 263 VAL THR TRP LEU LYS GLY ASN THR THR GLY ALA ALA SER
SEQRES 16 B 263 ILE ARG ALA GLY LEU PRO THR SER TRP THR ALA GLY ASP
SEQRES 17 B 263 LYS THR GLY SER GLY ASP TYR GLY THR THR ASN ASP ILE
SEQRES 18 B 263 ALA VAL ILE TRP PRO GLN GLY ARG ALA PRO LEU VAL LEU
SEQRES 19 B 263 VAL THR TYR PHE THR GLN PRO GLN GLN ASN ALA GLU SER
SEQRES 20 B 263 ARG ARG ASP VAL LEU ALA SER ALA ALA ARG ILE ILE ALA
SEQRES 21 B 263 GLU GLY LEU
HET GF1 A 1 17
HET GF1 A 2 17
HET GF1 A 4 17
HET PO4 A 6 5
HET DMS A 9 4
HET DMS A 10 4
HET GF1 B 3 17
HET GF1 B 5 17
HET PO4 B 7 5
HET DMS B 8 4
HETNAM GF1 (2S)-2-[(3AR,4R,7S,7AS)-1,3-DIOXOOCTAHYDRO-2H-4,7-
HETNAM 2 GF1 METHANOISOINDOL-2-YL]PROPANOIC ACID
HETNAM PO4 PHOSPHATE ION
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 3 GF1 5(C12 H15 N O4)
FORMUL 6 PO4 2(O4 P 3-)
FORMUL 7 DMS 3(C2 H6 O S)
FORMUL 13 HOH *356(H2 O)
HELIX 1 1 SER A 27 GLY A 41 1 15
HELIX 2 2 CYS A 69 THR A 71 5 3
HELIX 3 3 SER A 72 GLU A 85 1 14
HELIX 4 4 GLN A 89 ASN A 92 5 4
HELIX 5 5 LYS A 98 LEU A 102 5 5
HELIX 6 6 ILE A 108 HIS A 112 5 5
HELIX 7 7 LEU A 119 SER A 130 1 12
HELIX 8 8 ASP A 131 LEU A 142 1 12
HELIX 9 9 GLY A 144 ILE A 155 1 12
HELIX 10 10 PRO A 167 THR A 171 5 5
HELIX 11 11 THR A 182 LEU A 195 1 14
HELIX 12 12 GLY A 200 GLY A 213 1 14
HELIX 13 13 SER A 220 LEU A 225 5 6
HELIX 14 14 ARG A 275 GLY A 289 1 15
HELIX 15 15 SER B 27 GLY B 41 1 15
HELIX 16 16 CYS B 69 THR B 71 5 3
HELIX 17 17 SER B 72 GLU B 85 1 14
HELIX 18 18 GLN B 89 ASN B 92 5 4
HELIX 19 19 LYS B 98 LEU B 102 5 5
HELIX 20 20 ILE B 108 VAL B 113 5 6
HELIX 21 21 LEU B 119 SER B 130 1 12
HELIX 22 22 ASP B 131 LEU B 142 1 12
HELIX 23 23 GLY B 144 ILE B 155 1 12
HELIX 24 24 PRO B 167 THR B 171 5 5
HELIX 25 25 THR B 182 LEU B 195 1 14
HELIX 26 26 GLY B 200 GLY B 213 1 14
HELIX 27 27 SER B 220 LEU B 225 5 6
HELIX 28 28 ARG B 275 LEU B 290 1 16
SHEET 1 A 5 GLN A 56 TYR A 60 0
SHEET 2 A 5 ARG A 43 ASP A 50 -1 N LEU A 48 O VAL A 57
SHEET 3 A 5 LEU A 259 THR A 266 -1 O THR A 266 N ARG A 43
SHEET 4 A 5 THR A 243 TRP A 251 -1 N ILE A 250 O LEU A 259
SHEET 5 A 5 THR A 230 GLY A 238 -1 N THR A 230 O TRP 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 PRO A 94 ILE A 97 0
SHEET 2 C 2 GLY A 115 THR A 118 -1 O GLY A 115 N ILE A 97
SHEET 1 D 5 GLN B 56 TYR B 60 0
SHEET 2 D 5 ARG B 43 ASP B 50 -1 N LEU B 48 O VAL B 57
SHEET 3 D 5 LEU B 259 THR B 266 -1 O TYR B 264 N GLY B 45
SHEET 4 D 5 THR B 243 TRP B 251 -1 N ALA B 248 O LEU B 261
SHEET 5 D 5 THR B 230 GLY B 238 -1 N THR B 230 O TRP B 251
SHEET 1 E 2 PHE B 66 PRO B 67 0
SHEET 2 E 2 THR B 180 THR B 181 -1 O THR B 181 N PHE B 66
SHEET 1 F 2 PRO B 94 ILE B 97 0
SHEET 2 F 2 GLY B 115 THR B 118 -1 O GLY B 115 N ILE B 97
CISPEP 1 GLU A 166 PRO A 167 0 1.61
CISPEP 2 GLU B 166 PRO B 167 0 4.33
SITE 1 AC1 4 LYS A 111 TYR A 129 HOH A 338 HOH A 339
SITE 1 AC2 10 DMS A 10 GLU A 37 LYS A 38 GLY A 41
SITE 2 AC2 10 GLY A 42 ARG A 61 GLN B 56 ARG B 184
SITE 3 AC2 10 HOH B 325 HOH B 337
SITE 1 AC3 11 PO4 A 6 HOH A 11 SER A 70 ASN A 104
SITE 2 AC3 11 TYR A 105 SER A 130 ASN A 132 GLY A 236
SITE 3 AC3 11 SER A 237 HOH A 331 HOH A 349
SITE 1 AC4 9 GF1 A 4 HOH A 11 SER A 70 SER A 130
SITE 2 AC4 9 THR A 235 GLY A 236 SER A 237 HOH A 408
SITE 3 AC4 9 HOH A 454
SITE 1 AC5 5 ARG A 222 PRO A 226 THR A 227 TRP A 229
SITE 2 AC5 5 HOH A 371
SITE 1 AC6 7 GF1 A 2 ARG A 43 THR A 266 GLN A 267
SITE 2 AC6 7 PRO A 268 HOH A 398 ASP B 63
SITE 1 AC7 12 PO4 B 7 SER B 70 ASN B 104 TYR B 105
SITE 2 AC7 12 SER B 130 ASN B 132 GLY B 236 SER B 237
SITE 3 AC7 12 HOH B 329 HOH B 330 HOH B 384 HOH B 436
SITE 1 AC8 6 ARG A 65 TYR B 60 ARG B 61 HOH B 316
SITE 2 AC8 6 HOH B 335 HOH B 336
SITE 1 AC9 7 GF1 B 3 SER B 70 SER B 130 THR B 235
SITE 2 AC9 7 GLY B 236 SER B 237 HOH B 414
SITE 1 BC1 5 ARG B 222 PRO B 226 THR B 227 TRP B 229
SITE 2 BC1 5 HOH B 446
CRYST1 45.279 106.765 47.777 90.00 101.74 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 0.022085 0.000000 0.004589 0.00000
SCALE2 0.000000 0.009366 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021378 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
