HEADER HYDROLASE 08-MAY-07 2PU2
TITLE AMPC BETA-LACTAMASE WITH BOUND PHTHALAMIDE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-LACTAMASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CEPHALOSPORINASE;
COMPND 5 EC: 3.5.2.6;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: AMPC, AMPA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109
KEYWDS AMPC BETA-LACAMASE PHTHALAMIDE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.BABAOGLU,B.K.SHOICHET
REVDAT 5 30-AUG-23 2PU2 1 REMARK
REVDAT 4 18-OCT-17 2PU2 1 REMARK
REVDAT 3 24-FEB-09 2PU2 1 VERSN
REVDAT 2 27-MAY-08 2PU2 1 JRNL
REVDAT 1 15-APR-08 2PU2 0
JRNL AUTH K.BABAOGLU,A.SIMEONOV,J.J.IRWIN,M.E.NELSON,B.FENG,
JRNL AUTH 2 C.J.THOMAS,L.CANCIAN,M.P.COSTI,D.A.MALTBY,A.JADHAV,
JRNL AUTH 3 J.INGLESE,C.P.AUSTIN,B.K.SHOICHET
JRNL TITL COMPREHENSIVE MECHANISTIC ANALYSIS OF HITS FROM
JRNL TITL 2 HIGH-THROUGHPUT AND DOCKING SCREENS AGAINST BETA-LACTAMASE.
JRNL REF J.MED.CHEM. V. 51 2502 2008
JRNL REFN ISSN 0022-2623
JRNL PMID 18333608
JRNL DOI 10.1021/JM701500E
REMARK 2
REMARK 2 RESOLUTION. 1.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 65652
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3326
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) : 1.86
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4315
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.24
REMARK 3 BIN R VALUE (WORKING SET) : 0.2730
REMARK 3 BIN FREE R VALUE SET COUNT : 251
REMARK 3 BIN FREE R VALUE : 0.3490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5600
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 57
REMARK 3 SOLVENT ATOMS : 570
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08000
REMARK 3 B22 (A**2) : 1.11000
REMARK 3 B33 (A**2) : -1.13000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.07000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.140
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.129
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.094
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.106
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5947 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3978 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8154 ; 1.404 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9761 ; 0.899 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 750 ; 6.479 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 257 ;36.251 ;24.864
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 953 ;13.006 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;15.958 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 876 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6658 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1152 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1192 ; 0.201 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4004 ; 0.183 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2857 ; 0.176 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2817 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 443 ; 0.152 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.085 ; 0.200
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): 11 ; 0.253 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 40 ; 0.299 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 22 ; 0.154 ; 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): 4710 ; 0.997 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1456 ; 0.176 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5888 ; 1.123 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2881 ; 1.794 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2250 ; 2.502 ; 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 : 1.40
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 2PU2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000042775.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-06
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) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65664
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
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 (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.53900
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: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1L2S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.7, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 59.36050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.42100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 59.36050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 38.42100
REMARK 290 SMTRY3 4 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 300 REMARK: BIOLOGICAL UNIT 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 OD2 ASP A 87 OH TYR A 92 1.95
REMARK 500 OD2 ASP B 87 OH TYR B 92 2.05
REMARK 500 O14 DK2 A 702 O HOH A 999 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 LYS A 126 -55.18 -126.43
REMARK 500 VAL A 178 -61.41 -122.93
REMARK 500 TYR A 221 17.28 -151.86
REMARK 500 ALA A 307 117.54 -36.01
REMARK 500 ASN A 341 42.74 -97.45
REMARK 500 LYS B 126 -64.69 -126.39
REMARK 500 VAL B 178 -59.51 -123.00
REMARK 500 TYR B 221 19.59 -154.47
REMARK 500 ASN B 341 38.96 -99.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 290 ILE A 291 120.73
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 PO4 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DK2 B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DK2 A 702
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PU4 RELATED DB: PDB
DBREF 2PU2 A 4 361 UNP P00811 AMPC_ECOLI 20 377
DBREF 2PU2 B 4 361 UNP P00811 AMPC_ECOLI 20 377
SEQRES 1 A 358 ALA PRO GLN GLN ILE ASN ASP ILE VAL HIS ARG THR ILE
SEQRES 2 A 358 THR PRO LEU ILE GLU GLN GLN LYS ILE PRO GLY MET ALA
SEQRES 3 A 358 VAL ALA VAL ILE TYR GLN GLY LYS PRO TYR TYR PHE THR
SEQRES 4 A 358 TRP GLY TYR ALA ASP ILE ALA LYS LYS GLN PRO VAL THR
SEQRES 5 A 358 GLN GLN THR LEU PHE GLU LEU GLY SER VAL SER LYS THR
SEQRES 6 A 358 PHE THR GLY VAL LEU GLY GLY ASP ALA ILE ALA ARG GLY
SEQRES 7 A 358 GLU ILE LYS LEU SER ASP PRO THR THR LYS TYR TRP PRO
SEQRES 8 A 358 GLU LEU THR ALA LYS GLN TRP ASN GLY ILE THR LEU LEU
SEQRES 9 A 358 HIS LEU ALA THR TYR THR ALA GLY GLY LEU PRO LEU GLN
SEQRES 10 A 358 VAL PRO ASP GLU VAL LYS SER SER SER ASP LEU LEU ARG
SEQRES 11 A 358 PHE TYR GLN ASN TRP GLN PRO ALA TRP ALA PRO GLY THR
SEQRES 12 A 358 GLN ARG LEU TYR ALA ASN SER SER ILE GLY LEU PHE GLY
SEQRES 13 A 358 ALA LEU ALA VAL LYS PRO SER GLY LEU SER PHE GLU GLN
SEQRES 14 A 358 ALA MET GLN THR ARG VAL PHE GLN PRO LEU LYS LEU ASN
SEQRES 15 A 358 HIS THR TRP ILE ASN VAL PRO PRO ALA GLU GLU LYS ASN
SEQRES 16 A 358 TYR ALA TRP GLY TYR ARG GLU GLY LYS ALA VAL HIS VAL
SEQRES 17 A 358 SER PRO GLY ALA LEU ASP ALA GLU ALA TYR GLY VAL LYS
SEQRES 18 A 358 SER THR ILE GLU ASP MET ALA ARG TRP VAL GLN SER ASN
SEQRES 19 A 358 LEU LYS PRO LEU ASP ILE ASN GLU LYS THR LEU GLN GLN
SEQRES 20 A 358 GLY ILE GLN LEU ALA GLN SER ARG TYR TRP GLN THR GLY
SEQRES 21 A 358 ASP MET TYR GLN GLY LEU GLY TRP GLU MET LEU ASP TRP
SEQRES 22 A 358 PRO VAL ASN PRO ASP SER ILE ILE ASN GLY SER ASP ASN
SEQRES 23 A 358 LYS ILE ALA LEU ALA ALA ARG PRO VAL LYS ALA ILE THR
SEQRES 24 A 358 PRO PRO THR PRO ALA VAL ARG ALA SER TRP VAL HIS LYS
SEQRES 25 A 358 THR GLY ALA THR GLY GLY PHE GLY SER TYR VAL ALA PHE
SEQRES 26 A 358 ILE PRO GLU LYS GLU LEU GLY ILE VAL MET LEU ALA ASN
SEQRES 27 A 358 LYS ASN TYR PRO ASN PRO ALA ARG VAL ASP ALA ALA TRP
SEQRES 28 A 358 GLN ILE LEU ASN ALA LEU GLN
SEQRES 1 B 358 ALA PRO GLN GLN ILE ASN ASP ILE VAL HIS ARG THR ILE
SEQRES 2 B 358 THR PRO LEU ILE GLU GLN GLN LYS ILE PRO GLY MET ALA
SEQRES 3 B 358 VAL ALA VAL ILE TYR GLN GLY LYS PRO TYR TYR PHE THR
SEQRES 4 B 358 TRP GLY TYR ALA ASP ILE ALA LYS LYS GLN PRO VAL THR
SEQRES 5 B 358 GLN GLN THR LEU PHE GLU LEU GLY SER VAL SER LYS THR
SEQRES 6 B 358 PHE THR GLY VAL LEU GLY GLY ASP ALA ILE ALA ARG GLY
SEQRES 7 B 358 GLU ILE LYS LEU SER ASP PRO THR THR LYS TYR TRP PRO
SEQRES 8 B 358 GLU LEU THR ALA LYS GLN TRP ASN GLY ILE THR LEU LEU
SEQRES 9 B 358 HIS LEU ALA THR TYR THR ALA GLY GLY LEU PRO LEU GLN
SEQRES 10 B 358 VAL PRO ASP GLU VAL LYS SER SER SER ASP LEU LEU ARG
SEQRES 11 B 358 PHE TYR GLN ASN TRP GLN PRO ALA TRP ALA PRO GLY THR
SEQRES 12 B 358 GLN ARG LEU TYR ALA ASN SER SER ILE GLY LEU PHE GLY
SEQRES 13 B 358 ALA LEU ALA VAL LYS PRO SER GLY LEU SER PHE GLU GLN
SEQRES 14 B 358 ALA MET GLN THR ARG VAL PHE GLN PRO LEU LYS LEU ASN
SEQRES 15 B 358 HIS THR TRP ILE ASN VAL PRO PRO ALA GLU GLU LYS ASN
SEQRES 16 B 358 TYR ALA TRP GLY TYR ARG GLU GLY LYS ALA VAL HIS VAL
SEQRES 17 B 358 SER PRO GLY ALA LEU ASP ALA GLU ALA TYR GLY VAL LYS
SEQRES 18 B 358 SER THR ILE GLU ASP MET ALA ARG TRP VAL GLN SER ASN
SEQRES 19 B 358 LEU LYS PRO LEU ASP ILE ASN GLU LYS THR LEU GLN GLN
SEQRES 20 B 358 GLY ILE GLN LEU ALA GLN SER ARG TYR TRP GLN THR GLY
SEQRES 21 B 358 ASP MET TYR GLN GLY LEU GLY TRP GLU MET LEU ASP TRP
SEQRES 22 B 358 PRO VAL ASN PRO ASP SER ILE ILE ASN GLY SER ASP ASN
SEQRES 23 B 358 LYS ILE ALA LEU ALA ALA ARG PRO VAL LYS ALA ILE THR
SEQRES 24 B 358 PRO PRO THR PRO ALA VAL ARG ALA SER TRP VAL HIS LYS
SEQRES 25 B 358 THR GLY ALA THR GLY GLY PHE GLY SER TYR VAL ALA PHE
SEQRES 26 B 358 ILE PRO GLU LYS GLU LEU GLY ILE VAL MET LEU ALA ASN
SEQRES 27 B 358 LYS ASN TYR PRO ASN PRO ALA ARG VAL ASP ALA ALA TRP
SEQRES 28 B 358 GLN ILE LEU ASN ALA LEU GLN
HET PO4 A 601 5
HET DK2 A 702 26
HET DK2 B 701 26
HETNAM PO4 PHOSPHATE ION
HETNAM DK2 2-[(1R)-1-CARBOXY-2-(4-HYDROXYPHENYL)ETHYL]-1,3-
HETNAM 2 DK2 DIOXOISOINDOLINE-5-CARBOXYLIC ACID
FORMUL 3 PO4 O4 P 3-
FORMUL 4 DK2 2(C18 H13 N O7)
FORMUL 6 HOH *570(H2 O)
HELIX 1 1 PRO A 5 LYS A 24 1 20
HELIX 2 2 VAL A 65 ARG A 80 1 16
HELIX 3 3 PRO A 88 TRP A 93 1 6
HELIX 4 4 ALA A 98 ASN A 102 5 5
HELIX 5 5 THR A 105 THR A 111 1 7
HELIX 6 6 SER A 127 TRP A 138 1 12
HELIX 7 7 ALA A 151 VAL A 163 1 13
HELIX 8 8 SER A 169 VAL A 178 1 10
HELIX 9 9 PRO A 192 TYR A 199 5 8
HELIX 10 10 LEU A 216 TYR A 221 1 6
HELIX 11 11 THR A 226 LYS A 239 1 14
HELIX 12 12 PRO A 240 ILE A 243 5 4
HELIX 13 13 GLU A 245 GLN A 256 1 12
HELIX 14 14 ASN A 279 ASP A 288 1 10
HELIX 15 15 PRO A 330 GLU A 333 5 4
HELIX 16 16 PRO A 345 GLN A 361 1 17
HELIX 17 17 PRO B 5 LYS B 24 1 20
HELIX 18 18 VAL B 65 ARG B 80 1 16
HELIX 19 19 PRO B 88 TRP B 93 1 6
HELIX 20 20 ALA B 98 ASN B 102 5 5
HELIX 21 21 THR B 105 THR B 111 1 7
HELIX 22 22 SER B 127 TRP B 138 1 12
HELIX 23 23 ALA B 151 VAL B 163 1 13
HELIX 24 24 SER B 169 VAL B 178 1 10
HELIX 25 25 PRO B 192 TYR B 199 5 8
HELIX 26 26 LEU B 216 GLY B 222 1 7
HELIX 27 27 THR B 226 LYS B 239 1 14
HELIX 28 28 PRO B 240 ILE B 243 5 4
HELIX 29 29 GLU B 245 GLN B 256 1 12
HELIX 30 30 ASN B 279 SER B 287 1 9
HELIX 31 31 ASP B 288 LEU B 293 1 6
HELIX 32 32 PRO B 330 GLU B 333 5 4
HELIX 33 33 PRO B 345 GLN B 361 1 17
SHEET 1 A10 GLN A 52 PRO A 53 0
SHEET 2 A10 LYS A 37 ASP A 47 -1 N ALA A 46 O GLN A 52
SHEET 3 A10 GLY A 27 TYR A 34 -1 N VAL A 30 O PHE A 41
SHEET 4 A10 LEU A 334 ALA A 340 -1 O LEU A 339 N ALA A 29
SHEET 5 A10 PHE A 322 ILE A 329 -1 N ILE A 329 O LEU A 334
SHEET 6 A10 SER A 311 THR A 319 -1 N GLY A 317 O SER A 324
SHEET 7 A10 GLU A 272 ASP A 275 -1 N LEU A 274 O TRP A 312
SHEET 8 A10 MET A 265 GLN A 267 -1 N TYR A 266 O MET A 273
SHEET 9 A10 ARG A 258 THR A 262 -1 N THR A 262 O MET A 265
SHEET 10 A10 LYS A 299 THR A 305 -1 O LYS A 299 N GLN A 261
SHEET 1 B 3 PHE A 60 GLU A 61 0
SHEET 2 B 3 LYS A 224 SER A 225 -1 O SER A 225 N PHE A 60
SHEET 3 B 3 THR A 187 TRP A 188 -1 N TRP A 188 O LYS A 224
SHEET 1 C 2 GLN A 147 ARG A 148 0
SHEET 2 C 2 ARG A 296 PRO A 297 -1 O ARG A 296 N ARG A 148
SHEET 1 D 2 GLY A 202 ARG A 204 0
SHEET 2 D 2 LYS A 207 VAL A 209 -1 O VAL A 209 N GLY A 202
SHEET 1 E10 GLN B 52 PRO B 53 0
SHEET 2 E10 LYS B 37 ASP B 47 -1 N ALA B 46 O GLN B 52
SHEET 3 E10 GLY B 27 TYR B 34 -1 N TYR B 34 O LYS B 37
SHEET 4 E10 LEU B 334 ALA B 340 -1 O LEU B 339 N ALA B 29
SHEET 5 E10 GLY B 323 ILE B 329 -1 N ILE B 329 O LEU B 334
SHEET 6 E10 SER B 311 ALA B 318 -1 N GLY B 317 O SER B 324
SHEET 7 E10 GLU B 272 ASP B 275 -1 N GLU B 272 O HIS B 314
SHEET 8 E10 MET B 265 GLN B 267 -1 N TYR B 266 O MET B 273
SHEET 9 E10 ARG B 258 THR B 262 -1 N TYR B 259 O GLN B 267
SHEET 10 E10 LYS B 299 THR B 305 -1 O LYS B 299 N GLN B 261
SHEET 1 F 2 PHE B 60 GLU B 61 0
SHEET 2 F 2 LYS B 224 SER B 225 -1 O SER B 225 N PHE B 60
SHEET 1 G 2 GLN B 147 ARG B 148 0
SHEET 2 G 2 ARG B 296 PRO B 297 -1 O ARG B 296 N ARG B 148
SHEET 1 H 2 GLY B 202 ARG B 204 0
SHEET 2 H 2 LYS B 207 VAL B 209 -1 O VAL B 209 N GLY B 202
CISPEP 1 TRP A 276 PRO A 277 0 3.65
CISPEP 2 THR A 302 PRO A 303 0 -3.64
CISPEP 3 TRP B 276 PRO B 277 0 5.73
CISPEP 4 THR B 302 PRO B 303 0 0.95
SITE 1 AC1 6 ARG A 133 HIS A 186 HOH A 872 HOH A 993
SITE 2 AC1 6 HOH A 996 LYS B 290
SITE 1 AC2 13 SER B 64 LEU B 119 GLN B 120 TYR B 150
SITE 2 AC2 13 ASN B 152 TYR B 221 GLY B 317 ALA B 318
SITE 3 AC2 13 THR B 319 GLY B 320 HOH B 793 HOH B 835
SITE 4 AC2 13 HOH B 857
SITE 1 AC3 12 SER A 64 TYR A 150 ASN A 152 TYR A 221
SITE 2 AC3 12 GLY A 317 ALA A 318 THR A 319 GLY A 320
SITE 3 AC3 12 HOH A 910 HOH A 994 HOH A 999 ALA B 4
CRYST1 118.721 76.842 97.495 90.00 115.80 90.00 C 1 2 1 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 0.008423 0.000000 0.004072 0.00000
SCALE2 0.000000 0.013014 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011393 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
