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HEADER HYDROLASE 01-MAY-17 5VNP
TITLE X-RAY CRYSTAL STRUCTURE OF HALOTAG BOUND TO THE P1 BENZOXADIAZOLE
TITLE 2 FLUOROGENIC LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS RHODOCHROUS;
SOURCE 3 ORGANISM_TAXID: 1829;
SOURCE 4 GENE: DHAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS BIOSENSOR, CYTOTOXICITY, FLUORESCENT PROBE, PROTEIN AGGREGATION,
KEYWDS 2 PROTEOME STRESS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.P.DUNHAM,A.K.BOAL
REVDAT 3 22-NOV-17 5VNP 1 REMARK
REVDAT 2 26-JUL-17 5VNP 1 JRNL
REVDAT 1 14-JUN-17 5VNP 0
JRNL AUTH Y.LIU,M.FARES,N.P.DUNHAM,Z.GAO,K.MIAO,X.JIANG,S.S.BOLLINGER,
JRNL AUTH 2 A.K.BOAL,X.ZHANG
JRNL TITL AGHALO: A FACILE FLUOROGENIC SENSOR TO DETECT DRUG-INDUCED
JRNL TITL 2 PROTEOME STRESS.
JRNL REF ANGEW. CHEM. INT. ED. ENGL. V. 56 8672 2017
JRNL REFN ESSN 1521-3773
JRNL PMID 28557281
JRNL DOI 10.1002/ANIE.201702417
REMARK 2
REMARK 2 RESOLUTION. 2.23 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 24385
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1299
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) : 2.23
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1349
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 74.42
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE SET COUNT : 71
REMARK 3 BIN FREE R VALUE : 0.3320
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4656
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 81
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.51000
REMARK 3 B22 (A**2) : -0.46000
REMARK 3 B33 (A**2) : 0.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.36000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.435
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.232
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.183
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.497
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4884 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4578 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6676 ; 0.974 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10556 ; 0.730 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 578 ; 4.477 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 228 ;28.856 ;23.333
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 734 ;12.099 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;13.164 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 704 ; 0.055 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5438 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1126 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5VNP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1000227736.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-AUG-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000, DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL-2000, SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26164
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.230
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.14100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.61600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: PHASER
REMARK 200 STARTING MODEL: 5UY1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM ACETATE, SODIUM
REMARK 280 CACODYLATE, PH 6.5, EVAPORATION, TEMPERATURE 293K
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 34.74050
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP A 105 CG ASP A 105 OD2 0.187
REMARK 500 ASP B 105 CG ASP B 105 OD2 0.191
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 ASP A 30 35.11 -98.00
REMARK 500 PRO A 41 50.50 -107.22
REMARK 500 THR A 42 -169.25 -102.70
REMARK 500 GLU A 97 -84.47 -91.36
REMARK 500 ASP A 105 -126.88 57.96
REMARK 500 ASP A 155 -69.06 -98.23
REMARK 500 VAL A 244 -66.27 -136.47
REMARK 500 LEU A 270 -96.09 -121.96
REMARK 500 PRO B 41 46.51 -105.40
REMARK 500 THR B 42 -169.84 -100.68
REMARK 500 GLU B 97 -77.87 -105.66
REMARK 500 ASP B 105 -131.27 59.74
REMARK 500 GLU B 129 62.58 39.16
REMARK 500 ARG B 152 48.04 -86.89
REMARK 500 VAL B 244 -67.74 -133.80
REMARK 500 LEU B 270 -92.43 -120.75
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 9FM A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 9FM B 301 and ASP B
REMARK 800 105
DBREF 5VNP A 3 292 UNP P0A3G2 DHAA_RHORH 4 293
DBREF 5VNP B 3 292 UNP P0A3G2 DHAA_RHORH 4 293
SEQADV 5VNP VAL A 46 UNP P0A3G2 LEU 47 CONFLICT
SEQADV 5VNP THR A 57 UNP P0A3G2 SER 58 CONFLICT
SEQADV 5VNP GLY A 77 UNP P0A3G2 ASP 78 CONFLICT
SEQADV 5VNP PHE A 86 UNP P0A3G2 TYR 87 CONFLICT
SEQADV 5VNP MET A 87 UNP P0A3G2 LEU 88 CONFLICT
SEQADV 5VNP PHE A 127 UNP P0A3G2 CYS 128 CONFLICT
SEQADV 5VNP THR A 154 UNP P0A3G2 ALA 155 CONFLICT
SEQADV 5VNP LYS A 159 UNP P0A3G2 GLU 160 CONFLICT
SEQADV 5VNP VAL A 166 UNP P0A3G2 ALA 167 CONFLICT
SEQADV 5VNP THR A 171 UNP P0A3G2 ALA 172 CONFLICT
SEQADV 5VNP MET A 174 UNP P0A3G2 LYS 175 CONFLICT
SEQADV 5VNP GLY A 175 UNP P0A3G2 CYS 176 CONFLICT
SEQADV 5VNP ASN A 194 UNP P0A3G2 LYS 195 CONFLICT
SEQADV 5VNP GLU A 223 UNP P0A3G2 ALA 224 CONFLICT
SEQADV 5VNP ASP A 226 UNP P0A3G2 ASN 227 CONFLICT
SEQADV 5VNP LYS A 256 UNP P0A3G2 GLU 257 CONFLICT
SEQADV 5VNP ALA A 263 UNP P0A3G2 THR 264 CONFLICT
SEQADV 5VNP ASN A 271 UNP P0A3G2 HIS 272 CONFLICT
SEQADV 5VNP LEU A 272 UNP P0A3G2 TYR 273 CONFLICT
SEQADV 5VNP SER A 290 UNP P0A3G2 PRO 291 CONFLICT
SEQADV 5VNP THR A 291 UNP P0A3G2 ALA 292 CONFLICT
SEQADV 5VNP VAL B 46 UNP P0A3G2 LEU 47 CONFLICT
SEQADV 5VNP THR B 57 UNP P0A3G2 SER 58 CONFLICT
SEQADV 5VNP GLY B 77 UNP P0A3G2 ASP 78 CONFLICT
SEQADV 5VNP PHE B 86 UNP P0A3G2 TYR 87 CONFLICT
SEQADV 5VNP MET B 87 UNP P0A3G2 LEU 88 CONFLICT
SEQADV 5VNP PHE B 127 UNP P0A3G2 CYS 128 CONFLICT
SEQADV 5VNP THR B 154 UNP P0A3G2 ALA 155 CONFLICT
SEQADV 5VNP LYS B 159 UNP P0A3G2 GLU 160 CONFLICT
SEQADV 5VNP VAL B 166 UNP P0A3G2 ALA 167 CONFLICT
SEQADV 5VNP THR B 171 UNP P0A3G2 ALA 172 CONFLICT
SEQADV 5VNP MET B 174 UNP P0A3G2 LYS 175 CONFLICT
SEQADV 5VNP GLY B 175 UNP P0A3G2 CYS 176 CONFLICT
SEQADV 5VNP ASN B 194 UNP P0A3G2 LYS 195 CONFLICT
SEQADV 5VNP GLU B 223 UNP P0A3G2 ALA 224 CONFLICT
SEQADV 5VNP ASP B 226 UNP P0A3G2 ASN 227 CONFLICT
SEQADV 5VNP LYS B 256 UNP P0A3G2 GLU 257 CONFLICT
SEQADV 5VNP ALA B 263 UNP P0A3G2 THR 264 CONFLICT
SEQADV 5VNP ASN B 271 UNP P0A3G2 HIS 272 CONFLICT
SEQADV 5VNP LEU B 272 UNP P0A3G2 TYR 273 CONFLICT
SEQADV 5VNP SER B 290 UNP P0A3G2 PRO 291 CONFLICT
SEQADV 5VNP THR B 291 UNP P0A3G2 ALA 292 CONFLICT
SEQRES 1 A 290 ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL GLU
SEQRES 2 A 290 VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY PRO
SEQRES 3 A 290 ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 A 290 THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS VAL
SEQRES 5 A 290 ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 A 290 MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE PHE
SEQRES 7 A 290 ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU ALA
SEQRES 8 A 290 LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP TRP
SEQRES 9 A 290 GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN PRO
SEQRES 10 A 290 GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE ARG
SEQRES 11 A 290 PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA ARG
SEQRES 12 A 290 GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY ARG
SEQRES 13 A 290 LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY THR
SEQRES 14 A 290 LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL GLU
SEQRES 15 A 290 MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL ASP
SEQRES 16 A 290 ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO ILE
SEQRES 17 A 290 ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU GLU
SEQRES 18 A 290 TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS LEU
SEQRES 19 A 290 LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO ALA
SEQRES 20 A 290 GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS LYS
SEQRES 21 A 290 ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN GLU
SEQRES 22 A 290 ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG TRP
SEQRES 23 A 290 LEU SER THR LEU
SEQRES 1 B 290 ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL GLU
SEQRES 2 B 290 VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY PRO
SEQRES 3 B 290 ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 B 290 THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS VAL
SEQRES 5 B 290 ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 B 290 MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE PHE
SEQRES 7 B 290 ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU ALA
SEQRES 8 B 290 LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP TRP
SEQRES 9 B 290 GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN PRO
SEQRES 10 B 290 GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE ARG
SEQRES 11 B 290 PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA ARG
SEQRES 12 B 290 GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY ARG
SEQRES 13 B 290 LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY THR
SEQRES 14 B 290 LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL GLU
SEQRES 15 B 290 MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL ASP
SEQRES 16 B 290 ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO ILE
SEQRES 17 B 290 ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU GLU
SEQRES 18 B 290 TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS LEU
SEQRES 19 B 290 LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO ALA
SEQRES 20 B 290 GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS LYS
SEQRES 21 B 290 ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN GLU
SEQRES 22 B 290 ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG TRP
SEQRES 23 B 290 LEU SER THR LEU
HET 9FM A 301 32
HET CL A 302 1
HET 9FM B 301 32
HET CL B 302 1
HETNAM 9FM N-{2-[2-(HEXYLOXY)ETHOXY]ETHYL}-N~2~-METHYL-N~2~-{[7-
HETNAM 2 9FM (METHYLAMINO)-2,1,3-BENZOXADIAZOL-4-
HETNAM 3 9FM YL]SULFONYL}GLYCINAMIDE
HETNAM CL CHLORIDE ION
FORMUL 3 9FM 2(C20 H33 N5 O6 S)
FORMUL 4 CL 2(CL 1-)
FORMUL 7 HOH *81(H2 O)
HELIX 1 AA1 SER A 43 ARG A 48 5 6
HELIX 2 AA2 ILE A 50 ALA A 55 1 6
HELIX 3 AA3 PHE A 79 LEU A 94 1 16
HELIX 4 AA4 ASP A 105 ASN A 118 1 14
HELIX 5 AA5 THR A 136 TRP A 140 5 5
HELIX 6 AA6 PRO A 141 PHE A 143 5 3
HELIX 7 AA7 ALA A 144 ARG A 152 1 9
HELIX 8 AA8 ASP A 155 ILE A 162 1 8
HELIX 9 AA9 ASN A 165 GLY A 170 1 6
HELIX 10 AB1 GLY A 170 GLY A 175 1 6
HELIX 11 AB2 THR A 181 GLU A 190 1 10
HELIX 12 AB3 PRO A 191 LEU A 193 5 3
HELIX 13 AB4 ASN A 194 ASP A 197 5 4
HELIX 14 AB5 ARG A 198 LEU A 208 1 11
HELIX 15 AB6 PRO A 214 SER A 231 1 18
HELIX 16 AB7 PRO A 247 LEU A 258 1 12
HELIX 17 AB8 LEU A 272 ASN A 277 1 6
HELIX 18 AB9 ASN A 277 LEU A 292 1 16
HELIX 19 AC1 SER B 43 ARG B 48 5 6
HELIX 20 AC2 ILE B 50 ALA B 55 1 6
HELIX 21 AC3 PHE B 79 LEU B 94 1 16
HELIX 22 AC4 ASP B 105 ASN B 118 1 14
HELIX 23 AC5 THR B 136 TRP B 140 5 5
HELIX 24 AC6 PRO B 141 PHE B 143 5 3
HELIX 25 AC7 ALA B 144 ARG B 152 1 9
HELIX 26 AC8 ASP B 155 ILE B 162 1 8
HELIX 27 AC9 ASN B 165 GLY B 170 1 6
HELIX 28 AD1 LEU B 172 VAL B 176 5 5
HELIX 29 AD2 THR B 181 GLU B 190 1 10
HELIX 30 AD3 PRO B 191 LEU B 193 5 3
HELIX 31 AD4 ASN B 194 ASP B 197 5 4
HELIX 32 AD5 ARG B 198 LEU B 208 1 11
HELIX 33 AD6 PRO B 214 SER B 231 1 18
HELIX 34 AD7 PRO B 247 LEU B 258 1 12
HELIX 35 AD8 LEU B 272 ASN B 277 1 6
HELIX 36 AD9 ASN B 277 LEU B 292 1 16
SHEET 1 AA1 8 HIS A 12 VAL A 16 0
SHEET 2 AA1 8 GLU A 19 VAL A 26 -1 O GLU A 19 N VAL A 16
SHEET 3 AA1 8 CYS A 60 PRO A 63 -1 O CYS A 60 N VAL A 26
SHEET 4 AA1 8 VAL A 34 LEU A 37 1 N PHE A 36 O ILE A 61
SHEET 5 AA1 8 VAL A 99 HIS A 104 1 O VAL A 100 N LEU A 35
SHEET 6 AA1 8 VAL A 122 MET A 128 1 O ALA A 126 N LEU A 101
SHEET 7 AA1 8 LYS A 235 PRO A 242 1 O LEU A 236 N PHE A 127
SHEET 8 AA1 8 CYS A 261 GLY A 269 1 O ILE A 266 N TRP A 239
SHEET 1 AA2 8 HIS B 12 VAL B 16 0
SHEET 2 AA2 8 GLU B 19 VAL B 26 -1 O GLU B 19 N VAL B 16
SHEET 3 AA2 8 CYS B 60 PRO B 63 -1 O CYS B 60 N VAL B 26
SHEET 4 AA2 8 VAL B 34 LEU B 37 1 N PHE B 36 O ILE B 61
SHEET 5 AA2 8 VAL B 99 HIS B 104 1 O VAL B 100 N LEU B 35
SHEET 6 AA2 8 VAL B 122 MET B 128 1 O ALA B 126 N LEU B 101
SHEET 7 AA2 8 LYS B 235 PRO B 242 1 O LEU B 236 N PHE B 127
SHEET 8 AA2 8 CYS B 261 GLY B 269 1 O VAL B 264 N LEU B 237
LINK OD2 ASP A 105 C32 9FM A 301 1555 1555 1.41
LINK OD2 ASP B 105 C32 9FM B 301 1555 1555 1.42
CISPEP 1 ASN A 40 PRO A 41 0 -1.60
CISPEP 2 GLU A 213 PRO A 214 0 -5.04
CISPEP 3 THR A 241 PRO A 242 0 2.62
CISPEP 4 ASN B 40 PRO B 41 0 -0.08
CISPEP 5 GLU B 213 PRO B 214 0 -5.01
CISPEP 6 THR B 241 PRO B 242 0 0.87
SITE 1 AC1 9 ASP A 105 THR A 147 PHE A 148 GLN A 164
SITE 2 AC1 9 VAL A 166 THR A 171 MET A 174 ASN A 271
SITE 3 AC1 9 CL A 302
SITE 1 AC2 4 ASN A 40 TRP A 106 PRO A 205 9FM A 301
SITE 1 AC3 4 ASN B 40 TRP B 106 PRO B 205 9FM B 301
SITE 1 AC4 18 GLY B 39 ASN B 40 HIS B 104 TRP B 106
SITE 2 AC4 18 GLY B 107 SER B 108 ALA B 109 GLU B 129
SITE 3 AC4 18 ILE B 131 ALA B 144 THR B 147 GLY B 170
SITE 4 AC4 18 THR B 171 MET B 174 GLY B 175 LEU B 245
SITE 5 AC4 18 ASN B 271 CL B 302
CRYST1 44.272 69.481 88.950 90.00 95.82 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 0.022588 0.000000 0.002302 0.00000
SCALE2 0.000000 0.014392 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011301 0.00000
TER 2329 LEU A 292
TER 4658 LEU B 292
MASTER 307 0 4 36 16 0 10 6 4803 2 66 46
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