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HEADER FLUORESCENT PROTEIN 25-MAY-21 7OND
TITLE HALOTAG ENGINEERING FOR ENHANCED FLUOROGENICITY AND KINETICS WITH A
TITLE 2 STYRYLPYRIDINE DYE
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;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 ORGANISM_TAXID: 1831;
SOURCE 4 GENE: DHAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET30
KEYWDS HALOTAG, FLUORESCENCE, IMAGING, MAMMALIAN CELLS, FLUORESCENT
KEYWDS 2 REPORTER, CHANNEL DYE, DIRECTED EVOLUTION, FLUORESCENT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.STEIN,A.D.LIANG
REVDAT 1 21-JUL-21 7OND 0
JRNL AUTH C.MIRO-VINYALS,A.STEIN,S.FISCHER,T.R.WARD,A.D.LIANG
JRNL TITL HALOTAG ENGINEERING FOR ENHANCED FLUOROGENICITY AND KINETICS
JRNL TITL 2 WITH A STYRYLPYRIDINE DYE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
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) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 86202
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4538
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) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6328
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.51
REMARK 3 BIN R VALUE (WORKING SET) : 0.1970
REMARK 3 BIN FREE R VALUE SET COUNT : 343
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4738
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 51
REMARK 3 SOLVENT ATOMS : 617
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.38000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.40000
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): 0.070
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.069
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.043
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.106
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.965
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4988 ; 0.012 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4534 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6818 ; 1.823 ; 1.654
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10477 ; 1.501 ; 1.570
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 596 ; 6.026 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 267 ;30.513 ;21.798
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 743 ;12.978 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;22.006 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 613 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5620 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1132 ; 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 7OND COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAY-21.
REMARK 100 THE DEPOSITION ID IS D_1292116087.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAR-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000314
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90750
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 47.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.06203
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.6800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.37340
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: 5Y2X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE HEXAHYDRATE,
REMARK 280 20 % W/V PEG 3350, PH 5.9, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 34.27900
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 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 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 ALA A 2
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 HIS B 299
REMARK 465 HIS B 300
REMARK 465 HIS B 301
REMARK 465 HIS B 302
REMARK 465 HIS B 303
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 O GLU A 140 O HOH A 501 2.10
REMARK 500 OD1 ASP B 106 C19 VF2 B 401 2.19
REMARK 500 OD1 ASP A 106 C19 VF2 A 401 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 728 O HOH B 812 2556 2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 HIS A 144 CB - CA - C ANGL. DEV. = 12.3 DEGREES
REMARK 500 THR A 155 CA - CB - OG1 ANGL. DEV. = -26.6 DEGREES
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 PRO A 42 48.19 -108.31
REMARK 500 THR A 43 -160.08 -100.45
REMARK 500 GLU A 98 -88.98 -103.98
REMARK 500 ASP A 106 -135.57 52.88
REMARK 500 ARG A 153 37.10 -89.15
REMARK 500 ASP A 156 -74.82 -83.25
REMARK 500 ALA A 245 -73.61 -138.97
REMARK 500 LEU A 271 -119.61 -119.56
REMARK 500 SER A 296 126.22 -33.74
REMARK 500 PRO B 42 48.07 -107.55
REMARK 500 THR B 43 -160.39 -101.56
REMARK 500 GLU B 98 -90.75 -107.16
REMARK 500 ASP B 106 -135.18 51.93
REMARK 500 GLU B 130 61.94 38.41
REMARK 500 ARG B 153 46.54 -84.69
REMARK 500 ASP B 156 -75.75 -98.20
REMARK 500 ALA B 245 -74.47 -136.88
REMARK 500 LEU B 271 -120.39 -119.45
REMARK 500 SER B 296 127.67 -36.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 797 DISTANCE = 6.09 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 183 OE1
REMARK 620 2 HOH B 596 O 92.9
REMARK 620 3 HOH B 634 O 93.0 85.0
REMARK 620 4 HOH B 639 O 84.0 173.0 88.9
REMARK 620 5 HOH B 689 O 91.1 92.5 175.3 93.8
REMARK 620 6 HOH B 704 O 177.1 88.7 84.7 94.2 91.3
REMARK 620 N 1 2 3 4 5
DBREF 7OND A 3 293 UNP P0A3G3 DHAA_RHOSO 3 293
DBREF 7OND B 3 293 UNP P0A3G3 DHAA_RHOSO 3 293
SEQADV 7OND MET A 1 UNP P0A3G3 INITIATING METHIONINE
SEQADV 7OND ALA A 2 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND VAL A 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 7OND THR A 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 7OND GLY A 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 7OND PHE A 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 7OND MET A 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 7OND PHE A 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 7OND CYS A 133 UNP P0A3G3 ARG 133 ENGINEERED MUTATION
SEQADV 7OND MET A 143 UNP P0A3G3 GLU 143 ENGINEERED MUTATION
SEQADV 7OND HIS A 144 UNP P0A3G3 PHE 144 ENGINEERED MUTATION
SEQADV 7OND THR A 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 7OND LYS A 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 7OND VAL A 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 7OND THR A 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 7OND TYR A 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 7OND GLY A 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 7OND ASN A 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 7OND GLU A 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 7OND ASP A 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 7OND ALA A 245 UNP P0A3G3 VAL 245 ENGINEERED MUTATION
SEQADV 7OND LYS A 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 7OND ALA A 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 7OND ASN A 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 7OND LEU A 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 7OND SER A 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 7OND THR A 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 7OND GLU A 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND ILE A 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND SER A 296 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND GLY A 297 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND HIS A 298 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND HIS A 299 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND HIS A 300 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND HIS A 301 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND HIS A 302 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND HIS A 303 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND MET B 1 UNP P0A3G3 INITIATING METHIONINE
SEQADV 7OND ALA B 2 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND VAL B 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 7OND THR B 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 7OND GLY B 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 7OND PHE B 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 7OND MET B 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 7OND PHE B 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 7OND CYS B 133 UNP P0A3G3 ARG 133 ENGINEERED MUTATION
SEQADV 7OND MET B 143 UNP P0A3G3 GLU 143 ENGINEERED MUTATION
SEQADV 7OND HIS B 144 UNP P0A3G3 PHE 144 ENGINEERED MUTATION
SEQADV 7OND THR B 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 7OND LYS B 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 7OND VAL B 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 7OND THR B 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 7OND TYR B 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 7OND GLY B 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 7OND ASN B 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 7OND GLU B 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 7OND ASP B 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 7OND ALA B 245 UNP P0A3G3 VAL 245 ENGINEERED MUTATION
SEQADV 7OND LYS B 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 7OND ALA B 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 7OND ASN B 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 7OND LEU B 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 7OND SER B 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 7OND THR B 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 7OND GLU B 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND ILE B 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND SER B 296 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND GLY B 297 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND HIS B 298 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND HIS B 299 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND HIS B 300 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND HIS B 301 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND HIS B 302 UNP P0A3G3 EXPRESSION TAG
SEQADV 7OND HIS B 303 UNP P0A3G3 EXPRESSION TAG
SEQRES 1 A 303 MET ALA GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 A 303 TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP
SEQRES 3 A 303 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 A 303 GLY ASN PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE
SEQRES 5 A 303 PRO HIS VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 A 303 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY
SEQRES 7 A 303 TYR PHE PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE
SEQRES 8 A 303 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 A 303 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 A 303 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU
SEQRES 11 A 303 PHE ILE CYS PRO ILE PRO THR TRP ASP GLU TRP PRO MET
SEQRES 12 A 303 HIS ALA ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP
SEQRES 13 A 303 VAL GLY ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE
SEQRES 14 A 303 GLU GLY THR LEU PRO TYR GLY VAL VAL ARG PRO LEU THR
SEQRES 15 A 303 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN
SEQRES 16 A 303 PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 A 303 LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU
SEQRES 18 A 303 VAL GLU GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL
SEQRES 19 A 303 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY ALA LEU ILE
SEQRES 20 A 303 PRO PRO ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO
SEQRES 21 A 303 ASN CYS LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU
SEQRES 22 A 303 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 A 303 ALA ARG TRP LEU SER THR LEU GLU ILE SER GLY HIS HIS
SEQRES 24 A 303 HIS HIS HIS HIS
SEQRES 1 B 303 MET ALA GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 B 303 TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP
SEQRES 3 B 303 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 B 303 GLY ASN PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE
SEQRES 5 B 303 PRO HIS VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 B 303 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY
SEQRES 7 B 303 TYR PHE PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE
SEQRES 8 B 303 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 B 303 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 B 303 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU
SEQRES 11 B 303 PHE ILE CYS PRO ILE PRO THR TRP ASP GLU TRP PRO MET
SEQRES 12 B 303 HIS ALA ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP
SEQRES 13 B 303 VAL GLY ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE
SEQRES 14 B 303 GLU GLY THR LEU PRO TYR GLY VAL VAL ARG PRO LEU THR
SEQRES 15 B 303 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN
SEQRES 16 B 303 PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 B 303 LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU
SEQRES 18 B 303 VAL GLU GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL
SEQRES 19 B 303 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY ALA LEU ILE
SEQRES 20 B 303 PRO PRO ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO
SEQRES 21 B 303 ASN CYS LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU
SEQRES 22 B 303 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 B 303 ALA ARG TRP LEU SER THR LEU GLU ILE SER GLY HIS HIS
SEQRES 24 B 303 HIS HIS HIS HIS
HET VF2 A 401 24
HET CL A 402 1
HET VF2 B 401 24
HET CL B 402 1
HET MG B 403 1
HETNAM VF2 4-[(E)-2-[1-(7-CHLORANYLHEPTYL)PYRIDIN-1-IUM-4-
HETNAM 2 VF2 YL]ETHENYL]-N,N-DIMETHYL-ANILINE
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
FORMUL 3 VF2 2(C22 H30 CL N2 1+)
FORMUL 4 CL 2(CL 1-)
FORMUL 7 MG MG 2+
FORMUL 8 HOH *617(H2 O)
HELIX 1 AA1 SER A 44 ARG A 49 5 6
HELIX 2 AA2 ILE A 51 VAL A 55 5 5
HELIX 3 AA3 PHE A 80 LEU A 95 1 16
HELIX 4 AA4 ASP A 106 ASN A 119 1 14
HELIX 5 AA5 THR A 137 TRP A 141 5 5
HELIX 6 AA6 PRO A 142 ARG A 153 1 12
HELIX 7 AA7 ASP A 156 ILE A 163 1 8
HELIX 8 AA8 ASN A 166 GLY A 171 1 6
HELIX 9 AA9 GLY A 171 GLY A 176 1 6
HELIX 10 AB1 THR A 182 GLU A 191 1 10
HELIX 11 AB2 PRO A 192 LEU A 194 5 3
HELIX 12 AB3 ASN A 195 ASP A 198 5 4
HELIX 13 AB4 ARG A 199 LEU A 209 1 11
HELIX 14 AB5 PRO A 215 SER A 232 1 18
HELIX 15 AB6 PRO A 248 LEU A 259 1 12
HELIX 16 AB7 LEU A 273 ASN A 278 1 6
HELIX 17 AB8 ASN A 278 LEU A 293 1 16
HELIX 18 AB9 SER B 44 ARG B 49 5 6
HELIX 19 AC1 ILE B 51 ALA B 56 1 6
HELIX 20 AC2 PHE B 80 LEU B 95 1 16
HELIX 21 AC3 ASP B 106 ASN B 119 1 14
HELIX 22 AC4 THR B 137 TRP B 141 5 5
HELIX 23 AC5 PRO B 142 ARG B 153 1 12
HELIX 24 AC6 ASP B 156 ILE B 163 1 8
HELIX 25 AC7 ASN B 166 GLY B 171 1 6
HELIX 26 AC8 GLY B 171 GLY B 176 1 6
HELIX 27 AC9 THR B 182 GLU B 191 1 10
HELIX 28 AD1 PRO B 192 LEU B 194 5 3
HELIX 29 AD2 ASN B 195 ASP B 198 5 4
HELIX 30 AD3 ARG B 199 LEU B 209 1 11
HELIX 31 AD4 PRO B 215 SER B 232 1 18
HELIX 32 AD5 PRO B 248 LEU B 259 1 12
HELIX 33 AD6 LEU B 273 ASN B 278 1 6
HELIX 34 AD7 ASN B 278 THR B 292 1 15
SHEET 1 AA1 8 HIS A 13 VAL A 17 0
SHEET 2 AA1 8 GLU A 20 VAL A 27 -1 O GLU A 20 N VAL A 17
SHEET 3 AA1 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 AA1 8 VAL A 35 LEU A 38 1 N VAL A 35 O ILE A 62
SHEET 5 AA1 8 VAL A 100 HIS A 105 1 O VAL A 101 N LEU A 36
SHEET 6 AA1 8 VAL A 123 MET A 129 1 O ALA A 127 N LEU A 102
SHEET 7 AA1 8 LYS A 236 PRO A 243 1 O LEU A 237 N PHE A 128
SHEET 8 AA1 8 CYS A 262 GLY A 270 1 O ILE A 267 N TRP A 240
SHEET 1 AA2 8 HIS B 13 VAL B 17 0
SHEET 2 AA2 8 GLU B 20 VAL B 27 -1 O GLU B 20 N VAL B 17
SHEET 3 AA2 8 CYS B 61 PRO B 64 -1 O CYS B 61 N VAL B 27
SHEET 4 AA2 8 VAL B 35 LEU B 38 1 N VAL B 35 O ILE B 62
SHEET 5 AA2 8 VAL B 100 HIS B 105 1 O VAL B 101 N LEU B 36
SHEET 6 AA2 8 VAL B 123 MET B 129 1 O LYS B 124 N VAL B 100
SHEET 7 AA2 8 LYS B 236 PRO B 243 1 O LEU B 237 N PHE B 128
SHEET 8 AA2 8 CYS B 262 GLY B 270 1 O ILE B 267 N TRP B 240
LINK OD1 ASP A 106 C20 VF2 A 401 1555 1555 1.39
LINK OD1 ASP B 106 C20 VF2 B 401 1555 1555 1.39
LINK OE1 GLU B 183 MG MG B 403 1555 1555 2.06
LINK MG MG B 403 O HOH B 596 1555 1555 2.07
LINK MG MG B 403 O HOH B 634 1555 1555 2.10
LINK MG MG B 403 O HOH B 639 1555 1555 2.13
LINK MG MG B 403 O HOH B 689 1555 1555 2.02
LINK MG MG B 403 O HOH B 704 1555 1455 1.99
CISPEP 1 ASN A 41 PRO A 42 0 -1.35
CISPEP 2 GLU A 214 PRO A 215 0 -6.99
CISPEP 3 THR A 242 PRO A 243 0 1.47
CISPEP 4 ASN B 41 PRO B 42 0 -3.92
CISPEP 5 GLU B 214 PRO B 215 0 -5.62
CISPEP 6 THR B 242 PRO B 243 0 3.19
CRYST1 47.586 68.558 81.179 90.00 98.57 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 0.021015 0.000000 0.003168 0.00000
SCALE2 0.000000 0.014586 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012458 0.00000
TER 2390 HIS A 298
TER 4770 HIS B 298
MASTER 370 0 5 34 16 0 0 6 5406 2 57 48
END |