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HEADER HYDROLASE 04-AUG-21 7PCX
TITLE X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE HALOTAG7-Q165W LABELED
TITLE 2 WITH A CHLOROALKANE-TETRAMETHYLRHODAMINE FLUOROPHORE SUBSTRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: 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
KEYWDS HALOALKANE DEHALOGENASE, HALO, TAG, HALOTAG7, SELF-LABELING PROTEIN,
KEYWDS 2 FLUOROPHORE, TETRAMETHYLRHODAMINE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.TARNAWSKI,M.FREI,J.HIBLOT,K.JOHNSSON
REVDAT 1 15-DEC-21 7PCX 0
JRNL AUTH M.TARNAWSKI,M.FREI,J.HIBLOT,K.JOHNSSON
JRNL TITL X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE
JRNL TITL 2 HALOTAG7-Q165W LABELED WITH A
JRNL TITL 3 CHLOROALKANE-TETRAMETHYLRHODAMINE FLUOROPHORE SUBSTRATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.400
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 300480
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 15024
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 39.8600 - 4.3500 0.97 9496 500 0.1712 0.1962
REMARK 3 2 4.3500 - 3.4500 0.98 9492 500 0.1603 0.1808
REMARK 3 3 3.4500 - 3.0200 0.99 9550 502 0.1735 0.2015
REMARK 3 4 3.0200 - 2.7400 0.99 9546 503 0.1785 0.1864
REMARK 3 5 2.7400 - 2.5400 0.99 9568 503 0.1795 0.1853
REMARK 3 6 2.5400 - 2.3900 0.99 9548 503 0.1755 0.1826
REMARK 3 7 2.3900 - 2.2700 0.99 9499 500 0.1692 0.1952
REMARK 3 8 2.2700 - 2.1700 0.99 9515 501 0.1680 0.1878
REMARK 3 9 2.1700 - 2.0900 0.99 9500 500 0.1637 0.1826
REMARK 3 10 2.0900 - 2.0200 0.99 9476 498 0.1658 0.1943
REMARK 3 11 2.0200 - 1.9600 0.99 9487 500 0.1612 0.1867
REMARK 3 12 1.9600 - 1.9000 0.99 9537 502 0.1597 0.1955
REMARK 3 13 1.9000 - 1.8500 0.99 9534 501 0.1625 0.1815
REMARK 3 14 1.8500 - 1.8000 0.99 9560 504 0.1605 0.1883
REMARK 3 15 1.8000 - 1.7600 0.99 9513 500 0.1596 0.1843
REMARK 3 16 1.7600 - 1.7300 0.99 9513 501 0.1592 0.1830
REMARK 3 17 1.7300 - 1.6900 0.99 9510 501 0.1641 0.1926
REMARK 3 18 1.6900 - 1.6600 0.99 9525 501 0.1764 0.2032
REMARK 3 19 1.6600 - 1.6300 0.99 9520 501 0.1944 0.2202
REMARK 3 20 1.6300 - 1.6000 0.99 9577 504 0.1860 0.2152
REMARK 3 21 1.6000 - 1.5800 0.99 9519 501 0.1794 0.2143
REMARK 3 22 1.5800 - 1.5500 0.99 9538 502 0.1756 0.2113
REMARK 3 23 1.5500 - 1.5300 0.99 9491 500 0.1705 0.2048
REMARK 3 24 1.5300 - 1.5100 0.99 9428 496 0.1692 0.1962
REMARK 3 25 1.5100 - 1.4900 0.99 9609 505 0.1852 0.2330
REMARK 3 26 1.4900 - 1.4700 0.99 9465 499 0.2049 0.2391
REMARK 3 27 1.4700 - 1.4500 0.99 9512 500 0.2263 0.2651
REMARK 3 28 1.4500 - 1.4300 0.99 9486 500 0.2634 0.2916
REMARK 3 29 1.4300 - 1.4200 0.99 9457 497 0.3253 0.3338
REMARK 3 30 1.4200 - 1.4000 0.99 9485 499 0.3997 0.4031
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.169
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.452
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.72
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 15107
REMARK 3 ANGLE : 0.910 20684
REMARK 3 CHIRALITY : 0.084 2142
REMARK 3 PLANARITY : 0.009 2925
REMARK 3 DIHEDRAL : 11.940 5699
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 7PCX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-AUG-21.
REMARK 100 THE DEPOSITION ID IS D_1292117491.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-21
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 : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 300540
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
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 (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.420
REMARK 200 R MERGE (I) : 0.03100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 22.9600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.31
REMARK 200 R MERGE FOR SHELL (I) : 0.20600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.090
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: 6Y7A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.0, 1.0 M LITHIUM
REMARK 280 CHLORIDE, 21% (M/V) PEG 6000, VAPOR DIFFUSION, HANGING 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 74.57500
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, 3, 4, 5, 6
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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: 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 46.29 -104.70
REMARK 500 THR A 43 -160.07 -101.75
REMARK 500 GLU A 98 -79.37 -105.43
REMARK 500 ASP A 106 -131.92 56.03
REMARK 500 ARG A 153 47.54 -88.77
REMARK 500 ASP A 156 -77.37 -95.43
REMARK 500 VAL A 245 -68.99 -132.74
REMARK 500 LEU A 271 -99.72 -118.99
REMARK 500 PRO B 42 48.92 -107.86
REMARK 500 THR B 43 -160.49 -100.51
REMARK 500 GLU B 98 -90.70 -107.00
REMARK 500 ASP B 106 -130.28 54.89
REMARK 500 ARG B 153 44.24 -85.58
REMARK 500 ASP B 156 -79.45 -97.52
REMARK 500 VAL B 245 -68.19 -132.07
REMARK 500 LEU B 271 -100.59 -117.99
REMARK 500 PRO C 42 49.08 -106.58
REMARK 500 THR C 43 -159.29 -103.48
REMARK 500 GLU C 98 -88.79 -108.53
REMARK 500 ASP C 106 -131.45 53.00
REMARK 500 ARG C 153 47.11 -90.10
REMARK 500 ASP C 156 -79.44 -98.28
REMARK 500 VAL C 245 -68.54 -131.76
REMARK 500 LEU C 271 -100.35 -118.49
REMARK 500 PRO D 42 48.58 -108.91
REMARK 500 THR D 43 -158.55 -102.56
REMARK 500 GLU D 98 -85.93 -99.72
REMARK 500 ASP D 106 -129.74 55.25
REMARK 500 ARG D 153 45.44 -87.32
REMARK 500 ASP D 156 -78.34 -97.63
REMARK 500 VAL D 245 -67.86 -130.42
REMARK 500 LEU D 271 -100.20 -117.04
REMARK 500 PRO E 42 48.70 -106.87
REMARK 500 THR E 43 -159.58 -103.07
REMARK 500 GLU E 98 -87.77 -103.17
REMARK 500 ASP E 106 -131.32 53.32
REMARK 500 ARG E 153 47.62 -87.76
REMARK 500 ASP E 156 -79.53 -97.16
REMARK 500 VAL E 245 -69.22 -134.97
REMARK 500 LEU E 271 -98.57 -114.91
REMARK 500 ASN E 278 65.47 -150.57
REMARK 500 PRO F 42 48.38 -105.90
REMARK 500 THR F 43 -159.22 -102.96
REMARK 500 GLU F 98 -87.21 -105.73
REMARK 500 ASP F 106 -130.64 53.24
REMARK 500 ARG F 153 45.89 -87.46
REMARK 500 ASP F 156 -79.41 -95.93
REMARK 500 VAL F 245 -68.28 -134.78
REMARK 500 LEU F 271 -99.91 -117.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6ZVU RELATED DB: PDB
REMARK 900 RELATED ID: 6ZVV RELATED DB: PDB
REMARK 900 RELATED ID: 6ZVW RELATED DB: PDB
REMARK 900 RELATED ID: 6ZVX RELATED DB: PDB
REMARK 900 RELATED ID: 6ZVY RELATED DB: PDB
REMARK 900 RELATED ID: 7PCW RELATED DB: PDB
DBREF 7PCX A 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
DBREF 7PCX B 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
DBREF 7PCX C 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
DBREF 7PCX D 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
DBREF 7PCX E 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
DBREF 7PCX F 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
SEQADV 7PCX GLY A 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCX VAL A 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 7PCX THR A 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 7PCX GLY A 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 7PCX PHE A 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 7PCX MET A 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 7PCX PHE A 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 7PCX THR A 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 7PCX LYS A 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 7PCX TRP A 165 UNP P0A3G3 GLN 165 ENGINEERED MUTATION
SEQADV 7PCX VAL A 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 7PCX THR A 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 7PCX MET A 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 7PCX GLY A 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 7PCX ASN A 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 7PCX GLU A 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 7PCX ASP A 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 7PCX LYS A 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 7PCX ALA A 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 7PCX ASN A 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 7PCX LEU A 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 7PCX SER A 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 7PCX THR A 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 7PCX GLU A 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCX ILE A 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCX GLY B 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCX VAL B 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 7PCX THR B 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 7PCX GLY B 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 7PCX PHE B 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 7PCX MET B 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 7PCX PHE B 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 7PCX THR B 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 7PCX LYS B 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 7PCX TRP B 165 UNP P0A3G3 GLN 165 ENGINEERED MUTATION
SEQADV 7PCX VAL B 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 7PCX THR B 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 7PCX MET B 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 7PCX GLY B 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 7PCX ASN B 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 7PCX GLU B 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 7PCX ASP B 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 7PCX LYS B 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 7PCX ALA B 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 7PCX ASN B 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 7PCX LEU B 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 7PCX SER B 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 7PCX THR B 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 7PCX GLU B 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCX ILE B 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCX GLY C 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCX VAL C 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 7PCX THR C 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 7PCX GLY C 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 7PCX PHE C 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 7PCX MET C 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 7PCX PHE C 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 7PCX THR C 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 7PCX LYS C 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 7PCX TRP C 165 UNP P0A3G3 GLN 165 ENGINEERED MUTATION
SEQADV 7PCX VAL C 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 7PCX THR C 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 7PCX MET C 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 7PCX GLY C 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 7PCX ASN C 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 7PCX GLU C 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 7PCX ASP C 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 7PCX LYS C 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 7PCX ALA C 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 7PCX ASN C 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 7PCX LEU C 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 7PCX SER C 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 7PCX THR C 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 7PCX GLU C 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCX ILE C 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCX GLY D 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCX VAL D 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 7PCX THR D 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 7PCX GLY D 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 7PCX PHE D 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 7PCX MET D 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 7PCX PHE D 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 7PCX THR D 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 7PCX LYS D 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 7PCX TRP D 165 UNP P0A3G3 GLN 165 ENGINEERED MUTATION
SEQADV 7PCX VAL D 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 7PCX THR D 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 7PCX MET D 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 7PCX GLY D 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 7PCX ASN D 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 7PCX GLU D 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 7PCX ASP D 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 7PCX LYS D 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 7PCX ALA D 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 7PCX ASN D 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 7PCX LEU D 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 7PCX SER D 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 7PCX THR D 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 7PCX GLU D 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCX ILE D 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCX GLY E 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCX VAL E 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 7PCX THR E 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 7PCX GLY E 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 7PCX PHE E 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 7PCX MET E 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 7PCX PHE E 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 7PCX THR E 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 7PCX LYS E 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 7PCX TRP E 165 UNP P0A3G3 GLN 165 ENGINEERED MUTATION
SEQADV 7PCX VAL E 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 7PCX THR E 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 7PCX MET E 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 7PCX GLY E 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 7PCX ASN E 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 7PCX GLU E 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 7PCX ASP E 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 7PCX LYS E 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 7PCX ALA E 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 7PCX ASN E 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 7PCX LEU E 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 7PCX SER E 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 7PCX THR E 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 7PCX GLU E 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCX ILE E 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCX GLY F 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCX VAL F 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 7PCX THR F 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 7PCX GLY F 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 7PCX PHE F 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 7PCX MET F 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 7PCX PHE F 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 7PCX THR F 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 7PCX LYS F 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 7PCX TRP F 165 UNP P0A3G3 GLN 165 ENGINEERED MUTATION
SEQADV 7PCX VAL F 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 7PCX THR F 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 7PCX MET F 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 7PCX GLY F 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 7PCX ASN F 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 7PCX GLU F 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 7PCX ASP F 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 7PCX LYS F 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 7PCX ALA F 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 7PCX ASN F 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 7PCX LEU F 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 7PCX SER F 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 7PCX THR F 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 7PCX GLU F 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCX ILE F 295 UNP P0A3G3 EXPRESSION TAG
SEQRES 1 A 293 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 A 293 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 A 293 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 A 293 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 A 293 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 A 293 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 A 293 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 A 293 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 A 293 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 A 293 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 A 293 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 A 293 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 13 A 293 ARG LYS LEU ILE ILE ASP TRP ASN VAL PHE ILE GLU GLY
SEQRES 14 A 293 THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 A 293 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 A 293 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 A 293 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 A 293 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 A 293 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 A 293 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 A 293 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 A 293 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 A 293 TRP LEU SER THR LEU GLU ILE
SEQRES 1 B 293 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 B 293 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 B 293 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 B 293 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 B 293 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 B 293 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 B 293 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 B 293 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 B 293 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 B 293 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 B 293 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 B 293 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 13 B 293 ARG LYS LEU ILE ILE ASP TRP ASN VAL PHE ILE GLU GLY
SEQRES 14 B 293 THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 B 293 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 B 293 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 B 293 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 B 293 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 B 293 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 B 293 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 B 293 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 B 293 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 B 293 TRP LEU SER THR LEU GLU ILE
SEQRES 1 C 293 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 C 293 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 C 293 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 C 293 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 C 293 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 C 293 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 C 293 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 C 293 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 C 293 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 C 293 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 C 293 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 C 293 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 13 C 293 ARG LYS LEU ILE ILE ASP TRP ASN VAL PHE ILE GLU GLY
SEQRES 14 C 293 THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 C 293 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 C 293 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 C 293 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 C 293 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 C 293 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 C 293 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 C 293 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 C 293 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 C 293 TRP LEU SER THR LEU GLU ILE
SEQRES 1 D 293 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 D 293 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 D 293 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 D 293 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 D 293 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 D 293 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 D 293 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 D 293 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 D 293 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 D 293 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 D 293 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 D 293 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 13 D 293 ARG LYS LEU ILE ILE ASP TRP ASN VAL PHE ILE GLU GLY
SEQRES 14 D 293 THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 D 293 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 D 293 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 D 293 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 D 293 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 D 293 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 D 293 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 D 293 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 D 293 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 D 293 TRP LEU SER THR LEU GLU ILE
SEQRES 1 E 293 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 E 293 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 E 293 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 E 293 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 E 293 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 E 293 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 E 293 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 E 293 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 E 293 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 E 293 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 E 293 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 E 293 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 13 E 293 ARG LYS LEU ILE ILE ASP TRP ASN VAL PHE ILE GLU GLY
SEQRES 14 E 293 THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 E 293 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 E 293 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 E 293 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 E 293 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 E 293 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 E 293 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 E 293 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 E 293 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 E 293 TRP LEU SER THR LEU GLU ILE
SEQRES 1 F 293 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 F 293 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 F 293 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 F 293 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 F 293 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 F 293 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 F 293 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 F 293 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 F 293 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 F 293 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 F 293 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 F 293 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 13 F 293 ARG LYS LEU ILE ILE ASP TRP ASN VAL PHE ILE GLU GLY
SEQRES 14 F 293 THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 F 293 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 F 293 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 F 293 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 F 293 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 F 293 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 F 293 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 F 293 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 F 293 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 F 293 TRP LEU SER THR LEU GLU ILE
HET OEH A 301 44
HET CL A 302 1
HET GOL A 303 6
HET OEH B 301 44
HET CL B 302 1
HET GOL B 303 6
HET OEH C 301 88
HET CL C 302 1
HET GOL C 303 6
HET OEH D 301 44
HET CL D 302 1
HET GOL D 303 6
HET OEH E 301 44
HET CL E 302 1
HET GOL E 303 6
HET GOL E 304 6
HET OEH F 301 44
HET CL F 302 1
HET GOL F 303 6
HETNAM OEH [9-[2-CARBOXY-5-[2-[2-(6-CHLORANYLHEXOXY)
HETNAM 2 OEH ETHOXY]ETHYLCARBAMOYL]PHENYL]-6-(DIMETHYLAMINO)
HETNAM 3 OEH XANTHEN-3-YLIDENE]-DIMETHYL-AZANIUM
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 7 OEH 6(C35 H43 CL N3 O6 1+)
FORMUL 8 CL 6(CL 1-)
FORMUL 9 GOL 7(C3 H8 O3)
FORMUL 26 HOH *1159(H2 O)
HELIX 1 AA1 SER A 44 ARG A 49 5 6
HELIX 2 AA2 ILE A 51 ALA A 56 1 6
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 LEU A 173 VAL A 177 5 5
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 GLN A 231 1 17
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 THR A 292 1 15
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 LEU B 173 VAL B 177 5 5
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 GLN B 231 1 17
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 SER B 291 1 14
HELIX 35 AD8 SER C 44 ARG C 49 5 6
HELIX 36 AD9 ILE C 51 ALA C 56 1 6
HELIX 37 AE1 PHE C 80 LEU C 95 1 16
HELIX 38 AE2 ASP C 106 ASN C 119 1 14
HELIX 39 AE3 THR C 137 TRP C 141 5 5
HELIX 40 AE4 PRO C 142 ARG C 153 1 12
HELIX 41 AE5 ASP C 156 ILE C 163 1 8
HELIX 42 AE6 ASN C 166 GLY C 171 1 6
HELIX 43 AE7 LEU C 173 VAL C 177 5 5
HELIX 44 AE8 THR C 182 GLU C 191 1 10
HELIX 45 AE9 PRO C 192 LEU C 194 5 3
HELIX 46 AF1 ASN C 195 ASP C 198 5 4
HELIX 47 AF2 ARG C 199 LEU C 209 1 11
HELIX 48 AF3 PRO C 215 GLN C 231 1 17
HELIX 49 AF4 PRO C 248 LEU C 259 1 12
HELIX 50 AF5 LEU C 273 ASN C 278 1 6
HELIX 51 AF6 ASN C 278 SER C 291 1 14
HELIX 52 AF7 SER D 44 ARG D 49 5 6
HELIX 53 AF8 ILE D 51 ALA D 56 1 6
HELIX 54 AF9 PHE D 80 LEU D 95 1 16
HELIX 55 AG1 ASP D 106 ASN D 119 1 14
HELIX 56 AG2 THR D 137 TRP D 141 5 5
HELIX 57 AG3 PRO D 142 ARG D 153 1 12
HELIX 58 AG4 ASP D 156 ILE D 163 1 8
HELIX 59 AG5 ASN D 166 GLY D 171 1 6
HELIX 60 AG6 LEU D 173 VAL D 177 5 5
HELIX 61 AG7 THR D 182 GLU D 191 1 10
HELIX 62 AG8 PRO D 192 LEU D 194 5 3
HELIX 63 AG9 ASN D 195 ASP D 198 5 4
HELIX 64 AH1 ARG D 199 LEU D 209 1 11
HELIX 65 AH2 PRO D 215 GLN D 231 1 17
HELIX 66 AH3 PRO D 248 LEU D 259 1 12
HELIX 67 AH4 LEU D 273 ASN D 278 1 6
HELIX 68 AH5 ASN D 278 LEU D 293 1 16
HELIX 69 AH6 SER E 44 ARG E 49 5 6
HELIX 70 AH7 ILE E 51 ALA E 56 1 6
HELIX 71 AH8 PHE E 80 LEU E 95 1 16
HELIX 72 AH9 ASP E 106 ASN E 119 1 14
HELIX 73 AI1 THR E 137 TRP E 141 5 5
HELIX 74 AI2 PRO E 142 ARG E 153 1 12
HELIX 75 AI3 ASP E 156 ILE E 163 1 8
HELIX 76 AI4 ASN E 166 GLY E 171 1 6
HELIX 77 AI5 LEU E 173 VAL E 177 5 5
HELIX 78 AI6 THR E 182 GLU E 191 1 10
HELIX 79 AI7 PRO E 192 LEU E 194 5 3
HELIX 80 AI8 ASN E 195 ASP E 198 5 4
HELIX 81 AI9 ARG E 199 LEU E 209 1 11
HELIX 82 AJ1 PRO E 215 GLN E 231 1 17
HELIX 83 AJ2 PRO E 248 LEU E 259 1 12
HELIX 84 AJ3 LEU E 273 ASN E 278 1 6
HELIX 85 AJ4 ASN E 278 SER E 291 1 14
HELIX 86 AJ5 SER F 44 ARG F 49 5 6
HELIX 87 AJ6 ILE F 51 ALA F 56 1 6
HELIX 88 AJ7 PHE F 80 LEU F 95 1 16
HELIX 89 AJ8 ASP F 106 ASN F 119 1 14
HELIX 90 AJ9 THR F 137 TRP F 141 5 5
HELIX 91 AK1 PRO F 142 ARG F 153 1 12
HELIX 92 AK2 ASP F 156 ILE F 163 1 8
HELIX 93 AK3 ASN F 166 GLY F 171 1 6
HELIX 94 AK4 LEU F 173 VAL F 177 5 5
HELIX 95 AK5 THR F 182 GLU F 191 1 10
HELIX 96 AK6 PRO F 192 LEU F 194 5 3
HELIX 97 AK7 ASN F 195 ASP F 198 5 4
HELIX 98 AK8 ARG F 199 LEU F 209 1 11
HELIX 99 AK9 PRO F 215 GLN F 231 1 17
HELIX 100 AL1 PRO F 248 LEU F 259 1 12
HELIX 101 AL2 LEU F 273 ASN F 278 1 6
HELIX 102 AL3 ASN F 278 SER F 291 1 14
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 PHE A 37 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 LYS A 263 N LEU A 238
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 PHE B 37 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 LYS B 263 N LEU B 238
SHEET 1 AA3 8 HIS C 13 VAL C 17 0
SHEET 2 AA3 8 GLU C 20 VAL C 27 -1 O GLU C 20 N VAL C 17
SHEET 3 AA3 8 CYS C 61 PRO C 64 -1 O CYS C 61 N VAL C 27
SHEET 4 AA3 8 VAL C 35 LEU C 38 1 N PHE C 37 O ILE C 62
SHEET 5 AA3 8 VAL C 100 HIS C 105 1 O VAL C 101 N LEU C 36
SHEET 6 AA3 8 VAL C 123 MET C 129 1 O ALA C 127 N LEU C 102
SHEET 7 AA3 8 LYS C 236 PRO C 243 1 O LEU C 237 N PHE C 128
SHEET 8 AA3 8 CYS C 262 GLY C 270 1 O ILE C 267 N TRP C 240
SHEET 1 AA4 8 HIS D 13 VAL D 17 0
SHEET 2 AA4 8 GLU D 20 VAL D 27 -1 O GLU D 20 N VAL D 17
SHEET 3 AA4 8 CYS D 61 PRO D 64 -1 O CYS D 61 N VAL D 27
SHEET 4 AA4 8 VAL D 35 LEU D 38 1 N PHE D 37 O ILE D 62
SHEET 5 AA4 8 VAL D 100 HIS D 105 1 O VAL D 101 N LEU D 36
SHEET 6 AA4 8 VAL D 123 MET D 129 1 O ALA D 127 N LEU D 102
SHEET 7 AA4 8 LYS D 236 PRO D 243 1 O LEU D 237 N PHE D 128
SHEET 8 AA4 8 CYS D 262 GLY D 270 1 O ILE D 267 N TRP D 240
SHEET 1 AA5 8 HIS E 13 VAL E 17 0
SHEET 2 AA5 8 GLU E 20 VAL E 27 -1 O GLU E 20 N VAL E 17
SHEET 3 AA5 8 CYS E 61 PRO E 64 -1 O CYS E 61 N VAL E 27
SHEET 4 AA5 8 VAL E 35 LEU E 38 1 N PHE E 37 O ILE E 62
SHEET 5 AA5 8 VAL E 100 HIS E 105 1 O VAL E 101 N LEU E 36
SHEET 6 AA5 8 VAL E 123 MET E 129 1 O ALA E 127 N LEU E 102
SHEET 7 AA5 8 LYS E 236 PRO E 243 1 O LEU E 237 N PHE E 128
SHEET 8 AA5 8 CYS E 262 GLY E 270 1 O ILE E 267 N TRP E 240
SHEET 1 AA6 8 HIS F 13 VAL F 17 0
SHEET 2 AA6 8 GLU F 20 VAL F 27 -1 O GLU F 20 N VAL F 17
SHEET 3 AA6 8 CYS F 61 PRO F 64 -1 O CYS F 61 N VAL F 27
SHEET 4 AA6 8 VAL F 35 LEU F 38 1 N PHE F 37 O ILE F 62
SHEET 5 AA6 8 VAL F 100 HIS F 105 1 O VAL F 101 N LEU F 36
SHEET 6 AA6 8 VAL F 123 MET F 129 1 O ALA F 127 N LEU F 102
SHEET 7 AA6 8 LYS F 236 PRO F 243 1 O LEU F 237 N PHE F 128
SHEET 8 AA6 8 CYS F 262 GLY F 270 1 O ILE F 267 N TRP F 240
LINK OD2 ASP A 106 C20 OEH A 301 1555 1555 1.38
LINK OD2 ASP B 106 C20 OEH B 301 1555 1555 1.38
LINK OD2 ASP C 106 C20AOEH C 301 1555 1555 1.38
LINK OD2 ASP C 106 C20BOEH C 301 1555 1555 1.38
LINK OD2 ASP D 106 C20 OEH D 301 1555 1555 1.38
LINK OD2 ASP E 106 C20 OEH E 301 1555 1555 1.38
LINK OD2 ASP F 106 C20 OEH F 301 1555 1555 1.38
CISPEP 1 ASN A 41 PRO A 42 0 -2.26
CISPEP 2 GLU A 214 PRO A 215 0 -3.04
CISPEP 3 THR A 242 PRO A 243 0 3.82
CISPEP 4 ASN B 41 PRO B 42 0 1.11
CISPEP 5 GLU B 214 PRO B 215 0 -6.31
CISPEP 6 THR B 242 PRO B 243 0 4.89
CISPEP 7 ASN C 41 PRO C 42 0 0.38
CISPEP 8 GLU C 214 PRO C 215 0 -10.18
CISPEP 9 THR C 242 PRO C 243 0 5.43
CISPEP 10 ASN D 41 PRO D 42 0 2.87
CISPEP 11 GLU D 214 PRO D 215 0 -10.29
CISPEP 12 THR D 242 PRO D 243 0 3.62
CISPEP 13 ASN E 41 PRO E 42 0 0.72
CISPEP 14 GLU E 214 PRO E 215 0 -8.82
CISPEP 15 THR E 242 PRO E 243 0 6.65
CISPEP 16 ASN F 41 PRO F 42 0 0.11
CISPEP 17 GLU F 214 PRO F 215 0 -4.94
CISPEP 18 THR F 242 PRO F 243 0 1.31
CRYST1 74.960 149.150 79.920 90.00 117.97 90.00 P 1 21 1 12
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 0.013340 0.000000 0.007083 0.00000
SCALE2 0.000000 0.006705 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014167 0.00000
TER 2367 ILE A 295
TER 4731 ILE B 295
TER 7098 ILE C 295
TER 9487 ILE D 295
TER 11865 ILE E 295
TER 14243 ILE F 295
MASTER 318 0 19 102 48 0 0 615601 6 356 138
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